HEADER    MEMBRANE PROTEIN                        07-APR-22   7ZI0              
TITLE     STRUCTURE OF HUMAN SMOOTHENED IN COMPLEX WITH CHOLESTEROL AND SAG     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SMOOTHENED HOMOLOG,SOLUBLE CYTOCHROME B562;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: SMO,PROTEIN GX,CYTOCHROME B-562;                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: HUMAN SMOOTHENED WITH CYTOCHROME B562 (BRIL) INSERTED 
COMPND   7 IN A CYTOPLASMIC LOOP.,HUMAN SMOOTHENED WITH CYTOCHROME B562 (BRIL)  
COMPND   8 INSERTED IN A CYTOPLASMIC LOOP.,HUMAN SMOOTHENED WITH CYTOCHROME B562
COMPND   9 (BRIL) INSERTED IN A CYTOPLASMIC LOOP.                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SMO, SMOH, CYBC;                                               
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293 CELLS                            
KEYWDS    CLASS F G PROTEIN COUPLED RECEPTOR, HEDGEHOG SIGNALLING, ONCOPROTEIN, 
KEYWDS   2 DRUG TARGET, SIGNAL TRANSDUCTION, MORPHOGEN, CHOLESTEROL, MEMBRANE   
KEYWDS   3 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.F.X.BYRNE,R.E.WOOLLEY,B.ANSELL,M.S.P.SANSOM,S.NEWSTEAD,C.SIEBOLD    
REVDAT   1   15-JUN-22 7ZI0    0                                                
JRNL        AUTH   M.KINNEBREW,R.E.WOOLLEY,T.B.ANSELL,E.F.X.BYRNE,S.FRIGUI,     
JRNL        AUTH 2 G.LUCHETTI,R.SIRCAR,S.NACHTERGAELE,L.MYDOCK-MCGRANE,         
JRNL        AUTH 3 K.KRISHNAN,S.NEWSTEAD,M.S.P.SANSOM,D.F.COVEY,C.SIEBOLD,      
JRNL        AUTH 4 R.ROHATGI                                                    
JRNL        TITL   PATCHED 1 REGULATES SMOOTHENED BY CONTROLLING STEROL BINDING 
JRNL        TITL 2 TO ITS EXTRACELLULAR CYSTEINE-RICH DOMAIN.                   
JRNL        REF    SCI ADV                       V.   8 M5563 2022              
JRNL        REFN                   ESSN 2375-2548                               
JRNL        PMID   35658032                                                     
JRNL        DOI    10.1126/SCIADV.ABM5563                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 29738                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1480                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1909                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 93                           
REMARK   3   BIN FREE R VALUE                    : 0.4280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9245                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 164                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 130.6                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.35000                                             
REMARK   3    B22 (A**2) : 4.60000                                              
REMARK   3    B33 (A**2) : -2.26000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 4.81000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.476         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.498         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 64.946        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9674 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9148 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13165 ; 1.641 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20975 ; 1.422 ; 2.988       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1168 ; 5.828 ; 5.017       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   425 ;34.987 ;23.082       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1523 ;16.819 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    70 ;15.624 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1455 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10822 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2342 ; 0.006 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    58        A   190                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.3950 -34.1500 107.3750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6410 T22:   0.3597                                     
REMARK   3      T33:   0.5502 T12:   0.0765                                     
REMARK   3      T13:  -0.0707 T23:  -0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3236 L22:   1.4045                                     
REMARK   3      L33:   3.0807 L12:   0.2292                                     
REMARK   3      L13:  -2.3156 L23:  -1.2218                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3834 S12:  -0.1339 S13:  -0.2766                       
REMARK   3      S21:  -0.0602 S22:   0.1085 S23:  -0.1523                       
REMARK   3      S31:   0.0481 S32:  -0.0574 S33:   0.2750                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    58        B   190                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.7440 -16.7760  -5.1850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6344 T22:   1.2430                                     
REMARK   3      T33:   0.1848 T12:  -0.0150                                     
REMARK   3      T13:   0.0606 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2254 L22:   2.7337                                     
REMARK   3      L33:   1.4086 L12:  -1.9895                                     
REMARK   3      L13:  -2.1247 L23:   0.3865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1964 S12:   0.2093 S13:  -0.7295                       
REMARK   3      S21:  -0.1049 S22:  -0.4625 S23:  -0.1924                       
REMARK   3      S31:  -0.6186 S32:  -0.3239 S33:   0.2661                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   191        A   216                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.2700 -22.6060  85.2420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6091 T22:   0.6659                                     
REMARK   3      T33:   0.4825 T12:   0.0768                                     
REMARK   3      T13:  -0.0736 T23:   0.0466                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4000 L22:   2.9031                                     
REMARK   3      L33:   9.1774 L12:   2.3719                                     
REMARK   3      L13:  -5.2008 L23:  -2.4077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1986 S12:   0.3901 S13:   0.1969                       
REMARK   3      S21:   0.4056 S22:   0.2207 S23:  -0.0077                       
REMARK   3      S31:   0.0155 S32:  -0.5251 S33:  -0.4194                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   191        B   216                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.1200  -6.7690  16.7240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6151 T22:   0.8379                                     
REMARK   3      T33:   0.2542 T12:  -0.0501                                     
REMARK   3      T13:   0.1090 T23:   0.1061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9592 L22:   2.2022                                     
REMARK   3      L33:  12.1002 L12:  -2.6750                                     
REMARK   3      L13:  -1.4592 L23:  -3.1561                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2059 S12:   0.4329 S13:   0.3194                       
REMARK   3      S21:  -0.0652 S22:  -0.0570 S23:  -0.1211                       
REMARK   3      S31:  -0.1135 S32:  -0.4459 S33:  -0.1489                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   217        A   425                          
REMARK   3    RESIDUE RANGE :   A   551        A   657                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.0790 -19.7830  56.4710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6665 T22:   0.6717                                     
REMARK   3      T33:   0.3497 T12:   0.0501                                     
REMARK   3      T13:  -0.0046 T23:   0.0899                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9201 L22:   0.0795                                     
REMARK   3      L33:   4.1669 L12:   0.2411                                     
REMARK   3      L13:  -1.1721 L23:  -0.4209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0531 S12:   0.2803 S13:   0.0253                       
REMARK   3      S21:   0.0528 S22:   0.0695 S23:  -0.0474                       
REMARK   3      S31:  -0.1432 S32:  -0.4117 S33:  -0.1225                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   217        B   425                          
REMARK   3    RESIDUE RANGE :   B   551        B   655                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1030  -9.6420  47.5990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6639 T22:   0.8760                                     
REMARK   3      T33:   0.2558 T12:  -0.0733                                     
REMARK   3      T13:   0.0378 T23:   0.1870                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1831 L22:   0.0538                                     
REMARK   3      L33:   2.7005 L12:  -0.1510                                     
REMARK   3      L13:  -1.1316 L23:   0.1735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0671 S12:   0.2936 S13:  -0.1259                       
REMARK   3      S21:   0.0661 S22:  -0.0498 S23:  -0.0471                       
REMARK   3      S31:  -0.3176 S32:  -0.1146 S33:  -0.0173                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   426        A   550                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8510 -38.8640  13.9710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6335 T22:   1.1260                                     
REMARK   3      T33:   0.2820 T12:   0.0995                                     
REMARK   3      T13:   0.2448 T23:  -0.1646                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2982 L22:   1.9825                                     
REMARK   3      L33:   0.4501 L12:  -2.0986                                     
REMARK   3      L13:   0.1673 L23:   0.5005                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1224 S12:   0.6233 S13:  -0.4427                       
REMARK   3      S21:  -0.2815 S22:  -0.1763 S23:   0.2317                       
REMARK   3      S31:  -0.2130 S32:  -0.1119 S33:   0.0539                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   426        B   550                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.8050 -39.5220  89.7620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6733 T22:   0.4015                                     
REMARK   3      T33:   0.5112 T12:  -0.0760                                     
REMARK   3      T13:  -0.0738 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1638 L22:   2.5789                                     
REMARK   3      L33:   2.2378 L12:   2.2650                                     
REMARK   3      L13:  -1.8350 L23:  -2.1711                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0675 S12:   0.4216 S13:  -0.1330                       
REMARK   3      S21:   0.3148 S22:   0.0033 S23:  -0.0385                       
REMARK   3      S31:  -0.0705 S32:   0.0046 S33:  -0.0709                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 7ZI0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-APR-22.                  
REMARK 100 THE DEPOSITION ID IS D_1292122303.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS V1.1.3                       
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.23                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31218                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5L7D                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH6.0, 0.09-0.12 M POTASSIUM   
REMARK 280  FORMATE, 24-27% (V/V) PEG500 DME, 0.5 MM ZINC CHLORIDE, 0.1 M       
REMARK 280  AMMONIUM FLUORIDE, LIPIDIC CUBIC PHASE, TEMPERATURE 293K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       61.43000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.57500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       61.43000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.57500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     ASN A    35                                                      
REMARK 465     ALA A    36                                                      
REMARK 465     THR A    37                                                      
REMARK 465     GLY A    38                                                      
REMARK 465     PRO A    39                                                      
REMARK 465     GLY A    40                                                      
REMARK 465     PRO A    41                                                      
REMARK 465     ARG A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     ALA A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     GLY A    46                                                      
REMARK 465     SER A    47                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     ARG A    49                                                      
REMARK 465     ARG A    50                                                      
REMARK 465     SER A    51                                                      
REMARK 465     ALA A    52                                                      
REMARK 465     ALA A    53                                                      
REMARK 465     VAL A    54                                                      
REMARK 465     THR A    55                                                      
REMARK 465     GLY A    56                                                      
REMARK 465     PRO A    57                                                      
REMARK 465     LYS A   480                                                      
REMARK 465     LEU A   481                                                      
REMARK 465     GLU A   482                                                      
REMARK 465     ASP A   483                                                      
REMARK 465     LYS A   484                                                      
REMARK 465     SER A   485                                                      
REMARK 465     PRO A   486                                                      
REMARK 465     GLY A   658                                                      
REMARK 465     GLN A   659                                                      
REMARK 465     GLY A   660                                                      
REMARK 465     THR A   661                                                      
REMARK 465     GLU A   662                                                      
REMARK 465     THR A   663                                                      
REMARK 465     SER A   664                                                      
REMARK 465     GLN A   665                                                      
REMARK 465     VAL A   666                                                      
REMARK 465     ALA A   667                                                      
REMARK 465     PRO A   668                                                      
REMARK 465     ALA A   669                                                      
REMARK 465     SER B    32                                                      
REMARK 465     SER B    33                                                      
REMARK 465     GLY B    34                                                      
REMARK 465     ASN B    35                                                      
REMARK 465     ALA B    36                                                      
REMARK 465     THR B    37                                                      
REMARK 465     GLY B    38                                                      
REMARK 465     PRO B    39                                                      
REMARK 465     GLY B    40                                                      
REMARK 465     PRO B    41                                                      
REMARK 465     ARG B    42                                                      
REMARK 465     SER B    43                                                      
REMARK 465     ALA B    44                                                      
REMARK 465     GLY B    45                                                      
REMARK 465     GLY B    46                                                      
REMARK 465     SER B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     ARG B    49                                                      
REMARK 465     ARG B    50                                                      
REMARK 465     SER B    51                                                      
REMARK 465     ALA B    52                                                      
REMARK 465     ALA B    53                                                      
REMARK 465     VAL B    54                                                      
REMARK 465     THR B    55                                                      
REMARK 465     GLY B    56                                                      
REMARK 465     PRO B    57                                                      
REMARK 465     LYS B   480                                                      
REMARK 465     LEU B   481                                                      
REMARK 465     GLU B   482                                                      
REMARK 465     ASP B   483                                                      
REMARK 465     LYS B   484                                                      
REMARK 465     ALA B   596                                                      
REMARK 465     ASN B   597                                                      
REMARK 465     VAL B   598                                                      
REMARK 465     THR B   599                                                      
REMARK 465     ILE B   600                                                      
REMARK 465     GLY B   601                                                      
REMARK 465     LEU B   602                                                      
REMARK 465     PRO B   603                                                      
REMARK 465     THR B   604                                                      
REMARK 465     LYS B   605                                                      
REMARK 465     GLN B   606                                                      
REMARK 465     PRO B   607                                                      
REMARK 465     ILE B   608                                                      
REMARK 465     PRO B   609                                                      
REMARK 465     ASP B   610                                                      
REMARK 465     LEU B   656                                                      
REMARK 465     THR B   657                                                      
REMARK 465     GLY B   658                                                      
REMARK 465     GLN B   659                                                      
REMARK 465     GLY B   660                                                      
REMARK 465     THR B   661                                                      
REMARK 465     GLU B   662                                                      
REMARK 465     THR B   663                                                      
REMARK 465     SER B   664                                                      
REMARK 465     GLN B   665                                                      
REMARK 465     VAL B   666                                                      
REMARK 465     ALA B   667                                                      
REMARK 465     PRO B   668                                                      
REMARK 465     ALA B   669                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG A   400     OE1  GLN A   581              2.10            
REMARK 500   OD2  ASP A   209     NH2  ARG A   589              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD1  ASP A   172     NE2  GLN A   192     4446     1.55            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  74   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 199   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 400   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 400   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG B 467   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG B 543   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A  64       33.61    -83.24                                   
REMARK 500    THR A  90       37.34    -98.89                                   
REMARK 500    ALA A 115       65.08     92.87                                   
REMARK 500    ASP A 137       29.47     49.71                                   
REMARK 500    CYS A 154       38.24    -89.83                                   
REMARK 500    GLU A 181      -14.88     88.19                                   
REMARK 500    GLU A 208     -128.63     40.22                                   
REMARK 500    GLN A 351       85.91     55.00                                   
REMARK 500    ALA A 379       66.21     60.12                                   
REMARK 500    VAL A 404      -60.61   -128.46                                   
REMARK 500    TYR A 534      -60.80   -121.38                                   
REMARK 500    LYS A 605     -109.81      2.47                                   
REMARK 500    CYS B  64       33.50    -81.25                                   
REMARK 500    THR B  90       35.50    -98.83                                   
REMARK 500    ALA B 115       97.12    -66.42                                   
REMARK 500    CYS B 154       39.35    -90.94                                   
REMARK 500    GLU B 208     -137.97     51.38                                   
REMARK 500    THR B 348     -121.71     53.30                                   
REMARK 500    ALA B 379       65.51     61.08                                   
REMARK 500    VAL B 404      -61.77   -127.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MPG A  706                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 704  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  90   O                                                      
REMARK 620 2 ALA A  93   O    89.9                                              
REMARK 620 3 SER A  96   O    76.9  69.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 705  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 305   OE2                                                    
REMARK 620 2 THR A 307   O    85.4                                              
REMARK 620 N                    1                                               
DBREF  7ZI0 A   32   428  UNP    Q99835   SMO_HUMAN       32    428             
DBREF  7ZI0 A  434   538  UNP    P0ABE7   C562_ECOLX      23    127             
DBREF  7ZI0 A  547   659  UNP    Q99835   SMO_HUMAN      443    555             
DBREF  7ZI0 B   32   428  UNP    Q99835   SMO_HUMAN       32    428             
DBREF  7ZI0 B  434   538  UNP    P0ABE7   C562_ECOLX      23    127             
DBREF  7ZI0 B  547   659  UNP    Q99835   SMO_HUMAN      443    555             
SEQADV 7ZI0 PHE A  329  UNP  Q99835    VAL   329 CONFLICT                       
SEQADV 7ZI0 ALA A  429  UNP  Q99835              LINKER                         
SEQADV 7ZI0 ARG A  430  UNP  Q99835              LINKER                         
SEQADV 7ZI0 ARG A  431  UNP  Q99835              LINKER                         
SEQADV 7ZI0 GLN A  432  UNP  Q99835              LINKER                         
SEQADV 7ZI0 LEU A  433  UNP  Q99835              LINKER                         
SEQADV 7ZI0 TRP A  440  UNP  P0ABE7    MET    29 CONFLICT                       
SEQADV 7ZI0 ILE A  535  UNP  P0ABE7    HIS   124 CONFLICT                       
SEQADV 7ZI0 LEU A  539  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 GLU A  540  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 ARG A  541  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 ALA A  542  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 ARG A  543  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 SER A  544  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 THR A  545  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 LEU A  546  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 GLY A  660  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 THR A  661  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 GLU A  662  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 THR A  663  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 SER A  664  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 GLN A  665  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 VAL A  666  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 ALA A  667  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 PRO A  668  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 ALA A  669  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 PHE B  329  UNP  Q99835    VAL   329 CONFLICT                       
SEQADV 7ZI0 ALA B  429  UNP  Q99835              LINKER                         
SEQADV 7ZI0 ARG B  430  UNP  Q99835              LINKER                         
SEQADV 7ZI0 ARG B  431  UNP  Q99835              LINKER                         
SEQADV 7ZI0 GLN B  432  UNP  Q99835              LINKER                         
SEQADV 7ZI0 LEU B  433  UNP  Q99835              LINKER                         
SEQADV 7ZI0 TRP B  440  UNP  P0ABE7    MET    29 CONFLICT                       
SEQADV 7ZI0 ILE B  535  UNP  P0ABE7    HIS   124 CONFLICT                       
SEQADV 7ZI0 LEU B  539  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 GLU B  540  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 ARG B  541  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 ALA B  542  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 ARG B  543  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 SER B  544  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 THR B  545  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 LEU B  546  UNP  P0ABE7              LINKER                         
SEQADV 7ZI0 GLY B  660  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 THR B  661  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 GLU B  662  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 THR B  663  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 SER B  664  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 GLN B  665  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 VAL B  666  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 ALA B  667  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 PRO B  668  UNP  Q99835              EXPRESSION TAG                 
SEQADV 7ZI0 ALA B  669  UNP  Q99835              EXPRESSION TAG                 
SEQRES   1 A  638  SER SER GLY ASN ALA THR GLY PRO GLY PRO ARG SER ALA          
SEQRES   2 A  638  GLY GLY SER ALA ARG ARG SER ALA ALA VAL THR GLY PRO          
SEQRES   3 A  638  PRO PRO PRO LEU SER HIS CYS GLY ARG ALA ALA PRO CYS          
SEQRES   4 A  638  GLU PRO LEU ARG TYR ASN VAL CYS LEU GLY SER VAL LEU          
SEQRES   5 A  638  PRO TYR GLY ALA THR SER THR LEU LEU ALA GLY ASP SER          
SEQRES   6 A  638  ASP SER GLN GLU GLU ALA HIS GLY LYS LEU VAL LEU TRP          
SEQRES   7 A  638  SER GLY LEU ARG ASN ALA PRO ARG CYS TRP ALA VAL ILE          
SEQRES   8 A  638  GLN PRO LEU LEU CYS ALA VAL TYR MET PRO LYS CYS GLU          
SEQRES   9 A  638  ASN ASP ARG VAL GLU LEU PRO SER ARG THR LEU CYS GLN          
SEQRES  10 A  638  ALA THR ARG GLY PRO CYS ALA ILE VAL GLU ARG GLU ARG          
SEQRES  11 A  638  GLY TRP PRO ASP PHE LEU ARG CYS THR PRO ASP ARG PHE          
SEQRES  12 A  638  PRO GLU GLY CYS THR ASN GLU VAL GLN ASN ILE LYS PHE          
SEQRES  13 A  638  ASN SER SER GLY GLN CYS GLU VAL PRO LEU VAL ARG THR          
SEQRES  14 A  638  ASP ASN PRO LYS SER TRP TYR GLU ASP VAL GLU GLY CYS          
SEQRES  15 A  638  GLY ILE GLN CYS GLN ASN PRO LEU PHE THR GLU ALA GLU          
SEQRES  16 A  638  HIS GLN ASP MET HIS SER TYR ILE ALA ALA PHE GLY ALA          
SEQRES  17 A  638  VAL THR GLY LEU CYS THR LEU PHE THR LEU ALA THR PHE          
SEQRES  18 A  638  VAL ALA ASP TRP ARG ASN SER ASN ARG TYR PRO ALA VAL          
SEQRES  19 A  638  ILE LEU PHE TYR VAL ASN ALA CYS PHE PHE VAL GLY SER          
SEQRES  20 A  638  ILE GLY TRP LEU ALA GLN PHE MET ASP GLY ALA ARG ARG          
SEQRES  21 A  638  GLU ILE VAL CYS ARG ALA ASP GLY THR MET ARG LEU GLY          
SEQRES  22 A  638  GLU PRO THR SER ASN GLU THR LEU SER CYS VAL ILE ILE          
SEQRES  23 A  638  PHE VAL ILE VAL TYR TYR ALA LEU MET ALA GLY PHE VAL          
SEQRES  24 A  638  TRP PHE VAL VAL LEU THR TYR ALA TRP HIS THR SER PHE          
SEQRES  25 A  638  LYS ALA LEU GLY THR THR TYR GLN PRO LEU SER GLY LYS          
SEQRES  26 A  638  THR SER TYR PHE HIS LEU LEU THR TRP SER LEU PRO PHE          
SEQRES  27 A  638  VAL LEU THR VAL ALA ILE LEU ALA VAL ALA GLN VAL ASP          
SEQRES  28 A  638  GLY ASP SER VAL SER GLY ILE CYS PHE VAL GLY TYR LYS          
SEQRES  29 A  638  ASN TYR ARG TYR ARG ALA GLY PHE VAL LEU ALA PRO ILE          
SEQRES  30 A  638  GLY LEU VAL LEU ILE VAL GLY GLY TYR PHE LEU ILE ARG          
SEQRES  31 A  638  GLY VAL MET THR LEU PHE SER ALA ARG ARG GLN LEU ALA          
SEQRES  32 A  638  ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU          
SEQRES  33 A  638  LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS          
SEQRES  34 A  638  ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA          
SEQRES  35 A  638  GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO          
SEQRES  36 A  638  ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP          
SEQRES  37 A  638  ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA          
SEQRES  38 A  638  ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU          
SEQRES  39 A  638  GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR          
SEQRES  40 A  638  LEU GLU ARG ALA ARG SER THR LEU SER LYS ILE ASN GLU          
SEQRES  41 A  638  THR MET LEU ARG LEU GLY ILE PHE GLY PHE LEU ALA PHE          
SEQRES  42 A  638  GLY PHE VAL LEU ILE THR PHE SER CYS HIS PHE TYR ASP          
SEQRES  43 A  638  PHE PHE ASN GLN ALA GLU TRP GLU ARG SER PHE ARG ASP          
SEQRES  44 A  638  TYR VAL LEU CYS GLN ALA ASN VAL THR ILE GLY LEU PRO          
SEQRES  45 A  638  THR LYS GLN PRO ILE PRO ASP CYS GLU ILE LYS ASN ARG          
SEQRES  46 A  638  PRO SER LEU LEU VAL GLU LYS ILE ASN LEU PHE ALA MET          
SEQRES  47 A  638  PHE GLY THR GLY ILE ALA MET SER THR TRP VAL TRP THR          
SEQRES  48 A  638  LYS ALA THR LEU LEU ILE TRP ARG ARG THR TRP CYS ARG          
SEQRES  49 A  638  LEU THR GLY GLN GLY THR GLU THR SER GLN VAL ALA PRO          
SEQRES  50 A  638  ALA                                                          
SEQRES   1 B  638  SER SER GLY ASN ALA THR GLY PRO GLY PRO ARG SER ALA          
SEQRES   2 B  638  GLY GLY SER ALA ARG ARG SER ALA ALA VAL THR GLY PRO          
SEQRES   3 B  638  PRO PRO PRO LEU SER HIS CYS GLY ARG ALA ALA PRO CYS          
SEQRES   4 B  638  GLU PRO LEU ARG TYR ASN VAL CYS LEU GLY SER VAL LEU          
SEQRES   5 B  638  PRO TYR GLY ALA THR SER THR LEU LEU ALA GLY ASP SER          
SEQRES   6 B  638  ASP SER GLN GLU GLU ALA HIS GLY LYS LEU VAL LEU TRP          
SEQRES   7 B  638  SER GLY LEU ARG ASN ALA PRO ARG CYS TRP ALA VAL ILE          
SEQRES   8 B  638  GLN PRO LEU LEU CYS ALA VAL TYR MET PRO LYS CYS GLU          
SEQRES   9 B  638  ASN ASP ARG VAL GLU LEU PRO SER ARG THR LEU CYS GLN          
SEQRES  10 B  638  ALA THR ARG GLY PRO CYS ALA ILE VAL GLU ARG GLU ARG          
SEQRES  11 B  638  GLY TRP PRO ASP PHE LEU ARG CYS THR PRO ASP ARG PHE          
SEQRES  12 B  638  PRO GLU GLY CYS THR ASN GLU VAL GLN ASN ILE LYS PHE          
SEQRES  13 B  638  ASN SER SER GLY GLN CYS GLU VAL PRO LEU VAL ARG THR          
SEQRES  14 B  638  ASP ASN PRO LYS SER TRP TYR GLU ASP VAL GLU GLY CYS          
SEQRES  15 B  638  GLY ILE GLN CYS GLN ASN PRO LEU PHE THR GLU ALA GLU          
SEQRES  16 B  638  HIS GLN ASP MET HIS SER TYR ILE ALA ALA PHE GLY ALA          
SEQRES  17 B  638  VAL THR GLY LEU CYS THR LEU PHE THR LEU ALA THR PHE          
SEQRES  18 B  638  VAL ALA ASP TRP ARG ASN SER ASN ARG TYR PRO ALA VAL          
SEQRES  19 B  638  ILE LEU PHE TYR VAL ASN ALA CYS PHE PHE VAL GLY SER          
SEQRES  20 B  638  ILE GLY TRP LEU ALA GLN PHE MET ASP GLY ALA ARG ARG          
SEQRES  21 B  638  GLU ILE VAL CYS ARG ALA ASP GLY THR MET ARG LEU GLY          
SEQRES  22 B  638  GLU PRO THR SER ASN GLU THR LEU SER CYS VAL ILE ILE          
SEQRES  23 B  638  PHE VAL ILE VAL TYR TYR ALA LEU MET ALA GLY PHE VAL          
SEQRES  24 B  638  TRP PHE VAL VAL LEU THR TYR ALA TRP HIS THR SER PHE          
SEQRES  25 B  638  LYS ALA LEU GLY THR THR TYR GLN PRO LEU SER GLY LYS          
SEQRES  26 B  638  THR SER TYR PHE HIS LEU LEU THR TRP SER LEU PRO PHE          
SEQRES  27 B  638  VAL LEU THR VAL ALA ILE LEU ALA VAL ALA GLN VAL ASP          
SEQRES  28 B  638  GLY ASP SER VAL SER GLY ILE CYS PHE VAL GLY TYR LYS          
SEQRES  29 B  638  ASN TYR ARG TYR ARG ALA GLY PHE VAL LEU ALA PRO ILE          
SEQRES  30 B  638  GLY LEU VAL LEU ILE VAL GLY GLY TYR PHE LEU ILE ARG          
SEQRES  31 B  638  GLY VAL MET THR LEU PHE SER ALA ARG ARG GLN LEU ALA          
SEQRES  32 B  638  ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU          
SEQRES  33 B  638  LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS          
SEQRES  34 B  638  ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA          
SEQRES  35 B  638  GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO          
SEQRES  36 B  638  ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP          
SEQRES  37 B  638  ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA          
SEQRES  38 B  638  ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU          
SEQRES  39 B  638  GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR          
SEQRES  40 B  638  LEU GLU ARG ALA ARG SER THR LEU SER LYS ILE ASN GLU          
SEQRES  41 B  638  THR MET LEU ARG LEU GLY ILE PHE GLY PHE LEU ALA PHE          
SEQRES  42 B  638  GLY PHE VAL LEU ILE THR PHE SER CYS HIS PHE TYR ASP          
SEQRES  43 B  638  PHE PHE ASN GLN ALA GLU TRP GLU ARG SER PHE ARG ASP          
SEQRES  44 B  638  TYR VAL LEU CYS GLN ALA ASN VAL THR ILE GLY LEU PRO          
SEQRES  45 B  638  THR LYS GLN PRO ILE PRO ASP CYS GLU ILE LYS ASN ARG          
SEQRES  46 B  638  PRO SER LEU LEU VAL GLU LYS ILE ASN LEU PHE ALA MET          
SEQRES  47 B  638  PHE GLY THR GLY ILE ALA MET SER THR TRP VAL TRP THR          
SEQRES  48 B  638  LYS ALA THR LEU LEU ILE TRP ARG ARG THR TRP CYS ARG          
SEQRES  49 B  638  LEU THR GLY GLN GLY THR GLU THR SER GLN VAL ALA PRO          
SEQRES  50 B  638  ALA                                                          
HET    V0S  A 701      34                                                       
HET    CLR  A 702      28                                                       
HET    NAG  A 703      14                                                       
HET     NA  A 704       1                                                       
HET     NA  A 705       1                                                       
HET    MPG  A 706      24                                                       
HET    V0S  B 701      34                                                       
HET    CLR  B 702      28                                                       
HETNAM     V0S 3-CHLORO-N-[TRANS-4-(METHYLAMINO)CYCLOHEXYL]-N-{[3-              
HETNAM   2 V0S  (PYRIDIN-4-YL)PHENYL]METHYL}-1-BENZOTHIOPHENE-2-                
HETNAM   3 V0S  CARBOXAMIDE                                                     
HETNAM     CLR CHOLESTEROL                                                      
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      NA SODIUM ION                                                       
HETNAM     MPG [(Z)-OCTADEC-9-ENYL] (2R)-2,3-BIS(OXIDANYL)PROPANOATE            
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
FORMUL   3  V0S    2(C28 H28 CL N3 O S)                                         
FORMUL   4  CLR    2(C27 H46 O)                                                 
FORMUL   5  NAG    C8 H15 N O6                                                  
FORMUL   6   NA    2(NA 1+)                                                     
FORMUL   8  MPG    C21 H40 O4                                                   
HELIX    1 AA1 LEU A   61  HIS A   63  5                                   3    
HELIX    2 AA2 SER A   98  SER A  110  1                                  13    
HELIX    3 AA3 GLY A  111  ASN A  114  5                                   4    
HELIX    4 AA4 ALA A  115  MET A  131  1                                  17    
HELIX    5 AA5 SER A  143  GLY A  152  1                                  10    
HELIX    6 AA6 CYS A  154  ARG A  161  1                                   8    
HELIX    7 AA7 PRO A  164  ARG A  168  5                                   5    
HELIX    8 AA8 ASN A  202  TRP A  206  5                                   5    
HELIX    9 AA9 THR A  223  ASP A  255  1                                  33    
HELIX   10 AB1 ASP A  255  ASN A  260  1                                   6    
HELIX   11 AB2 PRO A  263  ALA A  283  1                                  21    
HELIX   12 AB3 GLN A  284  MET A  286  5                                   3    
HELIX   13 AB4 GLY A  288  CYS A  295  1                                   8    
HELIX   14 AB5 LEU A  312  PHE A  343  1                                  32    
HELIX   15 AB6 LYS A  344  GLY A  347  5                                   4    
HELIX   16 AB7 LYS A  356  ALA A  379  1                                  24    
HELIX   17 AB8 ASN A  396  VAL A  404  1                                   9    
HELIX   18 AB9 VAL A  404  ALA A  453  1                                  50    
HELIX   19 AC1 ASN A  455  ALA A  476  1                                  22    
HELIX   20 AC2 SER A  488  GLY A  515  1                                  28    
HELIX   21 AC3 LYS A  516  TYR A  534  1                                  19    
HELIX   22 AC4 TYR A  534  LYS A  548  1                                  15    
HELIX   23 AC5 ASN A  550  ILE A  600  1                                  51    
HELIX   24 AC6 SER A  618  THR A  638  1                                  21    
HELIX   25 AC7 TRP A  639  TRP A  641  5                                   3    
HELIX   26 AC8 THR A  642  THR A  657  1                                  16    
HELIX   27 AC9 SER B   98  SER B  110  1                                  13    
HELIX   28 AD1 GLY B  111  ASN B  114  5                                   4    
HELIX   29 AD2 ALA B  115  MET B  131  1                                  17    
HELIX   30 AD3 SER B  143  GLY B  152  1                                  10    
HELIX   31 AD4 CYS B  154  ARG B  161  1                                   8    
HELIX   32 AD5 PRO B  164  ARG B  168  5                                   5    
HELIX   33 AD6 THR B  223  ASP B  255  1                                  33    
HELIX   34 AD7 ASP B  255  ASN B  260  1                                   6    
HELIX   35 AD8 PRO B  263  ALA B  283  1                                  21    
HELIX   36 AD9 GLN B  284  MET B  286  5                                   3    
HELIX   37 AE1 GLY B  288  CYS B  295  1                                   8    
HELIX   38 AE2 LEU B  312  PHE B  343  1                                  32    
HELIX   39 AE3 LYS B  356  ALA B  379  1                                  24    
HELIX   40 AE4 ASN B  396  VAL B  404  1                                   9    
HELIX   41 AE5 VAL B  404  ALA B  453  1                                  50    
HELIX   42 AE6 ASN B  455  ALA B  476  1                                  22    
HELIX   43 AE7 SER B  488  GLY B  515  1                                  28    
HELIX   44 AE8 LYS B  516  ILE B  535  1                                  20    
HELIX   45 AE9 ILE B  535  LYS B  548  1                                  14    
HELIX   46 AF1 ASN B  550  GLN B  595  1                                  46    
HELIX   47 AF2 SER B  618  THR B  638  1                                  21    
HELIX   48 AF3 TRP B  639  TRP B  641  5                                   3    
HELIX   49 AF4 THR B  642  ARG B  655  1                                  14    
SHEET    1 AA1 3 GLY A  65  ALA A  67  0                                        
SHEET    2 AA1 3 ARG A 138  GLU A 140 -1  O  VAL A 139   N  ARG A  66           
SHEET    3 AA1 3 CYS A 134  GLU A 135 -1  N  GLU A 135   O  ARG A 138           
SHEET    1 AA2 2 GLU A  71  PRO A  72  0                                        
SHEET    2 AA2 2 ALA A  87  THR A  88 -1  O  THR A  88   N  GLU A  71           
SHEET    1 AA3 2 VAL A  77  CYS A  78  0                                        
SHEET    2 AA3 2 SER A  81  VAL A  82 -1  O  SER A  81   N  CYS A  78           
SHEET    1 AA4 2 LEU A 197  ARG A 199  0                                        
SHEET    2 AA4 2 CYS A 213  ILE A 215 -1  O  GLY A 214   N  VAL A 198           
SHEET    1 AA5 2 VAL A 381  ASP A 384  0                                        
SHEET    2 AA5 2 ILE A 389  VAL A 392 -1  O  PHE A 391   N  ASP A 382           
SHEET    1 AA6 2 GLY B  65  ALA B  67  0                                        
SHEET    2 AA6 2 ARG B 138  GLU B 140 -1  O  VAL B 139   N  ARG B  66           
SHEET    1 AA7 2 GLU B  71  PRO B  72  0                                        
SHEET    2 AA7 2 ALA B  87  THR B  88 -1  O  THR B  88   N  GLU B  71           
SHEET    1 AA8 2 VAL B  77  CYS B  78  0                                        
SHEET    2 AA8 2 SER B  81  VAL B  82 -1  O  SER B  81   N  CYS B  78           
SHEET    1 AA9 2 LEU B 197  ARG B 199  0                                        
SHEET    2 AA9 2 CYS B 213  ILE B 215 -1  O  GLY B 214   N  VAL B 198           
SHEET    1 AB1 2 VAL B 381  ASP B 384  0                                        
SHEET    2 AB1 2 ILE B 389  VAL B 392 -1  O  PHE B 391   N  ASP B 382           
SSBOND   1 CYS A   64    CYS A  178                          1555   1555  2.06  
SSBOND   2 CYS A   70    CYS A  134                          1555   1555  2.09  
SSBOND   3 CYS A   78    CYS A  127                          1555   1555  2.05  
SSBOND   4 CYS A  118    CYS A  154                          1555   1555  2.08  
SSBOND   5 CYS A  147    CYS A  169                          1555   1555  2.10  
SSBOND   6 CYS A  193    CYS A  213                          1555   1555  2.03  
SSBOND   7 CYS A  217    CYS A  295                          1555   1555  2.03  
SSBOND   8 CYS A  314    CYS A  390                          1555   1555  2.06  
SSBOND   9 CYS A  594    CYS A  611                          1555   1555  2.07  
SSBOND  10 CYS B   64    CYS B  178                          1555   1555  2.07  
SSBOND  11 CYS B   70    CYS B  134                          1555   1555  2.07  
SSBOND  12 CYS B   78    CYS B  127                          1555   1555  2.04  
SSBOND  13 CYS B  118    CYS B  154                          1555   1555  2.06  
SSBOND  14 CYS B  147    CYS B  169                          1555   1555  2.04  
SSBOND  15 CYS B  193    CYS B  213                          1555   1555  2.05  
SSBOND  16 CYS B  217    CYS B  295                          1555   1555  2.04  
SSBOND  17 CYS B  314    CYS B  390                          1555   1555  2.04  
SSBOND  18 CYS B  594    CYS B  611                          1555   1555  2.05  
LINK         ND2 ASN A 188                 C1  NAG A 703     1555   1555  1.42  
LINK         O   THR A  90                NA    NA A 704     1555   1555  2.34  
LINK         O   ALA A  93                NA    NA A 704     1555   1555  2.32  
LINK         O   SER A  96                NA    NA A 704     1555   1555  2.67  
LINK         OE2 GLU A 305                NA    NA A 705     1555   1555  3.05  
LINK         O   THR A 307                NA    NA A 705     1555   1555  3.04  
CISPEP   1 VAL A  195    PRO A  196          0        12.06                     
CISPEP   2 TYR A  262    PRO A  263          0        -1.47                     
CISPEP   3 GLU A  305    PRO A  306          0         3.32                     
CISPEP   4 VAL B  195    PRO B  196          0        11.86                     
CISPEP   5 TYR B  262    PRO B  263          0        -1.57                     
CRYST1  122.860   63.150  208.060  90.00  96.29  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008139  0.000000  0.000897        0.00000                         
SCALE2      0.000000  0.015835  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004835        0.00000                         
ATOM      1  N   PRO A  58     -65.718 -40.261 111.918  1.00198.19           N  
ANISOU    1  N   PRO A  58    24814  25227  25261    280   -162    661       N  
ATOM      2  CA  PRO A  58     -66.193 -40.598 113.270  1.00199.39           C  
ANISOU    2  CA  PRO A  58    24917  25344  25496    471    -49    837       C  
ATOM      3  C   PRO A  58     -65.173 -40.135 114.351  1.00200.81           C  
ANISOU    3  C   PRO A  58    25266  25353  25677    799    -39    904       C  
ATOM      4  O   PRO A  58     -64.215 -39.437 114.013  1.00206.28           O  
ANISOU    4  O   PRO A  58    26097  25974  26304    870   -137    816       O  
ATOM      5  CB  PRO A  58     -66.358 -42.123 113.189  1.00199.01           C  
ANISOU    5  CB  PRO A  58    24824  25144  25647    194    149    767       C  
ATOM      6  CG  PRO A  58     -65.370 -42.558 112.151  1.00195.66           C  
ANISOU    6  CG  PRO A  58    24531  24537  25273    -32    175    536       C  
ATOM      7  CD  PRO A  58     -65.103 -41.411 111.223  1.00194.05           C  
ANISOU    7  CD  PRO A  58    24359  24500  24869    -18    -38    461       C  
ATOM      8  N   PRO A  59     -65.381 -40.463 115.650  1.00200.31           N  
ANISOU    8  N   PRO A  59    25180  25262  25667    994     70   1063       N  
ATOM      9  CA  PRO A  59     -64.241 -40.269 116.603  1.00193.89           C  
ANISOU    9  CA  PRO A  59    24516  24308  24844   1239     91   1099       C  
ATOM     10  C   PRO A  59     -62.984 -41.064 116.174  1.00187.65           C  
ANISOU   10  C   PRO A  59    23839  23270  24188   1111    172    989       C  
ATOM     11  O   PRO A  59     -63.094 -42.076 115.486  1.00197.30           O  
ANISOU   11  O   PRO A  59    25028  24374  25561    856    292    912       O  
ATOM     12  CB  PRO A  59     -64.803 -40.755 117.945  1.00192.50           C  
ANISOU   12  CB  PRO A  59    24256  24181  24704   1416    226   1302       C  
ATOM     13  CG  PRO A  59     -66.070 -41.488 117.620  1.00196.38           C  
ANISOU   13  CG  PRO A  59    24569  24751  25293   1217    314   1355       C  
ATOM     14  CD  PRO A  59     -66.607 -40.883 116.352  1.00196.66           C  
ANISOU   14  CD  PRO A  59    24548  24932  25240   1026    165   1232       C  
ATOM     15  N   PRO A  60     -61.788 -40.616 116.595  1.00169.35           N  
ANISOU   15  N   PRO A  60    21649  20877  21819   1281    123    979       N  
ATOM     16  CA  PRO A  60     -60.599 -40.885 115.768  1.00156.19           C  
ANISOU   16  CA  PRO A  60    20091  19028  20225   1152    128    841       C  
ATOM     17  C   PRO A  60     -60.207 -42.359 115.584  1.00145.19           C  
ANISOU   17  C   PRO A  60    18695  17408  19063   1001    357    846       C  
ATOM     18  O   PRO A  60     -59.971 -43.081 116.557  1.00143.13           O  
ANISOU   18  O   PRO A  60    18404  17071  18905   1135    515   1014       O  
ATOM     19  CB  PRO A  60     -59.491 -40.087 116.460  1.00156.07           C  
ANISOU   19  CB  PRO A  60    20177  19024  20099   1379     32    865       C  
ATOM     20  CG  PRO A  60     -59.980 -39.830 117.847  1.00158.95           C  
ANISOU   20  CG  PRO A  60    20488  19537  20368   1617     44   1026       C  
ATOM     21  CD  PRO A  60     -61.457 -40.088 117.925  1.00164.70           C  
ANISOU   21  CD  PRO A  60    21090  20368  21118   1574    100   1103       C  
ATOM     22  N   LEU A  61     -60.147 -42.787 114.324  1.00135.23           N  
ANISOU   22  N   LEU A  61    17460  16040  17878    724    394    666       N  
ATOM     23  CA  LEU A  61     -59.871 -44.189 113.966  1.00133.59           C  
ANISOU   23  CA  LEU A  61    17269  15577  17911    534    650    619       C  
ATOM     24  C   LEU A  61     -58.511 -44.652 114.526  1.00130.07           C  
ANISOU   24  C   LEU A  61    16902  14929  17586    712    785    728       C  
ATOM     25  O   LEU A  61     -57.513 -43.932 114.461  1.00125.84           O  
ANISOU   25  O   LEU A  61    16444  14420  16947    833    653    709       O  
ATOM     26  CB  LEU A  61     -59.874 -44.418 112.435  1.00136.53           C  
ANISOU   26  CB  LEU A  61    17685  15891  18297    199    653    355       C  
ATOM     27  CG  LEU A  61     -61.062 -44.113 111.497  1.00135.72           C  
ANISOU   27  CG  LEU A  61    17485  16015  18066    -60    530    212       C  
ATOM     28  CD1 LEU A  61     -60.711 -44.387 110.032  1.00132.76           C  
ANISOU   28  CD1 LEU A  61    17176  15587  17679   -372    548    -53       C  
ATOM     29  CD2 LEU A  61     -62.285 -44.935 111.880  1.00137.31           C  
ANISOU   29  CD2 LEU A  61    17545  16249  18375   -197    668    269       C  
ATOM     30  N   SER A  62     -58.516 -45.841 115.108  1.00128.05           N  
ANISOU   30  N   SER A  62    16607  14490  17553    733   1056    870       N  
ATOM     31  CA  SER A  62     -57.350 -46.434 115.739  1.00126.08           C  
ANISOU   31  CA  SER A  62    16387  14073  17441    927   1230   1049       C  
ATOM     32  C   SER A  62     -56.145 -46.619 114.811  1.00118.42           C  
ANISOU   32  C   SER A  62    15532  12907  16552    841   1289    915       C  
ATOM     33  O   SER A  62     -55.001 -46.494 115.253  1.00111.60           O  
ANISOU   33  O   SER A  62    14686  12034  15681   1046   1290   1051       O  
ATOM     34  CB  SER A  62     -57.746 -47.799 116.333  1.00138.78           C  
ANISOU   34  CB  SER A  62    17923  15480  19324    927   1567   1231       C  
ATOM     35  OG  SER A  62     -58.245 -48.691 115.342  1.00147.04           O  
ANISOU   35  OG  SER A  62    19003  16289  20575    593   1769   1028       O  
ATOM     36  N   HIS A  63     -56.415 -46.950 113.548  1.00116.16           N  
ANISOU   36  N   HIS A  63    15311  12490  16335    532   1350    654       N  
ATOM     37  CA  HIS A  63     -55.363 -47.182 112.540  1.00115.35           C  
ANISOU   37  CA  HIS A  63    15325  12192  16308    421   1436    495       C  
ATOM     38  C   HIS A  63     -54.752 -45.898 111.977  1.00111.50           C  
ANISOU   38  C   HIS A  63    14894  11892  15577    457   1133    384       C  
ATOM     39  O   HIS A  63     -53.613 -45.922 111.471  1.00110.91           O  
ANISOU   39  O   HIS A  63    14899  11696  15544    473   1178    341       O  
ATOM     40  CB  HIS A  63     -55.903 -48.023 111.395  1.00117.62           C  
ANISOU   40  CB  HIS A  63    15664  12293  16731     52   1626    227       C  
ATOM     41  CG  HIS A  63     -56.300 -49.396 111.815  1.00125.17           C  
ANISOU   41  CG  HIS A  63    16594  12974  17990    -16   1992    308       C  
ATOM     42  ND1 HIS A  63     -55.490 -50.495 111.622  1.00129.87           N  
ANISOU   42  ND1 HIS A  63    17272  13195  18875    -32   2357    319       N  
ATOM     43  CD2 HIS A  63     -57.408 -49.853 112.447  1.00129.89           C  
ANISOU   43  CD2 HIS A  63    17087  13596  18668    -59   2078    402       C  
ATOM     44  CE1 HIS A  63     -56.090 -51.571 112.104  1.00131.75           C  
ANISOU   44  CE1 HIS A  63    17466  13218  19373    -90   2662    412       C  
ATOM     45  NE2 HIS A  63     -57.254 -51.212 112.613  1.00131.00           N  
ANISOU   45  NE2 HIS A  63    17254  13366  19154   -114   2493    463       N  
ATOM     46  N   CYS A  64     -55.492 -44.788 112.101  1.00107.79           N  
ANISOU   46  N   CYS A  64    14378  11702  14873    486    851    361       N  
ATOM     47  CA  CYS A  64     -55.023 -43.458 111.725  1.00103.72           C  
ANISOU   47  CA  CYS A  64    13907  11360  14140    550    574    292       C  
ATOM     48  C   CYS A  64     -54.180 -42.745 112.783  1.00 99.46           C  
ANISOU   48  C   CYS A  64    13363  10914  13512    843    455    467       C  
ATOM     49  O   CYS A  64     -54.233 -41.540 112.903  1.00102.65           O  
ANISOU   49  O   CYS A  64    13777  11498  13728    925    224    444       O  
ATOM     50  CB  CYS A  64     -56.219 -42.584 111.354  1.00106.07           C  
ANISOU   50  CB  CYS A  64    14153  11899  14250    458    365    206       C  
ATOM     51  SG  CYS A  64     -56.543 -42.624 109.604  1.00119.89           S  
ANISOU   51  SG  CYS A  64    15931  13676  15943    112    338    -63       S  
ATOM     52  N   GLY A  65     -53.395 -43.475 113.555  1.00 97.42           N  
ANISOU   52  N   GLY A  65    13082  10545  13386    997    623    647       N  
ATOM     53  CA  GLY A  65     -52.579 -42.875 114.608  1.00 94.83           C  
ANISOU   53  CA  GLY A  65    12720  10365  12945   1250    509    816       C  
ATOM     54  C   GLY A  65     -51.730 -43.921 115.279  1.00 96.52           C  
ANISOU   54  C   GLY A  65    12876  10464  13331   1397    742   1048       C  
ATOM     55  O   GLY A  65     -51.926 -45.115 115.062  1.00 98.63           O  
ANISOU   55  O   GLY A  65    13137  10507  13830   1326   1017   1093       O  
ATOM     56  N   ARG A  66     -50.749 -43.471 116.040  1.00 98.78           N  
ANISOU   56  N   ARG A  66    13115  10906  13509   1590    646   1193       N  
ATOM     57  CA  ARG A  66     -49.763 -44.390 116.588  1.00105.19           C  
ANISOU   57  CA  ARG A  66    13845  11653  14470   1751    858   1454       C  
ATOM     58  C   ARG A  66     -49.338 -43.971 117.974  1.00103.92           C  
ANISOU   58  C   ARG A  66    13561  11802  14121   1989    740   1680       C  
ATOM     59  O   ARG A  66     -49.376 -42.794 118.343  1.00 96.73           O  
ANISOU   59  O   ARG A  66    12663  11132  12957   2009    472   1577       O  
ATOM     60  CB  ARG A  66     -48.540 -44.535 115.665  1.00110.89           C  
ANISOU   60  CB  ARG A  66    14618  12218  15296   1694    923   1400       C  
ATOM     61  CG  ARG A  66     -48.075 -45.970 115.525  1.00120.96           C  
ANISOU   61  CG  ARG A  66    15866  13214  16877   1739   1300   1575       C  
ATOM     62  CD  ARG A  66     -46.842 -46.069 114.652  1.00129.88           C  
ANISOU   62  CD  ARG A  66    17043  14203  18102   1708   1376   1535       C  
ATOM     63  NE  ARG A  66     -47.153 -45.927 113.234  1.00137.73           N  
ANISOU   63  NE  ARG A  66    18191  15012  19128   1440   1369   1201       N  
ATOM     64  CZ  ARG A  66     -46.238 -45.801 112.257  1.00149.17           C  
ANISOU   64  CZ  ARG A  66    19709  16356  20612   1366   1392   1090       C  
ATOM     65  NH1 ARG A  66     -44.925 -45.789 112.542  1.00149.84           N  
ANISOU   65  NH1 ARG A  66    19714  16494  20722   1542   1421   1295       N  
ATOM     66  NH2 ARG A  66     -46.634 -45.672 110.976  1.00151.20           N  
ANISOU   66  NH2 ARG A  66    20098  16489  20861   1113   1381    782       N  
ATOM     67  N   ALA A  67     -48.988 -44.980 118.756  1.00111.92           N  
ANISOU   67  N   ALA A  67    14451  12809  15263   2167    968   1993       N  
ATOM     68  CA  ALA A  67     -48.691 -44.816 120.170  1.00114.91           C  
ANISOU   68  CA  ALA A  67    14677  13526  15457   2402    900   2258       C  
ATOM     69  C   ALA A  67     -47.278 -44.272 120.314  1.00109.90           C  
ANISOU   69  C   ALA A  67    13977  13097  14683   2475    757   2320       C  
ATOM     70  O   ALA A  67     -46.305 -44.987 120.097  1.00107.73           O  
ANISOU   70  O   ALA A  67    13633  12723  14577   2549    935   2509       O  
ATOM     71  CB  ALA A  67     -48.835 -46.154 120.902  1.00121.14           C  
ANISOU   71  CB  ALA A  67    15335  14240  16450   2578   1225   2619       C  
ATOM     72  N   ALA A  68     -47.190 -43.007 120.699  1.00106.44           N  
ANISOU   72  N   ALA A  68    13554  12941  13945   2451    451   2162       N  
ATOM     73  CA  ALA A  68     -45.907 -42.343 120.893  1.00106.31           C  
ANISOU   73  CA  ALA A  68    13467  13163  13761   2477    280   2181       C  
ATOM     74  C   ALA A  68     -46.000 -41.308 121.999  1.00103.24           C  
ANISOU   74  C   ALA A  68    13029  13174  13022   2523     30   2126       C  
ATOM     75  O   ALA A  68     -47.020 -40.643 122.095  1.00 99.52           O  
ANISOU   75  O   ALA A  68    12667  12701  12441   2461    -75   1920       O  
ATOM     76  CB  ALA A  68     -45.489 -41.670 119.604  1.00107.28           C  
ANISOU   76  CB  ALA A  68    13734  13089  13936   2279    168   1896       C  
ATOM     77  N   PRO A  69     -44.938 -41.168 122.824  1.00103.57           N  
ANISOU   77  N   PRO A  69    12900  13572  12879   2625    -52   2306       N  
ATOM     78  CA  PRO A  69     -44.969 -40.189 123.914  1.00103.39           C  
ANISOU   78  CA  PRO A  69    12831  13960  12491   2638   -281   2218       C  
ATOM     79  C   PRO A  69     -44.967 -38.783 123.380  1.00101.29           C  
ANISOU   79  C   PRO A  69    12737  13645  12100   2432   -517   1817       C  
ATOM     80  O   PRO A  69     -44.184 -38.492 122.472  1.00103.66           O  
ANISOU   80  O   PRO A  69    13082  13800  12501   2311   -567   1711       O  
ATOM     81  CB  PRO A  69     -43.667 -40.463 124.659  1.00105.48           C  
ANISOU   81  CB  PRO A  69    12851  14608  12616   2751   -304   2505       C  
ATOM     82  CG  PRO A  69     -42.762 -41.052 123.639  1.00106.57           C  
ANISOU   82  CG  PRO A  69    12967  14493  13032   2731   -176   2612       C  
ATOM     83  CD  PRO A  69     -43.660 -41.909 122.803  1.00105.72           C  
ANISOU   83  CD  PRO A  69    12999  13911  13259   2730     69   2605       C  
ATOM     84  N   CYS A  70     -45.825 -37.915 123.904  1.00 99.37           N  
ANISOU   84  N   CYS A  70    12594  13503  11658   2401   -637   1605       N  
ATOM     85  CA  CYS A  70     -45.895 -36.535 123.393  1.00 99.32           C  
ANISOU   85  CA  CYS A  70    12765  13405  11566   2220   -820   1232       C  
ATOM     86  C   CYS A  70     -44.916 -35.622 124.072  1.00 97.21           C  
ANISOU   86  C   CYS A  70    12437  13474  11024   2142  -1009   1117       C  
ATOM     87  O   CYS A  70     -44.712 -35.708 125.244  1.00103.77           O  
ANISOU   87  O   CYS A  70    13130  14684  11613   2226  -1046   1231       O  
ATOM     88  CB  CYS A  70     -47.297 -35.943 123.559  1.00102.98           C  
ANISOU   88  CB  CYS A  70    13377  13780  11970   2223   -829   1046       C  
ATOM     89  SG  CYS A  70     -48.659 -36.618 122.565  1.00114.12           S  
ANISOU   89  SG  CYS A  70    14888  14799  13672   2228   -662   1066       S  
ATOM     90  N   GLU A  71     -44.327 -34.724 123.328  1.00 96.13           N  
ANISOU   90  N   GLU A  71    12399  13211  10916   1966  -1128    884       N  
ATOM     91  CA  GLU A  71     -43.535 -33.650 123.887  1.00 99.90           C  
ANISOU   91  CA  GLU A  71    12856  13956  11142   1830  -1310    686       C  
ATOM     92  C   GLU A  71     -44.150 -32.319 123.431  1.00 99.25           C  
ANISOU   92  C   GLU A  71    13016  13631  11061   1688  -1380    313       C  
ATOM     93  O   GLU A  71     -44.618 -32.185 122.284  1.00 99.89           O  
ANISOU   93  O   GLU A  71    13237  13340  11375   1651  -1328    238       O  
ATOM     94  CB  GLU A  71     -42.044 -33.769 123.500  1.00105.35           C  
ANISOU   94  CB  GLU A  71    13404  14751  11872   1742  -1374    784       C  
ATOM     95  CG  GLU A  71     -41.735 -34.003 122.025  1.00107.62           C  
ANISOU   95  CG  GLU A  71    13768  14647  12474   1684  -1304    793       C  
ATOM     96  CD  GLU A  71     -40.260 -34.323 121.768  1.00114.50           C  
ANISOU   96  CD  GLU A  71    14457  15660  13386   1647  -1329    965       C  
ATOM     97  OE1 GLU A  71     -39.904 -35.506 121.600  1.00118.48           O  
ANISOU   97  OE1 GLU A  71    14825  16150  14041   1792  -1178   1279       O  
ATOM     98  OE2 GLU A  71     -39.426 -33.402 121.751  1.00119.82           O  
ANISOU   98  OE2 GLU A  71    15114  16461  13951   1474  -1484    797       O  
ATOM     99  N   PRO A  72     -44.159 -31.305 124.312  1.00 98.76           N  
ANISOU   99  N   PRO A  72    13003  13783  10738   1606  -1482     76       N  
ATOM    100  CA  PRO A  72     -44.662 -29.998 123.869  1.00 97.25           C  
ANISOU  100  CA  PRO A  72    13044  13323  10581   1481  -1508   -263       C  
ATOM    101  C   PRO A  72     -43.846 -29.383 122.711  1.00 94.50           C  
ANISOU  101  C   PRO A  72    12763  12726  10416   1304  -1563   -386       C  
ATOM    102  O   PRO A  72     -42.643 -29.646 122.562  1.00 98.75           O  
ANISOU  102  O   PRO A  72    13160  13405  10955   1221  -1633   -294       O  
ATOM    103  CB  PRO A  72     -44.536 -29.145 125.124  1.00 99.48           C  
ANISOU  103  CB  PRO A  72    13341  13920  10537   1402  -1587   -493       C  
ATOM    104  CG  PRO A  72     -43.397 -29.756 125.856  1.00101.51           C  
ANISOU  104  CG  PRO A  72    13346  14624  10596   1380  -1679   -314       C  
ATOM    105  CD  PRO A  72     -43.527 -31.223 125.633  1.00100.18           C  
ANISOU  105  CD  PRO A  72    13024  14456  10583   1589  -1577     90       C  
ATOM    106  N   LEU A  73     -44.492 -28.563 121.919  1.00 88.92           N  
ANISOU  106  N   LEU A  73    12253  11674   9859   1259  -1523   -566       N  
ATOM    107  CA  LEU A  73     -43.830 -27.980 120.775  1.00 86.35           C  
ANISOU  107  CA  LEU A  73    11992  11099   9716   1112  -1554   -655       C  
ATOM    108  C   LEU A  73     -42.810 -26.943 121.158  1.00 86.85           C  
ANISOU  108  C   LEU A  73    12063  11278   9656    901  -1660   -888       C  
ATOM    109  O   LEU A  73     -43.071 -26.157 122.004  1.00 88.25           O  
ANISOU  109  O   LEU A  73    12321  11547   9661    845  -1671  -1110       O  
ATOM    110  CB  LEU A  73     -44.863 -27.330 119.845  1.00 85.27           C  
ANISOU  110  CB  LEU A  73    12047  10589   9760   1140  -1470   -752       C  
ATOM    111  CG  LEU A  73     -45.447 -28.290 118.829  1.00 83.20           C  
ANISOU  111  CG  LEU A  73    11761  10157   9694   1246  -1392   -538       C  
ATOM    112  CD1 LEU A  73     -46.824 -27.811 118.428  1.00 82.72           C  
ANISOU  112  CD1 LEU A  73    11835   9888   9708   1329  -1310   -589       C  
ATOM    113  CD2 LEU A  73     -44.515 -28.344 117.620  1.00 83.94           C  
ANISOU  113  CD2 LEU A  73    11834  10101   9958   1135  -1415   -496       C  
ATOM    114  N   ARG A  74     -41.672 -26.939 120.487  1.00 88.40           N  
ANISOU  114  N   ARG A  74    12181  11455   9952    773  -1720   -847       N  
ATOM    115  CA  ARG A  74     -40.641 -25.921 120.625  1.00 93.62           C  
ANISOU  115  CA  ARG A  74    12842  12182  10546    531  -1815  -1068       C  
ATOM    116  C   ARG A  74     -40.678 -24.799 119.621  1.00 92.41           C  
ANISOU  116  C   ARG A  74    12874  11634  10601    408  -1771  -1256       C  
ATOM    117  O   ARG A  74     -39.931 -23.814 119.782  1.00 93.84           O  
ANISOU  117  O   ARG A  74    13086  11823  10747    185  -1823  -1482       O  
ATOM    118  CB  ARG A  74     -39.269 -26.577 120.589  1.00 99.75           C  
ANISOU  118  CB  ARG A  74    13380  13227  11294    462  -1908   -880       C  
ATOM    119  CG  ARG A  74     -39.008 -27.281 121.917  1.00109.68           C  
ANISOU  119  CG  ARG A  74    14432  14975  12266    526  -1973   -751       C  
ATOM    120  CD  ARG A  74     -37.576 -27.624 122.169  1.00117.29           C  
ANISOU  120  CD  ARG A  74    15132  16303  13128    422  -2084   -604       C  
ATOM    121  NE  ARG A  74     -37.550 -28.602 123.235  1.00123.30           N  
ANISOU  121  NE  ARG A  74    15679  17498  13668    580  -2098   -356       N  
ATOM    122  CZ  ARG A  74     -37.583 -29.930 123.089  1.00126.70           C  
ANISOU  122  CZ  ARG A  74    15967  17969  14202    815  -2003     22       C  
ATOM    123  NH1 ARG A  74     -37.567 -30.676 124.198  1.00138.88           N  
ANISOU  123  NH1 ARG A  74    17311  19936  15521    954  -2009    245       N  
ATOM    124  NH2 ARG A  74     -37.596 -30.540 121.895  1.00118.49           N  
ANISOU  124  NH2 ARG A  74    14972  16573  13475    910  -1886    188       N  
ATOM    125  N   TYR A  75     -41.501 -24.958 118.573  1.00 91.04           N  
ANISOU  125  N   TYR A  75    12807  11140  10642    539  -1671  -1152       N  
ATOM    126  CA  TYR A  75     -41.788 -23.900 117.567  1.00 90.43           C  
ANISOU  126  CA  TYR A  75    12907  10683  10768    479  -1598  -1275       C  
ATOM    127  C   TYR A  75     -43.269 -23.783 117.402  1.00 87.98           C  
ANISOU  127  C   TYR A  75    12732  10183  10514    657  -1484  -1259       C  
ATOM    128  O   TYR A  75     -43.960 -24.806 117.332  1.00 89.16           O  
ANISOU  128  O   TYR A  75    12820  10398  10657    820  -1460  -1068       O  
ATOM    129  CB  TYR A  75     -41.181 -24.246 116.254  1.00 90.10           C  
ANISOU  129  CB  TYR A  75    12811  10500  10922    455  -1598  -1110       C  
ATOM    130  CG  TYR A  75     -39.765 -24.683 116.403  1.00 95.59           C  
ANISOU  130  CG  TYR A  75    13323  11428  11566    333  -1699  -1040       C  
ATOM    131  CD1 TYR A  75     -38.725 -23.753 116.561  1.00 99.73           C  
ANISOU  131  CD1 TYR A  75    13832  11986  12074    102  -1766  -1214       C  
ATOM    132  CD2 TYR A  75     -39.451 -26.032 116.429  1.00 99.47           C  
ANISOU  132  CD2 TYR A  75    13646  12115  12033    444  -1711   -789       C  
ATOM    133  CE1 TYR A  75     -37.405 -24.165 116.698  1.00103.39           C  
ANISOU  133  CE1 TYR A  75    14090  12708  12482    -10  -1865  -1120       C  
ATOM    134  CE2 TYR A  75     -38.140 -26.464 116.610  1.00103.52           C  
ANISOU  134  CE2 TYR A  75    13962  12870  12500    362  -1786   -678       C  
ATOM    135  CZ  TYR A  75     -37.123 -25.535 116.730  1.00105.45           C  
ANISOU  135  CZ  TYR A  75    14170  13183  12713    137  -1874   -835       C  
ATOM    136  OH  TYR A  75     -35.849 -26.022 116.896  1.00110.02           O  
ANISOU  136  OH  TYR A  75    14520  14041  13240     68  -1950   -687       O  
ATOM    137  N   ASN A  76     -43.777 -22.558 117.391  1.00 87.37           N  
ANISOU  137  N   ASN A  76    12828   9874  10494    629  -1398  -1450       N  
ATOM    138  CA  ASN A  76     -45.230 -22.330 117.250  1.00 87.11           C  
ANISOU  138  CA  ASN A  76    12910   9670  10517    816  -1273  -1414       C  
ATOM    139  C   ASN A  76     -45.705 -22.469 115.805  1.00 84.08           C  
ANISOU  139  C   ASN A  76    12532   9073  10339    902  -1220  -1217       C  
ATOM    140  O   ASN A  76     -46.882 -22.555 115.550  1.00 82.17           O  
ANISOU  140  O   ASN A  76    12323   8763  10135   1062  -1141  -1116       O  
ATOM    141  CB  ASN A  76     -45.683 -20.993 117.842  1.00 91.61           C  
ANISOU  141  CB  ASN A  76    13662  10067  11079    791  -1155  -1669       C  
ATOM    142  CG  ASN A  76     -44.821 -19.801 117.414  1.00 96.77           C  
ANISOU  142  CG  ASN A  76    14413  10484  11869    590  -1119  -1853       C  
ATOM    143  OD1 ASN A  76     -44.036 -19.881 116.454  1.00 96.91           O  
ANISOU  143  OD1 ASN A  76    14368  10431  12022    499  -1171  -1752       O  
ATOM    144  ND2 ASN A  76     -44.926 -18.674 118.181  1.00102.28           N  
ANISOU  144  ND2 ASN A  76    15269  11056  12534    503  -1010  -2145       N  
ATOM    145  N   VAL A  77     -44.751 -22.544 114.884  1.00 83.95           N  
ANISOU  145  N   VAL A  77    12463   9000  10434    789  -1270  -1155       N  
ATOM    146  CA  VAL A  77     -44.943 -22.402 113.457  1.00 81.32           C  
ANISOU  146  CA  VAL A  77    12145   8474  10279    818  -1221  -1013       C  
ATOM    147  C   VAL A  77     -44.244 -23.558 112.699  1.00 80.59           C  
ANISOU  147  C   VAL A  77    11915   8494  10208    783  -1294   -846       C  
ATOM    148  O   VAL A  77     -43.102 -23.958 113.006  1.00 80.09           O  
ANISOU  148  O   VAL A  77    11762   8565  10102    675  -1372   -862       O  
ATOM    149  CB  VAL A  77     -44.424 -21.027 113.027  1.00 82.76           C  
ANISOU  149  CB  VAL A  77    12435   8407  10601    704  -1159  -1134       C  
ATOM    150  CG1 VAL A  77     -42.894 -20.868 113.152  1.00 85.41           C  
ANISOU  150  CG1 VAL A  77    12715   8798  10938    485  -1247  -1240       C  
ATOM    151  CG2 VAL A  77     -44.814 -20.740 111.624  1.00 84.02           C  
ANISOU  151  CG2 VAL A  77    12611   8386  10925    772  -1085   -963       C  
ATOM    152  N   CYS A  78     -44.944 -24.082 111.691  1.00 80.34           N  
ANISOU  152  N   CYS A  78    11862   8421  10242    870  -1253   -686       N  
ATOM    153  CA  CYS A  78     -44.405 -25.091 110.769  1.00 78.77           C  
ANISOU  153  CA  CYS A  78    11567   8275  10085    833  -1275   -551       C  
ATOM    154  C   CYS A  78     -44.422 -24.551 109.344  1.00 75.63           C  
ANISOU  154  C   CYS A  78    11202   7728   9805    807  -1231   -481       C  
ATOM    155  O   CYS A  78     -45.497 -24.280 108.783  1.00 72.69           O  
ANISOU  155  O   CYS A  78    10861   7309   9449    894  -1178   -411       O  
ATOM    156  CB  CYS A  78     -45.207 -26.365 110.852  1.00 80.59           C  
ANISOU  156  CB  CYS A  78    11732   8627  10261    927  -1253   -445       C  
ATOM    157  SG  CYS A  78     -44.456 -27.665 109.877  1.00 84.56           S  
ANISOU  157  SG  CYS A  78    12138   9165  10823    867  -1233   -325       S  
ATOM    158  N   LEU A  79     -43.208 -24.338 108.815  1.00 75.73           N  
ANISOU  158  N   LEU A  79    11190   7694   9887    690  -1253   -483       N  
ATOM    159  CA  LEU A  79     -42.959 -23.755 107.480  1.00 75.84           C  
ANISOU  159  CA  LEU A  79    11223   7580  10010    652  -1210   -408       C  
ATOM    160  C   LEU A  79     -43.842 -22.531 107.179  1.00 75.54           C  
ANISOU  160  C   LEU A  79    11279   7385  10036    725  -1135   -394       C  
ATOM    161  O   LEU A  79     -44.560 -22.453 106.167  1.00 73.64           O  
ANISOU  161  O   LEU A  79    11027   7139   9812    796  -1086   -258       O  
ATOM    162  CB  LEU A  79     -43.129 -24.819 106.401  1.00 74.79           C  
ANISOU  162  CB  LEU A  79    11024   7532   9858    666  -1190   -281       C  
ATOM    163  CG  LEU A  79     -42.180 -26.006 106.536  1.00 74.31           C  
ANISOU  163  CG  LEU A  79    10879   7574   9781    613  -1209   -266       C  
ATOM    164  CD1 LEU A  79     -42.812 -27.230 105.888  1.00 75.33           C  
ANISOU  164  CD1 LEU A  79    10972   7778   9871    645  -1154   -197       C  
ATOM    165  CD2 LEU A  79     -40.830 -25.683 105.915  1.00 74.35           C  
ANISOU  165  CD2 LEU A  79    10851   7529   9869    510  -1211   -243       C  
ATOM    166  N   GLY A  80     -43.780 -21.582 108.091  1.00 75.70           N  
ANISOU  166  N   GLY A  80    11383   7293  10086    707  -1113   -533       N  
ATOM    167  CA  GLY A  80     -44.478 -20.331 107.898  1.00 77.15           C  
ANISOU  167  CA  GLY A  80    11667   7274  10371    784   -996   -521       C  
ATOM    168  C   GLY A  80     -45.818 -20.249 108.570  1.00 76.42           C  
ANISOU  168  C   GLY A  80    11619   7199  10216    942   -941   -526       C  
ATOM    169  O   GLY A  80     -46.245 -19.119 108.915  1.00 79.98           O  
ANISOU  169  O   GLY A  80    12178   7455  10753   1000   -821   -584       O  
ATOM    170  N   SER A  81     -46.472 -21.395 108.789  1.00 72.87           N  
ANISOU  170  N   SER A  81    11092   6957   9638   1010  -1003   -468       N  
ATOM    171  CA  SER A  81     -47.848 -21.390 109.301  1.00 72.62           C  
ANISOU  171  CA  SER A  81    11075   6968   9547   1172   -947   -430       C  
ATOM    172  C   SER A  81     -47.937 -21.823 110.765  1.00 71.37           C  
ANISOU  172  C   SER A  81    10935   6914   9267   1181   -985   -579       C  
ATOM    173  O   SER A  81     -47.389 -22.840 111.136  1.00 70.63           O  
ANISOU  173  O   SER A  81    10768   6979   9087   1113  -1079   -602       O  
ATOM    174  CB  SER A  81     -48.756 -22.259 108.412  1.00 72.36           C  
ANISOU  174  CB  SER A  81    10930   7103   9461   1244   -966   -236       C  
ATOM    175  OG  SER A  81     -48.600 -21.977 107.009  1.00 74.47           O  
ANISOU  175  OG  SER A  81    11156   7344   9792   1221   -947    -92       O  
ATOM    176  N   VAL A  82     -48.626 -21.032 111.580  1.00 72.06           N  
ANISOU  176  N   VAL A  82    11117   6912   9349   1277   -891   -665       N  
ATOM    177  CA  VAL A  82     -48.851 -21.342 112.990  1.00 71.79           C  
ANISOU  177  CA  VAL A  82    11104   6999   9173   1304   -909   -802       C  
ATOM    178  C   VAL A  82     -49.773 -22.548 113.146  1.00 70.79           C  
ANISOU  178  C   VAL A  82    10866   7084   8944   1414   -946   -659       C  
ATOM    179  O   VAL A  82     -50.716 -22.700 112.392  1.00 69.58           O  
ANISOU  179  O   VAL A  82    10662   6943   8832   1513   -906   -490       O  
ATOM    180  CB  VAL A  82     -49.304 -20.085 113.771  1.00 72.96           C  
ANISOU  180  CB  VAL A  82    11404   6967   9349   1367   -764   -960       C  
ATOM    181  CG1 VAL A  82     -50.630 -19.582 113.325  1.00 74.27           C  
ANISOU  181  CG1 VAL A  82    11591   7027   9600   1573   -619   -798       C  
ATOM    182  CG2 VAL A  82     -49.392 -20.326 115.243  1.00 73.54           C  
ANISOU  182  CG2 VAL A  82    11506   7191   9244   1370   -782  -1134       C  
ATOM    183  N   LEU A  83     -49.470 -23.400 114.124  1.00 72.57           N  
ANISOU  183  N   LEU A  83    11041   7495   9037   1387  -1018   -717       N  
ATOM    184  CA  LEU A  83     -50.121 -24.713 114.287  1.00 74.02           C  
ANISOU  184  CA  LEU A  83    11108   7868   9147   1459  -1045   -578       C  
ATOM    185  C   LEU A  83     -51.295 -24.705 115.251  1.00 76.09           C  
ANISOU  185  C   LEU A  83    11381   8210   9318   1613   -976   -571       C  
ATOM    186  O   LEU A  83     -51.213 -24.090 116.285  1.00 78.11           O  
ANISOU  186  O   LEU A  83    11719   8469   9490   1635   -945   -722       O  
ATOM    187  CB  LEU A  83     -49.123 -25.758 114.805  1.00 73.78           C  
ANISOU  187  CB  LEU A  83    10990   8000   9041   1373  -1132   -584       C  
ATOM    188  CG  LEU A  83     -47.952 -25.941 113.866  1.00 73.06           C  
ANISOU  188  CG  LEU A  83    10865   7853   9040   1236  -1188   -564       C  
ATOM    189  CD1 LEU A  83     -47.045 -26.976 114.473  1.00 72.13           C  
ANISOU  189  CD1 LEU A  83    10642   7908   8852   1192  -1244   -528       C  
ATOM    190  CD2 LEU A  83     -48.405 -26.365 112.484  1.00 72.19           C  
ANISOU  190  CD2 LEU A  83    10719   7678   9032   1234  -1160   -428       C  
ATOM    191  N   PRO A  84     -52.364 -25.464 114.933  1.00 77.17           N  
ANISOU  191  N   PRO A  84    11426   8434   9459   1703   -950   -404       N  
ATOM    192  CA  PRO A  84     -53.523 -25.515 115.797  1.00 79.81           C  
ANISOU  192  CA  PRO A  84    11749   8858   9716   1856   -877   -366       C  
ATOM    193  C   PRO A  84     -53.381 -26.393 117.060  1.00 81.97           C  
ANISOU  193  C   PRO A  84    11971   9321   9851   1880   -901   -385       C  
ATOM    194  O   PRO A  84     -54.329 -26.430 117.854  1.00 89.39           O  
ANISOU  194  O   PRO A  84    12900  10348  10714   2014   -832   -352       O  
ATOM    195  CB  PRO A  84     -54.626 -26.058 114.879  1.00 78.88           C  
ANISOU  195  CB  PRO A  84    11520   8792   9658   1903   -854   -169       C  
ATOM    196  CG  PRO A  84     -53.934 -26.839 113.837  1.00 77.07           C  
ANISOU  196  CG  PRO A  84    11226   8568   9489   1749   -930   -126       C  
ATOM    197  CD  PRO A  84     -52.553 -26.276 113.713  1.00 76.11           C  
ANISOU  197  CD  PRO A  84    11191   8328   9398   1645   -979   -257       C  
ATOM    198  N   TYR A  85     -52.239 -27.042 117.265  1.00 79.45           N  
ANISOU  198  N   TYR A  85    11610   9079   9498   1771   -982   -413       N  
ATOM    199  CA  TYR A  85     -52.025 -27.896 118.430  1.00 79.87           C  
ANISOU  199  CA  TYR A  85    11586   9342   9417   1809   -997   -381       C  
ATOM    200  C   TYR A  85     -50.832 -27.352 119.205  1.00 82.01           C  
ANISOU  200  C   TYR A  85    11900   9692   9566   1723  -1064   -549       C  
ATOM    201  O   TYR A  85     -50.266 -26.364 118.797  1.00 82.37           O  
ANISOU  201  O   TYR A  85    12042   9596   9659   1626  -1087   -696       O  
ATOM    202  CB  TYR A  85     -51.838 -29.398 118.032  1.00 78.12           C  
ANISOU  202  CB  TYR A  85    11228   9186   9266   1779  -1001   -199       C  
ATOM    203  CG  TYR A  85     -51.060 -29.622 116.762  1.00 75.59           C  
ANISOU  203  CG  TYR A  85    10899   8736   9085   1645  -1039   -184       C  
ATOM    204  CD1 TYR A  85     -51.675 -29.452 115.525  1.00 74.37           C  
ANISOU  204  CD1 TYR A  85    10763   8452   9043   1609  -1018   -154       C  
ATOM    205  CD2 TYR A  85     -49.725 -29.981 116.795  1.00 75.02           C  
ANISOU  205  CD2 TYR A  85    10787   8701   9014   1560  -1090   -188       C  
ATOM    206  CE1 TYR A  85     -50.980 -29.593 114.345  1.00 73.53           C  
ANISOU  206  CE1 TYR A  85    10655   8246   9037   1487  -1044   -153       C  
ATOM    207  CE2 TYR A  85     -49.011 -30.159 115.623  1.00 75.33           C  
ANISOU  207  CE2 TYR A  85    10823   8619   9178   1448  -1106   -175       C  
ATOM    208  CZ  TYR A  85     -49.636 -29.962 114.379  1.00 74.76           C  
ANISOU  208  CZ  TYR A  85    10788   8407   9208   1408  -1081   -168       C  
ATOM    209  OH  TYR A  85     -48.913 -30.138 113.186  1.00 71.85           O  
ANISOU  209  OH  TYR A  85    10418   7939   8941   1294  -1089   -162       O  
ATOM    210  N   GLY A  86     -50.477 -28.008 120.326  1.00 83.52           N  
ANISOU  210  N   GLY A  86    12005  10131   9597   1754  -1091   -514       N  
ATOM    211  CA  GLY A  86     -49.307 -27.690 121.147  1.00 84.65           C  
ANISOU  211  CA  GLY A  86    12132  10453   9577   1656  -1175   -644       C  
ATOM    212  C   GLY A  86     -48.314 -28.819 121.434  1.00 86.50           C  
ANISOU  212  C   GLY A  86    12192  10911   9762   1632  -1237   -475       C  
ATOM    213  O   GLY A  86     -47.292 -28.557 122.064  1.00 91.54           O  
ANISOU  213  O   GLY A  86    12782  11747  10251   1538  -1323   -560       O  
ATOM    214  N   ALA A  87     -48.557 -30.056 120.994  1.00 86.78           N  
ANISOU  214  N   ALA A  87    12123  10925   9923   1707  -1183   -236       N  
ATOM    215  CA  ALA A  87     -47.617 -31.170 121.256  1.00 88.69           C  
ANISOU  215  CA  ALA A  87    12195  11348  10156   1717  -1193    -36       C  
ATOM    216  C   ALA A  87     -47.321 -31.989 120.008  1.00 89.86           C  
ANISOU  216  C   ALA A  87    12308  11287  10545   1679  -1139     98       C  
ATOM    217  O   ALA A  87     -48.221 -32.184 119.167  1.00 89.75           O  
ANISOU  217  O   ALA A  87    12357  11063  10679   1688  -1069    110       O  
ATOM    218  CB  ALA A  87     -48.172 -32.083 122.311  1.00 89.50           C  
ANISOU  218  CB  ALA A  87    12183  11671  10151   1878  -1120    154       C  
ATOM    219  N   THR A  88     -46.092 -32.531 119.927  1.00 90.11           N  
ANISOU  219  N   THR A  88    12225  11407  10603   1642  -1159    212       N  
ATOM    220  CA  THR A  88     -45.575 -33.188 118.710  1.00 87.13           C  
ANISOU  220  CA  THR A  88    11830  10826  10447   1588  -1097    304       C  
ATOM    221  C   THR A  88     -44.791 -34.465 119.008  1.00 84.97           C  
ANISOU  221  C   THR A  88    11384  10671  10228   1671  -1004    570       C  
ATOM    222  O   THR A  88     -44.684 -34.836 120.130  1.00 85.46           O  
ANISOU  222  O   THR A  88    11326  10989  10153   1777   -999    707       O  
ATOM    223  CB  THR A  88     -44.739 -32.175 117.864  1.00 87.79           C  
ANISOU  223  CB  THR A  88    11990  10794  10570   1429  -1197    132       C  
ATOM    224  OG1 THR A  88     -44.235 -32.802 116.659  1.00 88.17           O  
ANISOU  224  OG1 THR A  88    12025  10659  10815   1381  -1126    215       O  
ATOM    225  CG2 THR A  88     -43.584 -31.615 118.643  1.00 89.73           C  
ANISOU  225  CG2 THR A  88    12155  11284  10655   1363  -1317     83       C  
ATOM    226  N   SER A  89     -44.267 -35.123 117.989  1.00 84.28           N  
ANISOU  226  N   SER A  89    11283  10398  10341   1635   -912    653       N  
ATOM    227  CA  SER A  89     -43.483 -36.350 118.142  1.00 87.82           C  
ANISOU  227  CA  SER A  89    11575  10900  10891   1731   -774    924       C  
ATOM    228  C   SER A  89     -42.541 -36.524 116.924  1.00 90.90           C  
ANISOU  228  C   SER A  89    11979  11100  11457   1642   -725    923       C  
ATOM    229  O   SER A  89     -42.953 -36.327 115.722  1.00 93.25           O  
ANISOU  229  O   SER A  89    12417  11135  11876   1532   -699    766       O  
ATOM    230  CB  SER A  89     -44.429 -37.589 118.278  1.00 88.49           C  
ANISOU  230  CB  SER A  89    11641  10869  11112   1847   -566   1090       C  
ATOM    231  OG  SER A  89     -43.757 -38.842 118.454  1.00 86.31           O  
ANISOU  231  OG  SER A  89    11220  10597  10974   1967   -374   1381       O  
ATOM    232  N   THR A  90     -41.303 -36.921 117.207  1.00 90.14           N  
ANISOU  232  N   THR A  90    11722  11159  11365   1696   -701   1115       N  
ATOM    233  CA  THR A  90     -40.318 -37.138 116.164  1.00 92.97           C  
ANISOU  233  CA  THR A  90    12070  11367  11886   1638   -633   1149       C  
ATOM    234  C   THR A  90     -40.221 -38.651 115.830  1.00 96.42           C  
ANISOU  234  C   THR A  90    12452  11626  12557   1762   -343   1387       C  
ATOM    235  O   THR A  90     -39.101 -39.206 115.565  1.00 98.19           O  
ANISOU  235  O   THR A  90    12560  11851  12894   1821   -227   1577       O  
ATOM    236  CB  THR A  90     -38.941 -36.529 116.559  1.00 95.57           C  
ANISOU  236  CB  THR A  90    12249  11972  12090   1601   -781   1207       C  
ATOM    237  OG1 THR A  90     -38.593 -36.913 117.885  1.00100.12           O  
ANISOU  237  OG1 THR A  90    12622  12905  12514   1733   -799   1434       O  
ATOM    238  CG2 THR A  90     -38.960 -35.002 116.510  1.00 95.59           C  
ANISOU  238  CG2 THR A  90    12354  12025  11937   1423  -1015    912       C  
ATOM    239  N   LEU A  91     -41.385 -39.321 115.858  1.00 93.71           N  
ANISOU  239  N   LEU A  91    12185  11123  12298   1801   -206   1382       N  
ATOM    240  CA  LEU A  91     -41.501 -40.737 115.520  1.00 93.23           C  
ANISOU  240  CA  LEU A  91    12109  10828  12485   1884    102   1553       C  
ATOM    241  C   LEU A  91     -41.677 -40.861 114.024  1.00 92.51           C  
ANISOU  241  C   LEU A  91    12182  10411  12554   1724    200   1345       C  
ATOM    242  O   LEU A  91     -41.102 -41.764 113.399  1.00 97.53           O  
ANISOU  242  O   LEU A  91    12812  10849  13396   1749    441   1442       O  
ATOM    243  CB  LEU A  91     -42.698 -41.393 116.232  1.00 90.96           C  
ANISOU  243  CB  LEU A  91    11822  10518  12220   1966    214   1629       C  
ATOM    244  CG  LEU A  91     -43.001 -42.886 115.920  1.00 91.01           C  
ANISOU  244  CG  LEU A  91    11845  10217  12514   2010    567   1756       C  
ATOM    245  CD1 LEU A  91     -41.875 -43.828 116.337  1.00 94.07           C  
ANISOU  245  CD1 LEU A  91    12043  10678  13018   2244    794   2154       C  
ATOM    246  CD2 LEU A  91     -44.295 -43.337 116.574  1.00 89.88           C  
ANISOU  246  CD2 LEU A  91    11787   9970  12392   1953    611   1649       C  
ATOM    247  N   LEU A  92     -42.498 -39.986 113.459  1.00 87.96           N  
ANISOU  247  N   LEU A  92    11747   9789  11881   1569     35   1072       N  
ATOM    248  CA  LEU A  92     -42.860 -40.097 112.062  1.00 86.32           C  
ANISOU  248  CA  LEU A  92    11684   9334  11779   1406    113    872       C  
ATOM    249  C   LEU A  92     -41.709 -39.770 111.106  1.00 88.95           C  
ANISOU  249  C   LEU A  92    12034   9609  12152   1340    105    828       C  
ATOM    250  O   LEU A  92     -41.656 -40.304 109.981  1.00 85.72           O  
ANISOU  250  O   LEU A  92    11709   8986  11871   1245    270    738       O  
ATOM    251  CB  LEU A  92     -44.055 -39.196 111.792  1.00 83.52           C  
ANISOU  251  CB  LEU A  92    11434   9008  11289   1288    -66    649       C  
ATOM    252  CG  LEU A  92     -45.334 -39.544 112.527  1.00 82.44           C  
ANISOU  252  CG  LEU A  92    11289   8906  11127   1332    -37    672       C  
ATOM    253  CD1 LEU A  92     -46.488 -38.863 111.823  1.00 81.37           C  
ANISOU  253  CD1 LEU A  92    11254   8750  10911   1193   -151    461       C  
ATOM    254  CD2 LEU A  92     -45.565 -41.050 112.592  1.00 83.30           C  
ANISOU  254  CD2 LEU A  92    11366   8843  11439   1368    255    801       C  
ATOM    255  N   ALA A  93     -40.809 -38.887 111.568  1.00 92.83           N  
ANISOU  255  N   ALA A  93    12443  10303  12523   1375    -82    880       N  
ATOM    256  CA  ALA A  93     -39.595 -38.510 110.849  1.00 94.84           C  
ANISOU  256  CA  ALA A  93    12676  10548  12809   1328   -105    883       C  
ATOM    257  C   ALA A  93     -38.461 -39.434 111.299  1.00100.41           C  
ANISOU  257  C   ALA A  93    13216  11303  13632   1484     71   1171       C  
ATOM    258  O   ALA A  93     -38.003 -39.350 112.466  1.00108.56           O  
ANISOU  258  O   ALA A  93    14084  12595  14566   1600    -12   1359       O  
ATOM    259  CB  ALA A  93     -39.235 -37.057 111.148  1.00 94.70           C  
ANISOU  259  CB  ALA A  93    12643  10724  12613   1259   -388    785       C  
ATOM    260  N   GLY A  94     -38.024 -40.328 110.400  1.00 98.61           N  
ANISOU  260  N   GLY A  94    13020  10845  13601   1493    330   1217       N  
ATOM    261  CA  GLY A  94     -36.954 -41.296 110.702  1.00 98.61           C  
ANISOU  261  CA  GLY A  94    12864  10846  13756   1670    562   1523       C  
ATOM    262  C   GLY A  94     -35.602 -40.638 110.902  1.00 98.29           C  
ANISOU  262  C   GLY A  94    12657  11049  13637   1704    417   1664       C  
ATOM    263  O   GLY A  94     -34.825 -41.009 111.782  1.00101.23           O  
ANISOU  263  O   GLY A  94    12817  11634  14009   1869    456   1965       O  
ATOM    264  N   ASP A  95     -35.344 -39.668 110.028  1.00 95.93           N  
ANISOU  264  N   ASP A  95    12448  10728  13273   1540    259   1455       N  
ATOM    265  CA  ASP A  95     -34.148 -38.828 110.043  1.00 95.57           C  
ANISOU  265  CA  ASP A  95    12269  10892  13148   1506     91   1520       C  
ATOM    266  C   ASP A  95     -33.962 -37.921 111.266  1.00 96.94           C  
ANISOU  266  C   ASP A  95    12303  11423  13103   1488   -196   1550       C  
ATOM    267  O   ASP A  95     -32.875 -37.435 111.501  1.00102.46           O  
ANISOU  267  O   ASP A  95    12839  12347  13743   1468   -308   1655       O  
ATOM    268  CB  ASP A  95     -34.124 -37.967 108.757  1.00 93.10           C  
ANISOU  268  CB  ASP A  95    12112  10432  12826   1320      6   1268       C  
ATOM    269  CG  ASP A  95     -35.314 -36.996 108.637  1.00 88.68           C  
ANISOU  269  CG  ASP A  95    11723   9841  12129   1174   -200    985       C  
ATOM    270  OD1 ASP A  95     -36.274 -37.091 109.389  1.00 87.04           O  
ANISOU  270  OD1 ASP A  95    11545   9672  11851   1206   -248    948       O  
ATOM    271  OD2 ASP A  95     -35.301 -36.138 107.754  1.00 85.98           O  
ANISOU  271  OD2 ASP A  95    11478   9433  11757   1041   -296    819       O  
ATOM    272  N   SER A  96     -35.039 -37.712 112.021  1.00 97.37           N  
ANISOU  272  N   SER A  96    12423  11536  13037   1483   -302   1447       N  
ATOM    273  CA  SER A  96     -35.048 -36.826 113.169  1.00 97.22           C  
ANISOU  273  CA  SER A  96    12314  11836  12787   1444   -558   1410       C  
ATOM    274  C   SER A  96     -35.342 -37.558 114.460  1.00 98.33           C  
ANISOU  274  C   SER A  96    12316  12191  12852   1614   -509   1627       C  
ATOM    275  O   SER A  96     -36.271 -38.389 114.532  1.00 95.01           O  
ANISOU  275  O   SER A  96    11973  11603  12524   1710   -343   1665       O  
ATOM    276  CB  SER A  96     -36.126 -35.776 112.954  1.00 97.36           C  
ANISOU  276  CB  SER A  96    12541  11745  12705   1296   -723   1086       C  
ATOM    277  OG  SER A  96     -35.934 -35.099 111.708  1.00 96.51           O  
ANISOU  277  OG  SER A  96    12559  11439  12670   1153   -751    913       O  
ATOM    278  N   ASP A  97     -34.537 -37.243 115.478  1.00103.05           N  
ANISOU  278  N   ASP A  97    12694  13185  13274   1638   -653   1774       N  
ATOM    279  CA  ASP A  97     -34.713 -37.720 116.881  1.00104.72           C  
ANISOU  279  CA  ASP A  97    12731  13724  13332   1790   -662   1992       C  
ATOM    280  C   ASP A  97     -35.047 -36.592 117.856  1.00100.87           C  
ANISOU  280  C   ASP A  97    12247  13538  12541   1663   -941   1781       C  
ATOM    281  O   ASP A  97     -35.749 -36.803 118.819  1.00104.47           O  
ANISOU  281  O   ASP A  97    12678  14153  12862   1753   -953   1826       O  
ATOM    282  CB  ASP A  97     -33.446 -38.413 117.376  1.00107.56           C  
ANISOU  282  CB  ASP A  97    12779  14390  13697   1944   -579   2393       C  
ATOM    283  CG  ASP A  97     -32.969 -39.529 116.440  1.00109.20           C  
ANISOU  283  CG  ASP A  97    12975  14292  14222   2087   -261   2618       C  
ATOM    284  OD1 ASP A  97     -33.860 -40.232 115.864  1.00107.50           O  
ANISOU  284  OD1 ASP A  97    12953  13687  14206   2136    -44   2553       O  
ATOM    285  OD2 ASP A  97     -31.711 -39.699 116.327  1.00107.91           O  
ANISOU  285  OD2 ASP A  97    12599  14299  14100   2143   -221   2859       O  
ATOM    286  N   SER A  98     -34.538 -35.408 117.597  1.00 98.62           N  
ANISOU  286  N   SER A  98    11996  13315  12159   1453  -1141   1548       N  
ATOM    287  CA  SER A  98     -34.901 -34.206 118.308  1.00 99.55           C  
ANISOU  287  CA  SER A  98    12181  13612  12031   1290  -1369   1264       C  
ATOM    288  C   SER A  98     -35.866 -33.314 117.490  1.00 95.27           C  
ANISOU  288  C   SER A  98    11942  12686  11567   1156  -1402    911       C  
ATOM    289  O   SER A  98     -35.870 -33.327 116.260  1.00 91.00           O  
ANISOU  289  O   SER A  98    11524  11819  11232   1120  -1318    860       O  
ATOM    290  CB  SER A  98     -33.607 -33.440 118.598  1.00104.06           C  
ANISOU  290  CB  SER A  98    12568  14514  12454   1119  -1550   1241       C  
ATOM    291  OG  SER A  98     -33.854 -32.188 119.226  1.00109.63           O  
ANISOU  291  OG  SER A  98    13356  15362  12934    915  -1751    915       O  
ATOM    292  N   GLN A  99     -36.660 -32.509 118.179  1.00 95.03           N  
ANISOU  292  N   GLN A  99    12024  12720  11363   1089  -1516    680       N  
ATOM    293  CA  GLN A  99     -37.427 -31.463 117.493  1.00 93.90           C  
ANISOU  293  CA  GLN A  99    12135  12263  11278    962  -1555    369       C  
ATOM    294  C   GLN A  99     -36.547 -30.467 116.751  1.00 93.56           C  
ANISOU  294  C   GLN A  99    12122  12129  11297    761  -1642    217       C  
ATOM    295  O   GLN A  99     -36.955 -29.967 115.722  1.00 98.57           O  
ANISOU  295  O   GLN A  99    12931  12440  12078    705  -1605     84       O  
ATOM    296  CB  GLN A  99     -38.335 -30.660 118.447  1.00 95.50           C  
ANISOU  296  CB  GLN A  99    12446  12556  11282    929  -1640    144       C  
ATOM    297  CG  GLN A  99     -39.698 -31.280 118.769  1.00 94.47           C  
ANISOU  297  CG  GLN A  99    12399  12342  11153   1103  -1537    197       C  
ATOM    298  CD  GLN A  99     -40.587 -30.359 119.599  1.00 94.79           C  
ANISOU  298  CD  GLN A  99    12564  12438  11011   1071  -1602    -41       C  
ATOM    299  OE1 GLN A  99     -40.914 -29.259 119.180  1.00 92.96           O  
ANISOU  299  OE1 GLN A  99    12505  12001  10814    957  -1634   -288       O  
ATOM    300  NE2 GLN A  99     -40.998 -30.831 120.777  1.00 97.02           N  
ANISOU  300  NE2 GLN A  99    12759  12994  11108   1189  -1595     50       N  
ATOM    301  N   GLU A 100     -35.382 -30.160 117.298  1.00 95.82           N  
ANISOU  301  N   GLU A 100    12225  12721  11458    647  -1757    244       N  
ATOM    302  CA  GLU A 100     -34.431 -29.233 116.702  1.00 97.32           C  
ANISOU  302  CA  GLU A 100    12408  12862  11704    436  -1839    117       C  
ATOM    303  C   GLU A 100     -33.829 -29.796 115.423  1.00 96.00           C  
ANISOU  303  C   GLU A 100    12211  12487  11776    485  -1726    297       C  
ATOM    304  O   GLU A 100     -33.629 -29.074 114.438  1.00 89.25           O  
ANISOU  304  O   GLU A 100    11468  11386  11056    363  -1724    173       O  
ATOM    305  CB  GLU A 100     -33.326 -28.903 117.712  1.00102.29           C  
ANISOU  305  CB  GLU A 100    12802  13947  12114    290  -1994    124       C  
ATOM    306  CG  GLU A 100     -33.749 -27.921 118.808  1.00107.26           C  
ANISOU  306  CG  GLU A 100    13504  14752  12496    136  -2119   -177       C  
ATOM    307  CD  GLU A 100     -34.485 -28.490 120.029  1.00110.37           C  
ANISOU  307  CD  GLU A 100    13850  15421  12664    289  -2122   -114       C  
ATOM    308  OE1 GLU A 100     -34.863 -29.712 120.063  1.00111.42           O  
ANISOU  308  OE1 GLU A 100    13911  15571  12853    541  -2010    178       O  
ATOM    309  OE2 GLU A 100     -34.689 -27.642 120.950  1.00110.46           O  
ANISOU  309  OE2 GLU A 100    13908  15615  12445    138  -2223   -383       O  
ATOM    310  N   GLU A 101     -33.542 -31.093 115.459  1.00 99.52           N  
ANISOU  310  N   GLU A 101    12506  13031  12277    672  -1609    600       N  
ATOM    311  CA  GLU A 101     -33.059 -31.826 114.285  1.00100.91           C  
ANISOU  311  CA  GLU A 101    12665  12994  12681    751  -1449    778       C  
ATOM    312  C   GLU A 101     -34.108 -31.805 113.203  1.00 96.63           C  
ANISOU  312  C   GLU A 101    12379  12044  12289    769  -1343    636       C  
ATOM    313  O   GLU A 101     -33.794 -31.559 112.022  1.00 99.78           O  
ANISOU  313  O   GLU A 101    12853  12226  12830    704  -1292    597       O  
ATOM    314  CB  GLU A 101     -32.745 -33.274 114.644  1.00104.04           C  
ANISOU  314  CB  GLU A 101    12877  13529  13123    975  -1292   1124       C  
ATOM    315  CG  GLU A 101     -32.227 -34.112 113.493  1.00106.86           C  
ANISOU  315  CG  GLU A 101    13225  13655  13722   1068  -1081   1300       C  
ATOM    316  CD  GLU A 101     -31.904 -35.541 113.896  1.00111.59           C  
ANISOU  316  CD  GLU A 101    13644  14353  14400   1306   -877   1658       C  
ATOM    317  OE1 GLU A 101     -32.454 -36.044 114.908  1.00110.31           O  
ANISOU  317  OE1 GLU A 101    13422  14348  14139   1429   -863   1764       O  
ATOM    318  OE2 GLU A 101     -31.083 -36.157 113.172  1.00117.11           O  
ANISOU  318  OE2 GLU A 101    14263  14959  15273   1381   -707   1846       O  
ATOM    319  N   ALA A 102     -35.350 -32.076 113.600  1.00 91.62           N  
ANISOU  319  N   ALA A 102    11861  11337  11610    857  -1310    574       N  
ATOM    320  CA  ALA A 102     -36.492 -32.029 112.660  1.00 86.13           C  
ANISOU  320  CA  ALA A 102    11387  10317  11021    863  -1229    439       C  
ATOM    321  C   ALA A 102     -36.601 -30.679 111.968  1.00 82.95           C  
ANISOU  321  C   ALA A 102    11127   9756  10631    703  -1325    215       C  
ATOM    322  O   ALA A 102     -36.829 -30.606 110.753  1.00 81.23           O  
ANISOU  322  O   ALA A 102    11017   9310  10534    677  -1253    179       O  
ATOM    323  CB  ALA A 102     -37.811 -32.387 113.364  1.00 84.18           C  
ANISOU  323  CB  ALA A 102    11212  10071  10700    965  -1203    409       C  
ATOM    324  N   HIS A 103     -36.460 -29.626 112.750  1.00 83.96           N  
ANISOU  324  N   HIS A 103    11256  10012  10633    596  -1469     67       N  
ATOM    325  CA  HIS A 103     -36.575 -28.296 112.241  1.00 86.79           C  
ANISOU  325  CA  HIS A 103    11751  10199  11025    453  -1530   -136       C  
ATOM    326  C   HIS A 103     -35.484 -28.024 111.233  1.00 87.21           C  
ANISOU  326  C   HIS A 103    11756  10172  11206    351  -1517    -87       C  
ATOM    327  O   HIS A 103     -35.706 -27.352 110.220  1.00 90.16           O  
ANISOU  327  O   HIS A 103    12254  10316  11685    295  -1484   -161       O  
ATOM    328  CB  HIS A 103     -36.550 -27.269 113.378  1.00 91.87           C  
ANISOU  328  CB  HIS A 103    12405  10987  11513    338  -1654   -329       C  
ATOM    329  CG  HIS A 103     -36.627 -25.847 112.915  1.00 94.18           C  
ANISOU  329  CG  HIS A 103    12847  11061  11875    187  -1676   -541       C  
ATOM    330  ND1 HIS A 103     -35.512 -25.044 112.809  1.00 96.69           N  
ANISOU  330  ND1 HIS A 103    13107  11405  12225     -8  -1738   -619       N  
ATOM    331  CD2 HIS A 103     -37.679 -25.094 112.520  1.00 94.91           C  
ANISOU  331  CD2 HIS A 103    13132  10901  12028    211  -1621   -666       C  
ATOM    332  CE1 HIS A 103     -35.872 -23.853 112.374  1.00 99.44           C  
ANISOU  332  CE1 HIS A 103    13622  11494  12667   -100  -1707   -791       C  
ATOM    333  NE2 HIS A 103     -37.177 -23.867 112.162  1.00 98.10           N  
ANISOU  333  NE2 HIS A 103    13602  11153  12519     45  -1631   -806       N  
ATOM    334  N   GLY A 104     -34.300 -28.523 111.510  1.00 88.35           N  
ANISOU  334  N   GLY A 104    11704  10525  11338    336  -1535     62       N  
ATOM    335  CA  GLY A 104     -33.191 -28.346 110.573  1.00 88.55           C  
ANISOU  335  CA  GLY A 104    11658  10497  11487    251  -1510    139       C  
ATOM    336  C   GLY A 104     -33.413 -29.093 109.286  1.00 84.76           C  
ANISOU  336  C   GLY A 104    11250   9800  11155    355  -1348    246       C  
ATOM    337  O   GLY A 104     -33.072 -28.571 108.210  1.00 83.42           O  
ANISOU  337  O   GLY A 104    11134   9472  11088    279  -1317    223       O  
ATOM    338  N   LYS A 105     -33.946 -30.316 109.408  1.00 82.54           N  
ANISOU  338  N   LYS A 105    10962   9519  10880    517  -1234    361       N  
ATOM    339  CA  LYS A 105     -34.348 -31.067 108.216  1.00 81.90           C  
ANISOU  339  CA  LYS A 105    10977   9224  10917    587  -1064    404       C  
ATOM    340  C   LYS A 105     -35.372 -30.254 107.398  1.00 78.04           C  
ANISOU  340  C   LYS A 105    10683   8538  10430    521  -1088    227       C  
ATOM    341  O   LYS A 105     -35.277 -30.165 106.133  1.00 77.30           O  
ANISOU  341  O   LYS A 105    10654   8305  10412    485  -1012    222       O  
ATOM    342  CB  LYS A 105     -34.897 -32.452 108.574  1.00 82.97           C  
ANISOU  342  CB  LYS A 105    11094   9360  11070    743   -921    518       C  
ATOM    343  CG  LYS A 105     -33.853 -33.403 109.118  1.00 87.57           C  
ANISOU  343  CG  LYS A 105    11473  10104  11693    851   -830    762       C  
ATOM    344  CD  LYS A 105     -32.872 -33.816 108.029  1.00 92.35           C  
ANISOU  344  CD  LYS A 105    12036  10608  12443    857   -680    873       C  
ATOM    345  CE  LYS A 105     -31.807 -34.838 108.443  1.00 98.33           C  
ANISOU  345  CE  LYS A 105    12580  11502  13277   1001   -537   1163       C  
ATOM    346  NZ  LYS A 105     -30.968 -34.379 109.583  1.00103.43           N  
ANISOU  346  NZ  LYS A 105    13001  12491  13803    985   -710   1286       N  
ATOM    347  N   LEU A 106     -36.326 -29.646 108.116  1.00 74.84           N  
ANISOU  347  N   LEU A 106    10358   8143   9933    517  -1183    101       N  
ATOM    348  CA  LEU A 106     -37.326 -28.787 107.438  1.00 71.99           C  
ANISOU  348  CA  LEU A 106    10156   7620   9575    481  -1199    -25       C  
ATOM    349  C   LEU A 106     -36.703 -27.653 106.673  1.00 71.65           C  
ANISOU  349  C   LEU A 106    10142   7480   9599    367  -1232    -65       C  
ATOM    350  O   LEU A 106     -37.220 -27.238 105.613  1.00 73.36           O  
ANISOU  350  O   LEU A 106    10452   7565   9856    358  -1188    -79       O  
ATOM    351  CB  LEU A 106     -38.410 -28.272 108.394  1.00 70.89           C  
ANISOU  351  CB  LEU A 106    10091   7503   9340    515  -1271   -137       C  
ATOM    352  CG  LEU A 106     -39.404 -29.357 108.828  1.00 70.76           C  
ANISOU  352  CG  LEU A 106    10077   7533   9276    635  -1210    -93       C  
ATOM    353  CD1 LEU A 106     -40.191 -28.860 110.018  1.00 70.68           C  
ANISOU  353  CD1 LEU A 106    10103   7596   9155    675  -1284   -183       C  
ATOM    354  CD2 LEU A 106     -40.354 -29.812 107.718  1.00 70.22           C  
ANISOU  354  CD2 LEU A 106    10088   7345   9247    657  -1116    -87       C  
ATOM    355  N   VAL A 107     -35.609 -27.147 107.198  1.00 71.82           N  
ANISOU  355  N   VAL A 107    10070   7588   9629    274  -1306    -70       N  
ATOM    356  CA  VAL A 107     -34.899 -26.078 106.536  1.00 71.98           C  
ANISOU  356  CA  VAL A 107    10100   7509   9736    146  -1324    -99       C  
ATOM    357  C   VAL A 107     -34.232 -26.621 105.279  1.00 72.20           C  
ANISOU  357  C   VAL A 107    10084   7494   9854    160  -1222     39       C  
ATOM    358  O   VAL A 107     -34.086 -25.894 104.287  1.00 73.00           O  
ANISOU  358  O   VAL A 107    10236   7468  10030    104  -1189     44       O  
ATOM    359  CB  VAL A 107     -33.971 -25.331 107.513  1.00 73.74           C  
ANISOU  359  CB  VAL A 107    10230   7853   9933      1  -1435   -177       C  
ATOM    360  CG1 VAL A 107     -33.151 -24.291 106.804  1.00 75.06           C  
ANISOU  360  CG1 VAL A 107    10395   7903  10221   -149  -1433   -196       C  
ATOM    361  CG2 VAL A 107     -34.805 -24.625 108.580  1.00 75.17           C  
ANISOU  361  CG2 VAL A 107    10508   8031  10020    -23  -1503   -363       C  
ATOM    362  N   LEU A 108     -33.873 -27.904 105.268  1.00 73.25           N  
ANISOU  362  N   LEU A 108    10127   7719   9983    248  -1145    159       N  
ATOM    363  CA  LEU A 108     -33.324 -28.526 104.027  1.00 73.12           C  
ANISOU  363  CA  LEU A 108    10091   7643  10047    273  -1006    270       C  
ATOM    364  C   LEU A 108     -34.424 -28.793 103.020  1.00 71.54           C  
ANISOU  364  C   LEU A 108    10034   7323   9824    314   -919    219       C  
ATOM    365  O   LEU A 108     -34.229 -28.611 101.818  1.00 72.39           O  
ANISOU  365  O   LEU A 108    10176   7366   9963    283   -847    245       O  
ATOM    366  CB  LEU A 108     -32.585 -29.851 104.275  1.00 73.59           C  
ANISOU  366  CB  LEU A 108    10020   7801  10138    367   -897    421       C  
ATOM    367  CG  LEU A 108     -31.404 -29.907 105.222  1.00 75.22           C  
ANISOU  367  CG  LEU A 108    10024   8207  10347    356   -961    541       C  
ATOM    368  CD1 LEU A 108     -31.042 -31.370 105.363  1.00 75.99           C  
ANISOU  368  CD1 LEU A 108    10021   8360  10491    510   -795    722       C  
ATOM    369  CD2 LEU A 108     -30.219 -29.088 104.741  1.00 76.93           C  
ANISOU  369  CD2 LEU A 108    10146   8452  10630    233  -1001    587       C  
ATOM    370  N   TRP A 109     -35.563 -29.270 103.483  1.00 70.21           N  
ANISOU  370  N   TRP A 109     9930   7157   9587    377   -920    157       N  
ATOM    371  CA  TRP A 109     -36.643 -29.495 102.524  1.00 70.95           C  
ANISOU  371  CA  TRP A 109    10132   7187   9636    386   -853    105       C  
ATOM    372  C   TRP A 109     -37.050 -28.189 101.862  1.00 70.66           C  
ANISOU  372  C   TRP A 109    10164   7095   9585    336   -917     75       C  
ATOM    373  O   TRP A 109     -37.375 -28.146 100.695  1.00 69.94           O  
ANISOU  373  O   TRP A 109    10114   6994   9465    318   -858     90       O  
ATOM    374  CB  TRP A 109     -37.844 -30.188 103.193  1.00 72.18           C  
ANISOU  374  CB  TRP A 109    10328   7367   9727    450   -848     51       C  
ATOM    375  CG  TRP A 109     -37.598 -31.593 103.396  1.00 74.41           C  
ANISOU  375  CG  TRP A 109    10565   7657  10049    503   -715    101       C  
ATOM    376  CD1 TRP A 109     -37.175 -32.214 104.549  1.00 76.08           C  
ANISOU  376  CD1 TRP A 109    10686   7932  10289    580   -704    180       C  
ATOM    377  CD2 TRP A 109     -37.692 -32.592 102.411  1.00 77.06           C  
ANISOU  377  CD2 TRP A 109    10938   7931  10409    485   -542     87       C  
ATOM    378  NE1 TRP A 109     -37.030 -33.541 104.322  1.00 79.46           N  
ANISOU  378  NE1 TRP A 109    11096   8307  10787    632   -515    241       N  
ATOM    379  CE2 TRP A 109     -37.350 -33.809 103.013  1.00 79.33           C  
ANISOU  379  CE2 TRP A 109    11170   8196  10773    563   -405    160       C  
ATOM    380  CE3 TRP A 109     -38.067 -32.590 101.078  1.00 79.69           C  
ANISOU  380  CE3 TRP A 109    11344   8239  10694    407   -476     17       C  
ATOM    381  CZ2 TRP A 109     -37.378 -35.032 102.315  1.00 80.49           C  
ANISOU  381  CZ2 TRP A 109    11356   8242  10983    556   -178    139       C  
ATOM    382  CZ3 TRP A 109     -38.105 -33.805 100.383  1.00 81.06           C  
ANISOU  382  CZ3 TRP A 109    11552   8356  10889    377   -275    -28       C  
ATOM    383  CH2 TRP A 109     -37.765 -35.003 101.009  1.00 80.96           C  
ANISOU  383  CH2 TRP A 109    11506   8268  10984    448   -118     19       C  
ATOM    384  N   SER A 110     -37.039 -27.117 102.633  1.00 71.86           N  
ANISOU  384  N   SER A 110    10325   7221   9757    313  -1024     35       N  
ATOM    385  CA  SER A 110     -37.510 -25.862 102.146  1.00 73.15           C  
ANISOU  385  CA  SER A 110    10558   7295   9939    291  -1049     24       C  
ATOM    386  C   SER A 110     -36.649 -25.300 101.014  1.00 71.33           C  
ANISOU  386  C   SER A 110    10306   7012   9785    230   -999    111       C  
ATOM    387  O   SER A 110     -36.970 -24.271 100.481  1.00 72.38           O  
ANISOU  387  O   SER A 110    10485   7062   9953    225   -990    144       O  
ATOM    388  CB  SER A 110     -37.642 -24.875 103.314  1.00 77.41           C  
ANISOU  388  CB  SER A 110    11129   7781  10501    270  -1135    -67       C  
ATOM    389  OG  SER A 110     -36.346 -24.538 103.794  1.00 86.11           O  
ANISOU  389  OG  SER A 110    12155   8893  11667    168  -1178    -83       O  
ATOM    390  N   GLY A 111     -35.591 -25.955 100.623  1.00 71.40           N  
ANISOU  390  N   GLY A 111    10238   7064   9826    200   -946    170       N  
ATOM    391  CA  GLY A 111     -34.970 -25.667  99.323  1.00 74.89           C  
ANISOU  391  CA  GLY A 111    10662   7483  10308    165   -867    267       C  
ATOM    392  C   GLY A 111     -35.826 -26.011  98.076  1.00 77.72           C  
ANISOU  392  C   GLY A 111    11076   7892  10559    202   -788    294       C  
ATOM    393  O   GLY A 111     -35.460 -25.638  96.922  1.00 77.63           O  
ANISOU  393  O   GLY A 111    11054   7892  10549    180   -723    384       O  
ATOM    394  N   LEU A 112     -36.924 -26.765  98.301  1.00 78.71           N  
ANISOU  394  N   LEU A 112    11245   8080  10580    245   -791    219       N  
ATOM    395  CA  LEU A 112     -37.938 -27.009  97.296  1.00 78.39           C  
ANISOU  395  CA  LEU A 112    11240   8137  10404    250   -748    219       C  
ATOM    396  C   LEU A 112     -38.892 -25.889  97.168  1.00 79.47           C  
ANISOU  396  C   LEU A 112    11401   8280  10511    290   -809    275       C  
ATOM    397  O   LEU A 112     -39.852 -26.050  96.465  1.00 81.44           O  
ANISOU  397  O   LEU A 112    11652   8661  10628    299   -796    293       O  
ATOM    398  CB  LEU A 112     -38.746 -28.253  97.598  1.00 79.45           C  
ANISOU  398  CB  LEU A 112    11396   8338  10452    254   -717    114       C  
ATOM    399  CG  LEU A 112     -38.071 -29.564  97.248  1.00 83.59           C  
ANISOU  399  CG  LEU A 112    11912   8861  10984    219   -579     68       C  
ATOM    400  CD1 LEU A 112     -37.510 -30.204  98.501  1.00 88.43           C  
ANISOU  400  CD1 LEU A 112    12493   9398  11708    268   -572     61       C  
ATOM    401  CD2 LEU A 112     -39.031 -30.551  96.642  1.00 83.81           C  
ANISOU  401  CD2 LEU A 112    11980   8980  10882    163   -496    -38       C  
ATOM    402  N   ARG A 113     -38.676 -24.758  97.822  1.00 83.33           N  
ANISOU  402  N   ARG A 113    11903   8636  11119    311   -861    303       N  
ATOM    403  CA  ARG A 113     -39.461 -23.566  97.547  1.00 89.82           C  
ANISOU  403  CA  ARG A 113    12750   9420  11954    371   -865    397       C  
ATOM    404  C   ARG A 113     -39.419 -23.274  96.075  1.00 93.45           C  
ANISOU  404  C   ARG A 113    13172   9980  12355    373   -797    549       C  
ATOM    405  O   ARG A 113     -40.441 -22.818  95.552  1.00101.57           O  
ANISOU  405  O   ARG A 113    14187  11104  13301    443   -788    657       O  
ATOM    406  CB  ARG A 113     -38.938 -22.321  98.228  1.00 94.94           C  
ANISOU  406  CB  ARG A 113    13430   9861  12778    360   -875    399       C  
ATOM    407  CG  ARG A 113     -39.644 -21.994  99.519  1.00101.03           C  
ANISOU  407  CG  ARG A 113    14260  10550  13574    403   -925    289       C  
ATOM    408  CD  ARG A 113     -38.966 -20.738 100.093  1.00107.36           C  
ANISOU  408  CD  ARG A 113    15105  11133  14553    345   -906    251       C  
ATOM    409  NE  ARG A 113     -38.115 -21.037 101.240  1.00109.08           N  
ANISOU  409  NE  ARG A 113    15308  11341  14794    242   -981     91       N  
ATOM    410  CZ  ARG A 113     -38.543 -21.148 102.503  1.00111.09           C  
ANISOU  410  CZ  ARG A 113    15600  11603  15003    253  -1039    -52       C  
ATOM    411  NH1 ARG A 113     -37.673 -21.434 103.482  1.00112.18           N  
ANISOU  411  NH1 ARG A 113    15692  11796  15133    152  -1113   -170       N  
ATOM    412  NH2 ARG A 113     -39.840 -20.976 102.801  1.00110.33           N  
ANISOU  412  NH2 ARG A 113    15569  11493  14856    369  -1022    -62       N  
ATOM    413  N   ASN A 114     -38.252 -23.517  95.425  1.00 91.00           N  
ANISOU  413  N   ASN A 114    12828   9671  12075    307   -744    579       N  
ATOM    414  CA  ASN A 114     -38.068 -23.417  93.953  1.00 89.31           C  
ANISOU  414  CA  ASN A 114    12570   9592  11771    300   -666    717       C  
ATOM    415  C   ASN A 114     -38.582 -24.710  93.439  1.00 91.06           C  
ANISOU  415  C   ASN A 114    12787  10019  11790    262   -645    619       C  
ATOM    416  O   ASN A 114     -38.239 -25.745  93.965  1.00 99.68           O  
ANISOU  416  O   ASN A 114    13900  11079  12892    220   -634    477       O  
ATOM    417  CB  ASN A 114     -36.622 -23.222  93.603  1.00 86.65           C  
ANISOU  417  CB  ASN A 114    12201   9168  11554    244   -606    772       C  
ATOM    418  CG  ASN A 114     -35.899 -22.341  94.632  1.00 86.52           C  
ANISOU  418  CG  ASN A 114    12191   8918  11761    215   -646    756       C  
ATOM    419  OD1 ASN A 114     -36.149 -21.119  94.770  1.00 87.25           O  
ANISOU  419  OD1 ASN A 114    12306   8874  11969    241   -638    835       O  
ATOM    420  ND2 ASN A 114     -35.038 -22.970  95.415  1.00 85.45           N  
ANISOU  420  ND2 ASN A 114    12034   8745  11687    154   -677    649       N  
ATOM    421  N   ALA A 115     -39.451 -24.670  92.461  1.00 90.71           N  
ANISOU  421  N   ALA A 115    12709  10194  11560    272   -632    695       N  
ATOM    422  CA  ALA A 115     -40.403 -25.794  92.195  1.00 89.07           C  
ANISOU  422  CA  ALA A 115    12499  10202  11141    211   -637    562       C  
ATOM    423  C   ALA A 115     -41.721 -25.585  92.899  1.00 86.60           C  
ANISOU  423  C   ALA A 115    12178   9930  10796    269   -726    561       C  
ATOM    424  O   ALA A 115     -42.087 -26.340  93.801  1.00 86.76           O  
ANISOU  424  O   ALA A 115    12234   9892  10836    249   -756    411       O  
ATOM    425  CB  ALA A 115     -39.861 -27.218  92.464  1.00 86.95           C  
ANISOU  425  CB  ALA A 115    12279   9881  10876    121   -571    355       C  
ATOM    426  N   PRO A 116     -42.442 -24.545  92.496  1.00 86.05           N  
ANISOU  426  N   PRO A 116    12049   9960  10683    359   -750    756       N  
ATOM    427  CA  PRO A 116     -43.664 -24.221  93.221  1.00 85.00           C  
ANISOU  427  CA  PRO A 116    11900   9847  10546    444   -815    788       C  
ATOM    428  C   PRO A 116     -44.721 -25.304  93.201  1.00 84.57           C  
ANISOU  428  C   PRO A 116    11809  10027  10297    365   -856    662       C  
ATOM    429  O   PRO A 116     -45.370 -25.570  94.215  1.00 82.44           O  
ANISOU  429  O   PRO A 116    11563   9688  10072    395   -901    579       O  
ATOM    430  CB  PRO A 116     -44.160 -22.976  92.491  1.00 86.82           C  
ANISOU  430  CB  PRO A 116    12050  10184  10753    566   -790   1071       C  
ATOM    431  CG  PRO A 116     -42.934 -22.411  91.855  1.00 87.82           C  
ANISOU  431  CG  PRO A 116    12188  10197  10981    558   -716   1169       C  
ATOM    432  CD  PRO A 116     -42.196 -23.601  91.391  1.00 86.84           C  
ANISOU  432  CD  PRO A 116    12084  10160  10748    409   -700    989       C  
ATOM    433  N   ARG A 117     -44.872 -25.942  92.058  1.00 89.09           N  
ANISOU  433  N   ARG A 117    12321  10879  10646    248   -831    634       N  
ATOM    434  CA  ARG A 117     -45.898 -26.959  91.865  1.00 93.24           C  
ANISOU  434  CA  ARG A 117    12798  11663  10966    124   -859    498       C  
ATOM    435  C   ARG A 117     -45.688 -28.111  92.826  1.00 87.10           C  
ANISOU  435  C   ARG A 117    12116  10682  10294     46   -832    250       C  
ATOM    436  O   ARG A 117     -46.626 -28.734  93.307  1.00 87.70           O  
ANISOU  436  O   ARG A 117    12172  10833  10317     -2   -863    155       O  
ATOM    437  CB  ARG A 117     -45.881 -27.451  90.415  1.00102.28           C  
ANISOU  437  CB  ARG A 117    13878  13140  11843    -27   -816    465       C  
ATOM    438  CG  ARG A 117     -46.292 -26.409  89.360  1.00112.97           C  
ANISOU  438  CG  ARG A 117    15091  14804  13028     50   -844    752       C  
ATOM    439  CD  ARG A 117     -47.775 -26.334  89.148  1.00121.02           C  
ANISOU  439  CD  ARG A 117    15955  16194  13833     44   -930    856       C  
ATOM    440  NE  ARG A 117     -48.334 -27.676  88.901  1.00128.30           N  
ANISOU  440  NE  ARG A 117    16859  17343  14542   -199   -939    580       N  
ATOM    441  CZ  ARG A 117     -49.627 -27.953  88.853  1.00135.06           C  
ANISOU  441  CZ  ARG A 117    17581  18523  15209   -274  -1018    585       C  
ATOM    442  NH1 ARG A 117     -50.513 -26.970  88.982  1.00136.18           N  
ANISOU  442  NH1 ARG A 117    17579  18827  15333    -95  -1091    886       N  
ATOM    443  NH2 ARG A 117     -50.032 -29.213  88.679  1.00136.80           N  
ANISOU  443  NH2 ARG A 117    17807  18896  15272   -530  -1004    294       N  
ATOM    444  N   CYS A 118     -44.444 -28.390  93.092  1.00 82.28           N  
ANISOU  444  N   CYS A 118    11596   9827   9840     41   -764    171       N  
ATOM    445  CA  CYS A 118     -44.123 -29.330  94.106  1.00 80.98           C  
ANISOU  445  CA  CYS A 118    11505   9451   9810     17   -725      6       C  
ATOM    446  C   CYS A 118     -44.238 -28.758  95.525  1.00 77.73           C  
ANISOU  446  C   CYS A 118    11118   8841   9573    156   -803     57       C  
ATOM    447  O   CYS A 118     -44.752 -29.408  96.443  1.00 76.89           O  
ANISOU  447  O   CYS A 118    11028   8684   9503    158   -813    -32       O  
ATOM    448  CB  CYS A 118     -42.698 -29.806  93.843  1.00 83.03           C  
ANISOU  448  CB  CYS A 118    11823   9555  10167    -18   -613    -54       C  
ATOM    449  SG  CYS A 118     -41.914 -30.558  95.257  1.00 82.03           S  
ANISOU  449  SG  CYS A 118    11755   9140  10270     33   -566   -138       S  
ATOM    450  N   TRP A 119     -43.729 -27.554  95.718  1.00 76.08           N  
ANISOU  450  N   TRP A 119    10915   8515   9476    260   -841    192       N  
ATOM    451  CA  TRP A 119     -43.761 -26.915  97.040  1.00 74.24           C  
ANISOU  451  CA  TRP A 119    10717   8096   9394    368   -900    208       C  
ATOM    452  C   TRP A 119     -45.148 -26.878  97.603  1.00 76.20           C  
ANISOU  452  C   TRP A 119    10940   8432   9578    427   -953    216       C  
ATOM    453  O   TRP A 119     -45.326 -27.078  98.823  1.00 78.35           O  
ANISOU  453  O   TRP A 119    11247   8596   9924    475   -980    145       O  
ATOM    454  CB  TRP A 119     -43.269 -25.488  96.971  1.00 73.50           C  
ANISOU  454  CB  TRP A 119    10633   7878   9413    445   -910    345       C  
ATOM    455  CG  TRP A 119     -43.126 -24.785  98.236  1.00 72.18           C  
ANISOU  455  CG  TRP A 119    10518   7511   9396    516   -947    317       C  
ATOM    456  CD1 TRP A 119     -43.650 -23.593  98.522  1.00 74.13           C  
ANISOU  456  CD1 TRP A 119    10783   7671   9709    614   -947    407       C  
ATOM    457  CD2 TRP A 119     -42.351 -25.175  99.382  1.00 71.48           C  
ANISOU  457  CD2 TRP A 119    10465   7291   9402    489   -973    192       C  
ATOM    458  NE1 TRP A 119     -43.266 -23.197  99.777  1.00 75.18           N  
ANISOU  458  NE1 TRP A 119    10980   7616   9966    628   -970    306       N  
ATOM    459  CE2 TRP A 119     -42.456 -24.145 100.324  1.00 72.37           C  
ANISOU  459  CE2 TRP A 119    10624   7260   9613    548  -1002    180       C  
ATOM    460  CE3 TRP A 119     -41.621 -26.307  99.719  1.00 71.22           C  
ANISOU  460  CE3 TRP A 119    10420   7262   9375    430   -959    101       C  
ATOM    461  CZ2 TRP A 119     -41.840 -24.185 101.576  1.00 71.51           C  
ANISOU  461  CZ2 TRP A 119    10541   7056   9572    525  -1043     64       C  
ATOM    462  CZ3 TRP A 119     -41.021 -26.376 100.984  1.00 71.17           C  
ANISOU  462  CZ3 TRP A 119    10421   7169   9449    437   -999     32       C  
ATOM    463  CH2 TRP A 119     -41.133 -25.306 101.888  1.00 71.53           C  
ANISOU  463  CH2 TRP A 119    10503   7117   9555    472  -1054      6       C  
ATOM    464  N   ALA A 120     -46.120 -26.572  96.725  1.00 77.79           N  
ANISOU  464  N   ALA A 120    11065   8858   9633    433   -966    326       N  
ATOM    465  CA  ALA A 120     -47.496 -26.360  97.138  1.00 76.77           C  
ANISOU  465  CA  ALA A 120    10880   8849   9440    508  -1010    389       C  
ATOM    466  C   ALA A 120     -48.074 -27.600  97.722  1.00 75.31           C  
ANISOU  466  C   ALA A 120    10691   8718   9205    428  -1017    233       C  
ATOM    467  O   ALA A 120     -48.780 -27.504  98.710  1.00 79.98           O  
ANISOU  467  O   ALA A 120    11283   9266   9837    514  -1046    237       O  
ATOM    468  CB  ALA A 120     -48.329 -25.839  96.010  1.00 78.65           C  
ANISOU  468  CB  ALA A 120    10998   9369   9515    528  -1021    572       C  
ATOM    469  N   VAL A 121     -47.743 -28.760  97.197  1.00 73.04           N  
ANISOU  469  N   VAL A 121    10409   8492   8849    269   -968     92       N  
ATOM    470  CA  VAL A 121     -48.170 -30.008  97.873  1.00 71.46           C  
ANISOU  470  CA  VAL A 121    10223   8271   8657    191   -935    -60       C  
ATOM    471  C   VAL A 121     -47.209 -30.541  98.910  1.00 69.64           C  
ANISOU  471  C   VAL A 121    10078   7779   8601    228   -886   -145       C  
ATOM    472  O   VAL A 121     -47.634 -31.283  99.763  1.00 71.66           O  
ANISOU  472  O   VAL A 121    10337   7990   8897    231   -863   -207       O  
ATOM    473  CB  VAL A 121     -48.503 -31.161  96.912  1.00 72.11           C  
ANISOU  473  CB  VAL A 121    10271   8535   8592    -19   -868   -200       C  
ATOM    474  CG1 VAL A 121     -49.772 -30.851  96.183  1.00 73.83           C  
ANISOU  474  CG1 VAL A 121    10358   9089   8601    -73   -939   -121       C  
ATOM    475  CG2 VAL A 121     -47.359 -31.421  95.919  1.00 73.33           C  
ANISOU  475  CG2 VAL A 121    10476   8657   8728   -112   -782   -265       C  
ATOM    476  N   ILE A 122     -45.921 -30.267  98.844  1.00 68.75           N  
ANISOU  476  N   ILE A 122    10016   7520   8587    251   -860   -133       N  
ATOM    477  CA  ILE A 122     -45.021 -30.893  99.867  1.00 68.53           C  
ANISOU  477  CA  ILE A 122    10030   7302   8704    287   -812   -186       C  
ATOM    478  C   ILE A 122     -45.139 -30.285 101.297  1.00 66.56           C  
ANISOU  478  C   ILE A 122     9790   6968   8532    419   -894   -145       C  
ATOM    479  O   ILE A 122     -45.062 -31.012 102.288  1.00 64.09           O  
ANISOU  479  O   ILE A 122     9477   6600   8274    452   -866   -178       O  
ATOM    480  CB  ILE A 122     -43.546 -30.995  99.388  1.00 69.37           C  
ANISOU  480  CB  ILE A 122    10160   7307   8889    259   -743   -183       C  
ATOM    481  CG1 ILE A 122     -42.828 -32.138 100.086  1.00 69.25           C  
ANISOU  481  CG1 ILE A 122    10153   7171   8986    267   -638   -227       C  
ATOM    482  CG2 ILE A 122     -42.795 -29.663  99.557  1.00 69.69           C  
ANISOU  482  CG2 ILE A 122    10203   7276   8999    331   -826    -86       C  
ATOM    483  CD1 ILE A 122     -41.557 -32.547  99.363  1.00 70.94           C  
ANISOU  483  CD1 ILE A 122    10376   7317   9260    227   -519   -224       C  
ATOM    484  N   GLN A 123     -45.363 -28.959 101.382  1.00 67.46           N  
ANISOU  484  N   GLN A 123     9912   7075   8645    495   -975    -72       N  
ATOM    485  CA  GLN A 123     -45.506 -28.221 102.685  1.00 67.38           C  
ANISOU  485  CA  GLN A 123     9928   6980   8690    605  -1035    -67       C  
ATOM    486  C   GLN A 123     -46.454 -28.916 103.721  1.00 66.27           C  
ANISOU  486  C   GLN A 123     9772   6890   8515    657  -1038   -102       C  
ATOM    487  O   GLN A 123     -46.041 -29.201 104.846  1.00 65.16           O  
ANISOU  487  O   GLN A 123     9642   6700   8416    699  -1046   -137       O  
ATOM    488  CB  GLN A 123     -45.953 -26.777 102.450  1.00 68.09           C  
ANISOU  488  CB  GLN A 123    10037   7044   8787    678  -1067     13       C  
ATOM    489  CG  GLN A 123     -44.862 -25.829 102.124  1.00 69.75           C  
ANISOU  489  CG  GLN A 123    10282   7127   9093    659  -1064     40       C  
ATOM    490  CD  GLN A 123     -45.424 -24.441 101.882  1.00 73.78           C  
ANISOU  490  CD  GLN A 123    10815   7577   9641    747  -1048    141       C  
ATOM    491  OE1 GLN A 123     -45.273 -23.539 102.710  1.00 77.22           O  
ANISOU  491  OE1 GLN A 123    11313   7858  10167    795  -1043    102       O  
ATOM    492  NE2 GLN A 123     -46.113 -24.259 100.753  1.00 75.60           N  
ANISOU  492  NE2 GLN A 123    10988   7939   9797    769  -1024    275       N  
ATOM    493  N   PRO A 124     -47.706 -29.201 103.327  1.00 65.14           N  
ANISOU  493  N   PRO A 124     9586   6876   8286    649  -1030    -78       N  
ATOM    494  CA  PRO A 124     -48.572 -29.963 104.169  1.00 65.25           C  
ANISOU  494  CA  PRO A 124     9571   6941   8277    678  -1015   -100       C  
ATOM    495  C   PRO A 124     -48.057 -31.370 104.538  1.00 65.83           C  
ANISOU  495  C   PRO A 124     9640   6966   8403    617   -934   -162       C  
ATOM    496  O   PRO A 124     -48.258 -31.800 105.668  1.00 65.13           O  
ANISOU  496  O   PRO A 124     9543   6861   8342    688   -921   -157       O  
ATOM    497  CB  PRO A 124     -49.807 -30.145 103.290  1.00 65.70           C  
ANISOU  497  CB  PRO A 124     9555   7178   8226    619  -1014    -64       C  
ATOM    498  CG  PRO A 124     -49.739 -29.085 102.310  1.00 65.89           C  
ANISOU  498  CG  PRO A 124     9571   7253   8211    631  -1049     18       C  
ATOM    499  CD  PRO A 124     -48.311 -29.027 102.003  1.00 65.41           C  
ANISOU  499  CD  PRO A 124     9571   7055   8225    585  -1028    -24       C  
ATOM    500  N   LEU A 125     -47.414 -32.071 103.595  1.00 66.43           N  
ANISOU  500  N   LEU A 125     9721   7019   8497    500   -858   -207       N  
ATOM    501  CA  LEU A 125     -46.911 -33.410 103.892  1.00 66.61           C  
ANISOU  501  CA  LEU A 125     9745   6957   8604    460   -731   -246       C  
ATOM    502  C   LEU A 125     -45.799 -33.342 104.888  1.00 67.24           C  
ANISOU  502  C   LEU A 125     9828   6947   8773    564   -737   -191       C  
ATOM    503  O   LEU A 125     -45.784 -34.085 105.835  1.00 69.33           O  
ANISOU  503  O   LEU A 125    10064   7187   9089    626   -679   -156       O  
ATOM    504  CB  LEU A 125     -46.385 -34.090 102.650  1.00 67.62           C  
ANISOU  504  CB  LEU A 125     9893   7057   8739    320   -618   -318       C  
ATOM    505  CG  LEU A 125     -45.697 -35.462 102.783  1.00 67.80           C  
ANISOU  505  CG  LEU A 125     9932   6939   8887    288   -428   -352       C  
ATOM    506  CD1 LEU A 125     -46.554 -36.448 103.549  1.00 67.55           C  
ANISOU  506  CD1 LEU A 125     9878   6881   8905    289   -338   -362       C  
ATOM    507  CD2 LEU A 125     -45.391 -35.990 101.373  1.00 68.92           C  
ANISOU  507  CD2 LEU A 125    10113   7069   9002    127   -304   -463       C  
ATOM    508  N   LEU A 126     -44.874 -32.416 104.704  1.00 68.92           N  
ANISOU  508  N   LEU A 126    10056   7133   8997    581   -809   -170       N  
ATOM    509  CA  LEU A 126     -43.713 -32.292 105.606  1.00 69.48           C  
ANISOU  509  CA  LEU A 126    10101   7169   9129    648   -832   -121       C  
ATOM    510  C   LEU A 126     -44.132 -31.940 107.042  1.00 70.58           C  
ANISOU  510  C   LEU A 126    10222   7368   9224    749   -913   -106       C  
ATOM    511  O   LEU A 126     -43.609 -32.579 107.942  1.00 73.43           O  
ANISOU  511  O   LEU A 126    10527   7759   9611    807   -880    -47       O  
ATOM    512  CB  LEU A 126     -42.698 -31.267 105.095  1.00 68.77           C  
ANISOU  512  CB  LEU A 126    10022   7047   9058    612   -897   -115       C  
ATOM    513  CG  LEU A 126     -42.098 -31.524 103.720  1.00 68.49           C  
ANISOU  513  CG  LEU A 126     9998   6972   9053    526   -815   -115       C  
ATOM    514  CD1 LEU A 126     -41.503 -30.244 103.205  1.00 68.41           C  
ANISOU  514  CD1 LEU A 126    10002   6940   9050    498   -894    -98       C  
ATOM    515  CD2 LEU A 126     -41.075 -32.646 103.733  1.00 69.51           C  
ANISOU  515  CD2 LEU A 126    10083   7052   9272    530   -682    -71       C  
ATOM    516  N   CYS A 127     -45.058 -30.989 107.265  1.00 69.36           N  
ANISOU  516  N   CYS A 127    10107   7242   9002    782   -997   -143       N  
ATOM    517  CA  CYS A 127     -45.555 -30.753 108.633  1.00 70.70           C  
ANISOU  517  CA  CYS A 127    10271   7474   9116    879  -1045   -146       C  
ATOM    518  C   CYS A 127     -46.137 -31.971 109.212  1.00 67.20           C  
ANISOU  518  C   CYS A 127     9778   7082   8673    927   -965    -95       C  
ATOM    519  O   CYS A 127     -45.783 -32.351 110.320  1.00 68.47           O  
ANISOU  519  O   CYS A 127     9890   7306   8817    999   -961    -47       O  
ATOM    520  CB  CYS A 127     -46.622 -29.671 108.774  1.00 74.60           C  
ANISOU  520  CB  CYS A 127    10818   7972   9553    931  -1097   -183       C  
ATOM    521  SG  CYS A 127     -45.911 -28.067 108.495  1.00 89.18           S  
ANISOU  521  SG  CYS A 127    12736   9719  11429    899  -1161   -240       S  
ATOM    522  N   ALA A 128     -47.022 -32.599 108.479  1.00 65.16           N  
ANISOU  522  N   ALA A 128     9517   6812   8428    878   -896    -97       N  
ATOM    523  CA  ALA A 128     -47.700 -33.776 108.975  1.00 65.39           C  
ANISOU  523  CA  ALA A 128     9499   6861   8481    901   -796    -54       C  
ATOM    524  C   ALA A 128     -46.767 -34.901 109.392  1.00 66.42           C  
ANISOU  524  C   ALA A 128     9584   6942   8708    926   -677     21       C  
ATOM    525  O   ALA A 128     -47.170 -35.759 110.195  1.00 66.80           O  
ANISOU  525  O   ALA A 128     9583   7008   8788    993   -589     98       O  
ATOM    526  CB  ALA A 128     -48.692 -34.290 107.971  1.00 65.49           C  
ANISOU  526  CB  ALA A 128     9510   6878   8495    789   -734    -98       C  
ATOM    527  N   VAL A 129     -45.529 -34.865 108.895  1.00 67.74           N  
ANISOU  527  N   VAL A 129     9755   7056   8928    892   -663     28       N  
ATOM    528  CA  VAL A 129     -44.479 -35.819 109.256  1.00 70.57           C  
ANISOU  528  CA  VAL A 129    10049   7377   9387    944   -539    141       C  
ATOM    529  C   VAL A 129     -43.460 -35.335 110.334  1.00 71.72           C  
ANISOU  529  C   VAL A 129    10117   7651   9481   1041   -637    235       C  
ATOM    530  O   VAL A 129     -43.156 -36.059 111.306  1.00 76.56           O  
ANISOU  530  O   VAL A 129    10635   8340  10112   1150   -569    381       O  
ATOM    531  CB  VAL A 129     -43.726 -36.257 107.991  1.00 70.46           C  
ANISOU  531  CB  VAL A 129    10065   7236   9468    848   -424    108       C  
ATOM    532  CG1 VAL A 129     -42.538 -37.155 108.372  1.00 71.86           C  
ANISOU  532  CG1 VAL A 129    10163   7372   9766    934   -276    262       C  
ATOM    533  CG2 VAL A 129     -44.681 -37.006 107.056  1.00 69.88           C  
ANISOU  533  CG2 VAL A 129    10049   7071   9429    727   -295      4       C  
ATOM    534  N   TYR A 130     -42.917 -34.146 110.152  1.00 70.23           N  
ANISOU  534  N   TYR A 130     9953   7501   9228    992   -784    161       N  
ATOM    535  CA  TYR A 130     -41.901 -33.610 111.045  1.00 69.95           C  
ANISOU  535  CA  TYR A 130     9838   7609   9129   1025   -888    209       C  
ATOM    536  C   TYR A 130     -42.490 -32.917 112.265  1.00 69.07           C  
ANISOU  536  C   TYR A 130     9729   7641   8870   1075  -1007    156       C  
ATOM    537  O   TYR A 130     -41.882 -33.003 113.366  1.00 72.61           O  
ANISOU  537  O   TYR A 130    10072   8281   9233   1130  -1051    234       O  
ATOM    538  CB  TYR A 130     -40.977 -32.640 110.315  1.00 70.11           C  
ANISOU  538  CB  TYR A 130     9882   7592   9163    920   -973    139       C  
ATOM    539  CG  TYR A 130     -40.063 -33.308 109.386  1.00 69.43           C  
ANISOU  539  CG  TYR A 130     9759   7423   9198    893   -857    220       C  
ATOM    540  CD1 TYR A 130     -40.440 -33.564 108.134  1.00 70.05           C  
ANISOU  540  CD1 TYR A 130     9921   7351   9342    832   -766    163       C  
ATOM    541  CD2 TYR A 130     -38.832 -33.682 109.774  1.00 71.77           C  
ANISOU  541  CD2 TYR A 130     9925   7817   9527    930   -831    358       C  
ATOM    542  CE1 TYR A 130     -39.585 -34.182 107.237  1.00 72.74           C  
ANISOU  542  CE1 TYR A 130    10242   7607   9787    805   -634    217       C  
ATOM    543  CE2 TYR A 130     -37.957 -34.321 108.912  1.00 74.08           C  
ANISOU  543  CE2 TYR A 130    10181   8021   9944    926   -693    449       C  
ATOM    544  CZ  TYR A 130     -38.336 -34.564 107.619  1.00 73.54           C  
ANISOU  544  CZ  TYR A 130    10223   7769   9947    862   -586    363       C  
ATOM    545  OH  TYR A 130     -37.510 -35.197 106.710  1.00 72.70           O  
ANISOU  545  OH  TYR A 130    10101   7564   9956    854   -424    426       O  
ATOM    546  N   MET A 131     -43.625 -32.251 112.102  1.00 66.27           N  
ANISOU  546  N   MET A 131     9479   7227   8473   1062  -1048     39       N  
ATOM    547  CA  MET A 131     -44.289 -31.607 113.233  1.00 67.36           C  
ANISOU  547  CA  MET A 131     9638   7477   8478   1122  -1125    -22       C  
ATOM    548  C   MET A 131     -45.734 -32.086 113.484  1.00 66.54           C  
ANISOU  548  C   MET A 131     9556   7367   8359   1205  -1059      3       C  
ATOM    549  O   MET A 131     -46.620 -31.260 113.593  1.00 64.75           O  
ANISOU  549  O   MET A 131     9404   7122   8075   1224  -1099    -85       O  
ATOM    550  CB  MET A 131     -44.207 -30.072 113.090  1.00 68.30           C  
ANISOU  550  CB  MET A 131     9854   7542   8554   1048  -1228   -186       C  
ATOM    551  CG  MET A 131     -42.785 -29.594 113.228  1.00 71.16           C  
ANISOU  551  CG  MET A 131    10167   7964   8904    954  -1302   -218       C  
ATOM    552  SD  MET A 131     -42.431 -27.846 112.912  1.00 77.67           S  
ANISOU  552  SD  MET A 131    11104   8665   9739    824  -1382   -412       S  
ATOM    553  CE  MET A 131     -43.335 -27.002 114.225  1.00 78.42           C  
ANISOU  553  CE  MET A 131    11284   8824   9686    872  -1409   -570       C  
ATOM    554  N   PRO A 132     -45.963 -33.415 113.605  1.00 67.91           N  
ANISOU  554  N   PRO A 132     9657   7547   8595   1259   -939    137       N  
ATOM    555  CA  PRO A 132     -47.321 -33.919 113.663  1.00 68.91           C  
ANISOU  555  CA  PRO A 132     9795   7653   8735   1301   -866    160       C  
ATOM    556  C   PRO A 132     -47.896 -33.710 115.002  1.00 72.36           C  
ANISOU  556  C   PRO A 132    10205   8244   9044   1419   -897    187       C  
ATOM    557  O   PRO A 132     -47.172 -33.474 115.948  1.00 73.54           O  
ANISOU  557  O   PRO A 132    10307   8541   9091   1467   -954    208       O  
ATOM    558  CB  PRO A 132     -47.171 -35.411 113.436  1.00 68.88           C  
ANISOU  558  CB  PRO A 132     9724   7581   8866   1304   -698    287       C  
ATOM    559  CG  PRO A 132     -45.807 -35.764 113.950  1.00 69.95           C  
ANISOU  559  CG  PRO A 132     9774   7788   9015   1357   -680    405       C  
ATOM    560  CD  PRO A 132     -44.981 -34.513 113.767  1.00 70.04           C  
ANISOU  560  CD  PRO A 132     9822   7844   8944   1292   -842    291       C  
ATOM    561  N   LYS A 133     -49.219 -33.775 115.076  1.00 76.81           N  
ANISOU  561  N   LYS A 133    10784   8801   9595   1458   -860    186       N  
ATOM    562  CA  LYS A 133     -49.947 -33.540 116.324  1.00 79.62           C  
ANISOU  562  CA  LYS A 133    11123   9304   9823   1583   -871    210       C  
ATOM    563  C   LYS A 133     -49.894 -34.785 117.128  1.00 82.09           C  
ANISOU  563  C   LYS A 133    11324   9708  10156   1671   -764    389       C  
ATOM    564  O   LYS A 133     -50.226 -35.856 116.634  1.00 81.12           O  
ANISOU  564  O   LYS A 133    11161   9483  10178   1641   -637    480       O  
ATOM    565  CB  LYS A 133     -51.397 -33.200 116.062  1.00 82.04           C  
ANISOU  565  CB  LYS A 133    11465   9579  10127   1605   -853    180       C  
ATOM    566  CG  LYS A 133     -52.239 -32.927 117.289  1.00 85.19           C  
ANISOU  566  CG  LYS A 133    11851  10118  10398   1746   -842    206       C  
ATOM    567  CD  LYS A 133     -53.667 -32.689 116.898  1.00 88.48           C  
ANISOU  567  CD  LYS A 133    12273  10508  10835   1771   -808    215       C  
ATOM    568  CE  LYS A 133     -54.470 -32.335 118.105  1.00 92.02           C  
ANISOU  568  CE  LYS A 133    12717  11089  11158   1926   -781    238       C  
ATOM    569  NZ  LYS A 133     -55.808 -31.815 117.711  1.00 97.36           N  
ANISOU  569  NZ  LYS A 133    13395  11748  11847   1971   -753    252       N  
ATOM    570  N   CYS A 134     -49.459 -34.614 118.371  1.00 89.43           N  
ANISOU  570  N   CYS A 134    12201  10840  10935   1769   -806    436       N  
ATOM    571  CA  CYS A 134     -49.475 -35.697 119.349  1.00 94.98           C  
ANISOU  571  CA  CYS A 134    12777  11686  11623   1895   -700    651       C  
ATOM    572  C   CYS A 134     -50.406 -35.257 120.498  1.00 95.98           C  
ANISOU  572  C   CYS A 134    12903  11994  11569   2012   -722    641       C  
ATOM    573  O   CYS A 134     -50.209 -34.163 121.073  1.00 91.76           O  
ANISOU  573  O   CYS A 134    12425  11591  10849   2014   -838    492       O  
ATOM    574  CB  CYS A 134     -48.044 -35.955 119.785  1.00 98.31           C  
ANISOU  574  CB  CYS A 134    13099  12254  11999   1917   -727    756       C  
ATOM    575  SG  CYS A 134     -47.933 -37.416 120.773  1.00102.40           S  
ANISOU  575  SG  CYS A 134    13433  12924  12547   2092   -555   1095       S  
ATOM    576  N   GLU A 135     -51.439 -36.069 120.782  1.00 98.45           N  
ANISOU  576  N   GLU A 135    13162  12299  11945   2093   -594    781       N  
ATOM    577  CA  GLU A 135     -52.350 -35.760 121.905  1.00103.25           C  
ANISOU  577  CA  GLU A 135    13755  13091  12383   2225   -588    803       C  
ATOM    578  C   GLU A 135     -52.607 -37.017 122.725  1.00105.78           C  
ANISOU  578  C   GLU A 135    13931  13523  12735   2356   -437   1076       C  
ATOM    579  O   GLU A 135     -53.041 -38.026 122.177  1.00103.77           O  
ANISOU  579  O   GLU A 135    13634  13096  12696   2326   -295   1196       O  
ATOM    580  CB  GLU A 135     -53.670 -35.150 121.417  1.00106.82           C  
ANISOU  580  CB  GLU A 135    14291  13428  12865   2206   -588    689       C  
ATOM    581  CG  GLU A 135     -54.168 -33.984 122.274  1.00111.18           C  
ANISOU  581  CG  GLU A 135    14915  14121  13205   2298   -647    561       C  
ATOM    582  CD  GLU A 135     -55.484 -33.379 121.775  1.00115.35           C  
ANISOU  582  CD  GLU A 135    15504  14541  13781   2313   -622    498       C  
ATOM    583  OE1 GLU A 135     -56.093 -33.863 120.786  1.00118.04           O  
ANISOU  583  OE1 GLU A 135    15812  14745  14291   2238   -580    555       O  
ATOM    584  OE2 GLU A 135     -55.918 -32.374 122.350  1.00120.65           O  
ANISOU  584  OE2 GLU A 135    16252  15275  14313   2396   -635    388       O  
ATOM    585  N   ASN A 136     -52.292 -36.924 124.032  1.00108.55           N  
ANISOU  585  N   ASN A 136    14204  14173  12864   2488   -461   1167       N  
ATOM    586  CA  ASN A 136     -52.404 -38.013 125.015  1.00109.28           C  
ANISOU  586  CA  ASN A 136    14137  14442  12941   2650   -319   1469       C  
ATOM    587  C   ASN A 136     -51.754 -39.292 124.533  1.00107.10           C  
ANISOU  587  C   ASN A 136    13763  14017  12913   2647   -169   1696       C  
ATOM    588  O   ASN A 136     -52.403 -40.298 124.289  1.00103.56           O  
ANISOU  588  O   ASN A 136    13272  13391  12681   2665     16   1849       O  
ATOM    589  CB  ASN A 136     -53.854 -38.228 125.432  1.00112.01           C  
ANISOU  589  CB  ASN A 136    14473  14790  13295   2738   -216   1535       C  
ATOM    590  CG  ASN A 136     -54.438 -37.003 126.141  1.00118.99           C  
ANISOU  590  CG  ASN A 136    15441  15857  13912   2791   -323   1346       C  
ATOM    591  OD1 ASN A 136     -53.730 -36.099 126.620  1.00123.97           O  
ANISOU  591  OD1 ASN A 136    16120  16668  14314   2777   -455   1186       O  
ATOM    592  ND2 ASN A 136     -55.742 -36.945 126.157  1.00124.64           N  
ANISOU  592  ND2 ASN A 136    16178  16512  14667   2837   -251   1349       N  
ATOM    593  N   ASP A 137     -50.441 -39.198 124.389  1.00106.80           N  
ANISOU  593  N   ASP A 137    13690  14044  12845   2615   -239   1706       N  
ATOM    594  CA  ASP A 137     -49.591 -40.280 123.938  1.00109.25           C  
ANISOU  594  CA  ASP A 137    13909  14223  13379   2630    -91   1921       C  
ATOM    595  C   ASP A 137     -50.051 -40.996 122.657  1.00107.27           C  
ANISOU  595  C   ASP A 137    13743  13555  13460   2508     67   1873       C  
ATOM    596  O   ASP A 137     -49.690 -42.164 122.434  1.00110.29           O  
ANISOU  596  O   ASP A 137    14051  13780  14073   2550    285   2087       O  
ATOM    597  CB  ASP A 137     -49.288 -41.246 125.094  1.00116.44           C  
ANISOU  597  CB  ASP A 137    14613  15380  14247   2846     56   2304       C  
ATOM    598  CG  ASP A 137     -48.212 -40.676 126.086  1.00119.37           C  
ANISOU  598  CG  ASP A 137    14855  16206  14292   2921   -111   2372       C  
ATOM    599  OD1 ASP A 137     -47.765 -39.489 125.953  1.00112.54           O  
ANISOU  599  OD1 ASP A 137    14076  15447  13236   2789   -339   2087       O  
ATOM    600  OD2 ASP A 137     -47.794 -41.458 126.990  1.00128.21           O  
ANISOU  600  OD2 ASP A 137    15772  17586  15356   3107     -1   2728       O  
ATOM    601  N   ARG A 138     -50.744 -40.268 121.779  1.00103.26           N  
ANISOU  601  N   ARG A 138    13384  12879  12969   2350    -32   1592       N  
ATOM    602  CA  ARG A 138     -51.043 -40.739 120.432  1.00102.05           C  
ANISOU  602  CA  ARG A 138    13313  12393  13065   2184     66   1485       C  
ATOM    603  C   ARG A 138     -50.757 -39.656 119.368  1.00 97.52           C  
ANISOU  603  C   ARG A 138    12873  11734  12444   2020   -116   1203       C  
ATOM    604  O   ARG A 138     -51.293 -38.555 119.470  1.00 97.98           O  
ANISOU  604  O   ARG A 138    13000  11884  12341   2003   -276   1041       O  
ATOM    605  CB  ARG A 138     -52.478 -41.174 120.351  1.00102.94           C  
ANISOU  605  CB  ARG A 138    13433  12408  13272   2148    173   1484       C  
ATOM    606  CG  ARG A 138     -52.804 -42.023 119.126  1.00105.39           C  
ANISOU  606  CG  ARG A 138    13788  12407  13847   1964    335   1414       C  
ATOM    607  CD  ARG A 138     -54.303 -41.969 118.847  1.00105.09           C  
ANISOU  607  CD  ARG A 138    13763  12340  13825   1862    339   1319       C  
ATOM    608  NE  ARG A 138     -54.662 -40.676 118.281  1.00104.41           N  
ANISOU  608  NE  ARG A 138    13762  12330  13576   1784    113   1097       N  
ATOM    609  CZ  ARG A 138     -55.272 -40.521 117.110  1.00110.15           C  
ANISOU  609  CZ  ARG A 138    14538  12956  14357   1591     82    928       C  
ATOM    610  NH1 ARG A 138     -55.572 -41.580 116.333  1.00109.49           N  
ANISOU  610  NH1 ARG A 138    14440  12689  14471   1415    253    902       N  
ATOM    611  NH2 ARG A 138     -55.578 -39.280 116.680  1.00113.71           N  
ANISOU  611  NH2 ARG A 138    15048  13497  14659   1564   -108    781       N  
ATOM    612  N   VAL A 139     -49.903 -40.014 118.384  1.00 91.70           N  
ANISOU  612  N   VAL A 139    12166  10815  11860   1919    -61   1170       N  
ATOM    613  CA  VAL A 139     -49.496 -39.086 117.331  1.00 88.13           C  
ANISOU  613  CA  VAL A 139    11824  10283  11379   1774   -210    943       C  
ATOM    614  C   VAL A 139     -50.361 -39.367 116.109  1.00 86.90           C  
ANISOU  614  C   VAL A 139    11744   9915  11357   1606   -142    806       C  
ATOM    615  O   VAL A 139     -50.659 -40.530 115.808  1.00 88.49           O  
ANISOU  615  O   VAL A 139    11920   9960  11740   1559     61    874       O  
ATOM    616  CB  VAL A 139     -47.973 -39.162 117.002  1.00 90.05           C  
ANISOU  616  CB  VAL A 139    12042  10506  11667   1765   -212    986       C  
ATOM    617  CG1 VAL A 139     -47.513 -40.538 116.516  1.00 91.94           C  
ANISOU  617  CG1 VAL A 139    12238  10541  12151   1765     41   1133       C  
ATOM    618  CG2 VAL A 139     -47.569 -38.131 115.964  1.00 89.15           C  
ANISOU  618  CG2 VAL A 139    12034  10320  11515   1621   -365    766       C  
ATOM    619  N   GLU A 140     -50.792 -38.315 115.422  1.00 85.94           N  
ANISOU  619  N   GLU A 140    11707   9799  11145   1509   -297    617       N  
ATOM    620  CA  GLU A 140     -51.676 -38.454 114.291  1.00 88.18           C  
ANISOU  620  CA  GLU A 140    12033   9971  11498   1346   -267    497       C  
ATOM    621  C   GLU A 140     -50.862 -38.740 112.992  1.00 92.98           C  
ANISOU  621  C   GLU A 140    12697  10418  12212   1192   -217    399       C  
ATOM    622  O   GLU A 140     -49.986 -37.944 112.591  1.00 96.04           O  
ANISOU  622  O   GLU A 140    13132  10814  12543   1181   -332    334       O  
ATOM    623  CB  GLU A 140     -52.535 -37.208 114.123  1.00 89.25           C  
ANISOU  623  CB  GLU A 140    12208  10212  11488   1340   -433    391       C  
ATOM    624  CG  GLU A 140     -53.559 -36.983 115.206  1.00 93.40           C  
ANISOU  624  CG  GLU A 140    12686  10877  11921   1473   -446    467       C  
ATOM    625  CD  GLU A 140     -54.583 -35.872 114.880  1.00 98.51           C  
ANISOU  625  CD  GLU A 140    13361  11600  12466   1473   -557    388       C  
ATOM    626  OE1 GLU A 140     -54.508 -35.254 113.778  1.00101.86           O  
ANISOU  626  OE1 GLU A 140    13834  11980  12887   1370   -630    288       O  
ATOM    627  OE2 GLU A 140     -55.485 -35.615 115.728  1.00 99.71           O  
ANISOU  627  OE2 GLU A 140    13478  11865  12541   1594   -554    449       O  
ATOM    628  N   LEU A 141     -51.191 -39.853 112.320  1.00 94.59           N  
ANISOU  628  N   LEU A 141    12899  10473  12567   1060    -34    374       N  
ATOM    629  CA  LEU A 141     -50.517 -40.276 111.093  1.00 91.36           C  
ANISOU  629  CA  LEU A 141    12549   9905  12256    905     57    264       C  
ATOM    630  C   LEU A 141     -51.085 -39.563 109.884  1.00 91.06           C  
ANISOU  630  C   LEU A 141    12560   9924  12114    732    -67     82       C  
ATOM    631  O   LEU A 141     -52.303 -39.305 109.818  1.00 90.60           O  
ANISOU  631  O   LEU A 141    12467   9978  11977    677   -133     46       O  
ATOM    632  CB  LEU A 141     -50.696 -41.770 110.867  1.00 93.43           C  
ANISOU  632  CB  LEU A 141    12804   9969  12724    811    340    277       C  
ATOM    633  CG  LEU A 141     -49.993 -42.697 111.838  1.00 95.39           C  
ANISOU  633  CG  LEU A 141    12996  10117  13129    985    538    498       C  
ATOM    634  CD1 LEU A 141     -50.508 -44.117 111.595  1.00 98.50           C  
ANISOU  634  CD1 LEU A 141    13394  10280  13750    869    846    492       C  
ATOM    635  CD2 LEU A 141     -48.492 -42.647 111.681  1.00 97.03           C  
ANISOU  635  CD2 LEU A 141    13214  10272  13379   1070    565    566       C  
ATOM    636  N   PRO A 142     -50.220 -39.269 108.898  1.00 91.05           N  
ANISOU  636  N   PRO A 142    12620   9867  12107    651    -90     -9       N  
ATOM    637  CA  PRO A 142     -50.733 -38.544 107.730  1.00 89.82           C  
ANISOU  637  CA  PRO A 142    12490   9806  11829    503   -211   -147       C  
ATOM    638  C   PRO A 142     -51.392 -39.501 106.757  1.00 87.86           C  
ANISOU  638  C   PRO A 142    12243   9518  11621    268    -69   -284       C  
ATOM    639  O   PRO A 142     -50.899 -40.588 106.582  1.00 86.02           O  
ANISOU  639  O   PRO A 142    12044   9104  11536    199    141   -321       O  
ATOM    640  CB  PRO A 142     -49.469 -37.912 107.110  1.00 90.19           C  
ANISOU  640  CB  PRO A 142    12595   9813  11859    514   -271   -173       C  
ATOM    641  CG  PRO A 142     -48.314 -38.317 107.996  1.00 91.19           C  
ANISOU  641  CG  PRO A 142    12710   9841  12095    661   -192    -50       C  
ATOM    642  CD  PRO A 142     -48.770 -39.519 108.776  1.00 90.55           C  
ANISOU  642  CD  PRO A 142    12584   9686  12134    701    -11     33       C  
ATOM    643  N   SER A 143     -52.472 -39.075 106.107  1.00 88.90           N  
ANISOU  643  N   SER A 143    12331   9828  11617    140   -174   -359       N  
ATOM    644  CA  SER A 143     -53.222 -39.908 105.144  1.00 89.10           C  
ANISOU  644  CA  SER A 143    12335   9889  11630   -133    -67   -519       C  
ATOM    645  C   SER A 143     -52.448 -40.200 103.877  1.00 88.86           C  
ANISOU  645  C   SER A 143    12381   9794  11588   -306     15   -681       C  
ATOM    646  O   SER A 143     -51.577 -39.419 103.466  1.00 88.46           O  
ANISOU  646  O   SER A 143    12375   9755  11481   -228    -77   -659       O  
ATOM    647  CB  SER A 143     -54.557 -39.269 104.737  1.00 90.97           C  
ANISOU  647  CB  SER A 143    12464  10415  11684   -221   -228   -525       C  
ATOM    648  OG  SER A 143     -54.380 -38.084 103.989  1.00 91.34           O  
ANISOU  648  OG  SER A 143    12508  10625  11571   -188   -402   -507       O  
ATOM    649  N   ARG A 144     -52.791 -41.315 103.244  1.00 90.94           N  
ANISOU  649  N   ARG A 144    12659   9989  11903   -556    203   -857       N  
ATOM    650  CA  ARG A 144     -52.213 -41.663 101.956  1.00 95.11           C  
ANISOU  650  CA  ARG A 144    13264  10481  12390   -759    306  -1055       C  
ATOM    651  C   ARG A 144     -52.371 -40.567 100.843  1.00 93.61           C  
ANISOU  651  C   ARG A 144    13035  10593  11937   -835     88  -1095       C  
ATOM    652  O   ARG A 144     -51.396 -40.198 100.148  1.00 91.82           O  
ANISOU  652  O   ARG A 144    12876  10338  11671   -814     84  -1121       O  
ATOM    653  CB  ARG A 144     -52.795 -42.978 101.473  1.00100.99           C  
ANISOU  653  CB  ARG A 144    14027  11136  13206  -1061    542  -1278       C  
ATOM    654  CG  ARG A 144     -52.091 -43.434 100.199  1.00107.90           C  
ANISOU  654  CG  ARG A 144    15008  11939  14047  -1269    697  -1511       C  
ATOM    655  CD  ARG A 144     -52.803 -44.584  99.500  1.00114.07           C  
ANISOU  655  CD  ARG A 144    15810  12694  14836  -1644    911  -1806       C  
ATOM    656  NE  ARG A 144     -54.201 -44.205  99.203  1.00117.42           N  
ANISOU  656  NE  ARG A 144    16082  13501  15028  -1837    706  -1855       N  
ATOM    657  CZ  ARG A 144     -54.593 -43.353  98.251  1.00117.91           C  
ANISOU  657  CZ  ARG A 144    16058  13956  14785  -1946    478  -1894       C  
ATOM    658  NH1 ARG A 144     -55.894 -43.091  98.119  1.00116.48           N  
ANISOU  658  NH1 ARG A 144    15707  14129  14419  -2094    312  -1889       N  
ATOM    659  NH2 ARG A 144     -53.706 -42.777  97.411  1.00120.03           N  
ANISOU  659  NH2 ARG A 144    16390  14285  14930  -1904    425  -1915       N  
ATOM    660  N   THR A 145     -53.581 -40.045 100.706  1.00 93.54           N  
ANISOU  660  N   THR A 145    12902  10879  11756   -900    -78  -1064       N  
ATOM    661  CA  THR A 145     -53.903 -39.042  99.714  1.00 96.95           C  
ANISOU  661  CA  THR A 145    13260  11634  11940   -952   -269  -1046       C  
ATOM    662  C   THR A 145     -53.065 -37.791  99.842  1.00 95.33           C  
ANISOU  662  C   THR A 145    13092  11406  11724   -693   -407   -872       C  
ATOM    663  O   THR A 145     -52.864 -37.104  98.855  1.00100.58           O  
ANISOU  663  O   THR A 145    13737  12245  12231   -731   -494   -865       O  
ATOM    664  CB  THR A 145     -55.370 -38.591  99.808  1.00104.47           C  
ANISOU  664  CB  THR A 145    14039  12913  12739   -987   -425   -955       C  
ATOM    665  OG1 THR A 145     -55.649 -38.178 101.158  1.00117.90           O  
ANISOU  665  OG1 THR A 145    15720  14516  14558   -724   -481   -761       O  
ATOM    666  CG2 THR A 145     -56.374 -39.721  99.394  1.00106.70           C  
ANISOU  666  CG2 THR A 145    14242  13327  12970  -1327   -322  -1153       C  
ATOM    667  N   LEU A 146     -52.585 -37.478 101.045  1.00 94.60           N  
ANISOU  667  N   LEU A 146    13044  11114  11786   -443   -422   -730       N  
ATOM    668  CA  LEU A 146     -51.631 -36.360 101.270  1.00 91.84           C  
ANISOU  668  CA  LEU A 146    12744  10693  11457   -226   -526   -599       C  
ATOM    669  C   LEU A 146     -50.225 -36.664 100.741  1.00 89.76           C  
ANISOU  669  C   LEU A 146    12581  10252  11271   -252   -418   -669       C  
ATOM    670  O   LEU A 146     -49.506 -35.766 100.284  1.00 85.68           O  
ANISOU  670  O   LEU A 146    12086   9756  10711   -182   -499   -609       O  
ATOM    671  CB  LEU A 146     -51.548 -36.050 102.764  1.00 89.75           C  
ANISOU  671  CB  LEU A 146    12488  10300  11310      5   -564   -465       C  
ATOM    672  CG  LEU A 146     -50.857 -34.740 103.162  1.00 89.23           C  
ANISOU  672  CG  LEU A 146    12456  10199  11246    204   -690   -348       C  
ATOM    673  CD1 LEU A 146     -51.768 -33.540 102.934  1.00 91.16           C  
ANISOU  673  CD1 LEU A 146    12637  10634  11364    271   -831   -251       C  
ATOM    674  CD2 LEU A 146     -50.432 -34.821 104.616  1.00 88.50           C  
ANISOU  674  CD2 LEU A 146    12391   9965  11269    376   -677   -279       C  
ATOM    675  N   CYS A 147     -49.846 -37.935 100.817  1.00 93.16           N  
ANISOU  675  N   CYS A 147    13067  10497  11832   -346   -213   -780       N  
ATOM    676  CA  CYS A 147     -48.503 -38.345 100.428  1.00 95.94           C  
ANISOU  676  CA  CYS A 147    13507  10657  12287   -342    -69   -824       C  
ATOM    677  C   CYS A 147     -48.437 -38.524  98.938  1.00 96.53           C  
ANISOU  677  C   CYS A 147    13610  10841  12225   -560    -10   -992       C  
ATOM    678  O   CYS A 147     -47.482 -38.076  98.291  1.00 95.74           O  
ANISOU  678  O   CYS A 147    13548  10728  12098   -529    -14   -977       O  
ATOM    679  CB  CYS A 147     -48.161 -39.660 101.116  1.00100.80           C  
ANISOU  679  CB  CYS A 147    14165  11014  13119   -330    171   -846       C  
ATOM    680  SG  CYS A 147     -46.555 -40.356 100.701  1.00108.59           S  
ANISOU  680  SG  CYS A 147    15243  11746  14270   -300    412   -868       S  
ATOM    681  N   GLN A 148     -49.440 -39.222  98.395  1.00 97.81           N  
ANISOU  681  N   GLN A 148    13745  11123  12292   -797     53  -1162       N  
ATOM    682  CA  GLN A 148     -49.532 -39.471  96.938  1.00 99.11           C  
ANISOU  682  CA  GLN A 148    13925  11459  12272  -1055    110  -1364       C  
ATOM    683  C   GLN A 148     -49.598 -38.179  96.109  1.00 93.60           C  
ANISOU  683  C   GLN A 148    13155  11069  11339  -1022   -108  -1261       C  
ATOM    684  O   GLN A 148     -48.980 -38.095  95.049  1.00 94.33           O  
ANISOU  684  O   GLN A 148    13285  11231  11323  -1110    -61  -1340       O  
ATOM    685  CB  GLN A 148     -50.717 -40.417  96.630  1.00104.95           C  
ANISOU  685  CB  GLN A 148    14625  12316  12935  -1347    198  -1575       C  
ATOM    686  CG  GLN A 148     -50.923 -40.756  95.160  1.00109.01           C  
ANISOU  686  CG  GLN A 148    15142  13059  13215  -1664    258  -1827       C  
ATOM    687  CD  GLN A 148     -50.019 -41.838  94.686  1.00115.71           C  
ANISOU  687  CD  GLN A 148    16149  13621  14191  -1793    566  -2054       C  
ATOM    688  OE1 GLN A 148     -49.213 -41.651  93.750  1.00114.67           O  
ANISOU  688  OE1 GLN A 148    16080  13529  13960  -1825    616  -2122       O  
ATOM    689  NE2 GLN A 148     -50.115 -42.984  95.340  1.00126.79           N  
ANISOU  689  NE2 GLN A 148    17622  14715  15834  -1851    804  -2155       N  
ATOM    690  N   ALA A 149     -50.324 -37.193  96.593  1.00 87.99           N  
ANISOU  690  N   ALA A 149    12341  10527  10562   -884   -317  -1074       N  
ATOM    691  CA  ALA A 149     -50.373 -35.904  95.948  1.00 88.00           C  
ANISOU  691  CA  ALA A 149    12269  10771  10393   -802   -494   -920       C  
ATOM    692  C   ALA A 149     -49.038 -35.257  95.604  1.00 85.58           C  
ANISOU  692  C   ALA A 149    12038  10336  10142   -674   -485   -840       C  
ATOM    693  O   ALA A 149     -49.016 -34.435  94.684  1.00 85.43           O  
ANISOU  693  O   ALA A 149    11964  10537   9958   -677   -572   -756       O  
ATOM    694  CB  ALA A 149     -51.162 -34.941  96.809  1.00 90.65           C  
ANISOU  694  CB  ALA A 149    12515  11186  10739   -605   -663   -706       C  
ATOM    695  N   THR A 150     -47.966 -35.599  96.325  1.00 85.64           N  
ANISOU  695  N   THR A 150    12145  10021  10372   -559   -383   -838       N  
ATOM    696  CA  THR A 150     -46.603 -35.076  96.073  1.00 89.74           C  
ANISOU  696  CA  THR A 150    12721  10408  10968   -449   -361   -761       C  
ATOM    697  C   THR A 150     -45.748 -35.873  95.094  1.00 94.80           C  
ANISOU  697  C   THR A 150    13436  10988  11595   -586   -171   -913       C  
ATOM    698  O   THR A 150     -44.796 -35.318  94.491  1.00 98.57           O  
ANISOU  698  O   THR A 150    13931  11460  12062   -535   -167   -846       O  
ATOM    699  CB  THR A 150     -45.740 -35.000  97.347  1.00 89.88           C  
ANISOU  699  CB  THR A 150    12779  10154  11218   -254   -351   -657       C  
ATOM    700  OG1 THR A 150     -45.534 -36.326  97.857  1.00 89.62           O  
ANISOU  700  OG1 THR A 150    12794   9929  11327   -293   -164   -758       O  
ATOM    701  CG2 THR A 150     -46.376 -34.064  98.419  1.00 88.07           C  
ANISOU  701  CG2 THR A 150    12499   9952  11009    -94   -526   -513       C  
ATOM    702  N   ARG A 151     -46.091 -37.150  94.908  1.00 97.94           N  
ANISOU  702  N   ARG A 151    13879  11332  12001   -766      6  -1123       N  
ATOM    703  CA  ARG A 151     -45.279 -38.060  94.069  1.00 97.95           C  
ANISOU  703  CA  ARG A 151    13978  11218  12020   -897    249  -1302       C  
ATOM    704  C   ARG A 151     -45.057 -37.487  92.681  1.00 99.67           C  
ANISOU  704  C   ARG A 151    14178  11690  12000   -995    208  -1333       C  
ATOM    705  O   ARG A 151     -43.927 -37.555  92.137  1.00 99.08           O  
ANISOU  705  O   ARG A 151    14167  11511  11968   -963    337  -1340       O  
ATOM    706  CB  ARG A 151     -45.952 -39.405  93.911  1.00 99.54           C  
ANISOU  706  CB  ARG A 151    14229  11363  12226  -1130    450  -1561       C  
ATOM    707  CG  ARG A 151     -46.207 -40.156  95.200  1.00101.89           C  
ANISOU  707  CG  ARG A 151    14543  11403  12768  -1050    543  -1530       C  
ATOM    708  CD  ARG A 151     -44.944 -40.379  96.008  1.00100.60           C  
ANISOU  708  CD  ARG A 151    14429  10920  12873   -814    671  -1377       C  
ATOM    709  NE  ARG A 151     -44.715 -39.323  96.962  1.00 97.04           N  
ANISOU  709  NE  ARG A 151    13902  10500  12466   -572    441  -1121       N  
ATOM    710  CZ  ARG A 151     -43.805 -39.368  97.907  1.00 99.69           C  
ANISOU  710  CZ  ARG A 151    14233  10644  13000   -364    483   -953       C  
ATOM    711  NH1 ARG A 151     -43.004 -40.418  98.048  1.00101.93           N  
ANISOU  711  NH1 ARG A 151    14570  10680  13478   -328    755   -964       N  
ATOM    712  NH2 ARG A 151     -43.684 -38.340  98.722  1.00103.06           N  
ANISOU  712  NH2 ARG A 151    14592  11138  13425   -192    261   -768       N  
ATOM    713  N   GLY A 152     -46.149 -36.922  92.129  1.00 97.43           N  
ANISOU  713  N   GLY A 152    13792  11763  11463  -1101     35  -1325       N  
ATOM    714  CA  GLY A 152     -46.159 -36.354  90.796  1.00 96.47           C  
ANISOU  714  CA  GLY A 152    13616  11971  11065  -1200    -21  -1324       C  
ATOM    715  C   GLY A 152     -45.268 -35.149  90.704  1.00 93.16           C  
ANISOU  715  C   GLY A 152    13177  11525  10695   -978   -119  -1068       C  
ATOM    716  O   GLY A 152     -44.186 -35.238  90.160  1.00 94.60           O  
ANISOU  716  O   GLY A 152    13424  11608  10909   -963      4  -1088       O  
ATOM    717  N   PRO A 153     -45.721 -34.015  91.218  1.00 90.87           N  
ANISOU  717  N   PRO A 153    12796  11311  10419   -810   -320   -830       N  
ATOM    718  CA  PRO A 153     -44.941 -32.789  91.045  1.00 91.65           C  
ANISOU  718  CA  PRO A 153    12871  11383  10566   -627   -397   -594       C  
ATOM    719  C   PRO A 153     -43.590 -32.746  91.775  1.00 89.53           C  
ANISOU  719  C   PRO A 153    12689  10750  10576   -480   -324   -541       C  
ATOM    720  O   PRO A 153     -42.686 -32.060  91.280  1.00 90.72           O  
ANISOU  720  O   PRO A 153    12836  10882  10748   -408   -317   -418       O  
ATOM    721  CB  PRO A 153     -45.866 -31.685  91.578  1.00 91.50           C  
ANISOU  721  CB  PRO A 153    12751  11479  10536   -487   -586   -377       C  
ATOM    722  CG  PRO A 153     -46.792 -32.411  92.490  1.00 90.78           C  
ANISOU  722  CG  PRO A 153    12659  11342  10492   -534   -602   -491       C  
ATOM    723  CD  PRO A 153     -46.997 -33.769  91.890  1.00 90.63           C  
ANISOU  723  CD  PRO A 153    12676  11402  10356   -787   -462   -765       C  
ATOM    724  N   CYS A 154     -43.429 -33.461  92.893  1.00 87.37           N  
ANISOU  724  N   CYS A 154    12472  10221  10502   -438   -267   -612       N  
ATOM    725  CA  CYS A 154     -42.119 -33.497  93.561  1.00 86.89           C  
ANISOU  725  CA  CYS A 154    12458   9878  10676   -308   -197   -546       C  
ATOM    726  C   CYS A 154     -41.237 -34.626  93.057  1.00 90.19           C  
ANISOU  726  C   CYS A 154    12949  10168  11148   -385     40   -683       C  
ATOM    727  O   CYS A 154     -40.496 -35.227  93.852  1.00 89.07           O  
ANISOU  727  O   CYS A 154    12837   9789  11213   -300    149   -668       O  
ATOM    728  CB  CYS A 154     -42.269 -33.569  95.084  1.00 85.83           C  
ANISOU  728  CB  CYS A 154    12322   9567  10722   -187   -258   -496       C  
ATOM    729  SG  CYS A 154     -43.142 -32.146  95.793  1.00 87.31           S  
ANISOU  729  SG  CYS A 154    12445   9845  10883    -66   -498   -337       S  
ATOM    730  N   ALA A 155     -41.287 -34.895  91.739  1.00 93.22           N  
ANISOU  730  N   ALA A 155    13354  10722  11340   -536    136   -803       N  
ATOM    731  CA  ALA A 155     -40.536 -35.998  91.126  1.00 94.78           C  
ANISOU  731  CA  ALA A 155    13641  10799  11569   -626    404   -970       C  
ATOM    732  C   ALA A 155     -39.045 -35.742  91.126  1.00 93.48           C  
ANISOU  732  C   ALA A 155    13481  10468  11569   -481    490   -825       C  
ATOM    733  O   ALA A 155     -38.259 -36.675  91.069  1.00 95.72           O  
ANISOU  733  O   ALA A 155    13828  10561  11980   -474    730   -899       O  
ATOM    734  CB  ALA A 155     -41.005 -36.233  89.712  1.00 98.99           C  
ANISOU  734  CB  ALA A 155    14191  11606  11813   -839    470  -1150       C  
ATOM    735  N   ILE A 156     -38.654 -34.482  91.188  1.00 92.35           N  
ANISOU  735  N   ILE A 156    13263  10389  11435   -365    312   -611       N  
ATOM    736  CA  ILE A 156     -37.251 -34.119  91.313  1.00 93.64           C  
ANISOU  736  CA  ILE A 156    13399  10411  11766   -237    360   -450       C  
ATOM    737  C   ILE A 156     -36.546 -34.715  92.559  1.00 92.13           C  
ANISOU  737  C   ILE A 156    13199   9968  11836   -116    432   -391       C  
ATOM    738  O   ILE A 156     -35.324 -34.989  92.548  1.00 94.98           O  
ANISOU  738  O   ILE A 156    13541  10208  12337    -38    573   -305       O  
ATOM    739  CB  ILE A 156     -37.137 -32.582  91.149  1.00 94.60           C  
ANISOU  739  CB  ILE A 156    13441  10648  11851   -170    155   -247       C  
ATOM    740  CG1 ILE A 156     -35.693 -32.156  90.930  1.00 96.08           C  
ANISOU  740  CG1 ILE A 156    13590  10746  12170    -91    219    -95       C  
ATOM    741  CG2 ILE A 156     -37.726 -31.784  92.285  1.00 92.37           C  
ANISOU  741  CG2 ILE A 156    13118  10327  11650    -89    -54   -151       C  
ATOM    742  CD1 ILE A 156     -35.629 -30.920  90.076  1.00 97.23           C  
ANISOU  742  CD1 ILE A 156    13683  11048  12211    -88    124     52       C  
ATOM    743  N   VAL A 157     -37.327 -34.998  93.590  1.00 92.19           N  
ANISOU  743  N   VAL A 157    13207   9922  11896    -96    356   -423       N  
ATOM    744  CA  VAL A 157     -36.815 -35.626  94.813  1.00 94.13           C  
ANISOU  744  CA  VAL A 157    13427   9982  12356     22    423   -350       C  
ATOM    745  C   VAL A 157     -36.375 -37.036  94.510  1.00 95.87           C  
ANISOU  745  C   VAL A 157    13711  10041  12673      5    739   -446       C  
ATOM    746  O   VAL A 157     -35.282 -37.424  94.913  1.00 96.54           O  
ANISOU  746  O   VAL A 157    13751   9994  12935    130    873   -314       O  
ATOM    747  CB  VAL A 157     -37.857 -35.630  95.977  1.00 94.05           C  
ANISOU  747  CB  VAL A 157    13402   9972  12358     48    282   -360       C  
ATOM    748  CG1 VAL A 157     -37.316 -36.304  97.237  1.00 90.90           C  
ANISOU  748  CG1 VAL A 157    12957   9424  12156    182    358   -254       C  
ATOM    749  CG2 VAL A 157     -38.294 -34.189  96.281  1.00 94.35           C  
ANISOU  749  CG2 VAL A 157    13392  10138  12317     78      5   -270       C  
ATOM    750  N   GLU A 158     -37.208 -37.803  93.802  1.00101.31           N  
ANISOU  750  N   GLU A 158    14497  10745  13251   -153    875   -673       N  
ATOM    751  CA  GLU A 158     -36.865 -39.205  93.512  1.00108.58           C  
ANISOU  751  CA  GLU A 158    15507  11461  14287   -188   1228   -805       C  
ATOM    752  C   GLU A 158     -35.745 -39.337  92.510  1.00113.98           C  
ANISOU  752  C   GLU A 158    16220  12109  14976   -177   1429   -803       C  
ATOM    753  O   GLU A 158     -35.100 -40.380  92.459  1.00120.34           O  
ANISOU  753  O   GLU A 158    17079  12695  15947   -129   1748   -831       O  
ATOM    754  CB  GLU A 158     -38.048 -40.062  93.106  1.00112.15           C  
ANISOU  754  CB  GLU A 158    16059  11916  14637   -397   1344  -1086       C  
ATOM    755  CG  GLU A 158     -37.827 -41.470  93.622  1.00119.69           C  
ANISOU  755  CG  GLU A 158    17080  12560  15834   -361   1679  -1139       C  
ATOM    756  CD  GLU A 158     -38.894 -42.415  93.167  1.00133.91           C  
ANISOU  756  CD  GLU A 158    18992  14322  17566   -605   1847  -1450       C  
ATOM    757  OE1 GLU A 158     -40.046 -42.210  93.598  1.00143.73           O  
ANISOU  757  OE1 GLU A 158    20200  15692  18718   -691   1653  -1496       O  
ATOM    758  OE2 GLU A 158     -38.594 -43.376  92.406  1.00140.38           O  
ANISOU  758  OE2 GLU A 158    19933  14978  18427   -719   2188  -1656       O  
ATOM    759  N   ARG A 159     -35.493 -38.266  91.750  1.00116.13           N  
ANISOU  759  N   ARG A 159    16452  12584  15086   -201   1263   -744       N  
ATOM    760  CA  ARG A 159     -34.327 -38.160  90.856  1.00118.17           C  
ANISOU  760  CA  ARG A 159    16710  12842  15348   -161   1416   -684       C  
ATOM    761  C   ARG A 159     -33.058 -37.735  91.555  1.00111.46           C  
ANISOU  761  C   ARG A 159    15739  11904  14707     40   1385   -397       C  
ATOM    762  O   ARG A 159     -32.027 -38.316  91.279  1.00114.14           O  
ANISOU  762  O   ARG A 159    16077  12119  15172    122   1637   -338       O  
ATOM    763  CB  ARG A 159     -34.569 -37.201  89.673  1.00124.85           C  
ANISOU  763  CB  ARG A 159    17549  13962  15926   -271   1274   -716       C  
ATOM    764  CG  ARG A 159     -35.747 -37.576  88.813  1.00136.58           C  
ANISOU  764  CG  ARG A 159    19119  15626  17147   -495   1298   -990       C  
ATOM    765  CD  ARG A 159     -35.536 -38.857  88.017  1.00149.74           C  
ANISOU  765  CD  ARG A 159    20920  17185  18786   -620   1661  -1253       C  
ATOM    766  NE  ARG A 159     -36.730 -39.298  87.270  1.00164.24           N  
ANISOU  766  NE  ARG A 159    22830  19218  20353   -885   1680  -1560       N  
ATOM    767  CZ  ARG A 159     -37.812 -39.938  87.765  1.00173.18           C  
ANISOU  767  CZ  ARG A 159    24000  20313  21488  -1017   1674  -1737       C  
ATOM    768  NH1 ARG A 159     -37.954 -40.242  89.058  1.00168.64           N  
ANISOU  768  NH1 ARG A 159    23405  19502  21167   -895   1650  -1636       N  
ATOM    769  NH2 ARG A 159     -38.798 -40.271  86.927  1.00184.45           N  
ANISOU  769  NH2 ARG A 159    25469  21977  22633  -1290   1688  -2019       N  
ATOM    770  N   GLU A 160     -33.111 -36.726  92.421  1.00109.13           N  
ANISOU  770  N   GLU A 160    15336  11685  14443    110   1093   -227       N  
ATOM    771  CA  GLU A 160     -31.865 -36.166  92.948  1.00112.16           C  
ANISOU  771  CA  GLU A 160    15584  12049  14981    251   1036     26       C  
ATOM    772  C   GLU A 160     -31.267 -36.922  94.166  1.00113.40           C  
ANISOU  772  C   GLU A 160    15658  12067  15362    403   1135    172       C  
ATOM    773  O   GLU A 160     -30.042 -37.115  94.249  1.00123.53           O  
ANISOU  773  O   GLU A 160    16839  13308  16785    519   1265    355       O  
ATOM    774  CB  GLU A 160     -32.012 -34.656  93.203  1.00113.22           C  
ANISOU  774  CB  GLU A 160    15640  12326  15049    233    712    132       C  
ATOM    775  CG  GLU A 160     -31.832 -33.711  91.989  1.00119.43           C  
ANISOU  775  CG  GLU A 160    16431  13247  15701    165    661    155       C  
ATOM    776  CD  GLU A 160     -30.676 -34.075  91.047  1.00126.56           C  
ANISOU  776  CD  GLU A 160    17320  14129  16638    193    896    213       C  
ATOM    777  OE1 GLU A 160     -29.493 -33.815  91.393  1.00127.38           O  
ANISOU  777  OE1 GLU A 160    17304  14193  16899    284    911    407       O  
ATOM    778  OE2 GLU A 160     -30.939 -34.588  89.935  1.00133.31           O  
ANISOU  778  OE2 GLU A 160    18272  15031  17346    115   1068     62       O  
ATOM    779  N   ARG A 161     -32.095 -37.346  95.106  1.00110.26           N  
ANISOU  779  N   ARG A 161    15278  11622  14992    415   1082    125       N  
ATOM    780  CA  ARG A 161     -31.628 -38.179  96.221  1.00108.84           C  
ANISOU  780  CA  ARG A 161    15014  11333  15007    570   1206    281       C  
ATOM    781  C   ARG A 161     -32.525 -39.348  96.546  1.00104.58           C  
ANISOU  781  C   ARG A 161    14574  10640  14520    558   1389    150       C  
ATOM    782  O   ARG A 161     -32.198 -40.115  97.438  1.00108.16           O  
ANISOU  782  O   ARG A 161    14957  10993  15143    701   1528    302       O  
ATOM    783  CB  ARG A 161     -31.423 -37.321  97.494  1.00112.61           C  
ANISOU  783  CB  ARG A 161    15338  11946  15501    642    915    461       C  
ATOM    784  CG  ARG A 161     -30.220 -36.393  97.402  1.00122.01           C  
ANISOU  784  CG  ARG A 161    16388  13254  16715    668    801    637       C  
ATOM    785  CD  ARG A 161     -29.737 -35.805  98.749  1.00131.45           C  
ANISOU  785  CD  ARG A 161    17405  14590  17950    732    581    818       C  
ATOM    786  NE  ARG A 161     -29.056 -34.488  98.576  1.00147.15           N  
ANISOU  786  NE  ARG A 161    19303  16702  19902    654    376    879       N  
ATOM    787  CZ  ARG A 161     -28.382 -33.793  99.518  1.00154.87           C  
ANISOU  787  CZ  ARG A 161    20112  17829  20901    653    188   1013       C  
ATOM    788  NH1 ARG A 161     -28.224 -34.278 100.751  1.00161.22           N  
ANISOU  788  NH1 ARG A 161    20791  18727  21736    746    160   1132       N  
ATOM    789  NH2 ARG A 161     -27.835 -32.601  99.215  1.00150.91           N  
ANISOU  789  NH2 ARG A 161    19554  17397  20384    547     37   1031       N  
ATOM    790  N   GLY A 162     -33.653 -39.500  95.863  1.00102.40           N  
ANISOU  790  N   GLY A 162    14442  10362  14102    386   1394   -110       N  
ATOM    791  CA  GLY A 162     -34.675 -40.485  96.280  1.00103.15           C  
ANISOU  791  CA  GLY A 162    14620  10329  14241    336   1522   -250       C  
ATOM    792  C   GLY A 162     -35.505 -40.081  97.513  1.00100.80           C  
ANISOU  792  C   GLY A 162    14257  10119  13922    374   1265   -182       C  
ATOM    793  O   GLY A 162     -35.060 -39.328  98.388  1.00 97.73           O  
ANISOU  793  O   GLY A 162    13743   9839  13549    490   1054     12       O  
ATOM    794  N   TRP A 163     -36.728 -40.585  97.576  1.00100.85           N  
ANISOU  794  N   TRP A 163    14346  10090  13881    258   1291   -359       N  
ATOM    795  CA  TRP A 163     -37.594 -40.333  98.731  1.00 99.57           C  
ANISOU  795  CA  TRP A 163    14130   9999  13702    300   1090   -302       C  
ATOM    796  C   TRP A 163     -37.124 -41.196  99.876  1.00 99.34           C  
ANISOU  796  C   TRP A 163    14026   9828  13889    484   1258   -102       C  
ATOM    797  O   TRP A 163     -36.948 -42.421  99.681  1.00105.56           O  
ANISOU  797  O   TRP A 163    14872  10392  14845    498   1602   -130       O  
ATOM    798  CB  TRP A 163     -39.066 -40.710  98.449  1.00100.19           C  
ANISOU  798  CB  TRP A 163    14299  10091  13677    116   1091   -534       C  
ATOM    799  CG  TRP A 163     -39.827 -39.725  97.606  1.00 96.91           C  
ANISOU  799  CG  TRP A 163    13906   9901  13012    -40    857   -672       C  
ATOM    800  CD1 TRP A 163     -40.234 -39.911  96.331  1.00 98.39           C  
ANISOU  800  CD1 TRP A 163    14173  10157  13051   -241    936   -889       C  
ATOM    801  CD2 TRP A 163     -40.245 -38.415  97.978  1.00 92.23           C  
ANISOU  801  CD2 TRP A 163    13246   9504  12290      0    532   -584       C  
ATOM    802  NE1 TRP A 163     -40.867 -38.798  95.879  1.00 97.05           N  
ANISOU  802  NE1 TRP A 163    13969  10241  12665   -309    671   -901       N  
ATOM    803  CE2 TRP A 163     -40.890 -37.864  96.878  1.00 92.49           C  
ANISOU  803  CE2 TRP A 163    13309   9716  12116   -155    435   -713       C  
ATOM    804  CE3 TRP A 163     -40.143 -37.662  99.144  1.00 90.24           C  
ANISOU  804  CE3 TRP A 163    12912   9298  12075    149    331   -412       C  
ATOM    805  CZ2 TRP A 163     -41.457 -36.611  96.906  1.00 90.65           C  
ANISOU  805  CZ2 TRP A 163    13025   9673  11744   -140    169   -647       C  
ATOM    806  CZ3 TRP A 163     -40.689 -36.423  99.166  1.00 87.61           C  
ANISOU  806  CZ3 TRP A 163    12554   9127  11606    141     76   -392       C  
ATOM    807  CH2 TRP A 163     -41.345 -35.909  98.058  1.00 88.55           C  
ANISOU  807  CH2 TRP A 163    12702   9390  11551     11      6   -493       C  
ATOM    808  N   PRO A 164     -36.987 -40.608 101.069  1.00 96.31           N  
ANISOU  808  N   PRO A 164    13517   9573  13500    620   1042     91       N  
ATOM    809  CA  PRO A 164     -36.669 -41.463 102.183  1.00 98.79           C  
ANISOU  809  CA  PRO A 164    13739   9806  13987    799   1198    303       C  
ATOM    810  C   PRO A 164     -37.794 -42.460 102.462  1.00105.25           C  
ANISOU  810  C   PRO A 164    14635  10474  14879    749   1369    202       C  
ATOM    811  O   PRO A 164     -38.966 -42.185 102.171  1.00102.62           O  
ANISOU  811  O   PRO A 164    14384  10193  14414    586   1242     -4       O  
ATOM    812  CB  PRO A 164     -36.496 -40.495 103.347  1.00 95.53           C  
ANISOU  812  CB  PRO A 164    13186   9628  13482    901    888    471       C  
ATOM    813  CG  PRO A 164     -36.387 -39.152 102.735  1.00 94.50           C  
ANISOU  813  CG  PRO A 164    13077   9639  13188    790    625    367       C  
ATOM    814  CD  PRO A 164     -37.196 -39.219 101.492  1.00 94.05           C  
ANISOU  814  CD  PRO A 164    13174   9507  13054    612    681    117       C  
ATOM    815  N   ASP A 165     -37.400 -43.635 102.973  1.00114.66           N  
ANISOU  815  N   ASP A 165    15790  11479  16296    892   1680    367       N  
ATOM    816  CA  ASP A 165     -38.302 -44.738 103.374  1.00117.20           C  
ANISOU  816  CA  ASP A 165    16166  11608  16755    874   1912    326       C  
ATOM    817  C   ASP A 165     -39.624 -44.269 103.948  1.00107.66           C  
ANISOU  817  C   ASP A 165    14960  10547  15396    785   1656    231       C  
ATOM    818  O   ASP A 165     -40.690 -44.757 103.566  1.00102.54           O  
ANISOU  818  O   ASP A 165    14413   9796  14748    609   1747     17       O  
ATOM    819  CB  ASP A 165     -37.580 -45.653 104.398  1.00132.47           C  
ANISOU  819  CB  ASP A 165    17971  13432  18927   1141   2167    673       C  
ATOM    820  CG  ASP A 165     -36.881 -44.855 105.547  1.00145.11           C  
ANISOU  820  CG  ASP A 165    19362  15342  20432   1344   1889    980       C  
ATOM    821  OD1 ASP A 165     -35.843 -44.181 105.280  1.00149.67           O  
ANISOU  821  OD1 ASP A 165    19862  16058  20947   1385   1768   1062       O  
ATOM    822  OD2 ASP A 165     -37.352 -44.923 106.715  1.00155.82           O  
ANISOU  822  OD2 ASP A 165    20621  16814  21768   1449   1802   1135       O  
ATOM    823  N   PHE A 166     -39.518 -43.300 104.868  1.00102.58           N  
ANISOU  823  N   PHE A 166    14197  10157  14620    899   1342    386       N  
ATOM    824  CA  PHE A 166     -40.638 -42.788 105.669  1.00 97.51           C  
ANISOU  824  CA  PHE A 166    13531   9675  13843    880   1105    359       C  
ATOM    825  C   PHE A 166     -41.502 -41.758 104.974  1.00 93.79           C  
ANISOU  825  C   PHE A 166    13138   9338  13158    694    843    120       C  
ATOM    826  O   PHE A 166     -42.522 -41.340 105.522  1.00 96.00           O  
ANISOU  826  O   PHE A 166    13406   9737  13331    674    672     86       O  
ATOM    827  CB  PHE A 166     -40.169 -42.242 107.041  1.00 94.72           C  
ANISOU  827  CB  PHE A 166    13019   9540  13430   1082    915    615       C  
ATOM    828  CG  PHE A 166     -39.276 -41.056 106.970  1.00 89.98           C  
ANISOU  828  CG  PHE A 166    12360   9129  12697   1097    668    646       C  
ATOM    829  CD1 PHE A 166     -37.926 -41.242 106.886  1.00 92.40           C  
ANISOU  829  CD1 PHE A 166    12576   9436  13096   1199    769    819       C  
ATOM    830  CD2 PHE A 166     -39.770 -39.768 107.069  1.00 85.80           C  
ANISOU  830  CD2 PHE A 166    11853   8775  11971   1019    355    524       C  
ATOM    831  CE1 PHE A 166     -37.066 -40.149 106.839  1.00 92.48           C  
ANISOU  831  CE1 PHE A 166    12516   9626  12995   1190    545    849       C  
ATOM    832  CE2 PHE A 166     -38.930 -38.682 107.021  1.00 85.66           C  
ANISOU  832  CE2 PHE A 166    11786   8898  11861   1014    156    544       C  
ATOM    833  CZ  PHE A 166     -37.566 -38.867 106.921  1.00 88.37           C  
ANISOU  833  CZ  PHE A 166    12033   9254  12289   1088    240    701       C  
ATOM    834  N   LEU A 167     -41.073 -41.328 103.804  1.00 91.56           N  
ANISOU  834  N   LEU A 167    12920   9054  12812    580    821    -11       N  
ATOM    835  CA  LEU A 167     -41.836 -40.444 102.974  1.00 92.91           C  
ANISOU  835  CA  LEU A 167    13153   9356  12789    412    620   -204       C  
ATOM    836  C   LEU A 167     -42.337 -41.156 101.712  1.00100.08           C  
ANISOU  836  C   LEU A 167    14171  10167  13687    196    808   -441       C  
ATOM    837  O   LEU A 167     -42.895 -40.504 100.818  1.00102.52           O  
ANISOU  837  O   LEU A 167    14515  10621  13815     44    667   -592       O  
ATOM    838  CB  LEU A 167     -40.981 -39.227 102.598  1.00 92.24           C  
ANISOU  838  CB  LEU A 167    13042   9397  12606    441    422   -159       C  
ATOM    839  CG  LEU A 167     -40.757 -38.182 103.683  1.00 90.31           C  
ANISOU  839  CG  LEU A 167    12709   9303  12302    570    171    -17       C  
ATOM    840  CD1 LEU A 167     -39.697 -37.160 103.237  1.00 91.83           C  
ANISOU  840  CD1 LEU A 167    12875   9563  12453    575     46     25       C  
ATOM    841  CD2 LEU A 167     -42.090 -37.546 103.993  1.00 88.57           C  
ANISOU  841  CD2 LEU A 167    12509   9196  11947    525    -12    -98       C  
ATOM    842  N   ARG A 168     -42.130 -42.470 101.605  1.00102.98           N  
ANISOU  842  N   ARG A 168    14586  10300  14239    175   1140   -475       N  
ATOM    843  CA  ARG A 168     -42.728 -43.234 100.516  1.00105.32           C  
ANISOU  843  CA  ARG A 168    14996  10501  14520    -70   1341   -749       C  
ATOM    844  C   ARG A 168     -44.107 -43.601 100.948  1.00102.33           C  
ANISOU  844  C   ARG A 168    14608  10151  14120   -184   1316   -838       C  
ATOM    845  O   ARG A 168     -44.280 -43.953 102.113  1.00102.76           O  
ANISOU  845  O   ARG A 168    14602  10134  14305    -35   1350   -666       O  
ATOM    846  CB  ARG A 168     -41.890 -44.472 100.229  1.00114.21           C  
ANISOU  846  CB  ARG A 168    16193  11319  15882    -46   1751   -762       C  
ATOM    847  CG  ARG A 168     -40.531 -44.135  99.607  1.00121.32           C  
ANISOU  847  CG  ARG A 168    17098  12206  16792     44   1798   -690       C  
ATOM    848  CD  ARG A 168     -39.897 -45.286  98.856  1.00125.13           C  
ANISOU  848  CD  ARG A 168    17691  12401  17450     -3   2226   -801       C  
ATOM    849  NE  ARG A 168     -38.448 -45.235  99.009  1.00129.03           N  
ANISOU  849  NE  ARG A 168    18121  12827  18078    228   2329   -554       N  
ATOM    850  CZ  ARG A 168     -37.676 -46.299  98.925  1.00142.10           C  
ANISOU  850  CZ  ARG A 168    19814  14194  19981    330   2736   -486       C  
ATOM    851  NH1 ARG A 168     -38.207 -47.498  98.662  1.00147.19           N  
ANISOU  851  NH1 ARG A 168    20588  14554  20781    202   3097   -678       N  
ATOM    852  NH2 ARG A 168     -36.374 -46.166  99.109  1.00150.69           N  
ANISOU  852  NH2 ARG A 168    20805  15274  21174    555   2798   -221       N  
ATOM    853  N   CYS A 169     -45.089 -43.567 100.048  1.00101.22           N  
ANISOU  853  N   CYS A 169    14510  10137  13811   -445   1267  -1086       N  
ATOM    854  CA  CYS A 169     -46.496 -43.796 100.457  1.00105.24           C  
ANISOU  854  CA  CYS A 169    14978  10731  14276   -568   1204  -1156       C  
ATOM    855  C   CYS A 169     -46.920 -45.243 100.719  1.00105.56           C  
ANISOU  855  C   CYS A 169    15069  10503  14536   -680   1541  -1254       C  
ATOM    856  O   CYS A 169     -47.885 -45.719 100.180  1.00105.61           O  
ANISOU  856  O   CYS A 169    15097  10548  14479   -951   1606  -1485       O  
ATOM    857  CB  CYS A 169     -47.455 -43.147  99.473  1.00110.06           C  
ANISOU  857  CB  CYS A 169    15568  11646  14603   -801    997  -1343       C  
ATOM    858  SG  CYS A 169     -46.948 -41.479  98.977  1.00121.44           S  
ANISOU  858  SG  CYS A 169    16962  13360  15816   -682    665  -1224       S  
ATOM    859  N   THR A 170     -46.173 -45.888 101.597  1.00107.67           N  
ANISOU  859  N   THR A 170    15333  10515  15061   -460   1753  -1052       N  
ATOM    860  CA  THR A 170     -46.451 -47.172 102.160  1.00113.45           C  
ANISOU  860  CA  THR A 170    16088  10957  16057   -471   2085  -1034       C  
ATOM    861  C   THR A 170     -47.783 -47.100 102.911  1.00119.22           C  
ANISOU  861  C   THR A 170    16734  11825  16737   -521   1937  -1005       C  
ATOM    862  O   THR A 170     -48.026 -46.136 103.655  1.00119.41           O  
ANISOU  862  O   THR A 170    16656  12088  16623   -354   1626   -825       O  
ATOM    863  CB  THR A 170     -45.306 -47.551 103.147  1.00113.24           C  
ANISOU  863  CB  THR A 170    16015  10735  16274   -132   2258   -699       C  
ATOM    864  OG1 THR A 170     -44.068 -47.617 102.450  1.00110.45           O  
ANISOU  864  OG1 THR A 170    15751  10152  16060   -117   2547   -742       O  
ATOM    865  CG2 THR A 170     -45.537 -48.878 103.867  1.00116.27           C  
ANISOU  865  CG2 THR A 170    16354  10915  16907    -30   2497   -529       C  
ATOM    866  N   PRO A 171     -48.625 -48.138 102.761  1.00128.17           N  
ANISOU  866  N   PRO A 171    17908  12793  17996   -749   2182  -1182       N  
ATOM    867  CA  PRO A 171     -49.919 -48.120 103.435  1.00129.03           C  
ANISOU  867  CA  PRO A 171    17922  13038  18065   -811   2058  -1150       C  
ATOM    868  C   PRO A 171     -49.770 -48.053 104.957  1.00129.25           C  
ANISOU  868  C   PRO A 171    17849  13042  18218   -471   2024   -785       C  
ATOM    869  O   PRO A 171     -50.545 -47.366 105.622  1.00128.68           O  
ANISOU  869  O   PRO A 171    17673  13214  18002   -400   1760   -678       O  
ATOM    870  CB  PRO A 171     -50.567 -49.450 103.042  1.00131.19           C  
ANISOU  870  CB  PRO A 171    18266  13050  18527  -1112   2418  -1390       C  
ATOM    871  CG  PRO A 171     -49.469 -50.287 102.506  1.00131.81           C  
ANISOU  871  CG  PRO A 171    18486  12771  18823  -1112   2796  -1472       C  
ATOM    872  CD  PRO A 171     -48.377 -49.400 102.041  1.00129.76           C  
ANISOU  872  CD  PRO A 171    18245  12647  18409   -952   2615  -1408       C  
ATOM    873  N   ASP A 172     -48.800 -48.769 105.508  1.00132.08           N  
ANISOU  873  N   ASP A 172    18224  13127  18831   -257   2300   -583       N  
ATOM    874  CA  ASP A 172     -48.586 -48.722 106.944  1.00138.82           C  
ANISOU  874  CA  ASP A 172    18961  14014  19770     67   2268   -217       C  
ATOM    875  C   ASP A 172     -48.254 -47.332 107.493  1.00130.18           C  
ANISOU  875  C   ASP A 172    17778  13261  18423    276   1860    -57       C  
ATOM    876  O   ASP A 172     -48.779 -46.927 108.558  1.00128.29           O  
ANISOU  876  O   ASP A 172    17437  13201  18105    423   1691    118       O  
ATOM    877  CB  ASP A 172     -47.509 -49.718 107.375  1.00150.36           C  
ANISOU  877  CB  ASP A 172    20428  15162  21538    280   2646     13       C  
ATOM    878  CG  ASP A 172     -47.140 -49.538 108.833  1.00157.56           C  
ANISOU  878  CG  ASP A 172    21187  16204  22473    633   2569    421       C  
ATOM    879  OD1 ASP A 172     -46.465 -48.505 109.087  1.00160.19           O  
ANISOU  879  OD1 ASP A 172    21458  16800  22607    791   2272    532       O  
ATOM    880  OD2 ASP A 172     -47.510 -50.370 109.716  1.00150.16           O  
ANISOU  880  OD2 ASP A 172    20185  15134  21733    744   2795    628       O  
ATOM    881  N   ARG A 173     -47.387 -46.620 106.771  1.00125.46           N  
ANISOU  881  N   ARG A 173    17223  12741  17703    279   1725   -127       N  
ATOM    882  CA  ARG A 173     -46.932 -45.245 107.164  1.00121.07           C  
ANISOU  882  CA  ARG A 173    16601  12472  16925    443   1362    -10       C  
ATOM    883  C   ARG A 173     -47.913 -44.096 106.875  1.00105.80           C  
ANISOU  883  C   ARG A 173    14660  10810  14728    324   1025   -155       C  
ATOM    884  O   ARG A 173     -47.984 -43.095 107.630  1.00 96.35           O  
ANISOU  884  O   ARG A 173    13398   9824  13387    475    766    -35       O  
ATOM    885  CB  ARG A 173     -45.596 -44.883 106.500  1.00122.87           C  
ANISOU  885  CB  ARG A 173    16865  12674  17143    491   1357     -8       C  
ATOM    886  CG  ARG A 173     -44.457 -45.818 106.836  1.00129.97           C  
ANISOU  886  CG  ARG A 173    17741  13355  18287    668   1665    198       C  
ATOM    887  CD  ARG A 173     -43.229 -45.404 106.032  1.00130.11           C  
ANISOU  887  CD  ARG A 173    17789  13369  18278    685   1651    176       C  
ATOM    888  NE  ARG A 173     -42.063 -46.256 106.287  1.00135.85           N  
ANISOU  888  NE  ARG A 173    18472  13904  19238    875   1956    404       N  
ATOM    889  CZ  ARG A 173     -41.184 -46.097 107.289  1.00137.17           C  
ANISOU  889  CZ  ARG A 173    18487  14196  19432   1138   1909    731       C  
ATOM    890  NH1 ARG A 173     -41.292 -45.094 108.173  1.00132.66           N  
ANISOU  890  NH1 ARG A 173    17809  13934  18659   1227   1564    837       N  
ATOM    891  NH2 ARG A 173     -40.164 -46.952 107.399  1.00140.61           N  
ANISOU  891  NH2 ARG A 173    18870  14460  20094   1311   2223    957       N  
ATOM    892  N   PHE A 174     -48.642 -44.284 105.777  1.00100.91           N  
ANISOU  892  N   PHE A 174    14103  10186  14052     53   1056   -409       N  
ATOM    893  CA  PHE A 174     -49.631 -43.322 105.350  1.00 99.13           C  
ANISOU  893  CA  PHE A 174    13848  10227  13588    -68    781   -524       C  
ATOM    894  C   PHE A 174     -50.973 -44.038 105.137  1.00 99.24           C  
ANISOU  894  C   PHE A 174    13840  10251  13616   -298    876   -667       C  
ATOM    895  O   PHE A 174     -51.269 -44.488 104.032  1.00102.37           O  
ANISOU  895  O   PHE A 174    14285  10629  13980   -570    975   -904       O  
ATOM    896  CB  PHE A 174     -49.133 -42.617 104.073  1.00 99.74           C  
ANISOU  896  CB  PHE A 174    13982  10400  13513   -183    668   -673       C  
ATOM    897  CG  PHE A 174     -47.858 -41.827 104.275  1.00 97.95           C  
ANISOU  897  CG  PHE A 174    13762  10180  13274     19    561   -533       C  
ATOM    898  CD1 PHE A 174     -47.899 -40.522 104.691  1.00 96.67           C  
ANISOU  898  CD1 PHE A 174    13554  10212  12964    148    280   -435       C  
ATOM    899  CD2 PHE A 174     -46.619 -42.402 104.063  1.00 99.22           C  
ANISOU  899  CD2 PHE A 174    13970  10145  13584     76    761   -497       C  
ATOM    900  CE1 PHE A 174     -46.738 -39.793 104.887  1.00 94.40           C  
ANISOU  900  CE1 PHE A 174    13266   9932  12670    295    185   -328       C  
ATOM    901  CE2 PHE A 174     -45.454 -41.671 104.252  1.00 97.71           C  
ANISOU  901  CE2 PHE A 174    13757   9990  13376    242    652   -361       C  
ATOM    902  CZ  PHE A 174     -45.517 -40.367 104.678  1.00 93.93           C  
ANISOU  902  CZ  PHE A 174    13231   9715  12744    337    358   -286       C  
ATOM    903  N   PRO A 175     -51.765 -44.205 106.205  1.00 97.42           N  
ANISOU  903  N   PRO A 175    13527  10056  13431   -203    863   -529       N  
ATOM    904  CA  PRO A 175     -52.985 -44.975 106.106  1.00 99.19           C  
ANISOU  904  CA  PRO A 175    13712  10272  13702   -422    979   -640       C  
ATOM    905  C   PRO A 175     -54.027 -44.312 105.296  1.00101.70           C  
ANISOU  905  C   PRO A 175    13972  10885  13782   -631    765   -793       C  
ATOM    906  O   PRO A 175     -53.972 -43.105 105.047  1.00103.31           O  
ANISOU  906  O   PRO A 175    14152  11315  13785   -543    502   -753       O  
ATOM    907  CB  PRO A 175     -53.476 -45.074 107.541  1.00 99.42           C  
ANISOU  907  CB  PRO A 175    13651  10315  13809   -210    976   -400       C  
ATOM    908  CG  PRO A 175     -52.358 -44.603 108.395  1.00 99.38           C  
ANISOU  908  CG  PRO A 175    13650  10288  13820    105    916   -178       C  
ATOM    909  CD  PRO A 175     -51.583 -43.664 107.553  1.00 98.31           C  
ANISOU  909  CD  PRO A 175    13573  10243  13535     95    739   -272       C  
ATOM    910  N   GLU A 176     -54.985 -45.112 104.862  1.00110.24           N  
ANISOU  910  N   GLU A 176    15021  11972  14893   -917    891   -961       N  
ATOM    911  CA  GLU A 176     -56.070 -44.584 104.062  1.00116.72           C  
ANISOU  911  CA  GLU A 176    15744  13133  15470  -1143    693  -1090       C  
ATOM    912  C   GLU A 176     -57.133 -43.849 104.896  1.00118.19           C  
ANISOU  912  C   GLU A 176    15783  13571  15552   -995    481   -893       C  
ATOM    913  O   GLU A 176     -57.492 -44.274 105.990  1.00121.76           O  
ANISOU  913  O   GLU A 176    16193  13919  16149   -870    571   -746       O  
ATOM    914  CB  GLU A 176     -56.664 -45.633 103.100  1.00123.76           C  
ANISOU  914  CB  GLU A 176    16642  14004  16377  -1565    884  -1391       C  
ATOM    915  CG  GLU A 176     -56.209 -45.399 101.676  1.00129.21           C  
ANISOU  915  CG  GLU A 176    17396  14816  16882  -1775    844  -1623       C  
ATOM    916  CD  GLU A 176     -56.841 -44.137 101.082  1.00135.95           C  
ANISOU  916  CD  GLU A 176    18116  16133  17404  -1784    501  -1571       C  
ATOM    917  OE1 GLU A 176     -57.980 -44.297 100.608  1.00140.89           O  
ANISOU  917  OE1 GLU A 176    18611  17040  17881  -2056    440  -1683       O  
ATOM    918  OE2 GLU A 176     -56.229 -43.011 101.072  1.00142.05           O  
ANISOU  918  OE2 GLU A 176    18903  16997  18071  -1534    308  -1412       O  
ATOM    919  N   GLY A 177     -57.561 -42.697 104.372  1.00120.01           N  
ANISOU  919  N   GLY A 177    15936  14128  15534   -981    216   -866       N  
ATOM    920  CA  GLY A 177     -58.645 -41.860 104.893  1.00117.00           C  
ANISOU  920  CA  GLY A 177    15406  14028  15020   -858     17   -693       C  
ATOM    921  C   GLY A 177     -58.516 -41.309 106.299  1.00110.41           C  
ANISOU  921  C   GLY A 177    14575  13119  14254   -499    -36   -451       C  
ATOM    922  O   GLY A 177     -59.442 -41.390 107.113  1.00111.69           O  
ANISOU  922  O   GLY A 177    14635  13363  14438   -430    -39   -329       O  
ATOM    923  N   CYS A 178     -57.367 -40.686 106.533  1.00104.32           N  
ANISOU  923  N   CYS A 178    13914  12226  13494   -285    -88   -391       N  
ATOM    924  CA  CYS A 178     -57.067 -40.038 107.775  1.00102.19           C  
ANISOU  924  CA  CYS A 178    13663  11918  13246     29   -156   -204       C  
ATOM    925  C   CYS A 178     -57.416 -38.590 107.683  1.00102.03           C  
ANISOU  925  C   CYS A 178    13606  12111  13047    167   -376   -125       C  
ATOM    926  O   CYS A 178     -57.181 -37.934 106.672  1.00106.15           O  
ANISOU  926  O   CYS A 178    14143  12727  13460     97   -476   -186       O  
ATOM    927  CB  CYS A 178     -55.595 -40.122 108.097  1.00104.80           C  
ANISOU  927  CB  CYS A 178    14113  12027  13678    165    -93   -184       C  
ATOM    928  SG  CYS A 178     -54.954 -41.698 108.679  1.00111.78           S  
ANISOU  928  SG  CYS A 178    15037  12612  14822    157    204   -158       S  
ATOM    929  N   THR A 179     -57.970 -38.062 108.746  1.00101.81           N  
ANISOU  929  N   THR A 179    13534  12154  12995    375   -431     20       N  
ATOM    930  CA  THR A 179     -58.215 -36.651 108.777  1.00104.66           C  
ANISOU  930  CA  THR A 179    13884  12655  13223    540   -592    101       C  
ATOM    931  C   THR A 179     -56.852 -36.127 109.181  1.00102.92           C  
ANISOU  931  C   THR A 179    13801  12265  13036    690   -619     90       C  
ATOM    932  O   THR A 179     -56.423 -36.319 110.308  1.00106.53           O  
ANISOU  932  O   THR A 179    14295  12630  13550    836   -573    145       O  
ATOM    933  CB  THR A 179     -59.287 -36.269 109.781  1.00106.86           C  
ANISOU  933  CB  THR A 179    14077  13057  13465    712   -612    244       C  
ATOM    934  OG1 THR A 179     -58.786 -36.505 111.100  1.00122.75           O  
ANISOU  934  OG1 THR A 179    16152  14936  15548    889   -547    299       O  
ATOM    935  CG2 THR A 179     -60.551 -37.060 109.536  1.00107.50           C  
ANISOU  935  CG2 THR A 179    14003  13294  13546    541   -558    263       C  
ATOM    936  N   ASN A 180     -56.147 -35.501 108.252  1.00101.77           N  
ANISOU  936  N   ASN A 180    13715  12105  12848    641   -689     26       N  
ATOM    937  CA  ASN A 180     -54.707 -35.228 108.463  1.00102.37           C  
ANISOU  937  CA  ASN A 180    13905  12014  12976    719   -696     -4       C  
ATOM    938  C   ASN A 180     -54.343 -34.152 109.531  1.00100.65           C  
ANISOU  938  C   ASN A 180    13741  11774  12726    942   -775     57       C  
ATOM    939  O   ASN A 180     -53.271 -34.275 110.199  1.00101.23           O  
ANISOU  939  O   ASN A 180    13870  11746  12845   1009   -759     51       O  
ATOM    940  CB  ASN A 180     -54.060 -34.832 107.158  1.00101.32           C  
ANISOU  940  CB  ASN A 180    13813  11874  12807    602   -740    -80       C  
ATOM    941  CG  ASN A 180     -54.011 -35.968 106.160  1.00 99.22           C  
ANISOU  941  CG  ASN A 180    13534  11591  12573    366   -634   -194       C  
ATOM    942  OD1 ASN A 180     -53.300 -36.945 106.329  1.00 95.54           O  
ANISOU  942  OD1 ASN A 180    13114  10959  12226    320   -501   -242       O  
ATOM    943  ND2 ASN A 180     -54.780 -35.818 105.097  1.00103.50           N  
ANISOU  943  ND2 ASN A 180    14007  12320  12999    216   -681   -232       N  
ATOM    944  N   GLU A 181     -55.190 -33.121 109.606  1.00 92.77           N  
ANISOU  944  N   GLU A 181    12720  10881  11646   1039   -847    110       N  
ATOM    945  CA  GLU A 181     -55.050 -31.936 110.513  1.00 97.56           C  
ANISOU  945  CA  GLU A 181    13393  11460  12214   1232   -897    133       C  
ATOM    946  C   GLU A 181     -54.224 -30.807 109.897  1.00 94.17           C  
ANISOU  946  C   GLU A 181    13049  10946  11785   1235   -961     87       C  
ATOM    947  O   GLU A 181     -54.217 -29.677 110.416  1.00 90.38           O  
ANISOU  947  O   GLU A 181    12632  10422  11286   1363   -982     85       O  
ATOM    948  CB  GLU A 181     -54.541 -32.229 112.008  1.00103.07           C  
ANISOU  948  CB  GLU A 181    14126  12120  12915   1349   -868    130       C  
ATOM    949  CG  GLU A 181     -54.501 -30.988 112.923  1.00106.46           C  
ANISOU  949  CG  GLU A 181    14631  12543  13274   1508   -907    103       C  
ATOM    950  CD  GLU A 181     -55.752 -30.726 113.755  1.00111.57           C  
ANISOU  950  CD  GLU A 181    15241  13289  13860   1655   -866    171       C  
ATOM    951  OE1 GLU A 181     -56.488 -31.679 114.063  1.00117.75           O  
ANISOU  951  OE1 GLU A 181    15929  14159  14649   1655   -811    253       O  
ATOM    952  OE2 GLU A 181     -56.007 -29.585 114.165  1.00111.80           O  
ANISOU  952  OE2 GLU A 181    15337  13297  13845   1775   -866    144       O  
ATOM    953  N   VAL A 182     -53.502 -31.107 108.828  1.00 92.42           N  
ANISOU  953  N   VAL A 182    12836  10684  11593   1093   -969     44       N  
ATOM    954  CA  VAL A 182     -52.809 -30.095 108.033  1.00 88.25           C  
ANISOU  954  CA  VAL A 182    12367  10092  11073   1080  -1017     28       C  
ATOM    955  C   VAL A 182     -53.771 -29.517 107.032  1.00 88.99           C  
ANISOU  955  C   VAL A 182    12391  10311  11108   1075  -1035    118       C  
ATOM    956  O   VAL A 182     -53.490 -28.462 106.475  1.00 87.18           O  
ANISOU  956  O   VAL A 182    12196  10040  10887   1116  -1057    158       O  
ATOM    957  CB  VAL A 182     -51.596 -30.673 107.317  1.00 84.22           C  
ANISOU  957  CB  VAL A 182    11884   9504  10610    944  -1006    -37       C  
ATOM    958  CG1 VAL A 182     -50.544 -31.097 108.335  1.00 86.03           C  
ANISOU  958  CG1 VAL A 182    12154   9639  10894    978   -990    -78       C  
ATOM    959  CG2 VAL A 182     -51.974 -31.852 106.437  1.00 81.95           C  
ANISOU  959  CG2 VAL A 182    11532   9294  10310    784   -949    -60       C  
ATOM    960  N   GLN A 183     -54.903 -30.193 106.816  1.00 91.26           N  
ANISOU  960  N   GLN A 183    12566  10768  11339   1024  -1020    167       N  
ATOM    961  CA  GLN A 183     -55.913 -29.656 105.949  1.00 96.57           C  
ANISOU  961  CA  GLN A 183    13130  11633  11929   1029  -1046    289       C  
ATOM    962  C   GLN A 183     -56.531 -28.412 106.559  1.00 98.65           C  
ANISOU  962  C   GLN A 183    13401  11877  12203   1256  -1034    412       C  
ATOM    963  O   GLN A 183     -56.947 -27.485 105.865  1.00111.86           O  
ANISOU  963  O   GLN A 183    15023  13629  13849   1331  -1036    549       O  
ATOM    964  CB  GLN A 183     -56.976 -30.693 105.568  1.00104.32           C  
ANISOU  964  CB  GLN A 183    13964  12837  12834    886  -1038    302       C  
ATOM    965  CG  GLN A 183     -57.813 -30.323 104.300  1.00117.87           C  
ANISOU  965  CG  GLN A 183    15527  14839  14417    814  -1087    421       C  
ATOM    966  CD  GLN A 183     -57.496 -31.116 102.976  1.00126.85           C  
ANISOU  966  CD  GLN A 183    16620  16114  15463    542  -1101    311       C  
ATOM    967  OE1 GLN A 183     -56.739 -32.109 102.965  1.00135.20           O  
ANISOU  967  OE1 GLN A 183    17762  17027  16578    391  -1048    134       O  
ATOM    968  NE2 GLN A 183     -58.103 -30.675 101.867  1.00123.49           N  
ANISOU  968  NE2 GLN A 183    16051  15981  14885    487  -1156    426       N  
ATOM    969  N   ASN A 184     -56.576 -28.361 107.862  1.00 96.16           N  
ANISOU  969  N   ASN A 184    13152  11457  11928   1377  -1000    373       N  
ATOM    970  CA  ASN A 184     -56.985 -27.155 108.548  1.00 93.00           C  
ANISOU  970  CA  ASN A 184    12803  10980  11552   1590   -953    439       C  
ATOM    971  C   ASN A 184     -55.929 -26.076 108.525  1.00 84.03           C  
ANISOU  971  C   ASN A 184    11811   9625  10489   1632   -941    372       C  
ATOM    972  O   ASN A 184     -56.236 -24.952 108.872  1.00 85.31           O  
ANISOU  972  O   ASN A 184    12030   9689  10695   1791   -870    420       O  
ATOM    973  CB  ASN A 184     -57.438 -27.481 109.997  1.00 99.62           C  
ANISOU  973  CB  ASN A 184    13661  11809  12378   1698   -909    404       C  
ATOM    974  CG  ASN A 184     -58.665 -28.400 110.021  1.00102.99           C  
ANISOU  974  CG  ASN A 184    13926  12452  12752   1671   -899    505       C  
ATOM    975  OD1 ASN A 184     -59.434 -28.474 109.032  1.00 96.56           O  
ANISOU  975  OD1 ASN A 184    12971  11821  11893   1611   -921    624       O  
ATOM    976  ND2 ASN A 184     -58.839 -29.128 111.137  1.00107.57           N  
ANISOU  976  ND2 ASN A 184    14508  13035  13326   1703   -866    467       N  
ATOM    977  N   ILE A 185     -54.702 -26.376 108.186  1.00 76.57           N  
ANISOU  977  N   ILE A 185    10930   8588   9575   1495   -987    260       N  
ATOM    978  CA  ILE A 185     -53.679 -25.329 108.185  1.00 74.68           C  
ANISOU  978  CA  ILE A 185    10815   8143   9414   1512   -974    193       C  
ATOM    979  C   ILE A 185     -53.551 -24.809 106.797  1.00 74.17           C  
ANISOU  979  C   ILE A 185    10712   8095   9373   1475   -975    305       C  
ATOM    980  O   ILE A 185     -53.419 -25.531 105.842  1.00 73.27           O  
ANISOU  980  O   ILE A 185    10520   8110   9208   1346  -1021    331       O  
ATOM    981  CB  ILE A 185     -52.314 -25.851 108.682  1.00 73.24           C  
ANISOU  981  CB  ILE A 185    10705   7869   9253   1396  -1022     31       C  
ATOM    982  CG1 ILE A 185     -52.386 -26.173 110.152  1.00 73.04           C  
ANISOU  982  CG1 ILE A 185    10713   7853   9186   1458  -1016    -56       C  
ATOM    983  CG2 ILE A 185     -51.197 -24.849 108.512  1.00 73.41           C  
ANISOU  983  CG2 ILE A 185    10827   7707   9355   1362  -1020    -39       C  
ATOM    984  CD1 ILE A 185     -51.469 -27.304 110.492  1.00 73.06           C  
ANISOU  984  CD1 ILE A 185    10691   7893   9173   1353  -1059   -120       C  
ATOM    985  N   LYS A 186     -53.534 -23.516 106.698  1.00 77.21           N  
ANISOU  985  N   LYS A 186    11157   8337   9839   1586   -905    367       N  
ATOM    986  CA  LYS A 186     -53.383 -22.827 105.417  1.00 80.97           C  
ANISOU  986  CA  LYS A 186    11595   8816  10351   1587   -881    517       C  
ATOM    987  C   LYS A 186     -51.897 -22.583 105.130  1.00 81.64           C  
ANISOU  987  C   LYS A 186    11777   8723  10518   1464   -901    402       C  
ATOM    988  O   LYS A 186     -51.234 -21.937 105.922  1.00 81.69           O  
ANISOU  988  O   LYS A 186    11908   8510  10618   1474   -864    274       O  
ATOM    989  CB  LYS A 186     -54.129 -21.489 105.548  1.00 83.99           C  
ANISOU  989  CB  LYS A 186    11998   9089  10823   1800   -747    671       C  
ATOM    990  CG  LYS A 186     -54.420 -20.687 104.328  1.00 85.19           C  
ANISOU  990  CG  LYS A 186    12064   9292  11009   1882   -683    925       C  
ATOM    991  CD  LYS A 186     -55.206 -19.449 104.753  1.00 89.37           C  
ANISOU  991  CD  LYS A 186    12627   9668  11659   2129   -505   1076       C  
ATOM    992  CE  LYS A 186     -54.549 -18.156 104.289  1.00 94.69           C  
ANISOU  992  CE  LYS A 186    13395  10063  12518   2193   -365   1155       C  
ATOM    993  NZ  LYS A 186     -54.757 -17.063 105.282  1.00 98.87           N  
ANISOU  993  NZ  LYS A 186    14080  10266  13219   2355   -167   1097       N  
ATOM    994  N   PHE A 187     -51.392 -23.093 104.003  1.00 83.61           N  
ANISOU  994  N   PHE A 187    11963   9082  10722   1337   -954    441       N  
ATOM    995  CA  PHE A 187     -50.030 -22.825 103.560  1.00 85.24           C  
ANISOU  995  CA  PHE A 187    12234   9145  11006   1233   -961    377       C  
ATOM    996  C   PHE A 187     -50.058 -21.796 102.424  1.00 95.37           C  
ANISOU  996  C   PHE A 187    13484  10409  12341   1293   -894    575       C  
ATOM    997  O   PHE A 187     -50.293 -22.065 101.260  1.00 95.28           O  
ANISOU  997  O   PHE A 187    13366  10601  12234   1258   -913    710       O  
ATOM    998  CB  PHE A 187     -49.343 -24.091 103.186  1.00 82.00           C  
ANISOU  998  CB  PHE A 187    11788   8840  10524   1068  -1031    282       C  
ATOM    999  CG  PHE A 187     -49.069 -24.960 104.350  1.00 79.99           C  
ANISOU  999  CG  PHE A 187    11569   8559  10262   1031  -1066    124       C  
ATOM   1000  CD1 PHE A 187     -47.966 -24.719 105.172  1.00 81.47           C  
ANISOU 1000  CD1 PHE A 187    11837   8590  10527    998  -1080      1       C  
ATOM   1001  CD2 PHE A 187     -49.923 -25.972 104.681  1.00 79.55           C  
ANISOU 1001  CD2 PHE A 187    11453   8652  10121   1029  -1080    112       C  
ATOM   1002  CE1 PHE A 187     -47.704 -25.508 106.286  1.00 78.48           C  
ANISOU 1002  CE1 PHE A 187    11464   8235  10120    981  -1111   -105       C  
ATOM   1003  CE2 PHE A 187     -49.675 -26.775 105.786  1.00 79.64           C  
ANISOU 1003  CE2 PHE A 187    11485   8641  10133   1017  -1093      5       C  
ATOM   1004  CZ  PHE A 187     -48.559 -26.548 106.576  1.00 78.74           C  
ANISOU 1004  CZ  PHE A 187    11438   8400  10077   1004  -1110    -90       C  
ATOM   1005  N   ASN A 188     -49.864 -20.562 102.850  1.00111.78           N  
ANISOU 1005  N   ASN A 188    15658  12238  14574   1388   -796    590       N  
ATOM   1006  CA  ASN A 188     -49.978 -19.351 102.031  1.00121.88           C  
ANISOU 1006  CA  ASN A 188    16925  13421  15961   1499   -676    808       C  
ATOM   1007  C   ASN A 188     -48.878 -19.323 100.965  1.00127.48           C  
ANISOU 1007  C   ASN A 188    17616  14127  16694   1377   -696    849       C  
ATOM   1008  O   ASN A 188     -49.039 -18.679  99.936  1.00134.77           O  
ANISOU 1008  O   ASN A 188    18469  15096  17639   1452   -623   1085       O  
ATOM   1009  CB  ASN A 188     -49.827 -18.136 102.985  1.00129.25           C  
ANISOU 1009  CB  ASN A 188    18010  14005  17092   1587   -536    728       C  
ATOM   1010  CG  ASN A 188     -50.863 -17.058 102.806  1.00138.31           C  
ANISOU 1010  CG  ASN A 188    19140  15073  18339   1818   -360    967       C  
ATOM   1011  OD1 ASN A 188     -52.028 -17.272 102.438  1.00127.97           O  
ANISOU 1011  OD1 ASN A 188    17695  14004  16924   1953   -357   1178       O  
ATOM   1012  ND2 ASN A 188     -50.431 -15.861 103.135  1.00155.12           N  
ANISOU 1012  ND2 ASN A 188    21403  16850  20684   1861   -192    932       N  
ATOM   1013  N   SER A 189     -47.746 -19.982 101.230  1.00132.78           N  
ANISOU 1013  N   SER A 189    18337  14749  17361   1206   -779    646       N  
ATOM   1014  CA  SER A 189     -46.585 -19.899 100.339  1.00139.95           C  
ANISOU 1014  CA  SER A 189    19236  15622  18313   1094   -780    674       C  
ATOM   1015  C   SER A 189     -46.866 -20.656  99.069  1.00138.89           C  
ANISOU 1015  C   SER A 189    18976  15789  18004   1057   -824    803       C  
ATOM   1016  O   SER A 189     -47.080 -21.885  99.072  1.00130.25           O  
ANISOU 1016  O   SER A 189    17838  14887  16762    972   -906    700       O  
ATOM   1017  CB  SER A 189     -45.312 -20.456 100.990  1.00145.16           C  
ANISOU 1017  CB  SER A 189    19956  16185  19011    934   -850    447       C  
ATOM   1018  OG  SER A 189     -44.929 -19.711 102.129  1.00154.07           O  
ANISOU 1018  OG  SER A 189    21190  17076  20272    924   -818    302       O  
ATOM   1019  N   SER A 190     -46.864 -19.899  97.982  1.00145.31           N  
ANISOU 1019  N   SER A 190    19730  16641  18837   1116   -752   1029       N  
ATOM   1020  CA  SER A 190     -47.023 -20.451  96.639  1.00151.80           C  
ANISOU 1020  CA  SER A 190    20427  17781  19468   1067   -783   1160       C  
ATOM   1021  C   SER A 190     -45.672 -20.844  95.998  1.00145.79           C  
ANISOU 1021  C   SER A 190    19686  16994  18712    919   -792   1084       C  
ATOM   1022  O   SER A 190     -45.676 -21.731  95.164  1.00144.05           O  
ANISOU 1022  O   SER A 190    19396  17028  18306    824   -831   1066       O  
ATOM   1023  CB  SER A 190     -47.772 -19.449  95.739  1.00157.14           C  
ANISOU 1023  CB  SER A 190    20994  18582  20128   1230   -695   1495       C  
ATOM   1024  OG  SER A 190     -46.980 -18.299  95.491  1.00162.21           O  
ANISOU 1024  OG  SER A 190    21691  18962  20979   1285   -575   1620       O  
ATOM   1025  N   GLY A 191     -44.557 -20.193  96.375  1.00140.24           N  
ANISOU 1025  N   GLY A 191    20108  17019  16156    339    596    402       N  
ATOM   1026  CA  GLY A 191     -43.202 -20.569  95.913  1.00129.63           C  
ANISOU 1026  CA  GLY A 191    18659  15801  14792    218    219    272       C  
ATOM   1027  C   GLY A 191     -42.713 -19.745  94.727  1.00126.38           C  
ANISOU 1027  C   GLY A 191    18087  15428  14502    346    314    314       C  
ATOM   1028  O   GLY A 191     -43.526 -19.182  93.978  1.00126.32           O  
ANISOU 1028  O   GLY A 191    17937  15441  14617    602    586    502       O  
ATOM   1029  N   GLN A 192     -41.381 -19.650  94.589  1.00121.00           N  
ANISOU 1029  N   GLN A 192    17411  14794  13768    172    102    170       N  
ATOM   1030  CA  GLN A 192     -40.724 -18.871  93.506  1.00121.46           C  
ANISOU 1030  CA  GLN A 192    17352  14878  13919    234    177    169       C  
ATOM   1031  C   GLN A 192     -39.717 -19.701  92.749  1.00107.54           C  
ANISOU 1031  C   GLN A 192    15296  13365  12199    237   -229    125       C  
ATOM   1032  O   GLN A 192     -39.410 -20.806  93.139  1.00100.74           O  
ANISOU 1032  O   GLN A 192    14365  12624  11286    197   -530    104       O  
ATOM   1033  CB  GLN A 192     -39.998 -17.608  93.963  1.00134.67           C  
ANISOU 1033  CB  GLN A 192    19362  16342  15464    -33    451     21       C  
ATOM   1034  CG  GLN A 192     -39.080 -17.796  95.168  1.00149.58           C  
ANISOU 1034  CG  GLN A 192    21451  18288  17094   -462    250   -169       C  
ATOM   1035  CD  GLN A 192     -39.787 -17.320  96.478  1.00173.19           C  
ANISOU 1035  CD  GLN A 192    24890  20996  19915   -665    589   -228       C  
ATOM   1036  OE1 GLN A 192     -40.900 -17.745  96.798  1.00187.84           O  
ANISOU 1036  OE1 GLN A 192    26761  22762  21848   -457    683   -112       O  
ATOM   1037  NE2 GLN A 192     -39.140 -16.437  97.229  1.00183.76           N  
ANISOU 1037  NE2 GLN A 192    26611  22212  20997  -1119    799   -420       N  
ATOM   1038  N   CYS A 193     -39.294 -19.159  91.606  1.00 98.85           N  
ANISOU 1038  N   CYS A 193    14040  12313  11204    332   -174    144       N  
ATOM   1039  CA  CYS A 193     -38.326 -19.777  90.712  1.00 91.78           C  
ANISOU 1039  CA  CYS A 193    12875  11621  10373    361   -471    110       C  
ATOM   1040  C   CYS A 193     -36.978 -19.074  90.801  1.00 89.79           C  
ANISOU 1040  C   CYS A 193    12672  11406  10039    129   -503    -27       C  
ATOM   1041  O   CYS A 193     -36.872 -17.876  90.675  1.00 89.53           O  
ANISOU 1041  O   CYS A 193    12813  11226   9978     27   -214    -80       O  
ATOM   1042  CB  CYS A 193     -38.831 -19.760  89.265  1.00 91.71           C  
ANISOU 1042  CB  CYS A 193    12627  11703  10514    593   -406    234       C  
ATOM   1043  SG  CYS A 193     -40.233 -20.806  88.875  1.00 92.93           S  
ANISOU 1043  SG  CYS A 193    12607  12009  10692    745   -452    392       S  
ATOM   1044  N   GLU A 194     -35.941 -19.849  91.014  1.00 89.84           N  
ANISOU 1044  N   GLU A 194    12520  11627   9986     45   -825    -64       N  
ATOM   1045  CA  GLU A 194     -34.584 -19.343  91.140  1.00 93.67           C  
ANISOU 1045  CA  GLU A 194    12949  12294  10348   -214   -919   -163       C  
ATOM   1046  C   GLU A 194     -33.995 -19.111  89.744  1.00 92.58           C  
ANISOU 1046  C   GLU A 194    12584  12225  10365    -92   -912   -169       C  
ATOM   1047  O   GLU A 194     -34.349 -19.787  88.769  1.00 90.82           O  
ANISOU 1047  O   GLU A 194    12186  11998  10321    189   -965    -84       O  
ATOM   1048  CB  GLU A 194     -33.743 -20.394  91.881  1.00 99.93           C  
ANISOU 1048  CB  GLU A 194    13565  13384  11020   -257  -1273    -96       C  
ATOM   1049  CG  GLU A 194     -32.376 -19.934  92.360  1.00107.79           C  
ANISOU 1049  CG  GLU A 194    14444  14723  11785   -606  -1416   -146       C  
ATOM   1050  CD  GLU A 194     -32.474 -18.831  93.400  1.00113.47           C  
ANISOU 1050  CD  GLU A 194    15517  15376  12220  -1089  -1221   -308       C  
ATOM   1051  OE1 GLU A 194     -33.549 -18.717  94.046  1.00117.92           O  
ANISOU 1051  OE1 GLU A 194    16398  15641  12763  -1088  -1032   -332       O  
ATOM   1052  OE2 GLU A 194     -31.482 -18.076  93.569  1.00118.33           O  
ANISOU 1052  OE2 GLU A 194    16112  16236  12609  -1507  -1221   -419       O  
ATOM   1053  N   VAL A 195     -33.052 -18.187  89.653  1.00 94.95           N  
ANISOU 1053  N   VAL A 195    12903  12611  10560   -363   -841   -285       N  
ATOM   1054  CA  VAL A 195     -32.416 -17.854  88.379  1.00 95.71           C  
ANISOU 1054  CA  VAL A 195    12814  12767  10782   -293   -809   -310       C  
ATOM   1055  C   VAL A 195     -31.734 -19.065  87.805  1.00 93.77           C  
ANISOU 1055  C   VAL A 195    12202  12770  10656    -70  -1112   -214       C  
ATOM   1056  O   VAL A 195     -31.028 -19.752  88.529  1.00 95.08           O  
ANISOU 1056  O   VAL A 195    12214  13193  10719   -118  -1351   -154       O  
ATOM   1057  CB  VAL A 195     -31.422 -16.691  88.588  1.00100.58           C  
ANISOU 1057  CB  VAL A 195    13544  13469  11200   -726   -676   -480       C  
ATOM   1058  CG1 VAL A 195     -30.625 -16.357  87.341  1.00101.80           C  
ANISOU 1058  CG1 VAL A 195    13385  13874  11418   -736   -801   -505       C  
ATOM   1059  CG2 VAL A 195     -32.179 -15.449  89.070  1.00104.24           C  
ANISOU 1059  CG2 VAL A 195    14437  13528  11640   -816   -192   -559       C  
ATOM   1060  N   PRO A 196     -31.879 -19.313  86.506  1.00 93.46           N  
ANISOU 1060  N   PRO A 196    12030  12670  10811    170  -1070   -178       N  
ATOM   1061  CA  PRO A 196     -32.437 -18.390  85.516  1.00 90.68           C  
ANISOU 1061  CA  PRO A 196    11780  12129  10545    219   -807   -201       C  
ATOM   1062  C   PRO A 196     -33.886 -18.681  85.183  1.00 88.64           C  
ANISOU 1062  C   PRO A 196    11586  11723  10369    451   -702    -76       C  
ATOM   1063  O   PRO A 196     -34.395 -18.163  84.180  1.00 88.58           O  
ANISOU 1063  O   PRO A 196    11563  11660  10433    570   -528     -7       O  
ATOM   1064  CB  PRO A 196     -31.612 -18.704  84.288  1.00 90.74           C  
ANISOU 1064  CB  PRO A 196    11535  12267  10671    314   -886   -209       C  
ATOM   1065  CG  PRO A 196     -31.324 -20.180  84.414  1.00 92.08           C  
ANISOU 1065  CG  PRO A 196    11524  12564  10894    486  -1120   -129       C  
ATOM   1066  CD  PRO A 196     -31.229 -20.480  85.870  1.00 94.38           C  
ANISOU 1066  CD  PRO A 196    11873  12941  11044    387  -1256    -98       C  
ATOM   1067  N   LEU A 197     -34.558 -19.495  85.991  1.00 86.77           N  
ANISOU 1067  N   LEU A 197    11399  11473  10096    502   -803    -21       N  
ATOM   1068  CA  LEU A 197     -35.960 -19.778  85.739  1.00 83.09           C  
ANISOU 1068  CA  LEU A 197    10953  10953   9664    660   -708    104       C  
ATOM   1069  C   LEU A 197     -36.822 -18.585  86.133  1.00 85.57           C  
ANISOU 1069  C   LEU A 197    11466  11104   9943    677   -394    176       C  
ATOM   1070  O   LEU A 197     -36.460 -17.773  87.013  1.00 89.25           O  
ANISOU 1070  O   LEU A 197    12169  11421  10321    506   -249     83       O  
ATOM   1071  CB  LEU A 197     -36.375 -21.020  86.469  1.00 81.37           C  
ANISOU 1071  CB  LEU A 197    10755  10758   9404    679   -875    124       C  
ATOM   1072  CG  LEU A 197     -35.484 -22.246  86.190  1.00 81.58           C  
ANISOU 1072  CG  LEU A 197    10661  10869   9464    724  -1085     93       C  
ATOM   1073  CD1 LEU A 197     -36.013 -23.537  86.803  1.00 81.42           C  
ANISOU 1073  CD1 LEU A 197    10736  10804   9395    767  -1165    132       C  
ATOM   1074  CD2 LEU A 197     -35.349 -22.447  84.726  1.00 81.64           C  
ANISOU 1074  CD2 LEU A 197    10524  10933   9559    790  -1049     92       C  
ATOM   1075  N   VAL A 198     -37.981 -18.482  85.498  1.00 86.69           N  
ANISOU 1075  N   VAL A 198    11519  11295  10125    868   -250    364       N  
ATOM   1076  CA  VAL A 198     -38.979 -17.444  85.769  1.00 90.06           C  
ANISOU 1076  CA  VAL A 198    12088  11587  10542   1010    115    538       C  
ATOM   1077  C   VAL A 198     -40.323 -18.130  86.025  1.00 92.11           C  
ANISOU 1077  C   VAL A 198    12223  11998  10773   1128     93    717       C  
ATOM   1078  O   VAL A 198     -40.563 -19.240  85.563  1.00 90.35           O  
ANISOU 1078  O   VAL A 198    11790  12010  10528   1087   -157    721       O  
ATOM   1079  CB  VAL A 198     -39.064 -16.426  84.617  1.00 90.23           C  
ANISOU 1079  CB  VAL A 198    12049  11612  10621   1191    374    701       C  
ATOM   1080  CG1 VAL A 198     -39.531 -17.095  83.356  1.00 91.33           C  
ANISOU 1080  CG1 VAL A 198    11828  12096  10774   1303    196    860       C  
ATOM   1081  CG2 VAL A 198     -39.991 -15.268  84.940  1.00 94.08           C  
ANISOU 1081  CG2 VAL A 198    12732  11902  11110   1418    858    935       C  
ATOM   1082  N   ARG A 199     -41.160 -17.503  86.849  1.00 99.52           N  
ANISOU 1082  N   ARG A 199    13337  12784  11692   1228    392    840       N  
ATOM   1083  CA  ARG A 199     -42.398 -18.117  87.347  1.00103.22           C  
ANISOU 1083  CA  ARG A 199    13705  13395  12116   1300    392    991       C  
ATOM   1084  C   ARG A 199     -43.444 -18.150  86.301  1.00103.31           C  
ANISOU 1084  C   ARG A 199    13348  13783  12120   1509    449   1313       C  
ATOM   1085  O   ARG A 199     -43.717 -17.121  85.711  1.00113.24           O  
ANISOU 1085  O   ARG A 199    14548  15053  13424   1761    746   1557       O  
ATOM   1086  CB  ARG A 199     -42.884 -17.332  88.568  1.00109.14           C  
ANISOU 1086  CB  ARG A 199    14783  13835  12847   1349    758   1027       C  
ATOM   1087  CG  ARG A 199     -44.021 -17.987  89.351  1.00111.68           C  
ANISOU 1087  CG  ARG A 199    15059  14257  13117   1372    760   1128       C  
ATOM   1088  CD  ARG A 199     -43.648 -19.218  90.183  1.00104.68           C  
ANISOU 1088  CD  ARG A 199    14264  13361  12146   1089    395    875       C  
ATOM   1089  NE  ARG A 199     -44.810 -19.614  90.934  1.00105.50           N  
ANISOU 1089  NE  ARG A 199    14372  13517  12197   1117    493    985       N  
ATOM   1090  CZ  ARG A 199     -45.872 -20.279  90.451  1.00111.18           C  
ANISOU 1090  CZ  ARG A 199    14768  14597  12877   1177    431   1172       C  
ATOM   1091  NH1 ARG A 199     -45.949 -20.737  89.205  1.00110.82           N  
ANISOU 1091  NH1 ARG A 199    14384  14911  12811   1170    247   1257       N  
ATOM   1092  NH2 ARG A 199     -46.889 -20.521  91.258  1.00119.63           N  
ANISOU 1092  NH2 ARG A 199    15863  15700  13890   1182    561   1263       N  
ATOM   1093  N   THR A 200     -44.023 -19.317  86.058  1.00102.38           N  
ANISOU 1093  N   THR A 200    12991  13997  11912   1382    191   1330       N  
ATOM   1094  CA  THR A 200     -45.101 -19.409  85.034  1.00107.65           C  
ANISOU 1094  CA  THR A 200    13238  15177  12485   1481    212   1660       C  
ATOM   1095  C   THR A 200     -46.039 -20.543  85.394  1.00108.63           C  
ANISOU 1095  C   THR A 200    13220  15596  12457   1275     58   1669       C  
ATOM   1096  O   THR A 200     -45.599 -21.545  85.937  1.00104.63           O  
ANISOU 1096  O   THR A 200    12920  14915  11919   1023   -148   1373       O  
ATOM   1097  CB  THR A 200     -44.528 -19.647  83.612  1.00108.82           C  
ANISOU 1097  CB  THR A 200    13187  15563  12596   1379     21   1632       C  
ATOM   1098  OG1 THR A 200     -45.572 -19.822  82.638  1.00106.82           O  
ANISOU 1098  OG1 THR A 200    12504  15908  12172   1375      0   1952       O  
ATOM   1099  CG2 THR A 200     -43.603 -20.903  83.581  1.00110.69           C  
ANISOU 1099  CG2 THR A 200    13573  15676  12807   1051   -296   1252       C  
ATOM   1100  N   ASP A 201     -47.325 -20.380  85.114  1.00114.52           N  
ANISOU 1100  N   ASP A 201    13610  16808  13093   1389    186   2034       N  
ATOM   1101  CA  ASP A 201     -48.298 -21.438  85.379  1.00119.63           C  
ANISOU 1101  CA  ASP A 201    14085  17822  13544   1121     58   2049       C  
ATOM   1102  C   ASP A 201     -48.677 -22.254  84.126  1.00122.84           C  
ANISOU 1102  C   ASP A 201    14139  18839  13695    783   -164   2104       C  
ATOM   1103  O   ASP A 201     -49.355 -23.271  84.261  1.00124.89           O  
ANISOU 1103  O   ASP A 201    14320  19395  13737    426   -275   2037       O  
ATOM   1104  CB  ASP A 201     -49.534 -20.870  86.097  1.00124.06           C  
ANISOU 1104  CB  ASP A 201    14474  18559  14102   1384    351   2402       C  
ATOM   1105  CG  ASP A 201     -49.284 -20.623  87.624  1.00125.45           C  
ANISOU 1105  CG  ASP A 201    15121  18114  14430   1475    529   2201       C  
ATOM   1106  OD1 ASP A 201     -48.544 -21.406  88.327  1.00117.26           O  
ANISOU 1106  OD1 ASP A 201    14447  16709  13397   1204    322   1803       O  
ATOM   1107  OD2 ASP A 201     -49.859 -19.618  88.116  1.00132.53           O  
ANISOU 1107  OD2 ASP A 201    16026  18908  15422   1834    917   2482       O  
ATOM   1108  N   ASN A 202     -48.187 -21.862  82.940  1.00122.12           N  
ANISOU 1108  N   ASN A 202    13895  18908  13597    825   -214   2183       N  
ATOM   1109  CA  ASN A 202     -48.433 -22.602  81.696  1.00119.92           C  
ANISOU 1109  CA  ASN A 202    13339  19190  13033    430   -409   2199       C  
ATOM   1110  C   ASN A 202     -47.525 -23.839  81.628  1.00115.64           C  
ANISOU 1110  C   ASN A 202    13187  18298  12450     13   -592   1704       C  
ATOM   1111  O   ASN A 202     -46.306 -23.701  81.711  1.00111.24           O  
ANISOU 1111  O   ASN A 202    12938  17212  12113    144   -612   1463       O  
ATOM   1112  CB  ASN A 202     -48.188 -21.697  80.495  1.00122.76           C  
ANISOU 1112  CB  ASN A 202    13439  19803  13400    641   -369   2466       C  
ATOM   1113  CG  ASN A 202     -48.337 -22.427  79.180  1.00126.36           C  
ANISOU 1113  CG  ASN A 202    13656  20829  13526    171   -567   2452       C  
ATOM   1114  OD1 ASN A 202     -47.390 -22.511  78.404  1.00125.10           O  
ANISOU 1114  OD1 ASN A 202    13658  20473  13402     64   -643   2244       O  
ATOM   1115  ND2 ASN A 202     -49.528 -22.955  78.916  1.00131.07           N  
ANISOU 1115  ND2 ASN A 202    13866  22166  13768   -158   -634   2671       N  
ATOM   1116  N   PRO A 203     -48.097 -25.058  81.527  1.00117.15           N  
ANISOU 1116  N   PRO A 203    13391  18768  12352   -486   -678   1562       N  
ATOM   1117  CA  PRO A 203     -47.269 -26.292  81.570  1.00116.70           C  
ANISOU 1117  CA  PRO A 203    13798  18277  12264   -825   -736   1119       C  
ATOM   1118  C   PRO A 203     -46.408 -26.557  80.356  1.00118.43           C  
ANISOU 1118  C   PRO A 203    14105  18455  12435  -1006   -777    959       C  
ATOM   1119  O   PRO A 203     -45.521 -27.405  80.397  1.00119.94           O  
ANISOU 1119  O   PRO A 203    14705  18185  12681  -1134   -752    638       O  
ATOM   1120  CB  PRO A 203     -48.293 -27.416  81.714  1.00120.58           C  
ANISOU 1120  CB  PRO A 203    14300  19114  12400  -1354   -726   1045       C  
ATOM   1121  CG  PRO A 203     -49.566 -26.749  82.127  1.00122.96           C  
ANISOU 1121  CG  PRO A 203    14149  19945  12622  -1213   -694   1429       C  
ATOM   1122  CD  PRO A 203     -49.528 -25.390  81.500  1.00122.13           C  
ANISOU 1122  CD  PRO A 203    13653  20091  12658   -768   -673   1802       C  
ATOM   1123  N   LYS A 204     -46.696 -25.869  79.270  1.00124.13           N  
ANISOU 1123  N   LYS A 204    14446  19675  13040  -1006   -808   1213       N  
ATOM   1124  CA  LYS A 204     -45.917 -25.990  78.065  1.00128.74           C  
ANISOU 1124  CA  LYS A 204    15094  20252  13570  -1174   -833   1085       C  
ATOM   1125  C   LYS A 204     -44.577 -25.251  78.202  1.00123.62           C  
ANISOU 1125  C   LYS A 204    14631  19017  13319   -708   -813    990       C  
ATOM   1126  O   LYS A 204     -43.673 -25.451  77.387  1.00131.46           O  
ANISOU 1126  O   LYS A 204    15769  19839  14341   -799   -809    815       O  
ATOM   1127  CB  LYS A 204     -46.717 -25.430  76.876  1.00139.18           C  
ANISOU 1127  CB  LYS A 204    15908  22375  14598  -1325   -886   1443       C  
ATOM   1128  CG  LYS A 204     -48.132 -26.013  76.708  1.00149.21           C  
ANISOU 1128  CG  LYS A 204    16855  24431  15408  -1827   -931   1618       C  
ATOM   1129  CD  LYS A 204     -48.731 -25.811  75.302  1.00158.05           C  
ANISOU 1129  CD  LYS A 204    17508  26434  16107  -2181  -1019   1907       C  
ATOM   1130  CE  LYS A 204     -49.505 -24.504  75.133  1.00160.44           C  
ANISOU 1130  CE  LYS A 204    17177  27352  16428  -1688  -1032   2539       C  
ATOM   1131  NZ  LYS A 204     -48.688 -23.286  74.869  1.00159.78           N  
ANISOU 1131  NZ  LYS A 204    17104  26889  16714  -1047   -955   2703       N  
ATOM   1132  N   SER A 205     -44.453 -24.365  79.189  1.00115.13           N  
ANISOU 1132  N   SER A 205    13556  17669  12519   -253   -773   1106       N  
ATOM   1133  CA  SER A 205     -43.232 -23.567  79.388  1.00110.67           C  
ANISOU 1133  CA  SER A 205    13153  16624  12271    105   -741   1019       C  
ATOM   1134  C   SER A 205     -42.269 -24.185  80.425  1.00105.12           C  
ANISOU 1134  C   SER A 205    12827  15363  11750    151   -772    717       C  
ATOM   1135  O   SER A 205     -41.164 -23.668  80.631  1.00102.36           O  
ANISOU 1135  O   SER A 205    12594  14684  11614    361   -771    621       O  
ATOM   1136  CB  SER A 205     -43.601 -22.153  79.855  1.00111.53           C  
ANISOU 1136  CB  SER A 205    13108  16741  12526    518   -606   1314       C  
ATOM   1137  OG  SER A 205     -44.430 -21.501  78.934  1.00113.84           O  
ANISOU 1137  OG  SER A 205    13024  17559  12671    592   -543   1684       O  
ATOM   1138  N   TRP A 206     -42.689 -25.260  81.090  1.00 99.40           N  
ANISOU 1138  N   TRP A 206    12275  14576  10915    -50   -790    598       N  
ATOM   1139  CA  TRP A 206     -41.942 -25.767  82.247  1.00 94.11           C  
ANISOU 1139  CA  TRP A 206    11919  13442  10393     62   -810    415       C  
ATOM   1140  C   TRP A 206     -40.694 -26.472  81.880  1.00 88.93           C  
ANISOU 1140  C   TRP A 206    11474  12493   9821     55   -812    216       C  
ATOM   1141  O   TRP A 206     -40.689 -27.162  80.903  1.00 92.72           O  
ANISOU 1141  O   TRP A 206    12007  13054  10168   -184   -750    131       O  
ATOM   1142  CB  TRP A 206     -42.814 -26.708  83.083  1.00 96.34           C  
ANISOU 1142  CB  TRP A 206    12353  13729  10522   -129   -789    375       C  
ATOM   1143  CG  TRP A 206     -43.970 -26.013  83.722  1.00 97.79           C  
ANISOU 1143  CG  TRP A 206    12338  14154  10663    -53   -760    587       C  
ATOM   1144  CD1 TRP A 206     -44.100 -24.654  83.961  1.00 97.10           C  
ANISOU 1144  CD1 TRP A 206    12073  14103  10717    255   -699    790       C  
ATOM   1145  CD2 TRP A 206     -45.134 -26.625  84.258  1.00 98.81           C  
ANISOU 1145  CD2 TRP A 206    12461  14479  10600   -269   -725    627       C  
ATOM   1146  NE1 TRP A 206     -45.268 -24.407  84.626  1.00 99.42           N  
ANISOU 1146  NE1 TRP A 206    12249  14586  10938    292   -609    974       N  
ATOM   1147  CE2 TRP A 206     -45.933 -25.593  84.808  1.00100.39           C  
ANISOU 1147  CE2 TRP A 206    12434  14854  10855    -36   -652    882       C  
ATOM   1148  CE3 TRP A 206     -45.582 -27.937  84.326  1.00100.78           C  
ANISOU 1148  CE3 TRP A 206    12909  14757  10625   -650   -699    470       C  
ATOM   1149  CZ2 TRP A 206     -47.165 -25.840  85.410  1.00103.32           C  
ANISOU 1149  CZ2 TRP A 206    12701  15479  11075   -153   -588   1003       C  
ATOM   1150  CZ3 TRP A 206     -46.784 -28.196  84.939  1.00104.98           C  
ANISOU 1150  CZ3 TRP A 206    13366  15535  10985   -823   -654    554       C  
ATOM   1151  CH2 TRP A 206     -47.581 -27.148  85.455  1.00106.03           C  
ANISOU 1151  CH2 TRP A 206    13194  15904  11186   -569   -618    831       C  
ATOM   1152  N   TYR A 207     -39.642 -26.300  82.673  1.00 84.70           N  
ANISOU 1152  N   TYR A 207    11053  11650   9478    299   -859    162       N  
ATOM   1153  CA  TYR A 207     -38.344 -26.882  82.398  1.00 85.15           C  
ANISOU 1153  CA  TYR A 207    11237  11473   9642    389   -843     49       C  
ATOM   1154  C   TYR A 207     -38.154 -28.245  83.069  1.00 88.49           C  
ANISOU 1154  C   TYR A 207    11963  11635  10024    386   -770    -18       C  
ATOM   1155  O   TYR A 207     -37.924 -28.305  84.236  1.00 85.42           O  
ANISOU 1155  O   TYR A 207    11646  11122   9684    540   -840     25       O  
ATOM   1156  CB  TYR A 207     -37.249 -25.908  82.818  1.00 82.21           C  
ANISOU 1156  CB  TYR A 207    10750  11030   9455    627   -933     75       C  
ATOM   1157  CG  TYR A 207     -35.876 -26.544  82.833  1.00 83.53           C  
ANISOU 1157  CG  TYR A 207    10978  11029   9731    778   -933     30       C  
ATOM   1158  CD1 TYR A 207     -35.136 -26.743  81.659  1.00 83.48           C  
ANISOU 1158  CD1 TYR A 207    10928  11006   9785    789   -843    -23       C  
ATOM   1159  CD2 TYR A 207     -35.303 -26.927  84.024  1.00 86.24           C  
ANISOU 1159  CD2 TYR A 207    11395  11269  10104    930  -1006     81       C  
ATOM   1160  CE1 TYR A 207     -33.888 -27.318  81.678  1.00 84.83           C  
ANISOU 1160  CE1 TYR A 207    11115  11048  10067    988   -795     -8       C  
ATOM   1161  CE2 TYR A 207     -34.038 -27.492  84.050  1.00 87.97           C  
ANISOU 1161  CE2 TYR A 207    11589  11420  10413   1135   -992    130       C  
ATOM   1162  CZ  TYR A 207     -33.348 -27.680  82.877  1.00 87.76           C  
ANISOU 1162  CZ  TYR A 207    11506  11368  10470   1183   -872     93       C  
ATOM   1163  OH  TYR A 207     -32.122 -28.252  82.942  1.00 93.37           O  
ANISOU 1163  OH  TYR A 207    12162  12033  11279   1442   -815    195       O  
ATOM   1164  N   GLU A 208     -38.232 -29.318  82.297  1.00 96.10           N  
ANISOU 1164  N   GLU A 208    13137  12504  10871    196   -589   -118       N  
ATOM   1165  CA  GLU A 208     -38.152 -30.697  82.784  1.00104.07           C  
ANISOU 1165  CA  GLU A 208    14532  13199  11810    180   -402   -176       C  
ATOM   1166  C   GLU A 208     -38.884 -31.001  84.105  1.00103.10           C  
ANISOU 1166  C   GLU A 208    14540  13021  11610    173   -452   -133       C  
ATOM   1167  O   GLU A 208     -40.065 -30.766  84.205  1.00103.52           O  
ANISOU 1167  O   GLU A 208    14516  13302  11512    -77   -498   -139       O  
ATOM   1168  CB  GLU A 208     -36.684 -31.232  82.685  1.00113.38           C  
ANISOU 1168  CB  GLU A 208    15830  14080  13167    511   -270   -144       C  
ATOM   1169  CG  GLU A 208     -35.587 -30.426  83.342  1.00119.52           C  
ANISOU 1169  CG  GLU A 208    16324  14929  14158    883   -484     -1       C  
ATOM   1170  CD  GLU A 208     -34.177 -30.972  83.035  1.00126.90           C  
ANISOU 1170  CD  GLU A 208    17281  15692  15243   1204   -331     82       C  
ATOM   1171  OE1 GLU A 208     -33.295 -30.775  83.890  1.00130.14           O  
ANISOU 1171  OE1 GLU A 208    17516  16174  15756   1506   -470    253       O  
ATOM   1172  OE2 GLU A 208     -33.946 -31.551  81.932  1.00126.77           O  
ANISOU 1172  OE2 GLU A 208    17433  15513  15221   1138    -61     -4       O  
ATOM   1173  N   ASP A 209     -38.210 -31.608  85.062  1.00108.52           N  
ANISOU 1173  N   ASP A 209    15423  13433  12376    442   -417    -65       N  
ATOM   1174  CA  ASP A 209     -38.790 -31.995  86.355  1.00110.77           C  
ANISOU 1174  CA  ASP A 209    15883  13625  12579    448   -446    -20       C  
ATOM   1175  C   ASP A 209     -39.247 -30.785  87.184  1.00106.24           C  
ANISOU 1175  C   ASP A 209    15033  13292  12042    471   -703     46       C  
ATOM   1176  O   ASP A 209     -40.259 -30.858  87.878  1.00108.23           O  
ANISOU 1176  O   ASP A 209    15365  13582  12175    318   -707     38       O  
ATOM   1177  CB  ASP A 209     -37.774 -32.853  87.142  1.00114.96           C  
ANISOU 1177  CB  ASP A 209    16642  13850  13185    804   -351    110       C  
ATOM   1178  CG  ASP A 209     -36.346 -32.330  86.995  1.00120.38           C  
ANISOU 1178  CG  ASP A 209    17049  14618  14071   1157   -470    248       C  
ATOM   1179  OD1 ASP A 209     -36.138 -31.160  86.531  1.00123.21           O  
ANISOU 1179  OD1 ASP A 209    17064  15235  14514   1111   -660    215       O  
ATOM   1180  OD2 ASP A 209     -35.437 -33.093  87.327  1.00125.15           O  
ANISOU 1180  OD2 ASP A 209    17772  15044  14733   1485   -344    413       O  
ATOM   1181  N   VAL A 210     -38.525 -29.677  87.121  1.00100.85           N  
ANISOU 1181  N   VAL A 210    14066  12747  11504    637   -866    103       N  
ATOM   1182  CA  VAL A 210     -39.024 -28.449  87.776  1.00 98.51           C  
ANISOU 1182  CA  VAL A 210    13594  12615  11219    614   -998    144       C  
ATOM   1183  C   VAL A 210     -40.361 -28.001  87.161  1.00102.24           C  
ANISOU 1183  C   VAL A 210    13939  13302  11602    405   -929    141       C  
ATOM   1184  O   VAL A 210     -40.444 -27.875  85.980  1.00111.66           O  
ANISOU 1184  O   VAL A 210    14996  14642  12786    319   -886    126       O  
ATOM   1185  CB  VAL A 210     -38.063 -27.276  87.612  1.00 92.24           C  
ANISOU 1185  CB  VAL A 210    12574  11918  10554    739  -1103    171       C  
ATOM   1186  CG1 VAL A 210     -38.671 -26.050  88.241  1.00 87.08           C  
ANISOU 1186  CG1 VAL A 210    11860  11341   9885    685  -1113    197       C  
ATOM   1187  CG2 VAL A 210     -36.719 -27.614  88.219  1.00 94.51           C  
ANISOU 1187  CG2 VAL A 210    12869  12151  10888    921  -1204    230       C  
ATOM   1188  N   GLU A 211     -41.413 -27.799  87.925  1.00104.01           N  
ANISOU 1188  N   GLU A 211    14184  13590  11743    324   -908    185       N  
ATOM   1189  CA  GLU A 211     -42.709 -27.483  87.350  1.00104.69           C  
ANISOU 1189  CA  GLU A 211    14078  13979  11720    158   -831    258       C  
ATOM   1190  C   GLU A 211     -43.124 -26.216  88.007  1.00101.40           C  
ANISOU 1190  C   GLU A 211    13536  13614  11377    312   -798    387       C  
ATOM   1191  O   GLU A 211     -42.907 -26.041  89.211  1.00106.56           O  
ANISOU 1191  O   GLU A 211    14367  14056  12062    387   -810    363       O  
ATOM   1192  CB  GLU A 211     -43.687 -28.573  87.708  1.00114.62           C  
ANISOU 1192  CB  GLU A 211    15501  15269  12779    -98   -758    210       C  
ATOM   1193  CG  GLU A 211     -43.443 -29.958  87.109  1.00122.54           C  
ANISOU 1193  CG  GLU A 211    16762  16145  13650   -324   -668     59       C  
ATOM   1194  CD  GLU A 211     -44.552 -30.972  87.459  1.00134.49           C  
ANISOU 1194  CD  GLU A 211    18480  17708  14910   -675   -542    -11       C  
ATOM   1195  OE1 GLU A 211     -45.581 -30.630  88.113  1.00137.85           O  
ANISOU 1195  OE1 GLU A 211    18777  18336  15262   -745   -553     74       O  
ATOM   1196  OE2 GLU A 211     -44.394 -32.146  87.076  1.00144.66           O  
ANISOU 1196  OE2 GLU A 211    20093  18811  16057   -902   -381   -157       O  
ATOM   1197  N   GLY A 212     -43.668 -25.316  87.222  1.00 97.08           N  
ANISOU 1197  N   GLY A 212    12713  13331  10842    366   -720    539       N  
ATOM   1198  CA  GLY A 212     -43.944 -23.956  87.657  1.00 96.28           C  
ANISOU 1198  CA  GLY A 212    12539  13207  10834    579   -577    691       C  
ATOM   1199  C   GLY A 212     -42.881 -22.948  87.178  1.00 95.64           C  
ANISOU 1199  C   GLY A 212    12445  12997  10895    732   -555    674       C  
ATOM   1200  O   GLY A 212     -43.079 -21.720  87.288  1.00 94.15           O  
ANISOU 1200  O   GLY A 212    12241  12759  10773    902   -349    807       O  
ATOM   1201  N   CYS A 213     -41.748 -23.447  86.657  1.00 93.62           N  
ANISOU 1201  N   CYS A 213    12225  12664  10682    677   -712    518       N  
ATOM   1202  CA  CYS A 213     -40.627 -22.600  86.278  1.00 91.79           C  
ANISOU 1202  CA  CYS A 213    11985  12326  10565    766   -708    469       C  
ATOM   1203  C   CYS A 213     -40.253 -22.833  84.835  1.00 89.45           C  
ANISOU 1203  C   CYS A 213    11513  12188  10285    743   -759    461       C  
ATOM   1204  O   CYS A 213     -40.075 -23.976  84.437  1.00 91.61           O  
ANISOU 1204  O   CYS A 213    11810  12489  10507    626   -855    370       O  
ATOM   1205  CB  CYS A 213     -39.396 -22.952  87.113  1.00 94.92           C  
ANISOU 1205  CB  CYS A 213    12552  12525  10987    727   -852    309       C  
ATOM   1206  SG  CYS A 213     -39.541 -22.710  88.882  1.00 99.70           S  
ANISOU 1206  SG  CYS A 213    13408  12956  11516    667   -829    280       S  
ATOM   1207  N   GLY A 214     -40.101 -21.771  84.047  1.00 86.66           N  
ANISOU 1207  N   GLY A 214    11035  11902   9989    843   -651    552       N  
ATOM   1208  CA  GLY A 214     -39.561 -21.901  82.682  1.00 83.31           C  
ANISOU 1208  CA  GLY A 214    10470  11604   9579    805   -699    524       C  
ATOM   1209  C   GLY A 214     -38.295 -21.084  82.503  1.00 79.31           C  
ANISOU 1209  C   GLY A 214    10008  10930   9194    869   -675    428       C  
ATOM   1210  O   GLY A 214     -38.017 -20.228  83.323  1.00 76.99           O  
ANISOU 1210  O   GLY A 214     9846  10467   8937    912   -580    410       O  
ATOM   1211  N   ILE A 215     -37.531 -21.348  81.435  1.00 76.05           N  
ANISOU 1211  N   ILE A 215     9510  10569   8815    827   -731    351       N  
ATOM   1212  CA  ILE A 215     -36.273 -20.627  81.216  1.00 74.63           C  
ANISOU 1212  CA  ILE A 215     9342  10276   8736    850   -711    250       C  
ATOM   1213  C   ILE A 215     -36.615 -19.212  80.783  1.00 76.61           C  
ANISOU 1213  C   ILE A 215     9584  10528   8994    940   -496    382       C  
ATOM   1214  O   ILE A 215     -37.539 -18.983  80.051  1.00 76.57           O  
ANISOU 1214  O   ILE A 215     9458  10698   8934   1018   -406    576       O  
ATOM   1215  CB  ILE A 215     -35.374 -21.293  80.176  1.00 73.16           C  
ANISOU 1215  CB  ILE A 215     9072  10130   8594    804   -782    146       C  
ATOM   1216  CG1 ILE A 215     -35.081 -22.729  80.559  1.00 74.11           C  
ANISOU 1216  CG1 ILE A 215     9261  10186   8708    780   -886     64       C  
ATOM   1217  CG2 ILE A 215     -34.056 -20.561  80.077  1.00 72.94           C  
ANISOU 1217  CG2 ILE A 215     9019  10036   8657    807   -767     47       C  
ATOM   1218  CD1 ILE A 215     -34.320 -23.550  79.547  1.00 74.68           C  
ANISOU 1218  CD1 ILE A 215     9320  10236   8819    761   -857    -19       C  
ATOM   1219  N   GLN A 216     -35.892 -18.248  81.296  1.00 79.59           N  
ANISOU 1219  N   GLN A 216    10105  10725   9408    917   -381    301       N  
ATOM   1220  CA  GLN A 216     -36.158 -16.879  80.957  1.00 84.93           C  
ANISOU 1220  CA  GLN A 216    10880  11302  10087   1014    -78    421       C  
ATOM   1221  C   GLN A 216     -35.875 -16.674  79.479  1.00 90.39           C  
ANISOU 1221  C   GLN A 216    11419  12121  10804   1060    -56    476       C  
ATOM   1222  O   GLN A 216     -34.949 -17.274  78.924  1.00 88.45           O  
ANISOU 1222  O   GLN A 216    11074  11938  10594    945   -232    316       O  
ATOM   1223  CB  GLN A 216     -35.350 -15.893  81.842  1.00 86.82           C  
ANISOU 1223  CB  GLN A 216    11398  11286  10302    861     98    260       C  
ATOM   1224  CG  GLN A 216     -33.851 -16.081  81.823  1.00 86.62           C  
ANISOU 1224  CG  GLN A 216    11323  11311  10276    629    -81     22       C  
ATOM   1225  CD  GLN A 216     -33.102 -15.095  82.663  1.00 89.04           C  
ANISOU 1225  CD  GLN A 216    11888  11468  10474    355     92   -143       C  
ATOM   1226  OE1 GLN A 216     -33.648 -14.426  83.547  1.00 88.52           O  
ANISOU 1226  OE1 GLN A 216    12116  11194  10321    296    341   -132       O  
ATOM   1227  NE2 GLN A 216     -31.803 -14.974  82.360  1.00 91.59           N  
ANISOU 1227  NE2 GLN A 216    12115  11912  10772    140     -2   -307       N  
ATOM   1228  N   CYS A 217     -36.686 -15.794  78.872  1.00 97.89           N  
ANISOU 1228  N   CYS A 217    14266  12979   9946    958    163   1057       N  
ATOM   1229  CA  CYS A 217     -36.625 -15.449  77.451  1.00 99.86           C  
ANISOU 1229  CA  CYS A 217    14512  13240  10190   1031    196   1090       C  
ATOM   1230  C   CYS A 217     -35.227 -15.064  76.976  1.00 97.42           C  
ANISOU 1230  C   CYS A 217    14311  12752   9951    928    203   1033       C  
ATOM   1231  O   CYS A 217     -34.761 -15.551  75.912  1.00103.85           O  
ANISOU 1231  O   CYS A 217    15047  13594  10816    878    157   1026       O  
ATOM   1232  CB  CYS A 217     -37.604 -14.335  77.138  1.00106.04           C  
ANISOU 1232  CB  CYS A 217    15369  14064  10855   1264    319   1174       C  
ATOM   1233  SG  CYS A 217     -37.398 -13.822  75.442  1.00121.57           S  
ANISOU 1233  SG  CYS A 217    17351  16027  12811   1355    368   1218       S  
ATOM   1234  N   GLN A 218     -34.543 -14.241  77.755  1.00 94.39           N  
ANISOU 1234  N   GLN A 218    14101  12203   9558    876    261    989       N  
ATOM   1235  CA  GLN A 218     -33.171 -13.893  77.435  1.00 95.73           C  
ANISOU 1235  CA  GLN A 218    14362  12238   9770    739    265    930       C  
ATOM   1236  C   GLN A 218     -32.199 -14.998  77.867  1.00 85.80           C  
ANISOU 1236  C   GLN A 218    12982  11021   8595    557    144    873       C  
ATOM   1237  O   GLN A 218     -32.079 -15.304  79.015  1.00 78.40           O  
ANISOU 1237  O   GLN A 218    12035  10092   7659    486    111    846       O  
ATOM   1238  CB  GLN A 218     -32.815 -12.534  78.027  1.00107.22           C  
ANISOU 1238  CB  GLN A 218    16070  13514  11155    724    388    901       C  
ATOM   1239  CG  GLN A 218     -31.673 -11.814  77.319  1.00116.95           C  
ANISOU 1239  CG  GLN A 218    17433  14616  12383    617    438    860       C  
ATOM   1240  CD  GLN A 218     -30.822 -11.050  78.329  1.00133.48           C  
ANISOU 1240  CD  GLN A 218    19718  16575  14423    444    498    783       C  
ATOM   1241  OE1 GLN A 218     -30.043 -11.652  79.087  1.00138.00           O  
ANISOU 1241  OE1 GLN A 218    20199  17208  15026    269    411    727       O  
ATOM   1242  NE2 GLN A 218     -30.999  -9.735  78.384  1.00141.95           N  
ANISOU 1242  NE2 GLN A 218    21064  17472  15397    494    655    783       N  
ATOM   1243  N   ASN A 219     -31.509 -15.549  76.876  1.00 84.79           N  
ANISOU 1243  N   ASN A 219    12768  10923   8526    504     90    863       N  
ATOM   1244  CA  ASN A 219     -30.626 -16.686  77.011  1.00 86.19           C  
ANISOU 1244  CA  ASN A 219    12823  11153   8771    385    -11    830       C  
ATOM   1245  C   ASN A 219     -29.714 -16.568  78.234  1.00 83.29           C  
ANISOU 1245  C   ASN A 219    12496  10757   8391    256    -27    783       C  
ATOM   1246  O   ASN A 219     -28.813 -15.761  78.248  1.00 80.00           O  
ANISOU 1246  O   ASN A 219    12174  10281   7942    163     14    745       O  
ATOM   1247  CB  ASN A 219     -29.778 -16.838  75.738  1.00 91.33           C  
ANISOU 1247  CB  ASN A 219    13435  11805   9461    353    -30    820       C  
ATOM   1248  CG  ASN A 219     -29.174 -18.249  75.556  1.00 98.21           C  
ANISOU 1248  CG  ASN A 219    14166  12751  10396    300   -125    810       C  
ATOM   1249  OD1 ASN A 219     -28.824 -18.934  76.506  1.00 98.82           O  
ANISOU 1249  OD1 ASN A 219    14202  12857  10486    248   -174    798       O  
ATOM   1250  ND2 ASN A 219     -29.030 -18.667  74.296  1.00108.54           N  
ANISOU 1250  ND2 ASN A 219    15417  14086  11735    324   -140    817       N  
ATOM   1251  N   PRO A 220     -29.940 -17.416  79.258  1.00 83.93           N  
ANISOU 1251  N   PRO A 220    12502  10899   8486    235    -87    785       N  
ATOM   1252  CA  PRO A 220     -29.153 -17.367  80.483  1.00 83.53           C  
ANISOU 1252  CA  PRO A 220    12467  10858   8411    119   -105    750       C  
ATOM   1253  C   PRO A 220     -27.708 -17.742  80.311  1.00 82.97           C  
ANISOU 1253  C   PRO A 220    12328  10844   8352     13   -154    727       C  
ATOM   1254  O   PRO A 220     -26.894 -17.352  81.144  1.00 85.04           O  
ANISOU 1254  O   PRO A 220    12614  11136   8561   -105   -150    694       O  
ATOM   1255  CB  PRO A 220     -29.828 -18.402  81.371  1.00 83.29           C  
ANISOU 1255  CB  PRO A 220    12351  10895   8399    149   -164    776       C  
ATOM   1256  CG  PRO A 220     -30.451 -19.385  80.447  1.00 82.02           C  
ANISOU 1256  CG  PRO A 220    12100  10776   8288    225   -203    812       C  
ATOM   1257  CD  PRO A 220     -30.909 -18.543  79.294  1.00 84.20           C  
ANISOU 1257  CD  PRO A 220    12428  11014   8549    300   -140    822       C  
ATOM   1258  N   LEU A 221     -27.382 -18.469  79.251  1.00 81.11           N  
ANISOU 1258  N   LEU A 221    12005  10641   8169     52   -193    746       N  
ATOM   1259  CA  LEU A 221     -26.011 -18.875  79.009  1.00 82.57           C  
ANISOU 1259  CA  LEU A 221    12110  10906   8354    -15   -235    736       C  
ATOM   1260  C   LEU A 221     -25.074 -17.729  78.560  1.00 81.79           C  
ANISOU 1260  C   LEU A 221    12078  10798   8200   -126   -186    696       C  
ATOM   1261  O   LEU A 221     -23.881 -17.932  78.536  1.00 79.32           O  
ANISOU 1261  O   LEU A 221    11686  10593   7857   -205   -217    688       O  
ATOM   1262  CB  LEU A 221     -25.968 -20.041  78.000  1.00 84.17           C  
ANISOU 1262  CB  LEU A 221    12221  11137   8623     70   -279    767       C  
ATOM   1263  CG  LEU A 221     -26.374 -21.409  78.572  1.00 88.12           C  
ANISOU 1263  CG  LEU A 221    12661  11665   9154    128   -329    800       C  
ATOM   1264  CD1 LEU A 221     -27.890 -21.556  78.642  1.00 90.87           C  
ANISOU 1264  CD1 LEU A 221    13045  11963   9516    179   -315    813       C  
ATOM   1265  CD2 LEU A 221     -25.780 -22.588  77.810  1.00 89.71           C  
ANISOU 1265  CD2 LEU A 221    12798  11896   9389    184   -359    823       C  
ATOM   1266  N   PHE A 222     -25.604 -16.548  78.203  1.00 82.56           N  
ANISOU 1266  N   PHE A 222    12324  10776   8268   -128   -102    678       N  
ATOM   1267  CA  PHE A 222     -24.789 -15.426  77.684  1.00 81.81           C  
ANISOU 1267  CA  PHE A 222    12333  10642   8109   -246    -37    639       C  
ATOM   1268  C   PHE A 222     -25.213 -14.125  78.291  1.00 82.77           C  
ANISOU 1268  C   PHE A 222    12666  10631   8150   -302     67    606       C  
ATOM   1269  O   PHE A 222     -26.399 -13.856  78.397  1.00 81.57           O  
ANISOU 1269  O   PHE A 222    12600  10383   8009   -171    115    633       O  
ATOM   1270  CB  PHE A 222     -24.932 -15.314  76.153  1.00 82.12           C  
ANISOU 1270  CB  PHE A 222    12376  10634   8190   -163    -17    661       C  
ATOM   1271  CG  PHE A 222     -24.568 -16.564  75.425  1.00 81.23           C  
ANISOU 1271  CG  PHE A 222    12087  10627   8150   -101   -103    687       C  
ATOM   1272  CD1 PHE A 222     -23.251 -16.847  75.143  1.00 80.97           C  
ANISOU 1272  CD1 PHE A 222    11959  10707   8096   -188   -141    673       C  
ATOM   1273  CD2 PHE A 222     -25.551 -17.470  75.054  1.00 81.86           C  
ANISOU 1273  CD2 PHE A 222    12101  10702   8299     37   -136    726       C  
ATOM   1274  CE1 PHE A 222     -22.889 -18.018  74.501  1.00 82.09           C  
ANISOU 1274  CE1 PHE A 222    11961  10934   8293   -109   -204    701       C  
ATOM   1275  CE2 PHE A 222     -25.196 -18.665  74.424  1.00 84.57           C  
ANISOU 1275  CE2 PHE A 222    12320  11117   8695     82   -199    743       C  
ATOM   1276  CZ  PHE A 222     -23.850 -18.943  74.147  1.00 82.90           C  
ANISOU 1276  CZ  PHE A 222    12032  10995   8469     24   -229    732       C  
ATOM   1277  N   THR A 223     -24.236 -13.282  78.599  1.00 86.60           N  
ANISOU 1277  N   THR A 223    13247  11116   8538   -499    115    550       N  
ATOM   1278  CA  THR A 223     -24.474 -11.946  79.203  1.00 90.73           C  
ANISOU 1278  CA  THR A 223    14028  11487   8958   -593    242    503       C  
ATOM   1279  C   THR A 223     -25.175 -10.962  78.233  1.00 92.20           C  
ANISOU 1279  C   THR A 223    14423  11475   9132   -479    362    524       C  
ATOM   1280  O   THR A 223     -25.281 -11.239  77.047  1.00 93.72           O  
ANISOU 1280  O   THR A 223    14544  11678   9388   -371    339    566       O  
ATOM   1281  CB  THR A 223     -23.152 -11.296  79.699  1.00 92.54           C  
ANISOU 1281  CB  THR A 223    14319  11785   9058   -885    271    427       C  
ATOM   1282  OG1 THR A 223     -22.273 -11.029  78.603  1.00 94.96           O  
ANISOU 1282  OG1 THR A 223    14613  12124   9340   -977    279    415       O  
ATOM   1283  CG2 THR A 223     -22.399 -12.199  80.633  1.00 92.84           C  
ANISOU 1283  CG2 THR A 223    14138  12055   9080   -984    160    420       C  
ATOM   1284  N   GLU A 224     -25.667  -9.841  78.746  1.00 96.46           N  
ANISOU 1284  N   GLU A 224    15226  11839   9582   -488    496    501       N  
ATOM   1285  CA  GLU A 224     -26.273  -8.779  77.911  1.00101.98           C  
ANISOU 1285  CA  GLU A 224    16167  12338  10241   -365    639    531       C  
ATOM   1286  C   GLU A 224     -25.219  -8.171  76.960  1.00101.34           C  
ANISOU 1286  C   GLU A 224    16176  12217  10109   -530    684    497       C  
ATOM   1287  O   GLU A 224     -25.515  -7.835  75.780  1.00 99.72           O  
ANISOU 1287  O   GLU A 224    16032  11933   9923   -400    735    547       O  
ATOM   1288  CB  GLU A 224     -26.951  -7.702  78.801  1.00108.58           C  
ANISOU 1288  CB  GLU A 224    17304  12979  10970   -336    794    513       C  
ATOM   1289  CG  GLU A 224     -27.266  -6.323  78.184  1.00115.03           C  
ANISOU 1289  CG  GLU A 224    18470  13546  11688   -264    990    527       C  
ATOM   1290  CD  GLU A 224     -28.471  -6.304  77.240  1.00122.30           C  
ANISOU 1290  CD  GLU A 224    19380  14431  12654     77   1030    642       C  
ATOM   1291  OE1 GLU A 224     -29.360  -5.420  77.450  1.00121.44           O  
ANISOU 1291  OE1 GLU A 224    19524  14154  12460    260   1187    684       O  
ATOM   1292  OE2 GLU A 224     -28.503  -7.138  76.268  1.00127.44           O  
ANISOU 1292  OE2 GLU A 224    19780  15233  13407    163    915    692       O  
ATOM   1293  N   ALA A 225     -23.993  -8.056  77.461  1.00101.79           N  
ANISOU 1293  N   ALA A 225    16224  12360  10091   -819    662    418       N  
ATOM   1294  CA  ALA A 225     -22.859  -7.586  76.653  1.00105.74           C  
ANISOU 1294  CA  ALA A 225    16768  12880  10526  -1021    687    379       C  
ATOM   1295  C   ALA A 225     -22.640  -8.456  75.427  1.00104.23           C  
ANISOU 1295  C   ALA A 225    16328  12824  10448   -904    577    434       C  
ATOM   1296  O   ALA A 225     -22.364  -7.943  74.330  1.00108.08           O  
ANISOU 1296  O   ALA A 225    16902  13244  10917   -916    632    443       O  
ATOM   1297  CB  ALA A 225     -21.585  -7.573  77.483  1.00107.99           C  
ANISOU 1297  CB  ALA A 225    16995  13334  10702  -1352    650    294       C  
ATOM   1298  N   GLU A 226     -22.754  -9.766  75.635  1.00 97.69           N  
ANISOU 1298  N   GLU A 226    15214  12176   9728   -796    432    468       N  
ATOM   1299  CA  GLU A 226     -22.622 -10.729  74.564  1.00 94.26           C  
ANISOU 1299  CA  GLU A 226    14552  11861   9399   -674    332    517       C  
ATOM   1300  C   GLU A 226     -23.782 -10.707  73.596  1.00 91.39           C  
ANISOU 1300  C   GLU A 226    14228  11385   9111   -426    366    585       C  
ATOM   1301  O   GLU A 226     -23.594 -10.917  72.424  1.00 90.55           O  
ANISOU 1301  O   GLU A 226    14047  11311   9045   -374    344    611       O  
ATOM   1302  CB  GLU A 226     -22.423 -12.114  75.157  1.00 96.33           C  
ANISOU 1302  CB  GLU A 226    14548  12318   9732   -635    192    532       C  
ATOM   1303  CG  GLU A 226     -21.048 -12.256  75.811  1.00 99.58           C  
ANISOU 1303  CG  GLU A 226    14856  12921  10057   -863    144    485       C  
ATOM   1304  CD  GLU A 226     -20.890 -13.462  76.762  1.00100.75           C  
ANISOU 1304  CD  GLU A 226    14791  13247  10241   -821     34    508       C  
ATOM   1305  OE1 GLU A 226     -21.868 -13.974  77.362  1.00 95.49           O  
ANISOU 1305  OE1 GLU A 226    14114  12524   9642   -680     12    537       O  
ATOM   1306  OE2 GLU A 226     -19.732 -13.893  76.922  1.00104.06           O  
ANISOU 1306  OE2 GLU A 226    15050  13882  10605   -931    -25    501       O  
ATOM   1307  N   HIS A 227     -24.980 -10.461  74.087  1.00 93.95           N  
ANISOU 1307  N   HIS A 227    14654  11602   9438   -272    420    617       N  
ATOM   1308  CA  HIS A 227     -26.154 -10.303  73.238  1.00 98.01           C  
ANISOU 1308  CA  HIS A 227    15207  12046   9986    -31    469    693       C  
ATOM   1309  C   HIS A 227     -26.007  -9.106  72.274  1.00103.64           C  
ANISOU 1309  C   HIS A 227    16142  12608  10628    -27    599    706       C  
ATOM   1310  O   HIS A 227     -26.134  -9.281  71.055  1.00108.08           O  
ANISOU 1310  O   HIS A 227    16628  13205  11230     73    584    752       O  
ATOM   1311  CB  HIS A 227     -27.454 -10.167  74.077  1.00 99.74           C  
ANISOU 1311  CB  HIS A 227    15495  12210  10188    134    515    731       C  
ATOM   1312  CG  HIS A 227     -28.022 -11.477  74.576  1.00 99.87           C  
ANISOU 1312  CG  HIS A 227    15274  12383  10288    209    389    752       C  
ATOM   1313  ND1 HIS A 227     -27.449 -12.215  75.593  1.00 98.09           N  
ANISOU 1313  ND1 HIS A 227    14935  12246  10087     77    300    706       N  
ATOM   1314  CD2 HIS A 227     -29.151 -12.147  74.224  1.00100.19           C  
ANISOU 1314  CD2 HIS A 227    15184  12511  10373    395    350    817       C  
ATOM   1315  CE1 HIS A 227     -28.177 -13.294  75.814  1.00 96.96           C  
ANISOU 1315  CE1 HIS A 227    14622  12207  10008    180    215    742       C  
ATOM   1316  NE2 HIS A 227     -29.217 -13.276  75.002  1.00 96.55           N  
ANISOU 1316  NE2 HIS A 227    14555  12161   9965    357    242    803       N  
ATOM   1317  N   GLN A 228     -25.772  -7.901  72.788  1.00107.79           N  
ANISOU 1317  N   GLN A 228    16956  12958  11040   -136    735    667       N  
ATOM   1318  CA  GLN A 228     -25.698  -6.717  71.903  1.00110.86           C  
ANISOU 1318  CA  GLN A 228    17606  13168  11347   -122    883    687       C  
ATOM   1319  C   GLN A 228     -24.552  -6.828  70.888  1.00109.41           C  
ANISOU 1319  C   GLN A 228    17335  13062  11173   -287    835    658       C  
ATOM   1320  O   GLN A 228     -24.613  -6.257  69.799  1.00112.08           O  
ANISOU 1320  O   GLN A 228    17782  13315  11487   -217    910    700       O  
ATOM   1321  CB  GLN A 228     -25.459  -5.456  72.699  1.00116.77           C  
ANISOU 1321  CB  GLN A 228    18712  13700  11952   -270   1048    630       C  
ATOM   1322  CG  GLN A 228     -26.561  -4.977  73.608  1.00121.38           C  
ANISOU 1322  CG  GLN A 228    19482  14147  12488    -98   1153    659       C  
ATOM   1323  CD  GLN A 228     -26.000  -4.092  74.723  1.00132.57           C  
ANISOU 1323  CD  GLN A 228    21190  15408  13772   -348   1269    561       C  
ATOM   1324  OE1 GLN A 228     -26.405  -4.181  75.893  1.00136.67           O  
ANISOU 1324  OE1 GLN A 228    21732  15923  14273   -343   1272    536       O  
ATOM   1325  NE2 GLN A 228     -25.034  -3.239  74.371  1.00138.31           N  
ANISOU 1325  NE2 GLN A 228    22142  16016  14392   -594   1367    499       N  
ATOM   1326  N   ASP A 229     -23.486  -7.512  71.281  1.00106.26           N  
ANISOU 1326  N   ASP A 229    16748  12834  10793   -501    719    593       N  
ATOM   1327  CA  ASP A 229     -22.337  -7.747  70.424  1.00106.03           C  
ANISOU 1327  CA  ASP A 229    16591  12929  10764   -655    659    567       C  
ATOM   1328  C   ASP A 229     -22.685  -8.712  69.273  1.00101.91           C  
ANISOU 1328  C   ASP A 229    15829  12524  10366   -456    559    632       C  
ATOM   1329  O   ASP A 229     -22.325  -8.464  68.124  1.00102.14           O  
ANISOU 1329  O   ASP A 229    15866  12551  10390   -462    579    648       O  
ATOM   1330  CB  ASP A 229     -21.180  -8.295  71.266  1.00110.92           C  
ANISOU 1330  CB  ASP A 229    17046  13745  11351   -897    562    496       C  
ATOM   1331  CG  ASP A 229     -20.055  -8.899  70.419  1.00115.96           C  
ANISOU 1331  CG  ASP A 229    17463  14589  12006   -995    467    488       C  
ATOM   1332  OD1 ASP A 229     -19.193  -8.129  69.906  1.00119.58           O  
ANISOU 1332  OD1 ASP A 229    18029  15041  12364  -1194    529    451       O  
ATOM   1333  OD2 ASP A 229     -20.031 -10.164  70.284  1.00119.77           O  
ANISOU 1333  OD2 ASP A 229    17671  15241  12593   -873    337    519       O  
ATOM   1334  N   MET A 230     -23.358  -9.812  69.578  1.00 96.71           N  
ANISOU 1334  N   MET A 230    14967  11969   9807   -300    458    664       N  
ATOM   1335  CA  MET A 230     -23.840 -10.716  68.548  1.00 94.83           C  
ANISOU 1335  CA  MET A 230    14536  11827   9667   -125    381    718       C  
ATOM   1336  C   MET A 230     -24.949 -10.071  67.672  1.00 95.68           C  
ANISOU 1336  C   MET A 230    14764  11827   9762     79    475    794       C  
ATOM   1337  O   MET A 230     -25.068 -10.337  66.456  1.00 95.28           O  
ANISOU 1337  O   MET A 230    14620  11834   9746    166    453    833       O  
ATOM   1338  CB  MET A 230     -24.331 -11.997  69.206  1.00 96.24           C  
ANISOU 1338  CB  MET A 230    14514  12124   9928    -41    270    728       C  
ATOM   1339  CG  MET A 230     -24.856 -13.064  68.258  1.00 98.92           C  
ANISOU 1339  CG  MET A 230    14665  12566  10353    103    194    770       C  
ATOM   1340  SD  MET A 230     -23.624 -13.634  67.069  1.00100.35           S  
ANISOU 1340  SD  MET A 230    14701  12861  10565     21    130    748       S  
ATOM   1341  CE  MET A 230     -22.522 -14.532  68.156  1.00100.79           C  
ANISOU 1341  CE  MET A 230    14622  13046  10628   -106     38    701       C  
ATOM   1342  N   HIS A 231     -25.746  -9.200  68.277  1.00 99.98           N  
ANISOU 1342  N   HIS A 231    15519  12227  10242    165    586    820       N  
ATOM   1343  CA  HIS A 231     -26.742  -8.443  67.532  1.00102.96           C  
ANISOU 1343  CA  HIS A 231    16034  12511  10574    382    699    906       C  
ATOM   1344  C   HIS A 231     -26.107  -7.385  66.617  1.00103.81           C  
ANISOU 1344  C   HIS A 231    16345  12488  10609    315    809    910       C  
ATOM   1345  O   HIS A 231     -26.574  -7.209  65.471  1.00112.54           O  
ANISOU 1345  O   HIS A 231    17440  13608  11712    475    843    985       O  
ATOM   1346  CB  HIS A 231     -27.751  -7.799  68.478  1.00108.16           C  
ANISOU 1346  CB  HIS A 231    16874  13054  11166    521    803    941       C  
ATOM   1347  CG  HIS A 231     -28.580  -8.789  69.251  1.00112.23           C  
ANISOU 1347  CG  HIS A 231    17192  13709  11741    615    706    955       C  
ATOM   1348  ND1 HIS A 231     -28.807  -8.674  70.609  1.00112.02           N  
ANISOU 1348  ND1 HIS A 231    17245  13630  11688    582    726    923       N  
ATOM   1349  CD2 HIS A 231     -29.253  -9.899  68.849  1.00115.29           C  
ANISOU 1349  CD2 HIS A 231    17319  14286  12199    726    597    995       C  
ATOM   1350  CE1 HIS A 231     -29.590  -9.663  71.007  1.00113.67           C  
ANISOU 1350  CE1 HIS A 231    17246  13990  11952    677    630    948       C  
ATOM   1351  NE2 HIS A 231     -29.874 -10.422  69.961  1.00115.62           N  
ANISOU 1351  NE2 HIS A 231    17292  14383  12253    755    554    989       N  
ATOM   1352  N   SER A 232     -25.055  -6.702  67.074  1.00100.52           N  
ANISOU 1352  N   SER A 232    16106  11964  10122     70    865    832       N  
ATOM   1353  CA  SER A 232     -24.286  -5.795  66.204  1.00103.10           C  
ANISOU 1353  CA  SER A 232    16616  12183  10372    -51    959    822       C  
ATOM   1354  C   SER A 232     -23.750  -6.556  65.009  1.00101.76           C  
ANISOU 1354  C   SER A 232    16195  12189  10279    -66    845    831       C  
ATOM   1355  O   SER A 232     -23.852  -6.104  63.859  1.00107.48           O  
ANISOU 1355  O   SER A 232    16984  12870  10982     16    905    885       O  
ATOM   1356  CB  SER A 232     -23.074  -5.156  66.887  1.00105.29           C  
ANISOU 1356  CB  SER A 232    17066  12389  10550   -386   1008    719       C  
ATOM   1357  OG  SER A 232     -23.419  -4.371  68.007  1.00110.15           O  
ANISOU 1357  OG  SER A 232    17953  12823  11074   -423   1129    691       O  
ATOM   1358  N   TYR A 233     -23.165  -7.710  65.279  1.00 97.15           N  
ANISOU 1358  N   TYR A 233    15334  11801   9776   -163    690    782       N  
ATOM   1359  CA  TYR A 233     -22.636  -8.570  64.228  1.00 93.15           C  
ANISOU 1359  CA  TYR A 233    14584  11467   9341   -167    582    785       C  
ATOM   1360  C   TYR A 233     -23.746  -9.001  63.277  1.00 89.30           C  
ANISOU 1360  C   TYR A 233    13991  11021   8915     89    565    870       C  
ATOM   1361  O   TYR A 233     -23.550  -8.956  62.075  1.00 89.48           O  
ANISOU 1361  O   TYR A 233    13972  11083   8943    117    567    896       O  
ATOM   1362  CB  TYR A 233     -21.953  -9.776  64.867  1.00 94.12           C  
ANISOU 1362  CB  TYR A 233    14458  11776   9526   -267    438    731       C  
ATOM   1363  CG  TYR A 233     -21.153 -10.650  63.946  1.00 95.38           C  
ANISOU 1363  CG  TYR A 233    14392  12110   9738   -298    339    721       C  
ATOM   1364  CD1 TYR A 233     -19.816 -10.354  63.676  1.00 98.47           C  
ANISOU 1364  CD1 TYR A 233    14772  12580  10063   -507    337    674       C  
ATOM   1365  CD2 TYR A 233     -21.706 -11.801  63.364  1.00 95.53           C  
ANISOU 1365  CD2 TYR A 233    14212  12229   9855   -133    253    754       C  
ATOM   1366  CE1 TYR A 233     -19.047 -11.150  62.827  1.00 97.89           C  
ANISOU 1366  CE1 TYR A 233    14489  12679  10025   -517    253    670       C  
ATOM   1367  CE2 TYR A 233     -20.954 -12.595  62.508  1.00 96.68           C  
ANISOU 1367  CE2 TYR A 233    14178  12516  10037   -154    179    742       C  
ATOM   1368  CZ  TYR A 233     -19.621 -12.271  62.252  1.00 98.43           C  
ANISOU 1368  CZ  TYR A 233    14385  12815  10198   -330    178    703       C  
ATOM   1369  OH  TYR A 233     -18.854 -13.067  61.424  1.00101.21           O  
ANISOU 1369  OH  TYR A 233    14556  13321  10577   -331    109    695       O  
ATOM   1370  N   ILE A 234     -24.894  -9.431  63.796  1.00 89.05           N  
ANISOU 1370  N   ILE A 234    13905  11011   8919    262    547    910       N  
ATOM   1371  CA  ILE A 234     -25.990  -9.868  62.910  1.00 91.32           C  
ANISOU 1371  CA  ILE A 234    14068  11390   9236    482    529    990       C  
ATOM   1372  C   ILE A 234     -26.514  -8.739  62.080  1.00 90.62           C  
ANISOU 1372  C   ILE A 234    14162  11201   9066    624    663   1072       C  
ATOM   1373  O   ILE A 234     -26.815  -8.939  60.878  1.00 91.49           O  
ANISOU 1373  O   ILE A 234    14167  11410   9184    727    650   1126       O  
ATOM   1374  CB  ILE A 234     -27.121 -10.579  63.695  1.00 96.71           C  
ANISOU 1374  CB  ILE A 234    14643  12151   9949    611    483   1016       C  
ATOM   1375  CG1 ILE A 234     -26.681 -12.027  64.048  1.00 98.39           C  
ANISOU 1375  CG1 ILE A 234    14627  12501  10254    508    336    954       C  
ATOM   1376  CG2 ILE A 234     -28.451 -10.645  62.916  1.00 97.01           C  
ANISOU 1376  CG2 ILE A 234    14606  12292   9959    841    507   1114       C  
ATOM   1377  CD1 ILE A 234     -27.310 -12.592  65.308  1.00100.49           C  
ANISOU 1377  CD1 ILE A 234    14848  12791  10539    533    296    944       C  
ATOM   1378  N   ALA A 235     -26.584  -7.554  62.686  1.00 93.08           N  
ANISOU 1378  N   ALA A 235    14760  11315   9289    628    801   1083       N  
ATOM   1379  CA  ALA A 235     -27.026  -6.341  61.939  1.00 96.24           C  
ANISOU 1379  CA  ALA A 235    15399  11577   9589    782    962   1172       C  
ATOM   1380  C   ALA A 235     -26.146  -6.000  60.744  1.00 97.50           C  
ANISOU 1380  C   ALA A 235    15591  11719   9734    677    980   1167       C  
ATOM   1381  O   ALA A 235     -26.647  -5.853  59.618  1.00 97.41           O  
ANISOU 1381  O   ALA A 235    15543  11763   9702    846   1012   1254       O  
ATOM   1382  CB  ALA A 235     -27.090  -5.142  62.841  1.00 97.37           C  
ANISOU 1382  CB  ALA A 235    15894  11473   9628    773   1125   1169       C  
ATOM   1383  N   ALA A 236     -24.838  -5.927  60.987  1.00 99.82           N  
ANISOU 1383  N   ALA A 236    15926  11971  10028    395    953   1066       N  
ATOM   1384  CA  ALA A 236     -23.837  -5.692  59.912  1.00101.40           C  
ANISOU 1384  CA  ALA A 236    16128  12186  10211    250    954   1046       C  
ATOM   1385  C   ALA A 236     -23.953  -6.647  58.732  1.00102.02           C  
ANISOU 1385  C   ALA A 236    15915  12474  10373    344    839   1078       C  
ATOM   1386  O   ALA A 236     -24.186  -6.204  57.613  1.00105.20           O  
ANISOU 1386  O   ALA A 236    16363  12867  10740    450    898   1148       O  
ATOM   1387  CB  ALA A 236     -22.419  -5.749  60.449  1.00100.27           C  
ANISOU 1387  CB  ALA A 236    15982  12063  10052    -76    907    931       C  
ATOM   1388  N   PHE A 237     -23.841  -7.944  58.982  1.00102.98           N  
ANISOU 1388  N   PHE A 237    15757  12776  10594    313    687   1031       N  
ATOM   1389  CA  PHE A 237     -23.966  -8.944  57.907  1.00105.47           C  
ANISOU 1389  CA  PHE A 237    15812  13280  10979    386    585   1049       C  
ATOM   1390  C   PHE A 237     -25.365  -9.006  57.277  1.00104.97           C  
ANISOU 1390  C   PHE A 237    15695  13283  10904    641    612   1150       C  
ATOM   1391  O   PHE A 237     -25.472  -8.990  56.033  1.00108.66           O  
ANISOU 1391  O   PHE A 237    16097  13830  11359    709    618   1197       O  
ATOM   1392  CB  PHE A 237     -23.502 -10.323  58.366  1.00105.96           C  
ANISOU 1392  CB  PHE A 237    15635  13490  11133    297    439    975       C  
ATOM   1393  CG  PHE A 237     -22.020 -10.461  58.360  1.00111.24           C  
ANISOU 1393  CG  PHE A 237    16261  14202  11801     82    394    899       C  
ATOM   1394  CD1 PHE A 237     -21.251  -9.944  59.425  1.00116.53           C  
ANISOU 1394  CD1 PHE A 237    17051  14805  12420    -96    421    844       C  
ATOM   1395  CD2 PHE A 237     -21.367 -11.037  57.285  1.00112.82           C  
ANISOU 1395  CD2 PHE A 237    16305  14530  12030     49    334    885       C  
ATOM   1396  CE1 PHE A 237     -19.857 -10.032  59.427  1.00116.66           C  
ANISOU 1396  CE1 PHE A 237    17003  14915  12404   -305    382    781       C  
ATOM   1397  CE2 PHE A 237     -19.975 -11.129  57.280  1.00116.01           C  
ANISOU 1397  CE2 PHE A 237    16655  15010  12413   -137    298    824       C  
ATOM   1398  CZ  PHE A 237     -19.222 -10.617  58.348  1.00116.35           C  
ANISOU 1398  CZ  PHE A 237    16795  15018  12393   -315    320    776       C  
ATOM   1399  N   GLY A 238     -26.423  -9.047  58.095  1.00102.27           N  
ANISOU 1399  N   GLY A 238    15371  12936  10550    779    631   1189       N  
ATOM   1400  CA  GLY A 238     -27.789  -9.023  57.540  1.00101.56           C  
ANISOU 1400  CA  GLY A 238    15217  12957  10414   1025    666   1298       C  
ATOM   1401  C   GLY A 238     -28.097  -7.869  56.583  1.00103.43           C  
ANISOU 1401  C   GLY A 238    15618  13129  10550   1179    801   1404       C  
ATOM   1402  O   GLY A 238     -28.700  -8.076  55.487  1.00105.58           O  
ANISOU 1402  O   GLY A 238    15751  13570  10793   1314    792   1479       O  
ATOM   1403  N   ALA A 239     -27.701  -6.655  56.979  1.00100.62           N  
ANISOU 1403  N   ALA A 239    15569  12533  10127   1156    936   1412       N  
ATOM   1404  CA  ALA A 239     -28.004  -5.464  56.180  1.00101.32           C  
ANISOU 1404  CA  ALA A 239    15877  12514  10104   1322   1094   1522       C  
ATOM   1405  C   ALA A 239     -27.203  -5.402  54.857  1.00 99.95           C  
ANISOU 1405  C   ALA A 239    15662  12377   9937   1225   1078   1517       C  
ATOM   1406  O   ALA A 239     -27.756  -5.167  53.772  1.00101.95           O  
ANISOU 1406  O   ALA A 239    15874  12725  10136   1405   1121   1622       O  
ATOM   1407  CB  ALA A 239     -27.768  -4.217  57.006  1.00102.42           C  
ANISOU 1407  CB  ALA A 239    16401  12356  10157   1298   1259   1520       C  
ATOM   1408  N   VAL A 240     -25.905  -5.596  54.964  1.00 95.47           N  
ANISOU 1408  N   VAL A 240    15094  11756   9423    946   1018   1402       N  
ATOM   1409  CA  VAL A 240     -25.051  -5.625  53.810  1.00 94.35           C  
ANISOU 1409  CA  VAL A 240    14891  11666   9289    829    990   1383       C  
ATOM   1410  C   VAL A 240     -25.541  -6.698  52.834  1.00 96.50           C  
ANISOU 1410  C   VAL A 240    14840  12203   9620    931    872   1411       C  
ATOM   1411  O   VAL A 240     -25.703  -6.431  51.638  1.00100.56           O  
ANISOU 1411  O   VAL A 240    15331  12784  10092   1024    907   1483       O  
ATOM   1412  CB  VAL A 240     -23.598  -5.860  54.250  1.00 92.55           C  
ANISOU 1412  CB  VAL A 240    14654  11407   9101    512    923   1250       C  
ATOM   1413  CG1 VAL A 240     -22.709  -6.271  53.099  1.00 93.28           C  
ANISOU 1413  CG1 VAL A 240    14587  11631   9222    392    850   1218       C  
ATOM   1414  CG2 VAL A 240     -23.041  -4.612  54.903  1.00 92.81           C  
ANISOU 1414  CG2 VAL A 240    15039  11188   9034    368   1065   1225       C  
ATOM   1415  N   THR A 241     -25.783  -7.905  53.326  1.00 99.70           N  
ANISOU 1415  N   THR A 241    15012  12757  10111    905    742   1354       N  
ATOM   1416  CA  THR A 241     -26.323  -8.959  52.457  1.00104.22           C  
ANISOU 1416  CA  THR A 241    15307  13572  10720    977    644   1370       C  
ATOM   1417  C   THR A 241     -27.703  -8.587  51.892  1.00106.22           C  
ANISOU 1417  C   THR A 241    15537  13938  10880   1238    714   1507       C  
ATOM   1418  O   THR A 241     -28.037  -8.931  50.749  1.00105.73           O  
ANISOU 1418  O   THR A 241    15316  14062  10795   1300    686   1550       O  
ATOM   1419  CB  THR A 241     -26.433 -10.303  53.204  1.00105.42           C  
ANISOU 1419  CB  THR A 241    15261  13832  10960    902    515   1288       C  
ATOM   1420  OG1 THR A 241     -25.183 -10.592  53.849  1.00107.47           O  
ANISOU 1420  OG1 THR A 241    15542  14007  11284    696    461   1181       O  
ATOM   1421  CG2 THR A 241     -26.808 -11.475  52.248  1.00104.48           C  
ANISOU 1421  CG2 THR A 241    14885  13943  10867    914    421   1278       C  
ATOM   1422  N   GLY A 242     -28.505  -7.903  52.696  1.00109.55           N  
ANISOU 1422  N   GLY A 242    16110  14274  11238   1395    806   1577       N  
ATOM   1423  CA  GLY A 242     -29.793  -7.402  52.222  1.00115.84           C  
ANISOU 1423  CA  GLY A 242    16901  15195  11918   1679    894   1729       C  
ATOM   1424  C   GLY A 242     -29.716  -6.392  51.079  1.00119.03           C  
ANISOU 1424  C   GLY A 242    17441  15556  12228   1803   1012   1835       C  
ATOM   1425  O   GLY A 242     -30.510  -6.458  50.124  1.00121.16           O  
ANISOU 1425  O   GLY A 242    17563  16050  12419   1978   1022   1941       O  
ATOM   1426  N   LEU A 243     -28.749  -5.484  51.177  1.00116.83           N  
ANISOU 1426  N   LEU A 243    17439  15005  11944   1697   1101   1805       N  
ATOM   1427  CA  LEU A 243     -28.484  -4.509  50.137  1.00120.70           C  
ANISOU 1427  CA  LEU A 243    18101  15408  12349   1770   1220   1890       C  
ATOM   1428  C   LEU A 243     -27.840  -5.143  48.894  1.00118.92           C  
ANISOU 1428  C   LEU A 243    17661  15348  12175   1636   1116   1848       C  
ATOM   1429  O   LEU A 243     -28.209  -4.844  47.762  1.00116.57           O  
ANISOU 1429  O   LEU A 243    17322  15166  11803   1781   1162   1952       O  
ATOM   1430  CB  LEU A 243     -27.552  -3.411  50.669  1.00123.95           C  
ANISOU 1430  CB  LEU A 243    18890  15473  12729   1631   1347   1848       C  
ATOM   1431  CG  LEU A 243     -28.099  -2.471  51.744  1.00127.52           C  
ANISOU 1431  CG  LEU A 243    19658  15696  13096   1773   1503   1900       C  
ATOM   1432  CD1 LEU A 243     -26.931  -1.907  52.549  1.00130.23           C  
ANISOU 1432  CD1 LEU A 243    20282  15750  13447   1483   1556   1778       C  
ATOM   1433  CD2 LEU A 243     -28.982  -1.342  51.183  1.00127.98           C  
ANISOU 1433  CD2 LEU A 243    19947  15680  12997   2114   1702   2088       C  
ATOM   1434  N   CYS A 244     -26.836  -5.982  49.111  1.00118.86           N  
ANISOU 1434  N   CYS A 244    17526  15350  12283   1366    986   1700       N  
ATOM   1435  CA  CYS A 244     -26.177  -6.663  48.001  1.00120.63           C  
ANISOU 1435  CA  CYS A 244    17549  15728  12556   1239    889   1649       C  
ATOM   1436  C   CYS A 244     -27.123  -7.531  47.185  1.00121.75           C  
ANISOU 1436  C   CYS A 244    17403  16168  12687   1367    814   1698       C  
ATOM   1437  O   CYS A 244     -27.124  -7.449  45.960  1.00125.95           O  
ANISOU 1437  O   CYS A 244    17857  16821  13174   1410    822   1750       O  
ATOM   1438  CB  CYS A 244     -25.046  -7.538  48.514  1.00122.70           C  
ANISOU 1438  CB  CYS A 244    17707  15979  12931    973    766   1492       C  
ATOM   1439  SG  CYS A 244     -23.563  -6.630  48.983  1.00125.27           S  
ANISOU 1439  SG  CYS A 244    18294  16059  13243    729    830   1416       S  
ATOM   1440  N   THR A 245     -27.909  -8.366  47.865  1.00123.34           N  
ANISOU 1440  N   THR A 245    17450  16497  12915   1407    742   1678       N  
ATOM   1441  CA  THR A 245     -28.866  -9.245  47.181  1.00124.84           C  
ANISOU 1441  CA  THR A 245    17369  16993  13071   1486    674   1713       C  
ATOM   1442  C   THR A 245     -29.971  -8.482  46.486  1.00125.76           C  
ANISOU 1442  C   THR A 245    17484  17258  13038   1752    775   1885       C  
ATOM   1443  O   THR A 245     -30.354  -8.856  45.397  1.00125.03           O  
ANISOU 1443  O   THR A 245    17204  17411  12890   1786    744   1926       O  
ATOM   1444  CB  THR A 245     -29.543 -10.264  48.121  1.00128.36           C  
ANISOU 1444  CB  THR A 245    17669  17546  13553   1456    588   1658       C  
ATOM   1445  OG1 THR A 245     -30.151  -9.596  49.250  1.00128.11           O  
ANISOU 1445  OG1 THR A 245    17789  17401  13484   1592    664   1717       O  
ATOM   1446  CG2 THR A 245     -28.537 -11.294  48.597  1.00130.08           C  
ANISOU 1446  CG2 THR A 245    17832  17687  13906   1215    477   1499       C  
ATOM   1447  N   LEU A 246     -30.476  -7.419  47.108  1.00126.98           N  
ANISOU 1447  N   LEU A 246    17853  17276  13115   1948    902   1990       N  
ATOM   1448  CA  LEU A 246     -31.534  -6.593  46.501  1.00127.31           C  
ANISOU 1448  CA  LEU A 246    17919  17459  12993   2257   1023   2180       C  
ATOM   1449  C   LEU A 246     -31.050  -5.895  45.216  1.00126.03           C  
ANISOU 1449  C   LEU A 246    17837  17272  12776   2299   1094   2251       C  
ATOM   1450  O   LEU A 246     -31.729  -5.905  44.209  1.00121.63           O  
ANISOU 1450  O   LEU A 246    17118  16981  12112   2451   1107   2362       O  
ATOM   1451  CB  LEU A 246     -32.007  -5.556  47.515  1.00127.72           C  
ANISOU 1451  CB  LEU A 246    18244  17307  12976   2462   1167   2268       C  
ATOM   1452  CG  LEU A 246     -33.081  -4.570  47.077  1.00130.05           C  
ANISOU 1452  CG  LEU A 246    18621  17707  13083   2837   1325   2484       C  
ATOM   1453  CD1 LEU A 246     -34.402  -5.298  46.870  1.00128.50           C  
ANISOU 1453  CD1 LEU A 246    18084  17948  12789   2989   1259   2567       C  
ATOM   1454  CD2 LEU A 246     -33.147  -3.446  48.109  1.00132.44           C  
ANISOU 1454  CD2 LEU A 246    19296  17684  13338   2988   1490   2537       C  
ATOM   1455  N   PHE A 247     -29.861  -5.295  45.284  1.00124.57           N  
ANISOU 1455  N   PHE A 247    17897  16781  12653   2148   1140   2185       N  
ATOM   1456  CA  PHE A 247     -29.190  -4.673  44.136  1.00120.59           C  
ANISOU 1456  CA  PHE A 247    17490  16217  12111   2127   1200   2225       C  
ATOM   1457  C   PHE A 247     -29.054  -5.680  43.000  1.00117.75           C  
ANISOU 1457  C   PHE A 247    16808  16144  11785   2016   1067   2178       C  
ATOM   1458  O   PHE A 247     -29.333  -5.374  41.854  1.00123.77           O  
ANISOU 1458  O   PHE A 247    17511  17058  12455   2137   1109   2283       O  
ATOM   1459  CB  PHE A 247     -27.798  -4.175  44.582  1.00121.21           C  
ANISOU 1459  CB  PHE A 247    17830  15958  12263   1880   1230   2111       C  
ATOM   1460  CG  PHE A 247     -26.950  -3.683  43.481  1.00124.40           C  
ANISOU 1460  CG  PHE A 247    18316  16307  12643   1790   1269   2122       C  
ATOM   1461  CD1 PHE A 247     -27.006  -2.369  43.101  1.00128.85           C  
ANISOU 1461  CD1 PHE A 247    19185  16687  13084   1939   1451   2249       C  
ATOM   1462  CD2 PHE A 247     -26.085  -4.541  42.801  1.00127.60           C  
ANISOU 1462  CD2 PHE A 247    18504  16839  13136   1562   1134   2007       C  
ATOM   1463  CE1 PHE A 247     -26.216  -1.909  42.053  1.00134.49           C  
ANISOU 1463  CE1 PHE A 247    19980  17352  13767   1843   1490   2261       C  
ATOM   1464  CE2 PHE A 247     -25.314  -4.095  41.734  1.00130.08           C  
ANISOU 1464  CE2 PHE A 247    18876  17126  13419   1479   1168   2020       C  
ATOM   1465  CZ  PHE A 247     -25.368  -2.777  41.368  1.00131.40           C  
ANISOU 1465  CZ  PHE A 247    19342  17114  13468   1607   1342   2144       C  
ATOM   1466  N   THR A 248     -28.604  -6.879  43.336  1.00113.49           N  
ANISOU 1466  N   THR A 248    16081  15669  11369   1787    917   2021       N  
ATOM   1467  CA  THR A 248     -28.400  -7.948  42.385  1.00111.93           C  
ANISOU 1467  CA  THR A 248    15611  15707  11209   1653    796   1949       C  
ATOM   1468  C   THR A 248     -29.730  -8.492  41.853  1.00112.49           C  
ANISOU 1468  C   THR A 248    15428  16135  11176   1800    768   2034       C  
ATOM   1469  O   THR A 248     -29.803  -8.914  40.721  1.00112.08           O  
ANISOU 1469  O   THR A 248    15197  16304  11082   1769    727   2041       O  
ATOM   1470  CB  THR A 248     -27.514  -9.037  43.037  1.00114.15           C  
ANISOU 1470  CB  THR A 248    15816  15916  11640   1391    669   1763       C  
ATOM   1471  OG1 THR A 248     -26.262  -8.456  43.437  1.00115.70           O  
ANISOU 1471  OG1 THR A 248    16220  15841  11897   1251    700   1699       O  
ATOM   1472  CG2 THR A 248     -27.234 -10.219  42.101  1.00114.41           C  
ANISOU 1472  CG2 THR A 248    15603  16157  11709   1250    558   1675       C  
ATOM   1473  N   LEU A 249     -30.779  -8.492  42.659  1.00115.23           N  
ANISOU 1473  N   LEU A 249    15751  16564  11466   1945    789   2096       N  
ATOM   1474  CA  LEU A 249     -32.104  -8.909  42.200  1.00121.64           C  
ANISOU 1474  CA  LEU A 249    16314  17760  12141   2083    773   2191       C  
ATOM   1475  C   LEU A 249     -32.725  -7.870  41.287  1.00122.29           C  
ANISOU 1475  C   LEU A 249    16423  17986  12055   2361    894   2390       C  
ATOM   1476  O   LEU A 249     -33.422  -8.234  40.327  1.00122.40           O  
ANISOU 1476  O   LEU A 249    16193  18362  11950   2414    868   2458       O  
ATOM   1477  CB  LEU A 249     -33.044  -9.112  43.383  1.00126.16           C  
ANISOU 1477  CB  LEU A 249    16859  18391  12683   2172    771   2212       C  
ATOM   1478  CG  LEU A 249     -32.841 -10.370  44.218  1.00126.11           C  
ANISOU 1478  CG  LEU A 249    16752  18363  12798   1928    644   2041       C  
ATOM   1479  CD1 LEU A 249     -33.477 -10.175  45.579  1.00126.31           C  
ANISOU 1479  CD1 LEU A 249    16858  18316  12816   2031    674   2068       C  
ATOM   1480  CD2 LEU A 249     -33.431 -11.588  43.508  1.00128.96           C  
ANISOU 1480  CD2 LEU A 249    16815  19083  13101   1797    546   1993       C  
ATOM   1481  N   ALA A 250     -32.454  -6.597  41.604  1.00120.55           N  
ANISOU 1481  N   ALA A 250    16509  17480  11814   2528   1033   2482       N  
ATOM   1482  CA  ALA A 250     -32.928  -5.433  40.859  1.00122.62           C  
ANISOU 1482  CA  ALA A 250    16884  17790  11913   2828   1185   2687       C  
ATOM   1483  C   ALA A 250     -32.370  -5.372  39.437  1.00126.14           C  
ANISOU 1483  C   ALA A 250    17263  18323  12340   2763   1175   2701       C  
ATOM   1484  O   ALA A 250     -33.094  -4.989  38.517  1.00129.19           O  
ANISOU 1484  O   ALA A 250    17547  18972  12564   2985   1237   2866       O  
ATOM   1485  CB  ALA A 250     -32.584  -4.152  41.596  1.00121.73           C  
ANISOU 1485  CB  ALA A 250    17180  17275  11795   2965   1347   2748       C  
ATOM   1486  N   THR A 251     -31.097  -5.744  39.261  1.00124.97           N  
ANISOU 1486  N   THR A 251    17161  17979  12340   2470   1099   2538       N  
ATOM   1487  CA  THR A 251     -30.479  -5.813  37.938  1.00123.89           C  
ANISOU 1487  CA  THR A 251    16943  17930  12199   2373   1073   2528       C  
ATOM   1488  C   THR A 251     -31.095  -6.902  37.080  1.00123.34           C  
ANISOU 1488  C   THR A 251    16502  18283  12076   2316    960   2509       C  
ATOM   1489  O   THR A 251     -31.143  -6.752  35.877  1.00131.89           O  
ANISOU 1489  O   THR A 251    17485  19553  13072   2363    976   2581       O  
ATOM   1490  CB  THR A 251     -28.974  -6.117  38.001  1.00122.12           C  
ANISOU 1490  CB  THR A 251    16811  17449  12138   2062   1004   2346       C  
ATOM   1491  OG1 THR A 251     -28.751  -7.326  38.728  1.00123.17           O  
ANISOU 1491  OG1 THR A 251    16796  17605  12398   1850    867   2176       O  
ATOM   1492  CG2 THR A 251     -28.252  -4.985  38.631  1.00121.20           C  
ANISOU 1492  CG2 THR A 251    17062  16945  12043   2064   1123   2360       C  
ATOM   1493  N   PHE A 252     -31.534  -7.998  37.687  1.00120.62           N  
ANISOU 1493  N   PHE A 252    15970  18084  11776   2194    852   2406       N  
ATOM   1494  CA  PHE A 252     -32.162  -9.094  36.957  1.00121.05           C  
ANISOU 1494  CA  PHE A 252    15695  18535  11760   2096    753   2370       C  
ATOM   1495  C   PHE A 252     -33.531  -8.689  36.435  1.00120.30           C  
ANISOU 1495  C   PHE A 252    15438  18829  11441   2363    818   2569       C  
ATOM   1496  O   PHE A 252     -33.857  -8.917  35.267  1.00122.13           O  
ANISOU 1496  O   PHE A 252    15465  19382  11557   2361    800   2619       O  
ATOM   1497  CB  PHE A 252     -32.271 -10.346  37.842  1.00122.71           C  
ANISOU 1497  CB  PHE A 252    15796  18764  12063   1884    639   2206       C  
ATOM   1498  CG  PHE A 252     -31.048 -11.240  37.804  1.00124.16           C  
ANISOU 1498  CG  PHE A 252    15996  18762  12417   1590    544   2004       C  
ATOM   1499  CD1 PHE A 252     -30.860 -12.141  36.757  1.00125.16           C  
ANISOU 1499  CD1 PHE A 252    15939  19088  12525   1418    474   1920       C  
ATOM   1500  CD2 PHE A 252     -30.108 -11.218  38.815  1.00124.65           C  
ANISOU 1500  CD2 PHE A 252    16250  18473  12638   1491    529   1900       C  
ATOM   1501  CE1 PHE A 252     -29.755 -12.977  36.706  1.00123.01           C  
ANISOU 1501  CE1 PHE A 252    15689  18655  12394   1184    401   1745       C  
ATOM   1502  CE2 PHE A 252     -28.995 -12.051  38.780  1.00124.80           C  
ANISOU 1502  CE2 PHE A 252    16267  18360  12791   1256    449   1732       C  
ATOM   1503  CZ  PHE A 252     -28.819 -12.927  37.717  1.00124.82           C  
ANISOU 1503  CZ  PHE A 252    16098  18551  12775   1117    389   1659       C  
ATOM   1504  N   VAL A 253     -34.324  -8.046  37.273  1.00125.86           N  
ANISOU 1504  N   VAL A 253    16230  19523  12069   2606    901   2694       N  
ATOM   1505  CA  VAL A 253     -35.670  -7.585  36.862  1.00135.01           C  
ANISOU 1505  CA  VAL A 253    17228  21082  12988   2912    978   2911       C  
ATOM   1506  C   VAL A 253     -35.632  -6.405  35.882  1.00140.00           C  
ANISOU 1506  C   VAL A 253    17973  21721  13499   3178   1111   3103       C  
ATOM   1507  O   VAL A 253     -36.519  -6.281  35.024  1.00142.16           O  
ANISOU 1507  O   VAL A 253    18029  22417  13566   3362   1142   3262       O  
ATOM   1508  CB  VAL A 253     -36.616  -7.247  38.064  1.00137.26           C  
ANISOU 1508  CB  VAL A 253    17562  21388  13201   3133   1039   3004       C  
ATOM   1509  CG1 VAL A 253     -36.905  -8.496  38.895  1.00136.09           C  
ANISOU 1509  CG1 VAL A 253    17242  21341  13123   2883    906   2841       C  
ATOM   1510  CG2 VAL A 253     -36.075  -6.128  38.948  1.00135.46           C  
ANISOU 1510  CG2 VAL A 253    17734  20676  13058   3291   1164   3043       C  
ATOM   1511  N   ALA A 254     -34.607  -5.554  36.010  1.00141.66           N  
ANISOU 1511  N   ALA A 254    18522  21481  13820   3188   1192   3089       N  
ATOM   1512  CA  ALA A 254     -34.390  -4.438  35.081  1.00145.02           C  
ANISOU 1512  CA  ALA A 254    19111  21841  14147   3399   1326   3252       C  
ATOM   1513  C   ALA A 254     -34.111  -4.922  33.636  1.00145.26           C  
ANISOU 1513  C   ALA A 254    18909  22141  14143   3259   1252   3230       C  
ATOM   1514  O   ALA A 254     -34.651  -4.373  32.685  1.00153.18           O  
ANISOU 1514  O   ALA A 254    19835  23399  14967   3492   1330   3415       O  
ATOM   1515  CB  ALA A 254     -33.266  -3.534  35.588  1.00141.74           C  
ANISOU 1515  CB  ALA A 254    19121  20873  13857   3356   1422   3207       C  
ATOM   1516  N   ASP A 255     -33.303  -5.964  33.505  1.00140.13           N  
ANISOU 1516  N   ASP A 255    18146  21445  13651   2896   1106   3010       N  
ATOM   1517  CA  ASP A 255     -32.972  -6.588  32.241  1.00142.07           C  
ANISOU 1517  CA  ASP A 255    18174  21923  13880   2718   1024   2950       C  
ATOM   1518  C   ASP A 255     -33.573  -8.020  32.186  1.00146.26           C  
ANISOU 1518  C   ASP A 255    18364  22819  14388   2506    882   2827       C  
ATOM   1519  O   ASP A 255     -32.934  -8.945  31.687  1.00147.41           O  
ANISOU 1519  O   ASP A 255    18399  22987  14621   2220    779   2659       O  
ATOM   1520  CB  ASP A 255     -31.446  -6.608  32.164  1.00141.48           C  
ANISOU 1520  CB  ASP A 255    18291  21464  13998   2468    991   2788       C  
ATOM   1521  CG  ASP A 255     -30.911  -7.068  30.813  1.00144.95           C  
ANISOU 1521  CG  ASP A 255    18566  22078  14430   2303    928   2732       C  
ATOM   1522  OD1 ASP A 255     -31.203  -6.428  29.779  1.00141.69           O  
ANISOU 1522  OD1 ASP A 255    18115  21845  13875   2474   1001   2889       O  
ATOM   1523  OD2 ASP A 255     -30.162  -8.072  30.805  1.00144.96           O  
ANISOU 1523  OD2 ASP A 255    18487  22024  14566   2010    813   2531       O  
ATOM   1524  N   TRP A 256     -34.797  -8.190  32.710  1.00152.71           N  
ANISOU 1524  N   TRP A 256    19030  23918  15073   2645    888   2913       N  
ATOM   1525  CA  TRP A 256     -35.532  -9.489  32.768  1.00159.41           C  
ANISOU 1525  CA  TRP A 256    19572  25133  15860   2439    772   2810       C  
ATOM   1526  C   TRP A 256     -35.605 -10.341  31.483  1.00165.90           C  
ANISOU 1526  C   TRP A 256    20121  26322  16590   2227    694   2745       C  
ATOM   1527  O   TRP A 256     -35.532 -11.575  31.559  1.00167.12           O  
ANISOU 1527  O   TRP A 256    20151  26552  16793   1921    590   2560       O  
ATOM   1528  CB  TRP A 256     -36.959  -9.276  33.338  1.00160.80           C  
ANISOU 1528  CB  TRP A 256    19610  25642  15845   2678    817   2969       C  
ATOM   1529  CG  TRP A 256     -37.671 -10.559  33.740  1.00164.96           C  
ANISOU 1529  CG  TRP A 256    19886  26467  16321   2437    707   2847       C  
ATOM   1530  CD1 TRP A 256     -38.789 -11.087  33.178  1.00166.21           C  
ANISOU 1530  CD1 TRP A 256    19713  27195  16242   2408    677   2908       C  
ATOM   1531  CD2 TRP A 256     -37.279 -11.470  34.773  1.00169.19           C  
ANISOU 1531  CD2 TRP A 256    20498  26752  17034   2176    622   2642       C  
ATOM   1532  NE1 TRP A 256     -39.126 -12.271  33.793  1.00165.80           N  
ANISOU 1532  NE1 TRP A 256    19543  27246  16207   2123    582   2747       N  
ATOM   1533  CE2 TRP A 256     -38.216 -12.531  34.777  1.00167.26           C  
ANISOU 1533  CE2 TRP A 256    19980  26921  16649   1991    549   2585       C  
ATOM   1534  CE3 TRP A 256     -36.225 -11.493  35.698  1.00171.74           C  
ANISOU 1534  CE3 TRP A 256    21092  26555  17604   2075    604   2504       C  
ATOM   1535  CZ2 TRP A 256     -38.140 -13.596  35.674  1.00169.64           C  
ANISOU 1535  CZ2 TRP A 256    20297  27099  17057   1724    467   2401       C  
ATOM   1536  CZ3 TRP A 256     -36.144 -12.557  36.589  1.00170.87           C  
ANISOU 1536  CZ3 TRP A 256    20974  26347  17602   1830    517   2329       C  
ATOM   1537  CH2 TRP A 256     -37.103 -13.590  36.579  1.00171.20           C  
ANISOU 1537  CH2 TRP A 256    20766  26774  17507   1664    453   2281       C  
ATOM   1538  N   ARG A 257     -35.774  -9.700  30.326  1.00174.24           N  
ANISOU 1538  N   ARG A 257    21098  27603  17501   2389    754   2897       N  
ATOM   1539  CA  ARG A 257     -35.858 -10.427  29.042  1.00177.70           C  
ANISOU 1539  CA  ARG A 257    21277  28409  17832   2194    690   2846       C  
ATOM   1540  C   ARG A 257     -34.617 -11.255  28.754  1.00176.04           C  
ANISOU 1540  C   ARG A 257    21143  27923  17821   1855    605   2607       C  
ATOM   1541  O   ARG A 257     -34.722 -12.384  28.269  1.00179.98           O  
ANISOU 1541  O   ARG A 257    21457  28647  18281   1579    523   2466       O  
ATOM   1542  CB  ARG A 257     -36.088  -9.459  27.873  1.00184.68           C  
ANISOU 1542  CB  ARG A 257    22102  29524  18544   2450    779   3061       C  
ATOM   1543  CG  ARG A 257     -37.555  -9.192  27.575  1.00187.63           C  
ANISOU 1543  CG  ARG A 257    22206  30466  18617   2695    827   3279       C  
ATOM   1544  CD  ARG A 257     -38.057  -9.982  26.359  1.00186.50           C  
ANISOU 1544  CD  ARG A 257    21708  30874  18279   2501    759   3255       C  
ATOM   1545  NE  ARG A 257     -39.502 -10.248  26.364  1.00188.48           N  
ANISOU 1545  NE  ARG A 257    21634  31731  18246   2578    756   3376       N  
ATOM   1546  CZ  ARG A 257     -40.469  -9.360  26.103  1.00188.12           C  
ANISOU 1546  CZ  ARG A 257    21457  32066  17951   2963    853   3656       C  
ATOM   1547  NH1 ARG A 257     -40.195  -8.083  25.826  1.00190.11           N  
ANISOU 1547  NH1 ARG A 257    21909  32124  18199   3336    978   3857       N  
ATOM   1548  NH2 ARG A 257     -41.743  -9.751  26.131  1.00186.53           N  
ANISOU 1548  NH2 ARG A 257    20926  32463  17482   2981    834   3742       N  
ATOM   1549  N   ASN A 258     -33.454 -10.657  29.006  1.00174.79           N  
ANISOU 1549  N   ASN A 258    21261  27297  17851   1880    636   2571       N  
ATOM   1550  CA  ASN A 258     -32.168 -11.318  28.799  1.00174.08           C  
ANISOU 1550  CA  ASN A 258    21259  26932  17948   1603    567   2363       C  
ATOM   1551  C   ASN A 258     -31.695 -12.073  30.056  1.00168.42           C  
ANISOU 1551  C   ASN A 258    20662  25911  17416   1426    504   2182       C  
ATOM   1552  O   ASN A 258     -31.025 -13.110  29.957  1.00169.85           O  
ANISOU 1552  O   ASN A 258    20823  26009  17700   1167    428   1992       O  
ATOM   1553  CB  ASN A 258     -31.122 -10.289  28.341  1.00176.66           C  
ANISOU 1553  CB  ASN A 258    21797  26969  18354   1698    633   2421       C  
ATOM   1554  CG  ASN A 258     -29.867 -10.941  27.788  1.00179.43           C  
ANISOU 1554  CG  ASN A 258    22170  27162  18842   1434    565   2237       C  
ATOM   1555  OD1 ASN A 258     -29.866 -11.443  26.670  1.00188.39           O  
ANISOU 1555  OD1 ASN A 258    23131  28548  19900   1323    531   2203       O  
ATOM   1556  ND2 ASN A 258     -28.788 -10.927  28.563  1.00182.51           N  
ANISOU 1556  ND2 ASN A 258    22767  27156  19419   1338    550   2123       N  
ATOM   1557  N   SER A 259     -32.065 -11.568  31.229  1.00160.41           N  
ANISOU 1557  N   SER A 259    19775  24739  16433   1580    543   2247       N  
ATOM   1558  CA  SER A 259     -31.585 -12.115  32.479  1.00155.05           C  
ANISOU 1558  CA  SER A 259    19229  23756  15926   1446    495   2100       C  
ATOM   1559  C   SER A 259     -32.131 -13.535  32.708  1.00153.90           C  
ANISOU 1559  C   SER A 259    18904  23814  15755   1222    407   1961       C  
ATOM   1560  O   SER A 259     -31.369 -14.447  33.035  1.00152.97           O  
ANISOU 1560  O   SER A 259    18844  23500  15776   1003    344   1780       O  
ATOM   1561  CB  SER A 259     -31.967 -11.181  33.613  1.00154.57           C  
ANISOU 1561  CB  SER A 259    19338  23514  15874   1674    568   2216       C  
ATOM   1562  OG  SER A 259     -33.300 -11.438  34.020  1.00158.63           O  
ANISOU 1562  OG  SER A 259    19690  24332  16248   1766    567   2291       O  
ATOM   1563  N   ASN A 260     -33.440 -13.719  32.513  1.00153.14           N  
ANISOU 1563  N   ASN A 260    18598  24122  15463   1275    411   2050       N  
ATOM   1564  CA  ASN A 260     -34.128 -14.991  32.823  1.00148.54           C  
ANISOU 1564  CA  ASN A 260    17861  23756  14818   1051    343   1931       C  
ATOM   1565  C   ASN A 260     -33.739 -16.099  31.816  1.00143.79           C  
ANISOU 1565  C   ASN A 260    17158  23276  14198    759    289   1772       C  
ATOM   1566  O   ASN A 260     -34.546 -16.550  31.035  1.00153.96           O  
ANISOU 1566  O   ASN A 260    18232  24973  15293    661    279   1786       O  
ATOM   1567  CB  ASN A 260     -35.658 -14.740  32.888  1.00150.22           C  
ANISOU 1567  CB  ASN A 260    17866  24417  14794   1198    372   2091       C  
ATOM   1568  CG  ASN A 260     -36.459 -15.960  33.324  1.00150.11           C  
ANISOU 1568  CG  ASN A 260    17703  24640  14689    955    312   1979       C  
ATOM   1569  OD1 ASN A 260     -36.337 -16.426  34.444  1.00154.55           O  
ANISOU 1569  OD1 ASN A 260    18381  24969  15370    872    284   1882       O  
ATOM   1570  ND2 ASN A 260     -37.305 -16.459  32.443  1.00151.91           N  
ANISOU 1570  ND2 ASN A 260    17676  25352  14690    831    298   1996       N  
ATOM   1571  N   ARG A 261     -32.490 -16.531  31.858  1.00135.55           N  
ANISOU 1571  N   ARG A 261    16274  21886  13343    623    261   1621       N  
ATOM   1572  CA  ARG A 261     -31.965 -17.521  30.938  1.00134.91           C  
ANISOU 1572  CA  ARG A 261    16147  21853  13259    378    227   1469       C  
ATOM   1573  C   ARG A 261     -30.834 -18.286  31.623  1.00132.70           C  
ANISOU 1573  C   ARG A 261    16057  21175  13185    237    195   1290       C  
ATOM   1574  O   ARG A 261     -29.880 -17.673  32.103  1.00128.99           O  
ANISOU 1574  O   ARG A 261    15747  20386  12875    346    203   1302       O  
ATOM   1575  CB  ARG A 261     -31.415 -16.829  29.705  1.00141.17           C  
ANISOU 1575  CB  ARG A 261    16908  22702  14027    458    254   1539       C  
ATOM   1576  CG  ARG A 261     -32.371 -16.739  28.540  1.00151.81           C  
ANISOU 1576  CG  ARG A 261    18015  24528  15137    461    269   1637       C  
ATOM   1577  CD  ARG A 261     -31.631 -16.599  27.197  1.00162.29           C  
ANISOU 1577  CD  ARG A 261    19311  25895  16454    420    277   1623       C  
ATOM   1578  NE  ARG A 261     -31.417 -15.204  26.775  1.00171.07           N  
ANISOU 1578  NE  ARG A 261    20460  26978  17557    688    333   1809       N  
ATOM   1579  CZ  ARG A 261     -32.275 -14.462  26.053  1.00175.63           C  
ANISOU 1579  CZ  ARG A 261    20879  27910  17939    865    378   1999       C  
ATOM   1580  NH1 ARG A 261     -33.446 -14.948  25.627  1.00178.05           N  
ANISOU 1580  NH1 ARG A 261    20938  28688  18023    798    365   2034       N  
ATOM   1581  NH2 ARG A 261     -31.964 -13.203  25.753  1.00176.33           N  
ANISOU 1581  NH2 ARG A 261    21064  27897  18035   1113    445   2163       N  
ATOM   1582  N   TYR A 262     -30.935 -19.615  31.643  1.00131.64           N  
ANISOU 1582  N   TYR A 262    15914  21073  13029     -4    167   1130       N  
ATOM   1583  CA  TYR A 262     -29.978 -20.486  32.359  1.00129.83           C  
ANISOU 1583  CA  TYR A 262    15868  20493  12969   -119    148    968       C  
ATOM   1584  C   TYR A 262     -28.574 -20.369  31.774  1.00126.19           C  
ANISOU 1584  C   TYR A 262    15500  19815  12632   -104    150    914       C  
ATOM   1585  O   TYR A 262     -28.458 -20.181  30.581  1.00138.43           O  
ANISOU 1585  O   TYR A 262    16959  21531  14105   -122    162    933       O  
ATOM   1586  CB  TYR A 262     -30.472 -21.946  32.330  1.00135.06           C  
ANISOU 1586  CB  TYR A 262    16522  21254  13540   -384    143    816       C  
ATOM   1587  CG  TYR A 262     -31.631 -22.215  33.301  1.00143.38           C  
ANISOU 1587  CG  TYR A 262    17535  22430  14511   -426    134    839       C  
ATOM   1588  CD1 TYR A 262     -32.967 -21.950  32.952  1.00147.58           C  
ANISOU 1588  CD1 TYR A 262    17859  23384  14829   -437    139    940       C  
ATOM   1589  CD2 TYR A 262     -31.378 -22.693  34.602  1.00143.68           C  
ANISOU 1589  CD2 TYR A 262    17731  22183  14677   -441    123    771       C  
ATOM   1590  CE1 TYR A 262     -34.009 -22.168  33.869  1.00150.56           C  
ANISOU 1590  CE1 TYR A 262    18187  23897  15122   -471    131    967       C  
ATOM   1591  CE2 TYR A 262     -32.402 -22.903  35.517  1.00140.83           C  
ANISOU 1591  CE2 TYR A 262    17335  21927  14244   -476    114    795       C  
ATOM   1592  CZ  TYR A 262     -33.712 -22.644  35.159  1.00146.91           C  
ANISOU 1592  CZ  TYR A 262    17897  23117  14802   -496    118    890       C  
ATOM   1593  OH  TYR A 262     -34.716 -22.863  36.079  1.00149.33           O  
ANISOU 1593  OH  TYR A 262    18158  23552  15026   -535    110    914       O  
ATOM   1594  N   PRO A 263     -27.499 -20.451  32.553  1.00126.39           N  
ANISOU 1594  N   PRO A 263    15686  19506  12830    -70    140    853       N  
ATOM   1595  CA  PRO A 263     -27.492 -20.622  33.994  1.00130.20           C  
ANISOU 1595  CA  PRO A 263    16281  19774  13413    -39    126    833       C  
ATOM   1596  C   PRO A 263     -27.513 -19.318  34.823  1.00129.63           C  
ANISOU 1596  C   PRO A 263    16257  19591  13405    159    133    968       C  
ATOM   1597  O   PRO A 263     -27.671 -19.420  36.032  1.00126.77           O  
ANISOU 1597  O   PRO A 263    15972  19087  13105    183    122    960       O  
ATOM   1598  CB  PRO A 263     -26.172 -21.368  34.241  1.00127.95           C  
ANISOU 1598  CB  PRO A 263    16132  19219  13261    -96    118    703       C  
ATOM   1599  CG  PRO A 263     -25.265 -20.835  33.201  1.00127.42           C  
ANISOU 1599  CG  PRO A 263    16039  19163  13211    -56    127    721       C  
ATOM   1600  CD  PRO A 263     -26.134 -20.481  32.010  1.00128.12           C  
ANISOU 1600  CD  PRO A 263    15973  19559  13145    -74    142    791       C  
ATOM   1601  N   ALA A 264     -27.408 -18.137  34.198  1.00130.61           N  
ANISOU 1601  N   ALA A 264    16353  19772  13499    293    161   1091       N  
ATOM   1602  CA  ALA A 264     -27.454 -16.854  34.932  1.00129.25           C  
ANISOU 1602  CA  ALA A 264    16270  19472  13364    478    193   1220       C  
ATOM   1603  C   ALA A 264     -28.707 -16.663  35.823  1.00126.04           C  
ANISOU 1603  C   ALA A 264    15837  19161  12891    568    204   1301       C  
ATOM   1604  O   ALA A 264     -28.628 -16.050  36.870  1.00124.21           O  
ANISOU 1604  O   ALA A 264    15725  18740  12727    670    222   1346       O  
ATOM   1605  CB  ALA A 264     -27.293 -15.674  33.975  1.00132.33           C  
ANISOU 1605  CB  ALA A 264    16651  19930  13696    603    242   1347       C  
ATOM   1606  N   VAL A 265     -29.849 -17.204  35.417  1.00126.78           N  
ANISOU 1606  N   VAL A 265    15768  19563  12838    517    196   1315       N  
ATOM   1607  CA  VAL A 265     -31.100 -17.132  36.215  1.00126.77           C  
ANISOU 1607  CA  VAL A 265    15706  19715  12746    589    204   1390       C  
ATOM   1608  C   VAL A 265     -31.038 -17.901  37.535  1.00122.90           C  
ANISOU 1608  C   VAL A 265    15310  19029  12357    494    168   1285       C  
ATOM   1609  O   VAL A 265     -31.742 -17.554  38.476  1.00125.84           O  
ANISOU 1609  O   VAL A 265    15693  19411  12707    595    180   1354       O  
ATOM   1610  CB  VAL A 265     -32.341 -17.641  35.408  1.00128.08           C  
ANISOU 1610  CB  VAL A 265    15643  20325  12697    512    199   1421       C  
ATOM   1611  CG1 VAL A 265     -32.418 -19.171  35.318  1.00124.88           C  
ANISOU 1611  CG1 VAL A 265    15200  19981  12268    220    155   1244       C  
ATOM   1612  CG2 VAL A 265     -33.630 -17.087  35.993  1.00127.72           C  
ANISOU 1612  CG2 VAL A 265    15503  20507  12517    675    226   1567       C  
ATOM   1613  N   ILE A 266     -30.225 -18.957  37.597  1.00116.95           N  
ANISOU 1613  N   ILE A 266    14625  18109  11700    313    132   1125       N  
ATOM   1614  CA  ILE A 266     -30.043 -19.717  38.840  1.00111.93           C  
ANISOU 1614  CA  ILE A 266    14097  17267  11163    234    105   1029       C  
ATOM   1615  C   ILE A 266     -29.594 -18.756  39.955  1.00108.19           C  
ANISOU 1615  C   ILE A 266    13754  16542  10808    396    116   1095       C  
ATOM   1616  O   ILE A 266     -30.144 -18.804  41.076  1.00111.14           O  
ANISOU 1616  O   ILE A 266    14161  16872  11192    425    110   1110       O  
ATOM   1617  CB  ILE A 266     -29.035 -20.883  38.654  1.00108.99           C  
ANISOU 1617  CB  ILE A 266    13809  16724  10877     68     86    867       C  
ATOM   1618  CG1 ILE A 266     -29.660 -21.987  37.816  1.00108.94           C  
ANISOU 1618  CG1 ILE A 266    13718  16939  10735   -128     89    781       C  
ATOM   1619  CG2 ILE A 266     -28.594 -21.479  39.975  1.00106.45           C  
ANISOU 1619  CG2 ILE A 266    13625  16145  10674     40     67    791       C  
ATOM   1620  CD1 ILE A 266     -28.616 -22.830  37.131  1.00108.86           C  
ANISOU 1620  CD1 ILE A 266    13785  16799  10775   -240     96    653       C  
ATOM   1621  N   LEU A 267     -28.678 -17.843  39.627  1.00102.92           N  
ANISOU 1621  N   LEU A 267    13162  15735  10208    489    139   1138       N  
ATOM   1622  CA  LEU A 267     -28.185 -16.897  40.608  1.00102.54           C  
ANISOU 1622  CA  LEU A 267    13260  15449  10251    604    161   1189       C  
ATOM   1623  C   LEU A 267     -29.216 -15.859  41.046  1.00104.23           C  
ANISOU 1623  C   LEU A 267    13483  15736  10381    787    213   1336       C  
ATOM   1624  O   LEU A 267     -29.153 -15.326  42.171  1.00105.23           O  
ANISOU 1624  O   LEU A 267    13736  15681  10564    862    233   1363       O  
ATOM   1625  CB  LEU A 267     -26.904 -16.234  40.155  1.00102.33           C  
ANISOU 1625  CB  LEU A 267    13323  15260  10295    613    178   1186       C  
ATOM   1626  CG  LEU A 267     -25.785 -17.222  40.468  1.00104.90           C  
ANISOU 1626  CG  LEU A 267    13687  15438  10732    475    129   1044       C  
ATOM   1627  CD1 LEU A 267     -25.730 -18.326  39.424  1.00103.41           C  
ANISOU 1627  CD1 LEU A 267    13395  15391  10505    359    105    957       C  
ATOM   1628  CD2 LEU A 267     -24.469 -16.492  40.567  1.00109.36           C  
ANISOU 1628  CD2 LEU A 267    14356  15822  11371    479    142   1041       C  
ATOM   1629  N   PHE A 268     -30.197 -15.611  40.191  1.00105.99           N  
ANISOU 1629  N   PHE A 268    13570  16245  10456    865    240   1434       N  
ATOM   1630  CA  PHE A 268     -31.343 -14.794  40.585  1.00107.55           C  
ANISOU 1630  CA  PHE A 268    13745  16576  10541   1065    295   1584       C  
ATOM   1631  C   PHE A 268     -32.160 -15.436  41.719  1.00107.12           C  
ANISOU 1631  C   PHE A 268    13653  16573  10474   1028    264   1553       C  
ATOM   1632  O   PHE A 268     -32.392 -14.792  42.767  1.00107.30           O  
ANISOU 1632  O   PHE A 268    13785  16461  10520   1161    299   1612       O  
ATOM   1633  CB  PHE A 268     -32.207 -14.492  39.371  1.00107.69           C  
ANISOU 1633  CB  PHE A 268    13590  16947  10378   1160    328   1702       C  
ATOM   1634  CG  PHE A 268     -33.560 -14.000  39.718  1.00107.37           C  
ANISOU 1634  CG  PHE A 268    13461  17150  10183   1353    374   1851       C  
ATOM   1635  CD1 PHE A 268     -33.740 -12.658  40.057  1.00108.09           C  
ANISOU 1635  CD1 PHE A 268    13692  17134  10243   1625    470   2006       C  
ATOM   1636  CD2 PHE A 268     -34.655 -14.874  39.719  1.00106.53           C  
ANISOU 1636  CD2 PHE A 268    13145  17387   9944   1260    332   1836       C  
ATOM   1637  CE1 PHE A 268     -35.000 -12.200  40.384  1.00111.36           C  
ANISOU 1637  CE1 PHE A 268    14023  17789  10498   1840    524   2156       C  
ATOM   1638  CE2 PHE A 268     -35.923 -14.424  40.042  1.00107.76           C  
ANISOU 1638  CE2 PHE A 268    13190  17818   9933   1447    374   1983       C  
ATOM   1639  CZ  PHE A 268     -36.096 -13.091  40.374  1.00110.85           C  
ANISOU 1639  CZ  PHE A 268    13709  18109  10297   1756    470   2148       C  
ATOM   1640  N   TYR A 269     -32.549 -16.697  41.503  1.00107.51           N  
ANISOU 1640  N   TYR A 269    13568  16800  10480    836    205   1453       N  
ATOM   1641  CA  TYR A 269     -33.229 -17.535  42.530  1.00107.93           C  
ANISOU 1641  CA  TYR A 269    13591  16895  10520    739    169   1395       C  
ATOM   1642  C   TYR A 269     -32.406 -17.750  43.772  1.00102.23           C  
ANISOU 1642  C   TYR A 269    13047  15822   9974    699    146   1307       C  
ATOM   1643  O   TYR A 269     -32.916 -17.644  44.883  1.00101.64           O  
ANISOU 1643  O   TYR A 269    13008  15706   9904    754    148   1333       O  
ATOM   1644  CB  TYR A 269     -33.666 -18.879  41.952  1.00110.30           C  
ANISOU 1644  CB  TYR A 269    13759  17419  10731    498    126   1288       C  
ATOM   1645  CG  TYR A 269     -34.803 -18.689  40.997  1.00118.98           C  
ANISOU 1645  CG  TYR A 269    14643  18952  11611    528    146   1389       C  
ATOM   1646  CD1 TYR A 269     -36.083 -18.359  41.476  1.00127.47           C  
ANISOU 1646  CD1 TYR A 269    15594  20303  12535    638    165   1505       C  
ATOM   1647  CD2 TYR A 269     -34.624 -18.756  39.636  1.00119.57           C  
ANISOU 1647  CD2 TYR A 269    14623  19192  11613    471    151   1386       C  
ATOM   1648  CE1 TYR A 269     -37.159 -18.131  40.621  1.00128.86           C  
ANISOU 1648  CE1 TYR A 269    15543  20935  12480    690    186   1619       C  
ATOM   1649  CE2 TYR A 269     -35.693 -18.537  38.775  1.00126.51           C  
ANISOU 1649  CE2 TYR A 269    15285  20513  12270    508    171   1493       C  
ATOM   1650  CZ  TYR A 269     -36.959 -18.227  39.282  1.00129.61           C  
ANISOU 1650  CZ  TYR A 269    15543  21198  12503    621    188   1612       C  
ATOM   1651  OH  TYR A 269     -38.038 -17.986  38.469  1.00139.49           O  
ANISOU 1651  OH  TYR A 269    16552  22937  13509    677    209   1736       O  
ATOM   1652  N   VAL A 270     -31.129 -18.004  43.578  1.00 99.19           N  
ANISOU 1652  N   VAL A 270    12762  15206   9718    615    126   1213       N  
ATOM   1653  CA  VAL A 270     -30.207 -17.997  44.692  1.00100.67           C  
ANISOU 1653  CA  VAL A 270    13109  15083  10058    605    111   1153       C  
ATOM   1654  C   VAL A 270     -30.214 -16.667  45.472  1.00100.66           C  
ANISOU 1654  C   VAL A 270    13223  14942  10079    784    161   1257       C  
ATOM   1655  O   VAL A 270     -30.342 -16.696  46.693  1.00109.93           O  
ANISOU 1655  O   VAL A 270    14469  15996  11300    797    155   1245       O  
ATOM   1656  CB  VAL A 270     -28.782 -18.382  44.243  1.00102.76           C  
ANISOU 1656  CB  VAL A 270    13437  15176  10430    509     90   1055       C  
ATOM   1657  CG1 VAL A 270     -27.708 -17.960  45.261  1.00104.69           C  
ANISOU 1657  CG1 VAL A 270    13829  15143  10802    534     87   1031       C  
ATOM   1658  CG2 VAL A 270     -28.728 -19.884  43.961  1.00100.44           C  
ANISOU 1658  CG2 VAL A 270    13100  14929  10131    335     53    931       C  
ATOM   1659  N   ASN A 271     -30.079 -15.534  44.807  1.00 97.22           N  
ANISOU 1659  N   ASN A 271    12826  14509   9604    913    220   1355       N  
ATOM   1660  CA  ASN A 271     -30.080 -14.266  45.514  1.00 97.88           C  
ANISOU 1660  CA  ASN A 271    13067  14429   9691   1074    291   1449       C  
ATOM   1661  C   ASN A 271     -31.419 -13.975  46.159  1.00 97.48           C  
ANISOU 1661  C   ASN A 271    12980  14517   9540   1224    326   1548       C  
ATOM   1662  O   ASN A 271     -31.477 -13.305  47.210  1.00 99.08           O  
ANISOU 1662  O   ASN A 271    13327  14550   9766   1319    371   1584       O  
ATOM   1663  CB  ASN A 271     -29.709 -13.117  44.590  1.00103.89           C  
ANISOU 1663  CB  ASN A 271    13907  15157  10409   1184    366   1541       C  
ATOM   1664  CG  ASN A 271     -28.219 -12.818  44.607  1.00108.28           C  
ANISOU 1664  CG  ASN A 271    14606  15460  11074   1074    365   1467       C  
ATOM   1665  OD1 ASN A 271     -27.785 -11.763  45.087  1.00108.91           O  
ANISOU 1665  OD1 ASN A 271    14880  15334  11164   1130    434   1508       O  
ATOM   1666  ND2 ASN A 271     -27.422 -13.736  44.064  1.00109.96           N  
ANISOU 1666  ND2 ASN A 271    14731  15696  11350    912    294   1357       N  
ATOM   1667  N   ALA A 272     -32.499 -14.447  45.540  1.00 97.40           N  
ANISOU 1667  N   ALA A 272    12774  14832   9400   1242    312   1594       N  
ATOM   1668  CA  ALA A 272     -33.862 -14.303  46.106  1.00100.47           C  
ANISOU 1668  CA  ALA A 272    13078  15433   9663   1377    338   1691       C  
ATOM   1669  C   ALA A 272     -34.004 -14.967  47.481  1.00100.09           C  
ANISOU 1669  C   ALA A 272    13064  15277   9685   1283    292   1608       C  
ATOM   1670  O   ALA A 272     -34.534 -14.379  48.458  1.00 98.90           O  
ANISOU 1670  O   ALA A 272    12986  15078   9510   1428    335   1678       O  
ATOM   1671  CB  ALA A 272     -34.899 -14.890  45.154  1.00101.22           C  
ANISOU 1671  CB  ALA A 272    12922  15948   9589   1346    316   1732       C  
ATOM   1672  N   CYS A 273     -33.497 -16.191  47.543  1.00 98.54           N  
ANISOU 1672  N   CYS A 273    12834  15032   9573   1050    211   1462       N  
ATOM   1673  CA  CYS A 273     -33.419 -16.935  48.788  1.00 97.69           C  
ANISOU 1673  CA  CYS A 273    12780  14788   9549    940    165   1371       C  
ATOM   1674  C   CYS A 273     -32.639 -16.197  49.895  1.00 96.97           C  
ANISOU 1674  C   CYS A 273    12889  14375   9581   1013    190   1367       C  
ATOM   1675  O   CYS A 273     -33.143 -16.100  51.050  1.00 95.50           O  
ANISOU 1675  O   CYS A 273    12744  14148   9393   1063    196   1386       O  
ATOM   1676  CB  CYS A 273     -32.788 -18.314  48.544  1.00 96.25           C  
ANISOU 1676  CB  CYS A 273    12576  14558   9437    703     97   1221       C  
ATOM   1677  SG  CYS A 273     -33.848 -19.420  47.581  1.00 93.40           S  
ANISOU 1677  SG  CYS A 273    12011  14565   8909    541     72   1191       S  
ATOM   1678  N   PHE A 274     -31.437 -15.705  49.566  1.00 95.54           N  
ANISOU 1678  N   PHE A 274    12825  13986   9489    999    204   1340       N  
ATOM   1679  CA  PHE A 274     -30.644 -14.935  50.523  1.00 99.44           C  
ANISOU 1679  CA  PHE A 274    13510  14200  10071   1032    236   1332       C  
ATOM   1680  C   PHE A 274     -31.282 -13.576  50.837  1.00101.38           C  
ANISOU 1680  C   PHE A 274    13868  14414  10234   1245    337   1463       C  
ATOM   1681  O   PHE A 274     -31.106 -13.051  51.936  1.00109.28           O  
ANISOU 1681  O   PHE A 274    15020  15228  11271   1277    371   1462       O  
ATOM   1682  CB  PHE A 274     -29.179 -14.787  50.115  1.00100.74           C  
ANISOU 1682  CB  PHE A 274    13759  14188  10327    933    226   1266       C  
ATOM   1683  CG  PHE A 274     -28.390 -16.061  50.201  1.00106.46           C  
ANISOU 1683  CG  PHE A 274    14425  14882  11141    760    143   1139       C  
ATOM   1684  CD1 PHE A 274     -27.803 -16.468  51.378  1.00109.33           C  
ANISOU 1684  CD1 PHE A 274    14856  15096  11589    688    108   1070       C  
ATOM   1685  CD2 PHE A 274     -28.225 -16.874  49.078  1.00116.33           C  
ANISOU 1685  CD2 PHE A 274    15562  16258  12380    680    109   1093       C  
ATOM   1686  CE1 PHE A 274     -27.074 -17.667  51.448  1.00113.66           C  
ANISOU 1686  CE1 PHE A 274    15362  15618  12204    567     47    969       C  
ATOM   1687  CE2 PHE A 274     -27.484 -18.064  49.138  1.00118.83           C  
ANISOU 1687  CE2 PHE A 274    15856  16527  12765    549     53    982       C  
ATOM   1688  CZ  PHE A 274     -26.900 -18.460  50.324  1.00113.69           C  
ANISOU 1688  CZ  PHE A 274    15277  15725  12195    505     25    926       C  
ATOM   1689  N   PHE A 275     -32.073 -13.031  49.931  1.00103.21           N  
ANISOU 1689  N   PHE A 275    14034  14837  10343   1399    394   1580       N  
ATOM   1690  CA  PHE A 275     -32.803 -11.792  50.241  1.00106.80           C  
ANISOU 1690  CA  PHE A 275    14605  15276  10695   1647    508   1722       C  
ATOM   1691  C   PHE A 275     -33.975 -12.001  51.209  1.00106.77           C  
ANISOU 1691  C   PHE A 275    14535  15409  10624   1743    509   1767       C  
ATOM   1692  O   PHE A 275     -34.139 -11.253  52.193  1.00105.60           O  
ANISOU 1692  O   PHE A 275    14554  15101  10469   1865    580   1809       O  
ATOM   1693  CB  PHE A 275     -33.313 -11.111  48.975  1.00106.54           C  
ANISOU 1693  CB  PHE A 275    14519  15428  10530   1824    580   1857       C  
ATOM   1694  CG  PHE A 275     -34.057  -9.843  49.261  1.00108.39           C  
ANISOU 1694  CG  PHE A 275    14898  15641  10644   2118    719   2019       C  
ATOM   1695  CD1 PHE A 275     -33.368  -8.696  49.658  1.00110.38           C  
ANISOU 1695  CD1 PHE A 275    15456  15557  10927   2187    827   2041       C  
ATOM   1696  CD2 PHE A 275     -35.450  -9.804  49.178  1.00108.92           C  
ANISOU 1696  CD2 PHE A 275    14805  16028  10548   2324    751   2150       C  
ATOM   1697  CE1 PHE A 275     -34.049  -7.529  49.939  1.00113.45           C  
ANISOU 1697  CE1 PHE A 275    16022  15890  11193   2472    977   2191       C  
ATOM   1698  CE2 PHE A 275     -36.134  -8.647  49.434  1.00112.23           C  
ANISOU 1698  CE2 PHE A 275    15365  16433  10842   2634    892   2311       C  
ATOM   1699  CZ  PHE A 275     -35.434  -7.505  49.825  1.00115.19           C  
ANISOU 1699  CZ  PHE A 275    16081  16429  11257   2718   1011   2332       C  
ATOM   1700  N   VAL A 276     -34.794 -13.004  50.892  1.00108.52           N  
ANISOU 1700  N   VAL A 276    14517  15936  10778   1677    438   1756       N  
ATOM   1701  CA  VAL A 276     -35.935 -13.357  51.741  1.00108.20           C  
ANISOU 1701  CA  VAL A 276    14374  16080  10656   1730    427   1790       C  
ATOM   1702  C   VAL A 276     -35.398 -13.780  53.114  1.00110.49           C  
ANISOU 1702  C   VAL A 276    14783  16115  11083   1598    381   1678       C  
ATOM   1703  O   VAL A 276     -35.925 -13.293  54.143  1.00116.23           O  
ANISOU 1703  O   VAL A 276    15586  16795  11778   1725    427   1729       O  
ATOM   1704  CB  VAL A 276     -36.785 -14.477  51.105  1.00105.27           C  
ANISOU 1704  CB  VAL A 276    13730  16087  10177   1605    354   1772       C  
ATOM   1705  CG1 VAL A 276     -37.777 -15.075  52.093  1.00103.62           C  
ANISOU 1705  CG1 VAL A 276    13419  16048   9901   1574    321   1769       C  
ATOM   1706  CG2 VAL A 276     -37.505 -13.952  49.881  1.00104.18           C  
ANISOU 1706  CG2 VAL A 276    13451  16265   9867   1769    407   1910       C  
ATOM   1707  N   GLY A 277     -34.358 -14.644  53.134  1.00105.23           N  
ANISOU 1707  N   GLY A 277    14133  15292  10554   1367    299   1535       N  
ATOM   1708  CA  GLY A 277     -33.703 -15.014  54.414  1.00103.22           C  
ANISOU 1708  CA  GLY A 277    13993  14797  10427   1253    259   1437       C  
ATOM   1709  C   GLY A 277     -33.231 -13.850  55.290  1.00101.62           C  
ANISOU 1709  C   GLY A 277    14013  14332  10264   1358    334   1466       C  
ATOM   1710  O   GLY A 277     -33.447 -13.848  56.505  1.00100.97           O  
ANISOU 1710  O   GLY A 277    13994  14167  10202   1365    335   1451       O  
ATOM   1711  N   SER A 278     -32.622 -12.847  54.658  1.00102.96           N  
ANISOU 1711  N   SER A 278    14314  14374  10430   1428    406   1508       N  
ATOM   1712  CA  SER A 278     -32.152 -11.638  55.355  1.00106.23           C  
ANISOU 1712  CA  SER A 278    14981  14526  10853   1504    502   1534       C  
ATOM   1713  C   SER A 278     -33.260 -10.803  55.982  1.00109.06           C  
ANISOU 1713  C   SER A 278    15425  14911  11101   1738    604   1650       C  
ATOM   1714  O   SER A 278     -33.056 -10.189  57.040  1.00111.38           O  
ANISOU 1714  O   SER A 278    15914  14995  11410   1758    662   1638       O  
ATOM   1715  CB  SER A 278     -31.382 -10.746  54.424  1.00108.65           C  
ANISOU 1715  CB  SER A 278    15419  14712  11150   1523    572   1563       C  
ATOM   1716  OG  SER A 278     -30.210 -11.418  54.028  1.00117.18           O  
ANISOU 1716  OG  SER A 278    16445  15742  12333   1308    487   1451       O  
ATOM   1717  N   ILE A 279     -34.432 -10.798  55.353  1.00107.98           N  
ANISOU 1717  N   ILE A 279    15138  15051  10837   1914    629   1763       N  
ATOM   1718  CA  ILE A 279     -35.564 -10.114  55.928  1.00109.45           C  
ANISOU 1718  CA  ILE A 279    15369  15319  10897   2166    724   1886       C  
ATOM   1719  C   ILE A 279     -35.903 -10.790  57.258  1.00106.08           C  
ANISOU 1719  C   ILE A 279    14895  14897  10513   2080    659   1819       C  
ATOM   1720  O   ILE A 279     -35.971 -10.114  58.329  1.00105.52           O  
ANISOU 1720  O   ILE A 279    15012  14643  10436   2168    734   1833       O  
ATOM   1721  CB  ILE A 279     -36.749 -10.079  54.948  1.00112.62           C  
ANISOU 1721  CB  ILE A 279    15567  16092  11130   2366    752   2028       C  
ATOM   1722  CG1 ILE A 279     -36.410  -9.178  53.779  1.00114.45           C  
ANISOU 1722  CG1 ILE A 279    15900  16276  11310   2496    844   2116       C  
ATOM   1723  CG2 ILE A 279     -38.017  -9.534  55.596  1.00116.88           C  
ANISOU 1723  CG2 ILE A 279    16102  16790  11518   2642    841   2164       C  
ATOM   1724  CD1 ILE A 279     -37.203  -9.557  52.562  1.00119.62           C  
ANISOU 1724  CD1 ILE A 279    16285  17328  11837   2572    817   2205       C  
ATOM   1725  N   GLY A 280     -36.076 -12.107  57.205  1.00102.63           N  
ANISOU 1725  N   GLY A 280    14233  14645  10113   1897    532   1740       N  
ATOM   1726  CA  GLY A 280     -36.331 -12.887  58.400  1.00102.10           C  
ANISOU 1726  CA  GLY A 280    14118  14583  10092   1785    463   1669       C  
ATOM   1727  C   GLY A 280     -35.317 -12.626  59.495  1.00101.24           C  
ANISOU 1727  C   GLY A 280    14220  14136  10109   1686    466   1579       C  
ATOM   1728  O   GLY A 280     -35.685 -12.531  60.675  1.00109.36           O  
ANISOU 1728  O   GLY A 280    15306  15112  11132   1721    480   1577       O  
ATOM   1729  N   TRP A 281     -34.040 -12.507  59.124  1.00 98.47           N  
ANISOU 1729  N   TRP A 281    13973  13582   9859   1556    453   1506       N  
ATOM   1730  CA  TRP A 281     -32.951 -12.202  60.092  1.00 97.64           C  
ANISOU 1730  CA  TRP A 281    14056  13189   9851   1435    458   1420       C  
ATOM   1731  C   TRP A 281     -32.953 -10.761  60.604  1.00 99.66           C  
ANISOU 1731  C   TRP A 281    14575  13244  10046   1576    598   1479       C  
ATOM   1732  O   TRP A 281     -32.505 -10.512  61.710  1.00101.31           O  
ANISOU 1732  O   TRP A 281    14927  13274  10292   1500    614   1423       O  
ATOM   1733  CB  TRP A 281     -31.560 -12.507  59.516  1.00 96.08           C  
ANISOU 1733  CB  TRP A 281    13871  12882   9752   1247    404   1329       C  
ATOM   1734  CG  TRP A 281     -31.174 -13.918  59.627  1.00 96.94           C  
ANISOU 1734  CG  TRP A 281    13820  13064   9947   1074    280   1235       C  
ATOM   1735  CD1 TRP A 281     -31.320 -14.917  58.685  1.00 98.76           C  
ANISOU 1735  CD1 TRP A 281    13876  13462  10184   1015    213   1213       C  
ATOM   1736  CD2 TRP A 281     -30.576 -14.516  60.743  1.00 96.94           C  
ANISOU 1736  CD2 TRP A 281    13839  12967  10027    943    221   1151       C  
ATOM   1737  NE1 TRP A 281     -30.846 -16.104  59.167  1.00 97.24           N  
ANISOU 1737  NE1 TRP A 281    13620  13256  10071    865    125   1122       N  
ATOM   1738  CE2 TRP A 281     -30.394 -15.898  60.436  1.00 95.70           C  
ANISOU 1738  CE2 TRP A 281    13529  12909   9921    829    125   1089       C  
ATOM   1739  CE3 TRP A 281     -30.159 -14.026  61.984  1.00 98.13           C  
ANISOU 1739  CE3 TRP A 281    14129  12956  10198    908    245   1122       C  
ATOM   1740  CZ2 TRP A 281     -29.805 -16.776  61.304  1.00 93.63           C  
ANISOU 1740  CZ2 TRP A 281    13254  12588   9732    712     59   1014       C  
ATOM   1741  CZ3 TRP A 281     -29.569 -14.894  62.852  1.00 98.37           C  
ANISOU 1741  CZ3 TRP A 281    14117  12956  10300    776    167   1045       C  
ATOM   1742  CH2 TRP A 281     -29.388 -16.270  62.502  1.00 96.94           C  
ANISOU 1742  CH2 TRP A 281    13785  12875  10173    692     76    997       C  
ATOM   1743  N   LEU A 282     -33.405  -9.809  59.795  1.00102.15           N  
ANISOU 1743  N   LEU A 282    14973  13578  10259   1774    710   1591       N  
ATOM   1744  CA  LEU A 282     -33.377  -8.399  60.204  1.00104.64           C  
ANISOU 1744  CA  LEU A 282    15594  13663  10500   1916    872   1651       C  
ATOM   1745  C   LEU A 282     -34.623  -7.989  60.969  1.00106.77           C  
ANISOU 1745  C   LEU A 282    15903  14002  10662   2157    954   1747       C  
ATOM   1746  O   LEU A 282     -34.614  -6.928  61.634  1.00103.76           O  
ANISOU 1746  O   LEU A 282    15804  13395  10222   2261   1093   1777       O  
ATOM   1747  CB  LEU A 282     -33.147  -7.493  58.982  1.00106.28           C  
ANISOU 1747  CB  LEU A 282    15926  13814  10642   2025    975   1731       C  
ATOM   1748  CG  LEU A 282     -31.720  -7.598  58.426  1.00105.30           C  
ANISOU 1748  CG  LEU A 282    15842  13554  10612   1775    925   1628       C  
ATOM   1749  CD1 LEU A 282     -31.691  -7.071  57.009  1.00107.22           C  
ANISOU 1749  CD1 LEU A 282    16102  13841  10793   1879    988   1713       C  
ATOM   1750  CD2 LEU A 282     -30.692  -6.878  59.309  1.00105.71           C  
ANISOU 1750  CD2 LEU A 282    16176  13299  10687   1610    990   1543       C  
ATOM   1751  N   ALA A 283     -35.694  -8.804  60.830  1.00110.26           N  
ANISOU 1751  N   ALA A 283    16070  14763  11059   2241    880   1798       N  
ATOM   1752  CA  ALA A 283     -36.980  -8.598  61.592  1.00115.20           C  
ANISOU 1752  CA  ALA A 283    16666  15535  11567   2466    939   1893       C  
ATOM   1753  C   ALA A 283     -36.828  -8.157  63.041  1.00113.21           C  
ANISOU 1753  C   ALA A 283    16629  15048  11337   2453    993   1845       C  
ATOM   1754  O   ALA A 283     -37.379  -7.142  63.437  1.00115.00           O  
ANISOU 1754  O   ALA A 283    17053  15188  11452   2692   1143   1938       O  
ATOM   1755  CB  ALA A 283     -37.851  -9.865  61.551  1.00117.28           C  
ANISOU 1755  CB  ALA A 283    16588  16162  11811   2410    807   1891       C  
ATOM   1756  N   GLN A 284     -36.089  -8.955  63.805  1.00108.86           N  
ANISOU 1756  N   GLN A 284    16036  14405  10919   2181    876   1705       N  
ATOM   1757  CA  GLN A 284     -35.746  -8.656  65.200  1.00107.71           C  
ANISOU 1757  CA  GLN A 284    16077  14040  10808   2105    906   1635       C  
ATOM   1758  C   GLN A 284     -35.321  -7.226  65.556  1.00110.98           C  
ANISOU 1758  C   GLN A 284    16865  14138  11162   2185   1082   1650       C  
ATOM   1759  O   GLN A 284     -35.491  -6.820  66.709  1.00114.46           O  
ANISOU 1759  O   GLN A 284    17465  14449  11573   2210   1145   1632       O  
ATOM   1760  CB  GLN A 284     -34.617  -9.587  65.649  1.00103.02           C  
ANISOU 1760  CB  GLN A 284    15411  13366  10365   1784    766   1484       C  
ATOM   1761  CG  GLN A 284     -33.357  -9.455  64.851  1.00 98.59           C  
ANISOU 1761  CG  GLN A 284    14914  12671   9871   1620    750   1423       C  
ATOM   1762  CD  GLN A 284     -32.245 -10.239  65.431  1.00 96.79           C  
ANISOU 1762  CD  GLN A 284    14634  12377   9763   1347    635   1292       C  
ATOM   1763  OE1 GLN A 284     -31.739  -9.917  66.504  1.00 96.75           O  
ANISOU 1763  OE1 GLN A 284    14773  12215   9770   1245    658   1232       O  
ATOM   1764  NE2 GLN A 284     -31.833 -11.285  64.735  1.00 97.11           N  
ANISOU 1764  NE2 GLN A 284    14470  12545   9880   1229    516   1250       N  
ATOM   1765  N   PHE A 285     -34.736  -6.489  64.607  1.00113.95           N  
ANISOU 1765  N   PHE A 285    17398  14379  11516   2199   1164   1675       N  
ATOM   1766  CA  PHE A 285     -34.237  -5.144  64.891  1.00118.37           C  
ANISOU 1766  CA  PHE A 285    18354  14610  12008   2228   1343   1677       C  
ATOM   1767  C   PHE A 285     -35.300  -4.070  64.856  1.00127.99           C  
ANISOU 1767  C   PHE A 285    19776  15790  13061   2595   1539   1830       C  
ATOM   1768  O   PHE A 285     -35.017  -2.938  65.262  1.00136.88           O  
ANISOU 1768  O   PHE A 285    21282  16615  14111   2636   1714   1832       O  
ATOM   1769  CB  PHE A 285     -33.110  -4.779  63.952  1.00117.99           C  
ANISOU 1769  CB  PHE A 285    18418  14419  11993   2065   1360   1635       C  
ATOM   1770  CG  PHE A 285     -31.913  -5.619  64.141  1.00117.81           C  
ANISOU 1770  CG  PHE A 285    18262  14394  12107   1718   1203   1486       C  
ATOM   1771  CD1 PHE A 285     -30.997  -5.317  65.142  1.00116.50           C  
ANISOU 1771  CD1 PHE A 285    18282  14022  11960   1483   1222   1372       C  
ATOM   1772  CD2 PHE A 285     -31.709  -6.737  63.334  1.00117.46           C  
ANISOU 1772  CD2 PHE A 285    17902  14572  12155   1628   1043   1462       C  
ATOM   1773  CE1 PHE A 285     -29.885  -6.105  65.333  1.00114.36           C  
ANISOU 1773  CE1 PHE A 285    17864  13791  11793   1188   1080   1251       C  
ATOM   1774  CE2 PHE A 285     -30.607  -7.537  63.522  1.00115.75           C  
ANISOU 1774  CE2 PHE A 285    17566  14361  12051   1345    910   1338       C  
ATOM   1775  CZ  PHE A 285     -29.693  -7.220  64.523  1.00116.22           C  
ANISOU 1775  CZ  PHE A 285    17792  14241  12124   1137    927   1239       C  
ATOM   1776  N   MET A 286     -36.510  -4.401  64.390  1.00133.18           N  
ANISOU 1776  N   MET A 286    20200  16757  13644   2860   1523   1960       N  
ATOM   1777  CA  MET A 286     -37.666  -3.502  64.547  1.00139.08           C  
ANISOU 1777  CA  MET A 286    21095  17535  14215   3254   1704   2122       C  
ATOM   1778  C   MET A 286     -38.064  -3.397  66.039  1.00145.66           C  
ANISOU 1778  C   MET A 286    22036  18283  15025   3282   1743   2086       C  
ATOM   1779  O   MET A 286     -37.988  -4.394  66.805  1.00146.20           O  
ANISOU 1779  O   MET A 286    21889  18461  15195   3071   1582   1982       O  
ATOM   1780  CB  MET A 286     -38.857  -4.013  63.761  1.00139.75           C  
ANISOU 1780  CB  MET A 286    20839  18050  14209   3498   1654   2264       C  
ATOM   1781  CG  MET A 286     -38.614  -4.158  62.273  1.00143.63           C  
ANISOU 1781  CG  MET A 286    21194  18675  14704   3492   1615   2311       C  
ATOM   1782  SD  MET A 286     -40.081  -4.750  61.396  1.00154.08           S  
ANISOU 1782  SD  MET A 286    22099  20562  15882   3756   1561   2479       S  
ATOM   1783  CE  MET A 286     -40.358  -6.392  62.088  1.00147.60           C  
ANISOU 1783  CE  MET A 286    20895  20020  15164   3467   1326   2352       C  
ATOM   1784  N   ASP A 287     -38.512  -2.204  66.443  1.00151.03           N  
ANISOU 1784  N   ASP A 287    23056  18767  15561   3554   1964   2177       N  
ATOM   1785  CA  ASP A 287     -38.771  -1.899  67.856  1.00149.66           C  
ANISOU 1785  CA  ASP A 287    23064  18446  15351   3580   2037   2136       C  
ATOM   1786  C   ASP A 287     -39.771  -2.872  68.481  1.00145.49           C  
ANISOU 1786  C   ASP A 287    22177  18277  14824   3646   1904   2160       C  
ATOM   1787  O   ASP A 287     -40.936  -2.940  68.070  1.00140.29           O  
ANISOU 1787  O   ASP A 287    21324  17935  14042   3955   1929   2314       O  
ATOM   1788  CB  ASP A 287     -39.258  -0.455  68.031  1.00158.92           C  
ANISOU 1788  CB  ASP A 287    24668  19375  16337   3929   2323   2257       C  
ATOM   1789  CG  ASP A 287     -38.129   0.567  67.927  1.00168.72           C  
ANISOU 1789  CG  ASP A 287    26373  20158  17572   3764   2477   2180       C  
ATOM   1790  OD1 ASP A 287     -37.032   0.223  67.430  1.00172.29           O  
ANISOU 1790  OD1 ASP A 287    26773  20539  18147   3429   2364   2066       O  
ATOM   1791  OD2 ASP A 287     -38.343   1.736  68.341  1.00182.07           O  
ANISOU 1791  OD2 ASP A 287    28499  21560  19119   3968   2723   2235       O  
ATOM   1792  N   GLY A 288     -39.261  -3.663  69.428  1.00143.80           N  
ANISOU 1792  N   GLY A 288    21860  18034  14742   3334   1758   2008       N  
ATOM   1793  CA  GLY A 288     -40.038  -4.628  70.182  1.00142.31           C  
ANISOU 1793  CA  GLY A 288    21370  18130  14568   3324   1627   2001       C  
ATOM   1794  C   GLY A 288     -40.272  -5.945  69.472  1.00142.06           C  
ANISOU 1794  C   GLY A 288    20908  18458  14608   3198   1423   1996       C  
ATOM   1795  O   GLY A 288     -41.078  -6.762  69.962  1.00151.31           O  
ANISOU 1795  O   GLY A 288    21819  19911  15761   3204   1325   2009       O  
ATOM   1796  N   ALA A 289     -39.626  -6.160  68.312  1.00136.97           N  
ANISOU 1796  N   ALA A 289    20195  17816  14029   3082   1366   1978       N  
ATOM   1797  CA  ALA A 289     -39.942  -7.372  67.512  1.00136.17           C  
ANISOU 1797  CA  ALA A 289    19707  18064  13968   2982   1195   1982       C  
ATOM   1798  C   ALA A 289     -39.231  -8.610  68.065  1.00131.13           C  
ANISOU 1798  C   ALA A 289    18913  17413  13496   2620   1008   1822       C  
ATOM   1799  O   ALA A 289     -39.843  -9.708  68.206  1.00129.41           O  
ANISOU 1799  O   ALA A 289    18413  17473  13283   2542    883   1812       O  
ATOM   1800  CB  ALA A 289     -39.585  -7.159  66.052  1.00138.80           C  
ANISOU 1800  CB  ALA A 289    20019  18421  14295   3011   1210   2028       C  
ATOM   1801  N   ARG A 290     -37.968  -8.409  68.453  1.00126.13           N  
ANISOU 1801  N   ARG A 290    18479  16465  12979   2402   1002   1702       N  
ATOM   1802  CA  ARG A 290     -37.159  -9.490  69.000  1.00119.74           C  
ANISOU 1802  CA  ARG A 290    17552  15627  12317   2088    844   1563       C  
ATOM   1803  C   ARG A 290     -37.873 -10.197  70.150  1.00123.37           C  
ANISOU 1803  C   ARG A 290    17878  16224  12770   2067    777   1546       C  
ATOM   1804  O   ARG A 290     -37.893 -11.427  70.200  1.00117.98           O  
ANISOU 1804  O   ARG A 290    16970  15699  12156   1903    635   1494       O  
ATOM   1805  CB  ARG A 290     -35.780  -9.005  69.453  1.00112.79           C  
ANISOU 1805  CB  ARG A 290    16910  14425  11517   1885    869   1453       C  
ATOM   1806  CG  ARG A 290     -34.782 -10.154  69.565  1.00107.14           C  
ANISOU 1806  CG  ARG A 290    16037  13724  10944   1589    705   1333       C  
ATOM   1807  CD  ARG A 290     -33.422  -9.743  70.118  1.00103.45           C  
ANISOU 1807  CD  ARG A 290    15762  13012  10533   1373    719   1227       C  
ATOM   1808  NE  ARG A 290     -32.575  -9.115  69.126  1.00100.70           N  
ANISOU 1808  NE  ARG A 290    15534  12543  10184   1321    772   1220       N  
ATOM   1809  CZ  ARG A 290     -32.082  -7.876  69.185  1.00103.06           C  
ANISOU 1809  CZ  ARG A 290    16132  12610  10415   1311    913   1213       C  
ATOM   1810  NH1 ARG A 290     -32.281  -7.070  70.224  1.00103.61           N  
ANISOU 1810  NH1 ARG A 290    16438  12517  10411   1344   1027   1203       N  
ATOM   1811  NH2 ARG A 290     -31.342  -7.415  68.164  1.00106.02           N  
ANISOU 1811  NH2 ARG A 290    16591  12904  10787   1252    951   1210       N  
ATOM   1812  N   ARG A 291     -38.475  -9.410  71.045  1.00133.81           N  
ANISOU 1812  N   ARG A 291    19359  17482  14001   2239    891   1594       N  
ATOM   1813  CA  ARG A 291     -39.259  -9.953  72.164  1.00137.62           C  
ANISOU 1813  CA  ARG A 291    19725  18107  14456   2250    844   1592       C  
ATOM   1814  C   ARG A 291     -40.532 -10.639  71.697  1.00134.15           C  
ANISOU 1814  C   ARG A 291    18991  18057  13922   2373    791   1686       C  
ATOM   1815  O   ARG A 291     -40.947 -11.615  72.320  1.00137.01           O  
ANISOU 1815  O   ARG A 291    19170  18586  14301   2254    685   1652       O  
ATOM   1816  CB  ARG A 291     -39.561  -8.888  73.250  1.00145.73           C  
ANISOU 1816  CB  ARG A 291    21013  18960  15398   2409    992   1616       C  
ATOM   1817  CG  ARG A 291     -38.319  -8.466  74.020  1.00153.20           C  
ANISOU 1817  CG  ARG A 291    22214  19567  16428   2195   1017   1492       C  
ATOM   1818  CD  ARG A 291     -38.552  -7.983  75.449  1.00162.31           C  
ANISOU 1818  CD  ARG A 291    23543  20596  17530   2225   1094   1464       C  
ATOM   1819  NE  ARG A 291     -37.350  -7.267  75.913  1.00177.75           N  
ANISOU 1819  NE  ARG A 291    25793  22223  19519   2036   1162   1360       N  
ATOM   1820  CZ  ARG A 291     -37.219  -6.589  77.060  1.00186.04           C  
ANISOU 1820  CZ  ARG A 291    27088  23081  20516   2008   1262   1310       C  
ATOM   1821  NH1 ARG A 291     -38.224  -6.503  77.935  1.00188.09           N  
ANISOU 1821  NH1 ARG A 291    27345  23422  20696   2182   1309   1358       N  
ATOM   1822  NH2 ARG A 291     -36.056  -5.987  77.334  1.00187.48           N  
ANISOU 1822  NH2 ARG A 291    27521  23000  20713   1787   1318   1208       N  
ATOM   1823  N   GLU A 292     -41.163 -10.131  70.640  1.00128.63           N  
ANISOU 1823  N   GLU A 292    18247  17518  13107   2601    867   1808       N  
ATOM   1824  CA  GLU A 292     -42.399 -10.739  70.127  1.00134.57           C  
ANISOU 1824  CA  GLU A 292    18696  18699  13734   2707    822   1905       C  
ATOM   1825  C   GLU A 292     -42.113 -12.107  69.471  1.00134.73           C  
ANISOU 1825  C   GLU A 292    18471  18877  13841   2422    654   1824       C  
ATOM   1826  O   GLU A 292     -42.963 -13.030  69.510  1.00132.91           O  
ANISOU 1826  O   GLU A 292    17989  18968  13540   2353    572   1839       O  
ATOM   1827  CB  GLU A 292     -43.075  -9.763  69.150  1.00146.75           C  
ANISOU 1827  CB  GLU A 292    20263  20382  15113   3043    959   2067       C  
ATOM   1828  CG  GLU A 292     -44.229 -10.294  68.272  1.00153.54           C  
ANISOU 1828  CG  GLU A 292    20788  21734  15817   3147    918   2181       C  
ATOM   1829  CD  GLU A 292     -45.524 -10.555  69.016  1.00155.84           C  
ANISOU 1829  CD  GLU A 292    20889  22370  15950   3272    918   2258       C  
ATOM   1830  OE1 GLU A 292     -45.888  -9.739  69.873  1.00164.03           O  
ANISOU 1830  OE1 GLU A 292    22093  23313  16917   3500   1035   2316       O  
ATOM   1831  OE2 GLU A 292     -46.198 -11.553  68.709  1.00155.74           O  
ANISOU 1831  OE2 GLU A 292    20569  22737  15867   3142    809   2264       O  
ATOM   1832  N   ILE A 293     -40.934 -12.218  68.838  1.00132.36           N  
ANISOU 1832  N   ILE A 293    18256  18358  13675   2256    616   1742       N  
ATOM   1833  CA  ILE A 293     -40.556 -13.452  68.102  1.00126.96           C  
ANISOU 1833  CA  ILE A 293    17383  17784  13071   2007    480   1666       C  
ATOM   1834  C   ILE A 293     -39.997 -14.498  69.030  1.00120.86           C  
ANISOU 1834  C   ILE A 293    16593  16903  12424   1745    368   1540       C  
ATOM   1835  O   ILE A 293     -40.346 -15.652  68.898  1.00119.70           O  
ANISOU 1835  O   ILE A 293    16264  16943  12272   1588    273   1506       O  
ATOM   1836  CB  ILE A 293     -39.528 -13.136  66.999  1.00130.68           C  
ANISOU 1836  CB  ILE A 293    17944  18086  13621   1961    491   1638       C  
ATOM   1837  CG1 ILE A 293     -40.148 -12.151  65.988  1.00140.76           C  
ANISOU 1837  CG1 ILE A 293    19229  19493  14758   2234    606   1779       C  
ATOM   1838  CG2 ILE A 293     -39.065 -14.397  66.269  1.00126.84           C  
ANISOU 1838  CG2 ILE A 293    17294  17682  13216   1714    365   1554       C  
ATOM   1839  CD1 ILE A 293     -39.136 -11.237  65.327  1.00144.26           C  
ANISOU 1839  CD1 ILE A 293    19892  19660  15258   2269    683   1774       C  
ATOM   1840  N   VAL A 294     -39.135 -14.081  69.966  1.00116.09           N  
ANISOU 1840  N   VAL A 294    16189  16003  11917   1694    388   1474       N  
ATOM   1841  CA  VAL A 294     -38.398 -14.998  70.817  1.00112.00           C  
ANISOU 1841  CA  VAL A 294    15670  15363  11521   1460    289   1362       C  
ATOM   1842  C   VAL A 294     -39.098 -15.352  72.146  1.00112.78           C  
ANISOU 1842  C   VAL A 294    15731  15534  11584   1451    268   1359       C  
ATOM   1843  O   VAL A 294     -39.054 -16.540  72.574  1.00115.97           O  
ANISOU 1843  O   VAL A 294    16030  15994  12037   1269    168   1299       O  
ATOM   1844  CB  VAL A 294     -36.989 -14.435  71.062  1.00114.60           C  
ANISOU 1844  CB  VAL A 294    16203  15380  11958   1374    311   1289       C  
ATOM   1845  CG1 VAL A 294     -36.199 -15.268  72.075  1.00127.15           C  
ANISOU 1845  CG1 VAL A 294    17794  16863  13653   1168    221   1190       C  
ATOM   1846  CG2 VAL A 294     -36.211 -14.419  69.761  1.00115.77           C  
ANISOU 1846  CG2 VAL A 294    16347  15484  12154   1325    301   1274       C  
ATOM   1847  N   CYS A 295     -39.707 -14.360  72.810  1.00114.70           N  
ANISOU 1847  N   CYS A 295    16077  15763  11739   1645    369   1423       N  
ATOM   1848  CA  CYS A 295     -40.350 -14.569  74.129  1.00119.00           C  
ANISOU 1848  CA  CYS A 295    16601  16368  12243   1651    359   1422       C  
ATOM   1849  C   CYS A 295     -41.797 -15.015  74.040  1.00117.91           C  
ANISOU 1849  C   CYS A 295    16246  16590  11962   1742    346   1506       C  
ATOM   1850  O   CYS A 295     -42.503 -14.655  73.091  1.00118.76           O  
ANISOU 1850  O   CYS A 295    16263  16904  11955   1905    396   1600       O  
ATOM   1851  CB  CYS A 295     -40.352 -13.304  74.993  1.00126.21           C  
ANISOU 1851  CB  CYS A 295    17742  17097  13112   1815    485   1446       C  
ATOM   1852  SG  CYS A 295     -38.800 -12.389  75.153  1.00135.14           S  
ANISOU 1852  SG  CYS A 295    19172  17828  14344   1724    548   1361       S  
ATOM   1853  N   ARG A 296     -42.233 -15.785  75.047  1.00114.45           N  
ANISOU 1853  N   ARG A 296    15721  16246  11516   1632    282   1475       N  
ATOM   1854  CA  ARG A 296     -43.646 -16.203  75.189  1.00114.81           C  
ANISOU 1854  CA  ARG A 296    15560  16659  11403   1690    271   1549       C  
ATOM   1855  C   ARG A 296     -44.400 -15.096  75.898  1.00114.27           C  
ANISOU 1855  C   ARG A 296    15566  16636  11214   1967    387   1639       C  
ATOM   1856  O   ARG A 296     -43.788 -14.083  76.308  1.00111.97           O  
ANISOU 1856  O   ARG A 296    15513  16056  10971   2080    477   1628       O  
ATOM   1857  CB  ARG A 296     -43.754 -17.496  75.972  1.00116.48           C  
ANISOU 1857  CB  ARG A 296    15671  16934  11651   1442    161   1477       C  
ATOM   1858  CG  ARG A 296     -43.690 -18.733  75.126  1.00123.81           C  
ANISOU 1858  CG  ARG A 296    16463  17983  12595   1213     70   1431       C  
ATOM   1859  CD  ARG A 296     -43.516 -19.939  76.005  1.00135.96           C  
ANISOU 1859  CD  ARG A 296    17991  19471  14193    970    -16   1349       C  
ATOM   1860  NE  ARG A 296     -43.633 -21.191  75.265  1.00150.55           N  
ANISOU 1860  NE  ARG A 296    19734  21446  16021    743    -82   1306       N  
ATOM   1861  CZ  ARG A 296     -44.700 -21.992  75.253  1.00164.19           C  
ANISOU 1861  CZ  ARG A 296    21304  23477  17603    613   -111   1321       C  
ATOM   1862  NH1 ARG A 296     -45.804 -21.711  75.954  1.00168.02           N  
ANISOU 1862  NH1 ARG A 296    21681  24213  17945    700    -88   1388       N  
ATOM   1863  NH2 ARG A 296     -44.649 -23.114  74.531  1.00171.50           N  
ANISOU 1863  NH2 ARG A 296    22187  24461  18514    379   -156   1265       N  
ATOM   1864  N   ALA A 297     -45.713 -15.261  76.036  1.00114.04           N  
ANISOU 1864  N   ALA A 297    15346  16970  11012   2072    397   1727       N  
ATOM   1865  CA  ALA A 297     -46.512 -14.284  76.764  1.00115.24           C  
ANISOU 1865  CA  ALA A 297    15557  17196  11030   2359    513   1822       C  
ATOM   1866  C   ALA A 297     -46.040 -14.196  78.222  1.00116.96           C  
ANISOU 1866  C   ALA A 297    15947  17149  11342   2283    513   1740       C  
ATOM   1867  O   ALA A 297     -45.887 -13.079  78.757  1.00122.56           O  
ANISOU 1867  O   ALA A 297    16881  17652  12035   2478    635   1762       O  
ATOM   1868  CB  ALA A 297     -47.986 -14.634  76.690  1.00116.86           C  
ANISOU 1868  CB  ALA A 297    15484  17896  11020   2455    507   1928       C  
ATOM   1869  N   ASP A 298     -45.794 -15.360  78.852  1.00112.05           N  
ANISOU 1869  N   ASP A 298    15239  16526  10808   1997    386   1646       N  
ATOM   1870  CA  ASP A 298     -45.323 -15.413  80.241  1.00108.00           C  
ANISOU 1870  CA  ASP A 298    14860  15794  10381   1899    370   1569       C  
ATOM   1871  C   ASP A 298     -43.909 -14.862  80.525  1.00105.70           C  
ANISOU 1871  C   ASP A 298    14829  15084  10247   1830    395   1479       C  
ATOM   1872  O   ASP A 298     -43.615 -14.412  81.619  1.00111.68           O  
ANISOU 1872  O   ASP A 298    15739  15666  11027   1835    435   1440       O  
ATOM   1873  CB  ASP A 298     -45.508 -16.822  80.847  1.00109.01           C  
ANISOU 1873  CB  ASP A 298    14829  16051  10539   1631    238   1510       C  
ATOM   1874  CG  ASP A 298     -44.824 -17.960  80.060  1.00107.61           C  
ANISOU 1874  CG  ASP A 298    14584  15832  10470   1371    130   1438       C  
ATOM   1875  OD1 ASP A 298     -43.737 -17.751  79.492  1.00105.73           O  
ANISOU 1875  OD1 ASP A 298    14467  15349  10355   1333    129   1390       O  
ATOM   1876  OD2 ASP A 298     -45.379 -19.089  80.040  1.00104.09           O  
ANISOU 1876  OD2 ASP A 298    13975  15598   9974   1195     51   1428       O  
ATOM   1877  N   GLY A 299     -43.046 -14.861  79.535  1.00106.67           N  
ANISOU 1877  N   GLY A 299    14998  15069  10461   1759    378   1446       N  
ATOM   1878  CA  GLY A 299     -41.682 -14.328  79.680  1.00105.86           C  
ANISOU 1878  CA  GLY A 299    15121  14618  10483   1674    403   1365       C  
ATOM   1879  C   GLY A 299     -40.617 -15.397  79.675  1.00102.04           C  
ANISOU 1879  C   GLY A 299    14589  14034  10147   1397    275   1267       C  
ATOM   1880  O   GLY A 299     -39.462 -15.111  79.975  1.00 96.50           O  
ANISOU 1880  O   GLY A 299    14035  13094   9536   1294    278   1196       O  
ATOM   1881  N   THR A 300     -41.025 -16.623  79.332  1.00100.56           N  
ANISOU 1881  N   THR A 300    14201  14042   9964   1279    175   1267       N  
ATOM   1882  CA  THR A 300     -40.114 -17.700  79.037  1.00101.19           C  
ANISOU 1882  CA  THR A 300    14238  14044  10163   1060     72   1194       C  
ATOM   1883  C   THR A 300     -39.748 -17.686  77.550  1.00107.00           C  
ANISOU 1883  C   THR A 300    14946  14783  10923   1066     73   1202       C  
ATOM   1884  O   THR A 300     -40.348 -16.929  76.769  1.00113.64           O  
ANISOU 1884  O   THR A 300    15774  15725  11678   1238    145   1273       O  
ATOM   1885  CB  THR A 300     -40.704 -19.066  79.433  1.00 98.71           C  
ANISOU 1885  CB  THR A 300    13773  13901   9830    910    -17   1183       C  
ATOM   1886  OG1 THR A 300     -41.844 -19.380  78.639  1.00 93.77           O  
ANISOU 1886  OG1 THR A 300    12985  13555   9085    947    -17   1243       O  
ATOM   1887  CG2 THR A 300     -41.111 -19.064  80.875  1.00 98.88           C  
ANISOU 1887  CG2 THR A 300    13813  13935   9820    909    -17   1181       C  
ATOM   1888  N   MET A 301     -38.769 -18.515  77.169  1.00107.14           N  
ANISOU 1888  N   MET A 301    14956  14700  11049    898      0   1137       N  
ATOM   1889  CA  MET A 301     -38.322 -18.615  75.788  1.00110.58           C  
ANISOU 1889  CA  MET A 301    15367  15132  11517    882     -6   1134       C  
ATOM   1890  C   MET A 301     -39.417 -19.325  75.024  1.00109.11           C  
ANISOU 1890  C   MET A 301    15010  15211  11236    868    -30   1175       C  
ATOM   1891  O   MET A 301     -40.121 -20.141  75.609  1.00110.52           O  
ANISOU 1891  O   MET A 301    15101  15525  11364    782    -71   1173       O  
ATOM   1892  CB  MET A 301     -37.063 -19.480  75.681  1.00117.24           C  
ANISOU 1892  CB  MET A 301    16235  15829  12482    712    -77   1057       C  
ATOM   1893  CG  MET A 301     -35.823 -19.001  76.434  1.00121.34           C  
ANISOU 1893  CG  MET A 301    16886  16135  13082    674    -71   1009       C  
ATOM   1894  SD  MET A 301     -34.264 -19.902  76.083  1.00124.01           S  
ANISOU 1894  SD  MET A 301    17226  16355  13534    526   -141    944       S  
ATOM   1895  CE  MET A 301     -34.866 -21.540  76.428  1.00118.36           C  
ANISOU 1895  CE  MET A 301    16417  15739  12814    428   -211    938       C  
ATOM   1896  N   ARG A 302     -39.574 -19.041  73.732  1.00107.54           N  
ANISOU 1896  N   ARG A 302    14759  15103  10996    932     -4   1210       N  
ATOM   1897  CA  ARG A 302     -40.535 -19.827  72.941  1.00106.40           C  
ANISOU 1897  CA  ARG A 302    14439  15240  10748    870    -33   1237       C  
ATOM   1898  C   ARG A 302     -39.922 -21.165  72.583  1.00105.88           C  
ANISOU 1898  C   ARG A 302    14362  15110  10756    641   -108   1154       C  
ATOM   1899  O   ARG A 302     -38.823 -21.229  72.039  1.00105.43           O  
ANISOU 1899  O   ARG A 302    14381  14869  10805    603   -119   1109       O  
ATOM   1900  CB  ARG A 302     -40.968 -19.103  71.680  1.00107.20           C  
ANISOU 1900  CB  ARG A 302    14474  15495  10760   1018     22   1311       C  
ATOM   1901  CG  ARG A 302     -41.996 -18.035  71.946  1.00111.28           C  
ANISOU 1901  CG  ARG A 302    14962  16179  11139   1264    106   1421       C  
ATOM   1902  CD  ARG A 302     -42.507 -17.426  70.693  1.00113.88           C  
ANISOU 1902  CD  ARG A 302    15206  16703  11358   1425    163   1511       C  
ATOM   1903  NE  ARG A 302     -43.364 -16.294  71.002  1.00115.33           N  
ANISOU 1903  NE  ARG A 302    15402  17007  11408   1712    267   1629       N  
ATOM   1904  CZ  ARG A 302     -44.407 -15.919  70.287  1.00127.05           C  
ANISOU 1904  CZ  ARG A 302    16735  18823  12713   1893    319   1748       C  
ATOM   1905  NH1 ARG A 302     -45.074 -14.831  70.663  1.00136.80           N  
ANISOU 1905  NH1 ARG A 302    18021  20125  13830   2194    431   1861       N  
ATOM   1906  NH2 ARG A 302     -44.786 -16.588  69.199  1.00132.93           N  
ANISOU 1906  NH2 ARG A 302    17285  19840  13380   1788    270   1760       N  
ATOM   1907  N   LEU A 303     -40.648 -22.230  72.890  1.00108.06           N  
ANISOU 1907  N   LEU A 303    14553  15541  10962    491   -148   1138       N  
ATOM   1908  CA  LEU A 303     -40.211 -23.588  72.621  1.00111.04           C  
ANISOU 1908  CA  LEU A 303    14956  15851  11382    272   -197   1062       C  
ATOM   1909  C   LEU A 303     -41.389 -24.409  72.168  1.00111.60           C  
ANISOU 1909  C   LEU A 303    14896  16212  11293    124   -207   1068       C  
ATOM   1910  O   LEU A 303     -42.529 -24.161  72.580  1.00114.86           O  
ANISOU 1910  O   LEU A 303    15193  16875  11571    160   -195   1124       O  
ATOM   1911  CB  LEU A 303     -39.616 -24.216  73.867  1.00116.73           C  
ANISOU 1911  CB  LEU A 303    15784  16373  12192    190   -230   1015       C  
ATOM   1912  CG  LEU A 303     -38.318 -23.512  74.329  1.00121.91           C  
ANISOU 1912  CG  LEU A 303    16555  16784  12980    308   -222   1007       C  
ATOM   1913  CD1 LEU A 303     -37.715 -23.974  75.652  1.00129.26           C  
ANISOU 1913  CD1 LEU A 303    17540  17635  13937    325   -231   1007       C  
ATOM   1914  CD2 LEU A 303     -37.229 -23.557  73.269  1.00123.22           C  
ANISOU 1914  CD2 LEU A 303    16806  16748  13262    250   -243    952       C  
ATOM   1915  N   GLY A 304     -41.117 -25.362  71.290  1.00111.78           N  
ANISOU 1915  N   GLY A 304    14937  16220  11314    -46   -221   1010       N  
ATOM   1916  CA  GLY A 304     -42.132 -26.226  70.733  1.00117.10           C  
ANISOU 1916  CA  GLY A 304    15507  17162  11819   -245   -223    997       C  
ATOM   1917  C   GLY A 304     -43.267 -25.605  69.973  1.00118.17           C  
ANISOU 1917  C   GLY A 304    15441  17678  11778   -180   -201   1072       C  
ATOM   1918  O   GLY A 304     -44.385 -26.061  70.130  1.00127.92           O  
ANISOU 1918  O   GLY A 304    16554  19210  12840   -310   -205   1088       O  
ATOM   1919  N   GLU A 305     -42.966 -24.661  69.087  1.00114.62           N  
ANISOU 1919  N   GLU A 305    14954  17239  11355      1   -176   1119       N  
ATOM   1920  CA  GLU A 305     -43.964 -23.993  68.299  1.00117.30           C  
ANISOU 1920  CA  GLU A 305    15101  17943  11522    109   -146   1210       C  
ATOM   1921  C   GLU A 305     -44.251 -24.899  67.051  1.00114.36           C  
ANISOU 1921  C   GLU A 305    14644  17771  11035   -125   -157   1162       C  
ATOM   1922  O   GLU A 305     -43.367 -25.629  66.603  1.00105.84           O  
ANISOU 1922  O   GLU A 305    13696  16454  10061   -271   -170   1070       O  
ATOM   1923  CB  GLU A 305     -43.494 -22.585  67.947  1.00118.80           C  
ANISOU 1923  CB  GLU A 305    15323  18029  11785    410   -101   1285       C  
ATOM   1924  CG  GLU A 305     -43.568 -21.591  69.070  1.00118.79           C  
ANISOU 1924  CG  GLU A 305    15384  17929  11819    635    -66   1345       C  
ATOM   1925  CD  GLU A 305     -44.777 -20.686  69.028  1.00123.72           C  
ANISOU 1925  CD  GLU A 305    15856  18893  12256    861     -8   1477       C  
ATOM   1926  OE1 GLU A 305     -44.749 -19.685  69.782  1.00125.18           O  
ANISOU 1926  OE1 GLU A 305    16132  18961  12470   1089     44   1533       O  
ATOM   1927  OE2 GLU A 305     -45.753 -20.972  68.277  1.00127.65           O  
ANISOU 1927  OE2 GLU A 305    16151  19784  12565    814     -9   1527       O  
ATOM   1928  N   PRO A 306     -45.449 -24.854  66.463  1.00118.14           N  
ANISOU 1928  N   PRO A 306    14906  18695  11286   -161   -145   1224       N  
ATOM   1929  CA  PRO A 306     -46.550 -23.957  66.841  1.00121.62           C  
ANISOU 1929  CA  PRO A 306    15165  19477  11568     49   -117   1353       C  
ATOM   1930  C   PRO A 306     -47.343 -24.506  68.009  1.00123.70           C  
ANISOU 1930  C   PRO A 306    15383  19881  11736    -76   -137   1346       C  
ATOM   1931  O   PRO A 306     -47.757 -25.653  67.950  1.00122.10           O  
ANISOU 1931  O   PRO A 306    15150  19815  11426   -393   -163   1274       O  
ATOM   1932  CB  PRO A 306     -47.450 -23.921  65.588  1.00123.26           C  
ANISOU 1932  CB  PRO A 306    15135  20154  11543     12   -102   1415       C  
ATOM   1933  CG  PRO A 306     -46.968 -25.015  64.708  1.00122.82           C  
ANISOU 1933  CG  PRO A 306    15143  20017  11506   -299   -127   1294       C  
ATOM   1934  CD  PRO A 306     -45.797 -25.714  65.323  1.00119.99           C  
ANISOU 1934  CD  PRO A 306    15054  19155  11380   -420   -151   1172       C  
ATOM   1935  N   THR A 307     -47.531 -23.700  69.049  1.00130.93           N  
ANISOU 1935  N   THR A 307    16313  20751  12681    156   -117   1416       N  
ATOM   1936  CA  THR A 307     -48.330 -24.074  70.207  1.00140.66           C  
ANISOU 1936  CA  THR A 307    17488  22140  13816     75   -133   1424       C  
ATOM   1937  C   THR A 307     -49.539 -23.197  70.169  1.00145.74           C  
ANISOU 1937  C   THR A 307    17899  23234  14239    308    -89   1569       C  
ATOM   1938  O   THR A 307     -49.500 -22.105  69.591  1.00151.32           O  
ANISOU 1938  O   THR A 307    18574  23982  14937    606    -36   1665       O  
ATOM   1939  CB  THR A 307     -47.642 -23.872  71.577  1.00148.15           C  
ANISOU 1939  CB  THR A 307    18631  22701  14956    163   -140   1392       C  
ATOM   1940  OG1 THR A 307     -47.143 -22.518  71.719  1.00160.55           O  
ANISOU 1940  OG1 THR A 307    20287  24081  16634    503    -89   1459       O  
ATOM   1941  CG2 THR A 307     -46.521 -24.893  71.802  1.00143.83           C  
ANISOU 1941  CG2 THR A 307    18297  21752  14597    -67   -182   1260       C  
ATOM   1942  N   SER A 308     -50.599 -23.674  70.814  1.00147.18           N  
ANISOU 1942  N   SER A 308    17930  23754  14235    181   -105   1591       N  
ATOM   1943  CA  SER A 308     -51.963 -23.186  70.582  1.00149.89           C  
ANISOU 1943  CA  SER A 308    17982  24679  14288    319    -71   1727       C  
ATOM   1944  C   SER A 308     -52.250 -21.700  70.843  1.00152.93           C  
ANISOU 1944  C   SER A 308    18332  25129  14644    793      6   1880       C  
ATOM   1945  O   SER A 308     -52.694 -20.974  69.916  1.00166.59           O  
ANISOU 1945  O   SER A 308    19912  27151  16232   1018     58   1998       O  
ATOM   1946  CB  SER A 308     -52.909 -24.045  71.395  1.00145.79           C  
ANISOU 1946  CB  SER A 308    17337  24463  13593     63   -106   1705       C  
ATOM   1947  OG  SER A 308     -52.280 -24.299  72.632  1.00144.90           O  
ANISOU 1947  OG  SER A 308    17444  23929  13679     22   -128   1629       O  
ATOM   1948  N   ASN A 309     -52.031 -21.233  72.070  1.00142.78           N  
ANISOU 1948  N   ASN A 309    17191  23585  13473    953     26   1885       N  
ATOM   1949  CA  ASN A 309     -52.463 -19.855  72.409  1.00144.03           C  
ANISOU 1949  CA  ASN A 309    17334  23830  13560   1399    122   2033       C  
ATOM   1950  C   ASN A 309     -51.502 -18.719  71.999  1.00141.07           C  
ANISOU 1950  C   ASN A 309    17184  23056  13360   1695    195   2061       C  
ATOM   1951  O   ASN A 309     -51.845 -17.548  72.031  1.00143.01           O  
ANISOU 1951  O   ASN A 309    17445  23364  13525   2073    297   2191       O  
ATOM   1952  CB  ASN A 309     -52.744 -19.730  73.905  1.00149.16           C  
ANISOU 1952  CB  ASN A 309    18045  24406  14223   1464    131   2034       C  
ATOM   1953  CG  ASN A 309     -54.174 -20.158  74.313  1.00153.66           C  
ANISOU 1953  CG  ASN A 309    18324  25554  14505   1397    118   2106       C  
ATOM   1954  OD1 ASN A 309     -55.018 -20.591  73.512  1.00152.76           O  
ANISOU 1954  OD1 ASN A 309    17945  25939  14158   1276     99   2155       O  
ATOM   1955  ND2 ASN A 309     -54.443 -20.001  75.600  1.00155.74           N  
ANISOU 1955  ND2 ASN A 309    18635  25767  14773   1472    130   2114       N  
ATOM   1956  N   GLU A 310     -50.282 -19.056  71.632  1.00139.96           N  
ANISOU 1956  N   GLU A 310    17233  22498  13447   1526    153   1942       N  
ATOM   1957  CA  GLU A 310     -49.281 -18.055  71.260  1.00137.20           C  
ANISOU 1957  CA  GLU A 310    17107  21760  13263   1746    217   1952       C  
ATOM   1958  C   GLU A 310     -49.463 -17.546  69.813  1.00132.40           C  
ANISOU 1958  C   GLU A 310    16394  21361  12550   1899    264   2044       C  
ATOM   1959  O   GLU A 310     -50.036 -18.218  68.954  1.00130.42           O  
ANISOU 1959  O   GLU A 310    15920  21479  12153   1740    220   2056       O  
ATOM   1960  CB  GLU A 310     -47.884 -18.681  71.471  1.00137.21           C  
ANISOU 1960  CB  GLU A 310    17326  21274  13533   1493    148   1790       C  
ATOM   1961  CG  GLU A 310     -47.487 -18.915  72.942  1.00135.63           C  
ANISOU 1961  CG  GLU A 310    17275  20799  13459   1411    121   1714       C  
ATOM   1962  CD  GLU A 310     -47.217 -17.632  73.745  1.00134.43           C  
ANISOU 1962  CD  GLU A 310    17311  20403  13360   1703    213   1762       C  
ATOM   1963  OE1 GLU A 310     -46.933 -16.559  73.170  1.00132.66           O  
ANISOU 1963  OE1 GLU A 310    17192  20068  13142   1942    301   1825       O  
ATOM   1964  OE2 GLU A 310     -47.317 -17.679  74.977  1.00131.16           O  
ANISOU 1964  OE2 GLU A 310    16957  19906  12970   1690    208   1737       O  
ATOM   1965  N   THR A 311     -48.916 -16.356  69.566  1.00128.41           N  
ANISOU 1965  N   THR A 311    16073  20597  12117   2190    358   2104       N  
ATOM   1966  CA  THR A 311     -48.966 -15.675  68.261  1.00126.86           C  
ANISOU 1966  CA  THR A 311    15831  20529  11839   2389    422   2205       C  
ATOM   1967  C   THR A 311     -48.091 -16.355  67.196  1.00125.41           C  
ANISOU 1967  C   THR A 311    15659  20208  11783   2126    347   2099       C  
ATOM   1968  O   THR A 311     -47.213 -17.179  67.494  1.00124.33           O  
ANISOU 1968  O   THR A 311    15631  19775  11831   1836    263   1948       O  
ATOM   1969  CB  THR A 311     -48.533 -14.177  68.354  1.00125.13           C  
ANISOU 1969  CB  THR A 311    15871  20002  11668   2763    563   2290       C  
ATOM   1970  OG1 THR A 311     -47.125 -14.072  68.590  1.00124.28           O  
ANISOU 1970  OG1 THR A 311    16047  19355  11817   2630    547   2160       O  
ATOM   1971  CG2 THR A 311     -49.269 -13.436  69.463  1.00124.50           C  
ANISOU 1971  CG2 THR A 311    15845  19981  11478   3043    659   2385       C  
ATOM   1972  N   LEU A 312     -48.323 -15.973  65.947  1.00128.46           N  
ANISOU 1972  N   LEU A 312    15936  20813  12058   2252    386   2189       N  
ATOM   1973  CA  LEU A 312     -47.613 -16.578  64.811  1.00127.35           C  
ANISOU 1973  CA  LEU A 312    15780  20602  12004   2024    323   2104       C  
ATOM   1974  C   LEU A 312     -46.223 -15.990  64.510  1.00121.43           C  
ANISOU 1974  C   LEU A 312    15306  19349  11480   2070    352   2046       C  
ATOM   1975  O   LEU A 312     -45.472 -16.557  63.716  1.00120.08           O  
ANISOU 1975  O   LEU A 312    15151  19061  11413   1864    294   1954       O  
ATOM   1976  CB  LEU A 312     -48.497 -16.512  63.556  1.00126.74           C  
ANISOU 1976  CB  LEU A 312    15436  21029  11689   2104    344   2222       C  
ATOM   1977  CG  LEU A 312     -49.857 -17.221  63.618  1.00127.00           C  
ANISOU 1977  CG  LEU A 312    15148  21647  11458   1988    306   2272       C  
ATOM   1978  CD1 LEU A 312     -50.456 -17.101  62.228  1.00128.67           C  
ANISOU 1978  CD1 LEU A 312    15118  22315  11456   2050    325   2378       C  
ATOM   1979  CD2 LEU A 312     -49.807 -18.691  64.071  1.00125.54           C  
ANISOU 1979  CD2 LEU A 312    14924  21456  11318   1536    193   2106       C  
ATOM   1980  N   SER A 313     -45.871 -14.894  65.162  1.00118.44           N  
ANISOU 1980  N   SER A 313    15152  18680  11170   2318    443   2090       N  
ATOM   1981  CA  SER A 313     -44.600 -14.227  64.900  1.00120.30           C  
ANISOU 1981  CA  SER A 313    15651  18470  11585   2355    484   2043       C  
ATOM   1982  C   SER A 313     -43.352 -15.114  64.903  1.00119.49           C  
ANISOU 1982  C   SER A 313    15638  18059  11700   2024    380   1868       C  
ATOM   1983  O   SER A 313     -42.416 -14.838  64.173  1.00117.18           O  
ANISOU 1983  O   SER A 313    15458  17552  11510   2001    389   1835       O  
ATOM   1984  CB  SER A 313     -44.386 -13.120  65.911  1.00122.31           C  
ANISOU 1984  CB  SER A 313    16163  18430  11878   2579    591   2078       C  
ATOM   1985  OG  SER A 313     -45.505 -12.278  65.899  1.00129.71           O  
ANISOU 1985  OG  SER A 313    17042  19634  12606   2923    705   2249       O  
ATOM   1986  N   CYS A 314     -43.332 -16.154  65.741  1.00119.83           N  
ANISOU 1986  N   CYS A 314    15640  18083  11804   1787    289   1767       N  
ATOM   1987  CA  CYS A 314     -42.214 -17.091  65.798  1.00114.48           C  
ANISOU 1987  CA  CYS A 314    15042  17145  11311   1501    199   1616       C  
ATOM   1988  C   CYS A 314     -42.243 -18.051  64.598  1.00114.82           C  
ANISOU 1988  C   CYS A 314    14932  17375  11319   1305    137   1574       C  
ATOM   1989  O   CYS A 314     -41.225 -18.211  63.886  1.00112.33           O  
ANISOU 1989  O   CYS A 314    14695  16862  11121   1214    116   1508       O  
ATOM   1990  CB  CYS A 314     -42.256 -17.863  67.104  1.00112.85           C  
ANISOU 1990  CB  CYS A 314    14856  16864  11158   1343    140   1540       C  
ATOM   1991  SG  CYS A 314     -40.927 -19.075  67.360  1.00115.06           S  
ANISOU 1991  SG  CYS A 314    15241  16833  11640   1036     44   1376       S  
ATOM   1992  N   VAL A 315     -43.388 -18.697  64.360  1.00118.14           N  
ANISOU 1992  N   VAL A 315    15135  18187  11564   1224    111   1607       N  
ATOM   1993  CA  VAL A 315     -43.486 -19.614  63.185  1.00120.07           C  
ANISOU 1993  CA  VAL A 315    15243  18632  11746   1010     63   1561       C  
ATOM   1994  C   VAL A 315     -43.305 -18.890  61.846  1.00117.54           C  
ANISOU 1994  C   VAL A 315    14885  18387  11387   1157    109   1630       C  
ATOM   1995  O   VAL A 315     -42.708 -19.446  60.916  1.00117.47           O  
ANISOU 1995  O   VAL A 315    14877  18324  11430    994     75   1558       O  
ATOM   1996  CB  VAL A 315     -44.755 -20.504  63.153  1.00122.06           C  
ANISOU 1996  CB  VAL A 315    15267  19322  11786    835     30   1570       C  
ATOM   1997  CG1 VAL A 315     -44.730 -21.490  64.319  1.00124.24           C  
ANISOU 1997  CG1 VAL A 315    15610  19472  12120    612    -22   1471       C  
ATOM   1998  CG2 VAL A 315     -46.031 -19.675  63.163  1.00125.06           C  
ANISOU 1998  CG2 VAL A 315    15458  20114  11942   1084     88   1732       C  
ATOM   1999  N   ILE A 316     -43.785 -17.653  61.764  1.00115.01           N  
ANISOU 1999  N   ILE A 316    14552  18170  10973   1473    194   1773       N  
ATOM   2000  CA  ILE A 316     -43.574 -16.825  60.555  1.00114.49           C  
ANISOU 2000  CA  ILE A 316    14484  18142  10872   1652    253   1856       C  
ATOM   2001  C   ILE A 316     -42.092 -16.663  60.255  1.00108.24           C  
ANISOU 2001  C   ILE A 316    13909  16916  10299   1587    245   1763       C  
ATOM   2002  O   ILE A 316     -41.632 -16.994  59.147  1.00108.05           O  
ANISOU 2002  O   ILE A 316    13845  16912  10297   1478    219   1725       O  
ATOM   2003  CB  ILE A 316     -44.318 -15.450  60.659  1.00116.85           C  
ANISOU 2003  CB  ILE A 316    14788  18578  11029   2047    373   2038       C  
ATOM   2004  CG1 ILE A 316     -45.764 -15.632  60.154  1.00119.51           C  
ANISOU 2004  CG1 ILE A 316    14816  19502  11090   2120    380   2161       C  
ATOM   2005  CG2 ILE A 316     -43.613 -14.304  59.909  1.00113.08           C  
ANISOU 2005  CG2 ILE A 316    14482  17875  10605   2266    462   2104       C  
ATOM   2006  CD1 ILE A 316     -46.743 -14.650  60.749  1.00123.12           C  
ANISOU 2006  CD1 ILE A 316    15242  20156  11379   2479    483   2329       C  
ATOM   2007  N   ILE A 317     -41.373 -16.183  61.267  1.00101.27           N  
ANISOU 2007  N   ILE A 317    13244  15673   9560   1639    267   1726       N  
ATOM   2008  CA  ILE A 317     -39.949 -15.955  61.138  1.00 97.10           C  
ANISOU 2008  CA  ILE A 317    12916  14758   9218   1574    263   1642       C  
ATOM   2009  C   ILE A 317     -39.219 -17.270  60.903  1.00 91.35           C  
ANISOU 2009  C   ILE A 317    12155  13950   8601   1274    162   1500       C  
ATOM   2010  O   ILE A 317     -38.289 -17.316  60.105  1.00 89.83           O  
ANISOU 2010  O   ILE A 317    12016  13618   8495   1208    150   1452       O  
ATOM   2011  CB  ILE A 317     -39.422 -15.151  62.347  1.00 97.66           C  
ANISOU 2011  CB  ILE A 317    13214  14509   9382   1672    315   1633       C  
ATOM   2012  CG1 ILE A 317     -39.972 -13.698  62.338  1.00101.39           C  
ANISOU 2012  CG1 ILE A 317    13787  14995   9741   1997    451   1777       C  
ATOM   2013  CG2 ILE A 317     -37.908 -15.088  62.386  1.00 97.45           C  
ANISOU 2013  CG2 ILE A 317    13369  14123   9535   1544    295   1530       C  
ATOM   2014  CD1 ILE A 317     -39.753 -12.886  61.061  1.00102.02           C  
ANISOU 2014  CD1 ILE A 317    13907  15081   9773   2145    525   1858       C  
ATOM   2015  N   PHE A 318     -39.667 -18.336  61.554  1.00 89.04           N  
ANISOU 2015  N   PHE A 318    11784  13754   8292   1102     99   1440       N  
ATOM   2016  CA  PHE A 318     -39.086 -19.635  61.284  1.00 89.00           C  
ANISOU 2016  CA  PHE A 318    11772  13680   8362    836     25   1316       C  
ATOM   2017  C   PHE A 318     -39.238 -20.024  59.857  1.00 89.63           C  
ANISOU 2017  C   PHE A 318    11732  13957   8363    754     17   1313       C  
ATOM   2018  O   PHE A 318     -38.245 -20.387  59.234  1.00 87.11           O  
ANISOU 2018  O   PHE A 318    11483  13466   8148    657     -3   1238       O  
ATOM   2019  CB  PHE A 318     -39.716 -20.740  62.102  1.00 92.89           C  
ANISOU 2019  CB  PHE A 318    12209  14275   8810    657    -23   1263       C  
ATOM   2020  CG  PHE A 318     -39.513 -22.129  61.503  1.00 96.21           C  
ANISOU 2020  CG  PHE A 318    12605  14721   9228    387    -71   1158       C  
ATOM   2021  CD1 PHE A 318     -38.250 -22.755  61.575  1.00 97.29           C  
ANISOU 2021  CD1 PHE A 318    12893  14545   9527    280    -97   1057       C  
ATOM   2022  CD2 PHE A 318     -40.565 -22.822  60.892  1.00 95.23           C  
ANISOU 2022  CD2 PHE A 318    12319  14939   8923    237    -79   1160       C  
ATOM   2023  CE1 PHE A 318     -38.045 -24.032  61.044  1.00 96.02           C  
ANISOU 2023  CE1 PHE A 318    12752  14375   9356     55   -120    962       C  
ATOM   2024  CE2 PHE A 318     -40.364 -24.098  60.382  1.00 95.82           C  
ANISOU 2024  CE2 PHE A 318    12419  15002   8985    -28   -104   1053       C  
ATOM   2025  CZ  PHE A 318     -39.098 -24.694  60.433  1.00 95.43           C  
ANISOU 2025  CZ  PHE A 318    12550  14602   9105   -105   -118    955       C  
ATOM   2026  N   VAL A 319     -40.465 -19.966  59.329  1.00 93.92           N  
ANISOU 2026  N   VAL A 319    12086  14887   8712    791     34   1395       N  
ATOM   2027  CA  VAL A 319     -40.697 -20.346  57.892  1.00 97.09           C  
ANISOU 2027  CA  VAL A 319    12349  15532   9007    694     28   1394       C  
ATOM   2028  C   VAL A 319     -39.907 -19.436  56.948  1.00 96.19           C  
ANISOU 2028  C   VAL A 319    12300  15286   8962    851     67   1436       C  
ATOM   2029  O   VAL A 319     -39.114 -19.980  56.116  1.00 96.68           O  
ANISOU 2029  O   VAL A 319    12394  15243   9095    706     40   1351       O  
ATOM   2030  CB  VAL A 319     -42.163 -20.370  57.424  1.00 97.63           C  
ANISOU 2030  CB  VAL A 319    12170  16104   8820    708     42   1489       C  
ATOM   2031  CG1 VAL A 319     -42.207 -20.670  55.948  1.00 99.20           C  
ANISOU 2031  CG1 VAL A 319    12248  16518   8925    605     38   1480       C  
ATOM   2032  CG2 VAL A 319     -42.983 -21.435  58.137  1.00 97.71           C  
ANISOU 2032  CG2 VAL A 319    12095  16302   8727    480      1   1433       C  
ATOM   2033  N   ILE A 320     -40.026 -18.108  57.134  1.00 93.84           N  
ANISOU 2033  N   ILE A 320    12054  14950   8649   1134    136   1555       N  
ATOM   2034  CA  ILE A 320     -39.235 -17.203  56.311  1.00 94.45           C  
ANISOU 2034  CA  ILE A 320    12228  14867   8788   1271    184   1594       C  
ATOM   2035  C   ILE A 320     -37.765 -17.678  56.240  1.00 93.80           C  
ANISOU 2035  C   ILE A 320    12297  14436   8905   1099    138   1458       C  
ATOM   2036  O   ILE A 320     -37.245 -17.881  55.146  1.00 92.14           O  
ANISOU 2036  O   ILE A 320    12060  14234   8712   1028    126   1427       O  
ATOM   2037  CB  ILE A 320     -39.303 -15.724  56.755  1.00 95.20           C  
ANISOU 2037  CB  ILE A 320    12459  14839   8870   1575    283   1715       C  
ATOM   2038  CG1 ILE A 320     -40.714 -15.209  56.564  1.00 99.05           C  
ANISOU 2038  CG1 ILE A 320    12784  15713   9136   1796    344   1873       C  
ATOM   2039  CG2 ILE A 320     -38.393 -14.817  55.908  1.00 93.60           C  
ANISOU 2039  CG2 ILE A 320    12395  14437   8731   1679    340   1744       C  
ATOM   2040  CD1 ILE A 320     -40.987 -13.913  57.302  1.00103.20           C  
ANISOU 2040  CD1 ILE A 320    13464  16119   9626   2104    455   1992       C  
ATOM   2041  N   VAL A 321     -37.120 -17.889  57.384  1.00 91.80           N  
ANISOU 2041  N   VAL A 321    12183  13911   8785   1036    114   1384       N  
ATOM   2042  CA  VAL A 321     -35.695 -18.201  57.397  1.00 90.00           C  
ANISOU 2042  CA  VAL A 321    12087  13382   8724    917     80   1278       C  
ATOM   2043  C   VAL A 321     -35.409 -19.617  56.933  1.00 88.39           C  
ANISOU 2043  C   VAL A 321    11824  13212   8547    689     15   1170       C  
ATOM   2044  O   VAL A 321     -34.605 -19.802  56.014  1.00 92.78           O  
ANISOU 2044  O   VAL A 321    12395  13702   9152    631      7   1125       O  
ATOM   2045  CB  VAL A 321     -35.088 -17.889  58.779  1.00 91.57           C  
ANISOU 2045  CB  VAL A 321    12444  13314   9034    936     82   1247       C  
ATOM   2046  CG1 VAL A 321     -33.749 -18.565  59.015  1.00 91.20           C  
ANISOU 2046  CG1 VAL A 321    12485  13034   9132    784     31   1134       C  
ATOM   2047  CG2 VAL A 321     -34.963 -16.373  58.962  1.00 93.28           C  
ANISOU 2047  CG2 VAL A 321    12791  13410   9239   1138    169   1333       C  
ATOM   2048  N   TYR A 322     -36.063 -20.615  57.496  1.00 87.17           N  
ANISOU 2048  N   TYR A 322    11615  13158   8345    556    -19   1126       N  
ATOM   2049  CA  TYR A 322     -35.732 -22.011  57.164  1.00 89.42           C  
ANISOU 2049  CA  TYR A 322    11907  13417   8652    332    -59   1014       C  
ATOM   2050  C   TYR A 322     -36.078 -22.425  55.721  1.00 90.61           C  
ANISOU 2050  C   TYR A 322    11944  13789   8693    235    -54   1002       C  
ATOM   2051  O   TYR A 322     -35.262 -23.071  55.058  1.00 88.65           O  
ANISOU 2051  O   TYR A 322    11753  13426   8504    127    -64    921       O  
ATOM   2052  CB  TYR A 322     -36.427 -22.953  58.135  1.00 92.02           C  
ANISOU 2052  CB  TYR A 322    12231  13796   8934    198    -84    974       C  
ATOM   2053  CG  TYR A 322     -36.112 -24.410  57.914  1.00 93.86           C  
ANISOU 2053  CG  TYR A 322    12527  13960   9176    -29   -102    860       C  
ATOM   2054  CD1 TYR A 322     -34.982 -24.996  58.504  1.00 93.50           C  
ANISOU 2054  CD1 TYR A 322    12639  13614   9272    -60   -115    788       C  
ATOM   2055  CD2 TYR A 322     -36.931 -25.208  57.110  1.00 95.70           C  
ANISOU 2055  CD2 TYR A 322    12672  14433   9256   -212    -96    826       C  
ATOM   2056  CE1 TYR A 322     -34.682 -26.346  58.305  1.00 93.30           C  
ANISOU 2056  CE1 TYR A 322    12708  13498   9241   -238   -110    692       C  
ATOM   2057  CE2 TYR A 322     -36.640 -26.551  56.896  1.00 96.00           C  
ANISOU 2057  CE2 TYR A 322    12816  14373   9286   -430    -90    715       C  
ATOM   2058  CZ  TYR A 322     -35.520 -27.121  57.501  1.00 94.20           C  
ANISOU 2058  CZ  TYR A 322    12770  13813   9206   -427    -92    652       C  
ATOM   2059  OH  TYR A 322     -35.245 -28.439  57.309  1.00 92.96           O  
ANISOU 2059  OH  TYR A 322    12751  13540   9030   -609    -66    553       O  
ATOM   2060  N   TYR A 323     -37.275 -22.050  55.238  1.00 94.40           N  
ANISOU 2060  N   TYR A 323    12260  14603   9003    279    -35   1087       N  
ATOM   2061  CA  TYR A 323     -37.653 -22.341  53.850  1.00 97.20           C  
ANISOU 2061  CA  TYR A 323    12486  15214   9232    187    -28   1086       C  
ATOM   2062  C   TYR A 323     -36.650 -21.684  52.907  1.00 97.42           C  
ANISOU 2062  C   TYR A 323    12562  15101   9349    292    -12   1098       C  
ATOM   2063  O   TYR A 323     -36.120 -22.342  51.986  1.00 98.76           O  
ANISOU 2063  O   TYR A 323    12742  15249   9532    155    -21   1019       O  
ATOM   2064  CB  TYR A 323     -39.066 -21.850  53.519  1.00102.04           C  
ANISOU 2064  CB  TYR A 323    12888  16251   9628    265     -6   1204       C  
ATOM   2065  CG  TYR A 323     -39.563 -22.240  52.117  1.00107.50           C  
ANISOU 2065  CG  TYR A 323    13418  17272  10155    136     -3   1201       C  
ATOM   2066  CD1 TYR A 323     -40.251 -23.441  51.891  1.00108.19           C  
ANISOU 2066  CD1 TYR A 323    13424  17587  10096   -155    -21   1119       C  
ATOM   2067  CD2 TYR A 323     -39.344 -21.401  51.021  1.00109.89           C  
ANISOU 2067  CD2 TYR A 323    13659  17658  10433    289     25   1280       C  
ATOM   2068  CE1 TYR A 323     -40.693 -23.806  50.633  1.00108.46           C  
ANISOU 2068  CE1 TYR A 323    13314  17933   9963   -303    -15   1107       C  
ATOM   2069  CE2 TYR A 323     -39.770 -21.777  49.762  1.00111.13           C  
ANISOU 2069  CE2 TYR A 323    13663  18124  10435    162     26   1274       C  
ATOM   2070  CZ  TYR A 323     -40.447 -22.988  49.583  1.00110.57           C  
ANISOU 2070  CZ  TYR A 323    13505  18287  10216   -141      4   1184       C  
ATOM   2071  OH  TYR A 323     -40.863 -23.369  48.341  1.00111.89           O  
ANISOU 2071  OH  TYR A 323    13525  18773  10213   -297      9   1170       O  
ATOM   2072  N   ALA A 324     -36.385 -20.391  53.136  1.00 95.10           N  
ANISOU 2072  N   ALA A 324    12317  14707   9109    527     21   1193       N  
ATOM   2073  CA  ALA A 324     -35.428 -19.641  52.309  1.00 96.31           C  
ANISOU 2073  CA  ALA A 324    12533  14721   9339    624     45   1213       C  
ATOM   2074  C   ALA A 324     -34.037 -20.271  52.342  1.00 95.66           C  
ANISOU 2074  C   ALA A 324    12581  14344   9418    501     13   1091       C  
ATOM   2075  O   ALA A 324     -33.379 -20.372  51.323  1.00 96.20           O  
ANISOU 2075  O   ALA A 324    12647  14394   9510    460     13   1059       O  
ATOM   2076  CB  ALA A 324     -35.365 -18.166  52.737  1.00 95.44           C  
ANISOU 2076  CB  ALA A 324    12508  14504   9249    873    104   1326       C  
ATOM   2077  N   LEU A 325     -33.607 -20.666  53.531  1.00 97.21           N  
ANISOU 2077  N   LEU A 325    12885  14335   9715    458    -10   1034       N  
ATOM   2078  CA  LEU A 325     -32.350 -21.378  53.679  1.00 98.29           C  
ANISOU 2078  CA  LEU A 325    13129  14233   9981    360    -38    932       C  
ATOM   2079  C   LEU A 325     -32.312 -22.696  52.905  1.00 98.05           C  
ANISOU 2079  C   LEU A 325    13074  14265   9914    181    -52    839       C  
ATOM   2080  O   LEU A 325     -31.363 -22.927  52.154  1.00 99.46           O  
ANISOU 2080  O   LEU A 325    13290  14354  10147    153    -51    791       O  
ATOM   2081  CB  LEU A 325     -32.099 -21.673  55.169  1.00 99.75           C  
ANISOU 2081  CB  LEU A 325    13411  14240  10247    349    -58    900       C  
ATOM   2082  CG  LEU A 325     -30.841 -22.442  55.596  1.00 98.68           C  
ANISOU 2082  CG  LEU A 325    13383  13880  10229    281    -83    813       C  
ATOM   2083  CD1 LEU A 325     -29.680 -21.460  55.736  1.00 99.67           C  
ANISOU 2083  CD1 LEU A 325    13573  13852  10445    375    -76    834       C  
ATOM   2084  CD2 LEU A 325     -31.075 -23.179  56.893  1.00 98.27           C  
ANISOU 2084  CD2 LEU A 325    13388  13750  10199    228   -103    782       C  
ATOM   2085  N   MET A 326     -33.289 -23.573  53.132  1.00 96.93           N  
ANISOU 2085  N   MET A 326    12889  14264   9673     50    -58    810       N  
ATOM   2086  CA  MET A 326     -33.312 -24.847  52.420  1.00 98.36           C  
ANISOU 2086  CA  MET A 326    13088  14487   9796   -148    -53    712       C  
ATOM   2087  C   MET A 326     -33.495 -24.724  50.892  1.00 97.51           C  
ANISOU 2087  C   MET A 326    12874  14580   9592   -189    -37    717       C  
ATOM   2088  O   MET A 326     -32.889 -25.486  50.150  1.00 96.33           O  
ANISOU 2088  O   MET A 326    12785  14359   9453   -296    -24    633       O  
ATOM   2089  CB  MET A 326     -34.356 -25.800  53.010  1.00101.14           C  
ANISOU 2089  CB  MET A 326    13437  14952  10039   -318    -53    674       C  
ATOM   2090  CG  MET A 326     -33.938 -26.385  54.339  1.00104.74           C  
ANISOU 2090  CG  MET A 326    14039  15163  10592   -332    -63    632       C  
ATOM   2091  SD  MET A 326     -32.269 -27.100  54.294  1.00106.06           S  
ANISOU 2091  SD  MET A 326    14393  14993  10910   -316    -51    547       S  
ATOM   2092  CE  MET A 326     -31.772 -26.882  56.019  1.00109.92           C  
ANISOU 2092  CE  MET A 326    14969  15269  11524   -198    -77    576       C  
ATOM   2093  N   ALA A 327     -34.297 -23.779  50.415  1.00 95.22           N  
ANISOU 2093  N   ALA A 327    12434  14541   9203    -91    -29    820       N  
ATOM   2094  CA  ALA A 327     -34.419 -23.587  48.970  1.00 93.08           C  
ANISOU 2094  CA  ALA A 327    12053  14471   8839   -112    -14    838       C  
ATOM   2095  C   ALA A 327     -33.087 -23.128  48.350  1.00 92.19           C  
ANISOU 2095  C   ALA A 327    12018  14151   8859    -19     -9    826       C  
ATOM   2096  O   ALA A 327     -32.672 -23.569  47.265  1.00 90.76           O  
ANISOU 2096  O   ALA A 327    11826  14001   8656   -109     -1    769       O  
ATOM   2097  CB  ALA A 327     -35.514 -22.582  48.684  1.00 93.50           C  
ANISOU 2097  CB  ALA A 327    11932  14838   8752     23      0    976       C  
ATOM   2098  N   GLY A 328     -32.411 -22.235  49.055  1.00 91.92           N  
ANISOU 2098  N   GLY A 328    12062  13914   8948    146    -10    875       N  
ATOM   2099  CA  GLY A 328     -31.104 -21.746  48.626  1.00 91.91           C  
ANISOU 2099  CA  GLY A 328    12135  13724   9062    217     -6    865       C  
ATOM   2100  C   GLY A 328     -30.035 -22.806  48.538  1.00 93.12           C  
ANISOU 2100  C   GLY A 328    12384  13697   9300    106    -19    747       C  
ATOM   2101  O   GLY A 328     -29.139 -22.723  47.724  1.00 93.22           O  
ANISOU 2101  O   GLY A 328    12409  13658   9352    115    -13    723       O  
ATOM   2102  N   PHE A 329     -30.115 -23.800  49.400  1.00 96.76           N  
ANISOU 2102  N   PHE A 329    12921  14061   9781     17    -29    680       N  
ATOM   2103  CA  PHE A 329     -29.203 -24.914  49.322  1.00 99.69           C  
ANISOU 2103  CA  PHE A 329    13402  14269  10207    -62    -23    579       C  
ATOM   2104  C   PHE A 329     -29.442 -25.828  48.111  1.00100.80           C  
ANISOU 2104  C   PHE A 329    13530  14518  10248   -211      5    505       C  
ATOM   2105  O   PHE A 329     -28.495 -26.369  47.541  1.00 95.77           O  
ANISOU 2105  O   PHE A 329    12966  13772   9650   -225     24    442       O  
ATOM   2106  CB  PHE A 329     -29.295 -25.736  50.598  1.00102.43           C  
ANISOU 2106  CB  PHE A 329    13855  14477  10586   -106    -27    539       C  
ATOM   2107  CG  PHE A 329     -28.547 -25.162  51.766  1.00103.84           C  
ANISOU 2107  CG  PHE A 329    14085  14487  10882     20    -50    576       C  
ATOM   2108  CD1 PHE A 329     -27.264 -24.647  51.636  1.00104.65           C  
ANISOU 2108  CD1 PHE A 329    14206  14482  11071    114    -56    584       C  
ATOM   2109  CD2 PHE A 329     -29.103 -25.240  53.031  1.00108.33           C  
ANISOU 2109  CD2 PHE A 329    14684  15018  11458     22    -64    594       C  
ATOM   2110  CE1 PHE A 329     -26.574 -24.195  52.752  1.00106.88           C  
ANISOU 2110  CE1 PHE A 329    14534  14638  11437    194    -75    610       C  
ATOM   2111  CE2 PHE A 329     -28.425 -24.773  54.147  1.00106.60           C  
ANISOU 2111  CE2 PHE A 329    14515  14655  11333    117    -83    621       C  
ATOM   2112  CZ  PHE A 329     -27.153 -24.258  54.010  1.00105.83           C  
ANISOU 2112  CZ  PHE A 329    14433  14464  11312    195    -88    627       C  
ATOM   2113  N   VAL A 330     -30.711 -26.048  47.769  1.00105.29           N  
ANISOU 2113  N   VAL A 330    14013  15316  10675   -331     12    510       N  
ATOM   2114  CA  VAL A 330     -31.038 -26.884  46.594  1.00109.38           C  
ANISOU 2114  CA  VAL A 330    14518  15972  11070   -512     45    433       C  
ATOM   2115  C   VAL A 330     -30.808 -26.101  45.298  1.00106.84           C  
ANISOU 2115  C   VAL A 330    14073  15797  10721   -448     44    478       C  
ATOM   2116  O   VAL A 330     -30.291 -26.689  44.322  1.00106.43           O  
ANISOU 2116  O   VAL A 330    14062  15727  10647   -532     71    402       O  
ATOM   2117  CB  VAL A 330     -32.428 -27.584  46.634  1.00115.30           C  
ANISOU 2117  CB  VAL A 330    15221  16944  11642   -722     59    403       C  
ATOM   2118  CG1 VAL A 330     -32.432 -28.743  47.625  1.00119.18           C  
ANISOU 2118  CG1 VAL A 330    15896  17239  12146   -844     82    318       C  
ATOM   2119  CG2 VAL A 330     -33.534 -26.613  46.985  1.00120.63           C  
ANISOU 2119  CG2 VAL A 330    15715  17878  12240   -643     29    522       C  
ATOM   2120  N   TRP A 331     -31.079 -24.786  45.309  1.00100.70           N  
ANISOU 2120  N   TRP A 331    13176  15132   9952   -286     23    599       N  
ATOM   2121  CA  TRP A 331     -30.637 -23.945  44.188  1.00 98.96           C  
ANISOU 2121  CA  TRP A 331    12875  14991   9731   -194     28    652       C  
ATOM   2122  C   TRP A 331     -29.108 -23.947  44.001  1.00 98.14           C  
ANISOU 2122  C   TRP A 331    12878  14640   9768   -134     29    605       C  
ATOM   2123  O   TRP A 331     -28.624 -23.817  42.893  1.00100.29           O  
ANISOU 2123  O   TRP A 331    13113  14965  10026   -138     40    595       O  
ATOM   2124  CB  TRP A 331     -31.148 -22.530  44.300  1.00 99.67           C  
ANISOU 2124  CB  TRP A 331    12867  15201   9799    -12     27    797       C  
ATOM   2125  CG  TRP A 331     -32.558 -22.389  43.838  1.00105.74           C  
ANISOU 2125  CG  TRP A 331    13468  16325  10382    -41     36    867       C  
ATOM   2126  CD1 TRP A 331     -33.638 -22.118  44.604  1.00109.59           C  
ANISOU 2126  CD1 TRP A 331    13887  16962  10789      6     35    940       C  
ATOM   2127  CD2 TRP A 331     -33.046 -22.475  42.493  1.00109.73           C  
ANISOU 2127  CD2 TRP A 331    13831  17121  10738   -117     50    879       C  
ATOM   2128  NE1 TRP A 331     -34.776 -22.032  43.835  1.00110.58           N  
ANISOU 2128  NE1 TRP A 331    13824  17475  10715    -28     47   1004       N  
ATOM   2129  CE2 TRP A 331     -34.441 -22.253  42.534  1.00109.35           C  
ANISOU 2129  CE2 TRP A 331    13618  17416  10512   -111     55    967       C  
ATOM   2130  CE3 TRP A 331     -32.442 -22.732  41.260  1.00112.94           C  
ANISOU 2130  CE3 TRP A 331    14224  17552  11134   -191     59    825       C  
ATOM   2131  CZ2 TRP A 331     -35.240 -22.272  41.397  1.00112.03           C  
ANISOU 2131  CZ2 TRP A 331    13771  18137  10655   -181     66   1007       C  
ATOM   2132  CZ3 TRP A 331     -33.249 -22.759  40.119  1.00114.79           C  
ANISOU 2132  CZ3 TRP A 331    14287  18144  11183   -270     71    856       C  
ATOM   2133  CH2 TRP A 331     -34.632 -22.532  40.200  1.00113.18           C  
ANISOU 2133  CH2 TRP A 331    13910  18294  10795   -268     73    948       C  
ATOM   2134  N   PHE A 332     -28.347 -24.106  45.080  1.00 99.41           N  
ANISOU 2134  N   PHE A 332    13157  14561  10052    -80     17    581       N  
ATOM   2135  CA  PHE A 332     -26.896 -24.296  44.989  1.00 98.78           C  
ANISOU 2135  CA  PHE A 332    13162  14289  10077    -35     20    533       C  
ATOM   2136  C   PHE A 332     -26.569 -25.602  44.293  1.00101.61           C  
ANISOU 2136  C   PHE A 332    13589  14618  10397   -152     52    423       C  
ATOM   2137  O   PHE A 332     -25.664 -25.654  43.447  1.00107.77           O  
ANISOU 2137  O   PHE A 332    14373  15374  11198   -129     66    394       O  
ATOM   2138  CB  PHE A 332     -26.222 -24.213  46.365  1.00 98.70           C  
ANISOU 2138  CB  PHE A 332    13244  14078  10179     45      1    540       C  
ATOM   2139  CG  PHE A 332     -24.870 -24.846  46.414  1.00101.34           C  
ANISOU 2139  CG  PHE A 332    13662  14258  10585     71      9    479       C  
ATOM   2140  CD1 PHE A 332     -23.758 -24.174  45.938  1.00100.41           C  
ANISOU 2140  CD1 PHE A 332    13513  14125  10513    144      3    501       C  
ATOM   2141  CD2 PHE A 332     -24.703 -26.147  46.937  1.00106.97           C  
ANISOU 2141  CD2 PHE A 332    14491  14850  11301     30     32    406       C  
ATOM   2142  CE1 PHE A 332     -22.502 -24.781  45.987  1.00103.04           C  
ANISOU 2142  CE1 PHE A 332    13899  14362  10889    185     13    455       C  
ATOM   2143  CE2 PHE A 332     -23.446 -26.775  46.966  1.00106.87           C  
ANISOU 2143  CE2 PHE A 332    14555  14714  11333     95     53    365       C  
ATOM   2144  CZ  PHE A 332     -22.338 -26.080  46.506  1.00104.92           C  
ANISOU 2144  CZ  PHE A 332    14246  14490  11129    179     39    393       C  
ATOM   2145  N   VAL A 333     -27.299 -26.664  44.608  1.00103.38           N  
ANISOU 2145  N   VAL A 333    13883  14842  10553   -284     74    358       N  
ATOM   2146  CA  VAL A 333     -27.041 -27.948  43.950  1.00107.29           C  
ANISOU 2146  CA  VAL A 333    14493  15280  10991   -408    129    245       C  
ATOM   2147  C   VAL A 333     -27.406 -27.797  42.487  1.00108.30           C  
ANISOU 2147  C   VAL A 333    14515  15620  11012   -500    143    232       C  
ATOM   2148  O   VAL A 333     -26.662 -28.277  41.614  1.00112.95           O  
ANISOU 2148  O   VAL A 333    15159  16159  11595   -518    179    168       O  
ATOM   2149  CB  VAL A 333     -27.790 -29.154  44.577  1.00110.25           C  
ANISOU 2149  CB  VAL A 333    15003  15595  11291   -567    167    171       C  
ATOM   2150  CG1 VAL A 333     -27.534 -30.466  43.833  1.00108.33           C  
ANISOU 2150  CG1 VAL A 333    14926  15266  10968   -706    249     49       C  
ATOM   2151  CG2 VAL A 333     -27.357 -29.361  46.020  1.00114.26           C  
ANISOU 2151  CG2 VAL A 333    15622  15888  11904   -465    157    187       C  
ATOM   2152  N   VAL A 334     -28.510 -27.124  42.209  1.00105.93           N  
ANISOU 2152  N   VAL A 334    14058  15569  10620   -541    118    299       N  
ATOM   2153  CA  VAL A 334     -28.892 -26.857  40.814  1.00109.21           C  
ANISOU 2153  CA  VAL A 334    14342  16230  10920   -611    127    307       C  
ATOM   2154  C   VAL A 334     -27.793 -26.067  40.052  1.00108.94           C  
ANISOU 2154  C   VAL A 334    14266  16151  10972   -466    117    347       C  
ATOM   2155  O   VAL A 334     -27.531 -26.329  38.849  1.00112.59           O  
ANISOU 2155  O   VAL A 334    14703  16700  11375   -534    142    300       O  
ATOM   2156  CB  VAL A 334     -30.262 -26.151  40.747  1.00108.78           C  
ANISOU 2156  CB  VAL A 334    14105  16486  10741   -630    103    404       C  
ATOM   2157  CG1 VAL A 334     -30.523 -25.566  39.371  1.00108.05           C  
ANISOU 2157  CG1 VAL A 334    13849  16660  10543   -632    106    453       C  
ATOM   2158  CG2 VAL A 334     -31.363 -27.129  41.148  1.00109.00           C  
ANISOU 2158  CG2 VAL A 334    14155  16628  10631   -845    122    340       C  
ATOM   2159  N   LEU A 335     -27.145 -25.134  40.756  1.00104.76           N  
ANISOU 2159  N   LEU A 335    13739  15492  10571   -288     86    425       N  
ATOM   2160  CA  LEU A 335     -25.979 -24.456  40.205  1.00101.73           C  
ANISOU 2160  CA  LEU A 335    13343  15042  10267   -176     81    452       C  
ATOM   2161  C   LEU A 335     -24.824 -25.435  39.924  1.00100.35           C  
ANISOU 2161  C   LEU A 335    13279  14710  10137   -198    109    348       C  
ATOM   2162  O   LEU A 335     -24.208 -25.363  38.872  1.00 97.74           O  
ANISOU 2162  O   LEU A 335    12915  14427   9792   -195    122    329       O  
ATOM   2163  CB  LEU A 335     -25.535 -23.350  41.146  1.00102.65           C  
ANISOU 2163  CB  LEU A 335    13469  15044  10488    -25     53    541       C  
ATOM   2164  CG  LEU A 335     -24.395 -22.442  40.673  1.00103.85           C  
ANISOU 2164  CG  LEU A 335    13607  15147  10702     67     50    582       C  
ATOM   2165  CD1 LEU A 335     -24.582 -20.998  41.139  1.00104.28           C  
ANISOU 2165  CD1 LEU A 335    13646  15195  10778    176     44    699       C  
ATOM   2166  CD2 LEU A 335     -23.030 -22.970  41.136  1.00101.80           C  
ANISOU 2166  CD2 LEU A 335    13434  14710  10535     93     46    518       C  
ATOM   2167  N   THR A 336     -24.527 -26.347  40.845  1.00100.52           N  
ANISOU 2167  N   THR A 336    13438  14552  10204   -204    124    287       N  
ATOM   2168  CA  THR A 336     -23.443 -27.319  40.606  1.00105.26           C  
ANISOU 2168  CA  THR A 336    14159  15005  10828   -184    169    203       C  
ATOM   2169  C   THR A 336     -23.779 -28.356  39.528  1.00106.91           C  
ANISOU 2169  C   THR A 336    14432  15266  10921   -333    231    101       C  
ATOM   2170  O   THR A 336     -22.863 -28.922  38.931  1.00106.96           O  
ANISOU 2170  O   THR A 336    14513  15197  10929   -298    276     44       O  
ATOM   2171  CB  THR A 336     -23.024 -28.111  41.870  1.00105.54           C  
ANISOU 2171  CB  THR A 336    14346  14831  10924   -127    186    174       C  
ATOM   2172  OG1 THR A 336     -24.121 -28.898  42.353  1.00107.95           O  
ANISOU 2172  OG1 THR A 336    14740  15115  11161   -260    211    129       O  
ATOM   2173  CG2 THR A 336     -22.552 -27.196  42.941  1.00102.60           C  
ANISOU 2173  CG2 THR A 336    13923  14405  10654      1    131    258       C  
ATOM   2174  N   TYR A 337     -25.065 -28.639  39.343  1.00108.03           N  
ANISOU 2174  N   TYR A 337    14552  15542  10951   -502    240     78       N  
ATOM   2175  CA  TYR A 337     -25.503 -29.506  38.272  1.00115.76           C  
ANISOU 2175  CA  TYR A 337    15579  16612  11791   -689    301    -19       C  
ATOM   2176  C   TYR A 337     -25.430 -28.772  36.920  1.00121.46           C  
ANISOU 2176  C   TYR A 337    16135  17547  12466   -692    283     12       C  
ATOM   2177  O   TYR A 337     -24.974 -29.378  35.896  1.00135.26           O  
ANISOU 2177  O   TYR A 337    17940  19295  14157   -757    336    -70       O  
ATOM   2178  CB  TYR A 337     -26.916 -29.975  38.528  1.00120.19           C  
ANISOU 2178  CB  TYR A 337    16143  17300  12221   -896    313    -49       C  
ATOM   2179  CG  TYR A 337     -27.500 -30.798  37.413  1.00127.88           C  
ANISOU 2179  CG  TYR A 337    17154  18415  13017  -1141    376   -153       C  
ATOM   2180  CD1 TYR A 337     -27.209 -32.156  37.299  1.00130.64           C  
ANISOU 2180  CD1 TYR A 337    17759  18569  13308  -1266    475   -288       C  
ATOM   2181  CD2 TYR A 337     -28.363 -30.215  36.473  1.00131.57           C  
ANISOU 2181  CD2 TYR A 337    17412  19220  13357  -1249    347   -115       C  
ATOM   2182  CE1 TYR A 337     -27.732 -32.915  36.263  1.00136.44           C  
ANISOU 2182  CE1 TYR A 337    18553  19423  13862  -1522    546   -397       C  
ATOM   2183  CE2 TYR A 337     -28.886 -30.953  35.451  1.00137.83           C  
ANISOU 2183  CE2 TYR A 337    18228  20172  13970  -1496    405   -214       C  
ATOM   2184  CZ  TYR A 337     -28.572 -32.303  35.337  1.00140.44           C  
ANISOU 2184  CZ  TYR A 337    18826  20291  14244  -1650    505   -363       C  
ATOM   2185  OH  TYR A 337     -29.100 -33.029  34.282  1.00145.00           O  
ANISOU 2185  OH  TYR A 337    19445  21026  14622  -1928    573   -474       O  
ATOM   2186  N   ALA A 338     -25.839 -27.484  36.926  1.00118.03           N  
ANISOU 2186  N   ALA A 338    15515  17279  12052   -609    219    134       N  
ATOM   2187  CA  ALA A 338     -25.728 -26.621  35.731  1.00113.51           C  
ANISOU 2187  CA  ALA A 338    14785  16900  11442   -575    202    191       C  
ATOM   2188  C   ALA A 338     -24.313 -26.564  35.222  1.00113.77           C  
ANISOU 2188  C   ALA A 338    14860  16805  11561   -472    214    167       C  
ATOM   2189  O   ALA A 338     -24.073 -26.632  34.024  1.00127.33           O  
ANISOU 2189  O   ALA A 338    16530  18632  13217   -520    235    136       O  
ATOM   2190  CB  ALA A 338     -26.187 -25.210  36.043  1.00111.07           C  
ANISOU 2190  CB  ALA A 338    14331  16709  11159   -447    151    339       C  
ATOM   2191  N   TRP A 339     -23.372 -26.450  36.147  1.00115.71           N  
ANISOU 2191  N   TRP A 339    15184  16843  11936   -334    200    183       N  
ATOM   2192  CA  TRP A 339     -21.942 -26.416  35.856  1.00116.98           C  
ANISOU 2192  CA  TRP A 339    15372  16903  12169   -223    209    169       C  
ATOM   2193  C   TRP A 339     -21.412 -27.775  35.347  1.00116.62           C  
ANISOU 2193  C   TRP A 339    15469  16764  12078   -270    282     46       C  
ATOM   2194  O   TRP A 339     -20.622 -27.813  34.416  1.00123.30           O  
ANISOU 2194  O   TRP A 339    16293  17645  12910   -238    304     20       O  
ATOM   2195  CB  TRP A 339     -21.131 -25.911  37.091  1.00117.34           C  
ANISOU 2195  CB  TRP A 339    15446  16799  12339    -77    174    227       C  
ATOM   2196  CG  TRP A 339     -19.692 -25.750  36.804  1.00118.23           C  
ANISOU 2196  CG  TRP A 339    15547  16873  12499     25    177    227       C  
ATOM   2197  CD1 TRP A 339     -19.113 -24.783  35.998  1.00124.39           C  
ANISOU 2197  CD1 TRP A 339    16215  17763  13281     54    156    279       C  
ATOM   2198  CD2 TRP A 339     -18.647 -26.598  37.215  1.00113.06           C  
ANISOU 2198  CD2 TRP A 339    14990  16093  11875    114    210    179       C  
ATOM   2199  NE1 TRP A 339     -17.736 -24.980  35.900  1.00122.28           N  
ANISOU 2199  NE1 TRP A 339    15955  17462  13041    140    167    259       N  
ATOM   2200  CE2 TRP A 339     -17.428 -26.091  36.643  1.00116.60           C  
ANISOU 2200  CE2 TRP A 339    15355  16609  12337    193    201    203       C  
ATOM   2201  CE3 TRP A 339     -18.614 -27.751  37.965  1.00108.02           C  
ANISOU 2201  CE3 TRP A 339    14503  15302  11237    142    255    122       C  
ATOM   2202  CZ2 TRP A 339     -16.222 -26.699  36.836  1.00113.56           C  
ANISOU 2202  CZ2 TRP A 339    15013  16174  11960    310    231    179       C  
ATOM   2203  CZ3 TRP A 339     -17.453 -28.317  38.167  1.00112.27           C  
ANISOU 2203  CZ3 TRP A 339    15101  15766  11790    273    290    106       C  
ATOM   2204  CH2 TRP A 339     -16.245 -27.811  37.591  1.00115.08           C  
ANISOU 2204  CH2 TRP A 339    15351  16222  12152    364    278    135       C  
ATOM   2205  N   HIS A 340     -21.859 -28.873  35.928  1.00117.56           N  
ANISOU 2205  N   HIS A 340    15746  16759  12161   -344    331    -28       N  
ATOM   2206  CA  HIS A 340     -21.423 -30.210  35.502  1.00123.94           C  
ANISOU 2206  CA  HIS A 340    16744  17438  12907   -384    427   -145       C  
ATOM   2207  C   HIS A 340     -21.926 -30.553  34.140  1.00126.38           C  
ANISOU 2207  C   HIS A 340    17038  17894  13084   -558    471   -219       C  
ATOM   2208  O   HIS A 340     -21.173 -31.140  33.341  1.00128.18           O  
ANISOU 2208  O   HIS A 340    17352  18073  13277   -535    537   -289       O  
ATOM   2209  CB  HIS A 340     -21.933 -31.262  36.479  1.00131.41           C  
ANISOU 2209  CB  HIS A 340    17892  18207  13828   -448    480   -203       C  
ATOM   2210  CG  HIS A 340     -21.986 -32.670  35.939  1.00137.44           C  
ANISOU 2210  CG  HIS A 340    18894  18850  14475   -568    603   -336       C  
ATOM   2211  ND1 HIS A 340     -20.869 -33.458  35.762  1.00138.17           N  
ANISOU 2211  ND1 HIS A 340    19160  18764  14574   -429    691   -385       N  
ATOM   2212  CD2 HIS A 340     -23.047 -33.444  35.594  1.00141.89           C  
ANISOU 2212  CD2 HIS A 340    19570  19444  14896   -822    664   -430       C  
ATOM   2213  CE1 HIS A 340     -21.240 -34.650  35.321  1.00141.62           C  
ANISOU 2213  CE1 HIS A 340    19833  19091  14882   -583    810   -505       C  
ATOM   2214  NE2 HIS A 340     -22.557 -34.675  35.229  1.00140.53           N  
ANISOU 2214  NE2 HIS A 340    19666  19076  14650   -843    795   -541       N  
ATOM   2215  N   THR A 341     -23.202 -30.219  33.874  1.00129.45           N  
ANISOU 2215  N   THR A 341    17316  18483  13384   -728    439   -203       N  
ATOM   2216  CA  THR A 341     -23.764 -30.493  32.532  1.00131.69           C  
ANISOU 2216  CA  THR A 341    17553  18965  13515   -920    476   -269       C  
ATOM   2217  C   THR A 341     -23.367 -29.473  31.452  1.00127.85           C  
ANISOU 2217  C   THR A 341    16864  18672  13038   -849    430   -200       C  
ATOM   2218  O   THR A 341     -23.542 -29.744  30.290  1.00140.19           O  
ANISOU 2218  O   THR A 341    18399  20379  14488   -976    465   -259       O  
ATOM   2219  CB  THR A 341     -25.297 -30.621  32.573  1.00133.43           C  
ANISOU 2219  CB  THR A 341    17714  19387  13594  -1148    468   -280       C  
ATOM   2220  OG1 THR A 341     -25.878 -29.407  33.106  1.00137.89           O  
ANISOU 2220  OG1 THR A 341    18075  20107  14210  -1054    376   -137       O  
ATOM   2221  CG2 THR A 341     -25.676 -31.819  33.422  1.00130.89           C  
ANISOU 2221  CG2 THR A 341    17630  18872  13229  -1275    536   -376       C  
ATOM   2222  N   SER A 342     -22.831 -28.317  31.823  1.00123.81           N  
ANISOU 2222  N   SER A 342    16228  18163  12650   -661    358    -81       N  
ATOM   2223  CA  SER A 342     -22.369 -27.335  30.857  1.00125.82           C  
ANISOU 2223  CA  SER A 342    16322  18570  12914   -591    324    -11       C  
ATOM   2224  C   SER A 342     -21.225 -27.879  29.976  1.00134.25           C  
ANISOU 2224  C   SER A 342    17454  19576  13978   -560    376    -91       C  
ATOM   2225  O   SER A 342     -21.122 -27.475  28.802  1.00140.38           O  
ANISOU 2225  O   SER A 342    18117  20523  14696   -592    373    -80       O  
ATOM   2226  CB  SER A 342     -21.937 -26.035  31.547  1.00123.72           C  
ANISOU 2226  CB  SER A 342    15964  18271  12772   -415    257    121       C  
ATOM   2227  OG  SER A 342     -20.796 -26.218  32.370  1.00122.82           O  
ANISOU 2227  OG  SER A 342    15948  17944  12773   -285    258    109       O  
ATOM   2228  N   PHE A 343     -20.406 -28.788  30.534  1.00138.01           N  
ANISOU 2228  N   PHE A 343    18109  19824  14503   -485    428   -162       N  
ATOM   2229  CA  PHE A 343     -19.354 -29.530  29.785  1.00146.67           C  
ANISOU 2229  CA  PHE A 343    19305  20848  15574   -434    501   -245       C  
ATOM   2230  C   PHE A 343     -19.874 -30.660  28.885  1.00156.83           C  
ANISOU 2230  C   PHE A 343    20727  22147  16711   -623    596   -381       C  
ATOM   2231  O   PHE A 343     -19.239 -30.984  27.900  1.00174.36           O  
ANISOU 2231  O   PHE A 343    22973  24392  18881   -614    648   -438       O  
ATOM   2232  CB  PHE A 343     -18.300 -30.181  30.714  1.00143.26           C  
ANISOU 2232  CB  PHE A 343    19031  20181  15220   -254    542   -262       C  
ATOM   2233  CG  PHE A 343     -17.497 -29.205  31.500  1.00137.48           C  
ANISOU 2233  CG  PHE A 343    18179  19445  14611    -79    464   -150       C  
ATOM   2234  CD1 PHE A 343     -16.528 -28.433  30.899  1.00136.16           C  
ANISOU 2234  CD1 PHE A 343    17872  19391  14471     11    431    -97       C  
ATOM   2235  CD2 PHE A 343     -17.711 -29.065  32.839  1.00136.66           C  
ANISOU 2235  CD2 PHE A 343    18108  19234  14582    -27    429   -101       C  
ATOM   2236  CE1 PHE A 343     -15.785 -27.517  31.627  1.00135.47           C  
ANISOU 2236  CE1 PHE A 343    17684  19314  14472    130    366     -2       C  
ATOM   2237  CE2 PHE A 343     -16.989 -28.150  33.582  1.00137.30           C  
ANISOU 2237  CE2 PHE A 343    18086  19322  14758    102    362     -5       C  
ATOM   2238  CZ  PHE A 343     -16.011 -27.371  32.979  1.00134.85           C  
ANISOU 2238  CZ  PHE A 343    17644  19129  14464    172    333     41       C  
ATOM   2239  N   LYS A 344     -20.993 -31.288  29.249  1.00157.63           N  
ANISOU 2239  N   LYS A 344    20928  22231  16730   -805    627   -438       N  
ATOM   2240  CA  LYS A 344     -21.599 -32.355  28.425  1.00158.43           C  
ANISOU 2240  CA  LYS A 344    21176  22359  16660  -1043    726   -577       C  
ATOM   2241  C   LYS A 344     -22.262 -31.793  27.175  1.00164.67           C  
ANISOU 2241  C   LYS A 344    21762  23470  17336  -1207    692   -568       C  
ATOM   2242  O   LYS A 344     -22.400 -32.503  26.175  1.00169.57           O  
ANISOU 2242  O   LYS A 344    22466  24147  17816  -1378    771   -681       O  
ATOM   2243  CB  LYS A 344     -22.605 -33.173  29.210  1.00156.38           C  
ANISOU 2243  CB  LYS A 344    21084  22008  16325  -1223    771   -642       C  
ATOM   2244  CG  LYS A 344     -21.965 -33.927  30.329  1.00159.16           C  
ANISOU 2244  CG  LYS A 344    21678  22032  16760  -1074    831   -664       C  
ATOM   2245  CD  LYS A 344     -22.920 -34.654  31.260  1.00162.91           C  
ANISOU 2245  CD  LYS A 344    22324  22398  17176  -1237    869   -712       C  
ATOM   2246  CE  LYS A 344     -22.151 -35.722  32.040  1.00164.50           C  
ANISOU 2246  CE  LYS A 344    22844  22244  17415  -1097    979   -765       C  
ATOM   2247  NZ  LYS A 344     -23.039 -36.685  32.738  1.00168.00           N  
ANISOU 2247  NZ  LYS A 344    23527  22543  17761  -1298   1056   -843       N  
ATOM   2248  N   ALA A 345     -22.616 -30.505  27.223  1.00168.37           N  
ANISOU 2248  N   ALA A 345    21973  24141  17856  -1140    583   -429       N  
ATOM   2249  CA  ALA A 345     -23.060 -29.751  26.048  1.00175.77           C  
ANISOU 2249  CA  ALA A 345    22687  25394  18702  -1218    543   -379       C  
ATOM   2250  C   ALA A 345     -22.000 -29.770  24.932  1.00184.38           C  
ANISOU 2250  C   ALA A 345    23772  26489  19795  -1155    575   -417       C  
ATOM   2251  O   ALA A 345     -22.340 -29.712  23.755  1.00193.59           O  
ANISOU 2251  O   ALA A 345    24838  27881  20835  -1288    587   -443       O  
ATOM   2252  CB  ALA A 345     -23.383 -28.320  26.454  1.00171.82           C  
ANISOU 2252  CB  ALA A 345    21967  25034  18281  -1080    440   -205       C  
ATOM   2253  N   LEU A 346     -20.731 -29.953  25.307  1.00185.02           N  
ANISOU 2253  N   LEU A 346    23964  26337  19998   -961    597   -427       N  
ATOM   2254  CA  LEU A 346     -19.625 -30.013  24.357  1.00184.74           C  
ANISOU 2254  CA  LEU A 346    23926  26301  19964   -875    631   -460       C  
ATOM   2255  C   LEU A 346     -19.795 -31.172  23.380  1.00186.13           C  
ANISOU 2255  C   LEU A 346    24255  26482  19981  -1057    742   -617       C  
ATOM   2256  O   LEU A 346     -19.223 -31.135  22.300  1.00181.33           O  
ANISOU 2256  O   LEU A 346    23602  25966  19330  -1049    767   -646       O  
ATOM   2257  CB  LEU A 346     -18.292 -30.133  25.087  1.00184.28           C  
ANISOU 2257  CB  LEU A 346    23960  26018  20036   -634    643   -441       C  
ATOM   2258  CG  LEU A 346     -17.945 -29.127  26.157  1.00184.45           C  
ANISOU 2258  CG  LEU A 346    23875  26001  20205   -468    550   -308       C  
ATOM   2259  CD1 LEU A 346     -16.590 -29.435  26.789  1.00182.82           C  
ANISOU 2259  CD1 LEU A 346    23757  25619  20085   -254    575   -305       C  
ATOM   2260  CD2 LEU A 346     -17.976 -27.749  25.576  1.00182.36           C  
ANISOU 2260  CD2 LEU A 346    23378  25948  19961   -454    466   -194       C  
ATOM   2261  N   GLY A 347     -20.597 -32.176  23.745  1.00187.42           N  
ANISOU 2261  N   GLY A 347    24609  26551  20048  -1239    814   -720       N  
ATOM   2262  CA  GLY A 347     -20.985 -33.247  22.823  1.00193.79           C  
ANISOU 2262  CA  GLY A 347    25582  27380  20669  -1481    930   -879       C  
ATOM   2263  C   GLY A 347     -21.886 -32.831  21.668  1.00198.07           C  
ANISOU 2263  C   GLY A 347    25918  28281  21056  -1714    898   -881       C  
ATOM   2264  O   GLY A 347     -22.422 -31.709  21.621  1.00197.21           O  
ANISOU 2264  O   GLY A 347    25535  28423  20971  -1692    786   -748       O  
ATOM   2265  N   THR A 348     -22.061 -33.762  20.740  1.00201.82           N  
ANISOU 2265  N   THR A 348    26542  28782  21358  -1935   1007  -1032       N  
ATOM   2266  CA  THR A 348     -22.926 -33.531  19.598  1.00203.29           C  
ANISOU 2266  CA  THR A 348    26547  29332  21361  -2190    991  -1053       C  
ATOM   2267  C   THR A 348     -24.343 -33.042  19.968  1.00207.20           C  
ANISOU 2267  C   THR A 348    26844  30112  21768  -2362    911   -977       C  
ATOM   2268  O   THR A 348     -24.873 -32.141  19.326  1.00210.41           O  
ANISOU 2268  O   THR A 348    26960  30871  22114  -2390    830   -875       O  
ATOM   2269  CB  THR A 348     -23.036 -34.775  18.695  1.00200.22           C  
ANISOU 2269  CB  THR A 348    26399  28907  20766  -2462   1141  -1254       C  
ATOM   2270  OG1 THR A 348     -24.084 -34.578  17.743  1.00199.78           O  
ANISOU 2270  OG1 THR A 348    26148  29253  20503  -2758   1118  -1273       O  
ATOM   2271  CG2 THR A 348     -23.307 -36.028  19.505  1.00197.23           C  
ANISOU 2271  CG2 THR A 348    26385  28226  20327  -2600   1263  -1388       C  
ATOM   2272  N   THR A 349     -24.955 -33.643  20.976  1.00212.58           N  
ANISOU 2272  N   THR A 349    27682  30659  22429  -2468    940  -1020       N  
ATOM   2273  CA  THR A 349     -26.265 -33.182  21.423  1.00216.95           C  
ANISOU 2273  CA  THR A 349    28041  31492  22897  -2606    865   -939       C  
ATOM   2274  C   THR A 349     -26.095 -32.074  22.449  1.00216.62           C  
ANISOU 2274  C   THR A 349    27842  31398  23065  -2301    749   -756       C  
ATOM   2275  O   THR A 349     -25.413 -32.280  23.440  1.00212.50           O  
ANISOU 2275  O   THR A 349    27490  30540  22709  -2121    759   -754       O  
ATOM   2276  CB  THR A 349     -27.109 -34.312  22.020  1.00221.04           C  
ANISOU 2276  CB  THR A 349    28787  31929  23269  -2899    949  -1071       C  
ATOM   2277  OG1 THR A 349     -28.450 -33.839  22.162  1.00220.70           O  
ANISOU 2277  OG1 THR A 349    28496  32270  23087  -3069    877   -993       O  
ATOM   2278  CG2 THR A 349     -26.571 -34.789  23.372  1.00219.45           C  
ANISOU 2278  CG2 THR A 349    28846  31297  23238  -2728    981  -1083       C  
ATOM   2279  N   TYR A 350     -26.652 -30.900  22.191  1.00214.93           N  
ANISOU 2279  N   TYR A 350    27318  31507  22837  -2231    650   -600       N  
ATOM   2280  CA  TYR A 350     -26.614 -29.807  23.183  1.00211.80           C  
ANISOU 2280  CA  TYR A 350    26796  31063  22615  -1962    554   -426       C  
ATOM   2281  C   TYR A 350     -27.259 -30.094  24.554  1.00205.74           C  
ANISOU 2281  C   TYR A 350    26117  30177  21878  -1987    544   -419       C  
ATOM   2282  O   TYR A 350     -26.690 -29.710  25.559  1.00200.75           O  
ANISOU 2282  O   TYR A 350    25542  29296  21435  -1762    508   -352       O  
ATOM   2283  CB  TYR A 350     -27.177 -28.518  22.588  1.00217.61           C  
ANISOU 2283  CB  TYR A 350    27215  32168  23296  -1877    475   -255       C  
ATOM   2284  CG  TYR A 350     -28.639 -28.570  22.179  1.00229.66           C  
ANISOU 2284  CG  TYR A 350    28558  34128  24573  -2113    471   -238       C  
ATOM   2285  CD1 TYR A 350     -29.661 -28.251  23.080  1.00234.07           C  
ANISOU 2285  CD1 TYR A 350    29205  34810  24919  -2462    545   -405       C  
ATOM   2286  CD2 TYR A 350     -29.005 -28.955  20.884  1.00234.32           C  
ANISOU 2286  CD2 TYR A 350    28888  35025  25117  -1989    401    -49       C  
ATOM   2287  CE1 TYR A 350     -30.985 -28.310  22.708  1.00233.39           C  
ANISOU 2287  CE1 TYR A 350    28926  35171  24578  -2701    538   -388       C  
ATOM   2288  CE2 TYR A 350     -30.339 -29.028  20.507  1.00234.74           C  
ANISOU 2288  CE2 TYR A 350    28739  35535  24916  -2186    397    -16       C  
ATOM   2289  CZ  TYR A 350     -31.325 -28.701  21.421  1.00232.16           C  
ANISOU 2289  CZ  TYR A 350    28475  35357  24375  -2555    460   -188       C  
ATOM   2290  OH  TYR A 350     -32.650 -28.762  21.064  1.00224.20           O  
ANISOU 2290  OH  TYR A 350    27247  34848  23088  -2781    455   -159       O  
ATOM   2291  N   GLN A 351     -28.391 -30.819  24.595  1.00202.25           N  
ANISOU 2291  N   GLN A 351    25686  29919  21241  -2272    578   -491       N  
ATOM   2292  CA  GLN A 351     -29.123 -31.169  25.859  1.00196.94           C  
ANISOU 2292  CA  GLN A 351    25079  29179  20568  -2327    568   -484       C  
ATOM   2293  C   GLN A 351     -29.459 -29.903  26.665  1.00191.85           C  
ANISOU 2293  C   GLN A 351    24268  28551  20075  -2047    470   -295       C  
ATOM   2294  O   GLN A 351     -28.809 -29.660  27.704  1.00185.66           O  
ANISOU 2294  O   GLN A 351    23616  27471  19453  -1902    457   -279       O  
ATOM   2295  CB  GLN A 351     -28.359 -32.209  26.685  1.00198.21           C  
ANISOU 2295  CB  GLN A 351    25590  28909  20811  -2358    650   -621       C  
ATOM   2296  CG  GLN A 351     -28.321 -33.590  26.046  1.00202.11           C  
ANISOU 2296  CG  GLN A 351    26317  29360  21114  -2684    776   -820       C  
ATOM   2297  CD  GLN A 351     -27.752 -34.630  26.979  1.00200.76           C  
ANISOU 2297  CD  GLN A 351    26513  28792  20972  -2746    876   -944       C  
ATOM   2298  OE1 GLN A 351     -27.460 -34.356  28.141  1.00189.19           O  
ANISOU 2298  OE1 GLN A 351    25112  27109  19663  -2564    843   -881       O  
ATOM   2299  NE2 GLN A 351     -27.592 -35.842  26.474  1.00202.37           N  
ANISOU 2299  NE2 GLN A 351    26981  28898  21012  -3011   1010  -1122       N  
ATOM   2300  N   PRO A 352     -30.592 -29.227  26.379  1.00189.73           N  
ANISOU 2300  N   PRO A 352    23718  28628  19740  -1965    409   -149       N  
ATOM   2301  CA  PRO A 352     -30.908 -27.923  26.978  1.00179.22           C  
ANISOU 2301  CA  PRO A 352    22244  27322  18529  -1687    334     38       C  
ATOM   2302  C   PRO A 352     -31.314 -27.868  28.459  1.00169.65           C  
ANISOU 2302  C   PRO A 352    21051  26102  17305  -1715    317     64       C  
ATOM   2303  O   PRO A 352     -32.036 -28.737  28.911  1.00163.46           O  
ANISOU 2303  O   PRO A 352    20257  25516  16334  -1979    344     -9       O  
ATOM   2304  CB  PRO A 352     -32.083 -27.449  26.111  1.00181.25           C  
ANISOU 2304  CB  PRO A 352    22214  28022  18630  -1661    305    170       C  
ATOM   2305  CG  PRO A 352     -32.820 -28.727  25.783  1.00187.44           C  
ANISOU 2305  CG  PRO A 352    22947  29115  19156  -2005    347     56       C  
ATOM   2306  CD  PRO A 352     -31.739 -29.782  25.658  1.00191.12           C  
ANISOU 2306  CD  PRO A 352    23701  29255  19658  -2192    420   -156       C  
ATOM   2307  N   LEU A 353     -30.830 -26.835  29.158  1.00160.61           N  
ANISOU 2307  N   LEU A 353    19941  24731  16351  -1459    276    163       N  
ATOM   2308  CA  LEU A 353     -31.158 -26.558  30.584  1.00151.92           C  
ANISOU 2308  CA  LEU A 353    18848  23613  15261  -1439    254    209       C  
ATOM   2309  C   LEU A 353     -32.632 -26.152  30.708  1.00152.43           C  
ANISOU 2309  C   LEU A 353    18662  24132  15121  -1483    230    325       C  
ATOM   2310  O   LEU A 353     -33.229 -26.405  31.771  1.00159.70           O  
ANISOU 2310  O   LEU A 353    19573  25184  15919  -1657    236    288       O  
ATOM   2311  CB  LEU A 353     -30.231 -25.472  31.137  1.00143.75           C  
ANISOU 2311  CB  LEU A 353    17879  22280  14457  -1146    216    307       C  
ATOM   2312  CG  LEU A 353     -28.820 -25.933  31.498  1.00140.35           C  
ANISOU 2312  CG  LEU A 353    17643  21454  14227  -1040    228    237       C  
ATOM   2313  CD1 LEU A 353     -28.045 -24.816  32.179  1.00131.06           C  
ANISOU 2313  CD1 LEU A 353    16477  20083  13235   -771    187    354       C  
ATOM   2314  CD2 LEU A 353     -28.867 -27.162  32.391  1.00143.94           C  
ANISOU 2314  CD2 LEU A 353    18327  21656  14706  -1184    273     83       C  
ATOM   2315  N   SER A 354     -33.171 -25.501  29.670  1.00148.51           N  
ANISOU 2315  N   SER A 354    17959  23903  14564  -1334    209    468       N  
ATOM   2316  CA  SER A 354     -34.575 -25.009  29.643  1.00145.61           C  
ANISOU 2316  CA  SER A 354    17340  23986  13998  -1304    192    612       C  
ATOM   2317  C   SER A 354     -35.545 -26.185  29.802  1.00143.99           C  
ANISOU 2317  C   SER A 354    17090  24043  13575  -1631    208    513       C  
ATOM   2318  O   SER A 354     -36.549 -26.026  30.516  1.00147.11           O  
ANISOU 2318  O   SER A 354    17342  24701  13851  -1609    191    609       O  
ATOM   2319  CB  SER A 354     -34.839 -24.253  28.371  1.00149.58           C  
ANISOU 2319  CB  SER A 354    17634  24821  14378  -1220    193    725       C  
ATOM   2320  OG  SER A 354     -33.920 -23.180  28.228  1.00158.22           O  
ANISOU 2320  OG  SER A 354    18751  25723  15642   -891    182    864       O  
ATOM   2321  N   GLY A 355     -35.238 -27.327  29.180  1.00146.29           N  
ANISOU 2321  N   GLY A 355    17520  24259  13803  -1938    250    320       N  
ATOM   2322  CA  GLY A 355     -36.071 -28.540  29.294  1.00149.87           C  
ANISOU 2322  CA  GLY A 355    17993  24911  14039  -2308    283    193       C  
ATOM   2323  C   GLY A 355     -36.138 -29.033  30.731  1.00153.22           C  
ANISOU 2323  C   GLY A 355    18584  25079  14551  -2333    283    151       C  
ATOM   2324  O   GLY A 355     -37.226 -29.470  31.157  1.00163.52           O  
ANISOU 2324  O   GLY A 355    19795  26665  15668  -2521    282    152       O  
ATOM   2325  N   LYS A 356     -35.022 -28.919  31.462  1.00147.37           N  
ANISOU 2325  N   LYS A 356    18076  23835  14083  -2143    282    122       N  
ATOM   2326  CA  LYS A 356     -34.889 -29.379  32.871  1.00138.76           C  
ANISOU 2326  CA  LYS A 356    17165  22455  13101  -2139    283     83       C  
ATOM   2327  C   LYS A 356     -35.395 -28.318  33.859  1.00133.97           C  
ANISOU 2327  C   LYS A 356    16415  21940  12546  -1904    225    252       C  
ATOM   2328  O   LYS A 356     -35.331 -28.585  35.072  1.00138.79           O  
ANISOU 2328  O   LYS A 356    17167  22307  13257  -1883    222    227       O  
ATOM   2329  CB  LYS A 356     -33.423 -29.695  33.181  1.00136.19           C  
ANISOU 2329  CB  LYS A 356    17127  21591  13028  -2013    308     -2       C  
ATOM   2330  CG  LYS A 356     -32.724 -30.610  32.184  1.00139.54           C  
ANISOU 2330  CG  LYS A 356    17752  21858  13407  -2222    386   -178       C  
ATOM   2331  CD  LYS A 356     -31.266 -30.842  32.515  1.00137.56           C  
ANISOU 2331  CD  LYS A 356    17698  21168  13399  -1997    400   -207       C  
ATOM   2332  CE  LYS A 356     -30.576 -31.770  31.539  1.00139.07           C  
ANISOU 2332  CE  LYS A 356    18085  21201  13551  -2137    486   -362       C  
ATOM   2333  NZ  LYS A 356     -31.238 -33.095  31.484  1.00145.14           N  
ANISOU 2333  NZ  LYS A 356    19067  21931  14146  -2476    578   -522       N  
ATOM   2334  N   THR A 357     -35.883 -27.171  33.375  1.00129.36           N  
ANISOU 2334  N   THR A 357    15569  21692  11888  -1716    190    424       N  
ATOM   2335  CA  THR A 357     -36.355 -26.095  34.291  1.00124.43           C  
ANISOU 2335  CA  THR A 357    14812  21181  11282  -1468    153    597       C  
ATOM   2336  C   THR A 357     -37.492 -26.623  35.171  1.00124.95           C  
ANISOU 2336  C   THR A 357    14836  21438  11201  -1648    150    577       C  
ATOM   2337  O   THR A 357     -37.476 -26.333  36.382  1.00119.35           O  
ANISOU 2337  O   THR A 357    14180  20562  10604  -1488    130    636       O  
ATOM   2338  CB  THR A 357     -36.843 -24.873  33.503  1.00121.20           C  
ANISOU 2338  CB  THR A 357    14136  21155  10759  -1250    141    788       C  
ATOM   2339  OG1 THR A 357     -35.711 -24.271  32.877  1.00119.79           O  
ANISOU 2339  OG1 THR A 357    14018  20777  10718  -1109    146    797       O  
ATOM   2340  CG2 THR A 357     -37.546 -23.856  34.374  1.00121.74           C  
ANISOU 2340  CG2 THR A 357    14125  21257  10873   -929    124    975       C  
ATOM   2341  N   SER A 358     -38.420 -27.390  34.595  1.00133.88           N  
ANISOU 2341  N   SER A 358    15876  22919  12071  -1995    174    489       N  
ATOM   2342  CA  SER A 358     -39.541 -27.959  35.389  1.00142.41           C  
ANISOU 2342  CA  SER A 358    16935  24193  12980  -2245    179    441       C  
ATOM   2343  C   SER A 358     -38.970 -28.740  36.579  1.00139.53           C  
ANISOU 2343  C   SER A 358    16881  23333  12799  -2309    195    318       C  
ATOM   2344  O   SER A 358     -39.386 -28.469  37.720  1.00141.15           O  
ANISOU 2344  O   SER A 358    17077  23542  13012  -2267    175    365       O  
ATOM   2345  CB  SER A 358     -40.417 -28.833  34.531  1.00150.74           C  
ANISOU 2345  CB  SER A 358    17911  25641  13719  -2693    218    318       C  
ATOM   2346  OG  SER A 358     -41.109 -28.059  33.563  1.00157.87           O  
ANISOU 2346  OG  SER A 358    18462  27144  14374  -2673    199    453       O  
ATOM   2347  N   TYR A 359     -38.031 -29.651  36.306  1.00140.48           N  
ANISOU 2347  N   TYR A 359    17272  23050  13052  -2403    237    167       N  
ATOM   2348  CA  TYR A 359     -37.391 -30.488  37.341  1.00139.77           C  
ANISOU 2348  CA  TYR A 359    17501  22477  13128  -2448    267     51       C  
ATOM   2349  C   TYR A 359     -36.741 -29.627  38.438  1.00134.06           C  
ANISOU 2349  C   TYR A 359    16819  21441  12673  -2073    218    163       C  
ATOM   2350  O   TYR A 359     -36.757 -30.029  39.615  1.00135.09           O  
ANISOU 2350  O   TYR A 359    17096  21348  12882  -2081    219    135       O  
ATOM   2351  CB  TYR A 359     -36.291 -31.414  36.788  1.00143.87           C  
ANISOU 2351  CB  TYR A 359    18305  22626  13730  -2559    336   -111       C  
ATOM   2352  CG  TYR A 359     -36.673 -32.457  35.728  1.00152.73           C  
ANISOU 2352  CG  TYR A 359    19492  23927  14609  -2957    412   -265       C  
ATOM   2353  CD1 TYR A 359     -37.514 -33.535  36.021  1.00155.66           C  
ANISOU 2353  CD1 TYR A 359    19980  24394  14769  -3339    470   -385       C  
ATOM   2354  CD2 TYR A 359     -36.115 -32.391  34.433  1.00154.59           C  
ANISOU 2354  CD2 TYR A 359    19703  24208  14823  -2965    435   -302       C  
ATOM   2355  CE1 TYR A 359     -37.816 -34.469  35.031  1.00158.93           C  
ANISOU 2355  CE1 TYR A 359    20481  24955  14947  -3727    553   -537       C  
ATOM   2356  CE2 TYR A 359     -36.405 -33.322  33.449  1.00150.78           C  
ANISOU 2356  CE2 TYR A 359    19298  23874  14117  -3331    512   -451       C  
ATOM   2357  CZ  TYR A 359     -37.256 -34.351  33.747  1.00153.38           C  
ANISOU 2357  CZ  TYR A 359    19747  24300  14230  -3717    574   -570       C  
ATOM   2358  OH  TYR A 359     -37.536 -35.272  32.781  1.00153.11           O  
ANISOU 2358  OH  TYR A 359    19815  24400  13956  -4110    662   -728       O  
ATOM   2359  N   PHE A 360     -36.168 -28.471  38.061  1.00125.65           N  
ANISOU 2359  N   PHE A 360    15644  20359  11738  -1767    181    284       N  
ATOM   2360  CA  PHE A 360     -35.535 -27.559  39.033  1.00118.15           C  
ANISOU 2360  CA  PHE A 360    14738  19131  11022  -1435    143    388       C  
ATOM   2361  C   PHE A 360     -36.572 -26.932  39.961  1.00122.07           C  
ANISOU 2361  C   PHE A 360    15087  19836  11455  -1332    111    514       C  
ATOM   2362  O   PHE A 360     -36.510 -27.124  41.192  1.00122.41           O  
ANISOU 2362  O   PHE A 360    15253  19655  11602  -1294    101    501       O  
ATOM   2363  CB  PHE A 360     -34.705 -26.462  38.348  1.00111.95           C  
ANISOU 2363  CB  PHE A 360    13890  18286  10359  -1171    126    482       C  
ATOM   2364  CG  PHE A 360     -33.540 -26.978  37.539  1.00107.86           C  
ANISOU 2364  CG  PHE A 360    13516  17537   9928  -1223    154    371       C  
ATOM   2365  CD1 PHE A 360     -32.855 -28.145  37.890  1.00106.69           C  
ANISOU 2365  CD1 PHE A 360    13614  17068   9854  -1357    192    220       C  
ATOM   2366  CD2 PHE A 360     -33.111 -26.277  36.413  1.00106.44           C  
ANISOU 2366  CD2 PHE A 360    13230  17463   9749  -1118    151    426       C  
ATOM   2367  CE1 PHE A 360     -31.789 -28.605  37.121  1.00106.61           C  
ANISOU 2367  CE1 PHE A 360    13732  16866   9907  -1375    228    127       C  
ATOM   2368  CE2 PHE A 360     -32.031 -26.719  35.654  1.00104.62           C  
ANISOU 2368  CE2 PHE A 360    13118  17040   9592  -1155    177    328       C  
ATOM   2369  CZ  PHE A 360     -31.359 -27.881  36.012  1.00104.91           C  
ANISOU 2369  CZ  PHE A 360    13393  16770   9697  -1275    216    180       C  
ATOM   2370  N   HIS A 361     -37.535 -26.211  39.375  1.00129.11           N  
ANISOU 2370  N   HIS A 361    15716  21175  12164  -1280     99    639       N  
ATOM   2371  CA  HIS A 361     -38.631 -25.582  40.149  1.00132.05           C  
ANISOU 2371  CA  HIS A 361    15920  21816  12434  -1160     80    775       C  
ATOM   2372  C   HIS A 361     -39.446 -26.557  41.013  1.00134.01           C  
ANISOU 2372  C   HIS A 361    16201  22148  12568  -1417     81    694       C  
ATOM   2373  O   HIS A 361     -39.942 -26.165  42.069  1.00141.45           O  
ANISOU 2373  O   HIS A 361    17108  23108  13526  -1288     63    775       O  
ATOM   2374  CB  HIS A 361     -39.530 -24.745  39.228  1.00131.06           C  
ANISOU 2374  CB  HIS A 361    15496  22205  12093  -1056     81    929       C  
ATOM   2375  CG  HIS A 361     -38.912 -23.436  38.874  1.00134.77           C  
ANISOU 2375  CG  HIS A 361    15949  22565  12692   -700     85   1070       C  
ATOM   2376  ND1 HIS A 361     -39.183 -22.282  39.574  1.00135.83           N  
ANISOU 2376  ND1 HIS A 361    16042  22695  12870   -374     89   1237       N  
ATOM   2377  CD2 HIS A 361     -37.956 -23.113  37.969  1.00137.99           C  
ANISOU 2377  CD2 HIS A 361    16415  22812  13203   -626     93   1058       C  
ATOM   2378  CE1 HIS A 361     -38.449 -21.292  39.096  1.00139.13           C  
ANISOU 2378  CE1 HIS A 361    16506  22954  13403   -126    107   1324       C  
ATOM   2379  NE2 HIS A 361     -37.699 -21.768  38.113  1.00141.12           N  
ANISOU 2379  NE2 HIS A 361    16804  23122  13693   -276    105   1220       N  
ATOM   2380  N   LEU A 362     -39.566 -27.811  40.571  1.00131.36           N  
ANISOU 2380  N   LEU A 362    15951  21849  12110  -1783    111    532       N  
ATOM   2381  CA  LEU A 362     -40.189 -28.872  41.368  1.00129.01           C  
ANISOU 2381  CA  LEU A 362    15751  21559  11709  -2072    128    429       C  
ATOM   2382  C   LEU A 362     -39.391 -29.114  42.633  1.00127.10           C  
ANISOU 2382  C   LEU A 362    15771  20803  11717  -1957    125    384       C  
ATOM   2383  O   LEU A 362     -39.921 -28.933  43.726  1.00134.60           O  
ANISOU 2383  O   LEU A 362    16692  21775  12673  -1894    102    442       O  
ATOM   2384  CB  LEU A 362     -40.299 -30.179  40.578  1.00129.51           C  
ANISOU 2384  CB  LEU A 362    15926  21681  11599  -2495    184    249       C  
ATOM   2385  CG  LEU A 362     -40.725 -31.468  41.310  1.00129.38           C  
ANISOU 2385  CG  LEU A 362    16110  21566  11482  -2845    229    105       C  
ATOM   2386  CD1 LEU A 362     -42.220 -31.480  41.619  1.00130.48           C  
ANISOU 2386  CD1 LEU A 362    16007  22228  11341  -3037    211    161       C  
ATOM   2387  CD2 LEU A 362     -40.321 -32.680  40.482  1.00129.61           C  
ANISOU 2387  CD2 LEU A 362    16373  21447  11426  -3185    310    -86       C  
ATOM   2388  N   LEU A 363     -38.126 -29.500  42.479  1.00120.32           N  
ANISOU 2388  N   LEU A 363    15151  19513  11052  -1918    148    291       N  
ATOM   2389  CA  LEU A 363     -37.250 -29.846  43.620  1.00115.52           C  
ANISOU 2389  CA  LEU A 363    14799  18426  10669  -1816    152    243       C  
ATOM   2390  C   LEU A 363     -36.950 -28.673  44.546  1.00111.94           C  
ANISOU 2390  C   LEU A 363    14287  17847  10399  -1466    100    381       C  
ATOM   2391  O   LEU A 363     -36.977 -28.833  45.775  1.00111.18           O  
ANISOU 2391  O   LEU A 363    14287  17571  10382  -1427     89    383       O  
ATOM   2392  CB  LEU A 363     -35.909 -30.394  43.143  1.00115.88           C  
ANISOU 2392  CB  LEU A 363    15073  18092  10860  -1800    192    139       C  
ATOM   2393  CG  LEU A 363     -35.703 -31.897  42.969  1.00117.72           C  
ANISOU 2393  CG  LEU A 363    15574  18134  11021  -2093    275    -35       C  
ATOM   2394  CD1 LEU A 363     -36.789 -32.535  42.123  1.00122.31           C  
ANISOU 2394  CD1 LEU A 363    16076  19081  11313  -2457    315   -109       C  
ATOM   2395  CD2 LEU A 363     -34.336 -32.112  42.326  1.00115.80           C  
ANISOU 2395  CD2 LEU A 363    15495  17582  10921  -1981    311    -95       C  
ATOM   2396  N   THR A 364     -36.684 -27.500  43.964  1.00108.76           N  
ANISOU 2396  N   THR A 364    13739  17535  10047  -1225     76    495       N  
ATOM   2397  CA  THR A 364     -36.246 -26.352  44.751  1.00105.62           C  
ANISOU 2397  CA  THR A 364    13337  16969   9823   -906     45    613       C  
ATOM   2398  C   THR A 364     -37.282 -25.708  45.631  1.00106.89           C  
ANISOU 2398  C   THR A 364    13366  17334   9911   -797     26    729       C  
ATOM   2399  O   THR A 364     -36.909 -25.042  46.586  1.00106.90           O  
ANISOU 2399  O   THR A 364    13434  17121  10059   -588     12    790       O  
ATOM   2400  CB  THR A 364     -35.644 -25.233  43.904  1.00103.30           C  
ANISOU 2400  CB  THR A 364    12967  16685   9597   -683     41    703       C  
ATOM   2401  OG1 THR A 364     -36.601 -24.827  42.929  1.00104.09           O  
ANISOU 2401  OG1 THR A 364    12839  17216   9491   -702     48    784       O  
ATOM   2402  CG2 THR A 364     -34.318 -25.706  43.259  1.00102.43           C  
ANISOU 2402  CG2 THR A 364    13011  16292   9615   -721     56    599       C  
ATOM   2403  N   TRP A 365     -38.557 -25.833  45.282  1.00110.47           N  
ANISOU 2403  N   TRP A 365    13624  18222  10126   -926     29    768       N  
ATOM   2404  CA  TRP A 365     -39.652 -25.277  46.105  1.00111.84           C  
ANISOU 2404  CA  TRP A 365    13649  18648  10194   -819     17    887       C  
ATOM   2405  C   TRP A 365     -40.391 -26.354  46.904  1.00111.72           C  
ANISOU 2405  C   TRP A 365    13668  18709  10071  -1089     14    800       C  
ATOM   2406  O   TRP A 365     -40.888 -26.086  47.997  1.00110.09           O  
ANISOU 2406  O   TRP A 365    13441  18518   9870   -997      1    860       O  
ATOM   2407  CB  TRP A 365     -40.617 -24.432  45.232  1.00112.92           C  
ANISOU 2407  CB  TRP A 365    13502  19283  10117   -703     26   1035       C  
ATOM   2408  CG  TRP A 365     -39.877 -23.401  44.402  1.00114.59           C  
ANISOU 2408  CG  TRP A 365    13708  19402  10427   -449     39   1120       C  
ATOM   2409  CD1 TRP A 365     -39.809 -23.340  43.040  1.00119.12           C  
ANISOU 2409  CD1 TRP A 365    14175  20178  10904   -497     51   1127       C  
ATOM   2410  CD2 TRP A 365     -39.032 -22.336  44.881  1.00114.91           C  
ANISOU 2410  CD2 TRP A 365    13878  19102  10678   -141     47   1196       C  
ATOM   2411  NE1 TRP A 365     -39.003 -22.305  42.655  1.00120.51           N  
ANISOU 2411  NE1 TRP A 365    14404  20163  11219   -229     65   1209       N  
ATOM   2412  CE2 TRP A 365     -38.511 -21.685  43.769  1.00119.11           C  
ANISOU 2412  CE2 TRP A 365    14379  19649  11226    -22     66   1248       C  
ATOM   2413  CE3 TRP A 365     -38.660 -21.877  46.140  1.00113.42           C  
ANISOU 2413  CE3 TRP A 365    13835  18604  10653     23     45   1221       C  
ATOM   2414  CZ2 TRP A 365     -37.664 -20.576  43.879  1.00120.52           C  
ANISOU 2414  CZ2 TRP A 365    14676  19545  11568    245     87   1325       C  
ATOM   2415  CZ3 TRP A 365     -37.804 -20.792  46.241  1.00111.81           C  
ANISOU 2415  CZ3 TRP A 365    13748  18126  10609    277     66   1290       C  
ATOM   2416  CH2 TRP A 365     -37.332 -20.150  45.130  1.00115.76           C  
ANISOU 2416  CH2 TRP A 365    14223  18649  11112    380     89   1341       C  
ATOM   2417  N   SER A 366     -40.421 -27.575  46.364  1.00112.22           N  
ANISOU 2417  N   SER A 366    13808  18795  10033  -1429     36    655       N  
ATOM   2418  CA  SER A 366     -41.151 -28.696  46.938  1.00111.21           C  
ANISOU 2418  CA  SER A 366    13735  18755   9762  -1748     51    558       C  
ATOM   2419  C   SER A 366     -40.407 -29.277  48.125  1.00108.58           C  
ANISOU 2419  C   SER A 366    13681  17941   9632  -1742     55    478       C  
ATOM   2420  O   SER A 366     -40.988 -29.436  49.207  1.00109.72           O  
ANISOU 2420  O   SER A 366    13829  18111   9747  -1774     43    496       O  
ATOM   2421  CB  SER A 366     -41.368 -29.769  45.857  1.00112.93           C  
ANISOU 2421  CB  SER A 366    13984  19135   9790  -2125     93    423       C  
ATOM   2422  OG  SER A 366     -42.303 -30.750  46.218  1.00117.48           O  
ANISOU 2422  OG  SER A 366    14574  19909  10153  -2479    117    341       O  
ATOM   2423  N   LEU A 367     -39.122 -29.583  47.955  1.00105.89           N  
ANISOU 2423  N   LEU A 367    13562  17182   9487  -1686     73    400       N  
ATOM   2424  CA  LEU A 367     -38.339 -30.161  49.070  1.00105.25           C  
ANISOU 2424  CA  LEU A 367    13742  16659   9589  -1656     83    336       C  
ATOM   2425  C   LEU A 367     -38.273 -29.306  50.371  1.00107.25           C  
ANISOU 2425  C   LEU A 367    13966  16794   9988  -1388     37    442       C  
ATOM   2426  O   LEU A 367     -38.420 -29.864  51.458  1.00107.16           O  
ANISOU 2426  O   LEU A 367    14073  16642  10000  -1458     40    409       O  
ATOM   2427  CB  LEU A 367     -36.924 -30.538  48.639  1.00103.42           C  
ANISOU 2427  CB  LEU A 367    13722  16043   9527  -1593    113    256       C  
ATOM   2428  CG  LEU A 367     -36.811 -31.772  47.755  1.00104.42           C  
ANISOU 2428  CG  LEU A 367    14009  16128   9538  -1884    184    112       C  
ATOM   2429  CD1 LEU A 367     -35.412 -31.776  47.136  1.00104.79           C  
ANISOU 2429  CD1 LEU A 367    14188  15877   9748  -1732    206     75       C  
ATOM   2430  CD2 LEU A 367     -37.099 -33.075  48.486  1.00103.01           C  
ANISOU 2430  CD2 LEU A 367    14066  15787   9284  -2137    243      4       C  
ATOM   2431  N   PRO A 368     -38.042 -27.959  50.272  1.00107.99           N  
ANISOU 2431  N   PRO A 368    13926  16933  10172  -1090      5    566       N  
ATOM   2432  CA  PRO A 368     -38.095 -27.162  51.508  1.00104.31           C  
ANISOU 2432  CA  PRO A 368    13449  16373   9811   -868    -22    658       C  
ATOM   2433  C   PRO A 368     -39.484 -27.184  52.158  1.00103.71           C  
ANISOU 2433  C   PRO A 368    13230  16614   9559   -945    -31    711       C  
ATOM   2434  O   PRO A 368     -39.572 -27.210  53.384  1.00103.94           O  
ANISOU 2434  O   PRO A 368    13326  16511   9653   -898    -45    723       O  
ATOM   2435  CB  PRO A 368     -37.703 -25.740  51.054  1.00103.33           C  
ANISOU 2435  CB  PRO A 368    13228  16268   9765   -575    -31    776       C  
ATOM   2436  CG  PRO A 368     -37.112 -25.887  49.717  1.00105.31           C  
ANISOU 2436  CG  PRO A 368    13479  16521  10012   -628    -15    731       C  
ATOM   2437  CD  PRO A 368     -37.718 -27.115  49.099  1.00107.65           C  
ANISOU 2437  CD  PRO A 368    13765  17003  10133   -949      4    627       C  
ATOM   2438  N   PHE A 369     -40.538 -27.152  51.339  1.00102.50           N  
ANISOU 2438  N   PHE A 369    12868  16901   9176  -1058    -24    749       N  
ATOM   2439  CA  PHE A 369     -41.916 -27.214  51.808  1.00102.15           C  
ANISOU 2439  CA  PHE A 369    12648  17244   8919  -1152    -31    803       C  
ATOM   2440  C   PHE A 369     -42.122 -28.465  52.650  1.00105.57           C  
ANISOU 2440  C   PHE A 369    13236  17552   9321  -1438    -24    685       C  
ATOM   2441  O   PHE A 369     -42.652 -28.371  53.764  1.00107.58           O  
ANISOU 2441  O   PHE A 369    13469  17840   9563  -1399    -39    727       O  
ATOM   2442  CB  PHE A 369     -42.875 -27.214  50.615  1.00102.60           C  
ANISOU 2442  CB  PHE A 369    12459  17815   8706  -1290    -20    838       C  
ATOM   2443  CG  PHE A 369     -44.306 -27.453  50.973  1.00103.04           C  
ANISOU 2443  CG  PHE A 369    12313  18339   8497  -1447    -24    881       C  
ATOM   2444  CD1 PHE A 369     -45.128 -26.387  51.334  1.00103.61           C  
ANISOU 2444  CD1 PHE A 369    12160  18732   8475  -1178    -33   1053       C  
ATOM   2445  CD2 PHE A 369     -44.851 -28.734  50.914  1.00104.19           C  
ANISOU 2445  CD2 PHE A 369    12496  18626   8463  -1868     -8    753       C  
ATOM   2446  CE1 PHE A 369     -46.469 -26.591  51.642  1.00105.70           C  
ANISOU 2446  CE1 PHE A 369    12206  19484   8471  -1312    -36   1104       C  
ATOM   2447  CE2 PHE A 369     -46.191 -28.954  51.249  1.00106.93           C  
ANISOU 2447  CE2 PHE A 369    12638  19450   8540  -2042    -13    793       C  
ATOM   2448  CZ  PHE A 369     -47.002 -27.881  51.615  1.00107.28           C  
ANISOU 2448  CZ  PHE A 369    12422  19846   8490  -1758    -32    972       C  
ATOM   2449  N   VAL A 370     -41.700 -29.626  52.129  1.00106.05           N  
ANISOU 2449  N   VAL A 370    13472  17457   9364  -1716      9    540       N  
ATOM   2450  CA  VAL A 370     -41.829 -30.916  52.850  1.00105.49           C  
ANISOU 2450  CA  VAL A 370    13608  17220   9252  -2005     39    420       C  
ATOM   2451  C   VAL A 370     -41.128 -30.849  54.200  1.00102.20           C  
ANISOU 2451  C   VAL A 370    13368  16402   9061  -1820     22    431       C  
ATOM   2452  O   VAL A 370     -41.750 -31.133  55.222  1.00103.27           O  
ANISOU 2452  O   VAL A 370    13513  16582   9142  -1899     15    438       O  
ATOM   2453  CB  VAL A 370     -41.277 -32.120  52.035  1.00107.54           C  
ANISOU 2453  CB  VAL A 370    14094  17285   9478  -2282    102    263       C  
ATOM   2454  CG1 VAL A 370     -41.189 -33.396  52.887  1.00109.79           C  
ANISOU 2454  CG1 VAL A 370    14669  17285   9759  -2516    153    149       C  
ATOM   2455  CG2 VAL A 370     -42.149 -32.378  50.823  1.00109.87           C  
ANISOU 2455  CG2 VAL A 370    14222  18021   9501  -2555    124    231       C  
ATOM   2456  N   LEU A 371     -39.861 -30.431  54.200  1.00 98.83           N  
ANISOU 2456  N   LEU A 371    13060  15621   8869  -1579     15    438       N  
ATOM   2457  CA  LEU A 371     -39.117 -30.252  55.447  1.00 96.66           C  
ANISOU 2457  CA  LEU A 371    12926  15000   8800  -1389     -3    459       C  
ATOM   2458  C   LEU A 371     -39.755 -29.265  56.441  1.00 94.42           C  
ANISOU 2458  C   LEU A 371    12490  14861   8525  -1199    -46    577       C  
ATOM   2459  O   LEU A 371     -39.888 -29.588  57.638  1.00 94.93           O  
ANISOU 2459  O   LEU A 371    12639  14804   8625  -1219    -54    570       O  
ATOM   2460  CB  LEU A 371     -37.691 -29.838  55.177  1.00 96.54           C  
ANISOU 2460  CB  LEU A 371    13014  14666   8998  -1171     -7    458       C  
ATOM   2461  CG  LEU A 371     -36.836 -30.942  54.551  1.00 99.57           C  
ANISOU 2461  CG  LEU A 371    13613  14805   9411  -1309     45    340       C  
ATOM   2462  CD1 LEU A 371     -35.541 -30.350  53.980  1.00 99.09           C  
ANISOU 2462  CD1 LEU A 371    13577  14553   9520  -1089     36    357       C  
ATOM   2463  CD2 LEU A 371     -36.494 -32.034  55.552  1.00101.80           C  
ANISOU 2463  CD2 LEU A 371    14143  14795   9740  -1399     80    271       C  
ATOM   2464  N   THR A 372     -40.190 -28.107  55.957  1.00 91.00           N  
ANISOU 2464  N   THR A 372    11845  14688   8043  -1017    -63    686       N  
ATOM   2465  CA  THR A 372     -40.875 -27.120  56.789  1.00 90.29           C  
ANISOU 2465  CA  THR A 372    11617  14757   7931   -816    -84    807       C  
ATOM   2466  C   THR A 372     -42.152 -27.669  57.389  1.00 94.10           C  
ANISOU 2466  C   THR A 372    12001  15534   8217  -1004    -87    809       C  
ATOM   2467  O   THR A 372     -42.377 -27.598  58.605  1.00 94.97           O  
ANISOU 2467  O   THR A 372    12144  15571   8366   -948   -101    834       O  
ATOM   2468  CB  THR A 372     -41.186 -25.868  55.978  1.00 90.07           C  
ANISOU 2468  CB  THR A 372    11399  14979   7844   -588    -78    930       C  
ATOM   2469  OG1 THR A 372     -39.964 -25.419  55.401  1.00 88.77           O  
ANISOU 2469  OG1 THR A 372    11340  14534   7852   -451    -73    917       O  
ATOM   2470  CG2 THR A 372     -41.783 -24.744  56.829  1.00 88.74           C  
ANISOU 2470  CG2 THR A 372    11132  14925   7659   -324    -77   1063       C  
ATOM   2471  N   VAL A 373     -42.994 -28.247  56.539  1.00100.29           N  
ANISOU 2471  N   VAL A 373    12659  16670   8775  -1250    -73    779       N  
ATOM   2472  CA  VAL A 373     -44.251 -28.885  57.004  1.00103.92           C  
ANISOU 2472  CA  VAL A 373    13014  17465   9006  -1497    -72    769       C  
ATOM   2473  C   VAL A 373     -43.945 -29.991  58.042  1.00101.19           C  
ANISOU 2473  C   VAL A 373    12916  16795   8734  -1697    -63    660       C  
ATOM   2474  O   VAL A 373     -44.519 -29.966  59.113  1.00 98.90           O  
ANISOU 2474  O   VAL A 373    12593  16572   8409  -1689    -78    696       O  
ATOM   2475  CB  VAL A 373     -45.118 -29.418  55.810  1.00106.67           C  
ANISOU 2475  CB  VAL A 373    13196  18259   9072  -1790    -52    735       C  
ATOM   2476  CG1 VAL A 373     -46.209 -30.404  56.269  1.00108.75           C  
ANISOU 2476  CG1 VAL A 373    13422  18802   9094  -2155    -41    677       C  
ATOM   2477  CG2 VAL A 373     -45.731 -28.244  55.042  1.00107.39           C  
ANISOU 2477  CG2 VAL A 373    12987  18776   9039  -1558    -61    885       C  
ATOM   2478  N   ALA A 374     -43.023 -30.907  57.711  1.00 99.37           N  
ANISOU 2478  N   ALA A 374    12936  16217   8602  -1844    -31    537       N  
ATOM   2479  CA  ALA A 374     -42.600 -31.964  58.623  1.00 98.71           C  
ANISOU 2479  CA  ALA A 374    13123  15786   8594  -1993     -6    445       C  
ATOM   2480  C   ALA A 374     -42.137 -31.390  59.968  1.00 98.08           C  
ANISOU 2480  C   ALA A 374    13093  15460   8710  -1725    -42    510       C  
ATOM   2481  O   ALA A 374     -42.540 -31.891  61.025  1.00 97.83           O  
ANISOU 2481  O   ALA A 374    13132  15391   8647  -1828    -41    497       O  
ATOM   2482  CB  ALA A 374     -41.492 -32.796  58.005  1.00 98.01           C  
ANISOU 2482  CB  ALA A 374    13297  15333   8607  -2075     44    334       C  
ATOM   2483  N   ILE A 375     -41.309 -30.341  59.935  1.00 97.14           N  
ANISOU 2483  N   ILE A 375    12944  15184   8779  -1404    -69    579       N  
ATOM   2484  CA  ILE A 375     -40.909 -29.656  61.186  1.00 96.00           C  
ANISOU 2484  CA  ILE A 375    12831  14846   8799  -1160   -100    643       C  
ATOM   2485  C   ILE A 375     -42.132 -29.082  61.942  1.00 97.08           C  
ANISOU 2485  C   ILE A 375    12779  15298   8808  -1114   -122    732       C  
ATOM   2486  O   ILE A 375     -42.260 -29.294  63.176  1.00 95.72           O  
ANISOU 2486  O   ILE A 375    12675  15022   8672  -1117   -134    734       O  
ATOM   2487  CB  ILE A 375     -39.867 -28.528  60.926  1.00 93.05           C  
ANISOU 2487  CB  ILE A 375    12452  14288   8612   -856   -116    699       C  
ATOM   2488  CG1 ILE A 375     -38.538 -29.131  60.534  1.00 89.35           C  
ANISOU 2488  CG1 ILE A 375    12181  13479   8287   -872    -98    617       C  
ATOM   2489  CG2 ILE A 375     -39.643 -27.641  62.159  1.00 93.45           C  
ANISOU 2489  CG2 ILE A 375    12508  14211   8785   -624   -140    771       C  
ATOM   2490  CD1 ILE A 375     -37.654 -28.154  59.818  1.00 87.66           C  
ANISOU 2490  CD1 ILE A 375    11930  13184   8192   -659   -106    657       C  
ATOM   2491  N   LEU A 376     -43.001 -28.351  61.228  1.00 96.54           N  
ANISOU 2491  N   LEU A 376    12473  15620   8585  -1053   -124    813       N  
ATOM   2492  CA  LEU A 376     -44.181 -27.769  61.874  1.00 98.84           C  
ANISOU 2492  CA  LEU A 376    12570  16252   8732   -973   -135    913       C  
ATOM   2493  C   LEU A 376     -45.062 -28.847  62.493  1.00101.99           C  
ANISOU 2493  C   LEU A 376    12968  16815   8966  -1280   -135    857       C  
ATOM   2494  O   LEU A 376     -45.633 -28.650  63.567  1.00102.74           O  
ANISOU 2494  O   LEU A 376    13013  16995   9028  -1227   -149    905       O  
ATOM   2495  CB  LEU A 376     -44.970 -26.886  60.933  1.00 99.02           C  
ANISOU 2495  CB  LEU A 376    12336  16699   8588   -842   -124   1021       C  
ATOM   2496  CG  LEU A 376     -44.193 -25.622  60.571  1.00 99.19           C  
ANISOU 2496  CG  LEU A 376    12375  16543   8768   -496   -113   1101       C  
ATOM   2497  CD1 LEU A 376     -44.710 -25.057  59.248  1.00100.73           C  
ANISOU 2497  CD1 LEU A 376    12366  17101   8804   -423    -93   1180       C  
ATOM   2498  CD2 LEU A 376     -44.277 -24.566  61.657  1.00 98.44           C  
ANISOU 2498  CD2 LEU A 376    12285  16369   8747   -200   -106   1199       C  
ATOM   2499  N   ALA A 377     -45.123 -30.003  61.845  1.00105.63           N  
ANISOU 2499  N   ALA A 377    13513  17297   9323  -1612   -112    748       N  
ATOM   2500  CA  ALA A 377     -45.933 -31.127  62.320  1.00110.06           C  
ANISOU 2500  CA  ALA A 377    14113  18001   9703  -1964    -97    678       C  
ATOM   2501  C   ALA A 377     -45.455 -31.697  63.648  1.00108.00           C  
ANISOU 2501  C   ALA A 377    14084  17365   9585  -1983    -97    633       C  
ATOM   2502  O   ALA A 377     -46.282 -31.885  64.578  1.00109.62           O  
ANISOU 2502  O   ALA A 377    14231  17739   9680  -2077   -107    656       O  
ATOM   2503  CB  ALA A 377     -46.005 -32.231  61.256  1.00113.34           C  
ANISOU 2503  CB  ALA A 377    14620  18473   9971  -2331    -52    558       C  
ATOM   2504  N   VAL A 378     -44.148 -31.980  63.730  1.00105.24           N  
ANISOU 2504  N   VAL A 378    13982  16541   9461  -1893    -83    577       N  
ATOM   2505  CA  VAL A 378     -43.533 -32.419  65.018  1.00104.47           C  
ANISOU 2505  CA  VAL A 378    14101  16075   9519  -1849    -84    555       C  
ATOM   2506  C   VAL A 378     -43.367 -31.266  66.006  1.00101.43           C  
ANISOU 2506  C   VAL A 378    13617  15647   9273  -1523   -132    656       C  
ATOM   2507  O   VAL A 378     -43.088 -31.506  67.153  1.00 99.49           O  
ANISOU 2507  O   VAL A 378    13492  15193   9118  -1490   -140    653       O  
ATOM   2508  CB  VAL A 378     -42.189 -33.191  64.884  1.00103.19           C  
ANISOU 2508  CB  VAL A 378    14235  15446   9524  -1849    -45    473       C  
ATOM   2509  CG1 VAL A 378     -42.409 -34.517  64.205  1.00105.52           C  
ANISOU 2509  CG1 VAL A 378    14706  15720   9666  -2200     25    360       C  
ATOM   2510  CG2 VAL A 378     -41.135 -32.395  64.133  1.00104.10           C  
ANISOU 2510  CG2 VAL A 378    14326  15415   9809  -1591    -60    498       C  
ATOM   2511  N   ALA A 379     -43.557 -30.026  65.544  1.00101.32           N  
ANISOU 2511  N   ALA A 379    13401  15831   9262  -1289   -153    746       N  
ATOM   2512  CA  ALA A 379     -43.614 -28.817  66.376  1.00 99.65           C  
ANISOU 2512  CA  ALA A 379    13094  15634   9132   -991   -178    847       C  
ATOM   2513  C   ALA A 379     -42.325 -28.616  67.140  1.00 96.53           C  
ANISOU 2513  C   ALA A 379    12888  14805   8981   -823   -189    831       C  
ATOM   2514  O   ALA A 379     -42.285 -28.668  68.346  1.00 95.27           O  
ANISOU 2514  O   ALA A 379    12791  14528   8877   -788   -202    839       O  
ATOM   2515  CB  ALA A 379     -44.819 -28.821  67.309  1.00 99.82           C  
ANISOU 2515  CB  ALA A 379    12989  15937   8999  -1047   -188    895       C  
ATOM   2516  N   GLN A 380     -41.275 -28.354  66.393  1.00 96.26           N  
ANISOU 2516  N   GLN A 380    12927  14568   9077   -722   -183    811       N  
ATOM   2517  CA  GLN A 380     -39.952 -28.206  66.929  1.00 94.74           C  
ANISOU 2517  CA  GLN A 380    12894  14008   9092   -584   -191    793       C  
ATOM   2518  C   GLN A 380     -39.386 -26.816  66.651  1.00 91.86           C  
ANISOU 2518  C   GLN A 380    12476  13598   8828   -323   -194    856       C  
ATOM   2519  O   GLN A 380     -38.179 -26.633  66.639  1.00 90.24           O  
ANISOU 2519  O   GLN A 380    12378  13136   8772   -234   -197    834       O  
ATOM   2520  CB  GLN A 380     -39.072 -29.291  66.297  1.00 98.10           C  
ANISOU 2520  CB  GLN A 380    13487  14214   9570   -721   -170    703       C  
ATOM   2521  CG  GLN A 380     -39.372 -30.700  66.807  1.00 98.62           C  
ANISOU 2521  CG  GLN A 380    13697  14208   9563   -962   -146    636       C  
ATOM   2522  CD  GLN A 380     -39.217 -30.848  68.316  1.00 99.79           C  
ANISOU 2522  CD  GLN A 380    13929  14203   9782   -911   -163    655       C  
ATOM   2523  OE1 GLN A 380     -39.974 -31.552  68.932  1.00 99.73           O  
ANISOU 2523  OE1 GLN A 380    13955  14265   9670  -1080   -153    638       O  
ATOM   2524  NE2 GLN A 380     -38.243 -30.158  68.914  1.00102.76           N  
ANISOU 2524  NE2 GLN A 380    14334  14388  10322   -693   -187    689       N  
ATOM   2525  N   VAL A 381     -40.257 -25.832  66.469  1.00 91.63           N  
ANISOU 2525  N   VAL A 381    12290  13823   8702   -198   -184    939       N  
ATOM   2526  CA  VAL A 381     -39.833 -24.468  66.247  1.00 92.67           C  
ANISOU 2526  CA  VAL A 381    12404  13900   8902     49   -165   1006       C  
ATOM   2527  C   VAL A 381     -39.511 -23.856  67.608  1.00 90.89           C  
ANISOU 2527  C   VAL A 381    12263  13498   8771    181   -167   1029       C  
ATOM   2528  O   VAL A 381     -40.359 -23.842  68.475  1.00 92.56           O  
ANISOU 2528  O   VAL A 381    12424  13838   8906    186   -168   1062       O  
ATOM   2529  CB  VAL A 381     -40.926 -23.668  65.494  1.00 96.09           C  
ANISOU 2529  CB  VAL A 381    12655  14680   9172    162   -135   1101       C  
ATOM   2530  CG1 VAL A 381     -40.570 -22.171  65.340  1.00 96.78           C  
ANISOU 2530  CG1 VAL A 381    12766  14689   9313    442    -92   1183       C  
ATOM   2531  CG2 VAL A 381     -41.167 -24.303  64.122  1.00 98.36           C  
ANISOU 2531  CG2 VAL A 381    12856  15155   9360      5   -136   1070       C  
ATOM   2532  N   ASP A 382     -38.271 -23.402  67.806  1.00 89.28           N  
ANISOU 2532  N   ASP A 382    12184  13017   8720    266   -166   1007       N  
ATOM   2533  CA  ASP A 382     -37.866 -22.804  69.068  1.00 88.17           C  
ANISOU 2533  CA  ASP A 382    12131  12710   8659    363   -164   1019       C  
ATOM   2534  C   ASP A 382     -37.231 -21.417  68.823  1.00 90.47           C  
ANISOU 2534  C   ASP A 382    12483  12886   9005    542   -121   1057       C  
ATOM   2535  O   ASP A 382     -36.649 -21.194  67.778  1.00 95.28           O  
ANISOU 2535  O   ASP A 382    13100  13455   9645    558   -110   1050       O  
ATOM   2536  CB  ASP A 382     -36.840 -23.704  69.737  1.00 87.10           C  
ANISOU 2536  CB  ASP A 382    12108  12348   8638    253   -201    947       C  
ATOM   2537  CG  ASP A 382     -37.305 -25.205  69.915  1.00 88.31           C  
ANISOU 2537  CG  ASP A 382    12263  12551   8737     58   -226    900       C  
ATOM   2538  OD1 ASP A 382     -38.394 -25.445  70.465  1.00 87.65           O  
ANISOU 2538  OD1 ASP A 382    12117  12632   8552      3   -229    921       O  
ATOM   2539  OD2 ASP A 382     -36.505 -26.154  69.612  1.00 89.04           O  
ANISOU 2539  OD2 ASP A 382    12444  12499   8888    -36   -235    842       O  
ATOM   2540  N   GLY A 383     -37.324 -20.498  69.783  1.00 91.82           N  
ANISOU 2540  N   GLY A 383    12715  12991   9179    663    -88   1093       N  
ATOM   2541  CA  GLY A 383     -36.688 -19.169  69.679  1.00 90.50           C  
ANISOU 2541  CA  GLY A 383    12658  12676   9050    804    -28   1120       C  
ATOM   2542  C   GLY A 383     -35.402 -19.050  70.491  1.00 90.85           C  
ANISOU 2542  C   GLY A 383    12834  12473   9210    743    -44   1058       C  
ATOM   2543  O   GLY A 383     -35.230 -19.752  71.494  1.00 90.15           O  
ANISOU 2543  O   GLY A 383    12754  12339   9160    653    -89   1020       O  
ATOM   2544  N   ASP A 384     -34.515 -18.143  70.057  1.00 91.05           N  
ANISOU 2544  N   ASP A 384    12959  12360   9275    786     -2   1054       N  
ATOM   2545  CA  ASP A 384     -33.237 -17.847  70.716  1.00 93.97           C  
ANISOU 2545  CA  ASP A 384    13443  12538   9723    715     -7   1000       C  
ATOM   2546  C   ASP A 384     -32.982 -16.351  70.672  1.00 91.60           C  
ANISOU 2546  C   ASP A 384    13292  12122   9390    804     86   1025       C  
ATOM   2547  O   ASP A 384     -32.981 -15.751  69.615  1.00 92.96           O  
ANISOU 2547  O   ASP A 384    13487  12297   9535    875    134   1058       O  
ATOM   2548  CB  ASP A 384     -32.092 -18.604  70.031  1.00100.10           C  
ANISOU 2548  CB  ASP A 384    14184  13270  10576    605    -63    947       C  
ATOM   2549  CG  ASP A 384     -30.666 -18.388  70.704  1.00108.09           C  
ANISOU 2549  CG  ASP A 384    15276  14146  11647    519    -76    896       C  
ATOM   2550  OD1 ASP A 384     -30.552 -18.002  71.887  1.00103.69           O  
ANISOU 2550  OD1 ASP A 384    14785  13531  11081    499    -64    885       O  
ATOM   2551  OD2 ASP A 384     -29.632 -18.660  70.015  1.00120.83           O  
ANISOU 2551  OD2 ASP A 384    16870  15736  13303    462   -100    867       O  
ATOM   2552  N   SER A 385     -32.750 -15.760  71.840  1.00 92.96           N  
ANISOU 2552  N   SER A 385    13583  12183   9554    791    119   1006       N  
ATOM   2553  CA  SER A 385     -32.499 -14.331  71.965  1.00 91.99           C  
ANISOU 2553  CA  SER A 385    13654  11914   9381    849    229   1017       C  
ATOM   2554  C   SER A 385     -31.173 -13.872  71.387  1.00 90.69           C  
ANISOU 2554  C   SER A 385    13575  11631   9248    739    244    972       C  
ATOM   2555  O   SER A 385     -31.070 -12.708  71.033  1.00 90.93           O  
ANISOU 2555  O   SER A 385    13772  11551   9223    793    348    992       O  
ATOM   2556  CB  SER A 385     -32.554 -13.922  73.430  1.00 94.96           C  
ANISOU 2556  CB  SER A 385    14141  12206   9730    825    261    993       C  
ATOM   2557  OG  SER A 385     -31.619 -14.667  74.212  1.00 99.86           O  
ANISOU 2557  OG  SER A 385    14712  12811  10417    650    175    923       O  
ATOM   2558  N   VAL A 386     -30.157 -14.741  71.294  1.00 90.74           N  
ANISOU 2558  N   VAL A 386    13483  11664   9329    594    152    916       N  
ATOM   2559  CA  VAL A 386     -28.849 -14.313  70.720  1.00 92.47           C  
ANISOU 2559  CA  VAL A 386    13759  11812   9561    481    163    875       C  
ATOM   2560  C   VAL A 386     -28.939 -14.178  69.203  1.00 90.30           C  
ANISOU 2560  C   VAL A 386    13451  11569   9286    550    182    910       C  
ATOM   2561  O   VAL A 386     -28.467 -13.174  68.631  1.00 91.44           O  
ANISOU 2561  O   VAL A 386    13727  11623   9393    539    258    914       O  
ATOM   2562  CB  VAL A 386     -27.600 -15.155  71.162  1.00 92.47           C  
ANISOU 2562  CB  VAL A 386    13666  11855   9613    322     73    814       C  
ATOM   2563  CG1 VAL A 386     -27.541 -15.254  72.692  1.00 94.11           C  
ANISOU 2563  CG1 VAL A 386    13899  12051   9806    258     56    788       C  
ATOM   2564  CG2 VAL A 386     -27.575 -16.541  70.560  1.00 91.60           C  
ANISOU 2564  CG2 VAL A 386    13380  11853   9568    338    -17    818       C  
ATOM   2565  N   SER A 387     -29.537 -15.182  68.571  1.00 86.25           N  
ANISOU 2565  N   SER A 387    12778  11186   8806    605    119    933       N  
ATOM   2566  CA  SER A 387     -29.722 -15.196  67.125  1.00 85.53           C  
ANISOU 2566  CA  SER A 387    12629  11160   8709    665    128    967       C  
ATOM   2567  C   SER A 387     -30.840 -14.227  66.757  1.00 86.88           C  
ANISOU 2567  C   SER A 387    12871  11345   8794    839    224   1049       C  
ATOM   2568  O   SER A 387     -30.775 -13.574  65.732  1.00 88.59           O  
ANISOU 2568  O   SER A 387    13132  11548   8977    901    280   1087       O  
ATOM   2569  CB  SER A 387     -30.010 -16.630  66.614  1.00 84.18           C  
ANISOU 2569  CB  SER A 387    12279  11127   8578    639     40    954       C  
ATOM   2570  OG  SER A 387     -31.288 -17.106  67.029  1.00 83.71           O  
ANISOU 2570  OG  SER A 387    12149  11175   8480    701     28    988       O  
ATOM   2571  N   GLY A 388     -31.862 -14.144  67.600  1.00 88.14           N  
ANISOU 2571  N   GLY A 388    13037  11544   8906    931    247   1086       N  
ATOM   2572  CA  GLY A 388     -32.975 -13.239  67.362  1.00 89.00           C  
ANISOU 2572  CA  GLY A 388    13209  11695   8912   1136    348   1181       C  
ATOM   2573  C   GLY A 388     -33.966 -13.741  66.338  1.00 89.93           C  
ANISOU 2573  C   GLY A 388    13146  12043   8978   1237    326   1248       C  
ATOM   2574  O   GLY A 388     -34.749 -12.968  65.801  1.00 94.89           O  
ANISOU 2574  O   GLY A 388    13801  12744   9508   1426    412   1343       O  
ATOM   2575  N   ILE A 389     -33.956 -15.042  66.086  1.00 90.41           N  
ANISOU 2575  N   ILE A 389    13031  12231   9088   1114    219   1202       N  
ATOM   2576  CA  ILE A 389     -34.920 -15.686  65.182  1.00 94.46           C  
ANISOU 2576  CA  ILE A 389    13360  12994   9534   1152    190   1248       C  
ATOM   2577  C   ILE A 389     -35.459 -16.972  65.797  1.00 95.60           C  
ANISOU 2577  C   ILE A 389    13373  13265   9682   1035    106   1208       C  
ATOM   2578  O   ILE A 389     -34.935 -17.444  66.811  1.00 99.11           O  
ANISOU 2578  O   ILE A 389    13867  13587  10202    931     63   1144       O  
ATOM   2579  CB  ILE A 389     -34.300 -15.957  63.784  1.00 94.03           C  
ANISOU 2579  CB  ILE A 389    13251  12965   9511   1090    166   1228       C  
ATOM   2580  CG1 ILE A 389     -33.095 -16.906  63.829  1.00 93.96           C  
ANISOU 2580  CG1 ILE A 389    13237  12840   9621    898     85   1122       C  
ATOM   2581  CG2 ILE A 389     -33.859 -14.642  63.159  1.00 96.37           C  
ANISOU 2581  CG2 ILE A 389    13686  13144   9786   1206    259   1278       C  
ATOM   2582  CD1 ILE A 389     -33.375 -18.301  63.314  1.00 92.72           C  
ANISOU 2582  CD1 ILE A 389    12937  12827   9465    782     13   1081       C  
ATOM   2583  N   CYS A 390     -36.486 -17.547  65.190  1.00 94.25           N  
ANISOU 2583  N   CYS A 390    13041  13349   9418   1039     87   1245       N  
ATOM   2584  CA  CYS A 390     -36.944 -18.877  65.584  1.00 95.05           C  
ANISOU 2584  CA  CYS A 390    13036  13568   9509    880     14   1195       C  
ATOM   2585  C   CYS A 390     -36.486 -19.939  64.572  1.00 90.82           C  
ANISOU 2585  C   CYS A 390    12439  13061   9005    716    -37   1129       C  
ATOM   2586  O   CYS A 390     -36.550 -19.710  63.386  1.00 93.33           O  
ANISOU 2586  O   CYS A 390    12701  13480   9280    748    -18   1156       O  
ATOM   2587  CB  CYS A 390     -38.456 -18.905  65.673  1.00102.74           C  
ANISOU 2587  CB  CYS A 390    13869  14842  10325    948     31   1271       C  
ATOM   2588  SG  CYS A 390     -39.168 -18.048  67.088  1.00110.70           S  
ANISOU 2588  SG  CYS A 390    14935  15846  11279   1119     85   1337       S  
ATOM   2589  N   PHE A 391     -36.085 -21.110  65.032  1.00 85.00           N  
ANISOU 2589  N   PHE A 391    11724  12243   8329    550    -92   1048       N  
ATOM   2590  CA  PHE A 391     -35.541 -22.107  64.145  1.00 82.89           C  
ANISOU 2590  CA  PHE A 391    11446  11955   8092    410   -122    981       C  
ATOM   2591  C   PHE A 391     -35.903 -23.504  64.609  1.00 83.76           C  
ANISOU 2591  C   PHE A 391    11554  12094   8175    235   -156    922       C  
ATOM   2592  O   PHE A 391     -36.437 -23.681  65.692  1.00 86.41           O  
ANISOU 2592  O   PHE A 391    11895  12447   8488    220   -166    932       O  
ATOM   2593  CB  PHE A 391     -34.041 -21.935  64.136  1.00 82.24           C  
ANISOU 2593  CB  PHE A 391    11473  11630   8143    421   -129    937       C  
ATOM   2594  CG  PHE A 391     -33.378 -22.434  62.889  1.00 82.43           C  
ANISOU 2594  CG  PHE A 391    11487  11641   8191    357   -135    895       C  
ATOM   2595  CD1 PHE A 391     -33.585 -21.805  61.669  1.00 82.62           C  
ANISOU 2595  CD1 PHE A 391    11447  11779   8164    415   -108    933       C  
ATOM   2596  CD2 PHE A 391     -32.520 -23.509  62.941  1.00 80.26           C  
ANISOU 2596  CD2 PHE A 391    11273  11238   7981    258   -161    824       C  
ATOM   2597  CE1 PHE A 391     -32.967 -22.274  60.529  1.00 83.90           C  
ANISOU 2597  CE1 PHE A 391    11599  11931   8345    352   -113    891       C  
ATOM   2598  CE2 PHE A 391     -31.901 -23.968  61.797  1.00 80.74           C  
ANISOU 2598  CE2 PHE A 391    11335  11284   8056    214   -157    784       C  
ATOM   2599  CZ  PHE A 391     -32.101 -23.359  60.597  1.00 82.16           C  
ANISOU 2599  CZ  PHE A 391    11446  11577   8193    250   -137    812       C  
ATOM   2600  N   VAL A 392     -35.641 -24.500  63.780  1.00 84.97           N  
ANISOU 2600  N   VAL A 392    11717  12246   8321     99   -164    861       N  
ATOM   2601  CA  VAL A 392     -35.826 -25.882  64.192  1.00 86.83           C  
ANISOU 2601  CA  VAL A 392    12011  12448   8530    -77   -176    797       C  
ATOM   2602  C   VAL A 392     -34.754 -26.328  65.173  1.00 86.44           C  
ANISOU 2602  C   VAL A 392    12100  12136   8604    -62   -190    762       C  
ATOM   2603  O   VAL A 392     -33.626 -25.888  65.116  1.00 83.77           O  
ANISOU 2603  O   VAL A 392    11808  11649   8369     32   -194    760       O  
ATOM   2604  CB  VAL A 392     -35.898 -26.847  62.980  1.00 90.20           C  
ANISOU 2604  CB  VAL A 392    12444  12939   8888   -239   -160    737       C  
ATOM   2605  CG1 VAL A 392     -34.669 -26.738  62.077  1.00 91.51           C  
ANISOU 2605  CG1 VAL A 392    12663  12954   9150   -180   -152    708       C  
ATOM   2606  CG2 VAL A 392     -36.118 -28.318  63.390  1.00 90.83           C  
ANISOU 2606  CG2 VAL A 392    12636  12953   8919   -440   -148    665       C  
ATOM   2607  N   GLY A 393     -35.146 -27.225  66.072  1.00 91.60           N  
ANISOU 2607  N   GLY A 393    12812  12760   9229   -165   -196    739       N  
ATOM   2608  CA  GLY A 393     -34.224 -27.989  66.955  1.00 93.20           C  
ANISOU 2608  CA  GLY A 393    13155  12736   9519   -170   -200    708       C  
ATOM   2609  C   GLY A 393     -33.264 -27.231  67.864  1.00 91.74           C  
ANISOU 2609  C   GLY A 393    12990  12419   9445    -23   -222    738       C  
ATOM   2610  O   GLY A 393     -32.171 -27.727  68.173  1.00 91.20           O  
ANISOU 2610  O   GLY A 393    13009  12193   9449      6   -223    720       O  
ATOM   2611  N   TYR A 394     -33.653 -26.040  68.302  1.00 90.69           N  
ANISOU 2611  N   TYR A 394    12784  12362   9312     67   -231    786       N  
ATOM   2612  CA  TYR A 394     -32.803 -25.264  69.209  1.00 91.56           C  
ANISOU 2612  CA  TYR A 394    12926  12357   9504    168   -243    805       C  
ATOM   2613  C   TYR A 394     -32.723 -25.920  70.604  1.00 95.59           C  
ANISOU 2613  C   TYR A 394    13496  12792  10032    136   -262    800       C  
ATOM   2614  O   TYR A 394     -31.638 -26.231  71.106  1.00 95.74           O  
ANISOU 2614  O   TYR A 394    13571  12690  10113    161   -273    791       O  
ATOM   2615  CB  TYR A 394     -33.308 -23.832  69.330  1.00 90.27           C  
ANISOU 2615  CB  TYR A 394    12713  12268   9315    269   -225    853       C  
ATOM   2616  CG  TYR A 394     -32.744 -22.819  68.362  1.00 90.67           C  
ANISOU 2616  CG  TYR A 394    12758  12303   9389    348   -200    867       C  
ATOM   2617  CD1 TYR A 394     -31.542 -23.029  67.652  1.00 91.58           C  
ANISOU 2617  CD1 TYR A 394    12900  12328   9567    332   -207    834       C  
ATOM   2618  CD2 TYR A 394     -33.392 -21.603  68.180  1.00 90.15           C  
ANISOU 2618  CD2 TYR A 394    12669  12310   9271    452   -160    921       C  
ATOM   2619  CE1 TYR A 394     -31.049 -22.076  66.770  1.00 90.68           C  
ANISOU 2619  CE1 TYR A 394    12783  12206   9464    390   -182    847       C  
ATOM   2620  CE2 TYR A 394     -32.886 -20.644  67.321  1.00 89.41           C  
ANISOU 2620  CE2 TYR A 394    12598  12184   9189    523   -125    939       C  
ATOM   2621  CZ  TYR A 394     -31.713 -20.886  66.633  1.00 89.70           C  
ANISOU 2621  CZ  TYR A 394    12656  12135   9291    478   -140    898       C  
ATOM   2622  OH  TYR A 394     -31.209 -19.943  65.784  1.00 92.04           O  
ANISOU 2622  OH  TYR A 394    12976  12401   9591    532   -104    915       O  
ATOM   2623  N   LYS A 395     -33.887 -26.188  71.190  1.00 97.87           N  
ANISOU 2623  N   LYS A 395    13760  13176  10249     80   -264    813       N  
ATOM   2624  CA  LYS A 395     -33.988 -26.996  72.402  1.00 96.95           C  
ANISOU 2624  CA  LYS A 395    13704  13002  10131     25   -278    809       C  
ATOM   2625  C   LYS A 395     -33.631 -28.458  72.110  1.00 97.55           C  
ANISOU 2625  C   LYS A 395    13884  12980  10201    -69   -263    771       C  
ATOM   2626  O   LYS A 395     -32.607 -28.940  72.627  1.00 95.73           O  
ANISOU 2626  O   LYS A 395    13734  12607  10029    -23   -264    771       O  
ATOM   2627  CB  LYS A 395     -35.385 -26.861  73.015  1.00 95.83           C  
ANISOU 2627  CB  LYS A 395    13500  13014   9897    -18   -280    834       C  
ATOM   2628  CG  LYS A 395     -35.743 -27.800  74.155  1.00 95.51           C  
ANISOU 2628  CG  LYS A 395    13518  12943   9828   -108   -291    828       C  
ATOM   2629  CD  LYS A 395     -37.043 -27.334  74.811  1.00 96.26           C  
ANISOU 2629  CD  LYS A 395    13522  13218   9832   -118   -295    862       C  
ATOM   2630  CE  LYS A 395     -37.786 -28.322  75.688  1.00 99.44           C  
ANISOU 2630  CE  LYS A 395    13957  13661  10162   -254   -301    856       C  
ATOM   2631  NZ  LYS A 395     -37.917 -29.682  75.132  1.00101.04           N  
ANISOU 2631  NZ  LYS A 395    14248  13831  10308   -431   -280    812       N  
ATOM   2632  N   ASN A 396     -34.431 -29.137  71.272  1.00 98.58           N  
ANISOU 2632  N   ASN A 396    14019  13190  10244   -195   -240    743       N  
ATOM   2633  CA  ASN A 396     -34.189 -30.568  70.952  1.00100.37           C  
ANISOU 2633  CA  ASN A 396    14393  13299  10442   -305   -201    698       C  
ATOM   2634  C   ASN A 396     -33.215 -30.777  69.814  1.00 98.03           C  
ANISOU 2634  C   ASN A 396    14144  12910  10190   -260   -176    670       C  
ATOM   2635  O   ASN A 396     -33.616 -30.843  68.652  1.00 97.73           O  
ANISOU 2635  O   ASN A 396    14078  12958  10096   -339   -156    640       O  
ATOM   2636  CB  ASN A 396     -35.497 -31.251  70.650  1.00103.74           C  
ANISOU 2636  CB  ASN A 396    14824  13859  10730   -506   -177    669       C  
ATOM   2637  CG  ASN A 396     -36.471 -31.119  71.799  1.00105.86           C  
ANISOU 2637  CG  ASN A 396    15040  14239  10942   -555   -200    698       C  
ATOM   2638  OD1 ASN A 396     -37.480 -30.442  71.704  1.00104.86           O  
ANISOU 2638  OD1 ASN A 396    14766  14337  10739   -574   -218    723       O  
ATOM   2639  ND2 ASN A 396     -36.137 -31.738  72.907  1.00107.99           N  
ANISOU 2639  ND2 ASN A 396    15425  14363  11242   -553   -197    706       N  
ATOM   2640  N   TYR A 397     -31.930 -30.864  70.186  1.00 97.48           N  
ANISOU 2640  N   TYR A 397    14135  12693  10209   -131   -176    686       N  
ATOM   2641  CA  TYR A 397     -30.796 -30.833  69.246  1.00 98.56           C  
ANISOU 2641  CA  TYR A 397    14286  12763  10397    -42   -161    675       C  
ATOM   2642  C   TYR A 397     -30.761 -31.997  68.283  1.00100.84           C  
ANISOU 2642  C   TYR A 397    14711  12970  10631   -123    -97    625       C  
ATOM   2643  O   TYR A 397     -30.268 -31.865  67.151  1.00108.27           O  
ANISOU 2643  O   TYR A 397    15633  13916  11585    -96    -82    603       O  
ATOM   2644  CB  TYR A 397     -29.442 -30.681  69.974  1.00 98.84           C  
ANISOU 2644  CB  TYR A 397    14331  12714  10510    113   -176    713       C  
ATOM   2645  CG  TYR A 397     -29.007 -31.861  70.809  1.00 99.75           C  
ANISOU 2645  CG  TYR A 397    14592  12697  10611    149   -140    731       C  
ATOM   2646  CD1 TYR A 397     -28.248 -32.903  70.258  1.00102.04           C  
ANISOU 2646  CD1 TYR A 397    15022  12863  10885    206    -76    723       C  
ATOM   2647  CD2 TYR A 397     -29.330 -31.916  72.159  1.00102.59           C  
ANISOU 2647  CD2 TYR A 397    14959  13052  10965    145   -162    764       C  
ATOM   2648  CE1 TYR A 397     -27.853 -33.977  71.014  1.00106.03           C  
ANISOU 2648  CE1 TYR A 397    15684  13238  11363    271    -26    754       C  
ATOM   2649  CE2 TYR A 397     -28.922 -32.972  72.940  1.00108.20           C  
ANISOU 2649  CE2 TYR A 397    15809  13645  11657    195   -124    793       C  
ATOM   2650  CZ  TYR A 397     -28.188 -34.002  72.358  1.00112.01           C  
ANISOU 2650  CZ  TYR A 397    16441  13999  12118    266    -52    792       C  
ATOM   2651  OH  TYR A 397     -27.830 -35.074  73.138  1.00127.43           O  
ANISOU 2651  OH  TYR A 397    18558  15823  14035    340      3    835       O  
ATOM   2652  N   ARG A 398     -31.345 -33.102  68.704  1.00101.90           N  
ANISOU 2652  N   ARG A 398    14992  13030  10693   -240    -52    604       N  
ATOM   2653  CA  ARG A 398     -31.477 -34.237  67.829  1.00106.16           C  
ANISOU 2653  CA  ARG A 398    15702  13479  11154   -358     26    545       C  
ATOM   2654  C   ARG A 398     -32.350 -33.981  66.583  1.00101.58           C  
ANISOU 2654  C   ARG A 398    15035  13062  10495   -518     28    495       C  
ATOM   2655  O   ARG A 398     -32.123 -34.607  65.573  1.00103.06           O  
ANISOU 2655  O   ARG A 398    15327  13188  10640   -578     86    444       O  
ATOM   2656  CB  ARG A 398     -31.980 -35.418  68.637  1.00116.08           C  
ANISOU 2656  CB  ARG A 398    17158  14613  12331   -475     84    533       C  
ATOM   2657  CG  ARG A 398     -30.960 -35.870  69.672  1.00126.33           C  
ANISOU 2657  CG  ARG A 398    18571  15736  13690   -292    104    589       C  
ATOM   2658  CD  ARG A 398     -31.580 -36.759  70.748  1.00136.49           C  
ANISOU 2658  CD  ARG A 398    20021  16931  14908   -393    143    598       C  
ATOM   2659  NE  ARG A 398     -30.538 -37.521  71.434  1.00142.94           N  
ANISOU 2659  NE  ARG A 398    21010  17550  15749   -211    200    652       N  
ATOM   2660  CZ  ARG A 398     -29.996 -38.670  71.000  1.00153.47           C  
ANISOU 2660  CZ  ARG A 398    22604  18675  17030   -169    316    639       C  
ATOM   2661  NH1 ARG A 398     -30.379 -39.269  69.862  1.00153.84           N  
ANISOU 2661  NH1 ARG A 398    22796  18658  16995   -327    393    560       N  
ATOM   2662  NH2 ARG A 398     -29.042 -39.249  71.729  1.00161.74           N  
ANISOU 2662  NH2 ARG A 398    23781  19578  18092     42    366    713       N  
ATOM   2663  N   TYR A 399     -33.330 -33.080  66.647  1.00 98.87           N  
ANISOU 2663  N   TYR A 399    14505  12939  10121   -574    -28    514       N  
ATOM   2664  CA  TYR A 399     -34.136 -32.740  65.468  1.00 99.65           C  
ANISOU 2664  CA  TYR A 399    14486  13242  10131   -694    -30    486       C  
ATOM   2665  C   TYR A 399     -33.378 -31.852  64.528  1.00102.77           C  
ANISOU 2665  C   TYR A 399    14775  13666  10606   -550    -52    502       C  
ATOM   2666  O   TYR A 399     -33.583 -31.896  63.311  1.00105.55           O  
ANISOU 2666  O   TYR A 399    15093  14111  10898   -628    -31    467       O  
ATOM   2667  CB  TYR A 399     -35.424 -32.032  65.839  1.00101.41           C  
ANISOU 2667  CB  TYR A 399    14533  13721  10276   -758    -74    523       C  
ATOM   2668  CG  TYR A 399     -36.528 -32.949  66.294  1.00105.28           C  
ANISOU 2668  CG  TYR A 399    15089  14288  10622   -990    -46    490       C  
ATOM   2669  CD1 TYR A 399     -37.310 -33.640  65.383  1.00105.69           C  
ANISOU 2669  CD1 TYR A 399    15165  14476  10514  -1234     -2    429       C  
ATOM   2670  CD2 TYR A 399     -36.793 -33.127  67.647  1.00107.86           C  
ANISOU 2670  CD2 TYR A 399    15456  14566  10958   -988    -61    518       C  
ATOM   2671  CE1 TYR A 399     -38.321 -34.480  65.796  1.00107.83           C  
ANISOU 2671  CE1 TYR A 399    15503  14836  10631  -1485     28    393       C  
ATOM   2672  CE2 TYR A 399     -37.814 -33.970  68.073  1.00109.76           C  
ANISOU 2672  CE2 TYR A 399    15761  14886  11054  -1221    -32    488       C  
ATOM   2673  CZ  TYR A 399     -38.570 -34.644  67.146  1.00110.34           C  
ANISOU 2673  CZ  TYR A 399    15864  15097  10963  -1476     13    424       C  
ATOM   2674  OH  TYR A 399     -39.579 -35.469  67.611  1.00115.14           O  
ANISOU 2674  OH  TYR A 399    16540  15797  11408  -1739     45    391       O  
ATOM   2675  N   ARG A 400     -32.499 -31.032  65.095  1.00107.82           N  
ANISOU 2675  N   ARG A 400    15362  14236  11367   -355    -92    552       N  
ATOM   2676  CA  ARG A 400     -31.566 -30.185  64.321  1.00111.86           C  
ANISOU 2676  CA  ARG A 400    15795  14745  11958   -218   -108    568       C  
ATOM   2677  C   ARG A 400     -30.628 -31.036  63.402  1.00111.07           C  
ANISOU 2677  C   ARG A 400    15816  14517  11868   -213    -58    521       C  
ATOM   2678  O   ARG A 400     -30.241 -30.612  62.288  1.00104.16           O  
ANISOU 2678  O   ARG A 400    14879  13692  11005   -182    -57    510       O  
ATOM   2679  CB  ARG A 400     -30.757 -29.276  65.280  1.00113.58           C  
ANISOU 2679  CB  ARG A 400    15965  14908  12279    -55   -150    622       C  
ATOM   2680  CG  ARG A 400     -30.395 -27.906  64.696  1.00115.83           C  
ANISOU 2680  CG  ARG A 400    16129  15272  12609     40   -175    652       C  
ATOM   2681  CD  ARG A 400     -30.031 -26.877  65.749  1.00115.40           C  
ANISOU 2681  CD  ARG A 400    16035  15199  12613    138   -206    697       C  
ATOM   2682  NE  ARG A 400     -28.896 -27.426  66.529  1.00116.90           N  
ANISOU 2682  NE  ARG A 400    16296  15263  12857    191   -211    696       N  
ATOM   2683  CZ  ARG A 400     -28.712 -27.344  67.846  1.00115.70           C  
ANISOU 2683  CZ  ARG A 400    16160  15073  12728    222   -231    720       C  
ATOM   2684  NH1 ARG A 400     -29.596 -26.715  68.628  1.00113.51           N  
ANISOU 2684  NH1 ARG A 400    15846  14849  12431    205   -247    742       N  
ATOM   2685  NH2 ARG A 400     -27.625 -27.928  68.344  1.00115.41           N  
ANISOU 2685  NH2 ARG A 400    16171  14958  12719    283   -230    727       N  
ATOM   2686  N   ALA A 401     -30.294 -32.246  63.877  1.00111.49           N  
ANISOU 2686  N   ALA A 401    16052  14401  11906   -234     -8    497       N  
ATOM   2687  CA  ALA A 401     -29.525 -33.231  63.086  1.00107.16           C  
ANISOU 2687  CA  ALA A 401    15664  13709  11340   -222     64    452       C  
ATOM   2688  C   ALA A 401     -30.213 -33.625  61.783  1.00102.75           C  
ANISOU 2688  C   ALA A 401    15133  13224  10682   -399    107    383       C  
ATOM   2689  O   ALA A 401     -29.610 -33.562  60.718  1.00102.18           O  
ANISOU 2689  O   ALA A 401    15052  13150  10622   -358    127    360       O  
ATOM   2690  CB  ALA A 401     -29.234 -34.478  63.907  1.00106.97           C  
ANISOU 2690  CB  ALA A 401    15866  13484  11291   -207    131    449       C  
ATOM   2691  N   GLY A 402     -31.468 -34.032  61.877  1.00 99.91           N  
ANISOU 2691  N   GLY A 402    14797  12952  10211   -609    122    350       N  
ATOM   2692  CA  GLY A 402     -32.178 -34.558  60.718  1.00102.20           C  
ANISOU 2692  CA  GLY A 402    15126  13333  10369   -824    172    276       C  
ATOM   2693  C   GLY A 402     -32.843 -33.528  59.828  1.00101.73           C  
ANISOU 2693  C   GLY A 402    14825  13554  10273   -867    117    291       C  
ATOM   2694  O   GLY A 402     -33.309 -33.886  58.755  1.00102.89           O  
ANISOU 2694  O   GLY A 402    14977  13806  10308  -1033    154    233       O  
ATOM   2695  N   PHE A 403     -32.964 -32.286  60.298  1.00 98.80           N  
ANISOU 2695  N   PHE A 403    14256  13309   9974   -726     39    369       N  
ATOM   2696  CA  PHE A 403     -33.594 -31.227  59.532  1.00 97.82           C  
ANISOU 2696  CA  PHE A 403    13915  13444   9808   -719     -1    406       C  
ATOM   2697  C   PHE A 403     -32.648 -30.092  59.157  1.00 98.17           C  
ANISOU 2697  C   PHE A 403    13860  13462   9975   -504    -36    457       C  
ATOM   2698  O   PHE A 403     -33.059 -29.160  58.464  1.00 98.00           O  
ANISOU 2698  O   PHE A 403    13681  13629   9923   -467    -58    498       O  
ATOM   2699  CB  PHE A 403     -34.754 -30.662  60.342  1.00 98.94           C  
ANISOU 2699  CB  PHE A 403    13923  13781   9889   -744    -41    462       C  
ATOM   2700  CG  PHE A 403     -35.993 -31.547  60.350  1.00101.28           C  
ANISOU 2700  CG  PHE A 403    14238  14236  10006  -1006    -12    417       C  
ATOM   2701  CD1 PHE A 403     -36.722 -31.776  59.177  1.00100.20           C  
ANISOU 2701  CD1 PHE A 403    14025  14331   9713  -1188     11    379       C  
ATOM   2702  CD2 PHE A 403     -36.479 -32.104  61.555  1.00 99.29           C  
ANISOU 2702  CD2 PHE A 403    14067  13934   9722  -1089     -9    414       C  
ATOM   2703  CE1 PHE A 403     -37.883 -32.552  59.213  1.00100.82           C  
ANISOU 2703  CE1 PHE A 403    14109  14597   9599  -1465     39    335       C  
ATOM   2704  CE2 PHE A 403     -37.630 -32.886  61.571  1.00 97.75           C  
ANISOU 2704  CE2 PHE A 403    13888  13907   9344  -1359     19    370       C  
ATOM   2705  CZ  PHE A 403     -38.330 -33.107  60.412  1.00 99.52           C  
ANISOU 2705  CZ  PHE A 403    14035  14372   9404  -1555     44    329       C  
ATOM   2706  N   VAL A 404     -31.412 -30.120  59.650  1.00 99.56           N  
ANISOU 2706  N   VAL A 404    14123  13428  10274   -361    -39    464       N  
ATOM   2707  CA  VAL A 404     -30.420 -29.094  59.295  1.00 99.77           C  
ANISOU 2707  CA  VAL A 404    14070  13435  10401   -192    -67    504       C  
ATOM   2708  C   VAL A 404     -29.167 -29.810  58.829  1.00 97.64           C  
ANISOU 2708  C   VAL A 404    13915  13004  10178   -141    -31    463       C  
ATOM   2709  O   VAL A 404     -28.758 -29.614  57.699  1.00 95.99           O  
ANISOU 2709  O   VAL A 404    13669  12836   9967   -128    -20    447       O  
ATOM   2710  CB  VAL A 404     -30.092 -28.122  60.484  1.00104.22           C  
ANISOU 2710  CB  VAL A 404    14584  13961  11051    -55   -111    569       C  
ATOM   2711  CG1 VAL A 404     -29.326 -26.890  60.026  1.00105.05           C  
ANISOU 2711  CG1 VAL A 404    14606  14087  11221     66   -131    607       C  
ATOM   2712  CG2 VAL A 404     -31.360 -27.649  61.169  1.00105.55           C  
ANISOU 2712  CG2 VAL A 404    14679  14261  11163    -92   -131    608       C  
ATOM   2713  N   LEU A 405     -28.555 -30.626  59.698  1.00 98.29           N  
ANISOU 2713  N   LEU A 405    14133  12916  10293    -94     -8    456       N  
ATOM   2714  CA  LEU A 405     -27.318 -31.348  59.340  1.00 98.93           C  
ANISOU 2714  CA  LEU A 405    14328  12856  10403     -1     37    434       C  
ATOM   2715  C   LEU A 405     -27.478 -32.358  58.213  1.00 99.06           C  
ANISOU 2715  C   LEU A 405    14471  12828  10336   -109    113    360       C  
ATOM   2716  O   LEU A 405     -26.560 -32.526  57.403  1.00100.97           O  
ANISOU 2716  O   LEU A 405    14740  13028  10594    -28    144    344       O  
ATOM   2717  CB  LEU A 405     -26.677 -32.058  60.540  1.00102.19           C  
ANISOU 2717  CB  LEU A 405    14866  13115  10846     98     58    459       C  
ATOM   2718  CG  LEU A 405     -25.675 -31.254  61.395  1.00105.14           C  
ANISOU 2718  CG  LEU A 405    15137  13505  11305    263      4    526       C  
ATOM   2719  CD1 LEU A 405     -25.154 -32.085  62.570  1.00104.39           C  
ANISOU 2719  CD1 LEU A 405    15160  13288  11212    359     31    558       C  
ATOM   2720  CD2 LEU A 405     -24.474 -30.741  60.611  1.00106.18           C  
ANISOU 2720  CD2 LEU A 405    15185  13684  11472    375     -2    538       C  
ATOM   2721  N   ALA A 406     -28.616 -33.040  58.151  1.00 98.21           N  
ANISOU 2721  N   ALA A 406    14446  12741  10128   -304    148    312       N  
ATOM   2722  CA  ALA A 406     -28.851 -33.994  57.060  1.00 98.01           C  
ANISOU 2722  CA  ALA A 406    14559  12682   9998   -453    230    228       C  
ATOM   2723  C   ALA A 406     -28.932 -33.302  55.709  1.00 96.23           C  
ANISOU 2723  C   ALA A 406    14180  12630   9753   -488    207    214       C  
ATOM   2724  O   ALA A 406     -28.118 -33.594  54.858  1.00 96.70           O  
ANISOU 2724  O   ALA A 406    14299  12620   9820   -431    250    183       O  
ATOM   2725  CB  ALA A 406     -30.083 -34.844  57.324  1.00102.10           C  
ANISOU 2725  CB  ALA A 406    15197  13210  10384   -699    275    174       C  
ATOM   2726  N   PRO A 407     -29.857 -32.345  55.522  1.00 97.54           N  
ANISOU 2726  N   PRO A 407    14142  13026   9890   -553    143    247       N  
ATOM   2727  CA  PRO A 407     -29.879 -31.663  54.222  1.00 99.43           C  
ANISOU 2727  CA  PRO A 407    14236  13433  10106   -561    126    247       C  
ATOM   2728  C   PRO A 407     -28.576 -30.996  53.801  1.00 97.35           C  
ANISOU 2728  C   PRO A 407    13920  13110   9957   -363    106    280       C  
ATOM   2729  O   PRO A 407     -28.171 -31.118  52.656  1.00100.18           O  
ANISOU 2729  O   PRO A 407    14278  13492  10292   -377    134    244       O  
ATOM   2730  CB  PRO A 407     -31.035 -30.643  54.333  1.00100.12           C  
ANISOU 2730  CB  PRO A 407    14117  13776  10146   -597     66    309       C  
ATOM   2731  CG  PRO A 407     -31.422 -30.605  55.750  1.00101.47           C  
ANISOU 2731  CG  PRO A 407    14308  13899  10346   -572     40    347       C  
ATOM   2732  CD  PRO A 407     -30.960 -31.885  56.389  1.00101.22           C  
ANISOU 2732  CD  PRO A 407    14506  13628  10323   -614     95    290       C  
ATOM   2733  N   ILE A 408     -27.909 -30.326  54.709  1.00 96.08           N  
ANISOU 2733  N   ILE A 408    13716  12884   9904   -200     61    343       N  
ATOM   2734  CA  ILE A 408     -26.604 -29.750  54.377  1.00 97.92           C  
ANISOU 2734  CA  ILE A 408    13901  13077  10224    -41     46    371       C  
ATOM   2735  C   ILE A 408     -25.572 -30.861  54.063  1.00 98.99           C  
ANISOU 2735  C   ILE A 408    14192  13058  10358     14    111    323       C  
ATOM   2736  O   ILE A 408     -24.760 -30.726  53.111  1.00 98.35           O  
ANISOU 2736  O   ILE A 408    14080  12997  10288     75    125    312       O  
ATOM   2737  CB  ILE A 408     -26.122 -28.786  55.481  1.00100.74           C  
ANISOU 2737  CB  ILE A 408    14186  13419  10672     86    -10    442       C  
ATOM   2738  CG1 ILE A 408     -27.099 -27.613  55.581  1.00102.12           C  
ANISOU 2738  CG1 ILE A 408    14230  13736  10833     59    -52    493       C  
ATOM   2739  CG2 ILE A 408     -24.717 -28.244  55.205  1.00100.01           C  
ANISOU 2739  CG2 ILE A 408    14045  13311  10644    216    -22    466       C  
ATOM   2740  CD1 ILE A 408     -26.974 -26.826  56.877  1.00102.57           C  
ANISOU 2740  CD1 ILE A 408    14263  13758  10951    140    -90    549       C  
ATOM   2741  N   GLY A 409     -25.594 -31.960  54.834  1.00100.85           N  
ANISOU 2741  N   GLY A 409    14604  13141  10572      6    162    300       N  
ATOM   2742  CA  GLY A 409     -24.744 -33.130  54.532  1.00104.32           C  
ANISOU 2742  CA  GLY A 409    15234  13417  10983     77    252    261       C  
ATOM   2743  C   GLY A 409     -24.994 -33.636  53.102  1.00106.66           C  
ANISOU 2743  C   GLY A 409    15596  13732  11194    -45    315    181       C  
ATOM   2744  O   GLY A 409     -24.052 -33.851  52.328  1.00106.62           O  
ANISOU 2744  O   GLY A 409    15624  13693  11193     56    355    166       O  
ATOM   2745  N   LEU A 410     -26.276 -33.780  52.757  1.00106.70           N  
ANISOU 2745  N   LEU A 410    15604  13825  11112   -269    320    133       N  
ATOM   2746  CA  LEU A 410     -26.701 -34.151  51.418  1.00107.84           C  
ANISOU 2746  CA  LEU A 410    15779  14041  11153   -434    370     55       C  
ATOM   2747  C   LEU A 410     -26.270 -33.140  50.335  1.00105.98           C  
ANISOU 2747  C   LEU A 410    15341  13970  10956   -368    318     80       C  
ATOM   2748  O   LEU A 410     -25.666 -33.540  49.336  1.00106.27           O  
ANISOU 2748  O   LEU A 410    15441  13971  10963   -353    373     32       O  
ATOM   2749  CB  LEU A 410     -28.210 -34.357  51.390  1.00111.53           C  
ANISOU 2749  CB  LEU A 410    16236  14641  11498   -699    371     14       C  
ATOM   2750  CG  LEU A 410     -28.806 -34.995  50.130  1.00120.15           C  
ANISOU 2750  CG  LEU A 410    17397  15815  12437   -936    440    -83       C  
ATOM   2751  CD1 LEU A 410     -29.883 -36.030  50.497  1.00122.03           C  
ANISOU 2751  CD1 LEU A 410    17815  16024  12525  -1208    508   -156       C  
ATOM   2752  CD2 LEU A 410     -29.331 -33.945  49.119  1.00122.43           C  
ANISOU 2752  CD2 LEU A 410    17416  16407  12693   -990    370    -56       C  
ATOM   2753  N   VAL A 411     -26.524 -31.843  50.517  1.00103.71           N  
ANISOU 2753  N   VAL A 411    14830  13845  10726   -318    225    155       N  
ATOM   2754  CA  VAL A 411     -26.128 -30.882  49.470  1.00105.75           C  
ANISOU 2754  CA  VAL A 411    14922  14245  11010   -261    188    183       C  
ATOM   2755  C   VAL A 411     -24.611 -30.847  49.338  1.00106.30           C  
ANISOU 2755  C   VAL A 411    15017  14210  11162    -76    198    196       C  
ATOM   2756  O   VAL A 411     -24.095 -30.599  48.233  1.00109.83           O  
ANISOU 2756  O   VAL A 411    15405  14723  11600    -55    206    183       O  
ATOM   2757  CB  VAL A 411     -26.689 -29.429  49.590  1.00106.54           C  
ANISOU 2757  CB  VAL A 411    14811  14527  11140   -229    107    268       C  
ATOM   2758  CG1 VAL A 411     -28.199 -29.421  49.787  1.00109.54           C  
ANISOU 2758  CG1 VAL A 411    15137  15060  11422   -380     97    273       C  
ATOM   2759  CG2 VAL A 411     -25.981 -28.612  50.654  1.00109.44           C  
ANISOU 2759  CG2 VAL A 411    15137  14820  11622    -65     58    341       C  
ATOM   2760  N   LEU A 412     -23.892 -31.080  50.446  1.00106.35           N  
ANISOU 2760  N   LEU A 412    15092  14081  11233     56    198    228       N  
ATOM   2761  CA  LEU A 412     -22.437 -31.242  50.314  1.00106.07           C  
ANISOU 2761  CA  LEU A 412    15079  13983  11240    232    220    243       C  
ATOM   2762  C   LEU A 412     -22.030 -32.421  49.422  1.00102.33           C  
ANISOU 2762  C   LEU A 412    14773  13411  10694    236    322    171       C  
ATOM   2763  O   LEU A 412     -21.195 -32.253  48.530  1.00102.54           O  
ANISOU 2763  O   LEU A 412    14748  13490  10722    313    334    166       O  
ATOM   2764  CB  LEU A 412     -21.754 -31.373  51.677  1.00107.26           C  
ANISOU 2764  CB  LEU A 412    15264  14042  11444    378    208    297       C  
ATOM   2765  CG  LEU A 412     -21.434 -30.060  52.389  1.00106.20           C  
ANISOU 2765  CG  LEU A 412    14954  14010  11384    434    118    372       C  
ATOM   2766  CD1 LEU A 412     -20.862 -30.433  53.741  1.00110.42           C  
ANISOU 2766  CD1 LEU A 412    15542  14465  11945    552    118    415       C  
ATOM   2767  CD2 LEU A 412     -20.440 -29.198  51.629  1.00104.91           C  
ANISOU 2767  CD2 LEU A 412    14653  13964  11243    500     90    397       C  
ATOM   2768  N   ILE A 413     -22.625 -33.585  49.657  1.00 99.19           N  
ANISOU 2768  N   ILE A 413    14589  12871  10226    145    401    113       N  
ATOM   2769  CA  ILE A 413     -22.277 -34.782  48.900  1.00101.49           C  
ANISOU 2769  CA  ILE A 413    15101  13026  10434    144    524     38       C  
ATOM   2770  C   ILE A 413     -22.720 -34.646  47.435  1.00103.53           C  
ANISOU 2770  C   ILE A 413    15308  13404  10623    -18    537    -30       C  
ATOM   2771  O   ILE A 413     -21.912 -34.862  46.512  1.00103.01           O  
ANISOU 2771  O   ILE A 413    15270  13330  10538     63    586    -56       O  
ATOM   2772  CB  ILE A 413     -22.842 -36.061  49.543  1.00103.01           C  
ANISOU 2772  CB  ILE A 413    15579  13009  10548     61    624    -11       C  
ATOM   2773  CG1 ILE A 413     -22.081 -36.379  50.823  1.00104.16           C  
ANISOU 2773  CG1 ILE A 413    15804  13022  10749    283    638     63       C  
ATOM   2774  CG2 ILE A 413     -22.705 -37.258  48.627  1.00106.88           C  
ANISOU 2774  CG2 ILE A 413    16336  13346  10924      6    770   -106       C  
ATOM   2775  CD1 ILE A 413     -22.819 -37.331  51.741  1.00107.05           C  
ANISOU 2775  CD1 ILE A 413    16406  13208  11058    189    706     39       C  
ATOM   2776  N   VAL A 414     -23.959 -34.210  47.216  1.00104.26           N  
ANISOU 2776  N   VAL A 414    15298  13642  10673   -231    488    -49       N  
ATOM   2777  CA  VAL A 414     -24.471 -34.070  45.844  1.00104.49           C  
ANISOU 2777  CA  VAL A 414    15257  13826  10616   -397    498   -106       C  
ATOM   2778  C   VAL A 414     -23.790 -32.906  45.094  1.00100.79           C  
ANISOU 2778  C   VAL A 414    14558  13517  10219   -276    425    -49       C  
ATOM   2779  O   VAL A 414     -23.249 -33.087  44.004  1.00 99.28           O  
ANISOU 2779  O   VAL A 414    14380  13348   9994   -265    466    -90       O  
ATOM   2780  CB  VAL A 414     -26.012 -33.914  45.812  1.00107.01           C  
ANISOU 2780  CB  VAL A 414    15502  14316  10840   -650    467   -127       C  
ATOM   2781  CG1 VAL A 414     -26.508 -33.859  44.383  1.00109.38           C  
ANISOU 2781  CG1 VAL A 414    15727  14804  11027   -824    485   -184       C  
ATOM   2782  CG2 VAL A 414     -26.705 -35.080  46.501  1.00107.71           C  
ANISOU 2782  CG2 VAL A 414    15827  14258  10837   -812    545   -192       C  
ATOM   2783  N   GLY A 415     -23.818 -31.720  45.681  1.00100.52           N  
ANISOU 2783  N   GLY A 415    14333  13586  10273   -194    326     43       N  
ATOM   2784  CA  GLY A 415     -23.167 -30.560  45.095  1.00104.21           C  
ANISOU 2784  CA  GLY A 415    14610  14181  10801    -91    266    103       C  
ATOM   2785  C   GLY A 415     -21.679 -30.779  44.864  1.00108.86           C  
ANISOU 2785  C   GLY A 415    15236  14689  11434     80    295    104       C  
ATOM   2786  O   GLY A 415     -21.100 -30.396  43.798  1.00109.75           O  
ANISOU 2786  O   GLY A 415    15263  14896  11540    108    294    101       O  
ATOM   2787  N   GLY A 416     -21.048 -31.376  45.872  1.00111.75           N  
ANISOU 2787  N   GLY A 416    15717  14905  11835    206    322    117       N  
ATOM   2788  CA  GLY A 416     -19.641 -31.716  45.796  1.00116.45           C  
ANISOU 2788  CA  GLY A 416    16347  15450  12448    397    360    131       C  
ATOM   2789  C   GLY A 416     -19.351 -32.717  44.701  1.00118.86           C  
ANISOU 2789  C   GLY A 416    16798  15692  12669    393    463     51       C  
ATOM   2790  O   GLY A 416     -18.377 -32.551  43.953  1.00119.71           O  
ANISOU 2790  O   GLY A 416    16840  15868  12774    500    474     59       O  
ATOM   2791  N   TYR A 417     -20.200 -33.744  44.588  1.00118.73           N  
ANISOU 2791  N   TYR A 417    16986  15552  12572    254    544    -27       N  
ATOM   2792  CA  TYR A 417     -20.056 -34.685  43.468  1.00118.79           C  
ANISOU 2792  CA  TYR A 417    17163  15489  12481    208    657   -119       C  
ATOM   2793  C   TYR A 417     -20.044 -33.981  42.130  1.00113.01           C  
ANISOU 2793  C   TYR A 417    16259  14947  11732    130    619   -138       C  
ATOM   2794  O   TYR A 417     -19.092 -34.140  41.402  1.00112.48           O  
ANISOU 2794  O   TYR A 417    16198  14886  11650    250    661   -148       O  
ATOM   2795  CB  TYR A 417     -21.164 -35.704  43.482  1.00123.84           C  
ANISOU 2795  CB  TYR A 417    18035  16001  13015     -9    743   -212       C  
ATOM   2796  CG  TYR A 417     -21.163 -36.643  42.325  1.00126.57           C  
ANISOU 2796  CG  TYR A 417    18580  16271  13237   -109    869   -322       C  
ATOM   2797  CD1 TYR A 417     -20.330 -37.768  42.328  1.00128.91           C  
ANISOU 2797  CD1 TYR A 417    19157  16337  13484     50   1012   -355       C  
ATOM   2798  CD2 TYR A 417     -22.035 -36.441  41.239  1.00125.68           C  
ANISOU 2798  CD2 TYR A 417    18391  16320  13039   -365    858   -392       C  
ATOM   2799  CE1 TYR A 417     -20.353 -38.661  41.267  1.00132.88           C  
ANISOU 2799  CE1 TYR A 417    19883  16745  13861    -50   1147   -466       C  
ATOM   2800  CE2 TYR A 417     -22.057 -37.323  40.176  1.00128.36           C  
ANISOU 2800  CE2 TYR A 417    18927  16593  13251   -486    980   -504       C  
ATOM   2801  CZ  TYR A 417     -21.223 -38.428  40.190  1.00130.86           C  
ANISOU 2801  CZ  TYR A 417    19544  16651  13523   -337   1127   -547       C  
ATOM   2802  OH  TYR A 417     -21.257 -39.293  39.136  1.00133.18           O  
ANISOU 2802  OH  TYR A 417    20061  16860  13680   -463   1263   -665       O  
ATOM   2803  N   PHE A 418     -21.060 -33.165  41.851  1.00111.10           N  
ANISOU 2803  N   PHE A 418    15852  14873  11486    -46    539   -128       N  
ATOM   2804  CA  PHE A 418     -21.124 -32.402  40.586  1.00110.19           C  
ANISOU 2804  CA  PHE A 418    15560  14958  11348   -114    500   -129       C  
ATOM   2805  C   PHE A 418     -20.000 -31.404  40.405  1.00107.19           C  
ANISOU 2805  C   PHE A 418    15001  14670  11055     63    436    -50       C  
ATOM   2806  O   PHE A 418     -19.517 -31.258  39.304  1.00104.73           O  
ANISOU 2806  O   PHE A 418    14631  14446  10714     71    451    -70       O  
ATOM   2807  CB  PHE A 418     -22.453 -31.647  40.412  1.00110.09           C  
ANISOU 2807  CB  PHE A 418    15392  15135  11301   -298    431   -107       C  
ATOM   2808  CG  PHE A 418     -23.663 -32.539  40.248  1.00114.10           C  
ANISOU 2808  CG  PHE A 418    16026  15647  11677   -540    490   -195       C  
ATOM   2809  CD1 PHE A 418     -23.621 -33.659  39.441  1.00115.88           C  
ANISOU 2809  CD1 PHE A 418    16444  15793  11789   -657    599   -309       C  
ATOM   2810  CD2 PHE A 418     -24.871 -32.235  40.871  1.00116.11           C  
ANISOU 2810  CD2 PHE A 418    16208  16005  11900   -666    441   -165       C  
ATOM   2811  CE1 PHE A 418     -24.734 -34.478  39.294  1.00117.30           C  
ANISOU 2811  CE1 PHE A 418    16755  15989  11824   -924    662   -399       C  
ATOM   2812  CE2 PHE A 418     -25.979 -33.064  40.730  1.00116.28           C  
ANISOU 2812  CE2 PHE A 418    16334  16068  11776   -919    496   -247       C  
ATOM   2813  CZ  PHE A 418     -25.907 -34.186  39.943  1.00117.61           C  
ANISOU 2813  CZ  PHE A 418    16705  16153  11828  -1063    606   -368       C  
ATOM   2814  N   LEU A 419     -19.567 -30.737  41.474  1.00107.23           N  
ANISOU 2814  N   LEU A 419    14925  14663  11154    186    371     33       N  
ATOM   2815  CA  LEU A 419     -18.342 -29.908  41.369  1.00108.12           C  
ANISOU 2815  CA  LEU A 419    14893  14861  11324    336    326     98       C  
ATOM   2816  C   LEU A 419     -17.051 -30.704  41.056  1.00112.15           C  
ANISOU 2816  C   LEU A 419    15483  15320  11807    500    398     76       C  
ATOM   2817  O   LEU A 419     -16.269 -30.294  40.222  1.00109.61           O  
ANISOU 2817  O   LEU A 419    15057  15115  11475    551    391     86       O  
ATOM   2818  CB  LEU A 419     -18.127 -29.081  42.628  1.00106.56           C  
ANISOU 2818  CB  LEU A 419    14611  14667  11209    406    253    183       C  
ATOM   2819  CG  LEU A 419     -18.963 -27.809  42.722  1.00104.85           C  
ANISOU 2819  CG  LEU A 419    14263  14551  11024    308    177    237       C  
ATOM   2820  CD1 LEU A 419     -19.029 -27.351  44.159  1.00105.79           C  
ANISOU 2820  CD1 LEU A 419    14375  14613  11206    350    131    295       C  
ATOM   2821  CD2 LEU A 419     -18.357 -26.708  41.892  1.00102.48           C  
ANISOU 2821  CD2 LEU A 419    13816  14389  10732    319    142    279       C  
ATOM   2822  N   ILE A 420     -16.834 -31.837  41.726  1.00119.70           N  
ANISOU 2822  N   ILE A 420    16629  16109  12739    597    476     52       N  
ATOM   2823  CA  ILE A 420     -15.646 -32.659  41.457  1.00123.42           C  
ANISOU 2823  CA  ILE A 420    17195  16534  13164    795    564     44       C  
ATOM   2824  C   ILE A 420     -15.727 -33.247  40.060  1.00123.19           C  
ANISOU 2824  C   ILE A 420    17259  16494  13051    728    647    -44       C  
ATOM   2825  O   ILE A 420     -14.742 -33.230  39.325  1.00123.76           O  
ANISOU 2825  O   ILE A 420    17274  16652  13095    850    673    -38       O  
ATOM   2826  CB  ILE A 420     -15.468 -33.849  42.432  1.00131.44           C  
ANISOU 2826  CB  ILE A 420    18441  17347  14151    935    656     43       C  
ATOM   2827  CG1 ILE A 420     -15.289 -33.407  43.884  1.00136.54           C  
ANISOU 2827  CG1 ILE A 420    19006  18005  14867   1019    585    132       C  
ATOM   2828  CG2 ILE A 420     -14.229 -34.665  42.058  1.00133.86           C  
ANISOU 2828  CG2 ILE A 420    18845  17624  14388   1180    763     50       C  
ATOM   2829  CD1 ILE A 420     -15.727 -34.493  44.868  1.00142.78           C  
ANISOU 2829  CD1 ILE A 420    20040  18575  15633   1060    663    120       C  
ATOM   2830  N   ARG A 421     -16.885 -33.808  39.712  1.00127.25           N  
ANISOU 2830  N   ARG A 421    17919  16917  13510    527    694   -129       N  
ATOM   2831  CA  ARG A 421     -17.086 -34.467  38.409  1.00133.59           C  
ANISOU 2831  CA  ARG A 421    18842  17703  14212    420    785   -230       C  
ATOM   2832  C   ARG A 421     -16.939 -33.498  37.205  1.00128.14           C  
ANISOU 2832  C   ARG A 421    17921  17240  13526    354    716   -222       C  
ATOM   2833  O   ARG A 421     -16.483 -33.913  36.124  1.00128.85           O  
ANISOU 2833  O   ARG A 421    18061  17348  13546    369    787   -279       O  
ATOM   2834  CB  ARG A 421     -18.424 -35.224  38.387  1.00137.90           C  
ANISOU 2834  CB  ARG A 421    19582  18138  14675    171    846   -324       C  
ATOM   2835  CG  ARG A 421     -18.424 -36.294  37.298  1.00143.24           C  
ANISOU 2835  CG  ARG A 421    20489  18716  15219     87    989   -444       C  
ATOM   2836  CD  ARG A 421     -19.685 -37.118  37.164  1.00149.67           C  
ANISOU 2836  CD  ARG A 421    21516  19437  15913   -203   1067   -555       C  
ATOM   2837  NE  ARG A 421     -19.633 -38.013  36.001  1.00156.62           N  
ANISOU 2837  NE  ARG A 421    22608  20244  16654   -310   1205   -677       N  
ATOM   2838  CZ  ARG A 421     -20.692 -38.628  35.455  1.00159.97           C  
ANISOU 2838  CZ  ARG A 421    23185  20660  16934   -629   1277   -796       C  
ATOM   2839  NH1 ARG A 421     -21.927 -38.473  35.966  1.00159.49           N  
ANISOU 2839  NH1 ARG A 421    23076  20681  16842   -871   1220   -803       N  
ATOM   2840  NH2 ARG A 421     -20.522 -39.403  34.376  1.00158.92           N  
ANISOU 2840  NH2 ARG A 421    23253  20457  16669   -718   1410   -910       N  
ATOM   2841  N   GLY A 422     -17.264 -32.223  37.433  1.00117.90           N  
ANISOU 2841  N   GLY A 422    16390  16102  12304    299    590   -146       N  
ATOM   2842  CA  GLY A 422     -17.031 -31.198  36.459  1.00111.77           C  
ANISOU 2842  CA  GLY A 422    15402  15527  11538    267    526   -115       C  
ATOM   2843  C   GLY A 422     -15.562 -30.859  36.229  1.00111.11           C  
ANISOU 2843  C   GLY A 422    15218  15518  11480    458    518    -67       C  
ATOM   2844  O   GLY A 422     -15.112 -30.813  35.072  1.00118.32           O  
ANISOU 2844  O   GLY A 422    16080  16530  12346    457    541    -95       O  
ATOM   2845  N   VAL A 423     -14.791 -30.592  37.276  1.00111.91           N  
ANISOU 2845  N   VAL A 423    15273  15606  11640    612    483      6       N  
ATOM   2846  CA  VAL A 423     -13.350 -30.263  37.090  1.00117.16           C  
ANISOU 2846  CA  VAL A 423    15816  16396  12301    781    474     57       C  
ATOM   2847  C   VAL A 423     -12.601 -31.463  36.520  1.00120.64           C  
ANISOU 2847  C   VAL A 423    16400  16777  12658    932    593      4       C  
ATOM   2848  O   VAL A 423     -11.641 -31.282  35.780  1.00123.48           O  
ANISOU 2848  O   VAL A 423    16659  17277  12981   1023    603     17       O  
ATOM   2849  CB  VAL A 423     -12.566 -29.753  38.352  1.00121.19           C  
ANISOU 2849  CB  VAL A 423    16229  16954  12861    907    417    149       C  
ATOM   2850  CG1 VAL A 423     -12.902 -28.308  38.720  1.00119.94           C  
ANISOU 2850  CG1 VAL A 423    15908  16893  12768    780    307    211       C  
ATOM   2851  CG2 VAL A 423     -12.745 -30.665  39.564  1.00126.34           C  
ANISOU 2851  CG2 VAL A 423    17047  17433  13522   1005    462    152       C  
ATOM   2852  N   MET A 424     -13.041 -32.675  36.866  1.00123.69           N  
ANISOU 2852  N   MET A 424    17036  16954  13006    960    693    -53       N  
ATOM   2853  CA  MET A 424     -12.511 -33.904  36.260  1.00128.35           C  
ANISOU 2853  CA  MET A 424    17831  17435  13498   1094    838   -116       C  
ATOM   2854  C   MET A 424     -12.690 -33.866  34.739  1.00131.10           C  
ANISOU 2854  C   MET A 424    18160  17862  13787    963    866   -194       C  
ATOM   2855  O   MET A 424     -11.727 -34.128  33.981  1.00136.47           O  
ANISOU 2855  O   MET A 424    18830  18612  14408   1108    925   -201       O  
ATOM   2856  CB  MET A 424     -13.143 -35.167  36.880  1.00129.95           C  
ANISOU 2856  CB  MET A 424    18354  17363  13659   1095    954   -174       C  
ATOM   2857  CG  MET A 424     -12.495 -35.493  38.226  1.00132.18           C  
ANISOU 2857  CG  MET A 424    18683  17574  13965   1332    969    -87       C  
ATOM   2858  SD  MET A 424     -12.928 -36.979  39.145  1.00135.54           S  
ANISOU 2858  SD  MET A 424    19497  17666  14333   1411   1119   -121       S  
ATOM   2859  CE  MET A 424     -11.768 -38.186  38.515  1.00137.17           C  
ANISOU 2859  CE  MET A 424    19936  17772  14409   1719   1314   -135       C  
ATOM   2860  N   THR A 425     -13.884 -33.456  34.304  1.00127.52           N  
ANISOU 2860  N   THR A 425    17672  17435  13342    701    816   -240       N  
ATOM   2861  CA  THR A 425     -14.191 -33.288  32.884  1.00127.26           C  
ANISOU 2861  CA  THR A 425    17587  17516  13249    547    825   -305       C  
ATOM   2862  C   THR A 425     -13.305 -32.191  32.279  1.00123.74           C  
ANISOU 2862  C   THR A 425    16875  17301  12838    617    741   -233       C  
ATOM   2863  O   THR A 425     -12.691 -32.427  31.239  1.00129.88           O  
ANISOU 2863  O   THR A 425    17647  18149  13552    664    795   -271       O  
ATOM   2864  CB  THR A 425     -15.707 -33.011  32.642  1.00128.19           C  
ANISOU 2864  CB  THR A 425    17687  17669  13351    259    782   -347       C  
ATOM   2865  OG1 THR A 425     -16.478 -33.980  33.360  1.00131.42           O  
ANISOU 2865  OG1 THR A 425    18334  17876  13722    180    854   -406       O  
ATOM   2866  CG2 THR A 425     -16.097 -33.106  31.184  1.00127.85           C  
ANISOU 2866  CG2 THR A 425    17629  17737  13211     90    817   -427       C  
ATOM   2867  N   LEU A 426     -13.229 -31.024  32.924  1.00122.28           N  
ANISOU 2867  N   LEU A 426    14634  20710  11116   2799   3078   -492       N  
ATOM   2868  CA  LEU A 426     -12.357 -29.949  32.411  1.00121.79           C  
ANISOU 2868  CA  LEU A 426    14722  20578  10975   2745   2851   -703       C  
ATOM   2869  C   LEU A 426     -10.894 -30.354  32.282  1.00123.70           C  
ANISOU 2869  C   LEU A 426    15047  20762  11188   2674   2826   -703       C  
ATOM   2870  O   LEU A 426     -10.313 -30.244  31.230  1.00118.67           O  
ANISOU 2870  O   LEU A 426    14483  19963  10642   2496   2728   -778       O  
ATOM   2871  CB  LEU A 426     -12.436 -28.730  33.311  1.00125.20           C  
ANISOU 2871  CB  LEU A 426    15186  21168  11214   2961   2740   -844       C  
ATOM   2872  CG  LEU A 426     -11.588 -27.488  33.003  1.00125.30           C  
ANISOU 2872  CG  LEU A 426    15316  21101  11189   2945   2506  -1066       C  
ATOM   2873  CD1 LEU A 426     -12.125 -26.812  31.761  1.00124.27           C  
ANISOU 2873  CD1 LEU A 426    15221  20787  11208   2779   2385  -1149       C  
ATOM   2874  CD2 LEU A 426     -11.630 -26.537  34.200  1.00127.92           C  
ANISOU 2874  CD2 LEU A 426    15635  21626  11340   3213   2419  -1210       C  
ATOM   2875  N   PHE A 427     -10.293 -30.797  33.377  1.00135.48           N  
ANISOU 2875  N   PHE A 427    16527  22407  12541   2835   2916   -618       N  
ATOM   2876  CA  PHE A 427      -8.868 -31.207  33.400  1.00139.92           C  
ANISOU 2876  CA  PHE A 427    17160  22935  13068   2795   2893   -624       C  
ATOM   2877  C   PHE A 427      -8.577 -32.397  32.482  1.00138.08           C  
ANISOU 2877  C   PHE A 427    16901  22529  13031   2575   2985   -509       C  
ATOM   2878  O   PHE A 427      -7.515 -32.408  31.803  1.00142.00           O  
ANISOU 2878  O   PHE A 427    17478  22907  13566   2439   2896   -589       O  
ATOM   2879  CB  PHE A 427      -8.368 -31.460  34.849  1.00144.04           C  
ANISOU 2879  CB  PHE A 427    17664  23690  13374   3058   2970   -555       C  
ATOM   2880  CG  PHE A 427      -7.968 -30.191  35.571  1.00149.00           C  
ANISOU 2880  CG  PHE A 427    18347  24454  13810   3257   2790   -780       C  
ATOM   2881  CD1 PHE A 427      -6.749 -29.560  35.263  1.00150.15           C  
ANISOU 2881  CD1 PHE A 427    18581  24498  13970   3197   2606   -977       C  
ATOM   2882  CD2 PHE A 427      -8.817 -29.591  36.514  1.00149.00           C  
ANISOU 2882  CD2 PHE A 427    18293  24670  13648   3505   2795   -815       C  
ATOM   2883  CE1 PHE A 427      -6.375 -28.379  35.898  1.00150.56           C  
ANISOU 2883  CE1 PHE A 427    18654  24640  13912   3377   2420  -1216       C  
ATOM   2884  CE2 PHE A 427      -8.445 -28.415  37.150  1.00149.73           C  
ANISOU 2884  CE2 PHE A 427    18417  24878  13594   3698   2603  -1066       C  
ATOM   2885  CZ  PHE A 427      -7.230 -27.806  36.839  1.00152.48           C  
ANISOU 2885  CZ  PHE A 427    18841  25100  13994   3630   2409  -1275       C  
ATOM   2886  N   SER A 428      -9.517 -33.357  32.419  1.00135.82           N  
ANISOU 2886  N   SER A 428    16489  22219  12895   2539   3153   -338       N  
ATOM   2887  CA  SER A 428      -9.329 -34.469  31.487  1.00135.17           C  
ANISOU 2887  CA  SER A 428    16356  21958  13042   2335   3215   -272       C  
ATOM   2888  C   SER A 428      -9.306 -33.993  30.030  1.00134.78           C  
ANISOU 2888  C   SER A 428    16371  21747  13090   2137   3054   -447       C  
ATOM   2889  O   SER A 428      -8.390 -34.344  29.269  1.00136.20           O  
ANISOU 2889  O   SER A 428    16603  21822  13323   2001   3004   -496       O  
ATOM   2890  CB  SER A 428     -10.412 -35.511  31.648  1.00136.83           C  
ANISOU 2890  CB  SER A 428    16387  22139  13461   2333   3409    -83       C  
ATOM   2891  OG  SER A 428     -10.135 -36.573  30.766  1.00139.34           O  
ANISOU 2891  OG  SER A 428    16642  22275  14024   2148   3442    -61       O  
ATOM   2892  N   ALA A 429     -10.309 -33.185  29.666  1.00138.48           N  
ANISOU 2892  N   ALA A 429    16834  22214  13568   2142   2977   -533       N  
ATOM   2893  CA  ALA A 429     -10.389 -32.558  28.338  1.00139.04           C  
ANISOU 2893  CA  ALA A 429    16971  22168  13687   2003   2820   -684       C  
ATOM   2894  C   ALA A 429      -9.149 -31.732  28.028  1.00140.98           C  
ANISOU 2894  C   ALA A 429    17368  22386  13812   1970   2684   -788       C  
ATOM   2895  O   ALA A 429      -8.524 -31.900  26.985  1.00142.09           O  
ANISOU 2895  O   ALA A 429    17557  22426  14003   1833   2630   -833       O  
ATOM   2896  CB  ALA A 429     -11.622 -31.662  28.224  1.00140.34           C  
ANISOU 2896  CB  ALA A 429    17115  22360  13846   2059   2751   -752       C  
ATOM   2897  N   ARG A 430      -8.817 -30.835  28.943  1.00145.29           N  
ANISOU 2897  N   ARG A 430    17969  23023  14211   2110   2629   -834       N  
ATOM   2898  CA  ARG A 430      -7.667 -29.944  28.808  1.00152.06           C  
ANISOU 2898  CA  ARG A 430    18938  23837  15002   2098   2497   -945       C  
ATOM   2899  C   ARG A 430      -6.348 -30.726  28.662  1.00149.98           C  
ANISOU 2899  C   ARG A 430    18704  23527  14754   2014   2537   -912       C  
ATOM   2900  O   ARG A 430      -5.485 -30.314  27.872  1.00142.68           O  
ANISOU 2900  O   ARG A 430    17851  22499  13860   1908   2453   -977       O  
ATOM   2901  CB  ARG A 430      -7.655 -28.926  29.967  1.00160.26           C  
ANISOU 2901  CB  ARG A 430    19988  24989  15912   2296   2422  -1035       C  
ATOM   2902  CG  ARG A 430      -6.649 -27.778  29.820  1.00164.55           C  
ANISOU 2902  CG  ARG A 430    20610  25450  16458   2291   2258  -1185       C  
ATOM   2903  CD  ARG A 430      -7.247 -26.667  28.983  1.00166.31           C  
ANISOU 2903  CD  ARG A 430    20864  25564  16762   2235   2140  -1254       C  
ATOM   2904  NE  ARG A 430      -8.094 -25.717  29.716  1.00170.24           N  
ANISOU 2904  NE  ARG A 430    21328  26141  17214   2399   2062  -1350       N  
ATOM   2905  CZ  ARG A 430      -7.663 -24.637  30.383  1.00174.59           C  
ANISOU 2905  CZ  ARG A 430    21880  26697  17757   2527   1927  -1508       C  
ATOM   2906  NH1 ARG A 430      -6.350 -24.360  30.519  1.00168.18           N  
ANISOU 2906  NH1 ARG A 430    21095  25815  16991   2517   1856  -1591       N  
ATOM   2907  NH2 ARG A 430      -8.573 -23.838  30.963  1.00178.47           N  
ANISOU 2907  NH2 ARG A 430    22328  27267  18214   2678   1855  -1603       N  
ATOM   2908  N   ARG A 431      -6.195 -31.846  29.386  1.00151.70           N  
ANISOU 2908  N   ARG A 431    18860  23816  14963   2066   2673   -797       N  
ATOM   2909  CA  ARG A 431      -4.996 -32.672  29.174  1.00151.42           C  
ANISOU 2909  CA  ARG A 431    18844  23725  14963   1979   2710   -767       C  
ATOM   2910  C   ARG A 431      -5.045 -33.519  27.890  1.00147.36           C  
ANISOU 2910  C   ARG A 431    18300  23083  14606   1787   2742   -744       C  
ATOM   2911  O   ARG A 431      -4.020 -33.686  27.243  1.00156.65           O  
ANISOU 2911  O   ARG A 431    19526  24186  15805   1681   2706   -788       O  
ATOM   2912  CB  ARG A 431      -4.685 -33.568  30.380  1.00153.35           C  
ANISOU 2912  CB  ARG A 431    19035  24084  15146   2115   2837   -643       C  
ATOM   2913  CG  ARG A 431      -3.228 -34.025  30.380  1.00153.75           C  
ANISOU 2913  CG  ARG A 431    19130  24097  15189   2071   2823   -662       C  
ATOM   2914  CD  ARG A 431      -2.922 -35.062  31.438  1.00157.77           C  
ANISOU 2914  CD  ARG A 431    19583  24710  15652   2201   2959   -511       C  
ATOM   2915  NE  ARG A 431      -1.589 -35.631  31.232  1.00157.53           N  
ANISOU 2915  NE  ARG A 431    19585  24614  15653   2127   2945   -533       N  
ATOM   2916  CZ  ARG A 431      -0.905 -36.359  32.113  1.00157.08           C  
ANISOU 2916  CZ  ARG A 431    19509  24639  15532   2247   3017   -440       C  
ATOM   2917  NH1 ARG A 431      -1.408 -36.624  33.326  1.00158.45           N  
ANISOU 2917  NH1 ARG A 431    19632  24988  15584   2470   3123   -295       N  
ATOM   2918  NH2 ARG A 431       0.302 -36.823  31.770  1.00150.18           N  
ANISOU 2918  NH2 ARG A 431    18665  23686  14710   2157   2988   -484       N  
ATOM   2919  N   GLN A 432      -6.193 -34.094  27.544  1.00143.96           N  
ANISOU 2919  N   GLN A 432    17773  22630  14292   1753   2808   -690       N  
ATOM   2920  CA  GLN A 432      -6.260 -34.914  26.321  1.00146.17           C  
ANISOU 2920  CA  GLN A 432    18005  22802  14731   1596   2813   -716       C  
ATOM   2921  C   GLN A 432      -5.903 -34.171  25.045  1.00146.18           C  
ANISOU 2921  C   GLN A 432    18100  22750  14692   1499   2680   -839       C  
ATOM   2922  O   GLN A 432      -5.280 -34.758  24.143  1.00146.04           O  
ANISOU 2922  O   GLN A 432    18082  22677  14728   1394   2670   -877       O  
ATOM   2923  CB  GLN A 432      -7.628 -35.510  26.124  1.00154.39           C  
ANISOU 2923  CB  GLN A 432    18905  23816  15938   1588   2875   -681       C  
ATOM   2924  CG  GLN A 432      -7.794 -36.886  26.742  1.00166.87           C  
ANISOU 2924  CG  GLN A 432    20339  25367  17696   1599   3040   -538       C  
ATOM   2925  CD  GLN A 432      -9.202 -37.139  27.276  1.00181.09           C  
ANISOU 2925  CD  GLN A 432    21993  27184  19629   1671   3146   -442       C  
ATOM   2926  OE1 GLN A 432     -10.100 -36.277  27.192  1.00188.68           O  
ANISOU 2926  OE1 GLN A 432    22966  28189  20533   1715   3084   -502       O  
ATOM   2927  NE2 GLN A 432      -9.407 -38.341  27.813  1.00185.81           N  
ANISOU 2927  NE2 GLN A 432    22437  27734  20427   1683   3313   -282       N  
ATOM   2928  N   LEU A 433      -6.312 -32.903  24.960  1.00141.32           N  
ANISOU 2928  N   LEU A 433    17554  22157  13985   1548   2585   -890       N  
ATOM   2929  CA  LEU A 433      -5.889 -32.019  23.868  1.00134.36           C  
ANISOU 2929  CA  LEU A 433    16767  21229  13052   1485   2474   -960       C  
ATOM   2930  C   LEU A 433      -4.410 -31.730  23.931  1.00126.02           C  
ANISOU 2930  C   LEU A 433    15791  20140  11949   1452   2456   -968       C  
ATOM   2931  O   LEU A 433      -3.741 -31.831  22.942  1.00133.59           O  
ANISOU 2931  O   LEU A 433    16785  21059  12914   1363   2440   -983       O  
ATOM   2932  CB  LEU A 433      -6.618 -30.685  23.937  1.00138.98           C  
ANISOU 2932  CB  LEU A 433    17397  21826  13582   1559   2383   -993       C  
ATOM   2933  CG  LEU A 433      -6.174 -29.605  22.939  1.00137.98           C  
ANISOU 2933  CG  LEU A 433    17366  21641  13420   1518   2283  -1020       C  
ATOM   2934  CD1 LEU A 433      -7.047 -29.650  21.704  1.00136.55           C  
ANISOU 2934  CD1 LEU A 433    17171  21467  13243   1490   2242  -1037       C  
ATOM   2935  CD2 LEU A 433      -6.243 -28.218  23.560  1.00143.39           C  
ANISOU 2935  CD2 LEU A 433    18095  22304  14082   1606   2200  -1048       C  
ATOM   2936  N   ALA A 434      -3.926 -31.358  25.103  1.00122.51           N  
ANISOU 2936  N   ALA A 434    15364  19726  11457   1541   2457   -968       N  
ATOM   2937  CA  ALA A 434      -2.509 -31.083  25.305  1.00125.79           C  
ANISOU 2937  CA  ALA A 434    15832  20103  11858   1524   2430  -1000       C  
ATOM   2938  C   ALA A 434      -1.621 -32.254  24.912  1.00128.85           C  
ANISOU 2938  C   ALA A 434    16202  20468  12287   1428   2502   -972       C  
ATOM   2939  O   ALA A 434      -0.624 -32.076  24.225  1.00139.11           O  
ANISOU 2939  O   ALA A 434    17544  21707  13605   1345   2479   -997       O  
ATOM   2940  CB  ALA A 434      -2.248 -30.722  26.740  1.00129.16           C  
ANISOU 2940  CB  ALA A 434    16251  20598  12223   1672   2411  -1033       C  
ATOM   2941  N   ASP A 435      -2.003 -33.456  25.314  1.00133.76           N  
ANISOU 2941  N   ASP A 435    16748  21127  12945   1440   2596   -912       N  
ATOM   2942  CA  ASP A 435      -1.297 -34.680  24.904  1.00142.38           C  
ANISOU 2942  CA  ASP A 435    17801  22183  14112   1350   2661   -892       C  
ATOM   2943  C   ASP A 435      -1.324 -34.961  23.402  1.00152.42           C  
ANISOU 2943  C   ASP A 435    19067  23408  15436   1227   2637   -942       C  
ATOM   2944  O   ASP A 435      -0.311 -35.420  22.858  1.00163.68           O  
ANISOU 2944  O   ASP A 435    20504  24805  16881   1152   2646   -969       O  
ATOM   2945  CB  ASP A 435      -1.887 -35.917  25.588  1.00144.49           C  
ANISOU 2945  CB  ASP A 435    17959  22473  14466   1391   2775   -798       C  
ATOM   2946  CG  ASP A 435      -1.571 -35.981  27.058  1.00148.59           C  
ANISOU 2946  CG  ASP A 435    18476  23072  14908   1533   2828   -722       C  
ATOM   2947  OD1 ASP A 435      -0.465 -35.579  27.457  1.00153.84           O  
ANISOU 2947  OD1 ASP A 435    19207  23754  15491   1568   2780   -770       O  
ATOM   2948  OD2 ASP A 435      -2.438 -36.414  27.830  1.00158.03           O  
ANISOU 2948  OD2 ASP A 435    19594  24323  16123   1628   2919   -614       O  
ATOM   2949  N   LEU A 436      -2.474 -34.735  22.760  1.00157.65           N  
ANISOU 2949  N   LEU A 436    19705  24081  16113   1227   2604   -963       N  
ATOM   2950  CA  LEU A 436      -2.598 -34.921  21.314  1.00155.95           C  
ANISOU 2950  CA  LEU A 436    19483  23863  15909   1156   2562  -1030       C  
ATOM   2951  C   LEU A 436      -1.756 -33.881  20.631  1.00151.35           C  
ANISOU 2951  C   LEU A 436    19009  23278  15218   1133   2509  -1034       C  
ATOM   2952  O   LEU A 436      -1.054 -34.179  19.667  1.00157.92           O  
ANISOU 2952  O   LEU A 436    19852  24120  16030   1076   2511  -1062       O  
ATOM   2953  CB  LEU A 436      -4.052 -34.818  20.830  1.00157.96           C  
ANISOU 2953  CB  LEU A 436    19682  24140  16195   1189   2520  -1067       C  
ATOM   2954  CG  LEU A 436      -4.890 -36.060  20.944  1.00162.32           C  
ANISOU 2954  CG  LEU A 436    20080  24667  16924   1181   2569  -1091       C  
ATOM   2955  CD1 LEU A 436      -6.244 -35.868  20.265  1.00165.55           C  
ANISOU 2955  CD1 LEU A 436    20429  25096  17376   1212   2502  -1167       C  
ATOM   2956  CD2 LEU A 436      -4.168 -37.269  20.377  1.00160.89           C  
ANISOU 2956  CD2 LEU A 436    19829  24452  16848   1108   2595  -1149       C  
ATOM   2957  N   GLU A 437      -1.811 -32.670  21.149  1.00148.90           N  
ANISOU 2957  N   GLU A 437    18764  22951  14858   1185   2468  -1003       N  
ATOM   2958  CA  GLU A 437      -1.059 -31.561  20.602  1.00153.98           C  
ANISOU 2958  CA  GLU A 437    19489  23556  15459   1168   2428   -981       C  
ATOM   2959  C   GLU A 437       0.429 -31.885  20.599  1.00160.23           C  
ANISOU 2959  C   GLU A 437    20292  24311  16275   1105   2470   -980       C  
ATOM   2960  O   GLU A 437       1.113 -31.789  19.576  1.00170.06           O  
ANISOU 2960  O   GLU A 437    21562  25554  17499   1051   2487   -960       O  
ATOM   2961  CB  GLU A 437      -1.330 -30.287  21.414  1.00156.97           C  
ANISOU 2961  CB  GLU A 437    19902  23894  15844   1242   2368   -973       C  
ATOM   2962  CG  GLU A 437      -0.696 -29.030  20.839  1.00163.21           C  
ANISOU 2962  CG  GLU A 437    20749  24604  16658   1226   2327   -935       C  
ATOM   2963  CD  GLU A 437      -1.262 -28.619  19.509  1.00168.76           C  
ANISOU 2963  CD  GLU A 437    21482  25331  17306   1221   2312   -873       C  
ATOM   2964  OE1 GLU A 437      -2.313 -29.143  19.092  1.00168.22           O  
ANISOU 2964  OE1 GLU A 437    21392  25344  17180   1245   2300   -898       O  
ATOM   2965  OE2 GLU A 437      -0.697 -27.680  18.911  1.00171.77           O  
ANISOU 2965  OE2 GLU A 437    21901  25646  17718   1209   2308   -796       O  
ATOM   2966  N   ASP A 438       0.906 -32.380  21.730  1.00164.84           N  
ANISOU 2966  N   ASP A 438    20850  24885  16896   1125   2497   -999       N  
ATOM   2967  CA  ASP A 438       2.289 -32.789  21.890  1.00162.32           C  
ANISOU 2967  CA  ASP A 438    20530  24532  16612   1077   2530  -1016       C  
ATOM   2968  C   ASP A 438       2.727 -33.891  20.908  1.00155.27           C  
ANISOU 2968  C   ASP A 438    19605  23662  15727    992   2583  -1028       C  
ATOM   2969  O   ASP A 438       3.831 -33.855  20.364  1.00148.53           O  
ANISOU 2969  O   ASP A 438    18767  22784  14882    934   2603  -1033       O  
ATOM   2970  CB  ASP A 438       2.475 -33.274  23.336  1.00164.98           C  
ANISOU 2970  CB  ASP A 438    20836  24888  16959   1153   2545  -1030       C  
ATOM   2971  CG  ASP A 438       3.699 -32.698  23.979  1.00167.63           C  
ANISOU 2971  CG  ASP A 438    21192  25178  17322   1178   2507  -1080       C  
ATOM   2972  OD1 ASP A 438       4.634 -32.331  23.238  1.00174.79           O  
ANISOU 2972  OD1 ASP A 438    22115  26016  18278   1097   2504  -1092       O  
ATOM   2973  OD2 ASP A 438       3.704 -32.552  25.226  1.00169.95           O  
ANISOU 2973  OD2 ASP A 438    21474  25510  17588   1295   2478  -1113       O  
ATOM   2974  N   ASN A 439       1.865 -34.890  20.722  1.00155.80           N  
ANISOU 2974  N   ASN A 439    19610  23770  15816    992   2603  -1045       N  
ATOM   2975  CA  ASN A 439       2.150 -36.011  19.816  1.00160.32           C  
ANISOU 2975  CA  ASN A 439    20125  24364  16423    930   2631  -1099       C  
ATOM   2976  C   ASN A 439       2.154 -35.532  18.383  1.00167.18           C  
ANISOU 2976  C   ASN A 439    21028  25291  17202    916   2602  -1119       C  
ATOM   2977  O   ASN A 439       3.019 -35.933  17.580  1.00175.68           O  
ANISOU 2977  O   ASN A 439    22096  26399  18254    875   2626  -1153       O  
ATOM   2978  CB  ASN A 439       1.094 -37.128  19.948  1.00164.48           C  
ANISOU 2978  CB  ASN A 439    20543  24894  17055    943   2646  -1130       C  
ATOM   2979  CG  ASN A 439       1.248 -37.954  21.211  1.00166.15           C  
ANISOU 2979  CG  ASN A 439    20696  25060  17371    962   2712  -1076       C  
ATOM   2980  OD1 ASN A 439       2.367 -38.189  21.660  1.00176.94           O  
ANISOU 2980  OD1 ASN A 439    22084  26406  18739    947   2739  -1062       O  
ATOM   2981  ND2 ASN A 439       0.130 -38.380  21.802  1.00161.72           N  
ANISOU 2981  ND2 ASN A 439    20056  24489  16901   1008   2744  -1031       N  
ATOM   2982  N   TRP A 440       1.183 -34.683  18.052  1.00173.00           N  
ANISOU 2982  N   TRP A 440    21798  26057  17875    966   2555  -1093       N  
ATOM   2983  CA  TRP A 440       1.099 -34.093  16.716  1.00177.83           C  
ANISOU 2983  CA  TRP A 440    22451  26745  18370    989   2530  -1079       C  
ATOM   2984  C   TRP A 440       2.319 -33.219  16.437  1.00171.28           C  
ANISOU 2984  C   TRP A 440    21690  25884  17504    962   2573   -986       C  
ATOM   2985  O   TRP A 440       2.880 -33.275  15.360  1.00174.63           O  
ANISOU 2985  O   TRP A 440    22121  26382  17847    961   2605   -968       O  
ATOM   2986  CB  TRP A 440      -0.174 -33.273  16.630  1.00187.31           C  
ANISOU 2986  CB  TRP A 440    23676  27965  19528   1059   2469  -1054       C  
ATOM   2987  CG  TRP A 440      -0.410 -32.442  15.430  1.00199.99           C  
ANISOU 2987  CG  TRP A 440    25335  29649  21001   1117   2440  -1002       C  
ATOM   2988  CD1 TRP A 440      -0.032 -31.140  15.275  1.00205.19           C  
ANISOU 2988  CD1 TRP A 440    26071  30264  21625   1134   2451   -869       C  
ATOM   2989  CD2 TRP A 440      -1.172 -32.779  14.268  1.00210.74           C  
ANISOU 2989  CD2 TRP A 440    26667  31144  22258   1190   2388  -1074       C  
ATOM   2990  NE1 TRP A 440      -0.468 -30.653  14.071  1.00212.18           N  
ANISOU 2990  NE1 TRP A 440    26988  31254  22375   1214   2430   -815       N  
ATOM   2991  CE2 TRP A 440      -1.177 -31.632  13.431  1.00216.60           C  
ANISOU 2991  CE2 TRP A 440    27488  31942  22866   1261   2382   -951       C  
ATOM   2992  CE3 TRP A 440      -1.847 -33.929  13.844  1.00213.97           C  
ANISOU 2992  CE3 TRP A 440    26975  31628  22693   1216   2338  -1238       C  
ATOM   2993  CZ2 TRP A 440      -1.804 -31.609  12.177  1.00221.41           C  
ANISOU 2993  CZ2 TRP A 440    28096  32715  23313   1376   2330   -982       C  
ATOM   2994  CZ3 TRP A 440      -2.490 -33.900  12.594  1.00221.38           C  
ANISOU 2994  CZ3 TRP A 440    27899  32720  23495   1326   2265  -1311       C  
ATOM   2995  CH2 TRP A 440      -2.451 -32.747  11.776  1.00224.34           C  
ANISOU 2995  CH2 TRP A 440    28371  33182  23684   1414   2262  -1179       C  
ATOM   2996  N   GLU A 441       2.774 -32.475  17.434  1.00164.25           N  
ANISOU 2996  N   GLU A 441    20830  24886  16690    948   2575   -937       N  
ATOM   2997  CA  GLU A 441       3.991 -31.684  17.308  1.00166.09           C  
ANISOU 2997  CA  GLU A 441    21093  25047  16966    912   2615   -864       C  
ATOM   2998  C   GLU A 441       5.247 -32.552  17.228  1.00163.16           C  
ANISOU 2998  C   GLU A 441    20686  24676  16628    846   2675   -906       C  
ATOM   2999  O   GLU A 441       6.174 -32.198  16.490  1.00173.29           O  
ANISOU 2999  O   GLU A 441    21975  25956  17910    816   2734   -842       O  
ATOM   3000  CB  GLU A 441       4.112 -30.642  18.431  1.00168.48           C  
ANISOU 3000  CB  GLU A 441    21411  25224  17379    932   2571   -851       C  
ATOM   3001  CG  GLU A 441       4.921 -29.408  18.044  1.00173.47           C  
ANISOU 3001  CG  GLU A 441    22055  25750  18104    913   2592   -754       C  
ATOM   3002  CD  GLU A 441       4.535 -28.790  16.677  1.00181.60           C  
ANISOU 3002  CD  GLU A 441    23117  26830  19049    938   2629   -614       C  
ATOM   3003  OE1 GLU A 441       3.328 -28.552  16.402  1.00184.77           O  
ANISOU 3003  OE1 GLU A 441    23548  27294  19362   1002   2579   -599       O  
ATOM   3004  OE2 GLU A 441       5.441 -28.575  15.835  1.00190.67           O  
ANISOU 3004  OE2 GLU A 441    24259  27975  20210    908   2716   -511       O  
ATOM   3005  N   THR A 442       5.267 -33.676  17.957  1.00161.73           N  
ANISOU 3005  N   THR A 442    20461  24499  16486    831   2671   -997       N  
ATOM   3006  CA  THR A 442       6.342 -34.686  17.803  1.00164.13           C  
ANISOU 3006  CA  THR A 442    20723  24814  16824    775   2719  -1052       C  
ATOM   3007  C   THR A 442       6.409 -35.267  16.391  1.00166.58           C  
ANISOU 3007  C   THR A 442    21009  25240  17044    767   2749  -1080       C  
ATOM   3008  O   THR A 442       7.521 -35.447  15.866  1.00174.65           O  
ANISOU 3008  O   THR A 442    22017  26279  18062    728   2804  -1081       O  
ATOM   3009  CB  THR A 442       6.202 -35.846  18.819  1.00170.41           C  
ANISOU 3009  CB  THR A 442    21465  25589  17692    777   2713  -1120       C  
ATOM   3010  OG1 THR A 442       6.429 -35.344  20.132  1.00178.10           O  
ANISOU 3010  OG1 THR A 442    22459  26494  18714    814   2691  -1103       O  
ATOM   3011  CG2 THR A 442       7.209 -36.978  18.568  1.00167.28           C  
ANISOU 3011  CG2 THR A 442    21014  25198  17343    723   2753  -1185       C  
ATOM   3012  N   LEU A 443       5.240 -35.569  15.794  1.00167.71           N  
ANISOU 3012  N   LEU A 443    21134  25470  17116    817   2706  -1121       N  
ATOM   3013  CA  LEU A 443       5.196 -36.071  14.389  1.00169.13           C  
ANISOU 3013  CA  LEU A 443    21282  25798  17180    853   2708  -1184       C  
ATOM   3014  C   LEU A 443       5.779 -35.083  13.371  1.00169.33           C  
ANISOU 3014  C   LEU A 443    21365  25901  17071    887   2764  -1061       C  
ATOM   3015  O   LEU A 443       6.580 -35.464  12.513  1.00159.39           O  
ANISOU 3015  O   LEU A 443    20081  24741  15736    895   2817  -1079       O  
ATOM   3016  CB  LEU A 443       3.764 -36.440  13.966  1.00170.49           C  
ANISOU 3016  CB  LEU A 443    21412  26047  17317    924   2628  -1274       C  
ATOM   3017  CG  LEU A 443       3.204 -37.746  14.563  1.00173.04           C  
ANISOU 3017  CG  LEU A 443    21626  26314  17805    899   2592  -1408       C  
ATOM   3018  CD1 LEU A 443       1.682 -37.768  14.675  1.00172.65           C  
ANISOU 3018  CD1 LEU A 443    21533  26265  17799    951   2523  -1453       C  
ATOM   3019  CD2 LEU A 443       3.687 -38.943  13.756  1.00177.13           C  
ANISOU 3019  CD2 LEU A 443    22048  26906  18346    898   2581  -1565       C  
ATOM   3020  N   ASN A 444       5.370 -33.816  13.484  1.00170.39           N  
ANISOU 3020  N   ASN A 444    21566  25987  17187    916   2761   -925       N  
ATOM   3021  CA  ASN A 444       5.813 -32.761  12.550  1.00168.26           C  
ANISOU 3021  CA  ASN A 444    21341  25766  16822    959   2832   -755       C  
ATOM   3022  C   ASN A 444       7.273 -32.413  12.698  1.00168.51           C  
ANISOU 3022  C   ASN A 444    21363  25704  16959    885   2933   -666       C  
ATOM   3023  O   ASN A 444       7.921 -32.117  11.709  1.00175.20           O  
ANISOU 3023  O   ASN A 444    22208  26637  17722    916   3028   -552       O  
ATOM   3024  CB  ASN A 444       5.030 -31.461  12.720  1.00164.82           C  
ANISOU 3024  CB  ASN A 444    20963  25260  16398   1004   2801   -625       C  
ATOM   3025  CG  ASN A 444       3.612 -31.550  12.200  1.00167.56           C  
ANISOU 3025  CG  ASN A 444    21322  25731  16608   1105   2715   -676       C  
ATOM   3026  OD1 ASN A 444       3.187 -32.571  11.611  1.00168.37           O  
ANISOU 3026  OD1 ASN A 444    21380  25980  16610   1153   2673   -820       O  
ATOM   3027  ND2 ASN A 444       2.843 -30.496  12.465  1.00167.53           N  
ANISOU 3027  ND2 ASN A 444    21364  25659  16630   1143   2673   -584       N  
ATOM   3028  N   ASP A 445       7.780 -32.426  13.929  1.00171.51           N  
ANISOU 3028  N   ASP A 445    21727  25917  17520    803   2914   -715       N  
ATOM   3029  CA  ASP A 445       9.204 -32.174  14.188  1.00172.47           C  
ANISOU 3029  CA  ASP A 445    21817  25930  17781    730   2989   -673       C  
ATOM   3030  C   ASP A 445      10.081 -33.281  13.638  1.00169.13           C  
ANISOU 3030  C   ASP A 445    21346  25608  17307    702   3048   -752       C  
ATOM   3031  O   ASP A 445      11.129 -33.015  13.065  1.00168.87           O  
ANISOU 3031  O   ASP A 445    21285  25579  17297    680   3150   -667       O  
ATOM   3032  CB  ASP A 445       9.481 -31.994  15.692  1.00177.62           C  
ANISOU 3032  CB  ASP A 445    22458  26409  18620    684   2925   -751       C  
ATOM   3033  CG  ASP A 445       8.988 -30.649  16.228  1.00183.59           C  
ANISOU 3033  CG  ASP A 445    23239  27038  19478    713   2875   -677       C  
ATOM   3034  OD1 ASP A 445       9.036 -29.654  15.473  1.00188.42           O  
ANISOU 3034  OD1 ASP A 445    23858  27620  20111    728   2930   -522       O  
ATOM   3035  OD2 ASP A 445       8.557 -30.592  17.407  1.00186.25           O  
ANISOU 3035  OD2 ASP A 445    23579  27309  19876    733   2785   -769       O  
ATOM   3036  N   ASN A 446       9.656 -34.524  13.822  1.00168.49           N  
ANISOU 3036  N   ASN A 446    21240  25597  17181    705   2987   -913       N  
ATOM   3037  CA  ASN A 446      10.394 -35.658  13.273  1.00172.05           C  
ANISOU 3037  CA  ASN A 446    21631  26143  17594    688   3023  -1018       C  
ATOM   3038  C   ASN A 446      10.280 -35.805  11.765  1.00176.77           C  
ANISOU 3038  C   ASN A 446    22218  26955  17989    775   3066  -1003       C  
ATOM   3039  O   ASN A 446      11.172 -36.405  11.144  1.00194.85           O  
ANISOU 3039  O   ASN A 446    24459  29338  20238    774   3126  -1053       O  
ATOM   3040  CB  ASN A 446       9.954 -36.951  13.932  1.00167.30           C  
ANISOU 3040  CB  ASN A 446    20984  25524  17057    671   2944  -1188       C  
ATOM   3041  CG  ASN A 446      10.498 -37.089  15.323  1.00168.71           C  
ANISOU 3041  CG  ASN A 446    21157  25542  17403    609   2928  -1208       C  
ATOM   3042  OD1 ASN A 446      11.714 -37.001  15.536  1.00166.23           O  
ANISOU 3042  OD1 ASN A 446    20825  25167  17165    560   2975  -1201       O  
ATOM   3043  ND2 ASN A 446       9.614 -37.306  16.283  1.00176.88           N  
ANISOU 3043  ND2 ASN A 446    22197  26518  18489    627   2865  -1232       N  
ATOM   3044  N   LEU A 447       9.197 -35.301  11.171  1.00173.28           N  
ANISOU 3044  N   LEU A 447    21816  26611  17408    868   3031   -950       N  
ATOM   3045  CA  LEU A 447       9.132 -35.237   9.701  1.00178.46           C  
ANISOU 3045  CA  LEU A 447    22470  27505  17831    993   3077   -908       C  
ATOM   3046  C   LEU A 447      10.196 -34.300   9.117  1.00179.41           C  
ANISOU 3046  C   LEU A 447    22605  27641  17920   1001   3235   -679       C  
ATOM   3047  O   LEU A 447      10.863 -34.656   8.137  1.00174.21           O  
ANISOU 3047  O   LEU A 447    21909  27164  17119   1067   3319   -672       O  
ATOM   3048  CB  LEU A 447       7.730 -34.876   9.201  1.00182.15           C  
ANISOU 3048  CB  LEU A 447    22975  28083  18150   1113   2994   -903       C  
ATOM   3049  CG  LEU A 447       6.759 -36.067   9.119  1.00189.30           C  
ANISOU 3049  CG  LEU A 447    23816  29072  19036   1159   2856  -1162       C  
ATOM   3050  CD1 LEU A 447       5.319 -35.624   8.909  1.00190.59           C  
ANISOU 3050  CD1 LEU A 447    24009  29289  19117   1256   2760  -1168       C  
ATOM   3051  CD2 LEU A 447       7.156 -37.041   8.002  1.00193.80           C  
ANISOU 3051  CD2 LEU A 447    24307  29869  19456   1256   2851  -1326       C  
ATOM   3052  N   LYS A 448      10.412 -33.154   9.769  1.00185.13           N  
ANISOU 3052  N   LYS A 448    23365  28167  18809    934   3279   -505       N  
ATOM   3053  CA  LYS A 448      11.486 -32.222   9.385  1.00191.66           C  
ANISOU 3053  CA  LYS A 448    24174  28937  19711    915   3439   -275       C  
ATOM   3054  C   LYS A 448      12.866 -32.894   9.442  1.00199.29           C  
ANISOU 3054  C   LYS A 448    25066  29885  20768    836   3519   -344       C  
ATOM   3055  O   LYS A 448      13.670 -32.742   8.536  1.00222.60           O  
ANISOU 3055  O   LYS A 448    27979  32948  23647    879   3665   -213       O  
ATOM   3056  CB  LYS A 448      11.503 -30.961  10.271  1.00189.76           C  
ANISOU 3056  CB  LYS A 448    23949  28429  19722    843   3438   -138       C  
ATOM   3057  CG  LYS A 448      10.267 -30.086  10.144  1.00192.16           C  
ANISOU 3057  CG  LYS A 448    24318  28733  19961    923   3380    -30       C  
ATOM   3058  CD  LYS A 448      10.250 -28.915  11.135  1.00196.66           C  
ANISOU 3058  CD  LYS A 448    24886  29026  20810    855   3347     48       C  
ATOM   3059  CE  LYS A 448       8.837 -28.280  11.345  1.00208.33           C  
ANISOU 3059  CE  LYS A 448    26428  30487  22239    923   3237     67       C  
ATOM   3060  NZ  LYS A 448       8.067 -27.703  10.179  1.00216.34           N  
ANISOU 3060  NZ  LYS A 448    27490  31656  23052   1060   3278    256       N  
ATOM   3061  N   VAL A 449      13.109 -33.672  10.491  1.00193.84           N  
ANISOU 3061  N   VAL A 449    24353  29071  20225    737   3428   -544       N  
ATOM   3062  CA  VAL A 449      14.366 -34.426  10.666  1.00184.18           C  
ANISOU 3062  CA  VAL A 449    23058  27821  19100    663   3476   -645       C  
ATOM   3063  C   VAL A 449      14.614 -35.406   9.518  1.00186.57           C  
ANISOU 3063  C   VAL A 449    23319  28380  19188    742   3520   -731       C  
ATOM   3064  O   VAL A 449      15.738 -35.462   8.984  1.00180.33           O  
ANISOU 3064  O   VAL A 449    22470  27643  18402    735   3646   -677       O  
ATOM   3065  CB  VAL A 449      14.361 -35.202  11.994  1.00172.04           C  
ANISOU 3065  CB  VAL A 449    21511  26137  17717    579   3352   -844       C  
ATOM   3066  CG1 VAL A 449      15.575 -36.130  12.091  1.00169.31           C  
ANISOU 3066  CG1 VAL A 449    21092  25787  17450    521   3386   -967       C  
ATOM   3067  CG2 VAL A 449      14.345 -34.225  13.149  1.00166.00           C  
ANISOU 3067  CG2 VAL A 449    20770  25145  17157    526   3309   -787       C  
ATOM   3068  N   ILE A 450      13.556 -36.137   9.139  1.00191.23           N  
ANISOU 3068  N   ILE A 450    23924  29125  19606    829   3413   -875       N  
ATOM   3069  CA  ILE A 450      13.633 -37.121   8.063  1.00207.90           C  
ANISOU 3069  CA  ILE A 450    25981  31493  21518    933   3412  -1018       C  
ATOM   3070  C   ILE A 450      13.850 -36.411   6.747  1.00218.77           C  
ANISOU 3070  C   ILE A 450    27367  33097  22659   1073   3550   -823       C  
ATOM   3071  O   ILE A 450      14.650 -36.870   5.942  1.00232.87           O  
ANISOU 3071  O   ILE A 450    29092  35062  24325   1136   3636   -852       O  
ATOM   3072  CB  ILE A 450      12.380 -38.020   7.943  1.00215.44           C  
ANISOU 3072  CB  ILE A 450    26922  32546  22390   1007   3247  -1243       C  
ATOM   3073  CG1 ILE A 450      12.206 -38.853   9.210  1.00218.41           C  
ANISOU 3073  CG1 ILE A 450    27268  32709  23008    883   3140  -1406       C  
ATOM   3074  CG2 ILE A 450      12.525 -38.996   6.772  1.00217.40           C  
ANISOU 3074  CG2 ILE A 450    27089  33068  22446   1139   3228  -1430       C  
ATOM   3075  CD1 ILE A 450      10.776 -39.246   9.477  1.00214.62           C  
ANISOU 3075  CD1 ILE A 450    26785  32216  22545    919   3002  -1525       C  
ATOM   3076  N   GLU A 451      13.137 -35.300   6.538  1.00217.44           N  
ANISOU 3076  N   GLU A 451    27268  32927  22419   1135   3575   -615       N  
ATOM   3077  CA  GLU A 451      13.361 -34.471   5.331  1.00216.01           C  
ANISOU 3077  CA  GLU A 451    27099  32949  22026   1283   3735   -355       C  
ATOM   3078  C   GLU A 451      14.853 -34.095   5.138  1.00216.15           C  
ANISOU 3078  C   GLU A 451    27054  32917  22152   1224   3942   -169       C  
ATOM   3079  O   GLU A 451      15.426 -34.292   4.070  1.00224.74           O  
ANISOU 3079  O   GLU A 451    28097  34257  23034   1350   4070   -102       O  
ATOM   3080  CB  GLU A 451      12.510 -33.210   5.447  1.00214.26           C  
ANISOU 3080  CB  GLU A 451    26957  32632  21820   1314   3736   -127       C  
ATOM   3081  CG  GLU A 451      11.906 -32.671   4.166  1.00217.65           C  
ANISOU 3081  CG  GLU A 451    27423  33344  21930   1540   3796     51       C  
ATOM   3082  CD  GLU A 451      10.815 -31.631   4.446  1.00218.03           C  
ANISOU 3082  CD  GLU A 451    27551  33276  22015   1563   3735    199       C  
ATOM   3083  OE1 GLU A 451       9.954 -31.852   5.345  1.00223.40           O  
ANISOU 3083  OE1 GLU A 451    28261  33805  22816   1480   3563     16       O  
ATOM   3084  OE2 GLU A 451      10.819 -30.580   3.772  1.00218.42           O  
ANISOU 3084  OE2 GLU A 451    27625  33383  21980   1671   3869    514       O  
ATOM   3085  N   LYS A 452      15.476 -33.627   6.217  1.00211.90           N  
ANISOU 3085  N   LYS A 452    26500  32062  21947   1043   3963   -117       N  
ATOM   3086  CA  LYS A 452      16.869 -33.162   6.238  1.00212.28           C  
ANISOU 3086  CA  LYS A 452    26470  31988  22197    959   4143     45       C  
ATOM   3087  C   LYS A 452      17.931 -34.269   6.342  1.00222.67           C  
ANISOU 3087  C   LYS A 452    27705  33338  23561    895   4153   -161       C  
ATOM   3088  O   LYS A 452      19.106 -34.040   6.027  1.00234.05           O  
ANISOU 3088  O   LYS A 452    29062  34764  25099    866   4324    -35       O  
ATOM   3089  CB  LYS A 452      17.057 -32.243   7.440  1.00204.29           C  
ANISOU 3089  CB  LYS A 452    25455  30611  21554    804   4116    118       C  
ATOM   3090  CG  LYS A 452      16.203 -30.986   7.404  1.00199.06           C  
ANISOU 3090  CG  LYS A 452    24849  29859  20922    849   4123    344       C  
ATOM   3091  CD  LYS A 452      16.302 -30.212   8.703  1.00192.34           C  
ANISOU 3091  CD  LYS A 452    23982  28654  20441    710   4046    330       C  
ATOM   3092  CE  LYS A 452      17.703 -29.671   8.924  1.00192.29           C  
ANISOU 3092  CE  LYS A 452    23855  28439  20768    607   4185    438       C  
ATOM   3093  NZ  LYS A 452      17.711 -28.636   9.988  1.00189.19           N  
ANISOU 3093  NZ  LYS A 452    23428  27711  20744    517   4113    454       N  
ATOM   3094  N   ALA A 453      17.529 -35.445   6.824  1.00228.92           N  
ANISOU 3094  N   ALA A 453    28506  34151  24320    868   3976   -468       N  
ATOM   3095  CA  ALA A 453      18.437 -36.592   7.037  1.00234.37           C  
ANISOU 3095  CA  ALA A 453    29119  34848  25081    805   3954   -692       C  
ATOM   3096  C   ALA A 453      19.431 -36.922   5.917  1.00235.49           C  
ANISOU 3096  C   ALA A 453    29176  35223  25073    890   4115   -656       C  
ATOM   3097  O   ALA A 453      19.038 -37.201   4.758  1.00229.18           O  
ANISOU 3097  O   ALA A 453    28376  34739  23961   1069   4143   -662       O  
ATOM   3098  CB  ALA A 453      17.635 -37.848   7.337  1.00237.93           C  
ANISOU 3098  CB  ALA A 453    29580  35353  25468    821   3757   -993       C  
ATOM   3099  N   ASP A 454      20.711 -36.941   6.316  1.00232.79           N  
ANISOU 3099  N   ASP A 454    28757  34736  24958    775   4206   -647       N  
ATOM   3100  CA  ASP A 454      21.811 -37.474   5.510  1.00233.60           C  
ANISOU 3100  CA  ASP A 454    28758  35020  24978    825   4342   -673       C  
ATOM   3101  C   ASP A 454      21.817 -39.008   5.365  1.00230.88           C  
ANISOU 3101  C   ASP A 454    28372  34828  24521    864   4205  -1018       C  
ATOM   3102  O   ASP A 454      22.164 -39.525   4.298  1.00240.46           O  
ANISOU 3102  O   ASP A 454    29523  36330  25507   1000   4278  -1074       O  
ATOM   3103  CB  ASP A 454      23.146 -37.106   6.178  1.00231.66           C  
ANISOU 3103  CB  ASP A 454    28427  34521  25071    668   4444   -608       C  
ATOM   3104  CG  ASP A 454      24.310 -37.087   5.211  1.00242.68           C  
ANISOU 3104  CG  ASP A 454    29709  36085  26412    726   4670   -486       C  
ATOM   3105  OD1 ASP A 454      24.151 -36.806   4.009  1.00249.80           O  
ANISOU 3105  OD1 ASP A 454    30606  37270  27036    892   4818   -306       O  
ATOM   3106  OD2 ASP A 454      25.428 -37.341   5.659  1.00244.22           O  
ANISOU 3106  OD2 ASP A 454    29812  36137  26841    616   4708   -564       O  
ATOM   3107  N   ASN A 455      21.381 -39.709   6.418  1.00215.86           N  
ANISOU 3107  N   ASN A 455    26496  32740  22778    763   4010  -1239       N  
ATOM   3108  CA  ASN A 455      21.600 -41.156   6.575  1.00209.39           C  
ANISOU 3108  CA  ASN A 455    25611  31955  21990    753   3884  -1554       C  
ATOM   3109  C   ASN A 455      20.493 -41.868   7.382  1.00203.30           C  
ANISOU 3109  C   ASN A 455    24881  31064  21297    720   3671  -1742       C  
ATOM   3110  O   ASN A 455      19.609 -41.243   7.992  1.00206.17           O  
ANISOU 3110  O   ASN A 455    25332  31299  21705    688   3615  -1640       O  
ATOM   3111  CB  ASN A 455      23.009 -41.480   7.105  1.00209.22           C  
ANISOU 3111  CB  ASN A 455    25508  31787  22199    635   3940  -1611       C  
ATOM   3112  CG  ASN A 455      24.058 -41.635   5.975  1.00213.64           C  
ANISOU 3112  CG  ASN A 455    25966  32581  22624    719   4109  -1590       C  
ATOM   3113  OD1 ASN A 455      24.872 -40.734   5.684  1.00213.24           O  
ANISOU 3113  OD1 ASN A 455    25882  32517  22621    702   4303  -1357       O  
ATOM   3114  ND2 ASN A 455      24.039 -42.796   5.342  1.00203.95           N  
ANISOU 3114  ND2 ASN A 455    24673  31563  21251    818   4036  -1839       N  
ATOM   3115  N   ALA A 456      20.555 -43.194   7.347  1.00201.63           N  
ANISOU 3115  N   ALA A 456    24593  30897  21120    735   3561  -2013       N  
ATOM   3116  CA  ALA A 456      19.495 -44.090   7.814  1.00202.83           C  
ANISOU 3116  CA  ALA A 456    24737  30979  21348    737   3377  -2207       C  
ATOM   3117  C   ALA A 456      19.280 -44.107   9.306  1.00211.31           C  
ANISOU 3117  C   ALA A 456    25857  31753  22675    603   3304  -2173       C  
ATOM   3118  O   ALA A 456      18.156 -44.301   9.762  1.00213.75           O  
ANISOU 3118  O   ALA A 456    26196  31990  23027    607   3198  -2205       O  
ATOM   3119  CB  ALA A 456      19.810 -45.499   7.381  1.00201.58           C  
ANISOU 3119  CB  ALA A 456    24451  30915  21223    785   3294  -2500       C  
ATOM   3120  N   ALA A 457      20.364 -43.946  10.057  1.00222.32           N  
ANISOU 3120  N   ALA A 457    27247  32988  24234    501   3357  -2119       N  
ATOM   3121  CA  ALA A 457      20.304 -43.918  11.510  1.00228.18           C  
ANISOU 3121  CA  ALA A 457    28031  33479  25186    407   3290  -2087       C  
ATOM   3122  C   ALA A 457      19.456 -42.759  11.993  1.00225.01           C  
ANISOU 3122  C   ALA A 457    27735  33002  24754    402   3290  -1904       C  
ATOM   3123  O   ALA A 457      18.712 -42.923  12.933  1.00227.21           O  
ANISOU 3123  O   ALA A 457    28052  33159  25118    385   3201  -1909       O  
ATOM   3124  CB  ALA A 457      21.695 -43.815  12.103  1.00233.06           C  
ANISOU 3124  CB  ALA A 457    28615  33972  25963    329   3343  -2078       C  
ATOM   3125  N   GLN A 458      19.583 -41.605  11.338  1.00215.38           N  
ANISOU 3125  N   GLN A 458    26553  31857  23422    425   3399  -1734       N  
ATOM   3126  CA  GLN A 458      18.732 -40.440  11.599  1.00202.36           C  
ANISOU 3126  CA  GLN A 458    24995  30151  21738    434   3400  -1561       C  
ATOM   3127  C   GLN A 458      17.289 -40.746  11.294  1.00200.42           C  
ANISOU 3127  C   GLN A 458    24786  30005  21359    510   3309  -1608       C  
ATOM   3128  O   GLN A 458      16.424 -40.408  12.070  1.00192.98           O  
ANISOU 3128  O   GLN A 458    23902  28954  20466    497   3240  -1565       O  
ATOM   3129  CB  GLN A 458      19.137 -39.257  10.733  1.00203.90           C  
ANISOU 3129  CB  GLN A 458    25200  30423  21848    463   3549  -1355       C  
ATOM   3130  CG  GLN A 458      20.533 -38.745  11.024  1.00208.03           C  
ANISOU 3130  CG  GLN A 458    25666  30815  22558    382   3653  -1283       C  
ATOM   3131  CD  GLN A 458      21.016 -37.771   9.984  1.00217.87           C  
ANISOU 3131  CD  GLN A 458    26886  32154  23740    420   3837  -1062       C  
ATOM   3132  OE1 GLN A 458      21.011 -38.071   8.788  1.00231.79           O  
ANISOU 3132  OE1 GLN A 458    28625  34162  25280    519   3920  -1039       O  
ATOM   3133  NE2 GLN A 458      21.424 -36.594  10.425  1.00217.24           N  
ANISOU 3133  NE2 GLN A 458    26795  31883  23861    359   3903   -895       N  
ATOM   3134  N   VAL A 459      17.042 -41.394  10.155  1.00205.64           N  
ANISOU 3134  N   VAL A 459    25398  30880  21853    602   3304  -1717       N  
ATOM   3135  CA  VAL A 459      15.682 -41.686   9.680  1.00206.54           C  
ANISOU 3135  CA  VAL A 459    25520  31110  21843    696   3208  -1796       C  
ATOM   3136  C   VAL A 459      14.968 -42.693  10.575  1.00200.84           C  
ANISOU 3136  C   VAL A 459    24760  30247  21301    653   3075  -1952       C  
ATOM   3137  O   VAL A 459      13.810 -42.491  10.933  1.00201.81           O  
ANISOU 3137  O   VAL A 459    24920  30322  21434    669   3007  -1926       O  
ATOM   3138  CB  VAL A 459      15.669 -42.205   8.218  1.00211.33           C  
ANISOU 3138  CB  VAL A 459    26060  32006  22229    837   3214  -1924       C  
ATOM   3139  CG1 VAL A 459      14.279 -42.673   7.805  1.00212.77           C  
ANISOU 3139  CG1 VAL A 459    26220  32291  22332    941   3077  -2076       C  
ATOM   3140  CG2 VAL A 459      16.102 -41.109   7.263  1.00216.05           C  
ANISOU 3140  CG2 VAL A 459    26702  32778  22608    919   3366  -1710       C  
ATOM   3141  N   LYS A 460      15.667 -43.767  10.924  1.00193.29           N  
ANISOU 3141  N   LYS A 460    23721  29221  20499    604   3048  -2097       N  
ATOM   3142  CA  LYS A 460      15.106 -44.813  11.760  1.00188.64           C  
ANISOU 3142  CA  LYS A 460    23072  28484  20117    570   2947  -2214       C  
ATOM   3143  C   LYS A 460      14.679 -44.251  13.133  1.00185.77           C  
ANISOU 3143  C   LYS A 460    22791  27930  19861    510   2942  -2055       C  
ATOM   3144  O   LYS A 460      13.564 -44.531  13.622  1.00180.78           O  
ANISOU 3144  O   LYS A 460    22150  27231  19307    523   2879  -2058       O  
ATOM   3145  CB  LYS A 460      16.107 -45.964  11.921  1.00190.10           C  
ANISOU 3145  CB  LYS A 460    23155  28612  20460    530   2935  -2364       C  
ATOM   3146  CG  LYS A 460      15.405 -47.256  12.288  1.00190.88           C  
ANISOU 3146  CG  LYS A 460    23142  28606  20775    532   2830  -2517       C  
ATOM   3147  CD  LYS A 460      16.258 -48.238  13.075  1.00190.18           C  
ANISOU 3147  CD  LYS A 460    22982  28360  20917    471   2821  -2572       C  
ATOM   3148  CE  LYS A 460      15.362 -49.248  13.785  1.00186.09           C  
ANISOU 3148  CE  LYS A 460    22373  27675  20657    465   2748  -2612       C  
ATOM   3149  NZ  LYS A 460      16.149 -50.333  14.426  1.00182.07           N  
ANISOU 3149  NZ  LYS A 460    21773  27018  20385    428   2738  -2665       N  
ATOM   3150  N   ASP A 461      15.552 -43.415  13.710  1.00180.03           N  
ANISOU 3150  N   ASP A 461    22133  27129  19141    459   3008  -1924       N  
ATOM   3151  CA  ASP A 461      15.335 -42.765  15.006  1.00174.06           C  
ANISOU 3151  CA  ASP A 461    21449  26222  18462    431   2996  -1799       C  
ATOM   3152  C   ASP A 461      14.096 -41.890  14.956  1.00179.11           C  
ANISOU 3152  C   ASP A 461    22160  26888  19003    471   2977  -1698       C  
ATOM   3153  O   ASP A 461      13.216 -42.035  15.781  1.00188.80           O  
ANISOU 3153  O   ASP A 461    23401  28041  20292    484   2927  -1674       O  
ATOM   3154  CB  ASP A 461      16.553 -41.911  15.406  1.00170.10           C  
ANISOU 3154  CB  ASP A 461    20982  25653  17996    387   3055  -1722       C  
ATOM   3155  CG  ASP A 461      16.340 -41.128  16.709  1.00170.70           C  
ANISOU 3155  CG  ASP A 461    21122  25597  18138    389   3020  -1631       C  
ATOM   3156  OD1 ASP A 461      16.141 -41.763  17.763  1.00167.06           O  
ANISOU 3156  OD1 ASP A 461    20652  25061  17760    407   2966  -1659       O  
ATOM   3157  OD2 ASP A 461      16.350 -39.868  16.684  1.00173.61           O  
ANISOU 3157  OD2 ASP A 461    21541  25941  18480    388   3046  -1529       O  
ATOM   3158  N   ALA A 462      14.031 -40.973  13.996  1.00179.44           N  
ANISOU 3158  N   ALA A 462    22243  27039  18893    500   3025  -1623       N  
ATOM   3159  CA  ALA A 462      12.869 -40.090  13.855  1.00177.06           C  
ANISOU 3159  CA  ALA A 462    22010  26769  18494    548   3003  -1525       C  
ATOM   3160  C   ALA A 462      11.564 -40.850  13.597  1.00176.38           C  
ANISOU 3160  C   ALA A 462    21884  26742  18389    601   2920  -1630       C  
ATOM   3161  O   ALA A 462      10.504 -40.436  14.080  1.00186.64           O  
ANISOU 3161  O   ALA A 462    23223  27998  19695    621   2878  -1574       O  
ATOM   3162  CB  ALA A 462      13.104 -39.093  12.748  1.00177.76           C  
ANISOU 3162  CB  ALA A 462    22136  26978  18426    589   3082  -1410       C  
ATOM   3163  N   LEU A 463      11.643 -41.970  12.872  1.00167.31           N  
ANISOU 3163  N   LEU A 463    20640  25683  17246    627   2890  -1798       N  
ATOM   3164  CA  LEU A 463      10.464 -42.799  12.630  1.00161.98           C  
ANISOU 3164  CA  LEU A 463    19885  25035  16623    676   2797  -1937       C  
ATOM   3165  C   LEU A 463      10.028 -43.579  13.857  1.00158.17           C  
ANISOU 3165  C   LEU A 463    19350  24368  16378    625   2763  -1949       C  
ATOM   3166  O   LEU A 463       8.811 -43.679  14.102  1.00158.24           O  
ANISOU 3166  O   LEU A 463    19332  24341  16451    651   2714  -1954       O  
ATOM   3167  CB  LEU A 463      10.689 -43.774  11.482  1.00164.70           C  
ANISOU 3167  CB  LEU A 463    20117  25526  16935    737   2756  -2152       C  
ATOM   3168  CG  LEU A 463      10.708 -43.161  10.085  1.00170.58           C  
ANISOU 3168  CG  LEU A 463    20891  26519  17402    851   2774  -2160       C  
ATOM   3169  CD1 LEU A 463      11.247 -44.190   9.114  1.00172.56           C  
ANISOU 3169  CD1 LEU A 463    21021  26922  17621    920   2739  -2391       C  
ATOM   3170  CD2 LEU A 463       9.318 -42.723   9.649  1.00173.33           C  
ANISOU 3170  CD2 LEU A 463    21258  26953  17645    946   2700  -2169       C  
ATOM   3171  N   THR A 464      10.970 -44.149  14.624  1.00154.95           N  
ANISOU 3171  N   THR A 464    18917  23850  16106    565   2795  -1943       N  
ATOM   3172  CA  THR A 464      10.526 -44.866  15.844  1.00149.48           C  
ANISOU 3172  CA  THR A 464    18174  22995  15624    544   2783  -1906       C  
ATOM   3173  C   THR A 464       9.839 -43.912  16.801  1.00150.20           C  
ANISOU 3173  C   THR A 464    18363  23037  15669    559   2799  -1736       C  
ATOM   3174  O   THR A 464       8.897 -44.287  17.471  1.00151.89           O  
ANISOU 3174  O   THR A 464    18533  23178  15999    578   2790  -1694       O  
ATOM   3175  CB  THR A 464      11.616 -45.683  16.583  1.00150.61           C  
ANISOU 3175  CB  THR A 464    18273  23033  15916    503   2809  -1913       C  
ATOM   3176  OG1 THR A 464      12.731 -44.855  16.915  1.00156.67           O  
ANISOU 3176  OG1 THR A 464    19138  23809  16580    479   2854  -1836       O  
ATOM   3177  CG2 THR A 464      12.093 -46.869  15.744  1.00152.05           C  
ANISOU 3177  CG2 THR A 464    18324  23237  16208    494   2777  -2108       C  
ATOM   3178  N   LYS A 465      10.297 -42.664  16.844  1.00157.15           N  
ANISOU 3178  N   LYS A 465    19357  23953  16397    557   2827  -1642       N  
ATOM   3179  CA  LYS A 465       9.648 -41.624  17.659  1.00160.89           C  
ANISOU 3179  CA  LYS A 465    19918  24392  16819    585   2825  -1511       C  
ATOM   3180  C   LYS A 465       8.274 -41.254  17.139  1.00157.04           C  
ANISOU 3180  C   LYS A 465    19436  23962  16268    627   2789  -1506       C  
ATOM   3181  O   LYS A 465       7.362 -41.035  17.917  1.00157.02           O  
ANISOU 3181  O   LYS A 465    19444  23915  16298    658   2777  -1439       O  
ATOM   3182  CB  LYS A 465      10.507 -40.371  17.718  1.00163.89           C  
ANISOU 3182  CB  LYS A 465    20389  24772  17108    572   2850  -1439       C  
ATOM   3183  CG  LYS A 465      11.779 -40.572  18.510  1.00167.96           C  
ANISOU 3183  CG  LYS A 465    20898  25212  17705    547   2868  -1448       C  
ATOM   3184  CD  LYS A 465      12.629 -39.331  18.455  1.00173.92           C  
ANISOU 3184  CD  LYS A 465    21707  25943  18429    529   2888  -1401       C  
ATOM   3185  CE  LYS A 465      13.905 -39.523  19.240  1.00177.37           C  
ANISOU 3185  CE  LYS A 465    22121  26305  18965    514   2888  -1444       C  
ATOM   3186  NZ  LYS A 465      14.622 -38.223  19.196  1.00181.60           N  
ANISOU 3186  NZ  LYS A 465    22682  26787  19528    496   2901  -1407       N  
ATOM   3187  N   MET A 466       8.150 -41.189  15.819  1.00158.58           N  
ANISOU 3187  N   MET A 466    19618  24273  16361    645   2771  -1582       N  
ATOM   3188  CA  MET A 466       6.859 -40.951  15.151  1.00164.78           C  
ANISOU 3188  CA  MET A 466    20393  25136  17079    704   2717  -1614       C  
ATOM   3189  C   MET A 466       5.863 -42.052  15.407  1.00166.10           C  
ANISOU 3189  C   MET A 466    20437  25246  17428    715   2670  -1712       C  
ATOM   3190  O   MET A 466       4.670 -41.784  15.585  1.00167.53           O  
ANISOU 3190  O   MET A 466    20609  25416  17628    750   2637  -1690       O  
ATOM   3191  CB  MET A 466       7.036 -40.788  13.641  1.00172.77           C  
ANISOU 3191  CB  MET A 466    21403  26321  17919    758   2704  -1691       C  
ATOM   3192  CG  MET A 466       7.584 -39.415  13.260  1.00177.05           C  
ANISOU 3192  CG  MET A 466    22062  26921  18286    771   2764  -1535       C  
ATOM   3193  SD  MET A 466       7.955 -39.278  11.503  1.00189.52           S  
ANISOU 3193  SD  MET A 466    23635  28741  19633    867   2787  -1575       S  
ATOM   3194  CE  MET A 466       6.258 -39.186  10.916  1.00182.54           C  
ANISOU 3194  CE  MET A 466    22734  27962  18658    984   2677  -1652       C  
ATOM   3195  N   ARG A 467       6.370 -43.277  15.426  1.00171.36           N  
ANISOU 3195  N   ARG A 467    20993  25859  18253    683   2671  -1817       N  
ATOM   3196  CA  ARG A 467       5.541 -44.442  15.695  1.00179.01           C  
ANISOU 3196  CA  ARG A 467    21808  26730  19476    683   2638  -1903       C  
ATOM   3197  C   ARG A 467       4.903 -44.387  17.111  1.00183.66           C  
ANISOU 3197  C   ARG A 467    22402  27189  20190    676   2692  -1731       C  
ATOM   3198  O   ARG A 467       3.654 -44.511  17.289  1.00187.40           O  
ANISOU 3198  O   ARG A 467    22804  27622  20777    704   2675  -1725       O  
ATOM   3199  CB  ARG A 467       6.390 -45.707  15.554  1.00182.94           C  
ANISOU 3199  CB  ARG A 467    22188  27171  20149    648   2637  -2025       C  
ATOM   3200  CG  ARG A 467       5.575 -46.909  15.175  1.00185.53           C  
ANISOU 3200  CG  ARG A 467    22316  27428  20748    664   2569  -2200       C  
ATOM   3201  CD  ARG A 467       6.115 -48.198  15.764  1.00187.15           C  
ANISOU 3201  CD  ARG A 467    22388  27469  21250    617   2598  -2219       C  
ATOM   3202  NE  ARG A 467       5.016 -49.130  15.967  1.00190.27           N  
ANISOU 3202  NE  ARG A 467    22590  27714  21991    621   2572  -2274       N  
ATOM   3203  CZ  ARG A 467       5.128 -50.407  16.322  1.00193.61           C  
ANISOU 3203  CZ  ARG A 467    22833  27958  22771    592   2585  -2310       C  
ATOM   3204  NH1 ARG A 467       6.322 -50.975  16.496  1.00193.78           N  
ANISOU 3204  NH1 ARG A 467    22852  27940  22836    560   2610  -2315       N  
ATOM   3205  NH2 ARG A 467       4.020 -51.130  16.475  1.00194.75           N  
ANISOU 3205  NH2 ARG A 467    22784  27949  23262    596   2571  -2343       N  
ATOM   3206  N   ALA A 468       5.780 -44.118  18.083  1.00182.72           N  
ANISOU 3206  N   ALA A 468    22366  27027  20031    657   2756  -1598       N  
ATOM   3207  CA  ALA A 468       5.447 -44.022  19.500  1.00171.10           C  
ANISOU 3207  CA  ALA A 468    20914  25479  18616    686   2815  -1428       C  
ATOM   3208  C   ALA A 468       4.415 -42.947  19.757  1.00162.43           C  
ANISOU 3208  C   ALA A 468    19889  24426  17401    734   2804  -1349       C  
ATOM   3209  O   ALA A 468       3.518 -43.175  20.537  1.00157.92           O  
ANISOU 3209  O   ALA A 468    19264  23806  16932    772   2841  -1258       O  
ATOM   3210  CB  ALA A 468       6.693 -43.701  20.299  1.00167.07           C  
ANISOU 3210  CB  ALA A 468    20495  24963  18021    688   2850  -1350       C  
ATOM   3211  N   ALA A 469       4.584 -41.789  19.103  1.00158.68           N  
ANISOU 3211  N   ALA A 469    19527  24039  16724    736   2763  -1370       N  
ATOM   3212  CA  ALA A 469       3.650 -40.657  19.193  1.00159.37           C  
ANISOU 3212  CA  ALA A 469    19686  24168  16696    782   2737  -1310       C  
ATOM   3213  C   ALA A 469       2.306 -40.957  18.563  1.00163.95           C  
ANISOU 3213  C   ALA A 469    20180  24765  17346    804   2694  -1381       C  
ATOM   3214  O   ALA A 469       1.265 -40.510  19.068  1.00174.28           O  
ANISOU 3214  O   ALA A 469    21490  26065  18661    847   2693  -1318       O  
ATOM   3215  CB  ALA A 469       4.229 -39.413  18.535  1.00159.18           C  
ANISOU 3215  CB  ALA A 469    19783  24212  16485    778   2712  -1301       C  
ATOM   3216  N   ALA A 470       2.318 -41.710  17.469  1.00163.00           N  
ANISOU 3216  N   ALA A 470    19972  24677  17284    788   2650  -1534       N  
ATOM   3217  CA  ALA A 470       1.078 -42.106  16.813  1.00172.48           C  
ANISOU 3217  CA  ALA A 470    21059  25891  18584    823   2584  -1653       C  
ATOM   3218  C   ALA A 470       0.302 -43.165  17.616  1.00177.47           C  
ANISOU 3218  C   ALA A 470    21527  26381  19520    811   2623  -1635       C  
ATOM   3219  O   ALA A 470      -0.949 -43.072  17.718  1.00186.03           O  
ANISOU 3219  O   ALA A 470    22543  27442  20696    845   2605  -1638       O  
ATOM   3220  CB  ALA A 470       1.357 -42.598  15.405  1.00176.44           C  
ANISOU 3220  CB  ALA A 470    21498  26489  19050    842   2506  -1856       C  
ATOM   3221  N   LEU A 471       1.023 -44.139  18.197  1.00176.19           N  
ANISOU 3221  N   LEU A 471    21295  26121  19528    770   2687  -1599       N  
ATOM   3222  CA  LEU A 471       0.364 -45.130  19.097  1.00177.34           C  
ANISOU 3222  CA  LEU A 471    21280  26115  19986    766   2761  -1513       C  
ATOM   3223  C   LEU A 471      -0.263 -44.514  20.362  1.00174.12           C  
ANISOU 3223  C   LEU A 471    20928  25698  19530    815   2851  -1291       C  
ATOM   3224  O   LEU A 471      -1.357 -44.926  20.795  1.00165.70           O  
ANISOU 3224  O   LEU A 471    19730  24552  18676    837   2900  -1229       O  
ATOM   3225  CB  LEU A 471       1.345 -46.210  19.525  1.00176.80           C  
ANISOU 3225  CB  LEU A 471    21139  25945  20088    728   2820  -1481       C  
ATOM   3226  CG  LEU A 471       1.758 -47.121  18.386  1.00183.09           C  
ANISOU 3226  CG  LEU A 471    21814  26721  21029    692   2735  -1719       C  
ATOM   3227  CD1 LEU A 471       3.106 -47.724  18.743  1.00182.99           C  
ANISOU 3227  CD1 LEU A 471    21818  26664  21046    656   2781  -1683       C  
ATOM   3228  CD2 LEU A 471       0.696 -48.185  18.104  1.00187.04           C  
ANISOU 3228  CD2 LEU A 471    22065  27081  21919    689   2704  -1837       C  
ATOM   3229  N   ASP A 472       0.470 -43.560  20.934  1.00170.06           N  
ANISOU 3229  N   ASP A 472    20592  25265  18757    840   2871  -1188       N  
ATOM   3230  CA  ASP A 472       0.037 -42.752  22.055  1.00166.44           C  
ANISOU 3230  CA  ASP A 472    20213  24846  18179    914   2926  -1022       C  
ATOM   3231  C   ASP A 472      -1.133 -41.877  21.673  1.00163.97           C  
ANISOU 3231  C   ASP A 472    19922  24585  17791    943   2871  -1059       C  
ATOM   3232  O   ASP A 472      -2.128 -41.840  22.408  1.00175.32           O  
ANISOU 3232  O   ASP A 472    21301  26008  19302    999   2928   -957       O  
ATOM   3233  CB  ASP A 472       1.181 -41.810  22.522  1.00166.77           C  
ANISOU 3233  CB  ASP A 472    20427  24963  17972    939   2913   -981       C  
ATOM   3234  CG  ASP A 472       1.062 -41.424  23.973  1.00171.63           C  
ANISOU 3234  CG  ASP A 472    21085  25615  18510   1045   2979   -821       C  
ATOM   3235  OD1 ASP A 472       0.784 -42.301  24.820  1.00175.10           O  
ANISOU 3235  OD1 ASP A 472    21426  26016  19086   1096   3079   -691       O  
ATOM   3236  OD2 ASP A 472       1.249 -40.225  24.261  1.00173.52           O  
ANISOU 3236  OD2 ASP A 472    21446  25926  18555   1093   2930   -826       O  
ATOM   3237  N   ALA A 473      -1.045 -41.169  20.543  1.00158.40           N  
ANISOU 3237  N   ALA A 473    19294  23949  16939    920   2769  -1190       N  
ATOM   3238  CA  ALA A 473      -2.186 -40.353  20.088  1.00161.62           C  
ANISOU 3238  CA  ALA A 473    19720  24409  17279    959   2704  -1230       C  
ATOM   3239  C   ALA A 473      -3.426 -41.213  19.779  1.00169.46           C  
ANISOU 3239  C   ALA A 473    20526  25338  18523    962   2694  -1309       C  
ATOM   3240  O   ALA A 473      -4.556 -40.741  19.999  1.00167.28           O  
ANISOU 3240  O   ALA A 473    20224  25071  18262   1007   2686  -1284       O  
ATOM   3241  CB  ALA A 473      -1.821 -39.538  18.868  1.00163.40           C  
ANISOU 3241  CB  ALA A 473    20051  24728  17305    954   2609  -1331       C  
ATOM   3242  N   GLN A 474      -3.208 -42.445  19.275  1.00177.64           N  
ANISOU 3242  N   GLN A 474    21416  26301  19778    916   2687  -1420       N  
ATOM   3243  CA  GLN A 474      -4.308 -43.436  19.047  1.00186.64           C  
ANISOU 3243  CA  GLN A 474    22326  27332  21255    913   2677  -1515       C  
ATOM   3244  C   GLN A 474      -5.118 -43.792  20.314  1.00189.32           C  
ANISOU 3244  C   GLN A 474    22555  27565  21812    932   2813  -1319       C  
ATOM   3245  O   GLN A 474      -6.320 -44.023  20.223  1.00191.03           O  
ANISOU 3245  O   GLN A 474    22620  27720  22242    949   2806  -1362       O  
ATOM   3246  CB  GLN A 474      -3.739 -44.724  18.441  1.00190.62           C  
ANISOU 3246  CB  GLN A 474    22681  27752  21991    864   2648  -1666       C  
ATOM   3247  CG  GLN A 474      -4.731 -45.766  17.931  1.00199.95           C  
ANISOU 3247  CG  GLN A 474    23597  28808  23564    860   2594  -1843       C  
ATOM   3248  CD  GLN A 474      -4.026 -46.823  17.081  1.00209.97           C  
ANISOU 3248  CD  GLN A 474    24744  30034  24999    831   2516  -2062       C  
ATOM   3249  OE1 GLN A 474      -3.062 -47.445  17.531  1.00215.15           O  
ANISOU 3249  OE1 GLN A 474    25397  30619  25728    785   2590  -1978       O  
ATOM   3250  NE2 GLN A 474      -4.480 -47.015  15.846  1.00217.48           N  
ANISOU 3250  NE2 GLN A 474    25592  31044  25996    875   2355  -2359       N  
ATOM   3251  N   LYS A 475      -4.448 -43.837  21.470  1.00186.05           N  
ANISOU 3251  N   LYS A 475    22207  27142  21339    947   2937  -1107       N  
ATOM   3252  CA  LYS A 475      -5.108 -44.078  22.772  1.00179.87           C  
ANISOU 3252  CA  LYS A 475    21342  26309  20690   1004   3092   -874       C  
ATOM   3253  C   LYS A 475      -6.077 -42.974  23.247  1.00188.01           C  
ANISOU 3253  C   LYS A 475    22442  27435  21555   1082   3100   -803       C  
ATOM   3254  O   LYS A 475      -7.042 -43.271  23.942  1.00190.57           O  
ANISOU 3254  O   LYS A 475    22635  27712  22061   1127   3210   -671       O  
ATOM   3255  CB  LYS A 475      -4.061 -44.322  23.867  1.00168.97           C  
ANISOU 3255  CB  LYS A 475    20034  24944  19220   1042   3206   -677       C  
ATOM   3256  CG  LYS A 475      -3.321 -45.624  23.707  1.00163.87           C  
ANISOU 3256  CG  LYS A 475    19269  24169  18824    981   3241   -687       C  
ATOM   3257  CD  LYS A 475      -2.203 -45.717  24.721  1.00163.84           C  
ANISOU 3257  CD  LYS A 475    19366  24209  18675   1036   3328   -512       C  
ATOM   3258  CE  LYS A 475      -1.224 -46.842  24.397  1.00169.04           C  
ANISOU 3258  CE  LYS A 475    19946  24755  19523    969   3327   -562       C  
ATOM   3259  NZ  LYS A 475       0.157 -46.541  24.887  1.00168.86           N  
ANISOU 3259  NZ  LYS A 475    20089  24822  19247   1001   3323   -518       N  
ATOM   3260  N   ALA A 476      -5.790 -41.715  22.900  1.00196.79           N  
ANISOU 3260  N   ALA A 476    23749  28674  22345   1100   2994   -878       N  
ATOM   3261  CA  ALA A 476      -6.582 -40.524  23.321  1.00199.35           C  
ANISOU 3261  CA  ALA A 476    24158  29093  22491   1179   2977   -833       C  
ATOM   3262  C   ALA A 476      -8.050 -40.579  22.905  1.00200.21           C  
ANISOU 3262  C   ALA A 476    24126  29162  22781   1186   2951   -903       C  
ATOM   3263  O   ALA A 476      -8.408 -41.246  21.928  1.00202.83           O  
ANISOU 3263  O   ALA A 476    24330  29418  23317   1130   2883  -1062       O  
ATOM   3264  CB  ALA A 476      -5.951 -39.253  22.755  1.00202.10           C  
ANISOU 3264  CB  ALA A 476    24711  29541  22537   1178   2851   -925       C  
ATOM   3265  N   THR A 477      -8.884 -39.844  23.636  1.00197.47           N  
ANISOU 3265  N   THR A 477    23796  28876  22355   1269   2991   -811       N  
ATOM   3266  CA  THR A 477     -10.323 -39.772  23.366  1.00203.27           C  
ANISOU 3266  CA  THR A 477    24399  29580  23253   1288   2971   -870       C  
ATOM   3267  C   THR A 477     -10.793 -38.323  23.577  1.00210.49           C  
ANISOU 3267  C   THR A 477    25456  30616  23903   1368   2903   -875       C  
ATOM   3268  O   THR A 477     -10.437 -37.719  24.583  1.00217.87           O  
ANISOU 3268  O   THR A 477    26495  31636  24650   1444   2961   -749       O  
ATOM   3269  CB  THR A 477     -11.099 -40.722  24.313  1.00201.25           C  
ANISOU 3269  CB  THR A 477    23926  29235  23302   1318   3158   -694       C  
ATOM   3270  OG1 THR A 477     -10.331 -41.919  24.543  1.00203.20           O  
ANISOU 3270  OG1 THR A 477    24084  29381  23740   1270   3257   -605       O  
ATOM   3271  CG2 THR A 477     -12.485 -41.073  23.737  1.00199.54           C  
ANISOU 3271  CG2 THR A 477    23499  28921  23395   1298   3128   -808       C  
ATOM   3272  N   PRO A 478     -11.557 -37.738  22.622  1.00211.16           N  
ANISOU 3272  N   PRO A 478    25544  30714  23969   1365   2765  -1036       N  
ATOM   3273  CA  PRO A 478     -12.213 -36.438  22.938  1.00202.70           C  
ANISOU 3273  CA  PRO A 478    24569  29733  22712   1450   2715  -1026       C  
ATOM   3274  C   PRO A 478     -13.402 -36.616  23.923  1.00195.35           C  
ANISOU 3274  C   PRO A 478    23489  28799  21937   1521   2839   -917       C  
ATOM   3275  O   PRO A 478     -14.003 -37.683  23.942  1.00197.06           O  
ANISOU 3275  O   PRO A 478    23499  28916  22455   1490   2927   -896       O  
ATOM   3276  CB  PRO A 478     -12.610 -35.888  21.557  1.00202.70           C  
ANISOU 3276  CB  PRO A 478    24610  29749  22655   1436   2535  -1216       C  
ATOM   3277  CG  PRO A 478     -12.534 -37.035  20.591  1.00203.95           C  
ANISOU 3277  CG  PRO A 478    24637  29836  23017   1367   2498  -1350       C  
ATOM   3278  CD  PRO A 478     -11.834 -38.199  21.243  1.00209.33           C  
ANISOU 3278  CD  PRO A 478    25231  30436  23868   1311   2640  -1244       C  
ATOM   3279  N   PRO A 479     -13.737 -35.577  24.728  1.00184.86           N  
ANISOU 3279  N   PRO A 479    22244  27572  20422   1624   2848   -852       N  
ATOM   3280  CA  PRO A 479     -14.442 -35.799  26.023  1.00175.33           C  
ANISOU 3280  CA  PRO A 479    20921  26410  19284   1725   3021   -681       C  
ATOM   3281  C   PRO A 479     -15.846 -36.402  25.942  1.00161.81           C  
ANISOU 3281  C   PRO A 479    18978  24622  17880   1722   3094   -678       C  
ATOM   3282  O   PRO A 479     -16.178 -37.262  26.742  1.00144.98           O  
ANISOU 3282  O   PRO A 479    16682  22458  15943   1752   3286   -502       O  
ATOM   3283  CB  PRO A 479     -14.522 -34.393  26.642  1.00178.79           C  
ANISOU 3283  CB  PRO A 479    21505  26986  19441   1845   2957   -690       C  
ATOM   3284  CG  PRO A 479     -14.281 -33.424  25.528  1.00183.37           C  
ANISOU 3284  CG  PRO A 479    22230  27548  19892   1793   2750   -865       C  
ATOM   3285  CD  PRO A 479     -13.735 -34.153  24.326  1.00182.88           C  
ANISOU 3285  CD  PRO A 479    22162  27391  19934   1663   2690   -951       C  
ATOM   3286  N   ASP A 487     -16.157 -48.253  20.944  1.00222.50           N  
ANISOU 3286  N   ASP A 487    24506  30502  29530    957   3115  -1556       N  
ATOM   3287  CA  ASP A 487     -16.760 -48.762  19.718  1.00221.04           C  
ANISOU 3287  CA  ASP A 487    24083  30200  29700    945   2887  -1978       C  
ATOM   3288  C   ASP A 487     -17.554 -47.705  18.914  1.00230.05           C  
ANISOU 3288  C   ASP A 487    25320  31521  30565   1020   2675  -2245       C  
ATOM   3289  O   ASP A 487     -18.202 -48.073  17.950  1.00227.91           O  
ANISOU 3289  O   ASP A 487    24836  31174  30584   1042   2479  -2605       O  
ATOM   3290  CB  ASP A 487     -17.637 -49.999  20.029  1.00217.07           C  
ANISOU 3290  CB  ASP A 487    23137  29355  29983    896   3009  -1949       C  
ATOM   3291  CG  ASP A 487     -16.847 -51.174  20.609  1.00212.48           C  
ANISOU 3291  CG  ASP A 487    22422  28565  29746    828   3186  -1729       C  
ATOM   3292  OD1 ASP A 487     -15.588 -51.154  20.633  1.00205.05           O  
ANISOU 3292  OD1 ASP A 487    21711  27735  28461    816   3178  -1666       O  
ATOM   3293  OD2 ASP A 487     -17.517 -52.138  21.039  1.00208.78           O  
ANISOU 3293  OD2 ASP A 487    21595  27801  29931    789   3338  -1614       O  
ATOM   3294  N   SER A 488     -17.496 -46.413  19.285  1.00242.30           N  
ANISOU 3294  N   SER A 488    27178  33307  31576   1074   2698  -2088       N  
ATOM   3295  CA  SER A 488     -18.232 -45.312  18.598  1.00246.53           C  
ANISOU 3295  CA  SER A 488    27827  34017  31825   1155   2511  -2294       C  
ATOM   3296  C   SER A 488     -17.851 -45.161  17.109  1.00255.46           C  
ANISOU 3296  C   SER A 488    29035  35279  32746   1205   2221  -2679       C  
ATOM   3297  O   SER A 488     -16.664 -45.365  16.773  1.00265.27           O  
ANISOU 3297  O   SER A 488    30417  36588  33783   1183   2188  -2697       O  
ATOM   3298  CB  SER A 488     -17.950 -43.984  19.324  1.00237.63           C  
ANISOU 3298  CB  SER A 488    27032  33103  30151   1198   2596  -2032       C  
ATOM   3299  OG  SER A 488     -18.629 -42.890  18.735  1.00230.34           O  
ANISOU 3299  OG  SER A 488    26222  32333  28961   1278   2429  -2192       O  
ATOM   3300  N   PRO A 489     -18.834 -44.801  16.219  1.00255.74           N  
ANISOU 3300  N   PRO A 489    28982  35372  32815   1291   2013  -2982       N  
ATOM   3301  CA  PRO A 489     -18.501 -44.615  14.786  1.00255.63           C  
ANISOU 3301  CA  PRO A 489    29046  35532  32546   1384   1739  -3338       C  
ATOM   3302  C   PRO A 489     -17.490 -43.492  14.507  1.00259.21           C  
ANISOU 3302  C   PRO A 489    29897  36255  32336   1427   1707  -3219       C  
ATOM   3303  O   PRO A 489     -16.756 -43.567  13.527  1.00262.13           O  
ANISOU 3303  O   PRO A 489    30349  36759  32486   1481   1563  -3406       O  
ATOM   3304  CB  PRO A 489     -19.850 -44.263  14.135  1.00248.53           C  
ANISOU 3304  CB  PRO A 489    27999  34663  31766   1491   1555  -3615       C  
ATOM   3305  CG  PRO A 489     -20.890 -44.672  15.110  1.00247.05           C  
ANISOU 3305  CG  PRO A 489    27553  34239  32074   1424   1723  -3474       C  
ATOM   3306  CD  PRO A 489     -20.268 -44.543  16.466  1.00248.14           C  
ANISOU 3306  CD  PRO A 489    27841  34337  32103   1326   2018  -3016       C  
ATOM   3307  N   GLU A 490     -17.443 -42.483  15.381  1.00260.89           N  
ANISOU 3307  N   GLU A 490    30331  36537  32256   1410   1845  -2910       N  
ATOM   3308  CA  GLU A 490     -16.463 -41.374  15.296  1.00253.30           C  
ANISOU 3308  CA  GLU A 490    29724  35782  30733   1435   1843  -2757       C  
ATOM   3309  C   GLU A 490     -15.066 -41.841  15.694  1.00249.37           C  
ANISOU 3309  C   GLU A 490    29329  35260  30158   1348   1966  -2595       C  
ATOM   3310  O   GLU A 490     -14.076 -41.505  15.047  1.00230.86           O  
ANISOU 3310  O   GLU A 490    27169  33057  27488   1369   1898  -2629       O  
ATOM   3311  CB  GLU A 490     -16.856 -40.218  16.223  1.00252.09           C  
ANISOU 3311  CB  GLU A 490    29736  35679  30366   1446   1949  -2501       C  
ATOM   3312  CG  GLU A 490     -18.134 -39.531  15.828  1.00251.92           C  
ANISOU 3312  CG  GLU A 490    29666  35711  30341   1541   1822  -2639       C  
ATOM   3313  CD  GLU A 490     -17.969 -38.614  14.626  1.00255.95           C  
ANISOU 3313  CD  GLU A 490    30363  36428  30455   1655   1619  -2789       C  
ATOM   3314  OE1 GLU A 490     -16.821 -38.425  14.104  1.00258.34           O  
ANISOU 3314  OE1 GLU A 490    30847  36845  30463   1660   1592  -2763       O  
ATOM   3315  OE2 GLU A 490     -19.017 -38.070  14.197  1.00261.96           O  
ANISOU 3315  OE2 GLU A 490    31083  37244  31205   1752   1492  -2923       O  
ATOM   3316  N   MET A 491     -15.025 -42.607  16.782  1.00255.47           N  
ANISOU 3316  N   MET A 491    29972  35855  31240   1261   2157  -2404       N  
ATOM   3317  CA  MET A 491     -13.812 -43.237  17.295  1.00258.26           C  
ANISOU 3317  CA  MET A 491    30372  36151  31603   1182   2285  -2247       C  
ATOM   3318  C   MET A 491     -13.226 -44.303  16.387  1.00259.14           C  
ANISOU 3318  C   MET A 491    30350  36208  31903   1159   2180  -2490       C  
ATOM   3319  O   MET A 491     -11.991 -44.442  16.372  1.00265.42           O  
ANISOU 3319  O   MET A 491    31280  37049  32517   1123   2212  -2425       O  
ATOM   3320  CB  MET A 491     -14.135 -43.926  18.625  1.00259.91           C  
ANISOU 3320  CB  MET A 491    30420  36177  32157   1126   2513  -1988       C  
ATOM   3321  CG  MET A 491     -12.974 -44.285  19.509  1.00260.51           C  
ANISOU 3321  CG  MET A 491    30594  36226  32162   1075   2681  -1734       C  
ATOM   3322  SD  MET A 491     -12.142 -42.858  20.184  1.00263.46           S  
ANISOU 3322  SD  MET A 491    31335  36811  31957   1115   2730  -1512       S  
ATOM   3323  CE  MET A 491     -11.051 -43.710  21.320  1.00258.69           C  
ANISOU 3323  CE  MET A 491    30727  36124  31439   1074   2934  -1244       C  
ATOM   3324  N   LYS A 492     -14.092 -45.061  15.680  1.00249.58           N  
ANISOU 3324  N   LYS A 492    28860  34894  31073   1187   2052  -2779       N  
ATOM   3325  CA  LYS A 492     -13.641 -46.106  14.703  1.00232.30           C  
ANISOU 3325  CA  LYS A 492    26504  32661  29097   1194   1910  -3089       C  
ATOM   3326  C   LYS A 492     -12.680 -45.571  13.646  1.00223.71           C  
ANISOU 3326  C   LYS A 492    25645  31828  27526   1267   1765  -3233       C  
ATOM   3327  O   LYS A 492     -11.560 -46.112  13.456  1.00220.59           O  
ANISOU 3327  O   LYS A 492    25285  31441  27088   1231   1778  -3251       O  
ATOM   3328  CB  LYS A 492     -14.853 -46.720  13.957  1.00229.02           C  
ANISOU 3328  CB  LYS A 492    25766  32143  29108   1257   1736  -3448       C  
ATOM   3329  CG  LYS A 492     -15.438 -47.948  14.627  1.00224.21           C  
ANISOU 3329  CG  LYS A 492    24799  31204  29186   1169   1852  -3420       C  
ATOM   3330  CD  LYS A 492     -16.807 -48.246  14.019  1.00219.58           C  
ANISOU 3330  CD  LYS A 492    23906  30519  29003   1237   1686  -3752       C  
ATOM   3331  CE  LYS A 492     -17.612 -49.306  14.716  1.00216.56           C  
ANISOU 3331  CE  LYS A 492    23140  29786  29356   1152   1817  -3697       C  
ATOM   3332  NZ  LYS A 492     -18.955 -49.422  14.096  1.00217.79           N  
ANISOU 3332  NZ  LYS A 492    23011  29864  29872   1227   1639  -4039       N  
ATOM   3333  N   ASP A 493     -13.138 -44.496  12.999  1.00220.24           N  
ANISOU 3333  N   ASP A 493    25353  31593  26734   1377   1641  -3312       N  
ATOM   3334  CA  ASP A 493     -12.407 -43.767  11.965  1.00219.33           C  
ANISOU 3334  CA  ASP A 493    25462  31749  26125   1478   1520  -3400       C  
ATOM   3335  C   ASP A 493     -11.180 -43.020  12.496  1.00223.49           C  
ANISOU 3335  C   ASP A 493    26286  32357  26272   1413   1668  -3084       C  
ATOM   3336  O   ASP A 493     -10.191 -42.850  11.762  1.00215.73           O  
ANISOU 3336  O   ASP A 493    25437  31536  24994   1455   1624  -3128       O  
ATOM   3337  CB  ASP A 493     -13.345 -42.762  11.284  1.00216.32           C  
ANISOU 3337  CB  ASP A 493    25150  31540  25502   1620   1374  -3507       C  
ATOM   3338  CG  ASP A 493     -14.262 -43.408  10.262  1.00216.05           C  
ANISOU 3338  CG  ASP A 493    24855  31527  25706   1749   1149  -3926       C  
ATOM   3339  OD1 ASP A 493     -13.807 -43.806   9.164  1.00210.41           O  
ANISOU 3339  OD1 ASP A 493    24103  30967  24875   1861    995  -4195       O  
ATOM   3340  OD2 ASP A 493     -15.460 -43.493  10.563  1.00216.54           O  
ANISOU 3340  OD2 ASP A 493    24741  31463  26071   1752   1121  -3997       O  
ATOM   3341  N   PHE A 494     -11.241 -42.592  13.764  1.00231.16           N  
ANISOU 3341  N   PHE A 494    27342  33223  27262   1325   1842  -2779       N  
ATOM   3342  CA  PHE A 494     -10.107 -41.982  14.467  1.00236.48           C  
ANISOU 3342  CA  PHE A 494    28255  33935  27659   1261   1982  -2497       C  
ATOM   3343  C   PHE A 494      -9.014 -43.023  14.763  1.00246.78           C  
ANISOU 3343  C   PHE A 494    29505  35142  29119   1173   2067  -2467       C  
ATOM   3344  O   PHE A 494      -7.862 -42.833  14.354  1.00267.69           O  
ANISOU 3344  O   PHE A 494    32298  37895  31514   1168   2062  -2455       O  
ATOM   3345  CB  PHE A 494     -10.590 -41.257  15.747  1.00228.44           C  
ANISOU 3345  CB  PHE A 494    27316  32855  26624   1230   2118  -2228       C  
ATOM   3346  CG  PHE A 494      -9.525 -40.411  16.428  1.00216.34           C  
ANISOU 3346  CG  PHE A 494    26030  31383  24785   1198   2220  -1984       C  
ATOM   3347  CD1 PHE A 494      -8.993 -39.294  15.778  1.00209.54           C  
ANISOU 3347  CD1 PHE A 494    25380  30677  23557   1245   2151  -1970       C  
ATOM   3348  CD2 PHE A 494      -9.074 -40.703  17.718  1.00205.53           C  
ANISOU 3348  CD2 PHE A 494    24667  29916  23506   1137   2384  -1768       C  
ATOM   3349  CE1 PHE A 494      -8.014 -38.511  16.367  1.00203.66           C  
ANISOU 3349  CE1 PHE A 494    24829  29961  22590   1215   2231  -1775       C  
ATOM   3350  CE2 PHE A 494      -8.100 -39.923  18.309  1.00198.46           C  
ANISOU 3350  CE2 PHE A 494    23978  29081  22346   1126   2448  -1594       C  
ATOM   3351  CZ  PHE A 494      -7.573 -38.826  17.640  1.00199.75           C  
ANISOU 3351  CZ  PHE A 494    24331  29369  22193   1156   2368  -1609       C  
ATOM   3352  N   ARG A 495      -9.370 -44.121  15.437  1.00239.30           N  
ANISOU 3352  N   ARG A 495    28334  33987  28599   1109   2150  -2450       N  
ATOM   3353  CA  ARG A 495      -8.392 -45.178  15.739  1.00228.61           C  
ANISOU 3353  CA  ARG A 495    26906  32518  27434   1032   2228  -2417       C  
ATOM   3354  C   ARG A 495      -7.849 -45.838  14.456  1.00233.63           C  
ANISOU 3354  C   ARG A 495    27462  33221  28086   1067   2071  -2729       C  
ATOM   3355  O   ARG A 495      -6.651 -46.141  14.389  1.00231.69           O  
ANISOU 3355  O   ARG A 495    27291  33001  27738   1029   2104  -2704       O  
ATOM   3356  CB  ARG A 495      -8.996 -46.271  16.610  1.00215.93           C  
ANISOU 3356  CB  ARG A 495    25042  30661  26338    973   2347  -2332       C  
ATOM   3357  CG  ARG A 495      -9.452 -45.922  18.007  1.00210.29           C  
ANISOU 3357  CG  ARG A 495    24360  29878  25659    956   2539  -2001       C  
ATOM   3358  CD  ARG A 495     -10.309 -47.079  18.513  1.00207.71           C  
ANISOU 3358  CD  ARG A 495    23712  29303  25903    922   2635  -1967       C  
ATOM   3359  NE  ARG A 495     -11.680 -47.060  17.981  1.00206.46           N  
ANISOU 3359  NE  ARG A 495    23364  29097  25984    960   2532  -2166       N  
ATOM   3360  CZ  ARG A 495     -12.681 -47.828  18.414  1.00202.24           C  
ANISOU 3360  CZ  ARG A 495    22535  28345  25960    939   2617  -2133       C  
ATOM   3361  NH1 ARG A 495     -12.482 -48.701  19.395  1.00203.06           N  
ANISOU 3361  NH1 ARG A 495    22500  28260  26393    886   2823  -1876       N  
ATOM   3362  NH2 ARG A 495     -13.886 -47.742  17.849  1.00200.72           N  
ANISOU 3362  NH2 ARG A 495    22171  28118  25974    979   2499  -2352       N  
ATOM   3363  N   HIS A 496      -8.708 -46.021  13.432  1.00237.20           N  
ANISOU 3363  N   HIS A 496    27762  33720  28642   1156   1893  -3038       N  
ATOM   3364  CA  HIS A 496      -8.265 -46.588  12.134  1.00233.36           C  
ANISOU 3364  CA  HIS A 496    27192  33348  28126   1236   1718  -3377       C  
ATOM   3365  C   HIS A 496      -7.274 -45.693  11.384  1.00246.95           C  
ANISOU 3365  C   HIS A 496    29181  35346  29300   1306   1683  -3353       C  
ATOM   3366  O   HIS A 496      -6.297 -46.187  10.812  1.00255.91           O  
ANISOU 3366  O   HIS A 496    30316  36556  30362   1320   1650  -3472       O  
ATOM   3367  CB  HIS A 496      -9.452 -46.894  11.217  1.00223.67           C  
ANISOU 3367  CB  HIS A 496    25739  32142  27102   1354   1515  -3736       C  
ATOM   3368  CG  HIS A 496      -9.082 -47.688  10.006  1.00217.61           C  
ANISOU 3368  CG  HIS A 496    24824  31473  26384   1456   1326  -4126       C  
ATOM   3369  ND1 HIS A 496      -8.639 -48.990  10.082  1.00217.34           N  
ANISOU 3369  ND1 HIS A 496    24568  31252  26759   1394   1323  -4269       N  
ATOM   3370  CD2 HIS A 496      -9.082 -47.366   8.691  1.00213.01           C  
ANISOU 3370  CD2 HIS A 496    24279  31170  25485   1638   1133  -4408       C  
ATOM   3371  CE1 HIS A 496      -8.391 -49.440   8.863  1.00212.90           C  
ANISOU 3371  CE1 HIS A 496    23903  30850  26139   1530   1122  -4651       C  
ATOM   3372  NE2 HIS A 496      -8.646 -48.473   8.002  1.00209.87           N  
ANISOU 3372  NE2 HIS A 496    23678  30766  25297   1689   1008  -4738       N  
ATOM   3373  N   GLY A 497      -7.514 -44.377  11.410  1.00253.02           N  
ANISOU 3373  N   GLY A 497    30168  36257  29711   1350   1703  -3184       N  
ATOM   3374  CA  GLY A 497      -6.598 -43.397  10.812  1.00251.38           C  
ANISOU 3374  CA  GLY A 497    30213  36281  29019   1408   1707  -3087       C  
ATOM   3375  C   GLY A 497      -5.161 -43.497  11.299  1.00249.68           C  
ANISOU 3375  C   GLY A 497    30120  36035  28710   1305   1844  -2903       C  
ATOM   3376  O   GLY A 497      -4.229 -43.375  10.501  1.00250.30           O  
ANISOU 3376  O   GLY A 497    30286  36281  28536   1356   1822  -2954       O  
ATOM   3377  N   PHE A 498      -4.991 -43.737  12.602  1.00242.14           N  
ANISOU 3377  N   PHE A 498    29162  34880  27958   1176   1988  -2692       N  
ATOM   3378  CA  PHE A 498      -3.663 -43.967  13.205  1.00234.98           C  
ANISOU 3378  CA  PHE A 498    28343  33920  27017   1082   2110  -2534       C  
ATOM   3379  C   PHE A 498      -3.087 -45.338  12.917  1.00234.30           C  
ANISOU 3379  C   PHE A 498    28080  33754  27187   1051   2083  -2716       C  
ATOM   3380  O   PHE A 498      -1.888 -45.434  12.726  1.00240.92           O  
ANISOU 3380  O   PHE A 498    29000  34653  27885   1027   2117  -2697       O  
ATOM   3381  CB  PHE A 498      -3.674 -43.764  14.724  1.00225.81           C  
ANISOU 3381  CB  PHE A 498    27235  32603  25956    994   2263  -2252       C  
ATOM   3382  CG  PHE A 498      -3.673 -42.334  15.110  1.00217.47           C  
ANISOU 3382  CG  PHE A 498    26395  31633  24598   1012   2304  -2055       C  
ATOM   3383  CD1 PHE A 498      -2.517 -41.574  14.916  1.00213.73           C  
ANISOU 3383  CD1 PHE A 498    26109  31262  23838   1004   2334  -1961       C  
ATOM   3384  CD2 PHE A 498      -4.825 -41.720  15.587  1.00212.01           C  
ANISOU 3384  CD2 PHE A 498    25705  30918  23929   1043   2306  -1981       C  
ATOM   3385  CE1 PHE A 498      -2.498 -40.240  15.250  1.00209.63           C  
ANISOU 3385  CE1 PHE A 498    25763  30792  23094   1022   2362  -1795       C  
ATOM   3386  CE2 PHE A 498      -4.821 -40.379  15.932  1.00208.41           C  
ANISOU 3386  CE2 PHE A 498    25436  30531  23218   1068   2328  -1821       C  
ATOM   3387  CZ  PHE A 498      -3.649 -39.646  15.758  1.00206.74           C  
ANISOU 3387  CZ  PHE A 498    25398  30398  22753   1056   2352  -1733       C  
ATOM   3388  N   ASP A 499      -3.938 -46.374  12.884  1.00225.28           N  
ANISOU 3388  N   ASP A 499    26683  32465  26445   1053   2021  -2895       N  
ATOM   3389  CA  ASP A 499      -3.546 -47.744  12.472  1.00213.24           C  
ANISOU 3389  CA  ASP A 499    24941  30846  25235   1040   1960  -3130       C  
ATOM   3390  C   ASP A 499      -2.863 -47.726  11.112  1.00213.09           C  
ANISOU 3390  C   ASP A 499    24957  31063  24943   1145   1828  -3383       C  
ATOM   3391  O   ASP A 499      -1.857 -48.406  10.908  1.00202.98           O  
ANISOU 3391  O   ASP A 499    23641  29779  23702   1121   1833  -3463       O  
ATOM   3392  CB  ASP A 499      -4.764 -48.675  12.346  1.00210.73           C  
ANISOU 3392  CB  ASP A 499    24315  30352  25397   1060   1867  -3351       C  
ATOM   3393  CG  ASP A 499      -5.182 -49.295  13.659  1.00205.63           C  
ANISOU 3393  CG  ASP A 499    23535  29418  25174    950   2022  -3125       C  
ATOM   3394  OD1 ASP A 499      -4.310 -49.909  14.332  1.00197.35           O  
ANISOU 3394  OD1 ASP A 499    22481  28246  24254    870   2138  -2974       O  
ATOM   3395  OD2 ASP A 499      -6.395 -49.206  13.978  1.00203.68           O  
ANISOU 3395  OD2 ASP A 499    23172  29074  25140    959   2029  -3102       O  
ATOM   3396  N   ILE A 500      -3.420 -46.911  10.203  1.00215.95           N  
ANISOU 3396  N   ILE A 500    25393  31646  25011   1276   1718  -3494       N  
ATOM   3397  CA  ILE A 500      -2.901 -46.700   8.840  1.00214.71           C  
ANISOU 3397  CA  ILE A 500    25289  31780  24511   1426   1603  -3701       C  
ATOM   3398  C   ILE A 500      -1.509 -46.069   8.882  1.00213.20           C  
ANISOU 3398  C   ILE A 500    25329  31708  23969   1386   1733  -3474       C  
ATOM   3399  O   ILE A 500      -0.557 -46.611   8.297  1.00213.04           O  
ANISOU 3399  O   ILE A 500    25276  31783  23885   1417   1713  -3607       O  
ATOM   3400  CB  ILE A 500      -3.903 -45.850   8.001  1.00215.51           C  
ANISOU 3400  CB  ILE A 500    25433  32089  24360   1593   1477  -3802       C  
ATOM   3401  CG1 ILE A 500      -5.102 -46.724   7.637  1.00216.11           C  
ANISOU 3401  CG1 ILE A 500    25221  32079  24810   1668   1299  -4152       C  
ATOM   3402  CG2 ILE A 500      -3.281 -45.307   6.726  1.00216.20           C  
ANISOU 3402  CG2 ILE A 500    25643  32522  23981   1768   1415  -3887       C  
ATOM   3403  CD1 ILE A 500      -6.306 -45.974   7.126  1.00218.45           C  
ANISOU 3403  CD1 ILE A 500    25527  32507  24964   1808   1179  -4238       C  
ATOM   3404  N   LEU A 501      -1.423 -44.959   9.627  1.00212.94           N  
ANISOU 3404  N   LEU A 501    25504  31649  23752   1317   1861  -3146       N  
ATOM   3405  CA  LEU A 501      -0.193 -44.191   9.840  1.00208.04           C  
ANISOU 3405  CA  LEU A 501    25096  31096  22853   1264   1993  -2900       C  
ATOM   3406  C   LEU A 501       0.946 -44.974  10.492  1.00206.11           C  
ANISOU 3406  C   LEU A 501    24822  30712  22778   1141   2085  -2851       C  
ATOM   3407  O   LEU A 501       2.088 -44.863  10.047  1.00207.48           O  
ANISOU 3407  O   LEU A 501    25072  31001  22759   1149   2127  -2835       O  
ATOM   3408  CB  LEU A 501      -0.492 -42.954  10.690  1.00205.94           C  
ANISOU 3408  CB  LEU A 501    25007  30772  22468   1210   2088  -2601       C  
ATOM   3409  CG  LEU A 501       0.614 -41.914  10.725  1.00207.22           C  
ANISOU 3409  CG  LEU A 501    25374  31014  22343   1185   2197  -2372       C  
ATOM   3410  CD1 LEU A 501       0.649 -41.205   9.406  1.00211.74           C  
ANISOU 3410  CD1 LEU A 501    26021  31843  22587   1333   2149  -2406       C  
ATOM   3411  CD2 LEU A 501       0.420 -40.882  11.817  1.00208.60           C  
ANISOU 3411  CD2 LEU A 501    25685  31073  22500   1115   2281  -2111       C  
ATOM   3412  N   VAL A 502       0.629 -45.738  11.543  1.00211.15           N  
ANISOU 3412  N   VAL A 502    25345  31107  23772   1040   2125  -2811       N  
ATOM   3413  CA  VAL A 502       1.588 -46.634  12.229  1.00217.71           C  
ANISOU 3413  CA  VAL A 502    26120  31784  24813    938   2202  -2768       C  
ATOM   3414  C   VAL A 502       2.088 -47.701  11.273  1.00224.67           C  
ANISOU 3414  C   VAL A 502    26842  32721  25799    985   2105  -3064       C  
ATOM   3415  O   VAL A 502       3.278 -48.033  11.289  1.00230.56           O  
ANISOU 3415  O   VAL A 502    27617  33474  26509    944   2154  -3053       O  
ATOM   3416  CB  VAL A 502       1.002 -47.393  13.454  1.00217.01           C  
ANISOU 3416  CB  VAL A 502    25899  31430  25122    855   2266  -2665       C  
ATOM   3417  CG1 VAL A 502       2.026 -48.375  14.026  1.00213.23           C  
ANISOU 3417  CG1 VAL A 502    25354  30811  24851    777   2334  -2630       C  
ATOM   3418  CG2 VAL A 502       0.597 -46.431  14.557  1.00219.31           C  
ANISOU 3418  CG2 VAL A 502    26337  31676  25313    822   2372  -2373       C  
ATOM   3419  N   GLY A 503       1.175 -48.242  10.462  1.00219.65           N  
ANISOU 3419  N   GLY A 503    26027  32123  25306   1080   1957  -3349       N  
ATOM   3420  CA  GLY A 503       1.522 -49.205   9.411  1.00211.73           C  
ANISOU 3420  CA  GLY A 503    24851  31210  24386   1167   1825  -3698       C  
ATOM   3421  C   GLY A 503       2.350 -48.622   8.278  1.00199.26           C  
ANISOU 3421  C   GLY A 503    23401  29952  22355   1287   1800  -3770       C  
ATOM   3422  O   GLY A 503       3.134 -49.327   7.651  1.00192.94           O  
ANISOU 3422  O   GLY A 503    22513  29236  21557   1334   1752  -3974       O  
ATOM   3423  N   GLN A 504       2.132 -47.342   7.979  1.00188.73           N  
ANISOU 3423  N   GLN A 504    22261  28801  20646   1352   1836  -3603       N  
ATOM   3424  CA  GLN A 504       3.005 -46.630   7.046  1.00181.34           C  
ANISOU 3424  CA  GLN A 504    21469  28155  19273   1458   1871  -3563       C  
ATOM   3425  C   GLN A 504       4.366 -46.254   7.608  1.00180.78           C  
ANISOU 3425  C   GLN A 504    21549  28040  19098   1335   2042  -3304       C  
ATOM   3426  O   GLN A 504       5.335 -46.203   6.860  1.00178.91           O  
ANISOU 3426  O   GLN A 504    21347  27993  18636   1401   2074  -3340       O  
ATOM   3427  CB  GLN A 504       2.321 -45.382   6.527  1.00177.94           C  
ANISOU 3427  CB  GLN A 504    21182  27917  18510   1576   1861  -3444       C  
ATOM   3428  CG  GLN A 504       1.092 -45.700   5.691  1.00178.11           C  
ANISOU 3428  CG  GLN A 504    21054  28060  18557   1750   1667  -3748       C  
ATOM   3429  CD  GLN A 504       0.567 -44.500   4.957  1.00174.54           C  
ANISOU 3429  CD  GLN A 504    20744  27857  17714   1912   1648  -3647       C  
ATOM   3430  OE1 GLN A 504       1.238 -43.487   4.889  1.00166.84           O  
ANISOU 3430  OE1 GLN A 504    19964  26985  16442   1909   1784  -3362       O  
ATOM   3431  NE2 GLN A 504      -0.648 -44.591   4.428  1.00174.95           N  
ANISOU 3431  NE2 GLN A 504    20689  27989  17793   2056   1480  -3872       N  
ATOM   3432  N   ILE A 505       4.416 -45.918   8.895  1.00188.33           N  
ANISOU 3432  N   ILE A 505    22593  28767  20197   1179   2150  -3047       N  
ATOM   3433  CA  ILE A 505       5.682 -45.661   9.557  1.00197.46           C  
ANISOU 3433  CA  ILE A 505    23861  29849  21314   1064   2289  -2840       C  
ATOM   3434  C   ILE A 505       6.409 -46.988   9.547  1.00208.42           C  
ANISOU 3434  C   ILE A 505    25096  31161  22931   1028   2261  -3031       C  
ATOM   3435  O   ILE A 505       7.622 -47.029   9.359  1.00226.56           O  
ANISOU 3435  O   ILE A 505    27435  33521  25126   1007   2326  -3009       O  
ATOM   3436  CB  ILE A 505       5.516 -45.161  11.021  1.00198.12           C  
ANISOU 3436  CB  ILE A 505    24041  29711  21525    936   2382  -2574       C  
ATOM   3437  CG1 ILE A 505       5.042 -43.702  11.074  1.00197.23           C  
ANISOU 3437  CG1 ILE A 505    24094  29667  21176    965   2420  -2370       C  
ATOM   3438  CG2 ILE A 505       6.831 -45.234  11.761  1.00200.57           C  
ANISOU 3438  CG2 ILE A 505    24410  29924  21871    833   2487  -2442       C  
ATOM   3439  CD1 ILE A 505       4.622 -43.213  12.481  1.00193.51           C  
ANISOU 3439  CD1 ILE A 505    23692  29006  20826    878   2479  -2161       C  
ATOM   3440  N   ASP A 506       5.654 -48.061   9.796  1.00210.91           N  
ANISOU 3440  N   ASP A 506    25223  31319  23592   1015   2170  -3208       N  
ATOM   3441  CA  ASP A 506       6.199 -49.415   9.764  1.00216.34           C  
ANISOU 3441  CA  ASP A 506    25729  31902  24568    988   2124  -3413       C  
ATOM   3442  C   ASP A 506       6.916 -49.718   8.450  1.00227.18           C  
ANISOU 3442  C   ASP A 506    27048  33523  25745   1109   2052  -3669       C  
ATOM   3443  O   ASP A 506       8.082 -50.168   8.429  1.00238.69           O  
ANISOU 3443  O   ASP A 506    28494  34983  27211   1073   2096  -3698       O  
ATOM   3444  CB  ASP A 506       5.084 -50.447  10.028  1.00211.36           C  
ANISOU 3444  CB  ASP A 506    24867  31065  24373    981   2024  -3584       C  
ATOM   3445  CG  ASP A 506       5.630 -51.844  10.225  1.00209.65           C  
ANISOU 3445  CG  ASP A 506    24452  30669  24537    931   1993  -3743       C  
ATOM   3446  OD1 ASP A 506       6.861 -52.042  10.050  1.00211.35           O  
ANISOU 3446  OD1 ASP A 506    24708  30948  24644    915   2030  -3762       O  
ATOM   3447  OD2 ASP A 506       4.829 -52.739  10.570  1.00209.10           O  
ANISOU 3447  OD2 ASP A 506    24173  30377  24898    906   1938  -3841       O  
ATOM   3448  N   ASP A 507       6.214 -49.446   7.364  1.00226.30           N  
ANISOU 3448  N   ASP A 507    26904  33638  25439   1271   1941  -3853       N  
ATOM   3449  CA  ASP A 507       6.772 -49.593   6.028  1.00219.23           C  
ANISOU 3449  CA  ASP A 507    25968  33051  24278   1441   1873  -4089       C  
ATOM   3450  C   ASP A 507       7.991 -48.736   5.786  1.00218.82           C  
ANISOU 3450  C   ASP A 507    26105  33177  23859   1440   2029  -3863       C  
ATOM   3451  O   ASP A 507       8.978 -49.207   5.216  1.00222.82           O  
ANISOU 3451  O   ASP A 507    26559  33814  24286   1489   2038  -3994       O  
ATOM   3452  CB  ASP A 507       5.704 -49.247   5.009  1.00214.19           C  
ANISOU 3452  CB  ASP A 507    25292  32648  23441   1642   1736  -4274       C  
ATOM   3453  CG  ASP A 507       4.506 -50.151   5.117  1.00210.71           C  
ANISOU 3453  CG  ASP A 507    24622  32035  23403   1659   1563  -4553       C  
ATOM   3454  OD1 ASP A 507       4.639 -51.251   5.664  1.00206.87           O  
ANISOU 3454  OD1 ASP A 507    23962  31293  23342   1554   1533  -4674       O  
ATOM   3455  OD2 ASP A 507       3.418 -49.753   4.706  1.00208.13           O  
ANISOU 3455  OD2 ASP A 507    24278  31802  22999   1772   1465  -4636       O  
ATOM   3456  N   ALA A 508       7.932 -47.493   6.239  1.00220.80           N  
ANISOU 3456  N   ALA A 508    26555  33416  23920   1382   2153  -3528       N  
ATOM   3457  CA  ALA A 508       9.052 -46.582   6.076  1.00226.70           C  
ANISOU 3457  CA  ALA A 508    27465  34287  24382   1368   2314  -3284       C  
ATOM   3458  C   ALA A 508      10.273 -47.037   6.871  1.00226.67           C  
ANISOU 3458  C   ALA A 508    27458  34101  24562   1210   2408  -3211       C  
ATOM   3459  O   ALA A 508      11.404 -46.857   6.417  1.00228.50           O  
ANISOU 3459  O   ALA A 508    27725  34466  24626   1229   2500  -3168       O  
ATOM   3460  CB  ALA A 508       8.651 -45.188   6.503  1.00229.30           C  
ANISOU 3460  CB  ALA A 508    27978  34585  24558   1330   2408  -2961       C  
ATOM   3461  N   LEU A 509      10.046 -47.565   8.071  1.00228.43           N  
ANISOU 3461  N   LEU A 509    27643  34029  25117   1066   2396  -3173       N  
ATOM   3462  CA  LEU A 509      11.128 -48.079   8.905  1.00232.13           C  
ANISOU 3462  CA  LEU A 509    28101  34319  25776    935   2466  -3114       C  
ATOM   3463  C   LEU A 509      11.882 -49.231   8.246  1.00232.89           C  
ANISOU 3463  C   LEU A 509    28041  34485  25959    980   2407  -3389       C  
ATOM   3464  O   LEU A 509      13.096 -49.340   8.393  1.00239.68           O  
ANISOU 3464  O   LEU A 509    28922  35336  26808    926   2486  -3346       O  
ATOM   3465  CB  LEU A 509      10.638 -48.517  10.298  1.00232.50           C  
ANISOU 3465  CB  LEU A 509    28121  34063  26153    812   2464  -3014       C  
ATOM   3466  CG  LEU A 509      11.612 -48.922  11.417  1.00233.02           C  
ANISOU 3466  CG  LEU A 509    27984  33962  26589    809   2354  -3213       C  
ATOM   3467  CD1 LEU A 509      11.022 -48.515  12.753  1.00231.14           C  
ANISOU 3467  CD1 LEU A 509    27627  33616  26579    761   2348  -3334       C  
ATOM   3468  CD2 LEU A 509      12.018 -50.396  11.493  1.00227.87           C  
ANISOU 3468  CD2 LEU A 509    27322  33082  26175    741   2370  -3054       C  
ATOM   3469  N   LYS A 510      11.169 -50.111   7.546  1.00229.22           N  
ANISOU 3469  N   LYS A 510    27403  34080  25610   1085   2258  -3694       N  
ATOM   3470  CA  LYS A 510      11.852 -51.223   6.867  1.00228.09           C  
ANISOU 3470  CA  LYS A 510    27089  34011  25561   1149   2179  -4000       C  
ATOM   3471  C   LYS A 510      12.877 -50.713   5.836  1.00235.04           C  
ANISOU 3471  C   LYS A 510    28038  35212  26055   1258   2254  -4009       C  
ATOM   3472  O   LYS A 510      14.003 -51.242   5.748  1.00239.25           O  
ANISOU 3472  O   LYS A 510    28519  35757  26627   1235   2290  -4087       O  
ATOM   3473  CB  LYS A 510      10.865 -52.192   6.218  1.00219.92           C  
ANISOU 3473  CB  LYS A 510    25833  32995  24730   1267   1981  -4369       C  
ATOM   3474  CG  LYS A 510      11.453 -53.552   5.943  1.00213.71           C  
ANISOU 3474  CG  LYS A 510    24830  32150  24217   1288   1882  -4688       C  
ATOM   3475  CD  LYS A 510      11.796 -54.283   7.227  1.00205.23           C  
ANISOU 3475  CD  LYS A 510    23705  30705  23567   1100   1931  -4562       C  
ATOM   3476  CE  LYS A 510      12.446 -55.663   6.985  1.00201.59           C  
ANISOU 3476  CE  LYS A 510    23019  30156  23418   1115   1832  -4870       C  
ATOM   3477  NZ  LYS A 510      11.455 -56.588   6.360  1.00200.71           N  
ANISOU 3477  NZ  LYS A 510    22647  30009  23603   1224   1628  -5253       N  
ATOM   3478  N   LEU A 511      12.487 -49.683   5.083  1.00235.22           N  
ANISOU 3478  N   LEU A 511    28170  35487  25713   1383   2289  -3910       N  
ATOM   3479  CA  LEU A 511      13.385 -49.068   4.110  1.00229.43           C  
ANISOU 3479  CA  LEU A 511    27505  35068  24597   1503   2398  -3846       C  
ATOM   3480  C   LEU A 511      14.621 -48.541   4.820  1.00224.93           C  
ANISOU 3480  C   LEU A 511    27050  34370  24041   1341   2583  -3563       C  
ATOM   3481  O   LEU A 511      15.751 -48.719   4.350  1.00228.38           O  
ANISOU 3481  O   LEU A 511    27456  34939  24378   1372   2659  -3600       O  
ATOM   3482  CB  LEU A 511      12.738 -47.875   3.393  1.00224.08           C  
ANISOU 3482  CB  LEU A 511    26952  34636  23550   1647   2442  -3679       C  
ATOM   3483  CG  LEU A 511      11.599 -48.090   2.411  1.00219.81           C  
ANISOU 3483  CG  LEU A 511    26324  34330  22861   1872   2272  -3939       C  
ATOM   3484  CD1 LEU A 511      11.122 -46.768   1.857  1.00216.72           C  
ANISOU 3484  CD1 LEU A 511    26087  34157  22097   1998   2352  -3689       C  
ATOM   3485  CD2 LEU A 511      12.035 -49.090   1.333  1.00219.96           C  
ANISOU 3485  CD2 LEU A 511    26165  34614  22793   2066   2164  -4322       C  
ATOM   3486  N   ALA A 512      14.370 -47.912   5.971  1.00215.38           N  
ANISOU 3486  N   ALA A 512    25959  32904  22969   1181   2643  -3302       N  
ATOM   3487  CA  ALA A 512      15.429 -47.317   6.760  1.00210.06           C  
ANISOU 3487  CA  ALA A 512    25388  32086  22337   1035   2792  -3049       C  
ATOM   3488  C   ALA A 512      16.366 -48.392   7.297  1.00209.61           C  
ANISOU 3488  C   ALA A 512    25230  31873  22538    941   2774  -3187       C  
ATOM   3489  O   ALA A 512      17.582 -48.218   7.240  1.00211.47           O  
ANISOU 3489  O   ALA A 512    25481  32141  22726    905   2880  -3121       O  
ATOM   3490  CB  ALA A 512      14.852 -46.471   7.890  1.00206.65           C  
ANISOU 3490  CB  ALA A 512    25085  31433  22000    918   2826  -2794       C  
ATOM   3491  N   ASN A 513      15.812 -49.522   7.744  1.00206.23           N  
ANISOU 3491  N   ASN A 513    24681  31279  22396    913   2641  -3380       N  
ATOM   3492  CA  ASN A 513      16.618 -50.659   8.239  1.00201.16           C  
ANISOU 3492  CA  ASN A 513    23924  30474  22032    838   2609  -3519       C  
ATOM   3493  C   ASN A 513      17.433 -51.284   7.116  1.00204.21           C  
ANISOU 3493  C   ASN A 513    24191  31082  22315    945   2586  -3772       C  
ATOM   3494  O   ASN A 513      18.621 -51.595   7.311  1.00211.02           O  
ANISOU 3494  O   ASN A 513    25030  31905  23242    889   2645  -3781       O  
ATOM   3495  CB  ASN A 513      15.750 -51.763   8.857  1.00197.93           C  
ANISOU 3495  CB  ASN A 513    23382  29834  21988    803   2479  -3658       C  
ATOM   3496  CG  ASN A 513      15.286 -51.440  10.262  1.00193.20           C  
ANISOU 3496  CG  ASN A 513    22874  28976  21556    684   2525  -3399       C  
ATOM   3497  OD1 ASN A 513      16.092 -51.170  11.155  1.00184.87           O  
ANISOU 3497  OD1 ASN A 513    21904  27801  20534    594   2610  -3218       O  
ATOM   3498  ND2 ASN A 513      13.977 -51.491  10.472  1.00194.28           N  
ANISOU 3498  ND2 ASN A 513    22980  29034  21801    700   2461  -3394       N  
ATOM   3499  N   GLU A 514      16.807 -51.430   5.940  1.00206.00           N  
ANISOU 3499  N   GLU A 514    24341  31562  22366   1118   2499  -3984       N  
ATOM   3500  CA  GLU A 514      17.537 -51.927   4.754  1.00202.94           C  
ANISOU 3500  CA  GLU A 514    23841  31457  21810   1268   2479  -4237       C  
ATOM   3501  C   GLU A 514      18.591 -50.952   4.227  1.00192.60           C  
ANISOU 3501  C   GLU A 514    22643  30373  20160   1304   2670  -4026       C  
ATOM   3502  O   GLU A 514      19.566 -51.377   3.636  1.00186.31           O  
ANISOU 3502  O   GLU A 514    21764  29733  19290   1368   2704  -4163       O  
ATOM   3503  CB  GLU A 514      16.581 -52.319   3.630  1.00210.93           C  
ANISOU 3503  CB  GLU A 514    24732  32712  22697   1482   2320  -4543       C  
ATOM   3504  CG  GLU A 514      15.797 -53.574   3.990  1.00217.59           C  
ANISOU 3504  CG  GLU A 514    25384  33322  23967   1457   2120  -4837       C  
ATOM   3505  CD  GLU A 514      14.661 -53.930   3.055  1.00228.19           C  
ANISOU 3505  CD  GLU A 514    26590  34844  25268   1657   1931  -5159       C  
ATOM   3506  OE1 GLU A 514      14.821 -53.839   1.812  1.00233.46           O  
ANISOU 3506  OE1 GLU A 514    27215  35890  25598   1882   1892  -5354       O  
ATOM   3507  OE2 GLU A 514      13.595 -54.317   3.608  1.00235.70           O  
ANISOU 3507  OE2 GLU A 514    27463  35552  26538   1596   1822  -5215       O  
ATOM   3508  N   GLY A 515      18.406 -49.652   4.463  1.00187.34           N  
ANISOU 3508  N   GLY A 515    22149  29709  19320   1262   2801  -3690       N  
ATOM   3509  CA  GLY A 515      19.460 -48.652   4.139  1.00184.84           C  
ANISOU 3509  CA  GLY A 515    21926  29530  18775   1262   3011  -3433       C  
ATOM   3510  C   GLY A 515      19.029 -47.651   3.096  1.00183.08           C  
ANISOU 3510  C   GLY A 515    21776  29616  18169   1436   3096  -3283       C  
ATOM   3511  O   GLY A 515      19.788 -46.755   2.703  1.00180.95           O  
ANISOU 3511  O   GLY A 515    21568  29475  17710   1460   3289  -3036       O  
ATOM   3512  N   LYS A 516      17.792 -47.804   2.660  1.00185.67           N  
ANISOU 3512  N   LYS A 516    22085  30053  18405   1564   2955  -3425       N  
ATOM   3513  CA  LYS A 516      17.287 -47.077   1.534  1.00196.21           C  
ANISOU 3513  CA  LYS A 516    23466  31732  19353   1785   2995  -3350       C  
ATOM   3514  C   LYS A 516      16.741 -45.768   2.083  1.00191.77           C  
ANISOU 3514  C   LYS A 516    23072  31029  18762   1696   3090  -2984       C  
ATOM   3515  O   LYS A 516      15.542 -45.641   2.401  1.00199.29           O  
ANISOU 3515  O   LYS A 516    24061  31886  19771   1692   2971  -3006       O  
ATOM   3516  CB  LYS A 516      16.241 -47.931   0.822  1.00209.73           C  
ANISOU 3516  CB  LYS A 516    25055  33624  21008   1979   2769  -3729       C  
ATOM   3517  CG  LYS A 516      16.739 -49.314   0.373  1.00221.30           C  
ANISOU 3517  CG  LYS A 516    26324  35182  22578   2061   2641  -4143       C  
ATOM   3518  CD  LYS A 516      15.552 -50.255   0.233  1.00234.66           C  
ANISOU 3518  CD  LYS A 516    27871  36841  24447   2149   2376  -4528       C  
ATOM   3519  CE  LYS A 516      15.852 -51.537  -0.516  1.00243.94           C  
ANISOU 3519  CE  LYS A 516    28824  38184  25677   2309   2215  -4995       C  
ATOM   3520  NZ  LYS A 516      14.547 -52.131  -0.936  1.00249.04           N  
ANISOU 3520  NZ  LYS A 516    29329  38879  26413   2462   1961  -5353       N  
ATOM   3521  N   VAL A 517      17.640 -44.789   2.197  1.00189.89           N  
ANISOU 3521  N   VAL A 517    22919  30765  18463   1625   3304  -2655       N  
ATOM   3522  CA  VAL A 517      17.322 -43.491   2.814  1.00195.43           C  
ANISOU 3522  CA  VAL A 517    23765  31288  19202   1520   3403  -2302       C  
ATOM   3523  C   VAL A 517      16.352 -42.686   1.954  1.00201.02           C  
ANISOU 3523  C   VAL A 517    24541  32237  19600   1714   3411  -2174       C  
ATOM   3524  O   VAL A 517      15.365 -42.180   2.483  1.00203.13           O  
ANISOU 3524  O   VAL A 517    24889  32355  19935   1664   3341  -2089       O  
ATOM   3525  CB  VAL A 517      18.597 -42.665   3.129  1.00194.65           C  
ANISOU 3525  CB  VAL A 517    23702  31073  19181   1397   3624  -2007       C  
ATOM   3526  CG1 VAL A 517      18.269 -41.256   3.641  1.00189.34           C  
ANISOU 3526  CG1 VAL A 517    23152  30227  18559   1316   3719  -1661       C  
ATOM   3527  CG2 VAL A 517      19.448 -43.416   4.143  1.00196.17           C  
ANISOU 3527  CG2 VAL A 517    23839  30999  19698   1204   3588  -2140       C  
ATOM   3528  N   LYS A 518      16.625 -42.572   0.653  1.00207.60           N  
ANISOU 3528  N   LYS A 518    25340  33452  20085   1949   3497  -2156       N  
ATOM   3529  CA  LYS A 518      15.736 -41.837  -0.263  1.00218.28           C  
ANISOU 3529  CA  LYS A 518    26754  35082  21098   2179   3505  -2030       C  
ATOM   3530  C   LYS A 518      14.333 -42.461  -0.343  1.00221.61           C  
ANISOU 3530  C   LYS A 518    27145  35549  21505   2277   3244  -2343       C  
ATOM   3531  O   LYS A 518      13.347 -41.724  -0.318  1.00222.37           O  
ANISOU 3531  O   LYS A 518    27329  35633  21528   2321   3208  -2208       O  
ATOM   3532  CB  LYS A 518      16.352 -41.709  -1.663  1.00226.02           C  
ANISOU 3532  CB  LYS A 518    27689  36510  21677   2453   3651  -1962       C  
ATOM   3533  CG  LYS A 518      17.531 -40.749  -1.706  1.00223.99           C  
ANISOU 3533  CG  LYS A 518    27466  36217  21419   2385   3951  -1547       C  
ATOM   3534  CD  LYS A 518      18.330 -40.797  -3.007  1.00226.34           C  
ANISOU 3534  CD  LYS A 518    27691  36953  21353   2645   4126  -1480       C  
ATOM   3535  CE  LYS A 518      19.832 -40.686  -2.728  1.00224.78           C  
ANISOU 3535  CE  LYS A 518    27437  36621  21345   2486   4348  -1310       C  
ATOM   3536  NZ  LYS A 518      20.642 -40.107  -3.839  1.00227.53           N  
ANISOU 3536  NZ  LYS A 518    27747  37315  21387   2698   4634  -1008       N  
ATOM   3537  N   GLU A 519      14.265 -43.799  -0.410  1.00219.88           N  
ANISOU 3537  N   GLU A 519    26788  35357  21398   2304   3064  -2758       N  
ATOM   3538  CA  GLU A 519      12.984 -44.572  -0.367  1.00213.95           C  
ANISOU 3538  CA  GLU A 519    25958  34578  20753   2365   2801  -3106       C  
ATOM   3539  C   GLU A 519      12.220 -44.331   0.933  1.00208.69           C  
ANISOU 3539  C   GLU A 519    25361  33508  20424   2127   2743  -3005       C  
ATOM   3540  O   GLU A 519      11.019 -44.010   0.897  1.00198.78           O  
ANISOU 3540  O   GLU A 519    24136  32258  19130   2193   2637  -3022       O  
ATOM   3541  CB  GLU A 519      13.218 -46.086  -0.554  1.00210.11           C  
ANISOU 3541  CB  GLU A 519    25280  34121  20430   2401   2633  -3560       C  
ATOM   3542  CG  GLU A 519      13.814 -46.451  -1.917  1.00210.28           C  
ANISOU 3542  CG  GLU A 519    25207  34595  20094   2688   2645  -3745       C  
ATOM   3543  CD  GLU A 519      13.481 -47.873  -2.360  1.00208.85           C  
ANISOU 3543  CD  GLU A 519    24812  34510  20031   2821   2391  -4288       C  
ATOM   3544  OE1 GLU A 519      14.428 -48.645  -2.644  1.00206.02           O  
ANISOU 3544  OE1 GLU A 519    24340  34239  19698   2850   2398  -4482       O  
ATOM   3545  OE2 GLU A 519      12.286 -48.216  -2.461  1.00208.37           O  
ANISOU 3545  OE2 GLU A 519    24680  34439  20052   2907   2178  -4537       O  
ATOM   3546  N   ALA A 520      12.944 -44.469   2.059  1.00206.81           N  
ANISOU 3546  N   ALA A 520    25142  32942  20493   1871   2817  -2900       N  
ATOM   3547  CA  ALA A 520      12.381 -44.151   3.375  1.00200.01           C  
ANISOU 3547  CA  ALA A 520    24355  31719  19920   1658   2795  -2762       C  
ATOM   3548  C   ALA A 520      11.845 -42.695   3.471  1.00199.74           C  
ANISOU 3548  C   ALA A 520    24478  31675  19739   1665   2886  -2426       C  
ATOM   3549  O   ALA A 520      10.703 -42.443   3.928  1.00210.90           O  
ANISOU 3549  O   ALA A 520    25927  32970  21234   1642   2790  -2419       O  
ATOM   3550  CB  ALA A 520      13.423 -44.391   4.450  1.00196.77           C  
ANISOU 3550  CB  ALA A 520    23950  31028  19785   1434   2879  -2677       C  
ATOM   3551  N   GLN A 521      12.655 -41.741   3.022  1.00195.64           N  
ANISOU 3551  N   GLN A 521    24036  31273  19025   1702   3074  -2146       N  
ATOM   3552  CA  GLN A 521      12.275 -40.323   2.982  1.00196.85           C  
ANISOU 3552  CA  GLN A 521    24318  31421  19053   1725   3176  -1809       C  
ATOM   3553  C   GLN A 521      11.096 -40.037   2.052  1.00203.73           C  
ANISOU 3553  C   GLN A 521    25209  32555  19644   1957   3084  -1850       C  
ATOM   3554  O   GLN A 521      10.278 -39.151   2.326  1.00211.30           O  
ANISOU 3554  O   GLN A 521    26259  33427  20597   1950   3074  -1676       O  
ATOM   3555  CB  GLN A 521      13.437 -39.501   2.485  1.00196.15           C  
ANISOU 3555  CB  GLN A 521    24264  31432  18833   1750   3408  -1513       C  
ATOM   3556  CG  GLN A 521      14.470 -39.166   3.527  1.00193.03           C  
ANISOU 3556  CG  GLN A 521    23885  30725  18732   1514   3523  -1355       C  
ATOM   3557  CD  GLN A 521      15.686 -38.546   2.883  1.00197.18           C  
ANISOU 3557  CD  GLN A 521    24396  31366  19156   1554   3755  -1107       C  
ATOM   3558  OE1 GLN A 521      16.163 -39.048   1.859  1.00207.16           O  
ANISOU 3558  OE1 GLN A 521    25590  32928  20190   1713   3809  -1188       O  
ATOM   3559  NE2 GLN A 521      16.188 -37.460   3.450  1.00191.82           N  
ANISOU 3559  NE2 GLN A 521    23763  30460  18658   1424   3893   -812       N  
ATOM   3560  N   ALA A 522      11.039 -40.779   0.947  1.00205.16           N  
ANISOU 3560  N   ALA A 522    25296  33065  19588   2178   3009  -2097       N  
ATOM   3561  CA  ALA A 522       9.918 -40.735   0.012  1.00204.89           C  
ANISOU 3561  CA  ALA A 522    25250  33316  19282   2438   2876  -2230       C  
ATOM   3562  C   ALA A 522       8.636 -41.267   0.667  1.00208.13           C  
ANISOU 3562  C   ALA A 522    25615  33528  19936   2367   2653  -2480       C  
ATOM   3563  O   ALA A 522       7.578 -40.623   0.611  1.00211.23           O  
ANISOU 3563  O   ALA A 522    26069  33936  20252   2439   2590  -2407       O  
ATOM   3564  CB  ALA A 522      10.254 -41.543  -1.220  1.00202.98           C  
ANISOU 3564  CB  ALA A 522    24891  33469  18763   2697   2824  -2500       C  
ATOM   3565  N   ALA A 523       8.759 -42.418   1.336  1.00208.24           N  
ANISOU 3565  N   ALA A 523    25514  33335  20271   2219   2550  -2749       N  
ATOM   3566  CA  ALA A 523       7.667 -42.997   2.151  1.00203.34           C  
ANISOU 3566  CA  ALA A 523    24827  32460  19971   2110   2378  -2944       C  
ATOM   3567  C   ALA A 523       7.171 -42.048   3.243  1.00201.04           C  
ANISOU 3567  C   ALA A 523    24668  31889  19828   1934   2442  -2651       C  
ATOM   3568  O   ALA A 523       5.973 -41.984   3.510  1.00194.84           O  
ANISOU 3568  O   ALA A 523    23870  31024  19134   1945   2325  -2720       O  
ATOM   3569  CB  ALA A 523       8.102 -44.304   2.791  1.00197.14           C  
ANISOU 3569  CB  ALA A 523    23901  31463  19537   1962   2312  -3188       C  
ATOM   3570  N   ALA A 524       8.109 -41.338   3.881  1.00205.99           N  
ANISOU 3570  N   ALA A 524    25403  32365  20497   1779   2619  -2350       N  
ATOM   3571  CA  ALA A 524       7.747 -40.324   4.897  1.00208.32           C  
ANISOU 3571  CA  ALA A 524    25820  32414  20916   1634   2679  -2079       C  
ATOM   3572  C   ALA A 524       6.894 -39.144   4.374  1.00209.02           C  
ANISOU 3572  C   ALA A 524    26008  32630  20777   1769   2684  -1895       C  
ATOM   3573  O   ALA A 524       6.033 -38.618   5.109  1.00206.66           O  
ANISOU 3573  O   ALA A 524    25764  32156  20601   1698   2640  -1813       O  
ATOM   3574  CB  ALA A 524       9.010 -39.806   5.571  1.00211.11           C  
ANISOU 3574  CB  ALA A 524    26241  32602  21369   1472   2849  -1840       C  
ATOM   3575  N   GLU A 525       7.104 -38.750   3.111  1.00214.60           N  
ANISOU 3575  N   GLU A 525    26733  33653  21149   1979   2736  -1829       N  
ATOM   3576  CA  GLU A 525       6.298 -37.682   2.504  1.00218.55           C  
ANISOU 3576  CA  GLU A 525    27322  34304  21412   2142   2739  -1649       C  
ATOM   3577  C   GLU A 525       4.820 -38.105   2.395  1.00219.68           C  
ANISOU 3577  C   GLU A 525    27410  34491  21567   2243   2522  -1911       C  
ATOM   3578  O   GLU A 525       3.934 -37.243   2.509  1.00221.97           O  
ANISOU 3578  O   GLU A 525    27777  34744  21817   2278   2494  -1773       O  
ATOM   3579  CB  GLU A 525       6.816 -37.284   1.105  1.00222.04           C  
ANISOU 3579  CB  GLU A 525    27781  35120  21461   2392   2846  -1520       C  
ATOM   3580  CG  GLU A 525       8.280 -36.775   0.969  1.00221.10           C  
ANISOU 3580  CG  GLU A 525    27696  35005  21304   2335   3090  -1227       C  
ATOM   3581  CD  GLU A 525       8.787 -35.906   2.102  1.00222.41           C  
ANISOU 3581  CD  GLU A 525    27937  34805  21762   2083   3218   -944       C  
ATOM   3582  OE1 GLU A 525       8.061 -35.052   2.680  1.00225.18           O  
ANISOU 3582  OE1 GLU A 525    28365  34974  22219   2021   3192   -794       O  
ATOM   3583  OE2 GLU A 525       9.986 -36.074   2.377  1.00217.63           O  
ANISOU 3583  OE2 GLU A 525    27301  34106  21280   1960   3342   -884       O  
ATOM   3584  N   GLN A 526       4.558 -39.414   2.232  1.00219.34           N  
ANISOU 3584  N   GLN A 526    27218  34495  21624   2278   2367  -2291       N  
ATOM   3585  CA  GLN A 526       3.179 -39.955   2.254  1.00222.50           C  
ANISOU 3585  CA  GLN A 526    27521  34876  22141   2343   2154  -2578       C  
ATOM   3586  C   GLN A 526       2.484 -39.936   3.622  1.00216.59           C  
ANISOU 3586  C   GLN A 526    26778  33762  21753   2119   2125  -2538       C  
ATOM   3587  O   GLN A 526       1.268 -39.929   3.689  1.00212.79           O  
ANISOU 3587  O   GLN A 526    26255  33251  21343   2170   1995  -2655       O  
ATOM   3588  CB  GLN A 526       3.112 -41.380   1.679  1.00225.81           C  
ANISOU 3588  CB  GLN A 526    27745  35422  22629   2449   1990  -3016       C  
ATOM   3589  CG  GLN A 526       3.405 -41.486   0.182  1.00227.79           C  
ANISOU 3589  CG  GLN A 526    27959  36111  22480   2756   1952  -3155       C  
ATOM   3590  CD  GLN A 526       2.452 -40.682  -0.718  1.00228.26           C  
ANISOU 3590  CD  GLN A 526    28075  36452  22199   3026   1876  -3118       C  
ATOM   3591  OE1 GLN A 526       1.217 -40.762  -0.597  1.00218.05           O  
ANISOU 3591  OE1 GLN A 526    26726  35098  21022   3067   1707  -3291       O  
ATOM   3592  NE2 GLN A 526       3.032 -39.904  -1.642  1.00230.64           N  
ANISOU 3592  NE2 GLN A 526    28480  37069  22082   3225   2009  -2880       N  
ATOM   3593  N   LEU A 527       3.242 -39.893   4.704  1.00210.04           N  
ANISOU 3593  N   LEU A 527    25995  32673  21138   1892   2247  -2370       N  
ATOM   3594  CA  LEU A 527       2.671 -39.735   6.039  1.00208.38           C  
ANISOU 3594  CA  LEU A 527    25806  32154  21214   1709   2246  -2284       C  
ATOM   3595  C   LEU A 527       2.022 -38.357   6.199  1.00204.54           C  
ANISOU 3595  C   LEU A 527    25456  31650  20609   1735   2278  -2035       C  
ATOM   3596  O   LEU A 527       0.989 -38.210   6.892  1.00214.93           O  
ANISOU 3596  O   LEU A 527    26762  32818  22081   1687   2212  -2048       O  
ATOM   3597  CB  LEU A 527       3.774 -39.909   7.091  1.00215.98           C  
ANISOU 3597  CB  LEU A 527    26797  32893  22371   1504   2371  -2153       C  
ATOM   3598  CG  LEU A 527       4.537 -41.245   7.093  1.00217.25           C  
ANISOU 3598  CG  LEU A 527    26829  33028  22685   1454   2354  -2365       C  
ATOM   3599  CD1 LEU A 527       5.701 -41.207   8.071  1.00212.31           C  
ANISOU 3599  CD1 LEU A 527    26256  32211  22198   1277   2484  -2201       C  
ATOM   3600  CD2 LEU A 527       3.596 -42.389   7.408  1.00218.79           C  
ANISOU 3600  CD2 LEU A 527    26859  33108  23162   1439   2215  -2630       C  
ATOM   3601  N   LYS A 528       2.629 -37.351   5.564  1.00201.39           N  
ANISOU 3601  N   LYS A 528    25171  31393  19955   1815   2388  -1800       N  
ATOM   3602  CA  LYS A 528       2.036 -36.004   5.497  1.00205.13           C  
ANISOU 3602  CA  LYS A 528    25762  31873  20304   1875   2414  -1560       C  
ATOM   3603  C   LYS A 528       0.617 -36.000   4.930  1.00213.69           C  
ANISOU 3603  C   LYS A 528    26810  33095  21286   2044   2252  -1717       C  
ATOM   3604  O   LYS A 528      -0.233 -35.356   5.487  1.00215.33           O  
ANISOU 3604  O   LYS A 528    27064  33175  21577   2010   2216  -1636       O  
ATOM   3605  CB  LYS A 528       2.898 -35.035   4.685  1.00206.66           C  
ANISOU 3605  CB  LYS A 528    26050  32223  20249   1970   2565  -1279       C  
ATOM   3606  CG  LYS A 528       4.205 -34.657   5.354  1.00206.49           C  
ANISOU 3606  CG  LYS A 528    26071  32014  20372   1794   2733  -1069       C  
ATOM   3607  CD  LYS A 528       5.028 -33.713   4.498  1.00208.68           C  
ANISOU 3607  CD  LYS A 528    26410  32431  20448   1892   2902   -773       C  
ATOM   3608  CE  LYS A 528       6.219 -33.194   5.276  1.00204.48           C  
ANISOU 3608  CE  LYS A 528    25900  31657  20132   1704   3055   -569       C  
ATOM   3609  NZ  LYS A 528       7.115 -32.374   4.435  1.00207.05           N  
ANISOU 3609  NZ  LYS A 528    26251  32096  20319   1788   3244   -271       N  
ATOM   3610  N   THR A 529       0.346 -36.760   3.867  1.00221.10           N  
ANISOU 3610  N   THR A 529    27652  34291  22062   2232   2141  -1972       N  
ATOM   3611  CA  THR A 529      -1.016 -36.802   3.275  1.00227.60           C  
ANISOU 3611  CA  THR A 529    28419  35259  22796   2417   1961  -2168       C  
ATOM   3612  C   THR A 529      -1.999 -37.583   4.167  1.00225.44           C  
ANISOU 3612  C   THR A 529    28021  34752  22883   2292   1832  -2406       C  
ATOM   3613  O   THR A 529      -3.132 -37.141   4.416  1.00223.08           O  
ANISOU 3613  O   THR A 529    27726  34392  22642   2317   1750  -2411       O  
ATOM   3614  CB  THR A 529      -1.046 -37.403   1.851  1.00232.55           C  
ANISOU 3614  CB  THR A 529    28958  36256  23142   2694   1851  -2421       C  
ATOM   3615  OG1 THR A 529       0.080 -36.950   1.103  1.00244.35           O  
ANISOU 3615  OG1 THR A 529    30538  37965  24336   2794   2006  -2205       O  
ATOM   3616  CG2 THR A 529      -2.308 -36.981   1.092  1.00234.88           C  
ANISOU 3616  CG2 THR A 529    29247  36755  23241   2938   1693  -2523       C  
ATOM   3617  N   THR A 530      -1.538 -38.748   4.633  1.00222.34           N  
ANISOU 3617  N   THR A 530    27507  34228  22742   2163   1826  -2587       N  
ATOM   3618  CA  THR A 530      -2.286 -39.609   5.557  1.00215.10           C  
ANISOU 3618  CA  THR A 530    26448  33059  22218   2028   1748  -2767       C  
ATOM   3619  C   THR A 530      -2.695 -38.811   6.807  1.00216.62           C  
ANISOU 3619  C   THR A 530    26740  33006  22558   1867   1833  -2512       C  
ATOM   3620  O   THR A 530      -3.827 -38.933   7.276  1.00215.60           O  
ANISOU 3620  O   THR A 530    26533  32760  22621   1850   1755  -2597       O  
ATOM   3621  CB  THR A 530      -1.431 -40.840   5.943  1.00207.80           C  
ANISOU 3621  CB  THR A 530    25407  32012  21535   1901   1780  -2903       C  
ATOM   3622  OG1 THR A 530      -0.908 -41.448   4.770  1.00202.64           O  
ANISOU 3622  OG1 THR A 530    24677  31608  20708   2061   1712  -3125       O  
ATOM   3623  CG2 THR A 530      -2.207 -41.904   6.689  1.00203.94           C  
ANISOU 3623  CG2 THR A 530    24728  31287  21472   1800   1700  -3103       C  
ATOM   3624  N   ARG A 531      -1.774 -37.976   7.301  1.00219.95           N  
ANISOU 3624  N   ARG A 531    27318  33362  22891   1768   1988  -2215       N  
ATOM   3625  CA  ARG A 531      -2.018 -37.072   8.440  1.00221.05           C  
ANISOU 3625  CA  ARG A 531    27559  33299  23129   1646   2063  -1980       C  
ATOM   3626  C   ARG A 531      -3.080 -35.999   8.130  1.00216.05           C  
ANISOU 3626  C   ARG A 531    26996  32734  22357   1761   2000  -1900       C  
ATOM   3627  O   ARG A 531      -3.995 -35.762   8.948  1.00215.36           O  
ANISOU 3627  O   ARG A 531    26894  32501  22430   1708   1968  -1886       O  
ATOM   3628  CB  ARG A 531      -0.686 -36.421   8.871  1.00227.46           C  
ANISOU 3628  CB  ARG A 531    28497  34041  23887   1542   2219  -1728       C  
ATOM   3629  CG  ARG A 531      -0.737 -35.476  10.081  1.00231.31           C  
ANISOU 3629  CG  ARG A 531    29078  34325  24483   1429   2286  -1515       C  
ATOM   3630  CD  ARG A 531       0.459 -34.526  10.126  1.00231.47           C  
ANISOU 3630  CD  ARG A 531    29212  34315  24418   1385   2410  -1278       C  
ATOM   3631  NE  ARG A 531       0.451 -33.615   8.976  1.00230.54           N  
ANISOU 3631  NE  ARG A 531    29167  34369  24058   1524   2427  -1147       N  
ATOM   3632  CZ  ARG A 531       1.516 -32.996   8.461  1.00227.44           C  
ANISOU 3632  CZ  ARG A 531    28834  34027  23555   1538   2545   -958       C  
ATOM   3633  NH1 ARG A 531       2.728 -33.158   8.983  1.00227.06           N  
ANISOU 3633  NH1 ARG A 531    28784  33865  23624   1412   2645   -902       N  
ATOM   3634  NH2 ARG A 531       1.363 -32.197   7.405  1.00223.71           N  
ANISOU 3634  NH2 ARG A 531    28415  33721  22860   1691   2570   -811       N  
ATOM   3635  N   ASN A 532      -2.985 -35.384   6.947  1.00210.24           N  
ANISOU 3635  N   ASN A 532    26327  32230  21323   1933   1984  -1845       N  
ATOM   3636  CA  ASN A 532      -3.929 -34.320   6.541  1.00201.40           C  
ANISOU 3636  CA  ASN A 532    25281  31194  20048   2068   1925  -1748       C  
ATOM   3637  C   ASN A 532      -5.343 -34.850   6.272  1.00196.75           C  
ANISOU 3637  C   ASN A 532    24566  30659  19528   2174   1744  -2024       C  
ATOM   3638  O   ASN A 532      -6.344 -34.231   6.665  1.00181.44           O  
ANISOU 3638  O   ASN A 532    22647  28641  17648   2183   1691  -1984       O  
ATOM   3639  CB  ASN A 532      -3.435 -33.585   5.292  1.00193.93           C  
ANISOU 3639  CB  ASN A 532    24427  30503  18751   2255   1969  -1591       C  
ATOM   3640  CG  ASN A 532      -2.060 -32.940   5.469  1.00187.61           C  
ANISOU 3640  CG  ASN A 532    23731  29639  17912   2159   2160  -1295       C  
ATOM   3641  OD1 ASN A 532      -1.705 -32.439   6.539  1.00185.01           O  
ANISOU 3641  OD1 ASN A 532    23453  29064  17778   1983   2243  -1138       O  
ATOM   3642  ND2 ASN A 532      -1.276 -32.959   4.403  1.00185.29           N  
ANISOU 3642  ND2 ASN A 532    23455  29577  17370   2292   2228  -1231       N  
ATOM   3643  N   ALA A 533      -5.404 -36.018   5.630  1.00197.24           N  
ANISOU 3643  N   ALA A 533    24483  30843  19614   2254   1643  -2323       N  
ATOM   3644  CA  ALA A 533      -6.683 -36.639   5.294  1.00193.74           C  
ANISOU 3644  CA  ALA A 533    23880  30446  19286   2364   1454  -2636       C  
ATOM   3645  C   ALA A 533      -7.513 -37.160   6.492  1.00193.07           C  
ANISOU 3645  C   ALA A 533    23673  30074  19607   2195   1435  -2721       C  
ATOM   3646  O   ALA A 533      -8.733 -37.208   6.399  1.00189.69           O  
ANISOU 3646  O   ALA A 533    23147  29641  19284   2270   1307  -2883       O  
ATOM   3647  CB  ALA A 533      -6.444 -37.744   4.293  1.00193.39           C  
ANISOU 3647  CB  ALA A 533    23689  30597  19190   2504   1341  -2959       C  
ATOM   3648  N   TYR A 534      -6.874 -37.564   7.594  1.00194.90           N  
ANISOU 3648  N   TYR A 534    23900  30082  20067   1984   1565  -2609       N  
ATOM   3649  CA  TYR A 534      -7.617 -38.006   8.795  1.00204.94           C  
ANISOU 3649  CA  TYR A 534    25064  31101  21702   1842   1585  -2627       C  
ATOM   3650  C   TYR A 534      -7.311 -37.204  10.067  1.00219.68           C  
ANISOU 3650  C   TYR A 534    27068  32797  23600   1695   1736  -2321       C  
ATOM   3651  O   TYR A 534      -8.179 -36.535  10.644  1.00228.56           O  
ANISOU 3651  O   TYR A 534    28220  33850  24772   1691   1731  -2237       O  
ATOM   3652  CB  TYR A 534      -7.345 -39.489   9.102  1.00201.72           C  
ANISOU 3652  CB  TYR A 534    24462  30562  21617   1748   1588  -2813       C  
ATOM   3653  CG  TYR A 534      -7.399 -40.422   7.934  1.00202.66           C  
ANISOU 3653  CG  TYR A 534    24422  30830  21750   1881   1437  -3151       C  
ATOM   3654  CD1 TYR A 534      -8.612 -40.783   7.390  1.00205.26           C  
ANISOU 3654  CD1 TYR A 534    24577  31198  22214   2005   1263  -3433       C  
ATOM   3655  CD2 TYR A 534      -6.235 -40.973   7.383  1.00205.50           C  
ANISOU 3655  CD2 TYR A 534    24783  31292  22004   1895   1458  -3218       C  
ATOM   3656  CE1 TYR A 534      -8.686 -41.652   6.312  1.00207.86           C  
ANISOU 3656  CE1 TYR A 534    24735  31672  22568   2155   1095  -3795       C  
ATOM   3657  CE2 TYR A 534      -6.293 -41.826   6.299  1.00207.57           C  
ANISOU 3657  CE2 TYR A 534    24885  31712  22268   2044   1303  -3562       C  
ATOM   3658  CZ  TYR A 534      -7.525 -42.170   5.763  1.00208.13           C  
ANISOU 3658  CZ  TYR A 534    24779  31826  22474   2180   1113  -3863       C  
ATOM   3659  OH  TYR A 534      -7.618 -43.033   4.692  1.00204.70           O  
ANISOU 3659  OH  TYR A 534    24161  31554  22060   2353    930  -4256       O  
ATOM   3660  N   ILE A 535      -6.049 -37.234  10.480  1.00228.25           N  
ANISOU 3660  N   ILE A 535    28239  33835  24650   1592   1860  -2173       N  
ATOM   3661  CA  ILE A 535      -5.687 -36.813  11.823  1.00229.04           C  
ANISOU 3661  CA  ILE A 535    28418  33760  24846   1457   1985  -1955       C  
ATOM   3662  C   ILE A 535      -5.857 -35.289  11.951  1.00232.40           C  
ANISOU 3662  C   ILE A 535    29007  34206  25086   1495   2001  -1755       C  
ATOM   3663  O   ILE A 535      -6.221 -34.813  13.024  1.00242.83           O  
ANISOU 3663  O   ILE A 535    30356  35403  26504   1439   2043  -1645       O  
ATOM   3664  CB  ILE A 535      -4.200 -37.167  12.148  1.00227.43           C  
ANISOU 3664  CB  ILE A 535    28262  33512  24637   1356   2096  -1866       C  
ATOM   3665  CG1 ILE A 535      -3.742 -38.541  11.623  1.00232.57           C  
ANISOU 3665  CG1 ILE A 535    28775  34190  25401   1347   2068  -2068       C  
ATOM   3666  CG2 ILE A 535      -3.838 -36.967  13.620  1.00225.26           C  
ANISOU 3666  CG2 ILE A 535    28034  33065  24488   1239   2205  -1694       C  
ATOM   3667  CD1 ILE A 535      -4.483 -39.733  12.118  1.00233.80           C  
ANISOU 3667  CD1 ILE A 535    28733  34209  25891   1304   2037  -2222       C  
ATOM   3668  N   GLN A 536      -5.627 -34.530  10.869  1.00224.88           N  
ANISOU 3668  N   GLN A 536    28150  33414  23877   1605   1968  -1704       N  
ATOM   3669  CA  GLN A 536      -5.811 -33.075  10.914  1.00216.55           C  
ANISOU 3669  CA  GLN A 536    27232  32358  22688   1649   1980  -1505       C  
ATOM   3670  C   GLN A 536      -7.250 -32.649  11.242  1.00210.03           C  
ANISOU 3670  C   GLN A 536    26374  31494  21932   1701   1892  -1550       C  
ATOM   3671  O   GLN A 536      -7.449 -31.840  12.141  1.00198.54           O  
ANISOU 3671  O   GLN A 536    24979  29920  20537   1653   1926  -1419       O  
ATOM   3672  CB  GLN A 536      -5.339 -32.444   9.608  1.00224.65           C  
ANISOU 3672  CB  GLN A 536    28345  33573  23439   1780   1978  -1417       C  
ATOM   3673  CG  GLN A 536      -5.047 -30.965   9.645  1.00231.16           C  
ANISOU 3673  CG  GLN A 536    29307  34355  24165   1798   2039  -1149       C  
ATOM   3674  CD  GLN A 536      -4.736 -30.361   8.266  1.00243.19           C  
ANISOU 3674  CD  GLN A 536    30900  36085  25414   1963   2053  -1026       C  
ATOM   3675  OE1 GLN A 536      -4.426 -31.064   7.299  1.00242.76           O  
ANISOU 3675  OE1 GLN A 536    30805  36226  25204   2059   2038  -1131       O  
ATOM   3676  NE2 GLN A 536      -4.828 -29.040   8.179  1.00246.93           N  
ANISOU 3676  NE2 GLN A 536    31469  36518  25833   2011   2083   -795       N  
ATOM   3677  N   LYS A 537      -8.210 -33.241  10.523  1.00211.85           N  
ANISOU 3677  N   LYS A 537    26493  31828  22170   1804   1772  -1761       N  
ATOM   3678  CA  LYS A 537      -9.678 -33.083  10.691  1.00207.48           C  
ANISOU 3678  CA  LYS A 537    25864  31251  21716   1865   1670  -1865       C  
ATOM   3679  C   LYS A 537     -10.152 -33.260  12.129  1.00206.81           C  
ANISOU 3679  C   LYS A 537    25718  30970  21888   1741   1733  -1830       C  
ATOM   3680  O   LYS A 537     -10.942 -32.452  12.634  1.00207.22           O  
ANISOU 3680  O   LYS A 537    25801  30974  21959   1763   1714  -1764       O  
ATOM   3681  CB  LYS A 537     -10.401 -34.049   9.739  1.00206.47           C  
ANISOU 3681  CB  LYS A 537    25576  31245  21627   1978   1530  -2159       C  
ATOM   3682  CG  LYS A 537     -10.299 -33.615   8.287  1.00204.72           C  
ANISOU 3682  CG  LYS A 537    25421  31274  21087   2176   1438  -2195       C  
ATOM   3683  CD  LYS A 537     -10.994 -34.558   7.326  1.00202.86           C  
ANISOU 3683  CD  LYS A 537    25014  31186  20878   2323   1269  -2534       C  
ATOM   3684  CE  LYS A 537     -10.728 -34.075   5.906  1.00208.08           C  
ANISOU 3684  CE  LYS A 537    25762  32144  21154   2553   1197  -2536       C  
ATOM   3685  NZ  LYS A 537     -11.613 -34.640   4.849  1.00215.87           N  
ANISOU 3685  NZ  LYS A 537    26603  33331  22087   2774    987  -2877       N  
ATOM   3686  N   TYR A 538      -9.632 -34.292  12.791  1.00209.37           N  
ANISOU 3686  N   TYR A 538    25957  31195  22399   1626   1816  -1861       N  
ATOM   3687  CA  TYR A 538      -9.938 -34.581  14.202  1.00211.24           C  
ANISOU 3687  CA  TYR A 538    26129  31270  22859   1527   1907  -1793       C  
ATOM   3688  C   TYR A 538      -9.211 -33.677  15.209  1.00197.77           C  
ANISOU 3688  C   TYR A 538    24570  29499  21073   1471   2006  -1575       C  
ATOM   3689  O   TYR A 538      -9.789 -33.280  16.221  1.00182.08           O  
ANISOU 3689  O   TYR A 538    22575  27443  19161   1465   2041  -1506       O  
ATOM   3690  CB  TYR A 538      -9.665 -36.063  14.504  1.00218.85           C  
ANISOU 3690  CB  TYR A 538    26934  32151  24067   1447   1962  -1889       C  
ATOM   3691  CG  TYR A 538     -10.638 -36.980  13.781  1.00227.59           C  
ANISOU 3691  CG  TYR A 538    27839  33269  25365   1501   1853  -2138       C  
ATOM   3692  CD1 TYR A 538     -12.011 -36.943  14.090  1.00229.83           C  
ANISOU 3692  CD1 TYR A 538    28002  33496  25826   1536   1812  -2202       C  
ATOM   3693  CD2 TYR A 538     -10.218 -37.849  12.766  1.00228.01           C  
ANISOU 3693  CD2 TYR A 538    27807  33392  25432   1533   1777  -2334       C  
ATOM   3694  CE1 TYR A 538     -12.937 -37.755  13.435  1.00225.39           C  
ANISOU 3694  CE1 TYR A 538    27228  32925  25485   1590   1697  -2457       C  
ATOM   3695  CE2 TYR A 538     -11.145 -38.666  12.108  1.00227.36           C  
ANISOU 3695  CE2 TYR A 538    27514  33313  25558   1601   1649  -2608       C  
ATOM   3696  CZ  TYR A 538     -12.505 -38.608  12.452  1.00221.77           C  
ANISOU 3696  CZ  TYR A 538    26679  32527  25056   1625   1608  -2670       C  
ATOM   3697  OH  TYR A 538     -13.474 -39.362  11.841  1.00202.26           O  
ANISOU 3697  OH  TYR A 538    23976  30037  22834   1695   1472  -2958       O  
ATOM   3698  N   LEU A 539      -7.972 -33.295  14.904  1.00189.46           N  
ANISOU 3698  N   LEU A 539    23638  28476  19869   1446   2044  -1481       N  
ATOM   3699  CA  LEU A 539      -7.245 -32.398  15.802  1.00181.31           C  
ANISOU 3699  CA  LEU A 539    22722  27371  18794   1403   2114  -1312       C  
ATOM   3700  C   LEU A 539      -7.891 -30.993  15.879  1.00182.04           C  
ANISOU 3700  C   LEU A 539    22898  27460  18808   1473   2058  -1234       C  
ATOM   3701  O   LEU A 539      -7.928 -30.370  16.934  1.00173.50           O  
ANISOU 3701  O   LEU A 539    21847  26302  17771   1464   2084  -1164       O  
ATOM   3702  CB  LEU A 539      -5.779 -32.319  15.400  1.00174.68           C  
ANISOU 3702  CB  LEU A 539    21965  26546  17858   1357   2168  -1240       C  
ATOM   3703  CG  LEU A 539      -4.902 -31.632  16.445  1.00168.00           C  
ANISOU 3703  CG  LEU A 539    21198  25600  17034   1304   2233  -1113       C  
ATOM   3704  CD1 LEU A 539      -3.478 -32.169  16.487  1.00168.10           C  
ANISOU 3704  CD1 LEU A 539    21223  25590  17054   1227   2308  -1091       C  
ATOM   3705  CD2 LEU A 539      -4.825 -30.164  16.142  1.00165.06           C  
ANISOU 3705  CD2 LEU A 539    20928  25212  16574   1351   2201  -1002       C  
ATOM   3706  N   GLU A 540      -8.407 -30.515  14.752  1.00188.46           N  
ANISOU 3706  N   GLU A 540    23739  28365  19501   1563   1973  -1258       N  
ATOM   3707  CA  GLU A 540      -9.150 -29.250  14.695  1.00190.38           C  
ANISOU 3707  CA  GLU A 540    24046  28603  19687   1644   1906  -1192       C  
ATOM   3708  C   GLU A 540     -10.434 -29.299  15.543  1.00190.88           C  
ANISOU 3708  C   GLU A 540    24023  28621  19879   1663   1871  -1269       C  
ATOM   3709  O   GLU A 540     -10.757 -28.322  16.240  1.00181.40           O  
ANISOU 3709  O   GLU A 540    22867  27359  18695   1686   1858  -1202       O  
ATOM   3710  CB  GLU A 540      -9.494 -28.903  13.244  1.00197.92           C  
ANISOU 3710  CB  GLU A 540    25034  29694  20471   1764   1822  -1202       C  
ATOM   3711  CG  GLU A 540      -8.272 -28.585  12.380  1.00206.02           C  
ANISOU 3711  CG  GLU A 540    26152  30782  21343   1776   1878  -1070       C  
ATOM   3712  CD  GLU A 540      -8.570 -28.541  10.872  1.00215.90           C  
ANISOU 3712  CD  GLU A 540    27417  32228  22383   1931   1809  -1093       C  
ATOM   3713  OE1 GLU A 540      -9.561 -29.162  10.417  1.00225.76           O  
ANISOU 3713  OE1 GLU A 540    28579  33579  23621   2014   1704  -1284       O  
ATOM   3714  OE2 GLU A 540      -7.820 -27.864  10.122  1.00210.62           O  
ANISOU 3714  OE2 GLU A 540    26838  31622  21563   1987   1860   -917       O  
ATOM   3715  N   ARG A 541     -11.156 -30.428  15.478  1.00191.01           N  
ANISOU 3715  N   ARG A 541    23902  28662  20010   1659   1857  -1416       N  
ATOM   3716  CA  ARG A 541     -12.354 -30.648  16.318  1.00194.27           C  
ANISOU 3716  CA  ARG A 541    24200  29026  20586   1670   1856  -1476       C  
ATOM   3717  C   ARG A 541     -12.057 -30.630  17.814  1.00186.99           C  
ANISOU 3717  C   ARG A 541    23277  28022  19749   1615   1968  -1377       C  
ATOM   3718  O   ARG A 541     -12.825 -30.085  18.600  1.00172.87           O  
ANISOU 3718  O   ARG A 541    21470  26214  17999   1659   1968  -1356       O  
ATOM   3719  CB  ARG A 541     -13.024 -31.984  16.016  1.00201.11           C  
ANISOU 3719  CB  ARG A 541    24884  29896  21632   1660   1843  -1641       C  
ATOM   3720  CG  ARG A 541     -13.804 -32.057  14.721  1.00213.13           C  
ANISOU 3720  CG  ARG A 541    26351  31514  23114   1759   1698  -1810       C  
ATOM   3721  CD  ARG A 541     -14.326 -33.471  14.567  1.00225.87           C  
ANISOU 3721  CD  ARG A 541    27748  33092  24978   1735   1685  -2000       C  
ATOM   3722  NE  ARG A 541     -15.045 -33.706  13.318  1.00240.95           N  
ANISOU 3722  NE  ARG A 541    29572  35104  26874   1850   1522  -2223       N  
ATOM   3723  CZ  ARG A 541     -15.656 -34.850  13.010  1.00253.16           C  
ANISOU 3723  CZ  ARG A 541    30898  36614  28675   1856   1466  -2446       C  
ATOM   3724  NH1 ARG A 541     -15.639 -35.877  13.859  1.00255.29           N  
ANISOU 3724  NH1 ARG A 541    31013  36731  29253   1742   1580  -2439       N  
ATOM   3725  NH2 ARG A 541     -16.280 -34.980  11.843  1.00261.85           N  
ANISOU 3725  NH2 ARG A 541    31920  37831  29739   1990   1290  -2682       N  
ATOM   3726  N   ALA A 542     -10.945 -31.244  18.197  1.00182.32           N  
ANISOU 3726  N   ALA A 542    22699  27400  19172   1539   2059  -1325       N  
ATOM   3727  CA  ALA A 542     -10.515 -31.252  19.590  1.00173.60           C  
ANISOU 3727  CA  ALA A 542    21601  26250  18109   1518   2158  -1232       C  
ATOM   3728  C   ALA A 542     -10.204 -29.834  20.085  1.00168.62           C  
ANISOU 3728  C   ALA A 542    21093  25606  17367   1564   2121  -1163       C  
ATOM   3729  O   ALA A 542     -10.503 -29.477  21.202  1.00172.71           O  
ANISOU 3729  O   ALA A 542    21598  26121  17903   1613   2149  -1136       O  
ATOM   3730  CB  ALA A 542      -9.299 -32.138  19.723  1.00174.09           C  
ANISOU 3730  CB  ALA A 542    21664  26289  18194   1439   2240  -1202       C  
ATOM   3731  N   ARG A 543      -9.600 -29.026  19.224  1.00168.38           N  
ANISOU 3731  N   ARG A 543    21170  25570  17236   1561   2059  -1134       N  
ATOM   3732  CA  ARG A 543      -9.294 -27.629  19.534  1.00165.56           C  
ANISOU 3732  CA  ARG A 543    20906  25162  16834   1601   2012  -1073       C  
ATOM   3733  C   ARG A 543     -10.558 -26.793  19.667  1.00163.51           C  
ANISOU 3733  C   ARG A 543    20633  24909  16584   1689   1931  -1104       C  
ATOM   3734  O   ARG A 543     -10.640 -25.951  20.553  1.00151.85           O  
ANISOU 3734  O   ARG A 543    19172  23394  15130   1739   1906  -1100       O  
ATOM   3735  CB  ARG A 543      -8.355 -27.036  18.466  1.00170.28           C  
ANISOU 3735  CB  ARG A 543    21598  25738  17362   1576   1991   -997       C  
ATOM   3736  CG  ARG A 543      -6.919 -27.470  18.689  1.00172.91           C  
ANISOU 3736  CG  ARG A 543    21954  26035  17707   1495   2070   -960       C  
ATOM   3737  CD  ARG A 543      -6.088 -27.626  17.441  1.00174.36           C  
ANISOU 3737  CD  ARG A 543    22182  26249  17817   1458   2094   -903       C  
ATOM   3738  NE  ARG A 543      -5.641 -26.356  16.904  1.00177.68           N  
ANISOU 3738  NE  ARG A 543    22677  26610  18222   1483   2074   -783       N  
ATOM   3739  CZ  ARG A 543      -4.558 -26.165  16.148  1.00184.34           C  
ANISOU 3739  CZ  ARG A 543    23561  27442  19035   1451   2129   -679       C  
ATOM   3740  NH1 ARG A 543      -3.752 -27.162  15.792  1.00187.20           N  
ANISOU 3740  NH1 ARG A 543    23908  27863  19355   1392   2198   -701       N  
ATOM   3741  NH2 ARG A 543      -4.273 -24.937  15.728  1.00188.20           N  
ANISOU 3741  NH2 ARG A 543    24097  27853  19557   1482   2124   -539       N  
ATOM   3742  N   SER A 544     -11.539 -27.038  18.795  1.00169.31           N  
ANISOU 3742  N   SER A 544    21325  25697  17306   1722   1877  -1157       N  
ATOM   3743  CA  SER A 544     -12.798 -26.273  18.805  1.00170.03           C  
ANISOU 3743  CA  SER A 544    21396  25797  17409   1811   1790  -1197       C  
ATOM   3744  C   SER A 544     -13.705 -26.567  19.996  1.00163.77           C  
ANISOU 3744  C   SER A 544    20500  25015  16710   1843   1829  -1250       C  
ATOM   3745  O   SER A 544     -14.362 -25.638  20.497  1.00163.41           O  
ANISOU 3745  O   SER A 544    20459  24959  16670   1919   1774  -1264       O  
ATOM   3746  CB  SER A 544     -13.579 -26.479  17.504  1.00171.43           C  
ANISOU 3746  CB  SER A 544    21549  26044  17542   1858   1707  -1260       C  
ATOM   3747  OG  SER A 544     -13.985 -27.817  17.373  1.00171.70           O  
ANISOU 3747  OG  SER A 544    21459  26119  17659   1825   1741  -1365       O  
ATOM   3748  N   THR A 545     -13.745 -27.832  20.432  1.00161.76           N  
ANISOU 3748  N   THR A 545    20142  24779  16537   1796   1930  -1270       N  
ATOM   3749  CA  THR A 545     -14.569 -28.223  21.586  1.00165.47           C  
ANISOU 3749  CA  THR A 545    20497  25270  17104   1836   2009  -1275       C  
ATOM   3750  C   THR A 545     -14.056 -27.612  22.895  1.00167.21           C  
ANISOU 3750  C   THR A 545    20764  25504  17263   1890   2052  -1219       C  
ATOM   3751  O   THR A 545     -14.852 -27.172  23.713  1.00174.95           O  
ANISOU 3751  O   THR A 545    21695  26525  18250   1982   2056  -1234       O  
ATOM   3752  CB  THR A 545     -14.716 -29.753  21.737  1.00164.75           C  
ANISOU 3752  CB  THR A 545    20263  25175  17160   1778   2125  -1275       C  
ATOM   3753  OG1 THR A 545     -13.431 -30.362  21.645  1.00165.99           O  
ANISOU 3753  OG1 THR A 545    20469  25310  17287   1700   2181  -1228       O  
ATOM   3754  CG2 THR A 545     -15.594 -30.317  20.637  1.00167.59           C  
ANISOU 3754  CG2 THR A 545    20519  25524  17630   1764   2058  -1390       C  
ATOM   3755  N   LEU A 546     -12.742 -27.521  23.071  1.00167.29           N  
ANISOU 3755  N   LEU A 546    20861  25490  17211   1852   2070  -1175       N  
ATOM   3756  CA  LEU A 546     -12.175 -26.782  24.217  1.00165.07           C  
ANISOU 3756  CA  LEU A 546    20624  25223  16871   1927   2067  -1169       C  
ATOM   3757  C   LEU A 546     -12.254 -25.250  24.111  1.00166.44           C  
ANISOU 3757  C   LEU A 546    20869  25347  17023   1988   1930  -1218       C  
ATOM   3758  O   LEU A 546     -12.260 -24.582  25.118  1.00160.90           O  
ANISOU 3758  O   LEU A 546    20159  24671  16301   2089   1901  -1265       O  
ATOM   3759  CB  LEU A 546     -10.740 -27.217  24.488  1.00163.32           C  
ANISOU 3759  CB  LEU A 546    20449  24982  16620   1873   2121  -1129       C  
ATOM   3760  CG  LEU A 546     -10.665 -28.425  25.407  1.00163.99           C  
ANISOU 3760  CG  LEU A 546    20451  25138  16717   1891   2263  -1073       C  
ATOM   3761  CD1 LEU A 546     -10.973 -29.724  24.660  1.00161.90           C  
ANISOU 3761  CD1 LEU A 546    20107  24849  16557   1791   2340  -1040       C  
ATOM   3762  CD2 LEU A 546      -9.299 -28.444  26.059  1.00166.56           C  
ANISOU 3762  CD2 LEU A 546    20832  25468  16985   1901   2282  -1061       C  
ATOM   3763  N   SER A 547     -12.314 -24.705  22.896  1.00173.55           N  
ANISOU 3763  N   SER A 547    21829  26180  17932   1945   1847  -1207       N  
ATOM   3764  CA  SER A 547     -12.541 -23.260  22.675  1.00171.89           C  
ANISOU 3764  CA  SER A 547    21669  25897  17743   2005   1721  -1226       C  
ATOM   3765  C   SER A 547     -13.951 -22.842  23.049  1.00167.85           C  
ANISOU 3765  C   SER A 547    21094  25433  17247   2105   1668  -1296       C  
ATOM   3766  O   SER A 547     -14.181 -21.697  23.425  1.00160.25           O  
ANISOU 3766  O   SER A 547    20142  24425  16318   2187   1574  -1344       O  
ATOM   3767  CB  SER A 547     -12.304 -22.885  21.208  1.00171.25           C  
ANISOU 3767  CB  SER A 547    21661  25754  17651   1955   1670  -1153       C  
ATOM   3768  OG  SER A 547     -10.954 -23.069  20.865  1.00174.19           O  
ANISOU 3768  OG  SER A 547    22088  26076  18017   1873   1719  -1081       O  
ATOM   3769  N   LYS A 548     -14.876 -23.795  22.930  1.00168.35           N  
ANISOU 3769  N   LYS A 548    21075  25574  17316   2098   1728  -1310       N  
ATOM   3770  CA  LYS A 548     -16.284 -23.628  23.274  1.00175.37           C  
ANISOU 3770  CA  LYS A 548    21875  26516  18239   2184   1704  -1375       C  
ATOM   3771  C   LYS A 548     -16.485 -23.262  24.764  1.00174.01           C  
ANISOU 3771  C   LYS A 548    21653  26411  18050   2297   1736  -1415       C  
ATOM   3772  O   LYS A 548     -17.503 -22.654  25.133  1.00173.20           O  
ANISOU 3772  O   LYS A 548    21498  26344  17964   2396   1684  -1481       O  
ATOM   3773  CB  LYS A 548     -17.013 -24.942  22.892  1.00182.60           C  
ANISOU 3773  CB  LYS A 548    22681  27478  19218   2135   1788  -1380       C  
ATOM   3774  CG  LYS A 548     -18.442 -25.171  23.407  1.00189.07           C  
ANISOU 3774  CG  LYS A 548    23360  28355  20123   2207   1820  -1432       C  
ATOM   3775  CD  LYS A 548     -19.460 -24.623  22.447  1.00191.69           C  
ANISOU 3775  CD  LYS A 548    23680  28666  20486   2241   1687  -1513       C  
ATOM   3776  CE  LYS A 548     -20.862 -24.879  22.984  1.00191.39           C  
ANISOU 3776  CE  LYS A 548    23483  28675  20560   2306   1726  -1573       C  
ATOM   3777  NZ  LYS A 548     -21.804 -23.783  22.636  1.00192.97           N  
ANISOU 3777  NZ  LYS A 548    23695  28870  20754   2395   1579  -1658       N  
ATOM   3778  N   ILE A 549     -15.509 -23.615  25.602  1.00165.69           N  
ANISOU 3778  N   ILE A 549    20612  25392  16950   2301   1813  -1386       N  
ATOM   3779  CA  ILE A 549     -15.581 -23.324  27.024  1.00159.71           C  
ANISOU 3779  CA  ILE A 549    19808  24740  16134   2444   1840  -1433       C  
ATOM   3780  C   ILE A 549     -15.477 -21.791  27.280  1.00153.84           C  
ANISOU 3780  C   ILE A 549    19109  23943  15400   2540   1674  -1550       C  
ATOM   3781  O   ILE A 549     -14.387 -21.211  27.284  1.00144.00           O  
ANISOU 3781  O   ILE A 549    17928  22611  14175   2524   1602  -1580       O  
ATOM   3782  CB  ILE A 549     -14.482 -24.093  27.781  1.00161.95           C  
ANISOU 3782  CB  ILE A 549    20098  25081  16351   2443   1948  -1378       C  
ATOM   3783  CG1 ILE A 549     -14.671 -25.609  27.608  1.00163.69           C  
ANISOU 3783  CG1 ILE A 549    20249  25335  16608   2359   2115  -1259       C  
ATOM   3784  CG2 ILE A 549     -14.529 -23.744  29.257  1.00167.91           C  
ANISOU 3784  CG2 ILE A 549    20805  25986  17004   2636   1962  -1440       C  
ATOM   3785  CD1 ILE A 549     -13.525 -26.449  28.141  1.00164.66           C  
ANISOU 3785  CD1 ILE A 549    20388  25492  16683   2340   2218  -1185       C  
ATOM   3786  N   ASN A 550     -16.612 -21.149  27.533  1.00153.88           N  
ANISOU 3786  N   ASN A 550    19057  23988  15420   2644   1613  -1626       N  
ATOM   3787  CA  ASN A 550     -16.637 -19.681  27.682  1.00153.95           C  
ANISOU 3787  CA  ASN A 550    19089  23921  15483   2734   1440  -1750       C  
ATOM   3788  C   ASN A 550     -16.252 -19.341  29.116  1.00156.12           C  
ANISOU 3788  C   ASN A 550    19317  24313  15687   2902   1424  -1870       C  
ATOM   3789  O   ASN A 550     -16.130 -20.230  29.994  1.00163.00           O  
ANISOU 3789  O   ASN A 550    20142  25351  16436   2966   1559  -1833       O  
ATOM   3790  CB  ASN A 550     -18.007 -19.047  27.294  1.00155.35           C  
ANISOU 3790  CB  ASN A 550    19225  24085  15715   2786   1357  -1801       C  
ATOM   3791  CG  ASN A 550     -19.216 -19.764  27.918  1.00152.66           C  
ANISOU 3791  CG  ASN A 550    18768  23914  15320   2864   1471  -1804       C  
ATOM   3792  OD1 ASN A 550     -19.297 -19.850  29.109  1.00151.92           O  
ANISOU 3792  OD1 ASN A 550    18610  23967  15145   2997   1531  -1850       O  
ATOM   3793  ND2 ASN A 550     -20.123 -20.320  27.113  1.00153.86           N  
ANISOU 3793  ND2 ASN A 550    18882  24052  15525   2792   1509  -1753       N  
ATOM   3794  N   GLU A 551     -16.037 -18.055  29.363  1.00145.48           N  
ANISOU 3794  N   GLU A 551    18345  21187  15742     16    144    675       N  
ATOM   3795  CA  GLU A 551     -15.728 -17.580  30.716  1.00147.70           C  
ANISOU 3795  CA  GLU A 551    18712  21320  16086     34    132    703       C  
ATOM   3796  C   GLU A 551     -16.931 -17.705  31.673  1.00147.73           C  
ANISOU 3796  C   GLU A 551    18775  21235  16119     73    129    725       C  
ATOM   3797  O   GLU A 551     -16.726 -18.056  32.834  1.00158.93           O  
ANISOU 3797  O   GLU A 551    20250  22539  17597     87    112    693       O  
ATOM   3798  CB  GLU A 551     -15.190 -16.146  30.703  1.00149.39           C  
ANISOU 3798  CB  GLU A 551    18972  21509  16281      6    151    792       C  
ATOM   3799  CG  GLU A 551     -14.506 -15.740  32.009  1.00151.79           C  
ANISOU 3799  CG  GLU A 551    19357  21686  16627    -19    142    793       C  
ATOM   3800  CD  GLU A 551     -13.501 -14.604  31.848  1.00153.86           C  
ANISOU 3800  CD  GLU A 551    19658  21956  16844   -108    164    837       C  
ATOM   3801  OE1 GLU A 551     -12.569 -14.739  31.023  1.00152.60           O  
ANISOU 3801  OE1 GLU A 551    19413  21924  16644   -157    158    808       O  
ATOM   3802  OE2 GLU A 551     -13.625 -13.584  32.563  1.00153.79           O  
ANISOU 3802  OE2 GLU A 551    19776  21827  16828   -141    194    898       O  
ATOM   3803  N   THR A 552     -18.162 -17.490  31.186  1.00141.47           N  
ANISOU 3803  N   THR A 552    17955  20524  15273     94    143    780       N  
ATOM   3804  CA  THR A 552     -19.384 -17.663  32.012  1.00137.41           C  
ANISOU 3804  CA  THR A 552    17471  19976  14763    129    141    804       C  
ATOM   3805  C   THR A 552     -19.551 -19.089  32.573  1.00135.29           C  
ANISOU 3805  C   THR A 552    17213  19665  14526     92    121    691       C  
ATOM   3806  O   THR A 552     -20.087 -19.274  33.637  1.00131.67           O  
ANISOU 3806  O   THR A 552    16807  19119  14102    111    111    692       O  
ATOM   3807  CB  THR A 552     -20.662 -17.354  31.197  1.00136.91           C  
ANISOU 3807  CB  THR A 552    17330  20089  14599    156    161    881       C  
ATOM   3808  OG1 THR A 552     -20.439 -16.225  30.353  1.00146.99           O  
ANISOU 3808  OG1 THR A 552    18595  21426  15826    195    191    979       O  
ATOM   3809  CG2 THR A 552     -21.851 -17.069  32.062  1.00134.65           C  
ANISOU 3809  CG2 THR A 552    17071  19793  14297    221    167    950       C  
ATOM   3810  N   MET A 553     -19.075 -20.074  31.822  1.00138.44           N  
ANISOU 3810  N   MET A 553    17578  20119  14903     40    125    595       N  
ATOM   3811  CA  MET A 553     -18.984 -21.462  32.245  1.00137.05           C  
ANISOU 3811  CA  MET A 553    17457  19869  14747     11    130    483       C  
ATOM   3812  C   MET A 553     -18.062 -21.602  33.466  1.00136.75           C  
ANISOU 3812  C   MET A 553    17493  19665  14797     70    116    466       C  
ATOM   3813  O   MET A 553     -18.463 -22.117  34.492  1.00130.80           O  
ANISOU 3813  O   MET A 553    16809  18809  14079     80    111    443       O  
ATOM   3814  CB  MET A 553     -18.415 -22.313  31.085  1.00141.29           C  
ANISOU 3814  CB  MET A 553    17969  20482  15233    -33    158    393       C  
ATOM   3815  CG  MET A 553     -19.003 -23.716  30.972  1.00144.66           C  
ANISOU 3815  CG  MET A 553    18462  20894  15608   -109    193    283       C  
ATOM   3816  SD  MET A 553     -18.275 -24.838  29.742  1.00144.73           S  
ANISOU 3816  SD  MET A 553    18501  20939  15549   -152    251    161       S  
ATOM   3817  CE  MET A 553     -19.408 -24.650  28.362  1.00148.32           C  
ANISOU 3817  CE  MET A 553    18846  21638  15871   -293    259    165       C  
ATOM   3818  N   LEU A 554     -16.821 -21.117  33.342  1.00136.41           N  
ANISOU 3818  N   LEU A 554    17427  19625  14778    100    110    481       N  
ATOM   3819  CA  LEU A 554     -15.806 -21.272  34.401  1.00132.49           C  
ANISOU 3819  CA  LEU A 554    16969  19033  14336    150     96    468       C  
ATOM   3820  C   LEU A 554     -16.114 -20.424  35.646  1.00125.59           C  
ANISOU 3820  C   LEU A 554    16143  18063  13510    156     74    534       C  
ATOM   3821  O   LEU A 554     -15.934 -20.894  36.799  1.00129.33           O  
ANISOU 3821  O   LEU A 554    16670  18442  14029    190     63    513       O  
ATOM   3822  CB  LEU A 554     -14.421 -20.901  33.874  1.00130.81           C  
ANISOU 3822  CB  LEU A 554    16691  18909  14103    157     95    472       C  
ATOM   3823  CG  LEU A 554     -13.777 -21.819  32.836  1.00125.91           C  
ANISOU 3823  CG  LEU A 554    16028  18376  13436    181    123    401       C  
ATOM   3824  CD1 LEU A 554     -12.449 -21.191  32.480  1.00126.91           C  
ANISOU 3824  CD1 LEU A 554    16070  18616  13533    180    114    429       C  
ATOM   3825  CD2 LEU A 554     -13.506 -23.251  33.292  1.00123.36           C  
ANISOU 3825  CD2 LEU A 554    15775  17975  13117    262    154    323       C  
ATOM   3826  N   ARG A 555     -16.597 -19.202  35.384  1.00117.20           N  
ANISOU 3826  N   ARG A 555    15078  17023  12429    132     77    617       N  
ATOM   3827  CA  ARG A 555     -17.088 -18.285  36.399  1.00115.03           C  
ANISOU 3827  CA  ARG A 555    14875  16650  12179    143     76    686       C  
ATOM   3828  C   ARG A 555     -18.185 -18.982  37.305  1.00114.53           C  
ANISOU 3828  C   ARG A 555    14854  16516  12146    173     67    668       C  
ATOM   3829  O   ARG A 555     -18.103 -18.939  38.558  1.00107.62           O  
ANISOU 3829  O   ARG A 555    14039  15532  11318    188     54    670       O  
ATOM   3830  CB  ARG A 555     -17.608 -17.012  35.725  1.00115.49           C  
ANISOU 3830  CB  ARG A 555    14945  16746  12188    144    106    783       C  
ATOM   3831  CG  ARG A 555     -17.664 -15.804  36.635  1.00119.75           C  
ANISOU 3831  CG  ARG A 555    15598  17163  12736    151    130    858       C  
ATOM   3832  CD  ARG A 555     -18.267 -14.596  35.926  1.00121.20           C  
ANISOU 3832  CD  ARG A 555    15827  17366  12854    188    183    966       C  
ATOM   3833  NE  ARG A 555     -18.994 -13.697  36.843  1.00121.24           N  
ANISOU 3833  NE  ARG A 555    15964  17245  12855    248    223   1046       N  
ATOM   3834  CZ  ARG A 555     -18.583 -12.504  37.281  1.00125.13           C  
ANISOU 3834  CZ  ARG A 555    16608  17608  13327    223    276   1100       C  
ATOM   3835  NH1 ARG A 555     -17.420 -11.975  36.900  1.00128.36           N  
ANISOU 3835  NH1 ARG A 555    17051  18008  13710    115    291   1086       N  
ATOM   3836  NH2 ARG A 555     -19.361 -11.823  38.115  1.00125.92           N  
ANISOU 3836  NH2 ARG A 555    16837  17588  13417    298    323   1167       N  
ATOM   3837  N   LEU A 556     -19.148 -19.662  36.669  1.00111.09           N  
ANISOU 3837  N   LEU A 556    14379  16159  11669    162     74    644       N  
ATOM   3838  CA  LEU A 556     -20.128 -20.510  37.379  1.00106.40           C  
ANISOU 3838  CA  LEU A 556    13818  15528  11080    154     69    609       C  
ATOM   3839  C   LEU A 556     -19.500 -21.560  38.305  1.00104.36           C  
ANISOU 3839  C   LEU A 556    13625  15147  10877    163     60    531       C  
ATOM   3840  O   LEU A 556     -19.950 -21.784  39.422  1.00111.92           O  
ANISOU 3840  O   LEU A 556    14640  16015  11869    176     50    532       O  
ATOM   3841  CB  LEU A 556     -21.012 -21.230  36.377  1.00106.24           C  
ANISOU 3841  CB  LEU A 556    13742  15645  10978     93     84    571       C  
ATOM   3842  CG  LEU A 556     -22.272 -21.896  36.888  1.00104.34           C  
ANISOU 3842  CG  LEU A 556    13517  15429  10698     47     85    550       C  
ATOM   3843  CD1 LEU A 556     -23.290 -20.819  37.197  1.00105.54           C  
ANISOU 3843  CD1 LEU A 556    13626  15655  10817    101     81    665       C  
ATOM   3844  CD2 LEU A 556     -22.821 -22.853  35.847  1.00105.09           C  
ANISOU 3844  CD2 LEU A 556    13574  15661  10695    -64    108    476       C  
ATOM   3845  N   GLY A 557     -18.462 -22.217  37.840  1.00102.90           N  
ANISOU 3845  N   GLY A 557    13436  14966  10694    172     71    470       N  
ATOM   3846  CA  GLY A 557     -17.720 -23.167  38.680  1.00102.49           C  
ANISOU 3846  CA  GLY A 557    13449  14812  10679    222     76    416       C  
ATOM   3847  C   GLY A 557     -16.962 -22.499  39.823  1.00100.43           C  
ANISOU 3847  C   GLY A 557    13190  14496  10469    266     47    464       C  
ATOM   3848  O   GLY A 557     -16.922 -23.023  40.953  1.00101.64           O  
ANISOU 3848  O   GLY A 557    13403  14558  10658    305     41    452       O  
ATOM   3849  N   ILE A 558     -16.364 -21.345  39.536  1.00 97.25           N  
ANISOU 3849  N   ILE A 558    12734  14156  10060    245     34    517       N  
ATOM   3850  CA  ILE A 558     -15.722 -20.559  40.590  1.00 97.43           C  
ANISOU 3850  CA  ILE A 558    12768  14143  10106    240     14    558       C  
ATOM   3851  C   ILE A 558     -16.740 -20.182  41.674  1.00100.64           C  
ANISOU 3851  C   ILE A 558    13248  14440  10548    236      5    593       C  
ATOM   3852  O   ILE A 558     -16.484 -20.338  42.903  1.00106.42           O  
ANISOU 3852  O   ILE A 558    14017  15106  11312    253     -9    591       O  
ATOM   3853  CB  ILE A 558     -15.039 -19.318  40.020  1.00 95.25           C  
ANISOU 3853  CB  ILE A 558    12455  13942   9794    178     17    605       C  
ATOM   3854  CG1 ILE A 558     -13.774 -19.745  39.315  1.00 96.35           C  
ANISOU 3854  CG1 ILE A 558    12508  14207   9894    187     18    570       C  
ATOM   3855  CG2 ILE A 558     -14.662 -18.311  41.092  1.00 95.58           C  
ANISOU 3855  CG2 ILE A 558    12545  13931   9837    124     11    647       C  
ATOM   3856  CD1 ILE A 558     -13.457 -18.812  38.177  1.00101.35           C  
ANISOU 3856  CD1 ILE A 558    13098  14931  10477    119     31    602       C  
ATOM   3857  N   PHE A 559     -17.909 -19.730  41.239  1.00100.34           N  
ANISOU 3857  N   PHE A 559    13224  14405  10495    225     18    629       N  
ATOM   3858  CA  PHE A 559     -18.979 -19.444  42.200  1.00 98.80           C  
ANISOU 3858  CA  PHE A 559    13089  14130  10319    241     16    666       C  
ATOM   3859  C   PHE A 559     -19.425 -20.712  42.933  1.00 97.05           C  
ANISOU 3859  C   PHE A 559    12894  13855  10124    256      4    610       C  
ATOM   3860  O   PHE A 559     -19.637 -20.693  44.133  1.00 97.47           O  
ANISOU 3860  O   PHE A 559    12998  13824  10212    270     -8    620       O  
ATOM   3861  CB  PHE A 559     -20.151 -18.761  41.520  1.00 99.65           C  
ANISOU 3861  CB  PHE A 559    13185  14299  10379    254     39    730       C  
ATOM   3862  CG  PHE A 559     -19.990 -17.282  41.421  1.00101.91           C  
ANISOU 3862  CG  PHE A 559    13519  14559  10642    265     70    813       C  
ATOM   3863  CD1 PHE A 559     -19.037 -16.710  40.593  1.00101.64           C  
ANISOU 3863  CD1 PHE A 559    13469  14563  10584    227     83    821       C  
ATOM   3864  CD2 PHE A 559     -20.806 -16.452  42.166  1.00107.37           C  
ANISOU 3864  CD2 PHE A 559    14290  15179  11325    314     96    883       C  
ATOM   3865  CE1 PHE A 559     -18.900 -15.336  40.518  1.00105.05           C  
ANISOU 3865  CE1 PHE A 559    13986  14947  10981    220    128    896       C  
ATOM   3866  CE2 PHE A 559     -20.690 -15.071  42.097  1.00109.04           C  
ANISOU 3866  CE2 PHE A 559    14596  15332  11501    331    148    962       C  
ATOM   3867  CZ  PHE A 559     -19.729 -14.507  41.282  1.00107.25           C  
ANISOU 3867  CZ  PHE A 559    14376  15125  11248    275    166    967       C  
ATOM   3868  N   GLY A 560     -19.547 -21.813  42.205  1.00 98.15           N  
ANISOU 3868  N   GLY A 560    13016  14036  10239    243     15    547       N  
ATOM   3869  CA  GLY A 560     -19.916 -23.084  42.801  1.00 96.83           C  
ANISOU 3869  CA  GLY A 560    12912  13798  10079    241     22    487       C  
ATOM   3870  C   GLY A 560     -18.971 -23.476  43.889  1.00 94.71           C  
ANISOU 3870  C   GLY A 560    12688  13437   9859    301     13    475       C  
ATOM   3871  O   GLY A 560     -19.419 -23.831  44.990  1.00100.34           O  
ANISOU 3871  O   GLY A 560    13461  14065  10598    311      5    475       O  
ATOM   3872  N   PHE A 561     -17.677 -23.409  43.621  1.00 93.98           N  
ANISOU 3872  N   PHE A 561    12556  13386   9765    343     13    472       N  
ATOM   3873  CA  PHE A 561     -16.704 -23.740  44.668  1.00 99.71           C  
ANISOU 3873  CA  PHE A 561    13294  14077  10512    413      4    475       C  
ATOM   3874  C   PHE A 561     -16.739 -22.711  45.815  1.00100.38           C  
ANISOU 3874  C   PHE A 561    13376  14136  10627    384    -29    529       C  
ATOM   3875  O   PHE A 561     -16.694 -23.106  47.028  1.00102.94           O  
ANISOU 3875  O   PHE A 561    13740  14396  10974    420    -40    532       O  
ATOM   3876  CB  PHE A 561     -15.274 -23.907  44.127  1.00102.41           C  
ANISOU 3876  CB  PHE A 561    13567  14523  10819    471     14    468       C  
ATOM   3877  CG  PHE A 561     -15.026 -25.237  43.470  1.00105.47           C  
ANISOU 3877  CG  PHE A 561    14002  14895  11174    550     65    412       C  
ATOM   3878  CD1 PHE A 561     -14.946 -26.422  44.229  1.00104.61           C  
ANISOU 3878  CD1 PHE A 561    13994  14686  11064    648    100    390       C  
ATOM   3879  CD2 PHE A 561     -14.898 -25.325  42.086  1.00109.29           C  
ANISOU 3879  CD2 PHE A 561    14454  15450  11620    529     90    381       C  
ATOM   3880  CE1 PHE A 561     -14.730 -27.658  43.620  1.00105.48           C  
ANISOU 3880  CE1 PHE A 561    14197  14748  11130    727    172    337       C  
ATOM   3881  CE2 PHE A 561     -14.677 -26.571  41.475  1.00109.79           C  
ANISOU 3881  CE2 PHE A 561    14593  15479  11641    599    154    321       C  
ATOM   3882  CZ  PHE A 561     -14.590 -27.736  42.243  1.00106.34           C  
ANISOU 3882  CZ  PHE A 561    14282  14922  11199    700    201    299       C  
ATOM   3883  N   LEU A 562     -16.886 -21.425  45.463  1.00 98.91           N  
ANISOU 3883  N   LEU A 562    13164  13984  10431    319    -36    571       N  
ATOM   3884  CA  LEU A 562     -16.985 -20.398  46.537  1.00 99.33           C  
ANISOU 3884  CA  LEU A 562    13254  13985  10498    280    -49    616       C  
ATOM   3885  C   LEU A 562     -18.179 -20.613  47.477  1.00 99.63           C  
ANISOU 3885  C   LEU A 562    13362  13922  10571    297    -54    624       C  
ATOM   3886  O   LEU A 562     -18.043 -20.544  48.694  1.00103.19           O  
ANISOU 3886  O   LEU A 562    13846  14320  11041    299    -68    632       O  
ATOM   3887  CB  LEU A 562     -17.017 -18.986  45.991  1.00101.88           C  
ANISOU 3887  CB  LEU A 562    13591  14327  10792    215    -31    662       C  
ATOM   3888  CG  LEU A 562     -15.595 -18.441  45.743  1.00105.95           C  
ANISOU 3888  CG  LEU A 562    14126  14848  11281    139    -32    680       C  
ATOM   3889  CD1 LEU A 562     -14.847 -19.188  44.631  1.00107.05           C  
ANISOU 3889  CD1 LEU A 562    14167  15130  11377    111    -47    656       C  
ATOM   3890  CD2 LEU A 562     -15.636 -16.972  45.362  1.00110.52           C  
ANISOU 3890  CD2 LEU A 562    14789  15379  11824     71      8    730       C  
ATOM   3891  N   ALA A 563     -19.328 -20.945  46.906  1.00100.57           N  
ANISOU 3891  N   ALA A 563    13489  14040  10683    302    -42    620       N  
ATOM   3892  CA  ALA A 563     -20.498 -21.379  47.674  1.00 99.79           C  
ANISOU 3892  CA  ALA A 563    13435  13883  10595    310    -45    620       C  
ATOM   3893  C   ALA A 563     -20.261 -22.711  48.443  1.00100.54           C  
ANISOU 3893  C   ALA A 563    13572  13914  10714    334    -52    569       C  
ATOM   3894  O   ALA A 563     -20.666 -22.839  49.612  1.00101.33           O  
ANISOU 3894  O   ALA A 563    13717  13945  10838    342    -64    579       O  
ATOM   3895  CB  ALA A 563     -21.728 -21.479  46.763  1.00 99.04           C  
ANISOU 3895  CB  ALA A 563    13314  13862  10454    289    -29    627       C  
ATOM   3896  N   PHE A 564     -19.636 -23.695  47.788  1.00 98.45           N  
ANISOU 3896  N   PHE A 564    13305  13664  10434    356    -34    520       N  
ATOM   3897  CA  PHE A 564     -19.337 -24.986  48.448  1.00 98.41           C  
ANISOU 3897  CA  PHE A 564    13374  13580  10437    407    -17    481       C  
ATOM   3898  C   PHE A 564     -18.505 -24.819  49.712  1.00101.17           C  
ANISOU 3898  C   PHE A 564    13719  13906  10814    467    -40    513       C  
ATOM   3899  O   PHE A 564     -18.737 -25.517  50.752  1.00106.61           O  
ANISOU 3899  O   PHE A 564    14476  14511  11516    501    -37    510       O  
ATOM   3900  CB  PHE A 564     -18.569 -25.888  47.514  1.00 97.38           C  
ANISOU 3900  CB  PHE A 564    13258  13468  10273    454     22    435       C  
ATOM   3901  CG  PHE A 564     -18.303 -27.241  48.077  1.00 97.64           C  
ANISOU 3901  CG  PHE A 564    13404  13399  10295    532     65    403       C  
ATOM   3902  CD1 PHE A 564     -19.219 -28.267  47.893  1.00 99.41           C  
ANISOU 3902  CD1 PHE A 564    13754  13529  10487    476    112    348       C  
ATOM   3903  CD2 PHE A 564     -17.148 -27.511  48.783  1.00 97.36           C  
ANISOU 3903  CD2 PHE A 564    13359  13370  10261    657     68    432       C  
ATOM   3904  CE1 PHE A 564     -18.973 -29.551  48.388  1.00 98.20           C  
ANISOU 3904  CE1 PHE A 564    13752  13247  10310    551    173    320       C  
ATOM   3905  CE2 PHE A 564     -16.910 -28.792  49.283  1.00 98.43           C  
ANISOU 3905  CE2 PHE A 564    13622  13403  10374    763    124    417       C  
ATOM   3906  CZ  PHE A 564     -17.820 -29.814  49.080  1.00 96.94           C  
ANISOU 3906  CZ  PHE A 564    13595  13077  10160    713    182    360       C  
ATOM   3907  N   GLY A 565     -17.525 -23.906  49.627  1.00100.98           N  
ANISOU 3907  N   GLY A 565    13613  13969  10783    467    -60    544       N  
ATOM   3908  CA  GLY A 565     -16.676 -23.623  50.830  1.00 99.63           C  
ANISOU 3908  CA  GLY A 565    13415  13824  10612    492    -84    575       C  
ATOM   3909  C   GLY A 565     -17.446 -23.136  52.055  1.00 97.74           C  
ANISOU 3909  C   GLY A 565    13225  13506  10405    450   -105    598       C  
ATOM   3910  O   GLY A 565     -17.321 -23.668  53.162  1.00 94.82           O  
ANISOU 3910  O   GLY A 565    12880  13102  10043    494   -114    605       O  
ATOM   3911  N   PHE A 566     -18.311 -22.161  51.820  1.00 96.51           N  
ANISOU 3911  N   PHE A 566    13088  13322  10258    381   -106    614       N  
ATOM   3912  CA  PHE A 566     -19.228 -21.677  52.844  1.00 94.30           C  
ANISOU 3912  CA  PHE A 566    12865  12965   9999    356   -114    637       C  
ATOM   3913  C   PHE A 566     -20.171 -22.762  53.409  1.00 90.38           C  
ANISOU 3913  C   PHE A 566    12420  12397   9523    387   -114    619       C  
ATOM   3914  O   PHE A 566     -20.411 -22.840  54.628  1.00 85.82           O  
ANISOU 3914  O   PHE A 566    11878  11767   8962    393   -128    630       O  
ATOM   3915  CB  PHE A 566     -20.055 -20.506  52.276  1.00 95.25           C  
ANISOU 3915  CB  PHE A 566    13005  13078  10105    319    -94    671       C  
ATOM   3916  CG  PHE A 566     -19.261 -19.216  52.092  1.00 95.18           C  
ANISOU 3916  CG  PHE A 566    13003  13093  10068    263    -80    696       C  
ATOM   3917  CD1 PHE A 566     -18.452 -18.695  53.134  1.00 91.35           C  
ANISOU 3917  CD1 PHE A 566    12538  12600   9568    207    -87    698       C  
ATOM   3918  CD2 PHE A 566     -19.361 -18.495  50.902  1.00 95.44           C  
ANISOU 3918  CD2 PHE A 566    13031  13159  10072    248    -52    717       C  
ATOM   3919  CE1 PHE A 566     -17.744 -17.535  52.972  1.00 90.68           C  
ANISOU 3919  CE1 PHE A 566    12483  12536   9435    115    -63    711       C  
ATOM   3920  CE2 PHE A 566     -18.661 -17.312  50.750  1.00 96.35           C  
ANISOU 3920  CE2 PHE A 566    13184  13276  10149    177    -26    739       C  
ATOM   3921  CZ  PHE A 566     -17.855 -16.835  51.785  1.00 95.54           C  
ANISOU 3921  CZ  PHE A 566    13116  13158  10025     99    -29    731       C  
ATOM   3922  N   VAL A 567     -20.684 -23.599  52.511  1.00 88.50           N  
ANISOU 3922  N   VAL A 567    12191  12162   9270    389    -95    586       N  
ATOM   3923  CA  VAL A 567     -21.534 -24.707  52.915  1.00 88.07           C  
ANISOU 3923  CA  VAL A 567    12205  12043   9211    382    -83    557       C  
ATOM   3924  C   VAL A 567     -20.743 -25.651  53.826  1.00 85.09           C  
ANISOU 3924  C   VAL A 567    11880  11601   8847    451    -78    548       C  
ATOM   3925  O   VAL A 567     -21.222 -26.078  54.896  1.00 82.04           O  
ANISOU 3925  O   VAL A 567    11552  11146   8472    454    -83    553       O  
ATOM   3926  CB  VAL A 567     -22.127 -25.408  51.677  1.00 90.59           C  
ANISOU 3926  CB  VAL A 567    12538  12393   9486    335    -51    513       C  
ATOM   3927  CG1 VAL A 567     -22.884 -26.697  52.035  1.00 91.66           C  
ANISOU 3927  CG1 VAL A 567    12777  12456   9594    291    -23    468       C  
ATOM   3928  CG2 VAL A 567     -23.084 -24.450  50.968  1.00 92.18           C  
ANISOU 3928  CG2 VAL A 567    12672  12692   9658    283    -58    543       C  
ATOM   3929  N   LEU A 568     -19.517 -25.931  53.419  1.00 84.15           N  
ANISOU 3929  N   LEU A 568    11733  11521   8717    521    -66    544       N  
ATOM   3930  CA  LEU A 568     -18.651 -26.759  54.248  1.00 86.30           C  
ANISOU 3930  CA  LEU A 568    12038  11769   8982    626    -53    556       C  
ATOM   3931  C   LEU A 568     -18.336 -26.150  55.638  1.00 85.58           C  
ANISOU 3931  C   LEU A 568    11905  11703   8906    632    -94    601       C  
ATOM   3932  O   LEU A 568     -18.229 -26.869  56.621  1.00 84.32           O  
ANISOU 3932  O   LEU A 568    11796  11497   8744    698    -87    617       O  
ATOM   3933  CB  LEU A 568     -17.351 -27.062  53.491  1.00 88.64           C  
ANISOU 3933  CB  LEU A 568    12284  12152   9241    720    -29    557       C  
ATOM   3934  CG  LEU A 568     -16.458 -28.172  54.054  1.00 91.29           C  
ANISOU 3934  CG  LEU A 568    12666  12479   9541    882      9    579       C  
ATOM   3935  CD1 LEU A 568     -17.048 -29.580  53.946  1.00 92.05           C  
ANISOU 3935  CD1 LEU A 568    12946  12408   9621    931     83    542       C  
ATOM   3936  CD2 LEU A 568     -15.135 -28.125  53.315  1.00 92.94           C  
ANISOU 3936  CD2 LEU A 568    12775  12836   9699    975     23    595       C  
ATOM   3937  N   ILE A 569     -18.183 -24.829  55.702  1.00 85.53           N  
ANISOU 3937  N   ILE A 569    11824  11768   8906    558   -128    621       N  
ATOM   3938  CA  ILE A 569     -18.048 -24.113  56.995  1.00 84.41           C  
ANISOU 3938  CA  ILE A 569    11664  11641   8767    522   -159    652       C  
ATOM   3939  C   ILE A 569     -19.353 -24.243  57.833  1.00 85.22           C  
ANISOU 3939  C   ILE A 569    11846  11628   8902    495   -164    651       C  
ATOM   3940  O   ILE A 569     -19.312 -24.629  59.003  1.00 85.06           O  
ANISOU 3940  O   ILE A 569    11850  11583   8886    524   -175    667       O  
ATOM   3941  CB  ILE A 569     -17.720 -22.584  56.804  1.00 84.55           C  
ANISOU 3941  CB  ILE A 569    11634  11723   8766    419   -172    664       C  
ATOM   3942  CG1 ILE A 569     -16.457 -22.296  55.933  1.00 85.07           C  
ANISOU 3942  CG1 ILE A 569    11610  11927   8783    409   -168    664       C  
ATOM   3943  CG2 ILE A 569     -17.593 -21.865  58.136  1.00 84.34           C  
ANISOU 3943  CG2 ILE A 569    11616  11700   8726    358   -190    683       C  
ATOM   3944  CD1 ILE A 569     -15.188 -23.015  56.335  1.00 86.03           C  
ANISOU 3944  CD1 ILE A 569    11648  12183   8854    491   -176    681       C  
ATOM   3945  N   THR A 570     -20.497 -23.864  57.241  1.00 88.87           N  
ANISOU 3945  N   THR A 570    12337  12051   9378    442   -156    641       N  
ATOM   3946  CA  THR A 570     -21.842 -23.976  57.893  1.00 89.40           C  
ANISOU 3946  CA  THR A 570    12460  12052   9456    414   -158    644       C  
ATOM   3947  C   THR A 570     -22.038 -25.359  58.456  1.00 87.24           C  
ANISOU 3947  C   THR A 570    12252  11713   9183    447   -148    626       C  
ATOM   3948  O   THR A 570     -22.308 -25.505  59.652  1.00 89.19           O  
ANISOU 3948  O   THR A 570    12529  11917   9439    451   -162    641       O  
ATOM   3949  CB  THR A 570     -22.999 -23.698  56.898  1.00 91.56           C  
ANISOU 3949  CB  THR A 570    12728  12350   9710    373   -142    640       C  
ATOM   3950  OG1 THR A 570     -22.905 -22.340  56.454  1.00 98.49           O  
ANISOU 3950  OG1 THR A 570    13573  13268  10580    363   -137    672       O  
ATOM   3951  CG2 THR A 570     -24.378 -23.897  57.515  1.00 90.53           C  
ANISOU 3951  CG2 THR A 570    12628  12204   9565    344   -143    648       C  
ATOM   3952  N   PHE A 571     -21.864 -26.365  57.608  1.00 84.67           N  
ANISOU 3952  N   PHE A 571    11964  11368   8838    468   -115    593       N  
ATOM   3953  CA  PHE A 571     -21.998 -27.739  58.055  1.00 83.95           C  
ANISOU 3953  CA  PHE A 571    11982  11182   8730    500    -81    574       C  
ATOM   3954  C   PHE A 571     -21.201 -28.030  59.333  1.00 85.05           C  
ANISOU 3954  C   PHE A 571    12134  11301   8880    593    -91    613       C  
ATOM   3955  O   PHE A 571     -21.746 -28.530  60.329  1.00 85.54           O  
ANISOU 3955  O   PHE A 571    12266  11291   8942    587    -89    621       O  
ATOM   3956  CB  PHE A 571     -21.536 -28.668  56.974  1.00 84.02           C  
ANISOU 3956  CB  PHE A 571    12050  11164   8707    537    -28    536       C  
ATOM   3957  CG  PHE A 571     -21.666 -30.086  57.338  1.00 84.12           C  
ANISOU 3957  CG  PHE A 571    12226  11048   8687    570     31    515       C  
ATOM   3958  CD1 PHE A 571     -22.898 -30.695  57.277  1.00 84.97           C  
ANISOU 3958  CD1 PHE A 571    12437  11086   8759    445     59    472       C  
ATOM   3959  CD2 PHE A 571     -20.561 -30.807  57.751  1.00 85.36           C  
ANISOU 3959  CD2 PHE A 571    12438  11165   8830    726     68    544       C  
ATOM   3960  CE1 PHE A 571     -23.039 -32.017  57.622  1.00 87.86           C  
ANISOU 3960  CE1 PHE A 571    12993  11307   9080    452    131    448       C  
ATOM   3961  CE2 PHE A 571     -20.684 -32.121  58.099  1.00 88.25           C  
ANISOU 3961  CE2 PHE A 571    12992  11384   9155    776    143    533       C  
ATOM   3962  CZ  PHE A 571     -21.929 -32.730  58.049  1.00 89.63           C  
ANISOU 3962  CZ  PHE A 571    13303  11452   9299    628    177    480       C  
ATOM   3963  N   SER A 572     -19.913 -27.678  59.313  1.00 86.59           N  
ANISOU 3963  N   SER A 572    12246  11585   9068    672   -103    641       N  
ATOM   3964  CA  SER A 572     -19.003 -27.884  60.469  1.00 87.22           C  
ANISOU 3964  CA  SER A 572    12297  11709   9130    766   -114    689       C  
ATOM   3965  C   SER A 572     -19.427 -27.135  61.751  1.00 86.74           C  
ANISOU 3965  C   SER A 572    12208  11657   9090    700   -160    711       C  
ATOM   3966  O   SER A 572     -19.285 -27.679  62.857  1.00 88.59           O  
ANISOU 3966  O   SER A 572    12471  11874   9312    758   -161    742       O  
ATOM   3967  CB  SER A 572     -17.578 -27.467  60.136  1.00 86.40           C  
ANISOU 3967  CB  SER A 572    12071  11765   8989    830   -124    716       C  
ATOM   3968  OG  SER A 572     -17.205 -27.913  58.862  1.00 85.66           O  
ANISOU 3968  OG  SER A 572    11987  11679   8877    880    -85    693       O  
ATOM   3969  N   CYS A 573     -19.974 -25.936  61.596  1.00 83.65           N  
ANISOU 3969  N   CYS A 573    11777  11285   8720    590   -188    699       N  
ATOM   3970  CA  CYS A 573     -20.518 -25.245  62.743  1.00 85.21           C  
ANISOU 3970  CA  CYS A 573    11977  11466   8930    530   -215    713       C  
ATOM   3971  C   CYS A 573     -21.727 -25.971  63.387  1.00 85.04           C  
ANISOU 3971  C   CYS A 573    12044  11340   8924    522   -209    708       C  
ATOM   3972  O   CYS A 573     -21.772 -26.181  64.606  1.00 85.29           O  
ANISOU 3972  O   CYS A 573    12095  11356   8955    536   -223    730       O  
ATOM   3973  CB  CYS A 573     -20.864 -23.804  62.360  1.00 87.12           C  
ANISOU 3973  CB  CYS A 573    12195  11729   9177    439   -222    707       C  
ATOM   3974  SG  CYS A 573     -19.394 -22.774  62.015  1.00 89.30           S  
ANISOU 3974  SG  CYS A 573    12386  12133   9411    395   -228    713       S  
ATOM   3975  N   HIS A 574     -22.697 -26.352  62.553  1.00 86.63           N  
ANISOU 3975  N   HIS A 574    12294  11494   9128    484   -187    679       N  
ATOM   3976  CA  HIS A 574     -23.859 -27.135  63.021  1.00 89.66           C  
ANISOU 3976  CA  HIS A 574    12760  11805   9502    444   -175    667       C  
ATOM   3977  C   HIS A 574     -23.469 -28.472  63.611  1.00 91.64           C  
ANISOU 3977  C   HIS A 574    13107  11974   9737    508   -146    671       C  
ATOM   3978  O   HIS A 574     -24.092 -28.922  64.596  1.00 90.61           O  
ANISOU 3978  O   HIS A 574    13037  11789   9599    486   -146    681       O  
ATOM   3979  CB  HIS A 574     -24.909 -27.318  61.912  1.00 90.28           C  
ANISOU 3979  CB  HIS A 574    12855  11895   9552    365   -152    632       C  
ATOM   3980  CG  HIS A 574     -25.634 -26.057  61.601  1.00 92.18           C  
ANISOU 3980  CG  HIS A 574    13016  12217   9790    326   -172    649       C  
ATOM   3981  ND1 HIS A 574     -25.991 -25.712  60.324  1.00 94.89           N  
ANISOU 3981  ND1 HIS A 574    13316  12629  10109    296   -158    638       N  
ATOM   3982  CD2 HIS A 574     -26.010 -25.023  62.388  1.00 93.54           C  
ANISOU 3982  CD2 HIS A 574    13156  12411   9971    330   -192    683       C  
ATOM   3983  CE1 HIS A 574     -26.578 -24.533  60.327  1.00 93.87           C  
ANISOU 3983  CE1 HIS A 574    13133  12562   9970    301   -166    674       C  
ATOM   3984  NE2 HIS A 574     -26.591 -24.087  61.569  1.00 93.94           N  
ANISOU 3984  NE2 HIS A 574    13159  12533  10000    323   -182    699       N  
ATOM   3985  N   PHE A 575     -22.477 -29.093  62.978  1.00 94.91           N  
ANISOU 3985  N   PHE A 575    13543  12379  10137    595   -112    670       N  
ATOM   3986  CA  PHE A 575     -21.940 -30.363  63.431  1.00 99.04           C  
ANISOU 3986  CA  PHE A 575    14180  12820  10631    704    -63    689       C  
ATOM   3987  C   PHE A 575     -21.305 -30.182  64.799  1.00100.41           C  
ANISOU 3987  C   PHE A 575    14301  13044  10805    784    -94    749       C  
ATOM   3988  O   PHE A 575     -21.523 -30.988  65.739  1.00101.90           O  
ANISOU 3988  O   PHE A 575    14587  13153  10976    825    -72    774       O  
ATOM   3989  CB  PHE A 575     -20.888 -30.863  62.452  1.00100.10           C  
ANISOU 3989  CB  PHE A 575    14328  12966  10738    816    -16    687       C  
ATOM   3990  CG  PHE A 575     -20.410 -32.238  62.747  1.00103.69           C  
ANISOU 3990  CG  PHE A 575    14939  13313  11145    958     62    712       C  
ATOM   3991  CD1 PHE A 575     -19.330 -32.469  63.608  1.00107.30           C  
ANISOU 3991  CD1 PHE A 575    15358  13836  11574   1132     66    788       C  
ATOM   3992  CD2 PHE A 575     -21.028 -33.313  62.146  1.00107.09           C  
ANISOU 3992  CD2 PHE A 575    15566  13583  11538    918    144    662       C  
ATOM   3993  CE1 PHE A 575     -18.901 -33.749  63.889  1.00111.64           C  
ANISOU 3993  CE1 PHE A 575    16070  14280  12066   1301    155    827       C  
ATOM   3994  CE2 PHE A 575     -20.601 -34.604  62.414  1.00111.89           C  
ANISOU 3994  CE2 PHE A 575    16370  14054  12089   1059    241    688       C  
ATOM   3995  CZ  PHE A 575     -19.538 -34.829  63.291  1.00113.36           C  
ANISOU 3995  CZ  PHE A 575    16524  14293  12253   1271    249    777       C  
ATOM   3996  N   TYR A 576     -20.514 -29.119  64.923  1.00 98.70           N  
ANISOU 3996  N   TYR A 576    13935  12968  10596    791   -142    771       N  
ATOM   3997  CA  TYR A 576     -19.882 -28.800  66.194  1.00 97.18           C  
ANISOU 3997  CA  TYR A 576    13670  12867  10386    832   -176    822       C  
ATOM   3998  C   TYR A 576     -20.939 -28.547  67.245  1.00 94.48           C  
ANISOU 3998  C   TYR A 576    13364  12463  10068    743   -203    818       C  
ATOM   3999  O   TYR A 576     -20.832 -29.026  68.343  1.00 94.65           O  
ANISOU 3999  O   TYR A 576    13410  12479  10071    794   -204    856       O  
ATOM   4000  CB  TYR A 576     -18.982 -27.572  66.057  1.00 99.37           C  
ANISOU 4000  CB  TYR A 576    13795  13312  10647    789   -217    828       C  
ATOM   4001  CG  TYR A 576     -18.516 -27.009  67.386  1.00100.61           C  
ANISOU 4001  CG  TYR A 576    13872  13583  10772    764   -256    864       C  
ATOM   4002  CD1 TYR A 576     -17.345 -27.471  67.982  1.00102.43           C  
ANISOU 4002  CD1 TYR A 576    14023  13963  10930    878   -255    924       C  
ATOM   4003  CD2 TYR A 576     -19.239 -26.005  68.034  1.00 98.89           C  
ANISOU 4003  CD2 TYR A 576    13656  13338  10577    630   -286    841       C  
ATOM   4004  CE1 TYR A 576     -16.916 -26.961  69.180  1.00103.86           C  
ANISOU 4004  CE1 TYR A 576    14119  14279  11063    834   -291    954       C  
ATOM   4005  CE2 TYR A 576     -18.817 -25.469  69.228  1.00 99.76           C  
ANISOU 4005  CE2 TYR A 576    13707  13549  10646    584   -315    863       C  
ATOM   4006  CZ  TYR A 576     -17.656 -25.961  69.796  1.00105.26           C  
ANISOU 4006  CZ  TYR A 576    14314  14408  11270    673   -321    916       C  
ATOM   4007  OH  TYR A 576     -17.216 -25.461  71.011  1.00118.76           O  
ANISOU 4007  OH  TYR A 576    15950  16252  12919    611   -350    938       O  
ATOM   4008  N   ASP A 577     -21.956 -27.776  66.907  1.00 95.98           N  
ANISOU 4008  N   ASP A 577    13553  12624  10291    623   -221    779       N  
ATOM   4009  CA  ASP A 577     -23.025 -27.488  67.881  1.00 96.94           C  
ANISOU 4009  CA  ASP A 577    13701  12705  10424    550   -241    779       C  
ATOM   4010  C   ASP A 577     -23.743 -28.754  68.287  1.00 97.17           C  
ANISOU 4010  C   ASP A 577    13849  12629  10440    559   -212    779       C  
ATOM   4011  O   ASP A 577     -24.078 -28.952  69.470  1.00 97.46           O  
ANISOU 4011  O   ASP A 577    13913  12646  10472    554   -224    802       O  
ATOM   4012  CB  ASP A 577     -24.050 -26.480  67.350  1.00 98.85           C  
ANISOU 4012  CB  ASP A 577    13921  12953  10682    455   -250    751       C  
ATOM   4013  CG  ASP A 577     -23.472 -25.120  67.109  1.00100.67           C  
ANISOU 4013  CG  ASP A 577    14079  13254  10915    430   -265    753       C  
ATOM   4014  OD1 ASP A 577     -22.266 -24.962  67.299  1.00103.37           O  
ANISOU 4014  OD1 ASP A 577    14370  13662  11241    456   -275    766       O  
ATOM   4015  OD2 ASP A 577     -24.199 -24.217  66.630  1.00103.83           O  
ANISOU 4015  OD2 ASP A 577    14476  13654  11318    385   -257    744       O  
ATOM   4016  N   PHE A 578     -23.984 -29.618  67.312  1.00 97.61           N  
ANISOU 4016  N   PHE A 578    13992  12614  10482    557   -166    750       N  
ATOM   4017  CA  PHE A 578     -24.695 -30.849  67.585  1.00 98.21           C  
ANISOU 4017  CA  PHE A 578    14218  12570  10524    529   -120    739       C  
ATOM   4018  C   PHE A 578     -23.873 -31.725  68.502  1.00 99.64           C  
ANISOU 4018  C   PHE A 578    14475  12697  10684    662    -91    792       C  
ATOM   4019  O   PHE A 578     -24.402 -32.304  69.441  1.00 98.01           O  
ANISOU 4019  O   PHE A 578    14357  12423  10459    643    -79    809       O  
ATOM   4020  CB  PHE A 578     -24.994 -31.544  66.274  1.00100.72           C  
ANISOU 4020  CB  PHE A 578    14630  12827  10812    481    -64    688       C  
ATOM   4021  CG  PHE A 578     -25.625 -32.873  66.433  1.00101.67           C  
ANISOU 4021  CG  PHE A 578    14946  12808  10875    424      4    666       C  
ATOM   4022  CD1 PHE A 578     -26.931 -32.967  66.838  1.00100.34           C  
ANISOU 4022  CD1 PHE A 578    14808  12642  10675    269     -4    642       C  
ATOM   4023  CD2 PHE A 578     -24.891 -34.036  66.149  1.00105.42           C  
ANISOU 4023  CD2 PHE A 578    15588  13152  11311    529     89    670       C  
ATOM   4024  CE1 PHE A 578     -27.509 -34.202  67.003  1.00103.52           C  
ANISOU 4024  CE1 PHE A 578    15409  12915  11006    182     66    616       C  
ATOM   4025  CE2 PHE A 578     -25.463 -35.270  66.290  1.00106.61           C  
ANISOU 4025  CE2 PHE A 578    15966  13143  11395    463    172    645       C  
ATOM   4026  CZ  PHE A 578     -26.781 -35.353  66.699  1.00105.60           C  
ANISOU 4026  CZ  PHE A 578    15872  13017  11234    269    159    613       C  
ATOM   4027  N   PHE A 579     -22.577 -31.832  68.207  1.00107.19           N  
ANISOU 4027  N   PHE A 579    15393  13702  11631    806    -75    825       N  
ATOM   4028  CA  PHE A 579     -21.667 -32.671  69.031  1.00115.05           C  
ANISOU 4028  CA  PHE A 579    16443  14686  12584    980    -39    897       C  
ATOM   4029  C   PHE A 579     -21.553 -32.209  70.480  1.00108.32           C  
ANISOU 4029  C   PHE A 579    15499  13923  11732    989    -94    948       C  
ATOM   4030  O   PHE A 579     -21.521 -33.012  71.365  1.00112.65           O  
ANISOU 4030  O   PHE A 579    16139  14415  12247   1069    -63    997       O  
ATOM   4031  CB  PHE A 579     -20.264 -32.689  68.403  1.00126.48           C  
ANISOU 4031  CB  PHE A 579    17813  16239  14001   1141    -19    934       C  
ATOM   4032  CG  PHE A 579     -19.227 -33.387  69.240  1.00138.09           C  
ANISOU 4032  CG  PHE A 579    19291  17767  15407   1354     15   1028       C  
ATOM   4033  CD1 PHE A 579     -18.711 -32.757  70.369  1.00139.67           C  
ANISOU 4033  CD1 PHE A 579    19334  18143  15590   1373    -47   1084       C  
ATOM   4034  CD2 PHE A 579     -18.771 -34.688  68.920  1.00145.52           C  
ANISOU 4034  CD2 PHE A 579    20408  18594  16287   1542    122   1068       C  
ATOM   4035  CE1 PHE A 579     -17.763 -33.390  71.167  1.00144.27           C  
ANISOU 4035  CE1 PHE A 579    19898  18823  16093   1578    -17   1185       C  
ATOM   4036  CE2 PHE A 579     -17.815 -35.326  69.718  1.00144.60           C  
ANISOU 4036  CE2 PHE A 579    20295  18552  16093   1777    163   1176       C  
ATOM   4037  CZ  PHE A 579     -17.310 -34.679  70.843  1.00143.77           C  
ANISOU 4037  CZ  PHE A 579    19997  18658  15968   1798     89   1239       C  
ATOM   4038  N   ASN A 580     -21.482 -30.914  70.707  1.00104.23           N  
ANISOU 4038  N   ASN A 580    14820  13539  11243    903   -166    936       N  
ATOM   4039  CA  ASN A 580     -21.315 -30.377  72.055  1.00102.37           C  
ANISOU 4039  CA  ASN A 580    14498  13401  10997    890   -215    974       C  
ATOM   4040  C   ASN A 580     -22.592 -29.900  72.746  1.00101.25           C  
ANISOU 4040  C   ASN A 580    14379  13201  10887    749   -247    941       C  
ATOM   4041  O   ASN A 580     -22.513 -29.460  73.905  1.00102.77           O  
ANISOU 4041  O   ASN A 580    14513  13465  11068    730   -283    967       O  
ATOM   4042  CB  ASN A 580     -20.320 -29.240  72.029  1.00101.28           C  
ANISOU 4042  CB  ASN A 580    14187  13452  10841    871   -260    980       C  
ATOM   4043  CG  ASN A 580     -18.913 -29.721  71.920  1.00108.09           C  
ANISOU 4043  CG  ASN A 580    14978  14454  11635   1030   -240   1042       C  
ATOM   4044  OD1 ASN A 580     -18.394 -30.333  72.856  1.00119.47           O  
ANISOU 4044  OD1 ASN A 580    16408  15964  13020   1149   -230   1114       O  
ATOM   4045  ND2 ASN A 580     -18.286 -29.490  70.765  1.00111.13           N  
ANISOU 4045  ND2 ASN A 580    15310  14898  12014   1052   -229   1024       N  
ATOM   4046  N   GLN A 581     -23.757 -29.983  72.090  1.00 98.97           N  
ANISOU 4046  N   GLN A 581    14166  12812  10625    651   -232    890       N  
ATOM   4047  CA  GLN A 581     -24.965 -29.511  72.797  1.00 94.57           C  
ANISOU 4047  CA  GLN A 581    13610  12242  10079    539   -260    872       C  
ATOM   4048  C   GLN A 581     -25.356 -30.296  74.031  1.00 92.35           C  
ANISOU 4048  C   GLN A 581    13405  11908   9774    548   -254    905       C  
ATOM   4049  O   GLN A 581     -25.814 -29.705  75.008  1.00 89.80           O  
ANISOU 4049  O   GLN A 581    13036  11629   9454    497   -290    911       O  
ATOM   4050  CB  GLN A 581     -26.160 -29.412  71.877  1.00 95.49           C  
ANISOU 4050  CB  GLN A 581    13759  12322  10201    434   -248    822       C  
ATOM   4051  CG  GLN A 581     -27.418 -28.816  72.530  1.00 93.53           C  
ANISOU 4051  CG  GLN A 581    13485  12105   9946    341   -273    813       C  
ATOM   4052  CD  GLN A 581     -28.178 -27.890  71.568  1.00 94.67           C  
ANISOU 4052  CD  GLN A 581    13568  12312  10090    284   -276    785       C  
ATOM   4053  OE1 GLN A 581     -27.764 -27.608  70.412  1.00 98.21           O  
ANISOU 4053  OE1 GLN A 581    13988  12774  10550    299   -265    768       O  
ATOM   4054  NE2 GLN A 581     -29.346 -27.470  72.016  1.00 94.66           N  
ANISOU 4054  NE2 GLN A 581    13544  12358  10062    228   -286    787       N  
ATOM   4055  N   ALA A 582     -25.163 -31.609  74.009  1.00 92.67           N  
ANISOU 4055  N   ALA A 582    13577  11848   9783    617   -199    928       N  
ATOM   4056  CA  ALA A 582     -25.565 -32.455  75.114  1.00 89.66           C  
ANISOU 4056  CA  ALA A 582    13301  11395   9371    625   -179    963       C  
ATOM   4057  C   ALA A 582     -24.888 -32.049  76.403  1.00 90.31           C  
ANISOU 4057  C   ALA A 582    13284  11584   9446    698   -222   1022       C  
ATOM   4058  O   ALA A 582     -25.540 -31.947  77.431  1.00 92.09           O  
ANISOU 4058  O   ALA A 582    13510  11814   9666    637   -246   1031       O  
ATOM   4059  CB  ALA A 582     -25.230 -33.877  74.782  1.00 92.71           C  
ANISOU 4059  CB  ALA A 582    13874  11639   9712    717    -92    987       C  
ATOM   4060  N   GLU A 583     -23.590 -31.781  76.344  1.00 94.09           N  
ANISOU 4060  N   GLU A 583    13665  12173   9911    815   -231   1062       N  
ATOM   4061  CA  GLU A 583     -22.879 -31.289  77.526  1.00 96.92           C  
ANISOU 4061  CA  GLU A 583    13901  12684  10239    857   -275   1114       C  
ATOM   4062  C   GLU A 583     -23.403 -29.924  77.916  1.00 94.23           C  
ANISOU 4062  C   GLU A 583    13459  12416   9928    705   -334   1063       C  
ATOM   4063  O   GLU A 583     -23.535 -29.636  79.093  1.00 96.09           O  
ANISOU 4063  O   GLU A 583    13656  12708  10143    671   -363   1082       O  
ATOM   4064  CB  GLU A 583     -21.367 -31.233  77.325  1.00103.79           C  
ANISOU 4064  CB  GLU A 583    14658  13715  11059    992   -273   1167       C  
ATOM   4065  CG  GLU A 583     -20.600 -32.285  78.131  1.00114.38           C  
ANISOU 4065  CG  GLU A 583    16029  15104  12325   1185   -235   1271       C  
ATOM   4066  CD  GLU A 583     -20.432 -31.878  79.606  1.00122.09           C  
ANISOU 4066  CD  GLU A 583    16898  16231  13258   1158   -285   1315       C  
ATOM   4067  OE1 GLU A 583     -20.691 -32.703  80.558  1.00130.14           O  
ANISOU 4067  OE1 GLU A 583    18004  17195  14245   1233   -260   1376       O  
ATOM   4068  OE2 GLU A 583     -20.042 -30.701  79.795  1.00123.37           O  
ANISOU 4068  OE2 GLU A 583    16901  16562  13409   1049   -342   1284       O  
ATOM   4069  N   TRP A 584     -23.719 -29.071  76.935  1.00 89.79           N  
ANISOU 4069  N   TRP A 584    12865  11844   9404    620   -343   1002       N  
ATOM   4070  CA  TRP A 584     -24.196 -27.719  77.263  1.00 86.27           C  
ANISOU 4070  CA  TRP A 584    12358  11446   8973    501   -377    961       C  
ATOM   4071  C   TRP A 584     -25.505 -27.735  78.045  1.00 85.93           C  
ANISOU 4071  C   TRP A 584    12371  11340   8938    434   -383    950       C  
ATOM   4072  O   TRP A 584     -25.731 -26.822  78.853  1.00 83.99           O  
ANISOU 4072  O   TRP A 584    12087  11142   8682    373   -404    938       O  
ATOM   4073  CB  TRP A 584     -24.374 -26.860  76.025  1.00 85.91           C  
ANISOU 4073  CB  TRP A 584    12295  11387   8957    448   -370    911       C  
ATOM   4074  CG  TRP A 584     -23.181 -26.688  75.220  1.00 85.15           C  
ANISOU 4074  CG  TRP A 584    12138  11365   8850    490   -366    914       C  
ATOM   4075  CD1 TRP A 584     -21.915 -26.657  75.663  1.00 86.52           C  
ANISOU 4075  CD1 TRP A 584    12225  11674   8971    532   -379    950       C  
ATOM   4076  CD2 TRP A 584     -23.126 -26.440  73.809  1.00 84.19           C  
ANISOU 4076  CD2 TRP A 584    12015  11219   8752    485   -348    883       C  
ATOM   4077  NE1 TRP A 584     -21.054 -26.451  74.622  1.00 88.23           N  
ANISOU 4077  NE1 TRP A 584    12387  11956   9177    555   -371    943       N  
ATOM   4078  CE2 TRP A 584     -21.776 -26.318  73.473  1.00 86.02           C  
ANISOU 4078  CE2 TRP A 584    12167  11565   8951    528   -352    900       C  
ATOM   4079  CE3 TRP A 584     -24.085 -26.322  72.802  1.00 82.82           C  
ANISOU 4079  CE3 TRP A 584    11889  10964   8612    448   -331    847       C  
ATOM   4080  CZ2 TRP A 584     -21.346 -26.101  72.190  1.00 87.17           C  
ANISOU 4080  CZ2 TRP A 584    12289  11726   9106    536   -338    879       C  
ATOM   4081  CZ3 TRP A 584     -23.663 -26.118  71.529  1.00 83.23           C  
ANISOU 4081  CZ3 TRP A 584    11919  11029   8674    458   -317    828       C  
ATOM   4082  CH2 TRP A 584     -22.304 -25.992  71.235  1.00 86.07           C  
ANISOU 4082  CH2 TRP A 584    12209  11482   9010    500   -320    842       C  
ATOM   4083  N   GLU A 585     -26.359 -28.738  77.745  1.00 85.84           N  
ANISOU 4083  N   GLU A 585    12455  11226   8932    433   -357    948       N  
ATOM   4084  CA  GLU A 585     -27.610 -28.965  78.443  1.00 87.83           C  
ANISOU 4084  CA  GLU A 585    12756  11442   9172    363   -360    943       C  
ATOM   4085  C   GLU A 585     -27.379 -29.515  79.820  1.00 92.05           C  
ANISOU 4085  C   GLU A 585    13309  11985   9678    396   -370    991       C  
ATOM   4086  O   GLU A 585     -28.084 -29.091  80.752  1.00 93.91           O  
ANISOU 4086  O   GLU A 585    13526  12251   9904    337   -391    988       O  
ATOM   4087  CB  GLU A 585     -28.567 -29.887  77.682  1.00 88.83           C  
ANISOU 4087  CB  GLU A 585    12980  11484   9284    309   -324    921       C  
ATOM   4088  CG  GLU A 585     -29.378 -29.148  76.615  1.00 92.79           C  
ANISOU 4088  CG  GLU A 585    13437  12025   9792    240   -324    876       C  
ATOM   4089  CD  GLU A 585     -30.415 -30.008  75.845  1.00 97.62           C  
ANISOU 4089  CD  GLU A 585    14123  12605  10360    146   -290    847       C  
ATOM   4090  OE1 GLU A 585     -30.386 -31.254  75.903  1.00108.94           O  
ANISOU 4090  OE1 GLU A 585    15682  13944  11763    125   -253    850       O  
ATOM   4091  OE2 GLU A 585     -31.288 -29.460  75.154  1.00 96.12           O  
ANISOU 4091  OE2 GLU A 585    13877  12494  10149     85   -292    823       O  
ATOM   4092  N   ARG A 586     -26.444 -30.463  79.941  1.00 95.14           N  
ANISOU 4092  N   ARG A 586    13742  12356  10049    503   -347   1041       N  
ATOM   4093  CA  ARG A 586     -26.068 -31.054  81.233  1.00 98.70           C  
ANISOU 4093  CA  ARG A 586    14208  12832  10460    568   -349   1106       C  
ATOM   4094  C   ARG A 586     -25.516 -30.011  82.139  1.00 95.57           C  
ANISOU 4094  C   ARG A 586    13675  12588  10049    549   -399   1115       C  
ATOM   4095  O   ARG A 586     -25.743 -30.045  83.337  1.00 98.54           O  
ANISOU 4095  O   ARG A 586    14040  13002  10399    531   -417   1141       O  
ATOM   4096  CB  ARG A 586     -24.994 -32.150  81.075  1.00107.25           C  
ANISOU 4096  CB  ARG A 586    15352  13892  11506    734   -303   1176       C  
ATOM   4097  CG  ARG A 586     -25.489 -33.436  80.420  1.00117.31           C  
ANISOU 4097  CG  ARG A 586    16825  14977  12768    756   -228   1175       C  
ATOM   4098  CD  ARG A 586     -25.718 -34.620  81.364  1.00127.14           C  
ANISOU 4098  CD  ARG A 586    18224  16121  13960    811   -179   1239       C  
ATOM   4099  NE  ARG A 586     -24.834 -34.890  82.532  1.00130.90           N  
ANISOU 4099  NE  ARG A 586    18656  16693  14386    962   -182   1339       N  
ATOM   4100  CZ  ARG A 586     -25.055 -34.527  83.812  1.00127.23           C  
ANISOU 4100  CZ  ARG A 586    18112  16323  13907    921   -231   1365       C  
ATOM   4101  NH1 ARG A 586     -24.219 -34.930  84.743  1.00117.85           N  
ANISOU 4101  NH1 ARG A 586    16892  15228  12656   1072   -223   1464       N  
ATOM   4102  NH2 ARG A 586     -26.090 -33.763  84.187  1.00130.98           N  
ANISOU 4102  NH2 ARG A 586    18532  16816  14417    744   -284   1299       N  
ATOM   4103  N   SER A 587     -24.740 -29.105  81.565  1.00 94.58           N  
ANISOU 4103  N   SER A 587    13452  12554   9929    541   -415   1090       N  
ATOM   4104  CA  SER A 587     -24.079 -28.043  82.325  1.00 95.54           C  
ANISOU 4104  CA  SER A 587    13457  12830  10013    486   -450   1086       C  
ATOM   4105  C   SER A 587     -25.038 -27.042  82.839  1.00 92.70           C  
ANISOU 4105  C   SER A 587    13107  12445   9667    362   -464   1032       C  
ATOM   4106  O   SER A 587     -24.727 -26.333  83.804  1.00 95.06           O  
ANISOU 4106  O   SER A 587    13351  12844   9921    299   -483   1027       O  
ATOM   4107  CB  SER A 587     -23.048 -27.319  81.457  1.00 98.72           C  
ANISOU 4107  CB  SER A 587    13775  13329  10402    477   -452   1065       C  
ATOM   4108  OG  SER A 587     -21.953 -28.189  81.159  1.00103.34           O  
ANISOU 4108  OG  SER A 587    14321  13995  10948    617   -439   1129       O  
ATOM   4109  N   PHE A 588     -26.179 -26.941  82.158  1.00 91.96           N  
ANISOU 4109  N   PHE A 588    13081  12237   9620    327   -448    993       N  
ATOM   4110  CA  PHE A 588     -27.267 -26.029  82.545  1.00 89.41           C  
ANISOU 4110  CA  PHE A 588    12778  11892   9301    246   -446    953       C  
ATOM   4111  C   PHE A 588     -28.054 -26.660  83.657  1.00 87.65           C  
ANISOU 4111  C   PHE A 588    12586  11657   9060    237   -457    979       C  
ATOM   4112  O   PHE A 588     -28.299 -25.988  84.638  1.00 88.93           O  
ANISOU 4112  O   PHE A 588    12731  11861   9195    191   -466    968       O  
ATOM   4113  CB  PHE A 588     -28.173 -25.689  81.352  1.00 87.54           C  
ANISOU 4113  CB  PHE A 588    12575  11590   9097    234   -423    918       C  
ATOM   4114  CG  PHE A 588     -29.302 -24.770  81.693  1.00 87.30           C  
ANISOU 4114  CG  PHE A 588    12561  11558   9051    195   -408    895       C  
ATOM   4115  CD1 PHE A 588     -29.105 -23.430  81.798  1.00 88.42           C  
ANISOU 4115  CD1 PHE A 588    12711  11709   9175    170   -387    867       C  
ATOM   4116  CD2 PHE A 588     -30.582 -25.264  81.925  1.00 88.84           C  
ANISOU 4116  CD2 PHE A 588    12775  11748   9231    184   -407    905       C  
ATOM   4117  CE1 PHE A 588     -30.162 -22.592  82.128  1.00 88.85           C  
ANISOU 4117  CE1 PHE A 588    12802  11754   9202    170   -356    856       C  
ATOM   4118  CE2 PHE A 588     -31.654 -24.430  82.241  1.00 86.26           C  
ANISOU 4118  CE2 PHE A 588    12450  11452   8873    178   -387    896       C  
ATOM   4119  CZ  PHE A 588     -31.438 -23.090  82.350  1.00 86.53           C  
ANISOU 4119  CZ  PHE A 588    12503  11480   8894    189   -358    876       C  
ATOM   4120  N   ARG A 589     -28.428 -27.942  83.531  1.00 86.52           N  
ANISOU 4120  N   ARG A 589    12502  11449   8920    271   -447   1009       N  
ATOM   4121  CA  ARG A 589     -29.167 -28.592  84.610  1.00 85.81           C  
ANISOU 4121  CA  ARG A 589    12452  11346   8802    247   -453   1036       C  
ATOM   4122  C   ARG A 589     -28.374 -28.572  85.905  1.00 85.15           C  
ANISOU 4122  C   ARG A 589    12322  11345   8684    275   -476   1078       C  
ATOM   4123  O   ARG A 589     -28.905 -28.248  86.964  1.00 85.04           O  
ANISOU 4123  O   ARG A 589    12295  11370   8646    226   -492   1076       O  
ATOM   4124  CB  ARG A 589     -29.594 -30.014  84.303  1.00 87.69           C  
ANISOU 4124  CB  ARG A 589    12800  11487   9031    257   -423   1061       C  
ATOM   4125  CG  ARG A 589     -30.800 -30.360  85.135  1.00 93.76           C  
ANISOU 4125  CG  ARG A 589    13609  12250   9765    177   -425   1064       C  
ATOM   4126  CD  ARG A 589     -31.126 -31.820  85.148  1.00101.20           C  
ANISOU 4126  CD  ARG A 589    14689  13088  10672    160   -386   1093       C  
ATOM   4127  NE  ARG A 589     -32.104 -32.098  86.203  1.00107.46           N  
ANISOU 4127  NE  ARG A 589    15506  13902  11419     77   -394   1105       N  
ATOM   4128  CZ  ARG A 589     -32.523 -33.321  86.490  1.00115.49           C  
ANISOU 4128  CZ  ARG A 589    16662  14830  12386     30   -356   1131       C  
ATOM   4129  NH1 ARG A 589     -32.150 -34.397  85.752  1.00117.73           N  
ANISOU 4129  NH1 ARG A 589    17098  14977  12655     55   -295   1142       N  
ATOM   4130  NH2 ARG A 589     -33.350 -33.465  87.508  1.00121.22           N  
ANISOU 4130  NH2 ARG A 589    17392  15597  13067    -49   -368   1143       N  
ATOM   4131  N   ASP A 590     -27.105 -28.911  85.827  1.00 86.78           N  
ANISOU 4131  N   ASP A 590    12493  11604   8875    358   -476   1119       N  
ATOM   4132  CA  ASP A 590     -26.248 -28.867  87.002  1.00 88.89           C  
ANISOU 4132  CA  ASP A 590    12685  12003   9084    386   -499   1167       C  
ATOM   4133  C   ASP A 590     -26.163 -27.475  87.612  1.00 87.90           C  
ANISOU 4133  C   ASP A 590    12482  11981   8934    275   -524   1116       C  
ATOM   4134  O   ASP A 590     -25.980 -27.356  88.820  1.00 88.55           O  
ANISOU 4134  O   ASP A 590    12520  12161   8963    247   -543   1138       O  
ATOM   4135  CB  ASP A 590     -24.857 -29.408  86.673  1.00 91.48           C  
ANISOU 4135  CB  ASP A 590    12963  12419   9376    510   -491   1229       C  
ATOM   4136  CG  ASP A 590     -24.863 -30.909  86.413  1.00 95.82           C  
ANISOU 4136  CG  ASP A 590    13629  12855   9923    646   -446   1297       C  
ATOM   4137  OD1 ASP A 590     -25.673 -31.642  87.046  1.00 95.84           O  
ANISOU 4137  OD1 ASP A 590    13732  12761   9919    638   -431   1321       O  
ATOM   4138  OD2 ASP A 590     -24.019 -31.354  85.589  1.00102.40           O  
ANISOU 4138  OD2 ASP A 590    14464  13694  10746    761   -418   1328       O  
ATOM   4139  N   TYR A 591     -26.250 -26.443  86.784  1.00 86.32           N  
ANISOU 4139  N   TYR A 591    12281  11755   8761    213   -513   1050       N  
ATOM   4140  CA  TYR A 591     -26.249 -25.072  87.256  1.00 88.44           C  
ANISOU 4140  CA  TYR A 591    12531  12074   8996    102   -510    993       C  
ATOM   4141  C   TYR A 591     -27.564 -24.753  87.904  1.00 86.90           C  
ANISOU 4141  C   TYR A 591    12397  11810   8808     62   -500    968       C  
ATOM   4142  O   TYR A 591     -27.586 -24.152  88.958  1.00 92.75           O  
ANISOU 4142  O   TYR A 591    13131  12608   9499     -4   -501    951       O  
ATOM   4143  CB  TYR A 591     -25.979 -24.113  86.100  1.00 93.22           C  
ANISOU 4143  CB  TYR A 591    13152  12646   9621     63   -484    939       C  
ATOM   4144  CG  TYR A 591     -26.129 -22.635  86.410  1.00 97.56           C  
ANISOU 4144  CG  TYR A 591    13747  13188  10130    -51   -452    873       C  
ATOM   4145  CD1 TYR A 591     -25.235 -21.987  87.251  1.00101.09           C  
ANISOU 4145  CD1 TYR A 591    14158  13759  10490   -162   -453    852       C  
ATOM   4146  CD2 TYR A 591     -27.113 -21.879  85.803  1.00102.70           C  
ANISOU 4146  CD2 TYR A 591    14489  13718  10812    -48   -409    835       C  
ATOM   4147  CE1 TYR A 591     -25.331 -20.634  87.507  1.00106.02           C  
ANISOU 4147  CE1 TYR A 591    14870  14350  11062   -286   -404    783       C  
ATOM   4148  CE2 TYR A 591     -27.240 -20.527  86.067  1.00107.68           C  
ANISOU 4148  CE2 TYR A 591    15206  14313  11395   -130   -356    781       C  
ATOM   4149  CZ  TYR A 591     -26.349 -19.913  86.922  1.00110.06           C  
ANISOU 4149  CZ  TYR A 591    15503  14700  11612   -258   -349    749       C  
ATOM   4150  OH  TYR A 591     -26.485 -18.577  87.199  1.00120.21           O  
ANISOU 4150  OH  TYR A 591    16916  15921  12834   -356   -277    687       O  
ATOM   4151  N   VAL A 592     -28.665 -25.165  87.289  1.00 84.08           N  
ANISOU 4151  N   VAL A 592    12093  11353   8497     98   -488    968       N  
ATOM   4152  CA  VAL A 592     -30.024 -24.985  87.862  1.00 82.04           C  
ANISOU 4152  CA  VAL A 592    11873  11068   8230     75   -478    956       C  
ATOM   4153  C   VAL A 592     -30.146 -25.679  89.233  1.00 82.52           C  
ANISOU 4153  C   VAL A 592    11919  11177   8255     64   -505    996       C  
ATOM   4154  O   VAL A 592     -30.561 -25.069  90.194  1.00 82.76           O  
ANISOU 4154  O   VAL A 592    11950  11244   8248     20   -502    978       O  
ATOM   4155  CB  VAL A 592     -31.135 -25.519  86.898  1.00 80.83           C  
ANISOU 4155  CB  VAL A 592    11751  10854   8106    101   -465    959       C  
ATOM   4156  CG1 VAL A 592     -32.489 -25.644  87.579  1.00 81.60           C  
ANISOU 4156  CG1 VAL A 592    11859  10976   8169     76   -462    965       C  
ATOM   4157  CG2 VAL A 592     -31.268 -24.638  85.697  1.00 79.92           C  
ANISOU 4157  CG2 VAL A 592    11644  10710   8010    117   -434    924       C  
ATOM   4158  N   LEU A 593     -29.768 -26.945  89.295  1.00 84.14           N  
ANISOU 4158  N   LEU A 593    12128  11375   8466    112   -520   1051       N  
ATOM   4159  CA  LEU A 593     -29.816 -27.690  90.517  1.00 86.42           C  
ANISOU 4159  CA  LEU A 593    12416  11702   8716    116   -538   1102       C  
ATOM   4160  C   LEU A 593     -28.881 -27.114  91.555  1.00 90.55           C  
ANISOU 4160  C   LEU A 593    12864  12354   9187     93   -559   1109       C  
ATOM   4161  O   LEU A 593     -29.155 -27.187  92.740  1.00 91.90           O  
ANISOU 4161  O   LEU A 593    13022  12579   9316     63   -573   1127       O  
ATOM   4162  CB  LEU A 593     -29.424 -29.139  90.264  1.00 88.60           C  
ANISOU 4162  CB  LEU A 593    12742  11924   8995    198   -529   1169       C  
ATOM   4163  CG  LEU A 593     -30.440 -30.009  89.530  1.00 90.22           C  
ANISOU 4163  CG  LEU A 593    13051  12006   9221    180   -502   1165       C  
ATOM   4164  CD1 LEU A 593     -29.751 -31.282  89.088  1.00 92.61           C  
ANISOU 4164  CD1 LEU A 593    13440  12227   9518    272   -469   1222       C  
ATOM   4165  CD2 LEU A 593     -31.621 -30.376  90.412  1.00 91.36           C  
ANISOU 4165  CD2 LEU A 593    13234  12148   9330    107   -504   1172       C  
ATOM   4166  N   CYS A 594     -27.744 -26.589  91.129  1.00 98.53           N  
ANISOU 4166  N   CYS A 594    13818  13434  10183     94   -560   1097       N  
ATOM   4167  CA  CYS A 594     -26.783 -25.982  92.054  1.00106.96           C  
ANISOU 4167  CA  CYS A 594    14801  14665  11171     33   -577   1097       C  
ATOM   4168  C   CYS A 594     -27.396 -24.800  92.783  1.00107.40           C  
ANISOU 4168  C   CYS A 594    14887  14722  11197    -86   -563   1026       C  
ATOM   4169  O   CYS A 594     -27.213 -24.665  93.983  1.00108.82           O  
ANISOU 4169  O   CYS A 594    15028  15008  11308   -142   -577   1033       O  
ATOM   4170  CB  CYS A 594     -25.534 -25.545  91.289  1.00114.94           C  
ANISOU 4170  CB  CYS A 594    15746  15765  12158     25   -575   1086       C  
ATOM   4171  SG  CYS A 594     -24.242 -24.778  92.264  1.00126.65           S  
ANISOU 4171  SG  CYS A 594    17106  17506  13507    -93   -592   1078       S  
ATOM   4172  N   GLN A 595     -28.140 -23.969  92.059  1.00108.77           N  
ANISOU 4172  N   GLN A 595    15138  14778  11410   -112   -527    962       N  
ATOM   4173  CA  GLN A 595     -28.780 -22.800  92.645  1.00112.72           C  
ANISOU 4173  CA  GLN A 595    15704  15250  11873   -193   -489    898       C  
ATOM   4174  C   GLN A 595     -29.698 -23.170  93.837  1.00114.69           C  
ANISOU 4174  C   GLN A 595    15958  15517  12101   -190   -502    919       C  
ATOM   4175  O   GLN A 595     -29.662 -22.534  94.875  1.00123.76           O  
ANISOU 4175  O   GLN A 595    17118  16721  13183   -269   -489    888       O  
ATOM   4176  CB  GLN A 595     -29.553 -22.037  91.584  1.00113.66           C  
ANISOU 4176  CB  GLN A 595    15911  15240  12034   -163   -438    855       C  
ATOM   4177  CG  GLN A 595     -28.695 -21.546  90.426  1.00119.93           C  
ANISOU 4177  CG  GLN A 595    16713  16010  12843   -178   -419    829       C  
ATOM   4178  CD  GLN A 595     -27.993 -20.217  90.684  1.00127.56           C  
ANISOU 4178  CD  GLN A 595    17741  16993  13732   -307   -370    762       C  
ATOM   4179  OE1 GLN A 595     -26.772 -20.168  90.879  1.00132.69           O  
ANISOU 4179  OE1 GLN A 595    18326  17762  14326   -398   -390    756       O  
ATOM   4180  NE2 GLN A 595     -28.758 -19.128  90.651  1.00128.94           N  
ANISOU 4180  NE2 GLN A 595    18049  17056  13885   -316   -296    714       N  
ATOM   4181  N   ALA A 596     -30.488 -24.216  93.713  1.00113.10           N  
ANISOU 4181  N   ALA A 596    15754  15275  11943   -116   -523    969       N  
ATOM   4182  CA  ALA A 596     -31.322 -24.660  94.822  1.00117.96           C  
ANISOU 4182  CA  ALA A 596    16368  15919  12530   -124   -537    994       C  
ATOM   4183  C   ALA A 596     -30.568 -25.404  95.906  1.00118.03           C  
ANISOU 4183  C   ALA A 596    16315  16034  12494   -134   -577   1050       C  
ATOM   4184  O   ALA A 596     -30.918 -25.338  97.083  1.00117.13           O  
ANISOU 4184  O   ALA A 596    16190  15981  12332   -175   -585   1054       O  
ATOM   4185  CB  ALA A 596     -32.431 -25.554  94.305  1.00122.98           C  
ANISOU 4185  CB  ALA A 596    17030  16492  13205    -76   -540   1026       C  
ATOM   4186  N   ASN A 597     -29.581 -26.177  95.485  1.00123.52           N  
ANISOU 4186  N   ASN A 597    16971  16759  13201    -76   -596   1104       N  
ATOM   4187  CA  ASN A 597     -28.849 -27.064  96.380  1.00127.29           C  
ANISOU 4187  CA  ASN A 597    17389  17347  13626    -36   -625   1185       C  
ATOM   4188  C   ASN A 597     -27.908 -26.235  97.236  1.00123.21           C  
ANISOU 4188  C   ASN A 597    16783  17008  13021   -121   -638   1164       C  
ATOM   4189  O   ASN A 597     -27.618 -26.642  98.335  1.00131.11           O  
ANISOU 4189  O   ASN A 597    17727  18133  13956   -121   -660   1217       O  
ATOM   4190  CB  ASN A 597     -28.084 -28.125  95.545  1.00132.26           C  
ANISOU 4190  CB  ASN A 597    18018  17952  14280     86   -623   1257       C  
ATOM   4191  CG  ASN A 597     -27.475 -29.241  96.369  1.00138.34           C  
ANISOU 4191  CG  ASN A 597    18758  18810  14991    184   -634   1368       C  
ATOM   4192  OD1 ASN A 597     -27.943 -29.562  97.463  1.00137.43           O  
ANISOU 4192  OD1 ASN A 597    18650  18726  14840    165   -645   1400       O  
ATOM   4193  ND2 ASN A 597     -26.437 -29.881  95.806  1.00141.08           N  
ANISOU 4193  ND2 ASN A 597    19080  19199  15322    309   -623   1436       N  
ATOM   4194  N   VAL A 598     -27.441 -25.083  96.744  1.00120.36           N  
ANISOU 4194  N   VAL A 598    16419  16666  12644   -208   -617   1087       N  
ATOM   4195  CA  VAL A 598     -26.406 -24.316  97.450  1.00124.21           C  
ANISOU 4195  CA  VAL A 598    16827  17344  13021   -330   -622   1060       C  
ATOM   4196  C   VAL A 598     -27.002 -23.409  98.506  1.00128.75           C  
ANISOU 4196  C   VAL A 598    17453  17926  13539   -460   -600    990       C  
ATOM   4197  O   VAL A 598     -26.312 -23.080  99.491  1.00132.53           O  
ANISOU 4197  O   VAL A 598    17861  18588  13905   -571   -610    982       O  
ATOM   4198  CB  VAL A 598     -25.432 -23.551  96.493  1.00122.50           C  
ANISOU 4198  CB  VAL A 598    16591  17171  12782   -396   -603   1011       C  
ATOM   4199  CG1 VAL A 598     -26.012 -22.243  95.982  1.00119.35           C  
ANISOU 4199  CG1 VAL A 598    16324  16618  12405   -498   -545    901       C  
ATOM   4200  CG2 VAL A 598     -24.090 -23.307  97.181  1.00124.88           C  
ANISOU 4200  CG2 VAL A 598    16755  17752  12940   -502   -624   1025       C  
ATOM   4201  N   THR A 599     -28.273 -23.037  98.304  1.00133.65           N  
ANISOU 4201  N   THR A 599    18189  18368  14222   -442   -566    944       N  
ATOM   4202  CA  THR A 599     -29.053 -22.240  99.283  1.00136.80           C  
ANISOU 4202  CA  THR A 599    18659  18746  14570   -524   -531    884       C  
ATOM   4203  C   THR A 599     -29.355 -23.011 100.615  1.00133.11           C  
ANISOU 4203  C   THR A 599    18127  18384  14063   -515   -573    942       C  
ATOM   4204  O   THR A 599     -29.411 -22.421 101.675  1.00125.52           O  
ANISOU 4204  O   THR A 599    17176  17494  13019   -617   -557    901       O  
ATOM   4205  CB  THR A 599     -30.304 -21.538  98.615  1.00134.47           C  
ANISOU 4205  CB  THR A 599    18498  18261  14331   -474   -470    831       C  
ATOM   4206  OG1 THR A 599     -30.921 -20.654  99.535  1.00134.52           O  
ANISOU 4206  OG1 THR A 599    18589  18253  14270   -538   -419    773       O  
ATOM   4207  CG2 THR A 599     -31.382 -22.507  98.154  1.00135.18           C  
ANISOU 4207  CG2 THR A 599    18578  18277  14505   -344   -494    890       C  
ATOM   4208  N   ILE A 600     -29.482 -24.332 100.543  1.00137.88           N  
ANISOU 4208  N   ILE A 600    18679  18991  14716   -400   -617   1037       N  
ATOM   4209  CA  ILE A 600     -29.614 -25.201 101.737  1.00144.33           C  
ANISOU 4209  CA  ILE A 600    19440  19909  15490   -379   -654   1111       C  
ATOM   4210  C   ILE A 600     -28.289 -25.905 102.120  1.00157.94           C  
ANISOU 4210  C   ILE A 600    21042  21819  17146   -345   -692   1199       C  
ATOM   4211  O   ILE A 600     -27.387 -26.060 101.296  1.00168.73           O  
ANISOU 4211  O   ILE A 600    22367  23221  18521   -297   -695   1223       O  
ATOM   4212  CB  ILE A 600     -30.739 -26.267 101.568  1.00141.08           C  
ANISOU 4212  CB  ILE A 600    19080  19374  15147   -284   -662   1167       C  
ATOM   4213  CG1 ILE A 600     -30.453 -27.213 100.376  1.00141.36           C  
ANISOU 4213  CG1 ILE A 600    19153  19291  15265   -187   -657   1200       C  
ATOM   4214  CG2 ILE A 600     -32.096 -25.586 101.425  1.00139.92           C  
ANISOU 4214  CG2 ILE A 600    19002  19151  15009   -324   -633   1104       C  
ATOM   4215  CD1 ILE A 600     -31.382 -28.405 100.273  1.00142.22           C  
ANISOU 4215  CD1 ILE A 600    19304  19336  15396   -105   -666   1289       C  
ATOM   4216  N   GLY A 601     -28.193 -26.308 103.392  1.00169.20           N  
ANISOU 4216  N   GLY A 601    22404  23384  18496   -353   -718   1256       N  
ATOM   4217  CA  GLY A 601     -26.987 -26.986 103.906  1.00173.54           C  
ANISOU 4217  CA  GLY A 601    22825  24154  18957   -293   -748   1360       C  
ATOM   4218  C   GLY A 601     -25.808 -26.033 103.984  1.00179.80           C  
ANISOU 4218  C   GLY A 601    23506  25173  19636   -423   -752   1314       C  
ATOM   4219  O   GLY A 601     -24.665 -26.513 104.112  1.00182.01           O  
ANISOU 4219  O   GLY A 601    23658  25657  19838   -360   -772   1397       O  
ATOM   4220  N   LEU A 602     -26.084 -24.726 103.942  1.00183.39           N  
ANISOU 4220  N   LEU A 602    24016  25601  20062   -607   -723   1184       N  
ATOM   4221  CA  LEU A 602     -25.022 -23.685 103.979  1.00185.63           C  
ANISOU 4221  CA  LEU A 602    24233  26072  20223   -786   -711   1114       C  
ATOM   4222  C   LEU A 602     -25.241 -22.757 105.180  1.00191.23           C  
ANISOU 4222  C   LEU A 602    24960  26882  20816   -989   -691   1030       C  
ATOM   4223  O   LEU A 602     -26.399 -22.365 105.422  1.00187.32           O  
ANISOU 4223  O   LEU A 602    24589  26213  20369  -1004   -662    975       O  
ATOM   4224  CB  LEU A 602     -25.069 -22.900 102.665  1.00185.30           C  
ANISOU 4224  CB  LEU A 602    24299  25856  20248   -834   -666   1021       C  
ATOM   4225  CG  LEU A 602     -24.066 -21.753 102.552  1.00188.07           C  
ANISOU 4225  CG  LEU A 602    24625  26357  20473  -1048   -637    933       C  
ATOM   4226  CD1 LEU A 602     -22.689 -22.187 103.029  1.00192.41           C  
ANISOU 4226  CD1 LEU A 602    24959  27259  20889  -1063   -684   1016       C  
ATOM   4227  CD2 LEU A 602     -23.999 -21.232 101.125  1.00178.34           C  
ANISOU 4227  CD2 LEU A 602    23520  24906  19333  -1045   -591    864       C  
ATOM   4228  N   PRO A 603     -24.175 -22.363 105.913  1.00201.55           N  
ANISOU 4228  N   PRO A 603    26137  28491  21950  -1151   -702   1021       N  
ATOM   4229  CA  PRO A 603     -24.297 -21.465 107.069  1.00200.34           C  
ANISOU 4229  CA  PRO A 603    26008  28448  21662  -1376   -675    931       C  
ATOM   4230  C   PRO A 603     -24.790 -20.077 106.633  1.00201.44           C  
ANISOU 4230  C   PRO A 603    26368  28358  21809  -1545   -586    767       C  
ATOM   4231  O   PRO A 603     -24.465 -19.657 105.537  1.00215.08           O  
ANISOU 4231  O   PRO A 603    28162  29984  23573  -1567   -554    721       O  
ATOM   4232  CB  PRO A 603     -22.863 -21.349 107.609  1.00199.76           C  
ANISOU 4232  CB  PRO A 603    25730  28783  21386  -1522   -705    962       C  
ATOM   4233  CG  PRO A 603     -22.145 -22.549 107.034  1.00199.59           C  
ANISOU 4233  CG  PRO A 603    25551  28880  21403  -1293   -758   1111       C  
ATOM   4234  CD  PRO A 603     -22.790 -22.773 105.683  1.00201.40           C  
ANISOU 4234  CD  PRO A 603    25930  28761  21830  -1138   -737   1097       C  
ATOM   4235  N   THR A 604     -25.522 -19.388 107.513  1.00190.58           N  
ANISOU 4235  N   THR A 604    25115  26901  20393  -1647   -538    686       N  
ATOM   4236  CA  THR A 604     -26.097 -18.060 107.171  1.00179.49           C  
ANISOU 4236  CA  THR A 604    23963  25229  19003  -1743   -432    547       C  
ATOM   4237  C   THR A 604     -24.970 -17.088 106.811  1.00180.45           C  
ANISOU 4237  C   THR A 604    24152  25413  18998  -1988   -370    442       C  
ATOM   4238  O   THR A 604     -25.111 -16.437 105.763  1.00173.79           O  
ANISOU 4238  O   THR A 604    23472  24345  18216  -1978   -305    383       O  
ATOM   4239  CB  THR A 604     -26.894 -17.499 108.354  1.00171.77           C  
ANISOU 4239  CB  THR A 604    23111  24189  17963  -1824   -377    475       C  
ATOM   4240  OG1 THR A 604     -25.961 -17.173 109.384  1.00177.66           O  
ANISOU 4240  OG1 THR A 604    23830  25167  18505  -2105   -353    401       O  
ATOM   4241  CG2 THR A 604     -27.926 -18.470 108.884  1.00166.82           C  
ANISOU 4241  CG2 THR A 604    22380  23589  17414  -1639   -448    581       C  
ATOM   4242  N   LYS A 605     -23.887 -17.106 107.602  1.00189.05           N  
ANISOU 4242  N   LYS A 605    25104  26828  19896  -2211   -393    428       N  
ATOM   4243  CA  LYS A 605     -22.636 -16.288 107.527  1.00196.76           C  
ANISOU 4243  CA  LYS A 605    26089  27972  20698  -2504   -348    338       C  
ATOM   4244  C   LYS A 605     -22.627 -15.241 106.402  1.00198.12           C  
ANISOU 4244  C   LYS A 605    26491  27883  20901  -2583   -251    235       C  
ATOM   4245  O   LYS A 605     -23.272 -14.179 106.562  1.00206.67           O  
ANISOU 4245  O   LYS A 605    27857  28700  21968  -2674   -133    118       O  
ATOM   4246  CB  LYS A 605     -21.429 -17.216 107.355  1.00192.91           C  
ANISOU 4246  CB  LYS A 605    25282  27896  20117  -2504   -450    453       C  
ATOM   4247  CG  LYS A 605     -21.205 -18.213 108.484  1.00194.91           C  
ANISOU 4247  CG  LYS A 605    25335  28537  20183  -2636   -498    491       C  
ATOM   4248  CD  LYS A 605     -19.904 -18.977 108.354  1.00193.04           C  
ANISOU 4248  CD  LYS A 605    25236  28383  19728  -3033   -408    324       C  
ATOM   4249  CE  LYS A 605     -19.626 -19.882 109.535  1.00188.07           C  
ANISOU 4249  CE  LYS A 605    24348  28265  18845  -3245   -460    357       C  
ATOM   4250  NZ  LYS A 605     -18.298 -20.532 109.428  1.00186.33           N  
ANISOU 4250  NZ  LYS A 605    24292  28077  18427  -3611   -368    193       N  
ATOM   4251  N   GLN A 606     -21.797 -15.480 105.381  1.00187.07           N  
ANISOU 4251  N   GLN A 606    24980  26556  19542  -2527   -292    287       N  
ATOM   4252  CA  GLN A 606     -21.644 -14.584 104.201  1.00174.63           C  
ANISOU 4252  CA  GLN A 606    23586  24799  17966  -2633   -209    199       C  
ATOM   4253  C   GLN A 606     -22.733 -14.880 103.162  1.00165.58           C  
ANISOU 4253  C   GLN A 606    22579  23280  17051  -2339   -189    233       C  
ATOM   4254  O   GLN A 606     -23.420 -15.907 103.300  1.00152.62           O  
ANISOU 4254  O   GLN A 606    20886  21551  15549  -2092   -241    315       O  
ATOM   4255  CB  GLN A 606     -20.247 -14.720 103.592  1.00174.21           C  
ANISOU 4255  CB  GLN A 606    23318  25059  17812  -2741   -264    239       C  
ATOM   4256  CG  GLN A 606     -19.129 -14.292 104.532  1.00178.04           C  
ANISOU 4256  CG  GLN A 606    23719  25908  18018  -3116   -247    167       C  
ATOM   4257  CD  GLN A 606     -17.793 -14.224 103.835  1.00178.93           C  
ANISOU 4257  CD  GLN A 606    23716  26271  17996  -3307   -253    153       C  
ATOM   4258  OE1 GLN A 606     -17.710 -14.193 102.610  1.00175.56           O  
ANISOU 4258  OE1 GLN A 606    23384  25645  17673  -3230   -226    144       O  
ATOM   4259  NE2 GLN A 606     -16.728 -14.197 104.620  1.00182.52           N  
ANISOU 4259  NE2 GLN A 606    23948  27196  18202  -3561   -289    156       N  
ATOM   4260  N   PRO A 607     -22.908 -14.034 102.121  1.00169.84           N  
ANISOU 4260  N   PRO A 607    23293  23617  17622  -2372   -113    173       N  
ATOM   4261  CA  PRO A 607     -23.927 -14.252 101.082  1.00171.55           C  
ANISOU 4261  CA  PRO A 607    23617  23522  18041  -2091    -97    213       C  
ATOM   4262  C   PRO A 607     -23.794 -15.621 100.394  1.00169.43           C  
ANISOU 4262  C   PRO A 607    23105  23355  17915  -1849   -221    349       C  
ATOM   4263  O   PRO A 607     -22.679 -16.075 100.187  1.00162.60           O  
ANISOU 4263  O   PRO A 607    22035  22757  16986  -1905   -290    398       O  
ATOM   4264  CB  PRO A 607     -23.674 -13.126 100.067  1.00170.43           C  
ANISOU 4264  CB  PRO A 607    23695  23195  17862  -2214     11    123       C  
ATOM   4265  CG  PRO A 607     -22.264 -12.665 100.360  1.00168.38           C  
ANISOU 4265  CG  PRO A 607    23323  23225  17427  -2504     -5     84       C  
ATOM   4266  CD  PRO A 607     -22.109 -12.838 101.855  1.00171.23           C  
ANISOU 4266  CD  PRO A 607    23528  23880  17649  -2650    -56     88       C  
ATOM   4267  N   ILE A 608     -24.924 -16.213  99.990  1.00173.00           N  
ANISOU 4267  N   ILE A 608    23589  23604  18540  -1586   -237    408       N  
ATOM   4268  CA  ILE A 608     -24.895 -17.541  99.379  1.00172.11           C  
ANISOU 4268  CA  ILE A 608    23290  23546  18556  -1364   -337    530       C  
ATOM   4269  C   ILE A 608     -24.031 -17.466  98.114  1.00166.31           C  
ANISOU 4269  C   ILE A 608    22516  22833  17838  -1374   -341    534       C  
ATOM   4270  O   ILE A 608     -24.165 -16.506  97.329  1.00156.81           O  
ANISOU 4270  O   ILE A 608    21486  21451  16640  -1434   -261    459       O  
ATOM   4271  CB  ILE A 608     -26.285 -18.047  98.968  1.00169.39           C  
ANISOU 4271  CB  ILE A 608    23011  22976  18373  -1125   -340    575       C  
ATOM   4272  CG1 ILE A 608     -27.332 -17.756 100.043  1.00168.27           C  
ANISOU 4272  CG1 ILE A 608    22964  22762  18208  -1123   -303    546       C  
ATOM   4273  CG2 ILE A 608     -26.258 -19.546  98.697  1.00164.91           C  
ANISOU 4273  CG2 ILE A 608    22269  22484  17903   -937   -436    696       C  
ATOM   4274  CD1 ILE A 608     -28.735 -17.784  99.484  1.00166.43           C  
ANISOU 4274  CD1 ILE A 608    22835  22309  18089   -933   -270    562       C  
ATOM   4275  N   PRO A 609     -23.145 -18.471  97.921  1.00158.93           N  
ANISOU 4275  N   PRO A 609    21365  22119  16902  -1304   -426    626       N  
ATOM   4276  CA  PRO A 609     -22.201 -18.412  96.811  1.00151.16           C  
ANISOU 4276  CA  PRO A 609    20319  21205  15908  -1324   -432    633       C  
ATOM   4277  C   PRO A 609     -22.903 -18.711  95.504  1.00144.06           C  
ANISOU 4277  C   PRO A 609    19498  20054  15181  -1125   -424    657       C  
ATOM   4278  O   PRO A 609     -23.756 -19.585  95.439  1.00141.53           O  
ANISOU 4278  O   PRO A 609    19169  19623  14981   -927   -457    721       O  
ATOM   4279  CB  PRO A 609     -21.178 -19.497  97.160  1.00151.99           C  
ANISOU 4279  CB  PRO A 609    20167  21633  15948  -1257   -518    744       C  
ATOM   4280  CG  PRO A 609     -21.937 -20.477  97.991  1.00151.76           C  
ANISOU 4280  CG  PRO A 609    20099  21577  15984  -1088   -561    823       C  
ATOM   4281  CD  PRO A 609     -22.928 -19.667  98.770  1.00156.51           C  
ANISOU 4281  CD  PRO A 609    20868  22017  16579  -1197   -509    735       C  
ATOM   4282  N   ASP A 610     -22.565 -17.958  94.480  1.00144.08           N  
ANISOU 4282  N   ASP A 610    19585  19975  15181  -1198   -376    601       N  
ATOM   4283  CA  ASP A 610     -23.127 -18.183  93.148  1.00144.53           C  
ANISOU 4283  CA  ASP A 610    19703  19824  15385  -1025   -367    623       C  
ATOM   4284  C   ASP A 610     -22.473 -19.412  92.508  1.00135.94           C  
ANISOU 4284  C   ASP A 610    18431  18868  14350   -871   -444    721       C  
ATOM   4285  O   ASP A 610     -21.343 -19.738  92.805  1.00134.74           O  
ANISOU 4285  O   ASP A 610    18120  18975  14098   -924   -483    758       O  
ATOM   4286  CB  ASP A 610     -22.931 -16.940  92.274  1.00146.62           C  
ANISOU 4286  CB  ASP A 610    20128  19961  15618  -1154   -283    536       C  
ATOM   4287  CG  ASP A 610     -21.529 -16.391  92.368  1.00151.38           C  
ANISOU 4287  CG  ASP A 610    20666  20789  16060  -1394   -276    492       C  
ATOM   4288  OD1 ASP A 610     -20.807 -16.785  93.332  1.00154.27           O  
ANISOU 4288  OD1 ASP A 610    20871  21425  16316  -1482   -327    519       O  
ATOM   4289  OD2 ASP A 610     -21.160 -15.570  91.498  1.00151.33           O  
ANISOU 4289  OD2 ASP A 610    20764  20709  16024  -1500   -217    436       O  
ATOM   4290  N   CYS A 611     -23.213 -20.074  91.637  1.00126.48           N  
ANISOU 4290  N   CYS A 611    17263  17499  13293   -679   -454    763       N  
ATOM   4291  CA  CYS A 611     -22.761 -21.255  90.918  1.00124.34           C  
ANISOU 4291  CA  CYS A 611    16874  17287  13081   -515   -504    849       C  
ATOM   4292  C   CYS A 611     -22.246 -20.861  89.550  1.00119.89           C  
ANISOU 4292  C   CYS A 611    16324  16686  12540   -524   -482    823       C  
ATOM   4293  O   CYS A 611     -22.360 -19.711  89.175  1.00121.70           O  
ANISOU 4293  O   CYS A 611    16668  16822  12751   -649   -428    743       O  
ATOM   4294  CB  CYS A 611     -23.945 -22.188  90.715  1.00126.96           C  
ANISOU 4294  CB  CYS A 611    17258  17440  13537   -337   -516    895       C  
ATOM   4295  SG  CYS A 611     -24.709 -22.763  92.227  1.00133.52           S  
ANISOU 4295  SG  CYS A 611    18085  18292  14352   -313   -540    933       S  
ATOM   4296  N   GLU A 612     -21.736 -21.829  88.790  1.00115.42           N  
ANISOU 4296  N   GLU A 612    15663  16174  12016   -381   -515    892       N  
ATOM   4297  CA  GLU A 612     -21.210 -21.587  87.457  1.00114.58           C  
ANISOU 4297  CA  GLU A 612    15553  16048  11933   -374   -500    875       C  
ATOM   4298  C   GLU A 612     -21.753 -22.596  86.464  1.00112.12           C  
ANISOU 4298  C   GLU A 612    15266  15587  11745   -177   -508    923       C  
ATOM   4299  O   GLU A 612     -22.377 -23.589  86.838  1.00110.64           O  
ANISOU 4299  O   GLU A 612    15091  15336  11609    -54   -525    976       O  
ATOM   4300  CB  GLU A 612     -19.699 -21.716  87.474  1.00124.31           C  
ANISOU 4300  CB  GLU A 612    16616  17572  13044   -417   -525    912       C  
ATOM   4301  CG  GLU A 612     -19.003 -20.804  88.459  1.00136.13           C  
ANISOU 4301  CG  GLU A 612    18063  19279  14380   -649   -519    865       C  
ATOM   4302  CD  GLU A 612     -17.500 -21.067  88.543  1.00146.58           C  
ANISOU 4302  CD  GLU A 612    19173  20967  15553   -684   -552    919       C  
ATOM   4303  OE1 GLU A 612     -16.869 -21.352  87.491  1.00148.45           O  
ANISOU 4303  OE1 GLU A 612    19340  21262  15799   -603   -557    950       O  
ATOM   4304  OE2 GLU A 612     -16.946 -20.975  89.675  1.00152.82           O  
ANISOU 4304  OE2 GLU A 612    19853  22011  16200   -793   -571    934       O  
ATOM   4305  N   ILE A 613     -21.494 -22.335  85.182  1.00109.52           N  
ANISOU 4305  N   ILE A 613    14953  15205  11453   -166   -490    901       N  
ATOM   4306  CA  ILE A 613     -21.890 -23.198  84.074  1.00105.45           C  
ANISOU 4306  CA  ILE A 613    14464  14562  11038    -10   -489    932       C  
ATOM   4307  C   ILE A 613     -20.587 -23.724  83.502  1.00101.92           C  
ANISOU 4307  C   ILE A 613    13897  14284  10543     57   -504    981       C  
ATOM   4308  O   ILE A 613     -19.807 -22.964  82.994  1.00 98.86           O  
ANISOU 4308  O   ILE A 613    13464  13994  10101    -39   -495    948       O  
ATOM   4309  CB  ILE A 613     -22.689 -22.381  83.004  1.00107.43           C  
ANISOU 4309  CB  ILE A 613    14829  14629  11358    -46   -450    869       C  
ATOM   4310  CG1 ILE A 613     -23.931 -21.686  83.634  1.00108.39           C  
ANISOU 4310  CG1 ILE A 613    15063  14623  11497    -98   -422    829       C  
ATOM   4311  CG2 ILE A 613     -23.141 -23.262  81.831  1.00108.66           C  
ANISOU 4311  CG2 ILE A 613    15008  14674  11604     87   -448    894       C  
ATOM   4312  CD1 ILE A 613     -23.838 -20.170  83.759  1.00109.23           C  
ANISOU 4312  CD1 ILE A 613    15256  14703  11543   -246   -371    761       C  
ATOM   4313  N   LYS A 614     -20.346 -25.023  83.604  1.00102.08           N  
ANISOU 4313  N   LYS A 614    13876  14340  10568    227   -516   1063       N  
ATOM   4314  CA  LYS A 614     -19.158 -25.642  83.026  1.00104.73           C  
ANISOU 4314  CA  LYS A 614    14105  14835  10850    345   -517   1125       C  
ATOM   4315  C   LYS A 614     -18.864 -25.186  81.563  1.00102.05           C  
ANISOU 4315  C   LYS A 614    13773  14453  10547    323   -499   1080       C  
ATOM   4316  O   LYS A 614     -17.749 -24.797  81.247  1.00102.60           O  
ANISOU 4316  O   LYS A 614    13726  14724  10531    282   -505   1086       O  
ATOM   4317  CB  LYS A 614     -19.336 -27.169  83.011  1.00109.60           C  
ANISOU 4317  CB  LYS A 614    14770  15370  11500    567   -501   1211       C  
ATOM   4318  CG  LYS A 614     -18.933 -27.944  84.212  1.00117.88           C  
ANISOU 4318  CG  LYS A 614    15762  16559  12468    673   -509   1305       C  
ATOM   4319  CD  LYS A 614     -19.173 -29.420  83.877  1.00129.55           C  
ANISOU 4319  CD  LYS A 614    17355  17883  13983    894   -464   1380       C  
ATOM   4320  CE  LYS A 614     -19.217 -30.354  85.094  1.00141.97           C  
ANISOU 4320  CE  LYS A 614    18950  19489  15501   1016   -455   1477       C  
ATOM   4321  NZ  LYS A 614     -20.457 -30.212  85.925  1.00141.36           N  
ANISOU 4321  NZ  LYS A 614    18967  19261  15480    895   -472   1433       N  
ATOM   4322  N   ASN A 615     -19.840 -25.343  80.675  1.00 98.34           N  
ANISOU 4322  N   ASN A 615    13427  13747  10188    355   -478   1044       N  
ATOM   4323  CA  ASN A 615     -19.664 -25.068  79.264  1.00 99.85           C  
ANISOU 4323  CA  ASN A 615    13632  13887  10419    356   -460   1010       C  
ATOM   4324  C   ASN A 615     -20.922 -24.536  78.613  1.00 98.00           C  
ANISOU 4324  C   ASN A 615    13521  13436  10276    295   -440    946       C  
ATOM   4325  O   ASN A 615     -22.033 -24.774  79.105  1.00101.49           O  
ANISOU 4325  O   ASN A 615    14043  13755  10763    300   -438    941       O  
ATOM   4326  CB  ASN A 615     -19.127 -26.292  78.472  1.00102.50           C  
ANISOU 4326  CB  ASN A 615    13952  14230  10762    544   -442   1070       C  
ATOM   4327  CG  ASN A 615     -19.688 -27.638  78.934  1.00102.68           C  
ANISOU 4327  CG  ASN A 615    14065  14135  10812    691   -424   1126       C  
ATOM   4328  OD1 ASN A 615     -20.820 -27.958  78.666  1.00104.86           O  
ANISOU 4328  OD1 ASN A 615    14466  14212  11162    678   -408   1095       O  
ATOM   4329  ND2 ASN A 615     -18.854 -28.459  79.559  1.00106.95           N  
ANISOU 4329  ND2 ASN A 615    14546  14813  11274    835   -418   1215       N  
ATOM   4330  N   ARG A 616     -20.715 -23.824  77.503  1.00 94.09           N  
ANISOU 4330  N   ARG A 616    13030  12924   9795    243   -424    905       N  
ATOM   4331  CA  ARG A 616     -21.780 -23.201  76.746  1.00 92.59           C  
ANISOU 4331  CA  ARG A 616    12938  12569   9670    203   -398    857       C  
ATOM   4332  C   ARG A 616     -21.436 -23.145  75.235  1.00 95.02           C  
ANISOU 4332  C   ARG A 616    13237  12862  10004    231   -382    844       C  
ATOM   4333  O   ARG A 616     -20.282 -23.405  74.853  1.00 99.16           O  
ANISOU 4333  O   ARG A 616    13675  13513  10487    260   -390    864       O  
ATOM   4334  CB  ARG A 616     -22.042 -21.808  77.296  1.00 91.60           C  
ANISOU 4334  CB  ARG A 616    12866  12428   9509     64   -378    812       C  
ATOM   4335  CG  ARG A 616     -20.958 -20.809  77.002  1.00 93.93           C  
ANISOU 4335  CG  ARG A 616    13131  12827   9731    -59   -363    781       C  
ATOM   4336  CD  ARG A 616     -21.229 -19.491  77.687  1.00 96.36           C  
ANISOU 4336  CD  ARG A 616    13539  13089   9984   -208   -323    732       C  
ATOM   4337  NE  ARG A 616     -20.126 -18.562  77.437  1.00 99.82           N  
ANISOU 4337  NE  ARG A 616    13967  13632  10327   -368   -299    695       N  
ATOM   4338  CZ  ARG A 616     -20.215 -17.237  77.434  1.00103.66           C  
ANISOU 4338  CZ  ARG A 616    14591  14035  10758   -515   -234    641       C  
ATOM   4339  NH1 ARG A 616     -19.137 -16.519  77.141  1.00107.15           N  
ANISOU 4339  NH1 ARG A 616    15023  14588  11099   -683   -212    606       N  
ATOM   4340  NH2 ARG A 616     -21.373 -16.620  77.682  1.00105.43           N  
ANISOU 4340  NH2 ARG A 616    14976  14070  11013   -492   -181    623       N  
ATOM   4341  N   PRO A 617     -22.426 -22.809  74.370  1.00 93.21           N  
ANISOU 4341  N   PRO A 617    13082  12503   9830    229   -358    816       N  
ATOM   4342  CA  PRO A 617     -22.087 -22.724  72.975  1.00 93.73           C  
ANISOU 4342  CA  PRO A 617    13133  12565   9913    248   -343    804       C  
ATOM   4343  C   PRO A 617     -21.067 -21.594  72.650  1.00 98.46           C  
ANISOU 4343  C   PRO A 617    13700  13254  10457    147   -331    781       C  
ATOM   4344  O   PRO A 617     -21.075 -20.541  73.321  1.00101.35           O  
ANISOU 4344  O   PRO A 617    14110  13619  10778     36   -314    757       O  
ATOM   4345  CB  PRO A 617     -23.440 -22.470  72.316  1.00 94.47           C  
ANISOU 4345  CB  PRO A 617    13303  12538  10054    257   -319    788       C  
ATOM   4346  CG  PRO A 617     -24.487 -22.793  73.321  1.00 92.07           C  
ANISOU 4346  CG  PRO A 617    13038  12184   9757    267   -325    798       C  
ATOM   4347  CD  PRO A 617     -23.854 -22.520  74.615  1.00 92.47           C  
ANISOU 4347  CD  PRO A 617    13069  12296   9767    221   -342    804       C  
ATOM   4348  N   SER A 618     -20.206 -21.811  71.646  1.00 99.83           N  
ANISOU 4348  N   SER A 618    13810  13500  10620    173   -332    785       N  
ATOM   4349  CA  SER A 618     -19.150 -20.837  71.306  1.00 97.77           C  
ANISOU 4349  CA  SER A 618    13507  13353  10289     57   -322    764       C  
ATOM   4350  C   SER A 618     -19.688 -19.757  70.430  1.00 96.00           C  
ANISOU 4350  C   SER A 618    13380  13012  10082     -7   -278    731       C  
ATOM   4351  O   SER A 618     -20.249 -20.065  69.378  1.00 98.73           O  
ANISOU 4351  O   SER A 618    13744  13279  10487     73   -269    735       O  
ATOM   4352  CB  SER A 618     -18.022 -21.510  70.553  1.00 97.82           C  
ANISOU 4352  CB  SER A 618    13396  13504  10265    124   -337    789       C  
ATOM   4353  OG  SER A 618     -17.079 -20.539  70.164  1.00 97.33           O  
ANISOU 4353  OG  SER A 618    13291  13564  10124    -10   -326    766       O  
ATOM   4354  N   LEU A 619     -19.534 -18.502  70.844  1.00 95.96           N  
ANISOU 4354  N   LEU A 619    13451  12993  10014   -152   -243    700       N  
ATOM   4355  CA  LEU A 619     -20.028 -17.358  70.032  1.00 96.81           C  
ANISOU 4355  CA  LEU A 619    13689  12970  10122   -200   -179    679       C  
ATOM   4356  C   LEU A 619     -19.162 -17.089  68.799  1.00 96.92           C  
ANISOU 4356  C   LEU A 619    13661  13053  10110   -243   -170    671       C  
ATOM   4357  O   LEU A 619     -19.628 -16.530  67.805  1.00100.66           O  
ANISOU 4357  O   LEU A 619    14214  13426  10606   -222   -127    671       O  
ATOM   4358  CB  LEU A 619     -20.116 -16.091  70.847  1.00 96.94           C  
ANISOU 4358  CB  LEU A 619    13850  12917  10063   -342   -120    646       C  
ATOM   4359  CG  LEU A 619     -21.132 -16.164  71.972  1.00 99.63           C  
ANISOU 4359  CG  LEU A 619    14257  13170  10427   -292   -115    652       C  
ATOM   4360  CD1 LEU A 619     -20.450 -15.659  73.254  1.00105.14           C  
ANISOU 4360  CD1 LEU A 619    14979  13940  11026   -461   -107    618       C  
ATOM   4361  CD2 LEU A 619     -22.410 -15.413  71.674  1.00 98.02           C  
ANISOU 4361  CD2 LEU A 619    14211  12786  10246   -214    -44    663       C  
ATOM   4362  N   LEU A 620     -17.905 -17.490  68.865  1.00 95.98           N  
ANISOU 4362  N   LEU A 620    13408  13125   9932   -294   -207    672       N  
ATOM   4363  CA  LEU A 620     -17.026 -17.435  67.726  1.00 93.75           C  
ANISOU 4363  CA  LEU A 620    13053  12946   9621   -319   -208    671       C  
ATOM   4364  C   LEU A 620     -17.567 -18.385  66.683  1.00 93.63           C  
ANISOU 4364  C   LEU A 620    13000  12868   9704   -139   -225    695       C  
ATOM   4365  O   LEU A 620     -17.643 -18.008  65.503  1.00 95.07           O  
ANISOU 4365  O   LEU A 620    13212  13007   9903   -138   -199    688       O  
ATOM   4366  CB  LEU A 620     -15.628 -17.873  68.117  1.00 92.85           C  
ANISOU 4366  CB  LEU A 620    12769  13097   9411   -370   -249    683       C  
ATOM   4367  CG  LEU A 620     -14.537 -17.710  67.083  1.00 93.42           C  
ANISOU 4367  CG  LEU A 620    12744  13333   9417   -424   -248    681       C  
ATOM   4368  CD1 LEU A 620     -14.016 -16.287  67.134  1.00 95.33           C  
ANISOU 4368  CD1 LEU A 620    13068  13608   9543   -684   -201    634       C  
ATOM   4369  CD2 LEU A 620     -13.428 -18.733  67.291  1.00 92.80           C  
ANISOU 4369  CD2 LEU A 620    12459  13526   9274   -335   -297    725       C  
ATOM   4370  N   VAL A 621     -17.937 -19.599  67.096  1.00 90.18           N  
ANISOU 4370  N   VAL A 621    12515  12426   9323     -1   -260    720       N  
ATOM   4371  CA  VAL A 621     -18.535 -20.538  66.143  1.00 92.02           C  
ANISOU 4371  CA  VAL A 621    12745  12585   9633    138   -264    732       C  
ATOM   4372  C   VAL A 621     -19.836 -19.963  65.529  1.00 90.30           C  
ANISOU 4372  C   VAL A 621    12633  12209   9466    142   -230    721       C  
ATOM   4373  O   VAL A 621     -20.010 -19.994  64.304  1.00 89.47           O  
ANISOU 4373  O   VAL A 621    12525  12086   9383    175   -216    719       O  
ATOM   4374  CB  VAL A 621     -18.720 -21.958  66.761  1.00 92.34           C  
ANISOU 4374  CB  VAL A 621    12756  12623   9703    266   -289    758       C  
ATOM   4375  CG1 VAL A 621     -19.499 -22.912  65.837  1.00 89.28           C  
ANISOU 4375  CG1 VAL A 621    12409  12133   9379    369   -277    756       C  
ATOM   4376  CG2 VAL A 621     -17.363 -22.553  67.098  1.00 92.62           C  
ANISOU 4376  CG2 VAL A 621    12675  12845   9672    314   -309    789       C  
ATOM   4377  N   GLU A 622     -20.704 -19.414  66.368  1.00 91.82           N  
ANISOU 4377  N   GLU A 622    12912  12313   9663    116   -214    722       N  
ATOM   4378  CA  GLU A 622     -21.915 -18.762  65.881  1.00 95.28           C  
ANISOU 4378  CA  GLU A 622    13440  12639  10120    143   -173    729       C  
ATOM   4379  C   GLU A 622     -21.572 -17.647  64.864  1.00 94.36           C  
ANISOU 4379  C   GLU A 622    13375  12507   9970     90   -125    725       C  
ATOM   4380  O   GLU A 622     -22.232 -17.534  63.793  1.00 97.42           O  
ANISOU 4380  O   GLU A 622    13775  12863  10376    154   -102    743       O  
ATOM   4381  CB  GLU A 622     -22.766 -18.175  67.021  1.00101.06           C  
ANISOU 4381  CB  GLU A 622    14264  13292  10839    132   -149    735       C  
ATOM   4382  CG  GLU A 622     -23.287 -19.165  68.064  1.00111.71           C  
ANISOU 4382  CG  GLU A 622    15579  14646  12216    178   -190    743       C  
ATOM   4383  CD  GLU A 622     -23.742 -20.528  67.521  1.00121.69           C  
ANISOU 4383  CD  GLU A 622    16780  15927  13526    260   -222    752       C  
ATOM   4384  OE1 GLU A 622     -22.982 -21.507  67.733  1.00123.13           O  
ANISOU 4384  OE1 GLU A 622    16907  16159  13718    278   -254    750       O  
ATOM   4385  OE2 GLU A 622     -24.855 -20.626  66.926  1.00132.90           O  
ANISOU 4385  OE2 GLU A 622    18215  17322  14958    304   -207    762       O  
ATOM   4386  N   LYS A 623     -20.554 -16.832  65.173  1.00 90.85           N  
ANISOU 4386  N   LYS A 623    12960  12097   9461    -36   -106    705       N  
ATOM   4387  CA  LYS A 623     -20.130 -15.740  64.268  1.00 89.32           C  
ANISOU 4387  CA  LYS A 623    12839  11878   9218   -115    -50    698       C  
ATOM   4388  C   LYS A 623     -19.522 -16.243  62.945  1.00 87.54           C  
ANISOU 4388  C   LYS A 623    12505  11745   9010    -86    -75    700       C  
ATOM   4389  O   LYS A 623     -19.732 -15.665  61.869  1.00 84.34           O  
ANISOU 4389  O   LYS A 623    12148  11295   8599    -75    -35    712       O  
ATOM   4390  CB  LYS A 623     -19.126 -14.845  64.971  1.00 92.97           C  
ANISOU 4390  CB  LYS A 623    13362  12378   9584   -303    -22    665       C  
ATOM   4391  CG  LYS A 623     -19.730 -13.770  65.859  1.00 95.93           C  
ANISOU 4391  CG  LYS A 623    13930  12605   9912   -365     51    656       C  
ATOM   4392  CD  LYS A 623     -18.638 -12.982  66.574  1.00 99.48           C  
ANISOU 4392  CD  LYS A 623    14441  13113  10244   -599     81    608       C  
ATOM   4393  CE  LYS A 623     -19.230 -12.030  67.580  1.00100.95           C  
ANISOU 4393  CE  LYS A 623    14839  13141  10376   -663    162    589       C  
ATOM   4394  NZ  LYS A 623     -18.189 -11.629  68.557  1.00103.50           N  
ANISOU 4394  NZ  LYS A 623    15174  13570  10580   -905    167    535       N  
ATOM   4395  N   ILE A 624     -18.796 -17.353  63.040  1.00 86.92           N  
ANISOU 4395  N   ILE A 624    12286  11794   8946    -54   -136    695       N  
ATOM   4396  CA  ILE A 624     -18.302 -18.087  61.859  1.00 84.27           C  
ANISOU 4396  CA  ILE A 624    11846  11542   8630      8   -158    697       C  
ATOM   4397  C   ILE A 624     -19.475 -18.613  60.992  1.00 82.39           C  
ANISOU 4397  C   ILE A 624    11627  11217   8460    125   -152    709       C  
ATOM   4398  O   ILE A 624     -19.510 -18.397  59.780  1.00 83.49           O  
ANISOU 4398  O   ILE A 624    11758  11362   8600    137   -133    711       O  
ATOM   4399  CB  ILE A 624     -17.299 -19.202  62.280  1.00 81.30           C  
ANISOU 4399  CB  ILE A 624    11337  11315   8236     53   -206    701       C  
ATOM   4400  CG1 ILE A 624     -16.004 -18.553  62.755  1.00 80.37           C  
ANISOU 4400  CG1 ILE A 624    11160  11359   8015    -85   -210    693       C  
ATOM   4401  CG2 ILE A 624     -17.007 -20.165  61.134  1.00 80.27           C  
ANISOU 4401  CG2 ILE A 624    11131  11235   8132    161   -215    704       C  
ATOM   4402  CD1 ILE A 624     -15.176 -19.446  63.632  1.00 80.89           C  
ANISOU 4402  CD1 ILE A 624    11101  11594   8038    -35   -250    715       C  
ATOM   4403  N   ASN A 625     -20.432 -19.277  61.621  1.00 81.72           N  
ANISOU 4403  N   ASN A 625    11561  11072   8417    194   -166    716       N  
ATOM   4404  CA  ASN A 625     -21.596 -19.766  60.889  1.00 82.56           C  
ANISOU 4404  CA  ASN A 625    11675  11134   8557    269   -159    724       C  
ATOM   4405  C   ASN A 625     -22.355 -18.618  60.239  1.00 84.15           C  
ANISOU 4405  C   ASN A 625    11940  11293   8738    269   -111    750       C  
ATOM   4406  O   ASN A 625     -22.787 -18.721  59.072  1.00 87.82           O  
ANISOU 4406  O   ASN A 625    12378  11786   9202    306    -99    759       O  
ATOM   4407  CB  ASN A 625     -22.533 -20.500  61.829  1.00 83.41           C  
ANISOU 4407  CB  ASN A 625    11803  11199   8689    308   -176    729       C  
ATOM   4408  CG  ASN A 625     -23.418 -21.508  61.121  1.00 85.15           C  
ANISOU 4408  CG  ASN A 625    12005  11422   8924    351   -178    722       C  
ATOM   4409  OD1 ASN A 625     -23.617 -21.468  59.922  1.00 86.90           O  
ANISOU 4409  OD1 ASN A 625    12203  11676   9136    357   -163    719       O  
ATOM   4410  ND2 ASN A 625     -23.950 -22.438  61.891  1.00 87.01           N  
ANISOU 4410  ND2 ASN A 625    12257  11630   9170    364   -194    716       N  
ATOM   4411  N   LEU A 626     -22.511 -17.521  60.980  1.00 87.30           N  
ANISOU 4411  N   LEU A 626    12435  11626   9106    234    -74    765       N  
ATOM   4412  CA  LEU A 626     -23.150 -16.328  60.384  1.00 90.42           C  
ANISOU 4412  CA  LEU A 626    12927  11964   9464    263     -6    803       C  
ATOM   4413  C   LEU A 626     -22.355 -15.728  59.236  1.00 90.09           C  
ANISOU 4413  C   LEU A 626    12891  11942   9394    216     20    802       C  
ATOM   4414  O   LEU A 626     -22.934 -15.302  58.219  1.00 96.98           O  
ANISOU 4414  O   LEU A 626    13783  12814  10249    280     59    840       O  
ATOM   4415  CB  LEU A 626     -23.398 -15.243  61.431  1.00 92.99           C  
ANISOU 4415  CB  LEU A 626    13398  12184   9748    237     50    815       C  
ATOM   4416  CG  LEU A 626     -24.541 -15.588  62.380  1.00 95.12           C  
ANISOU 4416  CG  LEU A 626    13675  12434  10032    315     42    834       C  
ATOM   4417  CD1 LEU A 626     -24.301 -14.972  63.740  1.00 98.03           C  
ANISOU 4417  CD1 LEU A 626    14152  12722  10372    248     67    816       C  
ATOM   4418  CD2 LEU A 626     -25.886 -15.136  61.827  1.00 96.64           C  
ANISOU 4418  CD2 LEU A 626    13900  12626  10192    450     94    898       C  
ATOM   4419  N   PHE A 627     -21.042 -15.676  59.385  1.00 89.37           N  
ANISOU 4419  N   PHE A 627    12776  11893   9285    105      2    766       N  
ATOM   4420  CA  PHE A 627     -20.199 -15.166  58.291  1.00 91.39           C  
ANISOU 4420  CA  PHE A 627    13025  12191   9506     42     24    762       C  
ATOM   4421  C   PHE A 627     -20.297 -16.049  57.087  1.00 91.07           C  
ANISOU 4421  C   PHE A 627    12865  12232   9504    119     -9    764       C  
ATOM   4422  O   PHE A 627     -20.304 -15.539  55.988  1.00 90.95           O  
ANISOU 4422  O   PHE A 627    12864  12223   9466    125     23    783       O  
ATOM   4423  CB  PHE A 627     -18.747 -15.091  58.732  1.00 93.71           C  
ANISOU 4423  CB  PHE A 627    13276  12574   9753   -100      2    723       C  
ATOM   4424  CG  PHE A 627     -17.760 -14.810  57.637  1.00 92.89           C  
ANISOU 4424  CG  PHE A 627    13125  12562   9607   -174      9    714       C  
ATOM   4425  CD1 PHE A 627     -17.413 -13.521  57.351  1.00 93.84           C  
ANISOU 4425  CD1 PHE A 627    13376  12627   9650   -298     79    716       C  
ATOM   4426  CD2 PHE A 627     -17.089 -15.857  56.988  1.00 92.41           C  
ANISOU 4426  CD2 PHE A 627    12900  12642   9568   -127    -45    702       C  
ATOM   4427  CE1 PHE A 627     -16.443 -13.262  56.407  1.00 96.70           C  
ANISOU 4427  CE1 PHE A 627    13690  13090   9962   -389     84    706       C  
ATOM   4428  CE2 PHE A 627     -16.126 -15.612  56.041  1.00 93.38           C  
ANISOU 4428  CE2 PHE A 627    12966  12872   9642   -196    -41    694       C  
ATOM   4429  CZ  PHE A 627     -15.801 -14.312  55.742  1.00 95.82           C  
ANISOU 4429  CZ  PHE A 627    13387  13143   9877   -335     18    695       C  
ATOM   4430  N   ALA A 628     -20.329 -17.367  57.300  1.00 94.07           N  
ANISOU 4430  N   ALA A 628    13143  12667   9930    173    -65    742       N  
ATOM   4431  CA  ALA A 628     -20.502 -18.320  56.184  1.00 95.70           C  
ANISOU 4431  CA  ALA A 628    13264  12934  10162    236    -85    733       C  
ATOM   4432  C   ALA A 628     -21.884 -18.187  55.525  1.00 99.85           C  
ANISOU 4432  C   ALA A 628    13810  13441  10687    300    -60    764       C  
ATOM   4433  O   ALA A 628     -21.941 -18.053  54.303  1.00102.17           O  
ANISOU 4433  O   ALA A 628    14072  13784  10964    313    -44    774       O  
ATOM   4434  CB  ALA A 628     -20.273 -19.753  56.631  1.00 93.93           C  
ANISOU 4434  CB  ALA A 628    12978  12739   9970    278   -128    704       C  
ATOM   4435  N   MET A 629     -22.973 -18.204  56.312  1.00106.39           N  
ANISOU 4435  N   MET A 629    14677  14227  11519    341    -55    785       N  
ATOM   4436  CA  MET A 629     -24.321 -18.050  55.723  1.00115.13           C  
ANISOU 4436  CA  MET A 629    15775  15373  12596    408    -30    828       C  
ATOM   4437  C   MET A 629     -24.455 -16.754  54.943  1.00112.01           C  
ANISOU 4437  C   MET A 629    15435  14971  12152    444     30    884       C  
ATOM   4438  O   MET A 629     -24.835 -16.804  53.785  1.00116.08           O  
ANISOU 4438  O   MET A 629    15893  15573  12639    478     40    906       O  
ATOM   4439  CB  MET A 629     -25.449 -18.101  56.761  1.00130.09           C  
ANISOU 4439  CB  MET A 629    17698  17248  14480    451    -27    852       C  
ATOM   4440  CG  MET A 629     -26.854 -18.189  56.128  1.00148.98           C  
ANISOU 4440  CG  MET A 629    20035  19754  16816    516    -10    898       C  
ATOM   4441  SD  MET A 629     -28.220 -17.421  57.069  1.00169.65           S  
ANISOU 4441  SD  MET A 629    22700  22381  19376    619     31    973       S  
ATOM   4442  CE  MET A 629     -28.612 -18.736  58.248  1.00163.01           C  
ANISOU 4442  CE  MET A 629    21821  21545  18568    553    -28    920       C  
ATOM   4443  N   PHE A 630     -24.170 -15.613  55.573  1.00109.79           N  
ANISOU 4443  N   PHE A 630    15278  14586  11849    433     78    907       N  
ATOM   4444  CA  PHE A 630     -24.305 -14.293  54.909  1.00108.53           C  
ANISOU 4444  CA  PHE A 630    15225  14380  11629    477    160    968       C  
ATOM   4445  C   PHE A 630     -23.222 -14.014  53.868  1.00106.64           C  
ANISOU 4445  C   PHE A 630    14976  14161  11382    401    166    950       C  
ATOM   4446  O   PHE A 630     -23.410 -13.206  52.956  1.00109.63           O  
ANISOU 4446  O   PHE A 630    15409  14534  11710    447    226   1004       O  
ATOM   4447  CB  PHE A 630     -24.309 -13.157  55.941  1.00112.20           C  
ANISOU 4447  CB  PHE A 630    15875  14696  12057    470    231    990       C  
ATOM   4448  CG  PHE A 630     -25.563 -13.101  56.751  1.00114.25           C  
ANISOU 4448  CG  PHE A 630    16168  14941  12300    587    254   1034       C  
ATOM   4449  CD1 PHE A 630     -26.762 -12.765  56.155  1.00116.44           C  
ANISOU 4449  CD1 PHE A 630    16436  15286  12520    748    303   1120       C  
ATOM   4450  CD2 PHE A 630     -25.553 -13.402  58.093  1.00118.80           C  
ANISOU 4450  CD2 PHE A 630    16767  15467  12905    544    226    996       C  
ATOM   4451  CE1 PHE A 630     -27.939 -12.722  56.875  1.00118.24           C  
ANISOU 4451  CE1 PHE A 630    16672  15541  12713    868    326   1169       C  
ATOM   4452  CE2 PHE A 630     -26.725 -13.369  58.820  1.00124.91           C  
ANISOU 4452  CE2 PHE A 630    17560  16243  13656    653    246   1038       C  
ATOM   4453  CZ  PHE A 630     -27.930 -13.035  58.209  1.00123.17           C  
ANISOU 4453  CZ  PHE A 630    17323  16101  13372    817    296   1125       C  
ATOM   4454  N   GLY A 631     -22.082 -14.666  54.013  1.00103.80           N  
ANISOU 4454  N   GLY A 631    14544  13835  11058    294    109    883       N  
ATOM   4455  CA  GLY A 631     -20.978 -14.522  53.062  1.00102.51           C  
ANISOU 4455  CA  GLY A 631    14343  13725  10878    216    106    861       C  
ATOM   4456  C   GLY A 631     -21.278 -15.113  51.707  1.00 97.15           C  
ANISOU 4456  C   GLY A 631    13554  13151  10208    276     88    870       C  
ATOM   4457  O   GLY A 631     -20.906 -14.549  50.713  1.00 98.55           O  
ANISOU 4457  O   GLY A 631    13740  13353  10350    256    118    889       O  
ATOM   4458  N   THR A 632     -21.964 -16.239  51.691  1.00 93.79           N  
ANISOU 4458  N   THR A 632    13035  12786   9816    331     44    852       N  
ATOM   4459  CA  THR A 632     -22.475 -16.824  50.481  1.00 95.30           C  
ANISOU 4459  CA  THR A 632    13133  13082   9995    371     36    855       C  
ATOM   4460  C   THR A 632     -23.411 -15.862  49.786  1.00 96.16           C  
ANISOU 4460  C   THR A 632    13276  13218  10043    449     93    937       C  
ATOM   4461  O   THR A 632     -23.249 -15.617  48.601  1.00104.37           O  
ANISOU 4461  O   THR A 632    14278  14326  11050    454    110    957       O  
ATOM   4462  CB  THR A 632     -23.266 -18.099  50.780  1.00 98.91           C  
ANISOU 4462  CB  THR A 632    13525  13584  10471    389     -2    822       C  
ATOM   4463  OG1 THR A 632     -22.482 -18.938  51.646  1.00102.10           O  
ANISOU 4463  OG1 THR A 632    13929  13939  10925    350    -40    764       O  
ATOM   4464  CG2 THR A 632     -23.586 -18.885  49.520  1.00 99.63           C  
ANISOU 4464  CG2 THR A 632    13526  13792  10536    381    -10    800       C  
ATOM   4465  N   GLY A 633     -24.371 -15.300  50.506  1.00 94.43           N  
ANISOU 4465  N   GLY A 633    13125  12956   9796    525    129    994       N  
ATOM   4466  CA  GLY A 633     -25.262 -14.304  49.937  1.00 95.61           C  
ANISOU 4466  CA  GLY A 633    13321  13138   9869    643    200   1094       C  
ATOM   4467  C   GLY A 633     -24.515 -13.131  49.297  1.00 97.37           C  
ANISOU 4467  C   GLY A 633    13658  13280  10057    633    267   1131       C  
ATOM   4468  O   GLY A 633     -24.898 -12.646  48.230  1.00100.45           O  
ANISOU 4468  O   GLY A 633    14036  13744  10387    711    311   1199       O  
ATOM   4469  N   ILE A 634     -23.449 -12.674  49.947  1.00 97.11           N  
ANISOU 4469  N   ILE A 634    13737  13110  10048    525    277   1087       N  
ATOM   4470  CA  ILE A 634     -22.672 -11.571  49.428  1.00100.69           C  
ANISOU 4470  CA  ILE A 634    14322  13481  10454    470    346   1110       C  
ATOM   4471  C   ILE A 634     -21.885 -12.019  48.197  1.00102.24           C  
ANISOU 4471  C   ILE A 634    14394  13793  10660    401    304   1077       C  
ATOM   4472  O   ILE A 634     -21.923 -11.353  47.152  1.00105.60           O  
ANISOU 4472  O   ILE A 634    14854  14236  11031    437    358   1134       O  
ATOM   4473  CB  ILE A 634     -21.778 -10.942  50.520  1.00101.98           C  
ANISOU 4473  CB  ILE A 634    14641  13494  10611    335    375   1066       C  
ATOM   4474  CG1 ILE A 634     -22.683 -10.129  51.452  1.00104.73           C  
ANISOU 4474  CG1 ILE A 634    15170  13700  10919    432    458   1123       C  
ATOM   4475  CG2 ILE A 634     -20.715 -10.016  49.917  1.00103.61           C  
ANISOU 4475  CG2 ILE A 634    14962  13646  10758    205    432   1062       C  
ATOM   4476  CD1 ILE A 634     -22.077  -9.834  52.800  1.00107.08           C  
ANISOU 4476  CD1 ILE A 634    15591  13877  11218    299    468   1064       C  
ATOM   4477  N   ALA A 635     -21.198 -13.151  48.301  1.00100.39           N  
ANISOU 4477  N   ALA A 635    14020  13638  10486    320    218    993       N  
ATOM   4478  CA  ALA A 635     -20.436 -13.668  47.152  1.00 99.15           C  
ANISOU 4478  CA  ALA A 635    13741  13596  10332    269    182    957       C  
ATOM   4479  C   ALA A 635     -21.327 -13.931  45.921  1.00 96.97           C  
ANISOU 4479  C   ALA A 635    13377  13437  10031    365    187   1000       C  
ATOM   4480  O   ALA A 635     -21.014 -13.471  44.831  1.00 97.76           O  
ANISOU 4480  O   ALA A 635    13468  13584  10091    356    215   1027       O  
ATOM   4481  CB  ALA A 635     -19.661 -14.921  47.526  1.00 98.39           C  
ANISOU 4481  CB  ALA A 635    13527  13564  10293    212    104    871       C  
ATOM   4482  N   MET A 636     -22.444 -14.608  46.112  1.00 93.33           N  
ANISOU 4482  N   MET A 636    12849  13034   9576    442    166   1009       N  
ATOM   4483  CA  MET A 636     -23.347 -14.857  45.026  1.00 95.47           C  
ANISOU 4483  CA  MET A 636    13021  13455   9796    509    171   1049       C  
ATOM   4484  C   MET A 636     -23.907 -13.562  44.422  1.00 97.21           C  
ANISOU 4484  C   MET A 636    13316  13683   9934    616    253   1167       C  
ATOM   4485  O   MET A 636     -24.283 -13.565  43.228  1.00102.68           O  
ANISOU 4485  O   MET A 636    13921  14522  10569    658    264   1208       O  
ATOM   4486  CB  MET A 636     -24.514 -15.748  45.491  1.00 98.76           C  
ANISOU 4486  CB  MET A 636    13361  13955  10207    545    140   1040       C  
ATOM   4487  CG  MET A 636     -24.132 -17.148  45.979  1.00 99.01           C  
ANISOU 4487  CG  MET A 636    13341  13975  10302    455     76    932       C  
ATOM   4488  SD  MET A 636     -22.930 -18.054  44.979  1.00 98.87           S  
ANISOU 4488  SD  MET A 636    13254  13999  10311    368     44    842       S  
ATOM   4489  CE  MET A 636     -21.395 -17.825  45.894  1.00 99.82           C  
ANISOU 4489  CE  MET A 636    13443  13984  10497    324     29    804       C  
ATOM   4490  N   SER A 637     -24.003 -12.482  45.209  1.00 93.68           N  
ANISOU 4490  N   SER A 637    13040  13085   9467    669    320   1225       N  
ATOM   4491  CA  SER A 637     -24.481 -11.192  44.691  1.00 96.08           C  
ANISOU 4491  CA  SER A 637    13466  13358   9681    797    424   1347       C  
ATOM   4492  C   SER A 637     -23.469 -10.522  43.728  1.00 99.24           C  
ANISOU 4492  C   SER A 637    13932  13715  10057    724    461   1353       C  
ATOM   4493  O   SER A 637     -23.855  -9.728  42.878  1.00 98.89           O  
ANISOU 4493  O   SER A 637    13941  13700   9931    830    536   1454       O  
ATOM   4494  CB  SER A 637     -24.872 -10.255  45.835  1.00 95.86           C  
ANISOU 4494  CB  SER A 637    13642  13153   9628    877    504   1401       C  
ATOM   4495  OG  SER A 637     -23.745  -9.618  46.378  1.00 96.02           O  
ANISOU 4495  OG  SER A 637    13836  12976   9668    741    536   1353       O  
ATOM   4496  N   THR A 638     -22.189 -10.895  43.831  1.00101.22           N  
ANISOU 4496  N   THR A 638    14164  13927  10367    549    409   1251       N  
ATOM   4497  CA  THR A 638     -21.146 -10.402  42.904  1.00102.05           C  
ANISOU 4497  CA  THR A 638    14299  14031  10444    450    432   1244       C  
ATOM   4498  C   THR A 638     -21.186 -11.010  41.477  1.00104.73           C  
ANISOU 4498  C   THR A 638    14458  14563  10771    468    392   1244       C  
ATOM   4499  O   THR A 638     -20.311 -10.736  40.645  1.00107.22           O  
ANISOU 4499  O   THR A 638    14769  14904  11064    384    400   1232       O  
ATOM   4500  CB  THR A 638     -19.714 -10.616  43.472  1.00100.41           C  
ANISOU 4500  CB  THR A 638    14098  13774  10276    256    388   1141       C  
ATOM   4501  OG1 THR A 638     -19.361 -12.013  43.430  1.00 95.31           O  
ANISOU 4501  OG1 THR A 638    13253  13260   9700    220    285   1053       O  
ATOM   4502  CG2 THR A 638     -19.570 -10.068  44.873  1.00 99.78           C  
ANISOU 4502  CG2 THR A 638    14185  13529  10197    200    422   1127       C  
ATOM   4503  N   TRP A 639     -22.164 -11.860  41.196  1.00107.78           N  
ANISOU 4503  N   TRP A 639    14694  15096  11160    554    350   1249       N  
ATOM   4504  CA  TRP A 639     -22.367 -12.381  39.837  1.00112.49           C  
ANISOU 4504  CA  TRP A 639    15132  15887  11721    566    325   1253       C  
ATOM   4505  C   TRP A 639     -22.711 -11.280  38.824  1.00112.72           C  
ANISOU 4505  C   TRP A 639    15216  15957  11653    666    407   1376       C  
ATOM   4506  O   TRP A 639     -22.339 -11.365  37.651  1.00111.44           O  
ANISOU 4506  O   TRP A 639    14971  15907  11462    631    400   1374       O  
ATOM   4507  CB  TRP A 639     -23.491 -13.400  39.856  1.00115.86           C  
ANISOU 4507  CB  TRP A 639    15412  16469  12138    614    279   1239       C  
ATOM   4508  CG  TRP A 639     -23.751 -14.081  38.558  1.00116.03           C  
ANISOU 4508  CG  TRP A 639    15269  16704  12110    592    253   1222       C  
ATOM   4509  CD1 TRP A 639     -24.757 -13.812  37.696  1.00117.99           C  
ANISOU 4509  CD1 TRP A 639    15433  17144  12253    686    284   1315       C  
ATOM   4510  CD2 TRP A 639     -23.001 -15.167  37.994  1.00116.77           C  
ANISOU 4510  CD2 TRP A 639    15268  16854  12245    469    196   1106       C  
ATOM   4511  NE1 TRP A 639     -24.677 -14.654  36.612  1.00121.42           N  
ANISOU 4511  NE1 TRP A 639    15722  17753  12659    602    246   1255       N  
ATOM   4512  CE2 TRP A 639     -23.614 -15.506  36.785  1.00119.24           C  
ANISOU 4512  CE2 TRP A 639    15451  17380  12475    472    197   1123       C  
ATOM   4513  CE3 TRP A 639     -21.878 -15.904  38.412  1.00118.12           C  
ANISOU 4513  CE3 TRP A 639    15451  16928  12499    370    153    994       C  
ATOM   4514  CZ2 TRP A 639     -23.124 -16.535  35.961  1.00121.25           C  
ANISOU 4514  CZ2 TRP A 639    15613  17724  12732    366    161   1022       C  
ATOM   4515  CZ3 TRP A 639     -21.388 -16.951  37.593  1.00117.36           C  
ANISOU 4515  CZ3 TRP A 639    15261  16923  12405    297    122    904       C  
ATOM   4516  CH2 TRP A 639     -22.015 -17.257  36.396  1.00117.93           C  
ANISOU 4516  CH2 TRP A 639    15230  17177  12400    288    129    912       C  
ATOM   4517  N   VAL A 640     -23.402 -10.254  39.311  1.00113.59           N  
ANISOU 4517  N   VAL A 640    15479  15969  11708    800    494   1485       N  
ATOM   4518  CA  VAL A 640     -23.740  -9.099  38.503  1.00116.12           C  
ANISOU 4518  CA  VAL A 640    15904  16291  11924    931    597   1622       C  
ATOM   4519  C   VAL A 640     -22.727  -7.952  38.660  1.00117.11           C  
ANISOU 4519  C   VAL A 640    16280  16179  12037    851    681   1634       C  
ATOM   4520  O   VAL A 640     -22.958  -6.894  38.107  1.00119.43           O  
ANISOU 4520  O   VAL A 640    16720  16419  12237    961    789   1752       O  
ATOM   4521  CB  VAL A 640     -25.201  -8.579  38.708  1.00119.03           C  
ANISOU 4521  CB  VAL A 640    16302  16726  12196   1173    671   1767       C  
ATOM   4522  CG1 VAL A 640     -26.229  -9.689  38.482  1.00117.61           C  
ANISOU 4522  CG1 VAL A 640    15861  16829  11995   1214    591   1755       C  
ATOM   4523  CG2 VAL A 640     -25.365  -7.894  40.059  1.00121.50           C  
ANISOU 4523  CG2 VAL A 640    16837  16806  12520   1231    739   1790       C  
ATOM   4524  N   TRP A 641     -21.590  -8.140  39.333  1.00119.29           N  
ANISOU 4524  N   TRP A 641    16606  16332  12384    655    640   1518       N  
ATOM   4525  CA  TRP A 641     -20.589  -7.054  39.460  1.00125.36           C  
ANISOU 4525  CA  TRP A 641    17609  16906  13113    528    722   1519       C  
ATOM   4526  C   TRP A 641     -19.680  -6.965  38.196  1.00132.25           C  
ANISOU 4526  C   TRP A 641    18421  17872  13957    417    713   1505       C  
ATOM   4527  O   TRP A 641     -18.449  -7.115  38.249  1.00136.85           O  
ANISOU 4527  O   TRP A 641    18984  18451  14561    212    672   1411       O  
ATOM   4528  CB  TRP A 641     -19.765  -7.214  40.737  1.00123.26           C  
ANISOU 4528  CB  TRP A 641    17411  16517  12904    352    687   1411       C  
ATOM   4529  CG  TRP A 641     -20.506  -6.992  41.988  1.00123.08           C  
ANISOU 4529  CG  TRP A 641    17513  16360  12891    439    724   1432       C  
ATOM   4530  CD1 TRP A 641     -21.869  -6.996  42.176  1.00123.08           C  
ANISOU 4530  CD1 TRP A 641    17505  16385  12873    663    754   1520       C  
ATOM   4531  CD2 TRP A 641     -19.923  -6.777  43.271  1.00126.84           C  
ANISOU 4531  CD2 TRP A 641    18123  16685  13385    297    731   1361       C  
ATOM   4532  NE1 TRP A 641     -22.163  -6.782  43.503  1.00125.54           N  
ANISOU 4532  NE1 TRP A 641    17949  16550  13199    677    782   1507       N  
ATOM   4533  CE2 TRP A 641     -20.989  -6.631  44.197  1.00127.23           C  
ANISOU 4533  CE2 TRP A 641    18260  16645  13437    451    770   1409       C  
ATOM   4534  CE3 TRP A 641     -18.599  -6.682  43.734  1.00125.95           C  
ANISOU 4534  CE3 TRP A 641    18053  16531  13270     49    710   1265       C  
ATOM   4535  CZ2 TRP A 641     -20.767  -6.394  45.556  1.00125.95           C  
ANISOU 4535  CZ2 TRP A 641    18239  16330  13285    362    790   1357       C  
ATOM   4536  CZ3 TRP A 641     -18.383  -6.429  45.089  1.00126.13           C  
ANISOU 4536  CZ3 TRP A 641    18209  16421  13291    -48    730   1217       C  
ATOM   4537  CH2 TRP A 641     -19.460  -6.294  45.981  1.00125.20           C  
ANISOU 4537  CH2 TRP A 641    18189  16194  13187    106    769   1260       C  
ATOM   4538  N   THR A 642     -20.321  -6.663  37.068  1.00139.31           N  
ANISOU 4538  N   THR A 642    19281  18867  14784    561    757   1609       N  
ATOM   4539  CA  THR A 642     -19.721  -6.728  35.730  1.00139.84           C  
ANISOU 4539  CA  THR A 642    19242  19067  14821    494    739   1608       C  
ATOM   4540  C   THR A 642     -19.915  -5.397  35.015  1.00143.05           C  
ANISOU 4540  C   THR A 642    19863  19379  15110    586    878   1748       C  
ATOM   4541  O   THR A 642     -20.712  -4.577  35.480  1.00139.88           O  
ANISOU 4541  O   THR A 642    19661  18838  14648    750    987   1856       O  
ATOM   4542  CB  THR A 642     -20.342  -7.873  34.885  1.00138.20           C  
ANISOU 4542  CB  THR A 642    18742  19128  14636    573    646   1592       C  
ATOM   4543  OG1 THR A 642     -21.782  -7.788  34.895  1.00130.98           O  
ANISOU 4543  OG1 THR A 642    17801  18295  13670    791    682   1702       O  
ATOM   4544  CG2 THR A 642     -19.877  -9.255  35.420  1.00135.73           C  
ANISOU 4544  CG2 THR A 642    18250  18889  14432    451    521   1440       C  
ATOM   4545  N   LYS A 643     -19.170  -5.205  33.907  1.00147.27           N  
ANISOU 4545  N   LYS A 643    20363  19985  15605    489    882   1747       N  
ATOM   4546  CA  LYS A 643     -19.290  -4.035  32.986  1.00150.14           C  
ANISOU 4546  CA  LYS A 643    20910  20287  15848    574   1012   1885       C  
ATOM   4547  C   LYS A 643     -20.734  -3.828  32.497  1.00146.00           C  
ANISOU 4547  C   LYS A 643    20350  19870  15251    880   1070   2044       C  
ATOM   4548  O   LYS A 643     -21.285  -2.707  32.521  1.00138.12           O  
ANISOU 4548  O   LYS A 643    19605  18723  14149   1053   1218   2190       O  
ATOM   4549  CB  LYS A 643     -18.472  -4.277  31.706  1.00157.57           C  
ANISOU 4549  CB  LYS A 643    21703  21391  16773    448    965   1851       C  
ATOM   4550  CG  LYS A 643     -16.937  -4.379  31.750  1.00164.26           C  
ANISOU 4550  CG  LYS A 643    22548  22217  17645    155    919   1723       C  
ATOM   4551  CD  LYS A 643     -16.391  -5.065  30.464  1.00167.96           C  
ANISOU 4551  CD  LYS A 643    22764  22932  18120     89    836   1678       C  
ATOM   4552  CE  LYS A 643     -15.215  -4.368  29.773  1.00171.47           C  
ANISOU 4552  CE  LYS A 643    23303  23358  18487   -106    881   1671       C  
ATOM   4553  NZ  LYS A 643     -14.029  -4.197  30.656  1.00180.42           N  
ANISOU 4553  NZ  LYS A 643    24530  24397  19623   -361    871   1566       N  
ATOM   4554  N   ALA A 644     -21.309  -4.959  32.059  1.00148.00           N  
ANISOU 4554  N   ALA A 644    20289  20399  15545    937    955   2012       N  
ATOM   4555  CA  ALA A 644     -22.635  -5.069  31.446  1.00151.71           C  
ANISOU 4555  CA  ALA A 644    20617  21093  15933   1183    972   2141       C  
ATOM   4556  C   ALA A 644     -23.779  -4.486  32.295  1.00158.14           C  
ANISOU 4556  C   ALA A 644    21571  21825  16687   1424   1064   2265       C  
ATOM   4557  O   ALA A 644     -24.686  -3.849  31.773  1.00161.68           O  
ANISOU 4557  O   ALA A 644    22052  22367  17009   1673   1160   2438       O  
ATOM   4558  CB  ALA A 644     -22.926  -6.536  31.103  1.00144.06           C  
ANISOU 4558  CB  ALA A 644    19305  20409  15021   1119    826   2037       C  
ATOM   4559  N   THR A 645     -23.724  -4.726  33.598  1.00161.69           N  
ANISOU 4559  N   THR A 645    22094  22119  17220   1362   1038   2181       N  
ATOM   4560  CA  THR A 645     -24.771  -4.308  34.537  1.00161.75           C  
ANISOU 4560  CA  THR A 645    22220  22053  17182   1576   1113   2276       C  
ATOM   4561  C   THR A 645     -24.624  -2.836  34.985  1.00158.32           C  
ANISOU 4561  C   THR A 645    22190  21292  16670   1671   1294   2379       C  
ATOM   4562  O   THR A 645     -25.638  -2.204  35.336  1.00149.66           O  
ANISOU 4562  O   THR A 645    21221  20162  15478   1941   1406   2524       O  
ATOM   4563  CB  THR A 645     -24.741  -5.211  35.774  1.00161.37           C  
ANISOU 4563  CB  THR A 645    22089  21969  17256   1455   1009   2135       C  
ATOM   4564  OG1 THR A 645     -23.452  -5.082  36.379  1.00169.07           O  
ANISOU 4564  OG1 THR A 645    23217  22704  18315   1212    994   2008       O  
ATOM   4565  CG2 THR A 645     -25.012  -6.703  35.409  1.00152.50           C  
ANISOU 4565  CG2 THR A 645    20609  21141  16191   1371    852   2036       C  
ATOM   4566  N   LEU A 646     -23.380  -2.314  34.975  1.00159.35           N  
ANISOU 4566  N   LEU A 646    22526  21196  16824   1447   1330   2306       N  
ATOM   4567  CA  LEU A 646     -23.103  -0.875  35.181  1.00161.57           C  
ANISOU 4567  CA  LEU A 646    23230  21154  17004   1482   1521   2395       C  
ATOM   4568  C   LEU A 646     -23.755  -0.080  34.062  1.00166.81           C  
ANISOU 4568  C   LEU A 646    23975  21882  17522   1748   1650   2595       C  
ATOM   4569  O   LEU A 646     -24.168   1.060  34.277  1.00175.67           O  
ANISOU 4569  O   LEU A 646    25436  22783  18527   1942   1837   2734       O  
ATOM   4570  CB  LEU A 646     -21.597  -0.549  35.213  1.00162.39           C  
ANISOU 4570  CB  LEU A 646    23496  21068  17134   1140   1524   2270       C  
ATOM   4571  CG  LEU A 646     -20.750  -1.160  36.341  1.00169.19           C  
ANISOU 4571  CG  LEU A 646    24314  21859  18110    860   1419   2082       C  
ATOM   4572  CD1 LEU A 646     -19.286  -1.374  35.949  1.00168.74           C  
ANISOU 4572  CD1 LEU A 646    24196  21834  18084    529   1347   1952       C  
ATOM   4573  CD2 LEU A 646     -20.833  -0.323  37.602  1.00173.00           C  
ANISOU 4573  CD2 LEU A 646    25146  22033  18552    851   1544   2087       C  
ATOM   4574  N   LEU A 647     -23.872  -0.700  32.878  1.00166.23           N  
ANISOU 4574  N   LEU A 647    23598  22116  17444   1769   1557   2613       N  
ATOM   4575  CA  LEU A 647     -24.549  -0.112  31.712  1.00169.68           C  
ANISOU 4575  CA  LEU A 647    24034  22698  17736   2031   1656   2809       C  
ATOM   4576  C   LEU A 647     -26.069  -0.069  31.923  1.00168.75           C  
ANISOU 4576  C   LEU A 647    23833  22760  17523   2398   1707   2972       C  
ATOM   4577  O   LEU A 647     -26.710   0.907  31.539  1.00176.92           O  
ANISOU 4577  O   LEU A 647    25055  23762  18402   2695   1873   3176       O  
ATOM   4578  CB  LEU A 647     -24.214  -0.920  30.429  1.00171.15           C  
ANISOU 4578  CB  LEU A 647    23883  23197  17946   1913   1525   2760       C  
ATOM   4579  CG  LEU A 647     -24.281  -0.357  28.986  1.00175.99           C  
ANISOU 4579  CG  LEU A 647    24492  23944  18433   2035   1600   2906       C  
ATOM   4580  CD1 LEU A 647     -23.508  -1.252  28.012  1.00171.29           C  
ANISOU 4580  CD1 LEU A 647    23605  23569  17907   1792   1450   2777       C  
ATOM   4581  CD2 LEU A 647     -25.705  -0.125  28.474  1.00178.47           C  
ANISOU 4581  CD2 LEU A 647    24695  24519  18595   2417   1670   3122       C  
ATOM   4582  N   ILE A 648     -26.628  -1.122  32.524  1.00162.24           N  
ANISOU 4582  N   ILE A 648    22731  22135  16775   2381   1572   2889       N  
ATOM   4583  CA  ILE A 648     -28.082  -1.243  32.737  1.00157.44           C  
ANISOU 4583  CA  ILE A 648    21979  21773  16068   2693   1595   3028       C  
ATOM   4584  C   ILE A 648     -28.596  -0.201  33.724  1.00156.24           C  
ANISOU 4584  C   ILE A 648    22175  21349  15839   2935   1770   3148       C  
ATOM   4585  O   ILE A 648     -29.690   0.324  33.553  1.00158.85           O  
ANISOU 4585  O   ILE A 648    22521  21821  16012   3292   1882   3350       O  
ATOM   4586  CB  ILE A 648     -28.501  -2.670  33.176  1.00154.91           C  
ANISOU 4586  CB  ILE A 648    21295  21721  15842   2565   1409   2892       C  
ATOM   4587  CG1 ILE A 648     -28.065  -3.747  32.177  1.00158.62           C  
ANISOU 4587  CG1 ILE A 648    21443  22456  16369   2340   1254   2773       C  
ATOM   4588  CG2 ILE A 648     -30.001  -2.781  33.340  1.00153.02           C  
ANISOU 4588  CG2 ILE A 648    20885  21782  15472   2862   1433   3038       C  
ATOM   4589  CD1 ILE A 648     -28.490  -3.596  30.713  1.00164.95           C  
ANISOU 4589  CD1 ILE A 648    22075  23567  17029   2475   1278   2908       C  
ATOM   4590  N   TRP A 649     -27.815   0.101  34.747  1.00161.95           N  
ANISOU 4590  N   TRP A 649    23176  21700  16657   2747   1800   3028       N  
ATOM   4591  CA  TRP A 649     -28.169   1.176  35.714  1.00169.90           C  
ANISOU 4591  CA  TRP A 649    24580  22386  17586   2943   1988   3124       C  
ATOM   4592  C   TRP A 649     -27.958   2.588  35.174  1.00177.01           C  
ANISOU 4592  C   TRP A 649    25894  23020  18342   3099   2215   3279       C  
ATOM   4593  O   TRP A 649     -28.770   3.494  35.447  1.00184.40           O  
ANISOU 4593  O   TRP A 649    27087  23841  19133   3445   2405   3461       O  
ATOM   4594  CB  TRP A 649     -27.390   1.031  37.030  1.00167.75           C  
ANISOU 4594  CB  TRP A 649    24475  21813  17447   2661   1949   2934       C  
ATOM   4595  CG  TRP A 649     -27.852  -0.090  37.878  1.00155.97           C  
ANISOU 4595  CG  TRP A 649    22693  20505  16062   2608   1790   2828       C  
ATOM   4596  CD1 TRP A 649     -27.180  -1.227  38.128  1.00150.37           C  
ANISOU 4596  CD1 TRP A 649    21737  19883  15510   2299   1599   2631       C  
ATOM   4597  CD2 TRP A 649     -29.092  -0.177  38.580  1.00154.49           C  
ANISOU 4597  CD2 TRP A 649    22442  20438  15817   2879   1818   2921       C  
ATOM   4598  NE1 TRP A 649     -27.919  -2.026  38.934  1.00149.15           N  
ANISOU 4598  NE1 TRP A 649    21386  19879  15405   2348   1508   2592       N  
ATOM   4599  CE2 TRP A 649     -29.097  -1.407  39.241  1.00153.68           C  
ANISOU 4599  CE2 TRP A 649    22056  20484  15850   2688   1633   2763       C  
ATOM   4600  CE3 TRP A 649     -30.204   0.665  38.708  1.00159.59           C  
ANISOU 4600  CE3 TRP A 649    23245  21093  16298   3278   1988   3131       C  
ATOM   4601  CZ2 TRP A 649     -30.161  -1.825  40.051  1.00154.70           C  
ANISOU 4601  CZ2 TRP A 649    22052  20766  15960   2850   1605   2796       C  
ATOM   4602  CZ3 TRP A 649     -31.273   0.251  39.527  1.00161.17           C  
ANISOU 4602  CZ3 TRP A 649    23294  21468  16474   3458   1959   3169       C  
ATOM   4603  CH2 TRP A 649     -31.234  -0.984  40.186  1.00157.55           C  
ANISOU 4603  CH2 TRP A 649    22549  21153  16159   3226   1765   2997       C  
ATOM   4604  N   ARG A 650     -26.873   2.779  34.427  1.00183.11           N  
ANISOU 4604  N   ARG A 650    26744  23688  19142   2853   2207   3213       N  
ATOM   4605  CA  ARG A 650     -26.613   4.068  33.756  1.00196.25           C  
ANISOU 4605  CA  ARG A 650    28796  25110  20659   2968   2421   3358       C  
ATOM   4606  C   ARG A 650     -27.613   4.326  32.622  1.00196.28           C  
ANISOU 4606  C   ARG A 650    28665  25406  20505   3359   2492   3597       C  
ATOM   4607  O   ARG A 650     -27.850   5.475  32.261  1.00191.87           O  
ANISOU 4607  O   ARG A 650    28454  24660  19785   3612   2713   3783       O  
ATOM   4608  CB  ARG A 650     -25.185   4.192  33.210  1.00202.02           C  
ANISOU 4608  CB  ARG A 650    29624  25688  21443   2584   2390   3226       C  
ATOM   4609  CG  ARG A 650     -24.123   4.331  34.282  1.00208.52           C  
ANISOU 4609  CG  ARG A 650    30691  26184  22353   2219   2387   3034       C  
ATOM   4610  CD  ARG A 650     -22.763   4.777  33.759  1.00215.23           C  
ANISOU 4610  CD  ARG A 650    31725  26860  23191   1870   2416   2944       C  
ATOM   4611  NE  ARG A 650     -21.690   4.498  34.729  1.00217.30           N  
ANISOU 4611  NE  ARG A 650    32039  26971  23553   1465   2336   2726       N  
ATOM   4612  CZ  ARG A 650     -20.384   4.677  34.508  1.00211.34           C  
ANISOU 4612  CZ  ARG A 650    31375  26124  22799   1087   2320   2604       C  
ATOM   4613  NH1 ARG A 650     -19.948   5.169  33.347  1.00207.42           N  
ANISOU 4613  NH1 ARG A 650    30957  25635  22217   1045   2384   2671       N  
ATOM   4614  NH2 ARG A 650     -19.505   4.371  35.465  1.00206.29           N  
ANISOU 4614  NH2 ARG A 650    30741  25406  22232    747   2242   2418       N  
ATOM   4615  N   ARG A 651     -28.157   3.254  32.038  1.00196.69           N  
ANISOU 4615  N   ARG A 651    28223  25918  20592   3393   2313   3589       N  
ATOM   4616  CA  ARG A 651     -29.208   3.368  31.042  1.00194.25           C  
ANISOU 4616  CA  ARG A 651    27715  25971  20117   3755   2359   3811       C  
ATOM   4617  C   ARG A 651     -30.430   3.969  31.702  1.00194.60           C  
ANISOU 4617  C   ARG A 651    27900  26021  20017   4184   2514   4005       C  
ATOM   4618  O   ARG A 651     -31.053   4.865  31.169  1.00214.62           O  
ANISOU 4618  O   ARG A 651    30602  28581  22361   4558   2698   4246       O  
ATOM   4619  CB  ARG A 651     -29.532   1.983  30.507  1.00188.41           C  
ANISOU 4619  CB  ARG A 651    26422  25719  19444   3634   2126   3721       C  
ATOM   4620  CG  ARG A 651     -30.663   1.900  29.512  1.00190.52           C  
ANISOU 4620  CG  ARG A 651    26398  26458  19532   3955   2139   3927       C  
ATOM   4621  CD  ARG A 651     -30.475   2.896  28.399  1.00195.91           C  
ANISOU 4621  CD  ARG A 651    27277  27086  20071   4130   2294   4107       C  
ATOM   4622  NE  ARG A 651     -29.099   2.944  27.889  1.00188.64           N  
ANISOU 4622  NE  ARG A 651    26480  25929  19264   3776   2254   3960       N  
ATOM   4623  CZ  ARG A 651     -28.663   3.825  26.988  1.00184.07           C  
ANISOU 4623  CZ  ARG A 651    26129  25221  18588   3840   2386   4077       C  
ATOM   4624  NH1 ARG A 651     -29.478   4.747  26.473  1.00180.44           N  
ANISOU 4624  NH1 ARG A 651    25815  24828  17916   4262   2575   4351       N  
ATOM   4625  NH2 ARG A 651     -27.393   3.781  26.590  1.00183.54           N  
ANISOU 4625  NH2 ARG A 651    26142  24969  18623   3484   2334   3925       N  
ATOM   4626  N   THR A 652     -30.738   3.466  32.888  1.00187.05           N  
ANISOU 4626  N   THR A 652    26883  25038  19148   4134   2444   3902       N  
ATOM   4627  CA  THR A 652     -31.888   3.901  33.664  1.00189.95           C  
ANISOU 4627  CA  THR A 652    27350  25429  19392   4516   2570   4061       C  
ATOM   4628  C   THR A 652     -31.819   5.345  34.208  1.00204.24           C  
ANISOU 4628  C   THR A 652    29756  26754  21091   4740   2850   4186       C  
ATOM   4629  O   THR A 652     -32.817   6.080  34.171  1.00207.84           O  
ANISOU 4629  O   THR A 652    30347  27271  21352   5203   3033   4428       O  
ATOM   4630  CB  THR A 652     -32.115   2.933  34.831  1.00181.01           C  
ANISOU 4630  CB  THR A 652    26005  24371  18398   4349   2411   3891       C  
ATOM   4631  OG1 THR A 652     -30.881   2.752  35.539  1.00185.00           O  
ANISOU 4631  OG1 THR A 652    26691  24507  19093   3934   2344   3653       O  
ATOM   4632  CG2 THR A 652     -32.628   1.594  34.278  1.00173.14           C  
ANISOU 4632  CG2 THR A 652    24439  23912  17433   4256   2186   3836       C  
ATOM   4633  N   TRP A 653     -30.650   5.749  34.696  1.00216.36           N  
ANISOU 4633  N   TRP A 653    31650  27825  22729   4414   2893   4026       N  
ATOM   4634  CA  TRP A 653     -30.468   7.107  35.241  1.00227.55           C  
ANISOU 4634  CA  TRP A 653    33684  28736  24037   4550   3169   4112       C  
ATOM   4635  C   TRP A 653     -30.745   8.185  34.184  1.00244.64           C  
ANISOU 4635  C   TRP A 653    36116  30844  25992   4892   3396   4365       C  
ATOM   4636  O   TRP A 653     -31.398   9.200  34.477  1.00260.64           O  
ANISOU 4636  O   TRP A 653    38525  32663  27841   5286   3650   4562       O  
ATOM   4637  CB  TRP A 653     -29.067   7.294  35.828  1.00223.49           C  
ANISOU 4637  CB  TRP A 653    33474  27789  23651   4065   3161   3879       C  
ATOM   4638  CG  TRP A 653     -28.832   8.669  36.417  1.00225.55           C  
ANISOU 4638  CG  TRP A 653    34401  27510  23785   4140   3453   3941       C  
ATOM   4639  CD1 TRP A 653     -29.068   9.036  37.705  1.00218.26           C  
ANISOU 4639  CD1 TRP A 653    33770  26308  22850   4186   3559   3905       C  
ATOM   4640  CD2 TRP A 653     -28.314   9.843  35.755  1.00233.92           C  
ANISOU 4640  CD2 TRP A 653    35939  28236  24703   4159   3683   4042       C  
ATOM   4641  NE1 TRP A 653     -28.737  10.354  37.896  1.00223.24           N  
ANISOU 4641  NE1 TRP A 653    35041  26445  23335   4227   3847   3971       N  
ATOM   4642  CE2 TRP A 653     -28.273  10.878  36.718  1.00231.64           C  
ANISOU 4642  CE2 TRP A 653    36241  27457  24314   4210   3933   4057       C  
ATOM   4643  CE3 TRP A 653     -27.891  10.121  34.444  1.00229.32           C  
ANISOU 4643  CE3 TRP A 653    35355  27715  24058   4135   3711   4121       C  
ATOM   4644  CZ2 TRP A 653     -27.821  12.177  36.417  1.00228.40           C  
ANISOU 4644  CZ2 TRP A 653    36444  26599  23737   4223   4218   4145       C  
ATOM   4645  CZ3 TRP A 653     -27.439  11.420  34.145  1.00223.00           C  
ANISOU 4645  CZ3 TRP A 653    35150  26480  23098   4156   3987   4215       C  
ATOM   4646  CH2 TRP A 653     -27.410  12.426  35.129  1.00223.52           C  
ANISOU 4646  CH2 TRP A 653    35820  26046  23061   4195   4240   4225       C  
ATOM   4647  N   CYS A 654     -30.241   7.960  32.972  1.00245.28           N  
ANISOU 4647  N   CYS A 654    36008  31101  26085   4752   3313   4363       N  
ATOM   4648  CA  CYS A 654     -30.461   8.898  31.879  1.00242.60           C  
ANISOU 4648  CA  CYS A 654    35883  30743  25550   5059   3510   4602       C  
ATOM   4649  C   CYS A 654     -31.947   8.928  31.571  1.00249.51           C  
ANISOU 4649  C   CYS A 654    36530  32027  26245   5614   3572   4870       C  
ATOM   4650  O   CYS A 654     -32.514   9.994  31.336  1.00257.47           O  
ANISOU 4650  O   CYS A 654    37877  32907  27041   6050   3832   5123       O  
ATOM   4651  CB  CYS A 654     -29.657   8.516  30.625  1.00233.21           C  
ANISOU 4651  CB  CYS A 654    34465  29724  24417   4784   3379   4536       C  
ATOM   4652  SG  CYS A 654     -27.877   8.383  30.905  1.00225.05           S  
ANISOU 4652  SG  CYS A 654    33619  28313  23576   4122   3285   4226       S  
ATOM   4653  N   ARG A 655     -32.578   7.754  31.596  1.00245.30           N  
ANISOU 4653  N   ARG A 655    35429  31993  25780   5598   3342   4816       N  
ATOM   4654  CA  ARG A 655     -34.016   7.653  31.341  1.00237.77           C  
ANISOU 4654  CA  ARG A 655    34180  31519  24640   6081   3373   5056       C  
ATOM   4655  C   ARG A 655     -34.785   8.567  32.314  1.00236.52           C  
ANISOU 4655  C   ARG A 655    34409  31119  24336   6504   3615   5223       C  
ATOM   4656  O   ARG A 655     -35.579   9.425  31.901  1.00233.12           O  
ANISOU 4656  O   ARG A 655    34145  30762  23666   7015   3835   5514       O  
ATOM   4657  CB  ARG A 655     -34.482   6.185  31.440  1.00228.83           C  
ANISOU 4657  CB  ARG A 655    32420  30910  23615   5898   3084   4920       C  
ATOM   4658  CG  ARG A 655     -33.963   5.306  30.315  1.00221.15           C  
ANISOU 4658  CG  ARG A 655    31048  30250  22727   5582   2875   4806       C  
ATOM   4659  CD  ARG A 655     -34.447   3.880  30.525  1.00221.66           C  
ANISOU 4659  CD  ARG A 655    30565  30774  22879   5392   2620   4664       C  
ATOM   4660  NE  ARG A 655     -33.885   2.904  29.598  1.00222.25           N  
ANISOU 4660  NE  ARG A 655    30279  31107  23057   5038   2414   4511       N  
ATOM   4661  CZ  ARG A 655     -34.026   1.581  29.712  1.00220.02           C  
ANISOU 4661  CZ  ARG A 655    29575  31143  22878   4769   2188   4336       C  
ATOM   4662  NH1 ARG A 655     -33.482   0.783  28.800  1.00218.12           N  
ANISOU 4662  NH1 ARG A 655    29061  31103  22712   4472   2032   4207       N  
ATOM   4663  NH2 ARG A 655     -34.709   1.039  30.720  1.00220.06           N  
ANISOU 4663  NH2 ARG A 655    29442  31264  22904   4793   2126   4288       N  
ATOM   4664  N   LEU A 656     -34.483   8.405  33.595  1.00230.36           N  
ANISOU 4664  N   LEU A 656    33794  30035  23697   6288   3585   5039       N  
ATOM   4665  CA  LEU A 656     -35.099   9.226  34.635  1.00227.31           C  
ANISOU 4665  CA  LEU A 656    33802  29371  23194   6632   3810   5158       C  
ATOM   4666  C   LEU A 656     -34.750  10.724  34.536  1.00227.70           C  
ANISOU 4666  C   LEU A 656    34549  28874  23093   6844   4145   5304       C  
ATOM   4667  O   LEU A 656     -35.607  11.582  34.775  1.00229.81           O  
ANISOU 4667  O   LEU A 656    35102  29064  23148   7356   4395   5545       O  
ATOM   4668  CB  LEU A 656     -34.683   8.675  35.992  1.00221.79           C  
ANISOU 4668  CB  LEU A 656    33126  28449  22696   6276   3687   4896       C  
ATOM   4669  CG  LEU A 656     -35.079   7.207  36.213  1.00212.82           C  
ANISOU 4669  CG  LEU A 656    31356  27809  21696   6082   3381   4756       C  
ATOM   4670  CD1 LEU A 656     -34.832   6.811  37.657  1.00204.78           C  
ANISOU 4670  CD1 LEU A 656    30413  26555  20837   5831   3305   4546       C  
ATOM   4671  CD2 LEU A 656     -36.523   6.937  35.800  1.00213.38           C  
ANISOU 4671  CD2 LEU A 656    31028  28468  21575   6533   3373   4989       C  
ATOM   4672  N   THR A 657     -33.501  11.029  34.186  1.00221.79           N  
ANISOU 4672  N   THR A 657    34080  27753  22437   6451   4159   5161       N  
ATOM   4673  CA  THR A 657     -33.046  12.428  34.057  1.00217.10           C  
ANISOU 4673  CA  THR A 657    34183  26605  21697   6567   4479   5272       C  
ATOM   4674  C   THR A 657     -32.960  12.873  32.594  1.00212.48           C  
ANISOU 4674  C   THR A 657    33611  26142  20979   6731   4562   5457       C  
ATOM   4675  O   THR A 657     -33.766  12.473  31.755  1.00201.27           O  
ANISOU 4675  O   THR A 657    31753  25249  19469   7033   4485   5630       O  
ATOM   4676  CB  THR A 657     -31.662  12.634  34.704  1.00216.08           C  
ANISOU 4676  CB  THR A 657    34438  25943  21720   5994   4478   4994       C  
ATOM   4677  OG1 THR A 657     -30.756  11.622  34.231  1.00214.84           O  
ANISOU 4677  OG1 THR A 657    33853  26004  21770   5486   4182   4766       O  
ATOM   4678  CG2 THR A 657     -31.765  12.586  36.225  1.00213.22           C  
ANISOU 4678  CG2 THR A 657    34249  25335  21426   5908   4496   4858       C  
TER    4679      THR A 657                                                      
ATOM   4680  N   PRO B  58      39.489  -9.606 -17.412  1.00173.38           N  
ANISOU 4680  N   PRO B  58    22390  25196  18290    570   3946   2602       N  
ATOM   4681  CA  PRO B  58      40.369 -10.783 -17.395  1.00176.10           C  
ANISOU 4681  CA  PRO B  58    22485  25536  18886    360   3858   2520       C  
ATOM   4682  C   PRO B  58      39.577 -12.052 -17.265  1.00182.29           C  
ANISOU 4682  C   PRO B  58    23161  26670  19432    362   3539   2213       C  
ATOM   4683  O   PRO B  58      38.452 -11.987 -16.829  1.00178.40           O  
ANISOU 4683  O   PRO B  58    22752  26356  18674    408   3324   2050       O  
ATOM   4684  CB  PRO B  58      41.207 -10.581 -16.139  1.00173.81           C  
ANISOU 4684  CB  PRO B  58    22041  24898  19098    -95   3714   2522       C  
ATOM   4685  CG  PRO B  58      40.360  -9.731 -15.245  1.00169.81           C  
ANISOU 4685  CG  PRO B  58    21678  24352  18489   -165   3553   2437       C  
ATOM   4686  CD  PRO B  58      39.399  -8.951 -16.096  1.00170.83           C  
ANISOU 4686  CD  PRO B  58    22073  24624  18209    249   3762   2536       C  
ATOM   4687  N   PRO B  59      40.166 -13.207 -17.605  1.00195.53           N  
ANISOU 4687  N   PRO B  59    24631  28412  21250    299   3524   2128       N  
ATOM   4688  CA  PRO B  59      39.411 -14.450 -17.568  1.00198.08           C  
ANISOU 4688  CA  PRO B  59    24818  29029  21412    312   3272   1818       C  
ATOM   4689  C   PRO B  59      39.172 -14.822 -16.121  1.00193.66           C  
ANISOU 4689  C   PRO B  59    24135  28378  21069    -41   2938   1708       C  
ATOM   4690  O   PRO B  59      40.074 -14.595 -15.299  1.00192.06           O  
ANISOU 4690  O   PRO B  59    23838  27898  21235   -340   2905   1850       O  
ATOM   4691  CB  PRO B  59      40.341 -15.461 -18.240  1.00201.40           C  
ANISOU 4691  CB  PRO B  59    25033  29441  22047    300   3406   1799       C  
ATOM   4692  CG  PRO B  59      41.707 -14.938 -17.944  1.00200.83           C  
ANISOU 4692  CG  PRO B  59    24906  28989  22408     77   3579   2088       C  
ATOM   4693  CD  PRO B  59      41.590 -13.437 -17.875  1.00200.46           C  
ANISOU 4693  CD  PRO B  59    25099  28789  22276    161   3731   2302       C  
ATOM   4694  N   PRO B  60      37.966 -15.335 -15.789  1.00197.50           N  
ANISOU 4694  N   PRO B  60    24610  29106  21323      3   2699   1463       N  
ATOM   4695  CA  PRO B  60      37.732 -15.872 -14.428  1.00197.26           C  
ANISOU 4695  CA  PRO B  60    24432  29021  21495   -303   2405   1379       C  
ATOM   4696  C   PRO B  60      38.664 -17.058 -14.165  1.00191.64           C  
ANISOU 4696  C   PRO B  60    23423  28198  21192   -528   2372   1391       C  
ATOM   4697  O   PRO B  60      38.927 -17.840 -15.092  1.00189.09           O  
ANISOU 4697  O   PRO B  60    22986  27946  20912   -406   2506   1304       O  
ATOM   4698  CB  PRO B  60      36.243 -16.275 -14.419  1.00195.41           C  
ANISOU 4698  CB  PRO B  60    24225  29076  20944   -146   2232   1116       C  
ATOM   4699  CG  PRO B  60      35.632 -15.695 -15.656  1.00197.93           C  
ANISOU 4699  CG  PRO B  60    24740  29617  20847    242   2396   1064       C  
ATOM   4700  CD  PRO B  60      36.738 -15.295 -16.610  1.00198.35           C  
ANISOU 4700  CD  PRO B  60    24846  29556  20962    360   2700   1276       C  
ATOM   4701  N   LEU B  61      39.164 -17.162 -12.932  1.00184.19           N  
ANISOU 4701  N   LEU B  61    22350  27100  20532   -831   2206   1497       N  
ATOM   4702  CA  LEU B  61      39.994 -18.294 -12.544  1.00184.20           C  
ANISOU 4702  CA  LEU B  61    22051  27009  20928  -1032   2161   1549       C  
ATOM   4703  C   LEU B  61      39.280 -19.619 -12.832  1.00186.56           C  
ANISOU 4703  C   LEU B  61    22179  27463  21242   -949   2118   1333       C  
ATOM   4704  O   LEU B  61      38.084 -19.763 -12.550  1.00194.78           O  
ANISOU 4704  O   LEU B  61    23267  28669  22072   -877   1981   1162       O  
ATOM   4705  CB  LEU B  61      40.347 -18.240 -11.053  1.00179.55           C  
ANISOU 4705  CB  LEU B  61    21343  26339  20536  -1316   1934   1674       C  
ATOM   4706  CG  LEU B  61      40.872 -16.925 -10.484  1.00176.41           C  
ANISOU 4706  CG  LEU B  61    21075  25804  20145  -1442   1909   1794       C  
ATOM   4707  CD1 LEU B  61      41.317 -17.128  -9.050  1.00172.77           C  
ANISOU 4707  CD1 LEU B  61    20426  25342  19876  -1705   1662   1874       C  
ATOM   4708  CD2 LEU B  61      42.013 -16.403 -11.328  1.00177.67           C  
ANISOU 4708  CD2 LEU B  61    21247  25754  20506  -1429   2169   1930       C  
ATOM   4709  N   SER B  62      40.009 -20.578 -13.403  1.00184.34           N  
ANISOU 4709  N   SER B  62    21684  27110  21245   -961   2252   1323       N  
ATOM   4710  CA  SER B  62      39.466 -21.899 -13.746  1.00180.28           C  
ANISOU 4710  CA  SER B  62    20958  26688  20850   -900   2257   1082       C  
ATOM   4711  C   SER B  62      38.630 -22.510 -12.607  1.00183.63           C  
ANISOU 4711  C   SER B  62    21250  27151  21369  -1025   2045   1037       C  
ATOM   4712  O   SER B  62      37.640 -23.199 -12.861  1.00177.74           O  
ANISOU 4712  O   SER B  62    20420  26527  20585   -924   2022    770       O  
ATOM   4713  CB  SER B  62      40.600 -22.841 -14.152  1.00175.21           C  
ANISOU 4713  CB  SER B  62    20059  25883  20628   -977   2422   1144       C  
ATOM   4714  OG  SER B  62      41.558 -22.958 -13.119  1.00166.97           O  
ANISOU 4714  OG  SER B  62    18858  24649  19934  -1230   2348   1438       O  
ATOM   4715  N   HIS B  63      39.032 -22.243 -11.361  1.00191.30           N  
ANISOU 4715  N   HIS B  63    22188  28031  22463  -1230   1899   1290       N  
ATOM   4716  CA  HIS B  63      38.294 -22.682 -10.148  1.00187.90           C  
ANISOU 4716  CA  HIS B  63    21656  27660  22078  -1328   1712   1323       C  
ATOM   4717  C   HIS B  63      37.124 -21.794  -9.702  1.00174.78           C  
ANISOU 4717  C   HIS B  63    20241  26158  20007  -1256   1563   1229       C  
ATOM   4718  O   HIS B  63      36.233 -22.269  -9.047  1.00163.74           O  
ANISOU 4718  O   HIS B  63    18767  24840  18606  -1262   1462   1173       O  
ATOM   4719  CB  HIS B  63      39.271 -22.892  -8.980  1.00193.32           C  
ANISOU 4719  CB  HIS B  63    22161  28245  23047  -1546   1615   1639       C  
ATOM   4720  CG  HIS B  63      40.279 -23.965  -9.248  1.00208.71           C  
ANISOU 4720  CG  HIS B  63    23812  30036  25450  -1614   1753   1753       C  
ATOM   4721  ND1 HIS B  63      40.148 -25.250  -8.766  1.00215.91           N  
ANISOU 4721  ND1 HIS B  63    24427  30898  26709  -1655   1774   1819       N  
ATOM   4722  CD2 HIS B  63      41.408 -23.958  -9.998  1.00215.83           C  
ANISOU 4722  CD2 HIS B  63    24661  30801  26543  -1631   1911   1816       C  
ATOM   4723  CE1 HIS B  63      41.166 -25.982  -9.186  1.00219.46           C  
ANISOU 4723  CE1 HIS B  63    24652  31184  27546  -1699   1929   1915       C  
ATOM   4724  NE2 HIS B  63      41.944 -25.221  -9.936  1.00220.46           N  
ANISOU 4724  NE2 HIS B  63    24924  31266  27575  -1688   2007   1907       N  
ATOM   4725  N   CYS B  64      37.149 -20.514 -10.045  1.00172.35           N  
ANISOU 4725  N   CYS B  64    20215  25875  19393  -1183   1578   1232       N  
ATOM   4726  CA  CYS B  64      36.049 -19.555  -9.822  1.00166.77           C  
ANISOU 4726  CA  CYS B  64    19767  25305  18293  -1077   1481   1132       C  
ATOM   4727  C   CYS B  64      34.911 -19.583 -10.846  1.00164.87           C  
ANISOU 4727  C   CYS B  64    19630  25241  17770   -814   1541    858       C  
ATOM   4728  O   CYS B  64      34.248 -18.579 -11.093  1.00166.76           O  
ANISOU 4728  O   CYS B  64    20120  25580  17661   -662   1535    805       O  
ATOM   4729  CB  CYS B  64      36.600 -18.116  -9.739  1.00170.91           C  
ANISOU 4729  CB  CYS B  64    20529  25738  18669  -1106   1507   1266       C  
ATOM   4730  SG  CYS B  64      36.870 -17.562  -8.032  1.00178.63           S  
ANISOU 4730  SG  CYS B  64    21496  26683  19689  -1356   1282   1415       S  
ATOM   4731  N   GLY B  65      34.604 -20.746 -11.378  1.00166.91           N  
ANISOU 4731  N   GLY B  65    19675  25554  18187   -753   1588    664       N  
ATOM   4732  CA  GLY B  65      33.506 -20.855 -12.338  1.00170.87           C  
ANISOU 4732  CA  GLY B  65    20222  26275  18425   -500   1613    341       C  
ATOM   4733  C   GLY B  65      33.352 -22.295 -12.728  1.00172.79           C  
ANISOU 4733  C   GLY B  65    20147  26520  18983   -507   1663    101       C  
ATOM   4734  O   GLY B  65      34.238 -23.116 -12.436  1.00168.40           O  
ANISOU 4734  O   GLY B  65    19369  25772  18840   -679   1726    228       O  
ATOM   4735  N   ARG B  66      32.256 -22.605 -13.417  1.00177.99           N  
ANISOU 4735  N   ARG B  66    20760  27392  19473   -313   1643   -262       N  
ATOM   4736  CA  ARG B  66      31.987 -23.998 -13.771  1.00180.79           C  
ANISOU 4736  CA  ARG B  66    20775  27734  20183   -330   1695   -573       C  
ATOM   4737  C   ARG B  66      31.373 -24.127 -15.164  1.00185.28           C  
ANISOU 4737  C   ARG B  66    21322  28588  20487    -50   1736  -1015       C  
ATOM   4738  O   ARG B  66      30.668 -23.232 -15.631  1.00188.46           O  
ANISOU 4738  O   ARG B  66    21948  29252  20405    177   1670  -1106       O  
ATOM   4739  CB  ARG B  66      31.122 -24.662 -12.691  1.00180.31           C  
ANISOU 4739  CB  ARG B  66    20522  27596  20391   -469   1597   -602       C  
ATOM   4740  CG  ARG B  66      31.588 -26.071 -12.347  1.00182.35           C  
ANISOU 4740  CG  ARG B  66    20407  27608  21269   -648   1708   -593       C  
ATOM   4741  CD  ARG B  66      30.696 -26.722 -11.311  1.00181.47           C  
ANISOU 4741  CD  ARG B  66    20095  27412  21440   -751   1661   -582       C  
ATOM   4742  NE  ARG B  66      30.927 -26.195  -9.972  1.00182.69           N  
ANISOU 4742  NE  ARG B  66    20380  27499  21531   -883   1567   -138       N  
ATOM   4743  CZ  ARG B  66      30.175 -26.473  -8.911  1.00190.99           C  
ANISOU 4743  CZ  ARG B  66    21339  28523  22705   -945   1520    -27       C  
ATOM   4744  NH1 ARG B  66      29.125 -27.293  -9.020  1.00198.55           N  
ANISOU 4744  NH1 ARG B  66    22056  29466  23918   -905   1575   -319       N  
ATOM   4745  NH2 ARG B  66      30.464 -25.926  -7.723  1.00194.35           N  
ANISOU 4745  NH2 ARG B  66    21896  28944  23001  -1039   1425    361       N  
ATOM   4746  N   ALA B  67      31.649 -25.274 -15.786  1.00184.79           N  
ANISOU 4746  N   ALA B  67    20968  28484  20760    -61   1847  -1295       N  
ATOM   4747  CA  ALA B  67      31.233 -25.561 -17.149  1.00187.96           C  
ANISOU 4747  CA  ALA B  67    21290  29182  20944    200   1890  -1772       C  
ATOM   4748  C   ALA B  67      29.761 -25.943 -17.161  1.00197.94           C  
ANISOU 4748  C   ALA B  67    22392  30647  22170    287   1750  -2209       C  
ATOM   4749  O   ALA B  67      29.382 -27.027 -16.701  1.00204.25           O  
ANISOU 4749  O   ALA B  67    22863  31269  23472    119   1760  -2411       O  
ATOM   4750  CB  ALA B  67      32.077 -26.675 -17.740  1.00184.17           C  
ANISOU 4750  CB  ALA B  67    20530  28562  20883    136   2067  -1952       C  
ATOM   4751  N   ALA B  68      28.926 -25.033 -17.655  1.00203.87           N  
ANISOU 4751  N   ALA B  68    23357  31751  22353    554   1637  -2331       N  
ATOM   4752  CA  ALA B  68      27.482 -25.258 -17.719  1.00207.25           C  
ANISOU 4752  CA  ALA B  68    23638  32416  22690    666   1485  -2753       C  
ATOM   4753  C   ALA B  68      26.916 -24.560 -18.946  1.00209.71           C  
ANISOU 4753  C   ALA B  68    24095  33229  22354   1068   1422  -3027       C  
ATOM   4754  O   ALA B  68      27.320 -23.442 -19.240  1.00214.16           O  
ANISOU 4754  O   ALA B  68    24998  33906  22464   1241   1462  -2692       O  
ATOM   4755  CB  ALA B  68      26.802 -24.738 -16.452  1.00204.15           C  
ANISOU 4755  CB  ALA B  68    23367  31893  22308    531   1364  -2471       C  
ATOM   4756  N   PRO B  69      25.956 -25.203 -19.648  1.00208.53           N  
ANISOU 4756  N   PRO B  69    23671  33390  22171   1230   1329  -3635       N  
ATOM   4757  CA  PRO B  69      25.321 -24.554 -20.801  1.00201.17           C  
ANISOU 4757  CA  PRO B  69    22848  33018  20569   1658   1239  -3909       C  
ATOM   4758  C   PRO B  69      24.502 -23.322 -20.393  1.00188.11           C  
ANISOU 4758  C   PRO B  69    21490  31523  18460   1814   1111  -3634       C  
ATOM   4759  O   PRO B  69      23.733 -23.409 -19.437  1.00181.78           O  
ANISOU 4759  O   PRO B  69    20617  30558  17892   1637   1005  -3624       O  
ATOM   4760  CB  PRO B  69      24.404 -25.652 -21.344  1.00208.57           C  
ANISOU 4760  CB  PRO B  69    23346  34190  21710   1713   1133  -4663       C  
ATOM   4761  CG  PRO B  69      24.064 -26.477 -20.155  1.00211.81           C  
ANISOU 4761  CG  PRO B  69    23500  34150  22826   1330   1129  -4673       C  
ATOM   4762  CD  PRO B  69      25.334 -26.512 -19.357  1.00211.19           C  
ANISOU 4762  CD  PRO B  69    23563  33582  23097   1038   1301  -4096       C  
ATOM   4763  N   CYS B  70      24.675 -22.204 -21.099  1.00178.38           N  
ANISOU 4763  N   CYS B  70    20576  30584  16612   2149   1152  -3394       N  
ATOM   4764  CA  CYS B  70      23.964 -20.974 -20.751  1.00176.20           C  
ANISOU 4764  CA  CYS B  70    20591  30428  15928   2315   1072  -3100       C  
ATOM   4765  C   CYS B  70      22.586 -20.917 -21.395  1.00177.85           C  
ANISOU 4765  C   CYS B  70    20665  31166  15743   2655    881  -3555       C  
ATOM   4766  O   CYS B  70      22.414 -21.302 -22.538  1.00186.94           O  
ANISOU 4766  O   CYS B  70    21649  32756  16622   2942    848  -3977       O  
ATOM   4767  CB  CYS B  70      24.751 -19.732 -21.160  1.00174.40           C  
ANISOU 4767  CB  CYS B  70    20757  30226  15278   2531   1245  -2581       C  
ATOM   4768  SG  CYS B  70      26.373 -19.522 -20.353  1.00173.97           S  
ANISOU 4768  SG  CYS B  70    20885  29563  15652   2149   1458  -2005       S  
ATOM   4769  N   GLU B  71      21.599 -20.431 -20.653  1.00174.21           N  
ANISOU 4769  N   GLU B  71    20263  30687  15242   2632    750  -3484       N  
ATOM   4770  CA  GLU B  71      20.277 -20.127 -21.205  1.00178.79           C  
ANISOU 4770  CA  GLU B  71    20760  31777  15394   2987    567  -3821       C  
ATOM   4771  C   GLU B  71      19.961 -18.648 -20.960  1.00178.67           C  
ANISOU 4771  C   GLU B  71    21135  31817  14932   3204    591  -3327       C  
ATOM   4772  O   GLU B  71      20.359 -18.083 -19.929  1.00181.27           O  
ANISOU 4772  O   GLU B  71    21701  31706  15466   2949    678  -2861       O  
ATOM   4773  CB  GLU B  71      19.183 -21.039 -20.634  1.00182.97           C  
ANISOU 4773  CB  GLU B  71    20912  32266  16341   2789    389  -4298       C  
ATOM   4774  CG  GLU B  71      19.140 -21.165 -19.120  1.00191.57           C  
ANISOU 4774  CG  GLU B  71    22026  32807  17953   2365    415  -4002       C  
ATOM   4775  CD  GLU B  71      18.147 -22.233 -18.649  1.00200.34           C  
ANISOU 4775  CD  GLU B  71    22710  33849  19561   2174    302  -4481       C  
ATOM   4776  OE1 GLU B  71      18.588 -23.350 -18.296  1.00211.20           O  
ANISOU 4776  OE1 GLU B  71    23816  34894  21535   1865    386  -4627       O  
ATOM   4777  OE2 GLU B  71      16.926 -21.974 -18.616  1.00206.31           O  
ANISOU 4777  OE2 GLU B  71    23378  34857  20152   2332    150  -4700       O  
ATOM   4778  N   PRO B  72      19.277 -17.997 -21.924  1.00185.05           N  
ANISOU 4778  N   PRO B  72    22004  33180  15125   3696    527  -3425       N  
ATOM   4779  CA  PRO B  72      18.972 -16.579 -21.727  1.00184.26           C  
ANISOU 4779  CA  PRO B  72    22262  33106  14639   3926    589  -2934       C  
ATOM   4780  C   PRO B  72      18.014 -16.369 -20.558  1.00183.00           C  
ANISOU 4780  C   PRO B  72    22096  32724  14711   3717    462  -2907       C  
ATOM   4781  O   PRO B  72      17.230 -17.258 -20.216  1.00181.80           O  
ANISOU 4781  O   PRO B  72    21619  32602  14854   3554    286  -3352       O  
ATOM   4782  CB  PRO B  72      18.334 -16.177 -23.060  1.00186.92           C  
ANISOU 4782  CB  PRO B  72    22573  34154  14294   4525    526  -3122       C  
ATOM   4783  CG  PRO B  72      17.772 -17.440 -23.600  1.00186.87           C  
ANISOU 4783  CG  PRO B  72    22116  34503  14382   4536    311  -3865       C  
ATOM   4784  CD  PRO B  72      18.751 -18.492 -23.214  1.00186.41           C  
ANISOU 4784  CD  PRO B  72    21912  33994  14921   4082    399  -3979       C  
ATOM   4785  N   LEU B  73      18.108 -15.207 -19.926  1.00189.54           N  
ANISOU 4785  N   LEU B  73    23269  33300  15447   3712    575  -2390       N  
ATOM   4786  CA  LEU B  73      17.297 -14.918 -18.735  1.00193.36           C  
ANISOU 4786  CA  LEU B  73    23785  33540  16140   3507    487  -2317       C  
ATOM   4787  C   LEU B  73      15.839 -14.741 -19.094  1.00199.12           C  
ANISOU 4787  C   LEU B  73    24373  34728  16556   3839    304  -2612       C  
ATOM   4788  O   LEU B  73      15.535 -14.093 -20.069  1.00205.74           O  
ANISOU 4788  O   LEU B  73    25295  36002  16873   4301    313  -2570       O  
ATOM   4789  CB  LEU B  73      17.778 -13.653 -18.020  1.00190.07           C  
ANISOU 4789  CB  LEU B  73    23767  32755  15693   3437    665  -1734       C  
ATOM   4790  CG  LEU B  73      18.870 -13.917 -16.991  1.00186.12           C  
ANISOU 4790  CG  LEU B  73    23339  31700  15676   2951    760  -1502       C  
ATOM   4791  CD1 LEU B  73      19.720 -12.673 -16.826  1.00181.20           C  
ANISOU 4791  CD1 LEU B  73    23084  30802  14961   2972    982   -982       C  
ATOM   4792  CD2 LEU B  73      18.210 -14.301 -15.679  1.00189.01           C  
ANISOU 4792  CD2 LEU B  73    23594  31828  16392   2625    633  -1597       C  
ATOM   4793  N   ARG B  74      14.952 -15.323 -18.302  1.00203.91           N  
ANISOU 4793  N   ARG B  74    24749  35239  17488   3616    151  -2891       N  
ATOM   4794  CA  ARG B  74      13.514 -15.129 -18.469  1.00211.84           C  
ANISOU 4794  CA  ARG B  74    25599  36623  18266   3887    -25  -3162       C  
ATOM   4795  C   ARG B  74      13.056 -13.860 -17.761  1.00208.55           C  
ANISOU 4795  C   ARG B  74    25502  36051  17684   3967     45  -2724       C  
ATOM   4796  O   ARG B  74      12.084 -13.245 -18.190  1.00210.46           O  
ANISOU 4796  O   ARG B  74    25745  36667  17552   4342    -35  -2769       O  
ATOM   4797  CB  ARG B  74      12.735 -16.341 -17.939  1.00218.60           C  
ANISOU 4797  CB  ARG B  74    26031  37417  19608   3612   -187  -3666       C  
ATOM   4798  CG  ARG B  74      11.261 -16.350 -18.301  1.00224.80           C  
ANISOU 4798  CG  ARG B  74    26555  38656  20203   3899   -393  -4072       C  
ATOM   4799  CD  ARG B  74      10.682 -17.759 -18.145  1.00230.67           C  
ANISOU 4799  CD  ARG B  74    26789  39383  21472   3655   -526  -4684       C  
ATOM   4800  NE  ARG B  74      11.039 -18.595 -19.304  1.00242.61           N  
ANISOU 4800  NE  ARG B  74    28021  41231  22926   3779   -597  -5167       N  
ATOM   4801  CZ  ARG B  74      10.363 -18.698 -20.460  1.00248.68           C  
ANISOU 4801  CZ  ARG B  74    28541  42639  23304   4178   -784  -5654       C  
ATOM   4802  NH1 ARG B  74      10.838 -19.501 -21.406  1.00246.74           N  
ANISOU 4802  NH1 ARG B  74    28056  42646  23045   4243   -823  -6091       N  
ATOM   4803  NH2 ARG B  74       9.227 -18.026 -20.694  1.00253.95           N  
ANISOU 4803  NH2 ARG B  74    29178  43722  23588   4528   -938  -5729       N  
ATOM   4804  N   TYR B  75      13.765 -13.480 -16.689  1.00201.09           N  
ANISOU 4804  N   TYR B  75    24810  34573  17020   3624    193  -2324       N  
ATOM   4805  CA  TYR B  75      13.403 -12.344 -15.831  1.00189.76           C  
ANISOU 4805  CA  TYR B  75    23664  32909  15525   3619    274  -1952       C  
ATOM   4806  C   TYR B  75      14.535 -11.363 -15.848  1.00194.86           C  
ANISOU 4806  C   TYR B  75    24683  33286  16068   3624    506  -1459       C  
ATOM   4807  O   TYR B  75      15.692 -11.757 -15.697  1.00189.68           O  
ANISOU 4807  O   TYR B  75    24059  32357  15653   3354    592  -1358       O  
ATOM   4808  CB  TYR B  75      13.171 -12.782 -14.397  1.00177.44           C  
ANISOU 4808  CB  TYR B  75    22037  30960  14422   3188    238  -1969       C  
ATOM   4809  CG  TYR B  75      12.305 -14.002 -14.321  1.00169.28           C  
ANISOU 4809  CG  TYR B  75    20581  30078  13659   3090     63  -2455       C  
ATOM   4810  CD1 TYR B  75      10.926 -13.903 -14.432  1.00167.67           C  
ANISOU 4810  CD1 TYR B  75    20208  30172  13326   3316    -70  -2706       C  
ATOM   4811  CD2 TYR B  75      12.873 -15.263 -14.145  1.00163.84           C  
ANISOU 4811  CD2 TYR B  75    19636  29213  13401   2773     50  -2665       C  
ATOM   4812  CE1 TYR B  75      10.129 -15.032 -14.350  1.00171.00           C  
ANISOU 4812  CE1 TYR B  75    20204  30695  14071   3207   -210  -3177       C  
ATOM   4813  CE2 TYR B  75      12.092 -16.395 -14.066  1.00161.21           C  
ANISOU 4813  CE2 TYR B  75    18887  28961  13405   2671    -66  -3115       C  
ATOM   4814  CZ  TYR B  75      10.726 -16.278 -14.158  1.00164.87           C  
ANISOU 4814  CZ  TYR B  75    19177  29701  13764   2876   -194  -3380       C  
ATOM   4815  OH  TYR B  75       9.967 -17.411 -14.065  1.00162.70           O  
ANISOU 4815  OH  TYR B  75    18456  29466  13896   2754   -288  -3845       O  
ATOM   4816  N   ASN B  76      14.195 -10.089 -16.006  1.00202.47           N  
ANISOU 4816  N   ASN B  76    25906  34303  16720   3927    622  -1152       N  
ATOM   4817  CA  ASN B  76      15.201  -9.023 -16.060  1.00208.23           C  
ANISOU 4817  CA  ASN B  76    26977  34746  17393   3962    886   -675       C  
ATOM   4818  C   ASN B  76      15.690  -8.612 -14.678  1.00203.84           C  
ANISOU 4818  C   ASN B  76    26603  33639  17206   3538    972   -457       C  
ATOM   4819  O   ASN B  76      16.728  -7.957 -14.568  1.00205.87           O  
ANISOU 4819  O   ASN B  76    27081  33579  17560   3440   1176   -137       O  
ATOM   4820  CB  ASN B  76      14.708  -7.788 -16.842  1.00216.00           C  
ANISOU 4820  CB  ASN B  76    28156  35976  17935   4487   1033   -395       C  
ATOM   4821  CG  ASN B  76      13.332  -7.290 -16.401  1.00217.28           C  
ANISOU 4821  CG  ASN B  76    28307  36265  17982   4650    938   -454       C  
ATOM   4822  OD1 ASN B  76      12.818  -7.664 -15.341  1.00207.18           O  
ANISOU 4822  OD1 ASN B  76    26937  34799  16981   4335    806   -637       O  
ATOM   4823  ND2 ASN B  76      12.710  -6.453 -17.251  1.00225.84           N  
ANISOU 4823  ND2 ASN B  76    29469  37697  18641   5179   1016   -282       N  
ATOM   4824  N   VAL B  77      14.991  -9.077 -13.641  1.00205.78           N  
ANISOU 4824  N   VAL B  77    26723  33791  17673   3282    816   -656       N  
ATOM   4825  CA  VAL B  77      15.140  -8.622 -12.254  1.00199.00           C  
ANISOU 4825  CA  VAL B  77    26020  32518  17072   2949    864   -496       C  
ATOM   4826  C   VAL B  77      15.327  -9.817 -11.277  1.00187.71           C  
ANISOU 4826  C   VAL B  77    24375  30927  16018   2518    723   -693       C  
ATOM   4827  O   VAL B  77      14.671 -10.869 -11.404  1.00187.89           O  
ANISOU 4827  O   VAL B  77    24103  31158  16126   2506    569  -1006       O  
ATOM   4828  CB  VAL B  77      13.918  -7.749 -11.877  1.00190.34           C  
ANISOU 4828  CB  VAL B  77    25025  31487  15807   3156    867   -461       C  
ATOM   4829  CG1 VAL B  77      12.623  -8.548 -11.835  1.00186.24           C  
ANISOU 4829  CG1 VAL B  77    24218  31276  15267   3231    655   -813       C  
ATOM   4830  CG2 VAL B  77      14.151  -7.053 -10.573  1.00181.70           C  
ANISOU 4830  CG2 VAL B  77    24136  29986  14915   2874    956   -284       C  
ATOM   4831  N   CYS B  78      16.268  -9.658 -10.347  1.00177.83           N  
ANISOU 4831  N   CYS B  78    23249  29311  15006   2181    792   -505       N  
ATOM   4832  CA  CYS B  78      16.495 -10.625  -9.278  1.00180.31           C  
ANISOU 4832  CA  CYS B  78    23394  29463  15650   1802    693   -593       C  
ATOM   4833  C   CYS B  78      16.253  -9.930  -7.935  1.00178.73           C  
ANISOU 4833  C   CYS B  78    23360  29049  15499   1633    712   -466       C  
ATOM   4834  O   CYS B  78      17.012  -9.018  -7.556  1.00177.49           O  
ANISOU 4834  O   CYS B  78    23436  28657  15346   1539    821   -259       O  
ATOM   4835  CB  CYS B  78      17.911 -11.194  -9.319  1.00183.90           C  
ANISOU 4835  CB  CYS B  78    23804  29735  16334   1554    732   -501       C  
ATOM   4836  SG  CYS B  78      18.161 -12.527  -8.136  1.00187.52           S  
ANISOU 4836  SG  CYS B  78    24004  30049  17195   1157    626   -574       S  
ATOM   4837  N   LEU B  79      15.188 -10.377  -7.250  1.00172.26           N  
ANISOU 4837  N   LEU B  79    22398  28318  14732   1602    617   -616       N  
ATOM   4838  CA  LEU B  79      14.728  -9.855  -5.954  1.00168.03           C  
ANISOU 4838  CA  LEU B  79    21982  27652  14211   1478    626   -545       C  
ATOM   4839  C   LEU B  79      14.698  -8.327  -5.897  1.00172.77           C  
ANISOU 4839  C   LEU B  79    22900  28135  14607   1618    750   -390       C  
ATOM   4840  O   LEU B  79      15.308  -7.689  -5.026  1.00171.65           O  
ANISOU 4840  O   LEU B  79    22932  27763  14524   1427    810   -269       O  
ATOM   4841  CB  LEU B  79      15.577 -10.432  -4.822  1.00162.72           C  
ANISOU 4841  CB  LEU B  79    21256  26791  13779   1118    600   -455       C  
ATOM   4842  CG  LEU B  79      15.527 -11.958  -4.692  1.00157.63           C  
ANISOU 4842  CG  LEU B  79    20278  26208  13405    975    523   -566       C  
ATOM   4843  CD1 LEU B  79      16.797 -12.454  -4.014  1.00154.79           C  
ANISOU 4843  CD1 LEU B  79    19883  25673  13254    679    523   -406       C  
ATOM   4844  CD2 LEU B  79      14.276 -12.389  -3.946  1.00153.72           C  
ANISOU 4844  CD2 LEU B  79    19630  25800  12977    990    491   -670       C  
ATOM   4845  N   GLY B  80      14.024  -7.744  -6.878  1.00174.44           N  
ANISOU 4845  N   GLY B  80    23169  28515  14592   1968    798   -401       N  
ATOM   4846  CA  GLY B  80      13.861  -6.305  -6.930  1.00177.81           C  
ANISOU 4846  CA  GLY B  80    23873  28824  14860   2155    956   -235       C  
ATOM   4847  C   GLY B  80      14.869  -5.564  -7.781  1.00181.86           C  
ANISOU 4847  C   GLY B  80    24561  29206  15332   2264   1128    -23       C  
ATOM   4848  O   GLY B  80      14.536  -4.502  -8.308  1.00190.38           O  
ANISOU 4848  O   GLY B  80    25809  30275  16251   2558   1286    123       O  
ATOM   4849  N   SER B  81      16.076  -6.117  -7.955  1.00185.65           N  
ANISOU 4849  N   SER B  81    24987  29581  15969   2055   1124     16       N  
ATOM   4850  CA  SER B  81      17.163  -5.413  -8.663  1.00192.41           C  
ANISOU 4850  CA  SER B  81    26001  30258  16848   2118   1321    239       C  
ATOM   4851  C   SER B  81      17.418  -5.958 -10.077  1.00194.36           C  
ANISOU 4851  C   SER B  81    26140  30758  16948   2364   1334    252       C  
ATOM   4852  O   SER B  81      17.545  -7.167 -10.274  1.00202.92           O  
ANISOU 4852  O   SER B  81    27000  32007  18091   2258   1179     72       O  
ATOM   4853  CB  SER B  81      18.457  -5.468  -7.853  1.00194.78           C  
ANISOU 4853  CB  SER B  81    26329  30239  17438   1718   1337    295       C  
ATOM   4854  OG  SER B  81      18.244  -5.078  -6.507  1.00199.03           O  
ANISOU 4854  OG  SER B  81    26936  30612  18073   1492   1293    232       O  
ATOM   4855  N   VAL B  82      17.458  -5.058 -11.061  1.00190.39           N  
ANISOU 4855  N   VAL B  82    25788  30293  16255   2715   1538    465       N  
ATOM   4856  CA  VAL B  82      17.739  -5.419 -12.466  1.00181.00           C  
ANISOU 4856  CA  VAL B  82    24525  29385  14859   3012   1586    508       C  
ATOM   4857  C   VAL B  82      19.210  -5.882 -12.625  1.00178.92           C  
ANISOU 4857  C   VAL B  82    24232  28919  14828   2758   1653    585       C  
ATOM   4858  O   VAL B  82      20.102  -5.317 -12.008  1.00173.65           O  
ANISOU 4858  O   VAL B  82    23692  27862  14423   2506   1785    746       O  
ATOM   4859  CB  VAL B  82      17.314  -4.273 -13.439  1.00173.59           C  
ANISOU 4859  CB  VAL B  82    23758  28577  13618   3517   1816    777       C  
ATOM   4860  CG1 VAL B  82      18.115  -3.006 -13.226  1.00171.59           C  
ANISOU 4860  CG1 VAL B  82    23756  27873  13565   3478   2137   1123       C  
ATOM   4861  CG2 VAL B  82      17.429  -4.690 -14.883  1.00169.88           C  
ANISOU 4861  CG2 VAL B  82    23194  28510  12840   3886   1838    795       C  
ATOM   4862  N   LEU B  83      19.429  -6.917 -13.442  1.00179.16           N  
ANISOU 4862  N   LEU B  83    24072  29223  14775   2827   1558    435       N  
ATOM   4863  CA  LEU B  83      20.731  -7.619 -13.555  1.00178.88           C  
ANISOU 4863  CA  LEU B  83    23950  29032  14981   2566   1584    450       C  
ATOM   4864  C   LEU B  83      21.614  -7.096 -14.687  1.00185.33           C  
ANISOU 4864  C   LEU B  83    24883  29839  15693   2813   1848    720       C  
ATOM   4865  O   LEU B  83      21.103  -6.829 -15.774  1.00183.40           O  
ANISOU 4865  O   LEU B  83    24665  29932  15086   3258   1925    772       O  
ATOM   4866  CB  LEU B  83      20.526  -9.130 -13.785  1.00174.83           C  
ANISOU 4866  CB  LEU B  83    23138  28786  14503   2479   1359    109       C  
ATOM   4867  CG  LEU B  83      19.919  -9.979 -12.683  1.00169.84           C  
ANISOU 4867  CG  LEU B  83    22322  28121  14087   2179   1132   -140       C  
ATOM   4868  CD1 LEU B  83      20.439  -9.635 -11.301  1.00171.92           C  
ANISOU 4868  CD1 LEU B  83    22689  27999  14634   1802   1140      3       C  
ATOM   4869  CD2 LEU B  83      18.426  -9.813 -12.718  1.00168.86           C  
ANISOU 4869  CD2 LEU B  83    22156  28275  13725   2426   1020   -311       C  
ATOM   4870  N   PRO B  84      22.946  -7.005 -14.455  1.00186.30           N  
ANISOU 4870  N   PRO B  84    25050  29608  16127   2542   1986    890       N  
ATOM   4871  CA  PRO B  84      23.859  -6.506 -15.487  1.00185.92           C  
ANISOU 4871  CA  PRO B  84    25102  29503  16035   2760   2280   1177       C  
ATOM   4872  C   PRO B  84      24.191  -7.494 -16.610  1.00186.12           C  
ANISOU 4872  C   PRO B  84    24964  29863  15888   2932   2257   1062       C  
ATOM   4873  O   PRO B  84      24.897  -7.118 -17.535  1.00187.43           O  
ANISOU 4873  O   PRO B  84    25210  30034  15970   3159   2515   1309       O  
ATOM   4874  CB  PRO B  84      25.114  -6.135 -14.694  1.00181.84           C  
ANISOU 4874  CB  PRO B  84    24641  28478  15972   2357   2402   1336       C  
ATOM   4875  CG  PRO B  84      25.083  -6.990 -13.486  1.00179.71           C  
ANISOU 4875  CG  PRO B  84    24217  28131  15933   1927   2109   1073       C  
ATOM   4876  CD  PRO B  84      23.655  -7.332 -13.205  1.00182.26           C  
ANISOU 4876  CD  PRO B  84    24482  28750  16016   2042   1884    835       C  
ATOM   4877  N   TYR B  85      23.681  -8.727 -16.542  1.00187.27           N  
ANISOU 4877  N   TYR B  85    24875  30276  16000   2838   1977    687       N  
ATOM   4878  CA  TYR B  85      23.947  -9.758 -17.565  1.00191.60           C  
ANISOU 4878  CA  TYR B  85    25232  31145  16418   2977   1937    486       C  
ATOM   4879  C   TYR B  85      22.623 -10.161 -18.208  1.00190.83           C  
ANISOU 4879  C   TYR B  85    25001  31580  15925   3325   1752    169       C  
ATOM   4880  O   TYR B  85      21.583  -9.625 -17.835  1.00186.42           O  
ANISOU 4880  O   TYR B  85    24505  31105  15219   3442   1669    153       O  
ATOM   4881  CB  TYR B  85      24.698 -10.978 -16.984  1.00189.62           C  
ANISOU 4881  CB  TYR B  85    24764  30700  16581   2534   1805    289       C  
ATOM   4882  CG  TYR B  85      24.265 -11.380 -15.603  1.00189.87           C  
ANISOU 4882  CG  TYR B  85    24704  30535  16900   2156   1588    142       C  
ATOM   4883  CD1 TYR B  85      23.210 -12.274 -15.403  1.00192.22           C  
ANISOU 4883  CD1 TYR B  85    24785  31073  17175   2145   1355   -217       C  
ATOM   4884  CD2 TYR B  85      24.904 -10.849 -14.487  1.00190.53           C  
ANISOU 4884  CD2 TYR B  85    24904  30205  17283   1824   1629    357       C  
ATOM   4885  CE1 TYR B  85      22.811 -12.628 -14.120  1.00189.77           C  
ANISOU 4885  CE1 TYR B  85    24393  30582  17127   1826   1198   -300       C  
ATOM   4886  CE2 TYR B  85      24.515 -11.198 -13.198  1.00186.79           C  
ANISOU 4886  CE2 TYR B  85    24351  29598  17019   1514   1441    246       C  
ATOM   4887  CZ  TYR B  85      23.467 -12.085 -13.013  1.00183.56           C  
ANISOU 4887  CZ  TYR B  85    23745  29421  16576   1525   1241    -53       C  
ATOM   4888  OH  TYR B  85      23.077 -12.451 -11.738  1.00171.07           O  
ANISOU 4888  OH  TYR B  85    22080  27716  15200   1247   1092   -120       O  
ATOM   4889  N   GLY B  86      22.689 -11.050 -19.205  1.00189.99           N  
ANISOU 4889  N   GLY B  86    24701  31839  15646   3504   1698    -91       N  
ATOM   4890  CA  GLY B  86      21.516 -11.591 -19.901  1.00186.00           C  
ANISOU 4890  CA  GLY B  86    23996  31886  14786   3822   1493   -491       C  
ATOM   4891  C   GLY B  86      21.360 -13.115 -19.935  1.00182.13           C  
ANISOU 4891  C   GLY B  86    23149  31540  14510   3616   1269  -1017       C  
ATOM   4892  O   GLY B  86      20.340 -13.596 -20.435  1.00172.44           O  
ANISOU 4892  O   GLY B  86    21712  30753  13053   3841   1080  -1418       O  
ATOM   4893  N   ALA B  87      22.317 -13.888 -19.408  1.00179.75           N  
ANISOU 4893  N   ALA B  87    22748  30875  14672   3198   1291  -1037       N  
ATOM   4894  CA  ALA B  87      22.214 -15.364 -19.429  1.00183.10           C  
ANISOU 4894  CA  ALA B  87    22813  31374  15382   2996   1128  -1517       C  
ATOM   4895  C   ALA B  87      22.527 -15.983 -18.068  1.00187.10           C  
ANISOU 4895  C   ALA B  87    23219  31403  16466   2475   1067  -1488       C  
ATOM   4896  O   ALA B  87      23.408 -15.486 -17.344  1.00190.73           O  
ANISOU 4896  O   ALA B  87    23866  31467  17133   2233   1185  -1103       O  
ATOM   4897  CB  ALA B  87      23.138 -15.950 -20.480  1.00183.31           C  
ANISOU 4897  CB  ALA B  87    22743  31541  15363   3103   1248  -1621       C  
ATOM   4898  N   THR B  88      21.857 -17.108 -17.766  1.00183.55           N  
ANISOU 4898  N   THR B  88    22446  31003  16289   2317    899  -1904       N  
ATOM   4899  CA  THR B  88      21.901 -17.727 -16.425  1.00172.97           C  
ANISOU 4899  CA  THR B  88    20982  29268  15467   1883    842  -1866       C  
ATOM   4900  C   THR B  88      22.019 -19.252 -16.487  1.00171.11           C  
ANISOU 4900  C   THR B  88    20355  28976  15681   1682    806  -2242       C  
ATOM   4901  O   THR B  88      22.090 -19.810 -17.557  1.00167.73           O  
ANISOU 4901  O   THR B  88    19756  28805  15168   1857    813  -2571       O  
ATOM   4902  CB  THR B  88      20.681 -17.271 -15.582  1.00170.70           C  
ANISOU 4902  CB  THR B  88    20738  28999  15119   1883    716  -1871       C  
ATOM   4903  OG1 THR B  88      20.720 -17.848 -14.267  1.00171.21           O  
ANISOU 4903  OG1 THR B  88    20689  28717  15643   1501    685  -1795       O  
ATOM   4904  CG2 THR B  88      19.371 -17.639 -16.253  1.00173.92           C  
ANISOU 4904  CG2 THR B  88    20915  29826  15338   2149    566  -2337       C  
ATOM   4905  N   SER B  89      22.071 -19.910 -15.333  1.00175.80           N  
ANISOU 4905  N   SER B  89    20805  29232  16758   1329    789  -2178       N  
ATOM   4906  CA  SER B  89      22.162 -21.380 -15.239  1.00184.57           C  
ANISOU 4906  CA  SER B  89    21522  30204  18399   1117    800  -2480       C  
ATOM   4907  C   SER B  89      21.561 -21.858 -13.885  1.00189.67           C  
ANISOU 4907  C   SER B  89    22020  30591  19455    849    759  -2413       C  
ATOM   4908  O   SER B  89      21.811 -21.268 -12.814  1.00190.86           O  
ANISOU 4908  O   SER B  89    22381  30529  19607    695    768  -2003       O  
ATOM   4909  CB  SER B  89      23.633 -21.839 -15.398  1.00183.25           C  
ANISOU 4909  CB  SER B  89    21339  29796  18492    948    949  -2297       C  
ATOM   4910  OG  SER B  89      23.796 -23.254 -15.367  1.00186.59           O  
ANISOU 4910  OG  SER B  89    21377  30058  19461    759    999  -2570       O  
ATOM   4911  N   THR B  90      20.763 -22.930 -13.943  1.00192.08           N  
ANISOU 4911  N   THR B  90    21944  30923  20114    807    727  -2830       N  
ATOM   4912  CA  THR B  90      20.131 -23.523 -12.745  1.00182.86           C  
ANISOU 4912  CA  THR B  90    20579  29510  19388    583    736  -2778       C  
ATOM   4913  C   THR B  90      20.953 -24.747 -12.274  1.00176.26           C  
ANISOU 4913  C   THR B  90    19469  28309  19190    300    888  -2693       C  
ATOM   4914  O   THR B  90      20.405 -25.760 -11.794  1.00172.78           O  
ANISOU 4914  O   THR B  90    18680  27693  19273    163    953  -2856       O  
ATOM   4915  CB  THR B  90      18.641 -23.893 -13.017  1.00181.48           C  
ANISOU 4915  CB  THR B  90    20126  29552  19274    714    637  -3267       C  
ATOM   4916  OG1 THR B  90      18.536 -24.622 -14.244  1.00183.03           O  
ANISOU 4916  OG1 THR B  90    20032  29963  19548    843    617  -3816       O  
ATOM   4917  CG2 THR B  90      17.766 -22.647 -13.136  1.00176.54           C  
ANISOU 4917  CG2 THR B  90    19775  29234  18066    972    498  -3231       C  
ATOM   4918  N   LEU B  91      22.277 -24.638 -12.430  1.00171.61           N  
ANISOU 4918  N   LEU B  91    19024  27596  18581    226    967  -2421       N  
ATOM   4919  CA  LEU B  91      23.222 -25.647 -11.973  1.00177.75           C  
ANISOU 4919  CA  LEU B  91    19587  28035  19912    -18   1117  -2250       C  
ATOM   4920  C   LEU B  91      23.541 -25.392 -10.510  1.00181.08           C  
ANISOU 4920  C   LEU B  91    20137  28226  20437   -211   1133  -1719       C  
ATOM   4921  O   LEU B  91      23.648 -26.331  -9.719  1.00180.58           O  
ANISOU 4921  O   LEU B  91    19817  27908  20885   -389   1243  -1580       O  
ATOM   4922  CB  LEU B  91      24.525 -25.598 -12.784  1.00184.48           C  
ANISOU 4922  CB  LEU B  91    20533  28876  20684      0   1192  -2182       C  
ATOM   4923  CG  LEU B  91      25.663 -26.566 -12.371  1.00189.79           C  
ANISOU 4923  CG  LEU B  91    21020  29197  21892   -240   1351  -1929       C  
ATOM   4924  CD1 LEU B  91      25.289 -28.036 -12.522  1.00188.23           C  
ANISOU 4924  CD1 LEU B  91    20393  28889  22234   -282   1483  -2349       C  
ATOM   4925  CD2 LEU B  91      26.940 -26.275 -13.158  1.00195.27           C  
ANISOU 4925  CD2 LEU B  91    21977  29862  22354   -246   1388  -1607       C  
ATOM   4926  N   LEU B  92      23.711 -24.119 -10.153  1.00187.44           N  
ANISOU 4926  N   LEU B  92    21327  29129  20763   -159   1039  -1423       N  
ATOM   4927  CA  LEU B  92      24.120 -23.751  -8.799  1.00195.47           C  
ANISOU 4927  CA  LEU B  92    22486  29987  21796   -325   1029   -955       C  
ATOM   4928  C   LEU B  92      23.043 -23.994  -7.727  1.00197.90           C  
ANISOU 4928  C   LEU B  92    22684  30267  22240   -369   1014   -906       C  
ATOM   4929  O   LEU B  92      23.375 -24.283  -6.556  1.00206.53           O  
ANISOU 4929  O   LEU B  92    23727  31205  23537   -520   1059   -556       O  
ATOM   4930  CB  LEU B  92      24.576 -22.291  -8.783  1.00194.31           C  
ANISOU 4930  CB  LEU B  92    22754  29938  21136   -260    947   -729       C  
ATOM   4931  CG  LEU B  92      25.778 -21.945  -9.664  1.00190.74           C  
ANISOU 4931  CG  LEU B  92    22430  29469  20572   -231   1002   -667       C  
ATOM   4932  CD1 LEU B  92      26.349 -20.612  -9.202  1.00189.48           C  
ANISOU 4932  CD1 LEU B  92    22622  29288  20084   -253    959   -351       C  
ATOM   4933  CD2 LEU B  92      26.846 -23.036  -9.618  1.00191.31           C  
ANISOU 4933  CD2 LEU B  92    22247  29325  21115   -408   1112   -568       C  
ATOM   4934  N   ALA B  93      21.777 -23.884  -8.140  1.00190.72           N  
ANISOU 4934  N   ALA B  93    21724  29529  21209   -216    958  -1248       N  
ATOM   4935  CA  ALA B  93      20.624 -24.187  -7.296  1.00184.85           C  
ANISOU 4935  CA  ALA B  93    20833  28762  20638   -233    970  -1267       C  
ATOM   4936  C   ALA B  93      20.246 -25.660  -7.477  1.00183.29           C  
ANISOU 4936  C   ALA B  93    20162  28399  21078   -307   1111  -1533       C  
ATOM   4937  O   ALA B  93      19.782 -26.048  -8.557  1.00186.58           O  
ANISOU 4937  O   ALA B  93    20387  28926  21578   -206   1094  -2013       O  
ATOM   4938  CB  ALA B  93      19.463 -23.281  -7.684  1.00184.65           C  
ANISOU 4938  CB  ALA B  93    20973  29001  20182    -25    841  -1509       C  
ATOM   4939  N   GLY B  94      20.467 -26.468  -6.432  1.00180.69           N  
ANISOU 4939  N   GLY B  94    19634  27816  21204   -468   1261  -1225       N  
ATOM   4940  CA  GLY B  94      20.180 -27.914  -6.449  1.00180.94           C  
ANISOU 4940  CA  GLY B  94    19188  27603  21955   -557   1461  -1400       C  
ATOM   4941  C   GLY B  94      18.697 -28.215  -6.487  1.00182.97           C  
ANISOU 4941  C   GLY B  94    19208  27899  22413   -488   1482  -1759       C  
ATOM   4942  O   GLY B  94      18.243 -29.097  -7.219  1.00189.34           O  
ANISOU 4942  O   GLY B  94    19646  28632  23663   -490   1561  -2222       O  
ATOM   4943  N   ASP B  95      17.949 -27.437  -5.718  1.00183.48           N  
ANISOU 4943  N   ASP B  95    19478  28088  22147   -425   1405  -1576       N  
ATOM   4944  CA  ASP B  95      16.483 -27.472  -5.681  1.00192.76           C  
ANISOU 4944  CA  ASP B  95    20486  29340  23412   -338   1399  -1877       C  
ATOM   4945  C   ASP B  95      15.759 -27.061  -6.977  1.00193.01           C  
ANISOU 4945  C   ASP B  95    20507  29664  23162   -164   1216  -2467       C  
ATOM   4946  O   ASP B  95      14.560 -27.336  -7.128  1.00195.22           O  
ANISOU 4946  O   ASP B  95    20532  29998  23643   -101   1216  -2825       O  
ATOM   4947  CB  ASP B  95      15.987 -26.588  -4.521  1.00200.60           C  
ANISOU 4947  CB  ASP B  95    21763  30422  24033   -296   1357  -1493       C  
ATOM   4948  CG  ASP B  95      16.373 -25.102  -4.671  1.00207.63           C  
ANISOU 4948  CG  ASP B  95    23159  31572  24158   -194   1137  -1366       C  
ATOM   4949  OD1 ASP B  95      17.189 -24.742  -5.545  1.00214.14           O  
ANISOU 4949  OD1 ASP B  95    24141  32482  24737   -164   1042  -1460       O  
ATOM   4950  OD2 ASP B  95      15.891 -24.271  -3.874  1.00214.94           O  
ANISOU 4950  OD2 ASP B  95    24326  32597  24745   -141   1086  -1153       O  
ATOM   4951  N   SER B  96      16.463 -26.377  -7.879  1.00192.65           N  
ANISOU 4951  N   SER B  96    20729  29827  22643    -67   1068  -2550       N  
ATOM   4952  CA  SER B  96      15.900 -25.847  -9.115  1.00198.49           C  
ANISOU 4952  CA  SER B  96    21512  30918  22986    156    888  -3025       C  
ATOM   4953  C   SER B  96      16.520 -26.490 -10.374  1.00209.80           C  
ANISOU 4953  C   SER B  96    22750  32411  24552    185    892  -3423       C  
ATOM   4954  O   SER B  96      17.734 -26.638 -10.467  1.00210.46           O  
ANISOU 4954  O   SER B  96    22933  32359  24672     91    963  -3195       O  
ATOM   4955  CB  SER B  96      16.125 -24.340  -9.166  1.00195.46           C  
ANISOU 4955  CB  SER B  96    21635  30771  21858    312    737  -2759       C  
ATOM   4956  OG  SER B  96      15.623 -23.725  -7.992  1.00195.43           O  
ANISOU 4956  OG  SER B  96    21819  30711  21722    281    740  -2415       O  
ATOM   4957  N   ASP B  97      15.648 -26.873 -11.316  1.00216.46           N  
ANISOU 4957  N   ASP B  97    23298  33477  25469    321    811  -4040       N  
ATOM   4958  CA  ASP B  97      16.003 -27.370 -12.665  1.00209.11           C  
ANISOU 4958  CA  ASP B  97    22173  32729  24547    418    773  -4548       C  
ATOM   4959  C   ASP B  97      15.557 -26.411 -13.774  1.00209.77           C  
ANISOU 4959  C   ASP B  97    22452  33345  23905    755    547  -4839       C  
ATOM   4960  O   ASP B  97      16.179 -26.349 -14.815  1.00207.60           O  
ANISOU 4960  O   ASP B  97    22231  33290  23356    895    507  -5027       O  
ATOM   4961  CB  ASP B  97      15.356 -28.740 -12.915  1.00204.72           C  
ANISOU 4961  CB  ASP B  97    21028  32026  24729    311    870  -5124       C  
ATOM   4962  CG  ASP B  97      15.717 -29.762 -11.851  1.00200.94           C  
ANISOU 4962  CG  ASP B  97    20307  31006  25032     13   1143  -4818       C  
ATOM   4963  OD1 ASP B  97      16.870 -29.717 -11.358  1.00193.83           O  
ANISOU 4963  OD1 ASP B  97    19624  29886  24134   -107   1250  -4300       O  
ATOM   4964  OD2 ASP B  97      14.840 -30.596 -11.503  1.00201.63           O  
ANISOU 4964  OD2 ASP B  97    19976  30895  25740    -84   1261  -5081       O  
ATOM   4965  N   SER B  98      14.441 -25.716 -13.555  1.00210.36           N  
ANISOU 4965  N   SER B  98    22602  33635  23688    906    416  -4877       N  
ATOM   4966  CA  SER B  98      13.950 -24.672 -14.441  1.00210.98           C  
ANISOU 4966  CA  SER B  98    22896  34219  23045   1261    216  -5032       C  
ATOM   4967  C   SER B  98      14.220 -23.268 -13.867  1.00205.04           C  
ANISOU 4967  C   SER B  98    22682  33473  21750   1343    200  -4415       C  
ATOM   4968  O   SER B  98      14.315 -23.095 -12.648  1.00211.09           O  
ANISOU 4968  O   SER B  98    23590  33916  22698   1138    290  -3984       O  
ATOM   4969  CB  SER B  98      12.448 -24.876 -14.624  1.00213.55           C  
ANISOU 4969  CB  SER B  98    22887  34789  23460   1390     83  -5537       C  
ATOM   4970  OG  SER B  98      11.887 -23.855 -15.418  1.00219.81           O  
ANISOU 4970  OG  SER B  98    23870  36097  23548   1765   -112  -5652       O  
ATOM   4971  N   GLN B  99      14.362 -22.273 -14.744  1.00198.25           N  
ANISOU 4971  N   GLN B  99    22108  32981  20236   1653    104  -4374       N  
ATOM   4972  CA  GLN B  99      14.430 -20.874 -14.299  1.00192.12           C  
ANISOU 4972  CA  GLN B  99    21801  32221  18973   1768    101  -3864       C  
ATOM   4973  C   GLN B  99      13.168 -20.470 -13.556  1.00193.63           C  
ANISOU 4973  C   GLN B  99    21977  32439  19152   1804     31  -3855       C  
ATOM   4974  O   GLN B  99      13.243 -19.692 -12.624  1.00205.11           O  
ANISOU 4974  O   GLN B  99    23732  33698  20500   1725     85  -3414       O  
ATOM   4975  CB  GLN B  99      14.624 -19.895 -15.456  1.00191.92           C  
ANISOU 4975  CB  GLN B  99    22034  32604  18280   2153     44  -3836       C  
ATOM   4976  CG  GLN B  99      16.061 -19.658 -15.888  1.00190.97           C  
ANISOU 4976  CG  GLN B  99    22155  32382  18021   2135    172  -3540       C  
ATOM   4977  CD  GLN B  99      16.179 -18.545 -16.933  1.00187.51           C  
ANISOU 4977  CD  GLN B  99    22002  32327  16913   2552    167  -3410       C  
ATOM   4978  OE1 GLN B  99      15.810 -17.405 -16.680  1.00190.19           O  
ANISOU 4978  OE1 GLN B  99    22630  32713  16919   2713    173  -3100       O  
ATOM   4979  NE2 GLN B  99      16.710 -18.869 -18.096  1.00188.14           N  
ANISOU 4979  NE2 GLN B  99    22001  32674  16809   2740    185  -3624       N  
ATOM   4980  N   GLU B 100      12.020 -21.000 -13.977  1.00192.59           N  
ANISOU 4980  N   GLU B 100    21478  32556  19140   1924    -84  -4369       N  
ATOM   4981  CA  GLU B 100      10.723 -20.729 -13.346  1.00196.12           C  
ANISOU 4981  CA  GLU B 100    21841  33044  19629   1969   -147  -4423       C  
ATOM   4982  C   GLU B 100      10.616 -21.320 -11.941  1.00194.58           C  
ANISOU 4982  C   GLU B 100    21539  32384  20007   1617     -3  -4204       C  
ATOM   4983  O   GLU B 100      10.083 -20.681 -11.017  1.00192.05           O  
ANISOU 4983  O   GLU B 100    21398  31965  19605   1600     21  -3911       O  
ATOM   4984  CB  GLU B 100       9.587 -21.277 -14.224  1.00202.23           C  
ANISOU 4984  CB  GLU B 100    22175  34209  20454   2173   -312  -5095       C  
ATOM   4985  CG  GLU B 100       9.297 -20.470 -15.500  1.00200.88           C  
ANISOU 4985  CG  GLU B 100    22113  34627  19586   2627   -487  -5283       C  
ATOM   4986  CD  GLU B 100      10.099 -20.857 -16.745  1.00191.67           C  
ANISOU 4986  CD  GLU B 100    20872  33729  18223   2768   -522  -5559       C  
ATOM   4987  OE1 GLU B 100      11.195 -21.440 -16.643  1.00193.02           O  
ANISOU 4987  OE1 GLU B 100    21063  33593  18682   2525   -385  -5446       O  
ATOM   4988  OE2 GLU B 100       9.628 -20.535 -17.845  1.00179.41           O  
ANISOU 4988  OE2 GLU B 100    19246  32731  16189   3156   -684  -5875       O  
ATOM   4989  N   GLU B 101      11.141 -22.532 -11.790  1.00195.12           N  
ANISOU 4989  N   GLU B 101    21313  32176  20648   1358    110  -4330       N  
ATOM   4990  CA  GLU B 101      11.250 -23.183 -10.486  1.00198.92           C  
ANISOU 4990  CA  GLU B 101    21688  32208  21682   1044    290  -4043       C  
ATOM   4991  C   GLU B 101      12.158 -22.386  -9.547  1.00189.02           C  
ANISOU 4991  C   GLU B 101    20892  30749  20179    933    367  -3394       C  
ATOM   4992  O   GLU B 101      11.811 -22.175  -8.383  1.00181.43           O  
ANISOU 4992  O   GLU B 101    20017  29611  19304    831    441  -3084       O  
ATOM   4993  CB  GLU B 101      11.812 -24.592 -10.644  1.00209.73           C  
ANISOU 4993  CB  GLU B 101    22670  33319  23697    824    424  -4262       C  
ATOM   4994  CG  GLU B 101      11.920 -25.375  -9.339  1.00216.66           C  
ANISOU 4994  CG  GLU B 101    23389  33742  25189    537    649  -3937       C  
ATOM   4995  CD  GLU B 101      12.354 -26.818  -9.547  1.00223.55           C  
ANISOU 4995  CD  GLU B 101    23822  34333  26782    343    817  -4178       C  
ATOM   4996  OE1 GLU B 101      13.056 -27.118 -10.543  1.00236.73           O  
ANISOU 4996  OE1 GLU B 101    25435  36096  28415    373    776  -4443       O  
ATOM   4997  OE2 GLU B 101      12.042 -27.655  -8.693  1.00221.21           O  
ANISOU 4997  OE2 GLU B 101    23240  33703  27105    166   1019  -4072       O  
ATOM   4998  N   ALA B 102      13.306 -21.948 -10.070  1.00185.40           N  
ANISOU 4998  N   ALA B 102    20701  30327  19413    964    353  -3218       N  
ATOM   4999  CA  ALA B 102      14.245 -21.102  -9.319  1.00183.00           C  
ANISOU 4999  CA  ALA B 102    20817  29857  18856    869    405  -2668       C  
ATOM   5000  C   ALA B 102      13.607 -19.819  -8.822  1.00181.44           C  
ANISOU 5000  C   ALA B 102    20947  29771  18220   1011    346  -2453       C  
ATOM   5001  O   ALA B 102      13.763 -19.441  -7.638  1.00179.38           O  
ANISOU 5001  O   ALA B 102    20871  29317  17967    868    407  -2086       O  
ATOM   5002  CB  ALA B 102      15.459 -20.757 -10.167  1.00188.43           C  
ANISOU 5002  CB  ALA B 102    21711  30602  19282    924    402  -2580       C  
ATOM   5003  N   HIS B 103      12.851 -19.173  -9.711  1.00182.18           N  
ANISOU 5003  N   HIS B 103    21089  30195  17933   1307    232  -2695       N  
ATOM   5004  CA  HIS B 103      12.127 -17.952  -9.364  1.00183.25           C  
ANISOU 5004  CA  HIS B 103    21505  30447  17673   1483    190  -2528       C  
ATOM   5005  C   HIS B 103      11.092 -18.202  -8.247  1.00188.81           C  
ANISOU 5005  C   HIS B 103    22065  31034  18640   1378    222  -2517       C  
ATOM   5006  O   HIS B 103      10.958 -17.395  -7.324  1.00187.41           O  
ANISOU 5006  O   HIS B 103    22154  30757  18296   1351    262  -2210       O  
ATOM   5007  CB  HIS B 103      11.440 -17.378 -10.597  1.00181.52           C  
ANISOU 5007  CB  HIS B 103    21292  30641  17037   1857     69  -2803       C  
ATOM   5008  CG  HIS B 103      10.689 -16.118 -10.336  1.00177.05           C  
ANISOU 5008  CG  HIS B 103    20995  30190  16084   2070     47  -2624       C  
ATOM   5009  ND1 HIS B 103       9.322 -16.096 -10.144  1.00176.78           N  
ANISOU 5009  ND1 HIS B 103    20787  30310  16071   2196    -22  -2833       N  
ATOM   5010  CD2 HIS B 103      11.109 -14.838 -10.232  1.00171.12           C  
ANISOU 5010  CD2 HIS B 103    20659  29399  14959   2179    107  -2262       C  
ATOM   5011  CE1 HIS B 103       8.933 -14.854  -9.926  1.00174.72           C  
ANISOU 5011  CE1 HIS B 103    20833  30106  15444   2381     -8  -2594       C  
ATOM   5012  NE2 HIS B 103       9.997 -14.072  -9.976  1.00175.28           N  
ANISOU 5012  NE2 HIS B 103    21263  30050  15284   2372     77  -2252       N  
ATOM   5013  N   GLY B 104      10.399 -19.338  -8.306  1.00187.73           N  
ANISOU 5013  N   GLY B 104    21493  30889  18946   1313    226  -2857       N  
ATOM   5014  CA  GLY B 104       9.473 -19.726  -7.238  1.00184.71           C  
ANISOU 5014  CA  GLY B 104    20925  30354  18899   1202    306  -2825       C  
ATOM   5015  C   GLY B 104      10.150 -19.991  -5.905  1.00176.40           C  
ANISOU 5015  C   GLY B 104    19973  28968  18082    935    463  -2386       C  
ATOM   5016  O   GLY B 104       9.643 -19.571  -4.857  1.00173.92           O  
ANISOU 5016  O   GLY B 104    19780  28585  17716    913    524  -2149       O  
ATOM   5017  N   LYS B 105      11.309 -20.656  -5.948  1.00170.34           N  
ANISOU 5017  N   LYS B 105    19157  28024  17540    757    528  -2271       N  
ATOM   5018  CA  LYS B 105      12.143 -20.813  -4.744  1.00164.12           C  
ANISOU 5018  CA  LYS B 105    18491  26981  16887    539    651  -1814       C  
ATOM   5019  C   LYS B 105      12.571 -19.459  -4.182  1.00157.27           C  
ANISOU 5019  C   LYS B 105    18096  26160  15500    575    598  -1477       C  
ATOM   5020  O   LYS B 105      12.462 -19.214  -2.936  1.00160.50           O  
ANISOU 5020  O   LYS B 105    18620  26483  15879    495    665  -1180       O  
ATOM   5021  CB  LYS B 105      13.378 -21.671  -5.039  1.00169.62           C  
ANISOU 5021  CB  LYS B 105    19059  27510  17879    374    714  -1757       C  
ATOM   5022  CG  LYS B 105      13.064 -23.136  -5.342  1.00175.81           C  
ANISOU 5022  CG  LYS B 105    19341  28151  19304    284    827  -2048       C  
ATOM   5023  CD  LYS B 105      12.555 -23.850  -4.094  1.00180.58           C  
ANISOU 5023  CD  LYS B 105    19724  28531  20356    159   1016  -1818       C  
ATOM   5024  CE  LYS B 105      12.281 -25.337  -4.265  1.00182.51           C  
ANISOU 5024  CE  LYS B 105    19442  28548  21353     50   1195  -2055       C  
ATOM   5025  NZ  LYS B 105      11.284 -25.639  -5.320  1.00185.71           N  
ANISOU 5025  NZ  LYS B 105    19543  29093  21923    160   1116  -2670       N  
ATOM   5026  N   LEU B 106      12.981 -18.552  -5.086  1.00153.75           N  
ANISOU 5026  N   LEU B 106    17909  25862  14647    717    495  -1537       N  
ATOM   5027  CA  LEU B 106      13.287 -17.160  -4.646  1.00154.95           C  
ANISOU 5027  CA  LEU B 106    18492  26031  14350    768    468  -1270       C  
ATOM   5028  C   LEU B 106      12.130 -16.429  -3.950  1.00153.24           C  
ANISOU 5028  C   LEU B 106    18390  25886  13947    880    469  -1245       C  
ATOM   5029  O   LEU B 106      12.332 -15.656  -2.991  1.00155.38           O  
ANISOU 5029  O   LEU B 106    18923  26086  14027    821    497   -992       O  
ATOM   5030  CB  LEU B 106      13.794 -16.288  -5.787  1.00157.74           C  
ANISOU 5030  CB  LEU B 106    19079  26509  14345    942    409  -1318       C  
ATOM   5031  CG  LEU B 106      15.202 -16.645  -6.246  1.00158.37           C  
ANISOU 5031  CG  LEU B 106    19172  26480  14521    815    435  -1223       C  
ATOM   5032  CD1 LEU B 106      15.458 -15.973  -7.581  1.00159.21           C  
ANISOU 5032  CD1 LEU B 106    19428  26759  14305   1050    407  -1324       C  
ATOM   5033  CD2 LEU B 106      16.274 -16.253  -5.231  1.00159.41           C  
ANISOU 5033  CD2 LEU B 106    19515  26404  14649    598    478   -866       C  
ATOM   5034  N   VAL B 107      10.916 -16.722  -4.400  1.00150.99           N  
ANISOU 5034  N   VAL B 107    17878  25747  13743   1034    438  -1535       N  
ATOM   5035  CA  VAL B 107       9.731 -16.207  -3.740  1.00149.73           C  
ANISOU 5035  CA  VAL B 107    17758  25646  13484   1137    457  -1531       C  
ATOM   5036  C   VAL B 107       9.579 -16.839  -2.321  1.00145.15           C  
ANISOU 5036  C   VAL B 107    17061  24887  13200    941    585  -1317       C  
ATOM   5037  O   VAL B 107       9.083 -16.174  -1.414  1.00142.63           O  
ANISOU 5037  O   VAL B 107    16917  24570  12706    971    629  -1160       O  
ATOM   5038  CB  VAL B 107       8.484 -16.322  -4.670  1.00149.55           C  
ANISOU 5038  CB  VAL B 107    17497  25858  13465   1375    375  -1916       C  
ATOM   5039  CG1 VAL B 107       7.221 -15.868  -3.973  1.00149.87           C  
ANISOU 5039  CG1 VAL B 107    17540  25946  13457   1477    408  -1913       C  
ATOM   5040  CG2 VAL B 107       8.689 -15.455  -5.910  1.00148.72           C  
ANISOU 5040  CG2 VAL B 107    17587  25979  12938   1626    267  -2015       C  
ATOM   5041  N   LEU B 108      10.034 -18.079  -2.113  1.00143.47           N  
ANISOU 5041  N   LEU B 108    16562  24527  13422    761    666  -1285       N  
ATOM   5042  CA  LEU B 108      10.017 -18.674  -0.755  1.00146.16           C  
ANISOU 5042  CA  LEU B 108    16801  24714  14017    610    819   -997       C  
ATOM   5043  C   LEU B 108      11.120 -18.104   0.117  1.00144.84           C  
ANISOU 5043  C   LEU B 108    16950  24501  13580    497    816   -631       C  
ATOM   5044  O   LEU B 108      10.917 -17.841   1.305  1.00148.18           O  
ANISOU 5044  O   LEU B 108    17478  24928  13894    475    887   -394       O  
ATOM   5045  CB  LEU B 108      10.178 -20.191  -0.764  1.00151.16           C  
ANISOU 5045  CB  LEU B 108    17010  25174  15247    471    949  -1028       C  
ATOM   5046  CG  LEU B 108       9.187 -21.077  -1.519  1.00156.35           C  
ANISOU 5046  CG  LEU B 108    17236  25822  16347    523    984  -1436       C  
ATOM   5047  CD1 LEU B 108       9.740 -22.497  -1.486  1.00160.87           C  
ANISOU 5047  CD1 LEU B 108    17441  26156  17526    349   1141  -1407       C  
ATOM   5048  CD2 LEU B 108       7.778 -21.011  -0.951  1.00152.57           C  
ANISOU 5048  CD2 LEU B 108    16621  25372  15974    617   1068  -1496       C  
ATOM   5049  N   TRP B 109      12.304 -17.908  -0.452  1.00143.60           N  
ANISOU 5049  N   TRP B 109    16931  24318  13311    430    735   -598       N  
ATOM   5050  CA  TRP B 109      13.375 -17.257   0.341  1.00144.64           C  
ANISOU 5050  CA  TRP B 109    17350  24422  13182    320    708   -302       C  
ATOM   5051  C   TRP B 109      12.993 -15.845   0.770  1.00143.89           C  
ANISOU 5051  C   TRP B 109    17605  24418  12647    420    661   -282       C  
ATOM   5052  O   TRP B 109      13.246 -15.430   1.912  1.00140.54           O  
ANISOU 5052  O   TRP B 109    17333  24009  12053    354    677    -79       O  
ATOM   5053  CB  TRP B 109      14.706 -17.225  -0.410  1.00143.86           C  
ANISOU 5053  CB  TRP B 109    17328  24263  13068    234    642   -285       C  
ATOM   5054  CG  TRP B 109      15.352 -18.547  -0.411  1.00148.18           C  
ANISOU 5054  CG  TRP B 109    17572  24689  14038     94    712   -199       C  
ATOM   5055  CD1 TRP B 109      15.325 -19.485  -1.400  1.00152.91           C  
ANISOU 5055  CD1 TRP B 109    17890  25231  14976     96    743   -418       C  
ATOM   5056  CD2 TRP B 109      16.085 -19.114   0.664  1.00152.56           C  
ANISOU 5056  CD2 TRP B 109    18048  25174  14741    -52    777    126       C  
ATOM   5057  NE1 TRP B 109      16.013 -20.603  -1.011  1.00151.60           N  
ANISOU 5057  NE1 TRP B 109    17478  24915  15206    -54    845   -239       N  
ATOM   5058  CE2 TRP B 109      16.496 -20.398   0.255  1.00154.51           C  
ANISOU 5058  CE2 TRP B 109    17967  25284  15455   -136    867    124       C  
ATOM   5059  CE3 TRP B 109      16.443 -18.655   1.942  1.00152.93           C  
ANISOU 5059  CE3 TRP B 109    18259  25287  14557   -104    766    412       C  
ATOM   5060  CZ2 TRP B 109      17.245 -21.232   1.077  1.00158.08           C  
ANISOU 5060  CZ2 TRP B 109    18253  25645  16162   -255    962    450       C  
ATOM   5061  CZ3 TRP B 109      17.191 -19.482   2.757  1.00153.01           C  
ANISOU 5061  CZ3 TRP B 109    18103  25262  14769   -211    833    719       C  
ATOM   5062  CH2 TRP B 109      17.583 -20.761   2.322  1.00155.38           C  
ANISOU 5062  CH2 TRP B 109    18078  25409  15550   -280    938    763       C  
ATOM   5063  N   SER B 110      12.302 -15.141  -0.115  1.00145.82           N  
ANISOU 5063  N   SER B 110    17949  24742  12714    599    612   -504       N  
ATOM   5064  CA  SER B 110      11.911 -13.779   0.194  1.00150.02           C  
ANISOU 5064  CA  SER B 110    18799  25324  12876    712    598   -491       C  
ATOM   5065  C   SER B 110      10.955 -13.612   1.394  1.00148.95           C  
ANISOU 5065  C   SER B 110    18678  25233  12683    741    671   -420       C  
ATOM   5066  O   SER B 110      10.629 -12.501   1.760  1.00138.73           O  
ANISOU 5066  O   SER B 110    17640  23965  11105    824    677   -419       O  
ATOM   5067  CB  SER B 110      11.333 -13.136  -1.059  1.00158.49           C  
ANISOU 5067  CB  SER B 110    19941  26490  13786    941    552   -704       C  
ATOM   5068  OG  SER B 110      10.085 -13.714  -1.388  1.00156.50           O  
ANISOU 5068  OG  SER B 110    19425  26350  13688   1075    554   -909       O  
ATOM   5069  N   GLY B 111      10.521 -14.706   2.016  1.00154.42           N  
ANISOU 5069  N   GLY B 111    19088  25917  13665    681    755   -351       N  
ATOM   5070  CA  GLY B 111       9.920 -14.633   3.360  1.00156.35           C  
ANISOU 5070  CA  GLY B 111    19356  26206  13843    685    857   -191       C  
ATOM   5071  C   GLY B 111      10.868 -14.201   4.490  1.00156.42           C  
ANISOU 5071  C   GLY B 111    19579  26243  13609    567    845     43       C  
ATOM   5072  O   GLY B 111      10.408 -13.881   5.612  1.00154.50           O  
ANISOU 5072  O   GLY B 111    19421  26090  13190    604    914    149       O  
ATOM   5073  N   LEU B 112      12.181 -14.203   4.194  1.00151.21           N  
ANISOU 5073  N   LEU B 112    18986  25530  12935    434    756    103       N  
ATOM   5074  CA  LEU B 112      13.198 -13.613   5.067  1.00145.89           C  
ANISOU 5074  CA  LEU B 112    18518  24903  12009    321    696    245       C  
ATOM   5075  C   LEU B 112      13.327 -12.115   4.958  1.00145.09           C  
ANISOU 5075  C   LEU B 112    18755  24786  11585    357    634     97       C  
ATOM   5076  O   LEU B 112      14.237 -11.582   5.533  1.00146.13           O  
ANISOU 5076  O   LEU B 112    19033  24936  11552    247    571    142       O  
ATOM   5077  CB  LEU B 112      14.582 -14.199   4.799  1.00143.93           C  
ANISOU 5077  CB  LEU B 112    18179  24591  11916    160    630    362       C  
ATOM   5078  CG  LEU B 112      14.820 -15.593   5.361  1.00148.97           C  
ANISOU 5078  CG  LEU B 112    18509  25246  12844     94    710    606       C  
ATOM   5079  CD1 LEU B 112      14.675 -16.631   4.276  1.00151.21           C  
ANISOU 5079  CD1 LEU B 112    18518  25387  13545     89    765    523       C  
ATOM   5080  CD2 LEU B 112      16.206 -15.703   5.954  1.00149.66           C  
ANISOU 5080  CD2 LEU B 112    18614  25385  12865    -45    632    807       C  
ATOM   5081  N   ARG B 113      12.447 -11.435   4.226  1.00148.95           N  
ANISOU 5081  N   ARG B 113    19346  25239  12007    514    658    -79       N  
ATOM   5082  CA  ARG B 113      12.381  -9.959   4.218  1.00151.67           C  
ANISOU 5082  CA  ARG B 113    20003  25538  12083    582    658   -193       C  
ATOM   5083  C   ARG B 113      12.311  -9.292   5.560  1.00152.32           C  
ANISOU 5083  C   ARG B 113    20245  25696  11931    545    680   -181       C  
ATOM   5084  O   ARG B 113      12.823  -8.161   5.725  1.00153.28           O  
ANISOU 5084  O   ARG B 113    20604  25744  11890    505    664   -275       O  
ATOM   5085  CB  ARG B 113      11.135  -9.480   3.471  1.00160.04           C  
ANISOU 5085  CB  ARG B 113    21098  26601  13108    810    713   -334       C  
ATOM   5086  CG  ARG B 113      11.316  -9.157   1.993  1.00162.14           C  
ANISOU 5086  CG  ARG B 113    21402  26801  13401    924    688   -419       C  
ATOM   5087  CD  ARG B 113       9.940  -9.094   1.279  1.00160.82           C  
ANISOU 5087  CD  ARG B 113    21150  26729  13224   1179    715   -549       C  
ATOM   5088  NE  ARG B 113       9.990  -9.415  -0.152  1.00158.90           N  
ANISOU 5088  NE  ARG B 113    20789  26536  13046   1305    664   -637       N  
ATOM   5089  CZ  ARG B 113      10.114  -8.536  -1.159  1.00158.53           C  
ANISOU 5089  CZ  ARG B 113    20909  26483  12842   1486    678   -655       C  
ATOM   5090  NH1 ARG B 113      10.181  -8.994  -2.418  1.00159.02           N  
ANISOU 5090  NH1 ARG B 113    20830  26655  12935   1613    624   -739       N  
ATOM   5091  NH2 ARG B 113      10.156  -7.214  -0.953  1.00158.32           N  
ANISOU 5091  NH2 ARG B 113    21172  26347  12635   1563    765   -592       N  
ATOM   5092  N   ASN B 114      11.629  -9.960   6.491  1.00158.80           N  
ANISOU 5092  N   ASN B 114    20926  26660  12749    575    737    -83       N  
ATOM   5093  CA  ASN B 114      11.344  -9.350   7.813  1.00166.04           C  
ANISOU 5093  CA  ASN B 114    21985  27710  13392    593    776    -89       C  
ATOM   5094  C   ASN B 114      12.523  -9.089   8.765  1.00162.82           C  
ANISOU 5094  C   ASN B 114    21663  27408  12791    438    684    -54       C  
ATOM   5095  O   ASN B 114      12.538  -8.034   9.371  1.00164.05           O  
ANISOU 5095  O   ASN B 114    22026  27597  12707    440    679   -211       O  
ATOM   5096  CB  ASN B 114      10.223 -10.093   8.537  1.00171.97           C  
ANISOU 5096  CB  ASN B 114    22562  28597  14178    705    900     29       C  
ATOM   5097  CG  ASN B 114       8.943 -10.157   7.720  1.00172.69           C  
ANISOU 5097  CG  ASN B 114    22566  28609  14438    868    981    -71       C  
ATOM   5098  OD1 ASN B 114       8.619  -9.244   6.944  1.00165.61           O  
ANISOU 5098  OD1 ASN B 114    21828  27618  13478    960    963   -245       O  
ATOM   5099  ND2 ASN B 114       8.201 -11.232   7.914  1.00173.97           N  
ANISOU 5099  ND2 ASN B 114    22454  28816  14830    918   1082     42       N  
ATOM   5100  N   ALA B 115      13.445 -10.045   8.906  1.00158.97           N  
ANISOU 5100  N   ALA B 115    20996  26983  12421    317    616    128       N  
ATOM   5101  CA  ALA B 115      14.789  -9.900   9.569  1.00159.23           C  
ANISOU 5101  CA  ALA B 115    21057  27124  12316    159    485    156       C  
ATOM   5102  C   ALA B 115      15.781  -8.957   8.830  1.00159.37           C  
ANISOU 5102  C   ALA B 115    21238  26942  12372     31    393    -35       C  
ATOM   5103  O   ALA B 115      16.462  -9.429   7.918  1.00147.89           O  
ANISOU 5103  O   ALA B 115    19689  25347  11153    -44    358     35       O  
ATOM   5104  CB  ALA B 115      15.378 -11.294   9.622  1.00155.40           C  
ANISOU 5104  CB  ALA B 115    20297  26708  12039    100    470    439       C  
ATOM   5105  N   PRO B 116      15.908  -7.648   9.239  1.00164.54           N  
ANISOU 5105  N   PRO B 116    22117  27569  12829      5    374   -277       N  
ATOM   5106  CA  PRO B 116      16.779  -6.752   8.461  1.00165.62           C  
ANISOU 5106  CA  PRO B 116    22384  27454  13089   -104    345   -438       C  
ATOM   5107  C   PRO B 116      18.227  -7.178   8.390  1.00162.73           C  
ANISOU 5107  C   PRO B 116    21894  27089  12845   -293    217   -366       C  
ATOM   5108  O   PRO B 116      18.830  -7.124   7.323  1.00158.63           O  
ANISOU 5108  O   PRO B 116    21375  26345  12551   -349    231   -346       O  
ATOM   5109  CB  PRO B 116      16.651  -5.394   9.194  1.00168.24           C  
ANISOU 5109  CB  PRO B 116    22926  27773  13225   -114    368   -723       C  
ATOM   5110  CG  PRO B 116      15.341  -5.461   9.895  1.00168.71           C  
ANISOU 5110  CG  PRO B 116    23015  28007  13078     56    452   -717       C  
ATOM   5111  CD  PRO B 116      15.330  -6.895  10.377  1.00169.31           C  
ANISOU 5111  CD  PRO B 116    22856  28341  13131     70    402   -436       C  
ATOM   5112  N   ARG B 117      18.752  -7.632   9.518  1.00163.91           N  
ANISOU 5112  N   ARG B 117    21926  27519  12832   -365    100   -306       N  
ATOM   5113  CA  ARG B 117      20.146  -8.035   9.603  1.00164.32           C  
ANISOU 5113  CA  ARG B 117    21833  27621  12977   -535    -39   -235       C  
ATOM   5114  C   ARG B 117      20.457  -9.231   8.678  1.00161.60           C  
ANISOU 5114  C   ARG B 117    21302  27171  12926   -546    -14     35       C  
ATOM   5115  O   ARG B 117      21.491  -9.274   8.045  1.00165.11           O  
ANISOU 5115  O   ARG B 117    21695  27467  13571   -672    -62     48       O  
ATOM   5116  CB  ARG B 117      20.522  -8.343  11.058  1.00165.27           C  
ANISOU 5116  CB  ARG B 117    21842  28144  12807   -551   -173   -197       C  
ATOM   5117  CG  ARG B 117      20.572  -7.092  11.995  1.00166.89           C  
ANISOU 5117  CG  ARG B 117    22201  28482  12726   -585   -243   -561       C  
ATOM   5118  CD  ARG B 117      21.636  -6.009  11.611  1.00166.83           C  
ANISOU 5118  CD  ARG B 117    22265  28233  12887   -784   -313   -878       C  
ATOM   5119  NE  ARG B 117      22.263  -5.284  12.734  1.00171.23           N  
ANISOU 5119  NE  ARG B 117    22808  29037  13213   -882   -471  -1205       N  
ATOM   5120  CZ  ARG B 117      23.402  -5.625  13.367  1.00178.22           C  
ANISOU 5120  CZ  ARG B 117    23497  30199  14017   -994   -681  -1219       C  
ATOM   5121  NH1 ARG B 117      24.067  -6.757  13.102  1.00178.17           N  
ANISOU 5121  NH1 ARG B 117    23289  30274  14132  -1017   -751   -874       N  
ATOM   5122  NH2 ARG B 117      23.869  -4.829  14.340  1.00184.11           N  
ANISOU 5122  NH2 ARG B 117    24230  31178  14546  -1072   -830  -1607       N  
ATOM   5123  N   CYS B 118      19.538 -10.178   8.566  1.00158.33           N  
ANISOU 5123  N   CYS B 118    20776  26810  12571   -414     79    227       N  
ATOM   5124  CA  CYS B 118      19.714 -11.327   7.670  1.00153.87           C  
ANISOU 5124  CA  CYS B 118    20013  26127  12321   -420    125    426       C  
ATOM   5125  C   CYS B 118      19.380 -11.035   6.197  1.00158.22           C  
ANISOU 5125  C   CYS B 118    20648  26404  13061   -371    206    307       C  
ATOM   5126  O   CYS B 118      20.141 -11.435   5.272  1.00158.48           O  
ANISOU 5126  O   CYS B 118    20597  26292  13324   -440    198    355       O  
ATOM   5127  CB  CYS B 118      18.874 -12.497   8.163  1.00151.09           C  
ANISOU 5127  CB  CYS B 118    19461  25921  12025   -305    218    654       C  
ATOM   5128  SG  CYS B 118      18.617 -13.808   6.962  1.00148.16           S  
ANISOU 5128  SG  CYS B 118    18843  25353  12098   -279    328    781       S  
ATOM   5129  N   TRP B 119      18.230 -10.390   5.954  1.00164.92           N  
ANISOU 5129  N   TRP B 119    21647  27208  13805   -226    289    167       N  
ATOM   5130  CA  TRP B 119      17.813 -10.094   4.542  1.00162.64           C  
ANISOU 5130  CA  TRP B 119    21429  26727  13638   -120    363     70       C  
ATOM   5131  C   TRP B 119      18.857  -9.329   3.755  1.00151.02           C  
ANISOU 5131  C   TRP B 119    20086  25062  12232   -200    355      5       C  
ATOM   5132  O   TRP B 119      19.091  -9.642   2.575  1.00143.38           O  
ANISOU 5132  O   TRP B 119    19067  23986  11424   -159    391     30       O  
ATOM   5133  CB  TRP B 119      16.564  -9.235   4.522  1.00171.74           C  
ANISOU 5133  CB  TRP B 119    22752  27873  14624     53    444    -70       C  
ATOM   5134  CG  TRP B 119      15.936  -8.960   3.170  1.00171.50           C  
ANISOU 5134  CG  TRP B 119    22771  27732  14657    227    516   -148       C  
ATOM   5135  CD1 TRP B 119      15.601  -7.735   2.669  1.00171.76           C  
ANISOU 5135  CD1 TRP B 119    23028  27649  14582    354    591   -254       C  
ATOM   5136  CD2 TRP B 119      15.525  -9.923   2.187  1.00170.28           C  
ANISOU 5136  CD2 TRP B 119    22420  27604  14674    320    525   -133       C  
ATOM   5137  NE1 TRP B 119      15.007  -7.875   1.440  1.00165.13           N  
ANISOU 5137  NE1 TRP B 119    22148  26805  13787    546    635   -275       N  
ATOM   5138  CE2 TRP B 119      14.938  -9.204   1.123  1.00164.21           C  
ANISOU 5138  CE2 TRP B 119    21770  26788  13832    523    581   -237       C  
ATOM   5139  CE3 TRP B 119      15.587 -11.323   2.106  1.00171.99           C  
ANISOU 5139  CE3 TRP B 119    22351  27879  15117    263    504    -56       C  
ATOM   5140  CZ2 TRP B 119      14.429  -9.832  -0.009  1.00162.61           C  
ANISOU 5140  CZ2 TRP B 119    21410  26650  13723    671    580   -301       C  
ATOM   5141  CZ3 TRP B 119      15.072 -11.951   0.964  1.00167.90           C  
ANISOU 5141  CZ3 TRP B 119    21670  27372  14752    384    520   -151       C  
ATOM   5142  CH2 TRP B 119      14.513 -11.200  -0.077  1.00162.84           C  
ANISOU 5142  CH2 TRP B 119    21153  26737  13981    587    540   -288       C  
ATOM   5143  N   ALA B 120      19.483  -8.357   4.437  1.00147.22           N  
ANISOU 5143  N   ALA B 120    19748  24546  11640   -310    317    -90       N  
ATOM   5144  CA  ALA B 120      20.478  -7.502   3.837  1.00140.51           C  
ANISOU 5144  CA  ALA B 120    19012  23474  10900   -400    344   -161       C  
ATOM   5145  C   ALA B 120      21.658  -8.304   3.321  1.00139.96           C  
ANISOU 5145  C   ALA B 120    18772  23359  11047   -531    291    -26       C  
ATOM   5146  O   ALA B 120      22.139  -8.000   2.239  1.00152.81           O  
ANISOU 5146  O   ALA B 120    20450  24792  12819   -512    373    -13       O  
ATOM   5147  CB  ALA B 120      20.949  -6.442   4.795  1.00140.39           C  
ANISOU 5147  CB  ALA B 120    19117  23438  10786   -525    306   -339       C  
ATOM   5148  N   VAL B 121      22.107  -9.335   4.036  1.00134.23           N  
ANISOU 5148  N   VAL B 121    17840  22810  10350   -636    180    101       N  
ATOM   5149  CA  VAL B 121      23.144 -10.225   3.475  1.00133.04           C  
ANISOU 5149  CA  VAL B 121    17502  22606  10440   -738    151    250       C  
ATOM   5150  C   VAL B 121      22.641 -11.393   2.624  1.00134.65           C  
ANISOU 5150  C   VAL B 121    17546  22810  10806   -633    215    361       C  
ATOM   5151  O   VAL B 121      23.391 -11.867   1.770  1.00141.01           O  
ANISOU 5151  O   VAL B 121    18253  23504  11819   -678    240    423       O  
ATOM   5152  CB  VAL B 121      24.145 -10.791   4.515  1.00128.17           C  
ANISOU 5152  CB  VAL B 121    16704  22154   9838   -903     10    363       C  
ATOM   5153  CG1 VAL B 121      25.043  -9.680   5.004  1.00126.01           C  
ANISOU 5153  CG1 VAL B 121    16529  21837   9509  -1050    -68    195       C  
ATOM   5154  CG2 VAL B 121      23.440 -11.491   5.645  1.00127.31           C  
ANISOU 5154  CG2 VAL B 121    16486  22320   9564   -838    -33    476       C  
ATOM   5155  N   ILE B 122      21.426 -11.884   2.821  1.00137.86           N  
ANISOU 5155  N   ILE B 122    17899  23328  11152   -501    251    363       N  
ATOM   5156  CA  ILE B 122      21.014 -13.050   2.000  1.00145.82           C  
ANISOU 5156  CA  ILE B 122    18700  24320  12382   -426    311    408       C  
ATOM   5157  C   ILE B 122      20.662 -12.743   0.506  1.00152.46           C  
ANISOU 5157  C   ILE B 122    19618  25056  13251   -281    382    264       C  
ATOM   5158  O   ILE B 122      21.023 -13.546  -0.396  1.00159.80           O  
ANISOU 5158  O   ILE B 122    20388  25939  14388   -279    410    269       O  
ATOM   5159  CB  ILE B 122      19.913 -13.888   2.693  1.00145.81           C  
ANISOU 5159  CB  ILE B 122    18536  24455  12407   -349    346    467       C  
ATOM   5160  CG1 ILE B 122      19.993 -15.361   2.233  1.00145.06           C  
ANISOU 5160  CG1 ILE B 122    18129  24320  12666   -367    404    558       C  
ATOM   5161  CG2 ILE B 122      18.530 -13.272   2.488  1.00143.62           C  
ANISOU 5161  CG2 ILE B 122    18390  24211  11966   -171    397    301       C  
ATOM   5162  CD1 ILE B 122      19.268 -16.313   3.150  1.00145.08           C  
ANISOU 5162  CD1 ILE B 122    17916  24416  12790   -338    474    706       C  
ATOM   5163  N   GLN B 123      20.041 -11.584   0.245  1.00153.41           N  
ANISOU 5163  N   GLN B 123    19974  25152  13159   -150    420    145       N  
ATOM   5164  CA  GLN B 123      19.697 -11.142  -1.133  1.00155.00           C  
ANISOU 5164  CA  GLN B 123    20268  25307  13317     42    495     48       C  
ATOM   5165  C   GLN B 123      20.819 -11.321  -2.189  1.00157.47           C  
ANISOU 5165  C   GLN B 123    20548  25512  13770      8    533     96       C  
ATOM   5166  O   GLN B 123      20.602 -11.962  -3.229  1.00162.92           O  
ANISOU 5166  O   GLN B 123    21115  26261  14525    130    558     32       O  
ATOM   5167  CB  GLN B 123      19.239  -9.677  -1.143  1.00157.52           C  
ANISOU 5167  CB  GLN B 123    20868  25565  13417    168    560    -11       C  
ATOM   5168  CG  GLN B 123      17.806  -9.472  -0.762  1.00162.49           C  
ANISOU 5168  CG  GLN B 123    21531  26315  13891    325    567   -101       C  
ATOM   5169  CD  GLN B 123      17.460  -7.997  -0.771  1.00167.40           C  
ANISOU 5169  CD  GLN B 123    22426  26839  14337    448    658   -143       C  
ATOM   5170  OE1 GLN B 123      16.748  -7.528  -1.654  1.00179.74           O  
ANISOU 5170  OE1 GLN B 123    24065  28426  15799    691    732   -177       O  
ATOM   5171  NE2 GLN B 123      17.964  -7.261   0.212  1.00168.75           N  
ANISOU 5171  NE2 GLN B 123    22728  26910  14478    292    657   -151       N  
ATOM   5172  N   PRO B 124      22.020 -10.760  -1.935  1.00155.90           N  
ANISOU 5172  N   PRO B 124    20441  25167  13626   -152    540    184       N  
ATOM   5173  CA  PRO B 124      23.137 -11.006  -2.834  1.00155.65           C  
ANISOU 5173  CA  PRO B 124    20354  25025  13759   -199    592    254       C  
ATOM   5174  C   PRO B 124      23.514 -12.483  -2.986  1.00152.20           C  
ANISOU 5174  C   PRO B 124    19635  24646  13548   -287    546    295       C  
ATOM   5175  O   PRO B 124      23.875 -12.909  -4.094  1.00159.56           O  
ANISOU 5175  O   PRO B 124    20492  25556  14576   -216    609    278       O  
ATOM   5176  CB  PRO B 124      24.289 -10.275  -2.141  1.00159.09           C  
ANISOU 5176  CB  PRO B 124    20874  25306  14266   -408    579    321       C  
ATOM   5177  CG  PRO B 124      23.653  -9.272  -1.266  1.00159.88           C  
ANISOU 5177  CG  PRO B 124    21150  25411  14185   -396    564    236       C  
ATOM   5178  CD  PRO B 124      22.476  -9.999  -0.759  1.00159.79           C  
ANISOU 5178  CD  PRO B 124    21045  25604  14064   -315    493    198       C  
ATOM   5179  N   LEU B 125      23.453 -13.252  -1.891  1.00147.60           N  
ANISOU 5179  N   LEU B 125    18888  24135  13056   -423    459    359       N  
ATOM   5180  CA  LEU B 125      23.840 -14.664  -1.963  1.00147.20           C  
ANISOU 5180  CA  LEU B 125    18549  24096  13284   -506    453    431       C  
ATOM   5181  C   LEU B 125      22.851 -15.419  -2.830  1.00145.61           C  
ANISOU 5181  C   LEU B 125    18206  23964  13156   -342    503    271       C  
ATOM   5182  O   LEU B 125      23.243 -16.211  -3.676  1.00142.53           O  
ANISOU 5182  O   LEU B 125    17648  23536  12968   -337    548    225       O  
ATOM   5183  CB  LEU B 125      23.906 -15.304  -0.581  1.00147.96           C  
ANISOU 5183  CB  LEU B 125    18493  24270  13455   -638    385    586       C  
ATOM   5184  CG  LEU B 125      24.152 -16.820  -0.481  1.00153.47           C  
ANISOU 5184  CG  LEU B 125    18865  24959  14488   -701    420    710       C  
ATOM   5185  CD1 LEU B 125      25.385 -17.252  -1.254  1.00154.25           C  
ANISOU 5185  CD1 LEU B 125    18858  24928  14821   -790    453    763       C  
ATOM   5186  CD2 LEU B 125      24.286 -17.203   0.987  1.00163.21           C  
ANISOU 5186  CD2 LEU B 125    19992  26303  15718   -788    369    931       C  
ATOM   5187  N   LEU B 126      21.567 -15.169  -2.618  1.00149.17           N  
ANISOU 5187  N   LEU B 126    18706  24520  13450   -209    493    158       N  
ATOM   5188  CA  LEU B 126      20.534 -15.909  -3.349  1.00154.11           C  
ANISOU 5188  CA  LEU B 126    19149  25235  14168    -59    520    -42       C  
ATOM   5189  C   LEU B 126      20.578 -15.658  -4.860  1.00154.49           C  
ANISOU 5189  C   LEU B 126    19246  25332  14119    117    550   -213       C  
ATOM   5190  O   LEU B 126      20.487 -16.622  -5.616  1.00156.59           O  
ANISOU 5190  O   LEU B 126    19278  25638  14579    156    569   -372       O  
ATOM   5191  CB  LEU B 126      19.141 -15.593  -2.805  1.00152.96           C  
ANISOU 5191  CB  LEU B 126    19043  25200  13872     56    504   -129       C  
ATOM   5192  CG  LEU B 126      18.883 -15.919  -1.340  1.00145.06           C  
ANISOU 5192  CG  LEU B 126    17974  24205  12936    -61    500     33       C  
ATOM   5193  CD1 LEU B 126      17.667 -15.141  -0.878  1.00145.98           C  
ANISOU 5193  CD1 LEU B 126    18239  24419  12806     71    495    -43       C  
ATOM   5194  CD2 LEU B 126      18.717 -17.416  -1.107  1.00144.26           C  
ANISOU 5194  CD2 LEU B 126    17513  24070  13225   -133    561     68       C  
ATOM   5195  N   CYS B 127      20.747 -14.401  -5.298  1.00158.25           N  
ANISOU 5195  N   CYS B 127    20007  25806  14314    235    575   -180       N  
ATOM   5196  CA  CYS B 127      20.917 -14.128  -6.744  1.00164.86           C  
ANISOU 5196  CA  CYS B 127    20900  26715  15021    441    633   -273       C  
ATOM   5197  C   CYS B 127      22.098 -14.851  -7.302  1.00159.72           C  
ANISOU 5197  C   CYS B 127    20116  25978  14590    332    677   -232       C  
ATOM   5198  O   CYS B 127      21.972 -15.565  -8.295  1.00162.18           O  
ANISOU 5198  O   CYS B 127    20259  26406  14954    449    693   -415       O  
ATOM   5199  CB  CYS B 127      21.098 -12.657  -7.098  1.00171.75           C  
ANISOU 5199  CB  CYS B 127    22092  27545  15618    586    713   -159       C  
ATOM   5200  SG  CYS B 127      19.575 -11.732  -6.892  1.00185.31           S  
ANISOU 5200  SG  CYS B 127    23966  29399  17041    821    697   -242       S  
ATOM   5201  N   ALA B 128      23.234 -14.711  -6.634  1.00154.39           N  
ANISOU 5201  N   ALA B 128    19490  25116  14055    107    691    -20       N  
ATOM   5202  CA  ALA B 128      24.450 -15.372  -7.087  1.00154.03           C  
ANISOU 5202  CA  ALA B 128    19311  24965  14246    -10    743     49       C  
ATOM   5203  C   ALA B 128      24.326 -16.904  -7.278  1.00153.55           C  
ANISOU 5203  C   ALA B 128    18913  24939  14490    -65    732    -84       C  
ATOM   5204  O   ALA B 128      25.133 -17.486  -8.002  1.00155.70           O  
ANISOU 5204  O   ALA B 128    19064  25160  14932    -89    798   -101       O  
ATOM   5205  CB  ALA B 128      25.598 -15.044  -6.155  1.00152.96           C  
ANISOU 5205  CB  ALA B 128    19231  24649  14237   -256    728    281       C  
ATOM   5206  N   VAL B 129      23.337 -17.528  -6.620  1.00152.74           N  
ANISOU 5206  N   VAL B 129    18650  24897  14487    -85    678   -175       N  
ATOM   5207  CA  VAL B 129      23.059 -18.974  -6.717  1.00150.59           C  
ANISOU 5207  CA  VAL B 129    18024  24612  14579   -137    704   -319       C  
ATOM   5208  C   VAL B 129      21.907 -19.330  -7.678  1.00153.12           C  
ANISOU 5208  C   VAL B 129    18208  25114  14857     72    694   -693       C  
ATOM   5209  O   VAL B 129      22.032 -20.237  -8.502  1.00151.92           O  
ANISOU 5209  O   VAL B 129    17817  24977  14926     97    737   -915       O  
ATOM   5210  CB  VAL B 129      22.770 -19.537  -5.306  1.00150.02           C  
ANISOU 5210  CB  VAL B 129    17812  24464  14724   -296    691   -146       C  
ATOM   5211  CG1 VAL B 129      22.334 -20.989  -5.387  1.00150.77           C  
ANISOU 5211  CG1 VAL B 129    17524  24501  15260   -333    767   -287       C  
ATOM   5212  CG2 VAL B 129      24.013 -19.407  -4.428  1.00150.90           C  
ANISOU 5212  CG2 VAL B 129    17980  24454  14900   -490    680    185       C  
ATOM   5213  N   TYR B 130      20.777 -18.637  -7.544  1.00161.10           N  
ANISOU 5213  N   TYR B 130    19343  26271  15596    223    633   -786       N  
ATOM   5214  CA  TYR B 130      19.578 -18.957  -8.337  1.00166.03           C  
ANISOU 5214  CA  TYR B 130    19802  27105  16175    428    594  -1158       C  
ATOM   5215  C   TYR B 130      19.581 -18.287  -9.698  1.00169.94           C  
ANISOU 5215  C   TYR B 130    20442  27827  16301    700    578  -1318       C  
ATOM   5216  O   TYR B 130      19.095 -18.872 -10.674  1.00178.04           O  
ANISOU 5216  O   TYR B 130    21254  29050  17343    855    550  -1672       O  
ATOM   5217  CB  TYR B 130      18.302 -18.575  -7.580  1.00169.49           C  
ANISOU 5217  CB  TYR B 130    20273  27617  16509    488    542  -1184       C  
ATOM   5218  CG  TYR B 130      17.998 -19.490  -6.429  1.00169.49           C  
ANISOU 5218  CG  TYR B 130    20037  27457  16901    291    587  -1098       C  
ATOM   5219  CD1 TYR B 130      17.227 -20.623  -6.608  1.00170.22           C  
ANISOU 5219  CD1 TYR B 130    19754  27549  17370    286    621  -1375       C  
ATOM   5220  CD2 TYR B 130      18.497 -19.232  -5.168  1.00169.23           C  
ANISOU 5220  CD2 TYR B 130    20138  27284  16878    123    609   -743       C  
ATOM   5221  CE1 TYR B 130      16.956 -21.470  -5.560  1.00170.38           C  
ANISOU 5221  CE1 TYR B 130    19546  27397  17791    128    715  -1245       C  
ATOM   5222  CE2 TYR B 130      18.237 -20.072  -4.109  1.00171.21           C  
ANISOU 5222  CE2 TYR B 130    20173  27423  17455    -13    677   -607       C  
ATOM   5223  CZ  TYR B 130      17.465 -21.195  -4.314  1.00172.33           C  
ANISOU 5223  CZ  TYR B 130    19950  27531  17997     -5    749   -832       C  
ATOM   5224  OH  TYR B 130      17.193 -22.051  -3.272  1.00186.21           O  
ANISOU 5224  OH  TYR B 130    21475  29149  20124   -119    868   -653       O  
ATOM   5225  N   MET B 131      20.109 -17.059  -9.765  1.00170.92           N  
ANISOU 5225  N   MET B 131    20910  27933  16099    774    608  -1067       N  
ATOM   5226  CA  MET B 131      20.191 -16.334 -11.035  1.00173.51           C  
ANISOU 5226  CA  MET B 131    21397  28468  16060   1069    641  -1123       C  
ATOM   5227  C   MET B 131      21.625 -15.921 -11.382  1.00175.07           C  
ANISOU 5227  C   MET B 131    21766  28507  16243   1011    761   -864       C  
ATOM   5228  O   MET B 131      21.853 -14.752 -11.695  1.00172.01           O  
ANISOU 5228  O   MET B 131    21658  28126  15572   1166    839   -670       O  
ATOM   5229  CB  MET B 131      19.221 -15.132 -11.021  1.00172.56           C  
ANISOU 5229  CB  MET B 131    21509  28499  15556   1312    615  -1078       C  
ATOM   5230  CG  MET B 131      17.769 -15.598 -11.023  1.00176.11           C  
ANISOU 5230  CG  MET B 131    21741  29171  15999   1435    498  -1397       C  
ATOM   5231  SD  MET B 131      16.476 -14.355 -10.830  1.00185.11           S  
ANISOU 5231  SD  MET B 131    23092  30478  16761   1700    459  -1358       S  
ATOM   5232  CE  MET B 131      16.630 -13.398 -12.340  1.00194.61           C  
ANISOU 5232  CE  MET B 131    24493  31967  17481   2130    525  -1310       C  
ATOM   5233  N   PRO B 132      22.591 -16.888 -11.387  1.00176.57           N  
ANISOU 5233  N   PRO B 132    21770  28547  16772    803    800   -860       N  
ATOM   5234  CA  PRO B 132      23.989 -16.503 -11.605  1.00177.14           C  
ANISOU 5234  CA  PRO B 132    21984  28441  16879    719    919   -599       C  
ATOM   5235  C   PRO B 132      24.266 -16.182 -13.047  1.00181.78           C  
ANISOU 5235  C   PRO B 132    22649  29221  17197   1010   1022   -661       C  
ATOM   5236  O   PRO B 132      23.515 -16.599 -13.912  1.00180.22           O  
ANISOU 5236  O   PRO B 132    22317  29317  16840   1243    976   -965       O  
ATOM   5237  CB  PRO B 132      24.775 -17.759 -11.217  1.00178.71           C  
ANISOU 5237  CB  PRO B 132    21912  28457  17530    445    927   -603       C  
ATOM   5238  CG  PRO B 132      23.850 -18.897 -11.502  1.00178.55           C  
ANISOU 5238  CG  PRO B 132    21582  28583  17674    494    867   -966       C  
ATOM   5239  CD  PRO B 132      22.447 -18.360 -11.341  1.00177.66           C  
ANISOU 5239  CD  PRO B 132    21540  28665  17295    667    769  -1106       C  
ATOM   5240  N   LYS B 133      25.362 -15.468 -13.280  1.00187.60           N  
ANISOU 5240  N   LYS B 133    23578  29800  17899    998   1165   -378       N  
ATOM   5241  CA  LYS B 133      25.758 -15.082 -14.618  1.00186.65           C  
ANISOU 5241  CA  LYS B 133    23554  29845  17519   1292   1315   -352       C  
ATOM   5242  C   LYS B 133      26.396 -16.264 -15.302  1.00185.23           C  
ANISOU 5242  C   LYS B 133    23127  29713  17538   1250   1349   -538       C  
ATOM   5243  O   LYS B 133      27.353 -16.866 -14.763  1.00180.02           O  
ANISOU 5243  O   LYS B 133    22350  28781  17266    949   1375   -435       O  
ATOM   5244  CB  LYS B 133      26.751 -13.934 -14.580  1.00183.23           C  
ANISOU 5244  CB  LYS B 133    23383  29167  17067   1273   1501     31       C  
ATOM   5245  CG  LYS B 133      27.185 -13.418 -15.936  1.00184.63           C  
ANISOU 5245  CG  LYS B 133    23682  29495  16973   1610   1714    144       C  
ATOM   5246  CD  LYS B 133      28.210 -12.328 -15.757  1.00183.88           C  
ANISOU 5246  CD  LYS B 133    23804  29071  16988   1536   1929    532       C  
ATOM   5247  CE  LYS B 133      28.580 -11.780 -17.104  1.00189.00           C  
ANISOU 5247  CE  LYS B 133    24576  29867  17365   1912   2188    701       C  
ATOM   5248  NZ  LYS B 133      29.375 -10.547 -16.953  1.00192.46           N  
ANISOU 5248  NZ  LYS B 133    25232  29964  17930   1884   2440   1088       N  
ATOM   5249  N   CYS B 134      25.863 -16.572 -16.490  1.00181.83           N  
ANISOU 5249  N   CYS B 134    22608  29648  16831   1570   1349   -821       N  
ATOM   5250  CA  CYS B 134      26.472 -17.567 -17.351  1.00179.59           C  
ANISOU 5250  CA  CYS B 134    22109  29454  16670   1595   1412  -1036       C  
ATOM   5251  C   CYS B 134      26.887 -16.852 -18.648  1.00185.28           C  
ANISOU 5251  C   CYS B 134    23010  30417  16968   1974   1592   -917       C  
ATOM   5252  O   CYS B 134      26.062 -16.226 -19.290  1.00189.42           O  
ANISOU 5252  O   CYS B 134    23643  31287  17038   2337   1574   -975       O  
ATOM   5253  CB  CYS B 134      25.477 -18.697 -17.588  1.00174.68           C  
ANISOU 5253  CB  CYS B 134    21164  29077  16129   1633   1251  -1550       C  
ATOM   5254  SG  CYS B 134      26.202 -20.129 -18.385  1.00178.13           S  
ANISOU 5254  SG  CYS B 134    21268  29537  16876   1570   1324  -1892       S  
ATOM   5255  N   GLU B 135      28.168 -16.930 -19.018  1.00189.11           N  
ANISOU 5255  N   GLU B 135    23522  30727  17603   1907   1782   -719       N  
ATOM   5256  CA  GLU B 135      28.637 -16.324 -20.273  1.00187.60           C  
ANISOU 5256  CA  GLU B 135    23485  30759  17033   2281   2001   -572       C  
ATOM   5257  C   GLU B 135      29.542 -17.301 -21.001  1.00188.33           C  
ANISOU 5257  C   GLU B 135    23384  30877  17295   2256   2110   -733       C  
ATOM   5258  O   GLU B 135      30.557 -17.755 -20.442  1.00189.62           O  
ANISOU 5258  O   GLU B 135    23464  30659  17922   1912   2172   -595       O  
ATOM   5259  CB  GLU B 135      29.360 -14.999 -20.012  1.00188.88           C  
ANISOU 5259  CB  GLU B 135    23953  30628  17183   2278   2214    -42       C  
ATOM   5260  CG  GLU B 135      29.012 -13.910 -21.018  1.00195.49           C  
ANISOU 5260  CG  GLU B 135    25021  31764  17489   2774   2393    157       C  
ATOM   5261  CD  GLU B 135      29.727 -12.588 -20.766  1.00197.85           C  
ANISOU 5261  CD  GLU B 135    25594  31708  17869   2764   2655    679       C  
ATOM   5262  OE1 GLU B 135      30.571 -12.486 -19.850  1.00194.50           O  
ANISOU 5262  OE1 GLU B 135    25177  30824  17900   2365   2685    856       O  
ATOM   5263  OE2 GLU B 135      29.436 -11.626 -21.494  1.00207.27           O  
ANISOU 5263  OE2 GLU B 135    26981  33089  18682   3173   2843    913       O  
ATOM   5264  N   ASN B 136      29.149 -17.634 -22.230  1.00190.22           N  
ANISOU 5264  N   ASN B 136    23536  31588  17151   2631   2124  -1043       N  
ATOM   5265  CA  ASN B 136      29.856 -18.574 -23.082  1.00191.38           C  
ANISOU 5265  CA  ASN B 136    23487  31847  17382   2676   2229  -1283       C  
ATOM   5266  C   ASN B 136      30.167 -19.910 -22.382  1.00188.13           C  
ANISOU 5266  C   ASN B 136    22761  31125  17594   2241   2130  -1550       C  
ATOM   5267  O   ASN B 136      31.318 -20.273 -22.114  1.00183.55           O  
ANISOU 5267  O   ASN B 136    22131  30191  17418   1984   2267  -1356       O  
ATOM   5268  CB  ASN B 136      31.118 -17.921 -23.626  1.00196.60           C  
ANISOU 5268  CB  ASN B 136    24347  32368  17982   2785   2547   -837       C  
ATOM   5269  CG  ASN B 136      31.779 -18.758 -24.679  1.00207.89           C  
ANISOU 5269  CG  ASN B 136    25607  33996  19384   2926   2687  -1078       C  
ATOM   5270  OD1 ASN B 136      31.108 -19.322 -25.530  1.00213.61           O  
ANISOU 5270  OD1 ASN B 136    26174  35199  19788   3206   2593  -1543       O  
ATOM   5271  ND2 ASN B 136      33.101 -18.820 -24.658  1.00214.41           N  
ANISOU 5271  ND2 ASN B 136    26452  34477  20536   2749   2914   -786       N  
ATOM   5272  N   ASP B 137      29.091 -20.622 -22.070  1.00190.35           N  
ANISOU 5272  N   ASP B 137    22815  31536  17972   2175   1901  -1982       N  
ATOM   5273  CA  ASP B 137      29.106 -21.942 -21.404  1.00192.98           C  
ANISOU 5273  CA  ASP B 137    22808  31599  18914   1807   1815  -2270       C  
ATOM   5274  C   ASP B 137      29.893 -22.127 -20.085  1.00202.45           C  
ANISOU 5274  C   ASP B 137    24000  32243  20678   1357   1846  -1890       C  
ATOM   5275  O   ASP B 137      30.342 -23.236 -19.774  1.00210.17           O  
ANISOU 5275  O   ASP B 137    24704  32977  22172   1102   1877  -2020       O  
ATOM   5276  CB  ASP B 137      29.581 -23.028 -22.372  1.00188.62           C  
ANISOU 5276  CB  ASP B 137    21985  31181  18499   1874   1914  -2678       C  
ATOM   5277  CG  ASP B 137      28.668 -23.246 -23.498  1.00186.24           C  
ANISOU 5277  CG  ASP B 137    21555  31448  17759   2252   1819  -3224       C  
ATOM   5278  OD1 ASP B 137      27.436 -23.169 -23.360  1.00189.12           O  
ANISOU 5278  OD1 ASP B 137    21851  32051  17955   2350   1615  -3496       O  
ATOM   5279  OD2 ASP B 137      29.213 -23.555 -24.543  1.00181.63           O  
ANISOU 5279  OD2 ASP B 137    20910  31089  17010   2456   1950  -3412       O  
ATOM   5280  N   ARG B 138      30.067 -21.047 -19.337  1.00205.50           N  
ANISOU 5280  N   ARG B 138    24668  32447  20966   1280   1845  -1433       N  
ATOM   5281  CA  ARG B 138      30.706 -21.081 -18.032  1.00195.05           C  
ANISOU 5281  CA  ARG B 138    23345  30683  20079    893   1831  -1090       C  
ATOM   5282  C   ARG B 138      29.869 -20.194 -17.127  1.00192.98           C  
ANISOU 5282  C   ARG B 138    23276  30409  19637    865   1687   -927       C  
ATOM   5283  O   ARG B 138      29.609 -19.022 -17.479  1.00192.86           O  
ANISOU 5283  O   ARG B 138    23538  30541  19196   1099   1721   -770       O  
ATOM   5284  CB  ARG B 138      32.139 -20.567 -18.120  1.00192.97           C  
ANISOU 5284  CB  ARG B 138    23229  30181  19910    815   2024   -685       C  
ATOM   5285  CG  ARG B 138      32.936 -20.887 -16.875  1.00189.58           C  
ANISOU 5285  CG  ARG B 138    22704  29349  19979    418   1996   -410       C  
ATOM   5286  CD  ARG B 138      34.101 -19.959 -16.718  1.00192.81           C  
ANISOU 5286  CD  ARG B 138    23309  29534  20415    339   2131     11       C  
ATOM   5287  NE  ARG B 138      35.011 -20.394 -15.664  1.00196.03           N  
ANISOU 5287  NE  ARG B 138    23568  29613  21298    -14   2099    235       N  
ATOM   5288  CZ  ARG B 138      36.170 -19.805 -15.371  1.00207.38           C  
ANISOU 5288  CZ  ARG B 138    25083  30816  22893   -156   2194    566       C  
ATOM   5289  NH1 ARG B 138      36.569 -18.713 -16.041  1.00217.18           N  
ANISOU 5289  NH1 ARG B 138    26559  32060  23896     12   2362    736       N  
ATOM   5290  NH2 ARG B 138      36.928 -20.293 -14.395  1.00209.95           N  
ANISOU 5290  NH2 ARG B 138    25233  30908  23629   -456   2130    738       N  
ATOM   5291  N   VAL B 139      29.448 -20.740 -15.994  1.00193.99           N  
ANISOU 5291  N   VAL B 139    23255  30363  20090    604   1554   -950       N  
ATOM   5292  CA  VAL B 139      28.641 -20.012 -15.009  1.00191.49           C  
ANISOU 5292  CA  VAL B 139    23093  30025  19640    552   1418   -816       C  
ATOM   5293  C   VAL B 139      29.577 -19.529 -13.895  1.00178.83           C  
ANISOU 5293  C   VAL B 139    21607  28094  18244    273   1434   -395       C  
ATOM   5294  O   VAL B 139      30.508 -20.255 -13.516  1.00171.31           O  
ANISOU 5294  O   VAL B 139    20483  26922  17684     45   1479   -282       O  
ATOM   5295  CB  VAL B 139      27.467 -20.888 -14.482  1.00197.88           C  
ANISOU 5295  CB  VAL B 139    23652  30895  20637    484   1275  -1120       C  
ATOM   5296  CG1 VAL B 139      27.936 -22.181 -13.804  1.00195.94           C  
ANISOU 5296  CG1 VAL B 139    23090  30381  20975    191   1302  -1124       C  
ATOM   5297  CG2 VAL B 139      26.578 -20.109 -13.519  1.00200.99           C  
ANISOU 5297  CG2 VAL B 139    24213  31295  20856    464   1151   -990       C  
ATOM   5298  N   GLU B 140      29.337 -18.309 -13.402  1.00173.47           N  
ANISOU 5298  N   GLU B 140    21202  27396  17311    303   1399   -188       N  
ATOM   5299  CA  GLU B 140      30.192 -17.714 -12.367  1.00173.43           C  
ANISOU 5299  CA  GLU B 140    21307  27122  17466     55   1397    146       C  
ATOM   5300  C   GLU B 140      29.766 -18.192 -10.957  1.00177.02           C  
ANISOU 5300  C   GLU B 140    21635  27495  18127   -180   1235    175       C  
ATOM   5301  O   GLU B 140      28.598 -18.020 -10.540  1.00180.29           O  
ANISOU 5301  O   GLU B 140    22091  28034  18374   -111   1130     59       O  
ATOM   5302  CB  GLU B 140      30.146 -16.187 -12.439  1.00168.17           C  
ANISOU 5302  CB  GLU B 140    20965  26440  16490    183   1458    324       C  
ATOM   5303  CG  GLU B 140      30.787 -15.592 -13.680  1.00172.01           C  
ANISOU 5303  CG  GLU B 140    21588  26950  16815    406   1674    423       C  
ATOM   5304  CD  GLU B 140      30.974 -14.075 -13.609  1.00173.44           C  
ANISOU 5304  CD  GLU B 140    22060  27003  16834    483   1795    672       C  
ATOM   5305  OE1 GLU B 140      30.606 -13.452 -12.587  1.00167.56           O  
ANISOU 5305  OE1 GLU B 140    21416  26155  16093    351   1694    728       O  
ATOM   5306  OE2 GLU B 140      31.465 -13.484 -14.602  1.00179.90           O  
ANISOU 5306  OE2 GLU B 140    23003  27822  17528    695   2017    812       O  
ATOM   5307  N   LEU B 141      30.715 -18.792 -10.233  1.00173.02           N  
ANISOU 5307  N   LEU B 141    20965  26798  17974   -433   1226    349       N  
ATOM   5308  CA  LEU B 141      30.473 -19.327  -8.887  1.00169.93           C  
ANISOU 5308  CA  LEU B 141    20430  26354  17780   -629   1102    441       C  
ATOM   5309  C   LEU B 141      30.552 -18.213  -7.835  1.00169.75           C  
ANISOU 5309  C   LEU B 141    20620  26298  17580   -727   1005    628       C  
ATOM   5310  O   LEU B 141      31.400 -17.316  -7.963  1.00174.46           O  
ANISOU 5310  O   LEU B 141    21372  26792  18121   -766   1052    758       O  
ATOM   5311  CB  LEU B 141      31.498 -20.415  -8.529  1.00166.80           C  
ANISOU 5311  CB  LEU B 141    19755  25800  17819   -824   1141    589       C  
ATOM   5312  CG  LEU B 141      31.424 -21.735  -9.289  1.00164.88           C  
ANISOU 5312  CG  LEU B 141    19231  25539  17875   -782   1245    391       C  
ATOM   5313  CD1 LEU B 141      32.679 -22.534  -8.987  1.00166.72           C  
ANISOU 5313  CD1 LEU B 141    19238  25580  18525   -963   1314    608       C  
ATOM   5314  CD2 LEU B 141      30.184 -22.525  -8.920  1.00162.04           C  
ANISOU 5314  CD2 LEU B 141    18692  25249  17626   -752   1202    205       C  
ATOM   5315  N   PRO B 142      29.707 -18.284  -6.776  1.00163.94           N  
ANISOU 5315  N   PRO B 142    19867  25637  16784   -772    885    632       N  
ATOM   5316  CA  PRO B 142      29.760 -17.234  -5.756  1.00162.40           C  
ANISOU 5316  CA  PRO B 142    19862  25437  16404   -858    788    756       C  
ATOM   5317  C   PRO B 142      30.897 -17.472  -4.757  1.00166.78           C  
ANISOU 5317  C   PRO B 142    20284  25913  17169  -1087    718    980       C  
ATOM   5318  O   PRO B 142      31.171 -18.614  -4.430  1.00168.52           O  
ANISOU 5318  O   PRO B 142    20248  26126  17656  -1164    716   1076       O  
ATOM   5319  CB  PRO B 142      28.405 -17.354  -5.054  1.00162.86           C  
ANISOU 5319  CB  PRO B 142    19924  25636  16317   -793    705    667       C  
ATOM   5320  CG  PRO B 142      27.676 -18.494  -5.722  1.00162.32           C  
ANISOU 5320  CG  PRO B 142    19641  25622  16408   -688    761    492       C  
ATOM   5321  CD  PRO B 142      28.706 -19.309  -6.424  1.00161.50           C  
ANISOU 5321  CD  PRO B 142    19350  25407  16603   -749    854    520       C  
ATOM   5322  N   SER B 143      31.541 -16.386  -4.316  1.00169.19           N  
ANISOU 5322  N   SER B 143    20744  26161  17378  -1183    672   1051       N  
ATOM   5323  CA  SER B 143      32.698 -16.465  -3.385  1.00168.40           C  
ANISOU 5323  CA  SER B 143    20506  26028  17450  -1390    579   1224       C  
ATOM   5324  C   SER B 143      32.254 -16.875  -1.978  1.00168.87           C  
ANISOU 5324  C   SER B 143    20443  26263  17456  -1452    426   1319       C  
ATOM   5325  O   SER B 143      31.071 -16.680  -1.642  1.00160.19           O  
ANISOU 5325  O   SER B 143    19446  25282  16135  -1361    387   1235       O  
ATOM   5326  CB  SER B 143      33.470 -15.171  -3.361  1.00168.55           C  
ANISOU 5326  CB  SER B 143    20701  25941  17399  -1479    568   1202       C  
ATOM   5327  OG  SER B 143      32.636 -14.096  -2.955  1.00166.64           O  
ANISOU 5327  OG  SER B 143    20661  25771  16881  -1447    494   1087       O  
ATOM   5328  N   ARG B 144      33.182 -17.452  -1.209  1.00171.24           N  
ANISOU 5328  N   ARG B 144    20525  26596  17943  -1589    347   1509       N  
ATOM   5329  CA  ARG B 144      32.913 -17.898   0.184  1.00168.26           C  
ANISOU 5329  CA  ARG B 144    20009  26436  17486  -1621    207   1662       C  
ATOM   5330  C   ARG B 144      32.578 -16.679   1.050  1.00160.70           C  
ANISOU 5330  C   ARG B 144    19242  25642  16173  -1634     60   1553       C  
ATOM   5331  O   ARG B 144      31.623 -16.765   1.846  1.00161.18           O  
ANISOU 5331  O   ARG B 144    19307  25890  16042  -1557      8   1586       O  
ATOM   5332  CB  ARG B 144      34.140 -18.638   0.724  1.00173.94           C  
ANISOU 5332  CB  ARG B 144    20453  27184  18451  -1738    147   1900       C  
ATOM   5333  CG  ARG B 144      33.881 -19.428   1.998  1.00184.25           C  
ANISOU 5333  CG  ARG B 144    21539  28732  19734  -1712     54   2155       C  
ATOM   5334  CD  ARG B 144      34.720 -20.690   2.041  1.00192.44           C  
ANISOU 5334  CD  ARG B 144    22251  29715  21150  -1739    122   2434       C  
ATOM   5335  NE  ARG B 144      34.434 -21.559   0.908  1.00199.97           N  
ANISOU 5335  NE  ARG B 144    23093  30476  22410  -1658    339   2450       N  
ATOM   5336  CZ  ARG B 144      34.908 -22.790   0.764  1.00205.29           C  
ANISOU 5336  CZ  ARG B 144    23476  31034  23488  -1660    467   2661       C  
ATOM   5337  NH1 ARG B 144      35.697 -23.308   1.689  1.00210.94           N  
ANISOU 5337  NH1 ARG B 144    23977  31818  24350  -1722    401   2928       N  
ATOM   5338  NH2 ARG B 144      34.591 -23.501  -0.304  1.00200.95           N  
ANISOU 5338  NH2 ARG B 144    22831  30298  23223  -1594    668   2582       N  
ATOM   5339  N   THR B 145      33.311 -15.577   0.863  1.00156.38           N  
ANISOU 5339  N   THR B 145    18848  25002  15567  -1723     24   1409       N  
ATOM   5340  CA  THR B 145      33.086 -14.340   1.659  1.00158.12           C  
ANISOU 5340  CA  THR B 145    19247  25325  15504  -1756    -92   1237       C  
ATOM   5341  C   THR B 145      31.613 -13.926   1.574  1.00153.86           C  
ANISOU 5341  C   THR B 145    18947  24798  14713  -1606    -27   1090       C  
ATOM   5342  O   THR B 145      31.122 -13.306   2.534  1.00170.26           O  
ANISOU 5342  O   THR B 145    21121  27032  16537  -1599   -127    991       O  
ATOM   5343  CB  THR B 145      34.024 -13.209   1.222  1.00161.67           C  
ANISOU 5343  CB  THR B 145    19796  25582  16049  -1885    -79   1082       C  
ATOM   5344  OG1 THR B 145      33.711 -12.881  -0.131  1.00165.97           O  
ANISOU 5344  OG1 THR B 145    20475  25857  16726  -1808    134   1054       O  
ATOM   5345  CG2 THR B 145      35.486 -13.582   1.334  1.00165.57           C  
ANISOU 5345  CG2 THR B 145    20036  26106  16767  -2059   -193   1178       C  
ATOM   5346  N   LEU B 146      30.959 -14.219   0.446  1.00145.41           N  
ANISOU 5346  N   LEU B 146    17958  23589  13699  -1476    131   1058       N  
ATOM   5347  CA  LEU B 146      29.533 -13.885   0.260  1.00147.93           C  
ANISOU 5347  CA  LEU B 146    18461  23950  13795  -1308    186    930       C  
ATOM   5348  C   LEU B 146      28.584 -14.845   0.995  1.00150.81           C  
ANISOU 5348  C   LEU B 146    18695  24510  14094  -1233    146   1013       C  
ATOM   5349  O   LEU B 146      27.505 -14.459   1.454  1.00142.46           O  
ANISOU 5349  O   LEU B 146    17762  23556  12810  -1138    133    925       O  
ATOM   5350  CB  LEU B 146      29.186 -13.921  -1.228  1.00150.86           C  
ANISOU 5350  CB  LEU B 146    18911  24175  14234  -1166    350    862       C  
ATOM   5351  CG  LEU B 146      27.836 -13.329  -1.695  1.00147.36           C  
ANISOU 5351  CG  LEU B 146    18674  23761  13555   -964    417    709       C  
ATOM   5352  CD1 LEU B 146      27.885 -11.810  -1.722  1.00145.21           C  
ANISOU 5352  CD1 LEU B 146    18662  23375  13134   -949    460    617       C  
ATOM   5353  CD2 LEU B 146      27.463 -13.896  -3.061  1.00143.84           C  
ANISOU 5353  CD2 LEU B 146    18184  23290  13177   -799    535    656       C  
ATOM   5354  N   CYS B 147      28.999 -16.108   1.070  1.00156.96           N  
ANISOU 5354  N   CYS B 147    19208  25313  15114  -1268    159   1198       N  
ATOM   5355  CA  CYS B 147      28.219 -17.161   1.710  1.00159.56           C  
ANISOU 5355  CA  CYS B 147    19360  25775  15490  -1196    179   1331       C  
ATOM   5356  C   CYS B 147      28.376 -17.093   3.221  1.00161.46           C  
ANISOU 5356  C   CYS B 147    19551  26256  15540  -1233     51   1484       C  
ATOM   5357  O   CYS B 147      27.369 -17.168   3.939  1.00166.78           O  
ANISOU 5357  O   CYS B 147    20249  27079  16040  -1135     58   1506       O  
ATOM   5358  CB  CYS B 147      28.693 -18.526   1.217  1.00164.91           C  
ANISOU 5358  CB  CYS B 147    19750  26350  16558  -1216    279   1486       C  
ATOM   5359  SG  CYS B 147      27.835 -19.936   1.943  1.00167.76           S  
ANISOU 5359  SG  CYS B 147    19832  26790  17117  -1132    378   1692       S  
ATOM   5360  N   GLN B 148      29.634 -16.988   3.687  1.00161.29           N  
ANISOU 5360  N   GLN B 148    19437  26295  15548  -1358    -61   1588       N  
ATOM   5361  CA  GLN B 148      29.940 -16.906   5.127  1.00163.52           C  
ANISOU 5361  CA  GLN B 148    19645  26880  15602  -1375   -217   1715       C  
ATOM   5362  C   GLN B 148      29.281 -15.694   5.811  1.00163.37           C  
ANISOU 5362  C   GLN B 148    19874  27009  15191  -1349   -311   1485       C  
ATOM   5363  O   GLN B 148      28.781 -15.800   6.933  1.00169.64           O  
ANISOU 5363  O   GLN B 148    20642  28083  15731  -1265   -369   1569       O  
ATOM   5364  CB  GLN B 148      31.457 -16.940   5.330  1.00166.07           C  
ANISOU 5364  CB  GLN B 148    19806  27242  16048  -1513   -339   1809       C  
ATOM   5365  CG  GLN B 148      32.017 -16.982   6.754  1.00170.65           C  
ANISOU 5365  CG  GLN B 148    20239  28198  16401  -1517   -531   1950       C  
ATOM   5366  CD  GLN B 148      33.517 -17.287   6.753  1.00174.29           C  
ANISOU 5366  CD  GLN B 148    20469  28675  17076  -1636   -629   2078       C  
ATOM   5367  OE1 GLN B 148      34.140 -17.430   5.692  1.00174.43           O  
ANISOU 5367  OE1 GLN B 148    20454  28397  17425  -1727   -537   2060       O  
ATOM   5368  NE2 GLN B 148      34.105 -17.389   7.946  1.00177.94           N  
ANISOU 5368  NE2 GLN B 148    20759  29513  17337  -1618   -818   2207       N  
ATOM   5369  N   ALA B 149      29.222 -14.564   5.112  1.00156.04           N  
ANISOU 5369  N   ALA B 149    19180  25885  14222  -1396   -292   1209       N  
ATOM   5370  CA  ALA B 149      28.538 -13.366   5.612  1.00154.20           C  
ANISOU 5370  CA  ALA B 149    19189  25720  13679  -1367   -337    963       C  
ATOM   5371  C   ALA B 149      27.096 -13.555   6.089  1.00154.02           C  
ANISOU 5371  C   ALA B 149    19240  25837  13441  -1201   -276    979       C  
ATOM   5372  O   ALA B 149      26.644 -12.766   6.905  1.00154.12           O  
ANISOU 5372  O   ALA B 149    19390  26005  13162  -1174   -340    829       O  
ATOM   5373  CB  ALA B 149      28.562 -12.286   4.552  1.00153.93           C  
ANISOU 5373  CB  ALA B 149    19377  25385  13724  -1397   -244    734       C  
ATOM   5374  N   THR B 150      26.388 -14.562   5.558  1.00152.05           N  
ANISOU 5374  N   THR B 150    18888  25519  13364  -1096   -143   1127       N  
ATOM   5375  CA  THR B 150      24.999 -14.877   5.946  1.00151.24           C  
ANISOU 5375  CA  THR B 150    18805  25519  13140   -940    -58   1158       C  
ATOM   5376  C   THR B 150      24.856 -15.833   7.129  1.00148.47           C  
ANISOU 5376  C   THR B 150    18243  25430  12736   -874    -58   1446       C  
ATOM   5377  O   THR B 150      23.791 -15.851   7.784  1.00150.61           O  
ANISOU 5377  O   THR B 150    18553  25842  12828   -748      0   1472       O  
ATOM   5378  CB  THR B 150      24.192 -15.528   4.790  1.00149.51           C  
ANISOU 5378  CB  THR B 150    18532  25098  13174   -851     99   1133       C  
ATOM   5379  OG1 THR B 150      24.774 -16.801   4.451  1.00149.81           O  
ANISOU 5379  OG1 THR B 150    18296  25064  13561   -891    158   1337       O  
ATOM   5380  CG2 THR B 150      24.105 -14.601   3.571  1.00145.77           C  
ANISOU 5380  CG2 THR B 150    18273  24419  12693   -838    130    884       C  
ATOM   5381  N   ARG B 151      25.886 -16.642   7.370  1.00144.60           N  
ANISOU 5381  N   ARG B 151    17523  25001  12414   -936    -97   1689       N  
ATOM   5382  CA  ARG B 151      25.814 -17.693   8.391  1.00155.41           C  
ANISOU 5382  CA  ARG B 151    18655  26605  13788   -835    -51   2047       C  
ATOM   5383  C   ARG B 151      25.385 -17.134   9.749  1.00161.29           C  
ANISOU 5383  C   ARG B 151    19495  27715  14071   -736   -138   2056       C  
ATOM   5384  O   ARG B 151      24.546 -17.746  10.456  1.00163.05           O  
ANISOU 5384  O   ARG B 151    19628  28091  14230   -576    -12   2281       O  
ATOM   5385  CB  ARG B 151      27.166 -18.384   8.584  1.00158.84           C  
ANISOU 5385  CB  ARG B 151    18850  27107  14396   -907   -120   2302       C  
ATOM   5386  CG  ARG B 151      27.739 -19.067   7.363  1.00158.24           C  
ANISOU 5386  CG  ARG B 151    18639  26700  14784   -998    -22   2330       C  
ATOM   5387  CD  ARG B 151      26.798 -20.106   6.796  1.00158.90           C  
ANISOU 5387  CD  ARG B 151    18584  26578  15213   -910    211   2421       C  
ATOM   5388  NE  ARG B 151      25.917 -19.547   5.782  1.00156.82           N  
ANISOU 5388  NE  ARG B 151    18516  26111  14956   -906    263   2080       N  
ATOM   5389  CZ  ARG B 151      25.157 -20.267   4.969  1.00154.39           C  
ANISOU 5389  CZ  ARG B 151    18098  25598  14963   -856    431   2015       C  
ATOM   5390  NH1 ARG B 151      25.126 -21.601   5.055  1.00152.88           N  
ANISOU 5390  NH1 ARG B 151    17597  25322  15167   -824    598   2258       N  
ATOM   5391  NH2 ARG B 151      24.419 -19.639   4.058  1.00151.52           N  
ANISOU 5391  NH2 ARG B 151    17918  25120  14532   -827    440   1692       N  
ATOM   5392  N   GLY B 152      25.962 -15.972  10.084  1.00160.36           N  
ANISOU 5392  N   GLY B 152    19544  27723  13660   -827   -333   1794       N  
ATOM   5393  CA  GLY B 152      25.711 -15.278  11.340  1.00158.75           C  
ANISOU 5393  CA  GLY B 152    19440  27890  12988   -752   -451   1702       C  
ATOM   5394  C   GLY B 152      24.287 -14.792  11.449  1.00156.16           C  
ANISOU 5394  C   GLY B 152    19312  27535  12484   -637   -332   1554       C  
ATOM   5395  O   GLY B 152      23.489 -15.414  12.143  1.00161.58           O  
ANISOU 5395  O   GLY B 152    19919  28406  13066   -468   -215   1789       O  
ATOM   5396  N   PRO B 153      23.943 -13.711  10.734  1.00150.83           N  
ANISOU 5396  N   PRO B 153    18883  26615  11808   -710   -333   1196       N  
ATOM   5397  CA  PRO B 153      22.598 -13.153  10.871  1.00150.62           C  
ANISOU 5397  CA  PRO B 153    19049  26577  11604   -590   -228   1044       C  
ATOM   5398  C   PRO B 153      21.444 -14.013  10.346  1.00148.20           C  
ANISOU 5398  C   PRO B 153    18665  26116  11526   -463    -19   1214       C  
ATOM   5399  O   PRO B 153      20.339 -13.915  10.898  1.00150.61           O  
ANISOU 5399  O   PRO B 153    19032  26534  11657   -324     75   1217       O  
ATOM   5400  CB  PRO B 153      22.671 -11.821  10.111  1.00146.89           C  
ANISOU 5400  CB  PRO B 153    18827  25841  11141   -693   -260    662       C  
ATOM   5401  CG  PRO B 153      23.789 -12.020   9.169  1.00146.80           C  
ANISOU 5401  CG  PRO B 153    18732  25604  11441   -841   -300    687       C  
ATOM   5402  CD  PRO B 153      24.791 -12.893   9.860  1.00148.78           C  
ANISOU 5402  CD  PRO B 153    18731  26096  11702   -885   -412    938       C  
ATOM   5403  N   CYS B 154      21.677 -14.876   9.348  1.00146.30           N  
ANISOU 5403  N   CYS B 154    18268  25635  11683   -507     58   1337       N  
ATOM   5404  CA  CYS B 154      20.604 -15.784   8.881  1.00146.26           C  
ANISOU 5404  CA  CYS B 154    18128  25492  11950   -398    252   1452       C  
ATOM   5405  C   CYS B 154      20.592 -17.130   9.606  1.00146.53           C  
ANISOU 5405  C   CYS B 154    17867  25656  12151   -319    372   1850       C  
ATOM   5406  O   CYS B 154      20.313 -18.158   8.997  1.00143.61           O  
ANISOU 5406  O   CYS B 154    17283  25090  12192   -305    524   1969       O  
ATOM   5407  CB  CYS B 154      20.685 -15.992   7.365  1.00146.33           C  
ANISOU 5407  CB  CYS B 154    18111  25183  12304   -459    295   1311       C  
ATOM   5408  SG  CYS B 154      20.502 -14.453   6.434  1.00148.20           S  
ANISOU 5408  SG  CYS B 154    18682  25258  12366   -477    228    924       S  
ATOM   5409  N   ALA B 155      20.845 -17.098  10.918  1.00151.50           N  
ANISOU 5409  N   ALA B 155    18476  26624  12461   -248    322   2043       N  
ATOM   5410  CA  ALA B 155      20.906 -18.295  11.757  1.00148.65           C  
ANISOU 5410  CA  ALA B 155    17839  26438  12201   -128    455   2494       C  
ATOM   5411  C   ALA B 155      19.536 -18.927  11.938  1.00145.76           C  
ANISOU 5411  C   ALA B 155    17370  26004  12007     26    717   2639       C  
ATOM   5412  O   ALA B 155      19.473 -20.120  12.204  1.00141.53           O  
ANISOU 5412  O   ALA B 155    16554  25439  11781    109    914   3011       O  
ATOM   5413  CB  ALA B 155      21.507 -17.963  13.114  1.00150.74           C  
ANISOU 5413  CB  ALA B 155    18125  27159  11988    -51    314   2638       C  
ATOM   5414  N   ILE B 156      18.459 -18.142  11.778  1.00145.59           N  
ANISOU 5414  N   ILE B 156    17551  25934  11832     67    739   2356       N  
ATOM   5415  CA  ILE B 156      17.087 -18.692  11.764  1.00152.11           C  
ANISOU 5415  CA  ILE B 156    18261  26642  12891    194    988   2429       C  
ATOM   5416  C   ILE B 156      16.887 -19.812  10.766  1.00153.02           C  
ANISOU 5416  C   ILE B 156    18099  26413  13627    145   1152   2475       C  
ATOM   5417  O   ILE B 156      16.047 -20.696  10.985  1.00153.53           O  
ANISOU 5417  O   ILE B 156    17932  26389  14014    246   1404   2671       O  
ATOM   5418  CB  ILE B 156      15.955 -17.670  11.453  1.00156.43           C  
ANISOU 5418  CB  ILE B 156    19048  27130  13256    233    977   2067       C  
ATOM   5419  CG1 ILE B 156      16.165 -16.969  10.120  1.00166.99           C  
ANISOU 5419  CG1 ILE B 156    20544  28225  14677    103    832   1683       C  
ATOM   5420  CG2 ILE B 156      15.814 -16.610  12.501  1.00158.68           C  
ANISOU 5420  CG2 ILE B 156    19584  27726  12981    310    885   1986       C  
ATOM   5421  CD1 ILE B 156      14.846 -16.511   9.533  1.00179.15           C  
ANISOU 5421  CD1 ILE B 156    22172  29634  16261    184    906   1421       C  
ATOM   5422  N   VAL B 157      17.628 -19.751   9.657  1.00154.94           N  
ANISOU 5422  N   VAL B 157    18357  26454  14056     -6   1025   2270       N  
ATOM   5423  CA  VAL B 157      17.506 -20.736   8.589  1.00154.78           C  
ANISOU 5423  CA  VAL B 157    18082  26120  14605    -63   1153   2219       C  
ATOM   5424  C   VAL B 157      18.000 -22.080   9.093  1.00158.47           C  
ANISOU 5424  C   VAL B 157    18213  26549  15447    -41   1339   2649       C  
ATOM   5425  O   VAL B 157      17.299 -23.077   8.919  1.00161.49           O  
ANISOU 5425  O   VAL B 157    18314  26731  16314      2   1584   2738       O  
ATOM   5426  CB  VAL B 157      18.283 -20.328   7.322  1.00152.74           C  
ANISOU 5426  CB  VAL B 157    17931  25701  14401   -205    981   1921       C  
ATOM   5427  CG1 VAL B 157      18.155 -21.394   6.225  1.00153.80           C  
ANISOU 5427  CG1 VAL B 157    17781  25549  15105   -250   1113   1826       C  
ATOM   5428  CG2 VAL B 157      17.784 -18.979   6.817  1.00153.08           C  
ANISOU 5428  CG2 VAL B 157    18299  25769  14093   -192    839   1551       C  
ATOM   5429  N   GLU B 158      19.166 -22.106   9.752  1.00159.85           N  
ANISOU 5429  N   GLU B 158    18394  26918  15422    -60   1237   2918       N  
ATOM   5430  CA  GLU B 158      19.704 -23.372  10.238  1.00161.92           C  
ANISOU 5430  CA  GLU B 158    18329  27157  16036     -9   1424   3380       C  
ATOM   5431  C   GLU B 158      18.936 -23.936  11.417  1.00175.16           C  
ANISOU 5431  C   GLU B 158    19855  28988  17709    195   1676   3783       C  
ATOM   5432  O   GLU B 158      18.985 -25.145  11.657  1.00187.14           O  
ANISOU 5432  O   GLU B 158    21044  30374  19684    267   1945   4168       O  
ATOM   5433  CB  GLU B 158      21.183 -23.323  10.573  1.00156.42           C  
ANISOU 5433  CB  GLU B 158    17634  26642  15154    -64   1247   3576       C  
ATOM   5434  CG  GLU B 158      21.799 -24.681  10.264  1.00155.70           C  
ANISOU 5434  CG  GLU B 158    17186  26320  15652    -84   1441   3884       C  
ATOM   5435  CD  GLU B 158      23.231 -24.785  10.678  1.00157.31           C  
ANISOU 5435  CD  GLU B 158    17332  26717  15720   -106   1295   4147       C  
ATOM   5436  OE1 GLU B 158      24.019 -24.034  10.074  1.00158.73           O  
ANISOU 5436  OE1 GLU B 158    17689  26891  15728   -262   1044   3851       O  
ATOM   5437  OE2 GLU B 158      23.558 -25.608  11.566  1.00155.88           O  
ANISOU 5437  OE2 GLU B 158    16916  26687  15622     41   1445   4653       O  
ATOM   5438  N   ARG B 159      18.228 -23.068  12.142  1.00183.18           N  
ANISOU 5438  N   ARG B 159    21100  30265  18235    299   1620   3707       N  
ATOM   5439  CA  ARG B 159      17.385 -23.476  13.273  1.00186.62           C  
ANISOU 5439  CA  ARG B 159    21427  30876  18605    521   1875   4073       C  
ATOM   5440  C   ARG B 159      16.018 -24.020  12.806  1.00184.55           C  
ANISOU 5440  C   ARG B 159    20990  30284  18846    550   2161   3978       C  
ATOM   5441  O   ARG B 159      15.507 -24.956  13.409  1.00186.63           O  
ANISOU 5441  O   ARG B 159    20985  30493  19432    697   2493   4374       O  
ATOM   5442  CB  ARG B 159      17.203 -22.314  14.281  1.00189.47           C  
ANISOU 5442  CB  ARG B 159    22097  31676  18217    631   1704   4006       C  
ATOM   5443  CG  ARG B 159      18.480 -21.778  14.987  1.00192.30           C  
ANISOU 5443  CG  ARG B 159    22580  32441  18042    633   1426   4090       C  
ATOM   5444  CD  ARG B 159      18.364 -21.647  16.503  1.00199.56           C  
ANISOU 5444  CD  ARG B 159    23526  33873  18424    883   1467   4416       C  
ATOM   5445  NE  ARG B 159      17.501 -20.525  16.883  1.00206.82           N  
ANISOU 5445  NE  ARG B 159    24735  34963  18883    932   1393   4087       N  
ATOM   5446  CZ  ARG B 159      16.178 -20.590  17.083  1.00217.24           C  
ANISOU 5446  CZ  ARG B 159    26058  36202  20279   1057   1640   4115       C  
ATOM   5447  NH1 ARG B 159      15.501 -21.727  16.933  1.00225.23           N  
ANISOU 5447  NH1 ARG B 159    26787  36946  21844   1139   1989   4439       N  
ATOM   5448  NH2 ARG B 159      15.518 -19.485  17.428  1.00220.61           N  
ANISOU 5448  NH2 ARG B 159    26761  36797  20262   1095   1549   3796       N  
ATOM   5449  N   GLU B 160      15.426 -23.458  11.739  1.00180.79           N  
ANISOU 5449  N   GLU B 160    20639  29594  18458    427   2048   3467       N  
ATOM   5450  CA  GLU B 160      14.069 -23.876  11.316  1.00181.47           C  
ANISOU 5450  CA  GLU B 160    20546  29419  18983    462   2280   3311       C  
ATOM   5451  C   GLU B 160      13.981 -25.013  10.320  1.00180.98           C  
ANISOU 5451  C   GLU B 160    20123  28949  19689    360   2454   3218       C  
ATOM   5452  O   GLU B 160      13.248 -25.958  10.563  1.00180.68           O  
ANISOU 5452  O   GLU B 160    19763  28718  20166    433   2784   3411       O  
ATOM   5453  CB  GLU B 160      13.224 -22.693  10.834  1.00180.69           C  
ANISOU 5453  CB  GLU B 160    20733  29360  18560    448   2102   2834       C  
ATOM   5454  CG  GLU B 160      12.258 -22.204  11.907  1.00192.58           C  
ANISOU 5454  CG  GLU B 160    22356  31091  19724    625   2218   2963       C  
ATOM   5455  CD  GLU B 160      12.880 -21.814  13.255  1.00207.57           C  
ANISOU 5455  CD  GLU B 160    24424  33394  21048    743   2167   3308       C  
ATOM   5456  OE1 GLU B 160      13.975 -21.223  13.259  1.00230.16           O  
ANISOU 5456  OE1 GLU B 160    27482  36424  23543    658   1898   3234       O  
ATOM   5457  OE2 GLU B 160      12.259 -22.059  14.328  1.00201.05           O  
ANISOU 5457  OE2 GLU B 160    23531  32743  20115    934   2397   3636       O  
ATOM   5458  N   ARG B 161      14.684 -24.899   9.199  1.00186.57           N  
ANISOU 5458  N   ARG B 161    20874  29522  20491    199   2251   2899       N  
ATOM   5459  CA  ARG B 161      14.703 -25.969   8.179  1.00191.56           C  
ANISOU 5459  CA  ARG B 161    21159  29787  21837     95   2395   2741       C  
ATOM   5460  C   ARG B 161      16.105 -26.422   7.791  1.00192.37           C  
ANISOU 5460  C   ARG B 161    21196  29814  22081    -16   2319   2856       C  
ATOM   5461  O   ARG B 161      16.233 -27.355   7.016  1.00192.04           O  
ANISOU 5461  O   ARG B 161    20858  29473  22636    -99   2454   2744       O  
ATOM   5462  CB  ARG B 161      13.909 -25.561   6.921  1.00191.68           C  
ANISOU 5462  CB  ARG B 161    21206  29675  21946     32   2270   2139       C  
ATOM   5463  CG  ARG B 161      12.402 -25.506   7.169  1.00199.10           C  
ANISOU 5463  CG  ARG B 161    22053  30591  23002    137   2425   2019       C  
ATOM   5464  CD  ARG B 161      11.515 -25.453   5.922  1.00202.84           C  
ANISOU 5464  CD  ARG B 161    22411  30925  23733    100   2357   1445       C  
ATOM   5465  NE  ARG B 161      10.166 -24.926   6.247  1.00206.72           N  
ANISOU 5465  NE  ARG B 161    22949  31504  24090    218   2403   1318       N  
ATOM   5466  CZ  ARG B 161       9.102 -24.891   5.428  1.00201.65           C  
ANISOU 5466  CZ  ARG B 161    22158  30789  23670    238   2382    866       C  
ATOM   5467  NH1 ARG B 161       9.185 -25.341   4.177  1.00200.52           N  
ANISOU 5467  NH1 ARG B 161    21808  30509  23870    155   2302    448       N  
ATOM   5468  NH2 ARG B 161       7.936 -24.390   5.865  1.00195.07           N  
ANISOU 5468  NH2 ARG B 161    21372  30048  22698    355   2436    816       N  
ATOM   5469  N   GLY B 162      17.150 -25.817   8.359  1.00194.82           N  
ANISOU 5469  N   GLY B 162    21748  30391  21884    -16   2120   3071       N  
ATOM   5470  CA  GLY B 162      18.525 -26.114   7.949  1.00188.39           C  
ANISOU 5470  CA  GLY B 162    20890  29522  21166   -128   2016   3151       C  
ATOM   5471  C   GLY B 162      18.883 -25.506   6.601  1.00181.15           C  
ANISOU 5471  C   GLY B 162    20143  28505  20180   -272   1781   2653       C  
ATOM   5472  O   GLY B 162      18.022 -25.303   5.723  1.00176.20           O  
ANISOU 5472  O   GLY B 162    19529  27756  19659   -287   1767   2237       O  
ATOM   5473  N   TRP B 163      20.172 -25.212   6.432  1.00178.80           N  
ANISOU 5473  N   TRP B 163    19961  28278  19696   -361   1600   2706       N  
ATOM   5474  CA  TRP B 163      20.687 -24.722   5.153  1.00178.74           C  
ANISOU 5474  CA  TRP B 163    20093  28166  19653   -481   1420   2312       C  
ATOM   5475  C   TRP B 163      20.741 -25.892   4.176  1.00186.59           C  
ANISOU 5475  C   TRP B 163    20754  28843  21299   -542   1598   2185       C  
ATOM   5476  O   TRP B 163      21.314 -26.936   4.514  1.00196.00           O  
ANISOU 5476  O   TRP B 163    21664  29907  22900   -556   1775   2509       O  
ATOM   5477  CB  TRP B 163      22.112 -24.154   5.272  1.00172.95           C  
ANISOU 5477  CB  TRP B 163    19532  27566  18615   -567   1213   2425       C  
ATOM   5478  CG  TRP B 163      22.190 -22.812   5.902  1.00166.27           C  
ANISOU 5478  CG  TRP B 163    19033  26997  17143   -549    993   2376       C  
ATOM   5479  CD1 TRP B 163      22.688 -22.514   7.136  1.00166.76           C  
ANISOU 5479  CD1 TRP B 163    19156  27337  16865   -509    908   2666       C  
ATOM   5480  CD2 TRP B 163      21.760 -21.572   5.329  1.00157.53           C  
ANISOU 5480  CD2 TRP B 163    18243  25922  15687   -560    839   1997       C  
ATOM   5481  NE1 TRP B 163      22.594 -21.163   7.372  1.00165.84           N  
ANISOU 5481  NE1 TRP B 163    19370  27403  16236   -518    710   2442       N  
ATOM   5482  CE2 TRP B 163      22.026 -20.560   6.275  1.00160.00           C  
ANISOU 5482  CE2 TRP B 163    18796  26492  15504   -549    681   2055       C  
ATOM   5483  CE3 TRP B 163      21.165 -21.218   4.111  1.00149.81           C  
ANISOU 5483  CE3 TRP B 163    17357  24800  14764   -556    827   1615       C  
ATOM   5484  CZ2 TRP B 163      21.720 -19.210   6.032  1.00154.60           C  
ANISOU 5484  CZ2 TRP B 163    18437  25860  14443   -552    542   1750       C  
ATOM   5485  CZ3 TRP B 163      20.870 -19.877   3.872  1.00146.95           C  
ANISOU 5485  CZ3 TRP B 163    17324  24522  13985   -530    686   1367       C  
ATOM   5486  CH2 TRP B 163      21.147 -18.894   4.829  1.00147.60           C  
ANISOU 5486  CH2 TRP B 163    17638  24799  13642   -537    561   1440       C  
ATOM   5487  N   PRO B 164      20.198 -25.723   2.953  1.00189.76           N  
ANISOU 5487  N   PRO B 164    21173  29131  21796   -566   1553   1708       N  
ATOM   5488  CA  PRO B 164      20.397 -26.794   1.984  1.00191.40           C  
ANISOU 5488  CA  PRO B 164    21062  29068  22591   -631   1696   1525       C  
ATOM   5489  C   PRO B 164      21.894 -27.003   1.670  1.00197.65           C  
ANISOU 5489  C   PRO B 164    21847  29802  23447   -730   1645   1670       C  
ATOM   5490  O   PRO B 164      22.695 -26.046   1.748  1.00197.32           O  
ANISOU 5490  O   PRO B 164    22104  29931  22935   -761   1434   1727       O  
ATOM   5491  CB  PRO B 164      19.626 -26.305   0.749  1.00188.46           C  
ANISOU 5491  CB  PRO B 164    20776  28710  22120   -604   1585    963       C  
ATOM   5492  CG  PRO B 164      18.779 -25.169   1.216  1.00187.10           C  
ANISOU 5492  CG  PRO B 164    20902  28761  21424   -509   1452    914       C  
ATOM   5493  CD  PRO B 164      19.538 -24.553   2.342  1.00188.06           C  
ANISOU 5493  CD  PRO B 164    21258  29049  21148   -522   1365   1321       C  
ATOM   5494  N   ASP B 165      22.241 -28.252   1.342  1.00203.78           N  
ANISOU 5494  N   ASP B 165    22263  30317  24846   -780   1857   1722       N  
ATOM   5495  CA  ASP B 165      23.597 -28.691   0.916  1.00200.01           C  
ANISOU 5495  CA  ASP B 165    21697  29724  24574   -871   1865   1833       C  
ATOM   5496  C   ASP B 165      24.370 -27.659   0.071  1.00191.27           C  
ANISOU 5496  C   ASP B 165    20910  28744  23018   -921   1613   1594       C  
ATOM   5497  O   ASP B 165      25.533 -27.355   0.369  1.00189.58           O  
ANISOU 5497  O   ASP B 165    20803  28599  22630   -975   1516   1849       O  
ATOM   5498  CB  ASP B 165      23.499 -30.016   0.121  1.00199.28           C  
ANISOU 5498  CB  ASP B 165    21192  29295  25228   -917   2117   1631       C  
ATOM   5499  CG  ASP B 165      22.417 -29.978  -0.985  1.00202.58           C  
ANISOU 5499  CG  ASP B 165    21558  29671  25740   -898   2100   1014       C  
ATOM   5500  OD1 ASP B 165      21.198 -29.961  -0.658  1.00213.14           O  
ANISOU 5500  OD1 ASP B 165    22837  31031  27114   -834   2155    909       O  
ATOM   5501  OD2 ASP B 165      22.780 -29.934  -2.180  1.00200.90           O  
ANISOU 5501  OD2 ASP B 165    21361  29436  25535   -930   2024    630       O  
ATOM   5502  N   PHE B 166      23.671 -27.090  -0.917  1.00179.78           N  
ANISOU 5502  N   PHE B 166    19598  27339  21370   -882   1516   1128       N  
ATOM   5503  CA  PHE B 166      24.232 -26.156  -1.895  1.00174.71           C  
ANISOU 5503  CA  PHE B 166    19234  26796  20350   -888   1336    880       C  
ATOM   5504  C   PHE B 166      24.328 -24.707  -1.432  1.00169.91           C  
ANISOU 5504  C   PHE B 166    19030  26411  19115   -861   1128    968       C  
ATOM   5505  O   PHE B 166      24.890 -23.866  -2.145  1.00168.97           O  
ANISOU 5505  O   PHE B 166    19146  26346  18706   -863   1013    835       O  
ATOM   5506  CB  PHE B 166      23.476 -26.219  -3.233  1.00174.57           C  
ANISOU 5506  CB  PHE B 166    19166  26773  20389   -813   1337    353       C  
ATOM   5507  CG  PHE B 166      22.049 -25.789  -3.162  1.00177.85           C  
ANISOU 5507  CG  PHE B 166    19644  27317  20612   -702   1290    125       C  
ATOM   5508  CD1 PHE B 166      21.063 -26.705  -2.852  1.00180.68           C  
ANISOU 5508  CD1 PHE B 166    19683  27560  21404   -691   1448     44       C  
ATOM   5509  CD2 PHE B 166      21.682 -24.470  -3.459  1.00183.58           C  
ANISOU 5509  CD2 PHE B 166    20727  28259  20765   -601   1110    -15       C  
ATOM   5510  CE1 PHE B 166      19.737 -26.315  -2.788  1.00186.29           C  
ANISOU 5510  CE1 PHE B 166    20428  28389  21963   -588   1407   -172       C  
ATOM   5511  CE2 PHE B 166      20.358 -24.072  -3.399  1.00185.97           C  
ANISOU 5511  CE2 PHE B 166    21075  28685  20900   -486   1070   -217       C  
ATOM   5512  CZ  PHE B 166      19.380 -25.002  -3.080  1.00187.71           C  
ANISOU 5512  CZ  PHE B 166    20970  28809  21542   -482   1208   -309       C  
ATOM   5513  N   LEU B 167      23.778 -24.420  -0.258  1.00166.78           N  
ANISOU 5513  N   LEU B 167    18703  26133  18533   -829   1107   1184       N  
ATOM   5514  CA  LEU B 167      23.931 -23.134   0.385  1.00168.47           C  
ANISOU 5514  CA  LEU B 167    19258  26544  18209   -820    930   1278       C  
ATOM   5515  C   LEU B 167      24.804 -23.208   1.649  1.00172.25           C  
ANISOU 5515  C   LEU B 167    19709  27118  18618   -880    893   1697       C  
ATOM   5516  O   LEU B 167      24.943 -22.202   2.353  1.00181.52           O  
ANISOU 5516  O   LEU B 167    21125  28477  19365   -881    745   1759       O  
ATOM   5517  CB  LEU B 167      22.559 -22.579   0.728  1.00164.91           C  
ANISOU 5517  CB  LEU B 167    18935  26212  17509   -709    911   1139       C  
ATOM   5518  CG  LEU B 167      21.731 -22.057  -0.443  1.00163.21           C  
ANISOU 5518  CG  LEU B 167    18836  26007  17167   -614    871    722       C  
ATOM   5519  CD1 LEU B 167      20.304 -21.760   0.039  1.00166.58           C  
ANISOU 5519  CD1 LEU B 167    19303  26534  17453   -502    885    629       C  
ATOM   5520  CD2 LEU B 167      22.410 -20.811  -0.995  1.00158.74           C  
ANISOU 5520  CD2 LEU B 167    18602  25505  16207   -615    729    635       C  
ATOM   5521  N   ARG B 168      25.418 -24.362   1.917  1.00168.59           N  
ANISOU 5521  N   ARG B 168    18943  26546  18568   -920   1025   1968       N  
ATOM   5522  CA  ARG B 168      26.426 -24.468   2.965  1.00169.45           C  
ANISOU 5522  CA  ARG B 168    18997  26782  18603   -954    973   2370       C  
ATOM   5523  C   ARG B 168      27.760 -24.055   2.349  1.00170.32           C  
ANISOU 5523  C   ARG B 168    19189  26850  18675  -1069    851   2320       C  
ATOM   5524  O   ARG B 168      28.039 -24.417   1.229  1.00177.98           O  
ANISOU 5524  O   ARG B 168    20085  27621  19917  -1111    925   2134       O  
ATOM   5525  CB  ARG B 168      26.485 -25.894   3.514  1.00170.58           C  
ANISOU 5525  CB  ARG B 168    18761  26818  19231   -913   1201   2733       C  
ATOM   5526  CG  ARG B 168      25.229 -26.306   4.293  1.00172.33           C  
ANISOU 5526  CG  ARG B 168    18878  27080  19517   -788   1360   2862       C  
ATOM   5527  CD  ARG B 168      25.539 -27.474   5.269  1.00174.12           C  
ANISOU 5527  CD  ARG B 168    18773  27292  20090   -709   1576   3395       C  
ATOM   5528  NE  ARG B 168      25.337 -28.793   4.668  1.00176.10           N  
ANISOU 5528  NE  ARG B 168    18661  27183  21065   -724   1871   3400       N  
ATOM   5529  CZ  ARG B 168      24.193 -29.482   4.551  1.00174.80           C  
ANISOU 5529  CZ  ARG B 168    18289  26816  21309   -673   2115   3308       C  
ATOM   5530  NH1 ARG B 168      23.022 -29.028   4.989  1.00170.80           N  
ANISOU 5530  NH1 ARG B 168    17899  26429  20566   -590   2117   3223       N  
ATOM   5531  NH2 ARG B 168      24.231 -30.675   3.962  1.00177.60           N  
ANISOU 5531  NH2 ARG B 168    18287  26820  22373   -713   2378   3277       N  
ATOM   5532  N   CYS B 169      28.602 -23.324   3.085  1.00178.05           N  
ANISOU 5532  N   CYS B 169    20310  28025  19316  -1116    668   2456       N  
ATOM   5533  CA  CYS B 169      29.891 -22.882   2.479  1.00179.44           C  
ANISOU 5533  CA  CYS B 169    20577  28148  19452  -1235    552   2375       C  
ATOM   5534  C   CYS B 169      31.022 -23.874   2.785  1.00185.49           C  
ANISOU 5534  C   CYS B 169    21051  28803  20621  -1294    630   2634       C  
ATOM   5535  O   CYS B 169      32.153 -23.630   2.322  1.00167.98           O  
ANISOU 5535  O   CYS B 169    18856  26479  18488  -1388    594   2557       O  
ATOM   5536  CB  CYS B 169      30.288 -21.492   2.958  1.00179.49           C  
ANISOU 5536  CB  CYS B 169    20807  28382  19008  -1282    329   2358       C  
ATOM   5537  SG  CYS B 169      28.898 -20.516   3.586  1.00181.98           S  
ANISOU 5537  SG  CYS B 169    21438  28846  18858  -1196    257   2114       S  
ATOM   5538  N   THR B 170      30.726 -24.954   3.517  1.00214.99           N  
ANISOU 5538  N   THR B 170    24506  32556  24622  -1224    763   2962       N  
ATOM   5539  CA  THR B 170      31.755 -25.971   3.875  1.00237.86           C  
ANISOU 5539  CA  THR B 170    27085  35370  27920  -1242    865   3299       C  
ATOM   5540  C   THR B 170      32.297 -26.638   2.603  1.00236.78           C  
ANISOU 5540  C   THR B 170    26800  34891  28271  -1305   1041   3129       C  
ATOM   5541  O   THR B 170      33.529 -26.796   2.497  1.00248.06           O  
ANISOU 5541  O   THR B 170    28130  36251  29869  -1380   1025   3231       O  
ATOM   5542  CB  THR B 170      31.173 -27.019   4.832  1.00247.13           C  
ANISOU 5542  CB  THR B 170    27996  36650  29252  -1102   1013   3744       C  
ATOM   5543  OG1 THR B 170      30.702 -26.345   6.000  1.00250.69           O  
ANISOU 5543  OG1 THR B 170    28546  37490  29211  -1038    815   3950       O  
ATOM   5544  CG2 THR B 170      32.176 -28.081   5.225  1.00244.51           C  
ANISOU 5544  CG2 THR B 170    27281  36154  29466  -1080   1214   4122       C  
ATOM   5545  N   PRO B 171      31.437 -26.989   1.622  1.00224.59           N  
ANISOU 5545  N   PRO B 171    25227  33155  26950  -1270   1201   2845       N  
ATOM   5546  CA  PRO B 171      31.862 -27.627   0.369  1.00220.49           C  
ANISOU 5546  CA  PRO B 171    24566  32359  26851  -1321   1350   2624       C  
ATOM   5547  C   PRO B 171      32.624 -26.711  -0.603  1.00216.86           C  
ANISOU 5547  C   PRO B 171    24322  31894  26181  -1398   1224   2404       C  
ATOM   5548  O   PRO B 171      32.671 -25.513  -0.390  1.00211.22           O  
ANISOU 5548  O   PRO B 171    23892  31350  25010  -1419   1031   2349       O  
ATOM   5549  CB  PRO B 171      30.550 -28.090  -0.281  1.00221.36           C  
ANISOU 5549  CB  PRO B 171    24649  32360  27095  -1258   1472   2264       C  
ATOM   5550  CG  PRO B 171      29.514 -27.158   0.295  1.00221.86           C  
ANISOU 5550  CG  PRO B 171    24863  32620  26813  -1181   1391   2307       C  
ATOM   5551  CD  PRO B 171      29.980 -26.925   1.716  1.00224.61           C  
ANISOU 5551  CD  PRO B 171    25229  33177  26934  -1174   1289   2756       C  
ATOM   5552  N   ASP B 172      33.195 -27.329  -1.645  1.00211.31           N  
ANISOU 5552  N   ASP B 172    23468  30977  25841  -1434   1363   2279       N  
ATOM   5553  CA  ASP B 172      34.032 -26.708  -2.712  1.00202.63           C  
ANISOU 5553  CA  ASP B 172    22554  29847  24588  -1477   1308   2065       C  
ATOM   5554  C   ASP B 172      33.213 -25.872  -3.708  1.00206.10           C  
ANISOU 5554  C   ASP B 172    23315  30386  24604  -1406   1222   1692       C  
ATOM   5555  O   ASP B 172      33.844 -25.202  -4.548  1.00205.00           O  
ANISOU 5555  O   ASP B 172    23378  30262  24250  -1422   1167   1605       O  
ATOM   5556  CB  ASP B 172      34.801 -27.778  -3.490  1.00197.01           C  
ANISOU 5556  CB  ASP B 172    21601  28899  24354  -1498   1509   1969       C  
ATOM   5557  CG  ASP B 172      33.904 -28.602  -4.397  1.00195.13           C  
ANISOU 5557  CG  ASP B 172    21213  28542  24386  -1423   1676   1605       C  
ATOM   5558  OD1 ASP B 172      32.670 -28.457  -4.288  1.00188.45           O  
ANISOU 5558  OD1 ASP B 172    20325  27742  23535  -1374   1681   1578       O  
ATOM   5559  OD2 ASP B 172      34.444 -29.379  -5.209  1.00189.70           O  
ANISOU 5559  OD2 ASP B 172    20443  27734  23901  -1408   1796   1323       O  
ATOM   5560  N   ARG B 173      31.878 -25.908  -3.640  1.00208.60           N  
ANISOU 5560  N   ARG B 173    23641  30751  24866  -1316   1246   1486       N  
ATOM   5561  CA  ARG B 173      31.015 -25.165  -4.599  1.00206.44           C  
ANISOU 5561  CA  ARG B 173    23663  30621  24154  -1213   1149   1175       C  
ATOM   5562  C   ARG B 173      31.341 -23.667  -4.551  1.00207.20           C  
ANISOU 5562  C   ARG B 173    24115  30858  23751  -1216    981   1220       C  
ATOM   5563  O   ARG B 173      31.404 -23.057  -5.635  1.00197.76           O  
ANISOU 5563  O   ARG B 173    23148  29731  22261  -1114    955    974       O  
ATOM   5564  CB  ARG B 173      29.540 -25.386  -4.250  1.00206.16           C  
ANISOU 5564  CB  ARG B 173    23544  30638  24148  -1138   1173   1072       C  
ATOM   5565  CG  ARG B 173      28.984 -26.730  -4.700  1.00205.73           C  
ANISOU 5565  CG  ARG B 173    23199  30454  24514  -1092   1338    790       C  
ATOM   5566  CD  ARG B 173      27.580 -26.970  -4.177  1.00206.88           C  
ANISOU 5566  CD  ARG B 173    23225  30622  24756  -1041   1378    748       C  
ATOM   5567  NE  ARG B 173      26.926 -28.104  -4.813  1.00203.94           N  
ANISOU 5567  NE  ARG B 173    22534  30107  24846  -1012   1540    413       N  
ATOM   5568  CZ  ARG B 173      26.035 -28.005  -5.793  1.00202.41           C  
ANISOU 5568  CZ  ARG B 173    22354  30004  24549   -910   1508    -67       C  
ATOM   5569  NH1 ARG B 173      25.686 -26.816  -6.252  1.00201.25           N  
ANISOU 5569  NH1 ARG B 173    22542  30088  23836   -801   1337   -234       N  
ATOM   5570  NH2 ARG B 173      25.494 -29.095  -6.309  1.00202.48           N  
ANISOU 5570  NH2 ARG B 173    22011  29875  25045   -905   1656   -399       N  
ATOM   5571  N   PHE B 174      31.570 -23.097  -3.362  1.00210.08           N  
ANISOU 5571  N   PHE B 174    24514  31280  24025  -1316    874   1511       N  
ATOM   5572  CA  PHE B 174      31.899 -21.649  -3.287  1.00204.64           C  
ANISOU 5572  CA  PHE B 174    24122  30685  22944  -1350    728   1515       C  
ATOM   5573  C   PHE B 174      33.419 -21.457  -3.204  1.00206.62           C  
ANISOU 5573  C   PHE B 174    24310  30867  23328  -1486    696   1704       C  
ATOM   5574  O   PHE B 174      34.022 -21.844  -2.183  1.00193.21           O  
ANISOU 5574  O   PHE B 174    22475  29252  21681  -1568    605   1949       O  
ATOM   5575  CB  PHE B 174      31.209 -21.008  -2.080  1.00201.81           C  
ANISOU 5575  CB  PHE B 174    23874  30512  22292  -1340    595   1593       C  
ATOM   5576  CG  PHE B 174      29.725 -21.260  -2.001  1.00200.84           C  
ANISOU 5576  CG  PHE B 174    23803  30449  22056  -1209    632   1418       C  
ATOM   5577  CD1 PHE B 174      28.817 -20.279  -2.365  1.00199.06           C  
ANISOU 5577  CD1 PHE B 174    23853  30268  21512  -1113    602   1174       C  
ATOM   5578  CD2 PHE B 174      29.235 -22.482  -1.569  1.00199.76           C  
ANISOU 5578  CD2 PHE B 174    23420  30311  22169  -1171    721   1507       C  
ATOM   5579  CE1 PHE B 174      27.453 -20.513  -2.293  1.00197.00           C  
ANISOU 5579  CE1 PHE B 174    23613  30074  21160   -984    629   1001       C  
ATOM   5580  CE2 PHE B 174      27.871 -22.715  -1.499  1.00197.31           C  
ANISOU 5580  CE2 PHE B 174    23122  30037  21808  -1059    766   1319       C  
ATOM   5581  CZ  PHE B 174      26.982 -21.731  -1.860  1.00195.76           C  
ANISOU 5581  CZ  PHE B 174    23197  29913  21267   -967    704   1055       C  
ATOM   5582  N   PRO B 175      34.066 -20.879  -4.243  1.00216.57           N  
ANISOU 5582  N   PRO B 175    25653  31996  24636  -1491    777   1597       N  
ATOM   5583  CA  PRO B 175      35.510 -20.616  -4.233  1.00208.19           C  
ANISOU 5583  CA  PRO B 175    24507  30841  23753  -1622    771   1762       C  
ATOM   5584  C   PRO B 175      35.880 -19.544  -3.198  1.00195.22           C  
ANISOU 5584  C   PRO B 175    23040  29255  21880  -1717    626   1786       C  
ATOM   5585  O   PRO B 175      35.056 -18.695  -2.910  1.00177.06           O  
ANISOU 5585  O   PRO B 175    20993  27005  19276  -1661    586   1631       O  
ATOM   5586  CB  PRO B 175      35.812 -20.079  -5.640  1.00216.69           C  
ANISOU 5586  CB  PRO B 175    25619  31762  24952  -1560    950   1624       C  
ATOM   5587  CG  PRO B 175      34.659 -20.574  -6.481  1.00226.67           C  
ANISOU 5587  CG  PRO B 175    26921  33072  26132  -1394   1032   1382       C  
ATOM   5588  CD  PRO B 175      33.473 -20.556  -5.541  1.00226.34           C  
ANISOU 5588  CD  PRO B 175    27011  33181  25806  -1352    903   1336       C  
ATOM   5589  N   GLU B 176      37.104 -19.628  -2.668  1.00196.33           N  
ANISOU 5589  N   GLU B 176    23017  29376  22203  -1857    560   1961       N  
ATOM   5590  CA  GLU B 176      37.606 -18.686  -1.633  1.00200.07           C  
ANISOU 5590  CA  GLU B 176    23531  29960  22527  -1980    371   1986       C  
ATOM   5591  C   GLU B 176      37.593 -17.240  -2.146  1.00191.69           C  
ANISOU 5591  C   GLU B 176    22744  28790  21299  -2004    392   1783       C  
ATOM   5592  O   GLU B 176      36.911 -16.406  -1.520  1.00199.38           O  
ANISOU 5592  O   GLU B 176    23860  29875  22019  -2027    264   1673       O  
ATOM   5593  CB  GLU B 176      39.018 -19.082  -1.195  1.00199.91           C  
ANISOU 5593  CB  GLU B 176    23233  29931  22793  -2116    311   2186       C  
ATOM   5594  CG  GLU B 176      39.088 -20.442  -0.524  1.00202.48           C  
ANISOU 5594  CG  GLU B 176    23248  30400  23281  -2094    263   2464       C  
ATOM   5595  CD  GLU B 176      38.429 -20.522   0.842  1.00203.65           C  
ANISOU 5595  CD  GLU B 176    23348  30874  23153  -2067     55   2569       C  
ATOM   5596  OE1 GLU B 176      37.712 -19.571   1.209  1.00206.18           O  
ANISOU 5596  OE1 GLU B 176    23877  31333  23128  -2077    -78   2389       O  
ATOM   5597  OE2 GLU B 176      38.636 -21.537   1.537  1.00197.34           O  
ANISOU 5597  OE2 GLU B 176    22287  30202  22490  -2017     46   2855       O  
ATOM   5598  N   GLY B 177      38.304 -16.955  -3.243  1.00178.32           N  
ANISOU 5598  N   GLY B 177    21111  26875  19766  -1990    575   1747       N  
ATOM   5599  CA  GLY B 177      38.394 -15.570  -3.731  1.00174.96           C  
ANISOU 5599  CA  GLY B 177    20929  26298  19246  -1991    660   1609       C  
ATOM   5600  C   GLY B 177      37.814 -15.475  -5.108  1.00173.60           C  
ANISOU 5600  C   GLY B 177    20939  26020  18999  -1795    887   1542       C  
ATOM   5601  O   GLY B 177      38.491 -15.800  -6.054  1.00178.05           O  
ANISOU 5601  O   GLY B 177    21435  26450  19762  -1766   1055   1606       O  
ATOM   5602  N   CYS B 178      36.532 -15.111  -5.218  1.00172.78           N  
ANISOU 5602  N   CYS B 178    21045  26012  18592  -1639    888   1413       N  
ATOM   5603  CA  CYS B 178      35.845 -14.874  -6.510  1.00165.82           C  
ANISOU 5603  CA  CYS B 178    20349  25101  17554  -1404   1080   1328       C  
ATOM   5604  C   CYS B 178      35.327 -13.455  -6.698  1.00159.38           C  
ANISOU 5604  C   CYS B 178    19824  24223  16510  -1301   1156   1254       C  
ATOM   5605  O   CYS B 178      34.862 -12.824  -5.766  1.00145.02           O  
ANISOU 5605  O   CYS B 178    18095  22449  14556  -1364   1029   1186       O  
ATOM   5606  CB  CYS B 178      34.652 -15.830  -6.662  1.00162.94           C  
ANISOU 5606  CB  CYS B 178    19936  24922  17050  -1258   1036   1225       C  
ATOM   5607  SG  CYS B 178      34.993 -17.540  -7.156  1.00166.04           S  
ANISOU 5607  SG  CYS B 178    20015  25327  17745  -1263   1090   1252       S  
ATOM   5608  N   THR B 179      35.374 -12.997  -7.949  1.00168.74           N  
ANISOU 5608  N   THR B 179    21147  25318  17648  -1113   1386   1277       N  
ATOM   5609  CA  THR B 179      34.799 -11.715  -8.342  1.00171.25           C  
ANISOU 5609  CA  THR B 179    21736  25572  17758   -944   1522   1255       C  
ATOM   5610  C   THR B 179      33.288 -11.930  -8.398  1.00167.92           C  
ANISOU 5610  C   THR B 179    21414  25390  16995   -740   1436   1119       C  
ATOM   5611  O   THR B 179      32.830 -12.699  -9.235  1.00167.95           O  
ANISOU 5611  O   THR B 179    21366  25551  16895   -560   1473   1062       O  
ATOM   5612  CB  THR B 179      35.327 -11.217  -9.727  1.00168.14           C  
ANISOU 5612  CB  THR B 179    21444  25040  17400   -750   1832   1382       C  
ATOM   5613  OG1 THR B 179      34.857 -12.076 -10.776  1.00165.95           O  
ANISOU 5613  OG1 THR B 179    21134  24969  16949   -513   1891   1339       O  
ATOM   5614  CG2 THR B 179      36.865 -11.150  -9.767  1.00164.34           C  
ANISOU 5614  CG2 THR B 179    20821  24308  17311   -952   1943   1521       C  
ATOM   5615  N   ASN B 180      32.556 -11.271  -7.501  1.00167.78           N  
ANISOU 5615  N   ASN B 180    21515  25403  16829   -775   1322   1042       N  
ATOM   5616  CA  ASN B 180      31.100 -11.281  -7.488  1.00169.34           C  
ANISOU 5616  CA  ASN B 180    21817  25804  16720   -582   1256    919       C  
ATOM   5617  C   ASN B 180      30.476 -10.180  -8.334  1.00172.32           C  
ANISOU 5617  C   ASN B 180    22444  26158  16871   -302   1443    936       C  
ATOM   5618  O   ASN B 180      30.711  -8.983  -8.121  1.00171.07           O  
ANISOU 5618  O   ASN B 180    22443  25800  16754   -325   1555    994       O  
ATOM   5619  CB  ASN B 180      30.563 -11.203  -6.050  1.00164.48           C  
ANISOU 5619  CB  ASN B 180    21192  25260  16043   -738   1048    838       C  
ATOM   5620  CG  ASN B 180      30.665 -12.516  -5.320  1.00158.73           C  
ANISOU 5620  CG  ASN B 180    20211  24663  15434   -890    873    842       C  
ATOM   5621  OD1 ASN B 180      30.357 -13.568  -5.882  1.00151.62           O  
ANISOU 5621  OD1 ASN B 180    19171  23865  14572   -803    883    816       O  
ATOM   5622  ND2 ASN B 180      31.075 -12.463  -4.055  1.00156.76           N  
ANISOU 5622  ND2 ASN B 180    19887  24424  15250  -1102    723    869       N  
ATOM   5623  N   GLU B 181      29.664 -10.624  -9.289  1.00175.47           N  
ANISOU 5623  N   GLU B 181    22852  26772  17046    -27   1480    873       N  
ATOM   5624  CA  GLU B 181      28.862  -9.751 -10.087  1.00187.61           C  
ANISOU 5624  CA  GLU B 181    24595  28386  18300    299   1625    894       C  
ATOM   5625  C   GLU B 181      27.680  -9.187  -9.299  1.00194.22           C  
ANISOU 5625  C   GLU B 181    25551  29291  18952    339   1517    796       C  
ATOM   5626  O   GLU B 181      27.100  -8.171  -9.706  1.00208.12           O  
ANISOU 5626  O   GLU B 181    27506  31041  20525    577   1656    856       O  
ATOM   5627  CB  GLU B 181      28.422 -10.537 -11.317  1.00190.25           C  
ANISOU 5627  CB  GLU B 181    24848  28999  18439    577   1655    810       C  
ATOM   5628  CG  GLU B 181      27.744  -9.781 -12.456  1.00194.34           C  
ANISOU 5628  CG  GLU B 181    25541  29686  18613    998   1825    866       C  
ATOM   5629  CD  GLU B 181      28.665  -9.265 -13.548  1.00194.93           C  
ANISOU 5629  CD  GLU B 181    25703  29666  18693   1178   2114   1096       C  
ATOM   5630  OE1 GLU B 181      29.901  -9.472 -13.472  1.00195.32           O  
ANISOU 5630  OE1 GLU B 181    25675  29487  19048    957   2194   1202       O  
ATOM   5631  OE2 GLU B 181      28.122  -8.644 -14.488  1.00191.40           O  
ANISOU 5631  OE2 GLU B 181    25394  29391  17935   1566   2272   1188       O  
ATOM   5632  N   VAL B 182      27.376  -9.802  -8.145  1.00193.51           N  
ANISOU 5632  N   VAL B 182    25340  29255  18927    116   1297    679       N  
ATOM   5633  CA  VAL B 182      26.349  -9.299  -7.242  1.00190.33           C  
ANISOU 5633  CA  VAL B 182    25037  28906  18374    120   1198    588       C  
ATOM   5634  C   VAL B 182      26.843  -8.098  -6.420  1.00189.71           C  
ANISOU 5634  C   VAL B 182    25107  28576  18397    -39   1253    636       C  
ATOM   5635  O   VAL B 182      26.014  -7.340  -5.901  1.00184.37           O  
ANISOU 5635  O   VAL B 182    24571  27900  17578     24   1248    571       O  
ATOM   5636  CB  VAL B 182      25.767 -10.392  -6.301  1.00186.61           C  
ANISOU 5636  CB  VAL B 182    24378  28602  17921    -20    979    467       C  
ATOM   5637  CG1 VAL B 182      25.112 -11.494  -7.112  1.00181.64           C  
ANISOU 5637  CG1 VAL B 182    23582  28191  17242    143    944    353       C  
ATOM   5638  CG2 VAL B 182      26.837 -10.960  -5.363  1.00189.73           C  
ANISOU 5638  CG2 VAL B 182    24614  28903  18571   -338    875    532       C  
ATOM   5639  N   GLN B 183      28.168  -7.905  -6.317  1.00186.35           N  
ANISOU 5639  N   GLN B 183    24635  27933  18237   -244   1313    723       N  
ATOM   5640  CA  GLN B 183      28.720  -6.713  -5.677  1.00183.85           C  
ANISOU 5640  CA  GLN B 183    24424  27352  18075   -397   1390    717       C  
ATOM   5641  C   GLN B 183      28.480  -5.469  -6.534  1.00189.46           C  
ANISOU 5641  C   GLN B 183    25353  27874  18757   -152   1679    820       C  
ATOM   5642  O   GLN B 183      28.285  -4.386  -6.009  1.00185.31           O  
ANISOU 5642  O   GLN B 183    24956  27168  18283   -182   1758    764       O  
ATOM   5643  CB  GLN B 183      30.211  -6.897  -5.342  1.00180.10           C  
ANISOU 5643  CB  GLN B 183    23792  26708  17930   -687   1365    755       C  
ATOM   5644  CG  GLN B 183      30.749  -5.921  -4.280  1.00182.45           C  
ANISOU 5644  CG  GLN B 183    24108  26807  18407   -927   1335    633       C  
ATOM   5645  CD  GLN B 183      31.020  -6.507  -2.870  1.00183.11           C  
ANISOU 5645  CD  GLN B 183    24016  27068  18488  -1192   1034    496       C  
ATOM   5646  OE1 GLN B 183      30.998  -7.731  -2.643  1.00190.40           O  
ANISOU 5646  OE1 GLN B 183    24777  28220  19346  -1227    865    549       O  
ATOM   5647  NE2 GLN B 183      31.292  -5.614  -1.914  1.00180.86           N  
ANISOU 5647  NE2 GLN B 183    23749  26681  18285  -1365    981    317       N  
ATOM   5648  N   ASN B 184      28.416  -5.653  -7.848  1.00205.62           N  
ANISOU 5648  N   ASN B 184    27432  29990  20705    119   1844    967       N  
ATOM   5649  CA  ASN B 184      27.978  -4.580  -8.750  1.00220.86           C  
ANISOU 5649  CA  ASN B 184    29564  31825  22526    446   2130   1121       C  
ATOM   5650  C   ASN B 184      26.470  -4.309  -8.750  1.00223.61           C  
ANISOU 5650  C   ASN B 184    30033  32387  22539    712   2083   1053       C  
ATOM   5651  O   ASN B 184      26.038  -3.271  -9.213  1.00233.90           O  
ANISOU 5651  O   ASN B 184    31508  33589  23773    965   2310   1182       O  
ATOM   5652  CB  ASN B 184      28.449  -4.846 -10.178  1.00226.65           C  
ANISOU 5652  CB  ASN B 184    30286  32618  23213    693   2332   1320       C  
ATOM   5653  CG  ASN B 184      29.962  -4.878 -10.290  1.00232.57           C  
ANISOU 5653  CG  ASN B 184    30937  33097  24332    469   2457   1432       C  
ATOM   5654  OD1 ASN B 184      30.673  -4.365  -9.404  1.00241.86           O  
ANISOU 5654  OD1 ASN B 184    32081  33986  25828    165   2450   1381       O  
ATOM   5655  ND2 ASN B 184      30.470  -5.501 -11.363  1.00233.26           N  
ANISOU 5655  ND2 ASN B 184    30954  33292  24381    615   2562   1555       N  
ATOM   5656  N   ILE B 185      25.670  -5.209  -8.187  1.00218.19           N  
ANISOU 5656  N   ILE B 185    29244  31975  21680    656   1809    866       N  
ATOM   5657  CA  ILE B 185      24.229  -4.984  -8.065  1.00215.42           C  
ANISOU 5657  CA  ILE B 185    28979  31821  21050    877   1748    778       C  
ATOM   5658  C   ILE B 185      23.882  -4.377  -6.708  1.00210.19           C  
ANISOU 5658  C   ILE B 185    28386  31026  20450    676   1667    651       C  
ATOM   5659  O   ILE B 185      24.273  -4.895  -5.663  1.00216.28           O  
ANISOU 5659  O   ILE B 185    29044  31794  21339    371   1481    531       O  
ATOM   5660  CB  ILE B 185      23.445  -6.291  -8.279  1.00219.70           C  
ANISOU 5660  CB  ILE B 185    29346  32729  21400    956   1530    630       C  
ATOM   5661  CG1 ILE B 185      23.647  -6.774  -9.706  1.00221.37           C  
ANISOU 5661  CG1 ILE B 185    29496  33118  21497   1210   1619    699       C  
ATOM   5662  CG2 ILE B 185      21.950  -6.108  -8.057  1.00222.91           C  
ANISOU 5662  CG2 ILE B 185    29799  33336  21557   1156   1451    516       C  
ATOM   5663  CD1 ILE B 185      23.574  -8.271  -9.789  1.00228.10           C  
ANISOU 5663  CD1 ILE B 185    30097  34197  22370   1117   1418    521       C  
ATOM   5664  N   LYS B 186      23.118  -3.297  -6.761  1.00201.32           N  
ANISOU 5664  N   LYS B 186    27441  29821  19227    883   1817    684       N  
ATOM   5665  CA  LYS B 186      22.645  -2.591  -5.595  1.00200.23           C  
ANISOU 5665  CA  LYS B 186    27392  29567  19120    754   1781    544       C  
ATOM   5666  C   LYS B 186      21.329  -3.223  -5.113  1.00198.08           C  
ANISOU 5666  C   LYS B 186    27068  29607  18584    836   1574    400       C  
ATOM   5667  O   LYS B 186      20.364  -3.276  -5.871  1.00195.98           O  
ANISOU 5667  O   LYS B 186    26826  29538  18099   1151   1605    442       O  
ATOM   5668  CB  LYS B 186      22.428  -1.151  -6.015  1.00199.60           C  
ANISOU 5668  CB  LYS B 186    27513  29225  19101    972   2088    672       C  
ATOM   5669  CG  LYS B 186      22.195  -0.151  -4.914  1.00204.57           C  
ANISOU 5669  CG  LYS B 186    28246  29620  19858    828   2137    518       C  
ATOM   5670  CD  LYS B 186      22.032   1.226  -5.560  1.00207.10           C  
ANISOU 5670  CD  LYS B 186    28745  29639  20303   1087   2507    699       C  
ATOM   5671  CE  LYS B 186      20.732   1.914  -5.156  1.00207.49           C  
ANISOU 5671  CE  LYS B 186    28919  29716  20199   1278   2554    631       C  
ATOM   5672  NZ  LYS B 186      20.197   2.735  -6.272  1.00211.79           N  
ANISOU 5672  NZ  LYS B 186    29595  30189  20685   1713   2869    921       N  
ATOM   5673  N   PHE B 187      21.307  -3.745  -3.883  1.00193.19           N  
ANISOU 5673  N   PHE B 187    26356  29058  17987    570   1367    239       N  
ATOM   5674  CA  PHE B 187      20.079  -4.280  -3.275  1.00189.00           C  
ANISOU 5674  CA  PHE B 187    25771  28780  17259    629   1210    118       C  
ATOM   5675  C   PHE B 187      19.522  -3.251  -2.306  1.00187.80           C  
ANISOU 5675  C   PHE B 187    25771  28516  17065    605   1259     10       C  
ATOM   5676  O   PHE B 187      19.910  -3.157  -1.141  1.00180.68           O  
ANISOU 5676  O   PHE B 187    24856  27569  16224    355   1169   -110       O  
ATOM   5677  CB  PHE B 187      20.302  -5.651  -2.631  1.00189.55           C  
ANISOU 5677  CB  PHE B 187    25617  29035  17365    413    989     60       C  
ATOM   5678  CG  PHE B 187      20.529  -6.722  -3.636  1.00187.16           C  
ANISOU 5678  CG  PHE B 187    25148  28863  17100    484    953    118       C  
ATOM   5679  CD1 PHE B 187      19.453  -7.315  -4.289  1.00188.61           C  
ANISOU 5679  CD1 PHE B 187    25241  29277  17145    717    916     58       C  
ATOM   5680  CD2 PHE B 187      21.822  -7.093  -3.980  1.00191.69           C  
ANISOU 5680  CD2 PHE B 187    25642  29327  17862    328    966    204       C  
ATOM   5681  CE1 PHE B 187      19.662  -8.287  -5.255  1.00198.55           C  
ANISOU 5681  CE1 PHE B 187    26327  30665  18446    787    886     49       C  
ATOM   5682  CE2 PHE B 187      22.044  -8.059  -4.945  1.00198.22           C  
ANISOU 5682  CE2 PHE B 187    26315  30269  18729    403    952    232       C  
ATOM   5683  CZ  PHE B 187      20.964  -8.663  -5.580  1.00201.51           C  
ANISOU 5683  CZ  PHE B 187    26639  30924  19000    630    910    137       C  
ATOM   5684  N   ASN B 188      18.594  -2.481  -2.853  1.00190.44           N  
ANISOU 5684  N   ASN B 188    26241  28834  17282    898   1409     53       N  
ATOM   5685  CA  ASN B 188      17.950  -1.340  -2.200  1.00193.45           C  
ANISOU 5685  CA  ASN B 188    26789  29069  17642    953   1525    -29       C  
ATOM   5686  C   ASN B 188      17.101  -1.769  -1.000  1.00193.23           C  
ANISOU 5686  C   ASN B 188    26709  29239  17471    861   1353   -201       C  
ATOM   5687  O   ASN B 188      16.915  -0.997  -0.062  1.00202.17           O  
ANISOU 5687  O   ASN B 188    27944  30256  18613    777   1397   -337       O  
ATOM   5688  CB  ASN B 188      17.040  -0.633  -3.227  1.00194.62           C  
ANISOU 5688  CB  ASN B 188    27054  29220  17672   1353   1719    111       C  
ATOM   5689  CG  ASN B 188      17.168   0.880  -3.206  1.00194.26           C  
ANISOU 5689  CG  ASN B 188    27206  28815  17789   1429   2004    164       C  
ATOM   5690  OD1 ASN B 188      18.269   1.436  -3.123  1.00196.22           O  
ANISOU 5690  OD1 ASN B 188    27494  28756  18303   1247   2133    178       O  
ATOM   5691  ND2 ASN B 188      16.033   1.554  -3.325  1.00191.01           N  
ANISOU 5691  ND2 ASN B 188    26895  28422  17257   1710   2125    197       N  
ATOM   5692  N   SER B 189      16.595  -3.000  -1.020  1.00195.84           N  
ANISOU 5692  N   SER B 189    26864  29855  17689    880   1180   -205       N  
ATOM   5693  CA  SER B 189      15.710  -3.473   0.037  1.00199.12           C  
ANISOU 5693  CA  SER B 189    27210  30460  17985    834   1060   -319       C  
ATOM   5694  C   SER B 189      16.472  -3.711   1.341  1.00200.48           C  
ANISOU 5694  C   SER B 189    27339  30636  18198    524    945   -402       C  
ATOM   5695  O   SER B 189      17.387  -4.544   1.421  1.00213.17           O  
ANISOU 5695  O   SER B 189    28802  32290  19900    341    833   -348       O  
ATOM   5696  CB  SER B 189      14.998  -4.765  -0.356  1.00198.64           C  
ANISOU 5696  CB  SER B 189    26933  30665  17874    930    940   -301       C  
ATOM   5697  OG  SER B 189      14.188  -4.580  -1.498  1.00201.15           O  
ANISOU 5697  OG  SER B 189    27259  31063  18105   1241   1007   -273       O  
ATOM   5698  N   SER B 190      16.069  -2.959   2.355  1.00197.08           N  
ANISOU 5698  N   SER B 190    27024  30177  17681    491    977   -538       N  
ATOM   5699  CA  SER B 190      16.473  -3.175   3.728  1.00199.52           C  
ANISOU 5699  CA  SER B 190    27283  30599  17925    267    854   -648       C  
ATOM   5700  C   SER B 190      15.289  -3.898   4.396  1.00201.74           C  
ANISOU 5700  C   SER B 190    27476  31145  18030    366    798   -636       C  
ATOM   5701  O   SER B 190      14.187  -3.911   3.851  1.00206.90           O  
ANISOU 5701  O   SER B 190    28138  31830  18643    585    870   -605       O  
ATOM   5702  CB  SER B 190      16.788  -1.821   4.358  1.00203.15           C  
ANISOU 5702  CB  SER B 190    27917  30862  18409    184    945   -851       C  
ATOM   5703  OG  SER B 190      15.623  -1.026   4.521  1.00212.68           O  
ANISOU 5703  OG  SER B 190    29267  32025  19516    374   1081   -936       O  
ATOM   5704  N   GLY B 191      15.485  -4.524   5.550  1.00192.12           N  
ANISOU 5704  N   GLY B 191    23876  29158  19963   1327   1845   2592       N  
ATOM   5705  CA  GLY B 191      14.375  -5.260   6.171  1.00187.02           C  
ANISOU 5705  CA  GLY B 191    23359  28464  19236   1111   1631   2195       C  
ATOM   5706  C   GLY B 191      13.436  -4.374   6.968  1.00185.02           C  
ANISOU 5706  C   GLY B 191    23093  28023  19182   1008   1677   2298       C  
ATOM   5707  O   GLY B 191      13.791  -3.264   7.368  1.00181.99           O  
ANISOU 5707  O   GLY B 191    22734  27327  19084   1020   1853   2576       O  
ATOM   5708  N   GLN B 192      12.232  -4.887   7.199  1.00185.99           N  
ANISOU 5708  N   GLN B 192    23195  28343  19126    899   1518   2074       N  
ATOM   5709  CA  GLN B 192      11.201  -4.180   7.964  1.00186.90           C  
ANISOU 5709  CA  GLN B 192    23273  28408  19330    888   1563   2177       C  
ATOM   5710  C   GLN B 192      10.488  -5.163   8.897  1.00185.62           C  
ANISOU 5710  C   GLN B 192    23162  28214  19147    548   1341   1845       C  
ATOM   5711  O   GLN B 192      10.041  -6.196   8.431  1.00191.57           O  
ANISOU 5711  O   GLN B 192    23870  29272  19643    386   1151   1607       O  
ATOM   5712  CB  GLN B 192      10.224  -3.559   6.952  1.00188.09           C  
ANISOU 5712  CB  GLN B 192    23169  29144  19152   1242   1663   2451       C  
ATOM   5713  CG  GLN B 192      10.599  -2.179   6.451  1.00190.50           C  
ANISOU 5713  CG  GLN B 192    23465  29347  19569   1624   1978   2922       C  
ATOM   5714  CD  GLN B 192      10.518  -1.984   4.914  1.00192.91           C  
ANISOU 5714  CD  GLN B 192    23520  30266  19511   2016   2082   3190       C  
ATOM   5715  OE1 GLN B 192       9.651  -2.545   4.248  1.00186.99           O  
ANISOU 5715  OE1 GLN B 192    22536  30178  18331   2095   1934   3076       O  
ATOM   5716  NE2 GLN B 192      11.425  -1.172   4.358  1.00193.27           N  
ANISOU 5716  NE2 GLN B 192    23590  30132  19710   2237   2332   3566       N  
ATOM   5717  N   CYS B 193      10.331  -4.843  10.189  1.00176.97           N  
ANISOU 5717  N   CYS B 193    22172  26770  18297    430   1364   1832       N  
ATOM   5718  CA  CYS B 193       9.893  -5.852  11.177  1.00166.14           C  
ANISOU 5718  CA  CYS B 193    20856  25318  16950     99   1180   1566       C  
ATOM   5719  C   CYS B 193       8.397  -6.008  11.080  1.00163.92           C  
ANISOU 5719  C   CYS B 193    20324  25564  16393     65   1095   1613       C  
ATOM   5720  O   CYS B 193       7.685  -5.013  11.030  1.00159.39           O  
ANISOU 5720  O   CYS B 193    19595  25244  15722    367   1236   1884       O  
ATOM   5721  CB  CYS B 193      10.241  -5.463  12.613  1.00163.27           C  
ANISOU 5721  CB  CYS B 193    20653  24501  16879     32   1233   1548       C  
ATOM   5722  SG  CYS B 193      12.001  -5.484  12.974  1.00160.72           S  
ANISOU 5722  SG  CYS B 193    20535  23687  16843    -57   1268   1471       S  
ATOM   5723  N   GLU B 194       7.938  -7.262  11.011  1.00164.70           N  
ANISOU 5723  N   GLU B 194    20392  25843  16343   -299    876   1371       N  
ATOM   5724  CA  GLU B 194       6.529  -7.597  10.871  1.00170.41           C  
ANISOU 5724  CA  GLU B 194    20806  27167  16773   -480    739   1406       C  
ATOM   5725  C   GLU B 194       5.893  -7.709  12.250  1.00167.61           C  
ANISOU 5725  C   GLU B 194    20394  26748  16542   -642    731   1474       C  
ATOM   5726  O   GLU B 194       6.554  -8.106  13.200  1.00164.04           O  
ANISOU 5726  O   GLU B 194    20195  25769  16362   -778    736   1348       O  
ATOM   5727  CB  GLU B 194       6.403  -8.931  10.101  1.00177.34           C  
ANISOU 5727  CB  GLU B 194    21742  28198  17439   -901    485   1077       C  
ATOM   5728  CG  GLU B 194       5.005  -9.326   9.629  1.00182.88           C  
ANISOU 5728  CG  GLU B 194    22070  29653  17764  -1202    284   1080       C  
ATOM   5729  CD  GLU B 194       4.460  -8.558   8.460  1.00187.86           C  
ANISOU 5729  CD  GLU B 194    22336  31032  18007   -857    319   1281       C  
ATOM   5730  OE1 GLU B 194       5.241  -8.297   7.531  1.00200.22           O  
ANISOU 5730  OE1 GLU B 194    24033  32530  19511   -555    394   1239       O  
ATOM   5731  OE2 GLU B 194       3.244  -8.266   8.450  1.00190.03           O  
ANISOU 5731  OE2 GLU B 194    22161  32041  18001   -869    278   1511       O  
ATOM   5732  N   VAL B 195       4.614  -7.351  12.335  1.00170.26           N  
ANISOU 5732  N   VAL B 195    20355  27710  16627   -572    732   1713       N  
ATOM   5733  CA  VAL B 195       3.861  -7.403  13.575  1.00166.76           C  
ANISOU 5733  CA  VAL B 195    19769  27378  16211   -647    745   1855       C  
ATOM   5734  C   VAL B 195       3.957  -8.815  14.183  1.00169.22           C  
ANISOU 5734  C   VAL B 195    20211  27414  16670  -1247    552   1618       C  
ATOM   5735  O   VAL B 195       3.752  -9.804  13.480  1.00171.41           O  
ANISOU 5735  O   VAL B 195    20475  27826  16825  -1700    347   1423       O  
ATOM   5736  CB  VAL B 195       2.399  -6.954  13.350  1.00170.21           C  
ANISOU 5736  CB  VAL B 195    19687  28735  16249   -479    761   2195       C  
ATOM   5737  CG1 VAL B 195       1.523  -7.104  14.600  1.00176.09           C  
ANISOU 5737  CG1 VAL B 195    20141  29850  16913   -810    662   2324       C  
ATOM   5738  CG2 VAL B 195       2.406  -5.523  12.860  1.00165.35           C  
ANISOU 5738  CG2 VAL B 195    19096  28147  15581    259   1061   2501       C  
ATOM   5739  N   PRO B 196       4.232  -8.917  15.484  1.00165.49           N  
ANISOU 5739  N   PRO B 196    19890  26557  16430  -1244    623   1638       N  
ATOM   5740  CA  PRO B 196       4.215  -7.807  16.463  1.00162.28           C  
ANISOU 5740  CA  PRO B 196    19491  26080  16085   -757    827   1836       C  
ATOM   5741  C   PRO B 196       5.571  -7.192  16.772  1.00157.73           C  
ANISOU 5741  C   PRO B 196    19316  24821  15790   -500    949   1684       C  
ATOM   5742  O   PRO B 196       5.719  -6.507  17.778  1.00156.02           O  
ANISOU 5742  O   PRO B 196    19214  24407  15657   -228   1068   1733       O  
ATOM   5743  CB  PRO B 196       3.693  -8.497  17.702  1.00165.37           C  
ANISOU 5743  CB  PRO B 196    19777  26546  16509   -990    787   1919       C  
ATOM   5744  CG  PRO B 196       4.289  -9.857  17.602  1.00166.49           C  
ANISOU 5744  CG  PRO B 196    20148  26279  16829  -1518    633   1669       C  
ATOM   5745  CD  PRO B 196       4.365 -10.221  16.145  1.00166.50           C  
ANISOU 5745  CD  PRO B 196    20175  26374  16714  -1738    500   1491       C  
ATOM   5746  N   LEU B 197       6.562  -7.429  15.913  1.00151.75           N  
ANISOU 5746  N   LEU B 197    18759  23754  15144   -592    911   1501       N  
ATOM   5747  CA  LEU B 197       7.896  -6.912  16.129  1.00143.09           C  
ANISOU 5747  CA  LEU B 197    17956  22116  14294   -436   1005   1399       C  
ATOM   5748  C   LEU B 197       7.998  -5.505  15.617  1.00141.46           C  
ANISOU 5748  C   LEU B 197    17774  21895  14078    -49   1176   1565       C  
ATOM   5749  O   LEU B 197       7.253  -5.101  14.716  1.00157.96           O  
ANISOU 5749  O   LEU B 197    19669  24396  15951    132   1223   1742       O  
ATOM   5750  CB  LEU B 197       8.940  -7.810  15.483  1.00140.21           C  
ANISOU 5750  CB  LEU B 197    17766  21493  14013   -645    921   1197       C  
ATOM   5751  CG  LEU B 197       8.906  -9.307  15.876  1.00145.01           C  
ANISOU 5751  CG  LEU B 197    18476  21988  14633  -1008    787   1032       C  
ATOM   5752  CD1 LEU B 197      10.029 -10.101  15.225  1.00150.96           C  
ANISOU 5752  CD1 LEU B 197    19490  22444  15423  -1058    758    844       C  
ATOM   5753  CD2 LEU B 197       8.992  -9.489  17.398  1.00145.89           C  
ANISOU 5753  CD2 LEU B 197    18638  21903  14888  -1037    818   1059       C  
ATOM   5754  N   VAL B 198       8.869  -4.752  16.251  1.00138.36           N  
ANISOU 5754  N   VAL B 198    17621  21048  13901     64   1271   1523       N  
ATOM   5755  CA  VAL B 198       9.060  -3.359  15.927  1.00147.72           C  
ANISOU 5755  CA  VAL B 198    18944  22041  15141    378   1457   1679       C  
ATOM   5756  C   VAL B 198      10.551  -3.210  15.615  1.00154.38           C  
ANISOU 5756  C   VAL B 198    19951  22476  16228    215   1461   1597       C  
ATOM   5757  O   VAL B 198      11.374  -3.915  16.202  1.00160.53           O  
ANISOU 5757  O   VAL B 198    20779  23086  17128    -36   1348   1409       O  
ATOM   5758  CB  VAL B 198       8.524  -2.425  17.061  1.00150.06           C  
ANISOU 5758  CB  VAL B 198    19412  22183  15420    657   1573   1717       C  
ATOM   5759  CG1 VAL B 198       9.263  -2.643  18.373  1.00156.98           C  
ANISOU 5759  CG1 VAL B 198    20477  22704  16464    460   1482   1464       C  
ATOM   5760  CG2 VAL B 198       8.630  -0.961  16.671  1.00153.42           C  
ANISOU 5760  CG2 VAL B 198    20091  22302  15896   1002   1801   1889       C  
ATOM   5761  N   ARG B 199      10.877  -2.268  14.736  1.00157.05           N  
ANISOU 5761  N   ARG B 199    20345  22707  16617    386   1615   1794       N  
ATOM   5762  CA  ARG B 199      12.237  -2.053  14.274  1.00156.63           C  
ANISOU 5762  CA  ARG B 199    20358  22389  16766    229   1642   1821       C  
ATOM   5763  C   ARG B 199      13.085  -1.390  15.356  1.00151.82           C  
ANISOU 5763  C   ARG B 199    19988  21288  16406     35   1641   1700       C  
ATOM   5764  O   ARG B 199      12.699  -0.365  15.890  1.00150.14           O  
ANISOU 5764  O   ARG B 199    20019  20777  16247    169   1748   1722       O  
ATOM   5765  CB  ARG B 199      12.213  -1.168  13.022  1.00164.24           C  
ANISOU 5765  CB  ARG B 199    21290  23414  17699    481   1839   2147       C  
ATOM   5766  CG  ARG B 199      13.535  -1.053  12.272  1.00165.77           C  
ANISOU 5766  CG  ARG B 199    21437  23507  18039    345   1885   2280       C  
ATOM   5767  CD  ARG B 199      13.958  -2.312  11.528  1.00161.70           C  
ANISOU 5767  CD  ARG B 199    20704  23383  17351    294   1755   2190       C  
ATOM   5768  NE  ARG B 199      15.173  -2.035  10.775  1.00163.00           N  
ANISOU 5768  NE  ARG B 199    20783  23543  17606    272   1849   2411       N  
ATOM   5769  CZ  ARG B 199      16.412  -1.977  11.272  1.00164.67           C  
ANISOU 5769  CZ  ARG B 199    20997  23550  18020      6   1823   2408       C  
ATOM   5770  NH1 ARG B 199      16.682  -2.188  12.553  1.00163.66           N  
ANISOU 5770  NH1 ARG B 199    20974  23184  18023   -255   1694   2158       N  
ATOM   5771  NH2 ARG B 199      17.418  -1.706  10.457  1.00176.05           N  
ANISOU 5771  NH2 ARG B 199    22278  25117  19495     13   1928   2697       N  
ATOM   5772  N   THR B 200      14.236  -1.981  15.673  1.00149.85           N  
ANISOU 5772  N   THR B 200    19682  20985  16266   -256   1520   1568       N  
ATOM   5773  CA  THR B 200      15.145  -1.400  16.686  1.00158.08           C  
ANISOU 5773  CA  THR B 200    20881  21679  17500   -520   1472   1432       C  
ATOM   5774  C   THR B 200      16.559  -1.791  16.353  1.00157.43           C  
ANISOU 5774  C   THR B 200    20611  21703  17501   -773   1414   1490       C  
ATOM   5775  O   THR B 200      16.787  -2.890  15.843  1.00145.89           O  
ANISOU 5775  O   THR B 200    18957  20563  15908   -702   1370   1509       O  
ATOM   5776  CB  THR B 200      14.802  -1.884  18.126  1.00168.58           C  
ANISOU 5776  CB  THR B 200    22279  23015  18759   -558   1337   1151       C  
ATOM   5777  OG1 THR B 200      15.748  -1.378  19.092  1.00174.80           O  
ANISOU 5777  OG1 THR B 200    23185  23561  19668   -834   1251    976       O  
ATOM   5778  CG2 THR B 200      14.767  -3.434  18.218  1.00170.67           C  
ANISOU 5778  CG2 THR B 200    22330  23627  18887   -572   1223   1079       C  
ATOM   5779  N   ASP B 201      17.504  -0.896  16.627  1.00170.07           N  
ANISOU 5779  N   ASP B 201    22277  23047  19292  -1068   1419   1526       N  
ATOM   5780  CA  ASP B 201      18.918  -1.182  16.368  1.00181.47           C  
ANISOU 5780  CA  ASP B 201    23453  24713  20784  -1328   1367   1648       C  
ATOM   5781  C   ASP B 201      19.695  -1.609  17.629  1.00183.18           C  
ANISOU 5781  C   ASP B 201    23579  25050  20970  -1592   1179   1412       C  
ATOM   5782  O   ASP B 201      20.848  -2.033  17.515  1.00190.10           O  
ANISOU 5782  O   ASP B 201    24160  26261  21805  -1740   1130   1533       O  
ATOM   5783  CB  ASP B 201      19.584  -0.002  15.618  1.00188.39           C  
ANISOU 5783  CB  ASP B 201    24332  25378  21869  -1551   1498   1954       C  
ATOM   5784  CG  ASP B 201      19.208   0.041  14.099  1.00190.05           C  
ANISOU 5784  CG  ASP B 201    24443  25749  22017  -1209   1697   2305       C  
ATOM   5785  OD1 ASP B 201      19.075  -1.014  13.414  1.00190.17           O  
ANISOU 5785  OD1 ASP B 201    24256  26190  21807   -918   1689   2338       O  
ATOM   5786  OD2 ASP B 201      19.033   1.141  13.569  1.00191.75           O  
ANISOU 5786  OD2 ASP B 201    24815  25655  22383  -1209   1870   2549       O  
ATOM   5787  N   ASN B 202      19.061  -1.543  18.806  1.00182.77           N  
ANISOU 5787  N   ASN B 202    23739  24825  20880  -1583   1088   1114       N  
ATOM   5788  CA  ASN B 202      19.682  -1.986  20.074  1.00176.85           C  
ANISOU 5788  CA  ASN B 202    22889  24270  20036  -1760    912    886       C  
ATOM   5789  C   ASN B 202      19.657  -3.546  20.166  1.00167.83           C  
ANISOU 5789  C   ASN B 202    21541  23533  18693  -1482    893    906       C  
ATOM   5790  O   ASN B 202      18.581  -4.117  20.100  1.00155.62           O  
ANISOU 5790  O   ASN B 202    20109  21945  17075  -1215    940    868       O  
ATOM   5791  CB  ASN B 202      18.959  -1.325  21.261  1.00172.34           C  
ANISOU 5791  CB  ASN B 202    22644  23388  19446  -1769    845    573       C  
ATOM   5792  CG  ASN B 202      19.495  -1.766  22.606  1.00171.81           C  
ANISOU 5792  CG  ASN B 202    22465  23591  19221  -1892    661    328       C  
ATOM   5793  OD1 ASN B 202      18.767  -2.363  23.393  1.00174.89           O  
ANISOU 5793  OD1 ASN B 202    22902  24094  19453  -1623    641    198       O  
ATOM   5794  ND2 ASN B 202      20.773  -1.508  22.863  1.00170.49           N  
ANISOU 5794  ND2 ASN B 202    22094  23615  19068  -2296    530    310       N  
ATOM   5795  N   PRO B 203      20.841  -4.217  20.343  1.00162.58           N  
ANISOU 5795  N   PRO B 203    20586  23264  17922  -1550    836    990       N  
ATOM   5796  CA  PRO B 203      20.893  -5.697  20.378  1.00156.05           C  
ANISOU 5796  CA  PRO B 203    19663  22725  16901  -1227    870   1043       C  
ATOM   5797  C   PRO B 203      20.331  -6.363  21.617  1.00159.61           C  
ANISOU 5797  C   PRO B 203    20206  23200  17237  -1097    813    860       C  
ATOM   5798  O   PRO B 203      20.069  -7.560  21.609  1.00149.50           O  
ANISOU 5798  O   PRO B 203    18965  21994  15843   -836    876    911       O  
ATOM   5799  CB  PRO B 203      22.387  -6.021  20.262  1.00154.77           C  
ANISOU 5799  CB  PRO B 203    19158  23026  16620  -1268    861   1243       C  
ATOM   5800  CG  PRO B 203      23.021  -4.772  19.789  1.00161.24           C  
ANISOU 5800  CG  PRO B 203    19845  23813  17604  -1653    835   1359       C  
ATOM   5801  CD  PRO B 203      22.205  -3.657  20.363  1.00163.87           C  
ANISOU 5801  CD  PRO B 203    20483  23659  18120  -1907    766   1106       C  
ATOM   5802  N   LYS B 204      20.137  -5.572  22.663  1.00168.71           N  
ANISOU 5802  N   LYS B 204    21429  24261  18409  -1273    706    653       N  
ATOM   5803  CA  LYS B 204      19.531  -6.041  23.891  1.00171.87           C  
ANISOU 5803  CA  LYS B 204    21899  24728  18675  -1118    663    503       C  
ATOM   5804  C   LYS B 204      18.004  -6.198  23.752  1.00161.80           C  
ANISOU 5804  C   LYS B 204    20844  23197  17434   -923    744    486       C  
ATOM   5805  O   LYS B 204      17.378  -6.851  24.580  1.00160.22           O  
ANISOU 5805  O   LYS B 204    20662  23094  17120   -755    751    465       O  
ATOM   5806  CB  LYS B 204      19.868  -5.075  25.046  1.00187.06           C  
ANISOU 5806  CB  LYS B 204    23843  26689  20541  -1344    507    247       C  
ATOM   5807  CG  LYS B 204      21.362  -4.745  25.204  1.00196.29           C  
ANISOU 5807  CG  LYS B 204    24729  28191  21658  -1672    379    254       C  
ATOM   5808  CD  LYS B 204      21.742  -4.181  26.579  1.00201.02           C  
ANISOU 5808  CD  LYS B 204    25305  28988  22086  -1883    177    -48       C  
ATOM   5809  CE  LYS B 204      21.629  -2.661  26.677  1.00203.03           C  
ANISOU 5809  CE  LYS B 204    25872  28784  22485  -2283     68   -335       C  
ATOM   5810  NZ  LYS B 204      20.265  -2.126  26.934  1.00203.15           N  
ANISOU 5810  NZ  LYS B 204    26346  28301  22540  -2034    144   -527       N  
ATOM   5811  N   SER B 205      17.414  -5.586  22.726  1.00154.17           N  
ANISOU 5811  N   SER B 205    19997  21982  16598   -942    812    541       N  
ATOM   5812  CA  SER B 205      15.971  -5.634  22.507  1.00151.92           C  
ANISOU 5812  CA  SER B 205    19836  21590  16297   -768    881    569       C  
ATOM   5813  C   SER B 205      15.553  -6.715  21.525  1.00145.29           C  
ANISOU 5813  C   SER B 205    18943  20825  15432   -695    937    714       C  
ATOM   5814  O   SER B 205      14.349  -6.950  21.340  1.00149.23           O  
ANISOU 5814  O   SER B 205    19468  21349  15882   -620    966    757       O  
ATOM   5815  CB  SER B 205      15.486  -4.287  21.969  1.00155.47           C  
ANISOU 5815  CB  SER B 205    20451  21778  16842   -764    941    569       C  
ATOM   5816  OG  SER B 205      15.794  -3.239  22.869  1.00166.79           O  
ANISOU 5816  OG  SER B 205    22058  23022  18292   -855    887    375       O  
ATOM   5817  N   TRP B 206      16.516  -7.382  20.895  1.00141.92           N  
ANISOU 5817  N   TRP B 206    18446  20473  15001   -713    950    786       N  
ATOM   5818  CA  TRP B 206      16.192  -8.288  19.775  1.00142.06           C  
ANISOU 5818  CA  TRP B 206    18510  20498  14969   -641    996    860       C  
ATOM   5819  C   TRP B 206      15.552  -9.577  20.214  1.00133.00           C  
ANISOU 5819  C   TRP B 206    17456  19337  13739   -614    993    841       C  
ATOM   5820  O   TRP B 206      15.938 -10.103  21.228  1.00131.72           O  
ANISOU 5820  O   TRP B 206    17291  19213  13543   -566    997    845       O  
ATOM   5821  CB  TRP B 206      17.441  -8.584  18.941  1.00147.68           C  
ANISOU 5821  CB  TRP B 206    19161  21304  15645   -574   1038    952       C  
ATOM   5822  CG  TRP B 206      18.002  -7.325  18.245  1.00147.14           C  
ANISOU 5822  CG  TRP B 206    18974  21252  15678   -659   1063   1054       C  
ATOM   5823  CD1 TRP B 206      17.372  -6.119  18.063  1.00143.40           C  
ANISOU 5823  CD1 TRP B 206    18542  20621  15320   -741   1080   1064       C  
ATOM   5824  CD2 TRP B 206      19.291  -7.196  17.642  1.00140.45           C  
ANISOU 5824  CD2 TRP B 206    17959  20592  14812   -647   1105   1218       C  
ATOM   5825  NE1 TRP B 206      18.201  -5.246  17.388  1.00136.79           N  
ANISOU 5825  NE1 TRP B 206    17608  19783  14579   -831   1133   1222       N  
ATOM   5826  CE2 TRP B 206      19.380  -5.887  17.115  1.00137.76           C  
ANISOU 5826  CE2 TRP B 206    17560  20162  14621   -801   1138   1330       C  
ATOM   5827  CE3 TRP B 206      20.388  -8.070  17.505  1.00136.95           C  
ANISOU 5827  CE3 TRP B 206    17404  20415  14215   -478   1144   1327       C  
ATOM   5828  CZ2 TRP B 206      20.514  -5.433  16.481  1.00138.77           C  
ANISOU 5828  CZ2 TRP B 206    17476  20472  14776   -876   1189   1560       C  
ATOM   5829  CZ3 TRP B 206      21.516  -7.616  16.891  1.00134.15           C  
ANISOU 5829  CZ3 TRP B 206    16805  20325  13842   -491   1192   1553       C  
ATOM   5830  CH2 TRP B 206      21.572  -6.314  16.362  1.00138.20           C  
ANISOU 5830  CH2 TRP B 206    17217  20760  14530   -726   1207   1678       C  
ATOM   5831  N   TYR B 207      14.594 -10.072  19.426  1.00125.35           N  
ANISOU 5831  N   TYR B 207    16563  18336  12727   -670    986    836       N  
ATOM   5832  CA  TYR B 207      13.839 -11.270  19.761  1.00125.49           C  
ANISOU 5832  CA  TYR B 207    16694  18287  12696   -770    973    831       C  
ATOM   5833  C   TYR B 207      14.440 -12.535  19.157  1.00123.23           C  
ANISOU 5833  C   TYR B 207    16658  17820  12343   -727   1010    790       C  
ATOM   5834  O   TYR B 207      14.364 -12.750  17.974  1.00123.07           O  
ANISOU 5834  O   TYR B 207    16742  17772  12246   -743    988    713       O  
ATOM   5835  CB  TYR B 207      12.392 -11.129  19.295  1.00129.51           C  
ANISOU 5835  CB  TYR B 207    17125  18923  13159   -939    915    843       C  
ATOM   5836  CG  TYR B 207      11.669 -12.468  19.289  1.00139.21           C  
ANISOU 5836  CG  TYR B 207    18488  20062  14343  -1183    875    834       C  
ATOM   5837  CD1 TYR B 207      11.140 -13.023  20.457  1.00144.14           C  
ANISOU 5837  CD1 TYR B 207    19086  20679  15000  -1288    895    949       C  
ATOM   5838  CD2 TYR B 207      11.573 -13.214  18.121  1.00142.15           C  
ANISOU 5838  CD2 TYR B 207    19048  20332  14630  -1326    820    708       C  
ATOM   5839  CE1 TYR B 207      10.527 -14.263  20.438  1.00147.32           C  
ANISOU 5839  CE1 TYR B 207    19647  20926  15399  -1591    871    975       C  
ATOM   5840  CE2 TYR B 207      10.953 -14.455  18.093  1.00145.10           C  
ANISOU 5840  CE2 TYR B 207    19630  20523  14975  -1642    768    656       C  
ATOM   5841  CZ  TYR B 207      10.447 -14.982  19.251  1.00147.62           C  
ANISOU 5841  CZ  TYR B 207    19928  20782  15379  -1803    800    808       C  
ATOM   5842  OH  TYR B 207       9.805 -16.197  19.220  1.00154.99           O  
ANISOU 5842  OH  TYR B 207    21087  21483  16319  -2200    757    795       O  
ATOM   5843  N   GLU B 208      15.041 -13.373  19.987  1.00130.34           N  
ANISOU 5843  N   GLU B 208    17683  18607  13232   -613   1083    846       N  
ATOM   5844  CA  GLU B 208      15.630 -14.633  19.568  1.00138.38           C  
ANISOU 5844  CA  GLU B 208    19035  19383  14160   -469   1170    832       C  
ATOM   5845  C   GLU B 208      16.606 -14.473  18.363  1.00144.05           C  
ANISOU 5845  C   GLU B 208    19799  20172  14760   -232   1204    788       C  
ATOM   5846  O   GLU B 208      17.377 -13.519  18.302  1.00149.97           O  
ANISOU 5846  O   GLU B 208    20271  21190  15520   -121   1207    867       O  
ATOM   5847  CB  GLU B 208      14.503 -15.622  19.275  1.00145.03           C  
ANISOU 5847  CB  GLU B 208    20160  19938  15008   -763   1129    750       C  
ATOM   5848  CG  GLU B 208      13.797 -16.222  20.461  1.00151.51           C  
ANISOU 5848  CG  GLU B 208    21003  20649  15914   -939   1162    888       C  
ATOM   5849  CD  GLU B 208      13.164 -17.566  20.116  1.00166.54           C  
ANISOU 5849  CD  GLU B 208    23333  22122  17821  -1225   1170    832       C  
ATOM   5850  OE1 GLU B 208      13.787 -18.385  19.371  1.00172.77           O  
ANISOU 5850  OE1 GLU B 208    24565  22561  18517  -1077   1235    700       O  
ATOM   5851  OE2 GLU B 208      12.048 -17.816  20.613  1.00179.57           O  
ANISOU 5851  OE2 GLU B 208    24895  23781  19550  -1600   1117    929       O  
ATOM   5852  N   ASP B 209      16.544 -15.386  17.400  1.00146.29           N  
ANISOU 5852  N   ASP B 209    20441  20225  14917   -175   1226    665       N  
ATOM   5853  CA  ASP B 209      17.376 -15.347  16.207  1.00140.65           C  
ANISOU 5853  CA  ASP B 209    19794  19620  14024    119   1274    633       C  
ATOM   5854  C   ASP B 209      17.051 -14.152  15.272  1.00138.41           C  
ANISOU 5854  C   ASP B 209    19204  19632  13753      7   1180    617       C  
ATOM   5855  O   ASP B 209      17.943 -13.631  14.637  1.00142.60           O  
ANISOU 5855  O   ASP B 209    19571  20408  14200    253   1242    730       O  
ATOM   5856  CB  ASP B 209      17.254 -16.685  15.486  1.00143.21           C  
ANISOU 5856  CB  ASP B 209    20682  19564  14167    220   1314    442       C  
ATOM   5857  CG  ASP B 209      15.813 -17.167  15.408  1.00148.01           C  
ANISOU 5857  CG  ASP B 209    21494  19896  14846   -284   1166    238       C  
ATOM   5858  OD1 ASP B 209      14.868 -16.319  15.497  1.00148.91           O  
ANISOU 5858  OD1 ASP B 209    21241  20261  15076   -626   1029    252       O  
ATOM   5859  OD2 ASP B 209      15.625 -18.396  15.274  1.00155.59           O  
ANISOU 5859  OD2 ASP B 209    22990  20397  15730   -338   1196     84       O  
ATOM   5860  N   VAL B 210      15.796 -13.712  15.180  1.00136.42           N  
ANISOU 5860  N   VAL B 210    18844  19408  13582   -327   1056    537       N  
ATOM   5861  CA  VAL B 210      15.474 -12.470  14.436  1.00137.61           C  
ANISOU 5861  CA  VAL B 210    18689  19854  13742   -355   1015    600       C  
ATOM   5862  C   VAL B 210      16.290 -11.315  15.014  1.00140.64           C  
ANISOU 5862  C   VAL B 210    18783  20371  14282   -266   1084    802       C  
ATOM   5863  O   VAL B 210      16.210 -11.059  16.180  1.00154.86           O  
ANISOU 5863  O   VAL B 210    20506  22111  16220   -374   1072    832       O  
ATOM   5864  CB  VAL B 210      13.990 -12.048  14.546  1.00133.88           C  
ANISOU 5864  CB  VAL B 210    18072  19485  13311   -654    906    568       C  
ATOM   5865  CG1 VAL B 210      13.782 -10.718  13.844  1.00131.66           C  
ANISOU 5865  CG1 VAL B 210    17511  19489  13023   -557    928    702       C  
ATOM   5866  CG2 VAL B 210      13.067 -13.114  13.961  1.00135.92           C  
ANISOU 5866  CG2 VAL B 210    18550  19684  13407   -896    786    362       C  
ATOM   5867  N   GLU B 211      17.043 -10.592  14.211  1.00145.64           N  
ANISOU 5867  N   GLU B 211    19256  21195  14883   -104   1147    940       N  
ATOM   5868  CA  GLU B 211      17.909  -9.525  14.739  1.00146.42           C  
ANISOU 5868  CA  GLU B 211    19105  21384  15143   -133   1195   1127       C  
ATOM   5869  C   GLU B 211      17.468  -8.278  14.001  1.00145.32           C  
ANISOU 5869  C   GLU B 211    18819  21315  15078   -181   1222   1249       C  
ATOM   5870  O   GLU B 211      17.218  -8.321  12.806  1.00161.04           O  
ANISOU 5870  O   GLU B 211    20808  23456  16923    -36   1253   1288       O  
ATOM   5871  CB  GLU B 211      19.421  -9.839  14.579  1.00150.10           C  
ANISOU 5871  CB  GLU B 211    19472  22052  15506     84   1281   1285       C  
ATOM   5872  CG  GLU B 211      19.743 -10.709  13.386  1.00161.22           C  
ANISOU 5872  CG  GLU B 211    21035  23573  16645    420   1352   1282       C  
ATOM   5873  CD  GLU B 211      21.183 -11.209  13.333  1.00168.39           C  
ANISOU 5873  CD  GLU B 211    21860  24747  17372    758   1470   1472       C  
ATOM   5874  OE1 GLU B 211      21.965 -10.989  14.290  1.00163.35           O  
ANISOU 5874  OE1 GLU B 211    21000  24255  16807    692   1479   1611       O  
ATOM   5875  OE2 GLU B 211      21.538 -11.826  12.321  1.00185.35           O  
ANISOU 5875  OE2 GLU B 211    24148  27023  19254   1124   1555   1489       O  
ATOM   5876  N   GLY B 212      17.339  -7.184  14.725  1.00135.33           N  
ANISOU 5876  N   GLY B 212    17472  19933  14011   -350   1222   1303       N  
ATOM   5877  CA  GLY B 212      16.825  -5.925  14.204  1.00138.06           C  
ANISOU 5877  CA  GLY B 212    17768  20239  14449   -357   1290   1445       C  
ATOM   5878  C   GLY B 212      15.387  -5.697  14.628  1.00142.57           C  
ANISOU 5878  C   GLY B 212    18422  20736  15008   -364   1258   1347       C  
ATOM   5879  O   GLY B 212      14.862  -4.573  14.514  1.00141.77           O  
ANISOU 5879  O   GLY B 212    18336  20554  14976   -305   1342   1468       O  
ATOM   5880  N   CYS B 213      14.767  -6.723  15.211  1.00151.83           N  
ANISOU 5880  N   CYS B 213    19658  21935  16093   -420   1160   1170       N  
ATOM   5881  CA  CYS B 213      13.372  -6.651  15.628  1.00157.28           C  
ANISOU 5881  CA  CYS B 213    20345  22689  16725   -434   1126   1132       C  
ATOM   5882  C   CYS B 213      13.183  -6.996  17.109  1.00161.16           C  
ANISOU 5882  C   CYS B 213    20889  23069  17275   -535   1069   1023       C  
ATOM   5883  O   CYS B 213      13.671  -8.024  17.552  1.00152.88           O  
ANISOU 5883  O   CYS B 213    19896  21969  16221   -616   1020    935       O  
ATOM   5884  CB  CYS B 213      12.587  -7.663  14.820  1.00154.84           C  
ANISOU 5884  CB  CYS B 213    20010  22611  16211   -477   1047   1064       C  
ATOM   5885  SG  CYS B 213      12.561  -7.453  13.050  1.00145.25           S  
ANISOU 5885  SG  CYS B 213    18705  21679  14802   -309   1083   1154       S  
ATOM   5886  N   GLY B 214      12.442  -6.175  17.855  1.00164.40           N  
ANISOU 5886  N   GLY B 214    21299  23467  17699   -463   1100   1052       N  
ATOM   5887  CA  GLY B 214      12.046  -6.529  19.234  1.00165.97           C  
ANISOU 5887  CA  GLY B 214    21511  23671  17880   -492   1055    977       C  
ATOM   5888  C   GLY B 214      10.536  -6.609  19.370  1.00161.85           C  
ANISOU 5888  C   GLY B 214    20866  23428  17202   -422   1061   1079       C  
ATOM   5889  O   GLY B 214       9.824  -6.076  18.528  1.00171.62           O  
ANISOU 5889  O   GLY B 214    22015  24851  18340   -302   1111   1202       O  
ATOM   5890  N   ILE B 215      10.051  -7.213  20.455  1.00149.44           N  
ANISOU 5890  N   ILE B 215    19243  21959  15578   -465   1026   1081       N  
ATOM   5891  CA  ILE B 215       8.604  -7.321  20.669  1.00136.75           C  
ANISOU 5891  CA  ILE B 215    17434  20730  13794   -419   1035   1248       C  
ATOM   5892  C   ILE B 215       8.087  -5.929  21.034  1.00135.16           C  
ANISOU 5892  C   ILE B 215    17261  20601  13493    -34   1153   1327       C  
ATOM   5893  O   ILE B 215       8.719  -5.197  21.776  1.00129.48           O  
ANISOU 5893  O   ILE B 215    16754  19599  12841    117   1192   1198       O  
ATOM   5894  CB  ILE B 215       8.247  -8.348  21.758  1.00129.81           C  
ANISOU 5894  CB  ILE B 215    16473  19961  12888   -564    996   1301       C  
ATOM   5895  CG1 ILE B 215       8.830  -9.725  21.414  1.00128.84           C  
ANISOU 5895  CG1 ILE B 215    16454  19628  12870   -894    923   1223       C  
ATOM   5896  CG2 ILE B 215       6.741  -8.483  21.874  1.00130.54           C  
ANISOU 5896  CG2 ILE B 215    16268  20550  12780   -576   1002   1544       C  
ATOM   5897  CD1 ILE B 215       8.679 -10.793  22.473  1.00131.22           C  
ANISOU 5897  CD1 ILE B 215    16750  19918  13188  -1031    928   1316       C  
ATOM   5898  N   GLN B 216       6.941  -5.559  20.495  1.00141.84           N  
ANISOU 5898  N   GLN B 216    17913  21835  14143    137   1212   1534       N  
ATOM   5899  CA  GLN B 216       6.358  -4.260  20.819  1.00148.71           C  
ANISOU 5899  CA  GLN B 216    18864  22773  14864    622   1375   1653       C  
ATOM   5900  C   GLN B 216       6.008  -4.204  22.312  1.00158.78           C  
ANISOU 5900  C   GLN B 216    20169  24131  16025    828   1404   1644       C  
ATOM   5901  O   GLN B 216       5.622  -5.223  22.918  1.00165.04           O  
ANISOU 5901  O   GLN B 216    20730  25212  16765    627   1325   1720       O  
ATOM   5902  CB  GLN B 216       5.128  -3.944  19.945  1.00149.86           C  
ANISOU 5902  CB  GLN B 216    18722  23475  14742    853   1457   1954       C  
ATOM   5903  CG  GLN B 216       3.989  -4.955  20.027  1.00148.86           C  
ANISOU 5903  CG  GLN B 216    18140  24020  14400    632   1355   2154       C  
ATOM   5904  CD  GLN B 216       2.762  -4.561  19.245  1.00150.00           C  
ANISOU 5904  CD  GLN B 216    17915  24872  14205    881   1426   2481       C  
ATOM   5905  OE1 GLN B 216       2.826  -3.747  18.330  1.00155.81           O  
ANISOU 5905  OE1 GLN B 216    18723  25594  14883   1169   1537   2553       O  
ATOM   5906  NE2 GLN B 216       1.658  -5.204  19.549  1.00152.82           N  
ANISOU 5906  NE2 GLN B 216    17828  25912  14324    735   1361   2718       N  
ATOM   5907  N   CYS B 217       6.171  -3.012  22.886  1.00164.99           N  
ANISOU 5907  N   CYS B 217    20757  26093  15837    249    889   2224       N  
ATOM   5908  CA  CYS B 217       5.932  -2.755  24.312  1.00159.98           C  
ANISOU 5908  CA  CYS B 217    20280  25220  15282    206    892   2252       C  
ATOM   5909  C   CYS B 217       4.568  -3.241  24.817  1.00153.46           C  
ANISOU 5909  C   CYS B 217    19365  24496  14446    305    856   2204       C  
ATOM   5910  O   CYS B 217       4.462  -3.852  25.896  1.00155.06           O  
ANISOU 5910  O   CYS B 217    19563  24578  14774    205    803   2129       O  
ATOM   5911  CB  CYS B 217       6.086  -1.263  24.594  1.00164.45           C  
ANISOU 5911  CB  CYS B 217    21129  25589  15765    268   1007   2429       C  
ATOM   5912  SG  CYS B 217       5.598  -0.880  26.278  1.00173.76           S  
ANISOU 5912  SG  CYS B 217    22499  26507  17014    245   1020   2465       S  
ATOM   5913  N   GLN B 218       3.529  -2.946  24.040  1.00147.28           N  
ANISOU 5913  N   GLN B 218    18509  23948  13502    505    891   2253       N  
ATOM   5914  CA  GLN B 218       2.194  -3.397  24.365  1.00142.43           C  
ANISOU 5914  CA  GLN B 218    17779  23490  12847    604    861   2201       C  
ATOM   5915  C   GLN B 218       2.049  -4.883  23.993  1.00140.35           C  
ANISOU 5915  C   GLN B 218    17244  23425  12655    493    771   1999       C  
ATOM   5916  O   GLN B 218       2.137  -5.256  22.835  1.00139.31           O  
ANISOU 5916  O   GLN B 218    16950  23523  12457    513    762   1941       O  
ATOM   5917  CB  GLN B 218       1.143  -2.525  23.690  1.00141.27           C  
ANISOU 5917  CB  GLN B 218    17642  23551  12481    868    935   2329       C  
ATOM   5918  CG  GLN B 218      -0.205  -2.585  24.363  1.00143.67           C  
ANISOU 5918  CG  GLN B 218    17910  23947  12729    986    929   2327       C  
ATOM   5919  CD  GLN B 218      -1.321  -2.516  23.358  1.00148.66           C  
ANISOU 5919  CD  GLN B 218    18366  24968  13150   1204    949   2344       C  
ATOM   5920  OE1 GLN B 218      -1.590  -3.480  22.637  1.00148.14           O  
ANISOU 5920  OE1 GLN B 218    18042  25179  13063   1157    890   2198       O  
ATOM   5921  NE2 GLN B 218      -1.968  -1.361  23.277  1.00157.35           N  
ANISOU 5921  NE2 GLN B 218    19604  26101  14080   1451   1041   2524       N  
ATOM   5922  N   ASN B 219       1.815  -5.705  25.011  1.00138.55           N  
ANISOU 5922  N   ASN B 219    16985  23096  12560    376    717   1894       N  
ATOM   5923  CA  ASN B 219       1.752  -7.164  24.908  1.00134.98           C  
ANISOU 5923  CA  ASN B 219    16326  22753  12206    241    650   1697       C  
ATOM   5924  C   ASN B 219       0.945  -7.634  23.685  1.00132.18           C  
ANISOU 5924  C   ASN B 219    15737  22770  11712    322    647   1608       C  
ATOM   5925  O   ASN B 219      -0.275  -7.469  23.649  1.00129.53           O  
ANISOU 5925  O   ASN B 219    15331  22632  11252    447    662   1617       O  
ATOM   5926  CB  ASN B 219       1.123  -7.722  26.192  1.00138.08           C  
ANISOU 5926  CB  ASN B 219    16737  23027  12699    175    620   1636       C  
ATOM   5927  CG  ASN B 219       1.452  -9.192  26.435  1.00142.26           C  
ANISOU 5927  CG  ASN B 219    17142  23525  13384     -7    568   1452       C  
ATOM   5928  OD1 ASN B 219       1.565  -9.992  25.500  1.00138.43           O  
ANISOU 5928  OD1 ASN B 219    16488  23216  12890    -56    555   1328       O  
ATOM   5929  ND2 ASN B 219       1.564  -9.564  27.714  1.00147.41           N  
ANISOU 5929  ND2 ASN B 219    17884  23950  14175   -102    547   1434       N  
ATOM   5930  N   PRO B 220       1.620  -8.225  22.682  1.00130.13           N  
ANISOU 5930  N   PRO B 220    15349  22628  11466    250    629   1515       N  
ATOM   5931  CA  PRO B 220       0.938  -8.680  21.469  1.00128.06           C  
ANISOU 5931  CA  PRO B 220    14856  22734  11066    310    629   1417       C  
ATOM   5932  C   PRO B 220      -0.041  -9.819  21.669  1.00127.10           C  
ANISOU 5932  C   PRO B 220    14555  22776  10960    231    602   1232       C  
ATOM   5933  O   PRO B 220      -0.933 -10.004  20.854  1.00135.35           O  
ANISOU 5933  O   PRO B 220    15414  24161  11851    303    610   1165       O  
ATOM   5934  CB  PRO B 220       2.078  -9.155  20.584  1.00126.79           C  
ANISOU 5934  CB  PRO B 220    14627  22587  10959    211    614   1347       C  
ATOM   5935  CG  PRO B 220       3.138  -9.559  21.517  1.00129.95           C  
ANISOU 5935  CG  PRO B 220    15152  22658  11563     49    587   1325       C  
ATOM   5936  CD  PRO B 220       3.047  -8.585  22.657  1.00131.09           C  
ANISOU 5936  CD  PRO B 220    15516  22563  11729    101    607   1482       C  
ATOM   5937  N   LEU B 221       0.109 -10.563  22.747  1.00125.38           N  
ANISOU 5937  N   LEU B 221    14391  22331  10914     82    576   1151       N  
ATOM   5938  CA  LEU B 221      -0.776 -11.670  23.018  1.00126.33           C  
ANISOU 5938  CA  LEU B 221    14368  22569  11062    -16    565    972       C  
ATOM   5939  C   LEU B 221      -2.187 -11.245  23.456  1.00125.85           C  
ANISOU 5939  C   LEU B 221    14275  22668  10872     98    579   1011       C  
ATOM   5940  O   LEU B 221      -3.060 -12.108  23.512  1.00123.95           O  
ANISOU 5940  O   LEU B 221    13885  22597  10612     18    579    855       O  
ATOM   5941  CB  LEU B 221      -0.140 -12.618  24.065  1.00128.83           C  
ANISOU 5941  CB  LEU B 221    14768  22576  11603   -201    546    884       C  
ATOM   5942  CG  LEU B 221       0.992 -13.528  23.532  1.00128.56           C  
ANISOU 5942  CG  LEU B 221    14690  22471  11686   -335    538    770       C  
ATOM   5943  CD1 LEU B 221       2.311 -12.781  23.443  1.00125.86           C  
ANISOU 5943  CD1 LEU B 221    14483  21949  11387   -304    527    910       C  
ATOM   5944  CD2 LEU B 221       1.166 -14.802  24.355  1.00129.70           C  
ANISOU 5944  CD2 LEU B 221    14850  22423  12008   -502    539    629       C  
ATOM   5945  N   PHE B 222      -2.410  -9.961  23.781  1.00126.59           N  
ANISOU 5945  N   PHE B 222    14513  22709  10876    276    600   1211       N  
ATOM   5946  CA  PHE B 222      -3.718  -9.480  24.290  1.00130.06           C  
ANISOU 5946  CA  PHE B 222    14941  23284  11189    411    618   1269       C  
ATOM   5947  C   PHE B 222      -4.137  -8.183  23.638  1.00130.97           C  
ANISOU 5947  C   PHE B 222    15091  23580  11091    669    662   1450       C  
ATOM   5948  O   PHE B 222      -3.321  -7.301  23.458  1.00127.22           O  
ANISOU 5948  O   PHE B 222    14781  22936  10618    743    690   1599       O  
ATOM   5949  CB  PHE B 222      -3.690  -9.250  25.816  1.00129.97           C  
ANISOU 5949  CB  PHE B 222    15129  22942  11310    373    612   1340       C  
ATOM   5950  CG  PHE B 222      -3.267 -10.454  26.592  1.00130.68           C  
ANISOU 5950  CG  PHE B 222    15217  22826  11609    145    578   1192       C  
ATOM   5951  CD1 PHE B 222      -4.199 -11.446  26.907  1.00131.75           C  
ANISOU 5951  CD1 PHE B 222    15210  23093  11753     46    572   1031       C  
ATOM   5952  CD2 PHE B 222      -1.930 -10.640  26.952  1.00128.85           C  
ANISOU 5952  CD2 PHE B 222    15115  22289  11552     28    561   1206       C  
ATOM   5953  CE1 PHE B 222      -3.816 -12.598  27.586  1.00131.39           C  
ANISOU 5953  CE1 PHE B 222    15177  22849  11896   -156    559    898       C  
ATOM   5954  CE2 PHE B 222      -1.535 -11.793  27.628  1.00129.11           C  
ANISOU 5954  CE2 PHE B 222    15144  22146  11765   -157    540   1077       C  
ATOM   5955  CZ  PHE B 222      -2.485 -12.774  27.951  1.00130.97           C  
ANISOU 5955  CZ  PHE B 222    15259  22486  12014   -245    544    927       C  
ATOM   5956  N   THR B 223      -5.428  -8.078  23.328  1.00137.01           N  
ANISOU 5956  N   THR B 223    15700  24690  11664    806    676   1436       N  
ATOM   5957  CA  THR B 223      -5.987  -6.915  22.635  1.00144.31           C  
ANISOU 5957  CA  THR B 223    16630  25848  12351   1089    728   1608       C  
ATOM   5958  C   THR B 223      -5.993  -5.675  23.547  1.00145.76           C  
ANISOU 5958  C   THR B 223    17092  25759  12531   1248    776   1828       C  
ATOM   5959  O   THR B 223      -5.785  -5.792  24.739  1.00143.81           O  
ANISOU 5959  O   THR B 223    16988  25207  12444   1136    759   1825       O  
ATOM   5960  CB  THR B 223      -7.433  -7.200  22.104  1.00149.05           C  
ANISOU 5960  CB  THR B 223    16963  26941  12728   1198    730   1525       C  
ATOM   5961  OG1 THR B 223      -8.332  -7.447  23.184  1.00150.84           O  
ANISOU 5961  OG1 THR B 223    17184  27152  12975   1169    718   1483       O  
ATOM   5962  CG2 THR B 223      -7.484  -8.414  21.188  1.00150.27           C  
ANISOU 5962  CG2 THR B 223    16842  27382  12871   1025    696   1289       C  
ATOM   5963  N   GLU B 224      -6.236  -4.499  22.971  1.00149.70           N  
ANISOU 5963  N   GLU B 224    17670  26370  12840   1511    845   2017       N  
ATOM   5964  CA  GLU B 224      -6.403  -3.253  23.737  1.00154.58           C  
ANISOU 5964  CA  GLU B 224    18556  26761  13415   1695    915   2229       C  
ATOM   5965  C   GLU B 224      -7.637  -3.345  24.683  1.00155.23           C  
ANISOU 5965  C   GLU B 224    18597  26934  13447   1762    905   2212       C  
ATOM   5966  O   GLU B 224      -7.606  -2.855  25.832  1.00150.14           O  
ANISOU 5966  O   GLU B 224    18169  25987  12888   1766    925   2296       O  
ATOM   5967  CB  GLU B 224      -6.477  -2.043  22.770  1.00161.48           C  
ANISOU 5967  CB  GLU B 224    19512  27772  14070   1984   1009   2432       C  
ATOM   5968  CG  GLU B 224      -7.035  -0.718  23.310  1.00172.08           C  
ANISOU 5968  CG  GLU B 224    21093  29003  15285   2254   1109   2657       C  
ATOM   5969  CD  GLU B 224      -6.093   0.034  24.249  1.00178.33           C  
ANISOU 5969  CD  GLU B 224    22236  29283  16238   2174   1160   2769       C  
ATOM   5970  OE1 GLU B 224      -5.863   1.242  23.997  1.00182.48           O  
ANISOU 5970  OE1 GLU B 224    22993  29679  16661   2362   1273   2967       O  
ATOM   5971  OE2 GLU B 224      -5.605  -0.556  25.255  1.00186.32           O  
ANISOU 5971  OE2 GLU B 224    23299  30026  17467   1928   1096   2662       O  
ATOM   5972  N   ALA B 225      -8.706  -3.980  24.193  1.00156.08           N  
ANISOU 5972  N   ALA B 225    18420  27472  13410   1803    875   2094       N  
ATOM   5973  CA  ALA B 225      -9.916  -4.231  24.991  1.00150.97           C  
ANISOU 5973  CA  ALA B 225    17683  26974  12703   1838    860   2045       C  
ATOM   5974  C   ALA B 225      -9.584  -5.008  26.253  1.00145.72           C  
ANISOU 5974  C   ALA B 225    17095  25980  12291   1571    806   1927       C  
ATOM   5975  O   ALA B 225     -10.116  -4.731  27.330  1.00144.31           O  
ANISOU 5975  O   ALA B 225    17022  25678  12132   1613    814   1979       O  
ATOM   5976  CB  ALA B 225     -10.943  -5.001  24.167  1.00150.58           C  
ANISOU 5976  CB  ALA B 225    17281  27456  12475   1848    831   1888       C  
ATOM   5977  N   GLU B 226      -8.709  -5.994  26.092  1.00143.50           N  
ANISOU 5977  N   GLU B 226    16758  25571  12193   1309    756   1772       N  
ATOM   5978  CA  GLU B 226      -8.252  -6.823  27.198  1.00145.46           C  
ANISOU 5978  CA  GLU B 226    17076  25505  12684   1055    710   1660       C  
ATOM   5979  C   GLU B 226      -7.313  -6.096  28.161  1.00145.31           C  
ANISOU 5979  C   GLU B 226    17365  25025  12819   1039    725   1803       C  
ATOM   5980  O   GLU B 226      -7.386  -6.325  29.357  1.00146.05           O  
ANISOU 5980  O   GLU B 226    17552  24900  13038    944    706   1784       O  
ATOM   5981  CB  GLU B 226      -7.609  -8.101  26.662  1.00142.90           C  
ANISOU 5981  CB  GLU B 226    16602  25202  12490    807    666   1457       C  
ATOM   5982  CG  GLU B 226      -8.648  -9.031  26.045  1.00140.64           C  
ANISOU 5982  CG  GLU B 226    16017  25336  12083    750    653   1268       C  
ATOM   5983  CD  GLU B 226      -8.076 -10.129  25.172  1.00139.70           C  
ANISOU 5983  CD  GLU B 226    15740  25305  12033    553    633   1077       C  
ATOM   5984  OE1 GLU B 226      -6.971 -10.002  24.584  1.00137.25           O  
ANISOU 5984  OE1 GLU B 226    15497  24858  11791    531    630   1113       O  
ATOM   5985  OE2 GLU B 226      -8.772 -11.152  25.040  1.00142.20           O  
ANISOU 5985  OE2 GLU B 226    15856  25845  12327    411    627    879       O  
ATOM   5986  N   HIS B 227      -6.473  -5.208  27.640  1.00144.87           N  
ANISOU 5986  N   HIS B 227    17461  24840  12740   1130    766   1941       N  
ATOM   5987  CA  HIS B 227      -5.632  -4.341  28.472  1.00144.26           C  
ANISOU 5987  CA  HIS B 227    17682  24359  12769   1125    799   2084       C  
ATOM   5988  C   HIS B 227      -6.462  -3.410  29.389  1.00146.62           C  
ANISOU 5988  C   HIS B 227    18142  24582  12984   1303    850   2222       C  
ATOM   5989  O   HIS B 227      -6.301  -3.451  30.605  1.00149.23           O  
ANISOU 5989  O   HIS B 227    18606  24644  13448   1202    835   2221       O  
ATOM   5990  CB  HIS B 227      -4.661  -3.508  27.614  1.00146.73           C  
ANISOU 5990  CB  HIS B 227    18121  24586  13041   1191    852   2204       C  
ATOM   5991  CG  HIS B 227      -3.434  -4.252  27.167  1.00148.57           C  
ANISOU 5991  CG  HIS B 227    18300  24724  13423    975    805   2096       C  
ATOM   5992  ND1 HIS B 227      -3.464  -5.230  26.192  1.00154.63           N  
ANISOU 5992  ND1 HIS B 227    18819  25755  14175    902    760   1947       N  
ATOM   5993  CD2 HIS B 227      -2.135  -4.134  27.535  1.00146.30           C  
ANISOU 5993  CD2 HIS B 227    18172  24124  13290    824    801   2116       C  
ATOM   5994  CE1 HIS B 227      -2.241  -5.698  26.000  1.00153.69           C  
ANISOU 5994  CE1 HIS B 227    18717  25476  14201    726    731   1885       C  
ATOM   5995  NE2 HIS B 227      -1.415  -5.046  26.798  1.00147.53           N  
ANISOU 5995  NE2 HIS B 227    18174  24358  13521    679    753   1988       N  
ATOM   5996  N   GLN B 228      -7.361  -2.597  28.829  1.00150.55           N  
ANISOU 5996  N   GLN B 228    18623  25324  13254   1576    912   2341       N  
ATOM   5997  CA  GLN B 228      -8.171  -1.658  29.652  1.00154.02           C  
ANISOU 5997  CA  GLN B 228    19225  25697  13596   1777    973   2484       C  
ATOM   5998  C   GLN B 228      -9.054  -2.377  30.689  1.00153.26           C  
ANISOU 5998  C   GLN B 228    19025  25655  13551   1697    917   2376       C  
ATOM   5999  O   GLN B 228      -9.334  -1.837  31.755  1.00150.02           O  
ANISOU 5999  O   GLN B 228    18788  25048  13162   1752    944   2457       O  
ATOM   6000  CB  GLN B 228      -9.133  -0.844  28.803  1.00163.56           C  
ANISOU 6000  CB  GLN B 228    20382  27236  14526   2106   1047   2616       C  
ATOM   6001  CG  GLN B 228      -8.565   0.114  27.772  1.00172.99           C  
ANISOU 6001  CG  GLN B 228    21702  28417  15606   2273   1134   2771       C  
ATOM   6002  CD  GLN B 228      -9.555   0.313  26.595  1.00176.07           C  
ANISOU 6002  CD  GLN B 228    21885  29294  15720   2549   1167   2820       C  
ATOM   6003  OE1 GLN B 228     -10.729  -0.060  26.696  1.00173.87           O  
ANISOU 6003  OE1 GLN B 228    21404  29340  15316   2641   1138   2763       O  
ATOM   6004  NE2 GLN B 228      -9.083   0.897  25.488  1.00172.51           N  
ANISOU 6004  NE2 GLN B 228    21475  28908  15160   2678   1230   2926       N  
ATOM   6005  N   ASP B 229      -9.512  -3.578  30.342  1.00154.01           N  
ANISOU 6005  N   ASP B 229    18838  26022  13653   1567    847   2191       N  
ATOM   6006  CA  ASP B 229     -10.317  -4.420  31.224  1.00150.35           C  
ANISOU 6006  CA  ASP B 229    18253  25628  13243   1453    798   2063       C  
ATOM   6007  C   ASP B 229      -9.492  -4.934  32.402  1.00142.20           C  
ANISOU 6007  C   ASP B 229    17364  24193  12470   1209    757   2004       C  
ATOM   6008  O   ASP B 229      -9.939  -4.893  33.546  1.00144.13           O  
ANISOU 6008  O   ASP B 229    17688  24313  12762   1197    752   2018       O  
ATOM   6009  CB  ASP B 229     -10.911  -5.590  30.420  1.00155.52           C  
ANISOU 6009  CB  ASP B 229    18581  26672  13837   1347    752   1865       C  
ATOM   6010  CG  ASP B 229     -11.483  -6.692  31.311  1.00159.61           C  
ANISOU 6010  CG  ASP B 229    18985  27202  14458   1146    706   1697       C  
ATOM   6011  OD1 ASP B 229     -12.630  -6.537  31.805  1.00157.21           O  
ANISOU 6011  OD1 ASP B 229    18616  27083  14033   1251    716   1710       O  
ATOM   6012  OD2 ASP B 229     -10.778  -7.715  31.500  1.00162.39           O  
ANISOU 6012  OD2 ASP B 229    19313  27380  15005    888    667   1555       O  
ATOM   6013  N   MET B 230      -8.291  -5.425  32.124  1.00135.53           N  
ANISOU 6013  N   MET B 230    16546  23165  11785   1024    728   1941       N  
ATOM   6014  CA  MET B 230      -7.373  -5.836  33.188  1.00132.55           C  
ANISOU 6014  CA  MET B 230    16309  22415  11638    816    695   1905       C  
ATOM   6015  C   MET B 230      -6.868  -4.630  34.026  1.00126.61           C  
ANISOU 6015  C   MET B 230    15853  21338  10915    895    740   2078       C  
ATOM   6016  O   MET B 230      -6.638  -4.738  35.244  1.00123.05           O  
ANISOU 6016  O   MET B 230    15521  20636  10595    790    722   2075       O  
ATOM   6017  CB  MET B 230      -6.215  -6.635  32.574  1.00132.71           C  
ANISOU 6017  CB  MET B 230    16269  22361  11794    626    659   1801       C  
ATOM   6018  CG  MET B 230      -5.193  -7.161  33.561  1.00134.43           C  
ANISOU 6018  CG  MET B 230    16603  22238  12236    421    624   1759       C  
ATOM   6019  SD  MET B 230      -5.892  -8.293  34.793  1.00136.47           S  
ANISOU 6019  SD  MET B 230    16789  22452  12610    276    586   1630       S  
ATOM   6020  CE  MET B 230      -6.253  -9.711  33.763  1.00134.10           C  
ANISOU 6020  CE  MET B 230    16209  22441  12302    152    567   1418       C  
ATOM   6021  N   HIS B 231      -6.716  -3.484  33.376  1.00124.78           N  
ANISOU 6021  N   HIS B 231    15742  21116  10553   1077    808   2226       N  
ATOM   6022  CA  HIS B 231      -6.345  -2.253  34.077  1.00125.62           C  
ANISOU 6022  CA  HIS B 231    16142  20929  10656   1161    877   2388       C  
ATOM   6023  C   HIS B 231      -7.478  -1.720  34.967  1.00123.68           C  
ANISOU 6023  C   HIS B 231    15971  20700  10320   1321    911   2461       C  
ATOM   6024  O   HIS B 231      -7.224  -1.265  36.079  1.00119.87           O  
ANISOU 6024  O   HIS B 231    15690  19935   9918   1280    930   2514       O  
ATOM   6025  CB  HIS B 231      -5.877  -1.172  33.085  1.00131.51           C  
ANISOU 6025  CB  HIS B 231    17018  21669  11281   1313    962   2528       C  
ATOM   6026  CG  HIS B 231      -4.608  -1.509  32.348  1.00131.32           C  
ANISOU 6026  CG  HIS B 231    16969  21574  11353   1150    939   2477       C  
ATOM   6027  ND1 HIS B 231      -4.472  -1.328  30.987  1.00132.60           N  
ANISOU 6027  ND1 HIS B 231    17045  21937  11398   1247    967   2506       N  
ATOM   6028  CD2 HIS B 231      -3.428  -2.018  32.782  1.00129.08           C  
ANISOU 6028  CD2 HIS B 231    16727  21059  11258    909    892   2401       C  
ATOM   6029  CE1 HIS B 231      -3.265  -1.720  30.617  1.00133.08           C  
ANISOU 6029  CE1 HIS B 231    17097  21887  11579   1064    936   2446       C  
ATOM   6030  NE2 HIS B 231      -2.614  -2.143  31.686  1.00130.93           N  
ANISOU 6030  NE2 HIS B 231    16899  21359  11490    861    891   2383       N  
ATOM   6031  N   SER B 232      -8.723  -1.793  34.491  1.00128.38           N  
ANISOU 6031  N   SER B 232    16394  21642  10741   1499    917   2458       N  
ATOM   6032  CA  SER B 232      -9.894  -1.478  35.337  1.00133.04           C  
ANISOU 6032  CA  SER B 232    17005  22302  11240   1643    937   2505       C  
ATOM   6033  C   SER B 232      -9.895  -2.363  36.571  1.00129.27           C  
ANISOU 6033  C   SER B 232    16499  21673  10942   1424    865   2385       C  
ATOM   6034  O   SER B 232     -10.115  -1.894  37.678  1.00132.84           O  
ANISOU 6034  O   SER B 232    17112  21936  11422   1455    886   2447       O  
ATOM   6035  CB  SER B 232     -11.253  -1.706  34.624  1.00140.13           C  
ANISOU 6035  CB  SER B 232    17650  23669  11924   1827    935   2477       C  
ATOM   6036  OG  SER B 232     -11.424  -0.925  33.457  1.00144.14           O  
ANISOU 6036  OG  SER B 232    18152  24381  12232   2068   1003   2594       O  
ATOM   6037  N   TYR B 233      -9.680  -3.654  36.356  1.00126.05           N  
ANISOU 6037  N   TYR B 233    15890  21355  10647   1210    789   2213       N  
ATOM   6038  CA  TYR B 233      -9.641  -4.626  37.430  1.00125.69           C  
ANISOU 6038  CA  TYR B 233    15809  21174  10774    997    730   2095       C  
ATOM   6039  C   TYR B 233      -8.508  -4.322  38.391  1.00123.34           C  
ANISOU 6039  C   TYR B 233    15746  20466  10649    873    728   2146       C  
ATOM   6040  O   TYR B 233      -8.728  -4.312  39.591  1.00128.03           O  
ANISOU 6040  O   TYR B 233    16430  20904  11309    835    719   2156       O  
ATOM   6041  CB  TYR B 233      -9.492  -6.033  36.849  1.00127.81           C  
ANISOU 6041  CB  TYR B 233    15843  21593  11124    798    673   1908       C  
ATOM   6042  CG  TYR B 233      -9.655  -7.174  37.836  1.00128.40           C  
ANISOU 6042  CG  TYR B 233    15855  21580  11350    593    627   1775       C  
ATOM   6043  CD1 TYR B 233     -10.924  -7.689  38.126  1.00129.32           C  
ANISOU 6043  CD1 TYR B 233    15814  21934  11387    601    622   1695       C  
ATOM   6044  CD2 TYR B 233      -8.548  -7.765  38.456  1.00126.21           C  
ANISOU 6044  CD2 TYR B 233    15667  21000  11284    395    596   1730       C  
ATOM   6045  CE1 TYR B 233     -11.094  -8.742  39.019  1.00126.35           C  
ANISOU 6045  CE1 TYR B 233    15391  21470  11145    410    595   1576       C  
ATOM   6046  CE2 TYR B 233      -8.714  -8.819  39.351  1.00124.79           C  
ANISOU 6046  CE2 TYR B 233    15441  20738  11234    226    568   1621       C  
ATOM   6047  CZ  TYR B 233      -9.992  -9.299  39.625  1.00125.23           C  
ANISOU 6047  CZ  TYR B 233    15357  21009  11214    231    571   1545       C  
ATOM   6048  OH  TYR B 233     -10.171 -10.357  40.480  1.00127.17           O  
ANISOU 6048  OH  TYR B 233    15565  21167  11584     58    557   1438       O  
ATOM   6049  N   ILE B 234      -7.312  -4.042  37.877  1.00123.91           N  
ANISOU 6049  N   ILE B 234    15914  20382  10784    812    738   2178       N  
ATOM   6050  CA  ILE B 234      -6.166  -3.690  38.757  1.00121.77           C  
ANISOU 6050  CA  ILE B 234    15858  19750  10658    685    741   2222       C  
ATOM   6051  C   ILE B 234      -6.435  -2.406  39.540  1.00124.77           C  
ANISOU 6051  C   ILE B 234    16481  19959  10966    825    812   2367       C  
ATOM   6052  O   ILE B 234      -6.101  -2.329  40.740  1.00130.59           O  
ANISOU 6052  O   ILE B 234    17349  20460  11807    726    802   2373       O  
ATOM   6053  CB  ILE B 234      -4.826  -3.620  37.970  1.00119.11           C  
ANISOU 6053  CB  ILE B 234    15560  19315  10380    589    744   2223       C  
ATOM   6054  CG1 ILE B 234      -4.341  -5.045  37.693  1.00121.24           C  
ANISOU 6054  CG1 ILE B 234    15635  19646  10782    398    668   2065       C  
ATOM   6055  CG2 ILE B 234      -3.741  -2.869  38.712  1.00115.69           C  
ANISOU 6055  CG2 ILE B 234    15368  18558  10028    504    774   2299       C  
ATOM   6056  CD1 ILE B 234      -3.497  -5.203  36.444  1.00121.19           C  
ANISOU 6056  CD1 ILE B 234    15558  19715  10774    359    666   2039       C  
ATOM   6057  N   ALA B 235      -7.054  -1.421  38.881  1.00129.27           N  
ANISOU 6057  N   ALA B 235    17111  20653  11352   1060    889   2484       N  
ATOM   6058  CA  ALA B 235      -7.405  -0.156  39.573  1.00130.21           C  
ANISOU 6058  CA  ALA B 235    17480  20608  11383   1222    978   2627       C  
ATOM   6059  C   ALA B 235      -8.329  -0.359  40.763  1.00127.04           C  
ANISOU 6059  C   ALA B 235    17068  20208  10991   1245    954   2608       C  
ATOM   6060  O   ALA B 235      -8.063   0.146  41.858  1.00128.27           O  
ANISOU 6060  O   ALA B 235    17422  20105  11209   1202    980   2651       O  
ATOM   6061  CB  ALA B 235      -8.046   0.829  38.607  1.00136.32           C  
ANISOU 6061  CB  ALA B 235    18302  21551  11940   1507   1073   2760       C  
ATOM   6062  N   ALA B 236      -9.422  -1.083  40.534  1.00124.77           N  
ANISOU 6062  N   ALA B 236    16546  20226  10634   1307    909   2537       N  
ATOM   6063  CA  ALA B 236     -10.409  -1.373  41.596  1.00124.74           C  
ANISOU 6063  CA  ALA B 236    16497  20271  10625   1327    884   2508       C  
ATOM   6064  C   ALA B 236      -9.764  -2.007  42.812  1.00120.66           C  
ANISOU 6064  C   ALA B 236    16034  19496  10314   1087    826   2431       C  
ATOM   6065  O   ALA B 236      -9.885  -1.482  43.902  1.00117.26           O  
ANISOU 6065  O   ALA B 236    15767  18883   9902   1108    850   2488       O  
ATOM   6066  CB  ALA B 236     -11.545  -2.268  41.080  1.00126.36           C  
ANISOU 6066  CB  ALA B 236    16406  20868  10738   1364    839   2407       C  
ATOM   6067  N   PHE B 237      -9.094  -3.137  42.616  1.00118.81           N  
ANISOU 6067  N   PHE B 237    15662  19255  10224    871    756   2305       N  
ATOM   6068  CA  PHE B 237      -8.472  -3.847  43.725  1.00119.97           C  
ANISOU 6068  CA  PHE B 237    15840  19183  10558    658    703   2235       C  
ATOM   6069  C   PHE B 237      -7.304  -3.085  44.350  1.00119.78           C  
ANISOU 6069  C   PHE B 237    16058  18836  10617    588    729   2309       C  
ATOM   6070  O   PHE B 237      -7.259  -2.951  45.588  1.00125.45           O  
ANISOU 6070  O   PHE B 237    16888  19377  11398    534    725   2324       O  
ATOM   6071  CB  PHE B 237      -8.065  -5.264  43.323  1.00121.17           C  
ANISOU 6071  CB  PHE B 237    15795  19410  10832    467    638   2088       C  
ATOM   6072  CG  PHE B 237      -9.206  -6.240  43.347  1.00122.05           C  
ANISOU 6072  CG  PHE B 237    15696  19762  10914    448    611   1981       C  
ATOM   6073  CD1 PHE B 237     -10.091  -6.323  42.271  1.00124.51           C  
ANISOU 6073  CD1 PHE B 237    15832  20402  11072    559    625   1948       C  
ATOM   6074  CD2 PHE B 237      -9.394  -7.077  44.454  1.00120.23           C  
ANISOU 6074  CD2 PHE B 237    15441  19441  10800    314    578   1910       C  
ATOM   6075  CE1 PHE B 237     -11.144  -7.224  42.294  1.00129.34           C  
ANISOU 6075  CE1 PHE B 237    16242  21255  11645    516    607   1833       C  
ATOM   6076  CE2 PHE B 237     -10.434  -7.982  44.483  1.00120.81           C  
ANISOU 6076  CE2 PHE B 237    15330  19728  10844    273    566   1804       C  
ATOM   6077  CZ  PHE B 237     -11.317  -8.053  43.407  1.00127.87           C  
ANISOU 6077  CZ  PHE B 237    16045  20956  11582    364    581   1759       C  
ATOM   6078  N   GLY B 238      -6.405  -2.541  43.527  1.00121.01           N  
ANISOU 6078  N   GLY B 238    16294  18926  10758    586    763   2353       N  
ATOM   6079  CA  GLY B 238      -5.330  -1.682  44.068  1.00125.76           C  
ANISOU 6079  CA  GLY B 238    17133  19240  11409    513    805   2421       C  
ATOM   6080  C   GLY B 238      -5.761  -0.506  44.980  1.00129.76           C  
ANISOU 6080  C   GLY B 238    17873  19588  11841    626    881   2527       C  
ATOM   6081  O   GLY B 238      -5.189  -0.290  46.067  1.00128.03           O  
ANISOU 6081  O   GLY B 238    17792  19148  11704    507    882   2527       O  
ATOM   6082  N   ALA B 239      -6.781   0.243  44.544  1.00131.66           N  
ANISOU 6082  N   ALA B 239    18155  19953  11915    865    950   2615       N  
ATOM   6083  CA  ALA B 239      -7.258   1.429  45.281  1.00128.10           C  
ANISOU 6083  CA  ALA B 239    17943  19356  11371   1010   1043   2726       C  
ATOM   6084  C   ALA B 239      -7.985   1.061  46.586  1.00126.40           C  
ANISOU 6084  C   ALA B 239    17702  19126  11198    992   1001   2691       C  
ATOM   6085  O   ALA B 239      -7.689   1.590  47.656  1.00127.04           O  
ANISOU 6085  O   ALA B 239    17970  18979  11320    936   1032   2717       O  
ATOM   6086  CB  ALA B 239      -8.159   2.256  44.386  1.00127.36           C  
ANISOU 6086  CB  ALA B 239    17887  19428  11077   1298   1133   2838       C  
ATOM   6087  N   VAL B 240      -8.916   0.117  46.492  1.00123.93           N  
ANISOU 6087  N   VAL B 240    17151  19062  10872   1024    932   2622       N  
ATOM   6088  CA  VAL B 240      -9.625  -0.397  47.662  1.00120.81           C  
ANISOU 6088  CA  VAL B 240    16700  18682  10521    990    885   2577       C  
ATOM   6089  C   VAL B 240      -8.624  -0.948  48.690  1.00122.78           C  
ANISOU 6089  C   VAL B 240    16992  18700  10956    742    829   2510       C  
ATOM   6090  O   VAL B 240      -8.686  -0.570  49.868  1.00126.54           O  
ANISOU 6090  O   VAL B 240    17603  19017  11457    724    843   2536       O  
ATOM   6091  CB  VAL B 240     -10.650  -1.464  47.245  1.00116.71           C  
ANISOU 6091  CB  VAL B 240    15896  18482   9966   1015    824   2490       C  
ATOM   6092  CG1 VAL B 240     -11.163  -2.259  48.426  1.00114.52           C  
ANISOU 6092  CG1 VAL B 240    15539  18202   9771    912    767   2418       C  
ATOM   6093  CG2 VAL B 240     -11.805  -0.795  46.532  1.00118.80           C  
ANISOU 6093  CG2 VAL B 240    16123  18998  10015   1290    883   2569       C  
ATOM   6094  N   THR B 241      -7.689  -1.799  48.244  1.00120.45           N  
ANISOU 6094  N   THR B 241    16587  18396  10781    564    770   2428       N  
ATOM   6095  CA  THR B 241      -6.642  -2.317  49.147  1.00117.35           C  
ANISOU 6095  CA  THR B 241    16228  17808  10551    348    721   2375       C  
ATOM   6096  C   THR B 241      -5.762  -1.189  49.686  1.00116.09           C  
ANISOU 6096  C   THR B 241    16319  17398  10389    309    781   2444       C  
ATOM   6097  O   THR B 241      -5.354  -1.214  50.852  1.00113.07           O  
ANISOU 6097  O   THR B 241    16015  16863  10081    197    764   2430       O  
ATOM   6098  CB  THR B 241      -5.761  -3.372  48.457  1.00117.49           C  
ANISOU 6098  CB  THR B 241    16090  17871  10678    194    661   2286       C  
ATOM   6099  OG1 THR B 241      -6.609  -4.353  47.842  1.00122.57           O  
ANISOU 6099  OG1 THR B 241    16513  18748  11307    224    625   2211       O  
ATOM   6100  CG2 THR B 241      -4.827  -4.064  49.467  1.00115.43           C  
ANISOU 6100  CG2 THR B 241    15834  17453  10571      1    608   2233       C  
ATOM   6101  N   GLY B 242      -5.491  -0.190  48.851  1.00116.16           N  
ANISOU 6101  N   GLY B 242    16459  17371  10303    397    860   2517       N  
ATOM   6102  CA  GLY B 242      -4.763   0.999  49.303  1.00116.79           C  
ANISOU 6102  CA  GLY B 242    16803  17211  10358    359    944   2580       C  
ATOM   6103  C   GLY B 242      -5.455   1.787  50.412  1.00115.93           C  
ANISOU 6103  C   GLY B 242    16871  16985  10191    449   1003   2635       C  
ATOM   6104  O   GLY B 242      -4.799   2.260  51.353  1.00112.32           O  
ANISOU 6104  O   GLY B 242    16575  16326   9773    325   1030   2631       O  
ATOM   6105  N   LEU B 243      -6.773   1.948  50.277  1.00116.07           N  
ANISOU 6105  N   LEU B 243    16854  17147  10100    666   1027   2684       N  
ATOM   6106  CA  LEU B 243      -7.596   2.652  51.269  1.00121.34           C  
ANISOU 6106  CA  LEU B 243    17672  17737  10695    788   1083   2740       C  
ATOM   6107  C   LEU B 243      -7.806   1.826  52.548  1.00120.85           C  
ANISOU 6107  C   LEU B 243    17512  17669  10737    669    995   2667       C  
ATOM   6108  O   LEU B 243      -7.687   2.336  53.664  1.00120.32           O  
ANISOU 6108  O   LEU B 243    17603  17429  10682    625   1025   2680       O  
ATOM   6109  CB  LEU B 243      -8.967   3.001  50.681  1.00125.52           C  
ANISOU 6109  CB  LEU B 243    18160  18468  11061   1074   1130   2815       C  
ATOM   6110  CG  LEU B 243      -9.040   4.035  49.547  1.00129.45           C  
ANISOU 6110  CG  LEU B 243    18796  18977  11412   1270   1247   2923       C  
ATOM   6111  CD1 LEU B 243     -10.296   3.779  48.719  1.00129.68           C  
ANISOU 6111  CD1 LEU B 243    18636  19333  11303   1510   1237   2956       C  
ATOM   6112  CD2 LEU B 243      -8.985   5.479  50.055  1.00130.88           C  
ANISOU 6112  CD2 LEU B 243    19320  18903  11505   1374   1395   3027       C  
ATOM   6113  N   CYS B 244      -8.126   0.551  52.377  1.00117.72           N  
ANISOU 6113  N   CYS B 244    16859  17459  10410    615    895   2590       N  
ATOM   6114  CA  CYS B 244      -8.268  -0.339  53.516  1.00115.93           C  
ANISOU 6114  CA  CYS B 244    16534  17225  10287    495    817   2523       C  
ATOM   6115  C   CYS B 244      -7.008  -0.446  54.367  1.00114.04           C  
ANISOU 6115  C   CYS B 244    16378  16780  10171    281    791   2486       C  
ATOM   6116  O   CYS B 244      -7.079  -0.330  55.581  1.00111.57           O  
ANISOU 6116  O   CYS B 244    16139  16366   9884    237    786   2486       O  
ATOM   6117  CB  CYS B 244      -8.647  -1.727  53.043  1.00119.09           C  
ANISOU 6117  CB  CYS B 244    16665  17835  10748    444    734   2437       C  
ATOM   6118  SG  CYS B 244     -10.359  -1.872  52.542  1.00131.05           S  
ANISOU 6118  SG  CYS B 244    18028  19647  12118    655    744   2447       S  
ATOM   6119  N   THR B 245      -5.871  -0.699  53.719  1.00117.95           N  
ANISOU 6119  N   THR B 245    16843  17239  10731    152    771   2454       N  
ATOM   6120  CA  THR B 245      -4.597  -0.823  54.424  1.00119.61           C  
ANISOU 6120  CA  THR B 245    17106  17299  11041    -48    745   2417       C  
ATOM   6121  C   THR B 245      -4.173   0.471  55.086  1.00119.01           C  
ANISOU 6121  C   THR B 245    17284  17027  10907    -73    829   2463       C  
ATOM   6122  O   THR B 245      -3.650   0.435  56.175  1.00121.95           O  
ANISOU 6122  O   THR B 245    17703  17301  11331   -200    809   2435       O  
ATOM   6123  CB  THR B 245      -3.428  -1.301  53.515  1.00122.73           C  
ANISOU 6123  CB  THR B 245    17414  17715  11501   -171    713   2375       C  
ATOM   6124  OG1 THR B 245      -3.290  -0.452  52.359  1.00118.87           O  
ANISOU 6124  OG1 THR B 245    17014  17227  10923    -93    785   2424       O  
ATOM   6125  CG2 THR B 245      -3.628  -2.745  53.087  1.00124.73           C  
ANISOU 6125  CG2 THR B 245    17425  18127  11839   -197    631   2308       C  
ATOM   6126  N   LEU B 246      -4.362   1.598  54.417  1.00120.07           N  
ANISOU 6126  N   LEU B 246    17585  17105  10930     43    930   2531       N  
ATOM   6127  CA  LEU B 246      -3.992   2.900  54.978  1.00122.77           C  
ANISOU 6127  CA  LEU B 246    18202  17237  11206     16   1038   2571       C  
ATOM   6128  C   LEU B 246      -4.819   3.223  56.232  1.00123.42           C  
ANISOU 6128  C   LEU B 246    18376  17259  11256     84   1058   2588       C  
ATOM   6129  O   LEU B 246      -4.282   3.678  57.233  1.00121.09           O  
ANISOU 6129  O   LEU B 246    18218  16815  10976    -41   1085   2565       O  
ATOM   6130  CB  LEU B 246      -4.192   3.988  53.913  1.00126.21           C  
ANISOU 6130  CB  LEU B 246    18806  17628  11519    166   1160   2654       C  
ATOM   6131  CG  LEU B 246      -3.914   5.439  54.294  1.00126.42           C  
ANISOU 6131  CG  LEU B 246    19157  17416  11458    163   1310   2703       C  
ATOM   6132  CD1 LEU B 246      -2.414   5.628  54.524  1.00127.45           C  
ANISOU 6132  CD1 LEU B 246    19362  17412  11648   -109   1321   2639       C  
ATOM   6133  CD2 LEU B 246      -4.486   6.331  53.209  1.00124.89           C  
ANISOU 6133  CD2 LEU B 246    19102  17218  11131    389   1431   2808       C  
ATOM   6134  N   PHE B 247      -6.131   3.001  56.147  1.00124.91           N  
ANISOU 6134  N   PHE B 247    18484  17584  11392    282   1046   2624       N  
ATOM   6135  CA  PHE B 247      -7.053   3.174  57.274  1.00123.35           C  
ANISOU 6135  CA  PHE B 247    18337  17370  11160    367   1054   2641       C  
ATOM   6136  C   PHE B 247      -6.597   2.340  58.447  1.00123.70           C  
ANISOU 6136  C   PHE B 247    18282  17394  11323    181    960   2567       C  
ATOM   6137  O   PHE B 247      -6.586   2.801  59.579  1.00128.13           O  
ANISOU 6137  O   PHE B 247    18970  17837  11875    140    987   2564       O  
ATOM   6138  CB  PHE B 247      -8.471   2.745  56.856  1.00125.43           C  
ANISOU 6138  CB  PHE B 247    18447  17854  11356    582   1028   2672       C  
ATOM   6139  CG  PHE B 247      -9.455   2.683  57.995  1.00128.98           C  
ANISOU 6139  CG  PHE B 247    18893  18333  11780    658   1016   2678       C  
ATOM   6140  CD1 PHE B 247     -10.159   3.809  58.374  1.00132.61           C  
ANISOU 6140  CD1 PHE B 247    19556  18714  12113    837   1120   2753       C  
ATOM   6141  CD2 PHE B 247      -9.683   1.506  58.686  1.00130.56           C  
ANISOU 6141  CD2 PHE B 247    18895  18633  12076    559    910   2611       C  
ATOM   6142  CE1 PHE B 247     -11.078   3.770  59.418  1.00129.76           C  
ANISOU 6142  CE1 PHE B 247    19189  18391  11721    914   1109   2759       C  
ATOM   6143  CE2 PHE B 247     -10.584   1.459  59.742  1.00129.20           C  
ANISOU 6143  CE2 PHE B 247    18720  18492  11877    625    901   2618       C  
ATOM   6144  CZ  PHE B 247     -11.288   2.590  60.103  1.00127.74           C  
ANISOU 6144  CZ  PHE B 247    18725  18246  11564    802    995   2690       C  
ATOM   6145  N   THR B 248      -6.245   1.095  58.151  1.00122.93           N  
ANISOU 6145  N   THR B 248    17957  17418  11331     80    857   2508       N  
ATOM   6146  CA  THR B 248      -5.799   0.129  59.152  1.00118.66           C  
ANISOU 6146  CA  THR B 248    17299  16880  10904    -75    769   2447       C  
ATOM   6147  C   THR B 248      -4.411   0.476  59.697  1.00113.41           C  
ANISOU 6147  C   THR B 248    16736  16074  10281   -270    776   2416       C  
ATOM   6148  O   THR B 248      -4.155   0.261  60.844  1.00117.81           O  
ANISOU 6148  O   THR B 248    17294  16591  10877   -363    745   2391       O  
ATOM   6149  CB  THR B 248      -5.883  -1.305  58.554  1.00116.30           C  
ANISOU 6149  CB  THR B 248    16746  16747  10695   -104    679   2399       C  
ATOM   6150  OG1 THR B 248      -7.243  -1.565  58.145  1.00115.89           O  
ANISOU 6150  OG1 THR B 248    16598  16849  10584     58    679   2414       O  
ATOM   6151  CG2 THR B 248      -5.450  -2.357  59.531  1.00112.69           C  
ANISOU 6151  CG2 THR B 248    16178  16289  10351   -241    602   2350       C  
ATOM   6152  N   LEU B 249      -3.545   1.060  58.899  1.00111.31           N  
ANISOU 6152  N   LEU B 249    16556  15745   9991   -330    825   2419       N  
ATOM   6153  CA  LEU B 249      -2.256   1.538  59.384  1.00112.05           C  
ANISOU 6153  CA  LEU B 249    16754  15721  10095   -524    848   2383       C  
ATOM   6154  C   LEU B 249      -2.418   2.768  60.259  1.00110.91           C  
ANISOU 6154  C   LEU B 249    16855  15416   9866   -528    946   2401       C  
ATOM   6155  O   LEU B 249      -1.661   2.947  61.218  1.00109.95           O  
ANISOU 6155  O   LEU B 249    16786  15231   9756   -693    945   2354       O  
ATOM   6156  CB  LEU B 249      -1.340   1.886  58.208  1.00116.32           C  
ANISOU 6156  CB  LEU B 249    17327  16245  10622   -590    886   2380       C  
ATOM   6157  CG  LEU B 249      -0.748   0.718  57.420  1.00119.18           C  
ANISOU 6157  CG  LEU B 249    17462  16746  11074   -646    794   2344       C  
ATOM   6158  CD1 LEU B 249      -0.326   1.191  56.036  1.00123.56           C  
ANISOU 6158  CD1 LEU B 249    18059  17300  11585   -630    847   2364       C  
ATOM   6159  CD2 LEU B 249       0.419   0.107  58.164  1.00118.92           C  
ANISOU 6159  CD2 LEU B 249    17338  16731  11113   -837    728   2284       C  
ATOM   6160  N   ALA B 250      -3.379   3.623  59.882  1.00110.78           N  
ANISOU 6160  N   ALA B 250    16990  15345   9754   -343   1039   2466       N  
ATOM   6161  CA  ALA B 250      -3.677   4.893  60.574  1.00111.49           C  
ANISOU 6161  CA  ALA B 250    17351  15261   9748   -307   1161   2493       C  
ATOM   6162  C   ALA B 250      -4.198   4.689  61.991  1.00112.13           C  
ANISOU 6162  C   ALA B 250    17421  15341   9843   -311   1123   2473       C  
ATOM   6163  O   ALA B 250      -3.867   5.457  62.889  1.00109.02           O  
ANISOU 6163  O   ALA B 250    17204  14807   9409   -406   1190   2447       O  
ATOM   6164  CB  ALA B 250      -4.673   5.710  59.768  1.00110.88           C  
ANISOU 6164  CB  ALA B 250    17414  15154   9559    -61   1266   2584       C  
ATOM   6165  N   THR B 251      -5.011   3.652  62.181  1.00114.03           N  
ANISOU 6165  N   THR B 251    17452  15737  10134   -217   1022   2479       N  
ATOM   6166  CA  THR B 251      -5.512   3.296  63.507  1.00116.37           C  
ANISOU 6166  CA  THR B 251    17707  16054  10452   -222    975   2462       C  
ATOM   6167  C   THR B 251      -4.409   2.804  64.419  1.00117.59           C  
ANISOU 6167  C   THR B 251    17796  16200  10684   -448    910   2393       C  
ATOM   6168  O   THR B 251      -4.485   2.981  65.614  1.00116.38           O  
ANISOU 6168  O   THR B 251    17695  16004  10517   -495    911   2373       O  
ATOM   6169  CB  THR B 251      -6.549   2.171  63.452  1.00119.18           C  
ANISOU 6169  CB  THR B 251    17839  16591  10850   -101    884   2475       C  
ATOM   6170  OG1 THR B 251      -6.004   1.034  62.761  1.00122.39           O  
ANISOU 6170  OG1 THR B 251    18035  17111  11355   -184    796   2440       O  
ATOM   6171  CG2 THR B 251      -7.779   2.641  62.777  1.00122.07           C  
ANISOU 6171  CG2 THR B 251    18247  17014  11118    133    942   2540       C  
ATOM   6172  N   PHE B 252      -3.404   2.144  63.856  1.00119.72           N  
ANISOU 6172  N   PHE B 252    17933  16528  11024   -575    852   2358       N  
ATOM   6173  CA  PHE B 252      -2.283   1.645  64.643  1.00121.50           C  
ANISOU 6173  CA  PHE B 252    18077  16780  11307   -773    790   2299       C  
ATOM   6174  C   PHE B 252      -1.431   2.813  65.158  1.00122.37           C  
ANISOU 6174  C   PHE B 252    18392  16759  11344   -928    878   2259       C  
ATOM   6175  O   PHE B 252      -1.035   2.842  66.332  1.00118.39           O  
ANISOU 6175  O   PHE B 252    17895  16254  10832  -1044    862   2217       O  
ATOM   6176  CB  PHE B 252      -1.432   0.658  63.819  1.00122.54           C  
ANISOU 6176  CB  PHE B 252    18017  17018  11521   -847    715   2277       C  
ATOM   6177  CG  PHE B 252      -1.897  -0.783  63.910  1.00122.69           C  
ANISOU 6177  CG  PHE B 252    17813  17168  11634   -785    616   2282       C  
ATOM   6178  CD1 PHE B 252      -1.547  -1.571  64.989  1.00119.75           C  
ANISOU 6178  CD1 PHE B 252    17334  16848  11315   -859    550   2262       C  
ATOM   6179  CD2 PHE B 252      -2.637  -1.368  62.883  1.00123.54           C  
ANISOU 6179  CD2 PHE B 252    17817  17351  11771   -660    597   2303       C  
ATOM   6180  CE1 PHE B 252      -1.939  -2.891  65.061  1.00121.31           C  
ANISOU 6180  CE1 PHE B 252    17353  17141  11599   -808    480   2269       C  
ATOM   6181  CE2 PHE B 252      -3.049  -2.695  62.948  1.00119.30           C  
ANISOU 6181  CE2 PHE B 252    17091  16920  11318   -628    524   2295       C  
ATOM   6182  CZ  PHE B 252      -2.700  -3.453  64.036  1.00121.08           C  
ANISOU 6182  CZ  PHE B 252    17235  17166  11600   -701    471   2280       C  
ATOM   6183  N   VAL B 253      -1.138   3.768  64.276  1.00123.49           N  
ANISOU 6183  N   VAL B 253    18698  16796  11424   -939    978   2268       N  
ATOM   6184  CA  VAL B 253      -0.315   4.927  64.654  1.00123.53           C  
ANISOU 6184  CA  VAL B 253    18920  16663  11353  -1109   1085   2219       C  
ATOM   6185  C   VAL B 253      -1.059   5.889  65.587  1.00128.56           C  
ANISOU 6185  C   VAL B 253    19777  17158  11908  -1053   1181   2226       C  
ATOM   6186  O   VAL B 253      -0.433   6.545  66.433  1.00134.32           O  
ANISOU 6186  O   VAL B 253    20636  17810  12589  -1227   1239   2160       O  
ATOM   6187  CB  VAL B 253       0.288   5.692  63.434  1.00118.69           C  
ANISOU 6187  CB  VAL B 253    18441  15960  10694  -1156   1183   2225       C  
ATOM   6188  CG1 VAL B 253       1.269   4.817  62.670  1.00115.56           C  
ANISOU 6188  CG1 VAL B 253    17834  15704  10369  -1258   1092   2198       C  
ATOM   6189  CG2 VAL B 253      -0.778   6.245  62.506  1.00116.92           C  
ANISOU 6189  CG2 VAL B 253    18345  15659  10419   -919   1266   2314       C  
ATOM   6190  N   ALA B 254      -2.383   5.970  65.431  1.00131.71           N  
ANISOU 6190  N   ALA B 254    20214  17542  12285   -815   1200   2300       N  
ATOM   6191  CA  ALA B 254      -3.228   6.789  66.310  1.00133.19           C  
ANISOU 6191  CA  ALA B 254    20595  17614  12395   -721   1286   2317       C  
ATOM   6192  C   ALA B 254      -3.199   6.290  67.763  1.00134.83           C  
ANISOU 6192  C   ALA B 254    20707  17886  12633   -813   1207   2267       C  
ATOM   6193  O   ALA B 254      -3.104   7.084  68.696  1.00137.56           O  
ANISOU 6193  O   ALA B 254    21227  18122  12915   -893   1284   2225       O  
ATOM   6194  CB  ALA B 254      -4.650   6.839  65.777  1.00130.16           C  
ANISOU 6194  CB  ALA B 254    20225  17255  11974   -429   1308   2411       C  
ATOM   6195  N   ASP B 255      -3.243   4.976  67.934  1.00136.66           N  
ANISOU 6195  N   ASP B 255    20670  18295  12960   -807   1063   2268       N  
ATOM   6196  CA  ASP B 255      -3.172   4.316  69.242  1.00143.20           C  
ANISOU 6196  CA  ASP B 255    21373  19210  13824   -883    978   2233       C  
ATOM   6197  C   ASP B 255      -1.840   3.531  69.367  1.00148.27           C  
ANISOU 6197  C   ASP B 255    21839  19966  14530  -1083    890   2177       C  
ATOM   6198  O   ASP B 255      -1.834   2.433  69.918  1.00157.11           O  
ANISOU 6198  O   ASP B 255    22759  21217  15717  -1083    785   2181       O  
ATOM   6199  CB  ASP B 255      -4.391   3.383  69.317  1.00143.43           C  
ANISOU 6199  CB  ASP B 255    21241  19352  13902   -692    898   2292       C  
ATOM   6200  CG  ASP B 255      -4.609   2.747  70.674  1.00143.32           C  
ANISOU 6200  CG  ASP B 255    21122  19415  13916   -722    826   2277       C  
ATOM   6201  OD1 ASP B 255      -4.815   3.474  71.664  1.00156.77           O  
ANISOU 6201  OD1 ASP B 255    22966  21045  15554   -741    879   2258       O  
ATOM   6202  OD2 ASP B 255      -4.626   1.504  70.727  1.00135.89           O  
ANISOU 6202  OD2 ASP B 255    19964  18605  13062   -716    724   2288       O  
ATOM   6203  N   TRP B 256      -0.738   4.087  68.833  1.00148.39           N  
ANISOU 6203  N   TRP B 256    21930  19935  14515  -1242    942   2131       N  
ATOM   6204  CA  TRP B 256       0.608   3.460  68.835  1.00149.68           C  
ANISOU 6204  CA  TRP B 256    21930  20225  14715  -1428    871   2077       C  
ATOM   6205  C   TRP B 256       1.143   2.886  70.181  1.00161.16           C  
ANISOU 6205  C   TRP B 256    23251  21807  16173  -1542    795   2034       C  
ATOM   6206  O   TRP B 256       1.814   1.839  70.178  1.00162.75           O  
ANISOU 6206  O   TRP B 256    23239  22163  16433  -1583    698   2032       O  
ATOM   6207  CB  TRP B 256       1.636   4.433  68.253  1.00146.51           C  
ANISOU 6207  CB  TRP B 256    21675  19742  14247  -1603    967   2021       C  
ATOM   6208  CG  TRP B 256       2.947   3.794  67.915  1.00148.19           C  
ANISOU 6208  CG  TRP B 256    21710  20104  14491  -1760    898   1978       C  
ATOM   6209  CD1 TRP B 256       4.163   4.047  68.497  1.00151.27           C  
ANISOU 6209  CD1 TRP B 256    22080  20572  14823  -1993    905   1892       C  
ATOM   6210  CD2 TRP B 256       3.185   2.791  66.919  1.00147.71           C  
ANISOU 6210  CD2 TRP B 256    21458  20151  14515  -1694    815   2015       C  
ATOM   6211  NE1 TRP B 256       5.141   3.263  67.922  1.00149.47           N  
ANISOU 6211  NE1 TRP B 256    21654  20501  14634  -2061    829   1881       N  
ATOM   6212  CE2 TRP B 256       4.567   2.484  66.952  1.00148.73           C  
ANISOU 6212  CE2 TRP B 256    21462  20415  14633  -1878    775   1956       C  
ATOM   6213  CE3 TRP B 256       2.366   2.120  65.999  1.00143.35           C  
ANISOU 6213  CE3 TRP B 256    20821  19607  14035  -1500    774   2085       C  
ATOM   6214  CZ2 TRP B 256       5.146   1.542  66.092  1.00147.60           C  
ANISOU 6214  CZ2 TRP B 256    21128  20396  14557  -1860    699   1973       C  
ATOM   6215  CZ3 TRP B 256       2.944   1.173  65.149  1.00138.93           C  
ANISOU 6215  CZ3 TRP B 256    20075  19165  13546  -1500    701   2092       C  
ATOM   6216  CH2 TRP B 256       4.316   0.898  65.199  1.00141.49           C  
ANISOU 6216  CH2 TRP B 256    20292  19603  13864  -1671    666   2039       C  
ATOM   6217  N   ARG B 257       0.856   3.558  71.304  1.00167.22           N  
ANISOU 6217  N   ARG B 257    24146  22517  16873  -1583    844   2002       N  
ATOM   6218  CA  ARG B 257       1.291   3.086  72.640  1.00168.65           C  
ANISOU 6218  CA  ARG B 257    24206  22831  17039  -1680    778   1963       C  
ATOM   6219  C   ARG B 257       0.750   1.713  73.001  1.00167.59           C  
ANISOU 6219  C   ARG B 257    23854  22823  16996  -1538    660   2030       C  
ATOM   6220  O   ARG B 257       1.491   0.873  73.522  1.00170.84           O  
ANISOU 6220  O   ARG B 257    24086  23394  17430  -1603    581   2021       O  
ATOM   6221  CB  ARG B 257       0.876   4.060  73.737  1.00175.78           C  
ANISOU 6221  CB  ARG B 257    25295  23640  17853  -1722    857   1920       C  
ATOM   6222  CG  ARG B 257       1.889   5.159  73.977  1.00183.98           C  
ANISOU 6222  CG  ARG B 257    26488  24630  18786  -1965    955   1813       C  
ATOM   6223  CD  ARG B 257       2.762   4.914  75.206  1.00188.79           C  
ANISOU 6223  CD  ARG B 257    26971  25418  19340  -2145    904   1736       C  
ATOM   6224  NE  ARG B 257       4.070   5.580  75.044  1.00199.97           N  
ANISOU 6224  NE  ARG B 257    28434  26873  20670  -2408    966   1628       N  
ATOM   6225  CZ  ARG B 257       4.322   6.894  75.161  1.00206.05           C  
ANISOU 6225  CZ  ARG B 257    29452  27498  21339  -2578   1111   1536       C  
ATOM   6226  NH1 ARG B 257       3.360   7.764  75.481  1.00215.74           N  
ANISOU 6226  NH1 ARG B 257    30925  28515  22532  -2499   1217   1540       N  
ATOM   6227  NH2 ARG B 257       5.562   7.352  74.964  1.00198.23           N  
ANISOU 6227  NH2 ARG B 257    28470  26575  20273  -2835   1160   1433       N  
ATOM   6228  N   ASN B 258      -0.535   1.497  72.717  1.00166.53           N  
ANISOU 6228  N   ASN B 258    23742  22625  16906  -1343    659   2097       N  
ATOM   6229  CA  ASN B 258      -1.191   0.193  72.912  1.00167.49           C  
ANISOU 6229  CA  ASN B 258    23676  22846  17117  -1211    567   2158       C  
ATOM   6230  C   ASN B 258      -1.077  -0.759  71.667  1.00166.80           C  
ANISOU 6230  C   ASN B 258    23443  22810  17121  -1148    518   2192       C  
ATOM   6231  O   ASN B 258      -1.003  -1.990  71.815  1.00172.60           O  
ANISOU 6231  O   ASN B 258    23998  23647  17932  -1115    443   2220       O  
ATOM   6232  CB  ASN B 258      -2.657   0.414  73.313  1.00162.42           C  
ANISOU 6232  CB  ASN B 258    23112  22139  16460  -1050    593   2200       C  
ATOM   6233  CG  ASN B 258      -3.306  -0.838  73.885  1.00169.11           C  
ANISOU 6233  CG  ASN B 258    23784  23089  17378   -956    512   2247       C  
ATOM   6234  OD1 ASN B 258      -3.024  -1.228  75.018  1.00181.20           O  
ANISOU 6234  OD1 ASN B 258    25248  24693  18905  -1008    473   2242       O  
ATOM   6235  ND2 ASN B 258      -4.158  -1.489  73.101  1.00168.42           N  
ANISOU 6235  ND2 ASN B 258    23621  23018  17351   -825    492   2291       N  
ATOM   6236  N   SER B 259      -1.010  -0.183  70.468  1.00157.06           N  
ANISOU 6236  N   SER B 259    22296  21502  15876  -1138    569   2189       N  
ATOM   6237  CA  SER B 259      -0.998  -0.934  69.229  1.00153.67           C  
ANISOU 6237  CA  SER B 259    21751  21116  15520  -1075    535   2213       C  
ATOM   6238  C   SER B 259       0.251  -1.776  69.101  1.00151.82           C  
ANISOU 6238  C   SER B 259    21356  20993  15335  -1183    472   2192       C  
ATOM   6239  O   SER B 259       0.153  -2.968  68.789  1.00164.02           O  
ANISOU 6239  O   SER B 259    22741  22614  16965  -1119    412   2218       O  
ATOM   6240  CB  SER B 259      -1.003   0.004  68.013  1.00156.54           C  
ANISOU 6240  CB  SER B 259    22253  21384  15840  -1058    612   2212       C  
ATOM   6241  OG  SER B 259      -2.208   0.719  67.870  1.00166.84           O  
ANISOU 6241  OG  SER B 259    23696  22599  17093   -913    677   2249       O  
ATOM   6242  N   ASN B 260       1.416  -1.151  69.311  1.00142.18           N  
ANISOU 6242  N   ASN B 260    20181  19787  14052  -1346    495   2140       N  
ATOM   6243  CA  ASN B 260       2.718  -1.787  69.030  1.00135.16           C  
ANISOU 6243  CA  ASN B 260    19145  19024  13186  -1448    445   2117       C  
ATOM   6244  C   ASN B 260       3.039  -2.887  70.060  1.00136.82           C  
ANISOU 6244  C   ASN B 260    19185  19372  13428  -1439    368   2136       C  
ATOM   6245  O   ASN B 260       3.936  -2.758  70.867  1.00144.93           O  
ANISOU 6245  O   ASN B 260    20173  20499  14393  -1556    355   2102       O  
ATOM   6246  CB  ASN B 260       3.804  -0.707  68.963  1.00130.88           C  
ANISOU 6246  CB  ASN B 260    18705  18474  12548  -1638    503   2048       C  
ATOM   6247  CG  ASN B 260       5.168  -1.250  68.568  1.00129.53           C  
ANISOU 6247  CG  ASN B 260    18380  18455  12380  -1744    458   2020       C  
ATOM   6248  OD1 ASN B 260       5.366  -1.733  67.461  1.00133.19           O  
ANISOU 6248  OD1 ASN B 260    18771  18934  12899  -1698    439   2039       O  
ATOM   6249  ND2 ASN B 260       6.127  -1.113  69.452  1.00132.44           N  
ANISOU 6249  ND2 ASN B 260    18697  18948  12674  -1889    445   1971       N  
ATOM   6250  N   ARG B 261       2.264  -3.969  70.039  1.00135.21           N  
ANISOU 6250  N   ARG B 261    18883  19178  13313  -1299    327   2190       N  
ATOM   6251  CA  ARG B 261       2.381  -5.043  71.011  1.00133.44           C  
ANISOU 6251  CA  ARG B 261    18523  19054  13122  -1260    272   2226       C  
ATOM   6252  C   ARG B 261       1.951  -6.337  70.362  1.00127.09           C  
ANISOU 6252  C   ARG B 261    17604  18255  12428  -1141    244   2270       C  
ATOM   6253  O   ARG B 261       0.832  -6.418  69.873  1.00123.00           O  
ANISOU 6253  O   ARG B 261    17124  17657  11952  -1053    261   2284       O  
ATOM   6254  CB  ARG B 261       1.488  -4.750  72.217  1.00142.75           C  
ANISOU 6254  CB  ARG B 261    19771  20197  14269  -1222    282   2241       C  
ATOM   6255  CG  ARG B 261       2.186  -4.063  73.384  1.00158.69           C  
ANISOU 6255  CG  ARG B 261    21824  22283  16185  -1344    287   2201       C  
ATOM   6256  CD  ARG B 261       1.484  -4.331  74.716  1.00172.78           C  
ANISOU 6256  CD  ARG B 261    23600  24089  17959  -1285    271   2234       C  
ATOM   6257  NE  ARG B 261       0.471  -3.321  75.064  1.00187.56           N  
ANISOU 6257  NE  ARG B 261    25639  25839  19786  -1266    323   2217       N  
ATOM   6258  CZ  ARG B 261       0.693  -2.202  75.768  1.00201.74           C  
ANISOU 6258  CZ  ARG B 261    27559  27612  21479  -1372    367   2160       C  
ATOM   6259  NH1 ARG B 261       1.908  -1.891  76.226  1.00207.82           N  
ANISOU 6259  NH1 ARG B 261    28296  28492  22173  -1529    363   2103       N  
ATOM   6260  NH2 ARG B 261      -0.319  -1.375  76.027  1.00209.42           N  
ANISOU 6260  NH2 ARG B 261    28691  28462  22417  -1323    421   2155       N  
ATOM   6261  N   TYR B 262       2.830  -7.339  70.392  1.00127.48           N  
ANISOU 6261  N   TYR B 262    17515  18408  12511  -1139    207   2289       N  
ATOM   6262  CA  TYR B 262       2.594  -8.640  69.744  1.00130.39           C  
ANISOU 6262  CA  TYR B 262    17785  18773  12985  -1041    196   2323       C  
ATOM   6263  C   TYR B 262       1.382  -9.354  70.346  1.00128.61           C  
ANISOU 6263  C   TYR B 262    17556  18495  12815   -943    202   2364       C  
ATOM   6264  O   TYR B 262       1.145  -9.218  71.522  1.00132.36           O  
ANISOU 6264  O   TYR B 262    18051  18987  13253   -940    197   2386       O  
ATOM   6265  CB  TYR B 262       3.841  -9.541  69.840  1.00132.48           C  
ANISOU 6265  CB  TYR B 262    17917  19160  13258  -1042    168   2345       C  
ATOM   6266  CG  TYR B 262       4.925  -9.107  68.877  1.00141.53           C  
ANISOU 6266  CG  TYR B 262    19039  20363  14370  -1124    164   2302       C  
ATOM   6267  CD1 TYR B 262       5.828  -8.079  69.195  1.00144.99           C  
ANISOU 6267  CD1 TYR B 262    19506  20881  14702  -1256    162   2259       C  
ATOM   6268  CD2 TYR B 262       5.025  -9.700  67.611  1.00151.31           C  
ANISOU 6268  CD2 TYR B 262    20232  21579  15680  -1083    169   2296       C  
ATOM   6269  CE1 TYR B 262       6.814  -7.682  68.289  1.00153.18           C  
ANISOU 6269  CE1 TYR B 262    20520  21976  15703  -1344    165   2217       C  
ATOM   6270  CE2 TYR B 262       5.993  -9.303  66.694  1.00157.44           C  
ANISOU 6270  CE2 TYR B 262    20983  22410  16423  -1157    166   2258       C  
ATOM   6271  CZ  TYR B 262       6.887  -8.299  67.032  1.00160.83           C  
ANISOU 6271  CZ  TYR B 262    21439  22921  16748  -1287    164   2221       C  
ATOM   6272  OH  TYR B 262       7.846  -7.940  66.097  1.00175.45           O  
ANISOU 6272  OH  TYR B 262    23263  24833  18565  -1370    167   2182       O  
ATOM   6273  N   PRO B 263       0.578 -10.073  69.572  1.00131.72           N  
ANISOU 6273  N   PRO B 263    17924  18832  13289   -873    218   2367       N  
ATOM   6274  CA  PRO B 263       0.694 -10.255  68.127  1.00132.86           C  
ANISOU 6274  CA  PRO B 263    18043  18961  13477   -871    228   2336       C  
ATOM   6275  C   PRO B 263      -0.015  -9.209  67.238  1.00123.81           C  
ANISOU 6275  C   PRO B 263    16985  17761  12294   -874    249   2300       C  
ATOM   6276  O   PRO B 263       0.170  -9.267  66.030  1.00110.97           O  
ANISOU 6276  O   PRO B 263    15335  16137  10689   -874    256   2274       O  
ATOM   6277  CB  PRO B 263       0.055 -11.636  67.920  1.00135.72           C  
ANISOU 6277  CB  PRO B 263    18334  19299  13934   -800    246   2351       C  
ATOM   6278  CG  PRO B 263      -1.013 -11.690  68.954  1.00139.28           C  
ANISOU 6278  CG  PRO B 263    18820  19720  14379   -764    256   2377       C  
ATOM   6279  CD  PRO B 263      -0.534 -10.858  70.125  1.00137.00           C  
ANISOU 6279  CD  PRO B 263    18579  19465  14009   -800    233   2398       C  
ATOM   6280  N   ALA B 264      -0.813  -8.302  67.816  1.00125.15           N  
ANISOU 6280  N   ALA B 264    17256  17890  12404   -861    266   2304       N  
ATOM   6281  CA  ALA B 264      -1.539  -7.286  67.023  1.00128.30           C  
ANISOU 6281  CA  ALA B 264    17752  18241  12754   -831    299   2286       C  
ATOM   6282  C   ALA B 264      -0.628  -6.437  66.116  1.00126.78           C  
ANISOU 6282  C   ALA B 264    17615  18035  12518   -896    315   2261       C  
ATOM   6283  O   ALA B 264      -1.043  -6.039  65.038  1.00131.56           O  
ANISOU 6283  O   ALA B 264    18255  18622  13110   -854    342   2252       O  
ATOM   6284  CB  ALA B 264      -2.384  -6.391  67.928  1.00128.92           C  
ANISOU 6284  CB  ALA B 264    17946  18275  12762   -799    323   2301       C  
ATOM   6285  N   VAL B 265       0.607  -6.183  66.541  1.00123.04           N  
ANISOU 6285  N   VAL B 265    17142  17590  12015  -1000    303   2248       N  
ATOM   6286  CA  VAL B 265       1.580  -5.425  65.740  1.00118.01           C  
ANISOU 6286  CA  VAL B 265    16551  16951  11333  -1088    323   2217       C  
ATOM   6287  C   VAL B 265       2.023  -6.151  64.462  1.00116.63           C  
ANISOU 6287  C   VAL B 265    16271  16822  11218  -1073    306   2208       C  
ATOM   6288  O   VAL B 265       2.387  -5.495  63.486  1.00125.82           O  
ANISOU 6288  O   VAL B 265    17486  17969  12351  -1108    333   2189       O  
ATOM   6289  CB  VAL B 265       2.839  -5.071  66.559  1.00119.94           C  
ANISOU 6289  CB  VAL B 265    16795  17256  11520  -1222    312   2194       C  
ATOM   6290  CG1 VAL B 265       3.813  -6.255  66.717  1.00123.11           C  
ANISOU 6290  CG1 VAL B 265    17025  17782  11968  -1235    258   2203       C  
ATOM   6291  CG2 VAL B 265       3.565  -3.899  65.944  1.00121.65           C  
ANISOU 6291  CG2 VAL B 265    17119  17441  11661  -1336    359   2153       C  
ATOM   6292  N   ILE B 266       2.000  -7.483  64.448  1.00111.26           N  
ANISOU 6292  N   ILE B 266    15457  16193  10622  -1021    271   2220       N  
ATOM   6293  CA  ILE B 266       2.335  -8.234  63.243  1.00107.43           C  
ANISOU 6293  CA  ILE B 266    14878  15744  10196  -1000    263   2204       C  
ATOM   6294  C   ILE B 266       1.429  -7.758  62.090  1.00113.41           C  
ANISOU 6294  C   ILE B 266    15684  16462  10943   -945    294   2191       C  
ATOM   6295  O   ILE B 266       1.902  -7.549  60.938  1.00120.02           O  
ANISOU 6295  O   ILE B 266    16510  17319  11773   -964    303   2171       O  
ATOM   6296  CB  ILE B 266       2.192  -9.740  63.478  1.00103.94           C  
ANISOU 6296  CB  ILE B 266    14318  15328   9844   -941    245   2219       C  
ATOM   6297  CG1 ILE B 266       3.322 -10.237  64.348  1.00100.77           C  
ANISOU 6297  CG1 ILE B 266    13854  14994   9440   -974    219   2242       C  
ATOM   6298  CG2 ILE B 266       2.203 -10.544  62.181  1.00104.49           C  
ANISOU 6298  CG2 ILE B 266    14307  15415   9979   -909    251   2191       C  
ATOM   6299  CD1 ILE B 266       2.951 -11.501  65.081  1.00100.68           C  
ANISOU 6299  CD1 ILE B 266    13780  14975   9496   -900    220   2278       C  
ATOM   6300  N   LEU B 267       0.147  -7.535  62.385  1.00113.98           N  
ANISOU 6300  N   LEU B 267    15807  16497  11000   -872    313   2204       N  
ATOM   6301  CA  LEU B 267      -0.787  -7.119  61.336  1.00118.13           C  
ANISOU 6301  CA  LEU B 267    16363  17024  11498   -796    343   2198       C  
ATOM   6302  C   LEU B 267      -0.549  -5.714  60.828  1.00115.16           C  
ANISOU 6302  C   LEU B 267    16123  16600  11031   -808    386   2207       C  
ATOM   6303  O   LEU B 267      -0.907  -5.375  59.680  1.00115.76           O  
ANISOU 6303  O   LEU B 267    16211  16694  11078   -751    414   2207       O  
ATOM   6304  CB  LEU B 267      -2.245  -7.327  61.761  1.00122.94           C  
ANISOU 6304  CB  LEU B 267    16968  17640  12101   -705    353   2209       C  
ATOM   6305  CG  LEU B 267      -2.595  -8.798  61.498  1.00123.27           C  
ANISOU 6305  CG  LEU B 267    16865  17738  12233   -692    335   2181       C  
ATOM   6306  CD1 LEU B 267      -2.000  -9.667  62.610  1.00120.77           C  
ANISOU 6306  CD1 LEU B 267    16507  17399  11981   -740    311   2195       C  
ATOM   6307  CD2 LEU B 267      -4.080  -8.974  61.370  1.00123.95           C  
ANISOU 6307  CD2 LEU B 267    16922  17873  12297   -613    354   2171       C  
ATOM   6308  N   PHE B 268       0.050  -4.890  61.675  1.00111.63           N  
ANISOU 6308  N   PHE B 268    15784  16095  10534   -885    402   2214       N  
ATOM   6309  CA  PHE B 268       0.481  -3.569  61.234  1.00109.94           C  
ANISOU 6309  CA  PHE B 268    15720  15814  10236   -930    461   2215       C  
ATOM   6310  C   PHE B 268       1.551  -3.660  60.123  1.00110.34           C  
ANISOU 6310  C   PHE B 268    15719  15906  10299  -1000    457   2192       C  
ATOM   6311  O   PHE B 268       1.398  -3.053  59.041  1.00105.27           O  
ANISOU 6311  O   PHE B 268    15138  15242   9615   -961    502   2202       O  
ATOM   6312  CB  PHE B 268       0.961  -2.778  62.423  1.00107.17           C  
ANISOU 6312  CB  PHE B 268    15488  15402   9830  -1028    484   2208       C  
ATOM   6313  CG  PHE B 268       1.762  -1.597  62.061  1.00107.00           C  
ANISOU 6313  CG  PHE B 268    15609  15313   9730  -1132    550   2190       C  
ATOM   6314  CD1 PHE B 268       1.142  -0.421  61.698  1.00107.06           C  
ANISOU 6314  CD1 PHE B 268    15806  15210   9661  -1073    639   2214       C  
ATOM   6315  CD2 PHE B 268       3.153  -1.660  62.111  1.00110.06           C  
ANISOU 6315  CD2 PHE B 268    15947  15756  10114  -1290    531   2149       C  
ATOM   6316  CE1 PHE B 268       1.889   0.679  61.377  1.00110.96           C  
ANISOU 6316  CE1 PHE B 268    16457  15619  10081  -1181    719   2196       C  
ATOM   6317  CE2 PHE B 268       3.911  -0.566  61.782  1.00112.56           C  
ANISOU 6317  CE2 PHE B 268    16399  16014  10353  -1413    603   2122       C  
ATOM   6318  CZ  PHE B 268       3.280   0.609  61.411  1.00113.12           C  
ANISOU 6318  CZ  PHE B 268    16678  15946  10355  -1365    702   2145       C  
ATOM   6319  N   TYR B 269       2.601  -4.445  60.401  1.00109.31           N  
ANISOU 6319  N   TYR B 269    15469  15845  10217  -1089    405   2168       N  
ATOM   6320  CA  TYR B 269       3.663  -4.751  59.411  1.00107.70           C  
ANISOU 6320  CA  TYR B 269    15181  15706  10031  -1150    391   2144       C  
ATOM   6321  C   TYR B 269       3.145  -5.462  58.179  1.00106.68           C  
ANISOU 6321  C   TYR B 269    14959  15620   9956  -1053    380   2142       C  
ATOM   6322  O   TYR B 269       3.541  -5.153  57.050  1.00107.85           O  
ANISOU 6322  O   TYR B 269    15109  15785  10081  -1066    400   2133       O  
ATOM   6323  CB  TYR B 269       4.785  -5.557  60.051  1.00105.34           C  
ANISOU 6323  CB  TYR B 269    14760  15496   9766  -1230    338   2127       C  
ATOM   6324  CG  TYR B 269       5.554  -4.679  60.981  1.00108.67           C  
ANISOU 6324  CG  TYR B 269    15264  15916  10107  -1360    356   2111       C  
ATOM   6325  CD1 TYR B 269       6.377  -3.697  60.492  1.00113.03           C  
ANISOU 6325  CD1 TYR B 269    15898  16462  10586  -1481    400   2083       C  
ATOM   6326  CD2 TYR B 269       5.419  -4.770  62.343  1.00113.78           C  
ANISOU 6326  CD2 TYR B 269    15916  16569  10743  -1374    339   2119       C  
ATOM   6327  CE1 TYR B 269       7.092  -2.843  61.330  1.00116.77           C  
ANISOU 6327  CE1 TYR B 269    16453  16940  10973  -1631    430   2050       C  
ATOM   6328  CE2 TYR B 269       6.121  -3.913  63.197  1.00117.91           C  
ANISOU 6328  CE2 TYR B 269    16513  17106  11178  -1511    361   2090       C  
ATOM   6329  CZ  TYR B 269       6.955  -2.944  62.673  1.00119.19           C  
ANISOU 6329  CZ  TYR B 269    16755  17264  11265  -1647    409   2049       C  
ATOM   6330  OH  TYR B 269       7.692  -2.090  63.457  1.00128.42           O  
ANISOU 6330  OH  TYR B 269    17997  18456  12338  -1812    443   2002       O  
ATOM   6331  N   VAL B 270       2.253  -6.416  58.395  1.00106.12           N  
ANISOU 6331  N   VAL B 270    14804  15569   9947   -966    354   2145       N  
ATOM   6332  CA  VAL B 270       1.545  -7.022  57.267  1.00105.26           C  
ANISOU 6332  CA  VAL B 270    14612  15509   9872   -881    355   2129       C  
ATOM   6333  C   VAL B 270       0.806  -5.992  56.419  1.00103.92           C  
ANISOU 6333  C   VAL B 270    14537  15325   9622   -810    404   2147       C  
ATOM   6334  O   VAL B 270       0.961  -5.985  55.217  1.00100.23           O  
ANISOU 6334  O   VAL B 270    14031  14906   9144   -791    414   2135       O  
ATOM   6335  CB  VAL B 270       0.601  -8.142  57.755  1.00105.32           C  
ANISOU 6335  CB  VAL B 270    14532  15537   9946   -821    335   2119       C  
ATOM   6336  CG1 VAL B 270      -0.475  -8.484  56.725  1.00104.36           C  
ANISOU 6336  CG1 VAL B 270    14349  15478   9825   -739    351   2094       C  
ATOM   6337  CG2 VAL B 270       1.433  -9.376  58.116  1.00106.08           C  
ANISOU 6337  CG2 VAL B 270    14520  15656  10128   -866    302   2104       C  
ATOM   6338  N   ASN B 271       0.016  -5.127  57.047  1.00108.42           N  
ANISOU 6338  N   ASN B 271    15232  15834  10127   -758    439   2182       N  
ATOM   6339  CA  ASN B 271      -0.721  -4.095  56.296  1.00115.05           C  
ANISOU 6339  CA  ASN B 271    16179  16660  10875   -658    499   2216       C  
ATOM   6340  C   ASN B 271       0.215  -3.079  55.614  1.00118.18           C  
ANISOU 6340  C   ASN B 271    16690  17000  11212   -718    550   2229       C  
ATOM   6341  O   ASN B 271      -0.095  -2.584  54.530  1.00118.65           O  
ANISOU 6341  O   ASN B 271    16784  17083  11214   -638    593   2252       O  
ATOM   6342  CB  ASN B 271      -1.720  -3.345  57.185  1.00116.74           C  
ANISOU 6342  CB  ASN B 271    16519  16813  11024   -577    537   2255       C  
ATOM   6343  CG  ASN B 271      -3.097  -3.981  57.184  1.00116.39           C  
ANISOU 6343  CG  ASN B 271    16375  16862  10983   -455    520   2255       C  
ATOM   6344  OD1 ASN B 271      -4.040  -3.415  56.632  1.00120.64           O  
ANISOU 6344  OD1 ASN B 271    16953  17445  11436   -323    562   2287       O  
ATOM   6345  ND2 ASN B 271      -3.215  -5.165  57.775  1.00111.47           N  
ANISOU 6345  ND2 ASN B 271    15623  16282  10447   -498    465   2220       N  
ATOM   6346  N   ALA B 272       1.352  -2.785  56.251  1.00117.36           N  
ANISOU 6346  N   ALA B 272    16640  16838  11114   -861    549   2213       N  
ATOM   6347  CA  ALA B 272       2.388  -1.933  55.641  1.00113.92           C  
ANISOU 6347  CA  ALA B 272    16298  16359  10625   -959    598   2211       C  
ATOM   6348  C   ALA B 272       2.899  -2.489  54.295  1.00110.22           C  
ANISOU 6348  C   ALA B 272    15705  15986  10187   -958    575   2192       C  
ATOM   6349  O   ALA B 272       3.031  -1.748  53.299  1.00113.38           O  
ANISOU 6349  O   ALA B 272    16184  16367  10525   -940    633   2214       O  
ATOM   6350  CB  ALA B 272       3.548  -1.768  56.614  1.00116.00           C  
ANISOU 6350  CB  ALA B 272    16588  16598  10889  -1133    587   2177       C  
ATOM   6351  N   CYS B 273       3.192  -3.789  54.286  1.00106.31           N  
ANISOU 6351  N   CYS B 273    15023  15586   9781   -975    498   2155       N  
ATOM   6352  CA  CYS B 273       3.613  -4.502  53.082  1.00106.47           C  
ANISOU 6352  CA  CYS B 273    14908  15703   9840   -968    471   2128       C  
ATOM   6353  C   CYS B 273       2.596  -4.416  51.956  1.00110.77           C  
ANISOU 6353  C   CYS B 273    15439  16296  10353   -834    497   2144       C  
ATOM   6354  O   CYS B 273       2.948  -4.096  50.801  1.00118.88           O  
ANISOU 6354  O   CYS B 273    16465  17361  11344   -827    523   2147       O  
ATOM   6355  CB  CYS B 273       3.877  -5.977  53.396  1.00106.27           C  
ANISOU 6355  CB  CYS B 273    14709  15749   9917   -981    401   2089       C  
ATOM   6356  SG  CYS B 273       5.328  -6.243  54.422  1.00104.63           S  
ANISOU 6356  SG  CYS B 273    14468  15553   9731  -1119    365   2075       S  
ATOM   6357  N   PHE B 274       1.333  -4.685  52.270  1.00114.10           N  
ANISOU 6357  N   PHE B 274    15841  16735  10776   -726    493   2153       N  
ATOM   6358  CA  PHE B 274       0.263  -4.562  51.271  1.00112.56           C  
ANISOU 6358  CA  PHE B 274    15617  16623  10525   -588    520   2166       C  
ATOM   6359  C   PHE B 274      -0.007  -3.104  50.887  1.00112.73           C  
ANISOU 6359  C   PHE B 274    15819  16584  10426   -511    602   2235       C  
ATOM   6360  O   PHE B 274      -0.440  -2.831  49.784  1.00115.68           O  
ANISOU 6360  O   PHE B 274    16179  17038  10737   -409    634   2257       O  
ATOM   6361  CB  PHE B 274      -1.012  -5.282  51.733  1.00112.01           C  
ANISOU 6361  CB  PHE B 274    15463  16619  10477   -506    495   2148       C  
ATOM   6362  CG  PHE B 274      -0.886  -6.796  51.736  1.00112.99           C  
ANISOU 6362  CG  PHE B 274    15410  16809  10709   -563    440   2077       C  
ATOM   6363  CD1 PHE B 274      -1.080  -7.527  50.577  1.00115.75           C  
ANISOU 6363  CD1 PHE B 274    15623  17282  11073   -542    431   2024       C  
ATOM   6364  CD2 PHE B 274      -0.580  -7.491  52.887  1.00113.60           C  
ANISOU 6364  CD2 PHE B 274    15467  16825  10869   -635    406   2062       C  
ATOM   6365  CE1 PHE B 274      -0.978  -8.923  50.570  1.00114.18           C  
ANISOU 6365  CE1 PHE B 274    15287  17122  10973   -598    400   1953       C  
ATOM   6366  CE2 PHE B 274      -0.471  -8.882  52.889  1.00112.06           C  
ANISOU 6366  CE2 PHE B 274    15137  16670  10771   -674    376   2005       C  
ATOM   6367  CZ  PHE B 274      -0.672  -9.601  51.728  1.00111.73           C  
ANISOU 6367  CZ  PHE B 274    14976  16729  10746   -660    378   1947       C  
ATOM   6368  N   PHE B 275       0.265  -2.158  51.781  1.00114.13           N  
ANISOU 6368  N   PHE B 275    16174  16622  10567   -557    647   2271       N  
ATOM   6369  CA  PHE B 275       0.149  -0.734  51.413  1.00118.47           C  
ANISOU 6369  CA  PHE B 275    16932  17078  11003   -495    749   2337       C  
ATOM   6370  C   PHE B 275       1.247  -0.282  50.435  1.00118.06           C  
ANISOU 6370  C   PHE B 275    16921  17007  10926   -578    788   2339       C  
ATOM   6371  O   PHE B 275       0.966   0.398  49.429  1.00119.35           O  
ANISOU 6371  O   PHE B 275    17159  17181  11005   -475    856   2391       O  
ATOM   6372  CB  PHE B 275       0.158   0.182  52.661  1.00119.82           C  
ANISOU 6372  CB  PHE B 275    17302  17086  11136   -539    804   2362       C  
ATOM   6373  CG  PHE B 275       0.042   1.652  52.332  1.00119.82           C  
ANISOU 6373  CG  PHE B 275    17549  16958  11019   -476    933   2430       C  
ATOM   6374  CD1 PHE B 275      -1.178   2.173  51.904  1.00123.18           C  
ANISOU 6374  CD1 PHE B 275    18044  17407  11352   -257    993   2502       C  
ATOM   6375  CD2 PHE B 275       1.145   2.495  52.407  1.00116.28           C  
ANISOU 6375  CD2 PHE B 275    17261  16377  10541   -632   1003   2423       C  
ATOM   6376  CE1 PHE B 275      -1.296   3.511  51.577  1.00124.19           C  
ANISOU 6376  CE1 PHE B 275    18416  17404  11365   -174   1128   2577       C  
ATOM   6377  CE2 PHE B 275       1.029   3.831  52.081  1.00117.42           C  
ANISOU 6377  CE2 PHE B 275    17657  16380  10577   -577   1142   2486       C  
ATOM   6378  CZ  PHE B 275      -0.186   4.344  51.669  1.00120.97           C  
ANISOU 6378  CZ  PHE B 275    18192  16831  10939   -339   1209   2569       C  
ATOM   6379  N   VAL B 276       2.497  -0.608  50.786  1.00115.11           N  
ANISOU 6379  N   VAL B 276    16506  16614  10614   -761    749   2288       N  
ATOM   6380  CA  VAL B 276       3.653  -0.262  49.937  1.00111.93           C  
ANISOU 6380  CA  VAL B 276    16124  16213  10191   -869    778   2278       C  
ATOM   6381  C   VAL B 276       3.493  -0.947  48.580  1.00114.81           C  
ANISOU 6381  C   VAL B 276    16328  16722  10571   -783    744   2270       C  
ATOM   6382  O   VAL B 276       3.666  -0.293  47.541  1.00116.16           O  
ANISOU 6382  O   VAL B 276    16565  16895  10673   -749    807   2306       O  
ATOM   6383  CB  VAL B 276       4.986  -0.661  50.609  1.00106.96           C  
ANISOU 6383  CB  VAL B 276    15432  15589   9618  -1071    729   2217       C  
ATOM   6384  CG1 VAL B 276       6.155  -0.609  49.648  1.00104.63           C  
ANISOU 6384  CG1 VAL B 276    15093  15348   9311  -1176    737   2195       C  
ATOM   6385  CG2 VAL B 276       5.242   0.236  51.802  1.00108.22           C  
ANISOU 6385  CG2 VAL B 276    15769  15616   9733  -1177    783   2218       C  
ATOM   6386  N   GLY B 277       3.128  -2.243  48.603  1.00115.91           N  
ANISOU 6386  N   GLY B 277    16267  16977  10795   -748    655   2222       N  
ATOM   6387  CA  GLY B 277       2.844  -2.994  47.368  1.00118.58           C  
ANISOU 6387  CA  GLY B 277    16442  17464  11148   -671    624   2197       C  
ATOM   6388  C   GLY B 277       1.819  -2.339  46.449  1.00121.70           C  
ANISOU 6388  C   GLY B 277    16886  17914  11439   -500    684   2254       C  
ATOM   6389  O   GLY B 277       2.014  -2.279  45.216  1.00122.74           O  
ANISOU 6389  O   GLY B 277    16969  18134  11531   -463    701   2259       O  
ATOM   6390  N   SER B 278       0.737  -1.847  47.055  1.00120.16           N  
ANISOU 6390  N   SER B 278    16783  17680  11190   -387    718   2300       N  
ATOM   6391  CA  SER B 278      -0.330  -1.201  46.305  1.00119.25           C  
ANISOU 6391  CA  SER B 278    16714  17638  10956   -193    779   2365       C  
ATOM   6392  C   SER B 278       0.112   0.076  45.618  1.00123.11           C  
ANISOU 6392  C   SER B 278    17392  18040  11344   -158    883   2445       C  
ATOM   6393  O   SER B 278      -0.397   0.418  44.538  1.00126.61           O  
ANISOU 6393  O   SER B 278    17826  18588  11693     -8    928   2494       O  
ATOM   6394  CB  SER B 278      -1.491  -0.894  47.229  1.00118.25           C  
ANISOU 6394  CB  SER B 278    16658  17483  10788    -80    799   2402       C  
ATOM   6395  OG  SER B 278      -2.070  -2.094  47.662  1.00114.92           O  
ANISOU 6395  OG  SER B 278    16051  17168  10443    -94    715   2331       O  
ATOM   6396  N   ILE B 279       1.039   0.801  46.242  1.00122.16           N  
ANISOU 6396  N   ILE B 279    17445  17735  11232   -295    931   2457       N  
ATOM   6397  CA  ILE B 279       1.584   2.010  45.621  1.00124.63           C  
ANISOU 6397  CA  ILE B 279    17959  17940  11453   -298   1046   2523       C  
ATOM   6398  C   ILE B 279       2.291   1.629  44.307  1.00124.01           C  
ANISOU 6398  C   ILE B 279    17754  17981  11380   -335   1024   2502       C  
ATOM   6399  O   ILE B 279       1.969   2.156  43.217  1.00124.61           O  
ANISOU 6399  O   ILE B 279    17873  18112  11361   -199   1091   2568       O  
ATOM   6400  CB  ILE B 279       2.498   2.763  46.594  1.00125.20           C  
ANISOU 6400  CB  ILE B 279    18227  17807  11535   -482   1102   2513       C  
ATOM   6401  CG1 ILE B 279       1.661   3.336  47.730  1.00127.36           C  
ANISOU 6401  CG1 ILE B 279    18657  17958  11774   -409   1149   2548       C  
ATOM   6402  CG2 ILE B 279       3.233   3.911  45.911  1.00127.32           C  
ANISOU 6402  CG2 ILE B 279    18700  17957  11719   -536   1230   2563       C  
ATOM   6403  CD1 ILE B 279       2.483   3.540  48.971  1.00132.95           C  
ANISOU 6403  CD1 ILE B 279    19456  18530  12529   -620   1149   2494       C  
ATOM   6404  N   GLY B 280       3.177   0.648  44.407  1.00123.03           N  
ANISOU 6404  N   GLY B 280    17463  17916  11364   -495    929   2414       N  
ATOM   6405  CA  GLY B 280       3.848   0.088  43.247  1.00124.74           C  
ANISOU 6405  CA  GLY B 280    17530  18263  11602   -534    892   2378       C  
ATOM   6406  C   GLY B 280       2.896  -0.358  42.149  1.00128.41           C  
ANISOU 6406  C   GLY B 280    17852  18912  12023   -354    875   2388       C  
ATOM   6407  O   GLY B 280       3.162  -0.108  40.962  1.00144.14           O  
ANISOU 6407  O   GLY B 280    19828  20981  13956   -313    909   2414       O  
ATOM   6408  N   TRP B 281       1.785  -0.982  42.534  1.00125.34           N  
ANISOU 6408  N   TRP B 281    17361  18608  11651   -251    827   2367       N  
ATOM   6409  CA  TRP B 281       0.751  -1.394  41.565  1.00121.93           C  
ANISOU 6409  CA  TRP B 281    16782  18386  11158    -85    814   2365       C  
ATOM   6410  C   TRP B 281      -0.073  -0.242  41.003  1.00122.82           C  
ANISOU 6410  C   TRP B 281    17031  18521  11111    120    915   2478       C  
ATOM   6411  O   TRP B 281      -0.555  -0.344  39.891  1.00123.80           O  
ANISOU 6411  O   TRP B 281    17050  18832  11157    246    923   2491       O  
ATOM   6412  CB  TRP B 281      -0.208  -2.414  42.181  1.00121.48           C  
ANISOU 6412  CB  TRP B 281    16573  18425  11157    -56    742   2298       C  
ATOM   6413  CG  TRP B 281       0.306  -3.807  42.133  1.00118.69           C  
ANISOU 6413  CG  TRP B 281    16024  18140  10931   -189    654   2183       C  
ATOM   6414  CD1 TRP B 281       0.976  -4.488  43.113  1.00115.71           C  
ANISOU 6414  CD1 TRP B 281    15627  17657  10677   -336    601   2129       C  
ATOM   6415  CD2 TRP B 281       0.157  -4.705  41.052  1.00117.88           C  
ANISOU 6415  CD2 TRP B 281    15723  18229  10834   -175    618   2109       C  
ATOM   6416  NE1 TRP B 281       1.261  -5.753  42.699  1.00114.62           N  
ANISOU 6416  NE1 TRP B 281    15306  17617  10625   -402    543   2034       N  
ATOM   6417  CE2 TRP B 281       0.779  -5.917  41.430  1.00116.46           C  
ANISOU 6417  CE2 TRP B 281    15428  18027  10792   -317    552   2012       C  
ATOM   6418  CE3 TRP B 281      -0.437  -4.603  39.788  1.00117.70           C  
ANISOU 6418  CE3 TRP B 281    15609  18404  10707    -52    641   2115       C  
ATOM   6419  CZ2 TRP B 281       0.833  -7.019  40.594  1.00116.87           C  
ANISOU 6419  CZ2 TRP B 281    15295  18224  10887   -348    517   1915       C  
ATOM   6420  CZ3 TRP B 281      -0.386  -5.690  38.951  1.00118.26           C  
ANISOU 6420  CZ3 TRP B 281    15478  18639  10815    -94    596   2011       C  
ATOM   6421  CH2 TRP B 281       0.248  -6.892  39.358  1.00119.30           C  
ANISOU 6421  CH2 TRP B 281    15514  18721  11093   -247    538   1909       C  
ATOM   6422  N   LEU B 282      -0.273   0.828  41.770  1.00126.01           N  
ANISOU 6422  N   LEU B 282    17668  18748  11462    165    997   2560       N  
ATOM   6423  CA  LEU B 282      -1.086   1.960  41.312  1.00132.48           C  
ANISOU 6423  CA  LEU B 282    18644  19570  12122    389   1111   2683       C  
ATOM   6424  C   LEU B 282      -0.275   3.004  40.536  1.00136.61           C  
ANISOU 6424  C   LEU B 282    19354  19979  12570    383   1223   2763       C  
ATOM   6425  O   LEU B 282      -0.877   3.811  39.794  1.00144.94           O  
ANISOU 6425  O   LEU B 282    20507  21080  13481    593   1321   2871       O  
ATOM   6426  CB  LEU B 282      -1.823   2.617  42.477  1.00133.50           C  
ANISOU 6426  CB  LEU B 282    18946  19562  12214    469   1163   2737       C  
ATOM   6427  CG  LEU B 282      -2.944   1.732  43.038  1.00138.98           C  
ANISOU 6427  CG  LEU B 282    19458  20414  12933    540   1076   2684       C  
ATOM   6428  CD1 LEU B 282      -3.311   2.200  44.448  1.00140.55           C  
ANISOU 6428  CD1 LEU B 282    19818  20439  13144    538   1104   2708       C  
ATOM   6429  CD2 LEU B 282      -4.178   1.671  42.130  1.00138.39           C  
ANISOU 6429  CD2 LEU B 282    19253  20604  12722    783   1088   2724       C  
ATOM   6430  N   ALA B 283       1.061   2.975  40.687  1.00133.59           N  
ANISOU 6430  N   ALA B 283    19014  19468  12274    153   1213   2714       N  
ATOM   6431  CA  ALA B 283       1.997   3.839  39.888  1.00132.26           C  
ANISOU 6431  CA  ALA B 283    18999  19204  12046     98   1314   2769       C  
ATOM   6432  C   ALA B 283       1.643   4.041  38.410  1.00132.01           C  
ANISOU 6432  C   ALA B 283    18915  19340  11902    280   1359   2839       C  
ATOM   6433  O   ALA B 283       1.529   5.170  37.945  1.00130.38           O  
ANISOU 6433  O   ALA B 283    18922  19042  11573    401   1498   2955       O  
ATOM   6434  CB  ALA B 283       3.424   3.302  39.962  1.00132.49           C  
ANISOU 6434  CB  ALA B 283    18948  19203  12188   -169   1249   2673       C  
ATOM   6435  N   GLN B 284       1.501   2.928  37.687  1.00130.57           N  
ANISOU 6435  N   GLN B 284    18452  19399  11759    294   1248   2764       N  
ATOM   6436  CA  GLN B 284       1.084   2.903  36.276  1.00129.03           C  
ANISOU 6436  CA  GLN B 284    18145  19423  11456    465   1266   2808       C  
ATOM   6437  C   GLN B 284      -0.081   3.809  35.864  1.00135.27           C  
ANISOU 6437  C   GLN B 284    19050  20276  12069    759   1373   2944       C  
ATOM   6438  O   GLN B 284      -0.164   4.195  34.691  1.00143.73           O  
ANISOU 6438  O   GLN B 284    20117  21469  13025    899   1434   3017       O  
ATOM   6439  CB  GLN B 284       0.721   1.472  35.879  1.00125.02           C  
ANISOU 6439  CB  GLN B 284    17312  19174  11013    452   1128   2687       C  
ATOM   6440  CG  GLN B 284      -0.406   0.876  36.694  1.00123.09           C  
ANISOU 6440  CG  GLN B 284    16966  19009  10791    520   1066   2643       C  
ATOM   6441  CD  GLN B 284      -0.865  -0.450  36.155  1.00122.03           C  
ANISOU 6441  CD  GLN B 284    16530  19139  10694    514    961   2525       C  
ATOM   6442  OE1 GLN B 284      -1.435  -0.524  35.084  1.00125.20           O  
ANISOU 6442  OE1 GLN B 284    16807  19773  10987    655    970   2537       O  
ATOM   6443  NE2 GLN B 284      -0.626  -1.500  36.893  1.00123.30           N  
ANISOU 6443  NE2 GLN B 284    16577  19269  11001    351    869   2409       N  
ATOM   6444  N   PHE B 285      -0.993   4.105  36.791  1.00139.73           N  
ANISOU 6444  N   PHE B 285    19704  20782  12605    868   1396   2980       N  
ATOM   6445  CA  PHE B 285      -2.173   4.914  36.469  1.00146.81           C  
ANISOU 6445  CA  PHE B 285    20695  21762  13322   1175   1497   3113       C  
ATOM   6446  C   PHE B 285      -1.924   6.418  36.448  1.00151.59           C  
ANISOU 6446  C   PHE B 285    21656  22118  13821   1269   1682   3263       C  
ATOM   6447  O   PHE B 285      -2.805   7.162  36.009  1.00157.58           O  
ANISOU 6447  O   PHE B 285    22513  22947  14412   1553   1787   3395       O  
ATOM   6448  CB  PHE B 285      -3.322   4.586  37.409  1.00147.28           C  
ANISOU 6448  CB  PHE B 285    20689  21891  13378   1272   1448   3091       C  
ATOM   6449  CG  PHE B 285      -3.806   3.188  37.264  1.00147.49           C  
ANISOU 6449  CG  PHE B 285    20377  22192  13468   1224   1298   2959       C  
ATOM   6450  CD1 PHE B 285      -4.708   2.854  36.257  1.00148.92           C  
ANISOU 6450  CD1 PHE B 285    20352  22707  13522   1415   1279   2966       C  
ATOM   6451  CD2 PHE B 285      -3.342   2.196  38.110  1.00148.44           C  
ANISOU 6451  CD2 PHE B 285    20387  22244  13767    985   1185   2824       C  
ATOM   6452  CE1 PHE B 285      -5.160   1.549  36.109  1.00146.84           C  
ANISOU 6452  CE1 PHE B 285    19783  22694  13312   1344   1154   2826       C  
ATOM   6453  CE2 PHE B 285      -3.775   0.887  37.960  1.00151.51           C  
ANISOU 6453  CE2 PHE B 285    20488  22863  14216    932   1066   2698       C  
ATOM   6454  CZ  PHE B 285      -4.681   0.560  36.954  1.00146.52           C  
ANISOU 6454  CZ  PHE B 285    19658  22552  13461   1098   1054   2692       C  
ATOM   6455  N   MET B 286      -0.745   6.858  36.898  1.00150.84           N  
ANISOU 6455  N   MET B 286    21752  21747  13811   1037   1731   3243       N  
ATOM   6456  CA  MET B 286      -0.322   8.246  36.700  1.00158.37           C  
ANISOU 6456  CA  MET B 286    23050  22455  14667   1079   1924   3369       C  
ATOM   6457  C   MET B 286      -0.026   8.515  35.223  1.00163.70           C  
ANISOU 6457  C   MET B 286    23705  23249  15242   1178   1986   3444       C  
ATOM   6458  O   MET B 286       0.461   7.618  34.480  1.00164.95           O  
ANISOU 6458  O   MET B 286    23609  23603  15461   1075   1871   3358       O  
ATOM   6459  CB  MET B 286       0.942   8.551  37.483  1.00161.00           C  
ANISOU 6459  CB  MET B 286    23556  22504  15112    763   1954   3303       C  
ATOM   6460  CG  MET B 286       0.825   8.371  38.985  1.00162.01           C  
ANISOU 6460  CG  MET B 286    23725  22493  15335    638   1904   3228       C  
ATOM   6461  SD  MET B 286       2.383   8.805  39.810  1.00167.07           S  
ANISOU 6461  SD  MET B 286    24558  22844  16075    259   1952   3146       S  
ATOM   6462  CE  MET B 286       3.535   7.559  39.218  1.00163.92           C  
ANISOU 6462  CE  MET B 286    23840  22639  15804     23   1784   3014       C  
ATOM   6463  N   ASP B 287      -0.292   9.758  34.810  1.00168.62           N  
ANISOU 6463  N   ASP B 287    24610  23745  15711   1378   2178   3606       N  
ATOM   6464  CA  ASP B 287      -0.141  10.160  33.421  1.00174.78           C  
ANISOU 6464  CA  ASP B 287    25406  24632  16367   1519   2263   3707       C  
ATOM   6465  C   ASP B 287       1.261   9.837  32.892  1.00176.48           C  
ANISOU 6465  C   ASP B 287    25559  24813  16681   1232   2224   3622       C  
ATOM   6466  O   ASP B 287       2.270  10.389  33.363  1.00173.28           O  
ANISOU 6466  O   ASP B 287    25371  24131  16334    996   2304   3601       O  
ATOM   6467  CB  ASP B 287      -0.453  11.663  33.214  1.00179.79           C  
ANISOU 6467  CB  ASP B 287    26426  25055  16831   1747   2510   3902       C  
ATOM   6468  CG  ASP B 287      -1.952  11.970  33.166  1.00180.38           C  
ANISOU 6468  CG  ASP B 287    26504  25288  16743   2141   2558   4027       C  
ATOM   6469  OD1 ASP B 287      -2.763  11.127  33.585  1.00184.13           O  
ANISOU 6469  OD1 ASP B 287    26726  25984  17250   2199   2411   3951       O  
ATOM   6470  OD2 ASP B 287      -2.318  13.067  32.694  1.00180.50           O  
ANISOU 6470  OD2 ASP B 287    26781  25213  16588   2400   2755   4206       O  
ATOM   6471  N   GLY B 288       1.287   8.922  31.916  1.00177.31           N  
ANISOU 6471  N   GLY B 288    25356  25219  16795   1252   2101   3566       N  
ATOM   6472  CA  GLY B 288       2.490   8.569  31.173  1.00174.56           C  
ANISOU 6472  CA  GLY B 288    24912  24903  16510   1039   2061   3500       C  
ATOM   6473  C   GLY B 288       3.407   7.612  31.888  1.00167.72           C  
ANISOU 6473  C   GLY B 288    23887  24002  15836    712   1912   3323       C  
ATOM   6474  O   GLY B 288       4.492   7.332  31.379  1.00163.97           O  
ANISOU 6474  O   GLY B 288    23340  23544  15416    521   1881   3263       O  
ATOM   6475  N   ALA B 289       2.959   7.073  33.029  1.00162.42           N  
ANISOU 6475  N   ALA B 289    23147  23305  15258    664   1818   3244       N  
ATOM   6476  CA  ALA B 289       3.857   6.290  33.865  1.00154.73           C  
ANISOU 6476  CA  ALA B 289    22067  22266  14456    367   1699   3095       C  
ATOM   6477  C   ALA B 289       3.967   4.861  33.334  1.00148.35           C  
ANISOU 6477  C   ALA B 289    20901  21728  13736    315   1525   2972       C  
ATOM   6478  O   ALA B 289       5.091   4.294  33.246  1.00153.41           O  
ANISOU 6478  O   ALA B 289    21438  22374  14476     92   1456   2877       O  
ATOM   6479  CB  ALA B 289       3.386   6.317  35.310  1.00154.29           C  
ANISOU 6479  CB  ALA B 289    22098  22064  14460    335   1680   3067       C  
ATOM   6480  N   ARG B 290       2.822   4.284  32.945  1.00139.65           N  
ANISOU 6480  N   ARG B 290    19612  20860  12587    519   1464   2970       N  
ATOM   6481  CA  ARG B 290       2.790   2.896  32.480  1.00135.17           C  
ANISOU 6481  CA  ARG B 290    18716  20544  12097    470   1314   2841       C  
ATOM   6482  C   ARG B 290       3.779   2.674  31.359  1.00135.62           C  
ANISOU 6482  C   ARG B 290    18680  20691  12158    378   1303   2814       C  
ATOM   6483  O   ARG B 290       4.508   1.663  31.369  1.00130.21           O  
ANISOU 6483  O   ARG B 290    17814  20063  11595    200   1195   2688       O  
ATOM   6484  CB  ARG B 290       1.391   2.463  32.040  1.00137.31           C  
ANISOU 6484  CB  ARG B 290    18811  21081  12279    703   1277   2847       C  
ATOM   6485  CG  ARG B 290       1.235   0.942  31.985  1.00138.25           C  
ANISOU 6485  CG  ARG B 290    18619  21404  12504    610   1127   2684       C  
ATOM   6486  CD  ARG B 290      -0.124   0.494  31.454  1.00141.90           C  
ANISOU 6486  CD  ARG B 290    18886  22168  12861    811   1096   2669       C  
ATOM   6487  NE  ARG B 290      -1.212   0.554  32.450  1.00144.02           N  
ANISOU 6487  NE  ARG B 290    19187  22421  13112    906   1094   2684       N  
ATOM   6488  CZ  ARG B 290      -2.025   1.597  32.674  1.00145.66           C  
ANISOU 6488  CZ  ARG B 290    19565  22595  13183   1120   1191   2821       C  
ATOM   6489  NH1 ARG B 290      -1.902   2.722  31.987  1.00151.94           N  
ANISOU 6489  NH1 ARG B 290    20537  23348  13843   1273   1313   2966       N  
ATOM   6490  NH2 ARG B 290      -2.969   1.513  33.604  1.00144.63           N  
ANISOU 6490  NH2 ARG B 290    19436  22468  13048   1188   1174   2816       N  
ATOM   6491  N   ARG B 291       3.828   3.630  30.416  1.00143.91           N  
ANISOU 6491  N   ARG B 291    19863  21747  13070    505   1423   2936       N  
ATOM   6492  CA  ARG B 291       4.810   3.587  29.301  1.00146.32           C  
ANISOU 6492  CA  ARG B 291    20108  22127  13359    422   1433   2928       C  
ATOM   6493  C   ARG B 291       6.255   3.818  29.755  1.00142.58           C  
ANISOU 6493  C   ARG B 291    19754  21439  12979    146   1451   2888       C  
ATOM   6494  O   ARG B 291       7.164   3.185  29.198  1.00139.53           O  
ANISOU 6494  O   ARG B 291    19212  21150  12651      5   1384   2807       O  
ATOM   6495  CB  ARG B 291       4.434   4.530  28.163  1.00151.29           C  
ANISOU 6495  CB  ARG B 291    20844  22830  13806    645   1563   3078       C  
ATOM   6496  CG  ARG B 291       3.186   4.050  27.426  1.00158.47           C  
ANISOU 6496  CG  ARG B 291    21540  24058  14611    898   1517   3087       C  
ATOM   6497  CD  ARG B 291       3.079   4.454  25.954  1.00166.39           C  
ANISOU 6497  CD  ARG B 291    22506  25260  15453   1079   1587   3183       C  
ATOM   6498  NE  ARG B 291       1.682   4.278  25.505  1.00172.44           N  
ANISOU 6498  NE  ARG B 291    23121  26316  16081   1357   1574   3219       N  
ATOM   6499  CZ  ARG B 291       1.170   4.661  24.329  1.00183.53           C  
ANISOU 6499  CZ  ARG B 291    24474  27954  17302   1597   1638   3320       C  
ATOM   6500  NH1 ARG B 291       1.932   5.239  23.393  1.00194.36           N  
ANISOU 6500  NH1 ARG B 291    25939  29299  18607   1602   1724   3404       N  
ATOM   6501  NH2 ARG B 291      -0.124   4.448  24.076  1.00182.86           N  
ANISOU 6501  NH2 ARG B 291    24232  28155  17088   1835   1615   3337       N  
ATOM   6502  N   GLU B 292       6.454   4.631  30.806  1.00139.17           N  
ANISOU 6502  N   GLU B 292    19575  20741  12562     60   1533   2930       N  
ATOM   6503  CA  GLU B 292       7.811   4.857  31.366  1.00138.22           C  
ANISOU 6503  CA  GLU B 292    19558  20440  12519   -225   1550   2876       C  
ATOM   6504  C   GLU B 292       8.358   3.601  32.103  1.00134.24           C  
ANISOU 6504  C   GLU B 292    18830  19998  12174   -413   1386   2721       C  
ATOM   6505  O   GLU B 292       9.566   3.304  32.061  1.00124.66           O  
ANISOU 6505  O   GLU B 292    17554  18790  11021   -621   1350   2649       O  
ATOM   6506  CB  GLU B 292       7.777   6.074  32.287  1.00143.84           C  
ANISOU 6506  CB  GLU B 292    20602  20863  13187   -262   1692   2953       C  
ATOM   6507  CG  GLU B 292       9.004   6.329  33.166  1.00150.10           C  
ANISOU 6507  CG  GLU B 292    21506  21473  14051   -569   1711   2881       C  
ATOM   6508  CD  GLU B 292      10.219   6.841  32.422  1.00153.59           C  
ANISOU 6508  CD  GLU B 292    22022  21883  14449   -740   1794   2889       C  
ATOM   6509  OE1 GLU B 292      10.057   7.688  31.521  1.00166.29           O  
ANISOU 6509  OE1 GLU B 292    23790  23453  15939   -620   1930   3004       O  
ATOM   6510  OE2 GLU B 292      11.347   6.424  32.768  1.00152.92           O  
ANISOU 6510  OE2 GLU B 292    21845  21817  14440   -992   1729   2784       O  
ATOM   6511  N   ILE B 293       7.453   2.863  32.752  1.00136.45           N  
ANISOU 6511  N   ILE B 293    18990  20338  12514   -327   1294   2674       N  
ATOM   6512  CA  ILE B 293       7.814   1.661  33.514  1.00135.54           C  
ANISOU 6512  CA  ILE B 293    18683  20268  12544   -469   1154   2542       C  
ATOM   6513  C   ILE B 293       7.977   0.422  32.623  1.00133.37           C  
ANISOU 6513  C   ILE B 293    18122  20230  12321   -461   1045   2451       C  
ATOM   6514  O   ILE B 293       8.915  -0.330  32.805  1.00133.53           O  
ANISOU 6514  O   ILE B 293    18022  20277  12436   -621    970   2360       O  
ATOM   6515  CB  ILE B 293       6.772   1.385  34.629  1.00137.39           C  
ANISOU 6515  CB  ILE B 293    18924  20453  12822   -391   1114   2530       C  
ATOM   6516  CG1 ILE B 293       6.707   2.583  35.592  1.00136.44           C  
ANISOU 6516  CG1 ILE B 293    19093  20087  12658   -418   1224   2607       C  
ATOM   6517  CG2 ILE B 293       7.099   0.108  35.422  1.00141.04           C  
ANISOU 6517  CG2 ILE B 293    19199  20957  13431   -521    981   2404       C  
ATOM   6518  CD1 ILE B 293       5.351   2.766  36.225  1.00137.47           C  
ANISOU 6518  CD1 ILE B 293    19286  20191  12756   -237   1239   2655       C  
ATOM   6519  N   VAL B 294       7.057   0.208  31.688  1.00136.59           N  
ANISOU 6519  N   VAL B 294    18422  20816  12657   -271   1041   2472       N  
ATOM   6520  CA  VAL B 294       7.007  -1.038  30.893  1.00139.84           C  
ANISOU 6520  CA  VAL B 294    18558  21459  13114   -257    942   2368       C  
ATOM   6521  C   VAL B 294       7.809  -1.004  29.566  1.00142.56           C  
ANISOU 6521  C   VAL B 294    18829  21927  13408   -281    959   2370       C  
ATOM   6522  O   VAL B 294       8.462  -2.009  29.195  1.00128.81           O  
ANISOU 6522  O   VAL B 294    16900  20295  11744   -378    878   2263       O  
ATOM   6523  CB  VAL B 294       5.526  -1.416  30.643  1.00142.37           C  
ANISOU 6523  CB  VAL B 294    18765  21948  13379    -61    920   2364       C  
ATOM   6524  CG1 VAL B 294       5.386  -2.587  29.679  1.00145.62           C  
ANISOU 6524  CG1 VAL B 294    18909  22611  13809    -45    842   2253       C  
ATOM   6525  CG2 VAL B 294       4.858  -1.766  31.968  1.00141.41           C  
ANISOU 6525  CG2 VAL B 294    18664  21730  13334    -73    879   2330       C  
ATOM   6526  N   CYS B 295       7.751   0.138  28.862  1.00155.41           N  
ANISOU 6526  N   CYS B 295    20611  23535  14903   -184   1071   2493       N  
ATOM   6527  CA  CYS B 295       8.413   0.284  27.543  1.00163.14           C  
ANISOU 6527  CA  CYS B 295    21533  24638  15814   -185   1101   2512       C  
ATOM   6528  C   CYS B 295       9.858   0.752  27.646  1.00159.63           C  
ANISOU 6528  C   CYS B 295    21200  24054  15398   -394   1141   2516       C  
ATOM   6529  O   CYS B 295      10.208   1.511  28.556  1.00155.91           O  
ANISOU 6529  O   CYS B 295    20937  23365  14937   -496   1204   2558       O  
ATOM   6530  CB  CYS B 295       7.690   1.286  26.629  1.00170.46           C  
ANISOU 6530  CB  CYS B 295    22571  25628  16569     32   1215   2653       C  
ATOM   6531  SG  CYS B 295       5.900   1.123  26.472  1.00183.18           S  
ANISOU 6531  SG  CYS B 295    24090  27426  18083    313   1205   2686       S  
ATOM   6532  N   ARG B 296      10.667   0.316  26.674  1.00157.62           N  
ANISOU 6532  N   ARG B 296    20802  23943  15143   -457   1109   2469       N  
ATOM   6533  CA  ARG B 296      12.041   0.791  26.521  1.00154.77           C  
ANISOU 6533  CA  ARG B 296    20522  23504  14778   -645   1155   2476       C  
ATOM   6534  C   ARG B 296      12.038   2.117  25.758  1.00158.99           C  
ANISOU 6534  C   ARG B 296    21265  23976  15166   -573   1307   2619       C  
ATOM   6535  O   ARG B 296      10.988   2.568  25.295  1.00171.37           O  
ANISOU 6535  O   ARG B 296    22891  25584  16635   -355   1367   2712       O  
ATOM   6536  CB  ARG B 296      12.884  -0.247  25.764  1.00153.30           C  
ANISOU 6536  CB  ARG B 296    20090  23511  14645   -727   1061   2369       C  
ATOM   6537  CG  ARG B 296      13.546  -1.272  26.651  1.00147.46           C  
ANISOU 6537  CG  ARG B 296    19222  22760  14045   -880    953   2246       C  
ATOM   6538  CD  ARG B 296      14.111  -2.391  25.801  1.00144.79           C  
ANISOU 6538  CD  ARG B 296    18636  22626  13748   -899    868   2144       C  
ATOM   6539  NE  ARG B 296      14.933  -3.322  26.552  1.00142.18           N  
ANISOU 6539  NE  ARG B 296    18194  22291  13535  -1035    781   2040       N  
ATOM   6540  CZ  ARG B 296      16.265  -3.350  26.573  1.00138.25           C  
ANISOU 6540  CZ  ARG B 296    17665  21814  13047  -1193    773   2011       C  
ATOM   6541  NH1 ARG B 296      17.007  -2.497  25.872  1.00132.62           N  
ANISOU 6541  NH1 ARG B 296    17025  21121  12241  -1267    846   2066       N  
ATOM   6542  NH2 ARG B 296      16.857  -4.266  27.323  1.00143.66           N  
ANISOU 6542  NH2 ARG B 296    18240  22511  13830  -1274    694   1925       N  
ATOM   6543  N   ALA B 297      13.218   2.720  25.590  1.00153.93           N  
ANISOU 6543  N   ALA B 297    20732  23253  14501   -751   1377   2636       N  
ATOM   6544  CA  ALA B 297      13.359   3.937  24.783  1.00149.05           C  
ANISOU 6544  CA  ALA B 297    20319  22568  13744   -704   1536   2768       C  
ATOM   6545  C   ALA B 297      12.954   3.671  23.322  1.00145.30           C  
ANISOU 6545  C   ALA B 297    19692  22332  13183   -514   1527   2805       C  
ATOM   6546  O   ALA B 297      12.232   4.479  22.733  1.00148.32           O  
ANISOU 6546  O   ALA B 297    20210  22706  13437   -319   1639   2938       O  
ATOM   6547  CB  ALA B 297      14.780   4.480  24.863  1.00149.22           C  
ANISOU 6547  CB  ALA B 297    20450  22486  13760   -969   1603   2753       C  
ATOM   6548  N   ASP B 298      13.379   2.532  22.767  1.00137.16           N  
ANISOU 6548  N   ASP B 298    18381  21517  12215   -558   1399   2689       N  
ATOM   6549  CA  ASP B 298      13.029   2.176  21.388  1.00135.14           C  
ANISOU 6549  CA  ASP B 298    17953  21513  11880   -396   1380   2701       C  
ATOM   6550  C   ASP B 298      11.559   1.833  21.125  1.00131.34           C  
ANISOU 6550  C   ASP B 298    17371  21182  11349   -142   1347   2718       C  
ATOM   6551  O   ASP B 298      11.069   1.983  19.995  1.00136.08           O  
ANISOU 6551  O   ASP B 298    17905  21970  11829     34   1381   2778       O  
ATOM   6552  CB  ASP B 298      13.981   1.103  20.817  1.00137.63           C  
ANISOU 6552  CB  ASP B 298    18013  22012  12267   -525   1269   2568       C  
ATOM   6553  CG  ASP B 298      14.072  -0.172  21.669  1.00132.98           C  
ANISOU 6553  CG  ASP B 298    17244  21446  11835   -618   1125   2414       C  
ATOM   6554  OD1 ASP B 298      13.059  -0.597  22.240  1.00126.99           O  
ANISOU 6554  OD1 ASP B 298    16449  20682  11117   -517   1078   2387       O  
ATOM   6555  OD2 ASP B 298      15.173  -0.779  21.696  1.00132.14           O  
ANISOU 6555  OD2 ASP B 298    17023  21382  11801   -783   1063   2322       O  
ATOM   6556  N   GLY B 299      10.855   1.377  22.146  1.00126.86           N  
ANISOU 6556  N   GLY B 299    16782  20555  10864   -124   1283   2664       N  
ATOM   6557  CA  GLY B 299       9.442   1.020  22.001  1.00129.19           C  
ANISOU 6557  CA  GLY B 299    16969  21007  11108     95   1250   2667       C  
ATOM   6558  C   GLY B 299       9.182  -0.464  22.050  1.00127.51           C  
ANISOU 6558  C   GLY B 299    16473  20972  11001     58   1103   2496       C  
ATOM   6559  O   GLY B 299       8.076  -0.921  21.722  1.00126.09           O  
ANISOU 6559  O   GLY B 299    16152  20984  10770    214   1068   2467       O  
ATOM   6560  N   THR B 300      10.208  -1.217  22.430  1.00128.22           N  
ANISOU 6560  N   THR B 300    16481  21009  11227   -147   1026   2382       N  
ATOM   6561  CA  THR B 300      10.071  -2.624  22.754  1.00132.25           C  
ANISOU 6561  CA  THR B 300    16776  21611  11861   -206    905   2221       C  
ATOM   6562  C   THR B 300       9.776  -2.755  24.256  1.00132.13           C  
ANISOU 6562  C   THR B 300    16854  21399  11951   -268    877   2201       C  
ATOM   6563  O   THR B 300       9.816  -1.762  24.994  1.00129.70           O  
ANISOU 6563  O   THR B 300    16767  20890  11620   -284    947   2301       O  
ATOM   6564  CB  THR B 300      11.337  -3.429  22.379  1.00134.23           C  
ANISOU 6564  CB  THR B 300    16887  21918  12196   -367    843   2115       C  
ATOM   6565  OG1 THR B 300      12.442  -2.998  23.170  1.00134.11           O  
ANISOU 6565  OG1 THR B 300    17010  21705  12241   -538    861   2139       O  
ATOM   6566  CG2 THR B 300      11.676  -3.244  20.904  1.00136.69           C  
ANISOU 6566  CG2 THR B 300    17113  22420  12400   -312    874   2138       C  
ATOM   6567  N   MET B 301       9.450  -3.981  24.681  1.00133.31           N  
ANISOU 6567  N   MET B 301    16838  21605  12206   -301    784   2070       N  
ATOM   6568  CA  MET B 301       9.122  -4.282  26.077  1.00135.58           C  
ANISOU 6568  CA  MET B 301    17184  21731  12597   -353    749   2040       C  
ATOM   6569  C   MET B 301      10.408  -4.185  26.861  1.00132.95           C  
ANISOU 6569  C   MET B 301    16939  21221  12353   -536    739   2035       C  
ATOM   6570  O   MET B 301      11.463  -4.459  26.291  1.00131.58           O  
ANISOU 6570  O   MET B 301    16689  21107  12195   -627    722   1996       O  
ATOM   6571  CB  MET B 301       8.599  -5.716  26.217  1.00140.72           C  
ANISOU 6571  CB  MET B 301    17634  22491  13340   -361    664   1894       C  
ATOM   6572  CG  MET B 301       7.319  -6.052  25.449  1.00146.26           C  
ANISOU 6572  CG  MET B 301    18198  23419  13956   -213    662   1857       C  
ATOM   6573  SD  MET B 301       6.574  -7.656  25.832  1.00150.66           S  
ANISOU 6573  SD  MET B 301    18561  24062  14618   -254    588   1677       S  
ATOM   6574  CE  MET B 301       8.024  -8.681  25.542  1.00141.69           C  
ANISOU 6574  CE  MET B 301    17325  22904  13606   -410    542   1566       C  
ATOM   6575  N   ARG B 302      10.345  -3.802  28.141  1.00130.20           N  
ANISOU 6575  N   ARG B 302    16737  20679  12052   -590    750   2069       N  
ATOM   6576  CA  ARG B 302      11.575  -3.829  28.955  1.00127.67           C  
ANISOU 6576  CA  ARG B 302    16468  20230  11810   -773    731   2046       C  
ATOM   6577  C   ARG B 302      11.871  -5.225  29.403  1.00122.39           C  
ANISOU 6577  C   ARG B 302    15627  19605  11268   -833    635   1923       C  
ATOM   6578  O   ARG B 302      10.988  -5.890  29.967  1.00129.24           O  
ANISOU 6578  O   ARG B 302    16447  20463  12195   -776    597   1878       O  
ATOM   6579  CB  ARG B 302      11.479  -2.922  30.179  1.00128.34           C  
ANISOU 6579  CB  ARG B 302    16768  20102  11892   -824    781   2117       C  
ATOM   6580  CG  ARG B 302      11.700  -1.471  29.851  1.00131.11           C  
ANISOU 6580  CG  ARG B 302    17332  20356  12127   -829    899   2234       C  
ATOM   6581  CD  ARG B 302      11.717  -0.651  31.105  1.00132.15           C  
ANISOU 6581  CD  ARG B 302    17677  20269  12262   -907    953   2283       C  
ATOM   6582  NE  ARG B 302      11.682   0.788  30.903  1.00136.12           N  
ANISOU 6582  NE  ARG B 302    18429  20640  12651   -892   1092   2399       N  
ATOM   6583  CZ  ARG B 302      12.411   1.679  31.590  1.00137.56           C  
ANISOU 6583  CZ  ARG B 302    18809  20645  12813  -1055   1170   2427       C  
ATOM   6584  NH1 ARG B 302      13.299   1.310  32.509  1.00137.62           N  
ANISOU 6584  NH1 ARG B 302    18774  20616  12896  -1249   1115   2347       N  
ATOM   6585  NH2 ARG B 302      12.274   2.973  31.327  1.00145.03           N  
ANISOU 6585  NH2 ARG B 302    20000  21454  13648  -1025   1317   2535       N  
ATOM   6586  N   LEU B 303      13.087  -5.680  29.133  1.00118.01           N  
ANISOU 6586  N   LEU B 303    14983  19105  10750   -941    605   1872       N  
ATOM   6587  CA  LEU B 303      13.522  -7.018  29.486  1.00120.18           C  
ANISOU 6587  CA  LEU B 303    15105  19421  11136   -984    528   1765       C  
ATOM   6588  C   LEU B 303      14.948  -6.924  29.997  1.00123.44           C  
ANISOU 6588  C   LEU B 303    15530  19800  11570  -1130    517   1763       C  
ATOM   6589  O   LEU B 303      15.685  -6.060  29.536  1.00127.89           O  
ANISOU 6589  O   LEU B 303    16157  20380  12055  -1202    562   1814       O  
ATOM   6590  CB  LEU B 303      13.452  -7.927  28.274  1.00120.45           C  
ANISOU 6590  CB  LEU B 303    14957  19634  11172   -923    502   1682       C  
ATOM   6591  CG  LEU B 303      12.039  -8.169  27.737  1.00124.55           C  
ANISOU 6591  CG  LEU B 303    15444  20253  11624   -787    525   1686       C  
ATOM   6592  CD1 LEU B 303      12.149  -8.960  26.459  1.00125.69           C  
ANISOU 6592  CD1 LEU B 303    15394  20554  11808   -755    486   1560       C  
ATOM   6593  CD2 LEU B 303      11.127  -8.882  28.712  1.00125.67           C  
ANISOU 6593  CD2 LEU B 303    15676  20303  11767   -718    536   1721       C  
ATOM   6594  N   GLY B 304      15.317  -7.785  30.948  1.00123.89           N  
ANISOU 6594  N   GLY B 304    15530  19819  11720  -1172    464   1709       N  
ATOM   6595  CA  GLY B 304      16.634  -7.725  31.583  1.00128.68           C  
ANISOU 6595  CA  GLY B 304    16134  20424  12333  -1301    449   1708       C  
ATOM   6596  C   GLY B 304      16.921  -6.305  32.122  1.00138.75           C  
ANISOU 6596  C   GLY B 304    17592  21596  13531  -1411    509   1789       C  
ATOM   6597  O   GLY B 304      17.879  -5.700  31.734  1.00146.53           O  
ANISOU 6597  O   GLY B 304    18594  22632  14447  -1517    540   1807       O  
ATOM   6598  N   GLU B 305      16.031  -5.768  32.940  1.00146.78           N  
ANISOU 6598  N   GLU B 305    18748  22467  14551  -1385    534   1835       N  
ATOM   6599  CA  GLU B 305      15.860  -4.307  33.119  1.00155.87           C  
ANISOU 6599  CA  GLU B 305    20110  23496  15614  -1439    621   1920       C  
ATOM   6600  C   GLU B 305      17.000  -3.534  33.711  1.00158.73           C  
ANISOU 6600  C   GLU B 305    20561  23819  15926  -1629    659   1932       C  
ATOM   6601  O   GLU B 305      17.163  -2.356  33.360  1.00176.53           O  
ANISOU 6601  O   GLU B 305    22973  26010  18090  -1696    752   1990       O  
ATOM   6602  CB  GLU B 305      14.585  -3.928  33.911  1.00157.59           C  
ANISOU 6602  CB  GLU B 305    20463  23567  15846  -1352    644   1964       C  
ATOM   6603  CG  GLU B 305      14.371  -2.401  34.019  1.00161.86           C  
ANISOU 6603  CG  GLU B 305    21245  23966  16288  -1385    754   2057       C  
ATOM   6604  CD  GLU B 305      14.647  -1.631  32.715  1.00159.63           C  
ANISOU 6604  CD  GLU B 305    21016  23732  15904  -1376    833   2110       C  
ATOM   6605  OE1 GLU B 305      14.883  -0.415  32.826  1.00165.33           O  
ANISOU 6605  OE1 GLU B 305    21940  24331  16544  -1454    937   2175       O  
ATOM   6606  OE2 GLU B 305      14.684  -2.210  31.595  1.00144.39           O  
ANISOU 6606  OE2 GLU B 305    18936  21955  13970  -1302    801   2085       O  
ATOM   6607  N   PRO B 306      17.807  -4.150  34.588  1.00141.28           N  
ANISOU 6607  N   PRO B 306    18259  21655  13763  -1721    600   1878       N  
ATOM   6608  CA  PRO B 306      19.018  -3.383  35.023  1.00139.75           C  
ANISOU 6608  CA  PRO B 306    18123  21478  13495  -1927    640   1875       C  
ATOM   6609  C   PRO B 306      20.097  -3.435  33.909  1.00149.24           C  
ANISOU 6609  C   PRO B 306    19214  22849  14641  -1996    645   1852       C  
ATOM   6610  O   PRO B 306      21.004  -4.269  33.919  1.00157.88           O  
ANISOU 6610  O   PRO B 306    20130  24102  15754  -2026    580   1796       O  
ATOM   6611  CB  PRO B 306      19.419  -4.028  36.342  1.00128.83           C  
ANISOU 6611  CB  PRO B 306    16666  20118  12166  -1976    574   1832       C  
ATOM   6612  CG  PRO B 306      18.329  -5.008  36.593  1.00127.37           C  
ANISOU 6612  CG  PRO B 306    16424  19885  12086  -1796    515   1825       C  
ATOM   6613  CD  PRO B 306      17.552  -5.340  35.383  1.00126.23           C  
ANISOU 6613  CD  PRO B 306    16236  19764  11960  -1650    517   1830       C  
ATOM   6614  N   THR B 307      19.908  -2.569  32.914  1.00150.22           N  
ANISOU 6614  N   THR B 307    19445  22939  14692  -1995    726   1903       N  
ATOM   6615  CA  THR B 307      20.788  -2.468  31.763  1.00150.72           C  
ANISOU 6615  CA  THR B 307    19428  23146  14690  -2053    747   1894       C  
ATOM   6616  C   THR B 307      21.033  -1.026  31.397  1.00158.83           C  
ANISOU 6616  C   THR B 307    20661  24082  15606  -2180    876   1955       C  
ATOM   6617  O   THR B 307      20.279  -0.109  31.734  1.00162.62           O  
ANISOU 6617  O   THR B 307    21357  24374  16057  -2166    960   2018       O  
ATOM   6618  CB  THR B 307      20.228  -3.223  30.516  1.00144.23           C  
ANISOU 6618  CB  THR B 307    18477  22423  13901  -1868    708   1889       C  
ATOM   6619  OG1 THR B 307      18.815  -3.068  30.471  1.00132.70           O  
ANISOU 6619  OG1 THR B 307    17112  20845  12463  -1709    728   1936       O  
ATOM   6620  CG2 THR B 307      20.623  -4.703  30.572  1.00143.62           C  
ANISOU 6620  CG2 THR B 307    18167  22493  13910  -1808    599   1805       C  
ATOM   6621  N   SER B 308      22.108  -0.886  30.638  1.00161.61           N  
ANISOU 6621  N   SER B 308    20938  24573  15890  -2296    896   1935       N  
ATOM   6622  CA  SER B 308      22.701   0.376  30.293  1.00160.98           C  
ANISOU 6622  CA  SER B 308    21028  24441  15696  -2471   1023   1973       C  
ATOM   6623  C   SER B 308      21.808   1.140  29.331  1.00162.97           C  
ANISOU 6623  C   SER B 308    21446  24573  15900  -2341   1121   2070       C  
ATOM   6624  O   SER B 308      21.147   0.528  28.494  1.00164.65           O  
ANISOU 6624  O   SER B 308    21554  24859  16147  -2142   1072   2087       O  
ATOM   6625  CB  SER B 308      24.053   0.111  29.647  1.00160.13           C  
ANISOU 6625  CB  SER B 308    20751  24554  15533  -2605   1001   1919       C  
ATOM   6626  OG  SER B 308      23.972  -1.028  28.835  1.00157.04           O  
ANISOU 6626  OG  SER B 308    20142  24324  15200  -2437    903   1892       O  
ATOM   6627  N   ASN B 309      21.805   2.468  29.448  1.00167.04           N  
ANISOU 6627  N   ASN B 309    22223  24915  16329  -2454   1269   2132       N  
ATOM   6628  CA  ASN B 309      21.011   3.365  28.583  1.00171.77           C  
ANISOU 6628  CA  ASN B 309    23021  25385  16858  -2326   1393   2245       C  
ATOM   6629  C   ASN B 309      19.501   3.331  28.871  1.00171.82           C  
ANISOU 6629  C   ASN B 309    23114  25262  16908  -2085   1386   2309       C  
ATOM   6630  O   ASN B 309      18.736   3.813  28.039  1.00176.29           O  
ANISOU 6630  O   ASN B 309    23782  25783  17416  -1916   1461   2404       O  
ATOM   6631  CB  ASN B 309      21.333   3.148  27.069  1.00174.30           C  
ANISOU 6631  CB  ASN B 309    23218  25877  17131  -2256   1392   2267       C  
ATOM   6632  CG  ASN B 309      22.692   3.697  26.674  1.00175.86           C  
ANISOU 6632  CG  ASN B 309    23433  26143  17240  -2503   1466   2243       C  
ATOM   6633  OD1 ASN B 309      23.670   2.957  26.652  1.00175.20           O  
ANISOU 6633  OD1 ASN B 309    23131  26259  17178  -2610   1372   2154       O  
ATOM   6634  ND2 ASN B 309      22.765   4.992  26.367  1.00177.39           N  
ANISOU 6634  ND2 ASN B 309    23892  26178  17330  -2592   1642   2324       N  
ATOM   6635  N   GLU B 310      19.087   2.841  30.053  1.00166.44           N  
ANISOU 6635  N   GLU B 310    22401  24526  16311  -2071   1308   2263       N  
ATOM   6636  CA  GLU B 310      17.663   2.815  30.448  1.00162.63           C  
ANISOU 6636  CA  GLU B 310    21996  23929  15865  -1859   1302   2316       C  
ATOM   6637  C   GLU B 310      17.447   3.327  31.865  1.00155.11           C  
ANISOU 6637  C   GLU B 310    21216  22786  14931  -1949   1339   2311       C  
ATOM   6638  O   GLU B 310      18.289   3.150  32.743  1.00152.01           O  
ANISOU 6638  O   GLU B 310    20780  22410  14567  -2144   1301   2234       O  
ATOM   6639  CB  GLU B 310      16.983   1.435  30.262  1.00166.84           C  
ANISOU 6639  CB  GLU B 310    22278  24617  16495  -1673   1152   2266       C  
ATOM   6640  CG  GLU B 310      16.849   0.935  28.817  1.00176.23           C  
ANISOU 6640  CG  GLU B 310    23309  25988  17660  -1537   1122   2273       C  
ATOM   6641  CD  GLU B 310      15.898   1.768  27.943  1.00178.62           C  
ANISOU 6641  CD  GLU B 310    23757  26247  17864  -1355   1227   2390       C  
ATOM   6642  OE1 GLU B 310      14.962   2.448  28.463  1.00176.57           O  
ANISOU 6642  OE1 GLU B 310    23684  25829  17574  -1256   1297   2465       O  
ATOM   6643  OE2 GLU B 310      16.059   1.714  26.693  1.00177.63           O  
ANISOU 6643  OE2 GLU B 310    23549  26261  17681  -1291   1241   2412       O  
ATOM   6644  N   THR B 311      16.294   3.965  32.063  1.00149.52           N  
ANISOU 6644  N   THR B 311    20699  21915  14195  -1795   1415   2397       N  
ATOM   6645  CA  THR B 311      15.949   4.615  33.327  1.00146.84           C  
ANISOU 6645  CA  THR B 311    20563  21370  13857  -1856   1476   2407       C  
ATOM   6646  C   THR B 311      15.618   3.594  34.431  1.00149.50           C  
ANISOU 6646  C   THR B 311    20740  21753  14308  -1833   1332   2332       C  
ATOM   6647  O   THR B 311      15.371   2.401  34.179  1.00152.45           O  
ANISOU 6647  O   THR B 311    20873  22289  14760  -1721   1200   2287       O  
ATOM   6648  CB  THR B 311      14.756   5.591  33.181  1.00143.96           C  
ANISOU 6648  CB  THR B 311    20454  20824  13420  -1664   1607   2531       C  
ATOM   6649  OG1 THR B 311      13.540   4.863  32.962  1.00141.51           O  
ANISOU 6649  OG1 THR B 311    20009  20606  13150  -1400   1517   2557       O  
ATOM   6650  CG2 THR B 311      14.959   6.573  32.026  1.00145.98           C  
ANISOU 6650  CG2 THR B 311    20880  21028  13556  -1641   1761   2627       C  
ATOM   6651  N   LEU B 312      15.588   4.090  35.661  1.00146.86           N  
ANISOU 6651  N   LEU B 312    20556  21266  13978  -1939   1372   2318       N  
ATOM   6652  CA  LEU B 312      15.343   3.248  36.816  1.00138.28           C  
ANISOU 6652  CA  LEU B 312    19345  20206  12987  -1935   1253   2254       C  
ATOM   6653  C   LEU B 312      13.869   2.952  37.099  1.00134.76           C  
ANISOU 6653  C   LEU B 312    18912  19706  12584  -1696   1219   2300       C  
ATOM   6654  O   LEU B 312      13.546   2.135  37.966  1.00139.46           O  
ANISOU 6654  O   LEU B 312    19390  20333  13265  -1667   1117   2252       O  
ATOM   6655  CB  LEU B 312      16.004   3.878  38.042  1.00138.72           C  
ANISOU 6655  CB  LEU B 312    19536  20150  13019  -2166   1305   2208       C  
ATOM   6656  CG  LEU B 312      17.529   4.068  37.992  1.00141.26           C  
ANISOU 6656  CG  LEU B 312    19810  20568  13292  -2438   1325   2136       C  
ATOM   6657  CD1 LEU B 312      17.947   4.588  39.371  1.00145.92           C  
ANISOU 6657  CD1 LEU B 312    20515  21067  13859  -2647   1364   2080       C  
ATOM   6658  CD2 LEU B 312      18.330   2.816  37.609  1.00136.12           C  
ANISOU 6658  CD2 LEU B 312    18846  20174  12697  -2452   1181   2067       C  
ATOM   6659  N   SER B 313      12.960   3.615  36.400  1.00132.02           N  
ANISOU 6659  N   SER B 313    18703  19287  12169  -1519   1309   2397       N  
ATOM   6660  CA  SER B 313      11.521   3.461  36.667  1.00133.54           C  
ANISOU 6660  CA  SER B 313    18915  19446  12375  -1290   1291   2445       C  
ATOM   6661  C   SER B 313      10.990   2.022  36.718  1.00131.02           C  
ANISOU 6661  C   SER B 313    18323  19299  12159  -1181   1134   2381       C  
ATOM   6662  O   SER B 313      10.061   1.752  37.477  1.00132.77           O  
ANISOU 6662  O   SER B 313    18544  19483  12419  -1082   1098   2383       O  
ATOM   6663  CB  SER B 313      10.724   4.220  35.631  1.00133.69           C  
ANISOU 6663  CB  SER B 313    19064  19443  12289  -1088   1399   2560       C  
ATOM   6664  OG  SER B 313      11.162   5.554  35.612  1.00136.29           O  
ANISOU 6664  OG  SER B 313    19676  19584  12524  -1181   1565   2625       O  
ATOM   6665  N   CYS B 314      11.580   1.122  35.934  1.00125.47           N  
ANISOU 6665  N   CYS B 314    17402  18774  11497  -1206   1051   2323       N  
ATOM   6666  CA  CYS B 314      11.207  -0.282  35.959  1.00124.76           C  
ANISOU 6666  CA  CYS B 314    17067  18830  11505  -1131    920   2249       C  
ATOM   6667  C   CYS B 314      11.768  -1.009  37.198  1.00128.52           C  
ANISOU 6667  C   CYS B 314    17464  19287  12080  -1263    837   2171       C  
ATOM   6668  O   CYS B 314      11.013  -1.662  37.942  1.00126.01           O  
ANISOU 6668  O   CYS B 314    17089  18957  11829  -1191    778   2147       O  
ATOM   6669  CB  CYS B 314      11.699  -0.951  34.699  1.00126.68           C  
ANISOU 6669  CB  CYS B 314    17125  19256  11751  -1115    877   2210       C  
ATOM   6670  SG  CYS B 314      11.304  -2.721  34.522  1.00131.57           S  
ANISOU 6670  SG  CYS B 314    17456  20049  12483  -1034    741   2106       S  
ATOM   6671  N   VAL B 315      13.073  -0.877  37.442  1.00129.43           N  
ANISOU 6671  N   VAL B 315    17574  19410  12193  -1453    838   2135       N  
ATOM   6672  CA  VAL B 315      13.654  -1.474  38.666  1.00129.98           C  
ANISOU 6672  CA  VAL B 315    17571  19481  12332  -1569    768   2072       C  
ATOM   6673  C   VAL B 315      13.087  -0.915  39.984  1.00126.05           C  
ANISOU 6673  C   VAL B 315    17234  18823  11834  -1588    799   2095       C  
ATOM   6674  O   VAL B 315      12.879  -1.664  40.951  1.00127.01           O  
ANISOU 6674  O   VAL B 315    17276  18950  12031  -1576    726   2060       O  
ATOM   6675  CB  VAL B 315      15.198  -1.470  38.709  1.00136.02           C  
ANISOU 6675  CB  VAL B 315    18272  20333  13074  -1768    759   2023       C  
ATOM   6676  CG1 VAL B 315      15.760  -2.326  37.578  1.00141.01           C  
ANISOU 6676  CG1 VAL B 315    18704  21144  13727  -1734    703   1986       C  
ATOM   6677  CG2 VAL B 315      15.781  -0.066  38.660  1.00143.03           C  
ANISOU 6677  CG2 VAL B 315    19364  21124  13855  -1927    879   2056       C  
ATOM   6678  N   ILE B 316      12.790   0.378  40.010  1.00122.57           N  
ANISOU 6678  N   ILE B 316    17027  18235  11309  -1604    915   2159       N  
ATOM   6679  CA  ILE B 316      12.133   0.986  41.180  1.00124.76           C  
ANISOU 6679  CA  ILE B 316    17477  18349  11577  -1601    958   2185       C  
ATOM   6680  C   ILE B 316      10.796   0.294  41.488  1.00122.93           C  
ANISOU 6680  C   ILE B 316    17176  18123  11406  -1403    896   2199       C  
ATOM   6681  O   ILE B 316      10.564  -0.200  42.620  1.00113.84           O  
ANISOU 6681  O   ILE B 316    15987  16949  10317  -1417    838   2167       O  
ATOM   6682  CB  ILE B 316      11.951   2.517  40.995  1.00128.07           C  
ANISOU 6682  CB  ILE B 316    18184  18591  11885  -1622   1117   2259       C  
ATOM   6683  CG1 ILE B 316      13.218   3.226  41.493  1.00127.74           C  
ANISOU 6683  CG1 ILE B 316    18245  18494  11793  -1891   1182   2214       C  
ATOM   6684  CG2 ILE B 316      10.695   3.075  41.709  1.00129.61           C  
ANISOU 6684  CG2 ILE B 316    18554  18630  12062  -1485   1172   2318       C  
ATOM   6685  CD1 ILE B 316      13.469   4.565  40.839  1.00128.95           C  
ANISOU 6685  CD1 ILE B 316    18645  18514  11835  -1957   1349   2270       C  
ATOM   6686  N   ILE B 317       9.939   0.226  40.464  1.00122.71           N  
ANISOU 6686  N   ILE B 317    17120  18149  11353  -1223    909   2243       N  
ATOM   6687  CA  ILE B 317       8.629  -0.413  40.590  1.00118.17           C  
ANISOU 6687  CA  ILE B 317    16465  17617  10816  -1040    858   2249       C  
ATOM   6688  C   ILE B 317       8.779  -1.916  40.892  1.00111.44           C  
ANISOU 6688  C   ILE B 317    15376  16883  10080  -1059    733   2162       C  
ATOM   6689  O   ILE B 317       8.022  -2.457  41.719  1.00107.47           O  
ANISOU 6689  O   ILE B 317    14838  16362   9633  -1003    689   2145       O  
ATOM   6690  CB  ILE B 317       7.739  -0.110  39.341  1.00117.71           C  
ANISOU 6690  CB  ILE B 317    16412  17632  10678   -849    906   2311       C  
ATOM   6691  CG1 ILE B 317       7.375   1.383  39.286  1.00116.92           C  
ANISOU 6691  CG1 ILE B 317    16582  17381  10461   -788   1046   2417       C  
ATOM   6692  CG2 ILE B 317       6.467  -0.947  39.320  1.00118.24           C  
ANISOU 6692  CG2 ILE B 317    16340  17808  10777   -683    843   2293       C  
ATOM   6693  CD1 ILE B 317       6.720   1.961  40.535  1.00116.15           C  
ANISOU 6693  CD1 ILE B 317    16656  17121  10353   -764   1088   2449       C  
ATOM   6694  N   PHE B 318       9.772  -2.564  40.283  1.00104.29           N  
ANISOU 6694  N   PHE B 318    14327  16089   9209  -1139    687   2109       N  
ATOM   6695  CA  PHE B 318      10.041  -3.940  40.625  1.00101.34           C  
ANISOU 6695  CA  PHE B 318    13760  15802   8939  -1158    590   2033       C  
ATOM   6696  C   PHE B 318      10.343  -4.080  42.087  1.00102.62           C  
ANISOU 6696  C   PHE B 318    13956  15886   9149  -1247    562   2017       C  
ATOM   6697  O   PHE B 318       9.740  -4.931  42.738  1.00103.60           O  
ANISOU 6697  O   PHE B 318    14007  16009   9346  -1188    511   1992       O  
ATOM   6698  CB  PHE B 318      11.195  -4.511  39.855  1.00100.68           C  
ANISOU 6698  CB  PHE B 318    13538  15841   8874  -1232    557   1985       C  
ATOM   6699  CG  PHE B 318      11.816  -5.721  40.506  1.00101.01           C  
ANISOU 6699  CG  PHE B 318    13431  15937   9008  -1278    478   1920       C  
ATOM   6700  CD1 PHE B 318      11.168  -6.948  40.477  1.00100.72           C  
ANISOU 6700  CD1 PHE B 318    13267  15946   9056  -1181    428   1873       C  
ATOM   6701  CD2 PHE B 318      13.074  -5.630  41.149  1.00102.11           C  
ANISOU 6701  CD2 PHE B 318    13561  16094   9140  -1420    465   1906       C  
ATOM   6702  CE1 PHE B 318      11.743  -8.061  41.076  1.00104.22           C  
ANISOU 6702  CE1 PHE B 318    13597  16422   9580  -1205    375   1826       C  
ATOM   6703  CE2 PHE B 318      13.648  -6.727  41.761  1.00103.38           C  
ANISOU 6703  CE2 PHE B 318    13589  16319   9371  -1433    401   1862       C  
ATOM   6704  CZ  PHE B 318      12.980  -7.947  41.734  1.00105.47           C  
ANISOU 6704  CZ  PHE B 318    13748  16600   9725  -1317    360   1828       C  
ATOM   6705  N   VAL B 319      11.297  -3.293  42.602  1.00106.10           N  
ANISOU 6705  N   VAL B 319    14496  16272   9542  -1396    598   2027       N  
ATOM   6706  CA  VAL B 319      11.670  -3.428  44.047  1.00106.43           C  
ANISOU 6706  CA  VAL B 319    14552  16269   9614  -1491    568   2006       C  
ATOM   6707  C   VAL B 319      10.463  -3.147  44.956  1.00105.72           C  
ANISOU 6707  C   VAL B 319    14576  16056   9535  -1408    584   2039       C  
ATOM   6708  O   VAL B 319      10.149  -3.987  45.824  1.00109.04           O  
ANISOU 6708  O   VAL B 319    14918  16484  10028  -1375    523   2017       O  
ATOM   6709  CB  VAL B 319      12.880  -2.553  44.503  1.00106.24           C  
ANISOU 6709  CB  VAL B 319    14617  16231   9519  -1691    612   1995       C  
ATOM   6710  CG1 VAL B 319      13.075  -2.675  46.002  1.00106.07           C  
ANISOU 6710  CG1 VAL B 319    14604  16182   9516  -1767    582   1975       C  
ATOM   6711  CG2 VAL B 319      14.178  -2.947  43.817  1.00106.29           C  
ANISOU 6711  CG2 VAL B 319    14482  16391   9512  -1786    584   1954       C  
ATOM   6712  N   ILE B 320       9.788  -1.996  44.737  1.00102.88           N  
ANISOU 6712  N   ILE B 320    14402  15586   9099  -1363    671   2097       N  
ATOM   6713  CA  ILE B 320       8.610  -1.646  45.560  1.00 98.35           C  
ANISOU 6713  CA  ILE B 320    13945  14903   8521  -1268    694   2134       C  
ATOM   6714  C   ILE B 320       7.691  -2.854  45.639  1.00 98.66           C  
ANISOU 6714  C   ILE B 320    13825  15017   8642  -1136    616   2111       C  
ATOM   6715  O   ILE B 320       7.374  -3.289  46.709  1.00 99.02           O  
ANISOU 6715  O   ILE B 320    13852  15031   8737  -1137    577   2098       O  
ATOM   6716  CB  ILE B 320       7.841  -0.427  45.041  1.00 97.97           C  
ANISOU 6716  CB  ILE B 320    14094  14754   8375  -1172    802   2210       C  
ATOM   6717  CG1 ILE B 320       8.706   0.811  45.163  1.00101.84           C  
ANISOU 6717  CG1 ILE B 320    14782  15128   8785  -1325    902   2227       C  
ATOM   6718  CG2 ILE B 320       6.596  -0.168  45.862  1.00 96.23           C  
ANISOU 6718  CG2 ILE B 320    13969  14445   8145  -1052    820   2248       C  
ATOM   6719  CD1 ILE B 320       8.219   1.986  44.335  1.00106.01           C  
ANISOU 6719  CD1 ILE B 320    15509  15561   9208  -1232   1029   2309       C  
ATOM   6720  N   VAL B 321       7.343  -3.449  44.508  1.00101.56           N  
ANISOU 6720  N   VAL B 321    14070  15494   9023  -1041    594   2098       N  
ATOM   6721  CA  VAL B 321       6.379  -4.539  44.509  1.00102.69           C  
ANISOU 6721  CA  VAL B 321    14076  15710   9231   -932    539   2065       C  
ATOM   6722  C   VAL B 321       6.963  -5.853  45.065  1.00 95.96           C  
ANISOU 6722  C   VAL B 321    13072  14900   8486   -996    463   2000       C  
ATOM   6723  O   VAL B 321       6.378  -6.442  45.966  1.00 94.56           O  
ANISOU 6723  O   VAL B 321    12871  14693   8365   -969    434   1987       O  
ATOM   6724  CB  VAL B 321       5.741  -4.696  43.085  1.00109.69           C  
ANISOU 6724  CB  VAL B 321    14881  16716  10077   -813    552   2063       C  
ATOM   6725  CG1 VAL B 321       5.051  -6.053  42.900  1.00112.99           C  
ANISOU 6725  CG1 VAL B 321    15119  17242  10569   -754    495   1993       C  
ATOM   6726  CG2 VAL B 321       4.765  -3.544  42.826  1.00110.16           C  
ANISOU 6726  CG2 VAL B 321    15088  16739  10027   -690    628   2143       C  
ATOM   6727  N   TYR B 322       8.089  -6.309  44.537  1.00 93.05           N  
ANISOU 6727  N   TYR B 322    12609  14604   8141  -1069    439   1964       N  
ATOM   6728  CA  TYR B 322       8.609  -7.621  44.908  1.00 92.34           C  
ANISOU 6728  CA  TYR B 322    12375  14563   8144  -1093    380   1911       C  
ATOM   6729  C   TYR B 322       9.095  -7.652  46.346  1.00 96.97           C  
ANISOU 6729  C   TYR B 322    12999  15089   8754  -1164    360   1923       C  
ATOM   6730  O   TYR B 322       8.810  -8.641  47.072  1.00103.70           O  
ANISOU 6730  O   TYR B 322    13786  15932   9681  -1128    327   1904       O  
ATOM   6731  CB  TYR B 322       9.733  -8.030  43.979  1.00 91.89           C  
ANISOU 6731  CB  TYR B 322    12213  14610   8091  -1139    365   1876       C  
ATOM   6732  CG  TYR B 322      10.321  -9.362  44.265  1.00 89.92           C  
ANISOU 6732  CG  TYR B 322    11828  14412   7926  -1139    320   1829       C  
ATOM   6733  CD1 TYR B 322       9.775 -10.518  43.718  1.00 89.50           C  
ANISOU 6733  CD1 TYR B 322    11669  14396   7940  -1061    310   1776       C  
ATOM   6734  CD2 TYR B 322      11.453  -9.466  45.056  1.00 92.16           C  
ANISOU 6734  CD2 TYR B 322    12091  14715   8210  -1217    298   1836       C  
ATOM   6735  CE1 TYR B 322      10.340 -11.761  43.947  1.00 92.14           C  
ANISOU 6735  CE1 TYR B 322    11902  14755   8349  -1050    289   1737       C  
ATOM   6736  CE2 TYR B 322      12.019 -10.700  45.326  1.00 95.63           C  
ANISOU 6736  CE2 TYR B 322    12414  15206   8715  -1188    267   1807       C  
ATOM   6737  CZ  TYR B 322      11.457 -11.856  44.771  1.00 95.81           C  
ANISOU 6737  CZ  TYR B 322    12355  15234   8814  -1099    267   1761       C  
ATOM   6738  OH  TYR B 322      12.031 -13.086  45.069  1.00 97.28           O  
ANISOU 6738  OH  TYR B 322    12452  15446   9064  -1059    256   1739       O  
ATOM   6739  N   TYR B 323       9.813  -6.609  46.792  1.00 99.95           N  
ANISOU 6739  N   TYR B 323    13482  15430   9063  -1269    386   1950       N  
ATOM   6740  CA  TYR B 323      10.246  -6.575  48.216  1.00100.35           C  
ANISOU 6740  CA  TYR B 323    13562  15446   9118  -1344    367   1956       C  
ATOM   6741  C   TYR B 323       9.044  -6.606  49.138  1.00100.57           C  
ANISOU 6741  C   TYR B 323    13658  15379   9174  -1270    368   1978       C  
ATOM   6742  O   TYR B 323       8.984  -7.416  50.086  1.00109.05           O  
ANISOU 6742  O   TYR B 323    14672  16453  10306  -1253    330   1971       O  
ATOM   6743  CB  TYR B 323      11.088  -5.334  48.531  1.00100.76           C  
ANISOU 6743  CB  TYR B 323    13731  15474   9076  -1491    411   1967       C  
ATOM   6744  CG  TYR B 323      11.652  -5.307  49.924  1.00100.21           C  
ANISOU 6744  CG  TYR B 323    13668  15412   8995  -1583    390   1959       C  
ATOM   6745  CD1 TYR B 323      12.885  -5.860  50.189  1.00102.92           C  
ANISOU 6745  CD1 TYR B 323    13881  15891   9332  -1658    349   1931       C  
ATOM   6746  CD2 TYR B 323      10.948  -4.736  50.978  1.00100.15           C  
ANISOU 6746  CD2 TYR B 323    13786  15293   8970  -1586    413   1981       C  
ATOM   6747  CE1 TYR B 323      13.392  -5.839  51.469  1.00105.36           C  
ANISOU 6747  CE1 TYR B 323    14179  16238   9612  -1735    330   1925       C  
ATOM   6748  CE2 TYR B 323      11.434  -4.716  52.259  1.00100.72           C  
ANISOU 6748  CE2 TYR B 323    13856  15388   9023  -1670    394   1970       C  
ATOM   6749  CZ  TYR B 323      12.657  -5.264  52.496  1.00104.20           C  
ANISOU 6749  CZ  TYR B 323    14159  15978   9452  -1745    352   1942       C  
ATOM   6750  OH  TYR B 323      13.223  -5.229  53.745  1.00109.83           O  
ANISOU 6750  OH  TYR B 323    14851  16753  10126  -1829    333   1930       O  
ATOM   6751  N   ALA B 324       8.082  -5.733  48.861  1.00 98.93           N  
ANISOU 6751  N   ALA B 324    13573  15095   8918  -1216    417   2011       N  
ATOM   6752  CA  ALA B 324       6.850  -5.662  49.658  1.00 99.42           C  
ANISOU 6752  CA  ALA B 324    13702  15079   8991  -1134    423   2034       C  
ATOM   6753  C   ALA B 324       6.095  -6.980  49.663  1.00 98.24           C  
ANISOU 6753  C   ALA B 324    13420  14977   8929  -1042    379   2005       C  
ATOM   6754  O   ALA B 324       5.602  -7.409  50.702  1.00 98.54           O  
ANISOU 6754  O   ALA B 324    13456  14975   9007  -1023    360   2008       O  
ATOM   6755  CB  ALA B 324       5.953  -4.539  49.158  1.00 99.89           C  
ANISOU 6755  CB  ALA B 324    13905  15076   8969  -1060    491   2080       C  
ATOM   6756  N   LEU B 325       6.016  -7.619  48.497  1.00 99.57           N  
ANISOU 6756  N   LEU B 325    13480  15229   9122   -996    371   1971       N  
ATOM   6757  CA  LEU B 325       5.418  -8.968  48.397  1.00 99.05           C  
ANISOU 6757  CA  LEU B 325    13286  15208   9139   -937    344   1923       C  
ATOM   6758  C   LEU B 325       6.155 -10.031  49.208  1.00 96.77           C  
ANISOU 6758  C   LEU B 325    12923  14910   8931   -978    310   1904       C  
ATOM   6759  O   LEU B 325       5.536 -10.725  49.997  1.00 96.76           O  
ANISOU 6759  O   LEU B 325    12907  14871   8984   -947    304   1898       O  
ATOM   6760  CB  LEU B 325       5.405  -9.403  46.952  1.00103.91           C  
ANISOU 6760  CB  LEU B 325    13802  15922   9755   -904    349   1879       C  
ATOM   6761  CG  LEU B 325       4.856 -10.782  46.596  1.00107.08           C  
ANISOU 6761  CG  LEU B 325    14075  16376  10233   -866    340   1808       C  
ATOM   6762  CD1 LEU B 325       3.358 -10.695  46.427  1.00108.16           C  
ANISOU 6762  CD1 LEU B 325    14212  16547  10336   -793    360   1796       C  
ATOM   6763  CD2 LEU B 325       5.527 -11.301  45.310  1.00110.90           C  
ANISOU 6763  CD2 LEU B 325    14455  16953  10727   -877    338   1757       C  
ATOM   6764  N   MET B 326       7.463 -10.151  49.020  1.00 97.55           N  
ANISOU 6764  N   MET B 326    12978  15056   9031  -1039    295   1898       N  
ATOM   6765  CA  MET B 326       8.228 -11.125  49.806  1.00102.17           C  
ANISOU 6765  CA  MET B 326    13492  15652   9674  -1051    269   1894       C  
ATOM   6766  C   MET B 326       8.280 -10.844  51.327  1.00105.12           C  
ANISOU 6766  C   MET B 326    13929  15972  10036  -1080    257   1936       C  
ATOM   6767  O   MET B 326       8.226 -11.774  52.125  1.00109.54           O  
ANISOU 6767  O   MET B 326    14449  16515  10654  -1042    247   1941       O  
ATOM   6768  CB  MET B 326       9.648 -11.303  49.243  1.00104.01           C  
ANISOU 6768  CB  MET B 326    13646  15981   9890  -1097    254   1880       C  
ATOM   6769  CG  MET B 326       9.704 -12.067  47.926  1.00104.91           C  
ANISOU 6769  CG  MET B 326    13664  16153  10041  -1053    262   1830       C  
ATOM   6770  SD  MET B 326       8.789 -13.617  48.014  1.00109.04           S  
ANISOU 6770  SD  MET B 326    14130  16628  10673   -965    279   1785       S  
ATOM   6771  CE  MET B 326       8.275 -13.832  46.319  1.00108.81           C  
ANISOU 6771  CE  MET B 326    14037  16662  10642   -941    300   1715       C  
ATOM   6772  N   ALA B 327       8.350  -9.588  51.746  1.00105.94           N  
ANISOU 6772  N   ALA B 327    14142  16046  10064  -1144    268   1964       N  
ATOM   6773  CA  ALA B 327       8.284  -9.293  53.187  1.00108.63           C  
ANISOU 6773  CA  ALA B 327    14546  16340  10388  -1174    260   1994       C  
ATOM   6774  C   ALA B 327       6.924  -9.673  53.797  1.00109.80           C  
ANISOU 6774  C   ALA B 327    14726  16408  10583  -1091    265   2006       C  
ATOM   6775  O   ALA B 327       6.839 -10.217  54.915  1.00112.13           O  
ANISOU 6775  O   ALA B 327    15007  16685  10911  -1076    250   2024       O  
ATOM   6776  CB  ALA B 327       8.566  -7.822  53.434  1.00112.74           C  
ANISOU 6776  CB  ALA B 327    15195  16828  10812  -1271    288   2009       C  
ATOM   6777  N   GLY B 328       5.861  -9.375  53.054  1.00111.03           N  
ANISOU 6777  N   GLY B 328    14918  16536  10732  -1035    290   1998       N  
ATOM   6778  CA  GLY B 328       4.511  -9.735  53.455  1.00111.43           C  
ANISOU 6778  CA  GLY B 328    14981  16543  10813   -960    298   2000       C  
ATOM   6779  C   GLY B 328       4.303 -11.236  53.611  1.00111.46           C  
ANISOU 6779  C   GLY B 328    14878  16558  10911   -923    288   1970       C  
ATOM   6780  O   GLY B 328       3.518 -11.656  54.457  1.00115.73           O  
ANISOU 6780  O   GLY B 328    15432  17056  11484   -893    292   1979       O  
ATOM   6781  N   PHE B 329       5.002 -12.037  52.818  1.00108.98           N  
ANISOU 6781  N   PHE B 329    14472  16295  10640   -927    285   1935       N  
ATOM   6782  CA  PHE B 329       4.936 -13.471  52.960  1.00109.11           C  
ANISOU 6782  CA  PHE B 329    14412  16299  10744   -894    296   1907       C  
ATOM   6783  C   PHE B 329       5.646 -13.999  54.178  1.00106.27           C  
ANISOU 6783  C   PHE B 329    14050  15913  10413   -892    285   1950       C  
ATOM   6784  O   PHE B 329       5.167 -14.951  54.824  1.00107.06           O  
ANISOU 6784  O   PHE B 329    14143  15960  10575   -854    307   1952       O  
ATOM   6785  CB  PHE B 329       5.527 -14.144  51.745  1.00113.78           C  
ANISOU 6785  CB  PHE B 329    14917  16947  11365   -890    305   1857       C  
ATOM   6786  CG  PHE B 329       4.614 -14.194  50.564  1.00120.16           C  
ANISOU 6786  CG  PHE B 329    15692  17794  12168   -875    327   1797       C  
ATOM   6787  CD1 PHE B 329       3.261 -14.518  50.690  1.00122.33           C  
ANISOU 6787  CD1 PHE B 329    15968  18052  12457   -853    352   1765       C  
ATOM   6788  CD2 PHE B 329       5.132 -13.966  49.297  1.00125.84           C  
ANISOU 6788  CD2 PHE B 329    16365  18590  12859   -884    325   1766       C  
ATOM   6789  CE1 PHE B 329       2.458 -14.593  49.572  1.00130.64           C  
ANISOU 6789  CE1 PHE B 329    16967  19183  13487   -841    372   1702       C  
ATOM   6790  CE2 PHE B 329       4.324 -14.029  48.174  1.00129.26           C  
ANISOU 6790  CE2 PHE B 329    16751  19087  13273   -865    344   1709       C  
ATOM   6791  CZ  PHE B 329       2.986 -14.349  48.306  1.00131.54           C  
ANISOU 6791  CZ  PHE B 329    17031  19377  13568   -844    367   1674       C  
ATOM   6792  N   VAL B 330       6.782 -13.407  54.507  1.00103.82           N  
ANISOU 6792  N   VAL B 330    13744  15651  10050   -934    257   1983       N  
ATOM   6793  CA  VAL B 330       7.473 -13.822  55.738  1.00108.64           C  
ANISOU 6793  CA  VAL B 330    14340  16275  10663   -924    244   2029       C  
ATOM   6794  C   VAL B 330       6.772 -13.290  57.000  1.00105.33           C  
ANISOU 6794  C   VAL B 330    14001  15799  10220   -934    238   2066       C  
ATOM   6795  O   VAL B 330       6.704 -14.005  58.046  1.00109.39           O  
ANISOU 6795  O   VAL B 330    14505  16291  10765   -890    242   2101       O  
ATOM   6796  CB  VAL B 330       9.002 -13.553  55.743  1.00113.85           C  
ANISOU 6796  CB  VAL B 330    14944  17048  11262   -967    217   2044       C  
ATOM   6797  CG1 VAL B 330       9.735 -14.531  54.807  1.00115.44           C  
ANISOU 6797  CG1 VAL B 330    15050  17306  11505   -919    228   2020       C  
ATOM   6798  CG2 VAL B 330       9.323 -12.133  55.350  1.00118.45           C  
ANISOU 6798  CG2 VAL B 330    15580  17665  11758  -1069    205   2031       C  
ATOM   6799  N   TRP B 331       6.212 -12.078  56.917  1.00100.01           N  
ANISOU 6799  N   TRP B 331    13412  15098   9489   -978    237   2062       N  
ATOM   6800  CA  TRP B 331       5.355 -11.590  58.017  1.00 97.20           C  
ANISOU 6800  CA  TRP B 331    13139  14679   9112   -974    239   2091       C  
ATOM   6801  C   TRP B 331       4.126 -12.462  58.228  1.00 95.25           C  
ANISOU 6801  C   TRP B 331    12882  14373   8934   -904    259   2085       C  
ATOM   6802  O   TRP B 331       3.640 -12.590  59.362  1.00 98.69           O  
ANISOU 6802  O   TRP B 331    13350  14772   9376   -887    260   2116       O  
ATOM   6803  CB  TRP B 331       4.932 -10.127  57.842  1.00 96.56           C  
ANISOU 6803  CB  TRP B 331    13170  14565   8951  -1016    251   2091       C  
ATOM   6804  CG  TRP B 331       5.952  -9.143  58.293  1.00 95.81           C  
ANISOU 6804  CG  TRP B 331    13127  14499   8775  -1114    245   2099       C  
ATOM   6805  CD1 TRP B 331       6.692  -8.354  57.508  1.00 95.84           C  
ANISOU 6805  CD1 TRP B 331    13158  14533   8723  -1187    257   2081       C  
ATOM   6806  CD2 TRP B 331       6.366  -8.876  59.637  1.00 95.00           C  
ANISOU 6806  CD2 TRP B 331    13050  14411   8633  -1164    231   2120       C  
ATOM   6807  NE1 TRP B 331       7.531  -7.596  58.255  1.00 95.91           N  
ANISOU 6807  NE1 TRP B 331    13211  14571   8657  -1293    258   2080       N  
ATOM   6808  CE2 TRP B 331       7.366  -7.902  59.568  1.00 94.62           C  
ANISOU 6808  CE2 TRP B 331    13041  14408   8499  -1281    239   2101       C  
ATOM   6809  CE3 TRP B 331       6.012  -9.393  60.884  1.00 95.05           C  
ANISOU 6809  CE3 TRP B 331    13045  14408   8661  -1126    217   2149       C  
ATOM   6810  CZ2 TRP B 331       8.004  -7.392  60.690  1.00 96.71           C  
ANISOU 6810  CZ2 TRP B 331    13331  14721   8694  -1373    233   2100       C  
ATOM   6811  CZ3 TRP B 331       6.646  -8.890  62.017  1.00 97.58           C  
ANISOU 6811  CZ3 TRP B 331    13387  14776   8913  -1199    205   2159       C  
ATOM   6812  CH2 TRP B 331       7.631  -7.896  61.908  1.00 99.31           C  
ANISOU 6812  CH2 TRP B 331    13640  15052   9042  -1325    213   2129       C  
ATOM   6813  N   PHE B 332       3.634 -13.076  57.163  1.00 94.16           N  
ANISOU 6813  N   PHE B 332    12695  14238   8842   -875    281   2041       N  
ATOM   6814  CA  PHE B 332       2.579 -14.091  57.290  1.00 94.48           C  
ANISOU 6814  CA  PHE B 332    12711  14238   8949   -834    313   2017       C  
ATOM   6815  C   PHE B 332       3.070 -15.326  58.077  1.00 90.40           C  
ANISOU 6815  C   PHE B 332    12162  13686   8500   -807    330   2042       C  
ATOM   6816  O   PHE B 332       2.347 -15.834  58.935  1.00 89.88           O  
ANISOU 6816  O   PHE B 332    12119  13566   8465   -786    353   2059       O  
ATOM   6817  CB  PHE B 332       2.010 -14.487  55.911  1.00 95.96           C  
ANISOU 6817  CB  PHE B 332    12843  14458   9157   -827    338   1947       C  
ATOM   6818  CG  PHE B 332       1.304 -15.814  55.898  1.00 99.41           C  
ANISOU 6818  CG  PHE B 332    13237  14862   9670   -817    386   1901       C  
ATOM   6819  CD1 PHE B 332       0.014 -15.902  56.355  1.00101.68           C  
ANISOU 6819  CD1 PHE B 332    13542  15135   9955   -814    407   1887       C  
ATOM   6820  CD2 PHE B 332       1.944 -16.985  55.447  1.00101.04           C  
ANISOU 6820  CD2 PHE B 332    13393  15049   9946   -814    419   1869       C  
ATOM   6821  CE1 PHE B 332      -0.642 -17.128  56.367  1.00103.94           C  
ANISOU 6821  CE1 PHE B 332    13797  15387  10306   -829    465   1835       C  
ATOM   6822  CE2 PHE B 332       1.295 -18.210  55.466  1.00102.57           C  
ANISOU 6822  CE2 PHE B 332    13573  15189  10210   -819    484   1820       C  
ATOM   6823  CZ  PHE B 332      -0.013 -18.281  55.914  1.00103.45           C  
ANISOU 6823  CZ  PHE B 332    13702  15285  10317   -838    509   1799       C  
ATOM   6824  N   VAL B 333       4.280 -15.790  57.797  1.00 87.35           N  
ANISOU 6824  N   VAL B 333    11725  13333   8127   -798    326   2050       N  
ATOM   6825  CA  VAL B 333       4.795 -16.935  58.524  1.00 89.64           C  
ANISOU 6825  CA  VAL B 333    11994  13595   8468   -744    354   2088       C  
ATOM   6826  C   VAL B 333       4.968 -16.546  59.979  1.00 91.48           C  
ANISOU 6826  C   VAL B 333    12262  13836   8659   -736    328   2159       C  
ATOM   6827  O   VAL B 333       4.644 -17.310  60.889  1.00 90.11           O  
ANISOU 6827  O   VAL B 333    12105  13608   8521   -687    359   2198       O  
ATOM   6828  CB  VAL B 333       6.132 -17.466  57.946  1.00 91.36           C  
ANISOU 6828  CB  VAL B 333    12146  13874   8691   -714    355   2091       C  
ATOM   6829  CG1 VAL B 333       6.675 -18.637  58.759  1.00 91.72           C  
ANISOU 6829  CG1 VAL B 333    12180  13894   8774   -625    395   2148       C  
ATOM   6830  CG2 VAL B 333       5.942 -17.955  56.525  1.00 92.46           C  
ANISOU 6830  CG2 VAL B 333    12250  14003   8875   -721    387   2015       C  
ATOM   6831  N   VAL B 334       5.475 -15.333  60.201  1.00 97.35           N  
ANISOU 6831  N   VAL B 334    13021  14647   9319   -790    278   2173       N  
ATOM   6832  CA  VAL B 334       5.599 -14.814  61.592  1.00 99.04           C  
ANISOU 6832  CA  VAL B 334    13270  14882   9477   -801    253   2226       C  
ATOM   6833  C   VAL B 334       4.234 -14.774  62.314  1.00 98.35           C  
ANISOU 6833  C   VAL B 334    13248  14707   9411   -787    270   2235       C  
ATOM   6834  O   VAL B 334       4.137 -15.063  63.536  1.00 97.38           O  
ANISOU 6834  O   VAL B 334    13139  14577   9285   -756    273   2285       O  
ATOM   6835  CB  VAL B 334       6.277 -13.427  61.598  1.00100.54           C  
ANISOU 6835  CB  VAL B 334    13484  15146   9569   -892    214   2216       C  
ATOM   6836  CG1 VAL B 334       6.129 -12.740  62.949  1.00102.76           C  
ANISOU 6836  CG1 VAL B 334    13819  15435   9787   -923    197   2248       C  
ATOM   6837  CG2 VAL B 334       7.750 -13.568  61.219  1.00101.10           C  
ANISOU 6837  CG2 VAL B 334    13470  15338   9602   -909    196   2216       C  
ATOM   6838  N   LEU B 335       3.181 -14.443  61.563  1.00 97.67           N  
ANISOU 6838  N   LEU B 335    13195  14575   9339   -802    284   2188       N  
ATOM   6839  CA  LEU B 335       1.812 -14.551  62.102  1.00 96.55           C  
ANISOU 6839  CA  LEU B 335    13096  14373   9216   -782    306   2188       C  
ATOM   6840  C   LEU B 335       1.432 -16.006  62.473  1.00 91.55           C  
ANISOU 6840  C   LEU B 335    12434  13683   8665   -739    356   2197       C  
ATOM   6841  O   LEU B 335       0.874 -16.235  63.510  1.00 86.94           O  
ANISOU 6841  O   LEU B 335    11880  13064   8087   -720    369   2232       O  
ATOM   6842  CB  LEU B 335       0.817 -13.942  61.101  1.00 97.95           C  
ANISOU 6842  CB  LEU B 335    13290  14552   9371   -793    314   2135       C  
ATOM   6843  CG  LEU B 335      -0.642 -13.831  61.555  1.00 99.91           C  
ANISOU 6843  CG  LEU B 335    13572  14777   9609   -773    332   2130       C  
ATOM   6844  CD1 LEU B 335      -1.313 -12.579  61.009  1.00 99.02           C  
ANISOU 6844  CD1 LEU B 335    13510  14696   9418   -764    324   2116       C  
ATOM   6845  CD2 LEU B 335      -1.418 -15.079  61.142  1.00101.29           C  
ANISOU 6845  CD2 LEU B 335    13690  14938   9856   -767    380   2083       C  
ATOM   6846  N   THR B 336       1.732 -16.967  61.616  1.00 89.77           N  
ANISOU 6846  N   THR B 336    12163  13442   8500   -725    393   2163       N  
ATOM   6847  CA  THR B 336       1.414 -18.354  61.924  1.00 89.29           C  
ANISOU 6847  CA  THR B 336    12103  13305   8518   -691    463   2167       C  
ATOM   6848  C   THR B 336       2.220 -18.822  63.101  1.00 92.53           C  
ANISOU 6848  C   THR B 336    12523  13706   8927   -628    468   2256       C  
ATOM   6849  O   THR B 336       1.734 -19.565  63.940  1.00 98.23           O  
ANISOU 6849  O   THR B 336    13279  14360   9684   -596    518   2292       O  
ATOM   6850  CB  THR B 336       1.701 -19.269  60.745  1.00 90.07           C  
ANISOU 6850  CB  THR B 336    12164  13381   8676   -690    512   2107       C  
ATOM   6851  OG1 THR B 336       3.075 -19.090  60.369  1.00 91.65           O  
ANISOU 6851  OG1 THR B 336    12325  13644   8853   -663    478   2131       O  
ATOM   6852  CG2 THR B 336       0.779 -18.903  59.568  1.00 92.07           C  
ANISOU 6852  CG2 THR B 336    12392  13666   8922   -750    513   2014       C  
ATOM   6853  N   TYR B 337       3.463 -18.381  63.192  1.00 96.34           N  
ANISOU 6853  N   TYR B 337    12970  14274   9358   -611    421   2293       N  
ATOM   6854  CA  TYR B 337       4.309 -18.754  64.335  1.00 98.29           C  
ANISOU 6854  CA  TYR B 337    13206  14562   9578   -539    419   2382       C  
ATOM   6855  C   TYR B 337       3.774 -18.158  65.626  1.00 95.09           C  
ANISOU 6855  C   TYR B 337    12839  14164   9125   -552    392   2425       C  
ATOM   6856  O   TYR B 337       3.760 -18.837  66.695  1.00 92.81           O  
ANISOU 6856  O   TYR B 337    12564  13855   8844   -483    424   2496       O  
ATOM   6857  CB  TYR B 337       5.742 -18.305  64.123  1.00101.82           C  
ANISOU 6857  CB  TYR B 337    13587  15142   9956   -535    370   2399       C  
ATOM   6858  CG  TYR B 337       6.656 -18.582  65.297  1.00106.84           C  
ANISOU 6858  CG  TYR B 337    14186  15872  10534   -458    361   2488       C  
ATOM   6859  CD1 TYR B 337       7.185 -19.867  65.513  1.00107.99           C  
ANISOU 6859  CD1 TYR B 337    14312  16004  10712   -330    423   2551       C  
ATOM   6860  CD2 TYR B 337       6.996 -17.554  66.197  1.00108.25           C  
ANISOU 6860  CD2 TYR B 337    14351  16162  10614   -509    299   2509       C  
ATOM   6861  CE1 TYR B 337       8.056 -20.104  66.558  1.00109.14           C  
ANISOU 6861  CE1 TYR B 337    14411  16269  10785   -238    416   2642       C  
ATOM   6862  CE2 TYR B 337       7.846 -17.783  67.240  1.00109.67           C  
ANISOU 6862  CE2 TYR B 337    14478  16467  10722   -442    288   2584       C  
ATOM   6863  CZ  TYR B 337       8.387 -19.056  67.417  1.00110.75           C  
ANISOU 6863  CZ  TYR B 337    14581  16614  10885   -298    343   2656       C  
ATOM   6864  OH  TYR B 337       9.230 -19.313  68.460  1.00119.57           O  
ANISOU 6864  OH  TYR B 337    15634  17880  11915   -206    335   2742       O  
ATOM   6865  N   ALA B 338       3.343 -16.896  65.529  1.00 93.09           N  
ANISOU 6865  N   ALA B 338    12612  13938   8820   -630    341   2387       N  
ATOM   6866  CA  ALA B 338       2.740 -16.239  66.682  1.00 95.49           C  
ANISOU 6866  CA  ALA B 338    12963  14242   9076   -647    319   2416       C  
ATOM   6867  C   ALA B 338       1.537 -17.001  67.218  1.00 96.25           C  
ANISOU 6867  C   ALA B 338    13096  14244   9230   -614    371   2431       C  
ATOM   6868  O   ALA B 338       1.354 -17.107  68.429  1.00101.42           O  
ANISOU 6868  O   ALA B 338    13770  14900   9864   -584    374   2488       O  
ATOM   6869  CB  ALA B 338       2.323 -14.831  66.306  1.00 96.11           C  
ANISOU 6869  CB  ALA B 338    13087  14334   9096   -723    280   2367       C  
ATOM   6870  N   TRP B 339       0.717 -17.475  66.305  1.00 97.58           N  
ANISOU 6870  N   TRP B 339    13268  14346   9460   -631    413   2372       N  
ATOM   6871  CA  TRP B 339      -0.464 -18.266  66.637  1.00 96.28           C  
ANISOU 6871  CA  TRP B 339    13131  14100   9349   -627    475   2365       C  
ATOM   6872  C   TRP B 339      -0.087 -19.573  67.280  1.00 90.49           C  
ANISOU 6872  C   TRP B 339    12408  13304   8670   -561    543   2427       C  
ATOM   6873  O   TRP B 339      -0.681 -19.993  68.221  1.00 86.07           O  
ANISOU 6873  O   TRP B 339    11884  12698   8121   -542    579   2468       O  
ATOM   6874  CB  TRP B 339      -1.321 -18.471  65.351  1.00 97.04           C  
ANISOU 6874  CB  TRP B 339    13211  14174   9483   -677    507   2270       C  
ATOM   6875  CG  TRP B 339      -2.031 -19.777  65.252  1.00 97.13           C  
ANISOU 6875  CG  TRP B 339    13231  14101   9571   -690    601   2239       C  
ATOM   6876  CD1 TRP B 339      -1.544 -20.915  64.683  1.00 95.87           C  
ANISOU 6876  CD1 TRP B 339    13069  13876   9481   -678    671   2220       C  
ATOM   6877  CD2 TRP B 339      -3.332 -20.098  65.737  1.00 97.33           C  
ANISOU 6877  CD2 TRP B 339    13279  14094   9606   -725    647   2218       C  
ATOM   6878  NE1 TRP B 339      -2.480 -21.918  64.758  1.00 96.12           N  
ANISOU 6878  NE1 TRP B 339    13130  13823   9566   -717    767   2181       N  
ATOM   6879  CE2 TRP B 339      -3.580 -21.446  65.417  1.00 95.21           C  
ANISOU 6879  CE2 TRP B 339    13024  13735   9414   -752    751   2180       C  
ATOM   6880  CE3 TRP B 339      -4.314 -19.377  66.413  1.00 98.36           C  
ANISOU 6880  CE3 TRP B 339    13421  14267   9682   -739    617   2226       C  
ATOM   6881  CZ2 TRP B 339      -4.760 -22.080  65.749  1.00 94.31           C  
ANISOU 6881  CZ2 TRP B 339    12931  13578   9323   -810    826   2143       C  
ATOM   6882  CZ3 TRP B 339      -5.491 -20.013  66.741  1.00 97.56           C  
ANISOU 6882  CZ3 TRP B 339    13328  14138   9601   -782    682   2195       C  
ATOM   6883  CH2 TRP B 339      -5.709 -21.353  66.401  1.00 95.12           C  
ANISOU 6883  CH2 TRP B 339    13028  13744   9367   -826    786   2151       C  
ATOM   6884  N   HIS B 340       0.929 -20.193  66.753  1.00 91.47           N  
ANISOU 6884  N   HIS B 340    12505  13427   8820   -518    565   2438       N  
ATOM   6885  CA  HIS B 340       1.370 -21.471  67.255  1.00101.95           C  
ANISOU 6885  CA  HIS B 340    13855  14686  10192   -430    646   2505       C  
ATOM   6886  C   HIS B 340       1.953 -21.369  68.652  1.00107.74           C  
ANISOU 6886  C   HIS B 340    14587  15482  10866   -350    622   2615       C  
ATOM   6887  O   HIS B 340       1.695 -22.265  69.496  1.00113.11           O  
ANISOU 6887  O   HIS B 340    15315  16088  11574   -283    696   2683       O  
ATOM   6888  CB  HIS B 340       2.422 -22.074  66.312  1.00110.22           C  
ANISOU 6888  CB  HIS B 340    14871  15738  11267   -382    673   2494       C  
ATOM   6889  CG  HIS B 340       3.217 -23.168  66.925  1.00115.46           C  
ANISOU 6889  CG  HIS B 340    15555  16367  11944   -251    745   2590       C  
ATOM   6890  ND1 HIS B 340       4.333 -22.921  67.694  1.00119.67           N  
ANISOU 6890  ND1 HIS B 340    16040  17027  12399   -159    698   2683       N  
ATOM   6891  CD2 HIS B 340       3.036 -24.504  66.917  1.00118.78           C  
ANISOU 6891  CD2 HIS B 340    16046  16646  12437   -191    872   2611       C  
ATOM   6892  CE1 HIS B 340       4.820 -24.073  68.115  1.00126.29           C  
ANISOU 6892  CE1 HIS B 340    16912  17815  13257    -25    789   2768       C  
ATOM   6893  NE2 HIS B 340       4.053 -25.048  67.654  1.00126.50           N  
ANISOU 6893  NE2 HIS B 340    17023  17661  13380    -41    901   2728       N  
ATOM   6894  N   THR B 341       2.755 -20.322  68.884  1.00107.21           N  
ANISOU 6894  N   THR B 341    14468  15553  10712   -360    529   2630       N  
ATOM   6895  CA  THR B 341       3.326 -20.151  70.220  1.00105.57           C  
ANISOU 6895  CA  THR B 341    14241  15441  10428   -297    501   2722       C  
ATOM   6896  C   THR B 341       2.398 -19.450  71.208  1.00104.71           C  
ANISOU 6896  C   THR B 341    14169  15332  10284   -345    470   2728       C  
ATOM   6897  O   THR B 341       2.718 -19.394  72.390  1.00110.88           O  
ANISOU 6897  O   THR B 341    14937  16187  11003   -294    456   2802       O  
ATOM   6898  CB  THR B 341       4.640 -19.373  70.165  1.00106.19           C  
ANISOU 6898  CB  THR B 341    14240  15693  10412   -304    424   2727       C  
ATOM   6899  OG1 THR B 341       4.392 -18.017  69.756  1.00107.76           O  
ANISOU 6899  OG1 THR B 341    14444  15928  10569   -429    354   2649       O  
ATOM   6900  CG2 THR B 341       5.615 -20.064  69.218  1.00106.85           C  
ANISOU 6900  CG2 THR B 341    14277  15799  10520   -244    451   2727       C  
ATOM   6901  N   SER B 342       1.292 -18.885  70.750  1.00103.21           N  
ANISOU 6901  N   SER B 342    14017  15079  10118   -433    460   2653       N  
ATOM   6902  CA  SER B 342       0.348 -18.257  71.673  1.00105.41           C  
ANISOU 6902  CA  SER B 342    14334  15356  10360   -464    439   2660       C  
ATOM   6903  C   SER B 342      -0.226 -19.265  72.660  1.00109.00           C  
ANISOU 6903  C   SER B 342    14822  15743  10850   -403    508   2729       C  
ATOM   6904  O   SER B 342      -0.486 -18.942  73.809  1.00109.38           O  
ANISOU 6904  O   SER B 342    14882  15828  10847   -388    488   2777       O  
ATOM   6905  CB  SER B 342      -0.784 -17.582  70.899  1.00106.42           C  
ANISOU 6905  CB  SER B 342    14492  15441  10502   -544    427   2572       C  
ATOM   6906  OG  SER B 342      -1.575 -18.512  70.159  1.00105.03           O  
ANISOU 6906  OG  SER B 342    14323  15173  10408   -555    497   2529       O  
ATOM   6907  N   PHE B 343      -0.411 -20.497  72.191  1.00112.68           N  
ANISOU 6907  N   PHE B 343    15310  16102  11401   -371    597   2732       N  
ATOM   6908  CA  PHE B 343      -0.946 -21.575  73.033  1.00113.02           C  
ANISOU 6908  CA  PHE B 343    15405  16052  11484   -318    690   2798       C  
ATOM   6909  C   PHE B 343       0.005 -22.069  74.099  1.00118.88           C  
ANISOU 6909  C   PHE B 343    16139  16844  12184   -192    707   2923       C  
ATOM   6910  O   PHE B 343      -0.423 -22.661  75.061  1.00119.82           O  
ANISOU 6910  O   PHE B 343    16301  16915  12307   -142    766   2995       O  
ATOM   6911  CB  PHE B 343      -1.312 -22.792  72.185  1.00112.12           C  
ANISOU 6911  CB  PHE B 343    15335  15796  11470   -330    803   2759       C  
ATOM   6912  CG  PHE B 343      -2.477 -22.566  71.343  1.00109.52           C  
ANISOU 6912  CG  PHE B 343    15008  15428  11174   -449    810   2643       C  
ATOM   6913  CD1 PHE B 343      -3.727 -22.429  71.928  1.00107.34           C  
ANISOU 6913  CD1 PHE B 343    14756  15138  10891   -506    825   2627       C  
ATOM   6914  CD2 PHE B 343      -2.325 -22.421  69.977  1.00110.84           C  
ANISOU 6914  CD2 PHE B 343    15143  15603  11367   -501    796   2551       C  
ATOM   6915  CE1 PHE B 343      -4.833 -22.181  71.155  1.00108.14           C  
ANISOU 6915  CE1 PHE B 343    14840  15244  11001   -608    829   2519       C  
ATOM   6916  CE2 PHE B 343      -3.414 -22.159  69.192  1.00112.26           C  
ANISOU 6916  CE2 PHE B 343    15308  15785  11559   -603    799   2445       C  
ATOM   6917  CZ  PHE B 343      -4.681 -22.041  69.789  1.00111.12           C  
ANISOU 6917  CZ  PHE B 343    15180  15640  11398   -654    816   2429       C  
ATOM   6918  N   LYS B 344       1.305 -21.936  73.880  1.00131.43           N  
ANISOU 6918  N   LYS B 344    17670  18538  13729   -131    667   2952       N  
ATOM   6919  CA  LYS B 344       2.300 -22.375  74.873  1.00140.25           C  
ANISOU 6919  CA  LYS B 344    18756  19752  14780      7    679   3075       C  
ATOM   6920  C   LYS B 344       2.263 -21.435  76.073  1.00139.72           C  
ANISOU 6920  C   LYS B 344    18653  19822  14612    -10    599   3106       C  
ATOM   6921  O   LYS B 344       2.648 -21.843  77.194  1.00140.46           O  
ANISOU 6921  O   LYS B 344    18732  19988  14647     99    621   3214       O  
ATOM   6922  CB  LYS B 344       3.727 -22.440  74.267  1.00152.35           C  
ANISOU 6922  CB  LYS B 344    20214  21399  16273     73    654   3089       C  
ATOM   6923  CG  LYS B 344       3.891 -23.398  73.042  1.00160.85           C  
ANISOU 6923  CG  LYS B 344    21325  22345  17443    103    737   3057       C  
ATOM   6924  CD  LYS B 344       3.993 -24.866  73.443  1.00164.16           C  
ANISOU 6924  CD  LYS B 344    21818  22647  17906    255    875   3160       C  
ATOM   6925  CE  LYS B 344       3.612 -25.786  72.281  1.00160.07           C  
ANISOU 6925  CE  LYS B 344    21378  21935  17504    230    981   3094       C  
ATOM   6926  NZ  LYS B 344       3.374 -27.190  72.710  1.00158.01           N  
ANISOU 6926  NZ  LYS B 344    21235  21501  17300    341   1144   3178       N  
ATOM   6927  N   ALA B 345       1.808 -20.191  75.817  1.00138.50           N  
ANISOU 6927  N   ALA B 345    18490  19701  14430   -141    517   3013       N  
ATOM   6928  CA  ALA B 345       1.667 -19.160  76.829  1.00139.47           C  
ANISOU 6928  CA  ALA B 345    18598  19935  14460   -185    446   3015       C  
ATOM   6929  C   ALA B 345       0.671 -19.531  77.929  1.00141.93           C  
ANISOU 6929  C   ALA B 345    18959  20186  14779   -153    488   3072       C  
ATOM   6930  O   ALA B 345       0.875 -19.153  79.069  1.00152.91           O  
ANISOU 6930  O   ALA B 345    20324  21690  16084   -127    454   3122       O  
ATOM   6931  CB  ALA B 345       1.327 -17.817  76.194  1.00138.26           C  
ANISOU 6931  CB  ALA B 345    18456  19792  14284   -319    375   2905       C  
ATOM   6932  N   LEU B 346      -0.352 -20.325  77.632  1.00142.38           N  
ANISOU 6932  N   LEU B 346    19082  20081  14933   -157    568   3064       N  
ATOM   6933  CA  LEU B 346      -1.250 -20.829  78.718  1.00142.81           C  
ANISOU 6933  CA  LEU B 346    19185  20080  14994   -124    623   3128       C  
ATOM   6934  C   LEU B 346      -0.691 -21.973  79.580  1.00146.10           C  
ANISOU 6934  C   LEU B 346    19612  20495  15402     21    703   3263       C  
ATOM   6935  O   LEU B 346      -0.834 -21.940  80.798  1.00143.00           O  
ANISOU 6935  O   LEU B 346    19217  20165  14949     71    701   3339       O  
ATOM   6936  CB  LEU B 346      -2.656 -21.240  78.237  1.00138.47           C  
ANISOU 6936  CB  LEU B 346    18700  19378  14533   -201    689   3066       C  
ATOM   6937  CG  LEU B 346      -2.877 -22.209  77.044  1.00128.90           C  
ANISOU 6937  CG  LEU B 346    17523  18025  13425   -227    779   3016       C  
ATOM   6938  CD1 LEU B 346      -3.156 -23.640  77.479  1.00120.35           C  
ANISOU 6938  CD1 LEU B 346    16515  16808  12403   -167    918   3090       C  
ATOM   6939  CD2 LEU B 346      -3.986 -21.678  76.170  1.00127.47           C  
ANISOU 6939  CD2 LEU B 346    17343  17814  13273   -353    760   2893       C  
ATOM   6940  N   GLY B 347      -0.108 -22.990  78.946  1.00156.16           N  
ANISOU 6940  N   GLY B 347    20906  21693  16733     97    782   3297       N  
ATOM   6941  CA  GLY B 347       0.586 -24.085  79.643  1.00173.22           C  
ANISOU 6941  CA  GLY B 347    23085  23855  18875    269    870   3438       C  
ATOM   6942  C   GLY B 347       1.862 -23.676  80.410  1.00193.19           C  
ANISOU 6942  C   GLY B 347    25511  26620  21272    379    797   3521       C  
ATOM   6943  O   GLY B 347       2.824 -23.207  79.790  1.00197.91           O  
ANISOU 6943  O   GLY B 347    26030  27338  21828    372    730   3482       O  
ATOM   6944  N   THR B 348       1.845 -23.820  81.751  1.00208.42           N  
ANISOU 6944  N   THR B 348    27431  28632  23124    470    809   3628       N  
ATOM   6945  CA  THR B 348       2.962 -23.485  82.693  1.00213.17           C  
ANISOU 6945  CA  THR B 348    27922  29497  23577    580    747   3713       C  
ATOM   6946  C   THR B 348       3.500 -22.025  82.537  1.00223.24           C  
ANISOU 6946  C   THR B 348    29088  30972  24760    449    602   3606       C  
ATOM   6947  O   THR B 348       2.704 -21.093  82.653  1.00216.23           O  
ANISOU 6947  O   THR B 348    28221  30058  23876    305    543   3516       O  
ATOM   6948  CB  THR B 348       4.084 -24.570  82.733  1.00207.01           C  
ANISOU 6948  CB  THR B 348    27119  28775  22758    796    828   3845       C  
ATOM   6949  OG1 THR B 348       4.851 -24.528  81.527  1.00206.03           O  
ANISOU 6949  OG1 THR B 348    26956  28665  22660    780    806   3782       O  
ATOM   6950  CG2 THR B 348       3.528 -25.989  82.929  1.00202.85           C  
ANISOU 6950  CG2 THR B 348    26732  28021  22319    922    995   3953       C  
ATOM   6951  N   THR B 349       4.790 -21.794  82.248  1.00230.75           N  
ANISOU 6951  N   THR B 349    29933  32114  25625    488    552   3606       N  
ATOM   6952  CA  THR B 349       5.328 -20.421  82.265  1.00224.28           C  
ANISOU 6952  CA  THR B 349    29020  31493  24702    350    432   3506       C  
ATOM   6953  C   THR B 349       4.951 -19.663  80.989  1.00227.26           C  
ANISOU 6953  C   THR B 349    29441  31744  25163    177    391   3362       C  
ATOM   6954  O   THR B 349       4.908 -20.232  79.900  1.00226.53           O  
ANISOU 6954  O   THR B 349    29388  31509  25171    191    436   3341       O  
ATOM   6955  CB  THR B 349       6.861 -20.389  82.400  1.00216.47           C  
ANISOU 6955  CB  THR B 349    27886  30787  23574    431    394   3546       C  
ATOM   6956  OG1 THR B 349       7.450 -21.288  81.448  1.00208.71           O  
ANISOU 6956  OG1 THR B 349    26905  29744  22650    540    452   3583       O  
ATOM   6957  CG2 THR B 349       7.286 -20.758  83.814  1.00214.78           C  
ANISOU 6957  CG2 THR B 349    27597  30780  23227    581    405   3674       C  
ATOM   6958  N   TYR B 350       4.696 -18.364  81.150  1.00224.01           N  
ANISOU 6958  N   TYR B 350    29026  31389  24699     22    313   3263       N  
ATOM   6959  CA  TYR B 350       4.257 -17.467  80.062  1.00208.81           C  
ANISOU 6959  CA  TYR B 350    27153  29352  22831   -135    277   3133       C  
ATOM   6960  C   TYR B 350       5.408 -17.305  79.072  1.00193.90           C  
ANISOU 6960  C   TYR B 350    25195  27557  20918   -161    250   3090       C  
ATOM   6961  O   TYR B 350       6.542 -17.075  79.475  1.00181.63           O  
ANISOU 6961  O   TYR B 350    23536  26229  19245   -148    213   3106       O  
ATOM   6962  CB  TYR B 350       3.747 -16.100  80.615  1.00205.90           C  
ANISOU 6962  CB  TYR B 350    26817  29020  22395   -275    219   3052       C  
ATOM   6963  CG  TYR B 350       2.864 -16.273  81.852  1.00199.63           C  
ANISOU 6963  CG  TYR B 350    26059  28202  21587   -229    238   3110       C  
ATOM   6964  CD1 TYR B 350       1.537 -16.688  81.724  1.00194.19           C  
ANISOU 6964  CD1 TYR B 350    25462  27315  21005   -217    286   3116       C  
ATOM   6965  CD2 TYR B 350       3.368 -16.090  83.142  1.00193.65           C  
ANISOU 6965  CD2 TYR B 350    25233  27639  20703   -195    212   3160       C  
ATOM   6966  CE1 TYR B 350       0.731 -16.913  82.816  1.00190.54           C  
ANISOU 6966  CE1 TYR B 350    25031  26834  20532   -176    309   3172       C  
ATOM   6967  CE2 TYR B 350       2.563 -16.310  84.248  1.00197.77           C  
ANISOU 6967  CE2 TYR B 350    25788  28142  21214   -146    233   3219       C  
ATOM   6968  CZ  TYR B 350       1.240 -16.717  84.076  1.00197.73           C  
ANISOU 6968  CZ  TYR B 350    25881  27922  21324   -136    282   3226       C  
ATOM   6969  OH  TYR B 350       0.414 -16.934  85.160  1.00201.23           O  
ANISOU 6969  OH  TYR B 350    26355  28347  21754    -94    306   3284       O  
ATOM   6970  N   GLN B 351       5.117 -17.475  77.788  1.00198.07           N  
ANISOU 6970  N   GLN B 351    25772  27932  21553   -196    272   3035       N  
ATOM   6971  CA  GLN B 351       6.172 -17.461  76.735  1.00213.74           C  
ANISOU 6971  CA  GLN B 351    27692  29989  23528   -209    255   2999       C  
ATOM   6972  C   GLN B 351       5.993 -16.238  75.847  1.00223.42           C  
ANISOU 6972  C   GLN B 351    28955  31176  24758   -378    207   2875       C  
ATOM   6973  O   GLN B 351       5.071 -16.242  75.033  1.00222.47           O  
ANISOU 6973  O   GLN B 351    28913  30875  24737   -415    230   2829       O  
ATOM   6974  CB  GLN B 351       6.193 -18.752  75.879  1.00213.40           C  
ANISOU 6974  CB  GLN B 351    27669  29816  23595    -95    329   3042       C  
ATOM   6975  CG  GLN B 351       6.464 -20.028  76.659  1.00209.06           C  
ANISOU 6975  CG  GLN B 351    27106  29284  23040     92    401   3176       C  
ATOM   6976  CD  GLN B 351       7.883 -20.137  77.174  1.00201.71           C  
ANISOU 6976  CD  GLN B 351    26048  28615  21974    194    375   3246       C  
ATOM   6977  OE1 GLN B 351       8.754 -19.337  76.831  1.00194.93           O  
ANISOU 6977  OE1 GLN B 351    25102  27932  21031    110    306   3183       O  
ATOM   6978  NE2 GLN B 351       8.128 -21.157  77.989  1.00197.41           N  
ANISOU 6978  NE2 GLN B 351    25494  28111  21402    380    439   3378       N  
ATOM   6979  N   PRO B 352       6.861 -15.190  76.006  1.00228.36           N  
ANISOU 6979  N   PRO B 352    29524  31977  25263   -484    149   2821       N  
ATOM   6980  CA  PRO B 352       6.685 -13.949  75.239  1.00224.15           C  
ANISOU 6980  CA  PRO B 352    29052  31391  24724   -646    121   2710       C  
ATOM   6981  C   PRO B 352       7.337 -13.929  73.845  1.00215.76           C  
ANISOU 6981  C   PRO B 352    27962  30325  23692   -682    118   2661       C  
ATOM   6982  O   PRO B 352       8.461 -14.414  73.665  1.00206.04           O  
ANISOU 6982  O   PRO B 352    26626  29242  22418   -634    112   2689       O  
ATOM   6983  CB  PRO B 352       7.341 -12.892  76.139  1.00223.77           C  
ANISOU 6983  CB  PRO B 352    28967  31528  24525   -757     80   2669       C  
ATOM   6984  CG  PRO B 352       8.448 -13.635  76.801  1.00226.14           C  
ANISOU 6984  CG  PRO B 352    29125  32056  24740   -660     70   2743       C  
ATOM   6985  CD  PRO B 352       7.927 -15.032  77.030  1.00227.68           C  
ANISOU 6985  CD  PRO B 352    29327  32150  25030   -470    117   2856       C  
ATOM   6986  N   LEU B 353       6.605 -13.330  72.911  1.00212.44           N  
ANISOU 6986  N   LEU B 353    27633  29750  23335   -759    125   2593       N  
ATOM   6987  CA  LEU B 353       7.052 -13.012  71.567  1.00219.08           C  
ANISOU 6987  CA  LEU B 353    28470  30574  24196   -821    121   2532       C  
ATOM   6988  C   LEU B 353       7.791 -11.669  71.539  1.00233.61           C  
ANISOU 6988  C   LEU B 353    30317  32520  25921   -979     93   2459       C  
ATOM   6989  O   LEU B 353       8.466 -11.391  70.542  1.00250.34           O  
ANISOU 6989  O   LEU B 353    32412  34674  28031  -1039     88   2414       O  
ATOM   6990  CB  LEU B 353       5.852 -12.939  70.614  1.00210.13           C  
ANISOU 6990  CB  LEU B 353    27431  29241  23165   -824    148   2496       C  
ATOM   6991  CG  LEU B 353       5.083 -14.209  70.226  1.00199.60           C  
ANISOU 6991  CG  LEU B 353    26100  27785  21953   -712    191   2533       C  
ATOM   6992  CD1 LEU B 353       3.752 -13.816  69.608  1.00194.65           C  
ANISOU 6992  CD1 LEU B 353    25561  27014  21383   -741    208   2485       C  
ATOM   6993  CD2 LEU B 353       5.900 -15.050  69.258  1.00195.54           C  
ANISOU 6993  CD2 LEU B 353    25514  27298  21481   -661    206   2537       C  
ATOM   6994  N   SER B 354       7.646 -10.852  72.596  1.00233.25           N  
ANISOU 6994  N   SER B 354    30313  32520  25791  -1054     82   2440       N  
ATOM   6995  CA  SER B 354       8.375  -9.577  72.773  1.00235.15           C  
ANISOU 6995  CA  SER B 354    30571  32866  25907  -1227     72   2361       C  
ATOM   6996  C   SER B 354       9.909  -9.662  72.721  1.00237.42           C  
ANISOU 6996  C   SER B 354    30717  33396  26094  -1281     48   2345       C  
ATOM   6997  O   SER B 354      10.553  -8.678  72.350  1.00234.23           O  
ANISOU 6997  O   SER B 354    30331  33053  25609  -1444     53   2263       O  
ATOM   6998  CB  SER B 354       8.029  -8.936  74.137  1.00232.11           C  
ANISOU 6998  CB  SER B 354    30233  32518  25440  -1280     70   2350       C  
ATOM   6999  OG  SER B 354       8.119  -7.537  74.038  1.00235.28           O  
ANISOU 6999  OG  SER B 354    30741  32889  25765  -1454     92   2256       O  
ATOM   7000  N   GLY B 355      10.465 -10.799  73.165  1.00231.82           N  
ANISOU 7000  N   GLY B 355    29872  32832  25376  -1146     31   2424       N  
ATOM   7001  CA  GLY B 355      11.893 -11.148  73.033  1.00218.31           C  
ANISOU 7001  CA  GLY B 355    28001  31374  23572  -1142     10   2430       C  
ATOM   7002  C   GLY B 355      12.360 -11.551  71.631  1.00214.16           C  
ANISOU 7002  C   GLY B 355    27442  30819  23110  -1115     16   2422       C  
ATOM   7003  O   GLY B 355      13.446 -11.179  71.192  1.00216.59           O  
ANISOU 7003  O   GLY B 355    27665  31299  23329  -1208      1   2373       O  
ATOM   7004  N   LYS B 356      11.503 -12.276  70.911  1.00204.21           N  
ANISOU 7004  N   LYS B 356    26249  29343  21998  -1001     41   2459       N  
ATOM   7005  CA  LYS B 356      11.755 -12.688  69.515  1.00185.30           C  
ANISOU 7005  CA  LYS B 356    23838  26888  19678   -971     53   2445       C  
ATOM   7006  C   LYS B 356      11.598 -11.586  68.443  1.00173.93           C  
ANISOU 7006  C   LYS B 356    22485  25351  18247  -1127     57   2353       C  
ATOM   7007  O   LYS B 356      11.748 -11.881  67.262  1.00175.51           O  
ANISOU 7007  O   LYS B 356    22674  25503  18507  -1106     66   2338       O  
ATOM   7008  CB  LYS B 356      10.838 -13.863  69.140  1.00177.71           C  
ANISOU 7008  CB  LYS B 356    22921  25734  18864   -811     90   2504       C  
ATOM   7009  CG  LYS B 356      10.971 -15.087  70.039  1.00172.95           C  
ANISOU 7009  CG  LYS B 356    22258  25188  18268   -636    110   2607       C  
ATOM   7010  CD  LYS B 356       9.739 -15.971  69.903  1.00167.56           C  
ANISOU 7010  CD  LYS B 356    21668  24270  17727   -535    162   2645       C  
ATOM   7011  CE  LYS B 356       9.688 -17.130  70.875  1.00163.77           C  
ANISOU 7011  CE  LYS B 356    21166  23799  17258   -367    202   2752       C  
ATOM   7012  NZ  LYS B 356      10.939 -17.920  70.832  1.00164.78           N  
ANISOU 7012  NZ  LYS B 356    21182  24097  17329   -241    215   2815       N  
ATOM   7013  N   THR B 357      11.301 -10.339  68.839  1.00165.98           N  
ANISOU 7013  N   THR B 357    21574  24312  17179  -1275     59   2293       N  
ATOM   7014  CA  THR B 357      11.200  -9.181  67.906  1.00160.35           C  
ANISOU 7014  CA  THR B 357    20966  23503  16454  -1421     80   2214       C  
ATOM   7015  C   THR B 357      12.453  -8.966  67.029  1.00155.92           C  
ANISOU 7015  C   THR B 357    20320  23088  15831  -1512     74   2169       C  
ATOM   7016  O   THR B 357      12.334  -8.708  65.820  1.00150.36           O  
ANISOU 7016  O   THR B 357    19667  22286  15174  -1539     93   2140       O  
ATOM   7017  CB  THR B 357      10.856  -7.871  68.664  1.00156.88           C  
ANISOU 7017  CB  THR B 357    20651  23022  15933  -1567    101   2160       C  
ATOM   7018  OG1 THR B 357       9.718  -8.092  69.503  1.00151.17           O  
ANISOU 7018  OG1 THR B 357    19995  22182  15260  -1476    104   2203       O  
ATOM   7019  CG2 THR B 357      10.553  -6.725  67.701  1.00154.08           C  
ANISOU 7019  CG2 THR B 357    20444  22519  15577  -1682    145   2096       C  
ATOM   7020  N   SER B 358      13.633  -9.116  67.631  1.00150.27           N  
ANISOU 7020  N   SER B 358    19465  22626  15002  -1549     49   2167       N  
ATOM   7021  CA  SER B 358      14.889  -9.090  66.892  1.00149.34           C  
ANISOU 7021  CA  SER B 358    19233  22693  14814  -1617     39   2132       C  
ATOM   7022  C   SER B 358      14.958 -10.119  65.758  1.00142.88           C  
ANISOU 7022  C   SER B 358    18358  21829  14100  -1470     36   2175       C  
ATOM   7023  O   SER B 358      15.358  -9.774  64.657  1.00139.62           O  
ANISOU 7023  O   SER B 358    17948  21413  13689  -1543     45   2130       O  
ATOM   7024  CB  SER B 358      16.054  -9.322  67.848  1.00155.97           C  
ANISOU 7024  CB  SER B 358    19901  23850  15508  -1634      8   2138       C  
ATOM   7025  OG  SER B 358      17.291  -9.295  67.153  1.00159.82           O  
ANISOU 7025  OG  SER B 358    20262  24548  15913  -1700     -1   2102       O  
ATOM   7026  N   TYR B 359      14.586 -11.370  66.048  1.00141.75           N  
ANISOU 7026  N   TYR B 359    18170  21648  14039  -1270     32   2258       N  
ATOM   7027  CA  TYR B 359      14.614 -12.451  65.051  1.00140.68           C  
ANISOU 7027  CA  TYR B 359    17991  21455  14003  -1125     43   2295       C  
ATOM   7028  C   TYR B 359      13.604 -12.182  63.942  1.00138.39           C  
ANISOU 7028  C   TYR B 359    17828  20924  13830  -1149     68   2257       C  
ATOM   7029  O   TYR B 359      13.857 -12.532  62.797  1.00135.25           O  
ANISOU 7029  O   TYR B 359    17400  20510  13478  -1120     76   2242       O  
ATOM   7030  CB  TYR B 359      14.283 -13.835  65.630  1.00144.26           C  
ANISOU 7030  CB  TYR B 359    18411  21873  14527   -913     59   2389       C  
ATOM   7031  CG  TYR B 359      15.204 -14.394  66.686  1.00156.98           C  
ANISOU 7031  CG  TYR B 359    19890  23724  16031   -819     45   2455       C  
ATOM   7032  CD1 TYR B 359      16.537 -14.739  66.412  1.00162.34           C  
ANISOU 7032  CD1 TYR B 359    20416  24650  16615   -777     31   2468       C  
ATOM   7033  CD2 TYR B 359      14.717 -14.647  67.974  1.00168.67           C  
ANISOU 7033  CD2 TYR B 359    21390  25197  17498   -750     48   2515       C  
ATOM   7034  CE1 TYR B 359      17.363 -15.262  67.406  1.00166.98           C  
ANISOU 7034  CE1 TYR B 359    20870  25487  17085   -666     21   2538       C  
ATOM   7035  CE2 TYR B 359      15.524 -15.181  68.967  1.00170.88           C  
ANISOU 7035  CE2 TYR B 359    21545  25711  17668   -642     39   2587       C  
ATOM   7036  CZ  TYR B 359      16.845 -15.482  68.680  1.00171.33           C  
ANISOU 7036  CZ  TYR B 359    21447  26026  17622   -596     25   2600       C  
ATOM   7037  OH  TYR B 359      17.627 -16.004  69.677  1.00177.93           O  
ANISOU 7037  OH  TYR B 359    22149  27122  18332   -469     19   2678       O  
ATOM   7038  N   PHE B 360      12.440 -11.606  64.283  1.00138.60           N  
ANISOU 7038  N   PHE B 360    17987  20776  13896  -1186     81   2246       N  
ATOM   7039  CA  PHE B 360      11.380 -11.316  63.289  1.00134.79           C  
ANISOU 7039  CA  PHE B 360    17618  20091  13506  -1192    106   2217       C  
ATOM   7040  C   PHE B 360      11.827 -10.223  62.326  1.00134.71           C  
ANISOU 7040  C   PHE B 360    17647  20094  13441  -1332    114   2153       C  
ATOM   7041  O   PHE B 360      11.910 -10.468  61.110  1.00140.82           O  
ANISOU 7041  O   PHE B 360    18402  20841  14262  -1309    122   2136       O  
ATOM   7042  CB  PHE B 360      10.036 -10.916  63.944  1.00130.25           C  
ANISOU 7042  CB  PHE B 360    17168  19356  12965  -1185    121   2225       C  
ATOM   7043  CG  PHE B 360       9.400 -12.003  64.789  1.00127.40           C  
ANISOU 7043  CG  PHE B 360    16786  18949  12670  -1051    125   2287       C  
ATOM   7044  CD1 PHE B 360       9.543 -13.372  64.494  1.00125.30           C  
ANISOU 7044  CD1 PHE B 360    16445  18683  12480   -921    139   2327       C  
ATOM   7045  CD2 PHE B 360       8.634 -11.643  65.895  1.00129.51           C  
ANISOU 7045  CD2 PHE B 360    17124  19162  12921  -1057    126   2305       C  
ATOM   7046  CE1 PHE B 360       8.942 -14.344  65.294  1.00128.36           C  
ANISOU 7046  CE1 PHE B 360    16837  19010  12925   -808    161   2386       C  
ATOM   7047  CE2 PHE B 360       8.027 -12.606  66.701  1.00129.96           C  
ANISOU 7047  CE2 PHE B 360    17169  19175  13033   -943    137   2365       C  
ATOM   7048  CZ  PHE B 360       8.174 -13.958  66.396  1.00131.48           C  
ANISOU 7048  CZ  PHE B 360    17296  19359  13302   -821    158   2406       C  
ATOM   7049  N   HIS B 361      12.138  -9.042  62.869  1.00129.18           N  
ANISOU 7049  N   HIS B 361    17007  19436  12638  -1481    120   2115       N  
ATOM   7050  CA  HIS B 361      12.637  -7.924  62.048  1.00126.47           C  
ANISOU 7050  CA  HIS B 361    16723  19100  12230  -1635    145   2054       C  
ATOM   7051  C   HIS B 361      13.899  -8.211  61.226  1.00125.25           C  
ANISOU 7051  C   HIS B 361    16439  19113  12035  -1671    131   2033       C  
ATOM   7052  O   HIS B 361      14.076  -7.656  60.147  1.00122.58           O  
ANISOU 7052  O   HIS B 361    16144  18740  11690  -1742    155   1998       O  
ATOM   7053  CB  HIS B 361      12.819  -6.698  62.919  1.00128.53           C  
ANISOU 7053  CB  HIS B 361    17077  19379  12380  -1800    170   2010       C  
ATOM   7054  CG  HIS B 361      11.526  -6.023  63.226  1.00126.62           C  
ANISOU 7054  CG  HIS B 361    17011  18929  12169  -1787    206   2016       C  
ATOM   7055  ND1 HIS B 361      11.067  -4.959  62.481  1.00127.74           N  
ANISOU 7055  ND1 HIS B 361    17313  18923  12299  -1852    264   1988       N  
ATOM   7056  CD2 HIS B 361      10.576  -6.279  64.152  1.00121.48           C  
ANISOU 7056  CD2 HIS B 361    16402  18198  11557  -1699    198   2052       C  
ATOM   7057  CE1 HIS B 361       9.899  -4.570  62.949  1.00123.34           C  
ANISOU 7057  CE1 HIS B 361    16886  18211  11765  -1798    290   2007       C  
ATOM   7058  NE2 HIS B 361       9.582  -5.345  63.972  1.00120.44           N  
ANISOU 7058  NE2 HIS B 361    16446  17885  11429  -1714    248   2042       N  
ATOM   7059  N   LEU B 362      14.750  -9.101  61.723  1.00128.31           N  
ANISOU 7059  N   LEU B 362    16669  19689  12393  -1607     95   2061       N  
ATOM   7060  CA  LEU B 362      15.902  -9.580  60.957  1.00131.65           C  
ANISOU 7060  CA  LEU B 362    16950  20286  12782  -1599     79   2053       C  
ATOM   7061  C   LEU B 362      15.443 -10.326  59.704  1.00126.98           C  
ANISOU 7061  C   LEU B 362    16361  19572  12312  -1476     88   2069       C  
ATOM   7062  O   LEU B 362      15.786  -9.944  58.607  1.00124.75           O  
ANISOU 7062  O   LEU B 362    16080  19296  12020  -1541     99   2031       O  
ATOM   7063  CB  LEU B 362      16.774 -10.500  61.815  1.00137.85           C  
ANISOU 7063  CB  LEU B 362    17569  21297  13508  -1504     46   2099       C  
ATOM   7064  CG  LEU B 362      17.904 -11.283  61.130  1.00143.49           C  
ANISOU 7064  CG  LEU B 362    18121  22204  14193  -1430     30   2111       C  
ATOM   7065  CD1 LEU B 362      19.095 -10.398  60.788  1.00141.40           C  
ANISOU 7065  CD1 LEU B 362    17783  22154  13788  -1620     25   2041       C  
ATOM   7066  CD2 LEU B 362      18.314 -12.463  62.025  1.00151.25           C  
ANISOU 7066  CD2 LEU B 362    18978  23333  15155  -1246     14   2192       C  
ATOM   7067  N   LEU B 363      14.670 -11.392  59.894  1.00123.36           N  
ANISOU 7067  N   LEU B 363    15903  19008  11960  -1309     89   2120       N  
ATOM   7068  CA  LEU B 363      14.215 -12.260  58.788  1.00121.90           C  
ANISOU 7068  CA  LEU B 363    15711  18717  11888  -1194    105   2125       C  
ATOM   7069  C   LEU B 363      13.298 -11.551  57.822  1.00118.42           C  
ANISOU 7069  C   LEU B 363    15385  18115  11494  -1248    127   2085       C  
ATOM   7070  O   LEU B 363      13.417 -11.758  56.612  1.00122.09           O  
ANISOU 7070  O   LEU B 363    15822  18572  11992  -1232    136   2060       O  
ATOM   7071  CB  LEU B 363      13.455 -13.500  59.308  1.00123.85           C  
ANISOU 7071  CB  LEU B 363    15960  18862  12235  -1029    120   2178       C  
ATOM   7072  CG  LEU B 363      14.198 -14.805  59.562  1.00124.85           C  
ANISOU 7072  CG  LEU B 363    15975  19090  12371   -881    127   2230       C  
ATOM   7073  CD1 LEU B 363      15.456 -14.607  60.413  1.00127.94           C  
ANISOU 7073  CD1 LEU B 363    16257  19726  12629   -903     96   2257       C  
ATOM   7074  CD2 LEU B 363      13.243 -15.784  60.234  1.00124.29           C  
ANISOU 7074  CD2 LEU B 363    15957  18874  12393   -753    161   2281       C  
ATOM   7075  N   THR B 364      12.355 -10.769  58.357  1.00114.03           N  
ANISOU 7075  N   THR B 364    14953  17437  10936  -1294    140   2083       N  
ATOM   7076  CA  THR B 364      11.303 -10.183  57.530  1.00110.14           C  
ANISOU 7076  CA  THR B 364    14571  16794  10482  -1303    167   2062       C  
ATOM   7077  C   THR B 364      11.752  -9.087  56.611  1.00104.86           C  
ANISOU 7077  C   THR B 364    13952  16141   9747  -1418    187   2025       C  
ATOM   7078  O   THR B 364      11.080  -8.835  55.629  1.00103.25           O  
ANISOU 7078  O   THR B 364    13804  15852   9574  -1392    211   2014       O  
ATOM   7079  CB  THR B 364      10.128  -9.630  58.343  1.00110.91           C  
ANISOU 7079  CB  THR B 364    14791  16762  10584  -1299    182   2077       C  
ATOM   7080  OG1 THR B 364      10.627  -8.678  59.290  1.00113.64           O  
ANISOU 7080  OG1 THR B 364    15189  17153  10834  -1415    183   2071       O  
ATOM   7081  CG2 THR B 364       9.352 -10.779  59.020  1.00110.20           C  
ANISOU 7081  CG2 THR B 364    14669  16620  10580  -1174    175   2112       C  
ATOM   7082  N   TRP B 365      12.841  -8.408  56.943  1.00103.94           N  
ANISOU 7082  N   TRP B 365    13819  16140   9530  -1549    185   2005       N  
ATOM   7083  CA  TRP B 365      13.409  -7.348  56.073  1.00105.13           C  
ANISOU 7083  CA  TRP B 365    14024  16311   9608  -1683    218   1966       C  
ATOM   7084  C   TRP B 365      14.667  -7.798  55.312  1.00106.31           C  
ANISOU 7084  C   TRP B 365    14030  16633   9728  -1710    197   1946       C  
ATOM   7085  O   TRP B 365      14.929  -7.343  54.206  1.00106.58           O  
ANISOU 7085  O   TRP B 365    14083  16667   9743  -1762    222   1923       O  
ATOM   7086  CB  TRP B 365      13.652  -6.056  56.882  1.00105.19           C  
ANISOU 7086  CB  TRP B 365    14149  16307   9510  -1849    254   1940       C  
ATOM   7087  CG  TRP B 365      12.415  -5.638  57.706  1.00105.43           C  
ANISOU 7087  CG  TRP B 365    14321  16172   9564  -1807    275   1963       C  
ATOM   7088  CD1 TRP B 365      12.310  -5.531  59.094  1.00103.51           C  
ANISOU 7088  CD1 TRP B 365    14098  15942   9289  -1836    265   1967       C  
ATOM   7089  CD2 TRP B 365      11.105  -5.325  57.193  1.00100.67           C  
ANISOU 7089  CD2 TRP B 365    13844  15391   9013  -1715    310   1987       C  
ATOM   7090  NE1 TRP B 365      11.033  -5.170  59.432  1.00101.17           N  
ANISOU 7090  NE1 TRP B 365    13936  15476   9027  -1770    291   1990       N  
ATOM   7091  CE2 TRP B 365      10.285  -5.026  58.285  1.00 98.83           C  
ANISOU 7091  CE2 TRP B 365    13705  15068   8778  -1694    319   2004       C  
ATOM   7092  CE3 TRP B 365      10.550  -5.281  55.925  1.00 98.85           C  
ANISOU 7092  CE3 TRP B 365    13645  15092   8821  -1642    332   1996       C  
ATOM   7093  CZ2 TRP B 365       8.968  -4.654  58.124  1.00 93.28           C  
ANISOU 7093  CZ2 TRP B 365    13124  14213   8102  -1601    353   2030       C  
ATOM   7094  CZ3 TRP B 365       9.221  -4.950  55.801  1.00 95.91           C  
ANISOU 7094  CZ3 TRP B 365    13385  14582   8473  -1546    363   2023       C  
ATOM   7095  CH2 TRP B 365       8.466  -4.628  56.881  1.00 91.62           C  
ANISOU 7095  CH2 TRP B 365    12933  13957   7921  -1526    374   2040       C  
ATOM   7096  N   SER B 366      15.409  -8.728  55.896  1.00111.59           N  
ANISOU 7096  N   SER B 366    14553  17454  10392  -1657    157   1960       N  
ATOM   7097  CA  SER B 366      16.676  -9.201  55.361  1.00113.09           C  
ANISOU 7097  CA  SER B 366    14591  17841  10536  -1667    136   1946       C  
ATOM   7098  C   SER B 366      16.443 -10.185  54.220  1.00109.03           C  
ANISOU 7098  C   SER B 366    14020  17286  10120  -1526    132   1956       C  
ATOM   7099  O   SER B 366      17.039 -10.037  53.153  1.00107.01           O  
ANISOU 7099  O   SER B 366    13719  17098   9840  -1567    138   1928       O  
ATOM   7100  CB  SER B 366      17.488  -9.844  56.504  1.00117.99           C  
ANISOU 7100  CB  SER B 366    15080  18651  11098  -1630    100   1971       C  
ATOM   7101  OG  SER B 366      18.840 -10.038  56.177  1.00126.47           O  
ANISOU 7101  OG  SER B 366    16003  19963  12084  -1667     83   1954       O  
ATOM   7102  N   LEU B 367      15.588 -11.182  54.432  1.00108.30           N  
ANISOU 7102  N   LEU B 367    13930  17085  10132  -1373    130   1988       N  
ATOM   7103  CA  LEU B 367      15.328 -12.180  53.376  1.00112.18           C  
ANISOU 7103  CA  LEU B 367    14373  17532  10716  -1252    138   1982       C  
ATOM   7104  C   LEU B 367      14.799 -11.622  52.045  1.00111.09           C  
ANISOU 7104  C   LEU B 367    14295  17311  10600  -1290    160   1945       C  
ATOM   7105  O   LEU B 367      15.287 -12.038  50.969  1.00109.01           O  
ANISOU 7105  O   LEU B 367    13957  17112  10348  -1264    162   1921       O  
ATOM   7106  CB  LEU B 367      14.410 -13.303  53.846  1.00113.68           C  
ANISOU 7106  CB  LEU B 367    14578  17603  11013  -1107    150   2011       C  
ATOM   7107  CG  LEU B 367      15.054 -14.296  54.813  1.00116.82           C  
ANISOU 7107  CG  LEU B 367    14889  18091  11403  -1006    143   2060       C  
ATOM   7108  CD1 LEU B 367      13.949 -15.112  55.450  1.00114.90           C  
ANISOU 7108  CD1 LEU B 367    14707  17690  11256   -900    169   2090       C  
ATOM   7109  CD2 LEU B 367      16.082 -15.204  54.136  1.00120.89           C  
ANISOU 7109  CD2 LEU B 367    15284  18733  11915   -919    147   2061       C  
ATOM   7110  N   PRO B 368      13.835 -10.673  52.092  1.00109.46           N  
ANISOU 7110  N   PRO B 368    14223  16976  10389  -1342    180   1943       N  
ATOM   7111  CA  PRO B 368      13.433 -10.049  50.805  1.00107.74           C  
ANISOU 7111  CA  PRO B 368    14060  16709  10167  -1368    207   1919       C  
ATOM   7112  C   PRO B 368      14.551  -9.273  50.132  1.00104.62           C  
ANISOU 7112  C   PRO B 368    13644  16422   9681  -1488    215   1899       C  
ATOM   7113  O   PRO B 368      14.686  -9.324  48.893  1.00106.44           O  
ANISOU 7113  O   PRO B 368    13841  16681   9917  -1475    226   1879       O  
ATOM   7114  CB  PRO B 368      12.265  -9.128  51.187  1.00106.39           C  
ANISOU 7114  CB  PRO B 368    14043  16394   9987  -1383    235   1936       C  
ATOM   7115  CG  PRO B 368      11.837  -9.552  52.543  1.00106.70           C  
ANISOU 7115  CG  PRO B 368    14094  16390  10057  -1343    218   1961       C  
ATOM   7116  CD  PRO B 368      13.042 -10.149  53.213  1.00107.72           C  
ANISOU 7116  CD  PRO B 368    14110  16655  10163  -1361    187   1967       C  
ATOM   7117  N   PHE B 369      15.360  -8.592  50.947  1.00100.74           N  
ANISOU 7117  N   PHE B 369    13168  16006   9103  -1612    214   1898       N  
ATOM   7118  CA  PHE B 369      16.533  -7.863  50.449  1.00 98.01           C  
ANISOU 7118  CA  PHE B 369    12795  15787   8657  -1758    229   1869       C  
ATOM   7119  C   PHE B 369      17.501  -8.775  49.659  1.00 97.89           C  
ANISOU 7119  C   PHE B 369    12608  15938   8648  -1708    199   1854       C  
ATOM   7120  O   PHE B 369      17.885  -8.453  48.533  1.00 97.13           O  
ANISOU 7120  O   PHE B 369    12498  15881   8524  -1752    217   1833       O  
ATOM   7121  CB  PHE B 369      17.251  -7.191  51.601  1.00 94.96           C  
ANISOU 7121  CB  PHE B 369    12423  15485   8171  -1904    231   1856       C  
ATOM   7122  CG  PHE B 369      18.542  -6.550  51.218  1.00 94.79           C  
ANISOU 7122  CG  PHE B 369    12352  15629   8035  -2075    248   1815       C  
ATOM   7123  CD1 PHE B 369      18.556  -5.243  50.735  1.00 95.13           C  
ANISOU 7123  CD1 PHE B 369    12540  15592   8010  -2231    316   1791       C  
ATOM   7124  CD2 PHE B 369      19.747  -7.242  51.354  1.00 94.89           C  
ANISOU 7124  CD2 PHE B 369    12175  15881   7997  -2077    205   1802       C  
ATOM   7125  CE1 PHE B 369      19.742  -4.630  50.379  1.00 96.08           C  
ANISOU 7125  CE1 PHE B 369    12621  15864   8020  -2412    343   1746       C  
ATOM   7126  CE2 PHE B 369      20.939  -6.645  50.996  1.00 97.66           C  
ANISOU 7126  CE2 PHE B 369    12465  16410   8229  -2246    222   1756       C  
ATOM   7127  CZ  PHE B 369      20.939  -5.332  50.509  1.00 98.14           C  
ANISOU 7127  CZ  PHE B 369    12674  16384   8227  -2428    292   1723       C  
ATOM   7128  N   VAL B 370      17.837  -9.924  50.241  1.00 98.33           N  
ANISOU 7128  N   VAL B 370    12543  16080   8738  -1600    161   1870       N  
ATOM   7129  CA  VAL B 370      18.725 -10.911  49.589  1.00 97.67           C  
ANISOU 7129  CA  VAL B 370    12301  16146   8659  -1518    141   1863       C  
ATOM   7130  C   VAL B 370      18.127 -11.346  48.251  1.00 98.03           C  
ANISOU 7130  C   VAL B 370    12355  16103   8789  -1434    156   1845       C  
ATOM   7131  O   VAL B 370      18.814 -11.276  47.229  1.00 97.36           O  
ANISOU 7131  O   VAL B 370    12204  16117   8668  -1464    159   1819       O  
ATOM   7132  CB  VAL B 370      18.991 -12.159  50.474  1.00 96.36           C  
ANISOU 7132  CB  VAL B 370    12036  16049   8526  -1374    116   1899       C  
ATOM   7133  CG1 VAL B 370      19.697 -13.280  49.708  1.00 94.20           C  
ANISOU 7133  CG1 VAL B 370    11630  15886   8275  -1249    113   1897       C  
ATOM   7134  CG2 VAL B 370      19.805 -11.760  51.691  1.00 96.58           C  
ANISOU 7134  CG2 VAL B 370    12015  16237   8443  -1455     96   1913       C  
ATOM   7135  N   LEU B 371      16.862 -11.776  48.253  1.00 97.87           N  
ANISOU 7135  N   LEU B 371    12406  15912   8868  -1337    168   1852       N  
ATOM   7136  CA  LEU B 371      16.197 -12.155  46.996  1.00 99.36           C  
ANISOU 7136  CA  LEU B 371    12596  16033   9122  -1270    186   1823       C  
ATOM   7137  C   LEU B 371      16.158 -11.030  45.941  1.00 98.36           C  
ANISOU 7137  C   LEU B 371    12526  15907   8937  -1364    207   1807       C  
ATOM   7138  O   LEU B 371      16.465 -11.273  44.758  1.00 99.72           O  
ANISOU 7138  O   LEU B 371    12634  16144   9111  -1344    212   1779       O  
ATOM   7139  CB  LEU B 371      14.793 -12.667  47.244  1.00 99.81           C  
ANISOU 7139  CB  LEU B 371    12719  15932   9273  -1179    201   1824       C  
ATOM   7140  CG  LEU B 371      14.743 -14.032  47.908  1.00102.04           C  
ANISOU 7140  CG  LEU B 371    12947  16192   9631  -1064    201   1833       C  
ATOM   7141  CD1 LEU B 371      13.334 -14.279  48.460  1.00105.60           C  
ANISOU 7141  CD1 LEU B 371    13482  16485  10153  -1018    219   1837       C  
ATOM   7142  CD2 LEU B 371      15.122 -15.162  46.973  1.00100.61           C  
ANISOU 7142  CD2 LEU B 371    12672  16055   9499   -977    218   1796       C  
ATOM   7143  N   THR B 372      15.818  -9.817  46.374  1.00 96.67           N  
ANISOU 7143  N   THR B 372    12439  15621   8668  -1460    228   1827       N  
ATOM   7144  CA  THR B 372      15.800  -8.670  45.481  1.00 97.36           C  
ANISOU 7144  CA  THR B 372    12611  15691   8689  -1545    267   1826       C  
ATOM   7145  C   THR B 372      17.183  -8.387  44.887  1.00 99.94           C  
ANISOU 7145  C   THR B 372    12859  16176   8937  -1650    268   1805       C  
ATOM   7146  O   THR B 372      17.345  -8.269  43.666  1.00102.70           O  
ANISOU 7146  O   THR B 372    13183  16566   9271  -1648    284   1792       O  
ATOM   7147  CB  THR B 372      15.287  -7.445  46.231  1.00 97.70           C  
ANISOU 7147  CB  THR B 372    12824  15615   8681  -1628    305   1854       C  
ATOM   7148  OG1 THR B 372      14.014  -7.765  46.793  1.00 98.15           O  
ANISOU 7148  OG1 THR B 372    12937  15547   8806  -1522    300   1873       O  
ATOM   7149  CG2 THR B 372      15.134  -6.257  45.297  1.00 99.47           C  
ANISOU 7149  CG2 THR B 372    13168  15787   8837  -1689    367   1866       C  
ATOM   7150  N   VAL B 373      18.184  -8.307  45.746  1.00104.01           N  
ANISOU 7150  N   VAL B 373    13323  16802   9394  -1741    250   1800       N  
ATOM   7151  CA  VAL B 373      19.566  -8.094  45.282  1.00105.79           C  
ANISOU 7151  CA  VAL B 373    13450  17216   9529  -1851    248   1774       C  
ATOM   7152  C   VAL B 373      19.982  -9.212  44.337  1.00102.94           C  
ANISOU 7152  C   VAL B 373    12936  16964   9213  -1733    219   1758       C  
ATOM   7153  O   VAL B 373      20.459  -8.914  43.252  1.00104.98           O  
ANISOU 7153  O   VAL B 373    13162  17293   9430  -1779    235   1739       O  
ATOM   7154  CB  VAL B 373      20.556  -7.948  46.476  1.00111.81           C  
ANISOU 7154  CB  VAL B 373    14151  18123  10206  -1959    229   1765       C  
ATOM   7155  CG1 VAL B 373      22.032  -8.118  46.078  1.00113.01           C  
ANISOU 7155  CG1 VAL B 373    14141  18530  10266  -2032    212   1735       C  
ATOM   7156  CG2 VAL B 373      20.332  -6.602  47.176  1.00114.51           C  
ANISOU 7156  CG2 VAL B 373    14659  18370  10479  -2129    278   1761       C  
ATOM   7157  N   ALA B 374      19.780 -10.472  44.731  1.00 99.13           N  
ANISOU 7157  N   ALA B 374    12371  16482   8811  -1581    186   1764       N  
ATOM   7158  CA  ALA B 374      20.080 -11.622  43.871  1.00 99.94           C  
ANISOU 7158  CA  ALA B 374    12349  16658   8964  -1454    174   1744       C  
ATOM   7159  C   ALA B 374      19.394 -11.509  42.500  1.00100.80           C  
ANISOU 7159  C   ALA B 374    12493  16691   9112  -1426    197   1719       C  
ATOM   7160  O   ALA B 374      20.046 -11.724  41.471  1.00102.81           O  
ANISOU 7160  O   ALA B 374    12659  17060   9343  -1421    197   1693       O  
ATOM   7161  CB  ALA B 374      19.668 -12.912  44.532  1.00 98.98           C  
ANISOU 7161  CB  ALA B 374    12192  16479   8934  -1295    162   1758       C  
ATOM   7162  N   ILE B 375      18.105 -11.152  42.479  1.00 99.56           N  
ANISOU 7162  N   ILE B 375    12456  16368   9003  -1404    217   1728       N  
ATOM   7163  CA  ILE B 375      17.417 -10.907  41.200  1.00100.05           C  
ANISOU 7163  CA  ILE B 375    12547  16389   9077  -1377    242   1709       C  
ATOM   7164  C   ILE B 375      18.072  -9.772  40.399  1.00 99.10           C  
ANISOU 7164  C   ILE B 375    12455  16340   8856  -1496    268   1717       C  
ATOM   7165  O   ILE B 375      18.328  -9.913  39.180  1.00 97.08           O  
ANISOU 7165  O   ILE B 375    12135  16163   8586  -1477    275   1693       O  
ATOM   7166  CB  ILE B 375      15.905 -10.607  41.410  1.00102.90           C  
ANISOU 7166  CB  ILE B 375    13027  16588   9480  -1329    262   1725       C  
ATOM   7167  CG1 ILE B 375      15.163 -11.869  41.832  1.00102.58           C  
ANISOU 7167  CG1 ILE B 375    12945  16486   9543  -1213    249   1701       C  
ATOM   7168  CG2 ILE B 375      15.215 -10.086  40.140  1.00106.04           C  
ANISOU 7168  CG2 ILE B 375    13460  16976   9852  -1305    293   1719       C  
ATOM   7169  CD1 ILE B 375      13.854 -11.565  42.515  1.00103.85           C  
ANISOU 7169  CD1 ILE B 375    13215  16510   9733  -1186    261   1723       C  
ATOM   7170  N   LEU B 376      18.335  -8.653  41.070  1.00100.21           N  
ANISOU 7170  N   LEU B 376    12700  16450   8923  -1625    290   1746       N  
ATOM   7171  CA  LEU B 376      18.959  -7.514  40.371  1.00103.27           C  
ANISOU 7171  CA  LEU B 376    13143  16884   9210  -1759    335   1753       C  
ATOM   7172  C   LEU B 376      20.345  -7.847  39.812  1.00104.42           C  
ANISOU 7172  C   LEU B 376    13138  17233   9304  -1817    315   1721       C  
ATOM   7173  O   LEU B 376      20.702  -7.415  38.715  1.00103.07           O  
ANISOU 7173  O   LEU B 376    12959  17120   9082  -1861    344   1715       O  
ATOM   7174  CB  LEU B 376      19.039  -6.282  41.252  1.00104.62           C  
ANISOU 7174  CB  LEU B 376    13465  16975   9307  -1907    380   1777       C  
ATOM   7175  CG  LEU B 376      17.661  -5.702  41.556  1.00106.36           C  
ANISOU 7175  CG  LEU B 376    13859  16995   9556  -1848    418   1817       C  
ATOM   7176  CD1 LEU B 376      17.716  -4.886  42.838  1.00109.43           C  
ANISOU 7176  CD1 LEU B 376    14374  17302   9900  -1967    446   1828       C  
ATOM   7177  CD2 LEU B 376      17.118  -4.867  40.417  1.00105.74           C  
ANISOU 7177  CD2 LEU B 376    13890  16848   9436  -1827    483   1848       C  
ATOM   7178  N   ALA B 377      21.083  -8.681  40.532  1.00106.34           N  
ANISOU 7178  N   ALA B 377    13255  17593   9556  -1795    268   1704       N  
ATOM   7179  CA  ALA B 377      22.405  -9.132  40.095  1.00109.11           C  
ANISOU 7179  CA  ALA B 377    13441  18163   9851  -1821    245   1676       C  
ATOM   7180  C   ALA B 377      22.366  -9.961  38.800  1.00109.49           C  
ANISOU 7180  C   ALA B 377    13392  18259   9948  -1697    236   1652       C  
ATOM   7181  O   ALA B 377      23.138  -9.683  37.872  1.00113.31           O  
ANISOU 7181  O   ALA B 377    13812  18873  10365  -1760    247   1635       O  
ATOM   7182  CB  ALA B 377      23.080  -9.933  41.199  1.00111.69           C  
ANISOU 7182  CB  ALA B 377    13655  18609  10173  -1779    202   1676       C  
ATOM   7183  N   VAL B 378      21.490 -10.977  38.746  1.00106.97           N  
ANISOU 7183  N   VAL B 378    13062  17842   9740  -1535    222   1643       N  
ATOM   7184  CA  VAL B 378      21.278 -11.740  37.497  1.00105.60           C  
ANISOU 7184  CA  VAL B 378    12813  17694   9614  -1429    224   1606       C  
ATOM   7185  C   VAL B 378      20.500 -10.942  36.443  1.00106.26           C  
ANISOU 7185  C   VAL B 378    12981  17710   9682  -1455    258   1608       C  
ATOM   7186  O   VAL B 378      20.409 -11.391  35.305  1.00107.23           O  
ANISOU 7186  O   VAL B 378    13037  17885   9820  -1391    262   1573       O  
ATOM   7187  CB  VAL B 378      20.628 -13.144  37.693  1.00103.91           C  
ANISOU 7187  CB  VAL B 378    12561  17404   9516  -1265    215   1579       C  
ATOM   7188  CG1 VAL B 378      21.585 -14.053  38.436  1.00104.73           C  
ANISOU 7188  CG1 VAL B 378    12563  17607   9619  -1202    195   1584       C  
ATOM   7189  CG2 VAL B 378      19.274 -13.096  38.397  1.00102.41           C  
ANISOU 7189  CG2 VAL B 378    12489  17024   9396  -1232    225   1594       C  
ATOM   7190  N   ALA B 379      19.892  -9.821  36.849  1.00106.96           N  
ANISOU 7190  N   ALA B 379    13219  17682   9738  -1531    287   1650       N  
ATOM   7191  CA  ALA B 379      19.227  -8.869  35.950  1.00107.34           C  
ANISOU 7191  CA  ALA B 379    13369  17671   9744  -1549    333   1674       C  
ATOM   7192  C   ALA B 379      18.064  -9.485  35.176  1.00106.25           C  
ANISOU 7192  C   ALA B 379    13209  17491   9669  -1408    332   1650       C  
ATOM   7193  O   ALA B 379      18.110  -9.642  33.988  1.00104.32           O  
ANISOU 7193  O   ALA B 379    12898  17331   9406  -1372    340   1626       O  
ATOM   7194  CB  ALA B 379      20.221  -8.217  35.019  1.00110.81           C  
ANISOU 7194  CB  ALA B 379    13779  18234  10088  -1650    359   1676       C  
ATOM   7195  N   GLN B 380      17.034  -9.868  35.914  1.00108.83           N  
ANISOU 7195  N   GLN B 380    13583  17702  10065  -1337    323   1650       N  
ATOM   7196  CA  GLN B 380      15.878 -10.588  35.400  1.00106.74           C  
ANISOU 7196  CA  GLN B 380    13285  17411   9861  -1219    323   1611       C  
ATOM   7197  C   GLN B 380      14.583  -9.812  35.600  1.00104.53           C  
ANISOU 7197  C   GLN B 380    13131  17024   9560  -1185    352   1654       C  
ATOM   7198  O   GLN B 380      13.515 -10.379  35.638  1.00 99.68           O  
ANISOU 7198  O   GLN B 380    12501  16376   8994  -1103    349   1625       O  
ATOM   7199  CB  GLN B 380      15.801 -11.948  36.117  1.00107.71           C  
ANISOU 7199  CB  GLN B 380    13335  17503  10085  -1157    295   1563       C  
ATOM   7200  CG  GLN B 380      16.886 -12.925  35.685  1.00109.58           C  
ANISOU 7200  CG  GLN B 380    13439  17853  10344  -1138    279   1515       C  
ATOM   7201  CD  GLN B 380      16.883 -13.224  34.183  1.00109.45           C  
ANISOU 7201  CD  GLN B 380    13334  17940  10309  -1102    291   1460       C  
ATOM   7202  OE1 GLN B 380      17.938 -13.367  33.602  1.00107.92           O  
ANISOU 7202  OE1 GLN B 380    13056  17864  10081  -1120    284   1445       O  
ATOM   7203  NE2 GLN B 380      15.703 -13.296  33.556  1.00110.59           N  
ANISOU 7203  NE2 GLN B 380    13490  18063  10467  -1051    309   1427       N  
ATOM   7204  N   VAL B 381      14.687  -8.502  35.710  1.00106.34           N  
ANISOU 7204  N   VAL B 381    13489  17206   9709  -1250    389   1722       N  
ATOM   7205  CA  VAL B 381      13.520  -7.659  35.903  1.00109.15           C  
ANISOU 7205  CA  VAL B 381    13982  17460  10028  -1201    429   1777       C  
ATOM   7206  C   VAL B 381      12.938  -7.436  34.518  1.00111.21           C  
ANISOU 7206  C   VAL B 381    14215  17807  10232  -1115    458   1781       C  
ATOM   7207  O   VAL B 381      13.625  -6.976  33.646  1.00119.70           O  
ANISOU 7207  O   VAL B 381    15281  18954  11245  -1153    482   1797       O  
ATOM   7208  CB  VAL B 381      13.922  -6.333  36.617  1.00112.00           C  
ANISOU 7208  CB  VAL B 381    14516  17717  10321  -1307    476   1847       C  
ATOM   7209  CG1 VAL B 381      12.770  -5.318  36.693  1.00109.40           C  
ANISOU 7209  CG1 VAL B 381    14353  17277   9935  -1238    537   1916       C  
ATOM   7210  CG2 VAL B 381      14.488  -6.636  38.021  1.00113.80           C  
ANISOU 7210  CG2 VAL B 381    14746  17896  10596  -1391    441   1832       C  
ATOM   7211  N   ASP B 382      11.683  -7.782  34.300  1.00111.90           N  
ANISOU 7211  N   ASP B 382    14276  17909  10332  -1002    457   1764       N  
ATOM   7212  CA  ASP B 382      11.056  -7.583  32.998  1.00110.55           C  
ANISOU 7212  CA  ASP B 382    14061  17854  10089   -908    484   1767       C  
ATOM   7213  C   ASP B 382       9.745  -6.825  33.206  1.00110.24           C  
ANISOU 7213  C   ASP B 382    14130  17768   9987   -806    524   1832       C  
ATOM   7214  O   ASP B 382       9.120  -6.936  34.247  1.00110.23           O  
ANISOU 7214  O   ASP B 382    14180  17672  10028   -794    513   1836       O  
ATOM   7215  CB  ASP B 382      10.766  -8.947  32.366  1.00116.26           C  
ANISOU 7215  CB  ASP B 382    14600  18701  10871   -864    444   1658       C  
ATOM   7216  CG  ASP B 382      12.017  -9.885  32.259  1.00125.04           C  
ANISOU 7216  CG  ASP B 382    15601  19852  12054   -939    408   1589       C  
ATOM   7217  OD1 ASP B 382      13.081  -9.460  31.742  1.00130.66           O  
ANISOU 7217  OD1 ASP B 382    16307  20613  12722   -996    415   1612       O  
ATOM   7218  OD2 ASP B 382      11.938 -11.104  32.659  1.00135.48           O  
ANISOU 7218  OD2 ASP B 382    16841  21163  13472   -934    379   1509       O  
ATOM   7219  N   GLY B 383       9.302  -6.081  32.200  1.00113.25           N  
ANISOU 7219  N   GLY B 383    14541  18229  10259   -717    574   1887       N  
ATOM   7220  CA  GLY B 383       8.001  -5.370  32.241  1.00114.82           C  
ANISOU 7220  CA  GLY B 383    14828  18422  10374   -581    620   1957       C  
ATOM   7221  C   GLY B 383       6.891  -6.048  31.430  1.00118.10           C  
ANISOU 7221  C   GLY B 383    15084  19032  10754   -458    601   1899       C  
ATOM   7222  O   GLY B 383       7.171  -6.786  30.473  1.00118.60           O  
ANISOU 7222  O   GLY B 383    14990  19245  10825   -468    574   1821       O  
ATOM   7223  N   ASP B 384       5.636  -5.779  31.819  1.00120.30           N  
ANISOU 7223  N   ASP B 384    15401  19322  10984   -346    619   1932       N  
ATOM   7224  CA  ASP B 384       4.426  -6.325  31.168  1.00121.70           C  
ANISOU 7224  CA  ASP B 384    15425  19711  11103   -231    608   1876       C  
ATOM   7225  C   ASP B 384       3.353  -5.238  31.180  1.00117.95           C  
ANISOU 7225  C   ASP B 384    15058  19266  10489    -61    669   1991       C  
ATOM   7226  O   ASP B 384       3.001  -4.694  32.213  1.00120.70           O  
ANISOU 7226  O   ASP B 384    15550  19463  10844    -42    690   2055       O  
ATOM   7227  CB  ASP B 384       3.929  -7.593  31.914  1.00128.24           C  
ANISOU 7227  CB  ASP B 384    16141  20539  12045   -294    551   1754       C  
ATOM   7228  CG  ASP B 384       2.650  -8.260  31.277  1.00131.06           C  
ANISOU 7228  CG  ASP B 384    16323  21136  12338   -212    544   1667       C  
ATOM   7229  OD1 ASP B 384       2.353  -8.046  30.082  1.00131.81           O  
ANISOU 7229  OD1 ASP B 384    16328  21437  12316   -125    564   1669       O  
ATOM   7230  OD2 ASP B 384       1.947  -9.032  31.991  1.00130.73           O  
ANISOU 7230  OD2 ASP B 384    16226  21088  12356   -246    522   1590       O  
ATOM   7231  N   SER B 385       2.819  -4.952  30.015  1.00120.27           N  
ANISOU 7231  N   SER B 385    15277  19770  10650     72    700   2018       N  
ATOM   7232  CA  SER B 385       1.803  -3.926  29.835  1.00122.07           C  
ANISOU 7232  CA  SER B 385    15592  20069  10719    272    768   2139       C  
ATOM   7233  C   SER B 385       0.444  -4.279  30.403  1.00119.21           C  
ANISOU 7233  C   SER B 385    15155  19810  10326    359    749   2105       C  
ATOM   7234  O   SER B 385      -0.303  -3.359  30.705  1.00118.24           O  
ANISOU 7234  O   SER B 385    15156  19671  10098    514    807   2219       O  
ATOM   7235  CB  SER B 385       1.644  -3.618  28.335  1.00129.26           C  
ANISOU 7235  CB  SER B 385    16411  21220  11480    404    805   2175       C  
ATOM   7236  OG  SER B 385       1.323  -4.793  27.594  1.00133.95           O  
ANISOU 7236  OG  SER B 385    16745  22066  12082    373    743   2029       O  
ATOM   7237  N   VAL B 386       0.102  -5.575  30.524  1.00118.68           N  
ANISOU 7237  N   VAL B 386    14896  19853  10342    266    680   1951       N  
ATOM   7238  CA  VAL B 386      -1.227  -5.967  31.097  1.00122.17           C  
ANISOU 7238  CA  VAL B 386    15257  20408  10752    326    664   1905       C  
ATOM   7239  C   VAL B 386      -1.276  -5.768  32.609  1.00120.59           C  
ANISOU 7239  C   VAL B 386    15215  19956  10646    276    660   1944       C  
ATOM   7240  O   VAL B 386      -2.209  -5.167  33.129  1.00115.57           O  
ANISOU 7240  O   VAL B 386    14649  19334   9927    402    690   2017       O  
ATOM   7241  CB  VAL B 386      -1.725  -7.393  30.702  1.00125.66           C  
ANISOU 7241  CB  VAL B 386    15450  21063  11231    236    613   1720       C  
ATOM   7242  CG1 VAL B 386      -1.671  -7.567  29.184  1.00130.29           C  
ANISOU 7242  CG1 VAL B 386    15873  21915  11713    282    620   1674       C  
ATOM   7243  CG2 VAL B 386      -0.949  -8.520  31.363  1.00128.02           C  
ANISOU 7243  CG2 VAL B 386    15730  21183  11729     28    565   1602       C  
ATOM   7244  N   SER B 387      -0.217  -6.227  33.281  1.00122.46           N  
ANISOU 7244  N   SER B 387    15509  19973  11046    101    625   1902       N  
ATOM   7245  CA  SER B 387      -0.042  -6.045  34.708  1.00121.62           C  
ANISOU 7245  CA  SER B 387    15552  19624  11033     35    618   1937       C  
ATOM   7246  C   SER B 387       0.317  -4.577  35.012  1.00122.40           C  
ANISOU 7246  C   SER B 387    15890  19550  11066    103    685   2091       C  
ATOM   7247  O   SER B 387      -0.132  -4.028  36.005  1.00127.49           O  
ANISOU 7247  O   SER B 387    16669  20067  11702    143    709   2153       O  
ATOM   7248  CB  SER B 387       1.027  -7.013  35.262  1.00119.93           C  
ANISOU 7248  CB  SER B 387    15309  19264  10994   -156    565   1847       C  
ATOM   7249  OG  SER B 387       2.355  -6.669  34.863  1.00117.59           O  
ANISOU 7249  OG  SER B 387    15074  18879  10724   -229    572   1878       O  
ATOM   7250  N   GLY B 388       1.124  -3.951  34.161  1.00122.56           N  
ANISOU 7250  N   GLY B 388    15970  19559  11036    109    725   2148       N  
ATOM   7251  CA  GLY B 388       1.501  -2.552  34.336  1.00124.32           C  
ANISOU 7251  CA  GLY B 388    16435  19610  11188    157    811   2287       C  
ATOM   7252  C   GLY B 388       2.598  -2.338  35.360  1.00125.48           C  
ANISOU 7252  C   GLY B 388    16730  19501  11446    -20    808   2290       C  
ATOM   7253  O   GLY B 388       2.765  -1.221  35.868  1.00127.81           O  
ANISOU 7253  O   GLY B 388    17248  19618  11695     -7    884   2387       O  
ATOM   7254  N   ILE B 389       3.336  -3.404  35.675  1.00124.81           N  
ANISOU 7254  N   ILE B 389    16522  19402  11496   -182    728   2181       N  
ATOM   7255  CA  ILE B 389       4.460  -3.331  36.612  1.00127.23           C  
ANISOU 7255  CA  ILE B 389    16927  19516  11899   -354    715   2172       C  
ATOM   7256  C   ILE B 389       5.642  -4.124  36.065  1.00126.07           C  
ANISOU 7256  C   ILE B 389    16648  19425  11827   -484    664   2093       C  
ATOM   7257  O   ILE B 389       5.508  -4.844  35.068  1.00127.82           O  
ANISOU 7257  O   ILE B 389    16703  19818  12045   -447    634   2033       O  
ATOM   7258  CB  ILE B 389       4.072  -3.832  38.021  1.00129.70           C  
ANISOU 7258  CB  ILE B 389    17248  19730  12302   -400    670   2135       C  
ATOM   7259  CG1 ILE B 389       3.630  -5.315  38.027  1.00134.45           C  
ANISOU 7259  CG1 ILE B 389    17636  20454  12992   -412    591   2021       C  
ATOM   7260  CG2 ILE B 389       2.959  -2.976  38.602  1.00129.23           C  
ANISOU 7260  CG2 ILE B 389    17329  19610  12161   -270    724   2218       C  
ATOM   7261  CD1 ILE B 389       4.659  -6.268  38.596  1.00135.96           C  
ANISOU 7261  CD1 ILE B 389    17758  20582  13315   -564    533   1946       C  
ATOM   7262  N   CYS B 390       6.805  -3.957  36.688  1.00121.61           N  
ANISOU 7262  N   CYS B 390    16155  18734  11316   -635    659   2091       N  
ATOM   7263  CA  CYS B 390       7.966  -4.769  36.343  1.00121.33           C  
ANISOU 7263  CA  CYS B 390    15988  18758  11352   -753    607   2016       C  
ATOM   7264  C   CYS B 390       8.193  -5.830  37.390  1.00118.01           C  
ANISOU 7264  C   CYS B 390    15487  18298  11053   -827    537   1944       C  
ATOM   7265  O   CYS B 390       8.061  -5.558  38.558  1.00120.13           O  
ANISOU 7265  O   CYS B 390    15853  18444  11345   -860    539   1969       O  
ATOM   7266  CB  CYS B 390       9.200  -3.909  36.251  1.00124.75           C  
ANISOU 7266  CB  CYS B 390    16531  19121  11745   -873    651   2059       C  
ATOM   7267  SG  CYS B 390       9.285  -2.875  34.793  1.00131.97           S  
ANISOU 7267  SG  CYS B 390    17519  20097  12527   -808    738   2135       S  
ATOM   7268  N   PHE B 391       8.556  -7.040  36.988  1.00117.02           N  
ANISOU 7268  N   PHE B 391    15190  18270  11000   -849    484   1857       N  
ATOM   7269  CA  PHE B 391       8.671  -8.160  37.934  1.00115.34           C  
ANISOU 7269  CA  PHE B 391    14904  18017  10900   -891    432   1794       C  
ATOM   7270  C   PHE B 391       9.784  -9.096  37.542  1.00110.67           C  
ANISOU 7270  C   PHE B 391    14186  17495  10368   -952    398   1729       C  
ATOM   7271  O   PHE B 391      10.341  -8.973  36.461  1.00118.81           O  
ANISOU 7271  O   PHE B 391    15163  18620  11357   -959    407   1720       O  
ATOM   7272  CB  PHE B 391       7.338  -8.902  37.960  1.00119.03           C  
ANISOU 7272  CB  PHE B 391    15302  18527  11397   -802    422   1746       C  
ATOM   7273  CG  PHE B 391       7.068  -9.652  39.240  1.00124.88           C  
ANISOU 7273  CG  PHE B 391    16043  19173  12230   -827    395   1719       C  
ATOM   7274  CD1 PHE B 391       6.834  -8.961  40.445  1.00126.34           C  
ANISOU 7274  CD1 PHE B 391    16360  19233  12407   -839    403   1784       C  
ATOM   7275  CD2 PHE B 391       7.015 -11.039  39.252  1.00126.06           C  
ANISOU 7275  CD2 PHE B 391    16073  19352  12471   -836    373   1630       C  
ATOM   7276  CE1 PHE B 391       6.576  -9.650  41.621  1.00123.75           C  
ANISOU 7276  CE1 PHE B 391    16030  18827  12159   -856    379   1764       C  
ATOM   7277  CE2 PHE B 391       6.756 -11.731  40.429  1.00123.17           C  
ANISOU 7277  CE2 PHE B 391    15719  18891  12186   -851    360   1614       C  
ATOM   7278  CZ  PHE B 391       6.538 -11.041  41.608  1.00122.73           C  
ANISOU 7278  CZ  PHE B 391    15782  18729  12121   -859    359   1684       C  
ATOM   7279  N   VAL B 392      10.130 -10.008  38.426  1.00107.97           N  
ANISOU 7279  N   VAL B 392    13799  17106  10116   -985    364   1692       N  
ATOM   7280  CA  VAL B 392      11.119 -11.044  38.098  1.00114.42           C  
ANISOU 7280  CA  VAL B 392    14493  17989  10989  -1012    339   1632       C  
ATOM   7281  C   VAL B 392      10.559 -12.095  37.149  1.00114.72           C  
ANISOU 7281  C   VAL B 392    14412  18111  11065   -951    342   1544       C  
ATOM   7282  O   VAL B 392       9.378 -12.375  37.183  1.00116.45           O  
ANISOU 7282  O   VAL B 392    14626  18322  11296   -902    353   1514       O  
ATOM   7283  CB  VAL B 392      11.732 -11.716  39.367  1.00116.11           C  
ANISOU 7283  CB  VAL B 392    14703  18135  11276  -1045    313   1631       C  
ATOM   7284  CG1 VAL B 392      10.650 -12.304  40.268  1.00118.88           C  
ANISOU 7284  CG1 VAL B 392    15081  18392  11692   -998    313   1619       C  
ATOM   7285  CG2 VAL B 392      12.784 -12.781  39.021  1.00115.37           C  
ANISOU 7285  CG2 VAL B 392    14490  18116  11227  -1044    297   1581       C  
ATOM   7286  N   GLY B 393      11.428 -12.628  36.287  1.00119.94           N  
ANISOU 7286  N   GLY B 393    14974  18864  11731   -962    336   1497       N  
ATOM   7287  CA  GLY B 393      11.153 -13.817  35.456  1.00124.94           C  
ANISOU 7287  CA  GLY B 393    15489  19570  12411   -924    346   1394       C  
ATOM   7288  C   GLY B 393       9.951 -13.818  34.508  1.00123.12           C  
ANISOU 7288  C   GLY B 393    15213  19429  12138   -878    367   1343       C  
ATOM   7289  O   GLY B 393       9.363 -14.875  34.236  1.00120.25           O  
ANISOU 7289  O   GLY B 393    14775  19091  11823   -864    384   1244       O  
ATOM   7290  N   TYR B 394       9.573 -12.647  34.011  1.00118.09           N  
ANISOU 7290  N   TYR B 394    14620  18845  11401   -854    376   1406       N  
ATOM   7291  CA  TYR B 394       8.460 -12.582  33.105  1.00117.91           C  
ANISOU 7291  CA  TYR B 394    14540  18947  11313   -793    395   1368       C  
ATOM   7292  C   TYR B 394       8.847 -13.261  31.777  1.00120.40           C  
ANISOU 7292  C   TYR B 394    14718  19410  11618   -793    400   1277       C  
ATOM   7293  O   TYR B 394       8.144 -14.164  31.278  1.00122.80           O  
ANISOU 7293  O   TYR B 394    14922  19799  11937   -784    413   1167       O  
ATOM   7294  CB  TYR B 394       8.009 -11.128  32.914  1.00119.14           C  
ANISOU 7294  CB  TYR B 394    14793  19122  11353   -739    415   1477       C  
ATOM   7295  CG  TYR B 394       6.940 -10.575  33.859  1.00118.14           C  
ANISOU 7295  CG  TYR B 394    14767  18913  11205   -694    426   1534       C  
ATOM   7296  CD1 TYR B 394       6.074 -11.413  34.581  1.00119.17           C  
ANISOU 7296  CD1 TYR B 394    14864  19012  11401   -693    417   1471       C  
ATOM   7297  CD2 TYR B 394       6.737  -9.186  33.946  1.00117.66           C  
ANISOU 7297  CD2 TYR B 394    14842  18815  11049   -645    458   1652       C  
ATOM   7298  CE1 TYR B 394       5.086 -10.884  35.389  1.00122.86           C  
ANISOU 7298  CE1 TYR B 394    15414  19426  11839   -646    427   1524       C  
ATOM   7299  CE2 TYR B 394       5.739  -8.645  34.743  1.00118.75           C  
ANISOU 7299  CE2 TYR B 394    15075  18888  11156   -586    475   1707       C  
ATOM   7300  CZ  TYR B 394       4.921  -9.495  35.462  1.00124.74           C  
ANISOU 7300  CZ  TYR B 394    15782  19633  11980   -585    453   1642       C  
ATOM   7301  OH  TYR B 394       3.928  -8.974  36.258  1.00132.34           O  
ANISOU 7301  OH  TYR B 394    16830  20544  12908   -524    468   1695       O  
ATOM   7302  N   LYS B 395       9.955 -12.819  31.201  1.00122.55           N  
ANISOU 7302  N   LYS B 395    14986  19721  11856   -815    393   1315       N  
ATOM   7303  CA  LYS B 395      10.509 -13.444  29.999  1.00128.13           C  
ANISOU 7303  CA  LYS B 395    15566  20561  12553   -819    395   1235       C  
ATOM   7304  C   LYS B 395      11.075 -14.815  30.332  1.00125.02           C  
ANISOU 7304  C   LYS B 395    15115  20113  12273   -852    392   1142       C  
ATOM   7305  O   LYS B 395      10.550 -15.817  29.824  1.00127.42           O  
ANISOU 7305  O   LYS B 395    15332  20473  12608   -845    413   1026       O  
ATOM   7306  CB  LYS B 395      11.561 -12.533  29.336  1.00133.43           C  
ANISOU 7306  CB  LYS B 395    16255  21291  13150   -837    394   1309       C  
ATOM   7307  CG  LYS B 395      12.427 -13.156  28.231  1.00136.40           C  
ANISOU 7307  CG  LYS B 395    16506  21795  13523   -849    390   1237       C  
ATOM   7308  CD  LYS B 395      13.288 -12.094  27.552  1.00137.66           C  
ANISOU 7308  CD  LYS B 395    16691  22022  13590   -870    397   1321       C  
ATOM   7309  CE  LYS B 395      14.657 -12.555  27.003  1.00138.65           C  
ANISOU 7309  CE  LYS B 395    16729  22223  13727   -914    384   1284       C  
ATOM   7310  NZ  LYS B 395      14.821 -13.910  26.395  1.00140.68           N  
ANISOU 7310  NZ  LYS B 395    16848  22560  14041   -891    379   1156       N  
ATOM   7311  N   ASN B 396      12.102 -14.853  31.190  1.00120.12           N  
ANISOU 7311  N   ASN B 396    14545  19389  11703   -885    374   1192       N  
ATOM   7312  CA  ASN B 396      12.735 -16.111  31.585  1.00120.07           C  
ANISOU 7312  CA  ASN B 396    14500  19327  11794   -888    379   1128       C  
ATOM   7313  C   ASN B 396      12.016 -16.774  32.753  1.00124.79           C  
ANISOU 7313  C   ASN B 396    15156  19781  12476   -881    393   1112       C  
ATOM   7314  O   ASN B 396      12.371 -16.558  33.920  1.00125.09           O  
ANISOU 7314  O   ASN B 396    15269  19713  12544   -891    376   1185       O  
ATOM   7315  CB  ASN B 396      14.178 -15.874  31.922  1.00118.84           C  
ANISOU 7315  CB  ASN B 396    14349  19170  11631   -911    355   1191       C  
ATOM   7316  CG  ASN B 396      14.910 -15.286  30.773  1.00119.25           C  
ANISOU 7316  CG  ASN B 396    14342  19365  11601   -928    348   1202       C  
ATOM   7317  OD1 ASN B 396      15.331 -14.137  30.806  1.00121.98           O  
ANISOU 7317  OD1 ASN B 396    14741  19731  11875   -972    336   1287       O  
ATOM   7318  ND2 ASN B 396      15.021 -16.052  29.714  1.00120.89           N  
ANISOU 7318  ND2 ASN B 396    14446  19670  11813   -901    364   1111       N  
ATOM   7319  N   TYR B 397      11.033 -17.611  32.400  1.00125.56           N  
ANISOU 7319  N   TYR B 397    15212  19888  12606   -874    430   1006       N  
ATOM   7320  CA  TYR B 397      10.079 -18.201  33.338  1.00123.23           C  
ANISOU 7320  CA  TYR B 397    14968  19475  12377   -880    455    976       C  
ATOM   7321  C   TYR B 397      10.729 -19.099  34.366  1.00122.13           C  
ANISOU 7321  C   TYR B 397    14878  19189  12336   -870    474    986       C  
ATOM   7322  O   TYR B 397      10.213 -19.266  35.477  1.00132.09           O  
ANISOU 7322  O   TYR B 397    16213  20329  13645   -871    482   1015       O  
ATOM   7323  CB  TYR B 397       8.928 -18.923  32.601  1.00125.96           C  
ANISOU 7323  CB  TYR B 397    15244  19894  12719   -900    501    842       C  
ATOM   7324  CG  TYR B 397       9.287 -20.166  31.817  1.00130.90           C  
ANISOU 7324  CG  TYR B 397    15799  20545  13391   -915    553    711       C  
ATOM   7325  CD1 TYR B 397       9.267 -21.422  32.412  1.00133.17           C  
ANISOU 7325  CD1 TYR B 397    16128  20689  13780   -929    615    641       C  
ATOM   7326  CD2 TYR B 397       9.617 -20.095  30.466  1.00139.28           C  
ANISOU 7326  CD2 TYR B 397    16760  21768  14389   -913    551    654       C  
ATOM   7327  CE1 TYR B 397       9.605 -22.564  31.705  1.00137.27           C  
ANISOU 7327  CE1 TYR B 397    16606  21209  14340   -940    680    519       C  
ATOM   7328  CE2 TYR B 397       9.960 -21.236  29.738  1.00142.78           C  
ANISOU 7328  CE2 TYR B 397    17145  22231  14872   -927    606    527       C  
ATOM   7329  CZ  TYR B 397       9.949 -22.469  30.370  1.00141.73           C  
ANISOU 7329  CZ  TYR B 397    17069  21938  14842   -941    674    458       C  
ATOM   7330  OH  TYR B 397      10.277 -23.596  29.666  1.00144.34           O  
ANISOU 7330  OH  TYR B 397    17365  22266  15210   -952    745    330       O  
ATOM   7331  N   ARG B 398      11.862 -19.678  34.010  1.00120.78           N  
ANISOU 7331  N   ARG B 398    14667  19037  12187   -846    483    968       N  
ATOM   7332  CA  ARG B 398      12.607 -20.518  34.928  1.00120.99           C  
ANISOU 7332  CA  ARG B 398    14734  18946  12287   -805    506    993       C  
ATOM   7333  C   ARG B 398      13.149 -19.743  36.134  1.00116.73           C  
ANISOU 7333  C   ARG B 398    14257  18361  11732   -801    456   1123       C  
ATOM   7334  O   ARG B 398      13.293 -20.323  37.194  1.00119.47           O  
ANISOU 7334  O   ARG B 398    14657  18600  12136   -766    474   1155       O  
ATOM   7335  CB  ARG B 398      13.711 -21.259  34.184  1.00127.65           C  
ANISOU 7335  CB  ARG B 398    15511  19849  13139   -762    530    948       C  
ATOM   7336  CG  ARG B 398      13.174 -22.267  33.181  1.00136.31           C  
ANISOU 7336  CG  ARG B 398    16565  20957  14266   -771    600    802       C  
ATOM   7337  CD  ARG B 398      14.237 -22.639  32.139  1.00146.64           C  
ANISOU 7337  CD  ARG B 398    17792  22373  15551   -734    610    760       C  
ATOM   7338  NE  ARG B 398      13.904 -23.874  31.427  1.00156.32           N  
ANISOU 7338  NE  ARG B 398    19002  23567  16825   -734    699    615       N  
ATOM   7339  CZ  ARG B 398      14.132 -25.117  31.869  1.00164.95           C  
ANISOU 7339  CZ  ARG B 398    20160  24515  17998   -682    786    574       C  
ATOM   7340  NH1 ARG B 398      14.715 -25.357  33.046  1.00172.20           N  
ANISOU 7340  NH1 ARG B 398    21151  25319  18956   -606    791    675       N  
ATOM   7341  NH2 ARG B 398      13.765 -26.147  31.118  1.00169.93           N  
ANISOU 7341  NH2 ARG B 398    20787  25115  18662   -704    879    427       N  
ATOM   7342  N   TYR B 399      13.421 -18.448  35.999  1.00112.05           N  
ANISOU 7342  N   TYR B 399    13666  17848  11059   -839    401   1195       N  
ATOM   7343  CA  TYR B 399      13.836 -17.638  37.162  1.00111.51           C  
ANISOU 7343  CA  TYR B 399    13664  17738  10966   -860    362   1303       C  
ATOM   7344  C   TYR B 399      12.656 -17.334  38.084  1.00110.83           C  
ANISOU 7344  C   TYR B 399    13667  17540  10903   -873    364   1329       C  
ATOM   7345  O   TYR B 399      12.840 -17.164  39.286  1.00110.29           O  
ANISOU 7345  O   TYR B 399    13657  17398  10847   -875    349   1395       O  
ATOM   7346  CB  TYR B 399      14.483 -16.316  36.744  1.00110.06           C  
ANISOU 7346  CB  TYR B 399    13477  17655  10684   -917    324   1363       C  
ATOM   7347  CG  TYR B 399      15.934 -16.426  36.332  1.00109.61           C  
ANISOU 7347  CG  TYR B 399    13341  17714  10590   -920    310   1371       C  
ATOM   7348  CD1 TYR B 399      16.952 -16.481  37.273  1.00106.72           C  
ANISOU 7348  CD1 TYR B 399    12970  17365  10214   -922    290   1426       C  
ATOM   7349  CD2 TYR B 399      16.290 -16.462  34.984  1.00111.52           C  
ANISOU 7349  CD2 TYR B 399    13502  18073  10795   -920    316   1322       C  
ATOM   7350  CE1 TYR B 399      18.288 -16.547  36.889  1.00107.39           C  
ANISOU 7350  CE1 TYR B 399    12966  17590  10246   -924    277   1432       C  
ATOM   7351  CE2 TYR B 399      17.630 -16.542  34.588  1.00108.68           C  
ANISOU 7351  CE2 TYR B 399    13062  17837  10393   -923    303   1329       C  
ATOM   7352  CZ  TYR B 399      18.620 -16.575  35.544  1.00107.38           C  
ANISOU 7352  CZ  TYR B 399    12889  17696  10213   -925    283   1384       C  
ATOM   7353  OH  TYR B 399      19.916 -16.653  35.132  1.00107.71           O  
ANISOU 7353  OH  TYR B 399    12836  17889  10198   -925    271   1387       O  
ATOM   7354  N   ARG B 400      11.472 -17.216  37.492  1.00112.45           N  
ANISOU 7354  N   ARG B 400    13870  17755  11097   -880    381   1278       N  
ATOM   7355  CA  ARG B 400      10.213 -17.037  38.215  1.00113.58           C  
ANISOU 7355  CA  ARG B 400    14080  17817  11255   -884    389   1287       C  
ATOM   7356  C   ARG B 400       9.945 -18.224  39.166  1.00112.85           C  
ANISOU 7356  C   ARG B 400    14016  17600  11260   -865    426   1258       C  
ATOM   7357  O   ARG B 400       9.370 -18.046  40.264  1.00111.19           O  
ANISOU 7357  O   ARG B 400    13879  17298  11070   -867    421   1303       O  
ATOM   7358  CB  ARG B 400       9.055 -16.829  37.212  1.00117.15           C  
ANISOU 7358  CB  ARG B 400    14490  18359  11660   -884    406   1223       C  
ATOM   7359  CG  ARG B 400       7.946 -15.925  37.698  1.00123.01           C  
ANISOU 7359  CG  ARG B 400    15297  19085  12353   -878    396   1274       C  
ATOM   7360  CD  ARG B 400       7.134 -15.260  36.577  1.00130.41           C  
ANISOU 7360  CD  ARG B 400    16189  20166  13193   -853    402   1254       C  
ATOM   7361  NE  ARG B 400       6.980 -15.922  35.272  1.00140.27           N  
ANISOU 7361  NE  ARG B 400    17319  21550  14425   -853    424   1146       N  
ATOM   7362  CZ  ARG B 400       6.093 -16.860  34.942  1.00148.92           C  
ANISOU 7362  CZ  ARG B 400    18342  22695  15542   -871    460   1029       C  
ATOM   7363  NH1 ARG B 400       5.215 -17.362  35.831  1.00153.43           N  
ANISOU 7363  NH1 ARG B 400    18947  23186  16161   -890    481   1000       N  
ATOM   7364  NH2 ARG B 400       6.117 -17.287  33.670  1.00146.61           N  
ANISOU 7364  NH2 ARG B 400    17942  22546  15217   -878    478    933       N  
ATOM   7365  N   ALA B 401      10.402 -19.411  38.765  1.00113.86           N  
ANISOU 7365  N   ALA B 401    14099  17716  11445   -841    469   1187       N  
ATOM   7366  CA  ALA B 401      10.339 -20.608  39.614  1.00116.66           C  
ANISOU 7366  CA  ALA B 401    14499  17936  11890   -810    524   1169       C  
ATOM   7367  C   ALA B 401      11.107 -20.470  40.924  1.00116.71           C  
ANISOU 7367  C   ALA B 401    14559  17876  11907   -770    498   1279       C  
ATOM   7368  O   ALA B 401      10.561 -20.716  41.998  1.00125.41           O  
ANISOU 7368  O   ALA B 401    15729  18869  13050   -762    515   1310       O  
ATOM   7369  CB  ALA B 401      10.852 -21.830  38.872  1.00117.06           C  
ANISOU 7369  CB  ALA B 401    14508  17982  11987   -778    588   1081       C  
ATOM   7370  N   GLY B 402      12.367 -20.075  40.841  1.00113.29           N  
ANISOU 7370  N   GLY B 402    14087  17527  11428   -750    458   1335       N  
ATOM   7371  CA  GLY B 402      13.233 -20.011  42.022  1.00111.17           C  
ANISOU 7371  CA  GLY B 402    13843  17244  11153   -711    435   1431       C  
ATOM   7372  C   GLY B 402      13.185 -18.731  42.834  1.00109.30           C  
ANISOU 7372  C   GLY B 402    13649  17023  10855   -769    375   1512       C  
ATOM   7373  O   GLY B 402      13.702 -18.696  43.932  1.00108.85           O  
ANISOU 7373  O   GLY B 402    13613  16954  10788   -749    359   1581       O  
ATOM   7374  N   PHE B 403      12.585 -17.675  42.292  1.00108.50           N  
ANISOU 7374  N   PHE B 403    13565  16955  10705   -837    349   1504       N  
ATOM   7375  CA  PHE B 403      12.432 -16.399  43.004  1.00106.38           C  
ANISOU 7375  CA  PHE B 403    13364  16678  10377   -895    310   1575       C  
ATOM   7376  C   PHE B 403      10.963 -16.026  43.334  1.00106.61           C  
ANISOU 7376  C   PHE B 403    13468  16619  10418   -904    320   1571       C  
ATOM   7377  O   PHE B 403      10.723 -15.017  43.991  1.00103.77           O  
ANISOU 7377  O   PHE B 403    13182  16232  10013   -940    300   1628       O  
ATOM   7378  CB  PHE B 403      13.038 -15.286  42.156  1.00104.70           C  
ANISOU 7378  CB  PHE B 403    13133  16571  10074   -956    285   1589       C  
ATOM   7379  CG  PHE B 403      14.533 -15.246  42.166  1.00104.54           C  
ANISOU 7379  CG  PHE B 403    13050  16658  10010   -977    264   1613       C  
ATOM   7380  CD1 PHE B 403      15.227 -14.962  43.339  1.00106.38           C  
ANISOU 7380  CD1 PHE B 403    13301  16906  10212  -1004    242   1671       C  
ATOM   7381  CD2 PHE B 403      15.260 -15.444  41.009  1.00102.77           C  
ANISOU 7381  CD2 PHE B 403    12740  16545   9762   -973    266   1575       C  
ATOM   7382  CE1 PHE B 403      16.625 -14.905  43.341  1.00107.72           C  
ANISOU 7382  CE1 PHE B 403    13391  17216  10319  -1029    222   1688       C  
ATOM   7383  CE2 PHE B 403      16.652 -15.400  41.016  1.00103.63           C  
ANISOU 7383  CE2 PHE B 403    12778  16779   9817   -992    247   1596       C  
ATOM   7384  CZ  PHE B 403      17.336 -15.125  42.172  1.00105.35           C  
ANISOU 7384  CZ  PHE B 403    13003  17029   9996  -1021    225   1651       C  
ATOM   7385  N   VAL B 404       9.982 -16.804  42.853  1.00107.37           N  
ANISOU 7385  N   VAL B 404    13545  16685  10565   -878    357   1499       N  
ATOM   7386  CA  VAL B 404       8.565 -16.567  43.169  1.00105.44           C  
ANISOU 7386  CA  VAL B 404    13350  16389  10323   -882    369   1488       C  
ATOM   7387  C   VAL B 404       7.987 -17.868  43.704  1.00104.21           C  
ANISOU 7387  C   VAL B 404    13197  16141  10256   -861    417   1439       C  
ATOM   7388  O   VAL B 404       7.509 -17.888  44.840  1.00103.27           O  
ANISOU 7388  O   VAL B 404    13140  15934  10161   -857    419   1480       O  
ATOM   7389  CB  VAL B 404       7.744 -16.042  41.935  1.00105.05           C  
ANISOU 7389  CB  VAL B 404    13265  16435  10214   -888    375   1440       C  
ATOM   7390  CG1 VAL B 404       6.381 -15.489  42.346  1.00106.90           C  
ANISOU 7390  CG1 VAL B 404    13550  16650  10416   -879    379   1454       C  
ATOM   7391  CG2 VAL B 404       8.497 -14.936  41.222  1.00103.37           C  
ANISOU 7391  CG2 VAL B 404    13052  16305   9918   -903    348   1486       C  
ATOM   7392  N   LEU B 405       7.990 -18.926  42.881  1.00103.76           N  
ANISOU 7392  N   LEU B 405    13082  16097  10244   -854    464   1348       N  
ATOM   7393  CA  LEU B 405       7.406 -20.225  43.281  1.00104.88           C  
ANISOU 7393  CA  LEU B 405    13245  16134  10470   -849    535   1286       C  
ATOM   7394  C   LEU B 405       8.088 -20.891  44.453  1.00100.11           C  
ANISOU 7394  C   LEU B 405    12697  15416   9923   -799    556   1352       C  
ATOM   7395  O   LEU B 405       7.420 -21.515  45.282  1.00105.60           O  
ANISOU 7395  O   LEU B 405    13450  16002  10671   -797    602   1349       O  
ATOM   7396  CB  LEU B 405       7.314 -21.222  42.120  1.00107.49           C  
ANISOU 7396  CB  LEU B 405    13515  16494  10831   -865    597   1163       C  
ATOM   7397  CG  LEU B 405       6.040 -21.160  41.248  1.00112.28           C  
ANISOU 7397  CG  LEU B 405    14070  17188  11402   -925    618   1058       C  
ATOM   7398  CD1 LEU B 405       6.119 -22.181  40.113  1.00116.75           C  
ANISOU 7398  CD1 LEU B 405    14575  17790  11993   -953    685    925       C  
ATOM   7399  CD2 LEU B 405       4.749 -21.402  42.016  1.00112.59           C  
ANISOU 7399  CD2 LEU B 405    14151  17167  11461   -964    652   1032       C  
ATOM   7400  N   ALA B 406       9.394 -20.752  44.544  1.00 97.25           N  
ANISOU 7400  N   ALA B 406    12313  15094   9541   -755    525   1413       N  
ATOM   7401  CA  ALA B 406      10.123 -21.324  45.671  1.00 98.04           C  
ANISOU 7401  CA  ALA B 406    12451  15126   9672   -685    541   1488       C  
ATOM   7402  C   ALA B 406       9.748 -20.662  46.985  1.00 97.15           C  
ANISOU 7402  C   ALA B 406    12398  14970   9541   -697    503   1572       C  
ATOM   7403  O   ALA B 406       9.246 -21.360  47.871  1.00 98.15           O  
ANISOU 7403  O   ALA B 406    12584  14985   9721   -668    550   1587       O  
ATOM   7404  CB  ALA B 406      11.634 -21.302  45.443  1.00 98.99           C  
ANISOU 7404  CB  ALA B 406    12512  15345   9753   -631    515   1532       C  
ATOM   7405  N   PRO B 407       9.942 -19.324  47.117  1.00 98.04           N  
ANISOU 7405  N   PRO B 407    12508  15163   9578   -744    430   1621       N  
ATOM   7406  CA  PRO B 407       9.553 -18.708  48.392  1.00 98.09           C  
ANISOU 7406  CA  PRO B 407    12579  15124   9565   -759    401   1691       C  
ATOM   7407  C   PRO B 407       8.078 -18.933  48.778  1.00 99.07           C  
ANISOU 7407  C   PRO B 407    12759  15149   9732   -775    434   1662       C  
ATOM   7408  O   PRO B 407       7.790 -19.228  49.947  1.00100.95           O  
ANISOU 7408  O   PRO B 407    13049  15308   9997   -752    447   1708       O  
ATOM   7409  CB  PRO B 407       9.893 -17.208  48.219  1.00 95.95           C  
ANISOU 7409  CB  PRO B 407    12312  14940   9202   -825    338   1725       C  
ATOM   7410  CG  PRO B 407      10.208 -17.015  46.799  1.00 98.14           C  
ANISOU 7410  CG  PRO B 407    12531  15303   9454   -845    336   1673       C  
ATOM   7411  CD  PRO B 407      10.589 -18.344  46.221  1.00 98.87           C  
ANISOU 7411  CD  PRO B 407    12565  15392   9609   -788    381   1620       C  
ATOM   7412  N   ILE B 408       7.161 -18.844  47.825  1.00 98.58           N  
ANISOU 7412  N   ILE B 408    12678  15108   9668   -811    449   1585       N  
ATOM   7413  CA  ILE B 408       5.756 -19.145  48.129  1.00101.21           C  
ANISOU 7413  CA  ILE B 408    13044  15382  10029   -832    486   1544       C  
ATOM   7414  C   ILE B 408       5.551 -20.642  48.516  1.00102.20           C  
ANISOU 7414  C   ILE B 408    13191  15395  10246   -814    569   1504       C  
ATOM   7415  O   ILE B 408       4.809 -20.941  49.494  1.00110.17           O  
ANISOU 7415  O   ILE B 408    14256  16319  11285   -817    597   1523       O  
ATOM   7416  CB  ILE B 408       4.825 -18.693  46.994  1.00102.59           C  
ANISOU 7416  CB  ILE B 408    13173  15648  10158   -869    485   1469       C  
ATOM   7417  CG1 ILE B 408       4.935 -17.179  46.852  1.00107.20           C  
ANISOU 7417  CG1 ILE B 408    13775  16304  10650   -870    422   1532       C  
ATOM   7418  CG2 ILE B 408       3.360 -19.054  47.263  1.00101.98           C  
ANISOU 7418  CG2 ILE B 408    13106  15548  10094   -897    525   1415       C  
ATOM   7419  CD1 ILE B 408       4.394 -16.663  45.534  1.00111.80           C  
ANISOU 7419  CD1 ILE B 408    14304  17006  11168   -876    420   1480       C  
ATOM   7420  N   GLY B 409       6.233 -21.558  47.823  1.00100.17           N  
ANISOU 7420  N   GLY B 409    12903  15128  10028   -790    617   1457       N  
ATOM   7421  CA  GLY B 409       6.231 -22.975  48.205  1.00100.56           C  
ANISOU 7421  CA  GLY B 409    13000  15046  10159   -758    715   1431       C  
ATOM   7422  C   GLY B 409       6.684 -23.161  49.654  1.00104.84           C  
ANISOU 7422  C   GLY B 409    13608  15506  10719   -687    717   1546       C  
ATOM   7423  O   GLY B 409       6.031 -23.839  50.477  1.00104.53           O  
ANISOU 7423  O   GLY B 409    13639  15348  10729   -684    781   1553       O  
ATOM   7424  N   LEU B 410       7.793 -22.506  49.983  1.00107.73           N  
ANISOU 7424  N   LEU B 410    13945  15951  11034   -636    646   1634       N  
ATOM   7425  CA  LEU B 410       8.314 -22.502  51.356  1.00107.02           C  
ANISOU 7425  CA  LEU B 410    13893  15835  10934   -568    631   1746       C  
ATOM   7426  C   LEU B 410       7.335 -21.883  52.380  1.00107.99           C  
ANISOU 7426  C   LEU B 410    14068  15918  11045   -613    603   1782       C  
ATOM   7427  O   LEU B 410       7.074 -22.495  53.430  1.00113.76           O  
ANISOU 7427  O   LEU B 410    14857  16554  11810   -569    648   1831       O  
ATOM   7428  CB  LEU B 410       9.683 -21.784  51.391  1.00106.77           C  
ANISOU 7428  CB  LEU B 410    13797  15944  10826   -535    556   1813       C  
ATOM   7429  CG  LEU B 410      10.514 -21.909  52.680  1.00108.81           C  
ANISOU 7429  CG  LEU B 410    14061  16229  11051   -450    543   1923       C  
ATOM   7430  CD1 LEU B 410      11.985 -22.135  52.353  1.00106.29           C  
ANISOU 7430  CD1 LEU B 410    13664  16036  10684   -372    532   1956       C  
ATOM   7431  CD2 LEU B 410      10.297 -20.705  53.634  1.00109.84           C  
ANISOU 7431  CD2 LEU B 410    14206  16409  11118   -513    467   1976       C  
ATOM   7432  N   VAL B 411       6.799 -20.684  52.122  1.00104.77           N  
ANISOU 7432  N   VAL B 411    13645  15577  10583   -687    536   1767       N  
ATOM   7433  CA  VAL B 411       5.896 -20.083  53.130  1.00105.16           C  
ANISOU 7433  CA  VAL B 411    13748  15591  10615   -715    512   1804       C  
ATOM   7434  C   VAL B 411       4.625 -20.926  53.298  1.00106.36           C  
ANISOU 7434  C   VAL B 411    13939  15642  10828   -736    586   1750       C  
ATOM   7435  O   VAL B 411       4.056 -20.970  54.409  1.00107.61           O  
ANISOU 7435  O   VAL B 411    14150  15740  10996   -730    596   1795       O  
ATOM   7436  CB  VAL B 411       5.514 -18.580  52.923  1.00100.84           C  
ANISOU 7436  CB  VAL B 411    13203  15121   9988   -772    440   1810       C  
ATOM   7437  CG1 VAL B 411       6.744 -17.709  52.723  1.00 98.69           C  
ANISOU 7437  CG1 VAL B 411    12904  14942   9650   -781    382   1850       C  
ATOM   7438  CG2 VAL B 411       4.488 -18.394  51.830  1.00100.92           C  
ANISOU 7438  CG2 VAL B 411    13190  15164   9991   -813    454   1725       C  
ATOM   7439  N   LEU B 412       4.203 -21.602  52.219  1.00103.02           N  
ANISOU 7439  N   LEU B 412    13488  15212  10441   -770    642   1649       N  
ATOM   7440  CA  LEU B 412       3.118 -22.568  52.380  1.00103.07           C  
ANISOU 7440  CA  LEU B 412    13531  15125  10504   -811    732   1583       C  
ATOM   7441  C   LEU B 412       3.452 -23.708  53.336  1.00102.57           C  
ANISOU 7441  C   LEU B 412    13544  14919  10508   -752    815   1634       C  
ATOM   7442  O   LEU B 412       2.671 -24.007  54.256  1.00102.82           O  
ANISOU 7442  O   LEU B 412    13633  14871  10562   -768    855   1653       O  
ATOM   7443  CB  LEU B 412       2.688 -23.145  51.045  1.00105.75           C  
ANISOU 7443  CB  LEU B 412    13824  15495  10862   -873    788   1450       C  
ATOM   7444  CG  LEU B 412       1.687 -22.311  50.263  1.00106.39           C  
ANISOU 7444  CG  LEU B 412    13837  15708  10876   -942    745   1380       C  
ATOM   7445  CD1 LEU B 412       1.477 -23.007  48.924  1.00110.91           C  
ANISOU 7445  CD1 LEU B 412    14351  16328  11461  -1000    805   1245       C  
ATOM   7446  CD2 LEU B 412       0.363 -22.149  50.975  1.00105.73           C  
ANISOU 7446  CD2 LEU B 412    13775  15621  10775   -986    756   1371       C  
ATOM   7447  N   ILE B 413       4.611 -24.323  53.138  1.00103.13           N  
ANISOU 7447  N   ILE B 413    13617  14964  10602   -674    845   1663       N  
ATOM   7448  CA  ILE B 413       5.016 -25.451  53.989  1.00103.58           C  
ANISOU 7448  CA  ILE B 413    13755  14886  10712   -585    939   1726       C  
ATOM   7449  C   ILE B 413       5.254 -24.994  55.438  1.00100.77           C  
ANISOU 7449  C   ILE B 413    13426  14537  10324   -520    888   1856       C  
ATOM   7450  O   ILE B 413       4.724 -25.609  56.399  1.00102.22           O  
ANISOU 7450  O   ILE B 413    13688  14606  10542   -501    957   1895       O  
ATOM   7451  CB  ILE B 413       6.252 -26.196  53.417  1.00104.18           C  
ANISOU 7451  CB  ILE B 413    13824  14952  10806   -487    986   1736       C  
ATOM   7452  CG1 ILE B 413       5.871 -26.940  52.135  1.00103.18           C  
ANISOU 7452  CG1 ILE B 413    13698  14778  10726   -555   1072   1596       C  
ATOM   7453  CG2 ILE B 413       6.792 -27.210  54.418  1.00104.77           C  
ANISOU 7453  CG2 ILE B 413    13987  14908  10913   -354   1078   1835       C  
ATOM   7454  CD1 ILE B 413       7.058 -27.339  51.297  1.00101.22           C  
ANISOU 7454  CD1 ILE B 413    13415  14566  10475   -474   1089   1588       C  
ATOM   7455  N   VAL B 414       5.999 -23.905  55.600  1.00 98.01           N  
ANISOU 7455  N   VAL B 414    13015  14323   9901   -501    775   1916       N  
ATOM   7456  CA  VAL B 414       6.317 -23.439  56.946  1.00102.00           C  
ANISOU 7456  CA  VAL B 414    13534  14859  10362   -449    727   2029       C  
ATOM   7457  C   VAL B 414       5.064 -22.866  57.668  1.00103.45           C  
ANISOU 7457  C   VAL B 414    13757  15008  10539   -523    704   2026       C  
ATOM   7458  O   VAL B 414       4.734 -23.276  58.809  1.00101.08           O  
ANISOU 7458  O   VAL B 414    13514  14636  10255   -485    741   2089       O  
ATOM   7459  CB  VAL B 414       7.480 -22.417  56.969  1.00101.13           C  
ANISOU 7459  CB  VAL B 414    13348  14912  10164   -433    623   2081       C  
ATOM   7460  CG1 VAL B 414       7.837 -22.013  58.398  1.00 99.31           C  
ANISOU 7460  CG1 VAL B 414    13125  14730   9877   -388    581   2185       C  
ATOM   7461  CG2 VAL B 414       8.731 -23.007  56.340  1.00102.74           C  
ANISOU 7461  CG2 VAL B 414    13502  15173  10362   -349    645   2090       C  
ATOM   7462  N   GLY B 415       4.398 -21.909  57.021  1.00100.44           N  
ANISOU 7462  N   GLY B 415    13346  14690  10127   -615    646   1961       N  
ATOM   7463  CA  GLY B 415       3.163 -21.322  57.580  1.00 96.30           C  
ANISOU 7463  CA  GLY B 415    12851  14151   9584   -674    626   1953       C  
ATOM   7464  C   GLY B 415       2.079 -22.352  57.832  1.00 93.54           C  
ANISOU 7464  C   GLY B 415    12550  13689   9300   -700    723   1910       C  
ATOM   7465  O   GLY B 415       1.417 -22.357  58.887  1.00 88.78           O  
ANISOU 7465  O   GLY B 415    11993  13042   8697   -702    734   1952       O  
ATOM   7466  N   GLY B 416       1.951 -23.268  56.867  1.00 95.20           N  
ANISOU 7466  N   GLY B 416    12754  13853   9562   -729    801   1822       N  
ATOM   7467  CA  GLY B 416       1.025 -24.390  56.992  1.00 97.39           C  
ANISOU 7467  CA  GLY B 416    13086  14013   9902   -778    919   1762       C  
ATOM   7468  C   GLY B 416       1.366 -25.307  58.150  1.00 99.91           C  
ANISOU 7468  C   GLY B 416    13495  14198  10267   -699    997   1853       C  
ATOM   7469  O   GLY B 416       0.463 -25.716  58.933  1.00106.09           O  
ANISOU 7469  O   GLY B 416    14336  14900  11072   -734   1057   1858       O  
ATOM   7470  N   TYR B 417       2.657 -25.622  58.301  1.00 97.26           N  
ANISOU 7470  N   TYR B 417    13167  13850   9935   -583   1000   1932       N  
ATOM   7471  CA  TYR B 417       3.060 -26.392  59.468  1.00 95.06           C  
ANISOU 7471  CA  TYR B 417    12969  13471   9678   -475   1070   2043       C  
ATOM   7472  C   TYR B 417       2.604 -25.735  60.766  1.00 92.92           C  
ANISOU 7472  C   TYR B 417    12708  13229   9366   -471   1011   2125       C  
ATOM   7473  O   TYR B 417       1.937 -26.373  61.564  1.00 94.96           O  
ANISOU 7473  O   TYR B 417    13044  13379   9658   -472   1092   2151       O  
ATOM   7474  CB  TYR B 417       4.561 -26.580  59.484  1.00 96.54           C  
ANISOU 7474  CB  TYR B 417    13133  13705   9841   -334   1056   2129       C  
ATOM   7475  CG  TYR B 417       5.075 -27.298  60.721  1.00 97.23           C  
ANISOU 7475  CG  TYR B 417    13289  13726   9927   -188   1122   2263       C  
ATOM   7476  CD1 TYR B 417       5.031 -28.683  60.820  1.00 96.87           C  
ANISOU 7476  CD1 TYR B 417    13356  13501   9946   -119   1284   2277       C  
ATOM   7477  CD2 TYR B 417       5.614 -26.580  61.771  1.00 96.68           C  
ANISOU 7477  CD2 TYR B 417    13175  13776   9782   -120   1030   2373       C  
ATOM   7478  CE1 TYR B 417       5.505 -29.328  61.927  1.00 99.09           C  
ANISOU 7478  CE1 TYR B 417    13706  13726  10216     35   1352   2413       C  
ATOM   7479  CE2 TYR B 417       6.070 -27.213  62.895  1.00 99.92           C  
ANISOU 7479  CE2 TYR B 417    13634  14153  10175     22   1088   2500       C  
ATOM   7480  CZ  TYR B 417       6.012 -28.584  62.980  1.00102.02           C  
ANISOU 7480  CZ  TYR B 417    14014  14242  10504    111   1248   2528       C  
ATOM   7481  OH  TYR B 417       6.479 -29.162  64.163  1.00106.96           O  
ANISOU 7481  OH  TYR B 417    14692  14847  11100    277   1308   2674       O  
ATOM   7482  N   PHE B 418       2.959 -24.472  60.979  1.00 91.19           N  
ANISOU 7482  N   PHE B 418    12420  13153   9073   -473    879   2161       N  
ATOM   7483  CA  PHE B 418       2.559 -23.759  62.208  1.00 91.04           C  
ANISOU 7483  CA  PHE B 418    12412  13171   9008   -473    821   2231       C  
ATOM   7484  C   PHE B 418       1.066 -23.605  62.361  1.00 92.30           C  
ANISOU 7484  C   PHE B 418    12599  13287   9181   -572    839   2171       C  
ATOM   7485  O   PHE B 418       0.562 -23.649  63.484  1.00 94.94           O  
ANISOU 7485  O   PHE B 418    12976  13587   9509   -559    852   2229       O  
ATOM   7486  CB  PHE B 418       3.196 -22.375  62.331  1.00 89.71           C  
ANISOU 7486  CB  PHE B 418    12179  13154   8752   -479    691   2262       C  
ATOM   7487  CG  PHE B 418       4.682 -22.402  62.522  1.00 90.07           C  
ANISOU 7487  CG  PHE B 418    12181  13286   8755   -386    662   2336       C  
ATOM   7488  CD1 PHE B 418       5.271 -23.193  63.477  1.00 92.38           C  
ANISOU 7488  CD1 PHE B 418    12496  13558   9044   -266    711   2436       C  
ATOM   7489  CD2 PHE B 418       5.495 -21.629  61.752  1.00 89.33           C  
ANISOU 7489  CD2 PHE B 418    12019  13310   8611   -413    589   2308       C  
ATOM   7490  CE1 PHE B 418       6.657 -23.220  63.637  1.00 92.88           C  
ANISOU 7490  CE1 PHE B 418    12499  13742   9047   -168    684   2505       C  
ATOM   7491  CE2 PHE B 418       6.868 -21.615  61.948  1.00 89.81           C  
ANISOU 7491  CE2 PHE B 418    12022  13484   8616   -337    560   2370       C  
ATOM   7492  CZ  PHE B 418       7.453 -22.414  62.889  1.00 90.37           C  
ANISOU 7492  CZ  PHE B 418    12101  13559   8676   -211    604   2468       C  
ATOM   7493  N   LEU B 419       0.349 -23.400  61.264  1.00 94.30           N  
ANISOU 7493  N   LEU B 419    12820  13567   9443   -667    838   2058       N  
ATOM   7494  CA  LEU B 419      -1.120 -23.431  61.363  1.00 96.14           C  
ANISOU 7494  CA  LEU B 419    13065  13782   9680   -758    871   1992       C  
ATOM   7495  C   LEU B 419      -1.693 -24.787  61.785  1.00 97.61           C  
ANISOU 7495  C   LEU B 419    13326  13823   9935   -783   1010   1976       C  
ATOM   7496  O   LEU B 419      -2.597 -24.834  62.644  1.00 98.64           O  
ANISOU 7496  O   LEU B 419    13490  13927  10060   -816   1034   1993       O  
ATOM   7497  CB  LEU B 419      -1.769 -22.986  60.055  1.00 97.75           C  
ANISOU 7497  CB  LEU B 419    13202  14077   9861   -845    848   1872       C  
ATOM   7498  CG  LEU B 419      -1.836 -21.466  59.858  1.00 97.64           C  
ANISOU 7498  CG  LEU B 419    13138  14197   9761   -841    729   1886       C  
ATOM   7499  CD1 LEU B 419      -2.035 -21.122  58.404  1.00 99.78           C  
ANISOU 7499  CD1 LEU B 419    13341  14563  10007   -886    711   1789       C  
ATOM   7500  CD2 LEU B 419      -2.981 -20.864  60.634  1.00 99.11           C  
ANISOU 7500  CD2 LEU B 419    13337  14419   9901   -863    706   1899       C  
ATOM   7501  N   ILE B 420      -1.190 -25.880  61.195  1.00 99.05           N  
ANISOU 7501  N   ILE B 420    13546  13906  10180   -770   1110   1943       N  
ATOM   7502  CA  ILE B 420      -1.660 -27.223  61.602  1.00102.09           C  
ANISOU 7502  CA  ILE B 420    14034  14122  10632   -795   1269   1930       C  
ATOM   7503  C   ILE B 420      -1.250 -27.542  63.053  1.00103.89           C  
ANISOU 7503  C   ILE B 420    14340  14269  10864   -678   1297   2080       C  
ATOM   7504  O   ILE B 420      -2.080 -28.017  63.841  1.00103.59           O  
ANISOU 7504  O   ILE B 420    14369  14146  10844   -718   1374   2093       O  
ATOM   7505  CB  ILE B 420      -1.127 -28.364  60.729  1.00104.90           C  
ANISOU 7505  CB  ILE B 420    14441  14362  11052   -789   1391   1871       C  
ATOM   7506  CG1 ILE B 420      -1.539 -28.236  59.268  1.00107.11           C  
ANISOU 7506  CG1 ILE B 420    14645  14720  11329   -910   1383   1713       C  
ATOM   7507  CG2 ILE B 420      -1.650 -29.706  61.232  1.00106.27           C  
ANISOU 7507  CG2 ILE B 420    14750  14336  11290   -822   1574   1861       C  
ATOM   7508  CD1 ILE B 420      -0.554 -28.941  58.337  1.00108.78           C  
ANISOU 7508  CD1 ILE B 420    14878  14872  11582   -860   1446   1680       C  
ATOM   7509  N   ARG B 421       0.017 -27.279  63.390  1.00104.07           N  
ANISOU 7509  N   ARG B 421    14346  14336  10858   -538   1237   2190       N  
ATOM   7510  CA  ARG B 421       0.556 -27.557  64.734  1.00106.50           C  
ANISOU 7510  CA  ARG B 421    14707  14607  11149   -404   1257   2340       C  
ATOM   7511  C   ARG B 421      -0.184 -26.752  65.857  1.00106.95           C  
ANISOU 7511  C   ARG B 421    14749  14729  11157   -435   1182   2388       C  
ATOM   7512  O   ARG B 421      -0.320 -27.224  67.017  1.00108.82           O  
ANISOU 7512  O   ARG B 421    15053  14899  11395   -372   1239   2483       O  
ATOM   7513  CB  ARG B 421       2.080 -27.353  64.714  1.00106.95           C  
ANISOU 7513  CB  ARG B 421    14716  14757  11164   -259   1197   2429       C  
ATOM   7514  CG  ARG B 421       2.949 -27.730  65.918  1.00114.02           C  
ANISOU 7514  CG  ARG B 421    15641  15659  12021    -85   1220   2589       C  
ATOM   7515  CD  ARG B 421       2.910 -29.195  66.307  1.00122.13           C  
ANISOU 7515  CD  ARG B 421    16803  16492  13106      8   1401   2648       C  
ATOM   7516  NE  ARG B 421       3.400 -30.098  65.259  1.00129.19           N  
ANISOU 7516  NE  ARG B 421    17745  17285  14054     44   1506   2598       N  
ATOM   7517  CZ  ARG B 421       3.373 -31.438  65.321  1.00138.43           C  
ANISOU 7517  CZ  ARG B 421    19058  18253  15283    113   1692   2625       C  
ATOM   7518  NH1 ARG B 421       2.893 -32.085  66.400  1.00140.15           N  
ANISOU 7518  NH1 ARG B 421    19391  18342  15516    160   1801   2711       N  
ATOM   7519  NH2 ARG B 421       3.845 -32.147  64.290  1.00139.63           N  
ANISOU 7519  NH2 ARG B 421    19250  18322  15478    139   1781   2566       N  
ATOM   7520  N   GLY B 422      -0.702 -25.570  65.508  1.00102.52           N  
ANISOU 7520  N   GLY B 422    14109  14293  10551   -525   1065   2323       N  
ATOM   7521  CA  GLY B 422      -1.531 -24.790  66.437  1.00 99.23           C  
ANISOU 7521  CA  GLY B 422    13684  13933  10086   -561   1003   2349       C  
ATOM   7522  C   GLY B 422      -2.920 -25.362  66.715  1.00 98.42           C  
ANISOU 7522  C   GLY B 422    13629  13747  10016   -655   1094   2297       C  
ATOM   7523  O   GLY B 422      -3.320 -25.503  67.900  1.00 97.24           O  
ANISOU 7523  O   GLY B 422    13526  13564   9856   -630   1118   2370       O  
ATOM   7524  N   VAL B 423      -3.678 -25.694  65.664  1.00 97.69           N  
ANISOU 7524  N   VAL B 423    13523  13638   9955   -771   1146   2166       N  
ATOM   7525  CA  VAL B 423      -5.025 -26.297  65.885  1.00 98.79           C  
ANISOU 7525  CA  VAL B 423    13698  13721  10115   -886   1244   2098       C  
ATOM   7526  C   VAL B 423      -4.906 -27.649  66.604  1.00 99.42           C  
ANISOU 7526  C   VAL B 423    13902  13613  10259   -855   1400   2158       C  
ATOM   7527  O   VAL B 423      -5.780 -28.011  67.378  1.00 96.52           O  
ANISOU 7527  O   VAL B 423    13582  13195   9895   -908   1467   2167       O  
ATOM   7528  CB  VAL B 423      -5.928 -26.470  64.610  1.00 98.14           C  
ANISOU 7528  CB  VAL B 423    13562  13686  10037  -1035   1283   1929       C  
ATOM   7529  CG1 VAL B 423      -6.497 -25.148  64.111  1.00 97.24           C  
ANISOU 7529  CG1 VAL B 423    13336  13767   9842  -1067   1152   1878       C  
ATOM   7530  CG2 VAL B 423      -5.218 -27.191  63.492  1.00 99.68           C  
ANISOU 7530  CG2 VAL B 423    13771  13815  10287  -1043   1349   1865       C  
ATOM   7531  N   MET B 424      -3.817 -28.377  66.341  1.00103.03           N  
ANISOU 7531  N   MET B 424    14415  13970  10761   -761   1463   2203       N  
ATOM   7532  CA  MET B 424      -3.498 -29.605  67.084  1.00106.41           C  
ANISOU 7532  CA  MET B 424    14978  14213  11239   -681   1617   2292       C  
ATOM   7533  C   MET B 424      -3.432 -29.336  68.591  1.00103.13           C  
ANISOU 7533  C   MET B 424    14586  13816  10782   -579   1582   2441       C  
ATOM   7534  O   MET B 424      -4.043 -30.066  69.418  1.00100.69           O  
ANISOU 7534  O   MET B 424    14373  13387  10495   -595   1699   2482       O  
ATOM   7535  CB  MET B 424      -2.191 -30.236  66.567  1.00111.98           C  
ANISOU 7535  CB  MET B 424    15724  14845  11976   -552   1669   2337       C  
ATOM   7536  CG  MET B 424      -2.340 -30.967  65.236  1.00119.96           C  
ANISOU 7536  CG  MET B 424    16765  15768  13046   -654   1772   2193       C  
ATOM   7537  SD  MET B 424      -0.746 -31.532  64.541  1.00132.69           S  
ANISOU 7537  SD  MET B 424    18406  17329  14681   -487   1811   2243       S  
ATOM   7538  CE  MET B 424      -0.715 -33.257  65.091  1.00135.87           C  
ANISOU 7538  CE  MET B 424    19030  17440  15153   -415   2073   2305       C  
ATOM   7539  N   THR B 425      -2.736 -28.249  68.936  1.00101.85           N  
ANISOU 7539  N   THR B 425    14333  13811  10553   -490   1424   2512       N  
ATOM   7540  CA  THR B 425      -2.607 -27.803  70.331  1.00100.84           C  
ANISOU 7540  CA  THR B 425    14202  13743  10368   -399   1366   2642       C  
ATOM   7541  C   THR B 425      -3.970 -27.396  70.897  1.00100.92           C  
ANISOU 7541  C   THR B 425    14206  13778  10358   -513   1351   2601       C  
ATOM   7542  O   THR B 425      -4.361 -27.879  71.987  1.00106.54           O  
ANISOU 7542  O   THR B 425    14986  14423  11071   -484   1421   2680       O  
ATOM   7543  CB  THR B 425      -1.578 -26.662  70.490  1.00 99.46           C  
ANISOU 7543  CB  THR B 425    13926  13746  10115   -312   1205   2699       C  
ATOM   7544  OG1 THR B 425      -0.371 -27.007  69.796  1.00103.01           O  
ANISOU 7544  OG1 THR B 425    14363  14200  10576   -223   1216   2716       O  
ATOM   7545  CG2 THR B 425      -1.238 -26.420  71.937  1.00 99.14           C  
ANISOU 7545  CG2 THR B 425    13887  13768  10011   -204   1169   2835       C  
ATOM   7546  N   LEU B 426      -4.719 -26.575  70.153  1.00 98.90           N  
ANISOU 7546  N   LEU B 426    11460  15053  11062  -1549   -999   1601       N  
ATOM   7547  CA  LEU B 426      -6.099 -26.218  70.599  1.00 95.82           C  
ANISOU 7547  CA  LEU B 426    11028  14611  10766  -1506  -1006   1824       C  
ATOM   7548  C   LEU B 426      -7.026 -27.403  70.811  1.00 94.91           C  
ANISOU 7548  C   LEU B 426    10970  14517  10575  -1576  -1002   1672       C  
ATOM   7549  O   LEU B 426      -7.560 -27.575  71.896  1.00 92.47           O  
ANISOU 7549  O   LEU B 426    10783  13933  10417  -1451   -970   1647       O  
ATOM   7550  CB  LEU B 426      -6.737 -25.292  69.586  1.00 97.76           C  
ANISOU 7550  CB  LEU B 426    11017  15173  10953  -1603  -1050   2191       C  
ATOM   7551  CG  LEU B 426      -8.146 -24.790  69.814  1.00 98.22           C  
ANISOU 7551  CG  LEU B 426    10950  15233  11134  -1562  -1042   2520       C  
ATOM   7552  CD1 LEU B 426      -8.148 -23.833  70.996  1.00 97.97           C  
ANISOU 7552  CD1 LEU B 426    11035  14780  11409  -1324   -941   2636       C  
ATOM   7553  CD2 LEU B 426      -8.642 -24.087  68.562  1.00 99.20           C  
ANISOU 7553  CD2 LEU B 426    10768  15766  11155  -1713  -1109   2898       C  
ATOM   7554  N   PHE B 427      -7.207 -28.212  69.775  1.00 98.53           N  
ANISOU 7554  N   PHE B 427    11353  15298  10785  -1799  -1022   1564       N  
ATOM   7555  CA  PHE B 427      -8.073 -29.384  69.846  1.00101.85           C  
ANISOU 7555  CA  PHE B 427    11829  15767  11099  -1916  -1014   1406       C  
ATOM   7556  C   PHE B 427      -7.606 -30.396  70.889  1.00100.60           C  
ANISOU 7556  C   PHE B 427    11907  15259  11054  -1790   -942   1070       C  
ATOM   7557  O   PHE B 427      -8.457 -30.990  71.612  1.00104.06           O  
ANISOU 7557  O   PHE B 427    12426  15559  11554  -1756   -935   1024       O  
ATOM   7558  CB  PHE B 427      -8.290 -30.027  68.455  1.00105.86           C  
ANISOU 7558  CB  PHE B 427    12238  16706  11276  -2243  -1033   1335       C  
ATOM   7559  CG  PHE B 427      -9.364 -29.330  67.644  1.00113.12           C  
ANISOU 7559  CG  PHE B 427    12902  18002  12074  -2414  -1141   1730       C  
ATOM   7560  CD1 PHE B 427     -10.727 -29.534  67.945  1.00118.83           C  
ANISOU 7560  CD1 PHE B 427    13552  18776  12819  -2457  -1191   1910       C  
ATOM   7561  CD2 PHE B 427      -9.047 -28.427  66.629  1.00114.38           C  
ANISOU 7561  CD2 PHE B 427    12868  18465  12124  -2523  -1196   1973       C  
ATOM   7562  CE1 PHE B 427     -11.732 -28.873  67.232  1.00119.55           C  
ANISOU 7562  CE1 PHE B 427    13365  19223  12834  -2609  -1295   2344       C  
ATOM   7563  CE2 PHE B 427     -10.047 -27.772  65.915  1.00114.73           C  
ANISOU 7563  CE2 PHE B 427    12641  18866  12083  -2680  -1304   2399       C  
ATOM   7564  CZ  PHE B 427     -11.379 -27.988  66.216  1.00117.77           C  
ANISOU 7564  CZ  PHE B 427    12937  19305  12504  -2721  -1355   2599       C  
ATOM   7565  N   SER B 428      -6.290 -30.585  71.019  1.00100.22           N  
ANISOU 7565  N   SER B 428    11954  15068  11056  -1715   -889    873       N  
ATOM   7566  CA  SER B 428      -5.801 -31.496  72.075  1.00101.02           C  
ANISOU 7566  CA  SER B 428    12244  14834  11302  -1584   -828    621       C  
ATOM   7567  C   SER B 428      -6.163 -31.021  73.491  1.00 96.65           C  
ANISOU 7567  C   SER B 428    11793  13963  10966  -1390   -863    733       C  
ATOM   7568  O   SER B 428      -6.714 -31.793  74.317  1.00 95.91           O  
ANISOU 7568  O   SER B 428    11815  13686  10939  -1346   -844    623       O  
ATOM   7569  CB  SER B 428      -4.298 -31.700  71.981  1.00103.80           C  
ANISOU 7569  CB  SER B 428    12634  15098  11704  -1529   -766    464       C  
ATOM   7570  OG  SER B 428      -3.887 -32.577  73.035  1.00110.66           O  
ANISOU 7570  OG  SER B 428    13650  15658  12738  -1405   -717    285       O  
ATOM   7571  N   ALA B 429      -5.851 -29.749  73.753  1.00 95.03           N  
ANISOU 7571  N   ALA B 429    11557  13687  10862  -1295   -896    945       N  
ATOM   7572  CA  ALA B 429      -6.230 -29.086  75.028  1.00 92.62           C  
ANISOU 7572  CA  ALA B 429    11367  13083  10741  -1150   -893   1065       C  
ATOM   7573  C   ALA B 429      -7.725 -29.135  75.303  1.00 90.78           C  
ANISOU 7573  C   ALA B 429    11113  12845  10534  -1146   -874   1187       C  
ATOM   7574  O   ALA B 429      -8.159 -29.563  76.369  1.00 86.76           O  
ANISOU 7574  O   ALA B 429    10747  12096  10119  -1071   -845   1110       O  
ATOM   7575  CB  ALA B 429      -5.780 -27.637  75.015  1.00 92.81           C  
ANISOU 7575  CB  ALA B 429    11351  13066  10845  -1096   -895   1283       C  
ATOM   7576  N   ARG B 430      -8.483 -28.701  74.302  1.00 94.42           N  
ANISOU 7576  N   ARG B 430    11373  13593  10908  -1240   -894   1403       N  
ATOM   7577  CA  ARG B 430      -9.925 -28.679  74.375  1.00 97.40           C  
ANISOU 7577  CA  ARG B 430    11662  14028  11313  -1253   -883   1594       C  
ATOM   7578  C   ARG B 430     -10.526 -30.074  74.585  1.00 94.12           C  
ANISOU 7578  C   ARG B 430    11322  13626  10811  -1332   -894   1379       C  
ATOM   7579  O   ARG B 430     -11.499 -30.189  75.332  1.00 91.48           O  
ANISOU 7579  O   ARG B 430    11025  13150  10580  -1264   -862   1454       O  
ATOM   7580  CB  ARG B 430     -10.476 -27.965  73.138  1.00105.96           C  
ANISOU 7580  CB  ARG B 430    12473  15477  12307  -1372   -928   1912       C  
ATOM   7581  CG  ARG B 430     -11.947 -27.625  73.168  1.00118.68           C  
ANISOU 7581  CG  ARG B 430    13923  17165  14004  -1366   -913   2240       C  
ATOM   7582  CD  ARG B 430     -12.441 -27.089  71.851  1.00129.30           C  
ANISOU 7582  CD  ARG B 430    14961  18935  15229  -1531   -988   2579       C  
ATOM   7583  NE  ARG B 430     -12.214 -25.654  71.828  1.00140.24           N  
ANISOU 7583  NE  ARG B 430    16241  20232  16809  -1393   -927   2885       N  
ATOM   7584  CZ  ARG B 430     -13.126 -24.741  72.167  1.00149.80           C  
ANISOU 7584  CZ  ARG B 430    17320  21329  18269  -1258   -831   3264       C  
ATOM   7585  NH1 ARG B 430     -14.350 -25.119  72.584  1.00147.40           N  
ANISOU 7585  NH1 ARG B 430    16958  20999  18046  -1237   -799   3397       N  
ATOM   7586  NH2 ARG B 430     -12.812 -23.432  72.071  1.00151.23           N  
ANISOU 7586  NH2 ARG B 430    17415  21412  18634  -1143   -747   3527       N  
ATOM   7587  N   ARG B 431      -9.954 -31.119  73.984  1.00 95.54           N  
ANISOU 7587  N   ARG B 431    11536  13942  10820  -1468   -910   1110       N  
ATOM   7588  CA  ARG B 431     -10.437 -32.493  74.264  1.00 99.18           C  
ANISOU 7588  CA  ARG B 431    12100  14359  11222  -1541   -891    875       C  
ATOM   7589  C   ARG B 431      -9.968 -33.057  75.595  1.00 97.36           C  
ANISOU 7589  C   ARG B 431    12084  13745  11161  -1374   -846    674       C  
ATOM   7590  O   ARG B 431     -10.752 -33.715  76.278  1.00 99.73           O  
ANISOU 7590  O   ARG B 431    12462  13921  11508  -1354   -833    620       O  
ATOM   7591  CB  ARG B 431     -10.075 -33.502  73.183  1.00105.14           C  
ANISOU 7591  CB  ARG B 431    12845  15355  11749  -1764   -870    638       C  
ATOM   7592  CG  ARG B 431     -10.955 -34.752  73.230  1.00111.44           C  
ANISOU 7592  CG  ARG B 431    13706  16182  12453  -1905   -848    473       C  
ATOM   7593  CD  ARG B 431     -10.450 -35.879  72.337  1.00119.18           C  
ANISOU 7593  CD  ARG B 431    14751  17298  13234  -2125   -760    158       C  
ATOM   7594  NE  ARG B 431     -11.116 -37.146  72.647  1.00126.57           N  
ANISOU 7594  NE  ARG B 431    15803  18149  14136  -2222   -706    -47       N  
ATOM   7595  CZ  ARG B 431     -11.038 -38.264  71.927  1.00138.55           C  
ANISOU 7595  CZ  ARG B 431    17404  19766  15473  -2460   -598   -329       C  
ATOM   7596  NH1 ARG B 431     -10.336 -38.302  70.787  1.00144.29           N  
ANISOU 7596  NH1 ARG B 431    18111  20702  16008  -2645   -520   -451       N  
ATOM   7597  NH2 ARG B 431     -11.694 -39.357  72.341  1.00142.81           N  
ANISOU 7597  NH2 ARG B 431    18057  20188  16014  -2530   -546   -497       N  
ATOM   7598  N   GLN B 432      -8.727 -32.793  76.001  1.00 97.33           N  
ANISOU 7598  N   GLN B 432    12165  13567  11249  -1266   -833    592       N  
ATOM   7599  CA  GLN B 432      -8.286 -33.281  77.335  1.00 96.13           C  
ANISOU 7599  CA  GLN B 432    12197  13076  11252  -1134   -814    457       C  
ATOM   7600  C   GLN B 432      -9.106 -32.800  78.525  1.00 90.45           C  
ANISOU 7600  C   GLN B 432    11575  12133  10660  -1029   -809    586       C  
ATOM   7601  O   GLN B 432      -9.331 -33.568  79.466  1.00 91.47           O  
ANISOU 7601  O   GLN B 432    11833  12064  10855   -985   -796    470       O  
ATOM   7602  CB  GLN B 432      -6.853 -32.920  77.605  1.00102.58           C  
ANISOU 7602  CB  GLN B 432    13058  13774  12143  -1063   -825    423       C  
ATOM   7603  CG  GLN B 432      -5.869 -33.971  77.176  1.00112.97           C  
ANISOU 7603  CG  GLN B 432    14369  15111  13443  -1096   -778    208       C  
ATOM   7604  CD  GLN B 432      -4.589 -33.373  76.620  1.00133.72           C  
ANISOU 7604  CD  GLN B 432    16921  17817  16070  -1089   -784    246       C  
ATOM   7605  OE1 GLN B 432      -4.365 -32.132  76.596  1.00145.10           O  
ANISOU 7605  OE1 GLN B 432    18323  19290  17515  -1065   -840    430       O  
ATOM   7606  NE2 GLN B 432      -3.712 -34.257  76.163  1.00151.92           N  
ANISOU 7606  NE2 GLN B 432    19201  20135  18384  -1108   -703     77       N  
ATOM   7607  N   LEU B 433      -9.525 -31.545  78.504  1.00 86.17           N  
ANISOU 7607  N   LEU B 433    10974  11602  10163   -987   -796    827       N  
ATOM   7608  CA  LEU B 433     -10.446 -31.038  79.506  1.00 86.66           C  
ANISOU 7608  CA  LEU B 433    11121  11452  10351   -897   -734    960       C  
ATOM   7609  C   LEU B 433     -11.793 -31.692  79.382  1.00 88.74           C  
ANISOU 7609  C   LEU B 433    11312  11812  10590   -936   -722   1003       C  
ATOM   7610  O   LEU B 433     -12.387 -32.079  80.386  1.00 93.00           O  
ANISOU 7610  O   LEU B 433    11977  12149  11211   -878   -680    962       O  
ATOM   7611  CB  LEU B 433     -10.650 -29.546  79.328  1.00 88.90           C  
ANISOU 7611  CB  LEU B 433    11330  11728  10719   -845   -673   1231       C  
ATOM   7612  CG  LEU B 433     -11.660 -28.848  80.269  1.00 90.19           C  
ANISOU 7612  CG  LEU B 433    11551  11672  11043   -747   -539   1414       C  
ATOM   7613  CD1 LEU B 433     -11.232 -28.926  81.718  1.00 89.35           C  
ANISOU 7613  CD1 LEU B 433    11704  11208  11035   -685   -453   1339       C  
ATOM   7614  CD2 LEU B 433     -11.850 -27.390  79.861  1.00 92.70           C  
ANISOU 7614  CD2 LEU B 433    11650  12132  11438   -722   -471   1753       C  
ATOM   7615  N   ALA B 434     -12.319 -31.744  78.163  1.00 89.17           N  
ANISOU 7615  N   ALA B 434    11160  12195  10525  -1055   -764   1116       N  
ATOM   7616  CA  ALA B 434     -13.634 -32.339  77.913  1.00 90.95           C  
ANISOU 7616  CA  ALA B 434    11283  12574  10699  -1140   -776   1198       C  
ATOM   7617  C   ALA B 434     -13.706 -33.769  78.417  1.00 89.55           C  
ANISOU 7617  C   ALA B 434    11250  12295  10479  -1182   -784    913       C  
ATOM   7618  O   ALA B 434     -14.681 -34.150  79.038  1.00 90.07           O  
ANISOU 7618  O   ALA B 434    11346  12271  10603  -1157   -760    952       O  
ATOM   7619  CB  ALA B 434     -13.945 -32.306  76.434  1.00 94.98           C  
ANISOU 7619  CB  ALA B 434    11560  13503  11023  -1335   -849   1331       C  
ATOM   7620  N   ASP B 435     -12.669 -34.543  78.152  1.00 89.30           N  
ANISOU 7620  N   ASP B 435    11298  12263  10368  -1237   -799    645       N  
ATOM   7621  CA  ASP B 435     -12.584 -35.893  78.675  1.00 91.96           C  
ANISOU 7621  CA  ASP B 435    11774  12454  10710  -1254   -778    381       C  
ATOM   7622  C   ASP B 435     -12.541 -35.966  80.170  1.00 89.85           C  
ANISOU 7622  C   ASP B 435    11680  11844  10615  -1093   -753    350       C  
ATOM   7623  O   ASP B 435     -13.101 -36.883  80.764  1.00 92.80           O  
ANISOU 7623  O   ASP B 435    12134  12107  11019  -1096   -738    249       O  
ATOM   7624  CB  ASP B 435     -11.338 -36.595  78.165  1.00 98.78           C  
ANISOU 7624  CB  ASP B 435    12680  13330  11519  -1306   -751    135       C  
ATOM   7625  CG  ASP B 435     -11.437 -36.958  76.718  1.00106.99           C  
ANISOU 7625  CG  ASP B 435    13607  14698  12346  -1526   -740     68       C  
ATOM   7626  OD1 ASP B 435     -12.555 -37.322  76.263  1.00117.69           O  
ANISOU 7626  OD1 ASP B 435    14897  16245  13574  -1687   -762    113       O  
ATOM   7627  OD2 ASP B 435     -10.383 -36.882  76.030  1.00114.57           O  
ANISOU 7627  OD2 ASP B 435    14544  15733  13252  -1560   -707    -24       O  
ATOM   7628  N   LEU B 436     -11.819 -35.045  80.790  1.00 87.38           N  
ANISOU 7628  N   LEU B 436    11436  11364  10399   -978   -748    424       N  
ATOM   7629  CA  LEU B 436     -11.770 -34.976  82.248  1.00 84.93           C  
ANISOU 7629  CA  LEU B 436    11309  10746  10215   -871   -724    411       C  
ATOM   7630  C   LEU B 436     -13.092 -34.638  82.852  1.00 83.04           C  
ANISOU 7630  C   LEU B 436    11090  10422  10037   -827   -663    558       C  
ATOM   7631  O   LEU B 436     -13.505 -35.249  83.846  1.00 83.72           O  
ANISOU 7631  O   LEU B 436    11305  10326  10178   -796   -641    486       O  
ATOM   7632  CB  LEU B 436     -10.752 -33.935  82.688  1.00 84.82           C  
ANISOU 7632  CB  LEU B 436    11370  10604  10251   -817   -728    473       C  
ATOM   7633  CG  LEU B 436     -10.314 -33.876  84.179  1.00 83.78           C  
ANISOU 7633  CG  LEU B 436    11454  10181  10197   -775   -724    432       C  
ATOM   7634  CD1 LEU B 436      -9.274 -34.986  84.417  1.00 84.27           C  
ANISOU 7634  CD1 LEU B 436    11545  10203  10268   -793   -796    268       C  
ATOM   7635  CD2 LEU B 436      -9.715 -32.511  84.488  1.00 82.89           C  
ANISOU 7635  CD2 LEU B 436    11416   9975  10104   -769   -698    547       C  
ATOM   7636  N   GLU B 437     -13.750 -33.668  82.239  1.00 81.16           N  
ANISOU 7636  N   GLU B 437    10710  10318   9806   -822   -625    787       N  
ATOM   7637  CA  GLU B 437     -15.007 -33.212  82.688  1.00 82.33           C  
ANISOU 7637  CA  GLU B 437    10834  10394  10053   -763   -533    984       C  
ATOM   7638  C   GLU B 437     -15.998 -34.335  82.636  1.00 82.53           C  
ANISOU 7638  C   GLU B 437    10809  10513  10035   -826   -563    939       C  
ATOM   7639  O   GLU B 437     -16.851 -34.443  83.526  1.00 86.67           O  
ANISOU 7639  O   GLU B 437    11406  10869  10654   -762   -488    992       O  
ATOM   7640  CB  GLU B 437     -15.443 -32.068  81.834  1.00 87.09           C  
ANISOU 7640  CB  GLU B 437    11233  11165  10690   -752   -491   1277       C  
ATOM   7641  CG  GLU B 437     -16.466 -31.173  82.478  1.00 93.22           C  
ANISOU 7641  CG  GLU B 437    12003  11763  11652   -634   -324   1530       C  
ATOM   7642  CD  GLU B 437     -15.780 -30.315  83.537  1.00 98.58           C  
ANISOU 7642  CD  GLU B 437    12924  12094  12434   -544   -196   1472       C  
ATOM   7643  OE1 GLU B 437     -14.951 -29.440  83.156  1.00100.12           O  
ANISOU 7643  OE1 GLU B 437    13111  12298  12632   -542   -192   1516       O  
ATOM   7644  OE2 GLU B 437     -16.022 -30.548  84.756  1.00105.04           O  
ANISOU 7644  OE2 GLU B 437    13956  12642  13310   -503   -106   1368       O  
ATOM   7645  N   ASP B 438     -15.881 -35.150  81.581  1.00 82.57           N  
ANISOU 7645  N   ASP B 438    10700  10783   9888   -971   -657    836       N  
ATOM   7646  CA  ASP B 438     -16.751 -36.301  81.335  1.00 83.80           C  
ANISOU 7646  CA  ASP B 438    10810  11068   9961  -1091   -693    765       C  
ATOM   7647  C   ASP B 438     -16.585 -37.372  82.355  1.00 79.57           C  
ANISOU 7647  C   ASP B 438    10469  10286   9476  -1052   -679    530       C  
ATOM   7648  O   ASP B 438     -17.572 -37.924  82.873  1.00 79.64           O  
ANISOU 7648  O   ASP B 438    10497  10240   9519  -1057   -660    553       O  
ATOM   7649  CB  ASP B 438     -16.438 -36.914  79.972  1.00 89.52           C  
ANISOU 7649  CB  ASP B 438    11424  12105  10483  -1297   -764    651       C  
ATOM   7650  CG  ASP B 438     -17.622 -37.612  79.335  1.00 96.07           C  
ANISOU 7650  CG  ASP B 438    12128  13190  11181  -1494   -808    712       C  
ATOM   7651  OD1 ASP B 438     -17.849 -38.854  79.574  1.00 94.85           O  
ANISOU 7651  OD1 ASP B 438    12078  12977  10984  -1580   -802    493       O  
ATOM   7652  OD2 ASP B 438     -18.276 -36.888  78.533  1.00105.92           O  
ANISOU 7652  OD2 ASP B 438    13161  14717  12367  -1582   -851    999       O  
ATOM   7653  N   ASN B 439     -15.339 -37.643  82.673  1.00 77.49           N  
ANISOU 7653  N   ASN B 439    10333   9876   9232  -1010   -687    336       N  
ATOM   7654  CA  ASN B 439     -15.030 -38.586  83.719  1.00 77.77           C  
ANISOU 7654  CA  ASN B 439    10537   9666   9342   -961   -678    157       C  
ATOM   7655  C   ASN B 439     -15.493 -38.099  85.101  1.00 76.59           C  
ANISOU 7655  C   ASN B 439    10522   9268   9309   -845   -632    259       C  
ATOM   7656  O   ASN B 439     -16.027 -38.887  85.927  1.00 76.04           O  
ANISOU 7656  O   ASN B 439    10545   9059   9285   -833   -618    196       O  
ATOM   7657  CB  ASN B 439     -13.533 -38.820  83.787  1.00 78.69           C  
ANISOU 7657  CB  ASN B 439    10722   9691   9486   -933   -697      7       C  
ATOM   7658  CG  ASN B 439     -13.023 -39.632  82.634  1.00 81.29           C  
ANISOU 7658  CG  ASN B 439    10971  10187   9728  -1043   -687   -159       C  
ATOM   7659  OD1 ASN B 439     -13.681 -40.572  82.203  1.00 84.73           O  
ANISOU 7659  OD1 ASN B 439    11385  10705  10100  -1153   -661   -264       O  
ATOM   7660  ND2 ASN B 439     -11.804 -39.309  82.154  1.00 82.34           N  
ANISOU 7660  ND2 ASN B 439    11073  10355   9858  -1029   -689   -197       N  
ATOM   7661  N   TRP B 440     -15.255 -36.831  85.371  1.00 76.08           N  
ANISOU 7661  N   TRP B 440    10486   9132   9288   -776   -591    400       N  
ATOM   7662  CA  TRP B 440     -15.663 -36.284  86.629  1.00 79.34           C  
ANISOU 7662  CA  TRP B 440    11056   9298   9790   -699   -502    476       C  
ATOM   7663  C   TRP B 440     -17.174 -36.323  86.704  1.00 81.49           C  
ANISOU 7663  C   TRP B 440    11255   9595  10112   -677   -423    620       C  
ATOM   7664  O   TRP B 440     -17.733 -36.569  87.770  1.00 85.98           O  
ANISOU 7664  O   TRP B 440    11955   9972  10741   -639   -355    609       O  
ATOM   7665  CB  TRP B 440     -15.118 -34.883  86.742  1.00 83.73           C  
ANISOU 7665  CB  TRP B 440    11662   9774  10377   -659   -439    588       C  
ATOM   7666  CG  TRP B 440     -15.093 -34.248  88.122  1.00 89.93           C  
ANISOU 7666  CG  TRP B 440    12685  10265  11219   -630   -328    599       C  
ATOM   7667  CD1 TRP B 440     -14.188 -34.503  89.136  1.00 93.77           C  
ANISOU 7667  CD1 TRP B 440    13374  10587  11668   -683   -378    468       C  
ATOM   7668  CD2 TRP B 440     -15.905 -33.177  88.586  1.00 94.34           C  
ANISOU 7668  CD2 TRP B 440    13306  10665  11871   -571   -131    758       C  
ATOM   7669  NE1 TRP B 440     -14.413 -33.652  90.209  1.00 95.31           N  
ANISOU 7669  NE1 TRP B 440    13781  10544  11885   -696   -232    511       N  
ATOM   7670  CE2 TRP B 440     -15.469 -32.845  89.894  1.00 96.21           C  
ANISOU 7670  CE2 TRP B 440    13824  10636  12096   -615    -55    672       C  
ATOM   7671  CE3 TRP B 440     -16.968 -32.465  88.029  1.00101.03           C  
ANISOU 7671  CE3 TRP B 440    13992  11569  12826   -494      3    988       C  
ATOM   7672  CZ2 TRP B 440     -16.082 -31.851  90.659  1.00103.48           C  
ANISOU 7672  CZ2 TRP B 440    14905  11315  13098   -588    186    761       C  
ATOM   7673  CZ3 TRP B 440     -17.591 -31.436  88.812  1.00107.96           C  
ANISOU 7673  CZ3 TRP B 440    14998  12185  13837   -426    258   1116       C  
ATOM   7674  CH2 TRP B 440     -17.130 -31.139  90.100  1.00106.56           C  
ANISOU 7674  CH2 TRP B 440    15136  11716  13634   -476    362    978       C  
ATOM   7675  N   GLU B 441     -17.857 -36.063  85.595  1.00 85.44           N  
ANISOU 7675  N   GLU B 441    11532  10344  10585   -713   -431    782       N  
ATOM   7676  CA  GLU B 441     -19.316 -36.135  85.595  1.00 88.92           C  
ANISOU 7676  CA  GLU B 441    11854  10847  11083   -706   -371    972       C  
ATOM   7677  C   GLU B 441     -19.824 -37.544  85.747  1.00 81.58           C  
ANISOU 7677  C   GLU B 441    10942   9957  10096   -789   -440    826       C  
ATOM   7678  O   GLU B 441     -20.862 -37.770  86.381  1.00 78.11           O  
ANISOU 7678  O   GLU B 441    10511   9434   9732   -754   -375    916       O  
ATOM   7679  CB  GLU B 441     -19.901 -35.439  84.359  1.00102.94           C  
ANISOU 7679  CB  GLU B 441    13351  12915  12844   -750   -382   1247       C  
ATOM   7680  CG  GLU B 441     -21.308 -34.886  84.606  1.00122.38           C  
ANISOU 7680  CG  GLU B 441    15677  15360  15459   -672   -253   1571       C  
ATOM   7681  CD  GLU B 441     -21.486 -34.083  85.950  1.00136.15           C  
ANISOU 7681  CD  GLU B 441    17616  16715  17399   -496    -30   1623       C  
ATOM   7682  OE1 GLU B 441     -20.671 -33.144  86.228  1.00138.30           O  
ANISOU 7682  OE1 GLU B 441    18015  16814  17717   -431     56   1596       O  
ATOM   7683  OE2 GLU B 441     -22.456 -34.409  86.718  1.00141.46           O  
ANISOU 7683  OE2 GLU B 441    18324  17258  18165   -446     69   1683       O  
ATOM   7684  N   THR B 442     -19.073 -38.498  85.183  1.00 78.23           N  
ANISOU 7684  N   THR B 442    10531   9638   9554   -897   -547    597       N  
ATOM   7685  CA  THR B 442     -19.344 -39.957  85.409  1.00 74.67           C  
ANISOU 7685  CA  THR B 442    10141   9162   9065   -980   -588    404       C  
ATOM   7686  C   THR B 442     -19.214 -40.358  86.845  1.00 72.62           C  
ANISOU 7686  C   THR B 442    10085   8596   8910   -880   -548    309       C  
ATOM   7687  O   THR B 442     -20.074 -41.131  87.327  1.00 73.07           O  
ANISOU 7687  O   THR B 442    10166   8604   8993   -902   -536    295       O  
ATOM   7688  CB  THR B 442     -18.436 -40.856  84.550  1.00 74.18           C  
ANISOU 7688  CB  THR B 442    10078   9214   8894  -1103   -648    165       C  
ATOM   7689  OG1 THR B 442     -18.782 -40.682  83.174  1.00 76.40           O  
ANISOU 7689  OG1 THR B 442    10176   9824   9028  -1262   -688    242       O  
ATOM   7690  CG2 THR B 442     -18.571 -42.320  84.872  1.00 74.44           C  
ANISOU 7690  CG2 THR B 442    10200   9151   8930  -1170   -646    -44       C  
ATOM   7691  N   LEU B 443     -18.168 -39.849  87.526  1.00 71.00           N  
ANISOU 7691  N   LEU B 443    10020   8207   8750   -798   -536    257       N  
ATOM   7692  CA  LEU B 443     -18.014 -40.122  88.980  1.00 70.72           C  
ANISOU 7692  CA  LEU B 443    10185   7899   8783   -742   -508    198       C  
ATOM   7693  C   LEU B 443     -19.167 -39.628  89.824  1.00 70.88           C  
ANISOU 7693  C   LEU B 443    10264   7797   8868   -684   -393    345       C  
ATOM   7694  O   LEU B 443     -19.697 -40.362  90.691  1.00 71.85           O  
ANISOU 7694  O   LEU B 443    10480   7794   9023   -683   -375    302       O  
ATOM   7695  CB  LEU B 443     -16.743 -39.516  89.536  1.00 72.23           C  
ANISOU 7695  CB  LEU B 443    10505   7957   8979   -715   -526    163       C  
ATOM   7696  CG  LEU B 443     -15.441 -40.251  89.138  1.00 74.31           C  
ANISOU 7696  CG  LEU B 443    10744   8259   9229   -749   -626     16       C  
ATOM   7697  CD1 LEU B 443     -14.203 -39.324  89.124  1.00 75.62           C  
ANISOU 7697  CD1 LEU B 443    10943   8409   9378   -741   -657     47       C  
ATOM   7698  CD2 LEU B 443     -15.200 -41.426  90.057  1.00 74.49           C  
ANISOU 7698  CD2 LEU B 443    10862   8127   9312   -756   -662    -81       C  
ATOM   7699  N   ASN B 444     -19.567 -38.399  89.589  1.00 71.79           N  
ANISOU 7699  N   ASN B 444    10323   7932   9021   -631   -291    529       N  
ATOM   7700  CA  ASN B 444     -20.646 -37.805  90.374  1.00 75.26           C  
ANISOU 7700  CA  ASN B 444    10814   8219   9560   -556   -119    689       C  
ATOM   7701  C   ASN B 444     -22.006 -38.417  90.135  1.00 76.48           C  
ANISOU 7701  C   ASN B 444    10815   8487   9754   -563   -104    806       C  
ATOM   7702  O   ASN B 444     -22.846 -38.468  91.041  1.00 77.63           O  
ANISOU 7702  O   ASN B 444    11040   8475   9980   -513     16    870       O  
ATOM   7703  CB  ASN B 444     -20.723 -36.318  90.098  1.00 78.85           C  
ANISOU 7703  CB  ASN B 444    11223   8644  10089   -485     25    882       C  
ATOM   7704  CG  ASN B 444     -19.467 -35.594  90.537  1.00 82.05           C  
ANISOU 7704  CG  ASN B 444    11820   8899  10455   -498     38    776       C  
ATOM   7705  OD1 ASN B 444     -18.622 -36.114  91.335  1.00 81.41           O  
ANISOU 7705  OD1 ASN B 444    11931   8701  10300   -560    -42    590       O  
ATOM   7706  ND2 ASN B 444     -19.341 -34.343  90.053  1.00 85.86           N  
ANISOU 7706  ND2 ASN B 444    12244   9383  10994   -452    142    925       N  
ATOM   7707  N   ASP B 445     -22.253 -38.810  88.894  1.00 78.43           N  
ANISOU 7707  N   ASP B 445    10841   9022   9936   -645   -217    853       N  
ATOM   7708  CA  ASP B 445     -23.513 -39.469  88.533  1.00 80.48           C  
ANISOU 7708  CA  ASP B 445    10932   9447  10197   -708   -240    975       C  
ATOM   7709  C   ASP B 445     -23.625 -40.856  89.159  1.00 76.05           C  
ANISOU 7709  C   ASP B 445    10494   8798   9601   -768   -303    767       C  
ATOM   7710  O   ASP B 445     -24.698 -41.241  89.631  1.00 75.18           O  
ANISOU 7710  O   ASP B 445    10357   8658   9548   -762   -255    862       O  
ATOM   7711  CB  ASP B 445     -23.677 -39.559  86.984  1.00 83.58           C  
ANISOU 7711  CB  ASP B 445    11071  10209  10474   -852   -362   1068       C  
ATOM   7712  CG  ASP B 445     -24.029 -38.220  86.341  1.00 85.82           C  
ANISOU 7712  CG  ASP B 445    11154  10624  10829   -795   -293   1392       C  
ATOM   7713  OD1 ASP B 445     -24.759 -37.415  86.988  1.00 89.31           O  
ANISOU 7713  OD1 ASP B 445    11575  10908  11449   -652   -121   1625       O  
ATOM   7714  OD2 ASP B 445     -23.589 -37.985  85.188  1.00 86.48           O  
ANISOU 7714  OD2 ASP B 445    11095  10959  10801   -896   -391   1424       O  
ATOM   7715  N   ASN B 446     -22.539 -41.598  89.113  1.00 72.30           N  
ANISOU 7715  N   ASN B 446    10129   8286   9054   -821   -399    510       N  
ATOM   7716  CA  ASN B 446     -22.524 -42.898  89.750  1.00 72.53           C  
ANISOU 7716  CA  ASN B 446    10275   8197   9086   -862   -439    327       C  
ATOM   7717  C   ASN B 446     -22.508 -42.852  91.288  1.00 71.65           C  
ANISOU 7717  C   ASN B 446    10367   7797   9059   -765   -366    313       C  
ATOM   7718  O   ASN B 446     -22.923 -43.840  91.936  1.00 70.10           O  
ANISOU 7718  O   ASN B 446    10235   7509   8888   -789   -378    243       O  
ATOM   7719  CB  ASN B 446     -21.322 -43.688  89.293  1.00 72.39           C  
ANISOU 7719  CB  ASN B 446    10300   8190   9014   -927   -523     91       C  
ATOM   7720  CG  ASN B 446     -21.502 -44.214  87.920  1.00 73.60           C  
ANISOU 7720  CG  ASN B 446    10306   8602   9057  -1085   -574     32       C  
ATOM   7721  OD1 ASN B 446     -22.487 -44.909  87.624  1.00 73.49           O  
ANISOU 7721  OD1 ASN B 446    10222   8701   8999  -1201   -587     47       O  
ATOM   7722  ND2 ASN B 446     -20.557 -43.903  87.055  1.00 74.60           N  
ANISOU 7722  ND2 ASN B 446    10391   8836   9118  -1118   -600    -38       N  
ATOM   7723  N   LEU B 447     -22.014 -41.745  91.876  1.00 69.38           N  
ANISOU 7723  N   LEU B 447    10192   7370   8798   -684   -287    370       N  
ATOM   7724  CA  LEU B 447     -22.170 -41.575  93.315  1.00 67.80           C  
ANISOU 7724  CA  LEU B 447    10198   6921   8640   -640   -189    374       C  
ATOM   7725  C   LEU B 447     -23.648 -41.461  93.699  1.00 68.65           C  
ANISOU 7725  C   LEU B 447    10263   6993   8826   -594    -51    536       C  
ATOM   7726  O   LEU B 447     -24.073 -42.073  94.679  1.00 70.01           O  
ANISOU 7726  O   LEU B 447    10553   7029   9018   -600    -19    498       O  
ATOM   7727  CB  LEU B 447     -21.342 -40.413  93.842  1.00 66.97           C  
ANISOU 7727  CB  LEU B 447    10251   6674   8518   -615   -115    382       C  
ATOM   7728  CG  LEU B 447     -19.869 -40.755  94.115  1.00 65.94           C  
ANISOU 7728  CG  LEU B 447    10228   6504   8321   -677   -253    230       C  
ATOM   7729  CD1 LEU B 447     -19.012 -39.516  94.378  1.00 65.33           C  
ANISOU 7729  CD1 LEU B 447    10277   6344   8201   -692   -202    253       C  
ATOM   7730  CD2 LEU B 447     -19.752 -41.684  95.314  1.00 66.39           C  
ANISOU 7730  CD2 LEU B 447    10437   6416   8369   -727   -299    152       C  
ATOM   7731  N   LYS B 448     -24.443 -40.749  92.908  1.00 70.55           N  
ANISOU 7731  N   LYS B 448    10311   7371   9121   -553     25    742       N  
ATOM   7732  CA  LYS B 448     -25.901 -40.656  93.153  1.00 72.99           C  
ANISOU 7732  CA  LYS B 448    10519   7675   9538   -501    162    955       C  
ATOM   7733  C   LYS B 448     -26.577 -42.012  93.134  1.00 70.88           C  
ANISOU 7733  C   LYS B 448    10184   7504   9242   -584     50    904       C  
ATOM   7734  O   LYS B 448     -27.392 -42.334  93.956  1.00 70.49           O  
ANISOU 7734  O   LYS B 448    10186   7339   9255   -555    138    957       O  
ATOM   7735  CB  LYS B 448     -26.575 -39.720  92.162  1.00 78.03           C  
ANISOU 7735  CB  LYS B 448    10899   8489  10258   -454    235   1243       C  
ATOM   7736  CG  LYS B 448     -26.117 -38.274  92.267  1.00 83.99           C  
ANISOU 7736  CG  LYS B 448    11718   9101  11090   -352    408   1335       C  
ATOM   7737  CD  LYS B 448     -26.724 -37.370  91.165  1.00 90.86           C  
ANISOU 7737  CD  LYS B 448    12287  10170  12066   -303    466   1664       C  
ATOM   7738  CE  LYS B 448     -26.227 -35.918  91.228  1.00 96.03           C  
ANISOU 7738  CE  LYS B 448    13006  10658  12821   -198    659   1757       C  
ATOM   7739  NZ  LYS B 448     -25.100 -35.492  90.303  1.00 98.11           N  
ANISOU 7739  NZ  LYS B 448    13226  11070  12981   -250    516   1686       N  
ATOM   7740  N   VAL B 449     -26.188 -42.825  92.190  1.00 70.55           N  
ANISOU 7740  N   VAL B 449    10043   7663   9098   -702   -130    785       N  
ATOM   7741  CA  VAL B 449     -26.701 -44.179  92.052  1.00 70.12           C  
ANISOU 7741  CA  VAL B 449     9944   7695   9001   -818   -233    697       C  
ATOM   7742  C   VAL B 449     -26.434 -45.011  93.296  1.00 68.28           C  
ANISOU 7742  C   VAL B 449     9927   7218   8796   -797   -227    527       C  
ATOM   7743  O   VAL B 449     -27.339 -45.764  93.739  1.00 68.02           O  
ANISOU 7743  O   VAL B 449     9885   7162   8797   -827   -216    559       O  
ATOM   7744  CB  VAL B 449     -26.051 -44.871  90.836  1.00 70.41           C  
ANISOU 7744  CB  VAL B 449     9900   7939   8912   -970   -383    532       C  
ATOM   7745  CG1 VAL B 449     -26.440 -46.358  90.774  1.00 71.91           C  
ANISOU 7745  CG1 VAL B 449    10101   8159   9061  -1111   -455    385       C  
ATOM   7746  CG2 VAL B 449     -26.492 -44.176  89.577  1.00 72.15           C  
ANISOU 7746  CG2 VAL B 449     9884   8455   9072  -1042   -411    730       C  
ATOM   7747  N   ILE B 450     -25.195 -44.907  93.814  1.00 66.92           N  
ANISOU 7747  N   ILE B 450     9929   6890   8606   -763   -250    372       N  
ATOM   7748  CA  ILE B 450     -24.779 -45.688  94.963  1.00 66.93           C  
ANISOU 7748  CA  ILE B 450    10115   6689   8626   -764   -272    245       C  
ATOM   7749  C   ILE B 450     -25.521 -45.218  96.168  1.00 68.23           C  
ANISOU 7749  C   ILE B 450    10402   6686   8835   -705   -129    356       C  
ATOM   7750  O   ILE B 450     -25.964 -46.015  96.975  1.00 67.36           O  
ANISOU 7750  O   ILE B 450    10365   6478   8748   -725   -127    332       O  
ATOM   7751  CB  ILE B 450     -23.281 -45.622  95.239  1.00 66.27           C  
ANISOU 7751  CB  ILE B 450    10153   6511   8515   -764   -341    116       C  
ATOM   7752  CG1 ILE B 450     -22.497 -46.276  94.107  1.00 67.36           C  
ANISOU 7752  CG1 ILE B 450    10180   6778   8635   -818   -447    -15       C  
ATOM   7753  CG2 ILE B 450     -22.932 -46.434  96.490  1.00 66.33           C  
ANISOU 7753  CG2 ILE B 450    10318   6334   8548   -784   -375     51       C  
ATOM   7754  CD1 ILE B 450     -21.094 -45.729  93.949  1.00 67.34           C  
ANISOU 7754  CD1 ILE B 450    10217   6757   8611   -796   -492    -66       C  
ATOM   7755  N   GLU B 451     -25.657 -43.912  96.285  1.00 71.93           N  
ANISOU 7755  N   GLU B 451    10900   7108   9321   -635     13    477       N  
ATOM   7756  CA  GLU B 451     -26.446 -43.333  97.368  1.00 76.60           C  
ANISOU 7756  CA  GLU B 451    11620   7518   9967   -579    220    584       C  
ATOM   7757  C   GLU B 451     -27.868 -43.959  97.446  1.00 75.92           C  
ANISOU 7757  C   GLU B 451    11408   7477   9960   -564    272    712       C  
ATOM   7758  O   GLU B 451     -28.328 -44.359  98.502  1.00 77.63           O  
ANISOU 7758  O   GLU B 451    11754   7548  10191   -568    346    701       O  
ATOM   7759  CB  GLU B 451     -26.516 -41.834  97.140  1.00 83.72           C  
ANISOU 7759  CB  GLU B 451    12516   8376  10918   -499    406    719       C  
ATOM   7760  CG  GLU B 451     -26.537 -40.931  98.354  1.00 93.09           C  
ANISOU 7760  CG  GLU B 451    13961   9294  12113   -479    650    723       C  
ATOM   7761  CD  GLU B 451     -26.294 -39.451  97.978  1.00103.92           C  
ANISOU 7761  CD  GLU B 451    15341  10605  13538   -415    829    817       C  
ATOM   7762  OE1 GLU B 451     -25.376 -39.142  97.152  1.00108.61           O  
ANISOU 7762  OE1 GLU B 451    15865  11319  14080   -433    692    774       O  
ATOM   7763  OE2 GLU B 451     -27.027 -38.575  98.512  1.00114.10           O  
ANISOU 7763  OE2 GLU B 451    16708  11707  14936   -343   1135    940       O  
ATOM   7764  N   LYS B 452     -28.537 -44.034  96.305  1.00 75.28           N  
ANISOU 7764  N   LYS B 452    11068   7621   9914   -569    222    846       N  
ATOM   7765  CA  LYS B 452     -29.917 -44.502  96.181  1.00 75.09           C  
ANISOU 7765  CA  LYS B 452    10870   7695   9962   -577    255   1022       C  
ATOM   7766  C   LYS B 452     -30.091 -46.033  96.165  1.00 73.35           C  
ANISOU 7766  C   LYS B 452    10638   7544   9687   -699     85    886       C  
ATOM   7767  O   LYS B 452     -31.174 -46.565  96.343  1.00 72.95           O  
ANISOU 7767  O   LYS B 452    10497   7535   9685   -724    107   1001       O  
ATOM   7768  CB  LYS B 452     -30.470 -43.953  94.875  1.00 77.47           C  
ANISOU 7768  CB  LYS B 452    10878   8259  10295   -586    235   1251       C  
ATOM   7769  CG  LYS B 452     -30.539 -42.446  94.818  1.00 80.99           C  
ANISOU 7769  CG  LYS B 452    11283   8637  10851   -450    438   1454       C  
ATOM   7770  CD  LYS B 452     -30.971 -41.939  93.453  1.00 86.45           C  
ANISOU 7770  CD  LYS B 452    11653   9623  11570   -476    383   1712       C  
ATOM   7771  CE  LYS B 452     -32.412 -42.365  93.143  1.00 91.53           C  
ANISOU 7771  CE  LYS B 452    12030  10457  12288   -521    377   1998       C  
ATOM   7772  NZ  LYS B 452     -32.953 -41.564  92.007  1.00 97.31           N  
ANISOU 7772  NZ  LYS B 452    12427  11456  13088   -526    378   2358       N  
ATOM   7773  N   ALA B 453     -29.015 -46.737  95.862  1.00 72.14           N  
ANISOU 7773  N   ALA B 453    10557   7404   9448   -777    -72    654       N  
ATOM   7774  CA  ALA B 453     -29.019 -48.214  95.739  1.00 70.90           C  
ANISOU 7774  CA  ALA B 453    10398   7279   9261   -896   -204    500       C  
ATOM   7775  C   ALA B 453     -29.710 -49.017  96.835  1.00 69.84           C  
ANISOU 7775  C   ALA B 453    10352   6999   9182   -897   -168    507       C  
ATOM   7776  O   ALA B 453     -29.308 -48.917  98.016  1.00 68.09           O  
ANISOU 7776  O   ALA B 453    10322   6568   8980   -834   -111    464       O  
ATOM   7777  CB  ALA B 453     -27.567 -48.710  95.603  1.00 70.10           C  
ANISOU 7777  CB  ALA B 453    10407   7109   9119   -926   -306    264       C  
ATOM   7778  N   ASP B 454     -30.697 -49.831  96.414  1.00 69.68           N  
ANISOU 7778  N   ASP B 454    10197   7109   9166   -998   -213    561       N  
ATOM   7779  CA  ASP B 454     -31.291 -50.859  97.277  1.00 69.36           C  
ANISOU 7779  CA  ASP B 454    10225   6954   9174  -1031   -211    538       C  
ATOM   7780  C   ASP B 454     -30.465 -52.148  97.351  1.00 66.90           C  
ANISOU 7780  C   ASP B 454    10016   6543   8859  -1113   -315    298       C  
ATOM   7781  O   ASP B 454     -30.835 -52.991  98.091  1.00 66.59           O  
ANISOU 7781  O   ASP B 454    10038   6392   8870  -1134   -315    281       O  
ATOM   7782  CB  ASP B 454     -32.730 -51.172  96.857  1.00 73.05           C  
ANISOU 7782  CB  ASP B 454    10500   7599   9656  -1118   -209    722       C  
ATOM   7783  CG  ASP B 454     -33.731 -50.072  97.225  1.00 78.06           C  
ANISOU 7783  CG  ASP B 454    11035   8248  10374   -994    -48   1019       C  
ATOM   7784  OD1 ASP B 454     -33.294 -48.959  97.648  1.00 83.63           O  
ANISOU 7784  OD1 ASP B 454    11830   8830  11115   -851     80   1060       O  
ATOM   7785  OD2 ASP B 454     -34.988 -50.276  97.055  1.00 83.21           O  
ANISOU 7785  OD2 ASP B 454    11507   9036  11071  -1045    -30   1234       O  
ATOM   7786  N   ASN B 455     -29.423 -52.345  96.544  1.00 64.97           N  
ANISOU 7786  N   ASN B 455     9773   6336   8576  -1160   -385    132       N  
ATOM   7787  CA  ASN B 455     -28.718 -53.602  96.473  1.00 64.58           C  
ANISOU 7787  CA  ASN B 455     9788   6179   8569  -1232   -435    -70       C  
ATOM   7788  C   ASN B 455     -27.314 -53.566  95.842  1.00 64.40           C  
ANISOU 7788  C   ASN B 455     9791   6134   8542  -1222   -462   -229       C  
ATOM   7789  O   ASN B 455     -26.937 -52.615  95.197  1.00 62.32           O  
ANISOU 7789  O   ASN B 455     9478   5992   8208  -1196   -467   -204       O  
ATOM   7790  CB  ASN B 455     -29.567 -54.652  95.666  1.00 65.54           C  
ANISOU 7790  CB  ASN B 455     9819   6423   8660  -1423   -458   -132       C  
ATOM   7791  CG  ASN B 455     -29.623 -54.384  94.166  1.00 65.51           C  
ANISOU 7791  CG  ASN B 455     9690   6676   8524  -1573   -490   -172       C  
ATOM   7792  OD1 ASN B 455     -28.633 -54.557  93.471  1.00 64.79           O  
ANISOU 7792  OD1 ASN B 455     9631   6578   8408  -1612   -490   -348       O  
ATOM   7793  ND2 ASN B 455     -30.803 -54.014  93.655  1.00 66.32           N  
ANISOU 7793  ND2 ASN B 455     9638   7016   8542  -1675   -515      9       N  
ATOM   7794  N   ALA B 456     -26.599 -54.687  96.000  1.00 65.53           N  
ANISOU 7794  N   ALA B 456     9997   6116   8785  -1245   -463   -377       N  
ATOM   7795  CA  ALA B 456     -25.177 -54.773  95.688  1.00 66.04           C  
ANISOU 7795  CA  ALA B 456    10087   6099   8906  -1200   -461   -494       C  
ATOM   7796  C   ALA B 456     -24.827 -54.711  94.235  1.00 66.71           C  
ANISOU 7796  C   ALA B 456    10100   6334   8913  -1298   -438   -631       C  
ATOM   7797  O   ALA B 456     -23.774 -54.262  93.869  1.00 65.77           O  
ANISOU 7797  O   ALA B 456     9975   6214   8797  -1242   -437   -675       O  
ATOM   7798  CB  ALA B 456     -24.628 -56.071  96.260  1.00 67.30           C  
ANISOU 7798  CB  ALA B 456    10300   6026   9242  -1190   -433   -569       C  
ATOM   7799  N   ALA B 457     -25.710 -55.267  93.419  1.00 68.84           N  
ANISOU 7799  N   ALA B 457    10319   6733   9101  -1473   -418   -704       N  
ATOM   7800  CA  ALA B 457     -25.526 -55.324  91.972  1.00 69.36           C  
ANISOU 7800  CA  ALA B 457    10333   6974   9045  -1639   -389   -850       C  
ATOM   7801  C   ALA B 457     -25.514 -53.962  91.425  1.00 68.24           C  
ANISOU 7801  C   ALA B 457    10100   7057   8771  -1607   -447   -723       C  
ATOM   7802  O   ALA B 457     -24.732 -53.693  90.541  1.00 70.30           O  
ANISOU 7802  O   ALA B 457    10340   7397   8972  -1644   -428   -824       O  
ATOM   7803  CB  ALA B 457     -26.627 -56.138  91.314  1.00 71.32           C  
ANISOU 7803  CB  ALA B 457    10555   7352   9190  -1891   -375   -920       C  
ATOM   7804  N   GLN B 458     -26.365 -53.096  91.949  1.00 67.27           N  
ANISOU 7804  N   GLN B 458     9919   7020   8619  -1533   -494   -496       N  
ATOM   7805  CA  GLN B 458     -26.353 -51.666  91.606  1.00 66.61           C  
ANISOU 7805  CA  GLN B 458     9746   7102   8460  -1459   -521   -329       C  
ATOM   7806  C   GLN B 458     -25.066 -51.023  91.990  1.00 66.24           C  
ANISOU 7806  C   GLN B 458     9777   6917   8472  -1297   -512   -363       C  
ATOM   7807  O   GLN B 458     -24.534 -50.263  91.236  1.00 66.35           O  
ANISOU 7807  O   GLN B 458     9734   7056   8417  -1295   -524   -357       O  
ATOM   7808  CB  GLN B 458     -27.476 -50.923  92.319  1.00 66.23           C  
ANISOU 7808  CB  GLN B 458     9642   7085   8437  -1373   -510    -71       C  
ATOM   7809  CG  GLN B 458     -28.865 -51.389  91.936  1.00 67.75           C  
ANISOU 7809  CG  GLN B 458     9709   7458   8574  -1534   -534     41       C  
ATOM   7810  CD  GLN B 458     -29.930 -50.859  92.853  1.00 67.68           C  
ANISOU 7810  CD  GLN B 458     9656   7409   8647  -1419   -483    294       C  
ATOM   7811  OE1 GLN B 458     -29.889 -51.057  94.053  1.00 65.85           O  
ANISOU 7811  OE1 GLN B 458     9558   6946   8514  -1298   -432    279       O  
ATOM   7812  NE2 GLN B 458     -30.943 -50.222  92.258  1.00 69.80           N  
ANISOU 7812  NE2 GLN B 458     9722   7920   8877  -1474   -489    549       N  
ATOM   7813  N   VAL B 459     -24.597 -51.319  93.189  1.00 67.84           N  
ANISOU 7813  N   VAL B 459    10102   6880   8792  -1180   -501   -375       N  
ATOM   7814  CA  VAL B 459     -23.442 -50.677  93.755  1.00 69.47           C  
ANISOU 7814  CA  VAL B 459    10386   6966   9042  -1054   -512   -361       C  
ATOM   7815  C   VAL B 459     -22.209 -51.081  93.008  1.00 72.67           C  
ANISOU 7815  C   VAL B 459    10775   7359   9477  -1073   -513   -517       C  
ATOM   7816  O   VAL B 459     -21.352 -50.232  92.725  1.00 75.45           O  
ANISOU 7816  O   VAL B 459    11114   7754   9798  -1019   -531   -498       O  
ATOM   7817  CB  VAL B 459     -23.273 -50.993  95.272  1.00 69.17           C  
ANISOU 7817  CB  VAL B 459    10477   6706   9098   -977   -518   -308       C  
ATOM   7818  CG1 VAL B 459     -21.953 -50.474  95.814  1.00 68.81           C  
ANISOU 7818  CG1 VAL B 459    10505   6563   9076   -905   -555   -289       C  
ATOM   7819  CG2 VAL B 459     -24.363 -50.323  96.093  1.00 68.90           C  
ANISOU 7819  CG2 VAL B 459    10486   6663   9027   -941   -476   -150       C  
ATOM   7820  N   LYS B 460     -22.080 -52.361  92.733  1.00 76.68           N  
ANISOU 7820  N   LYS B 460    11289   7785  10061  -1146   -471   -667       N  
ATOM   7821  CA  LYS B 460     -20.911 -52.902  92.078  1.00 82.16           C  
ANISOU 7821  CA  LYS B 460    11972   8413  10830  -1155   -414   -821       C  
ATOM   7822  C   LYS B 460     -20.740 -52.253  90.689  1.00 82.24           C  
ANISOU 7822  C   LYS B 460    11906   8651  10687  -1243   -401   -890       C  
ATOM   7823  O   LYS B 460     -19.631 -51.844  90.299  1.00 80.89           O  
ANISOU 7823  O   LYS B 460    11715   8482  10537  -1186   -388   -922       O  
ATOM   7824  CB  LYS B 460     -20.994 -54.444  92.005  1.00 88.07           C  
ANISOU 7824  CB  LYS B 460    12753   8999  11707  -1232   -313   -976       C  
ATOM   7825  CG  LYS B 460     -19.622 -55.063  91.819  1.00 95.68           C  
ANISOU 7825  CG  LYS B 460    13714   9784  12853  -1167   -213  -1073       C  
ATOM   7826  CD  LYS B 460     -19.611 -56.400  91.103  1.00103.56           C  
ANISOU 7826  CD  LYS B 460    14741  10658  13947  -1287    -32  -1296       C  
ATOM   7827  CE  LYS B 460     -18.202 -56.669  90.556  1.00109.95           C  
ANISOU 7827  CE  LYS B 460    15521  11341  14914  -1220    110  -1389       C  
ATOM   7828  NZ  LYS B 460     -18.095 -58.054  90.006  1.00116.42           N  
ANISOU 7828  NZ  LYS B 460    16392  11955  15884  -1318    354  -1610       N  
ATOM   7829  N   ASP B 461     -21.859 -52.133  89.979  1.00 84.19           N  
ANISOU 7829  N   ASP B 461    12097   9110  10779  -1392   -416   -881       N  
ATOM   7830  CA  ASP B 461     -21.921 -51.573  88.624  1.00 84.94           C  
ANISOU 7830  CA  ASP B 461    12103   9474  10695  -1529   -422   -912       C  
ATOM   7831  C   ASP B 461     -21.485 -50.147  88.625  1.00 78.36           C  
ANISOU 7831  C   ASP B 461    11214   8735   9824  -1403   -483   -753       C  
ATOM   7832  O   ASP B 461     -20.603 -49.790  87.902  1.00 78.33           O  
ANISOU 7832  O   ASP B 461    11183   8796   9781  -1408   -467   -819       O  
ATOM   7833  CB  ASP B 461     -23.349 -51.662  88.063  1.00 91.09           C  
ANISOU 7833  CB  ASP B 461    12803  10491  11316  -1728   -461   -843       C  
ATOM   7834  CG  ASP B 461     -23.493 -50.974  86.689  1.00 99.96           C  
ANISOU 7834  CG  ASP B 461    13804  11946  12229  -1899   -498   -809       C  
ATOM   7835  OD1 ASP B 461     -22.837 -51.449  85.725  1.00107.61           O  
ANISOU 7835  OD1 ASP B 461    14805  12965  13115  -2047   -429  -1021       O  
ATOM   7836  OD2 ASP B 461     -24.272 -49.986  86.561  1.00104.42           O  
ANISOU 7836  OD2 ASP B 461    14237  12718  12719  -1894   -578   -558       O  
ATOM   7837  N   ALA B 462     -22.109 -49.334  89.443  1.00 74.17           N  
ANISOU 7837  N   ALA B 462    10675   8193   9311  -1294   -529   -548       N  
ATOM   7838  CA  ALA B 462     -21.721 -47.943  89.552  1.00 72.20           C  
ANISOU 7838  CA  ALA B 462    10400   7987   9045  -1176   -552   -399       C  
ATOM   7839  C   ALA B 462     -20.250 -47.742  89.963  1.00 71.91           C  
ANISOU 7839  C   ALA B 462    10444   7789   9088  -1062   -555   -465       C  
ATOM   7840  O   ALA B 462     -19.618 -46.780  89.538  1.00 71.24           O  
ANISOU 7840  O   ALA B 462    10322   7784   8959  -1025   -570   -417       O  
ATOM   7841  CB  ALA B 462     -22.622 -47.238  90.542  1.00 71.55           C  
ANISOU 7841  CB  ALA B 462    10339   7843   9003  -1078   -539   -195       C  
ATOM   7842  N   LEU B 463     -19.708 -48.629  90.809  1.00 71.53           N  
ANISOU 7842  N   LEU B 463    10488   7523   9165  -1015   -546   -543       N  
ATOM   7843  CA  LEU B 463     -18.314 -48.525  91.230  1.00 70.13           C  
ANISOU 7843  CA  LEU B 463    10353   7214   9077   -927   -565   -554       C  
ATOM   7844  C   LEU B 463     -17.376 -48.946  90.159  1.00 69.79           C  
ANISOU 7844  C   LEU B 463    10244   7217   9056   -962   -516   -696       C  
ATOM   7845  O   LEU B 463     -16.314 -48.301  90.016  1.00 70.43           O  
ANISOU 7845  O   LEU B 463    10302   7309   9147   -905   -540   -662       O  
ATOM   7846  CB  LEU B 463     -18.042 -49.347  92.477  1.00 70.81           C  
ANISOU 7846  CB  LEU B 463    10522   7077   9303   -876   -578   -531       C  
ATOM   7847  CG  LEU B 463     -18.598 -48.794  93.789  1.00 70.40           C  
ANISOU 7847  CG  LEU B 463    10575   6947   9224   -841   -619   -385       C  
ATOM   7848  CD1 LEU B 463     -18.499 -49.885  94.842  1.00 71.71           C  
ANISOU 7848  CD1 LEU B 463    10799   6930   9516   -833   -635   -371       C  
ATOM   7849  CD2 LEU B 463     -17.822 -47.583  94.257  1.00 69.65           C  
ANISOU 7849  CD2 LEU B 463    10540   6850   9074   -805   -664   -282       C  
ATOM   7850  N   THR B 464     -17.707 -50.012  89.413  1.00 70.21           N  
ANISOU 7850  N   THR B 464    10277   7285   9114  -1071   -432   -861       N  
ATOM   7851  CA  THR B 464     -16.794 -50.407  88.310  1.00 71.68           C  
ANISOU 7851  CA  THR B 464    10421   7499   9313  -1123   -333  -1025       C  
ATOM   7852  C   THR B 464     -16.705 -49.294  87.286  1.00 70.65           C  
ANISOU 7852  C   THR B 464    10217   7622   9004  -1178   -370   -997       C  
ATOM   7853  O   THR B 464     -15.625 -49.051  86.740  1.00 71.36           O  
ANISOU 7853  O   THR B 464    10270   7726   9115  -1148   -331  -1043       O  
ATOM   7854  CB  THR B 464     -17.061 -51.765  87.603  1.00 73.11           C  
ANISOU 7854  CB  THR B 464    10632   7628   9519  -1270   -181  -1251       C  
ATOM   7855  OG1 THR B 464     -18.398 -51.812  87.108  1.00 74.40           O  
ANISOU 7855  OG1 THR B 464    10791   7981   9495  -1450   -211  -1275       O  
ATOM   7856  CG2 THR B 464     -16.809 -52.916  88.532  1.00 73.66           C  
ANISOU 7856  CG2 THR B 464    10755   7404   9828  -1187   -109  -1273       C  
ATOM   7857  N   LYS B 465     -17.796 -48.586  87.086  1.00 69.94           N  
ANISOU 7857  N   LYS B 465    10087   7724   8762  -1243   -442   -886       N  
ATOM   7858  CA  LYS B 465     -17.788 -47.443  86.212  1.00 71.58           C  
ANISOU 7858  CA  LYS B 465    10201   8174   8822  -1283   -486   -798       C  
ATOM   7859  C   LYS B 465     -16.961 -46.308  86.744  1.00 70.80           C  
ANISOU 7859  C   LYS B 465    10106   8015   8777  -1122   -539   -662       C  
ATOM   7860  O   LYS B 465     -16.310 -45.588  85.997  1.00 70.60           O  
ANISOU 7860  O   LYS B 465    10018   8117   8688  -1128   -547   -647       O  
ATOM   7861  CB  LYS B 465     -19.212 -46.958  85.948  1.00 73.33           C  
ANISOU 7861  CB  LYS B 465    10342   8606   8914  -1378   -542   -644       C  
ATOM   7862  CG  LYS B 465     -20.005 -47.925  85.103  1.00 77.17           C  
ANISOU 7862  CG  LYS B 465    10801   9245   9275  -1616   -512   -766       C  
ATOM   7863  CD  LYS B 465     -21.414 -47.455  84.936  1.00 80.04           C  
ANISOU 7863  CD  LYS B 465    11047   9829   9532  -1709   -586   -550       C  
ATOM   7864  CE  LYS B 465     -22.185 -48.447  84.102  1.00 84.10           C  
ANISOU 7864  CE  LYS B 465    11540  10522   9889  -2000   -577   -665       C  
ATOM   7865  NZ  LYS B 465     -23.530 -47.831  83.936  1.00 88.28           N  
ANISOU 7865  NZ  LYS B 465    11905  11306  10331  -2082   -670   -372       N  
ATOM   7866  N   MET B 466     -17.069 -46.091  88.038  1.00 71.98           N  
ANISOU 7866  N   MET B 466    10338   7987   9021  -1006   -574   -555       N  
ATOM   7867  CA  MET B 466     -16.303 -45.038  88.728  1.00 72.05           C  
ANISOU 7867  CA  MET B 466    10395   7917   9064   -896   -618   -433       C  
ATOM   7868  C   MET B 466     -14.836 -45.304  88.652  1.00 69.94           C  
ANISOU 7868  C   MET B 466    10122   7573   8877   -857   -622   -502       C  
ATOM   7869  O   MET B 466     -14.031 -44.369  88.566  1.00 67.66           O  
ANISOU 7869  O   MET B 466     9820   7321   8566   -820   -658   -429       O  
ATOM   7870  CB  MET B 466     -16.740 -44.923  90.195  1.00 73.95           C  
ANISOU 7870  CB  MET B 466    10759   7977   9361   -834   -635   -334       C  
ATOM   7871  CG  MET B 466     -18.044 -44.154  90.383  1.00 76.67           C  
ANISOU 7871  CG  MET B 466    11104   8377   9650   -829   -601   -199       C  
ATOM   7872  SD  MET B 466     -18.634 -44.166  92.088  1.00 80.54           S  
ANISOU 7872  SD  MET B 466    11764   8640  10194   -782   -572   -120       S  
ATOM   7873  CE  MET B 466     -17.405 -42.993  92.764  1.00 80.23           C  
ANISOU 7873  CE  MET B 466    11849   8501  10131   -755   -590    -62       C  
ATOM   7874  N   ARG B 467     -14.497 -46.586  88.727  1.00 70.27           N  
ANISOU 7874  N   ARG B 467    10170   7495   9035   -863   -571   -620       N  
ATOM   7875  CA  ARG B 467     -13.100 -46.990  88.686  1.00 71.68           C  
ANISOU 7875  CA  ARG B 467    10311   7574   9347   -808   -544   -650       C  
ATOM   7876  C   ARG B 467     -12.461 -46.595  87.354  1.00 72.07           C  
ANISOU 7876  C   ARG B 467    10271   7784   9326   -845   -491   -728       C  
ATOM   7877  O   ARG B 467     -11.363 -45.958  87.289  1.00 72.30           O  
ANISOU 7877  O   ARG B 467    10256   7828   9386   -789   -524   -654       O  
ATOM   7878  CB  ARG B 467     -13.014 -48.480  88.956  1.00 73.53           C  
ANISOU 7878  CB  ARG B 467    10555   7626   9756   -800   -452   -746       C  
ATOM   7879  CG  ARG B 467     -11.695 -48.860  89.529  1.00 77.24           C  
ANISOU 7879  CG  ARG B 467    10979   7936  10431   -704   -449   -656       C  
ATOM   7880  CD  ARG B 467     -11.271 -50.241  89.104  1.00 82.88           C  
ANISOU 7880  CD  ARG B 467    11646   8493  11351   -686   -268   -784       C  
ATOM   7881  NE  ARG B 467      -9.833 -50.295  89.214  1.00 87.33           N  
ANISOU 7881  NE  ARG B 467    12103   8970  12105   -588   -243   -667       N  
ATOM   7882  CZ  ARG B 467      -9.106 -51.384  89.116  1.00 91.84           C  
ANISOU 7882  CZ  ARG B 467    12598   9352  12945   -519    -74   -683       C  
ATOM   7883  NH1 ARG B 467      -7.790 -51.250  89.250  1.00 93.21           N  
ANISOU 7883  NH1 ARG B 467    12643   9480  13293   -424    -73   -513       N  
ATOM   7884  NH2 ARG B 467      -9.663 -52.583  88.908  1.00 95.82           N  
ANISOU 7884  NH2 ARG B 467    13145   9702  13559   -548    103   -846       N  
ATOM   7885  N   ALA B 468     -13.194 -46.964  86.299  1.00 71.92           N  
ANISOU 7885  N   ALA B 468    10229   7904   9194   -966   -415   -869       N  
ATOM   7886  CA  ALA B 468     -12.781 -46.816  84.933  1.00 71.43           C  
ANISOU 7886  CA  ALA B 468    10097   8013   9028  -1056   -340   -981       C  
ATOM   7887  C   ALA B 468     -12.585 -45.413  84.621  1.00 71.01           C  
ANISOU 7887  C   ALA B 468     9986   8134   8859  -1036   -437   -840       C  
ATOM   7888  O   ALA B 468     -11.662 -45.071  83.917  1.00 73.00           O  
ANISOU 7888  O   ALA B 468    10179   8459   9097  -1034   -404   -865       O  
ATOM   7889  CB  ALA B 468     -13.857 -47.370  84.033  1.00 73.42           C  
ANISOU 7889  CB  ALA B 468    10354   8420   9121  -1251   -278  -1120       C  
ATOM   7890  N   ALA B 469     -13.496 -44.574  85.095  1.00 71.91           N  
ANISOU 7890  N   ALA B 469    10113   8311   8898  -1022   -533   -684       N  
ATOM   7891  CA  ALA B 469     -13.439 -43.083  84.897  1.00 71.35           C  
ANISOU 7891  CA  ALA B 469     9991   8376   8742   -991   -605   -514       C  
ATOM   7892  C   ALA B 469     -12.288 -42.461  85.634  1.00 70.65           C  
ANISOU 7892  C   ALA B 469     9945   8152   8746   -879   -650   -432       C  
ATOM   7893  O   ALA B 469     -11.728 -41.495  85.167  1.00 70.62           O  
ANISOU 7893  O   ALA B 469     9890   8249   8693   -869   -676   -360       O  
ATOM   7894  CB  ALA B 469     -14.751 -42.416  85.350  1.00 70.89           C  
ANISOU 7894  CB  ALA B 469     9940   8356   8637   -985   -641   -352       C  
ATOM   7895  N   ALA B 470     -11.959 -42.999  86.803  1.00 70.83           N  
ANISOU 7895  N   ALA B 470    10056   7961   8894   -816   -670   -423       N  
ATOM   7896  CA  ALA B 470     -10.871 -42.468  87.579  1.00 71.69           C  
ANISOU 7896  CA  ALA B 470    10204   7967   9068   -759   -736   -319       C  
ATOM   7897  C   ALA B 470      -9.537 -42.851  86.982  1.00 72.70           C  
ANISOU 7897  C   ALA B 470    10234   8107   9281   -737   -709   -364       C  
ATOM   7898  O   ALA B 470      -8.609 -42.006  86.955  1.00 72.42           O  
ANISOU 7898  O   ALA B 470    10170   8111   9235   -722   -765   -268       O  
ATOM   7899  CB  ALA B 470     -10.984 -42.935  89.017  1.00 72.66           C  
ANISOU 7899  CB  ALA B 470    10438   7896   9273   -738   -780   -261       C  
ATOM   7900  N   LEU B 471      -9.429 -44.092  86.482  1.00 74.15           N  
ANISOU 7900  N   LEU B 471    10369   8246   9557   -741   -602   -508       N  
ATOM   7901  CA  LEU B 471      -8.186 -44.513  85.772  1.00 76.53           C  
ANISOU 7901  CA  LEU B 471    10567   8541   9968   -710   -511   -561       C  
ATOM   7902  C   LEU B 471      -7.855 -43.736  84.477  1.00 80.36           C  
ANISOU 7902  C   LEU B 471    10975   9238  10317   -760   -479   -606       C  
ATOM   7903  O   LEU B 471      -6.680 -43.426  84.190  1.00 79.98           O  
ANISOU 7903  O   LEU B 471    10848   9207  10334   -717   -469   -551       O  
ATOM   7904  CB  LEU B 471      -8.216 -45.976  85.430  1.00 76.53           C  
ANISOU 7904  CB  LEU B 471    10555   8419  10104   -715   -338   -729       C  
ATOM   7905  CG  LEU B 471      -8.107 -46.836  86.652  1.00 76.83           C  
ANISOU 7905  CG  LEU B 471    10620   8228  10344   -640   -353   -646       C  
ATOM   7906  CD1 LEU B 471      -8.751 -48.174  86.294  1.00 80.47           C  
ANISOU 7906  CD1 LEU B 471    11116   8579  10877   -683   -177   -844       C  
ATOM   7907  CD2 LEU B 471      -6.677 -47.010  87.135  1.00 77.35           C  
ANISOU 7907  CD2 LEU B 471    10578   8176  10632   -538   -358   -480       C  
ATOM   7908  N   ASP B 472      -8.903 -43.441  83.701  1.00 84.66           N  
ANISOU 7908  N   ASP B 472    11529   9959  10676   -863   -469   -678       N  
ATOM   7909  CA  ASP B 472      -8.813 -42.564  82.533  1.00 90.25           C  
ANISOU 7909  CA  ASP B 472    12160  10908  11220   -936   -471   -673       C  
ATOM   7910  C   ASP B 472      -8.498 -41.156  82.878  1.00 85.28           C  
ANISOU 7910  C   ASP B 472    11517  10330  10555   -880   -595   -479       C  
ATOM   7911  O   ASP B 472      -7.720 -40.553  82.207  1.00 89.20           O  
ANISOU 7911  O   ASP B 472    11938  10935  11016   -885   -595   -449       O  
ATOM   7912  CB  ASP B 472     -10.091 -42.565  81.713  1.00100.34           C  
ANISOU 7912  CB  ASP B 472    13426  12392  12306  -1084   -459   -730       C  
ATOM   7913  CG  ASP B 472     -10.295 -43.861  80.924  1.00115.80           C  
ANISOU 7913  CG  ASP B 472    15402  14367  14226  -1221   -304   -969       C  
ATOM   7914  OD1 ASP B 472      -9.342 -44.711  80.817  1.00127.88           O  
ANISOU 7914  OD1 ASP B 472    16946  15743  15898  -1183   -160  -1108       O  
ATOM   7915  OD2 ASP B 472     -11.449 -44.047  80.446  1.00130.51           O  
ANISOU 7915  OD2 ASP B 472    17269  16390  15929  -1378   -313  -1006       O  
ATOM   7916  N   ALA B 473      -9.151 -40.622  83.892  1.00 82.94           N  
ANISOU 7916  N   ALA B 473    11302   9947  10261   -843   -679   -356       N  
ATOM   7917  CA  ALA B 473      -8.923 -39.233  84.286  1.00 81.87           C  
ANISOU 7917  CA  ALA B 473    11192   9821  10093   -812   -758   -186       C  
ATOM   7918  C   ALA B 473      -7.509 -39.109  84.746  1.00 82.48           C  
ANISOU 7918  C   ALA B 473    11269   9806  10262   -770   -804   -137       C  
ATOM   7919  O   ALA B 473      -6.912 -38.058  84.537  1.00 83.05           O  
ANISOU 7919  O   ALA B 473    11317   9945  10292   -776   -846    -39       O  
ATOM   7920  CB  ALA B 473      -9.896 -38.778  85.386  1.00 80.30           C  
ANISOU 7920  CB  ALA B 473    11116   9500   9893   -792   -783    -89       C  
ATOM   7921  N   GLN B 474      -6.997 -40.178  85.376  1.00 83.43           N  
ANISOU 7921  N   GLN B 474    11402   9777  10518   -736   -795   -176       N  
ATOM   7922  CA  GLN B 474      -5.595 -40.251  85.796  1.00 84.48           C  
ANISOU 7922  CA  GLN B 474    11486   9839  10770   -703   -842    -83       C  
ATOM   7923  C   GLN B 474      -4.619 -40.129  84.652  1.00 87.77           C  
ANISOU 7923  C   GLN B 474    11762  10379  11206   -690   -782   -109       C  
ATOM   7924  O   GLN B 474      -3.539 -39.559  84.845  1.00 92.34           O  
ANISOU 7924  O   GLN B 474    12290  10970  11823   -683   -852     24       O  
ATOM   7925  CB  GLN B 474      -5.347 -41.581  86.532  1.00 85.16           C  
ANISOU 7925  CB  GLN B 474    11566   9753  11037   -659   -814    -92       C  
ATOM   7926  CG  GLN B 474      -4.011 -41.724  87.250  1.00 85.24           C  
ANISOU 7926  CG  GLN B 474    11503   9685  11198   -634   -889     86       C  
ATOM   7927  CD  GLN B 474      -4.009 -42.905  88.230  1.00 85.36           C  
ANISOU 7927  CD  GLN B 474    11518   9526  11387   -601   -889    143       C  
ATOM   7928  OE1 GLN B 474      -4.315 -44.038  87.860  1.00 86.87           O  
ANISOU 7928  OE1 GLN B 474    11671   9632  11704   -544   -746     17       O  
ATOM   7929  NE2 GLN B 474      -3.692 -42.639  89.482  1.00 85.10           N  
ANISOU 7929  NE2 GLN B 474    11538   9444  11351   -661  -1043    335       N  
ATOM   7930  N   LYS B 475      -4.968 -40.676  83.479  1.00 91.29           N  
ANISOU 7930  N   LYS B 475    12151  10923  11612   -710   -649   -277       N  
ATOM   7931  CA  LYS B 475      -4.114 -40.584  82.256  1.00 93.35           C  
ANISOU 7931  CA  LYS B 475    12290  11315  11861   -721   -555   -333       C  
ATOM   7932  C   LYS B 475      -3.967 -39.192  81.654  1.00 92.49           C  
ANISOU 7932  C   LYS B 475    12143  11399  11600   -763   -634   -239       C  
ATOM   7933  O   LYS B 475      -2.920 -38.897  81.057  1.00 91.99           O  
ANISOU 7933  O   LYS B 475    11978  11408  11562   -750   -607   -206       O  
ATOM   7934  CB  LYS B 475      -4.615 -41.508  81.167  1.00 96.37           C  
ANISOU 7934  CB  LYS B 475    12660  11764  12190   -792   -377   -560       C  
ATOM   7935  CG  LYS B 475      -4.413 -42.968  81.485  1.00102.21           C  
ANISOU 7935  CG  LYS B 475    13414  12290  13130   -743   -226   -673       C  
ATOM   7936  CD  LYS B 475      -5.121 -43.826  80.447  1.00109.17           C  
ANISOU 7936  CD  LYS B 475    14337  13234  13909   -871    -39   -929       C  
ATOM   7937  CE  LYS B 475      -5.253 -45.285  80.879  1.00116.70           C  
ANISOU 7937  CE  LYS B 475    15344  13941  15054   -839    121  -1056       C  
ATOM   7938  NZ  LYS B 475      -6.474 -45.928  80.304  1.00121.27           N  
ANISOU 7938  NZ  LYS B 475    16022  14586  15466  -1010    209  -1270       N  
ATOM   7939  N   ALA B 476      -4.972 -38.338  81.843  1.00 93.76           N  
ANISOU 7939  N   ALA B 476    12370  11624  11630   -802   -717   -174       N  
ATOM   7940  CA  ALA B 476      -4.995 -36.964  81.295  1.00100.84           C  
ANISOU 7940  CA  ALA B 476    13227  12682  12404   -835   -773    -57       C  
ATOM   7941  C   ALA B 476      -3.772 -36.091  81.632  1.00108.51           C  
ANISOU 7941  C   ALA B 476    14178  13624  13425   -808   -851     82       C  
ATOM   7942  O   ALA B 476      -3.177 -36.246  82.713  1.00117.95           O  
ANISOU 7942  O   ALA B 476    15434  14658  14723   -782   -914    151       O  
ATOM   7943  CB  ALA B 476      -6.267 -36.232  81.726  1.00 99.89           C  
ANISOU 7943  CB  ALA B 476    13183  12557  12212   -850   -814     33       C  
ATOM   7944  N   THR B 477      -3.431 -35.181  80.698  1.00113.44           N  
ANISOU 7944  N   THR B 477    14713  14423  13963   -839   -854    142       N  
ATOM   7945  CA  THR B 477      -2.226 -34.313  80.761  1.00112.22           C  
ANISOU 7945  CA  THR B 477    14518  14282  13837   -836   -920    272       C  
ATOM   7946  C   THR B 477      -2.551 -32.891  80.223  1.00115.77           C  
ANISOU 7946  C   THR B 477    14949  14860  14176   -875   -948    391       C  
ATOM   7947  O   THR B 477      -3.354 -32.810  79.308  1.00109.97           O  
ANISOU 7947  O   THR B 477    14147  14288  13348   -905   -900    367       O  
ATOM   7948  CB  THR B 477      -1.104 -34.891  79.867  1.00112.17           C  
ANISOU 7948  CB  THR B 477    14364  14369  13884   -820   -847    212       C  
ATOM   7949  OG1 THR B 477      -1.107 -36.329  79.913  1.00111.88           O  
ANISOU 7949  OG1 THR B 477    14318  14238  13952   -782   -738     66       O  
ATOM   7950  CG2 THR B 477       0.275 -34.335  80.288  1.00113.89           C  
ANISOU 7950  CG2 THR B 477    14532  14552  14188   -806   -931    370       C  
ATOM   7951  N   PRO B 478      -1.924 -31.780  80.746  1.00121.57           N  
ANISOU 7951  N   PRO B 478    15735  15533  14923   -895  -1020    535       N  
ATOM   7952  CA  PRO B 478      -2.163 -30.464  80.117  1.00125.50           C  
ANISOU 7952  CA  PRO B 478    16195  16139  15349   -921  -1014    656       C  
ATOM   7953  C   PRO B 478      -1.270 -30.249  78.881  1.00133.56           C  
ANISOU 7953  C   PRO B 478    17042  17376  16329   -939  -1011    676       C  
ATOM   7954  O   PRO B 478      -0.333 -31.015  78.658  1.00140.05           O  
ANISOU 7954  O   PRO B 478    17789  18226  17195   -926  -1003    605       O  
ATOM   7955  CB  PRO B 478      -1.830 -29.446  81.244  1.00122.15           C  
ANISOU 7955  CB  PRO B 478    15932  15524  14952   -963  -1061    770       C  
ATOM   7956  CG  PRO B 478      -1.361 -30.244  82.411  1.00121.07           C  
ANISOU 7956  CG  PRO B 478    15902  15230  14869   -984  -1123    721       C  
ATOM   7957  CD  PRO B 478      -1.021 -31.615  81.895  1.00120.46           C  
ANISOU 7957  CD  PRO B 478    15687  15234  14845   -924  -1108    611       C  
ATOM   7958  N   PRO B 479      -1.532 -29.197  78.089  1.00140.73           N  
ANISOU 7958  N   PRO B 479    17873  18427  17169   -965  -1001    794       N  
ATOM   7959  CA  PRO B 479      -0.742 -28.985  76.874  1.00142.07           C  
ANISOU 7959  CA  PRO B 479    17876  18822  17279   -997   -995    815       C  
ATOM   7960  C   PRO B 479       0.596 -28.309  77.207  1.00132.55           C  
ANISOU 7960  C   PRO B 479    16672  17558  16131  -1005  -1059    911       C  
ATOM   7961  O   PRO B 479       1.630 -28.719  76.708  1.00126.41           O  
ANISOU 7961  O   PRO B 479    15788  16872  15370  -1004  -1053    878       O  
ATOM   7962  CB  PRO B 479      -1.636 -28.062  76.035  1.00149.16           C  
ANISOU 7962  CB  PRO B 479    18686  19892  18094  -1032   -975    955       C  
ATOM   7963  CG  PRO B 479      -2.516 -27.363  77.034  1.00150.80           C  
ANISOU 7963  CG  PRO B 479    19030  19889  18379   -993   -964   1063       C  
ATOM   7964  CD  PRO B 479      -2.440 -28.068  78.357  1.00145.49           C  
ANISOU 7964  CD  PRO B 479    18537  18964  17778   -963   -978    942       C  
ATOM   7965  N   SER B 485       4.559 -30.425  82.371  1.00227.70           N  
ANISOU 7965  N   SER B 485    28941  28971  28602  -1126  -1459   1154       N  
ATOM   7966  CA  SER B 485       5.318 -31.638  82.066  1.00226.31           C  
ANISOU 7966  CA  SER B 485    28565  28826  28595  -1023  -1411   1170       C  
ATOM   7967  C   SER B 485       4.598 -32.932  82.560  1.00228.09           C  
ANISOU 7967  C   SER B 485    28832  28920  28908   -943  -1344   1054       C  
ATOM   7968  O   SER B 485       3.776 -32.888  83.498  1.00224.62           O  
ANISOU 7968  O   SER B 485    28575  28365  28402  -1000  -1398   1022       O  
ATOM   7969  CB  SER B 485       6.720 -31.497  82.678  1.00216.69           C  
ANISOU 7969  CB  SER B 485    27239  27632  27461  -1108  -1550   1419       C  
ATOM   7970  OG  SER B 485       7.552 -32.609  82.417  1.00213.20           O  
ANISOU 7970  OG  SER B 485    26571  27200  27236   -992  -1478   1493       O  
ATOM   7971  N   PRO B 486       4.893 -34.090  81.930  1.00225.45           N  
ANISOU 7971  N   PRO B 486    28341  28588  28730   -818  -1201    983       N  
ATOM   7972  CA  PRO B 486       4.473 -35.377  82.521  1.00216.33           C  
ANISOU 7972  CA  PRO B 486    27204  27283  27707   -749  -1139    920       C  
ATOM   7973  C   PRO B 486       5.276 -35.707  83.785  1.00204.98           C  
ANISOU 7973  C   PRO B 486    25719  25759  26405   -792  -1281   1165       C  
ATOM   7974  O   PRO B 486       4.757 -36.334  84.701  1.00189.27           O  
ANISOU 7974  O   PRO B 486    23815  23647  24451   -801  -1317   1165       O  
ATOM   7975  CB  PRO B 486       4.709 -36.394  81.396  1.00219.56           C  
ANISOU 7975  CB  PRO B 486    27464  27705  28253   -625   -904    779       C  
ATOM   7976  CG  PRO B 486       5.603 -35.725  80.403  1.00221.67           C  
ANISOU 7976  CG  PRO B 486    27594  28131  28499   -627   -867    834       C  
ATOM   7977  CD  PRO B 486       5.702 -34.260  80.709  1.00221.79           C  
ANISOU 7977  CD  PRO B 486    27683  28242  28343   -745  -1067    968       C  
ATOM   7978  N   ASP B 487       6.502 -35.191  83.843  1.00202.23           N  
ANISOU 7978  N   ASP B 487    25233  25499  26106   -846  -1380   1394       N  
ATOM   7979  CA  ASP B 487       7.405 -35.333  84.995  1.00198.15           C  
ANISOU 7979  CA  ASP B 487    24634  24964  25687   -943  -1557   1698       C  
ATOM   7980  C   ASP B 487       7.002 -34.440  86.193  1.00186.33           C  
ANISOU 7980  C   ASP B 487    23379  23456  23961  -1172  -1769   1760       C  
ATOM   7981  O   ASP B 487       7.534 -34.602  87.302  1.00196.14           O  
ANISOU 7981  O   ASP B 487    24602  24695  25226  -1311  -1936   1996       O  
ATOM   7982  CB  ASP B 487       8.831 -34.935  84.568  1.00200.14           C  
ANISOU 7982  CB  ASP B 487    24654  25348  26040   -957  -1600   1939       C  
ATOM   7983  CG  ASP B 487       9.242 -35.571  83.246  1.00199.23           C  
ANISOU 7983  CG  ASP B 487    24335  25248  26113   -753  -1346   1845       C  
ATOM   7984  OD1 ASP B 487       9.462 -36.785  83.274  1.00196.06           O  
ANISOU 7984  OD1 ASP B 487    23792  24734  25968   -614  -1199   1881       O  
ATOM   7985  OD2 ASP B 487       9.297 -34.888  82.188  1.00195.85           O  
ANISOU 7985  OD2 ASP B 487    23902  24931  25579   -741  -1272   1727       O  
ATOM   7986  N   SER B 488       6.084 -33.503  85.952  1.00162.88           N  
ANISOU 7986  N   SER B 488    20628  20482  20778  -1224  -1746   1565       N  
ATOM   7987  CA  SER B 488       5.818 -32.372  86.842  1.00146.51           C  
ANISOU 7987  CA  SER B 488    18798  18385  18482  -1451  -1879   1599       C  
ATOM   7988  C   SER B 488       5.295 -32.781  88.228  1.00143.18           C  
ANISOU 7988  C   SER B 488    18552  17847  18002  -1576  -1964   1625       C  
ATOM   7989  O   SER B 488       4.496 -33.734  88.312  1.00155.05           O  
ANISOU 7989  O   SER B 488    20068  19256  19588  -1444  -1874   1503       O  
ATOM   7990  CB  SER B 488       4.802 -31.458  86.171  1.00139.48           C  
ANISOU 7990  CB  SER B 488    18070  17475  17450  -1418  -1764   1388       C  
ATOM   7991  OG  SER B 488       4.533 -30.309  86.917  1.00138.73           O  
ANISOU 7991  OG  SER B 488    18221  17317  17172  -1619  -1823   1402       O  
ATOM   7992  N   PRO B 489       5.703 -32.062  89.316  1.00131.40           N  
ANISOU 7992  N   PRO B 489    17214  16365  16347  -1856  -2130   1774       N  
ATOM   7993  CA  PRO B 489       5.151 -32.364  90.654  1.00124.22           C  
ANISOU 7993  CA  PRO B 489    16506  15357  15335  -2018  -2202   1784       C  
ATOM   7994  C   PRO B 489       3.630 -32.186  90.797  1.00117.94           C  
ANISOU 7994  C   PRO B 489    15972  14400  14439  -1962  -2047   1514       C  
ATOM   7995  O   PRO B 489       3.017 -32.862  91.602  1.00114.50           O  
ANISOU 7995  O   PRO B 489    15630  13875  13997  -1981  -2051   1484       O  
ATOM   7996  CB  PRO B 489       5.870 -31.377  91.584  1.00127.06           C  
ANISOU 7996  CB  PRO B 489    17020  15779  15478  -2382  -2378   1954       C  
ATOM   7997  CG  PRO B 489       7.022 -30.864  90.806  1.00129.85           C  
ANISOU 7997  CG  PRO B 489    17167  16282  15886  -2386  -2440   2107       C  
ATOM   7998  CD  PRO B 489       6.613 -30.904  89.370  1.00129.55           C  
ANISOU 7998  CD  PRO B 489    17005  16232  15983  -2072  -2248   1919       C  
ATOM   7999  N   GLU B 490       3.049 -31.280  90.023  1.00118.84           N  
ANISOU 7999  N   GLU B 490    16177  14484  14491  -1893  -1913   1354       N  
ATOM   8000  CA  GLU B 490       1.607 -31.023  90.014  1.00114.71           C  
ANISOU 8000  CA  GLU B 490    15852  13820  13911  -1817  -1745   1145       C  
ATOM   8001  C   GLU B 490       0.922 -32.201  89.392  1.00106.60           C  
ANISOU 8001  C   GLU B 490    14673  12792  13038  -1566  -1656   1035       C  
ATOM   8002  O   GLU B 490      -0.083 -32.668  89.907  1.00106.36           O  
ANISOU 8002  O   GLU B 490    14762  12650  12998  -1534  -1593    936       O  
ATOM   8003  CB  GLU B 490       1.265 -29.747  89.225  1.00118.26           C  
ANISOU 8003  CB  GLU B 490    16373  14260  14301  -1793  -1623   1071       C  
ATOM   8004  CG  GLU B 490       1.924 -28.494  89.802  1.00127.05           C  
ANISOU 8004  CG  GLU B 490    17668  15345  15259  -2062  -1676   1155       C  
ATOM   8005  CD  GLU B 490       3.456 -28.566  89.741  1.00135.86           C  
ANISOU 8005  CD  GLU B 490    18603  16631  16386  -2178  -1872   1355       C  
ATOM   8006  OE1 GLU B 490       3.998 -29.563  89.197  1.00153.20           O  
ANISOU 8006  OE1 GLU B 490    20520  18947  18741  -2015  -1932   1430       O  
ATOM   8007  OE2 GLU B 490       4.121 -27.649  90.241  1.00136.38           O  
ANISOU 8007  OE2 GLU B 490    18802  16705  16312  -2438  -1949   1445       O  
ATOM   8008  N   MET B 491       1.447 -32.658  88.266  1.00101.77           N  
ANISOU 8008  N   MET B 491    13811  12298  12556  -1407  -1631   1041       N  
ATOM   8009  CA  MET B 491       0.901 -33.850  87.608  1.00103.24           C  
ANISOU 8009  CA  MET B 491    13862  12483  12879  -1206  -1525    919       C  
ATOM   8010  C   MET B 491       0.994 -35.097  88.494  1.00 95.77           C  
ANISOU 8010  C   MET B 491    12886  11454  12047  -1198  -1575    976       C  
ATOM   8011  O   MET B 491       0.064 -35.885  88.566  1.00 90.59           O  
ANISOU 8011  O   MET B 491    12269  10717  11434  -1109  -1493    849       O  
ATOM   8012  CB  MET B 491       1.580 -34.056  86.263  1.00112.35           C  
ANISOU 8012  CB  MET B 491    14782  13772  14133  -1082  -1461    908       C  
ATOM   8013  CG  MET B 491       0.891 -33.317  85.096  1.00117.60           C  
ANISOU 8013  CG  MET B 491    15449  14524  14706  -1025  -1353    782       C  
ATOM   8014  SD  MET B 491      -0.937 -33.486  84.906  1.00113.99           S  
ANISOU 8014  SD  MET B 491    15115  14014  14182   -962  -1230    601       S  
ATOM   8015  CE  MET B 491      -1.507 -32.112  85.932  1.00114.81           C  
ANISOU 8015  CE  MET B 491    15472  13990  14161  -1088  -1256    668       C  
ATOM   8016  N   LYS B 492       2.126 -35.216  89.178  1.00 94.58           N  
ANISOU 8016  N   LYS B 492    12656  11337  11942  -1308  -1720   1196       N  
ATOM   8017  CA  LYS B 492       2.361 -36.289  90.145  1.00 94.44           C  
ANISOU 8017  CA  LYS B 492    12584  11259  12038  -1333  -1797   1332       C  
ATOM   8018  C   LYS B 492       1.294 -36.258  91.240  1.00 95.28           C  
ANISOU 8018  C   LYS B 492    12949  11250  12000  -1445  -1818   1253       C  
ATOM   8019  O   LYS B 492       0.737 -37.302  91.606  1.00 89.28           O  
ANISOU 8019  O   LYS B 492    12178  10402  11339  -1364  -1779   1215       O  
ATOM   8020  CB  LYS B 492       3.751 -36.160  90.751  1.00 93.29           C  
ANISOU 8020  CB  LYS B 492    12306  11211  11927  -1489  -1982   1645       C  
ATOM   8021  CG  LYS B 492       4.396 -37.379  91.375  1.00 94.33           C  
ANISOU 8021  CG  LYS B 492    12233  11330  12277  -1462  -2053   1888       C  
ATOM   8022  CD  LYS B 492       5.839 -37.046  91.726  1.00 96.41           C  
ANISOU 8022  CD  LYS B 492    12316  11742  12571  -1622  -2239   2239       C  
ATOM   8023  CE  LYS B 492       6.667 -38.305  92.017  1.00 99.06           C  
ANISOU 8023  CE  LYS B 492    12336  12078  13222  -1526  -2266   2547       C  
ATOM   8024  NZ  LYS B 492       6.607 -38.600  93.472  1.00100.65           N  
ANISOU 8024  NZ  LYS B 492    12609  12293  13339  -1752  -2461   2765       N  
ATOM   8025  N   ASP B 493       1.063 -35.045  91.758  1.00 97.42           N  
ANISOU 8025  N   ASP B 493    13457  11511  12047  -1639  -1858   1233       N  
ATOM   8026  CA  ASP B 493       0.023 -34.809  92.757  1.00 99.53           C  
ANISOU 8026  CA  ASP B 493    14006  11653  12159  -1761  -1828   1137       C  
ATOM   8027  C   ASP B 493      -1.337 -35.171  92.212  1.00 93.67           C  
ANISOU 8027  C   ASP B 493    13302  10818  11468  -1557  -1650    917       C  
ATOM   8028  O   ASP B 493      -2.171 -35.752  92.914  1.00 91.91           O  
ANISOU 8028  O   ASP B 493    13189  10495  11238  -1557  -1618    860       O  
ATOM   8029  CB  ASP B 493      -0.022 -33.341  93.182  1.00107.92           C  
ANISOU 8029  CB  ASP B 493    15327  12683  12994  -1985  -1819   1113       C  
ATOM   8030  CG  ASP B 493       1.158 -32.927  94.019  1.00123.04           C  
ANISOU 8030  CG  ASP B 493    17398  14614  14735  -2320  -1980   1270       C  
ATOM   8031  OD1 ASP B 493       1.870 -33.852  94.515  1.00136.87           O  
ANISOU 8031  OD1 ASP B 493    19261  16301  16441  -2405  -2008   1278       O  
ATOM   8032  OD2 ASP B 493       1.369 -31.682  94.190  1.00139.12           O  
ANISOU 8032  OD2 ASP B 493    19451  16742  16664  -2522  -2084   1393       O  
ATOM   8033  N   PHE B 494      -1.576 -34.775  90.970  1.00 88.02           N  
ANISOU 8033  N   PHE B 494    12497  10155  10789  -1409  -1541    813       N  
ATOM   8034  CA  PHE B 494      -2.842 -35.030  90.301  1.00 82.74           C  
ANISOU 8034  CA  PHE B 494    11832   9450  10153  -1247  -1388    641       C  
ATOM   8035  C   PHE B 494      -3.048 -36.524  90.122  1.00 81.16           C  
ANISOU 8035  C   PHE B 494    11493   9238  10106  -1115  -1366    589       C  
ATOM   8036  O   PHE B 494      -4.107 -37.049  90.424  1.00 77.70           O  
ANISOU 8036  O   PHE B 494    11133   8717   9672  -1072  -1302    496       O  
ATOM   8037  CB  PHE B 494      -2.833 -34.328  88.958  1.00 81.21           C  
ANISOU 8037  CB  PHE B 494    11530   9369   9956  -1158  -1312    595       C  
ATOM   8038  CG  PHE B 494      -3.935 -34.734  88.033  1.00 78.35           C  
ANISOU 8038  CG  PHE B 494    11096   9044   9628  -1015  -1187    461       C  
ATOM   8039  CD1 PHE B 494      -5.192 -34.180  88.151  1.00 77.32           C  
ANISOU 8039  CD1 PHE B 494    11089   8850   9437  -1005  -1088    419       C  
ATOM   8040  CD2 PHE B 494      -3.713 -35.668  87.032  1.00 77.28           C  
ANISOU 8040  CD2 PHE B 494    10768   9010   9585   -911  -1152    391       C  
ATOM   8041  CE1 PHE B 494      -6.217 -34.531  87.274  1.00 75.07           C  
ANISOU 8041  CE1 PHE B 494    10711   8640   9171   -905   -997    341       C  
ATOM   8042  CE2 PHE B 494      -4.729 -36.035  86.173  1.00 76.45           C  
ANISOU 8042  CE2 PHE B 494    10610   8969   9467   -840  -1049    270       C  
ATOM   8043  CZ  PHE B 494      -5.991 -35.471  86.302  1.00 74.84           C  
ANISOU 8043  CZ  PHE B 494    10505   8738   9190   -844   -993    262       C  
ATOM   8044  N   ARG B 495      -2.026 -37.206  89.648  1.00 83.39           N  
ANISOU 8044  N   ARG B 495    11568   9586  10528  -1053  -1400    658       N  
ATOM   8045  CA  ARG B 495      -2.098 -38.638  89.467  1.00 87.67           C  
ANISOU 8045  CA  ARG B 495    11981  10080  11249   -931  -1337    612       C  
ATOM   8046  C   ARG B 495      -2.256 -39.353  90.806  1.00 87.43           C  
ANISOU 8046  C   ARG B 495    12026   9934  11259   -994  -1416    707       C  
ATOM   8047  O   ARG B 495      -2.965 -40.338  90.890  1.00 83.79           O  
ANISOU 8047  O   ARG B 495    11563   9386  10884   -914  -1342    616       O  
ATOM   8048  CB  ARG B 495      -0.873 -39.158  88.719  1.00 96.66           C  
ANISOU 8048  CB  ARG B 495    12881  11280  12565   -847  -1309    690       C  
ATOM   8049  CG  ARG B 495      -0.839 -38.705  87.255  1.00104.50           C  
ANISOU 8049  CG  ARG B 495    13791  12392  13518   -779  -1197    559       C  
ATOM   8050  CD  ARG B 495       0.121 -39.511  86.381  1.00113.59           C  
ANISOU 8050  CD  ARG B 495    14723  13567  14868   -671  -1082    565       C  
ATOM   8051  NE  ARG B 495       1.506 -39.139  86.687  1.00122.35           N  
ANISOU 8051  NE  ARG B 495    15702  14724  16059   -706  -1191    810       N  
ATOM   8052  CZ  ARG B 495       2.232 -38.264  85.997  1.00128.13           C  
ANISOU 8052  CZ  ARG B 495    16358  15588  16735   -729  -1211    862       C  
ATOM   8053  NH1 ARG B 495       1.739 -37.605  84.951  1.00131.65           N  
ANISOU 8053  NH1 ARG B 495    16843  16137  17038   -721  -1135    697       N  
ATOM   8054  NH2 ARG B 495       3.473 -38.022  86.395  1.00134.23           N  
ANISOU 8054  NH2 ARG B 495    17003  16405  17593   -777  -1325   1114       N  
ATOM   8055  N   HIS B 496      -1.555 -38.889  91.833  1.00 89.48           N  
ANISOU 8055  N   HIS B 496    12342  10206  11447  -1160  -1572    901       N  
ATOM   8056  CA  HIS B 496      -1.623 -39.517  93.143  1.00 91.43           C  
ANISOU 8056  CA  HIS B 496    12654  10380  11704  -1263  -1671   1028       C  
ATOM   8057  C   HIS B 496      -3.035 -39.454  93.707  1.00 86.03           C  
ANISOU 8057  C   HIS B 496    12204   9592  10892  -1291  -1604    868       C  
ATOM   8058  O   HIS B 496      -3.548 -40.449  94.254  1.00 84.70           O  
ANISOU 8058  O   HIS B 496    12038   9338  10805  -1254  -1592    864       O  
ATOM   8059  CB  HIS B 496      -0.614 -38.888  94.114  1.00 96.71           C  
ANISOU 8059  CB  HIS B 496    13360  11128  12257  -1507  -1867   1275       C  
ATOM   8060  CG  HIS B 496      -0.486 -39.637  95.409  1.00103.31           C  
ANISOU 8060  CG  HIS B 496    14205  11936  13109  -1640  -1996   1467       C  
ATOM   8061  ND1 HIS B 496       0.053 -40.916  95.494  1.00106.94           N  
ANISOU 8061  ND1 HIS B 496    14414  12380  13835  -1527  -2020   1649       N  
ATOM   8062  CD2 HIS B 496      -0.870 -39.307  96.663  1.00106.03           C  
ANISOU 8062  CD2 HIS B 496    14783  12262  13240  -1881  -2087   1510       C  
ATOM   8063  CE1 HIS B 496      -0.002 -41.333  96.742  1.00110.61           C  
ANISOU 8063  CE1 HIS B 496    14936  12838  14251  -1691  -2148   1821       C  
ATOM   8064  NE2 HIS B 496      -0.525 -40.363  97.477  1.00112.97           N  
ANISOU 8064  NE2 HIS B 496    15534  13148  14239  -1925  -2200   1736       N  
ATOM   8065  N   GLY B 497      -3.661 -38.293  93.589  1.00 81.54           N  
ANISOU 8065  N   GLY B 497    11819   9018  10143  -1350  -1544    754       N  
ATOM   8066  CA  GLY B 497      -5.035 -38.141  94.046  1.00 77.87           C  
ANISOU 8066  CA  GLY B 497    11558   8443   9583  -1356  -1440    619       C  
ATOM   8067  C   GLY B 497      -5.969 -39.228  93.541  1.00 74.38           C  
ANISOU 8067  C   GLY B 497    11026   7959   9274  -1175  -1339    493       C  
ATOM   8068  O   GLY B 497      -6.858 -39.661  94.280  1.00 71.66           O  
ANISOU 8068  O   GLY B 497    10798   7519   8909  -1192  -1307    454       O  
ATOM   8069  N   PHE B 498      -5.804 -39.598  92.262  1.00 73.23           N  
ANISOU 8069  N   PHE B 498    10691   7888   9242  -1027  -1275    418       N  
ATOM   8070  CA  PHE B 498      -6.601 -40.664  91.635  1.00 72.36           C  
ANISOU 8070  CA  PHE B 498    10497   7755   9240   -896  -1170    281       C  
ATOM   8071  C   PHE B 498      -6.216 -42.040  92.094  1.00 74.50           C  
ANISOU 8071  C   PHE B 498    10674   7942   9688   -857  -1191    333       C  
ATOM   8072  O   PHE B 498      -7.076 -42.877  92.211  1.00 72.34           O  
ANISOU 8072  O   PHE B 498    10424   7593   9466   -812  -1126    243       O  
ATOM   8073  CB  PHE B 498      -6.589 -40.595  90.105  1.00 70.82           C  
ANISOU 8073  CB  PHE B 498    10162   7678   9066   -806  -1076    167       C  
ATOM   8074  CG  PHE B 498      -7.505 -39.541  89.561  1.00 68.51           C  
ANISOU 8074  CG  PHE B 498     9936   7460   8632   -815  -1018    111       C  
ATOM   8075  CD1 PHE B 498      -8.848 -39.698  89.602  1.00 67.61           C  
ANISOU 8075  CD1 PHE B 498     9886   7320   8481   -797   -948     42       C  
ATOM   8076  CD2 PHE B 498      -7.008 -38.384  89.048  1.00 68.49           C  
ANISOU 8076  CD2 PHE B 498     9917   7551   8555   -840  -1033    164       C  
ATOM   8077  CE1 PHE B 498      -9.697 -38.702  89.163  1.00 67.58           C  
ANISOU 8077  CE1 PHE B 498     9910   7380   8385   -796   -886     55       C  
ATOM   8078  CE2 PHE B 498      -7.851 -37.407  88.574  1.00 68.24           C  
ANISOU 8078  CE2 PHE B 498     9921   7573   8431   -837   -966    158       C  
ATOM   8079  CZ  PHE B 498      -9.199 -37.557  88.628  1.00 67.56           C  
ANISOU 8079  CZ  PHE B 498     9880   7461   8328   -810   -889    119       C  
ATOM   8080  N   ASP B 499      -4.917 -42.256  92.322  1.00 79.29           N  
ANISOU 8080  N   ASP B 499    11156   8564  10403   -875  -1276    501       N  
ATOM   8081  CA  ASP B 499      -4.384 -43.516  92.859  1.00 82.61           C  
ANISOU 8081  CA  ASP B 499    11450   8895  11040   -834  -1295    632       C  
ATOM   8082  C   ASP B 499      -5.119 -43.843  94.122  1.00 78.93           C  
ANISOU 8082  C   ASP B 499    11130   8344  10515   -920  -1362    679       C  
ATOM   8083  O   ASP B 499      -5.427 -45.032  94.372  1.00 79.75           O  
ANISOU 8083  O   ASP B 499    11176   8340  10783   -849  -1310    679       O  
ATOM   8084  CB  ASP B 499      -2.859 -43.427  93.183  1.00 90.48           C  
ANISOU 8084  CB  ASP B 499    12286   9949  12141   -883  -1418    904       C  
ATOM   8085  CG  ASP B 499      -1.957 -43.728  91.978  1.00 99.36           C  
ANISOU 8085  CG  ASP B 499    13188  11104  13457   -744  -1302    897       C  
ATOM   8086  OD1 ASP B 499      -2.152 -44.815  91.337  1.00109.41           O  
ANISOU 8086  OD1 ASP B 499    14365  12275  14929   -601  -1120    777       O  
ATOM   8087  OD2 ASP B 499      -1.072 -42.863  91.665  1.00100.34           O  
ANISOU 8087  OD2 ASP B 499    13251  11348  13526   -792  -1372    998       O  
ATOM   8088  N   ILE B 500      -5.325 -42.799  94.928  1.00 74.28           N  
ANISOU 8088  N   ILE B 500    10731   7790   9699  -1084  -1460    725       N  
ATOM   8089  CA  ILE B 500      -5.961 -42.924  96.239  1.00 72.43           C  
ANISOU 8089  CA  ILE B 500    10673   7488   9359  -1213  -1520    776       C  
ATOM   8090  C   ILE B 500      -7.382 -43.369  96.050  1.00 70.30           C  
ANISOU 8090  C   ILE B 500    10488   7129   9093  -1114  -1384    579       C  
ATOM   8091  O   ILE B 500      -7.837 -44.373  96.661  1.00 69.67           O  
ANISOU 8091  O   ILE B 500    10407   6962   9102  -1097  -1383    602       O  
ATOM   8092  CB  ILE B 500      -5.824 -41.587  97.028  1.00 71.99           C  
ANISOU 8092  CB  ILE B 500    10837   7476   9037  -1441  -1602    830       C  
ATOM   8093  CG1 ILE B 500      -4.383 -41.437  97.553  1.00 73.81           C  
ANISOU 8093  CG1 ILE B 500    10973   7811   9257  -1607  -1789   1093       C  
ATOM   8094  CG2 ILE B 500      -6.749 -41.513  98.207  1.00 71.71           C  
ANISOU 8094  CG2 ILE B 500    11043   7358   8846  -1580  -1590    803       C  
ATOM   8095  CD1 ILE B 500      -4.025 -40.041  98.020  1.00 75.07           C  
ANISOU 8095  CD1 ILE B 500    11334   8034   9153  -1853  -1855   1123       C  
ATOM   8096  N   LEU B 501      -8.048 -42.622  95.166  1.00 69.15           N  
ANISOU 8096  N   LEU B 501    10391   7019   8862  -1053  -1276    413       N  
ATOM   8097  CA  LEU B 501      -9.463 -42.827  94.806  1.00 67.62           C  
ANISOU 8097  CA  LEU B 501    10255   6784   8652   -972  -1148    250       C  
ATOM   8098  C   LEU B 501      -9.810 -44.189  94.191  1.00 67.29           C  
ANISOU 8098  C   LEU B 501    10075   6709   8784   -854  -1077    156       C  
ATOM   8099  O   LEU B 501     -10.815 -44.801  94.559  1.00 65.14           O  
ANISOU 8099  O   LEU B 501     9861   6364   8525   -842  -1031     99       O  
ATOM   8100  CB  LEU B 501      -9.910 -41.718  93.872  1.00 65.94           C  
ANISOU 8100  CB  LEU B 501    10061   6654   8339   -940  -1064    163       C  
ATOM   8101  CG  LEU B 501     -11.419 -41.621  93.692  1.00 64.93           C  
ANISOU 8101  CG  LEU B 501     9996   6504   8168   -895   -946     72       C  
ATOM   8102  CD1 LEU B 501     -12.018 -41.000  94.897  1.00 64.89           C  
ANISOU 8102  CD1 LEU B 501    10206   6389   8057   -983   -915    119       C  
ATOM   8103  CD2 LEU B 501     -11.770 -40.785  92.486  1.00 65.23           C  
ANISOU 8103  CD2 LEU B 501     9960   6663   8162   -843   -871     31       C  
ATOM   8104  N   VAL B 502      -8.945 -44.648  93.295  1.00 69.29           N  
ANISOU 8104  N   VAL B 502    10156   7000   9169   -782  -1051    139       N  
ATOM   8105  CA  VAL B 502      -9.067 -45.976  92.699  1.00 72.08           C  
ANISOU 8105  CA  VAL B 502    10395   7288   9704   -695   -943     37       C  
ATOM   8106  C   VAL B 502      -8.971 -46.967  93.830  1.00 73.20           C  
ANISOU 8106  C   VAL B 502    10537   7290   9986   -699   -988    160       C  
ATOM   8107  O   VAL B 502      -9.840 -47.827  93.961  1.00 73.18           O  
ANISOU 8107  O   VAL B 502    10565   7199  10039   -677   -919     72       O  
ATOM   8108  CB  VAL B 502      -7.997 -46.289  91.631  1.00 73.53           C  
ANISOU 8108  CB  VAL B 502    10408   7504  10026   -625   -864      8       C  
ATOM   8109  CG1 VAL B 502      -8.154 -47.713  91.110  1.00 74.49           C  
ANISOU 8109  CG1 VAL B 502    10451   7506  10343   -558   -698   -119       C  
ATOM   8110  CG2 VAL B 502      -8.142 -45.360  90.427  1.00 74.81           C  
ANISOU 8110  CG2 VAL B 502    10561   7827  10035   -636   -819   -112       C  
ATOM   8111  N   GLY B 503      -7.956 -46.795  94.667  1.00 73.97           N  
ANISOU 8111  N   GLY B 503    10596   7385  10122   -751  -1116    383       N  
ATOM   8112  CA  GLY B 503      -7.726 -47.712  95.773  1.00 76.64           C  
ANISOU 8112  CA  GLY B 503    10897   7620  10599   -775  -1183    566       C  
ATOM   8113  C   GLY B 503      -8.834 -47.721  96.793  1.00 76.75           C  
ANISOU 8113  C   GLY B 503    11095   7590  10474   -861  -1226    549       C  
ATOM   8114  O   GLY B 503      -9.089 -48.729  97.431  1.00 79.91           O  
ANISOU 8114  O   GLY B 503    11470   7887  11002   -849  -1226    618       O  
ATOM   8115  N   GLN B 504      -9.519 -46.609  96.924  1.00 76.55           N  
ANISOU 8115  N   GLN B 504    11250   7628  10206   -941  -1237    462       N  
ATOM   8116  CA  GLN B 504     -10.754 -46.594  97.706  1.00 76.48           C  
ANISOU 8116  CA  GLN B 504    11419   7562  10077   -998  -1214    407       C  
ATOM   8117  C   GLN B 504     -11.961 -47.176  97.008  1.00 76.01           C  
ANISOU 8117  C   GLN B 504    11349   7460  10069   -893  -1077    218       C  
ATOM   8118  O   GLN B 504     -12.848 -47.706  97.667  1.00 77.60           O  
ANISOU 8118  O   GLN B 504    11628   7587  10269   -910  -1057    208       O  
ATOM   8119  CB  GLN B 504     -11.069 -45.168  98.103  1.00 77.13           C  
ANISOU 8119  CB  GLN B 504    11700   7692   9913  -1115  -1220    391       C  
ATOM   8120  CG  GLN B 504      -9.994 -44.594  99.016  1.00 80.55           C  
ANISOU 8120  CG  GLN B 504    12196   8172  10236  -1296  -1366    576       C  
ATOM   8121  CD  GLN B 504     -10.394 -43.288  99.626  1.00 81.58           C  
ANISOU 8121  CD  GLN B 504    12581   8298  10115  -1455  -1331    539       C  
ATOM   8122  OE1 GLN B 504     -11.557 -42.958  99.591  1.00 84.24           O  
ANISOU 8122  OE1 GLN B 504    13040   8570  10394  -1411  -1190    410       O  
ATOM   8123  NE2 GLN B 504      -9.449 -42.571 100.240  1.00 83.39           N  
ANISOU 8123  NE2 GLN B 504    12893   8588  10200  -1656  -1442    664       N  
ATOM   8124  N   ILE B 505     -12.051 -47.049  95.687  1.00 76.88           N  
ANISOU 8124  N   ILE B 505    11370   7637  10200   -812   -989     77       N  
ATOM   8125  CA  ILE B 505     -13.144 -47.692  94.928  1.00 76.14           C  
ANISOU 8125  CA  ILE B 505    11251   7538  10138   -762   -873    -89       C  
ATOM   8126  C   ILE B 505     -12.967 -49.192  94.990  1.00 77.72           C  
ANISOU 8126  C   ILE B 505    11365   7613  10551   -719   -827   -108       C  
ATOM   8127  O   ILE B 505     -13.924 -49.906  95.156  1.00 78.55           O  
ANISOU 8127  O   ILE B 505    11507   7656  10682   -725   -776   -175       O  
ATOM   8128  CB  ILE B 505     -13.182 -47.257  93.462  1.00 74.38           C  
ANISOU 8128  CB  ILE B 505    10947   7449   9865   -735   -799   -220       C  
ATOM   8129  CG1 ILE B 505     -13.661 -45.816  93.355  1.00 72.58           C  
ANISOU 8129  CG1 ILE B 505    10793   7329   9455   -763   -812   -189       C  
ATOM   8130  CG2 ILE B 505     -14.120 -48.155  92.646  1.00 74.43           C  
ANISOU 8130  CG2 ILE B 505    10910   7468   9899   -739   -693   -382       C  
ATOM   8131  CD1 ILE B 505     -13.350 -45.214  92.039  1.00 72.14           C  
ANISOU 8131  CD1 ILE B 505    10638   7424   9346   -750   -779   -250       C  
ATOM   8132  N   ASP B 506     -11.738 -49.663  94.889  1.00 81.01           N  
ANISOU 8132  N   ASP B 506    11661   7979  11141   -675   -830    -27       N  
ATOM   8133  CA  ASP B 506     -11.459 -51.106  95.035  1.00 85.91           C  
ANISOU 8133  CA  ASP B 506    12184   8433  12022   -617   -750     -3       C  
ATOM   8134  C   ASP B 506     -11.955 -51.715  96.355  1.00 85.05           C  
ANISOU 8134  C   ASP B 506    12136   8220  11958   -651   -821    127       C  
ATOM   8135  O   ASP B 506     -12.625 -52.817  96.409  1.00 85.74           O  
ANISOU 8135  O   ASP B 506    12223   8181  12172   -628   -728     53       O  
ATOM   8136  CB  ASP B 506      -9.978 -51.352  94.835  1.00 92.74           C  
ANISOU 8136  CB  ASP B 506    12884   9258  13094   -550   -735    134       C  
ATOM   8137  CG  ASP B 506      -9.497 -51.023  93.379  1.00 99.84           C  
ANISOU 8137  CG  ASP B 506    13712  10234  13987   -509   -611    -29       C  
ATOM   8138  OD1 ASP B 506     -10.343 -50.741  92.463  1.00 99.34           O  
ANISOU 8138  OD1 ASP B 506    13721  10261  13760   -548   -536   -255       O  
ATOM   8139  OD2 ASP B 506      -8.237 -51.051  93.190  1.00104.79           O  
ANISOU 8139  OD2 ASP B 506    14196  10843  14774   -449   -594    100       O  
ATOM   8140  N   ASP B 507     -11.670 -50.975  97.413  1.00 83.41           N  
ANISOU 8140  N   ASP B 507    11997   8071  11623   -732   -981    312       N  
ATOM   8141  CA  ASP B 507     -12.149 -51.333  98.737  1.00 83.90           C  
ANISOU 8141  CA  ASP B 507    12145   8075  11659   -807  -1065    445       C  
ATOM   8142  C   ASP B 507     -13.652 -51.393  98.810  1.00 76.43           C  
ANISOU 8142  C   ASP B 507    11336   7108  10595   -823   -997    285       C  
ATOM   8143  O   ASP B 507     -14.215 -52.307  99.408  1.00 76.42           O  
ANISOU 8143  O   ASP B 507    11346   7005  10682   -825   -983    315       O  
ATOM   8144  CB  ASP B 507     -11.622 -50.352  99.771  1.00 90.39           C  
ANISOU 8144  CB  ASP B 507    13060   8992  12290   -953  -1231    634       C  
ATOM   8145  CG  ASP B 507     -10.107 -50.518 100.031  1.00101.19           C  
ANISOU 8145  CG  ASP B 507    14258  10392  13799   -976  -1344    894       C  
ATOM   8146  OD1 ASP B 507      -9.565 -51.705 100.128  1.00107.17           O  
ANISOU 8146  OD1 ASP B 507    14825  11045  14847   -893  -1323   1047       O  
ATOM   8147  OD2 ASP B 507      -9.491 -49.407 100.192  1.00111.47           O  
ANISOU 8147  OD2 ASP B 507    15616  11818  14919  -1088  -1448    966       O  
ATOM   8148  N   ALA B 508     -14.282 -50.406  98.225  1.00 71.05           N  
ANISOU 8148  N   ALA B 508    10740   6527   9728   -833   -957    147       N  
ATOM   8149  CA  ALA B 508     -15.704 -50.298  98.252  1.00 69.70           C  
ANISOU 8149  CA  ALA B 508    10671   6361   9450   -846   -891     41       C  
ATOM   8150  C   ALA B 508     -16.316 -51.391  97.448  1.00 70.61           C  
ANISOU 8150  C   ALA B 508    10702   6429   9694   -796   -788   -100       C  
ATOM   8151  O   ALA B 508     -17.333 -51.917  97.798  1.00 69.36           O  
ANISOU 8151  O   ALA B 508    10591   6224   9537   -814   -756   -128       O  
ATOM   8152  CB  ALA B 508     -16.157 -48.955  97.713  1.00 68.51           C  
ANISOU 8152  CB  ALA B 508    10586   6328   9115   -856   -854    -22       C  
ATOM   8153  N   LEU B 509     -15.698 -51.715  96.335  1.00 74.00           N  
ANISOU 8153  N   LEU B 509    11019   6875  10222   -752   -723   -200       N  
ATOM   8154  CA  LEU B 509     -16.124 -52.839  95.528  1.00 78.24           C  
ANISOU 8154  CA  LEU B 509    11499   7349  10877   -748   -595   -362       C  
ATOM   8155  C   LEU B 509     -16.017 -54.170  96.251  1.00 83.54           C  
ANISOU 8155  C   LEU B 509    12145   7822  11772   -723   -562   -301       C  
ATOM   8156  O   LEU B 509     -16.901 -55.035  96.061  1.00 83.13           O  
ANISOU 8156  O   LEU B 509    12116   7704  11764   -757   -476   -415       O  
ATOM   8157  CB  LEU B 509     -15.297 -52.982  94.268  1.00 78.78           C  
ANISOU 8157  CB  LEU B 509    11471   7443  11017   -724   -495   -485       C  
ATOM   8158  CG  LEU B 509     -15.731 -52.090  93.124  1.00 78.24           C  
ANISOU 8158  CG  LEU B 509    11405   7579  10743   -779   -477   -611       C  
ATOM   8159  CD1 LEU B 509     -14.571 -51.652  92.254  1.00 79.05           C  
ANISOU 8159  CD1 LEU B 509    11426   7744  10863   -747   -443   -642       C  
ATOM   8160  CD2 LEU B 509     -16.699 -52.896  92.309  1.00 80.00           C  
ANISOU 8160  CD2 LEU B 509    11635   7822  10936   -874   -365   -798       C  
ATOM   8161  N   LYS B 510     -14.916 -54.367  97.004  1.00 89.79           N  
ANISOU 8161  N   LYS B 510    12871   8527  12715   -676   -625   -105       N  
ATOM   8162  CA  LYS B 510     -14.819 -55.616  97.771  1.00 95.59           C  
ANISOU 8162  CA  LYS B 510    13556   9073  13687   -648   -598     10       C  
ATOM   8163  C   LYS B 510     -15.971 -55.771  98.744  1.00 92.43           C  
ANISOU 8163  C   LYS B 510    13270   8663  13184   -711   -664     49       C  
ATOM   8164  O   LYS B 510     -16.461 -56.888  98.925  1.00 97.49           O  
ANISOU 8164  O   LYS B 510    13899   9162  13980   -704   -586     24       O  
ATOM   8165  CB  LYS B 510     -13.500 -55.771  98.511  1.00105.96           C  
ANISOU 8165  CB  LYS B 510    14747  10331  15181   -606   -682    291       C  
ATOM   8166  CG  LYS B 510     -12.308 -56.241  97.624  1.00119.26           C  
ANISOU 8166  CG  LYS B 510    16261  11923  17129   -501   -541    293       C  
ATOM   8167  CD  LYS B 510     -10.914 -55.894  98.218  1.00129.06           C  
ANISOU 8167  CD  LYS B 510    17356  13205  18475   -478   -670    614       C  
ATOM   8168  CE  LYS B 510      -9.913 -55.291  97.246  1.00132.41           C  
ANISOU 8168  CE  LYS B 510    17687  13702  18919   -425   -619    579       C  
ATOM   8169  NZ  LYS B 510      -8.962 -54.309  97.893  1.00132.56           N  
ANISOU 8169  NZ  LYS B 510    17653  13882  18828   -489   -836    846       N  
ATOM   8170  N   LEU B 511     -16.434 -54.685  99.346  1.00 85.56           N  
ANISOU 8170  N   LEU B 511    12517   7923  12065   -776   -776    100       N  
ATOM   8171  CA  LEU B 511     -17.631 -54.744 100.185  1.00 82.30           C  
ANISOU 8171  CA  LEU B 511    12223   7503  11542   -835   -800    116       C  
ATOM   8172  C   LEU B 511     -18.824 -55.115  99.395  1.00 80.55           C  
ANISOU 8172  C   LEU B 511    12017   7291  11298   -838   -690    -76       C  
ATOM   8173  O   LEU B 511     -19.668 -55.882  99.859  1.00 81.45           O  
ANISOU 8173  O   LEU B 511    12160   7328  11460   -862   -665    -75       O  
ATOM   8174  CB  LEU B 511     -17.915 -53.391 100.827  1.00 80.95           C  
ANISOU 8174  CB  LEU B 511    12194   7448  11112   -905   -874    174       C  
ATOM   8175  CG  LEU B 511     -16.839 -52.898 101.772  1.00 79.94           C  
ANISOU 8175  CG  LEU B 511    12095   7345  10931   -978  -1004    373       C  
ATOM   8176  CD1 LEU B 511     -17.111 -51.485 102.179  1.00 78.26           C  
ANISOU 8176  CD1 LEU B 511    12055   7226  10454  -1066  -1018    368       C  
ATOM   8177  CD2 LEU B 511     -16.809 -53.843 102.972  1.00 82.61           C  
ANISOU 8177  CD2 LEU B 511    12428   7594  11365  -1034  -1074    555       C  
ATOM   8178  N   ALA B 512     -18.948 -54.524  98.220  1.00 81.13           N  
ANISOU 8178  N   ALA B 512    12066   7482  11275   -836   -637   -222       N  
ATOM   8179  CA  ALA B 512     -20.105 -54.760  97.362  1.00 81.91           C  
ANISOU 8179  CA  ALA B 512    12163   7651  11308   -885   -556   -379       C  
ATOM   8180  C   ALA B 512     -20.164 -56.235  96.936  1.00 83.44           C  
ANISOU 8180  C   ALA B 512    12311   7702  11688   -910   -449   -499       C  
ATOM   8181  O   ALA B 512     -21.240 -56.826  96.945  1.00 81.25           O  
ANISOU 8181  O   ALA B 512    12062   7414  11396   -978   -413   -555       O  
ATOM   8182  CB  ALA B 512     -20.078 -53.814  96.158  1.00 81.44           C  
ANISOU 8182  CB  ALA B 512    12064   7773  11103   -903   -537   -472       C  
ATOM   8183  N   ASN B 513     -19.010 -56.805  96.591  1.00 86.37           N  
ANISOU 8183  N   ASN B 513    12615   7954  12247   -859   -380   -525       N  
ATOM   8184  CA  ASN B 513     -18.933 -58.202  96.176  1.00 92.14           C  
ANISOU 8184  CA  ASN B 513    13316   8496  13196   -876   -219   -647       C  
ATOM   8185  C   ASN B 513     -19.377 -59.100  97.306  1.00 93.97           C  
ANISOU 8185  C   ASN B 513    13567   8564  13571   -864   -237   -525       C  
ATOM   8186  O   ASN B 513     -20.047 -60.112  97.089  1.00 91.81           O  
ANISOU 8186  O   ASN B 513    13320   8180  13383   -929   -126   -643       O  
ATOM   8187  CB  ASN B 513     -17.498 -58.579  95.741  1.00 97.07           C  
ANISOU 8187  CB  ASN B 513    13847   8986  14049   -788   -107   -645       C  
ATOM   8188  CG  ASN B 513     -17.168 -58.125  94.323  1.00102.21           C  
ANISOU 8188  CG  ASN B 513    14487   9755  14591   -833     -9   -847       C  
ATOM   8189  OD1 ASN B 513     -17.890 -58.470  93.363  1.00110.11           O  
ANISOU 8189  OD1 ASN B 513    15542  10806  15489   -966    102  -1074       O  
ATOM   8190  ND2 ASN B 513     -16.066 -57.378  94.165  1.00101.51           N  
ANISOU 8190  ND2 ASN B 513    14328   9726  14514   -751    -51   -759       N  
ATOM   8191  N   GLU B 514     -18.924 -58.747  98.508  1.00 97.79           N  
ANISOU 8191  N   GLU B 514    14040   9035  14077   -803   -376   -284       N  
ATOM   8192  CA  GLU B 514     -19.242 -59.512  99.699  1.00104.49           C  
ANISOU 8192  CA  GLU B 514    14898   9754  15047   -801   -418   -122       C  
ATOM   8193  C   GLU B 514     -20.703 -59.395 100.059  1.00 98.51           C  
ANISOU 8193  C   GLU B 514    14244   9076  14109   -882   -456   -168       C  
ATOM   8194  O   GLU B 514     -21.240 -60.283 100.693  1.00101.24           O  
ANISOU 8194  O   GLU B 514    14602   9303  14562   -901   -439   -115       O  
ATOM   8195  CB  GLU B 514     -18.321 -59.136 100.898  1.00112.41           C  
ANISOU 8195  CB  GLU B 514    15863  10765  16083   -767   -572    170       C  
ATOM   8196  CG  GLU B 514     -16.817 -59.448 100.745  1.00122.36           C  
ANISOU 8196  CG  GLU B 514    16968  11931  17592   -680   -544    311       C  
ATOM   8197  CD  GLU B 514     -16.544 -60.887 100.204  1.00139.21           C  
ANISOU 8197  CD  GLU B 514    18997  13807  20085   -605   -327    251       C  
ATOM   8198  OE1 GLU B 514     -17.222 -61.901 100.611  1.00140.29           O  
ANISOU 8198  OE1 GLU B 514    19152  13793  20357   -621   -260    254       O  
ATOM   8199  OE2 GLU B 514     -15.641 -61.016  99.335  1.00151.67           O  
ANISOU 8199  OE2 GLU B 514    20484  15317  21826   -533   -191    191       O  
ATOM   8200  N   GLY B 515     -21.345 -58.316  99.649  1.00 93.02           N  
ANISOU 8200  N   GLY B 515    13606   8573  13163   -922   -494   -242       N  
ATOM   8201  CA  GLY B 515     -22.790 -58.150  99.843  1.00 90.55           C  
ANISOU 8201  CA  GLY B 515    13358   8346  12699   -988   -502   -265       C  
ATOM   8202  C   GLY B 515     -23.159 -57.043 100.802  1.00 86.27           C  
ANISOU 8202  C   GLY B 515    12902   7897  11979   -982   -586   -121       C  
ATOM   8203  O   GLY B 515     -24.347 -56.775 101.066  1.00 82.07           O  
ANISOU 8203  O   GLY B 515    12417   7428  11338  -1016   -570   -103       O  
ATOM   8204  N   LYS B 516     -22.123 -56.369 101.289  1.00 84.91           N  
ANISOU 8204  N   LYS B 516    12752   7733  11777   -951   -657    -17       N  
ATOM   8205  CA  LYS B 516     -22.287 -55.396 102.330  1.00 84.69           C  
ANISOU 8205  CA  LYS B 516    12843   7754  11579   -983   -711    107       C  
ATOM   8206  C   LYS B 516     -22.621 -54.074 101.678  1.00 77.61           C  
ANISOU 8206  C   LYS B 516    11979   6994  10512   -971   -668     43       C  
ATOM   8207  O   LYS B 516     -21.736 -53.265 101.445  1.00 76.73           O  
ANISOU 8207  O   LYS B 516    11874   6935  10344   -960   -701     51       O  
ATOM   8208  CB  LYS B 516     -21.008 -55.383 103.191  1.00 89.05           C  
ANISOU 8208  CB  LYS B 516    13404   8263  12168  -1008   -818    268       C  
ATOM   8209  CG  LYS B 516     -20.614 -56.763 103.773  1.00 92.92           C  
ANISOU 8209  CG  LYS B 516    13809   8613  12882  -1004   -855    388       C  
ATOM   8210  CD  LYS B 516     -19.139 -56.762 104.102  1.00 98.83           C  
ANISOU 8210  CD  LYS B 516    14475   9354  13720  -1008   -955    563       C  
ATOM   8211  CE  LYS B 516     -18.697 -57.902 104.976  1.00106.65           C  
ANISOU 8211  CE  LYS B 516    15372  10229  14918  -1021  -1012    784       C  
ATOM   8212  NZ  LYS B 516     -17.353 -57.526 105.540  1.00113.62           N  
ANISOU 8212  NZ  LYS B 516    16188  11181  15801  -1078  -1154   1028       N  
ATOM   8213  N   VAL B 517     -23.906 -53.877 101.407  1.00 74.52           N  
ANISOU 8213  N   VAL B 517    11593   6661  10060   -974   -592      8       N  
ATOM   8214  CA  VAL B 517     -24.384 -52.698 100.689  1.00 74.51           C  
ANISOU 8214  CA  VAL B 517    11577   6791   9941   -951   -531    -10       C  
ATOM   8215  C   VAL B 517     -24.230 -51.410 101.492  1.00 77.41           C  
ANISOU 8215  C   VAL B 517    12085   7146  10181   -950   -493     76       C  
ATOM   8216  O   VAL B 517     -23.694 -50.441 100.975  1.00 74.85           O  
ANISOU 8216  O   VAL B 517    11759   6886   9795   -928   -484     62       O  
ATOM   8217  CB  VAL B 517     -25.838 -52.843 100.230  1.00 73.13           C  
ANISOU 8217  CB  VAL B 517    11333   6696   9756   -964   -460     -5       C  
ATOM   8218  CG1 VAL B 517     -26.384 -51.559  99.600  1.00 71.48           C  
ANISOU 8218  CG1 VAL B 517    11078   6622   9457   -930   -387     51       C  
ATOM   8219  CG2 VAL B 517     -25.945 -54.020  99.265  1.00 72.90           C  
ANISOU 8219  CG2 VAL B 517    11189   6697   9811  -1019   -484   -125       C  
ATOM   8220  N   LYS B 518     -24.635 -51.423 102.769  1.00 83.73           N  
ANISOU 8220  N   LYS B 518    13022   7854  10934   -994   -461    155       N  
ATOM   8221  CA  LYS B 518     -24.490 -50.240 103.638  1.00 86.07           C  
ANISOU 8221  CA  LYS B 518    13503   8110  11086  -1041   -386    209       C  
ATOM   8222  C   LYS B 518     -23.051 -49.862 103.837  1.00 82.93           C  
ANISOU 8222  C   LYS B 518    13163   7719  10627  -1104   -493    215       C  
ATOM   8223  O   LYS B 518     -22.724 -48.673 103.801  1.00 79.90           O  
ANISOU 8223  O   LYS B 518    12872   7349  10134  -1126   -433    209       O  
ATOM   8224  CB  LYS B 518     -25.194 -50.435 104.997  1.00 94.10           C  
ANISOU 8224  CB  LYS B 518    14677   9030  12044  -1114   -316    278       C  
ATOM   8225  CG  LYS B 518     -26.705 -50.361 104.875  1.00104.16           C  
ANISOU 8225  CG  LYS B 518    15915  10300  13361  -1046   -157    305       C  
ATOM   8226  CD  LYS B 518     -27.473 -50.790 106.121  1.00115.20           C  
ANISOU 8226  CD  LYS B 518    17437  11603  14727  -1108    -84    368       C  
ATOM   8227  CE  LYS B 518     -28.715 -51.621 105.733  1.00122.77           C  
ANISOU 8227  CE  LYS B 518    18243  12591  15812  -1044    -55    401       C  
ATOM   8228  NZ  LYS B 518     -29.861 -51.559 106.691  1.00126.46           N  
ANISOU 8228  NZ  LYS B 518    18807  12982  16258  -1057    108    483       N  
ATOM   8229  N   GLU B 519     -22.207 -50.870 104.058  1.00 84.01           N  
ANISOU 8229  N   GLU B 519    13233   7838  10848  -1136   -640    250       N  
ATOM   8230  CA  GLU B 519     -20.764 -50.662 104.201  1.00 88.71           C  
ANISOU 8230  CA  GLU B 519    13827   8460  11419  -1197   -766    306       C  
ATOM   8231  C   GLU B 519     -20.188 -50.042 102.930  1.00 84.61           C  
ANISOU 8231  C   GLU B 519    13203   8020  10923  -1116   -761    225       C  
ATOM   8232  O   GLU B 519     -19.380 -49.078 103.004  1.00 84.78           O  
ANISOU 8232  O   GLU B 519    13293   8083  10836  -1173   -790    250       O  
ATOM   8233  CB  GLU B 519     -20.031 -51.977 104.551  1.00 96.66           C  
ANISOU 8233  CB  GLU B 519    14717   9424  12584  -1212   -900    407       C  
ATOM   8234  CG  GLU B 519     -20.397 -52.578 105.898  1.00106.82           C  
ANISOU 8234  CG  GLU B 519    16096  10652  13836  -1320   -938    531       C  
ATOM   8235  CD  GLU B 519     -19.295 -53.459 106.516  1.00119.94           C  
ANISOU 8235  CD  GLU B 519    17656  12301  15613  -1384  -1099    727       C  
ATOM   8236  OE1 GLU B 519     -19.574 -54.644 106.831  1.00127.90           O  
ANISOU 8236  OE1 GLU B 519    18579  13230  16785  -1355  -1117    799       O  
ATOM   8237  OE2 GLU B 519     -18.142 -52.984 106.705  1.00129.21           O  
ANISOU 8237  OE2 GLU B 519    18820  13546  16728  -1469  -1208    839       O  
ATOM   8238  N   ALA B 520     -20.548 -50.650 101.781  1.00 79.66           N  
ANISOU 8238  N   ALA B 520    12416   7422  10427  -1010   -731    129       N  
ATOM   8239  CA  ALA B 520     -20.119 -50.164 100.482  1.00 75.42           C  
ANISOU 8239  CA  ALA B 520    11771   6979   9903   -948   -717     45       C  
ATOM   8240  C   ALA B 520     -20.543 -48.704 100.255  1.00 74.66           C  
ANISOU 8240  C   ALA B 520    11752   6948   9664   -943   -630     42       C  
ATOM   8241  O   ALA B 520     -19.730 -47.846  99.829  1.00 75.81           O  
ANISOU 8241  O   ALA B 520    11897   7150   9758   -943   -650     39       O  
ATOM   8242  CB  ALA B 520     -20.620 -51.082  99.394  1.00 73.16           C  
ANISOU 8242  CB  ALA B 520    11341   6722   9732   -897   -679    -65       C  
ATOM   8243  N   GLN B 521     -21.796 -48.432 100.551  1.00 72.41           N  
ANISOU 8243  N   GLN B 521    11525   6645   9343   -933   -518     62       N  
ATOM   8244  CA  GLN B 521     -22.332 -47.124 100.416  1.00 72.31           C  
ANISOU 8244  CA  GLN B 521    11571   6652   9249   -908   -387     94       C  
ATOM   8245  C   GLN B 521     -21.677 -46.122 101.339  1.00 77.52           C  
ANISOU 8245  C   GLN B 521    12436   7233   9785   -992   -351    126       C  
ATOM   8246  O   GLN B 521     -21.573 -44.898 101.032  1.00 78.67           O  
ANISOU 8246  O   GLN B 521    12630   7385   9875   -978   -253    134       O  
ATOM   8247  CB  GLN B 521     -23.784 -47.171 100.760  1.00 71.38           C  
ANISOU 8247  CB  GLN B 521    11469   6498   9153   -879   -253    147       C  
ATOM   8248  CG  GLN B 521     -24.687 -47.585  99.652  1.00 70.58           C  
ANISOU 8248  CG  GLN B 521    11165   6521   9128   -822   -243    153       C  
ATOM   8249  CD  GLN B 521     -26.087 -47.806 100.175  1.00 71.91           C  
ANISOU 8249  CD  GLN B 521    11337   6650   9333   -807   -131    240       C  
ATOM   8250  OE1 GLN B 521     -26.277 -48.435 101.211  1.00 71.74           O  
ANISOU 8250  OE1 GLN B 521    11426   6519   9313   -847   -132    240       O  
ATOM   8251  NE2 GLN B 521     -27.084 -47.290  99.462  1.00 74.09           N  
ANISOU 8251  NE2 GLN B 521    11474   7028   9647   -754    -34    345       N  
ATOM   8252  N   ALA B 522     -21.342 -46.605 102.527  1.00 82.89           N  
ANISOU 8252  N   ALA B 522    13248   7834  10410  -1101   -413    156       N  
ATOM   8253  CA  ALA B 522     -20.631 -45.798 103.504  1.00 88.08           C  
ANISOU 8253  CA  ALA B 522    14121   8439  10905  -1256   -406    185       C  
ATOM   8254  C   ALA B 522     -19.229 -45.437 102.973  1.00 88.21           C  
ANISOU 8254  C   ALA B 522    14076   8538  10900  -1288   -544    190       C  
ATOM   8255  O   ALA B 522     -18.793 -44.274 103.055  1.00 89.94           O  
ANISOU 8255  O   ALA B 522    14423   8748  11001  -1363   -485    181       O  
ATOM   8256  CB  ALA B 522     -20.533 -46.564 104.818  1.00 90.98           C  
ANISOU 8256  CB  ALA B 522    14605   8754  11208  -1399   -484    248       C  
ATOM   8257  N   ALA B 523     -18.538 -46.462 102.458  1.00 85.97           N  
ANISOU 8257  N   ALA B 523    13601   8317  10746  -1234   -705    207       N  
ATOM   8258  CA  ALA B 523     -17.236 -46.295 101.814  1.00 82.58           C  
ANISOU 8258  CA  ALA B 523    13060   7968  10346  -1231   -824    226       C  
ATOM   8259  C   ALA B 523     -17.305 -45.312 100.668  1.00 80.41           C  
ANISOU 8259  C   ALA B 523    12733   7756  10061  -1142   -738    151       C  
ATOM   8260  O   ALA B 523     -16.352 -44.540 100.477  1.00 81.53           O  
ANISOU 8260  O   ALA B 523    12893   7946  10139  -1193   -785    172       O  
ATOM   8261  CB  ALA B 523     -16.697 -47.637 101.313  1.00 81.67           C  
ANISOU 8261  CB  ALA B 523    12733   7870  10429  -1148   -931    245       C  
ATOM   8262  N   ALA B 524     -18.395 -45.373  99.892  1.00 79.03           N  
ANISOU 8262  N   ALA B 524    12473   7602   9950  -1024   -629     89       N  
ATOM   8263  CA  ALA B 524     -18.590 -44.458  98.776  1.00 78.55           C  
ANISOU 8263  CA  ALA B 524    12334   7626   9885   -946   -549     59       C  
ATOM   8264  C   ALA B 524     -18.705 -42.968  99.206  1.00 83.43           C  
ANISOU 8264  C   ALA B 524    13126   8181  10391   -993   -415     95       C  
ATOM   8265  O   ALA B 524     -18.269 -42.051  98.458  1.00 83.66           O  
ANISOU 8265  O   ALA B 524    13113   8270  10403   -966   -391     98       O  
ATOM   8266  CB  ALA B 524     -19.795 -44.866  97.979  1.00 77.25           C  
ANISOU 8266  CB  ALA B 524    12032   7522   9795   -856   -477     37       C  
ATOM   8267  N   GLU B 525     -19.257 -42.701 100.392  1.00 86.42           N  
ANISOU 8267  N   GLU B 525    13711   8427  10695  -1073   -305    117       N  
ATOM   8268  CA  GLU B 525     -19.346 -41.322 100.844  1.00 91.26           C  
ANISOU 8268  CA  GLU B 525    14526   8937  11211  -1137   -124    126       C  
ATOM   8269  C   GLU B 525     -17.940 -40.723 101.054  1.00 91.90           C  
ANISOU 8269  C   GLU B 525    14708   9039  11169  -1283   -231    118       C  
ATOM   8270  O   GLU B 525     -17.734 -39.499 100.866  1.00 97.08           O  
ANISOU 8270  O   GLU B 525    15460   9651  11774  -1312   -108    112       O  
ATOM   8271  CB  GLU B 525     -20.191 -41.210 102.087  1.00 97.70           C  
ANISOU 8271  CB  GLU B 525    15567   9593  11961  -1219     49    129       C  
ATOM   8272  CG  GLU B 525     -20.773 -39.834 102.275  1.00107.46           C  
ANISOU 8272  CG  GLU B 525    16970  10681  13178  -1216    348    134       C  
ATOM   8273  CD  GLU B 525     -21.957 -39.457 101.352  1.00113.00           C  
ANISOU 8273  CD  GLU B 525    17482  11386  14064  -1001    530    218       C  
ATOM   8274  OE1 GLU B 525     -22.336 -40.230 100.428  1.00117.36           O  
ANISOU 8274  OE1 GLU B 525    17768  12095  14727   -877    401    261       O  
ATOM   8275  OE2 GLU B 525     -22.485 -38.319 101.513  1.00118.87           O  
ANISOU 8275  OE2 GLU B 525    18341  11976  14845   -972    819    258       O  
ATOM   8276  N   GLN B 526     -16.968 -41.567 101.434  1.00 88.52           N  
ANISOU 8276  N   GLN B 526    14246   8678  10710  -1380   -452    144       N  
ATOM   8277  CA  GLN B 526     -15.559 -41.099 101.556  1.00 85.96           C  
ANISOU 8277  CA  GLN B 526    13963   8415  10283  -1526   -591    182       C  
ATOM   8278  C   GLN B 526     -14.922 -40.689 100.264  1.00 80.37           C  
ANISOU 8278  C   GLN B 526    13070   7811   9652  -1411   -638    173       C  
ATOM   8279  O   GLN B 526     -14.070 -39.831 100.256  1.00 79.36           O  
ANISOU 8279  O   GLN B 526    13014   7707   9432  -1517   -666    193       O  
ATOM   8280  CB  GLN B 526     -14.696 -42.114 102.291  1.00 88.99           C  
ANISOU 8280  CB  GLN B 526    14308   8855  10647  -1651   -813    278       C  
ATOM   8281  CG  GLN B 526     -15.133 -42.137 103.757  1.00 96.28           C  
ANISOU 8281  CG  GLN B 526    15484   9690  11406  -1857   -765    299       C  
ATOM   8282  CD  GLN B 526     -15.239 -40.679 104.312  1.00 97.37           C  
ANISOU 8282  CD  GLN B 526    15930   9733  11333  -2041   -578    233       C  
ATOM   8283  OE1 GLN B 526     -14.252 -39.918 104.298  1.00 94.58           O  
ANISOU 8283  OE1 GLN B 526    15644   9429  10862  -2193   -643    255       O  
ATOM   8284  NE2 GLN B 526     -16.445 -40.285 104.732  1.00 95.29           N  
ANISOU 8284  NE2 GLN B 526    15843   9319  11043  -2021   -322    152       N  
ATOM   8285  N   LEU B 527     -15.384 -41.259  99.157  1.00 77.37           N  
ANISOU 8285  N   LEU B 527    12467   7502   9426  -1219   -636    140       N  
ATOM   8286  CA  LEU B 527     -14.847 -40.945  97.857  1.00 74.05           C  
ANISOU 8286  CA  LEU B 527    11867   7200   9067  -1121   -671    125       C  
ATOM   8287  C   LEU B 527     -15.159 -39.509  97.608  1.00 74.98           C  
ANISOU 8287  C   LEU B 527    12080   7283   9125  -1121   -515    129       C  
ATOM   8288  O   LEU B 527     -14.348 -38.793  97.034  1.00 73.37           O  
ANISOU 8288  O   LEU B 527    11837   7143   8897  -1134   -549    143       O  
ATOM   8289  CB  LEU B 527     -15.487 -41.810  96.803  1.00 72.62           C  
ANISOU 8289  CB  LEU B 527    11472   7102   9016   -972   -667     75       C  
ATOM   8290  CG  LEU B 527     -15.277 -43.308  96.924  1.00 73.87           C  
ANISOU 8290  CG  LEU B 527    11531   7259   9275   -955   -771     54       C  
ATOM   8291  CD1 LEU B 527     -16.078 -44.066  95.880  1.00 74.34           C  
ANISOU 8291  CD1 LEU B 527    11428   7389   9426   -856   -726    -24       C  
ATOM   8292  CD2 LEU B 527     -13.809 -43.677  96.810  1.00 74.96           C  
ANISOU 8292  CD2 LEU B 527    11580   7438   9463   -983   -907     95       C  
ATOM   8293  N   LYS B 528     -16.328 -39.066  98.074  1.00 77.40           N  
ANISOU 8293  N   LYS B 528    12511   7471   9427  -1102   -321    132       N  
ATOM   8294  CA  LYS B 528     -16.645 -37.630  98.022  1.00 80.29           C  
ANISOU 8294  CA  LYS B 528    12996   7741   9767  -1104   -111    157       C  
ATOM   8295  C   LYS B 528     -15.591 -36.800  98.697  1.00 78.69           C  
ANISOU 8295  C   LYS B 528    13010   7470   9416  -1297   -124    139       C  
ATOM   8296  O   LYS B 528     -15.219 -35.758  98.146  1.00 77.62           O  
ANISOU 8296  O   LYS B 528    12877   7335   9279  -1291    -55    156       O  
ATOM   8297  CB  LYS B 528     -18.006 -37.280  98.622  1.00 84.22           C  
ANISOU 8297  CB  LYS B 528    13619   8075  10306  -1064    146    180       C  
ATOM   8298  CG  LYS B 528     -19.176 -37.803  97.811  1.00 86.43           C  
ANISOU 8298  CG  LYS B 528    13662   8440  10737   -883    186    246       C  
ATOM   8299  CD  LYS B 528     -20.489 -37.467  98.480  1.00 91.12           C  
ANISOU 8299  CD  LYS B 528    14361   8865  11395   -837    452    305       C  
ATOM   8300  CE  LYS B 528     -21.627 -37.821  97.554  1.00 96.47           C  
ANISOU 8300  CE  LYS B 528    14764   9665  12224   -675    481    425       C  
ATOM   8301  NZ  LYS B 528     -22.940 -37.679  98.242  1.00102.01           N  
ANISOU 8301  NZ  LYS B 528    15530  10211  13015   -618    731    512       N  
ATOM   8302  N   THR B 529     -15.114 -37.246  99.871  1.00 78.72           N  
ANISOU 8302  N   THR B 529    13189   7432   9288  -1488   -218    121       N  
ATOM   8303  CA  THR B 529     -14.180 -36.423 100.656  1.00 79.56           C  
ANISOU 8303  CA  THR B 529    13537   7487   9205  -1745   -228    114       C  
ATOM   8304  C   THR B 529     -12.801 -36.490 100.047  1.00 77.55           C  
ANISOU 8304  C   THR B 529    13122   7401   8940  -1780   -467    169       C  
ATOM   8305  O   THR B 529     -12.146 -35.450  99.887  1.00 84.19           O  
ANISOU 8305  O   THR B 529    14051   8235   9702  -1883   -436    170       O  
ATOM   8306  CB  THR B 529     -14.148 -36.801 102.135  1.00 80.45           C  
ANISOU 8306  CB  THR B 529    13893   7531   9141  -1992   -253    106       C  
ATOM   8307  OG1 THR B 529     -13.643 -38.094 102.210  1.00 84.92           O  
ANISOU 8307  OG1 THR B 529    14274   8237   9751  -1980   -517    180       O  
ATOM   8308  CG2 THR B 529     -15.563 -36.849 102.781  1.00 81.39           C  
ANISOU 8308  CG2 THR B 529    14167   7478   9281  -1948      1     51       C  
ATOM   8309  N   THR B 530     -12.391 -37.671  99.640  1.00 74.53           N  
ANISOU 8309  N   THR B 530    12500   7155   8662  -1683   -674    216       N  
ATOM   8310  CA  THR B 530     -11.150 -37.867  98.892  1.00 74.13           C  
ANISOU 8310  CA  THR B 530    12243   7259   8662  -1660   -867    281       C  
ATOM   8311  C   THR B 530     -11.086 -36.987  97.622  1.00 76.48           C  
ANISOU 8311  C   THR B 530    12429   7607   9022  -1526   -785    250       C  
ATOM   8312  O   THR B 530     -10.055 -36.339  97.322  1.00 74.29           O  
ANISOU 8312  O   THR B 530    12134   7399   8695  -1605   -861    294       O  
ATOM   8313  CB  THR B 530     -11.055 -39.357  98.486  1.00 71.82           C  
ANISOU 8313  CB  THR B 530    11700   7048   8537  -1514  -1000    309       C  
ATOM   8314  OG1 THR B 530     -11.199 -40.148  99.639  1.00 69.85           O  
ANISOU 8314  OG1 THR B 530    11539   6749   8251  -1625  -1065    361       O  
ATOM   8315  CG2 THR B 530      -9.755 -39.688  97.868  1.00 72.13           C  
ANISOU 8315  CG2 THR B 530    11533   7216   8657  -1492  -1163    391       C  
ATOM   8316  N   ARG B 531     -12.206 -36.990  96.899  1.00 81.34           N  
ANISOU 8316  N   ARG B 531    12958   8204   9743  -1339   -640    201       N  
ATOM   8317  CA  ARG B 531     -12.322 -36.307  95.645  1.00 88.30           C  
ANISOU 8317  CA  ARG B 531    13693   9161  10693  -1207   -570    205       C  
ATOM   8318  C   ARG B 531     -12.109 -34.822  95.898  1.00 84.94           C  
ANISOU 8318  C   ARG B 531    13456   8635  10182  -1311   -436    223       C  
ATOM   8319  O   ARG B 531     -11.335 -34.167  95.176  1.00 85.58           O  
ANISOU 8319  O   ARG B 531    13458   8798  10259  -1312   -480    254       O  
ATOM   8320  CB  ARG B 531     -13.697 -36.585  94.993  1.00 98.68           C  
ANISOU 8320  CB  ARG B 531    14884  10490  12118  -1035   -445    196       C  
ATOM   8321  CG  ARG B 531     -13.999 -35.872  93.645  1.00110.56           C  
ANISOU 8321  CG  ARG B 531    16208  12109  13690   -914   -372    247       C  
ATOM   8322  CD  ARG B 531     -15.513 -35.820  93.345  1.00121.55           C  
ANISOU 8322  CD  ARG B 531    17524  13488  15170   -799   -213    308       C  
ATOM   8323  NE  ARG B 531     -16.222 -34.991  94.342  1.00135.17           N  
ANISOU 8323  NE  ARG B 531    19468  14986  16902   -823     11    348       N  
ATOM   8324  CZ  ARG B 531     -17.515 -35.096  94.695  1.00146.08           C  
ANISOU 8324  CZ  ARG B 531    20864  16277  18362   -754    174    402       C  
ATOM   8325  NH1 ARG B 531     -18.322 -35.989  94.110  1.00151.41           N  
ANISOU 8325  NH1 ARG B 531    21334  17090  19103   -667    114    437       N  
ATOM   8326  NH2 ARG B 531     -18.024 -34.296  95.646  1.00144.11           N  
ANISOU 8326  NH2 ARG B 531    20842  15789  18124   -786    421    421       N  
ATOM   8327  N   ASN B 532     -12.754 -34.297  96.922  1.00 84.04           N  
ANISOU 8327  N   ASN B 532    13600   8330  10000  -1410   -256    198       N  
ATOM   8328  CA  ASN B 532     -12.675 -32.869  97.189  1.00 87.62           C  
ANISOU 8328  CA  ASN B 532    14267   8633  10388  -1517    -59    194       C  
ATOM   8329  C   ASN B 532     -11.288 -32.491  97.624  1.00 85.20           C  
ANISOU 8329  C   ASN B 532    14084   8368   9917  -1758   -210    193       C  
ATOM   8330  O   ASN B 532     -10.734 -31.500  97.139  1.00 86.51           O  
ANISOU 8330  O   ASN B 532    14265   8534  10070  -1793   -169    213       O  
ATOM   8331  CB  ASN B 532     -13.673 -32.429  98.273  1.00 93.42           C  
ANISOU 8331  CB  ASN B 532    15288   9119  11085  -1595    220    145       C  
ATOM   8332  CG  ASN B 532     -15.134 -32.725  97.909  1.00 98.41           C  
ANISOU 8332  CG  ASN B 532    15788   9703  11897  -1360    393    187       C  
ATOM   8333  OD1 ASN B 532     -15.557 -32.613  96.753  1.00103.98           O  
ANISOU 8333  OD1 ASN B 532    16238  10510  12757  -1159    409    272       O  
ATOM   8334  ND2 ASN B 532     -15.912 -33.121  98.910  1.00101.83           N  
ANISOU 8334  ND2 ASN B 532    16388  10001  12301  -1409    513    146       N  
ATOM   8335  N   ALA B 533     -10.743 -33.264  98.554  1.00 83.69           N  
ANISOU 8335  N   ALA B 533    13973   8222   9603  -1936   -388    196       N  
ATOM   8336  CA  ALA B 533      -9.457 -32.958  99.130  1.00 84.48           C  
ANISOU 8336  CA  ALA B 533    14188   8384   9523  -2216   -552    240       C  
ATOM   8337  C   ALA B 533      -8.259 -33.183  98.172  1.00 86.56           C  
ANISOU 8337  C   ALA B 533    14171   8859   9856  -2149   -789    336       C  
ATOM   8338  O   ALA B 533      -7.246 -32.510  98.306  1.00 91.26           O  
ANISOU 8338  O   ALA B 533    14836   9504  10333  -2346   -873    387       O  
ATOM   8339  CB  ALA B 533      -9.279 -33.762 100.377  1.00 84.55           C  
ANISOU 8339  CB  ALA B 533    14322   8410   9393  -2430   -684    270       C  
ATOM   8340  N   TYR B 534      -8.345 -34.105  97.224  1.00 87.43           N  
ANISOU 8340  N   TYR B 534    13978   9090  10149  -1896   -880    358       N  
ATOM   8341  CA  TYR B 534      -7.213 -34.313  96.301  1.00 87.26           C  
ANISOU 8341  CA  TYR B 534    13701   9248  10203  -1830  -1056    438       C  
ATOM   8342  C   TYR B 534      -7.542 -33.833  94.866  1.00 88.34           C  
ANISOU 8342  C   TYR B 534    13666   9437  10460  -1609   -951    398       C  
ATOM   8343  O   TYR B 534      -6.826 -33.012  94.359  1.00 95.17           O  
ANISOU 8343  O   TYR B 534    14503  10358  11298  -1649   -969    436       O  
ATOM   8344  CB  TYR B 534      -6.777 -35.777  96.313  1.00 86.99           C  
ANISOU 8344  CB  TYR B 534    13454   9316  10282  -1757  -1234    507       C  
ATOM   8345  CG  TYR B 534      -6.245 -36.280  97.633  1.00 85.26           C  
ANISOU 8345  CG  TYR B 534    13335   9098   9959  -1986  -1384    619       C  
ATOM   8346  CD1 TYR B 534      -4.930 -36.083  97.982  1.00 87.21           C  
ANISOU 8346  CD1 TYR B 534    13547   9458  10128  -2187  -1568    782       C  
ATOM   8347  CD2 TYR B 534      -7.030 -36.991  98.487  1.00 84.79           C  
ANISOU 8347  CD2 TYR B 534    13376   8954   9884  -2010  -1356    595       C  
ATOM   8348  CE1 TYR B 534      -4.399 -36.550  99.183  1.00 89.66           C  
ANISOU 8348  CE1 TYR B 534    13918   9814  10333  -2432  -1735    940       C  
ATOM   8349  CE2 TYR B 534      -6.531 -37.453  99.697  1.00 89.18           C  
ANISOU 8349  CE2 TYR B 534    14010   9539  10332  -2245  -1508    728       C  
ATOM   8350  CZ  TYR B 534      -5.193 -37.227 100.061  1.00 90.78           C  
ANISOU 8350  CZ  TYR B 534    14172   9875  10444  -2470  -1708    915       C  
ATOM   8351  OH  TYR B 534      -4.647 -37.682 101.278  1.00 90.43           O  
ANISOU 8351  OH  TYR B 534    14178   9905  10276  -2746  -1890   1104       O  
ATOM   8352  N   ILE B 535      -8.649 -34.273  94.259  1.00 85.50           N  
ANISOU 8352  N   ILE B 535    13202   9070  10213  -1408   -843    338       N  
ATOM   8353  CA  ILE B 535      -8.842 -34.063  92.844  1.00 84.32           C  
ANISOU 8353  CA  ILE B 535    12839   9038  10159  -1234   -800    335       C  
ATOM   8354  C   ILE B 535      -9.366 -32.644  92.533  1.00 84.49           C  
ANISOU 8354  C   ILE B 535    12948   8983  10170  -1221   -614    362       C  
ATOM   8355  O   ILE B 535      -8.805 -31.974  91.702  1.00 86.05           O  
ANISOU 8355  O   ILE B 535    13046   9272  10377  -1201   -629    406       O  
ATOM   8356  CB  ILE B 535      -9.758 -35.134  92.197  1.00 87.92           C  
ANISOU 8356  CB  ILE B 535    13123   9562  10720  -1068   -781    282       C  
ATOM   8357  CG1 ILE B 535      -9.030 -36.471  92.090  1.00 87.67           C  
ANISOU 8357  CG1 ILE B 535    12947   9612  10749  -1048   -931    259       C  
ATOM   8358  CG2 ILE B 535     -10.212 -34.710  90.784  1.00 91.43           C  
ANISOU 8358  CG2 ILE B 535    13381  10143  11215   -944   -711    297       C  
ATOM   8359  CD1 ILE B 535      -9.533 -37.423  93.110  1.00 89.50           C  
ANISOU 8359  CD1 ILE B 535    13269   9739  10998  -1074   -947    237       C  
ATOM   8360  N   GLN B 536     -10.484 -32.239  93.124  1.00 86.45           N  
ANISOU 8360  N   GLN B 536    13357   9060  10428  -1212   -419    351       N  
ATOM   8361  CA  GLN B 536     -11.239 -31.001  92.745  1.00 90.79           C  
ANISOU 8361  CA  GLN B 536    13942   9506  11045  -1144   -182    413       C  
ATOM   8362  C   GLN B 536     -10.362 -29.778  92.354  1.00 91.32           C  
ANISOU 8362  C   GLN B 536    14045   9569  11081  -1217   -156    460       C  
ATOM   8363  O   GLN B 536     -10.530 -29.163  91.297  1.00 89.79           O  
ANISOU 8363  O   GLN B 536    13681   9456  10977  -1101    -97    550       O  
ATOM   8364  CB  GLN B 536     -12.168 -30.628  93.910  1.00 96.93           C  
ANISOU 8364  CB  GLN B 536    14988  10024  11815  -1201     52    384       C  
ATOM   8365  CG  GLN B 536     -12.914 -29.293  93.709  1.00105.04           C  
ANISOU 8365  CG  GLN B 536    16081  10875  12954  -1132    362    468       C  
ATOM   8366  CD  GLN B 536     -14.168 -29.432  92.939  1.00113.24           C  
ANISOU 8366  CD  GLN B 536    16885  11967  14171   -912    474    592       C  
ATOM   8367  OE1 GLN B 536     -14.111 -29.576  91.725  1.00121.61           O  
ANISOU 8367  OE1 GLN B 536    17663  13254  15288   -803    354    681       O  
ATOM   8368  NE2 GLN B 536     -15.317 -29.352  93.609  1.00121.85           N  
ANISOU 8368  NE2 GLN B 536    18084  12865  15346   -862    712    619       N  
ATOM   8369  N   LYS B 537      -9.440 -29.450  93.244  1.00 95.94           N  
ANISOU 8369  N   LYS B 537    14852  10073  11528  -1435   -210    415       N  
ATOM   8370  CA  LYS B 537      -8.426 -28.396  93.101  1.00 99.25           C  
ANISOU 8370  CA  LYS B 537    15347  10485  11879  -1572   -221    445       C  
ATOM   8371  C   LYS B 537      -7.869 -28.347  91.708  1.00 97.29           C  
ANISOU 8371  C   LYS B 537    14800  10459  11705  -1437   -344    521       C  
ATOM   8372  O   LYS B 537      -7.642 -27.284  91.145  1.00101.73           O  
ANISOU 8372  O   LYS B 537    15348  11004  12298  -1433   -255    583       O  
ATOM   8373  CB  LYS B 537      -7.213 -28.753  94.012  1.00110.20           C  
ANISOU 8373  CB  LYS B 537    16866  11917  13086  -1831   -434    420       C  
ATOM   8374  CG  LYS B 537      -6.299 -27.609  94.365  1.00124.16           C  
ANISOU 8374  CG  LYS B 537    18833  13620  14722  -2078   -414    432       C  
ATOM   8375  CD  LYS B 537      -4.945 -28.053  94.930  1.00134.70           C  
ANISOU 8375  CD  LYS B 537    20176  15104  15899  -2320   -698    484       C  
ATOM   8376  CE  LYS B 537      -4.120 -26.783  95.265  1.00144.17           C  
ANISOU 8376  CE  LYS B 537    21596  16235  16944  -2608   -660    495       C  
ATOM   8377  NZ  LYS B 537      -2.651 -26.961  95.469  1.00143.83           N  
ANISOU 8377  NZ  LYS B 537    21483  16392  16773  -2835   -952    611       N  
ATOM   8378  N   TYR B 538      -7.563 -29.521  91.182  1.00 96.03           N  
ANISOU 8378  N   TYR B 538    14415  10501  11571  -1347   -542    512       N  
ATOM   8379  CA  TYR B 538      -6.946 -29.676  89.882  1.00 96.00           C  
ANISOU 8379  CA  TYR B 538    14136  10722  11614  -1245   -659    557       C  
ATOM   8380  C   TYR B 538      -7.953 -29.486  88.748  1.00 96.01           C  
ANISOU 8380  C   TYR B 538    13950  10811  11718  -1065   -546    608       C  
ATOM   8381  O   TYR B 538      -7.589 -28.952  87.672  1.00102.18           O  
ANISOU 8381  O   TYR B 538    14565  11736  12520  -1019   -562    679       O  
ATOM   8382  CB  TYR B 538      -6.203 -31.034  89.799  1.00 96.08           C  
ANISOU 8382  CB  TYR B 538    13998  10878  11628  -1233   -863    521       C  
ATOM   8383  CG  TYR B 538      -4.972 -31.063  90.691  1.00 98.95           C  
ANISOU 8383  CG  TYR B 538    14465  11224  11907  -1422  -1011    560       C  
ATOM   8384  CD1 TYR B 538      -3.899 -30.208  90.447  1.00102.23           C  
ANISOU 8384  CD1 TYR B 538    14872  11699  12271  -1528  -1074    635       C  
ATOM   8385  CD2 TYR B 538      -4.891 -31.897  91.789  1.00100.99           C  
ANISOU 8385  CD2 TYR B 538    14821  11421  12130  -1517  -1095    552       C  
ATOM   8386  CE1 TYR B 538      -2.773 -30.214  91.253  1.00105.84           C  
ANISOU 8386  CE1 TYR B 538    15402  12173  12639  -1734  -1229    710       C  
ATOM   8387  CE2 TYR B 538      -3.775 -31.886  92.625  1.00104.26           C  
ANISOU 8387  CE2 TYR B 538    15307  11854  12452  -1727  -1250    640       C  
ATOM   8388  CZ  TYR B 538      -2.714 -31.053  92.335  1.00107.32           C  
ANISOU 8388  CZ  TYR B 538    15670  12319  12785  -1840  -1322    724       C  
ATOM   8389  OH  TYR B 538      -1.583 -30.987  93.115  1.00111.13           O  
ANISOU 8389  OH  TYR B 538    16202  12855  13165  -2080  -1494    849       O  
ATOM   8390  N   LEU B 539      -9.198 -29.915  88.941  1.00 93.73           N  
ANISOU 8390  N   LEU B 539    13665  10462  11485   -979   -443    597       N  
ATOM   8391  CA  LEU B 539     -10.166 -29.796  87.847  1.00 91.34           C  
ANISOU 8391  CA  LEU B 539    13147  10288  11268   -841   -365    692       C  
ATOM   8392  C   LEU B 539     -10.500 -28.321  87.574  1.00 91.61           C  
ANISOU 8392  C   LEU B 539    13198  10230  11380   -811   -178    844       C  
ATOM   8393  O   LEU B 539     -10.696 -27.913  86.430  1.00 87.65           O  
ANISOU 8393  O   LEU B 539    12475   9899  10927   -738   -171    975       O  
ATOM   8394  CB  LEU B 539     -11.389 -30.640  88.138  1.00 89.38           C  
ANISOU 8394  CB  LEU B 539    12882  10013  11064   -774   -314    672       C  
ATOM   8395  CG  LEU B 539     -12.315 -30.757  86.938  1.00 90.36           C  
ANISOU 8395  CG  LEU B 539    12744  10344  11243   -678   -293    788       C  
ATOM   8396  CD1 LEU B 539     -13.093 -32.062  86.907  1.00 93.50           C  
ANISOU 8396  CD1 LEU B 539    13066  10827  11631   -658   -351    718       C  
ATOM   8397  CD2 LEU B 539     -13.319 -29.659  86.991  1.00 92.45           C  
ANISOU 8397  CD2 LEU B 539    13006  10489  11631   -605    -75    980       C  
ATOM   8398  N   GLU B 540     -10.537 -27.539  88.639  1.00 95.14           N  
ANISOU 8398  N   GLU B 540    13912  10402  11834   -886    -15    829       N  
ATOM   8399  CA  GLU B 540     -10.734 -26.105  88.541  1.00 99.93           C  
ANISOU 8399  CA  GLU B 540    14583  10848  12536   -873    209    954       C  
ATOM   8400  C   GLU B 540      -9.610 -25.403  87.785  1.00 98.51           C  
ANISOU 8400  C   GLU B 540    14321  10788  12318   -924    113   1001       C  
ATOM   8401  O   GLU B 540      -9.869 -24.519  86.950  1.00100.84           O  
ANISOU 8401  O   GLU B 540    14471  11118  12725   -840    222   1169       O  
ATOM   8402  CB  GLU B 540     -10.883 -25.525  89.942  1.00107.24           C  
ANISOU 8402  CB  GLU B 540    15873  11430  13443   -996    424    870       C  
ATOM   8403  CG  GLU B 540     -12.155 -25.997  90.657  1.00117.13           C  
ANISOU 8403  CG  GLU B 540    17205  12532  14767   -924    589    857       C  
ATOM   8404  CD  GLU B 540     -12.180 -25.734  92.172  1.00131.21           C  
ANISOU 8404  CD  GLU B 540    19383  14005  16464  -1099    767    715       C  
ATOM   8405  OE1 GLU B 540     -11.112 -25.518  92.795  1.00146.94           O  
ANISOU 8405  OE1 GLU B 540    21593  15952  18284  -1321    678    600       O  
ATOM   8406  OE2 GLU B 540     -13.280 -25.780  92.782  1.00138.02           O  
ANISOU 8406  OE2 GLU B 540    20344  14679  17415  -1039    995    724       O  
ATOM   8407  N   ARG B 541      -8.375 -25.797  88.059  1.00 98.61           N  
ANISOU 8407  N   ARG B 541    14402  10874  12188  -1059    -89    884       N  
ATOM   8408  CA  ARG B 541      -7.214 -25.298  87.296  1.00103.89           C  
ANISOU 8408  CA  ARG B 541    14962  11695  12814  -1108   -213    930       C  
ATOM   8409  C   ARG B 541      -7.279 -25.612  85.805  1.00 97.17           C  
ANISOU 8409  C   ARG B 541    13773  11142  12004   -974   -314   1020       C  
ATOM   8410  O   ARG B 541      -6.873 -24.804  84.982  1.00 98.21           O  
ANISOU 8410  O   ARG B 541    13788  11366  12162   -962   -305   1130       O  
ATOM   8411  CB  ARG B 541      -5.890 -25.882  87.812  1.00115.22           C  
ANISOU 8411  CB  ARG B 541    16470  13197  14110  -1264   -436    829       C  
ATOM   8412  CG  ARG B 541      -5.398 -25.341  89.143  1.00130.55           C  
ANISOU 8412  CG  ARG B 541    18740  14916  15944  -1493   -393    770       C  
ATOM   8413  CD  ARG B 541      -4.145 -26.115  89.561  1.00139.61           C  
ANISOU 8413  CD  ARG B 541    19876  16198  16972  -1639   -656    739       C  
ATOM   8414  NE  ARG B 541      -3.672 -25.802  90.913  1.00143.01           N  
ANISOU 8414  NE  ARG B 541    20611  16473  17252  -1916   -666    697       N  
ATOM   8415  CZ  ARG B 541      -2.559 -26.296  91.450  1.00147.28           C  
ANISOU 8415  CZ  ARG B 541    21156  17123  17680  -2096   -892    728       C  
ATOM   8416  NH1 ARG B 541      -1.771 -27.102  90.739  1.00145.50           N  
ANISOU 8416  NH1 ARG B 541    20642  17127  17514  -1995  -1095    798       N  
ATOM   8417  NH2 ARG B 541      -2.209 -25.955  92.685  1.00154.20           N  
ANISOU 8417  NH2 ARG B 541    22320  17884  18385  -2397   -903    707       N  
ATOM   8418  N   ALA B 542      -7.713 -26.817  85.463  1.00 92.12           N  
ANISOU 8418  N   ALA B 542    12988  10661  11351   -902   -412    962       N  
ATOM   8419  CA  ALA B 542      -7.821 -27.227  84.075  1.00 88.56           C  
ANISOU 8419  CA  ALA B 542    12248  10505  10894   -829   -496   1016       C  
ATOM   8420  C   ALA B 542      -8.843 -26.361  83.332  1.00 90.51           C  
ANISOU 8420  C   ALA B 542    12347  10801  11239   -746   -355   1228       C  
ATOM   8421  O   ALA B 542      -8.657 -26.004  82.166  1.00 92.03           O  
ANISOU 8421  O   ALA B 542    12328  11219  11420   -734   -398   1345       O  
ATOM   8422  CB  ALA B 542      -8.200 -28.691  84.003  1.00 86.36           C  
ANISOU 8422  CB  ALA B 542    11898  10336  10577   -805   -586    891       C  
ATOM   8423  N   ARG B 543      -9.923 -26.028  84.021  1.00 93.43           N  
ANISOU 8423  N   ARG B 543    12818  10965  11717   -691   -176   1300       N  
ATOM   8424  CA  ARG B 543     -10.962 -25.181  83.476  1.00 95.06           C  
ANISOU 8424  CA  ARG B 543    12870  11175  12071   -595     -7   1557       C  
ATOM   8425  C   ARG B 543     -10.463 -23.763  83.258  1.00 96.78           C  
ANISOU 8425  C   ARG B 543    13109  11287  12374   -598    113   1699       C  
ATOM   8426  O   ARG B 543     -10.777 -23.142  82.235  1.00 97.92           O  
ANISOU 8426  O   ARG B 543    13012  11593  12600   -540    145   1937       O  
ATOM   8427  CB  ARG B 543     -12.201 -25.226  84.384  1.00 95.88           C  
ANISOU 8427  CB  ARG B 543    13085  11044  12299   -525    190   1600       C  
ATOM   8428  CG  ARG B 543     -13.014 -26.468  84.141  1.00 96.71           C  
ANISOU 8428  CG  ARG B 543    13050  11337  12359   -501     81   1572       C  
ATOM   8429  CD  ARG B 543     -13.725 -27.003  85.346  1.00103.97           C  
ANISOU 8429  CD  ARG B 543    14164  12023  13314   -482    182   1470       C  
ATOM   8430  NE  ARG B 543     -14.900 -26.259  85.738  1.00114.07           N  
ANISOU 8430  NE  ARG B 543    15448  13098  14794   -379    456   1675       N  
ATOM   8431  CZ  ARG B 543     -15.940 -26.727  86.448  1.00120.42           C  
ANISOU 8431  CZ  ARG B 543    16309  13774  15670   -328    571   1683       C  
ATOM   8432  NH1 ARG B 543     -16.046 -27.994  86.853  1.00111.90           N  
ANISOU 8432  NH1 ARG B 543    15285  12759  14473   -375    422   1498       N  
ATOM   8433  NH2 ARG B 543     -16.935 -25.881  86.741  1.00133.81           N  
ANISOU 8433  NH2 ARG B 543    17991  15259  17589   -217    868   1907       N  
ATOM   8434  N   SER B 544      -9.683 -23.259  84.209  1.00 99.65           N  
ANISOU 8434  N   SER B 544    13757  11394  12709   -688    175   1567       N  
ATOM   8435  CA  SER B 544      -9.190 -21.877  84.135  1.00105.69           C  
ANISOU 8435  CA  SER B 544    14595  12007  13555   -718    320   1676       C  
ATOM   8436  C   SER B 544      -8.114 -21.651  83.070  1.00104.91           C  
ANISOU 8436  C   SER B 544    14315  12172  13372   -761    132   1720       C  
ATOM   8437  O   SER B 544      -8.075 -20.568  82.464  1.00106.70           O  
ANISOU 8437  O   SER B 544    14444  12389  13707   -728    240   1914       O  
ATOM   8438  CB  SER B 544      -8.678 -21.419  85.495  1.00107.44           C  
ANISOU 8438  CB  SER B 544    15204  11887  13730   -863    443   1506       C  
ATOM   8439  OG  SER B 544      -7.566 -22.191  85.871  1.00112.49           O  
ANISOU 8439  OG  SER B 544    15937  12634  14167  -1005    191   1309       O  
ATOM   8440  N   THR B 545      -7.252 -22.657  82.850  1.00102.95           N  
ANISOU 8440  N   THR B 545    14018  12143  12954   -826   -121   1556       N  
ATOM   8441  CA  THR B 545      -6.181 -22.569  81.833  1.00102.46           C  
ANISOU 8441  CA  THR B 545    13781  12340  12807   -866   -290   1581       C  
ATOM   8442  C   THR B 545      -6.744 -22.528  80.421  1.00102.98           C  
ANISOU 8442  C   THR B 545    13522  12704  12899   -785   -315   1770       C  
ATOM   8443  O   THR B 545      -6.254 -21.761  79.592  1.00113.05           O  
ANISOU 8443  O   THR B 545    14662  14106  14185   -797   -330   1909       O  
ATOM   8444  CB  THR B 545      -5.112 -23.671  81.950  1.00 98.40           C  
ANISOU 8444  CB  THR B 545    13280  11961  12146   -942   -509   1382       C  
ATOM   8445  OG1 THR B 545      -5.757 -24.926  82.057  1.00104.61           O  
ANISOU 8445  OG1 THR B 545    14027  12817  12904   -894   -559   1275       O  
ATOM   8446  CG2 THR B 545      -4.242 -23.458  83.187  1.00 98.05           C  
ANISOU 8446  CG2 THR B 545    13512  11690  12052  -1077   -530   1272       C  
ATOM   8447  N   LEU B 546      -7.783 -23.298  80.149  1.00100.67           N  
ANISOU 8447  N   LEU B 546    13104  12535  12609   -728   -322   1795       N  
ATOM   8448  CA  LEU B 546      -8.473 -23.175  78.860  1.00102.24           C  
ANISOU 8448  CA  LEU B 546    12995  13034  12817   -698   -341   2022       C  
ATOM   8449  C   LEU B 546      -9.322 -21.918  78.702  1.00102.30           C  
ANISOU 8449  C   LEU B 546    12901  12934  13031   -612   -144   2350       C  
ATOM   8450  O   LEU B 546      -9.606 -21.512  77.583  1.00104.98           O  
ANISOU 8450  O   LEU B 546    12967  13533  13385   -609   -172   2600       O  
ATOM   8451  CB  LEU B 546      -9.321 -24.406  78.563  1.00103.57           C  
ANISOU 8451  CB  LEU B 546    13050  13399  12901   -709   -421   1964       C  
ATOM   8452  CG  LEU B 546      -8.550 -25.468  77.790  1.00105.34           C  
ANISOU 8452  CG  LEU B 546    13194  13906  12922   -808   -604   1765       C  
ATOM   8453  CD1 LEU B 546      -7.634 -26.296  78.721  1.00104.65           C  
ANISOU 8453  CD1 LEU B 546    13333  13639  12790   -824   -662   1466       C  
ATOM   8454  CD2 LEU B 546      -9.573 -26.323  77.061  1.00105.87           C  
ANISOU 8454  CD2 LEU B 546    13084  14243  12900   -863   -654   1806       C  
ATOM   8455  N   SER B 547      -9.771 -21.332  79.800  1.00105.02           N  
ANISOU 8455  N   SER B 547    13457  12903  13542   -548     72   2367       N  
ATOM   8456  CA  SER B 547     -10.491 -20.057  79.751  1.00110.22           C  
ANISOU 8456  CA  SER B 547    14045  13380  14454   -447    329   2680       C  
ATOM   8457  C   SER B 547      -9.545 -18.930  79.369  1.00112.23           C  
ANISOU 8457  C   SER B 547    14306  13589  14746   -482    365   2764       C  
ATOM   8458  O   SER B 547      -9.967 -17.915  78.838  1.00110.22           O  
ANISOU 8458  O   SER B 547    13883  13310  14686   -406    519   3080       O  
ATOM   8459  CB  SER B 547     -11.170 -19.768  81.094  1.00112.12           C  
ANISOU 8459  CB  SER B 547    14555  13184  14858   -386    604   2629       C  
ATOM   8460  OG  SER B 547     -12.192 -20.736  81.340  1.00114.61           O  
ANISOU 8460  OG  SER B 547    14814  13562  15169   -337    583   2615       O  
ATOM   8461  N   LYS B 548      -8.268 -19.130  79.665  1.00116.46           N  
ANISOU 8461  N   LYS B 548    15027  14112  15110   -599    224   2503       N  
ATOM   8462  CA  LYS B 548      -7.191 -18.205  79.270  1.00124.01           C  
ANISOU 8462  CA  LYS B 548    15990  15070  16057   -663    206   2550       C  
ATOM   8463  C   LYS B 548      -7.052 -17.977  77.751  1.00130.78           C  
ANISOU 8463  C   LYS B 548    16491  16311  16886   -650     78   2784       C  
ATOM   8464  O   LYS B 548      -6.519 -16.949  77.315  1.00137.96           O  
ANISOU 8464  O   LYS B 548    17349  17202  17867   -664    130   2936       O  
ATOM   8465  CB  LYS B 548      -5.850 -18.634  79.869  1.00123.28           C  
ANISOU 8465  CB  LYS B 548    16124  14943  15772   -806     43   2251       C  
ATOM   8466  CG  LYS B 548      -5.893 -18.492  81.364  1.00128.08           C  
ANISOU 8466  CG  LYS B 548    17099  15161  16401   -873    194   2076       C  
ATOM   8467  CD  LYS B 548      -4.707 -18.978  82.152  1.00134.62           C  
ANISOU 8467  CD  LYS B 548    18153  15953  17042  -1042     28   1824       C  
ATOM   8468  CE  LYS B 548      -4.988 -18.753  83.649  1.00142.72           C  
ANISOU 8468  CE  LYS B 548    19551  16597  18076  -1142    211   1684       C  
ATOM   8469  NZ  LYS B 548      -4.397 -19.822  84.519  1.00145.09           N  
ANISOU 8469  NZ  LYS B 548    20007  16928  18193  -1269     18   1460       N  
ATOM   8470  N   ILE B 549      -7.543 -18.910  76.944  1.00129.02           N  
ANISOU 8470  N   ILE B 549    16032  16439  16550   -647    -79   2817       N  
ATOM   8471  CA  ILE B 549      -7.578 -18.727  75.487  1.00127.06           C  
ANISOU 8471  CA  ILE B 549    15443  16588  16245   -675   -191   3059       C  
ATOM   8472  C   ILE B 549      -8.499 -17.555  75.187  1.00139.74           C  
ANISOU 8472  C   ILE B 549    16867  18114  18114   -573      9   3477       C  
ATOM   8473  O   ILE B 549      -9.649 -17.607  75.577  1.00140.75           O  
ANISOU 8473  O   ILE B 549    16960  18122  18395   -483    146   3618       O  
ATOM   8474  CB  ILE B 549      -8.083 -19.999  74.782  1.00117.49           C  
ANISOU 8474  CB  ILE B 549    14053  15747  14839   -740   -367   2999       C  
ATOM   8475  CG1 ILE B 549      -7.059 -21.102  75.028  1.00112.39           C  
ANISOU 8475  CG1 ILE B 549    13575  15145  13983   -823   -521   2606       C  
ATOM   8476  CG2 ILE B 549      -8.242 -19.775  73.290  1.00118.41           C  
ANISOU 8476  CG2 ILE B 549    13827  16297  14866   -818   -471   3270       C  
ATOM   8477  CD1 ILE B 549      -7.465 -22.476  74.573  1.00110.87           C  
ANISOU 8477  CD1 ILE B 549    13297  15218  13607   -898   -644   2456       C  
ATOM   8478  N   ASN B 550      -7.993 -16.511  74.512  1.00152.70           N  
ANISOU 8478  N   ASN B 550    18379  19810  19828   -579     38   3696       N  
ATOM   8479  CA  ASN B 550      -8.793 -15.284  74.242  1.00157.55           C  
ANISOU 8479  CA  ASN B 550    18806  20306  20749   -465    264   4139       C  
ATOM   8480  C   ASN B 550      -9.396 -15.322  72.856  1.00158.74           C  
ANISOU 8480  C   ASN B 550    18524  20929  20860   -498    130   4514       C  
ATOM   8481  O   ASN B 550      -8.911 -16.048  71.989  1.00166.42           O  
ANISOU 8481  O   ASN B 550    19376  22313  21543   -640   -125   4406       O  
ATOM   8482  CB  ASN B 550      -7.945 -14.006  74.320  1.00163.15           C  
ANISOU 8482  CB  ASN B 550    19618  20774  21598   -459    404   4208       C  
ATOM   8483  CG  ASN B 550      -7.072 -13.917  75.566  1.00168.05           C  
ANISOU 8483  CG  ASN B 550    20672  20999  22178   -513    485   3828       C  
ATOM   8484  OD1 ASN B 550      -6.136 -13.117  75.626  1.00165.60           O  
ANISOU 8484  OD1 ASN B 550    20483  20553  21884   -573    525   3794       O  
ATOM   8485  ND2 ASN B 550      -7.413 -14.674  76.588  1.00177.29           N  
ANISOU 8485  ND2 ASN B 550    22078  21982  23302   -509    518   3570       N  
ATOM   8486  N   GLU B 551     -10.407 -14.497  72.628  1.00142.19           N  
ANISOU 8486  N   GLU B 551    19138  20117  14767   -605    465   2389       N  
ATOM   8487  CA  GLU B 551     -10.897 -14.364  71.282  1.00141.83           C  
ANISOU 8487  CA  GLU B 551    19047  20134  14708   -614    474   2317       C  
ATOM   8488  C   GLU B 551      -9.787 -13.820  70.368  1.00138.57           C  
ANISOU 8488  C   GLU B 551    18655  19693  14303   -607    440   2309       C  
ATOM   8489  O   GLU B 551      -9.670 -14.284  69.230  1.00145.46           O  
ANISOU 8489  O   GLU B 551    19476  20578  15212   -637    458   2257       O  
ATOM   8490  CB  GLU B 551     -12.160 -13.517  71.201  1.00146.87           C  
ANISOU 8490  CB  GLU B 551    19676  20883  15242   -562    469   2295       C  
ATOM   8491  CG  GLU B 551     -12.892 -13.683  69.869  1.00149.72           C  
ANISOU 8491  CG  GLU B 551    19954  21352  15579   -573    492   2216       C  
ATOM   8492  CD  GLU B 551     -14.377 -13.358  69.944  1.00152.35           C  
ANISOU 8492  CD  GLU B 551    20236  21836  15812   -532    507   2190       C  
ATOM   8493  OE1 GLU B 551     -15.081 -13.951  70.790  1.00157.90           O  
ANISOU 8493  OE1 GLU B 551    20914  22562  16519   -567    535   2192       O  
ATOM   8494  OE2 GLU B 551     -14.848 -12.512  69.153  1.00146.98           O  
ANISOU 8494  OE2 GLU B 551    19541  21263  15040   -457    495   2171       O  
ATOM   8495  N   THR B 552      -8.953 -12.883  70.852  1.00124.11           N  
ANISOU 8495  N   THR B 552    16896  17826  12434   -581    398   2353       N  
ATOM   8496  CA  THR B 552      -7.829 -12.342  70.008  1.00119.42           C  
ANISOU 8496  CA  THR B 552    16324  17209  11841   -592    371   2343       C  
ATOM   8497  C   THR B 552      -6.823 -13.415  69.567  1.00110.28           C  
ANISOU 8497  C   THR B 552    15114  16011  10775   -635    381   2338       C  
ATOM   8498  O   THR B 552      -6.209 -13.327  68.497  1.00110.02           O  
ANISOU 8498  O   THR B 552    15063  15982  10758   -649    374   2308       O  
ATOM   8499  CB  THR B 552      -7.083 -11.188  70.686  1.00118.45           C  
ANISOU 8499  CB  THR B 552    16289  17059  11655   -586    337   2378       C  
ATOM   8500  OG1 THR B 552      -6.906 -11.532  72.042  1.00121.32           O  
ANISOU 8500  OG1 THR B 552    16660  17409  12025   -592    331   2424       O  
ATOM   8501  CG2 THR B 552      -7.891  -9.915  70.606  1.00121.38           C  
ANISOU 8501  CG2 THR B 552    16738  17451  11929   -532    341   2370       C  
ATOM   8502  N   MET B 553      -6.691 -14.437  70.384  1.00105.61           N  
ANISOU 8502  N   MET B 553    14504  15384  10239   -643    405   2374       N  
ATOM   8503  CA  MET B 553      -5.921 -15.605  70.030  1.00105.74           C  
ANISOU 8503  CA  MET B 553    14481  15354  10340   -661    436   2377       C  
ATOM   8504  C   MET B 553      -6.535 -16.326  68.818  1.00102.27           C  
ANISOU 8504  C   MET B 553    13991  14916   9948   -696    483   2301       C  
ATOM   8505  O   MET B 553      -5.838 -16.636  67.846  1.00105.77           O  
ANISOU 8505  O   MET B 553    14407  15348  10430   -711    489   2270       O  
ATOM   8506  CB  MET B 553      -5.878 -16.549  71.247  1.00111.15           C  
ANISOU 8506  CB  MET B 553    15175  15993  11062   -644    473   2441       C  
ATOM   8507  CG  MET B 553      -4.583 -17.335  71.426  1.00117.21           C  
ANISOU 8507  CG  MET B 553    15932  16723  11876   -617    486   2493       C  
ATOM   8508  SD  MET B 553      -4.534 -18.449  72.840  1.00119.57           S  
ANISOU 8508  SD  MET B 553    16252  16972  12206   -566    544   2588       S  
ATOM   8509  CE  MET B 553      -4.364 -17.225  74.149  1.00117.44           C  
ANISOU 8509  CE  MET B 553    16001  16787  11833   -544    466   2641       C  
ATOM   8510  N   LEU B 554      -7.813 -16.639  68.906  1.00 99.40           N  
ANISOU 8510  N   LEU B 554    13609  14581   9578   -717    522   2266       N  
ATOM   8511  CA  LEU B 554      -8.458 -17.464  67.901  1.00100.62           C  
ANISOU 8511  CA  LEU B 554    13706  14754   9769   -774    579   2182       C  
ATOM   8512  C   LEU B 554      -8.631 -16.702  66.601  1.00106.02           C  
ANISOU 8512  C   LEU B 554    14350  15529  10404   -769    548   2119       C  
ATOM   8513  O   LEU B 554      -8.490 -17.287  65.470  1.00112.13           O  
ANISOU 8513  O   LEU B 554    15074  16315  11216   -811    578   2051       O  
ATOM   8514  CB  LEU B 554      -9.821 -17.955  68.399  1.00 98.70           C  
ANISOU 8514  CB  LEU B 554    13441  14547   9513   -814    632   2153       C  
ATOM   8515  CG  LEU B 554      -9.831 -18.989  69.513  1.00 96.96           C  
ANISOU 8515  CG  LEU B 554    13259  14228   9350   -834    694   2202       C  
ATOM   8516  CD1 LEU B 554     -11.264 -19.259  69.864  1.00 97.73           C  
ANISOU 8516  CD1 LEU B 554    13327  14390   9414   -887    740   2161       C  
ATOM   8517  CD2 LEU B 554      -9.178 -20.332  69.174  1.00 97.09           C  
ANISOU 8517  CD2 LEU B 554    13293  14128   9467   -873    776   2191       C  
ATOM   8518  N   ARG B 555      -8.963 -15.417  66.772  1.00105.53           N  
ANISOU 8518  N   ARG B 555    14314  15529  10250   -713    496   2143       N  
ATOM   8519  CA  ARG B 555      -9.085 -14.475  65.678  1.00107.39           C  
ANISOU 8519  CA  ARG B 555    14536  15846  10419   -678    469   2111       C  
ATOM   8520  C   ARG B 555      -7.784 -14.459  64.829  1.00103.89           C  
ANISOU 8520  C   ARG B 555    14097  15357  10018   -692    450   2106       C  
ATOM   8521  O   ARG B 555      -7.840 -14.561  63.572  1.00103.43           O  
ANISOU 8521  O   ARG B 555    13984  15357   9957   -704    459   2047       O  
ATOM   8522  CB  ARG B 555      -9.427 -13.102  66.258  1.00112.84           C  
ANISOU 8522  CB  ARG B 555    15298  16563  11010   -603    433   2160       C  
ATOM   8523  CG  ARG B 555     -10.080 -12.171  65.271  1.00118.85           C  
ANISOU 8523  CG  ARG B 555    16049  17431  11676   -538    429   2134       C  
ATOM   8524  CD  ARG B 555     -10.389 -10.827  65.890  1.00121.15           C  
ANISOU 8524  CD  ARG B 555    16439  17720  11869   -451    413   2189       C  
ATOM   8525  NE  ARG B 555     -10.842  -9.967  64.799  1.00123.50           N  
ANISOU 8525  NE  ARG B 555    16739  18109  12075   -369    422   2176       N  
ATOM   8526  CZ  ARG B 555     -10.561  -8.678  64.648  1.00130.45           C  
ANISOU 8526  CZ  ARG B 555    17731  18952  12879   -296    422   2219       C  
ATOM   8527  NH1 ARG B 555      -9.780  -8.032  65.516  1.00135.93           N  
ANISOU 8527  NH1 ARG B 555    18546  19522  13578   -314    411   2263       N  
ATOM   8528  NH2 ARG B 555     -11.045  -8.028  63.589  1.00134.60           N  
ANISOU 8528  NH2 ARG B 555    18252  19571  13318   -205    441   2214       N  
ATOM   8529  N   LEU B 556      -6.630 -14.405  65.508  1.00 98.07           N  
ANISOU 8529  N   LEU B 556    13411  14537   9314   -692    425   2165       N  
ATOM   8530  CA  LEU B 556      -5.328 -14.587  64.844  1.00 98.48           C  
ANISOU 8530  CA  LEU B 556    13453  14557   9408   -711    412   2163       C  
ATOM   8531  C   LEU B 556      -5.185 -15.873  63.986  1.00 99.37           C  
ANISOU 8531  C   LEU B 556    13498  14655   9603   -749    459   2107       C  
ATOM   8532  O   LEU B 556      -4.646 -15.839  62.845  1.00102.58           O  
ANISOU 8532  O   LEU B 556    13872  15085  10018   -759    453   2068       O  
ATOM   8533  CB  LEU B 556      -4.216 -14.593  65.864  1.00101.47           C  
ANISOU 8533  CB  LEU B 556    13869  14882   9801   -707    388   2231       C  
ATOM   8534  CG  LEU B 556      -2.790 -14.437  65.353  1.00105.74           C  
ANISOU 8534  CG  LEU B 556    14401  15424  10350   -720    362   2239       C  
ATOM   8535  CD1 LEU B 556      -2.569 -12.987  64.969  1.00107.31           C  
ANISOU 8535  CD1 LEU B 556    14651  15654  10466   -727    326   2234       C  
ATOM   8536  CD2 LEU B 556      -1.806 -14.856  66.433  1.00106.93           C  
ANISOU 8536  CD2 LEU B 556    14554  15556  10515   -709    352   2303       C  
ATOM   8537  N   GLY B 557      -5.655 -16.998  64.510  1.00 97.56           N  
ANISOU 8537  N   GLY B 557    13257  14378   9431   -773    515   2100       N  
ATOM   8538  CA  GLY B 557      -5.663 -18.253  63.737  1.00 98.90           C  
ANISOU 8538  CA  GLY B 557    13384  14516   9675   -821    582   2034       C  
ATOM   8539  C   GLY B 557      -6.617 -18.203  62.545  1.00102.05           C  
ANISOU 8539  C   GLY B 557    13715  15016  10042   -865    601   1933       C  
ATOM   8540  O   GLY B 557      -6.309 -18.688  61.415  1.00103.77           O  
ANISOU 8540  O   GLY B 557    13889  15247  10291   -898    626   1865       O  
ATOM   8541  N   ILE B 558      -7.783 -17.586  62.769  1.00102.89           N  
ANISOU 8541  N   ILE B 558    13806  15214  10074   -857    588   1920       N  
ATOM   8542  CA  ILE B 558      -8.736 -17.373  61.663  1.00101.50           C  
ANISOU 8542  CA  ILE B 558    13547  15183   9833   -877    598   1831       C  
ATOM   8543  C   ILE B 558      -8.091 -16.543  60.548  1.00102.22           C  
ANISOU 8543  C   ILE B 558    13625  15329   9885   -833    551   1827       C  
ATOM   8544  O   ILE B 558      -8.196 -16.882  59.331  1.00109.15           O  
ANISOU 8544  O   ILE B 558    14428  16284  10760   -867    572   1746       O  
ATOM   8545  CB  ILE B 558     -10.038 -16.730  62.168  1.00 99.27           C  
ANISOU 8545  CB  ILE B 558    13248  15012   9455   -846    588   1836       C  
ATOM   8546  CG1 ILE B 558     -10.838 -17.765  62.918  1.00 99.97           C  
ANISOU 8546  CG1 ILE B 558    13321  15082   9581   -923    653   1805       C  
ATOM   8547  CG2 ILE B 558     -10.904 -16.218  61.032  1.00101.33           C  
ANISOU 8547  CG2 ILE B 558    13420  15464   9617   -826    583   1768       C  
ATOM   8548  CD1 ILE B 558     -11.681 -17.124  63.982  1.00102.71           C  
ANISOU 8548  CD1 ILE B 558    13690  15475   9857   -874    632   1857       C  
ATOM   8549  N   PHE B 559      -7.419 -15.466  60.948  1.00 97.82           N  
ANISOU 8549  N   PHE B 559    13140  14733   9293   -767    494   1909       N  
ATOM   8550  CA  PHE B 559      -6.713 -14.653  59.958  1.00 95.67           C  
ANISOU 8550  CA  PHE B 559    12873  14492   8984   -733    460   1914       C  
ATOM   8551  C   PHE B 559      -5.583 -15.446  59.289  1.00 93.14           C  
ANISOU 8551  C   PHE B 559    12524  14117   8747   -779    470   1886       C  
ATOM   8552  O   PHE B 559      -5.402 -15.371  58.074  1.00 93.74           O  
ANISOU 8552  O   PHE B 559    12550  14257   8807   -783    469   1837       O  
ATOM   8553  CB  PHE B 559      -6.200 -13.374  60.574  1.00 94.75           C  
ANISOU 8553  CB  PHE B 559    12855  14331   8812   -679    416   1997       C  
ATOM   8554  CG  PHE B 559      -7.205 -12.269  60.570  1.00 96.23           C  
ANISOU 8554  CG  PHE B 559    13075  14598   8890   -604    411   2015       C  
ATOM   8555  CD1 PHE B 559      -8.333 -12.332  61.348  1.00 98.29           C  
ANISOU 8555  CD1 PHE B 559    13330  14899   9117   -581    425   2019       C  
ATOM   8556  CD2 PHE B 559      -7.006 -11.144  59.788  1.00 99.40           C  
ANISOU 8556  CD2 PHE B 559    13521  15033   9213   -546    401   2034       C  
ATOM   8557  CE1 PHE B 559      -9.248 -11.291  61.357  1.00101.86           C  
ANISOU 8557  CE1 PHE B 559    13813  15432   9454   -488    426   2043       C  
ATOM   8558  CE2 PHE B 559      -7.912 -10.091  59.781  1.00100.60           C  
ANISOU 8558  CE2 PHE B 559    13721  15250   9253   -449    411   2064       C  
ATOM   8559  CZ  PHE B 559      -9.050 -10.163  60.565  1.00102.09           C  
ANISOU 8559  CZ  PHE B 559    13896  15489   9403   -413    422   2069       C  
ATOM   8560  N   GLY B 560      -4.862 -16.235  60.072  1.00 90.55           N  
ANISOU 8560  N   GLY B 560    12225  13681   8499   -801    484   1918       N  
ATOM   8561  CA  GLY B 560      -3.804 -17.084  59.514  1.00 88.99           C  
ANISOU 8561  CA  GLY B 560    12004  13432   8376   -825    504   1898       C  
ATOM   8562  C   GLY B 560      -4.304 -18.020  58.459  1.00 88.87           C  
ANISOU 8562  C   GLY B 560    11919  13452   8395   -877    562   1795       C  
ATOM   8563  O   GLY B 560      -3.730 -18.101  57.379  1.00 89.86           O  
ANISOU 8563  O   GLY B 560    12004  13608   8528   -885    559   1754       O  
ATOM   8564  N   PHE B 561      -5.403 -18.709  58.749  1.00 92.97           N  
ANISOU 8564  N   PHE B 561    12419  13977   8926   -924    618   1745       N  
ATOM   8565  CA  PHE B 561      -5.971 -19.604  57.718  1.00 97.59           C  
ANISOU 8565  CA  PHE B 561    12933  14614   9531  -1001    685   1624       C  
ATOM   8566  C   PHE B 561      -6.512 -18.802  56.538  1.00100.62           C  
ANISOU 8566  C   PHE B 561    13236  15173   9822   -991    649   1566       C  
ATOM   8567  O   PHE B 561      -6.331 -19.206  55.355  1.00102.00           O  
ANISOU 8567  O   PHE B 561    13347  15403  10004  -1029    672   1483       O  
ATOM   8568  CB  PHE B 561      -7.047 -20.544  58.286  1.00 98.97           C  
ANISOU 8568  CB  PHE B 561    13105  14766   9729  -1080    766   1570       C  
ATOM   8569  CG  PHE B 561      -6.487 -21.734  59.035  1.00 99.39           C  
ANISOU 8569  CG  PHE B 561    13237  14638   9887  -1101    843   1598       C  
ATOM   8570  CD1 PHE B 561      -5.874 -22.782  58.353  1.00 96.84           C  
ANISOU 8570  CD1 PHE B 561    12923  14231   9638  -1140    917   1540       C  
ATOM   8571  CD2 PHE B 561      -6.589 -21.799  60.466  1.00101.75           C  
ANISOU 8571  CD2 PHE B 561    13608  14848  10203  -1070    848   1690       C  
ATOM   8572  CE1 PHE B 561      -5.352 -23.858  59.072  1.00 98.71           C  
ANISOU 8572  CE1 PHE B 561    13250  14291   9962  -1132   1001   1583       C  
ATOM   8573  CE2 PHE B 561      -6.078 -22.888  61.187  1.00100.43           C  
ANISOU 8573  CE2 PHE B 561    13520  14517  10121  -1066    928   1733       C  
ATOM   8574  CZ  PHE B 561      -5.449 -23.919  60.486  1.00100.46           C  
ANISOU 8574  CZ  PHE B 561    13544  14430  10196  -1090   1008   1684       C  
ATOM   8575  N   LEU B 562      -7.145 -17.658  56.839  1.00106.07           N  
ANISOU 8575  N   LEU B 562    13930  15952  10418   -929    598   1614       N  
ATOM   8576  CA  LEU B 562      -7.659 -16.811  55.725  1.00113.36           C  
ANISOU 8576  CA  LEU B 562    14785  17051  11236   -887    571   1580       C  
ATOM   8577  C   LEU B 562      -6.543 -16.359  54.753  1.00114.30           C  
ANISOU 8577  C   LEU B 562    14907  17163  11356   -855    538   1595       C  
ATOM   8578  O   LEU B 562      -6.697 -16.416  53.516  1.00113.48           O  
ANISOU 8578  O   LEU B 562    14720  17180  11214   -864    547   1524       O  
ATOM   8579  CB  LEU B 562      -8.479 -15.608  56.218  1.00117.17           C  
ANISOU 8579  CB  LEU B 562    15293  17618  11608   -797    535   1643       C  
ATOM   8580  CG  LEU B 562      -9.958 -15.976  56.471  1.00125.75           C  
ANISOU 8580  CG  LEU B 562    16266  18932  12580   -782    554   1570       C  
ATOM   8581  CD1 LEU B 562     -10.153 -16.967  57.629  1.00128.62           C  
ANISOU 8581  CD1 LEU B 562    16554  19359  12957   -884    611   1479       C  
ATOM   8582  CD2 LEU B 562     -10.798 -14.755  56.771  1.00129.84           C  
ANISOU 8582  CD2 LEU B 562    16819  19540  12972   -651    521   1648       C  
ATOM   8583  N   ALA B 563      -5.420 -15.931  55.329  1.00113.24           N  
ANISOU 8583  N   ALA B 563    14860  16903  11260   -824    501   1683       N  
ATOM   8584  CA  ALA B 563      -4.198 -15.609  54.557  1.00107.75           C  
ANISOU 8584  CA  ALA B 563    14173  16189  10576   -812    474   1700       C  
ATOM   8585  C   ALA B 563      -3.578 -16.848  53.869  1.00103.60           C  
ANISOU 8585  C   ALA B 563    13592  15633  10137   -871    512   1626       C  
ATOM   8586  O   ALA B 563      -3.197 -16.772  52.700  1.00105.15           O  
ANISOU 8586  O   ALA B 563    13736  15897  10316   -873    508   1584       O  
ATOM   8587  CB  ALA B 563      -3.182 -14.904  55.454  1.00103.38           C  
ANISOU 8587  CB  ALA B 563    13717  15532  10031   -785    432   1799       C  
ATOM   8588  N   PHE B 564      -3.531 -17.980  54.578  1.00100.54           N  
ANISOU 8588  N   PHE B 564    13223  15142   9836   -914    560   1612       N  
ATOM   8589  CA  PHE B 564      -3.042 -19.230  53.985  1.00101.03           C  
ANISOU 8589  CA  PHE B 564    13254  15153   9979   -963    619   1541       C  
ATOM   8590  C   PHE B 564      -3.786 -19.637  52.691  1.00102.97           C  
ANISOU 8590  C   PHE B 564    13405  15523  10197  -1023    660   1411       C  
ATOM   8591  O   PHE B 564      -3.179 -20.125  51.689  1.00103.14           O  
ANISOU 8591  O   PHE B 564    13385  15555  10245  -1044    681   1350       O  
ATOM   8592  CB  PHE B 564      -3.170 -20.374  54.994  1.00101.98           C  
ANISOU 8592  CB  PHE B 564    13427  15138  10182   -993    689   1546       C  
ATOM   8593  CG  PHE B 564      -2.585 -21.666  54.514  1.00104.82           C  
ANISOU 8593  CG  PHE B 564    13790  15409  10625  -1027    769   1487       C  
ATOM   8594  CD1 PHE B 564      -1.255 -21.948  54.736  1.00103.21           C  
ANISOU 8594  CD1 PHE B 564    13627  15115  10470   -965    764   1555       C  
ATOM   8595  CD2 PHE B 564      -3.349 -22.589  53.772  1.00107.08           C  
ANISOU 8595  CD2 PHE B 564    14036  15716  10931  -1121    856   1355       C  
ATOM   8596  CE1 PHE B 564      -0.700 -23.139  54.265  1.00105.11           C  
ANISOU 8596  CE1 PHE B 564    13882  15271  10783   -974    848   1506       C  
ATOM   8597  CE2 PHE B 564      -2.780 -23.770  53.285  1.00106.07           C  
ANISOU 8597  CE2 PHE B 564    13930  15489  10880  -1151    945   1294       C  
ATOM   8598  CZ  PHE B 564      -1.459 -24.054  53.544  1.00103.72           C  
ANISOU 8598  CZ  PHE B 564    13688  15084  10636  -1067    943   1376       C  
ATOM   8599  N   GLY B 565      -5.104 -19.459  52.723  1.00105.15           N  
ANISOU 8599  N   GLY B 565    13636  15908  10409  -1050    672   1364       N  
ATOM   8600  CA  GLY B 565      -5.918 -19.783  51.539  1.00108.06           C  
ANISOU 8600  CA  GLY B 565    13891  16440  10723  -1112    709   1234       C  
ATOM   8601  C   GLY B 565      -5.538 -18.994  50.295  1.00107.78           C  
ANISOU 8601  C   GLY B 565    13795  16538  10617  -1059    660   1229       C  
ATOM   8602  O   GLY B 565      -5.340 -19.548  49.194  1.00106.15           O  
ANISOU 8602  O   GLY B 565    13518  16394  10417  -1108    690   1133       O  
ATOM   8603  N   PHE B 566      -5.430 -17.687  50.479  1.00108.87           N  
ANISOU 8603  N   PHE B 566    13969  16711  10683   -961    591   1332       N  
ATOM   8604  CA  PHE B 566      -4.966 -16.795  49.406  1.00112.48           C  
ANISOU 8604  CA  PHE B 566    14398  17268  11070   -897    550   1354       C  
ATOM   8605  C   PHE B 566      -3.562 -17.149  48.863  1.00109.79           C  
ANISOU 8605  C   PHE B 566    14071  16839  10803   -914    544   1354       C  
ATOM   8606  O   PHE B 566      -3.303 -17.134  47.656  1.00110.43           O  
ANISOU 8606  O   PHE B 566    14082  17020  10853   -916    544   1302       O  
ATOM   8607  CB  PHE B 566      -4.997 -15.342  49.908  1.00114.29           C  
ANISOU 8607  CB  PHE B 566    14708  17495  11220   -794    498   1476       C  
ATOM   8608  CG  PHE B 566      -6.399 -14.759  50.043  1.00117.79           C  
ANISOU 8608  CG  PHE B 566    15118  18084  11550   -736    502   1479       C  
ATOM   8609  CD1 PHE B 566      -7.321 -14.826  48.995  1.00116.32           C  
ANISOU 8609  CD1 PHE B 566    14805  18121  11267   -725    522   1397       C  
ATOM   8610  CD2 PHE B 566      -6.793 -14.107  51.211  1.00118.63           C  
ANISOU 8610  CD2 PHE B 566    15314  18126  11632   -684    487   1563       C  
ATOM   8611  CE1 PHE B 566      -8.596 -14.298  49.136  1.00113.89           C  
ANISOU 8611  CE1 PHE B 566    14454  17977  10839   -656    526   1405       C  
ATOM   8612  CE2 PHE B 566      -8.076 -13.553  51.326  1.00115.64           C  
ANISOU 8612  CE2 PHE B 566    14903  17895  11139   -613    493   1571       C  
ATOM   8613  CZ  PHE B 566      -8.965 -13.642  50.284  1.00111.23           C  
ANISOU 8613  CZ  PHE B 566    14213  17568  10481   -593    512   1495       C  
ATOM   8614  N   VAL B 567      -2.670 -17.491  49.781  1.00111.47           N  
ANISOU 8614  N   VAL B 567    14365  16881  11105   -922    540   1413       N  
ATOM   8615  CA  VAL B 567      -1.313 -17.914  49.435  1.00108.96           C  
ANISOU 8615  CA  VAL B 567    14057  16487  10853   -928    538   1420       C  
ATOM   8616  C   VAL B 567      -1.406 -19.185  48.593  1.00107.17           C  
ANISOU 8616  C   VAL B 567    13762  16278  10679   -993    605   1296       C  
ATOM   8617  O   VAL B 567      -0.745 -19.297  47.535  1.00108.16           O  
ANISOU 8617  O   VAL B 567    13839  16454  10803   -995    604   1255       O  
ATOM   8618  CB  VAL B 567      -0.441 -18.083  50.714  1.00107.92           C  
ANISOU 8618  CB  VAL B 567    14014  16201  10789   -910    527   1511       C  
ATOM   8619  CG1 VAL B 567       0.924 -18.706  50.421  1.00106.31           C  
ANISOU 8619  CG1 VAL B 567    13806  15938  10646   -904    535   1516       C  
ATOM   8620  CG2 VAL B 567      -0.246 -16.714  51.364  1.00108.07           C  
ANISOU 8620  CG2 VAL B 567    14099  16219  10742   -864    464   1616       C  
ATOM   8621  N   LEU B 568      -2.247 -20.119  49.034  1.00105.56           N  
ANISOU 8621  N   LEU B 568    13557  16035  10515  -1056    672   1229       N  
ATOM   8622  CA  LEU B 568      -2.444 -21.337  48.242  1.00107.58           C  
ANISOU 8622  CA  LEU B 568    13762  16299  10814  -1140    756   1092       C  
ATOM   8623  C   LEU B 568      -3.021 -21.056  46.835  1.00112.05           C  
ANISOU 8623  C   LEU B 568    14206  17076  11290  -1170    750    990       C  
ATOM   8624  O   LEU B 568      -2.672 -21.757  45.877  1.00116.93           O  
ANISOU 8624  O   LEU B 568    14777  17718  11933  -1217    794    893       O  
ATOM   8625  CB  LEU B 568      -3.340 -22.311  49.003  1.00108.88           C  
ANISOU 8625  CB  LEU B 568    13959  16385  11025  -1222    841   1034       C  
ATOM   8626  CG  LEU B 568      -3.413 -23.750  48.494  1.00108.28           C  
ANISOU 8626  CG  LEU B 568    13881  16243  11016  -1326    959    898       C  
ATOM   8627  CD1 LEU B 568      -2.119 -24.530  48.680  1.00109.19           C  
ANISOU 8627  CD1 LEU B 568    14085  16169  11233  -1282   1003    940       C  
ATOM   8628  CD2 LEU B 568      -4.524 -24.450  49.238  1.00109.30           C  
ANISOU 8628  CD2 LEU B 568    14038  16327  11161  -1423   1043    839       C  
ATOM   8629  N   ILE B 569      -3.906 -20.050  46.708  1.00111.52           N  
ANISOU 8629  N   ILE B 569    14088  17171  11112  -1133    702   1011       N  
ATOM   8630  CA  ILE B 569      -4.432 -19.617  45.371  1.00109.11           C  
ANISOU 8630  CA  ILE B 569    13659  17101  10696  -1127    689    938       C  
ATOM   8631  C   ILE B 569      -3.314 -18.989  44.504  1.00107.84           C  
ANISOU 8631  C   ILE B 569    13494  16959  10519  -1059    639    989       C  
ATOM   8632  O   ILE B 569      -3.074 -19.409  43.372  1.00103.96           O  
ANISOU 8632  O   ILE B 569    12923  16557  10017  -1093    661    899       O  
ATOM   8633  CB  ILE B 569      -5.587 -18.566  45.502  1.00109.13           C  
ANISOU 8633  CB  ILE B 569    13620  17279  10566  -1060    651    979       C  
ATOM   8634  CG1 ILE B 569      -6.791 -19.027  46.367  1.00108.00           C  
ANISOU 8634  CG1 ILE B 569    13464  17156  10413  -1122    692    934       C  
ATOM   8635  CG2 ILE B 569      -6.080 -18.134  44.126  1.00110.15           C  
ANISOU 8635  CG2 ILE B 569    13615  17668  10565  -1030    642    917       C  
ATOM   8636  CD1 ILE B 569      -7.406 -20.360  45.994  1.00110.51           C  
ANISOU 8636  CD1 ILE B 569    13704  17527  10758  -1275    782    762       C  
ATOM   8637  N   THR B 570      -2.623 -17.983  45.064  1.00113.05           N  
ANISOU 8637  N   THR B 570    14243  17535  11173   -973    579   1130       N  
ATOM   8638  CA  THR B 570      -1.442 -17.322  44.403  1.00110.53           C  
ANISOU 8638  CA  THR B 570    13939  17213  10841   -922    536   1191       C  
ATOM   8639  C   THR B 570      -0.470 -18.377  43.912  1.00110.77           C  
ANISOU 8639  C   THR B 570    13947  17176  10962   -974    567   1124       C  
ATOM   8640  O   THR B 570      -0.132 -18.388  42.728  1.00111.13           O  
ANISOU 8640  O   THR B 570    13921  17326  10976   -975    567   1073       O  
ATOM   8641  CB  THR B 570      -0.674 -16.385  45.380  1.00110.73           C  
ANISOU 8641  CB  THR B 570    14085  17108  10877   -868    487   1334       C  
ATOM   8642  OG1 THR B 570      -1.536 -15.318  45.765  1.00114.61           O  
ANISOU 8642  OG1 THR B 570    14615  17654  11278   -807    467   1398       O  
ATOM   8643  CG2 THR B 570       0.567 -15.785  44.776  1.00109.80           C  
ANISOU 8643  CG2 THR B 570    13984  16987  10745   -844    454   1385       C  
ATOM   8644  N   PHE B 571      -0.033 -19.265  44.822  1.00107.89           N  
ANISOU 8644  N   PHE B 571    13647  16641  10703  -1004    600   1130       N  
ATOM   8645  CA  PHE B 571       0.889 -20.335  44.448  1.00103.80           C  
ANISOU 8645  CA  PHE B 571    13124  16043  10269  -1031    644   1076       C  
ATOM   8646  C   PHE B 571       0.439 -21.079  43.180  1.00103.08           C  
ANISOU 8646  C   PHE B 571    12936  16065  10164  -1097    701    924       C  
ATOM   8647  O   PHE B 571       1.203 -21.203  42.219  1.00104.65           O  
ANISOU 8647  O   PHE B 571    13090  16311  10361  -1088    698    891       O  
ATOM   8648  CB  PHE B 571       1.058 -21.311  45.586  1.00101.17           C  
ANISOU 8648  CB  PHE B 571    12876  15528  10037  -1045    699   1093       C  
ATOM   8649  CG  PHE B 571       2.020 -22.396  45.279  1.00 99.76           C  
ANISOU 8649  CG  PHE B 571    12711  15254   9936  -1044    757   1054       C  
ATOM   8650  CD1 PHE B 571       3.374 -22.169  45.347  1.00 99.50           C  
ANISOU 8650  CD1 PHE B 571    12697  15189   9917   -973    716   1139       C  
ATOM   8651  CD2 PHE B 571       1.568 -23.640  44.898  1.00100.58           C  
ANISOU 8651  CD2 PHE B 571    12812  15312  10092  -1116    861    926       C  
ATOM   8652  CE1 PHE B 571       4.272 -23.170  45.030  1.00100.44           C  
ANISOU 8652  CE1 PHE B 571    12826  15237  10098   -949    774   1108       C  
ATOM   8653  CE2 PHE B 571       2.453 -24.653  44.606  1.00101.42           C  
ANISOU 8653  CE2 PHE B 571    12949  15315  10267  -1099    930    893       C  
ATOM   8654  CZ  PHE B 571       3.810 -24.419  44.668  1.00100.89           C  
ANISOU 8654  CZ  PHE B 571    12896  15224  10211  -1003    884    989       C  
ATOM   8655  N   SER B 572      -0.801 -21.538  43.187  1.00103.05           N  
ANISOU 8655  N   SER B 572    12893  16120  10139  -1169    752    827       N  
ATOM   8656  CA  SER B 572      -1.346 -22.289  42.068  1.00107.23           C  
ANISOU 8656  CA  SER B 572    13324  16773  10643  -1257    815    662       C  
ATOM   8657  C   SER B 572      -1.390 -21.491  40.770  1.00110.85           C  
ANISOU 8657  C   SER B 572    13668  17457  10991  -1222    764    640       C  
ATOM   8658  O   SER B 572      -1.214 -22.057  39.680  1.00116.68           O  
ANISOU 8658  O   SER B 572    14330  18279  11721  -1270    801    526       O  
ATOM   8659  CB  SER B 572      -2.751 -22.772  42.385  1.00109.47           C  
ANISOU 8659  CB  SER B 572    13575  17117  10901  -1354    875    563       C  
ATOM   8660  OG  SER B 572      -2.836 -23.300  43.680  1.00110.94           O  
ANISOU 8660  OG  SER B 572    13872  17107  11173  -1374    916    608       O  
ATOM   8661  N   CYS B 573      -1.668 -20.186  40.860  1.00112.46           N  
ANISOU 8661  N   CYS B 573    13865  17762  11102  -1134    688    747       N  
ATOM   8662  CA  CYS B 573      -1.644 -19.309  39.647  1.00114.45           C  
ANISOU 8662  CA  CYS B 573    14026  18219  11238  -1074    644    755       C  
ATOM   8663  C   CYS B 573      -0.229 -19.189  39.016  1.00112.36           C  
ANISOU 8663  C   CYS B 573    13779  17903  11010  -1040    619    794       C  
ATOM   8664  O   CYS B 573      -0.056 -19.430  37.820  1.00108.35           O  
ANISOU 8664  O   CYS B 573    13178  17525  10465  -1058    632    710       O  
ATOM   8665  CB  CYS B 573      -2.220 -17.923  39.953  1.00113.10           C  
ANISOU 8665  CB  CYS B 573    13877  18135  10960   -971    589    875       C  
ATOM   8666  SG  CYS B 573      -3.997 -17.925  40.265  1.00113.64           S  
ANISOU 8666  SG  CYS B 573    13870  18374  10931   -987    614    815       S  
ATOM   8667  N   HIS B 574       0.761 -18.912  39.866  1.00112.91           N  
ANISOU 8667  N   HIS B 574    13957  17792  11148  -1002    588    909       N  
ATOM   8668  CA  HIS B 574       2.169 -18.903  39.456  1.00114.89           C  
ANISOU 8668  CA  HIS B 574    14224  17990  11437   -980    568    946       C  
ATOM   8669  C   HIS B 574       2.654 -20.247  38.941  1.00112.92           C  
ANISOU 8669  C   HIS B 574    13938  17699  11267  -1035    629    830       C  
ATOM   8670  O   HIS B 574       3.441 -20.296  37.960  1.00111.84           O  
ANISOU 8670  O   HIS B 574    13748  17628  11117  -1024    623    803       O  
ATOM   8671  CB  HIS B 574       3.085 -18.400  40.599  1.00115.12           C  
ANISOU 8671  CB  HIS B 574    14365  17860  11512   -941    527   1083       C  
ATOM   8672  CG  HIS B 574       2.901 -16.944  40.903  1.00116.70           C  
ANISOU 8672  CG  HIS B 574    14618  18093  11627   -889    475   1198       C  
ATOM   8673  ND1 HIS B 574       3.338 -15.925  40.067  1.00121.45           N  
ANISOU 8673  ND1 HIS B 574    15208  18791  12145   -851    444   1248       N  
ATOM   8674  CD2 HIS B 574       2.276 -16.337  41.932  1.00116.22           C  
ANISOU 8674  CD2 HIS B 574    14632  17976  11548   -867    460   1270       C  
ATOM   8675  CE1 HIS B 574       3.001 -14.757  40.586  1.00118.94           C  
ANISOU 8675  CE1 HIS B 574    14970  18458  11762   -808    421   1347       C  
ATOM   8676  NE2 HIS B 574       2.348 -14.979  41.715  1.00117.16           N  
ANISOU 8676  NE2 HIS B 574    14795  18146  11574   -815    427   1360       N  
ATOM   8677  N   PHE B 575       2.168 -21.312  39.588  1.00111.84           N  
ANISOU 8677  N   PHE B 575    13836  17451  11206  -1093    697    761       N  
ATOM   8678  CA  PHE B 575       2.464 -22.681  39.189  1.00116.51           C  
ANISOU 8678  CA  PHE B 575    14421  17971  11873  -1150    784    640       C  
ATOM   8679  C   PHE B 575       1.865 -22.984  37.817  1.00118.74           C  
ANISOU 8679  C   PHE B 575    14582  18440  12091  -1217    819    487       C  
ATOM   8680  O   PHE B 575       2.560 -23.549  36.955  1.00127.55           O  
ANISOU 8680  O   PHE B 575    15664  19569  13227  -1227    851    416       O  
ATOM   8681  CB  PHE B 575       1.923 -23.663  40.223  1.00122.24           C  
ANISOU 8681  CB  PHE B 575    15232  18530  12683  -1204    865    605       C  
ATOM   8682  CG  PHE B 575       2.371 -25.079  40.003  1.00130.63           C  
ANISOU 8682  CG  PHE B 575    16337  19462  13835  -1246    975    505       C  
ATOM   8683  CD1 PHE B 575       1.652 -25.930  39.135  1.00137.60           C  
ANISOU 8683  CD1 PHE B 575    17164  20410  14707  -1361   1066    322       C  
ATOM   8684  CD2 PHE B 575       3.496 -25.574  40.649  1.00129.78           C  
ANISOU 8684  CD2 PHE B 575    16325  19175  13810  -1169    997    589       C  
ATOM   8685  CE1 PHE B 575       2.057 -27.248  38.918  1.00139.12           C  
ANISOU 8685  CE1 PHE B 575    17419  20458  14980  -1404   1188    222       C  
ATOM   8686  CE2 PHE B 575       3.904 -26.887  40.428  1.00134.95           C  
ANISOU 8686  CE2 PHE B 575    17037  19697  14540  -1185   1115    503       C  
ATOM   8687  CZ  PHE B 575       3.184 -27.729  39.566  1.00137.12           C  
ANISOU 8687  CZ  PHE B 575    17278  20005  14814  -1305   1216    319       C  
ATOM   8688  N   TYR B 576       0.604 -22.594  37.619  1.00116.22           N  
ANISOU 8688  N   TYR B 576    14190  18282  11683  -1256    812    437       N  
ATOM   8689  CA  TYR B 576      -0.066 -22.744  36.334  1.00116.64           C  
ANISOU 8689  CA  TYR B 576    14104  18567  11644  -1316    837    294       C  
ATOM   8690  C   TYR B 576       0.673 -21.960  35.274  1.00115.73           C  
ANISOU 8690  C   TYR B 576    13922  18588  11460  -1237    773    342       C  
ATOM   8691  O   TYR B 576       0.946 -22.493  34.219  1.00116.98           O  
ANISOU 8691  O   TYR B 576    14005  18835  11607  -1277    807    231       O  
ATOM   8692  CB  TYR B 576      -1.514 -22.255  36.423  1.00123.10           C  
ANISOU 8692  CB  TYR B 576    14846  19570  12353  -1339    826    266       C  
ATOM   8693  CG  TYR B 576      -2.241 -22.125  35.096  1.00131.05           C  
ANISOU 8693  CG  TYR B 576    15684  20884  13225  -1370    831    146       C  
ATOM   8694  CD1 TYR B 576      -2.871 -23.224  34.520  1.00133.70           C  
ANISOU 8694  CD1 TYR B 576    15934  21314  13549  -1516    921    -58       C  
ATOM   8695  CD2 TYR B 576      -2.299 -20.892  34.421  1.00134.85           C  
ANISOU 8695  CD2 TYR B 576    16093  21565  13578  -1252    755    236       C  
ATOM   8696  CE1 TYR B 576      -3.524 -23.119  33.303  1.00136.91           C  
ANISOU 8696  CE1 TYR B 576    16169  22033  13817  -1550    925   -176       C  
ATOM   8697  CE2 TYR B 576      -2.917 -20.780  33.182  1.00139.07           C  
ANISOU 8697  CE2 TYR B 576    16463  22401  13974  -1262    761    135       C  
ATOM   8698  CZ  TYR B 576      -3.549 -21.890  32.634  1.00142.13           C  
ANISOU 8698  CZ  TYR B 576    16746  22907  14347  -1412    841    -74       C  
ATOM   8699  OH  TYR B 576      -4.185 -21.791  31.412  1.00148.95           O  
ANISOU 8699  OH  TYR B 576    17430  24105  15059  -1428    846   -184       O  
ATOM   8700  N   ASP B 577       1.019 -20.697  35.561  1.00118.38           N  
ANISOU 8700  N   ASP B 577    14297  18932  11750  -1132    690    504       N  
ATOM   8701  CA  ASP B 577       1.778 -19.863  34.591  1.00117.46           C  
ANISOU 8701  CA  ASP B 577    14135  18930  11565  -1059    637    565       C  
ATOM   8702  C   ASP B 577       3.163 -20.417  34.292  1.00114.97           C  
ANISOU 8702  C   ASP B 577    13844  18507  11332  -1061    646    559       C  
ATOM   8703  O   ASP B 577       3.629 -20.307  33.182  1.00117.95           O  
ANISOU 8703  O   ASP B 577    14145  19007  11661  -1048    637    525       O  
ATOM   8704  CB  ASP B 577       1.937 -18.415  35.054  1.00118.70           C  
ANISOU 8704  CB  ASP B 577    14361  19076  11661   -960    568    740       C  
ATOM   8705  CG  ASP B 577       0.599 -17.637  35.044  1.00123.68           C  
ANISOU 8705  CG  ASP B 577    14953  19869  12171   -915    557    762       C  
ATOM   8706  OD1 ASP B 577      -0.332 -17.882  34.232  1.00120.95           O  
ANISOU 8706  OD1 ASP B 577    14480  19737  11736   -935    582    655       O  
ATOM   8707  OD2 ASP B 577       0.461 -16.753  35.890  1.00134.86           O  
ANISOU 8707  OD2 ASP B 577    16463  21207  13569   -854    527    887       O  
ATOM   8708  N   PHE B 578       3.810 -21.020  35.280  1.00116.39           N  
ANISOU 8708  N   PHE B 578    14125  18470  11625  -1068    666    595       N  
ATOM   8709  CA  PHE B 578       5.096 -21.687  35.079  1.00120.75           C  
ANISOU 8709  CA  PHE B 578    14698  18928  12251  -1055    686    587       C  
ATOM   8710  C   PHE B 578       4.982 -22.957  34.232  1.00126.76           C  
ANISOU 8710  C   PHE B 578    15404  19712  13046  -1122    773    413       C  
ATOM   8711  O   PHE B 578       5.719 -23.114  33.252  1.00131.04           O  
ANISOU 8711  O   PHE B 578    15888  20329  13572  -1108    774    372       O  
ATOM   8712  CB  PHE B 578       5.709 -22.017  36.424  1.00119.77           C  
ANISOU 8712  CB  PHE B 578    14692  18590  12223  -1025    693    677       C  
ATOM   8713  CG  PHE B 578       6.987 -22.775  36.337  1.00119.18           C  
ANISOU 8713  CG  PHE B 578    14640  18427  12216   -989    722    677       C  
ATOM   8714  CD1 PHE B 578       8.133 -22.132  35.948  1.00117.93           C  
ANISOU 8714  CD1 PHE B 578    14452  18332  12020   -935    662    755       C  
ATOM   8715  CD2 PHE B 578       7.054 -24.127  36.666  1.00118.71           C  
ANISOU 8715  CD2 PHE B 578    14636  18219  12248  -1003    818    603       C  
ATOM   8716  CE1 PHE B 578       9.321 -22.829  35.866  1.00118.55           C  
ANISOU 8716  CE1 PHE B 578    14539  18358  12147   -889    688    758       C  
ATOM   8717  CE2 PHE B 578       8.246 -24.823  36.599  1.00117.54           C  
ANISOU 8717  CE2 PHE B 578    14514  17996  12150   -941    853    615       C  
ATOM   8718  CZ  PHE B 578       9.382 -24.170  36.193  1.00117.69           C  
ANISOU 8718  CZ  PHE B 578    14484  18107  12125   -879    782    693       C  
ATOM   8719  N   PHE B 579       4.021 -23.811  34.573  1.00134.72           N  
ANISOU 8719  N   PHE B 579    16430  20666  14090  -1204    850    306       N  
ATOM   8720  CA  PHE B 579       3.745 -25.046  33.809  1.00143.01           C  
ANISOU 8720  CA  PHE B 579    17441  21729  15164  -1299    955    116       C  
ATOM   8721  C   PHE B 579       3.340 -24.830  32.344  1.00136.39           C  
ANISOU 8721  C   PHE B 579    16450  21152  14217  -1340    946      0       C  
ATOM   8722  O   PHE B 579       3.535 -25.725  31.539  1.00136.12           O  
ANISOU 8722  O   PHE B 579    16382  21137  14200  -1400   1020   -141       O  
ATOM   8723  CB  PHE B 579       2.671 -25.869  34.548  1.00158.43           C  
ANISOU 8723  CB  PHE B 579    19451  23582  17163  -1402   1046     26       C  
ATOM   8724  CG  PHE B 579       2.355 -27.229  33.945  1.00173.12           C  
ANISOU 8724  CG  PHE B 579    21308  25411  19058  -1527   1181   -179       C  
ATOM   8725  CD1 PHE B 579       3.038 -28.365  34.373  1.00176.82           C  
ANISOU 8725  CD1 PHE B 579    21908  25630  19643  -1524   1287   -202       C  
ATOM   8726  CD2 PHE B 579       1.306 -27.395  33.019  1.00181.89           C  
ANISOU 8726  CD2 PHE B 579    22291  26741  20077  -1650   1218   -352       C  
ATOM   8727  CE1 PHE B 579       2.721 -29.633  33.868  1.00177.63           C  
ANISOU 8727  CE1 PHE B 579    22038  25671  19780  -1649   1435   -396       C  
ATOM   8728  CE2 PHE B 579       1.003 -28.654  32.496  1.00182.45           C  
ANISOU 8728  CE2 PHE B 579    22368  26777  20175  -1792   1356   -558       C  
ATOM   8729  CZ  PHE B 579       1.710 -29.773  32.923  1.00180.32           C  
ANISOU 8729  CZ  PHE B 579    22253  26226  20032  -1795   1470   -581       C  
ATOM   8730  N   ASN B 580       2.801 -23.664  31.984  1.00135.09           N  
ANISOU 8730  N   ASN B 580    16200  21191  13936  -1301    865     61       N  
ATOM   8731  CA  ASN B 580       2.339 -23.406  30.598  1.00139.02           C  
ANISOU 8731  CA  ASN B 580    16541  21969  14308  -1323    856    -38       C  
ATOM   8732  C   ASN B 580       3.104 -22.410  29.724  1.00139.78           C  
ANISOU 8732  C   ASN B 580    16578  22204  14326  -1223    778     57       C  
ATOM   8733  O   ASN B 580       2.782 -22.235  28.551  1.00141.71           O  
ANISOU 8733  O   ASN B 580    16692  22685  14464  -1230    774    -19       O  
ATOM   8734  CB  ASN B 580       0.867 -23.025  30.656  1.00137.34           C  
ANISOU 8734  CB  ASN B 580    16249  21942  13991  -1360    852    -80       C  
ATOM   8735  CG  ASN B 580       0.019 -24.208  31.042  1.00140.10           C  
ANISOU 8735  CG  ASN B 580    16608  22233  14388  -1507    954   -244       C  
ATOM   8736  OD1 ASN B 580      -0.175 -25.133  30.233  1.00137.58           O  
ANISOU 8736  OD1 ASN B 580    16219  21993  14059  -1620   1034   -431       O  
ATOM   8737  ND2 ASN B 580      -0.487 -24.209  32.273  1.00142.86           N  
ANISOU 8737  ND2 ASN B 580    17050  22442  14788  -1518    961   -184       N  
ATOM   8738  N   GLN B 581       4.103 -21.740  30.288  1.00142.60           N  
ANISOU 8738  N   GLN B 581    17028  22427  14726  -1135    719    222       N  
ATOM   8739  CA  GLN B 581       4.842 -20.710  29.535  1.00143.75           C  
ANISOU 8739  CA  GLN B 581    17135  22689  14794  -1053    654    323       C  
ATOM   8740  C   GLN B 581       5.609 -21.296  28.356  1.00146.09           C  
ANISOU 8740  C   GLN B 581    17350  23069  15088  -1069    678    226       C  
ATOM   8741  O   GLN B 581       5.722 -20.660  27.318  1.00149.48           O  
ANISOU 8741  O   GLN B 581    17690  23689  15415  -1031    647    238       O  
ATOM   8742  CB  GLN B 581       5.750 -19.920  30.457  1.00142.37           C  
ANISOU 8742  CB  GLN B 581    17078  22352  14661   -987    598    502       C  
ATOM   8743  CG  GLN B 581       6.445 -18.801  29.733  1.00144.40           C  
ANISOU 8743  CG  GLN B 581    17312  22720  14832   -923    545    605       C  
ATOM   8744  CD  GLN B 581       6.048 -17.465  30.194  1.00149.75           C  
ANISOU 8744  CD  GLN B 581    18054  23408  15436   -865    503    747       C  
ATOM   8745  OE1 GLN B 581       4.880 -17.262  30.462  1.00154.95           O  
ANISOU 8745  OE1 GLN B 581    18706  24119  16049   -855    511    738       O  
ATOM   8746  NE2 GLN B 581       6.993 -16.515  30.229  1.00149.90           N  
ANISOU 8746  NE2 GLN B 581    18134  23389  15429   -828    466    875       N  
ATOM   8747  N   ALA B 582       6.097 -22.518  28.519  1.00147.19           N  
ANISOU 8747  N   ALA B 582    17526  23065  15333  -1119    742    131       N  
ATOM   8748  CA  ALA B 582       6.767 -23.239  27.443  1.00146.66           C  
ANISOU 8748  CA  ALA B 582    17390  23061  15270  -1137    782     18       C  
ATOM   8749  C   ALA B 582       5.974 -23.270  26.145  1.00148.98           C  
ANISOU 8749  C   ALA B 582    17534  23621  15451  -1188    800   -119       C  
ATOM   8750  O   ALA B 582       6.557 -23.024  25.084  1.00160.85           O  
ANISOU 8750  O   ALA B 582    18953  25268  16893  -1156    778   -130       O  
ATOM   8751  CB  ALA B 582       7.064 -24.657  27.880  1.00151.10           C  
ANISOU 8751  CB  ALA B 582    18033  23420  15956  -1186    879    -83       C  
ATOM   8752  N   GLU B 583       4.669 -23.565  26.212  1.00145.59           N  
ANISOU 8752  N   GLU B 583    17059  23276  14981  -1268    840   -227       N  
ATOM   8753  CA  GLU B 583       3.788 -23.542  25.014  1.00143.40           C  
ANISOU 8753  CA  GLU B 583    16614  23303  14568  -1318    854   -364       C  
ATOM   8754  C   GLU B 583       3.363 -22.151  24.529  1.00138.84           C  
ANISOU 8754  C   GLU B 583    15949  22965  13838  -1217    771   -244       C  
ATOM   8755  O   GLU B 583       3.256 -21.926  23.311  1.00149.35           O  
ANISOU 8755  O   GLU B 583    17143  24551  15052  -1202    763   -301       O  
ATOM   8756  CB  GLU B 583       2.542 -24.417  25.198  1.00148.59           C  
ANISOU 8756  CB  GLU B 583    17234  24003  15217  -1457    937   -543       C  
ATOM   8757  CG  GLU B 583       2.666 -25.799  24.548  1.00158.47           C  
ANISOU 8757  CG  GLU B 583    18462  25234  16515  -1588   1048   -766       C  
ATOM   8758  CD  GLU B 583       2.736 -25.822  23.007  1.00168.84           C  
ANISOU 8758  CD  GLU B 583    19608  26829  17712  -1607   1050   -888       C  
ATOM   8759  OE1 GLU B 583       3.810 -26.135  22.437  1.00173.05           O  
ANISOU 8759  OE1 GLU B 583    20156  27304  18289  -1574   1060   -899       O  
ATOM   8760  OE2 GLU B 583       1.726 -25.526  22.334  1.00174.55           O  
ANISOU 8760  OE2 GLU B 583    20175  27856  18289  -1648   1042   -973       O  
ATOM   8761  N   TRP B 584       3.177 -21.216  25.455  1.00134.72           N  
ANISOU 8761  N   TRP B 584    15515  22358  13314  -1140    718    -74       N  
ATOM   8762  CA  TRP B 584       2.802 -19.844  25.088  1.00133.26           C  
ANISOU 8762  CA  TRP B 584    15284  22360  12985  -1024    656     59       C  
ATOM   8763  C   TRP B 584       3.887 -19.126  24.291  1.00133.94           C  
ANISOU 8763  C   TRP B 584    15363  22494  13032   -940    615    160       C  
ATOM   8764  O   TRP B 584       3.544 -18.321  23.424  1.00139.07           O  
ANISOU 8764  O   TRP B 584    15925  23377  13536   -862    594    203       O  
ATOM   8765  CB  TRP B 584       2.460 -18.994  26.307  1.00132.86           C  
ANISOU 8765  CB  TRP B 584    15356  22173  12949   -959    620    221       C  
ATOM   8766  CG  TRP B 584       1.344 -19.509  27.157  1.00135.40           C  
ANISOU 8766  CG  TRP B 584    15687  22461  13295  -1027    653    150       C  
ATOM   8767  CD1 TRP B 584       0.270 -20.244  26.746  1.00135.80           C  
ANISOU 8767  CD1 TRP B 584    15613  22698  13286  -1119    703    -25       C  
ATOM   8768  CD2 TRP B 584       1.190 -19.320  28.571  1.00134.76           C  
ANISOU 8768  CD2 TRP B 584    15744  22161  13296  -1019    642    247       C  
ATOM   8769  NE1 TRP B 584      -0.539 -20.533  27.815  1.00135.92           N  
ANISOU 8769  NE1 TRP B 584    15682  22617  13343  -1172    726    -41       N  
ATOM   8770  CE2 TRP B 584       0.006 -19.980  28.946  1.00135.78           C  
ANISOU 8770  CE2 TRP B 584    15826  22347  13415  -1105    687    127       C  
ATOM   8771  CE3 TRP B 584       1.942 -18.650  29.556  1.00130.26           C  
ANISOU 8771  CE3 TRP B 584    15328  21364  12800   -956    600    418       C  
ATOM   8772  CZ2 TRP B 584      -0.427 -20.022  30.263  1.00137.51           C  
ANISOU 8772  CZ2 TRP B 584    16150  22393  13703  -1121    691    179       C  
ATOM   8773  CZ3 TRP B 584       1.500 -18.674  30.860  1.00129.28           C  
ANISOU 8773  CZ3 TRP B 584    15303  21076  12738   -970    602    466       C  
ATOM   8774  CH2 TRP B 584       0.319 -19.360  31.202  1.00134.53           C  
ANISOU 8774  CH2 TRP B 584    15921  21795  13398  -1046    646    351       C  
ATOM   8775  N   GLU B 585       5.161 -19.431  24.582  1.00134.45           N  
ANISOU 8775  N   GLU B 585    15516  22355  13214   -952    609    198       N  
ATOM   8776  CA  GLU B 585       6.321 -18.936  23.828  1.00138.10           C  
ANISOU 8776  CA  GLU B 585    15965  22855  13649   -899    579    270       C  
ATOM   8777  C   GLU B 585       6.435 -19.593  22.446  1.00144.57           C  
ANISOU 8777  C   GLU B 585    16637  23876  14415   -933    609    118       C  
ATOM   8778  O   GLU B 585       6.727 -18.916  21.467  1.00154.05           O  
ANISOU 8778  O   GLU B 585    17767  25253  15512   -873    584    164       O  
ATOM   8779  CB  GLU B 585       7.641 -19.146  24.598  1.00140.08           C  
ANISOU 8779  CB  GLU B 585    16334  22858  14029   -905    566    344       C  
ATOM   8780  CG  GLU B 585       7.924 -18.092  25.659  1.00143.06           C  
ANISOU 8780  CG  GLU B 585    16845  23088  14421   -857    522    529       C  
ATOM   8781  CD  GLU B 585       9.237 -18.297  26.452  1.00143.82           C  
ANISOU 8781  CD  GLU B 585    17036  22981  14625   -866    507    597       C  
ATOM   8782  OE1 GLU B 585       9.804 -19.414  26.463  1.00145.41           O  
ANISOU 8782  OE1 GLU B 585    17224  23109  14914   -897    539    506       O  
ATOM   8783  OE2 GLU B 585       9.695 -17.339  27.122  1.00137.60           O  
ANISOU 8783  OE2 GLU B 585    16342  22108  13829   -841    471    742       O  
ATOM   8784  N   ARG B 586       6.206 -20.910  22.372  1.00145.44           N  
ANISOU 8784  N   ARG B 586    16711  23955  14593  -1032    671    -65       N  
ATOM   8785  CA  ARG B 586       6.165 -21.672  21.088  1.00144.50           C  
ANISOU 8785  CA  ARG B 586    16451  24030  14421  -1088    715   -246       C  
ATOM   8786  C   ARG B 586       5.051 -21.231  20.180  1.00137.80           C  
ANISOU 8786  C   ARG B 586    15446  23509  13403  -1079    710   -304       C  
ATOM   8787  O   ARG B 586       5.241 -21.153  18.984  1.00140.19           O  
ANISOU 8787  O   ARG B 586    15627  24029  13610  -1062    708   -357       O  
ATOM   8788  CB  ARG B 586       5.989 -23.179  21.324  1.00153.28           C  
ANISOU 8788  CB  ARG B 586    17584  25014  15639  -1212    806   -441       C  
ATOM   8789  CG  ARG B 586       7.298 -23.818  21.696  1.00160.15           C  
ANISOU 8789  CG  ARG B 586    18564  25639  16647  -1198    829   -418       C  
ATOM   8790  CD  ARG B 586       7.221 -25.248  22.200  1.00166.75           C  
ANISOU 8790  CD  ARG B 586    19481  26271  17605  -1291    934   -566       C  
ATOM   8791  NE  ARG B 586       8.586 -25.765  22.390  1.00172.64           N  
ANISOU 8791  NE  ARG B 586    20315  26826  18453  -1235    953   -525       N  
ATOM   8792  CZ  ARG B 586       9.420 -25.520  23.421  1.00170.47           C  
ANISOU 8792  CZ  ARG B 586    20160  26348  18262  -1154    918   -363       C  
ATOM   8793  NH1 ARG B 586       9.071 -24.765  24.456  1.00165.06           N  
ANISOU 8793  NH1 ARG B 586    19541  25585  17586  -1127    863   -224       N  
ATOM   8794  NH2 ARG B 586      10.643 -26.052  23.422  1.00174.38           N  
ANISOU 8794  NH2 ARG B 586    20702  26729  18822  -1096    941   -344       N  
ATOM   8795  N   SER B 587       3.895 -20.950  20.763  1.00133.92           N  
ANISOU 8795  N   SER B 587    14952  23066  12864  -1084    709   -292       N  
ATOM   8796  CA  SER B 587       2.747 -20.438  20.020  1.00134.74           C  
ANISOU 8796  CA  SER B 587    14900  23509  12783  -1050    702   -327       C  
ATOM   8797  C   SER B 587       2.964 -19.036  19.457  1.00135.36           C  
ANISOU 8797  C   SER B 587    14960  23738  12731   -887    643   -139       C  
ATOM   8798  O   SER B 587       2.310 -18.654  18.477  1.00136.16           O  
ANISOU 8798  O   SER B 587    14910  24164  12661   -832    641   -167       O  
ATOM   8799  CB  SER B 587       1.513 -20.390  20.914  1.00132.63           C  
ANISOU 8799  CB  SER B 587    14648  23249  12496  -1075    712   -333       C  
ATOM   8800  OG  SER B 587       1.123 -21.692  21.264  1.00128.44           O  
ANISOU 8800  OG  SER B 587    14116  22632  12054  -1240    784   -529       O  
ATOM   8801  N   PHE B 588       3.852 -18.274  20.097  1.00132.70           N  
ANISOU 8801  N   PHE B 588    14779  23174  12466   -812    604     49       N  
ATOM   8802  CA  PHE B 588       4.229 -16.948  19.635  1.00131.67           C  
ANISOU 8802  CA  PHE B 588    14672  23124  12230   -674    567    234       C  
ATOM   8803  C   PHE B 588       5.225 -17.061  18.509  1.00134.28           C  
ANISOU 8803  C   PHE B 588    14934  23546  12539   -672    564    206       C  
ATOM   8804  O   PHE B 588       5.052 -16.379  17.510  1.00144.06           O  
ANISOU 8804  O   PHE B 588    16083  25026  13627   -582    559    253       O  
ATOM   8805  CB  PHE B 588       4.817 -16.119  20.765  1.00129.40           C  
ANISOU 8805  CB  PHE B 588    14583  22557  12025   -626    539    427       C  
ATOM   8806  CG  PHE B 588       5.221 -14.730  20.357  1.00126.18           C  
ANISOU 8806  CG  PHE B 588    14233  22195  11512   -502    521    617       C  
ATOM   8807  CD1 PHE B 588       4.286 -13.728  20.213  1.00125.24           C  
ANISOU 8807  CD1 PHE B 588    14113  22227  11243   -375    528    723       C  
ATOM   8808  CD2 PHE B 588       6.553 -14.414  20.163  1.00125.43           C  
ANISOU 8808  CD2 PHE B 588    14207  21986  11464   -509    508    694       C  
ATOM   8809  CE1 PHE B 588       4.673 -12.442  19.875  1.00123.19           C  
ANISOU 8809  CE1 PHE B 588    13941  21976  10890   -257    534    905       C  
ATOM   8810  CE2 PHE B 588       6.946 -13.125  19.826  1.00124.11           C  
ANISOU 8810  CE2 PHE B 588    14116  21838  11202   -415    509    867       C  
ATOM   8811  CZ  PHE B 588       6.001 -12.133  19.689  1.00121.95           C  
ANISOU 8811  CZ  PHE B 588    13862  21686  10786   -288    527    975       C  
ATOM   8812  N   ARG B 589       6.252 -17.910  18.631  1.00136.06           N  
ANISOU 8812  N   ARG B 589    15197  23596  12903   -757    573    134       N  
ATOM   8813  CA  ARG B 589       7.225 -18.060  17.521  1.00141.26           C  
ANISOU 8813  CA  ARG B 589    15778  24355  13535   -754    572     99       C  
ATOM   8814  C   ARG B 589       6.535 -18.532  16.261  1.00138.27           C  
ANISOU 8814  C   ARG B 589    15206  24297  13032   -774    599    -64       C  
ATOM   8815  O   ARG B 589       6.759 -17.981  15.200  1.00134.66           O  
ANISOU 8815  O   ARG B 589    14660  24050  12454   -705    587    -25       O  
ATOM   8816  CB  ARG B 589       8.416 -18.991  17.809  1.00148.57           C  
ANISOU 8816  CB  ARG B 589    16763  25068  14618   -827    585     36       C  
ATOM   8817  CG  ARG B 589       9.609 -18.634  16.881  1.00158.51           C  
ANISOU 8817  CG  ARG B 589    17984  26405  15838   -786    565     89       C  
ATOM   8818  CD  ARG B 589      10.650 -19.726  16.616  1.00164.48           C  
ANISOU 8818  CD  ARG B 589    18722  27080  16693   -842    590    -25       C  
ATOM   8819  NE  ARG B 589      11.637 -19.842  17.686  1.00174.24           N  
ANISOU 8819  NE  ARG B 589    20095  28048  18060   -845    577     62       N  
ATOM   8820  CZ  ARG B 589      12.394 -20.918  17.886  1.00176.45           C  
ANISOU 8820  CZ  ARG B 589    20396  28195  18448   -878    610    -25       C  
ATOM   8821  NH1 ARG B 589      12.309 -21.980  17.070  1.00177.47           N  
ANISOU 8821  NH1 ARG B 589    20437  28412  18581   -920    665   -210       N  
ATOM   8822  NH2 ARG B 589      13.242 -20.942  18.914  1.00174.05           N  
ANISOU 8822  NH2 ARG B 589    20208  27679  18244   -863    595     70       N  
ATOM   8823  N   ASP B 590       5.675 -19.537  16.392  1.00138.46           N  
ANISOU 8823  N   ASP B 590    15164  24365  13077   -876    642   -249       N  
ATOM   8824  CA  ASP B 590       4.874 -20.029  15.254  1.00140.15           C  
ANISOU 8824  CA  ASP B 590    15178  24913  13157   -921    675   -432       C  
ATOM   8825  C   ASP B 590       3.976 -18.960  14.618  1.00140.96           C  
ANISOU 8825  C   ASP B 590    15166  25343  13050   -798    648   -342       C  
ATOM   8826  O   ASP B 590       3.781 -18.956  13.420  1.00140.98           O  
ANISOU 8826  O   ASP B 590    15003  25651  12910   -776    656   -417       O  
ATOM   8827  CB  ASP B 590       4.022 -21.230  15.654  1.00142.03           C  
ANISOU 8827  CB  ASP B 590    15384  25129  13449  -1075    738   -646       C  
ATOM   8828  CG  ASP B 590       4.842 -22.470  15.912  1.00143.64           C  
ANISOU 8828  CG  ASP B 590    15671  25077  13826  -1190    793   -776       C  
ATOM   8829  OD1 ASP B 590       5.903 -22.643  15.281  1.00145.42           O  
ANISOU 8829  OD1 ASP B 590    15892  25279  14080  -1170    791   -780       O  
ATOM   8830  OD2 ASP B 590       4.435 -23.273  16.773  1.00153.88           O  
ANISOU 8830  OD2 ASP B 590    17047  26191  15227  -1293    845   -867       O  
ATOM   8831  N   TYR B 591       3.490 -18.027  15.424  1.00140.88           N  
ANISOU 8831  N   TYR B 591    15251  25263  13014   -702    622   -172       N  
ATOM   8832  CA  TYR B 591       2.761 -16.872  14.929  1.00141.54           C  
ANISOU 8832  CA  TYR B 591    15267  25613  12899   -542    604    -40       C  
ATOM   8833  C   TYR B 591       3.692 -15.869  14.239  1.00143.76           C  
ANISOU 8833  C   TYR B 591    15590  25912  13119   -415    583    134       C  
ATOM   8834  O   TYR B 591       3.362 -15.384  13.180  1.00152.58           O  
ANISOU 8834  O   TYR B 591    16579  27335  14058   -314    587    157       O  
ATOM   8835  CB  TYR B 591       2.030 -16.208  16.079  1.00143.80           C  
ANISOU 8835  CB  TYR B 591    15670  25778  13189   -475    594     91       C  
ATOM   8836  CG  TYR B 591       1.344 -14.915  15.729  1.00150.09           C  
ANISOU 8836  CG  TYR B 591    16443  26796  13788   -278    587    263       C  
ATOM   8837  CD1 TYR B 591       0.228 -14.900  14.910  1.00151.24           C  
ANISOU 8837  CD1 TYR B 591    16385  27350  13729   -216    602    187       C  
ATOM   8838  CD2 TYR B 591       1.794 -13.692  16.257  1.00156.20           C  
ANISOU 8838  CD2 TYR B 591    17407  27371  14569   -147    576    505       C  
ATOM   8839  CE1 TYR B 591      -0.424 -13.715  14.611  1.00155.82           C  
ANISOU 8839  CE1 TYR B 591    16949  28141  14115     -4    605    360       C  
ATOM   8840  CE2 TYR B 591       1.153 -12.497  15.961  1.00157.43           C  
ANISOU 8840  CE2 TYR B 591    17570  27705  14542     51    589    673       C  
ATOM   8841  CZ  TYR B 591       0.045 -12.516  15.144  1.00158.01           C  
ANISOU 8841  CZ  TYR B 591    17438  28185  14411    135    603    607       C  
ATOM   8842  OH  TYR B 591      -0.586 -11.331  14.868  1.00162.99           O  
ANISOU 8842  OH  TYR B 591    18083  28996  14850    361    625    789       O  
ATOM   8843  N   VAL B 592       4.850 -15.570  14.833  1.00141.87           N  
ANISOU 8843  N   VAL B 592    15526  25360  13017   -424    566    254       N  
ATOM   8844  CA  VAL B 592       5.863 -14.683  14.217  1.00141.89           C  
ANISOU 8844  CA  VAL B 592    15581  25356  12975   -338    555    408       C  
ATOM   8845  C   VAL B 592       6.300 -15.228  12.858  1.00138.78           C  
ANISOU 8845  C   VAL B 592    15018  25193  12517   -366    562    282       C  
ATOM   8846  O   VAL B 592       6.318 -14.505  11.879  1.00132.70           O  
ANISOU 8846  O   VAL B 592    14180  24643  11595   -257    566    363       O  
ATOM   8847  CB  VAL B 592       7.111 -14.485  15.156  1.00146.12           C  
ANISOU 8847  CB  VAL B 592    16313  25524  13679   -388    537    515       C  
ATOM   8848  CG1 VAL B 592       8.319 -13.830  14.471  1.00146.43           C  
ANISOU 8848  CG1 VAL B 592    16387  25559  13689   -353    533    626       C  
ATOM   8849  CG2 VAL B 592       6.745 -13.636  16.361  1.00151.03           C  
ANISOU 8849  CG2 VAL B 592    17109  25945  14328   -337    533    674       C  
ATOM   8850  N   LEU B 593       6.679 -16.502  12.828  1.00139.92           N  
ANISOU 8850  N   LEU B 593    15109  25273  12779   -506    571     90       N  
ATOM   8851  CA  LEU B 593       7.138 -17.176  11.612  1.00140.66           C  
ANISOU 8851  CA  LEU B 593    15052  25560  12832   -550    585    -55       C  
ATOM   8852  C   LEU B 593       6.055 -17.268  10.586  1.00143.64           C  
ANISOU 8852  C   LEU B 593    15222  26331  13021   -521    602   -166       C  
ATOM   8853  O   LEU B 593       6.328 -17.181   9.404  1.00150.28           O  
ANISOU 8853  O   LEU B 593    15937  27411  13750   -483    605   -195       O  
ATOM   8854  CB  LEU B 593       7.604 -18.597  11.901  1.00138.86           C  
ANISOU 8854  CB  LEU B 593    14830  25163  12768   -702    611   -250       C  
ATOM   8855  CG  LEU B 593       8.932 -18.720  12.632  1.00141.58           C  
ANISOU 8855  CG  LEU B 593    15333  25179  13281   -727    597   -170       C  
ATOM   8856  CD1 LEU B 593       9.067 -20.138  13.118  1.00142.23           C  
ANISOU 8856  CD1 LEU B 593    15440  25086  13514   -851    640   -354       C  
ATOM   8857  CD2 LEU B 593      10.117 -18.374  11.746  1.00146.05           C  
ANISOU 8857  CD2 LEU B 593    15867  25811  13811   -684    580   -109       C  
ATOM   8858  N   CYS B 594       4.823 -17.440  11.033  1.00146.64           N  
ANISOU 8858  N   CYS B 594    15558  26802  13356   -539    615   -230       N  
ATOM   8859  CA  CYS B 594       3.686 -17.468  10.124  1.00152.04           C  
ANISOU 8859  CA  CYS B 594    16026  27906  13833   -506    631   -334       C  
ATOM   8860  C   CYS B 594       3.558 -16.165   9.320  1.00153.56           C  
ANISOU 8860  C   CYS B 594    16169  28350  13824   -300    615   -140       C  
ATOM   8861  O   CYS B 594       3.304 -16.215   8.137  1.00160.83           O  
ANISOU 8861  O   CYS B 594    16904  29621  14583   -263    624   -214       O  
ATOM   8862  CB  CYS B 594       2.415 -17.746  10.911  1.00158.48           C  
ANISOU 8862  CB  CYS B 594    16820  28760  14633   -554    646   -407       C  
ATOM   8863  SG  CYS B 594       0.915 -17.813   9.929  1.00168.03           S  
ANISOU 8863  SG  CYS B 594    17744  30526  15571   -526    667   -547       S  
ATOM   8864  N   GLN B 595       3.795 -15.011   9.938  1.00156.89           N  
ANISOU 8864  N   GLN B 595    16769  28586  14256   -168    600    106       N  
ATOM   8865  CA  GLN B 595       3.707 -13.717   9.252  1.00157.05           C  
ANISOU 8865  CA  GLN B 595    16786  28795  14089     38    606    313       C  
ATOM   8866  C   GLN B 595       4.922 -13.612   8.312  1.00149.65           C  
ANISOU 8866  C   GLN B 595    15838  27866  13154     39    604    341       C  
ATOM   8867  O   GLN B 595       4.829 -13.317   7.128  1.00148.28           O  
ANISOU 8867  O   GLN B 595    15523  28006  12808    133    615    352       O  
ATOM   8868  CB  GLN B 595       3.814 -12.581  10.283  1.00164.10           C  
ANISOU 8868  CB  GLN B 595    17920  29403  15026    145    608    558       C  
ATOM   8869  CG  GLN B 595       2.952 -12.636  11.563  1.00162.97           C  
ANISOU 8869  CG  GLN B 595    17862  29109  14948    125    605    562       C  
ATOM   8870  CD  GLN B 595       1.644 -11.936  11.428  1.00164.11           C  
ANISOU 8870  CD  GLN B 595    17935  29532  14886    300    624    644       C  
ATOM   8871  OE1 GLN B 595       0.590 -12.570  11.315  1.00166.87           O  
ANISOU 8871  OE1 GLN B 595    18108  30138  15154    264    624    488       O  
ATOM   8872  NE2 GLN B 595       1.687 -10.630  11.459  1.00165.21           N  
ANISOU 8872  NE2 GLN B 595    18213  29626  14932    490    649    885       N  
ATOM   8873  N   CYS B 611      -2.600 -14.561  10.507  1.00162.63           N  
ANISOU 8873  N   CYS B 611    16943  30566  14282     92    647    -53       N  
ATOM   8874  CA  CYS B 611      -2.269 -15.735  11.302  1.00164.38           C  
ANISOU 8874  CA  CYS B 611    17238  30479  14739   -163    651   -237       C  
ATOM   8875  C   CYS B 611      -2.890 -15.643  12.686  1.00166.65           C  
ANISOU 8875  C   CYS B 611    17655  30551  15114   -179    649   -185       C  
ATOM   8876  O   CYS B 611      -3.431 -14.607  13.051  1.00171.67           O  
ANISOU 8876  O   CYS B 611    18348  31234  15644     12    641      7       O  
ATOM   8877  CB  CYS B 611      -0.760 -15.827  11.487  1.00164.83           C  
ANISOU 8877  CB  CYS B 611    17486  30130  15012   -221    638   -175       C  
ATOM   8878  SG  CYS B 611       0.195 -15.893   9.964  1.00169.09           S  
ANISOU 8878  SG  CYS B 611    17911  30851  15482   -203    638   -212       S  
ATOM   8879  N   GLU B 612      -2.771 -16.720  13.465  1.00167.49           N  
ANISOU 8879  N   GLU B 612    17822  30403  15412   -400    663   -349       N  
ATOM   8880  CA  GLU B 612      -3.326 -16.801  14.817  1.00165.78           C  
ANISOU 8880  CA  GLU B 612    17725  29967  15295   -446    664   -325       C  
ATOM   8881  C   GLU B 612      -2.295 -17.317  15.821  1.00160.31           C  
ANISOU 8881  C   GLU B 612    17259  28768  14882   -573    662   -316       C  
ATOM   8882  O   GLU B 612      -1.247 -17.812  15.442  1.00162.91           O  
ANISOU 8882  O   GLU B 612    17627  28947  15324   -652    666   -371       O  
ATOM   8883  CB  GLU B 612      -4.536 -17.735  14.797  1.00172.88           C  
ANISOU 8883  CB  GLU B 612    18432  31142  16110   -604    701   -569       C  
ATOM   8884  CG  GLU B 612      -5.621 -17.334  13.794  1.00182.24           C  
ANISOU 8884  CG  GLU B 612    19354  32892  16995   -490    704   -604       C  
ATOM   8885  CD  GLU B 612      -6.750 -18.346  13.678  1.00184.77           C  
ANISOU 8885  CD  GLU B 612    19460  33522  17220   -687    747   -881       C  
ATOM   8886  OE1 GLU B 612      -7.115 -18.955  14.703  1.00187.95           O  
ANISOU 8886  OE1 GLU B 612    19943  33718  17749   -840    771   -967       O  
ATOM   8887  OE2 GLU B 612      -7.278 -18.525  12.566  1.00179.22           O  
ANISOU 8887  OE2 GLU B 612    18507  33278  16309   -695    762  -1015       O  
ATOM   8888  N   ILE B 613      -2.629 -17.217  17.103  1.00159.48           N  
ANISOU 8888  N   ILE B 613    17294  28424  14875   -586    658   -250       N  
ATOM   8889  CA  ILE B 613      -1.801 -17.696  18.222  1.00152.57           C  
ANISOU 8889  CA  ILE B 613    16629  27089  14248   -694    658   -232       C  
ATOM   8890  C   ILE B 613      -2.556 -18.863  18.874  1.00148.05           C  
ANISOU 8890  C   ILE B 613    16022  26479  13750   -888    703   -436       C  
ATOM   8891  O   ILE B 613      -3.644 -18.653  19.382  1.00145.81           O  
ANISOU 8891  O   ILE B 613    15697  26320  13384   -869    707   -431       O  
ATOM   8892  CB  ILE B 613      -1.580 -16.549  19.253  1.00152.74           C  
ANISOU 8892  CB  ILE B 613    16855  26859  14317   -547    622     23       C  
ATOM   8893  CG1 ILE B 613      -0.973 -15.296  18.579  1.00154.17           C  
ANISOU 8893  CG1 ILE B 613    17080  27096  14399   -357    597    227       C  
ATOM   8894  CG2 ILE B 613      -0.694 -16.997  20.415  1.00152.74           C  
ANISOU 8894  CG2 ILE B 613    17058  26417  14557   -648    618     48       C  
ATOM   8895  CD1 ILE B 613      -1.907 -14.101  18.431  1.00152.98           C  
ANISOU 8895  CD1 ILE B 613    16901  27179  14043   -146    597    384       C  
ATOM   8896  N   LYS B 614      -2.018 -20.086  18.818  1.00147.82           N  
ANISOU 8896  N   LYS B 614    16009  26294  13861  -1072    749   -616       N  
ATOM   8897  CA  LYS B 614      -2.640 -21.276  19.453  1.00150.65           C  
ANISOU 8897  CA  LYS B 614    16368  26567  14305  -1275    815   -815       C  
ATOM   8898  C   LYS B 614      -3.107 -21.065  20.905  1.00148.78           C  
ANISOU 8898  C   LYS B 614    16272  26103  14152  -1267    807   -714       C  
ATOM   8899  O   LYS B 614      -4.260 -21.322  21.231  1.00146.60           O  
ANISOU 8899  O   LYS B 614    15916  25982  13803  -1340    836   -809       O  
ATOM   8900  CB  LYS B 614      -1.649 -22.444  19.473  1.00157.97           C  
ANISOU 8900  CB  LYS B 614    17391  27210  15419  -1423    871   -945       C  
ATOM   8901  CG  LYS B 614      -1.661 -23.371  18.277  1.00166.07           C  
ANISOU 8901  CG  LYS B 614    18263  28449  16386  -1559    933  -1187       C  
ATOM   8902  CD  LYS B 614      -0.798 -24.639  18.447  1.00174.09           C  
ANISOU 8902  CD  LYS B 614    19402  29150  17592  -1706   1013  -1324       C  
ATOM   8903  CE  LYS B 614       0.733 -24.341  18.434  1.00176.09           C  
ANISOU 8903  CE  LYS B 614    19789  29149  17968  -1586    968  -1166       C  
ATOM   8904  NZ  LYS B 614       1.549 -25.337  19.195  1.00175.72           N  
ANISOU 8904  NZ  LYS B 614    19926  28707  18130  -1665   1032  -1206       N  
ATOM   8905  N   ASN B 615      -2.194 -20.613  21.764  1.00144.69           N  
ANISOU 8905  N   ASN B 615    15958  25234  13781  -1185    769   -529       N  
ATOM   8906  CA  ASN B 615      -2.486 -20.412  23.177  1.00140.60           C  
ANISOU 8906  CA  ASN B 615    15588  24475  13356  -1175    759   -426       C  
ATOM   8907  C   ASN B 615      -1.740 -19.226  23.756  1.00141.34           C  
ANISOU 8907  C   ASN B 615    15841  24367  13491  -1005    692   -167       C  
ATOM   8908  O   ASN B 615      -0.704 -18.787  23.228  1.00147.13           O  
ANISOU 8908  O   ASN B 615    16613  25048  14241   -932    663    -77       O  
ATOM   8909  CB  ASN B 615      -2.222 -21.679  24.015  1.00139.95           C  
ANISOU 8909  CB  ASN B 615    15619  24088  13465  -1349    823   -549       C  
ATOM   8910  CG  ASN B 615      -1.002 -22.474  23.562  1.00140.07           C  
ANISOU 8910  CG  ASN B 615    15687  23926  13604  -1412    856   -622       C  
ATOM   8911  OD1 ASN B 615       0.131 -22.069  23.797  1.00142.42           O  
ANISOU 8911  OD1 ASN B 615    16104  24017  13992  -1322    814   -475       O  
ATOM   8912  ND2 ASN B 615      -1.228 -23.633  22.954  1.00139.44           N  
ANISOU 8912  ND2 ASN B 615    15525  23927  13529  -1574    940   -854       N  
ATOM   8913  N   ARG B 616      -2.296 -18.712  24.851  1.00141.43           N  
ANISOU 8913  N   ARG B 616    15946  24275  13514   -954    675    -57       N  
ATOM   8914  CA  ARG B 616      -1.763 -17.551  25.557  1.00139.93           C  
ANISOU 8914  CA  ARG B 616    15920  23892  13354   -810    624    177       C  
ATOM   8915  C   ARG B 616      -2.073 -17.645  27.065  1.00135.20           C  
ANISOU 8915  C   ARG B 616    15459  23045  12864   -844    625    228       C  
ATOM   8916  O   ARG B 616      -2.860 -18.498  27.487  1.00132.88           O  
ANISOU 8916  O   ARG B 616    15119  22771  12595   -961    665     93       O  
ATOM   8917  CB  ARG B 616      -2.349 -16.276  24.944  1.00139.82           C  
ANISOU 8917  CB  ARG B 616    15842  24143  13140   -627    599    306       C  
ATOM   8918  CG  ARG B 616      -3.816 -16.078  25.219  1.00141.55           C  
ANISOU 8918  CG  ARG B 616    15970  24588  13224   -586    610    284       C  
ATOM   8919  CD  ARG B 616      -4.321 -14.885  24.459  1.00141.94           C  
ANISOU 8919  CD  ARG B 616    15948  24922  13058   -379    597    412       C  
ATOM   8920  NE  ARG B 616      -5.756 -14.742  24.654  1.00147.19           N  
ANISOU 8920  NE  ARG B 616    16499  25853  13572   -326    609    383       N  
ATOM   8921  CZ  ARG B 616      -6.427 -13.593  24.610  1.00146.99           C  
ANISOU 8921  CZ  ARG B 616    16474  25998  13375   -113    604    541       C  
ATOM   8922  NH1 ARG B 616      -5.805 -12.442  24.363  1.00142.47           N  
ANISOU 8922  NH1 ARG B 616    16029  25338  12762     62    597    742       N  
ATOM   8923  NH2 ARG B 616      -7.742 -13.599  24.827  1.00149.84           N  
ANISOU 8923  NH2 ARG B 616    16713  26619  13597    -75    616    497       N  
ATOM   8924  N   PRO B 617      -1.465 -16.762  27.879  1.00131.34           N  
ANISOU 8924  N   PRO B 617    15139  22328  12433   -751    588    418       N  
ATOM   8925  CA  PRO B 617      -1.785 -16.818  29.291  1.00132.23           C  
ANISOU 8925  CA  PRO B 617    15375  22230  12637   -777    587    466       C  
ATOM   8926  C   PRO B 617      -3.266 -16.475  29.578  1.00131.31           C  
ANISOU 8926  C   PRO B 617    15187  22311  12391   -729    595    462       C  
ATOM   8927  O   PRO B 617      -3.852 -15.646  28.877  1.00125.41           O  
ANISOU 8927  O   PRO B 617    14357  21821  11473   -602    585    518       O  
ATOM   8928  CB  PRO B 617      -0.813 -15.797  29.922  1.00129.96           C  
ANISOU 8928  CB  PRO B 617    15266  21709  12404   -685    547    666       C  
ATOM   8929  CG  PRO B 617       0.228 -15.525  28.911  1.00129.63           C  
ANISOU 8929  CG  PRO B 617    15204  21703  12344   -655    535    694       C  
ATOM   8930  CD  PRO B 617      -0.448 -15.732  27.594  1.00132.46           C  
ANISOU 8930  CD  PRO B 617    15375  22391  12563   -641    553    583       C  
ATOM   8931  N   SER B 618      -3.841 -17.123  30.598  1.00129.98           N  
ANISOU 8931  N   SER B 618    15053  22033  12300   -823    617    401       N  
ATOM   8932  CA  SER B 618      -5.253 -16.940  30.918  1.00132.68           C  
ANISOU 8932  CA  SER B 618    15315  22573  12523   -799    628    378       C  
ATOM   8933  C   SER B 618      -5.453 -15.687  31.748  1.00131.18           C  
ANISOU 8933  C   SER B 618    15253  22298  12292   -638    592    580       C  
ATOM   8934  O   SER B 618      -4.842 -15.573  32.803  1.00137.51           O  
ANISOU 8934  O   SER B 618    16221  22798  13226   -650    577    670       O  
ATOM   8935  CB  SER B 618      -5.788 -18.124  31.711  1.00133.79           C  
ANISOU 8935  CB  SER B 618    15452  22620  12761   -973    675    233       C  
ATOM   8936  OG  SER B 618      -7.137 -17.870  32.082  1.00135.40           O  
ANISOU 8936  OG  SER B 618    15577  23025  12842   -947    682    221       O  
ATOM   8937  N   LEU B 619      -6.318 -14.778  31.300  1.00127.94           N  
ANISOU 8937  N   LEU B 619    14764  22154  11690   -485    586    648       N  
ATOM   8938  CA  LEU B 619      -6.593 -13.547  32.056  1.00126.19           C  
ANISOU 8938  CA  LEU B 619    14676  21854  11413   -317    568    840       C  
ATOM   8939  C   LEU B 619      -7.450 -13.782  33.292  1.00123.13           C  
ANISOU 8939  C   LEU B 619    14323  21401  11057   -357    574    827       C  
ATOM   8940  O   LEU B 619      -7.433 -13.004  34.235  1.00122.92           O  
ANISOU 8940  O   LEU B 619    14451  21201  11052   -267    562    970       O  
ATOM   8941  CB  LEU B 619      -7.268 -12.516  31.168  1.00130.71           C  
ANISOU 8941  CB  LEU B 619    15164  22737  11759   -114    574    927       C  
ATOM   8942  CG  LEU B 619      -6.388 -12.029  30.011  1.00133.59           C  
ANISOU 8942  CG  LEU B 619    15529  23147  12081    -41    571    984       C  
ATOM   8943  CD1 LEU B 619      -7.203 -12.052  28.738  1.00134.71           C  
ANISOU 8943  CD1 LEU B 619    15445  23720  12016     34    586    911       C  
ATOM   8944  CD2 LEU B 619      -5.790 -10.648  30.273  1.00136.13           C  
ANISOU 8944  CD2 LEU B 619    16057  23280  12384    123    573   1206       C  
ATOM   8945  N   LEU B 620      -8.229 -14.854  33.271  1.00123.14           N  
ANISOU 8945  N   LEU B 620    14180  21552  11053   -499    601    649       N  
ATOM   8946  CA  LEU B 620      -9.003 -15.282  34.432  1.00117.37           C  
ANISOU 8946  CA  LEU B 620    13473  20754  10367   -575    615    612       C  
ATOM   8947  C   LEU B 620      -8.039 -15.688  35.499  1.00116.34           C  
ANISOU 8947  C   LEU B 620    13529  20218  10454   -668    609    650       C  
ATOM   8948  O   LEU B 620      -8.200 -15.276  36.635  1.00119.33           O  
ANISOU 8948  O   LEU B 620    14030  20435  10874   -626    596    750       O  
ATOM   8949  CB  LEU B 620      -9.867 -16.479  34.080  1.00117.86           C  
ANISOU 8949  CB  LEU B 620    13348  21040  10391   -752    661    388       C  
ATOM   8950  CG  LEU B 620     -10.855 -16.949  35.128  1.00119.46           C  
ANISOU 8950  CG  LEU B 620    13540  21244  10604   -842    687    329       C  
ATOM   8951  CD1 LEU B 620     -12.120 -16.104  35.045  1.00122.78           C  
ANISOU 8951  CD1 LEU B 620    13842  22005  10801   -686    675    383       C  
ATOM   8952  CD2 LEU B 620     -11.160 -18.434  34.951  1.00119.81           C  
ANISOU 8952  CD2 LEU B 620    13482  21333  10706  -1095    754     92       C  
ATOM   8953  N   VAL B 621      -7.014 -16.465  35.135  1.00113.87           N  
ANISOU 8953  N   VAL B 621    13238  19754  10271   -782    620    577       N  
ATOM   8954  CA  VAL B 621      -5.976 -16.850  36.100  1.00111.64           C  
ANISOU 8954  CA  VAL B 621    13126  19106  10183   -849    615    624       C  
ATOM   8955  C   VAL B 621      -5.285 -15.597  36.637  1.00113.19           C  
ANISOU 8955  C   VAL B 621    13482  19134  10389   -707    567    828       C  
ATOM   8956  O   VAL B 621      -5.130 -15.448  37.861  1.00119.80           O  
ANISOU 8956  O   VAL B 621    14452  19754  11311   -708    556    908       O  
ATOM   8957  CB  VAL B 621      -4.984 -17.892  35.521  1.00110.76           C  
ANISOU 8957  CB  VAL B 621    13003  18890  10190   -970    642    514       C  
ATOM   8958  CG1 VAL B 621      -3.808 -18.159  36.447  1.00108.69           C  
ANISOU 8958  CG1 VAL B 621    12909  18285  10103   -997    634    589       C  
ATOM   8959  CG2 VAL B 621      -5.722 -19.197  35.235  1.00111.86           C  
ANISOU 8959  CG2 VAL B 621    13024  19141  10335  -1138    712    303       C  
ATOM   8960  N   GLU B 622      -4.916 -14.672  35.753  1.00115.29           N  
ANISOU 8960  N   GLU B 622    13741  19504  10560   -589    546    910       N  
ATOM   8961  CA  GLU B 622      -4.315 -13.391  36.197  1.00119.83           C  
ANISOU 8961  CA  GLU B 622    14480  19926  11125   -466    519   1098       C  
ATOM   8962  C   GLU B 622      -5.238 -12.617  37.175  1.00117.14           C  
ANISOU 8962  C   GLU B 622    14215  19573  10717   -368    519   1195       C  
ATOM   8963  O   GLU B 622      -4.777 -12.122  38.235  1.00118.23           O  
ANISOU 8963  O   GLU B 622    14517  19474  10928   -355    506   1300       O  
ATOM   8964  CB  GLU B 622      -3.930 -12.476  35.013  1.00123.74           C  
ANISOU 8964  CB  GLU B 622    14957  20554  11502   -348    516   1171       C  
ATOM   8965  CG  GLU B 622      -2.894 -13.014  34.004  1.00127.88           C  
ANISOU 8965  CG  GLU B 622    15421  21088  12079   -421    513   1101       C  
ATOM   8966  CD  GLU B 622      -1.675 -13.710  34.624  1.00131.36           C  
ANISOU 8966  CD  GLU B 622    15949  21257  12704   -544    500   1081       C  
ATOM   8967  OE1 GLU B 622      -0.783 -13.023  35.159  1.00134.47           O  
ANISOU 8967  OE1 GLU B 622    16486  21459  13145   -521    482   1200       O  
ATOM   8968  OE2 GLU B 622      -1.598 -14.955  34.584  1.00132.40           O  
ANISOU 8968  OE2 GLU B 622    16009  21370  12925   -665    517    943       O  
ATOM   8969  N   LYS B 623      -6.529 -12.562  36.852  1.00116.78           N  
ANISOU 8969  N   LYS B 623    14043  19795  10530   -306    535   1152       N  
ATOM   8970  CA  LYS B 623      -7.516 -11.909  37.716  1.00119.64           C  
ANISOU 8970  CA  LYS B 623    14455  20188  10814   -204    539   1233       C  
ATOM   8971  C   LYS B 623      -7.702 -12.628  39.073  1.00119.58           C  
ANISOU 8971  C   LYS B 623    14505  19992  10938   -325    537   1191       C  
ATOM   8972  O   LYS B 623      -7.909 -11.985  40.124  1.00119.82           O  
ANISOU 8972  O   LYS B 623    14662  19889  10974   -260    531   1296       O  
ATOM   8973  CB  LYS B 623      -8.868 -11.818  36.997  1.00124.13           C  
ANISOU 8973  CB  LYS B 623    14840  21137  11186   -114    558   1180       C  
ATOM   8974  CG  LYS B 623      -8.999 -10.639  36.060  1.00126.05           C  
ANISOU 8974  CG  LYS B 623    15079  21563  11252     96    568   1298       C  
ATOM   8975  CD  LYS B 623     -10.337 -10.664  35.349  1.00127.68           C  
ANISOU 8975  CD  LYS B 623    15074  22189  11250    188    586   1236       C  
ATOM   8976  CE  LYS B 623     -10.403  -9.571  34.309  1.00131.85           C  
ANISOU 8976  CE  LYS B 623    15591  22912  11594    412    605   1357       C  
ATOM   8977  NZ  LYS B 623     -11.478  -9.875  33.330  1.00135.55           N  
ANISOU 8977  NZ  LYS B 623    15800  23839  11863    465    616   1257       N  
ATOM   8978  N   ILE B 624      -7.648 -13.960  39.041  1.00115.93           N  
ANISOU 8978  N   ILE B 624    13955  19515  10575   -499    552   1037       N  
ATOM   8979  CA  ILE B 624      -7.652 -14.792  40.256  1.00114.41           C  
ANISOU 8979  CA  ILE B 624    13828  19117  10524   -626    563    996       C  
ATOM   8980  C   ILE B 624      -6.410 -14.515  41.123  1.00112.07           C  
ANISOU 8980  C   ILE B 624    13719  18493  10369   -627    537   1108       C  
ATOM   8981  O   ILE B 624      -6.537 -14.250  42.333  1.00113.56           O  
ANISOU 8981  O   ILE B 624    14016  18530  10600   -612    528   1183       O  
ATOM   8982  CB  ILE B 624      -7.802 -16.303  39.911  1.00113.89           C  
ANISOU 8982  CB  ILE B 624    13648  19095  10529   -811    608    804       C  
ATOM   8983  CG1 ILE B 624      -9.230 -16.579  39.434  1.00115.10           C  
ANISOU 8983  CG1 ILE B 624    13620  19577  10534   -839    639    684       C  
ATOM   8984  CG2 ILE B 624      -7.495 -17.207  41.101  1.00112.53           C  
ANISOU 8984  CG2 ILE B 624    13579  18653  10523   -933    633    779       C  
ATOM   8985  CD1 ILE B 624      -9.362 -17.825  38.592  1.00115.52           C  
ANISOU 8985  CD1 ILE B 624    13534  19752  10602  -1011    693    481       C  
ATOM   8986  N   ASN B 625      -5.237 -14.525  40.505  1.00107.96           N  
ANISOU 8986  N   ASN B 625    13226  17890   9904   -642    525   1120       N  
ATOM   8987  CA  ASN B 625      -4.029 -14.191  41.222  1.00112.23           C  
ANISOU 8987  CA  ASN B 625    13920  18171  10550   -643    500   1222       C  
ATOM   8988  C   ASN B 625      -4.112 -12.785  41.842  1.00114.62           C  
ANISOU 8988  C   ASN B 625    14354  18412  10782   -522    480   1377       C  
ATOM   8989  O   ASN B 625      -3.705 -12.570  43.022  1.00117.12           O  
ANISOU 8989  O   ASN B 625    14798  18528  11172   -538    467   1449       O  
ATOM   8990  CB  ASN B 625      -2.826 -14.269  40.289  1.00115.41           C  
ANISOU 8990  CB  ASN B 625    14311  18552  10987   -663    490   1213       C  
ATOM   8991  CG  ASN B 625      -1.516 -14.518  41.020  1.00122.60           C  
ANISOU 8991  CG  ASN B 625    15329  19221  12031   -718    474   1260       C  
ATOM   8992  OD1 ASN B 625      -1.382 -14.308  42.252  1.00128.48           O  
ANISOU 8992  OD1 ASN B 625    16182  19806  12827   -720    462   1332       O  
ATOM   8993  ND2 ASN B 625      -0.539 -15.009  40.271  1.00122.62           N  
ANISOU 8993  ND2 ASN B 625    15292  19214  12081   -761    474   1215       N  
ATOM   8994  N   LEU B 626      -4.625 -11.830  41.055  1.00118.37           N  
ANISOU 8994  N   LEU B 626    14805  19059  11110   -397    487   1428       N  
ATOM   8995  CA  LEU B 626      -4.806 -10.459  41.594  1.00122.21           C  
ANISOU 8995  CA  LEU B 626    15436  19482  11516   -268    490   1575       C  
ATOM   8996  C   LEU B 626      -5.824 -10.373  42.739  1.00122.91           C  
ANISOU 8996  C   LEU B 626    15559  19552  11586   -237    495   1596       C  
ATOM   8997  O   LEU B 626      -5.605  -9.658  43.729  1.00118.73           O  
ANISOU 8997  O   LEU B 626    15186  18849  11077   -205    493   1694       O  
ATOM   8998  CB  LEU B 626      -5.207  -9.493  40.487  1.00122.67           C  
ANISOU 8998  CB  LEU B 626    15469  19731  11407   -115    514   1634       C  
ATOM   8999  CG  LEU B 626      -4.055  -9.133  39.550  1.00123.02           C  
ANISOU 8999  CG  LEU B 626    15546  19738  11458   -121    515   1666       C  
ATOM   9000  CD1 LEU B 626      -4.600  -8.836  38.166  1.00128.18           C  
ANISOU 9000  CD1 LEU B 626    16081  20664  11959     -7    536   1658       C  
ATOM   9001  CD2 LEU B 626      -3.232  -7.966  40.076  1.00120.65           C  
ANISOU 9001  CD2 LEU B 626    15457  19220  11163    -85    529   1802       C  
ATOM   9002  N   PHE B 627      -6.924 -11.108  42.599  1.00124.93           N  
ANISOU 9002  N   PHE B 627    15668  19999  11800   -258    504   1497       N  
ATOM   9003  CA  PHE B 627      -7.935 -11.170  43.666  1.00124.54           C  
ANISOU 9003  CA  PHE B 627    15628  19956  11733   -245    510   1501       C  
ATOM   9004  C   PHE B 627      -7.347 -11.781  44.907  1.00119.70           C  
ANISOU 9004  C   PHE B 627    15109  19088  11283   -366    496   1497       C  
ATOM   9005  O   PHE B 627      -7.644 -11.311  45.986  1.00119.11           O  
ANISOU 9005  O   PHE B 627    15135  18912  11209   -326    493   1570       O  
ATOM   9006  CB  PHE B 627      -9.150 -11.993  43.225  1.00128.56           C  
ANISOU 9006  CB  PHE B 627    15942  20736  12168   -285    529   1371       C  
ATOM   9007  CG  PHE B 627     -10.138 -12.290  44.317  1.00129.68           C  
ANISOU 9007  CG  PHE B 627    16075  20890  12307   -310    537   1351       C  
ATOM   9008  CD1 PHE B 627     -11.129 -11.390  44.618  1.00130.35           C  
ANISOU 9008  CD1 PHE B 627    16167  21109  12248   -156    542   1430       C  
ATOM   9009  CD2 PHE B 627     -10.081 -13.493  45.033  1.00131.10           C  
ANISOU 9009  CD2 PHE B 627    16241  20947  12623   -482    548   1256       C  
ATOM   9010  CE1 PHE B 627     -12.041 -11.663  45.627  1.00131.13           C  
ANISOU 9010  CE1 PHE B 627    16251  21232  12339   -181    550   1410       C  
ATOM   9011  CE2 PHE B 627     -10.987 -13.773  46.047  1.00128.09           C  
ANISOU 9011  CE2 PHE B 627    15854  20576  12238   -513    561   1239       C  
ATOM   9012  CZ  PHE B 627     -11.962 -12.853  46.349  1.00129.06           C  
ANISOU 9012  CZ  PHE B 627    15974  20845  12218   -367    557   1314       C  
ATOM   9013  N   ALA B 628      -6.535 -12.836  44.753  1.00118.40           N  
ANISOU 9013  N   ALA B 628    14911  18827  11246   -501    495   1415       N  
ATOM   9014  CA  ALA B 628      -5.851 -13.463  45.906  1.00116.22           C  
ANISOU 9014  CA  ALA B 628    14725  18311  11121   -597    488   1423       C  
ATOM   9015  C   ALA B 628      -4.836 -12.525  46.557  1.00114.68           C  
ANISOU 9015  C   ALA B 628    14690  17924  10956   -555    460   1550       C  
ATOM   9016  O   ALA B 628      -4.899 -12.329  47.770  1.00114.69           O  
ANISOU 9016  O   ALA B 628    14785  17798  10992   -555    452   1607       O  
ATOM   9017  CB  ALA B 628      -5.172 -14.771  45.513  1.00114.66           C  
ANISOU 9017  CB  ALA B 628    14466  18059  11040   -723    506   1317       C  
ATOM   9018  N   MET B 629      -3.920 -11.940  45.760  1.00116.56           N  
ANISOU 9018  N   MET B 629    14958  18154  11174   -528    450   1590       N  
ATOM   9019  CA  MET B 629      -2.931 -10.987  46.343  1.00117.38           C  
ANISOU 9019  CA  MET B 629    15216  18090  11293   -512    434   1698       C  
ATOM   9020  C   MET B 629      -3.599  -9.825  47.065  1.00115.81           C  
ANISOU 9020  C   MET B 629    15134  17860  11006   -416    445   1793       C  
ATOM   9021  O   MET B 629      -3.286  -9.595  48.213  1.00116.91           O  
ANISOU 9021  O   MET B 629    15378  17850  11191   -445    435   1841       O  
ATOM   9022  CB  MET B 629      -1.962 -10.404  45.300  1.00124.75           C  
ANISOU 9022  CB  MET B 629    16165  19038  12192   -499    433   1726       C  
ATOM   9023  CG  MET B 629      -0.784  -9.645  45.924  1.00128.10           C  
ANISOU 9023  CG  MET B 629    16733  19292  12644   -534    423   1809       C  
ATOM   9024  SD  MET B 629      -0.096  -8.271  44.961  1.00139.98           S  
ANISOU 9024  SD  MET B 629    18332  20805  14047   -486    450   1887       S  
ATOM   9025  CE  MET B 629       0.975  -9.155  43.790  1.00136.80           C  
ANISOU 9025  CE  MET B 629    17798  20475  13705   -562    429   1810       C  
ATOM   9026  N   PHE B 630      -4.487  -9.093  46.382  1.00118.95           N  
ANISOU 9026  N   PHE B 630    15515  18407  11270   -294    469   1821       N  
ATOM   9027  CA  PHE B 630      -5.160  -7.908  46.977  1.00118.66           C  
ANISOU 9027  CA  PHE B 630    15606  18345  11133   -172    495   1920       C  
ATOM   9028  C   PHE B 630      -6.214  -8.274  48.017  1.00116.48           C  
ANISOU 9028  C   PHE B 630    15307  18089  10861   -162    491   1903       C  
ATOM   9029  O   PHE B 630      -6.559  -7.467  48.875  1.00112.39           O  
ANISOU 9029  O   PHE B 630    14913  17491  10299    -94    505   1980       O  
ATOM   9030  CB  PHE B 630      -5.807  -7.032  45.881  1.00124.10           C  
ANISOU 9030  CB  PHE B 630    16284  19206  11662    -13    533   1968       C  
ATOM   9031  CG  PHE B 630      -4.811  -6.281  45.042  1.00129.78           C  
ANISOU 9031  CG  PHE B 630    17086  19869  12354      3    555   2024       C  
ATOM   9032  CD1 PHE B 630      -4.061  -5.257  45.607  1.00135.79           C  
ANISOU 9032  CD1 PHE B 630    18050  20425  13117     -1    583   2114       C  
ATOM   9033  CD2 PHE B 630      -4.592  -6.604  43.707  1.00128.70           C  
ANISOU 9033  CD2 PHE B 630    16829  19882  12188      7    553   1978       C  
ATOM   9034  CE1 PHE B 630      -3.110  -4.573  44.855  1.00134.86           C  
ANISOU 9034  CE1 PHE B 630    18015  20250  12973     -9    613   2159       C  
ATOM   9035  CE2 PHE B 630      -3.648  -5.921  42.960  1.00129.88           C  
ANISOU 9035  CE2 PHE B 630    17058  19977  12313     14    576   2031       C  
ATOM   9036  CZ  PHE B 630      -2.911  -4.900  43.527  1.00131.36           C  
ANISOU 9036  CZ  PHE B 630    17450  19957  12501      3    609   2123       C  
ATOM   9037  N   GLY B 631      -6.748  -9.488  47.914  1.00116.22           N  
ANISOU 9037  N   GLY B 631    15119  18164  10873   -235    479   1798       N  
ATOM   9038  CA  GLY B 631      -7.759  -9.980  48.845  1.00114.30           C  
ANISOU 9038  CA  GLY B 631    14838  17955  10636   -250    480   1767       C  
ATOM   9039  C   GLY B 631      -7.196 -10.209  50.210  1.00110.25           C  
ANISOU 9039  C   GLY B 631    14430  17222  10238   -329    463   1797       C  
ATOM   9040  O   GLY B 631      -7.858  -9.938  51.194  1.00111.99           O  
ANISOU 9040  O   GLY B 631    14701  17415  10434   -293    466   1834       O  
ATOM   9041  N   THR B 632      -5.969 -10.711  50.263  1.00108.77           N  
ANISOU 9041  N   THR B 632    14266  16894  10165   -430    446   1783       N  
ATOM   9042  CA  THR B 632      -5.225 -10.860  51.513  1.00108.35           C  
ANISOU 9042  CA  THR B 632    14309  16647  10209   -495    428   1822       C  
ATOM   9043  C   THR B 632      -5.081  -9.502  52.164  1.00106.33           C  
ANISOU 9043  C   THR B 632    14210  16301   9888   -426    429   1925       C  
ATOM   9044  O   THR B 632      -5.381  -9.355  53.330  1.00106.16           O  
ANISOU 9044  O   THR B 632    14254  16203   9877   -424    426   1959       O  
ATOM   9045  CB  THR B 632      -3.821 -11.467  51.263  1.00109.08           C  
ANISOU 9045  CB  THR B 632    14394  16646  10405   -586    412   1801       C  
ATOM   9046  OG1 THR B 632      -3.957 -12.631  50.456  1.00109.29           O  
ANISOU 9046  OG1 THR B 632    14290  16756  10477   -639    427   1701       O  
ATOM   9047  CG2 THR B 632      -3.152 -11.881  52.544  1.00110.72           C  
ANISOU 9047  CG2 THR B 632    14662  16700  10704   -648    397   1830       C  
ATOM   9048  N   GLY B 633      -4.617  -8.517  51.408  1.00106.82           N  
ANISOU 9048  N   GLY B 633    14339  16365   9882   -374    442   1971       N  
ATOM   9049  CA  GLY B 633      -4.489  -7.155  51.922  1.00110.12           C  
ANISOU 9049  CA  GLY B 633    14929  16682  10227   -314    467   2062       C  
ATOM   9050  C   GLY B 633      -5.785  -6.609  52.509  1.00111.70           C  
ANISOU 9050  C   GLY B 633    15175  16927  10339   -198    491   2101       C  
ATOM   9051  O   GLY B 633      -5.779  -5.950  53.563  1.00112.96           O  
ANISOU 9051  O   GLY B 633    15467  16966  10485   -188    503   2154       O  
ATOM   9052  N   ILE B 634      -6.903  -6.895  51.842  1.00109.76           N  
ANISOU 9052  N   ILE B 634    14810  16871  10023   -113    500   2070       N  
ATOM   9053  CA  ILE B 634      -8.197  -6.438  52.326  1.00110.54           C  
ANISOU 9053  CA  ILE B 634    14924  17054  10020      9    523   2104       C  
ATOM   9054  C   ILE B 634      -8.599  -7.214  53.578  1.00106.95           C  
ANISOU 9054  C   ILE B 634    14436  16557   9642    -66    498   2070       C  
ATOM   9055  O   ILE B 634      -8.985  -6.602  54.585  1.00109.52           O  
ANISOU 9055  O   ILE B 634    14868  16810   9933    -14    509   2126       O  
ATOM   9056  CB  ILE B 634      -9.259  -6.480  51.217  1.00114.27           C  
ANISOU 9056  CB  ILE B 634    15260  17785  10371    126    542   2079       C  
ATOM   9057  CG1 ILE B 634      -8.962  -5.346  50.231  1.00117.74           C  
ANISOU 9057  CG1 ILE B 634    15791  18239  10704    252    584   2156       C  
ATOM   9058  CG2 ILE B 634     -10.678  -6.323  51.786  1.00114.61           C  
ANISOU 9058  CG2 ILE B 634    15267  17966  10314    237    557   2093       C  
ATOM   9059  CD1 ILE B 634      -9.585  -5.521  48.867  1.00120.68           C  
ANISOU 9059  CD1 ILE B 634    16007  18873  10971    342    595   2124       C  
ATOM   9060  N   ALA B 635      -8.475  -8.538  53.542  1.00101.49           N  
ANISOU 9060  N   ALA B 635    13613  15895   9053   -189    472   1983       N  
ATOM   9061  CA  ALA B 635      -8.830  -9.348  54.710  1.00 99.00           C  
ANISOU 9061  CA  ALA B 635    13273  15529   8813   -264    459   1954       C  
ATOM   9062  C   ALA B 635      -7.994  -8.969  55.926  1.00 98.82           C  
ANISOU 9062  C   ALA B 635    13394  15299   8853   -305    444   2017       C  
ATOM   9063  O   ALA B 635      -8.538  -8.740  57.002  1.00100.65           O  
ANISOU 9063  O   ALA B 635    13680  15495   9067   -279    446   2050       O  
ATOM   9064  CB  ALA B 635      -8.702 -10.833  54.412  1.00 97.97           C  
ANISOU 9064  CB  ALA B 635    13008  15431   8785   -392    456   1853       C  
ATOM   9065  N   MET B 636      -6.683  -8.858  55.757  1.00 97.94           N  
ANISOU 9065  N   MET B 636    13339  15072   8803   -369    430   2032       N  
ATOM   9066  CA  MET B 636      -5.798  -8.480  56.862  1.00 98.91           C  
ANISOU 9066  CA  MET B 636    13580  15030   8968   -421    416   2081       C  
ATOM   9067  C   MET B 636      -6.099  -7.076  57.427  1.00101.78           C  
ANISOU 9067  C   MET B 636    14101  15335   9233   -339    442   2153       C  
ATOM   9068  O   MET B 636      -5.865  -6.826  58.594  1.00101.36           O  
ANISOU 9068  O   MET B 636    14132  15182   9197   -372    436   2182       O  
ATOM   9069  CB  MET B 636      -4.327  -8.572  56.422  1.00 97.20           C  
ANISOU 9069  CB  MET B 636    13375  14744   8811   -505    400   2075       C  
ATOM   9070  CG  MET B 636      -3.814  -9.952  55.994  1.00 95.33           C  
ANISOU 9070  CG  MET B 636    13009  14532   8678   -582    382   2012       C  
ATOM   9071  SD  MET B 636      -4.273 -11.362  57.028  1.00 97.33           S  
ANISOU 9071  SD  MET B 636    13192  14760   9026   -631    381   1979       S  
ATOM   9072  CE  MET B 636      -5.618 -12.120  56.119  1.00 94.86           C  
ANISOU 9072  CE  MET B 636    12749  14598   8693   -614    411   1894       C  
ATOM   9073  N   SER B 637      -6.629  -6.181  56.595  1.00107.09           N  
ANISOU 9073  N   SER B 637    14817  16073   9797   -226    479   2182       N  
ATOM   9074  CA  SER B 637      -7.045  -4.848  57.045  1.00110.81           C  
ANISOU 9074  CA  SER B 637    15454  16483  10163   -122    525   2254       C  
ATOM   9075  C   SER B 637      -8.307  -4.861  57.954  1.00112.22           C  
ANISOU 9075  C   SER B 637    15626  16716  10296    -40    530   2268       C  
ATOM   9076  O   SER B 637      -8.485  -3.948  58.760  1.00116.88           O  
ANISOU 9076  O   SER B 637    16365  17214  10830     11    561   2320       O  
ATOM   9077  CB  SER B 637      -7.252  -3.917  55.842  1.00113.68           C  
ANISOU 9077  CB  SER B 637    15874  16903  10415      0    577   2294       C  
ATOM   9078  OG  SER B 637      -8.535  -4.086  55.270  1.00118.00           O  
ANISOU 9078  OG  SER B 637    16314  17644  10877    134    588   2290       O  
ATOM   9079  N   THR B 638      -9.142  -5.905  57.857  1.00108.12           N  
ANISOU 9079  N   THR B 638    14939  16341   9798    -43    505   2215       N  
ATOM   9080  CA  THR B 638     -10.298  -6.066  58.747  1.00108.20           C  
ANISOU 9080  CA  THR B 638    14921  16419   9772     10    506   2218       C  
ATOM   9081  C   THR B 638      -9.938  -6.493  60.208  1.00109.15           C  
ANISOU 9081  C   THR B 638    15082  16406   9983    -91    479   2220       C  
ATOM   9082  O   THR B 638     -10.828  -6.745  61.040  1.00106.20           O  
ANISOU 9082  O   THR B 638    14678  16079   9592    -67    478   2220       O  
ATOM   9083  CB  THR B 638     -11.320  -7.095  58.213  1.00108.53           C  
ANISOU 9083  CB  THR B 638    14764  16671   9801     10    497   2147       C  
ATOM   9084  OG1 THR B 638     -10.797  -8.437  58.348  1.00109.32           O  
ANISOU 9084  OG1 THR B 638    14765  16731  10038   -149    469   2077       O  
ATOM   9085  CG2 THR B 638     -11.698  -6.801  56.790  1.00106.56           C  
ANISOU 9085  CG2 THR B 638    14442  16592   9454    105    518   2137       C  
ATOM   9086  N   TRP B 639      -8.651  -6.592  60.528  1.00108.26           N  
ANISOU 9086  N   TRP B 639    15026  16150   9958   -202    459   2222       N  
ATOM   9087  CA  TRP B 639      -8.225  -6.834  61.904  1.00109.27           C  
ANISOU 9087  CA  TRP B 639    15201  16168  10148   -279    438   2236       C  
ATOM   9088  C   TRP B 639      -8.646  -5.722  62.846  1.00113.11           C  
ANISOU 9088  C   TRP B 639    15832  16592  10550   -208    463   2288       C  
ATOM   9089  O   TRP B 639      -8.896  -5.945  64.041  1.00122.37           O  
ANISOU 9089  O   TRP B 639    17017  17734  11742   -231    450   2298       O  
ATOM   9090  CB  TRP B 639      -6.716  -6.983  61.946  1.00108.22           C  
ANISOU 9090  CB  TRP B 639    15095  15930  10091   -394    415   2231       C  
ATOM   9091  CG  TRP B 639      -6.150  -7.318  63.297  1.00106.57           C  
ANISOU 9091  CG  TRP B 639    14910  15642   9938   -472    390   2245       C  
ATOM   9092  CD1 TRP B 639      -5.520  -6.476  64.145  1.00104.73           C  
ANISOU 9092  CD1 TRP B 639    14799  15320   9672   -507    394   2273       C  
ATOM   9093  CD2 TRP B 639      -6.123  -8.614  63.912  1.00105.10           C  
ANISOU 9093  CD2 TRP B 639    14622  15467   9843   -525    366   2228       C  
ATOM   9094  NE1 TRP B 639      -5.109  -7.156  65.264  1.00105.28           N  
ANISOU 9094  NE1 TRP B 639    14832  15367   9799   -571    364   2278       N  
ATOM   9095  CE2 TRP B 639      -5.461  -8.475  65.136  1.00105.59           C  
ANISOU 9095  CE2 TRP B 639    14741  15458   9917   -574    350   2259       C  
ATOM   9096  CE3 TRP B 639      -6.580  -9.887  63.527  1.00103.90           C  
ANISOU 9096  CE3 TRP B 639    14343  15374   9758   -542    368   2188       C  
ATOM   9097  CZ2 TRP B 639      -5.280  -9.552  66.012  1.00107.45           C  
ANISOU 9097  CZ2 TRP B 639    14912  15686  10225   -613    333   2266       C  
ATOM   9098  CZ3 TRP B 639      -6.401 -10.961  64.399  1.00105.39           C  
ANISOU 9098  CZ3 TRP B 639    14487  15528  10027   -592    363   2191       C  
ATOM   9099  CH2 TRP B 639      -5.754 -10.788  65.614  1.00106.33           C  
ANISOU 9099  CH2 TRP B 639    14664  15581  10153   -616    345   2238       C  
ATOM   9100  N   VAL B 640      -8.707  -4.523  62.303  1.00113.40           N  
ANISOU 9100  N   VAL B 640    15991  16604  10491   -120    509   2324       N  
ATOM   9101  CA  VAL B 640      -9.078  -3.346  63.035  1.00117.10           C  
ANISOU 9101  CA  VAL B 640    16628  16996  10868    -39    555   2373       C  
ATOM   9102  C   VAL B 640     -10.571  -2.996  62.883  1.00116.84           C  
ANISOU 9102  C   VAL B 640    16581  17088  10724    138    588   2402       C  
ATOM   9103  O   VAL B 640     -11.014  -1.974  63.417  1.00123.08           O  
ANISOU 9103  O   VAL B 640    17520  17820  11422    239    639   2449       O  
ATOM   9104  CB  VAL B 640      -8.092  -2.241  62.572  1.00122.29           C  
ANISOU 9104  CB  VAL B 640    17454  17523  11488    -63    604   2396       C  
ATOM   9105  CG1 VAL B 640      -8.464  -0.820  62.997  1.00127.03           C  
ANISOU 9105  CG1 VAL B 640    18271  18020  11973     36    685   2447       C  
ATOM   9106  CG2 VAL B 640      -6.672  -2.640  63.015  1.00121.98           C  
ANISOU 9106  CG2 VAL B 640    17405  17395  11545   -249    564   2361       C  
ATOM   9107  N   TRP B 641     -11.375  -3.849  62.245  1.00113.43           N  
ANISOU 9107  N   TRP B 641    15971  16836  10291    175    565   2369       N  
ATOM   9108  CA  TRP B 641     -12.822  -3.546  62.074  1.00115.36           C  
ANISOU 9108  CA  TRP B 641    16173  17250  10408    347    595   2392       C  
ATOM   9109  C   TRP B 641     -13.639  -3.926  63.332  1.00121.72           C  
ANISOU 9109  C   TRP B 641    16941  18092  11214    346    578   2387       C  
ATOM   9110  O   TRP B 641     -14.536  -4.790  63.297  1.00119.33           O  
ANISOU 9110  O   TRP B 641    16472  17961  10906    343    558   2346       O  
ATOM   9111  CB  TRP B 641     -13.376  -4.215  60.802  1.00111.67           C  
ANISOU 9111  CB  TRP B 641    15520  16996   9912    380    585   2348       C  
ATOM   9112  CG  TRP B 641     -12.870  -3.634  59.527  1.00106.86           C  
ANISOU 9112  CG  TRP B 641    14952  16390   9259    438    613   2370       C  
ATOM   9113  CD1 TRP B 641     -11.754  -2.855  59.346  1.00105.67           C  
ANISOU 9113  CD1 TRP B 641    14966  16052   9129    407    639   2407       C  
ATOM   9114  CD2 TRP B 641     -13.414  -3.847  58.248  1.00105.14           C  
ANISOU 9114  CD2 TRP B 641    14598  16382   8967    517    621   2348       C  
ATOM   9115  NE1 TRP B 641     -11.584  -2.570  58.031  1.00105.86           N  
ANISOU 9115  NE1 TRP B 641    14972  16145   9101    471    664   2418       N  
ATOM   9116  CE2 TRP B 641     -12.602  -3.149  57.323  1.00105.59           C  
ANISOU 9116  CE2 TRP B 641    14753  16360   9004    549    652   2385       C  
ATOM   9117  CE3 TRP B 641     -14.519  -4.554  57.778  1.00104.91           C  
ANISOU 9117  CE3 TRP B 641    14367  16616   8876    558    608   2296       C  
ATOM   9118  CZ2 TRP B 641     -12.871  -3.128  55.939  1.00102.17           C  
ANISOU 9118  CZ2 TRP B 641    14223  16105   8491    638    667   2381       C  
ATOM   9119  CZ3 TRP B 641     -14.791  -4.539  56.404  1.00102.06           C  
ANISOU 9119  CZ3 TRP B 641    13900  16448   8429    637    623   2281       C  
ATOM   9120  CH2 TRP B 641     -13.965  -3.822  55.507  1.00101.40           C  
ANISOU 9120  CH2 TRP B 641    13919  16279   8328    685    650   2328       C  
ATOM   9121  N   THR B 642     -13.309  -3.258  64.445  1.00130.57           N  
ANISOU 9121  N   THR B 642    18220  19054  12336    337    592   2424       N  
ATOM   9122  CA  THR B 642     -13.769  -3.625  65.802  1.00132.94           C  
ANISOU 9122  CA  THR B 642    18504  19347  12658    303    570   2422       C  
ATOM   9123  C   THR B 642     -14.385  -2.412  66.483  1.00131.44           C  
ANISOU 9123  C   THR B 642    18477  19116  12348    449    624   2479       C  
ATOM   9124  O   THR B 642     -14.199  -1.283  66.011  1.00124.28           O  
ANISOU 9124  O   THR B 642    17726  18132  11360    550    684   2522       O  
ATOM   9125  CB  THR B 642     -12.606  -4.180  66.677  1.00135.40           C  
ANISOU 9125  CB  THR B 642    18836  19507  13101    123    529   2401       C  
ATOM   9126  OG1 THR B 642     -11.480  -3.282  66.650  1.00135.52           O  
ANISOU 9126  OG1 THR B 642    19014  19360  13118     81    551   2419       O  
ATOM   9127  CG2 THR B 642     -12.167  -5.584  66.198  1.00134.58           C  
ANISOU 9127  CG2 THR B 642    18564  19451  13118     -5    483   2347       C  
ATOM   9128  N   LYS B 643     -15.130  -2.677  67.564  1.00136.42           N  
ANISOU 9128  N   LYS B 643    19073  19795  12965    463    610   2481       N  
ATOM   9129  CA  LYS B 643     -15.699  -1.642  68.455  1.00148.70           C  
ANISOU 9129  CA  LYS B 643    20780  21302  14416    588    658   2529       C  
ATOM   9130  C   LYS B 643     -14.625  -0.629  68.937  1.00151.65           C  
ANISOU 9130  C   LYS B 643    21382  21437  14798    537    698   2548       C  
ATOM   9131  O   LYS B 643     -14.832   0.605  68.946  1.00146.97           O  
ANISOU 9131  O   LYS B 643    20978  20763  14098    667    777   2592       O  
ATOM   9132  CB  LYS B 643     -16.253  -2.297  69.745  1.00154.50           C  
ANISOU 9132  CB  LYS B 643    21437  22083  15180    538    621   2515       C  
ATOM   9133  CG  LYS B 643     -17.467  -3.241  69.688  1.00161.79           C  
ANISOU 9133  CG  LYS B 643    22155  23238  16079    568    596   2490       C  
ATOM   9134  CD  LYS B 643     -17.562  -4.107  70.977  1.00168.10           C  
ANISOU 9134  CD  LYS B 643    22888  24024  16956    448    557   2471       C  
ATOM   9135  CE  LYS B 643     -18.948  -4.184  71.647  1.00171.55           C  
ANISOU 9135  CE  LYS B 643    23252  24630  17298    543    567   2479       C  
ATOM   9136  NZ  LYS B 643     -20.019  -4.705  70.754  1.00175.24           N  
ANISOU 9136  NZ  LYS B 643    23538  25349  17695    599    572   2447       N  
ATOM   9137  N   ALA B 644     -13.510  -1.217  69.398  1.00151.30           N  
ANISOU 9137  N   ALA B 644    21314  21293  14876    343    648   2511       N  
ATOM   9138  CA  ALA B 644     -12.376  -0.537  70.031  1.00147.02           C  
ANISOU 9138  CA  ALA B 644    20939  20564  14355    234    669   2503       C  
ATOM   9139  C   ALA B 644     -11.773   0.581  69.198  1.00145.49           C  
ANISOU 9139  C   ALA B 644    20923  20250  14107    262    743   2518       C  
ATOM   9140  O   ALA B 644     -11.393   1.619  69.725  1.00137.12           O  
ANISOU 9140  O   ALA B 644    20064  19042  12994    247    808   2523       O  
ATOM   9141  CB  ALA B 644     -11.300  -1.570  70.386  1.00146.43           C  
ANISOU 9141  CB  ALA B 644    20752  20470  14413     39    596   2463       C  
ATOM   9142  N   THR B 645     -11.681   0.349  67.893  1.00155.06           N  
ANISOU 9142  N   THR B 645    22062  21524  15329    292    740   2521       N  
ATOM   9143  CA  THR B 645     -11.067   1.290  66.934  1.00157.52           C  
ANISOU 9143  CA  THR B 645    22525  21731  15594    314    811   2540       C  
ATOM   9144  C   THR B 645     -12.027   2.406  66.500  1.00154.60           C  
ANISOU 9144  C   THR B 645    22304  21359  15077    544    911   2605       C  
ATOM   9145  O   THR B 645     -11.579   3.506  66.158  1.00150.36           O  
ANISOU 9145  O   THR B 645    21979  20670  14477    572   1006   2632       O  
ATOM   9146  CB  THR B 645     -10.568   0.532  65.688  1.00156.06           C  
ANISOU 9146  CB  THR B 645    22189  21627  15477    259    766   2518       C  
ATOM   9147  OG1 THR B 645     -11.683  -0.130  65.087  1.00159.24           O  
ANISOU 9147  OG1 THR B 645    22420  22228  15854    383    738   2526       O  
ATOM   9148  CG2 THR B 645      -9.488  -0.523  66.078  1.00154.30           C  
ANISOU 9148  CG2 THR B 645    21840  21392  15393     47    682   2461       C  
ATOM   9149  N   LEU B 646     -13.336   2.117  66.527  1.00157.86           N  
ANISOU 9149  N   LEU B 646    22609  21945  15426    708    899   2632       N  
ATOM   9150  CA  LEU B 646     -14.386   3.149  66.336  1.00163.77           C  
ANISOU 9150  CA  LEU B 646    23489  22721  16014    961    994   2704       C  
ATOM   9151  C   LEU B 646     -14.329   4.187  67.466  1.00162.05           C  
ANISOU 9151  C   LEU B 646    23515  22312  15742    980   1073   2722       C  
ATOM   9152  O   LEU B 646     -14.676   5.349  67.265  1.00160.46           O  
ANISOU 9152  O   LEU B 646    23525  22022  15418   1152   1190   2782       O  
ATOM   9153  CB  LEU B 646     -15.801   2.529  66.254  1.00169.19           C  
ANISOU 9153  CB  LEU B 646    23975  23674  16635   1115    955   2718       C  
ATOM   9154  CG  LEU B 646     -16.120   1.544  65.106  1.00173.23           C  
ANISOU 9154  CG  LEU B 646    24237  24414  17166   1118    894   2692       C  
ATOM   9155  CD1 LEU B 646     -17.194   0.522  65.478  1.00176.40           C  
ANISOU 9155  CD1 LEU B 646    24405  25054  17563   1127    828   2656       C  
ATOM   9156  CD2 LEU B 646     -16.519   2.288  63.848  1.00172.30           C  
ANISOU 9156  CD2 LEU B 646    24168  24381  16915   1327    968   2755       C  
ATOM   9157  N   LEU B 647     -13.861   3.753  68.632  1.00161.62           N  
ANISOU 9157  N   LEU B 647    23436  22196  15774    804   1016   2669       N  
ATOM   9158  CA  LEU B 647     -13.675   4.632  69.787  1.00162.89           C  
ANISOU 9158  CA  LEU B 647    23812  22183  15896    776   1082   2663       C  
ATOM   9159  C   LEU B 647     -12.433   5.494  69.630  1.00158.41           C  
ANISOU 9159  C   LEU B 647    23462  21389  15336    640   1159   2639       C  
ATOM   9160  O   LEU B 647     -12.435   6.665  70.005  1.00158.45           O  
ANISOU 9160  O   LEU B 647    23725  21225  15254    691   1277   2653       O  
ATOM   9161  CB  LEU B 647     -13.605   3.819  71.088  1.00162.52           C  
ANISOU 9161  CB  LEU B 647    23643  22179  15929    636    991   2615       C  
ATOM   9162  CG  LEU B 647     -14.731   2.790  71.284  1.00162.01           C  
ANISOU 9162  CG  LEU B 647    23343  22338  15873    719    912   2625       C  
ATOM   9163  CD1 LEU B 647     -14.411   1.857  72.448  1.00155.99           C  
ANISOU 9163  CD1 LEU B 647    22458  21598  15211    549    824   2580       C  
ATOM   9164  CD2 LEU B 647     -16.098   3.439  71.462  1.00160.14           C  
ANISOU 9164  CD2 LEU B 647    23168  22184  15493    965    975   2681       C  
ATOM   9165  N   ILE B 648     -11.384   4.920  69.056  1.00155.83           N  
ANISOU 9165  N   ILE B 648    23037  21060  15108    465   1102   2598       N  
ATOM   9166  CA  ILE B 648     -10.108   5.621  68.891  1.00152.79           C  
ANISOU 9166  CA  ILE B 648    22826  20491  14735    299   1165   2562       C  
ATOM   9167  C   ILE B 648     -10.241   6.833  67.994  1.00153.40           C  
ANISOU 9167  C   ILE B 648    23140  20439  14705    437   1309   2617       C  
ATOM   9168  O   ILE B 648      -9.676   7.907  68.288  1.00150.62           O  
ANISOU 9168  O   ILE B 648    23047  19880  14300    366   1427   2599       O  
ATOM   9169  CB  ILE B 648      -9.018   4.711  68.313  1.00149.57           C  
ANISOU 9169  CB  ILE B 648    22243  20142  14444    111   1073   2516       C  
ATOM   9170  CG1 ILE B 648      -8.853   3.480  69.235  1.00153.35           C  
ANISOU 9170  CG1 ILE B 648    22502  20737  15024    -10    945   2473       C  
ATOM   9171  CG2 ILE B 648      -7.724   5.499  68.130  1.00146.92           C  
ANISOU 9171  CG2 ILE B 648    22083  19638  14101    -64   1146   2475       C  
ATOM   9172  CD1 ILE B 648      -7.652   2.622  68.936  1.00153.42           C  
ANISOU 9172  CD1 ILE B 648    22362  20788  15142   -200    864   2426       C  
ATOM   9173  N   TRP B 649     -10.997   6.681  66.911  1.00152.74           N  
ANISOU 9173  N   TRP B 649    22975  20478  14578    636   1312   2682       N  
ATOM   9174  CA  TRP B 649     -11.167   7.800  66.011  1.00158.38           C  
ANISOU 9174  CA  TRP B 649    23911  21085  15180    799   1454   2752       C  
ATOM   9175  C   TRP B 649     -11.915   8.932  66.696  1.00166.87           C  
ANISOU 9175  C   TRP B 649    25243  22031  16128    971   1588   2800       C  
ATOM   9176  O   TRP B 649     -11.540  10.092  66.571  1.00176.03           O  
ANISOU 9176  O   TRP B 649    26696  22971  17217    984   1739   2820       O  
ATOM   9177  CB  TRP B 649     -11.850   7.380  64.708  1.00157.61           C  
ANISOU 9177  CB  TRP B 649    23653  21184  15046    990   1426   2814       C  
ATOM   9178  CG  TRP B 649     -10.964   6.524  63.891  1.00154.04           C  
ANISOU 9178  CG  TRP B 649    23019  20804  14704    822   1335   2768       C  
ATOM   9179  CD1 TRP B 649     -11.112   5.194  63.646  1.00154.20           C  
ANISOU 9179  CD1 TRP B 649    22740  21032  14814    767   1196   2730       C  
ATOM   9180  CD2 TRP B 649      -9.739   6.913  63.272  1.00153.09           C  
ANISOU 9180  CD2 TRP B 649    23009  20540  14618    668   1381   2747       C  
ATOM   9181  NE1 TRP B 649     -10.072   4.727  62.892  1.00153.32           N  
ANISOU 9181  NE1 TRP B 649    22546  20916  14790    608   1152   2691       N  
ATOM   9182  CE2 TRP B 649      -9.203   5.758  62.656  1.00153.47           C  
ANISOU 9182  CE2 TRP B 649    22802  20730  14776    542   1257   2700       C  
ATOM   9183  CE3 TRP B 649      -9.038   8.125  63.181  1.00151.89           C  
ANISOU 9183  CE3 TRP B 649    23151  20148  14409    616   1524   2758       C  
ATOM   9184  CZ2 TRP B 649      -8.000   5.773  61.951  1.00152.45           C  
ANISOU 9184  CZ2 TRP B 649    22690  20533  14700    379   1261   2670       C  
ATOM   9185  CZ3 TRP B 649      -7.841   8.144  62.477  1.00150.77           C  
ANISOU 9185  CZ3 TRP B 649    23026  19938  14320    437   1531   2723       C  
ATOM   9186  CH2 TRP B 649      -7.332   6.969  61.870  1.00150.91           C  
ANISOU 9186  CH2 TRP B 649    22770  20121  14445    325   1395   2681       C  
ATOM   9187  N   ARG B 650     -12.943   8.577  67.452  1.00173.63           N  
ANISOU 9187  N   ARG B 650    25996  23018  16957   1092   1538   2813       N  
ATOM   9188  CA  ARG B 650     -13.726   9.581  68.169  1.00182.36           C  
ANISOU 9188  CA  ARG B 650    27329  24020  17939   1272   1658   2858       C  
ATOM   9189  C   ARG B 650     -12.857  10.308  69.192  1.00180.23           C  
ANISOU 9189  C   ARG B 650    27298  23494  17685   1068   1735   2788       C  
ATOM   9190  O   ARG B 650     -12.952  11.522  69.324  1.00179.63           O  
ANISOU 9190  O   ARG B 650    27530  23214  17505   1162   1902   2818       O  
ATOM   9191  CB  ARG B 650     -14.935   8.923  68.853  1.00188.89           C  
ANISOU 9191  CB  ARG B 650    27961  25065  18742   1407   1571   2872       C  
ATOM   9192  CG  ARG B 650     -15.720   8.082  67.871  1.00193.98           C  
ANISOU 9192  CG  ARG B 650    28337  25993  19373   1554   1487   2914       C  
ATOM   9193  CD  ARG B 650     -17.213   8.078  68.119  1.00193.54           C  
ANISOU 9193  CD  ARG B 650    28200  26141  19195   1820   1491   2973       C  
ATOM   9194  NE  ARG B 650     -17.895   7.579  66.927  1.00188.61           N  
ANISOU 9194  NE  ARG B 650    27369  25777  18515   1979   1453   3017       N  
ATOM   9195  CZ  ARG B 650     -19.207   7.394  66.823  1.00184.68           C  
ANISOU 9195  CZ  ARG B 650    26728  25541  17900   2207   1441   3063       C  
ATOM   9196  NH1 ARG B 650     -20.014   7.620  67.863  1.00185.33           N  
ANISOU 9196  NH1 ARG B 650    26844  25658  17913   2311   1458   3076       N  
ATOM   9197  NH2 ARG B 650     -19.708   6.958  65.674  1.00181.22           N  
ANISOU 9197  NH2 ARG B 650    26097  25351  17405   2325   1410   3090       N  
ATOM   9198  N   ARG B 651     -12.011   9.553  69.893  1.00177.52           N  
ANISOU 9198  N   ARG B 651    26812  23171  17464    794   1621   2694       N  
ATOM   9199  CA  ARG B 651     -11.076  10.143  70.862  1.00176.72           C  
ANISOU 9199  CA  ARG B 651    26896  22874  17375    564   1679   2609       C  
ATOM   9200  C   ARG B 651     -10.141  11.101  70.138  1.00171.71           C  
ANISOU 9200  C   ARG B 651    26510  22024  16708    466   1818   2596       C  
ATOM   9201  O   ARG B 651      -9.880  12.215  70.622  1.00167.12           O  
ANISOU 9201  O   ARG B 651    26226  21217  16052    417   1970   2568       O  
ATOM   9202  CB  ARG B 651     -10.254   9.057  71.608  1.00173.12           C  
ANISOU 9202  CB  ARG B 651    26204  22524  17047    297   1523   2519       C  
ATOM   9203  CG  ARG B 651     -10.951   8.463  72.791  1.00168.61           C  
ANISOU 9203  CG  ARG B 651    25498  22075  16491    329   1436   2509       C  
ATOM   9204  CD  ARG B 651     -10.809   9.313  74.053  1.00170.23           C  
ANISOU 9204  CD  ARG B 651    25915  22129  16634    248   1522   2454       C  
ATOM   9205  NE  ARG B 651     -11.559   8.717  75.165  1.00178.51           N  
ANISOU 9205  NE  ARG B 651    26823  23310  17691    298   1437   2454       N  
ATOM   9206  CZ  ARG B 651     -11.685   9.253  76.385  1.00183.33           C  
ANISOU 9206  CZ  ARG B 651    27564  23844  18247    261   1485   2412       C  
ATOM   9207  NH1 ARG B 651     -11.118  10.424  76.681  1.00188.36           N  
ANISOU 9207  NH1 ARG B 651    28489  24265  18815    164   1628   2358       N  
ATOM   9208  NH2 ARG B 651     -12.385   8.610  77.323  1.00178.62           N  
ANISOU 9208  NH2 ARG B 651    26814  23389  17663    312   1398   2419       N  
ATOM   9209  N   THR B 652      -9.618  10.627  69.002  1.00170.05           N  
ANISOU 9209  N   THR B 652    26172  21883  16554    422   1767   2610       N  
ATOM   9210  CA  THR B 652      -8.733  11.458  68.189  1.00176.87           C  
ANISOU 9210  CA  THR B 652    27249  22562  17389    330   1894   2605       C  
ATOM   9211  C   THR B 652      -9.450  12.688  67.607  1.00184.57           C  
ANISOU 9211  C   THR B 652    28528  23376  18224    590   2090   2703       C  
ATOM   9212  O   THR B 652      -8.863  13.774  67.473  1.00176.60           O  
ANISOU 9212  O   THR B 652    27824  22120  17155    512   2261   2689       O  
ATOM   9213  CB  THR B 652      -8.107  10.652  67.048  1.00174.44           C  
ANISOU 9213  CB  THR B 652    26727  22384  17165    255   1795   2607       C  
ATOM   9214  OG1 THR B 652      -7.739   9.351  67.526  1.00171.11           O  
ANISOU 9214  OG1 THR B 652    25998  22149  16866     98   1609   2544       O  
ATOM   9215  CG2 THR B 652      -6.879  11.378  66.445  1.00168.20           C  
ANISOU 9215  CG2 THR B 652    26127  21414  16367     62   1904   2568       C  
ATOM   9216  N   TRP B 653     -10.718  12.501  67.266  1.00196.95           N  
ANISOU 9216  N   TRP B 653    30010  25091  19732    898   2070   2802       N  
ATOM   9217  CA  TRP B 653     -11.532  13.564  66.699  1.00208.24           C  
ANISOU 9217  CA  TRP B 653    31693  26416  21013   1202   2247   2916       C  
ATOM   9218  C   TRP B 653     -11.647  14.758  67.652  1.00216.79           C  
ANISOU 9218  C   TRP B 653    33129  27235  22003   1221   2425   2902       C  
ATOM   9219  O   TRP B 653     -11.567  15.912  67.231  1.00218.66           O  
ANISOU 9219  O   TRP B 653    33698  27240  22141   1315   2629   2954       O  
ATOM   9220  CB  TRP B 653     -12.924  13.011  66.364  1.00207.17           C  
ANISOU 9220  CB  TRP B 653    31343  26552  20819   1518   2169   3009       C  
ATOM   9221  CG  TRP B 653     -13.989  14.019  66.166  1.00203.05           C  
ANISOU 9221  CG  TRP B 653    31049  25976  20124   1872   2334   3128       C  
ATOM   9222  CD1 TRP B 653     -14.782  14.555  67.137  1.00200.85           C  
ANISOU 9222  CD1 TRP B 653    30912  25641  19758   2021   2407   3148       C  
ATOM   9223  CD2 TRP B 653     -14.415  14.591  64.929  1.00198.79           C  
ANISOU 9223  CD2 TRP B 653    30613  25450  19465   2146   2448   3252       C  
ATOM   9224  NE1 TRP B 653     -15.676  15.430  66.578  1.00201.62           N  
ANISOU 9224  NE1 TRP B 653    31200  25716  19687   2381   2563   3280       N  
ATOM   9225  CE2 TRP B 653     -15.477  15.471  65.223  1.00201.18           C  
ANISOU 9225  CE2 TRP B 653    31125  25707  19606   2469   2593   3350       C  
ATOM   9226  CE3 TRP B 653     -14.009  14.441  63.596  1.00196.79           C  
ANISOU 9226  CE3 TRP B 653    30293  25256  19219   2161   2445   3294       C  
ATOM   9227  CZ2 TRP B 653     -16.130  16.218  64.235  1.00200.12           C  
ANISOU 9227  CZ2 TRP B 653    31140  25585  19311   2818   2739   3495       C  
ATOM   9228  CZ3 TRP B 653     -14.661  15.183  62.610  1.00195.94           C  
ANISOU 9228  CZ3 TRP B 653    30330  25162  18955   2496   2587   3435       C  
ATOM   9229  CH2 TRP B 653     -15.710  16.060  62.940  1.00199.30           C  
ANISOU 9229  CH2 TRP B 653    30966  25543  19215   2826   2733   3538       C  
ATOM   9230  N   CYS B 654     -11.853  14.471  68.935  1.00216.32           N  
ANISOU 9230  N   CYS B 654    33006  27209  21973   1134   2356   2835       N  
ATOM   9231  CA  CYS B 654     -11.934  15.528  69.940  1.00210.86           C  
ANISOU 9231  CA  CYS B 654    32634  26280  21201   1124   2516   2802       C  
ATOM   9232  C   CYS B 654     -10.602  16.262  70.023  1.00210.72           C  
ANISOU 9232  C   CYS B 654    32865  25995  21201    818   2639   2704       C  
ATOM   9233  O   CYS B 654     -10.573  17.483  70.109  1.00225.57           O  
ANISOU 9233  O   CYS B 654    35119  27604  22982    859   2858   2713       O  
ATOM   9234  CB  CYS B 654     -12.295  14.958  71.317  1.00203.26           C  
ANISOU 9234  CB  CYS B 654    31517  25434  20278   1054   2397   2735       C  
ATOM   9235  SG  CYS B 654     -12.271  16.162  72.662  1.00194.57           S  
ANISOU 9235  SG  CYS B 654    30784  24056  19089    989   2578   2665       S  
ATOM   9236  N   ARG B 655      -9.507  15.505  69.988  1.00200.43           N  
ANISOU 9236  N   ARG B 655    31357  24778  20018    511   2506   2610       N  
ATOM   9237  CA  ARG B 655      -8.169  16.091  70.094  1.00193.32           C  
ANISOU 9237  CA  ARG B 655    30642  23677  19131    182   2604   2500       C  
ATOM   9238  C   ARG B 655      -7.918  17.193  69.082  1.00183.72           C  
ANISOU 9238  C   ARG B 655    29754  22219  17832    244   2822   2555       C  
ATOM   9239  O   ARG B 655      -8.309  17.061  67.933  1.00183.84           O  
ANISOU 9239  O   ARG B 655    29715  22302  17831    457   2819   2667       O  
ATOM   9240  CB  ARG B 655      -7.128  15.006  69.884  1.00196.68           C  
ANISOU 9240  CB  ARG B 655    30754  24288  19687    -84   2418   2424       C  
ATOM   9241  CG  ARG B 655      -5.668  15.403  69.890  1.00204.47           C  
ANISOU 9241  CG  ARG B 655    31849  25149  20689   -442   2483   2305       C  
ATOM   9242  CD  ARG B 655      -4.854  14.166  69.515  1.00209.59           C  
ANISOU 9242  CD  ARG B 655    32139  26035  21460   -613   2279   2267       C  
ATOM   9243  NE  ARG B 655      -3.409  14.333  69.578  1.00215.23           N  
ANISOU 9243  NE  ARG B 655    32878  26707  22191   -966   2302   2146       N  
ATOM   9244  CZ  ARG B 655      -2.533  13.458  69.080  1.00217.41           C  
ANISOU 9244  CZ  ARG B 655    32895  27156  22553  -1121   2165   2114       C  
ATOM   9245  NH1 ARG B 655      -2.939  12.337  68.477  1.00214.26           N  
ANISOU 9245  NH1 ARG B 655    32205  26964  22239   -964   2000   2189       N  
ATOM   9246  NH2 ARG B 655      -1.230  13.705  69.178  1.00223.00           N  
ANISOU 9246  NH2 ARG B 655    33636  27838  23254  -1441   2200   2001       N  
TER    9247      ARG B 655                                                      
HETATM 9248  C10 V0S A 701     -27.207 -23.042  68.275  1.00102.78           C  
HETATM 9249  C14 V0S A 701     -28.787 -22.168  70.014  1.00 92.25           C  
HETATM 9250  C13 V0S A 701     -27.979 -21.826  68.762  1.00102.29           C  
HETATM 9251  C12 V0S A 701     -26.866 -23.530  65.871  1.00114.92           C  
HETATM 9252  C15 V0S A 701     -28.464 -22.271  73.460  1.00 81.08           C  
HETATM 9253  C17 V0S A 701     -28.538 -23.933  75.383  1.00 87.41           C  
HETATM 9254  C19 V0S A 701     -29.318 -24.261  76.545  1.00 81.70           C  
HETATM 9255  C20 V0S A 701     -30.235 -23.232  76.833  1.00 85.09           C  
HETATM 9256  C21 V0S A 701     -31.069 -23.347  77.934  1.00 86.84           C  
HETATM 9257  C24 V0S A 701     -30.113 -25.477  78.454  1.00 96.41           C  
HETATM 9258  C03 V0S A 701     -31.536 -22.736  72.734  1.00 76.65           C  
HETATM 9259  C04 V0S A 701     -30.827 -23.893  73.023  1.00 74.63           C  
HETATM 9260  C05 V0S A 701     -29.516 -24.178  72.335  1.00 78.14           C  
HETATM 9261  C07 V0S A 701     -27.878 -22.711  71.115  1.00 87.57           C  
HETATM 9262  C08 V0S A 701     -27.073 -23.909  70.627  1.00 87.46           C  
HETATM 9263  C09 V0S A 701     -26.283 -23.552  69.368  1.00 98.65           C  
HETATM 9264  C16 V0S A 701     -28.926 -22.779  74.769  1.00 85.69           C  
HETATM 9265  C23 V0S A 701     -31.020 -24.462  78.737  1.00 92.60           C  
HETATM 9266  C25 V0S A 701     -29.276 -25.368  77.361  1.00 85.77           C  
HETATM 9267  C29 V0S A 701     -31.325 -24.780  73.983  1.00 72.32           C  
HETATM 9268  C30 V0S A 701     -32.523 -24.522  74.656  1.00 76.67           C  
HETATM 9269  C31 V0S A 701     -33.027 -25.428  75.643  1.00 77.30           C  
HETATM 9270  C32 V0S A 701     -32.328 -26.571  76.003  1.00 85.33           C  
HETATM 9271  C33 V0S A 701     -32.843 -27.419  76.971  1.00 91.99           C  
HETATM 9272  C35 V0S A 701     -34.676 -26.091  77.255  1.00 93.84           C  
HETATM 9273  C36 V0S A 701     -34.221 -25.189  76.306  1.00 80.12           C  
HETATM 9274  C37 V0S A 701     -33.211 -23.345  74.337  1.00 78.72           C  
HETATM 9275  C38 V0S A 701     -32.720 -22.463  73.387  1.00 75.88           C  
HETATM 9276  N06 V0S A 701     -28.615 -23.007  72.376  1.00 78.79           N  
HETATM 9277  N11 V0S A 701     -26.459 -22.743  67.029  1.00107.52           N  
HETATM 9278  N34 V0S A 701     -34.007 -27.199  77.588  1.00 94.40           N  
HETATM 9279  O28 V0S A 701     -27.969 -21.162  73.434  1.00 90.31           O  
HETATM 9280  S27 V0S A 701     -30.151 -21.932  75.685  1.00 82.74           S  
HETATM 9281 CL18 V0S A 701     -27.250 -24.971  74.864  1.00 89.81          CL  
HETATM 9282  C1  CLR A 702     -33.474 -33.439 103.422  1.00 84.82           C  
HETATM 9283  C2  CLR A 702     -33.236 -34.357 104.625  1.00 87.03           C  
HETATM 9284  C3  CLR A 702     -33.805 -35.776 104.451  1.00 87.14           C  
HETATM 9285  C4  CLR A 702     -33.265 -36.406 103.176  1.00 84.74           C  
HETATM 9286  C5  CLR A 702     -33.556 -35.486 102.008  1.00 80.37           C  
HETATM 9287  C6  CLR A 702     -34.220 -35.980 100.948  1.00 82.82           C  
HETATM 9288  C7  CLR A 702     -34.500 -35.186  99.682  1.00 84.25           C  
HETATM 9289  C8  CLR A 702     -33.633 -33.950  99.588  1.00 80.94           C  
HETATM 9290  C9  CLR A 702     -33.730 -33.223 100.931  1.00 83.10           C  
HETATM 9291  C10 CLR A 702     -33.072 -34.047 102.075  1.00 84.25           C  
HETATM 9292  C11 CLR A 702     -33.233 -31.776 100.844  1.00 77.56           C  
HETATM 9293  C12 CLR A 702     -33.815 -31.049  99.645  1.00 79.49           C  
HETATM 9294  C13 CLR A 702     -33.446 -31.740  98.336  1.00 80.28           C  
HETATM 9295  C14 CLR A 702     -34.104 -33.091  98.420  1.00 77.63           C  
HETATM 9296  C15 CLR A 702     -33.915 -33.641  97.017  1.00 79.53           C  
HETATM 9297  C16 CLR A 702     -34.048 -32.436  96.085  1.00 75.48           C  
HETATM 9298  C17 CLR A 702     -34.086 -31.231  97.026  1.00 80.85           C  
HETATM 9299  C18 CLR A 702     -31.914 -31.809  98.197  1.00 79.89           C  
HETATM 9300  C19 CLR A 702     -31.534 -34.070 101.989  1.00 81.07           C  
HETATM 9301  C20 CLR A 702     -33.524 -29.970  96.351  1.00 86.97           C  
HETATM 9302  C21 CLR A 702     -33.249 -28.803  97.295  1.00 90.51           C  
HETATM 9303  C22 CLR A 702     -34.482 -29.502  95.247  1.00 94.51           C  
HETATM 9304  C23 CLR A 702     -33.686 -29.314  93.964  1.00 97.42           C  
HETATM 9305  C24 CLR A 702     -34.540 -29.076  92.725  1.00 93.92           C  
HETATM 9306  C25 CLR A 702     -34.543 -27.609  92.303  1.00 90.21           C  
HETATM 9307  C26 CLR A 702     -34.622 -27.438  90.774  1.00 94.36           C  
HETATM 9308  C27 CLR A 702     -35.593 -26.835  93.097  1.00 82.12           C  
HETATM 9309  O1  CLR A 702     -33.501 -36.633 105.591  1.00 92.21           O  
HETATM 9310  C1  NAG A 703     -51.251 -14.706 103.028  1.00153.44           C  
HETATM 9311  C2  NAG A 703     -51.629 -14.159 101.652  1.00176.15           C  
HETATM 9312  C3  NAG A 703     -52.089 -12.708 101.835  1.00197.22           C  
HETATM 9313  C4  NAG A 703     -53.126 -12.554 102.967  1.00194.23           C  
HETATM 9314  C5  NAG A 703     -52.723 -13.324 104.251  1.00176.27           C  
HETATM 9315  C6  NAG A 703     -53.826 -13.343 105.316  1.00162.76           C  
HETATM 9316  C7  NAG A 703     -50.478 -14.775  99.516  1.00129.13           C  
HETATM 9317  C8  NAG A 703     -49.189 -14.754  98.726  1.00121.48           C  
HETATM 9318  N2  NAG A 703     -50.480 -14.228 100.741  1.00150.33           N  
HETATM 9319  O3  NAG A 703     -52.608 -12.207 100.591  1.00221.76           O  
HETATM 9320  O4  NAG A 703     -53.306 -11.147 103.233  1.00188.35           O  
HETATM 9321  O5  NAG A 703     -52.354 -14.679 103.937  1.00157.99           O  
HETATM 9322  O6  NAG A 703     -53.402 -14.078 106.477  1.00135.22           O  
HETATM 9323  O7  NAG A 703     -51.477 -15.270  99.039  1.00121.36           O  
HETATM 9324 NA    NA A 704     -37.694 -40.639 114.373  1.00 91.24          NA1+
HETATM 9325 NA    NA A 705     -48.549 -20.620  67.116  1.00 85.46          NA1+
HETATM 9326  C2  MPG A 706     -48.510 -34.237  66.866  1.00169.45           C  
HETATM 9327  C3  MPG A 706     -49.372 -33.423  65.902  1.00167.92           C  
HETATM 9328  C4  MPG A 706     -50.689 -32.934  66.515  1.00164.06           C  
HETATM 9329  C5  MPG A 706     -51.460 -31.850  65.754  1.00157.08           C  
HETATM 9330  C6  MPG A 706     -50.585 -30.708  65.230  1.00151.96           C  
HETATM 9331  C7  MPG A 706     -50.140 -30.804  63.764  1.00147.50           C  
HETATM 9332  C8  MPG A 706     -49.917 -32.185  63.126  1.00138.57           C  
HETATM 9333  C9  MPG A 706     -49.934 -32.033  61.617  1.00130.40           C  
HETATM 9334  C10 MPG A 706     -50.435 -32.984  60.836  1.00120.48           C  
HETATM 9335  C11 MPG A 706     -50.435 -32.797  59.334  1.00120.74           C  
HETATM 9336  C12 MPG A 706     -49.130 -33.326  58.734  1.00123.17           C  
HETATM 9337  C13 MPG A 706     -48.890 -32.940  57.264  1.00124.20           C  
HETATM 9338  C14 MPG A 706     -50.119 -33.131  56.373  1.00129.45           C  
HETATM 9339  C15 MPG A 706     -49.789 -33.287  54.885  1.00128.79           C  
HETATM 9340  C16 MPG A 706     -48.955 -32.156  54.274  1.00135.33           C  
HETATM 9341  C17 MPG A 706     -49.381 -30.708  54.591  1.00129.23           C  
HETATM 9342  C18 MPG A 706     -50.638 -30.270  53.887  1.00117.96           C  
HETATM 9343  O1  MPG A 706     -46.491 -35.628  66.637  1.00162.99           O  
HETATM 9344  C1  MPG A 706     -47.094 -34.378  66.303  1.00164.47           C  
HETATM 9345  CXD MPG A 706     -45.124 -37.216  65.087  1.00144.62           C  
HETATM 9346  O2  MPG A 706     -43.909 -37.859  65.515  1.00148.01           O  
HETATM 9347  C21 MPG A 706     -45.133 -36.892  63.571  1.00136.05           C  
HETATM 9348  O3  MPG A 706     -44.538 -37.897  62.719  1.00119.11           O  
HETATM 9349  CX3 MPG A 706     -45.262 -35.977  65.940  1.00149.93           C  
HETATM 9350  C10 V0S B 701       2.395 -14.032  34.188  1.00163.73           C  
HETATM 9351  C14 V0S B 701       2.957 -12.382  32.396  1.00163.34           C  
HETATM 9352  C13 V0S B 701       2.128 -12.640  33.652  1.00168.81           C  
HETATM 9353  C12 V0S B 701       2.514 -14.490  36.600  1.00156.03           C  
HETATM 9354  C15 V0S B 701       2.958 -12.738  28.994  1.00128.56           C  
HETATM 9355  C17 V0S B 701       3.952 -14.152  27.116  1.00119.32           C  
HETATM 9356  C19 V0S B 701       4.743 -14.047  25.918  1.00123.60           C  
HETATM 9357  C20 V0S B 701       4.980 -12.700  25.598  1.00124.85           C  
HETATM 9358  C21 V0S B 701       5.738 -12.393  24.478  1.00125.87           C  
HETATM 9359  C24 V0S B 701       6.048 -14.724  24.018  1.00124.83           C  
HETATM 9360  C03 V0S B 701       5.984 -11.246  29.939  1.00128.07           C  
HETATM 9361  C04 V0S B 701       5.935 -12.586  29.581  1.00126.70           C  
HETATM 9362  C05 V0S B 701       4.959 -13.528  30.256  1.00134.19           C  
HETATM 9363  C07 V0S B 701       2.690 -13.443  31.326  1.00156.74           C  
HETATM 9364  C08 V0S B 701       2.863 -14.863  31.872  1.00165.71           C  
HETATM 9365  C09 V0S B 701       2.043 -15.073  33.144  1.00171.09           C  
HETATM 9366  C16 V0S B 701       3.628 -12.953  27.673  1.00121.77           C  
HETATM 9367  C23 V0S B 701       6.273 -13.392  23.692  1.00133.57           C  
HETATM 9368  C25 V0S B 701       5.293 -15.039  25.127  1.00122.64           C  
HETATM 9369  C29 V0S B 701       6.814 -13.060  28.596  1.00111.33           C  
HETATM 9370  C30 V0S B 701       7.722 -12.209  27.958  1.00115.85           C  
HETATM 9371  C31 V0S B 701       8.588 -12.692  26.930  1.00128.91           C  
HETATM 9372  C32 V0S B 701       8.582 -14.025  26.542  1.00130.98           C  
HETATM 9373  C33 V0S B 701       9.421 -14.451  25.527  1.00124.31           C  
HETATM 9374  C35 V0S B 701      10.256 -12.345  25.242  1.00126.67           C  
HETATM 9375  C36 V0S B 701       9.448 -11.843  26.246  1.00125.14           C  
HETATM 9376  C37 V0S B 701       7.737 -10.862  28.341  1.00120.81           C  
HETATM 9377  C38 V0S B 701       6.878 -10.389  29.323  1.00121.09           C  
HETATM 9378  N06 V0S B 701       3.515 -13.201  30.104  1.00138.17           N  
HETATM 9379  N11 V0S B 701       1.664 -14.255  35.449  1.00150.29           N  
HETATM 9380  N34 V0S B 701      10.253 -13.631  24.883  1.00128.00           N  
HETATM 9381  O28 V0S B 701       1.916 -12.107  29.019  1.00125.99           O  
HETATM 9382  S27 V0S B 701       4.213 -11.611  26.718  1.00116.60           S  
HETATM 9383 CL18 V0S B 701       3.596 -15.704  27.788  1.00128.51          CL  
HETATM 9384  C1  CLR B 702      13.774 -22.958   0.180  1.00130.08           C  
HETATM 9385  C2  CLR B 702      13.981 -24.146  -0.780  1.00131.64           C  
HETATM 9386  C3  CLR B 702      14.938 -25.241  -0.268  1.00143.45           C  
HETATM 9387  C4  CLR B 702      14.576 -25.687   1.148  1.00148.28           C  
HETATM 9388  C5  CLR B 702      14.475 -24.455   2.048  1.00153.54           C  
HETATM 9389  C6  CLR B 702      15.262 -24.400   3.155  1.00153.24           C  
HETATM 9390  C7  CLR B 702      15.246 -23.235   4.121  1.00150.82           C  
HETATM 9391  C8  CLR B 702      13.911 -22.501   4.017  1.00151.72           C  
HETATM 9392  C9  CLR B 702      13.719 -22.083   2.540  1.00147.50           C  
HETATM 9393  C10 CLR B 702      13.504 -23.338   1.645  1.00145.31           C  
HETATM 9394  C11 CLR B 702      12.690 -20.941   2.326  1.00144.87           C  
HETATM 9395  C12 CLR B 702      12.641 -19.865   3.434  1.00146.83           C  
HETATM 9396  C13 CLR B 702      12.618 -20.415   4.865  1.00144.63           C  
HETATM 9397  C14 CLR B 702      13.851 -21.308   4.984  1.00150.17           C  
HETATM 9398  C15 CLR B 702      13.946 -21.591   6.477  1.00143.34           C  
HETATM 9399  C16 CLR B 702      13.453 -20.299   7.128  1.00137.75           C  
HETATM 9400  C17 CLR B 702      12.879 -19.405   6.017  1.00136.69           C  
HETATM 9401  C18 CLR B 702      11.303 -21.184   5.101  1.00147.39           C  
HETATM 9402  C19 CLR B 702      12.061 -23.865   1.788  1.00150.58           C  
HETATM 9403  C20 CLR B 702      11.761 -18.459   6.530  1.00136.07           C  
HETATM 9404  C21 CLR B 702      11.206 -17.561   5.426  1.00132.90           C  
HETATM 9405  C22 CLR B 702      12.239 -17.601   7.703  1.00136.30           C  
HETATM 9406  C23 CLR B 702      11.132 -16.863   8.462  1.00143.66           C  
HETATM 9407  C24 CLR B 702      11.415 -15.375   8.733  1.00150.28           C  
HETATM 9408  C25 CLR B 702      10.820 -14.861  10.065  1.00155.76           C  
HETATM 9409  C26 CLR B 702      11.762 -15.087  11.251  1.00154.99           C  
HETATM 9410  C27 CLR B 702      10.435 -13.383  10.006  1.00149.25           C  
HETATM 9411  O1  CLR B 702      14.964 -26.398  -1.140  1.00141.91           O  
CONECT   51  928                                                                
CONECT   89  575                                                                
CONECT  157  521                                                                
CONECT  235 9324                                                                
CONECT  258 9324                                                                
CONECT  275 9324                                                                
CONECT  449  729                                                                
CONECT  521  157                                                                
CONECT  575   89                                                                
CONECT  680  858                                                                
CONECT  729  449                                                                
CONECT  858  680                                                                
CONECT  928   51                                                                
CONECT 1012 9310                                                                
CONECT 1043 1206                                                                
CONECT 1206 1043                                                                
CONECT 1233 1852                                                                
CONECT 1852 1233                                                                
CONECT 1927 9325                                                                
CONECT 1938 9325                                                                
CONECT 1991 2588                                                                
CONECT 2588 1991                                                                
CONECT 4171 4295                                                                
CONECT 4295 4171                                                                
CONECT 4730 5607                                                                
CONECT 4768 5254                                                                
CONECT 4836 5200                                                                
CONECT 5128 5408                                                                
CONECT 5200 4836                                                                
CONECT 5254 4768                                                                
CONECT 5359 5537                                                                
CONECT 5408 5128                                                                
CONECT 5537 5359                                                                
CONECT 5607 4730                                                                
CONECT 5722 5885                                                                
CONECT 5885 5722                                                                
CONECT 5912 6531                                                                
CONECT 6531 5912                                                                
CONECT 6670 7267                                                                
CONECT 7267 6670                                                                
CONECT 8863 8878                                                                
CONECT 8878 8863                                                                
CONECT 9248 9250 9263 9277                                                      
CONECT 9249 9250 9261                                                           
CONECT 9250 9248 9249                                                           
CONECT 9251 9277                                                                
CONECT 9252 9264 9276 9279                                                      
CONECT 9253 9254 9264 9281                                                      
CONECT 9254 9253 9255 9266                                                      
CONECT 9255 9254 9256 9280                                                      
CONECT 9256 9255 9265                                                           
CONECT 9257 9265 9266                                                           
CONECT 9258 9259 9275                                                           
CONECT 9259 9258 9260 9267                                                      
CONECT 9260 9259 9276                                                           
CONECT 9261 9249 9262 9276                                                      
CONECT 9262 9261 9263                                                           
CONECT 9263 9248 9262                                                           
CONECT 9264 9252 9253 9280                                                      
CONECT 9265 9256 9257                                                           
CONECT 9266 9254 9257                                                           
CONECT 9267 9259 9268                                                           
CONECT 9268 9267 9269 9274                                                      
CONECT 9269 9268 9270 9273                                                      
CONECT 9270 9269 9271                                                           
CONECT 9271 9270 9278                                                           
CONECT 9272 9273 9278                                                           
CONECT 9273 9269 9272                                                           
CONECT 9274 9268 9275                                                           
CONECT 9275 9258 9274                                                           
CONECT 9276 9252 9260 9261                                                      
CONECT 9277 9248 9251                                                           
CONECT 9278 9271 9272                                                           
CONECT 9279 9252                                                                
CONECT 9280 9255 9264                                                           
CONECT 9281 9253                                                                
CONECT 9282 9283 9291                                                           
CONECT 9283 9282 9284                                                           
CONECT 9284 9283 9285 9309                                                      
CONECT 9285 9284 9286                                                           
CONECT 9286 9285 9287 9291                                                      
CONECT 9287 9286 9288                                                           
CONECT 9288 9287 9289                                                           
CONECT 9289 9288 9290 9295                                                      
CONECT 9290 9289 9291 9292                                                      
CONECT 9291 9282 9286 9290 9300                                                 
CONECT 9292 9290 9293                                                           
CONECT 9293 9292 9294                                                           
CONECT 9294 9293 9295 9298 9299                                                 
CONECT 9295 9289 9294 9296                                                      
CONECT 9296 9295 9297                                                           
CONECT 9297 9296 9298                                                           
CONECT 9298 9294 9297 9301                                                      
CONECT 9299 9294                                                                
CONECT 9300 9291                                                                
CONECT 9301 9298 9302 9303                                                      
CONECT 9302 9301                                                                
CONECT 9303 9301 9304                                                           
CONECT 9304 9303 9305                                                           
CONECT 9305 9304 9306                                                           
CONECT 9306 9305 9307 9308                                                      
CONECT 9307 9306                                                                
CONECT 9308 9306                                                                
CONECT 9309 9284                                                                
CONECT 9310 1012 9311 9321                                                      
CONECT 9311 9310 9312 9318                                                      
CONECT 9312 9311 9313 9319                                                      
CONECT 9313 9312 9314 9320                                                      
CONECT 9314 9313 9315 9321                                                      
CONECT 9315 9314 9322                                                           
CONECT 9316 9317 9318 9323                                                      
CONECT 9317 9316                                                                
CONECT 9318 9311 9316                                                           
CONECT 9319 9312                                                                
CONECT 9320 9313                                                                
CONECT 9321 9310 9314                                                           
CONECT 9322 9315                                                                
CONECT 9323 9316                                                                
CONECT 9324  235  258  275                                                      
CONECT 9325 1927 1938                                                           
CONECT 9326 9327 9344                                                           
CONECT 9327 9326 9328                                                           
CONECT 9328 9327 9329                                                           
CONECT 9329 9328 9330                                                           
CONECT 9330 9329 9331                                                           
CONECT 9331 9330 9332                                                           
CONECT 9332 9331 9333                                                           
CONECT 9333 9332 9334                                                           
CONECT 9334 9333 9335                                                           
CONECT 9335 9334 9336                                                           
CONECT 9336 9335 9337                                                           
CONECT 9337 9336 9338                                                           
CONECT 9338 9337 9339                                                           
CONECT 9339 9338 9340                                                           
CONECT 9340 9339 9341                                                           
CONECT 9341 9340 9342                                                           
CONECT 9342 9341                                                                
CONECT 9343 9344 9349                                                           
CONECT 9344 9326 9343                                                           
CONECT 9345 9346 9347 9349                                                      
CONECT 9346 9345                                                                
CONECT 9347 9345 9348                                                           
CONECT 9348 9347                                                                
CONECT 9349 9343 9345                                                           
CONECT 9350 9352 9365 9379                                                      
CONECT 9351 9352 9363                                                           
CONECT 9352 9350 9351                                                           
CONECT 9353 9379                                                                
CONECT 9354 9366 9378 9381                                                      
CONECT 9355 9356 9366 9383                                                      
CONECT 9356 9355 9357 9368                                                      
CONECT 9357 9356 9358 9382                                                      
CONECT 9358 9357 9367                                                           
CONECT 9359 9367 9368                                                           
CONECT 9360 9361 9377                                                           
CONECT 9361 9360 9362 9369                                                      
CONECT 9362 9361 9378                                                           
CONECT 9363 9351 9364 9378                                                      
CONECT 9364 9363 9365                                                           
CONECT 9365 9350 9364                                                           
CONECT 9366 9354 9355 9382                                                      
CONECT 9367 9358 9359                                                           
CONECT 9368 9356 9359                                                           
CONECT 9369 9361 9370                                                           
CONECT 9370 9369 9371 9376                                                      
CONECT 9371 9370 9372 9375                                                      
CONECT 9372 9371 9373                                                           
CONECT 9373 9372 9380                                                           
CONECT 9374 9375 9380                                                           
CONECT 9375 9371 9374                                                           
CONECT 9376 9370 9377                                                           
CONECT 9377 9360 9376                                                           
CONECT 9378 9354 9362 9363                                                      
CONECT 9379 9350 9353                                                           
CONECT 9380 9373 9374                                                           
CONECT 9381 9354                                                                
CONECT 9382 9357 9366                                                           
CONECT 9383 9355                                                                
CONECT 9384 9385 9393                                                           
CONECT 9385 9384 9386                                                           
CONECT 9386 9385 9387 9411                                                      
CONECT 9387 9386 9388                                                           
CONECT 9388 9387 9389 9393                                                      
CONECT 9389 9388 9390                                                           
CONECT 9390 9389 9391                                                           
CONECT 9391 9390 9392 9397                                                      
CONECT 9392 9391 9393 9394                                                      
CONECT 9393 9384 9388 9392 9402                                                 
CONECT 9394 9392 9395                                                           
CONECT 9395 9394 9396                                                           
CONECT 9396 9395 9397 9400 9401                                                 
CONECT 9397 9391 9396 9398                                                      
CONECT 9398 9397 9399                                                           
CONECT 9399 9398 9400                                                           
CONECT 9400 9396 9399 9403                                                      
CONECT 9401 9396                                                                
CONECT 9402 9393                                                                
CONECT 9403 9400 9404 9405                                                      
CONECT 9404 9403                                                                
CONECT 9405 9403 9406                                                           
CONECT 9406 9405 9407                                                           
CONECT 9407 9406 9408                                                           
CONECT 9408 9407 9409 9410                                                      
CONECT 9409 9408                                                                
CONECT 9410 9408                                                                
CONECT 9411 9386                                                                
MASTER      617    0    8   49   21    0    0    6 9409    2  206  100          
END