HEADER    MEMBRANE PROTEIN                        03-JUN-16   5L7D              
TITLE     STRUCTURE OF HUMAN SMOOTHENED IN COMPLEX WITH CHOLESTEROL             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SMOOTHENED HOMOLOG,SOLUBLE CYTOCHROME B562,SMOOTHENED      
COMPND   3 HOMOLOG;                                                             
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: UNP RESIDUES 32-428,UNP RESIDUES 23-127,UNP RESIDUES 443-  
COMPND   6 555;                                                                 
COMPND   7 SYNONYM: SMO,PROTEIN GX,CYTOCHROME B-562,SMO,PROTEIN GX;             
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: HUMAN SMOOTHENED WITH AN SOLUBLE E. COLI CYTOCHROME   
COMPND  10 B562 PROTEIN REPLACING SMOOTHENED RESIDUES 429 TO 445.               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 562;                                           
SOURCE   5 GENE: SMO, SMOH, CYBC;                                               
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK-293S-GNTI-;                         
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    G PROTEIN COUPLED RECEPTOR, MORPHOGEN SIGNALING, HEDGEHOG SIGNALING,  
KEYWDS   2 CHOLESTEROL, SIGNALING PROTEIN, MEMBRANE PROTEIN                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.F.X.BYRNE,R.SIRCAR,P.S.MILLER,G.HEDGER,G.LUCHETTI,S.NACHTERGAELE,   
AUTHOR   2 M.D.TULLY,L.MYDOCK-MCGRANE,D.F.COVEY,R.P.RAMBO,M.S.P.SANSOM,         
AUTHOR   3 S.NEWSTEAD,R.ROHATGI,C.SIEBOLD                                       
REVDAT   4   29-JUL-20 5L7D    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   10-AUG-16 5L7D    1       JRNL                                     
REVDAT   2   03-AUG-16 5L7D    1       JRNL                                     
REVDAT   1   20-JUL-16 5L7D    0                                                
JRNL        AUTH   E.F.BYRNE,R.SIRCAR,P.S.MILLER,G.HEDGER,G.LUCHETTI,           
JRNL        AUTH 2 S.NACHTERGAELE,M.D.TULLY,L.MYDOCK-MCGRANE,D.F.COVEY,         
JRNL        AUTH 3 R.P.RAMBO,M.S.SANSOM,S.NEWSTEAD,R.ROHATGI,C.SIEBOLD          
JRNL        TITL   STRUCTURAL BASIS OF SMOOTHENED REGULATION BY ITS             
JRNL        TITL 2 EXTRACELLULAR DOMAINS.                                       
JRNL        REF    NATURE                        V. 535   517 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   27437577                                                     
JRNL        DOI    10.1038/NATURE18934                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 25151                          
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)  : 0.232                          
REMARK   3   R VALUE            (WORKING SET)  : 0.230                          
REMARK   3   FREE R VALUE                      : 0.264                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.180                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1302                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.33                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 72.86                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2181                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2576                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2086                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2584                   
REMARK   3   BIN FREE R VALUE                        : 0.2372                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.36                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 95                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9207                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 76.23                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 137.8                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 13.64150                                             
REMARK   3    B22 (A**2) : -25.08140                                            
REMARK   3    B33 (A**2) : 11.43990                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -23.54590                                            
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.628               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.504               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.895                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.888                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 9525   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 12971  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 4307   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 200    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1390   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 9525   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1237   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 10952  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.90                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.05                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.97                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|58 - A|190 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -46.0203   -3.9808  107.8299           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0336 T22:   -0.2889                                    
REMARK   3     T33:    0.0931 T12:    0.0945                                    
REMARK   3     T13:   -0.0188 T23:   -0.0254                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    7.7190 L22:    5.2841                                    
REMARK   3     L33:    7.8227 L12:   -0.0448                                    
REMARK   3     L13:   -2.2833 L23:   -1.0917                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0331 S12:   -0.2428 S13:   -0.3801                     
REMARK   3     S21:    0.0453 S22:   -0.0301 S23:   -0.2783                     
REMARK   3     S31:   -0.0232 S32:   -0.1463 S33:    0.0632                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|191 - A|216 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -41.2594    7.3390   85.4941           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1104 T22:    0.1396                                    
REMARK   3     T33:   -0.0189 T12:    0.0622                                    
REMARK   3     T13:    0.1018 T23:    0.0258                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.1615 L22:    0.1016                                    
REMARK   3     L33:    1.4860 L12:    0.8072                                    
REMARK   3     L13:   -0.4723 L23:   -0.4256                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0166 S12:    0.0175 S13:   -0.0266                     
REMARK   3     S21:   -0.0139 S22:   -0.0135 S23:    0.0930                     
REMARK   3     S31:    0.1228 S32:   -0.0195 S33:   -0.0031                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|217 - A|553 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -29.3951   10.6650   56.6725           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1752 T22:    0.3294                                    
REMARK   3     T33:   -0.2687 T12:    0.0338                                    
REMARK   3     T13:    0.0421 T23:    0.0893                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6166 L22:    0.7908                                    
REMARK   3     L33:    5.6272 L12:   -0.0818                                    
REMARK   3     L13:   -0.4438 L23:   -0.7001                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0444 S12:    0.5113 S13:   -0.0771                     
REMARK   3     S21:    0.0041 S22:    0.1004 S23:    0.0301                     
REMARK   3     S31:   -0.0983 S32:   -0.5741 S33:   -0.1448                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { A|1011 - A|1131 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):    1.1285   -8.4131   13.1706           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0617 T22:    0.3339                                    
REMARK   3     T33:   -0.1309 T12:    0.0017                                    
REMARK   3     T13:    0.2228 T23:   -0.0976                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4756 L22:    1.8024                                    
REMARK   3     L33:    3.3058 L12:   -1.5947                                    
REMARK   3     L13:    0.5172 L23:    1.4680                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0037 S12:   -0.0127 S13:   -0.0227                     
REMARK   3     S21:   -0.0643 S22:   -0.0273 S23:    0.0463                     
REMARK   3     S31:   -0.0015 S32:   -0.0068 S33:    0.0310                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { B|58 - B|190 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   22.8309   14.1804   -5.2432           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0074 T22:    0.3734                                    
REMARK   3     T33:   -0.2235 T12:   -0.0381                                    
REMARK   3     T13:    0.1821 T23:    0.0097                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.6941 L22:    0.0051                                    
REMARK   3     L33:    4.9280 L12:   -1.0329                                    
REMARK   3     L13:   -1.2333 L23:   -1.0791                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0492 S12:   -0.0110 S13:   -0.1456                     
REMARK   3     S21:   -0.1723 S22:   -0.0512 S23:   -0.0770                     
REMARK   3     S31:   -0.0317 S32:   -0.0264 S33:    0.0019                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { B|191 - B|216 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   13.1380   23.8969   16.5240           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0280 T22:    0.2612                                    
REMARK   3     T33:   -0.1701 T12:   -0.0502                                    
REMARK   3     T13:    0.0975 T23:    0.0682                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8473 L22:    0.0000                                    
REMARK   3     L33:    1.9485 L12:   -0.5452                                    
REMARK   3     L13:   -0.7060 L23:   -0.6270                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0066 S12:    0.0263 S13:    0.0447                     
REMARK   3     S21:   -0.0032 S22:    0.0060 S23:   -0.0416                     
REMARK   3     S31:    0.0044 S32:   -0.0078 S33:    0.0006                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { B|217 - B|551 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):    1.4431   20.6318   47.9173           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2244 T22:    0.4753                                    
REMARK   3     T33:   -0.3472 T12:   -0.1449                                    
REMARK   3     T13:    0.0842 T23:    0.1682                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4808 L22:    0.7870                                    
REMARK   3     L33:    3.0739 L12:    0.2053                                    
REMARK   3     L13:   -0.3519 L23:    0.2882                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0612 S12:    0.4426 S13:   -0.2068                     
REMARK   3     S21:    0.0211 S22:    0.0342 S23:   -0.1518                     
REMARK   3     S31:   -0.4139 S32:    0.1398 S33:   -0.0955                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { B|1011 - B|1131 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.5375   -9.7922   90.5620           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0909 T22:   -0.1507                                    
REMARK   3     T33:    0.0190 T12:   -0.1265                                    
REMARK   3     T13:   -0.0443 T23:   -0.0748                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.6160 L22:    4.0122                                    
REMARK   3     L33:    3.6242 L12:    3.4513                                    
REMARK   3     L13:   -2.9937 L23:   -2.9251                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0241 S12:    0.2293 S13:   -0.0770                     
REMARK   3     S21:    0.0528 S22:   -0.1330 S23:   -0.0659                     
REMARK   3     S31:    0.0891 S32:    0.2891 S33:    0.1089                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: { D|1 }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -34.4722   -2.2365   98.9728           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0656 T22:    0.0456                                    
REMARK   3     T33:    0.0437 T12:   -0.0537                                    
REMARK   3     T13:    0.0167 T23:    0.0759                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6195 L22:    0.0000                                    
REMARK   3     L33:   -0.0745 L12:   -0.0072                                    
REMARK   3     L13:   -0.2841 L23:   -0.7273                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0017 S12:    0.0080 S13:    0.0154                     
REMARK   3     S21:   -0.0225 S22:   -0.0005 S23:    0.0002                     
REMARK   3     S31:   -0.0096 S32:   -0.0011 S33:   -0.0013                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5L7D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200000252.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-SEP-15                          
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 PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25214                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.30500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.600                              
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: 4QIM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6, 30% (V/V) PEG500 DME,    
REMARK 280  0.1 M SODIUM ACETATE, 0.5 MM ZINC CHLORIDE, 0.1 M AMMONIUM          
REMARK 280  FLUORIDE, PH 6.0, 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       61.45000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.51000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       61.45000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.51000            
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     GLY A   347                                                      
REMARK 465     THR A   348                                                      
REMARK 465     THR A   349                                                      
REMARK 465     TYR A   350                                                      
REMARK 465     LYS A  1062                                                      
REMARK 465     LEU A  1063                                                      
REMARK 465     GLU A  1064                                                      
REMARK 465     ASP A  1065                                                      
REMARK 465     LYS A  1066                                                      
REMARK 465     SER A  1067                                                      
REMARK 465     PRO A  1068                                                      
REMARK 465     ASP A  1069                                                      
REMARK 465     GLY A   554                                                      
REMARK 465     GLN A   555                                                      
REMARK 465     GLY A   556                                                      
REMARK 465     THR A   557                                                      
REMARK 465     GLU A   558                                                      
REMARK 465     THR A   559                                                      
REMARK 465     SER A   560                                                      
REMARK 465     GLN A   561                                                      
REMARK 465     VAL A   562                                                      
REMARK 465     ALA A   563                                                      
REMARK 465     PRO A   564                                                      
REMARK 465     ALA A   565                                                      
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  1062                                                      
REMARK 465     LEU B  1063                                                      
REMARK 465     GLU B  1064                                                      
REMARK 465     ASP B  1065                                                      
REMARK 465     LYS B  1066                                                      
REMARK 465     ALA B   492                                                      
REMARK 465     ASN B   493                                                      
REMARK 465     VAL B   494                                                      
REMARK 465     THR B   495                                                      
REMARK 465     ILE B   496                                                      
REMARK 465     GLY B   497                                                      
REMARK 465     LEU B   498                                                      
REMARK 465     PRO B   499                                                      
REMARK 465     THR B   500                                                      
REMARK 465     LYS B   501                                                      
REMARK 465     GLN B   502                                                      
REMARK 465     PRO B   503                                                      
REMARK 465     ILE B   504                                                      
REMARK 465     PRO B   505                                                      
REMARK 465     ASP B   506                                                      
REMARK 465     LEU B   552                                                      
REMARK 465     THR B   553                                                      
REMARK 465     GLY B   554                                                      
REMARK 465     GLN B   555                                                      
REMARK 465     GLY B   556                                                      
REMARK 465     THR B   557                                                      
REMARK 465     GLU B   558                                                      
REMARK 465     THR B   559                                                      
REMARK 465     SER B   560                                                      
REMARK 465     GLN B   561                                                      
REMARK 465     VAL B   562                                                      
REMARK 465     ALA B   563                                                      
REMARK 465     PRO B   564                                                      
REMARK 465     ALA B   565                                                      
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    THR A  90       31.17    -92.68                                   
REMARK 500    ALA A 115       74.08     89.27                                   
REMARK 500    MET A 131       65.00   -119.85                                   
REMARK 500    CYS A 154       42.17    -92.24                                   
REMARK 500    GLU A 160      -63.41    -97.77                                   
REMARK 500    GLU A 181      -33.31     80.99                                   
REMARK 500    GLU A 208     -125.39     35.79                                   
REMARK 500    ASP A 287      105.90    -51.88                                   
REMARK 500    THR A 307     -128.75     56.44                                   
REMARK 500    SER A 308      -66.02   -144.70                                   
REMARK 500    ALA A 379       76.13     50.98                                   
REMARK 500    VAL A 404      -54.71   -125.49                                   
REMARK 500    TRP A 537       57.31    -97.42                                   
REMARK 500    THR B  90       31.12    -92.56                                   
REMARK 500    CYS B 154       42.38    -92.75                                   
REMARK 500    GLU B 160      -71.45    -72.98                                   
REMARK 500    GLU B 176      -80.25    -42.60                                   
REMARK 500    GLU B 208     -119.11     40.28                                   
REMARK 500    ASP B 287      105.81    -51.60                                   
REMARK 500    THR B 348     -125.37     56.33                                   
REMARK 500    ALA B 379       73.87     50.92                                   
REMARK 500    VAL B 404      -54.70   -125.49                                   
REMARK 500    SER B1070      139.33    -39.74                                   
REMARK 500    TRP B 537       57.13    -97.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A1204  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  90   O                                                      
REMARK 620 2 ALA A  93   O    73.6                                              
REMARK 620 3 SER A  96   O    73.8  75.1                                        
REMARK 620 N                    1     2                                         
DBREF  5L7D A   32   428  UNP    Q99835   SMO_HUMAN       32    428             
DBREF  5L7D A 1016  1120  UNP    P0ABE7   C562_ECOLX      23    127             
DBREF  5L7D A 1129   555  UNP    Q99835   SMO_HUMAN      443    555             
DBREF  5L7D B   32   428  UNP    Q99835   SMO_HUMAN       32    428             
DBREF  5L7D B 1016  1120  UNP    P0ABE7   C562_ECOLX      23    127             
DBREF  5L7D B 1129   555  UNP    Q99835   SMO_HUMAN      443    555             
SEQADV 5L7D PHE A  329  UNP  Q99835    VAL   329 CONFLICT                       
SEQADV 5L7D ALA A 1011  UNP  Q99835              LINKER                         
SEQADV 5L7D ARG A 1012  UNP  Q99835              LINKER                         
SEQADV 5L7D ARG A 1013  UNP  Q99835              LINKER                         
SEQADV 5L7D GLN A 1014  UNP  Q99835              LINKER                         
SEQADV 5L7D LEU A 1015  UNP  Q99835              LINKER                         
SEQADV 5L7D TRP A 1022  UNP  P0ABE7    MET    29 CONFLICT                       
SEQADV 5L7D ILE A 1117  UNP  P0ABE7    HIS   124 CONFLICT                       
SEQADV 5L7D LEU A 1121  UNP  P0ABE7              LINKER                         
SEQADV 5L7D GLU A 1122  UNP  P0ABE7              LINKER                         
SEQADV 5L7D ARG A 1123  UNP  P0ABE7              LINKER                         
SEQADV 5L7D ALA A 1124  UNP  P0ABE7              LINKER                         
SEQADV 5L7D ARG A 1125  UNP  P0ABE7              LINKER                         
SEQADV 5L7D SER A 1126  UNP  P0ABE7              LINKER                         
SEQADV 5L7D THR A 1127  UNP  P0ABE7              LINKER                         
SEQADV 5L7D LEU A 1128  UNP  P0ABE7              LINKER                         
SEQADV 5L7D GLY A  556  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D THR A  557  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D GLU A  558  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D THR A  559  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D SER A  560  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D GLN A  561  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D VAL A  562  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D ALA A  563  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D PRO A  564  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D ALA A  565  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D PHE B  329  UNP  Q99835    VAL   329 CONFLICT                       
SEQADV 5L7D ALA B 1011  UNP  Q99835              LINKER                         
SEQADV 5L7D ARG B 1012  UNP  Q99835              LINKER                         
SEQADV 5L7D ARG B 1013  UNP  Q99835              LINKER                         
SEQADV 5L7D GLN B 1014  UNP  Q99835              LINKER                         
SEQADV 5L7D LEU B 1015  UNP  Q99835              LINKER                         
SEQADV 5L7D TRP B 1022  UNP  P0ABE7    MET    29 CONFLICT                       
SEQADV 5L7D ILE B 1117  UNP  P0ABE7    HIS   124 CONFLICT                       
SEQADV 5L7D LEU B 1121  UNP  P0ABE7              LINKER                         
SEQADV 5L7D GLU B 1122  UNP  P0ABE7              LINKER                         
SEQADV 5L7D ARG B 1123  UNP  P0ABE7              LINKER                         
SEQADV 5L7D ALA B 1124  UNP  P0ABE7              LINKER                         
SEQADV 5L7D ARG B 1125  UNP  P0ABE7              LINKER                         
SEQADV 5L7D SER B 1126  UNP  P0ABE7              LINKER                         
SEQADV 5L7D THR B 1127  UNP  P0ABE7              LINKER                         
SEQADV 5L7D LEU B 1128  UNP  P0ABE7              LINKER                         
SEQADV 5L7D GLY B  556  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D THR B  557  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D GLU B  558  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D THR B  559  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D SER B  560  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D GLN B  561  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D VAL B  562  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D ALA B  563  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D PRO B  564  UNP  Q99835              EXPRESSION TAG                 
SEQADV 5L7D ALA B  565  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    NAG  A1201      14                                                       
HET    NAG  A1202      14                                                       
HET    CLR  A1203      28                                                       
HET     NA  A1204       1                                                       
HET     NA  A1205       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     CLR CHOLESTEROL                                                      
HETNAM      NA SODIUM ION                                                       
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   5  CLR    C27 H46 O                                                    
FORMUL   6   NA    2(NA 1+)                                                     
HELIX    1 AA1 SER A   98  SER A  110  1                                  13    
HELIX    2 AA2 GLY A  111  ASN A  114  5                                   4    
HELIX    3 AA3 ALA A  115  MET A  131  1                                  17    
HELIX    4 AA4 SER A  143  GLY A  152  1                                  10    
HELIX    5 AA5 CYS A  154  ARG A  161  1                                   8    
HELIX    6 AA6 PRO A  164  ARG A  168  5                                   5    
HELIX    7 AA7 THR A  223  ASP A  255  1                                  33    
HELIX    8 AA8 ASP A  255  ASN A  260  1                                   6    
HELIX    9 AA9 PRO A  263  ALA A  283  1                                  21    
HELIX   10 AB1 GLN A  284  MET A  286  5                                   3    
HELIX   11 AB2 GLY A  288  CYS A  295  1                                   8    
HELIX   12 AB3 LEU A  312  PHE A  343  1                                  32    
HELIX   13 AB4 LYS A  344  LEU A  346  5                                   3    
HELIX   14 AB5 LYS A  356  ALA A  379  1                                  24    
HELIX   15 AB6 ASN A  396  VAL A  404  1                                   9    
HELIX   16 AB7 VAL A  404  ALA A 1035  1                                  50    
HELIX   17 AB8 ASN A 1037  LYS A 1057  1                                  21    
HELIX   18 AB9 PRO A 1071  GLY A 1097  1                                  27    
HELIX   19 AC1 LYS A 1098  TYR A 1116  1                                  19    
HELIX   20 AC2 TYR A 1116  LYS A 1130  1                                  15    
HELIX   21 AC3 ASN A  446  VAL A  494  1                                  49    
HELIX   22 AC4 SER A  514  MET A  532  1                                  19    
HELIX   23 AC5 SER A  533  TRP A  537  5                                   5    
HELIX   24 AC6 THR A  538  THR A  553  1                                  16    
HELIX   25 AC7 SER B   98  SER B  110  1                                  13    
HELIX   26 AC8 GLY B  111  ARG B  113  5                                   3    
HELIX   27 AC9 ALA B  115  MET B  131  1                                  17    
HELIX   28 AD1 SER B  143  GLY B  152  1                                  10    
HELIX   29 AD2 CYS B  154  ARG B  161  1                                   8    
HELIX   30 AD3 PRO B  164  ARG B  168  5                                   5    
HELIX   31 AD4 ASN B  180  ASN B  184  5                                   5    
HELIX   32 AD5 THR B  223  ASP B  255  1                                  33    
HELIX   33 AD6 ASP B  255  ASN B  260  1                                   6    
HELIX   34 AD7 PRO B  263  ALA B  283  1                                  21    
HELIX   35 AD8 GLN B  284  MET B  286  5                                   3    
HELIX   36 AD9 GLY B  288  CYS B  295  1                                   8    
HELIX   37 AE1 LEU B  312  PHE B  343  1                                  32    
HELIX   38 AE2 LYS B  356  ALA B  379  1                                  24    
HELIX   39 AE3 ASN B  396  VAL B  404  1                                   9    
HELIX   40 AE4 VAL B  404  ALA B 1035  1                                  50    
HELIX   41 AE5 ASN B 1037  ALA B 1058  1                                  22    
HELIX   42 AE6 SER B 1070  GLY B 1097  1                                  28    
HELIX   43 AE7 LYS B 1098  TYR B 1116  1                                  19    
HELIX   44 AE8 TYR B 1116  LYS B 1130  1                                  15    
HELIX   45 AE9 ASN B  446  GLN B  491  1                                  46    
HELIX   46 AF1 SER B  514  MET B  532  1                                  19    
HELIX   47 AF2 SER B  533  TRP B  537  5                                   5    
HELIX   48 AF3 THR B  538  ARG B  551  1                                  14    
SHEET    1 AA1 2 GLY A  65  ALA A  67  0                                        
SHEET    2 AA1 2 ARG A 138  GLU A 140 -1  O  VAL A 139   N  ARG A  66           
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  GLY A 383  0                                        
SHEET    2 AA5 2 CYS A 390  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  GLY B 383  0                                        
SHEET    2 AB1 2 CYS B 390  VAL B 392 -1  O  PHE B 391   N  ASP B 382           
SSBOND   1 CYS A   64    CYS A  178                          1555   1555  2.04  
SSBOND   2 CYS A   70    CYS A  134                          1555   1555  2.04  
SSBOND   3 CYS A   78    CYS A  127                          1555   1555  2.04  
SSBOND   4 CYS A  118    CYS A  154                          1555   1555  2.03  
SSBOND   5 CYS A  147    CYS A  169                          1555   1555  2.04  
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  2.03  
SSBOND   9 CYS A  490    CYS A  507                          1555   1555  2.04  
SSBOND  10 CYS B   64    CYS B  178                          1555   1555  2.04  
SSBOND  11 CYS B   70    CYS B  134                          1555   1555  2.04  
SSBOND  12 CYS B   78    CYS B  127                          1555   1555  2.04  
SSBOND  13 CYS B  118    CYS B  154                          1555   1555  2.04  
SSBOND  14 CYS B  147    CYS B  169                          1555   1555  2.04  
SSBOND  15 CYS B  193    CYS B  213                          1555   1555  2.04  
SSBOND  16 CYS B  217    CYS B  295                          1555   1555  2.03  
SSBOND  17 CYS B  314    CYS B  390                          1555   1555  2.03  
SSBOND  18 CYS B  490    CYS B  507                          1555   1555  2.03  
LINK         ND2 ASN A 188                 C1  NAG A1201     1555   1555  1.44  
LINK         ND2 ASN A 493                 C1  NAG A1202     1555   1555  1.43  
LINK         O   THR A  90                NA    NA A1204     1555   1555  2.85  
LINK         O   ALA A  93                NA    NA A1204     1555   1555  2.33  
LINK         O   SER A  96                NA    NA A1204     1555   1555  2.48  
LINK         O   PRO A 306                NA    NA A1205     1555   1555  2.76  
CISPEP   1 VAL A  195    PRO A  196          0         7.08                     
CISPEP   2 TYR A  262    PRO A  263          0         3.53                     
CISPEP   3 GLU A  305    PRO A  306          0         9.52                     
CISPEP   4 VAL B  195    PRO B  196          0         7.64                     
CISPEP   5 TYR B  262    PRO B  263          0         3.67                     
CISPEP   6 GLU B  305    PRO B  306          0         6.41                     
CRYST1  122.900   63.020  208.590  90.00  96.64  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      0.008137  0.000000  0.000947        0.00000                         
SCALE2      0.000000  0.015868  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004826        0.00000                         
ATOM      1  N   PRO A  58     -67.220  -6.826 114.969  1.00171.37           N  
ANISOU    1  N   PRO A  58    17029  24998  23086    176   1975   1568       N  
ATOM      2  CA  PRO A  58     -67.148  -8.259 115.290  1.00172.58           C  
ANISOU    2  CA  PRO A  58    17215  24923  23434   -475   2057   1706       C  
ATOM      3  C   PRO A  58     -65.862  -8.633 116.051  1.00171.93           C  
ANISOU    3  C   PRO A  58    17841  24258  23226   -471   2122   1754       C  
ATOM      4  O   PRO A  58     -64.855  -7.926 115.903  1.00166.90           O  
ANISOU    4  O   PRO A  58    17667  23327  22420   -110   1948   1575       O  
ATOM      5  CB  PRO A  58     -67.195  -8.927 113.911  1.00174.38           C  
ANISOU    5  CB  PRO A  58    17277  25050  23930   -946   1666   1502       C  
ATOM      6  CG  PRO A  58     -66.636  -7.908 112.962  1.00174.75           C  
ANISOU    6  CG  PRO A  58    17530  25033  23834   -503   1336   1256       C  
ATOM      7  CD  PRO A  58     -66.799  -6.541 113.582  1.00169.92           C  
ANISOU    7  CD  PRO A  58    16927  24665  22972    203   1534   1326       C  
ATOM      8  N   PRO A  59     -65.844  -9.746 116.843  1.00170.07           N  
ANISOU    8  N   PRO A  59    17687  23850  23081   -874   2362   2024       N  
ATOM      9  CA  PRO A  59     -64.607 -10.130 117.555  1.00166.46           C  
ANISOU    9  CA  PRO A  59    17862  22894  22490   -826   2391   2134       C  
ATOM     10  C   PRO A  59     -63.522 -10.581 116.579  1.00163.69           C  
ANISOU   10  C   PRO A  59    17886  21966  22344   -980   2028   1915       C  
ATOM     11  O   PRO A  59     -63.870 -11.203 115.577  1.00164.37           O  
ANISOU   11  O   PRO A  59    17760  21954  22740  -1378   1866   1773       O  
ATOM     12  CB  PRO A  59     -65.065 -11.282 118.457  1.00173.52           C  
ANISOU   12  CB  PRO A  59    18658  23781  23492  -1244   2746   2542       C  
ATOM     13  CG  PRO A  59     -66.570 -11.110 118.556  1.00183.58           C  
ANISOU   13  CG  PRO A  59    19243  25684  24826  -1359   2998   2639       C  
ATOM     14  CD  PRO A  59     -66.930 -10.689 117.166  1.00177.82           C  
ANISOU   14  CD  PRO A  59    18183  25089  24290  -1383   2634   2287       C  
ATOM     15  N   PRO A  60     -62.230 -10.241 116.806  1.00153.98           N  
ANISOU   15  N   PRO A  60    17178  20396  20930   -677   1894   1852       N  
ATOM     16  CA  PRO A  60     -61.193 -10.607 115.822  1.00149.12           C  
ANISOU   16  CA  PRO A  60    16870  19275  20513   -774   1585   1638       C  
ATOM     17  C   PRO A  60     -60.931 -12.104 115.759  1.00151.35           C  
ANISOU   17  C   PRO A  60    17289  19085  21133  -1235   1649   1801       C  
ATOM     18  O   PRO A  60     -60.932 -12.776 116.794  1.00154.04           O  
ANISOU   18  O   PRO A  60    17726  19340  21462  -1336   1907   2170       O  
ATOM     19  CB  PRO A  60     -59.953  -9.830 116.278  1.00147.15           C  
ANISOU   19  CB  PRO A  60    17058  18877  19976   -341   1478   1584       C  
ATOM     20  CG  PRO A  60     -60.179  -9.513 117.703  1.00154.31           C  
ANISOU   20  CG  PRO A  60    17999  20084  20546   -143   1747   1830       C  
ATOM     21  CD  PRO A  60     -61.666  -9.487 117.944  1.00154.35           C  
ANISOU   21  CD  PRO A  60    17527  20553  20566   -253   2016   1942       C  
ATOM     22  N   LEU A  61     -60.728 -12.616 114.526  1.00143.81           N  
ANISOU   22  N   LEU A  61    16361  17816  20465  -1503   1438   1526       N  
ATOM     23  CA  LEU A  61     -60.461 -14.030 114.245  1.00144.63           C  
ANISOU   23  CA  LEU A  61    16643  17359  20950  -1946   1503   1575       C  
ATOM     24  C   LEU A  61     -59.185 -14.471 114.955  1.00142.72           C  
ANISOU   24  C   LEU A  61    16877  16649  20701  -1718   1572   1835       C  
ATOM     25  O   LEU A  61     -58.200 -13.728 114.948  1.00137.74           O  
ANISOU   25  O   LEU A  61    16472  16013  19851  -1302   1397   1744       O  
ATOM     26  CB  LEU A  61     -60.341 -14.285 112.725  1.00144.05           C  
ANISOU   26  CB  LEU A  61    16577  17071  21083  -2187   1244   1126       C  
ATOM     27  CG  LEU A  61     -61.497 -13.837 111.823  1.00150.59           C  
ANISOU   27  CG  LEU A  61    16918  18423  21877  -2396   1075    846       C  
ATOM     28  CD1 LEU A  61     -61.051 -13.719 110.385  1.00148.84           C  
ANISOU   28  CD1 LEU A  61    16812  18085  21656  -2428    765    407       C  
ATOM     29  CD2 LEU A  61     -62.680 -14.787 111.914  1.00159.78           C  
ANISOU   29  CD2 LEU A  61    17710  19679  23320  -3016   1242    922       C  
ATOM     30  N   SER A  62     -59.206 -15.667 115.578  1.00140.56           N  
ANISOU   30  N   SER A  62    16733  15998  20675  -1991   1831   2190       N  
ATOM     31  CA  SER A  62     -58.073 -16.249 116.307  1.00139.38           C  
ANISOU   31  CA  SER A  62    16993  15418  20548  -1766   1916   2546       C  
ATOM     32  C   SER A  62     -56.823 -16.405 115.418  1.00137.42           C  
ANISOU   32  C   SER A  62    17054  14693  20467  -1587   1697   2283       C  
ATOM     33  O   SER A  62     -55.703 -16.386 115.931  1.00135.52           O  
ANISOU   33  O   SER A  62    17070  14302  20120  -1222   1651   2502       O  
ATOM     34  CB  SER A  62     -58.455 -17.600 116.905  1.00149.13           C  
ANISOU   34  CB  SER A  62    18304  16250  22109  -2137   2259   2981       C  
ATOM     35  OG  SER A  62     -58.780 -18.549 115.904  1.00160.55           O  
ANISOU   35  OG  SER A  62    19762  17190  24050  -2631   2298   2720       O  
ATOM     36  N   HIS A  63     -57.022 -16.536 114.094  1.00131.44           N  
ANISOU   36  N   HIS A  63    16240  13766  19934  -1838   1563   1815       N  
ATOM     37  CA  HIS A  63     -55.963 -16.706 113.098  1.00127.95           C  
ANISOU   37  CA  HIS A  63    16064  12905  19647  -1708   1406   1505       C  
ATOM     38  C   HIS A  63     -55.458 -15.372 112.536  1.00124.08           C  
ANISOU   38  C   HIS A  63    15522  12801  18823  -1344   1117   1202       C  
ATOM     39  O   HIS A  63     -54.365 -15.347 111.978  1.00121.44           O  
ANISOU   39  O   HIS A  63    15405  12197  18539  -1124   1014   1052       O  
ATOM     40  CB  HIS A  63     -56.456 -17.600 111.953  1.00131.97           C  
ANISOU   40  CB  HIS A  63    16584  13035  20522  -2210   1441   1127       C  
ATOM     41  CG  HIS A  63     -56.752 -18.996 112.386  1.00141.45           C  
ANISOU   41  CG  HIS A  63    17933  13664  22146  -2592   1756   1387       C  
ATOM     42  ND1 HIS A  63     -55.808 -19.994 112.273  1.00145.44           N  
ANISOU   42  ND1 HIS A  63    18844  13414  23003  -2515   1915   1467       N  
ATOM     43  CD2 HIS A  63     -57.869 -19.509 112.952  1.00147.91           C  
ANISOU   43  CD2 HIS A  63    18543  14553  23104  -3027   1971   1617       C  
ATOM     44  CE1 HIS A  63     -56.381 -21.082 112.756  1.00150.95           C  
ANISOU   44  CE1 HIS A  63    19613  13686  24056  -2911   2220   1741       C  
ATOM     45  NE2 HIS A  63     -57.618 -20.834 113.185  1.00152.95           N  
ANISOU   45  NE2 HIS A  63    19496  14427  24191  -3256   2264   1845       N  
ATOM     46  N   CYS A  64     -56.221 -14.274 112.686  1.00117.44           N  
ANISOU   46  N   CYS A  64    14398  12557  17669  -1261   1022   1136       N  
ATOM     47  CA  CYS A  64     -55.807 -12.958 112.191  1.00112.15           C  
ANISOU   47  CA  CYS A  64    13706  12196  16711   -919    789    890       C  
ATOM     48  C   CYS A  64     -54.982 -12.199 113.248  1.00110.89           C  
ANISOU   48  C   CYS A  64    13688  12176  16271   -506    770   1116       C  
ATOM     49  O   CYS A  64     -54.890 -10.967 113.225  1.00107.56           O  
ANISOU   49  O   CYS A  64    13225  12066  15578   -246    646    979       O  
ATOM     50  CB  CYS A  64     -57.013 -12.152 111.723  1.00113.05           C  
ANISOU   50  CB  CYS A  64    13463  12823  16667   -992    706    703       C  
ATOM     51  SG  CYS A  64     -57.526 -12.529 110.028  1.00118.69           S  
ANISOU   51  SG  CYS A  64    14040  13518  17540  -1354    531    268       S  
ATOM     52  N   GLY A  65     -54.351 -12.973 114.123  1.00107.29           N  
ANISOU   52  N   GLY A  65    13415  11462  15890   -460    888   1457       N  
ATOM     53  CA  GLY A  65     -53.489 -12.506 115.197  1.00105.27           C  
ANISOU   53  CA  GLY A  65    13293  11351  15354   -129    844   1701       C  
ATOM     54  C   GLY A  65     -52.593 -13.610 115.714  1.00109.05           C  
ANISOU   54  C   GLY A  65    13973  11442  16019    -70    922   2066       C  
ATOM     55  O   GLY A  65     -52.902 -14.796 115.557  1.00111.96           O  
ANISOU   55  O   GLY A  65    14393  11412  16732   -307   1106   2217       O  
ATOM     56  N   ARG A  66     -51.478 -13.221 116.341  1.00102.60           N  
ANISOU   56  N   ARG A  66    13260  10736  14986    245    782   2217       N  
ATOM     57  CA  ARG A  66     -50.485 -14.143 116.887  1.00104.15           C  
ANISOU   57  CA  ARG A  66    13602  10656  15315    413    809   2625       C  
ATOM     58  C   ARG A  66     -50.081 -13.751 118.308  1.00107.40           C  
ANISOU   58  C   ARG A  66    14030  11507  15271    640    730   2981       C  
ATOM     59  O   ARG A  66     -50.008 -12.562 118.631  1.00104.31           O  
ANISOU   59  O   ARG A  66    13588  11560  14485    736    567   2762       O  
ATOM     60  CB  ARG A  66     -49.251 -14.185 115.978  1.00102.52           C  
ANISOU   60  CB  ARG A  66    13453  10156  15342    591    663   2431       C  
ATOM     61  CG  ARG A  66     -48.549 -15.535 115.969  1.00118.76           C  
ANISOU   61  CG  ARG A  66    15649  11681  17795    699    806   2767       C  
ATOM     62  CD  ARG A  66     -47.356 -15.542 115.035  1.00128.67           C  
ANISOU   62  CD  ARG A  66    16921  12689  19280    909    711   2551       C  
ATOM     63  NE  ARG A  66     -47.755 -15.627 113.629  1.00135.69           N  
ANISOU   63  NE  ARG A  66    17855  13283  20420    684    787   2055       N  
ATOM     64  CZ  ARG A  66     -46.909 -15.594 112.604  1.00148.50           C  
ANISOU   64  CZ  ARG A  66    19503  14703  22218    811    762   1776       C  
ATOM     65  NH1 ARG A  66     -45.603 -15.470 112.815  1.00135.59           N  
ANISOU   65  NH1 ARG A  66    17806  13121  20592   1161    668   1951       N  
ATOM     66  NH2 ARG A  66     -47.361 -15.682 111.361  1.00133.62           N  
ANISOU   66  NH2 ARG A  66    17681  12616  20473    584    830   1323       N  
ATOM     67  N   ALA A  67     -49.814 -14.761 119.151  1.00107.51           N  
ANISOU   67  N   ALA A  67    14137  11384  15329    725    853   3531       N  
ATOM     68  CA  ALA A  67     -49.399 -14.572 120.539  1.00109.74           C  
ANISOU   68  CA  ALA A  67    14446  12122  15128    943    770   3943       C  
ATOM     69  C   ALA A  67     -47.958 -14.062 120.593  1.00111.33           C  
ANISOU   69  C   ALA A  67    14615  12509  15178   1236    434   3894       C  
ATOM     70  O   ALA A  67     -47.037 -14.752 120.149  1.00111.59           O  
ANISOU   70  O   ALA A  67    14653  12182  15565   1404    393   4052       O  
ATOM     71  CB  ALA A  67     -49.536 -15.878 121.309  1.00116.38           C  
ANISOU   71  CB  ALA A  67    15399  12728  16094    963   1015   4615       C  
ATOM     72  N   ALA A  68     -47.781 -12.821 121.084  1.00105.71           N  
ANISOU   72  N   ALA A  68    13854  12345  13965   1278    214   3632       N  
ATOM     73  CA  ALA A  68     -46.485 -12.146 121.214  1.00104.55           C  
ANISOU   73  CA  ALA A  68    13632  12476  13618   1460   -131   3517       C  
ATOM     74  C   ALA A  68     -46.510 -11.105 122.348  1.00108.59           C  
ANISOU   74  C   ALA A  68    14168  13647  13444   1461   -300   3413       C  
ATOM     75  O   ALA A  68     -47.491 -10.367 122.456  1.00106.73           O  
ANISOU   75  O   ALA A  68    13997  13567  12990   1322   -168   3104       O  
ATOM     76  CB  ALA A  68     -46.105 -11.473 119.901  1.00100.44           C  
ANISOU   76  CB  ALA A  68    13042  11717  13403   1397   -231   2985       C  
ATOM     77  N   PRO A  69     -45.448 -11.012 123.192  1.00107.42           N  
ANISOU   77  N   PRO A  69    13961  13915  12938   1621   -590   3640       N  
ATOM     78  CA  PRO A  69     -45.460 -10.014 124.282  1.00108.90           C  
ANISOU   78  CA  PRO A  69    14211  14749  12417   1574   -761   3460       C  
ATOM     79  C   PRO A  69     -45.373  -8.578 123.754  1.00107.95           C  
ANISOU   79  C   PRO A  69    14106  14672  12235   1413   -889   2750       C  
ATOM     80  O   PRO A  69     -44.521  -8.272 122.916  1.00105.16           O  
ANISOU   80  O   PRO A  69    13629  14122  12203   1396  -1066   2525       O  
ATOM     81  CB  PRO A  69     -44.243 -10.390 125.131  1.00115.65           C  
ANISOU   81  CB  PRO A  69    14946  16028  12968   1764  -1091   3887       C  
ATOM     82  CG  PRO A  69     -43.344 -11.127 124.213  1.00119.31           C  
ANISOU   82  CG  PRO A  69    15225  16055  14051   1921  -1156   4083       C  
ATOM     83  CD  PRO A  69     -44.211 -11.822 123.209  1.00111.69           C  
ANISOU   83  CD  PRO A  69    14359  14393  13686   1862   -774   4069       C  
ATOM     84  N   CYS A  70     -46.283  -7.709 124.230  1.00103.89           N  
ANISOU   84  N   CYS A  70    13753  14386  11334   1312   -749   2420       N  
ATOM     85  CA  CYS A  70     -46.398  -6.317 123.793  1.00100.76           C  
ANISOU   85  CA  CYS A  70    13439  13952  10892   1188   -784   1770       C  
ATOM     86  C   CYS A  70     -45.452  -5.391 124.546  1.00105.61           C  
ANISOU   86  C   CYS A  70    14101  15004  11020   1105  -1114   1484       C  
ATOM     87  O   CYS A  70     -45.268  -5.527 125.755  1.00110.19           O  
ANISOU   87  O   CYS A  70    14735  16103  11029   1131  -1232   1673       O  
ATOM     88  CB  CYS A  70     -47.840  -5.828 123.914  1.00101.04           C  
ANISOU   88  CB  CYS A  70    13613  13984  10795   1172   -436   1552       C  
ATOM     89  SG  CYS A  70     -49.059  -6.849 123.041  1.00102.79           S  
ANISOU   89  SG  CYS A  70    13715  13776  11564   1173    -77   1830       S  
ATOM     90  N   GLU A  71     -44.895  -4.418 123.819  1.00 98.34           N  
ANISOU   90  N   GLU A  71    13171  13885  10307    973  -1252   1013       N  
ATOM     91  CA  GLU A  71     -44.010  -3.377 124.340  1.00100.46           C  
ANISOU   91  CA  GLU A  71    13487  14469  10214    789  -1553    615       C  
ATOM     92  C   GLU A  71     -44.520  -2.000 123.862  1.00100.75           C  
ANISOU   92  C   GLU A  71    13755  14204  10322    661  -1386    -13       C  
ATOM     93  O   GLU A  71     -45.003  -1.909 122.729  1.00 95.83           O  
ANISOU   93  O   GLU A  71    13119  13099  10195    716  -1180    -76       O  
ATOM     94  CB  GLU A  71     -42.533  -3.620 123.943  1.00102.37           C  
ANISOU   94  CB  GLU A  71    13429  14761  10707    726  -1913    744       C  
ATOM     95  CG  GLU A  71     -42.256  -3.758 122.451  1.00109.80           C  
ANISOU   95  CG  GLU A  71    14218  15145  12354    746  -1821    725       C  
ATOM     96  CD  GLU A  71     -40.801  -3.992 122.096  1.00136.90           C  
ANISOU   96  CD  GLU A  71    17315  18674  16028    713  -2120    863       C  
ATOM     97  OE1 GLU A  71     -40.410  -5.170 121.933  1.00131.87           O  
ANISOU   97  OE1 GLU A  71    16463  18009  15633    939  -2137   1358       O  
ATOM     98  OE2 GLU A  71     -40.052  -2.996 121.974  1.00137.80           O  
ANISOU   98  OE2 GLU A  71    17371  18871  16117    463  -2312    479       O  
ATOM     99  N   PRO A  72     -44.465  -0.931 124.698  1.00 99.94           N  
ANISOU   99  N   PRO A  72    13887  14362   9724    506  -1451   -477       N  
ATOM    100  CA  PRO A  72     -44.973   0.380 124.248  1.00 98.39           C  
ANISOU  100  CA  PRO A  72    13956  13781   9648    433  -1237  -1046       C  
ATOM    101  C   PRO A  72     -44.188   0.959 123.069  1.00 99.13           C  
ANISOU  101  C   PRO A  72    13958  13430  10276    271  -1346  -1248       C  
ATOM    102  O   PRO A  72     -42.981   0.741 122.963  1.00 99.59           O  
ANISOU  102  O   PRO A  72    13783  13631  10424    100  -1669  -1156       O  
ATOM    103  CB  PRO A  72     -44.831   1.264 125.488  1.00106.09           C  
ANISOU  103  CB  PRO A  72    15213  15140   9958    263  -1324  -1504       C  
ATOM    104  CG  PRO A  72     -43.779   0.611 126.302  1.00114.35           C  
ANISOU  104  CG  PRO A  72    16052  16780  10618    136  -1746  -1241       C  
ATOM    105  CD  PRO A  72     -43.953  -0.858 126.080  1.00107.38           C  
ANISOU  105  CD  PRO A  72    14891  15950   9957    395  -1712   -518       C  
ATOM    106  N   LEU A  73     -44.888   1.684 122.180  1.00 92.68           N  
ANISOU  106  N   LEU A  73    13299  12109   9807    348  -1060  -1477       N  
ATOM    107  CA  LEU A  73     -44.321   2.309 120.987  1.00 89.92           C  
ANISOU  107  CA  LEU A  73    12914  11301   9952    224  -1078  -1633       C  
ATOM    108  C   LEU A  73     -43.348   3.429 121.344  1.00 99.19           C  
ANISOU  108  C   LEU A  73    14229  12464  10995   -133  -1269  -2101       C  
ATOM    109  O   LEU A  73     -43.706   4.349 122.088  1.00102.77           O  
ANISOU  109  O   LEU A  73    15018  12913  11118   -212  -1168  -2537       O  
ATOM    110  CB  LEU A  73     -45.440   2.860 120.088  1.00 86.85           C  
ANISOU  110  CB  LEU A  73    12687  10443   9868    442   -717  -1720       C  
ATOM    111  CG  LEU A  73     -46.013   1.905 119.049  1.00 86.46           C  
ANISOU  111  CG  LEU A  73    12407  10249  10192    657   -602  -1312       C  
ATOM    112  CD1 LEU A  73     -47.418   2.306 118.673  1.00 85.52           C  
ANISOU  112  CD1 LEU A  73    12407   9934  10152    918   -271  -1357       C  
ATOM    113  CD2 LEU A  73     -45.157   1.886 117.799  1.00 86.16           C  
ANISOU  113  CD2 LEU A  73    12216   9924  10596    554   -702  -1236       C  
ATOM    114  N   ARG A  74     -42.113   3.338 120.809  1.00 96.43           N  
ANISOU  114  N   ARG A  74    13613  12107  10917   -365  -1524  -2028       N  
ATOM    115  CA  ARG A  74     -41.040   4.318 121.010  1.00101.00           C  
ANISOU  115  CA  ARG A  74    14226  12684  11465   -797  -1737  -2436       C  
ATOM    116  C   ARG A  74     -41.150   5.465 119.990  1.00104.47           C  
ANISOU  116  C   ARG A  74    14899  12455  12339   -899  -1477  -2718       C  
ATOM    117  O   ARG A  74     -40.538   6.519 120.183  1.00108.36           O  
ANISOU  117  O   ARG A  74    15556  12789  12827  -1281  -1540  -3149       O  
ATOM    118  CB  ARG A  74     -39.657   3.647 120.945  1.00103.32           C  
ANISOU  118  CB  ARG A  74    14042  13356  11858   -986  -2117  -2170       C  
ATOM    119  CG  ARG A  74     -39.358   2.821 122.193  1.00122.03           C  
ANISOU  119  CG  ARG A  74    16229  16437  13699   -951  -2435  -1958       C  
ATOM    120  CD  ARG A  74     -37.946   2.275 122.249  1.00139.60           C  
ANISOU  120  CD  ARG A  74    17945  19105  15991  -1111  -2840  -1702       C  
ATOM    121  NE  ARG A  74     -37.777   1.399 123.411  1.00154.22           N  
ANISOU  121  NE  ARG A  74    19629  21645  17324   -977  -3126  -1385       N  
ATOM    122  CZ  ARG A  74     -37.814   0.069 123.370  1.00167.59           C  
ANISOU  122  CZ  ARG A  74    21073  23500  19103   -598  -3134   -765       C  
ATOM    123  NH1 ARG A  74     -37.666  -0.639 124.481  1.00160.10           N  
ANISOU  123  NH1 ARG A  74    20011  23170  17650   -472  -3381   -444       N  
ATOM    124  NH2 ARG A  74     -37.986  -0.563 122.216  1.00148.54           N  
ANISOU  124  NH2 ARG A  74    18547  20623  17270   -346  -2885   -462       N  
ATOM    125  N   TYR A  75     -41.953   5.258 118.926  1.00 96.22           N  
ANISOU  125  N   TYR A  75    13880  11029  11652   -572  -1186  -2466       N  
ATOM    126  CA  TYR A  75     -42.232   6.229 117.865  1.00 94.89           C  
ANISOU  126  CA  TYR A  75    13931  10246  11876   -552   -907  -2595       C  
ATOM    127  C   TYR A  75     -43.737   6.355 117.684  1.00 96.34           C  
ANISOU  127  C   TYR A  75    14350  10210  12043   -128   -570  -2546       C  
ATOM    128  O   TYR A  75     -44.418   5.357 117.437  1.00 92.80           O  
ANISOU  128  O   TYR A  75    13710   9947  11602    162   -528  -2193       O  
ATOM    129  CB  TYR A  75     -41.558   5.823 116.541  1.00 93.17           C  
ANISOU  129  CB  TYR A  75    13415   9875  12110   -574   -926  -2270       C  
ATOM    130  CG  TYR A  75     -40.156   5.285 116.712  1.00 97.50           C  
ANISOU  130  CG  TYR A  75    13570  10791  12686   -868  -1255  -2168       C  
ATOM    131  CD1 TYR A  75     -39.064   6.143 116.800  1.00103.90           C  
ANISOU  131  CD1 TYR A  75    14346  11545  13587  -1327  -1387  -2447       C  
ATOM    132  CD2 TYR A  75     -39.921   3.916 116.811  1.00 96.62           C  
ANISOU  132  CD2 TYR A  75    13102  11081  12529   -686  -1423  -1780       C  
ATOM    133  CE1 TYR A  75     -37.773   5.654 116.985  1.00107.28           C  
ANISOU  133  CE1 TYR A  75    14324  12397  14042  -1585  -1706  -2331       C  
ATOM    134  CE2 TYR A  75     -38.636   3.415 117.006  1.00 99.80           C  
ANISOU  134  CE2 TYR A  75    13100  11854  12966   -879  -1718  -1642       C  
ATOM    135  CZ  TYR A  75     -37.564   4.288 117.087  1.00112.31           C  
ANISOU  135  CZ  TYR A  75    14586  13462  14624  -1321  -1871  -1911       C  
ATOM    136  OH  TYR A  75     -36.294   3.797 117.264  1.00116.84           O  
ANISOU  136  OH  TYR A  75    14674  14473  15245  -1497  -2172  -1749       O  
ATOM    137  N   ASN A  76     -44.261   7.576 117.819  1.00 95.34           N  
ANISOU  137  N   ASN A  76    14624   9684  11916    -94   -319  -2900       N  
ATOM    138  CA  ASN A  76     -45.691   7.857 117.677  1.00 94.29           C  
ANISOU  138  CA  ASN A  76    14688   9353  11787    350     26  -2865       C  
ATOM    139  C   ASN A  76     -46.117   7.881 116.207  1.00 93.16           C  
ANISOU  139  C   ASN A  76    14449   8878  12069    601    188  -2531       C  
ATOM    140  O   ASN A  76     -47.309   7.788 115.917  1.00 91.74           O  
ANISOU  140  O   ASN A  76    14262   8683  11911    998    400  -2362       O  
ATOM    141  CB  ASN A  76     -46.053   9.198 118.359  1.00103.10           C  
ANISOU  141  CB  ASN A  76    16291  10114  12770    348    275  -3374       C  
ATOM    142  CG  ASN A  76     -45.263  10.421 117.912  1.00132.39           C  
ANISOU  142  CG  ASN A  76    20284  13236  16782     33    338  -3672       C  
ATOM    143  OD1 ASN A  76     -44.215  10.332 117.252  1.00128.78           O  
ANISOU  143  OD1 ASN A  76    19634  12716  16581   -290    146  -3548       O  
ATOM    144  ND2 ASN A  76     -45.733  11.600 118.308  1.00125.84           N  
ANISOU  144  ND2 ASN A  76    19929  11945  15937    110    642  -4084       N  
ATOM    145  N   VAL A  77     -45.143   7.988 115.286  1.00 87.71           N  
ANISOU  145  N   VAL A  77    13654   7988  11685    366     86  -2422       N  
ATOM    146  CA  VAL A  77     -45.375   8.096 113.847  1.00 84.66           C  
ANISOU  146  CA  VAL A  77    13211   7315  11641    554    228  -2118       C  
ATOM    147  C   VAL A  77     -44.715   6.917 113.071  1.00 84.59           C  
ANISOU  147  C   VAL A  77    12803   7586  11751    465     25  -1784       C  
ATOM    148  O   VAL A  77     -43.623   6.464 113.424  1.00 84.42           O  
ANISOU  148  O   VAL A  77    12590   7782  11703    161   -203  -1817       O  
ATOM    149  CB  VAL A  77     -44.893   9.496 113.367  1.00 92.33           C  
ANISOU  149  CB  VAL A  77    14510   7692  12879    389    410  -2296       C  
ATOM    150  CG1 VAL A  77     -43.374   9.669 113.458  1.00 94.27           C  
ANISOU  150  CG1 VAL A  77    14671   7919  13227   -155    214  -2452       C  
ATOM    151  CG2 VAL A  77     -45.407   9.833 111.980  1.00 90.84           C  
ANISOU  151  CG2 VAL A  77    14359   7192  12964    690    624  -1960       C  
ATOM    152  N   CYS A  78     -45.416   6.416 112.039  1.00 78.63           N  
ANISOU  152  N   CYS A  78    11917   6848  11109    750    112  -1477       N  
ATOM    153  CA  CYS A  78     -44.966   5.328 111.168  1.00 75.57           C  
ANISOU  153  CA  CYS A  78    11222   6657  10835    720     -6  -1205       C  
ATOM    154  C   CYS A  78     -44.983   5.817 109.715  1.00 78.18           C  
ANISOU  154  C   CYS A  78    11608   6721  11376    815    147  -1029       C  
ATOM    155  O   CYS A  78     -46.052   6.045 109.146  1.00 76.39           O  
ANISOU  155  O   CYS A  78    11452   6439  11135   1118    279   -900       O  
ATOM    156  CB  CYS A  78     -45.825   4.078 111.361  1.00 74.02           C  
ANISOU  156  CB  CYS A  78    10819   6800  10505    915    -65  -1038       C  
ATOM    157  SG  CYS A  78     -45.185   2.589 110.540  1.00 75.38           S  
ANISOU  157  SG  CYS A  78    10668   7162  10811    849   -194   -794       S  
ATOM    158  N   LEU A  79     -43.782   6.034 109.145  1.00 76.62           N  
ANISOU  158  N   LEU A  79    11361   6399  11354    557    136  -1004       N  
ATOM    159  CA  LEU A  79     -43.528   6.505 107.775  1.00 77.54           C  
ANISOU  159  CA  LEU A  79    11530   6291  11639    584    299   -809       C  
ATOM    160  C   LEU A  79     -44.321   7.797 107.425  1.00 84.64           C  
ANISOU  160  C   LEU A  79    12773   6796  12590    797    530   -769       C  
ATOM    161  O   LEU A  79     -44.855   7.917 106.312  1.00 84.83           O  
ANISOU  161  O   LEU A  79    12827   6785  12620   1044    646   -507       O  
ATOM    162  CB  LEU A  79     -43.815   5.397 106.733  1.00 74.91           C  
ANISOU  162  CB  LEU A  79    10978   6224  11261    762    273   -574       C  
ATOM    163  CG  LEU A  79     -42.925   4.153 106.768  1.00 78.54           C  
ANISOU  163  CG  LEU A  79    11134   6956  11752    610    133   -558       C  
ATOM    164  CD1 LEU A  79     -43.624   2.970 106.128  1.00 76.30           C  
ANISOU  164  CD1 LEU A  79    10717   6896  11378    811    107   -440       C  
ATOM    165  CD2 LEU A  79     -41.582   4.402 106.078  1.00 83.36           C  
ANISOU  165  CD2 LEU A  79    11646   7484  12544    382    213   -500       C  
ATOM    166  N   GLY A  80     -44.368   8.742 108.371  1.00 83.03           N  
ANISOU  166  N   GLY A  80    12833   6306  12408    711    599  -1029       N  
ATOM    167  CA  GLY A  80     -45.030  10.033 108.193  1.00 85.67           C  
ANISOU  167  CA  GLY A  80    13541   6164  12847    931    864  -1020       C  
ATOM    168  C   GLY A  80     -46.478  10.133 108.631  1.00 88.48           C  
ANISOU  168  C   GLY A  80    13983   6577  13058   1384    951  -1026       C  
ATOM    169  O   GLY A  80     -47.059  11.223 108.566  1.00 92.10           O  
ANISOU  169  O   GLY A  80    14753   6617  13623   1639   1200  -1016       O  
ATOM    170  N   SER A  81     -47.071   9.007 109.099  1.00 79.96           N  
ANISOU  170  N   SER A  81    12623   5996  11764   1496    778  -1026       N  
ATOM    171  CA  SER A  81     -48.465   8.939 109.569  1.00 78.79           C  
ANISOU  171  CA  SER A  81    12451   6017  11470   1896    861  -1014       C  
ATOM    172  C   SER A  81     -48.545   8.495 111.046  1.00 79.13           C  
ANISOU  172  C   SER A  81    12467   6304  11293   1775    779  -1312       C  
ATOM    173  O   SER A  81     -47.979   7.456 111.401  1.00 76.32           O  
ANISOU  173  O   SER A  81    11884   6285  10831   1521    553  -1324       O  
ATOM    174  CB  SER A  81     -49.271   7.982 108.692  1.00 78.73           C  
ANISOU  174  CB  SER A  81    12104   6419  11391   2128    763   -693       C  
ATOM    175  OG  SER A  81     -49.168   8.282 107.310  1.00 84.71           O  
ANISOU  175  OG  SER A  81    12870   7062  12252   2229    805   -408       O  
ATOM    176  N   VAL A  82     -49.241   9.284 111.901  1.00 76.56           N  
ANISOU  176  N   VAL A  82    12391   5811  10886   1987    986  -1535       N  
ATOM    177  CA  VAL A  82     -49.414   8.990 113.338  1.00 76.31           C  
ANISOU  177  CA  VAL A  82    12388   6038  10568   1911    961  -1826       C  
ATOM    178  C   VAL A  82     -50.269   7.696 113.501  1.00 77.15           C  
ANISOU  178  C   VAL A  82    12104   6708  10500   2069    866  -1590       C  
ATOM    179  O   VAL A  82     -51.153   7.435 112.679  1.00 75.75           O  
ANISOU  179  O   VAL A  82    11714   6647  10418   2357    919  -1303       O  
ATOM    180  CB  VAL A  82     -49.957  10.203 114.157  1.00 83.87           C  
ANISOU  180  CB  VAL A  82    13751   6649  11468   2121   1271  -2166       C  
ATOM    181  CG1 VAL A  82     -51.382  10.576 113.773  1.00 84.99           C  
ANISOU  181  CG1 VAL A  82    13857   6748  11689   2710   1555  -1955       C  
ATOM    182  CG2 VAL A  82     -49.845   9.968 115.658  1.00 85.25           C  
ANISOU  182  CG2 VAL A  82    14015   7108  11269   1940   1225  -2532       C  
ATOM    183  N   LEU A  83     -49.947   6.870 114.524  1.00 72.27           N  
ANISOU  183  N   LEU A  83    11382   6448   9628   1845    709  -1690       N  
ATOM    184  CA  LEU A  83     -50.583   5.575 114.782  1.00 69.25           C  
ANISOU  184  CA  LEU A  83    10664   6542   9107   1900    631  -1457       C  
ATOM    185  C   LEU A  83     -51.770   5.646 115.746  1.00 77.02           C  
ANISOU  185  C   LEU A  83    11651   7764   9851   2167    862  -1521       C  
ATOM    186  O   LEU A  83     -51.684   6.329 116.765  1.00 80.57           O  
ANISOU  186  O   LEU A  83    12381   8157  10074   2165    985  -1836       O  
ATOM    187  CB  LEU A  83     -49.551   4.552 115.301  1.00 67.03           C  
ANISOU  187  CB  LEU A  83    10254   6512   8705   1551    356  -1422       C  
ATOM    188  CG  LEU A  83     -48.485   4.154 114.294  1.00 67.38           C  
ANISOU  188  CG  LEU A  83    10171   6430   9000   1336    157  -1284       C  
ATOM    189  CD1 LEU A  83     -47.398   3.339 114.864  1.00 66.68           C  
ANISOU  189  CD1 LEU A  83     9957   6558   8820   1062    -87  -1253       C  
ATOM    190  CD2 LEU A  83     -49.038   3.662 112.992  1.00 66.38           C  
ANISOU  190  CD2 LEU A  83     9846   6284   9092   1485    185  -1019       C  
ATOM    191  N   PRO A  84     -52.859   4.890 115.455  1.00 73.44           N  
ANISOU  191  N   PRO A  84    10867   7612   9425   2359    926  -1241       N  
ATOM    192  CA  PRO A  84     -54.045   4.915 116.337  1.00 77.28           C  
ANISOU  192  CA  PRO A  84    11278   8382   9702   2620   1189  -1257       C  
ATOM    193  C   PRO A  84     -53.921   4.072 117.615  1.00 84.75           C  
ANISOU  193  C   PRO A  84    12192   9705  10304   2426   1160  -1267       C  
ATOM    194  O   PRO A  84     -54.831   4.099 118.452  1.00 88.05           O  
ANISOU  194  O   PRO A  84    12568  10390  10496   2618   1415  -1287       O  
ATOM    195  CB  PRO A  84     -55.157   4.351 115.447  1.00 77.64           C  
ANISOU  195  CB  PRO A  84    10907   8654   9938   2810   1222   -926       C  
ATOM    196  CG  PRO A  84     -54.481   3.553 114.421  1.00 77.47           C  
ANISOU  196  CG  PRO A  84    10743   8584  10110   2540    930   -752       C  
ATOM    197  CD  PRO A  84     -53.080   4.034 114.273  1.00 71.51           C  
ANISOU  197  CD  PRO A  84    10297   7472   9402   2327    780   -930       C  
ATOM    198  N   TYR A  85     -52.817   3.323 117.760  1.00 80.02           N  
ANISOU  198  N   TYR A  85    11593   9152   9658   2080    873  -1212       N  
ATOM    199  CA  TYR A  85     -52.570   2.425 118.887  1.00 81.23           C  
ANISOU  199  CA  TYR A  85    11707   9671   9487   1905    800  -1119       C  
ATOM    200  C   TYR A  85     -51.273   2.809 119.610  1.00 88.77           C  
ANISOU  200  C   TYR A  85    12932  10599  10200   1664    591  -1378       C  
ATOM    201  O   TYR A  85     -50.527   3.660 119.117  1.00 88.20           O  
ANISOU  201  O   TYR A  85    13038  10187  10287   1571    498  -1616       O  
ATOM    202  CB  TYR A  85     -52.539   0.963 118.398  1.00 79.06           C  
ANISOU  202  CB  TYR A  85    11109   9530   9402   1752    646   -722       C  
ATOM    203  CG  TYR A  85     -51.697   0.751 117.159  1.00 76.84           C  
ANISOU  203  CG  TYR A  85    10764   8955   9475   1614    416   -665       C  
ATOM    204  CD1 TYR A  85     -52.242   0.901 115.886  1.00 76.46           C  
ANISOU  204  CD1 TYR A  85    10582   8740   9731   1724    456   -605       C  
ATOM    205  CD2 TYR A  85     -50.362   0.382 117.257  1.00 76.98           C  
ANISOU  205  CD2 TYR A  85    10829   8924   9498   1392    164   -651       C  
ATOM    206  CE1 TYR A  85     -51.464   0.733 114.743  1.00 74.61           C  
ANISOU  206  CE1 TYR A  85    10317   8271   9759   1607    281   -568       C  
ATOM    207  CE2 TYR A  85     -49.578   0.195 116.121  1.00 75.37           C  
ANISOU  207  CE2 TYR A  85    10552   8474   9611   1291      8   -603       C  
ATOM    208  CZ  TYR A  85     -50.135   0.369 114.864  1.00 81.32           C  
ANISOU  208  CZ  TYR A  85    11224   9044  10629   1393     82   -573       C  
ATOM    209  OH  TYR A  85     -49.373   0.192 113.735  1.00 79.55           O  
ANISOU  209  OH  TYR A  85    10952   8616  10659   1300    -36   -535       O  
ATOM    210  N   GLY A  86     -51.030   2.195 120.774  1.00 89.04           N  
ANISOU  210  N   GLY A  86    12976  11019   9837   1549    520  -1311       N  
ATOM    211  CA  GLY A  86     -49.873   2.493 121.617  1.00 91.86           C  
ANISOU  211  CA  GLY A  86    13534  11508   9862   1309    281  -1545       C  
ATOM    212  C   GLY A  86     -48.824   1.418 121.842  1.00 95.24           C  
ANISOU  212  C   GLY A  86    13771  12182  10233   1093    -62  -1241       C  
ATOM    213  O   GLY A  86     -47.735   1.739 122.326  1.00 97.08           O  
ANISOU  213  O   GLY A  86    14093  12532  10259    874   -326  -1431       O  
ATOM    214  N   ALA A  87     -49.122   0.143 121.519  1.00 89.76           N  
ANISOU  214  N   ALA A  87    12807  11570   9729   1149    -61   -772       N  
ATOM    215  CA  ALA A  87     -48.153  -0.941 121.716  1.00 89.90           C  
ANISOU  215  CA  ALA A  87    12650  11764   9746   1024   -340   -424       C  
ATOM    216  C   ALA A  87     -47.833  -1.675 120.410  1.00 92.02           C  
ANISOU  216  C   ALA A  87    12694  11697  10571   1013   -410   -185       C  
ATOM    217  O   ALA A  87     -48.695  -1.783 119.532  1.00 90.08           O  
ANISOU  217  O   ALA A  87    12380  11217  10629   1102   -219   -150       O  
ATOM    218  CB  ALA A  87     -48.655  -1.920 122.757  1.00 93.17           C  
ANISOU  218  CB  ALA A  87    13014  12572   9816   1092   -251    -51       C  
ATOM    219  N   THR A  88     -46.581  -2.171 120.287  1.00 88.52           N  
ANISOU  219  N   THR A  88    12122  11275  10238    911   -684    -34       N  
ATOM    220  CA  THR A  88     -46.093  -2.869 119.097  1.00 85.04           C  
ANISOU  220  CA  THR A  88    11492  10528  10290    914   -733    151       C  
ATOM    221  C   THR A  88     -45.294  -4.146 119.451  1.00 90.38           C  
ANISOU  221  C   THR A  88    11987  11343  11011    950   -891    583       C  
ATOM    222  O   THR A  88     -45.034  -4.412 120.625  1.00 92.68           O  
ANISOU  222  O   THR A  88    12283  12011  10921    965  -1010    764       O  
ATOM    223  CB  THR A  88     -45.264  -1.904 118.227  1.00 91.80           C  
ANISOU  223  CB  THR A  88    12361  11148  11369    801   -839   -158       C  
ATOM    224  OG1 THR A  88     -44.989  -2.520 116.970  1.00 88.35           O  
ANISOU  224  OG1 THR A  88    11773  10422  11373    834   -809    -15       O  
ATOM    225  CG2 THR A  88     -43.965  -1.473 118.886  1.00 95.04           C  
ANISOU  225  CG2 THR A  88    12728  11801  11582    632  -1127   -270       C  
ATOM    226  N   SER A  89     -44.915  -4.926 118.414  1.00 86.06           N  
ANISOU  226  N   SER A  89    11294  10490  10916    992   -872    751       N  
ATOM    227  CA  SER A  89     -44.133  -6.159 118.520  1.00 88.15           C  
ANISOU  227  CA  SER A  89    11392  10752  11349   1095   -961   1164       C  
ATOM    228  C   SER A  89     -43.227  -6.343 117.285  1.00 91.59           C  
ANISOU  228  C   SER A  89    11680  10887  12232   1115   -991   1112       C  
ATOM    229  O   SER A  89     -43.694  -6.214 116.148  1.00 88.40           O  
ANISOU  229  O   SER A  89    11328  10164  12097   1081   -830    919       O  
ATOM    230  CB  SER A  89     -45.052  -7.366 118.694  1.00 92.38           C  
ANISOU  230  CB  SER A  89    11964  11153  11985   1175   -740   1515       C  
ATOM    231  OG  SER A  89     -44.323  -8.524 119.070  1.00103.90           O  
ANISOU  231  OG  SER A  89    13316  12607  13553   1320   -802   1973       O  
ATOM    232  N   THR A  90     -41.931  -6.648 117.517  1.00 90.85           N  
ANISOU  232  N   THR A  90    11377  10952  12188   1186  -1195   1302       N  
ATOM    233  CA  THR A  90     -40.928  -6.858 116.458  1.00 89.92           C  
ANISOU  233  CA  THR A  90    11068  10621  12475   1241  -1197   1289       C  
ATOM    234  C   THR A  90     -40.842  -8.360 116.089  1.00 93.80           C  
ANISOU  234  C   THR A  90    11504  10815  13321   1475  -1031   1655       C  
ATOM    235  O   THR A  90     -39.778  -8.856 115.692  1.00 94.96           O  
ANISOU  235  O   THR A  90    11435  10903  13741   1636  -1056   1812       O  
ATOM    236  CB  THR A  90     -39.556  -6.274 116.875  1.00101.96           C  
ANISOU  236  CB  THR A  90    12331  12518  13893   1179  -1493   1270       C  
ATOM    237  OG1 THR A  90     -39.182  -6.778 118.160  1.00105.74           O  
ANISOU  237  OG1 THR A  90    12690  13417  14071   1287  -1712   1620       O  
ATOM    238  CG2 THR A  90     -39.539  -4.747 116.877  1.00 99.15           C  
ANISOU  238  CG2 THR A  90    12069  12271  13334    886  -1588    814       C  
ATOM    239  N   LEU A  91     -41.982  -9.065 116.215  1.00 88.81           N  
ANISOU  239  N   LEU A  91    11064   9973  12707   1486   -833   1778       N  
ATOM    240  CA  LEU A  91     -42.139 -10.488 115.924  1.00 89.58           C  
ANISOU  240  CA  LEU A  91    11201   9683  13150   1640   -623   2082       C  
ATOM    241  C   LEU A  91     -42.435 -10.698 114.440  1.00 90.98           C  
ANISOU  241  C   LEU A  91    11460   9414  13694   1572   -406   1779       C  
ATOM    242  O   LEU A  91     -41.986 -11.694 113.865  1.00 92.09           O  
ANISOU  242  O   LEU A  91    11592   9200  14199   1724   -252   1901       O  
ATOM    243  CB  LEU A  91     -43.276 -11.066 116.789  1.00 90.75           C  
ANISOU  243  CB  LEU A  91    11512   9836  13131   1591   -499   2335       C  
ATOM    244  CG  LEU A  91     -43.539 -12.567 116.685  1.00 97.42           C  
ANISOU  244  CG  LEU A  91    12447  10230  14337   1694   -253   2691       C  
ATOM    245  CD1 LEU A  91     -43.028 -13.293 117.911  1.00102.66           C  
ANISOU  245  CD1 LEU A  91    13064  11073  14870   1930   -322   3285       C  
ATOM    246  CD2 LEU A  91     -45.013 -12.844 116.477  1.00 97.44           C  
ANISOU  246  CD2 LEU A  91    12617  10018  14388   1446    -21   2578       C  
ATOM    247  N   LEU A  92     -43.192  -9.767 113.826  1.00 84.35           N  
ANISOU  247  N   LEU A  92    10711   8599  12737   1368   -385   1389       N  
ATOM    248  CA  LEU A  92     -43.589  -9.864 112.420  1.00 82.34           C  
ANISOU  248  CA  LEU A  92    10538   8032  12717   1281   -219   1092       C  
ATOM    249  C   LEU A  92     -42.417  -9.549 111.484  1.00 86.36           C  
ANISOU  249  C   LEU A  92    10936   8484  13393   1367   -227    943       C  
ATOM    250  O   LEU A  92     -42.344 -10.112 110.387  1.00 85.27           O  
ANISOU  250  O   LEU A  92    10853   8048  13498   1390    -51    805       O  
ATOM    251  CB  LEU A  92     -44.806  -8.974 112.117  1.00 79.82           C  
ANISOU  251  CB  LEU A  92    10312   7825  12192   1093   -209    812       C  
ATOM    252  CG  LEU A  92     -46.107  -9.234 112.921  1.00 85.37           C  
ANISOU  252  CG  LEU A  92    11073   8624  12742    994   -145    931       C  
ATOM    253  CD1 LEU A  92     -47.293  -8.589 112.251  1.00 83.94           C  
ANISOU  253  CD1 LEU A  92    10914   8503  12478    858    -94    658       C  
ATOM    254  CD2 LEU A  92     -46.409 -10.724 113.077  1.00 89.86           C  
ANISOU  254  CD2 LEU A  92    11684   8899  13560    971     19   1188       C  
ATOM    255  N   ALA A  93     -41.488  -8.687 111.932  1.00 84.59           N  
ANISOU  255  N   ALA A  93    10550   8560  13030   1391   -416    960       N  
ATOM    256  CA  ALA A  93     -40.277  -8.358 111.183  1.00 85.32           C  
ANISOU  256  CA  ALA A  93    10465   8663  13287   1450   -414    875       C  
ATOM    257  C   ALA A  93     -39.153  -9.309 111.617  1.00 95.06           C  
ANISOU  257  C   ALA A  93    11467   9917  14734   1710   -434   1217       C  
ATOM    258  O   ALA A  93     -38.722  -9.279 112.774  1.00 97.08           O  
ANISOU  258  O   ALA A  93    11570  10485  14832   1769   -650   1475       O  
ATOM    259  CB  ALA A  93     -39.887  -6.905 111.413  1.00 85.04           C  
ANISOU  259  CB  ALA A  93    10355   8922  13033   1276   -595    701       C  
ATOM    260  N   GLY A  94     -38.752 -10.192 110.703  1.00 93.95           N  
ANISOU  260  N   GLY A  94    11316   9450  14930   1890   -196   1225       N  
ATOM    261  CA  GLY A  94     -37.711 -11.189 110.942  1.00 98.16           C  
ANISOU  261  CA  GLY A  94    11634   9917  15745   2227   -136   1564       C  
ATOM    262  C   GLY A  94     -36.318 -10.604 111.056  1.00104.08           C  
ANISOU  262  C   GLY A  94    11972  11052  16521   2315   -292   1657       C  
ATOM    263  O   GLY A  94     -35.483 -11.121 111.803  1.00107.86           O  
ANISOU  263  O   GLY A  94    12168  11727  17086   2575   -410   2038       O  
ATOM    264  N   ASP A  95     -36.069  -9.517 110.312  1.00 98.28           N  
ANISOU  264  N   ASP A  95    11181  10446  15716   2091   -294   1340       N  
ATOM    265  CA  ASP A  95     -34.799  -8.794 110.277  1.00100.00           C  
ANISOU  265  CA  ASP A  95    10993  11028  15976   2056   -415   1363       C  
ATOM    266  C   ASP A  95     -34.580  -7.948 111.539  1.00105.48           C  
ANISOU  266  C   ASP A  95    11517  12201  16360   1843   -813   1438       C  
ATOM    267  O   ASP A  95     -33.436  -7.605 111.845  1.00108.75           O  
ANISOU  267  O   ASP A  95    11508  12998  16813   1825   -990   1550       O  
ATOM    268  CB  ASP A  95     -34.731  -7.895 109.021  1.00 99.28           C  
ANISOU  268  CB  ASP A  95    10967  10852  15905   1840   -232   1014       C  
ATOM    269  CG  ASP A  95     -35.836  -6.856 108.854  1.00101.44           C  
ANISOU  269  CG  ASP A  95    11589  11057  15896   1514   -283    718       C  
ATOM    270  OD1 ASP A  95     -36.876  -6.967 109.543  1.00100.11           O  
ANISOU  270  OD1 ASP A  95    11664  10840  15535   1467   -392    721       O  
ATOM    271  OD2 ASP A  95     -35.685  -5.970 107.994  1.00104.26           O  
ANISOU  271  OD2 ASP A  95    11976  11400  16239   1339   -176    515       O  
ATOM    272  N   SER A  96     -35.668  -7.613 112.261  1.00 99.93           N  
ANISOU  272  N   SER A  96    11124  11507  15339   1670   -944   1353       N  
ATOM    273  CA  SER A  96     -35.629  -6.770 113.457  1.00100.74           C  
ANISOU  273  CA  SER A  96    11169  12036  15071   1444  -1285   1329       C  
ATOM    274  C   SER A  96     -35.908  -7.544 114.741  1.00107.73           C  
ANISOU  274  C   SER A  96    12068  13129  15737   1620  -1457   1680       C  
ATOM    275  O   SER A  96     -36.727  -8.467 114.760  1.00107.03           O  
ANISOU  275  O   SER A  96    12215  12738  15712   1798  -1277   1847       O  
ATOM    276  CB  SER A  96     -36.631  -5.628 113.333  1.00 99.99           C  
ANISOU  276  CB  SER A  96    11428  11827  14738   1131  -1262    941       C  
ATOM    277  OG  SER A  96     -36.422  -4.900 112.135  1.00106.65           O  
ANISOU  277  OG  SER A  96    12293  12468  15762    987  -1087    682       O  
ATOM    278  N   ASP A  97     -35.221  -7.137 115.822  1.00107.69           N  
ANISOU  278  N   ASP A  97    11808  13663  15446   1534  -1812   1792       N  
ATOM    279  CA  ASP A  97     -35.352  -7.677 117.179  1.00110.40           C  
ANISOU  279  CA  ASP A  97    12135  14363  15450   1672  -2039   2148       C  
ATOM    280  C   ASP A  97     -35.726  -6.547 118.138  1.00112.91           C  
ANISOU  280  C   ASP A  97    12605  15066  15232   1318  -2298   1850       C  
ATOM    281  O   ASP A  97     -36.436  -6.777 119.118  1.00113.89           O  
ANISOU  281  O   ASP A  97    12938  15358  14978   1356  -2359   1989       O  
ATOM    282  CB  ASP A  97     -34.051  -8.369 117.628  1.00117.85           C  
ANISOU  282  CB  ASP A  97    12576  15707  16494   1963  -2258   2614       C  
ATOM    283  CG  ASP A  97     -33.629  -9.565 116.788  1.00128.72           C  
ANISOU  283  CG  ASP A  97    13815  16680  18414   2395  -1960   2932       C  
ATOM    284  OD1 ASP A  97     -34.524 -10.278 116.266  1.00126.41           O  
ANISOU  284  OD1 ASP A  97    13888  15815  18328   2523  -1620   2939       O  
ATOM    285  OD2 ASP A  97     -32.408  -9.818 116.690  1.00138.56           O  
ANISOU  285  OD2 ASP A  97    14576  18193  19877   2608  -2061   3171       O  
ATOM    286  N   SER A  98     -35.255  -5.322 117.828  1.00107.25           N  
ANISOU  286  N   SER A  98    11807  14450  14491    965  -2407   1428       N  
ATOM    287  CA  SER A  98     -35.510  -4.096 118.579  1.00107.24           C  
ANISOU  287  CA  SER A  98    11988  14709  14048    582  -2606   1025       C  
ATOM    288  C   SER A  98     -36.413  -3.149 117.792  1.00104.83           C  
ANISOU  288  C   SER A  98    12080  13911  13840    379  -2325    572       C  
ATOM    289  O   SER A  98     -36.483  -3.245 116.565  1.00101.50           O  
ANISOU  289  O   SER A  98    11676  13068  13822    451  -2062    541       O  
ATOM    290  CB  SER A  98     -34.190  -3.399 118.898  1.00115.20           C  
ANISOU  290  CB  SER A  98    12586  16201  14985    290  -2958    897       C  
ATOM    291  OG  SER A  98     -34.396  -2.196 119.620  1.00125.74           O  
ANISOU  291  OG  SER A  98    14140  17733  15900   -128  -3139    434       O  
ATOM    292  N   GLN A  99     -37.086  -2.219 118.497  1.00100.20           N  
ANISOU  292  N   GLN A  99    11812  13397  12862    152  -2374    226       N  
ATOM    293  CA  GLN A  99     -37.929  -1.192 117.877  1.00 96.08           C  
ANISOU  293  CA  GLN A  99    11662  12434  12410     -1  -2120   -183       C  
ATOM    294  C   GLN A  99     -37.057  -0.199 117.105  1.00 99.33           C  
ANISOU  294  C   GLN A  99    11956  12689  13094   -307  -2129   -458       C  
ATOM    295  O   GLN A  99     -37.485   0.342 116.084  1.00 95.85           O  
ANISOU  295  O   GLN A  99    11712  11796  12912   -328  -1861   -613       O  
ATOM    296  CB  GLN A  99     -38.753  -0.456 118.935  1.00 98.97           C  
ANISOU  296  CB  GLN A  99    12381  12933  12289   -123  -2147   -482       C  
ATOM    297  CG  GLN A  99     -40.174  -0.963 119.065  1.00104.90           C  
ANISOU  297  CG  GLN A  99    13403  13523  12930    146  -1888   -356       C  
ATOM    298  CD  GLN A  99     -40.991  -0.043 119.929  1.00121.10           C  
ANISOU  298  CD  GLN A  99    15810  15651  14554     45  -1826   -718       C  
ATOM    299  OE1 GLN A  99     -41.509   0.979 119.470  1.00113.88           O  
ANISOU  299  OE1 GLN A  99    15152  14381  13735    -32  -1629  -1071       O  
ATOM    300  NE2 GLN A  99     -41.158  -0.409 121.188  1.00115.81           N  
ANISOU  300  NE2 GLN A  99    15175  15434  13391     86  -1956   -613       N  
ATOM    301  N   GLU A 100     -35.826   0.021 117.607  1.00 99.48           N  
ANISOU  301  N   GLU A 100    11627  13124  13045   -552  -2445   -480       N  
ATOM    302  CA  GLU A 100     -34.808   0.894 117.032  1.00101.05           C  
ANISOU  302  CA  GLU A 100    11612  13276  13506   -918  -2489   -698       C  
ATOM    303  C   GLU A 100     -34.301   0.302 115.720  1.00101.73           C  
ANISOU  303  C   GLU A 100    11422  13138  14091   -719  -2268   -421       C  
ATOM    304  O   GLU A 100     -34.099   1.039 114.754  1.00100.46           O  
ANISOU  304  O   GLU A 100    11312  12645  14213   -908  -2060   -585       O  
ATOM    305  CB  GLU A 100     -33.658   1.106 118.029  1.00108.96           C  
ANISOU  305  CB  GLU A 100    12226  14909  14266  -1235  -2933   -758       C  
ATOM    306  CG  GLU A 100     -34.026   1.988 119.217  1.00125.47           C  
ANISOU  306  CG  GLU A 100    14639  17199  15835  -1561  -3134  -1192       C  
ATOM    307  CD  GLU A 100     -34.627   1.333 120.452  1.00149.82           C  
ANISOU  307  CD  GLU A 100    17855  20703  18367  -1325  -3310  -1042       C  
ATOM    308  OE1 GLU A 100     -35.304   0.287 120.324  1.00143.29           O  
ANISOU  308  OE1 GLU A 100    17084  19778  17581   -868  -3139   -640       O  
ATOM    309  OE2 GLU A 100     -34.453   1.901 121.554  1.00147.76           O  
ANISOU  309  OE2 GLU A 100    17673  20860  17611  -1630  -3597  -1352       O  
ATOM    310  N   GLU A 101     -34.138  -1.039 115.683  1.00 96.99           N  
ANISOU  310  N   GLU A 101    10572  12690  13588   -320  -2274      6       N  
ATOM    311  CA  GLU A 101     -33.714  -1.798 114.507  1.00 94.54           C  
ANISOU  311  CA  GLU A 101    10037  12170  13715    -55  -2027    260       C  
ATOM    312  C   GLU A 101     -34.805  -1.736 113.439  1.00 90.98           C  
ANISOU  312  C   GLU A 101    10012  11156  13403     67  -1650    144       C  
ATOM    313  O   GLU A 101     -34.496  -1.509 112.271  1.00 89.68           O  
ANISOU  313  O   GLU A 101     9802  10751  13523     41  -1414    102       O  
ATOM    314  CB  GLU A 101     -33.392  -3.258 114.886  1.00 97.67           C  
ANISOU  314  CB  GLU A 101    10150  12795  14164    373  -2105    724       C  
ATOM    315  CG  GLU A 101     -32.785  -4.070 113.750  1.00110.38           C  
ANISOU  315  CG  GLU A 101    11501  14208  16231    668  -1836    951       C  
ATOM    316  CD  GLU A 101     -32.245  -5.445 114.096  1.00135.93           C  
ANISOU  316  CD  GLU A 101    14415  17626  19605   1117  -1883   1424       C  
ATOM    317  OE1 GLU A 101     -32.679  -6.028 115.117  1.00137.82           O  
ANISOU  317  OE1 GLU A 101    14753  18024  19589   1281  -2056   1653       O  
ATOM    318  OE2 GLU A 101     -31.402  -5.954 113.320  1.00127.02           O  
ANISOU  318  OE2 GLU A 101    12954  16460  18849   1338  -1705   1587       O  
ATOM    319  N   ALA A 102     -36.077  -1.909 113.857  1.00 83.24           N  
ANISOU  319  N   ALA A 102     9414  10025  12187    188  -1599    104       N  
ATOM    320  CA  ALA A 102     -37.254  -1.859 112.992  1.00 78.06           C  
ANISOU  320  CA  ALA A 102     9123   8939  11599    300  -1304      4       C  
ATOM    321  C   ALA A 102     -37.358  -0.501 112.306  1.00 79.49           C  
ANISOU  321  C   ALA A 102     9500   8869  11834     48  -1175   -295       C  
ATOM    322  O   ALA A 102     -37.575  -0.451 111.095  1.00 76.68           O  
ANISOU  322  O   ALA A 102     9230   8231  11673    121   -931   -294       O  
ATOM    323  CB  ALA A 102     -38.512  -2.148 113.801  1.00 77.50           C  
ANISOU  323  CB  ALA A 102     9334   8873  11241    416  -1314     15       C  
ATOM    324  N   HIS A 103     -37.134   0.589 113.073  1.00 77.72           N  
ANISOU  324  N   HIS A 103     9352   8747  11430   -257  -1333   -545       N  
ATOM    325  CA  HIS A 103     -37.173   1.971 112.593  1.00 77.58           C  
ANISOU  325  CA  HIS A 103     9564   8426  11486   -526  -1200   -824       C  
ATOM    326  C   HIS A 103     -36.097   2.217 111.530  1.00 80.85           C  
ANISOU  326  C   HIS A 103     9723   8758  12239   -681  -1082   -754       C  
ATOM    327  O   HIS A 103     -36.376   2.881 110.528  1.00 79.27           O  
ANISOU  327  O   HIS A 103     9730   8202  12185   -709   -825   -798       O  
ATOM    328  CB  HIS A 103     -37.013   2.953 113.762  1.00 82.18           C  
ANISOU  328  CB  HIS A 103    10276   9134  11815   -859  -1403  -1146       C  
ATOM    329  CG  HIS A 103     -36.990   4.384 113.335  1.00 87.37           C  
ANISOU  329  CG  HIS A 103    11206   9389  12602  -1157  -1239  -1440       C  
ATOM    330  ND1 HIS A 103     -35.801   5.085 113.233  1.00 93.20           N  
ANISOU  330  ND1 HIS A 103    11739  10152  13521  -1590  -1316  -1570       N  
ATOM    331  CD2 HIS A 103     -38.007   5.187 112.949  1.00 88.02           C  
ANISOU  331  CD2 HIS A 103    11727   9023  12693  -1061   -981  -1579       C  
ATOM    332  CE1 HIS A 103     -36.132   6.295 112.816  1.00 93.81           C  
ANISOU  332  CE1 HIS A 103    12189   9735  13718  -1769  -1085  -1790       C  
ATOM    333  NE2 HIS A 103     -37.449   6.403 112.627  1.00 91.14           N  
ANISOU  333  NE2 HIS A 103    12249   9098  13282  -1423   -878  -1788       N  
ATOM    334  N   GLY A 104     -34.902   1.669 111.759  1.00 78.55           N  
ANISOU  334  N   GLY A 104     8963   8827  12053   -749  -1255   -605       N  
ATOM    335  CA  GLY A 104     -33.765   1.776 110.849  1.00 79.39           C  
ANISOU  335  CA  GLY A 104     8721   8959  12484   -880  -1131   -503       C  
ATOM    336  C   GLY A 104     -34.003   1.075 109.528  1.00 78.19           C  
ANISOU  336  C   GLY A 104     8597   8587  12522   -549   -805   -307       C  
ATOM    337  O   GLY A 104     -33.578   1.569 108.478  1.00 77.98           O  
ANISOU  337  O   GLY A 104     8538   8396  12693   -661   -557   -295       O  
ATOM    338  N   LYS A 105     -34.701  -0.083 109.575  1.00 70.97           N  
ANISOU  338  N   LYS A 105     7767   7668  11532   -165   -788   -162       N  
ATOM    339  CA  LYS A 105     -35.051  -0.873 108.393  1.00 67.70           C  
ANISOU  339  CA  LYS A 105     7433   7047  11245    135   -500    -48       C  
ATOM    340  C   LYS A 105     -36.109  -0.129 107.567  1.00 68.75           C  
ANISOU  340  C   LYS A 105     7996   6846  11280    109   -300   -188       C  
ATOM    341  O   LYS A 105     -36.067  -0.183 106.339  1.00 67.73           O  
ANISOU  341  O   LYS A 105     7914   6583  11238    189    -44   -150       O  
ATOM    342  CB  LYS A 105     -35.530  -2.282 108.783  1.00 68.36           C  
ANISOU  342  CB  LYS A 105     7513   7165  11294    477   -546    111       C  
ATOM    343  CG  LYS A 105     -34.484  -3.165 109.476  1.00 83.93           C  
ANISOU  343  CG  LYS A 105     9052   9447  13390    623   -706    352       C  
ATOM    344  CD  LYS A 105     -33.359  -3.636 108.551  1.00 98.71           C  
ANISOU  344  CD  LYS A 105    10568  11362  15577    766   -490    481       C  
ATOM    345  CE  LYS A 105     -32.397  -4.590 109.222  1.00116.23           C  
ANISOU  345  CE  LYS A 105    12333  13883  17946   1015   -628    778       C  
ATOM    346  NZ  LYS A 105     -31.456  -3.888 110.136  1.00129.80           N  
ANISOU  346  NZ  LYS A 105    13646  16067  19606    744   -962    819       N  
ATOM    347  N   LEU A 106     -37.009   0.618 108.248  1.00 64.36           N  
ANISOU  347  N   LEU A 106     7739   6189  10523     12   -409   -338       N  
ATOM    348  CA  LEU A 106     -38.042   1.456 107.635  1.00 62.11           C  
ANISOU  348  CA  LEU A 106     7835   5615  10148     30   -247   -432       C  
ATOM    349  C   LEU A 106     -37.400   2.622 106.869  1.00 68.21           C  
ANISOU  349  C   LEU A 106     8649   6202  11064   -207    -72   -455       C  
ATOM    350  O   LEU A 106     -37.945   3.049 105.850  1.00 67.24           O  
ANISOU  350  O   LEU A 106     8754   5870  10925   -112    140   -400       O  
ATOM    351  CB  LEU A 106     -39.028   1.989 108.689  1.00 61.46           C  
ANISOU  351  CB  LEU A 106     8015   5487   9848     19   -374   -585       C  
ATOM    352  CG  LEU A 106     -40.055   1.001 109.232  1.00 63.67           C  
ANISOU  352  CG  LEU A 106     8345   5884   9962    264   -449   -529       C  
ATOM    353  CD1 LEU A 106     -40.687   1.526 110.506  1.00 64.84           C  
ANISOU  353  CD1 LEU A 106     8667   6090   9877    216   -571   -681       C  
ATOM    354  CD2 LEU A 106     -41.137   0.700 108.201  1.00 62.84           C  
ANISOU  354  CD2 LEU A 106     8395   5641   9840    482   -276   -469       C  
ATOM    355  N   VAL A 107     -36.231   3.113 107.350  1.00 67.27           N  
ANISOU  355  N   VAL A 107     8290   6189  11081   -530   -166   -510       N  
ATOM    356  CA  VAL A 107     -35.446   4.176 106.715  1.00 69.96           C  
ANISOU  356  CA  VAL A 107     8609   6357  11615   -843     12   -514       C  
ATOM    357  C   VAL A 107     -34.814   3.595 105.425  1.00 74.77           C  
ANISOU  357  C   VAL A 107     8989   7050  12370   -714    266   -293       C  
ATOM    358  O   VAL A 107     -34.698   4.308 104.424  1.00 75.18           O  
ANISOU  358  O   VAL A 107     9174   6895  12495   -802    539   -204       O  
ATOM    359  CB  VAL A 107     -34.401   4.785 107.695  1.00 78.08           C  
ANISOU  359  CB  VAL A 107     9391   7536  12739  -1292   -200   -676       C  
ATOM    360  CG1 VAL A 107     -33.458   5.762 106.997  1.00 81.82           C  
ANISOU  360  CG1 VAL A 107     9764   7845  13479  -1683     12   -652       C  
ATOM    361  CG2 VAL A 107     -35.089   5.473 108.871  1.00 78.65           C  
ANISOU  361  CG2 VAL A 107     9787   7489  12609  -1426   -391   -962       C  
ATOM    362  N   LEU A 108     -34.460   2.289 105.438  1.00 71.68           N  
ANISOU  362  N   LEU A 108     8292   6938  12003   -474    211   -193       N  
ATOM    363  CA  LEU A 108     -33.909   1.590 104.271  1.00 72.42           C  
ANISOU  363  CA  LEU A 108     8194   7114  12207   -289    483    -38       C  
ATOM    364  C   LEU A 108     -35.011   1.346 103.232  1.00 74.19           C  
ANISOU  364  C   LEU A 108     8799   7152  12239    -22    679    -27       C  
ATOM    365  O   LEU A 108     -34.783   1.532 102.034  1.00 75.44           O  
ANISOU  365  O   LEU A 108     9003   7272  12389      4    970     60       O  
ATOM    366  CB  LEU A 108     -33.242   0.257 104.667  1.00 73.26           C  
ANISOU  366  CB  LEU A 108     7900   7506  12427    -62    390     52       C  
ATOM    367  CG  LEU A 108     -31.998   0.331 105.556  1.00 82.35           C  
ANISOU  367  CG  LEU A 108     8544   8986  13760   -269    182    109       C  
ATOM    368  CD1 LEU A 108     -31.688  -1.019 106.157  1.00 83.21           C  
ANISOU  368  CD1 LEU A 108     8355   9336  13926     64     36    251       C  
ATOM    369  CD2 LEU A 108     -30.784   0.839 104.790  1.00 89.62           C  
ANISOU  369  CD2 LEU A 108     9106  10026  14920   -488    423    200       C  
ATOM    370  N   TRP A 109     -36.212   0.962 103.697  1.00 67.36           N  
ANISOU  370  N   TRP A 109     8186   6216  11190    153    516   -109       N  
ATOM    371  CA  TRP A 109     -37.363   0.721 102.837  1.00 65.44           C  
ANISOU  371  CA  TRP A 109     8251   5872  10741    367    624   -119       C  
ATOM    372  C   TRP A 109     -37.941   2.028 102.294  1.00 69.84           C  
ANISOU  372  C   TRP A 109     9113   6238  11186    290    730    -76       C  
ATOM    373  O   TRP A 109     -38.549   2.010 101.224  1.00 68.85           O  
ANISOU  373  O   TRP A 109     9170   6107  10884    443    874    -13       O  
ATOM    374  CB  TRP A 109     -38.443  -0.068 103.583  1.00 62.18           C  
ANISOU  374  CB  TRP A 109     7941   5476  10207    530    421   -198       C  
ATOM    375  CG  TRP A 109     -38.190  -1.542 103.627  1.00 63.46           C  
ANISOU  375  CG  TRP A 109     7930   5728  10454    701    422   -192       C  
ATOM    376  CD1 TRP A 109     -37.807  -2.276 104.710  1.00 66.87           C  
ANISOU  376  CD1 TRP A 109     8160   6248  11001    743    257   -144       C  
ATOM    377  CD2 TRP A 109     -38.325  -2.468 102.540  1.00 63.73           C  
ANISOU  377  CD2 TRP A 109     8015   5743  10458    867    616   -234       C  
ATOM    378  NE1 TRP A 109     -37.695  -3.602 104.369  1.00 67.05           N  
ANISOU  378  NE1 TRP A 109     8114   6239  11123    950    362   -121       N  
ATOM    379  CE2 TRP A 109     -37.996  -3.747 103.038  1.00 68.55           C  
ANISOU  379  CE2 TRP A 109     8467   6348  11231   1010    590   -218       C  
ATOM    380  CE3 TRP A 109     -38.693  -2.342 101.188  1.00 65.45           C  
ANISOU  380  CE3 TRP A 109     8416   5956  10498    911    813   -287       C  
ATOM    381  CZ2 TRP A 109     -38.006  -4.890 102.227  1.00 68.97           C  
ANISOU  381  CZ2 TRP A 109     8569   6313  11323   1178    788   -306       C  
ATOM    382  CZ3 TRP A 109     -38.703  -3.474 100.387  1.00 67.95           C  
ANISOU  382  CZ3 TRP A 109     8765   6269  10785   1051    974   -402       C  
ATOM    383  CH2 TRP A 109     -38.371  -4.731 100.908  1.00 69.25           C  
ANISOU  383  CH2 TRP A 109     8801   6351  11160   1174    975   -437       C  
ATOM    384  N   SER A 110     -37.728   3.167 102.999  1.00 68.47           N  
ANISOU  384  N   SER A 110     9004   5904  11108     55    669   -108       N  
ATOM    385  CA  SER A 110     -38.214   4.483 102.549  1.00 69.80           C  
ANISOU  385  CA  SER A 110     9496   5788  11238      4    813    -36       C  
ATOM    386  C   SER A 110     -37.423   4.992 101.314  1.00 74.68           C  
ANISOU  386  C   SER A 110    10096   6350  11929   -104   1123    165       C  
ATOM    387  O   SER A 110     -37.650   6.112 100.852  1.00 75.78           O  
ANISOU  387  O   SER A 110    10501   6217  12074   -158   1292    301       O  
ATOM    388  CB  SER A 110     -38.194   5.509 103.683  1.00 76.09           C  
ANISOU  388  CB  SER A 110    10419   6355  12138   -233    699   -187       C  
ATOM    389  OG  SER A 110     -36.880   5.887 104.054  1.00 91.56           O  
ANISOU  389  OG  SER A 110    12141   8325  14323   -616    695   -242       O  
ATOM    390  N   GLY A 111     -36.549   4.140 100.779  1.00 71.61           N  
ANISOU  390  N   GLY A 111     9410   6208  11590    -96   1229    207       N  
ATOM    391  CA  GLY A 111     -35.777   4.401  99.569  1.00 74.47           C  
ANISOU  391  CA  GLY A 111     9710   6612  11975   -161   1566    401       C  
ATOM    392  C   GLY A 111     -36.576   4.093  98.321  1.00 77.55           C  
ANISOU  392  C   GLY A 111    10343   7091  12032    135   1719    511       C  
ATOM    393  O   GLY A 111     -36.118   4.336  97.197  1.00 78.88           O  
ANISOU  393  O   GLY A 111    10535   7326  12108    129   2024    697       O  
ATOM    394  N   LEU A 112     -37.794   3.556  98.532  1.00 71.80           N  
ANISOU  394  N   LEU A 112     9779   6406  11094    375   1501    396       N  
ATOM    395  CA  LEU A 112     -38.756   3.218  97.492  1.00 71.35           C  
ANISOU  395  CA  LEU A 112     9931   6502  10676    629   1541    445       C  
ATOM    396  C   LEU A 112     -39.747   4.371  97.323  1.00 76.45           C  
ANISOU  396  C   LEU A 112    10885   6980  11184    723   1516    636       C  
ATOM    397  O   LEU A 112     -40.759   4.223  96.635  1.00 75.65           O  
ANISOU  397  O   LEU A 112    10932   7049  10762    950   1461    701       O  
ATOM    398  CB  LEU A 112     -39.464   1.895  97.806  1.00 68.46           C  
ANISOU  398  CB  LEU A 112     9504   6302  10205    787   1326    208       C  
ATOM    399  CG  LEU A 112     -38.677   0.650  97.450  1.00 73.64           C  
ANISOU  399  CG  LEU A 112     9960   7111  10908    820   1450     64       C  
ATOM    400  CD1 LEU A 112     -37.866   0.176  98.628  1.00 73.44           C  
ANISOU  400  CD1 LEU A 112     9648   7022  11233    732   1345    -13       C  
ATOM    401  CD2 LEU A 112     -39.588  -0.456  97.052  1.00 74.87           C  
ANISOU  401  CD2 LEU A 112    10215   7402  10832    973   1357   -131       C  
ATOM    402  N   ARG A 113     -39.410   5.546  97.914  1.00 75.45           N  
ANISOU  402  N   ARG A 113    10844   6517  11306    544   1571    730       N  
ATOM    403  CA  ARG A 113     -40.138   6.814  97.806  1.00 77.80           C  
ANISOU  403  CA  ARG A 113    11461   6522  11578    640   1634    945       C  
ATOM    404  C   ARG A 113     -40.190   7.194  96.337  1.00 87.19           C  
ANISOU  404  C   ARG A 113    12810   7812  12505    782   1884   1294       C  
ATOM    405  O   ARG A 113     -41.196   7.731  95.862  1.00 88.58           O  
ANISOU  405  O   ARG A 113    13216   7974  12465   1058   1873   1523       O  
ATOM    406  CB  ARG A 113     -39.429   7.896  98.625  1.00 80.63           C  
ANISOU  406  CB  ARG A 113    11883   6448  12303    325   1720    918       C  
ATOM    407  CG  ARG A 113     -40.156   8.298  99.887  1.00 95.35           C  
ANISOU  407  CG  ARG A 113    13881   8076  14273    356   1517    708       C  
ATOM    408  CD  ARG A 113     -39.511   9.525 100.502  1.00118.89           C  
ANISOU  408  CD  ARG A 113    17020  10576  17576     19   1647    657       C  
ATOM    409  NE  ARG A 113     -38.831   9.225 101.765  1.00135.43           N  
ANISOU  409  NE  ARG A 113    18894  12723  19839   -306   1438    302       N  
ATOM    410  CZ  ARG A 113     -39.392   9.337 102.968  1.00153.18           C  
ANISOU  410  CZ  ARG A 113    21240  14884  22078   -287   1239     26       C  
ATOM    411  NH1 ARG A 113     -38.699   9.040 104.059  1.00143.17           N  
ANISOU  411  NH1 ARG A 113    19756  13749  20893   -591   1032   -263       N  
ATOM    412  NH2 ARG A 113     -40.649   9.751 103.087  1.00140.01           N  
ANISOU  412  NH2 ARG A 113    19866  13040  20292     54   1254     55       N  
ATOM    413  N   ASN A 114     -39.089   6.833  95.624  1.00 86.66           N  
ANISOU  413  N   ASN A 114    12584   7912  12431    620   2112   1345       N  
ATOM    414  CA  ASN A 114     -38.859   6.881  94.181  1.00 90.27           C  
ANISOU  414  CA  ASN A 114    13127   8598  12573    714   2391   1626       C  
ATOM    415  C   ASN A 114     -39.490   5.605  93.623  1.00 93.94           C  
ANISOU  415  C   ASN A 114    13530   9525  12638    947   2232   1425       C  
ATOM    416  O   ASN A 114     -39.247   4.528  94.172  1.00 91.68           O  
ANISOU  416  O   ASN A 114    13021   9349  12465    895   2096   1087       O  
ATOM    417  CB  ASN A 114     -37.359   6.983  93.884  1.00 92.26           C  
ANISOU  417  CB  ASN A 114    13176   8833  13043    411   2722   1698       C  
ATOM    418  CG  ASN A 114     -36.645   8.030  94.713  1.00110.32           C  
ANISOU  418  CG  ASN A 114    15436  10673  15808     51   2803   1750       C  
ATOM    419  OD1 ASN A 114     -37.035   9.206  94.761  1.00106.11           O  
ANISOU  419  OD1 ASN A 114    15204   9744  15368     27   2883   1979       O  
ATOM    420  ND2 ASN A 114     -35.587   7.621  95.395  1.00100.87           N  
ANISOU  420  ND2 ASN A 114    13873   9524  14930   -236   2780   1529       N  
ATOM    421  N   ALA A 115     -40.344   5.733  92.586  1.00 92.40           N  
ANISOU  421  N   ALA A 115    13539   9591  11979   1197   2230   1633       N  
ATOM    422  CA  ALA A 115     -41.231   4.710  91.990  1.00 91.54           C  
ANISOU  422  CA  ALA A 115    13427   9935  11419   1391   2024   1439       C  
ATOM    423  C   ALA A 115     -42.553   4.796  92.768  1.00 92.48           C  
ANISOU  423  C   ALA A 115    13560  10007  11571   1546   1662   1375       C  
ATOM    424  O   ALA A 115     -42.810   3.981  93.660  1.00 87.58           O  
ANISOU  424  O   ALA A 115    12780   9364  11133   1482   1444   1036       O  
ATOM    425  CB  ALA A 115     -40.627   3.301  92.038  1.00 90.59           C  
ANISOU  425  CB  ALA A 115    13102   9986  11330   1282   2039   1017       C  
ATOM    426  N   PRO A 116     -43.351   5.866  92.501  1.00 92.33           N  
ANISOU  426  N   PRO A 116    13724   9936  11420   1769   1636   1751       N  
ATOM    427  CA  PRO A 116     -44.561   6.119  93.303  1.00 90.87           C  
ANISOU  427  CA  PRO A 116    13523   9678  11324   1958   1358   1736       C  
ATOM    428  C   PRO A 116     -45.591   4.989  93.335  1.00 93.48           C  
ANISOU  428  C   PRO A 116    13669  10445  11405   2026   1027   1443       C  
ATOM    429  O   PRO A 116     -46.078   4.700  94.429  1.00 89.98           O  
ANISOU  429  O   PRO A 116    13101   9877  11211   2002    847   1227       O  
ATOM    430  CB  PRO A 116     -45.137   7.381  92.660  1.00 97.01           C  
ANISOU  430  CB  PRO A 116    14526  10399  11935   2259   1455   2260       C  
ATOM    431  CG  PRO A 116     -43.943   8.073  92.101  1.00104.13           C  
ANISOU  431  CG  PRO A 116    15598  11039  12927   2100   1836   2528       C  
ATOM    432  CD  PRO A 116     -43.142   6.957  91.525  1.00 98.66           C  
ANISOU  432  CD  PRO A 116    14757  10696  12032   1886   1904   2256       C  
ATOM    433  N   ARG A 117     -45.900   4.340  92.180  1.00 93.13           N  
ANISOU  433  N   ARG A 117    13609  10911  10866   2070    958   1413       N  
ATOM    434  CA  ARG A 117     -46.870   3.239  92.087  1.00 92.84           C  
ANISOU  434  CA  ARG A 117    13399  11301  10576   2050    645   1098       C  
ATOM    435  C   ARG A 117     -46.582   2.119  93.074  1.00 92.81           C  
ANISOU  435  C   ARG A 117    13244  11103  10917   1805    580    640       C  
ATOM    436  O   ARG A 117     -47.523   1.473  93.535  1.00 91.36           O  
ANISOU  436  O   ARG A 117    12902  11074  10735   1776    325    437       O  
ATOM    437  CB  ARG A 117     -46.932   2.662  90.679  1.00 98.46           C  
ANISOU  437  CB  ARG A 117    14165  12548  10700   2034    631   1034       C  
ATOM    438  CG  ARG A 117     -47.865   3.418  89.758  1.00117.07           C  
ANISOU  438  CG  ARG A 117    16565  15353  12563   2321    488   1449       C  
ATOM    439  CD  ARG A 117     -49.303   2.933  89.924  1.00131.16           C  
ANISOU  439  CD  ARG A 117    18101  17562  14173   2375     70   1308       C  
ATOM    440  NE  ARG A 117     -49.957   2.684  88.638  1.00148.69           N  
ANISOU  440  NE  ARG A 117    20293  20508  15693   2435   -139   1358       N  
ATOM    441  CZ  ARG A 117     -51.214   2.274  88.503  1.00168.54           C  
ANISOU  441  CZ  ARG A 117    22545  23556  17937   2447   -532   1259       C  
ATOM    442  NH1 ARG A 117     -51.959   2.007  89.567  1.00154.22           N  
ANISOU  442  NH1 ARG A 117    20472  21611  16513   2405   -718   1105       N  
ATOM    443  NH2 ARG A 117     -51.719   2.092  87.280  1.00162.71           N  
ANISOU  443  NH2 ARG A 117    21782  23541  16499   2473   -743   1300       N  
ATOM    444  N   CYS A 118     -45.300   1.909  93.419  1.00 87.64           N  
ANISOU  444  N   CYS A 118    12609  10124  10565   1637    813    522       N  
ATOM    445  CA  CYS A 118     -44.915   0.907  94.397  1.00 84.26           C  
ANISOU  445  CA  CYS A 118    12040   9493  10484   1460    770    178       C  
ATOM    446  C   CYS A 118     -45.017   1.490  95.823  1.00 84.09           C  
ANISOU  446  C   CYS A 118    11957   9130  10865   1460    688    245       C  
ATOM    447  O   CYS A 118     -45.524   0.807  96.713  1.00 81.38           O  
ANISOU  447  O   CYS A 118    11490   8760  10669   1408    515     50       O  
ATOM    448  CB  CYS A 118     -43.517   0.378  94.100  1.00 85.36           C  
ANISOU  448  CB  CYS A 118    12168   9520  10743   1335   1043     48       C  
ATOM    449  SG  CYS A 118     -42.735  -0.477  95.493  1.00 86.28           S  
ANISOU  449  SG  CYS A 118    12088   9306  11387   1196   1032   -190       S  
ATOM    450  N   TRP A 119     -44.562   2.751  96.027  1.00 80.40           N  
ANISOU  450  N   TRP A 119    11599   8396  10555   1499    831    511       N  
ATOM    451  CA  TRP A 119     -44.577   3.451  97.319  1.00 78.17           C  
ANISOU  451  CA  TRP A 119    11321   7771  10608   1476    789    529       C  
ATOM    452  C   TRP A 119     -45.990   3.575  97.894  1.00 80.68           C  
ANISOU  452  C   TRP A 119    11611   8178  10867   1663    579    531       C  
ATOM    453  O   TRP A 119     -46.148   3.464  99.108  1.00 78.63           O  
ANISOU  453  O   TRP A 119    11286   7769  10820   1612    491    383       O  
ATOM    454  CB  TRP A 119     -43.931   4.843  97.195  1.00 79.20           C  
ANISOU  454  CB  TRP A 119    11635   7573  10885   1459   1014    797       C  
ATOM    455  CG  TRP A 119     -43.757   5.600  98.483  1.00 79.45           C  
ANISOU  455  CG  TRP A 119    11719   7213  11254   1364   1006    732       C  
ATOM    456  CD1 TRP A 119     -44.254   6.836  98.772  1.00 84.52           C  
ANISOU  456  CD1 TRP A 119    12579   7547  11987   1500   1077    899       C  
ATOM    457  CD2 TRP A 119     -42.998   5.194  99.635  1.00 77.13           C  
ANISOU  457  CD2 TRP A 119    11281   6800  11226   1116    934    472       C  
ATOM    458  NE1 TRP A 119     -43.871   7.220 100.035  1.00 83.54           N  
ANISOU  458  NE1 TRP A 119    12482   7110  12148   1315   1059    693       N  
ATOM    459  CE2 TRP A 119     -43.090   6.236 100.585  1.00 82.22           C  
ANISOU  459  CE2 TRP A 119    12078   7097  12066   1069    947    444       C  
ATOM    460  CE3 TRP A 119     -42.260   4.045  99.963  1.00 76.24           C  
ANISOU  460  CE3 TRP A 119    10928   6845  11194    957    862    271       C  
ATOM    461  CZ2 TRP A 119     -42.482   6.156 101.845  1.00 80.37           C  
ANISOU  461  CZ2 TRP A 119    11753   6749  12037    829    849    199       C  
ATOM    462  CZ3 TRP A 119     -41.661   3.968 101.210  1.00 76.52           C  
ANISOU  462  CZ3 TRP A 119    10845   6769  11461    769    761    105       C  
ATOM    463  CH2 TRP A 119     -41.777   5.012 102.136  1.00 78.13           C  
ANISOU  463  CH2 TRP A 119    11192   6704  11789    686    735     58       C  
ATOM    464  N   ALA A 120     -47.005   3.774  97.034  1.00 78.53           N  
ANISOU  464  N   ALA A 120    11355   8204  10280   1886    498    709       N  
ATOM    465  CA  ALA A 120     -48.409   3.917  97.424  1.00 78.42           C  
ANISOU  465  CA  ALA A 120    11235   8368  10193   2104    311    761       C  
ATOM    466  C   ALA A 120     -48.968   2.669  98.107  1.00 79.06           C  
ANISOU  466  C   ALA A 120    11086   8642  10312   1956    116    453       C  
ATOM    467  O   ALA A 120     -49.765   2.809  99.036  1.00 78.49           O  
ANISOU  467  O   ALA A 120    10913   8554  10356   2051     38    437       O  
ATOM    468  CB  ALA A 120     -49.258   4.257  96.217  1.00 82.81           C  
ANISOU  468  CB  ALA A 120    11781   9319  10363   2356    232   1039       C  
ATOM    469  N   VAL A 121     -48.547   1.465  97.672  1.00 73.56           N  
ANISOU  469  N   VAL A 121    10323   8090   9535   1730     80    214       N  
ATOM    470  CA  VAL A 121     -49.040   0.199  98.232  1.00 71.41           C  
ANISOU  470  CA  VAL A 121     9871   7931   9330   1555    -66    -59       C  
ATOM    471  C   VAL A 121     -48.068  -0.417  99.255  1.00 71.82           C  
ANISOU  471  C   VAL A 121     9929   7650   9711   1378     19   -226       C  
ATOM    472  O   VAL A 121     -48.521  -1.209 100.082  1.00 70.73           O  
ANISOU  472  O   VAL A 121     9668   7510   9697   1280    -71   -355       O  
ATOM    473  CB  VAL A 121     -49.413  -0.853  97.152  1.00 77.09           C  
ANISOU  473  CB  VAL A 121    10529   9001   9761   1413   -170   -258       C  
ATOM    474  CG1 VAL A 121     -50.657  -0.438  96.371  1.00 80.02           C  
ANISOU  474  CG1 VAL A 121    10783   9845   9776   1563   -362   -107       C  
ATOM    475  CG2 VAL A 121     -48.242  -1.149  96.221  1.00 77.72           C  
ANISOU  475  CG2 VAL A 121    10777   9018   9737   1331     12   -351       C  
ATOM    476  N   ILE A 122     -46.760  -0.095  99.199  1.00 67.01           N  
ANISOU  476  N   ILE A 122     9424   6800   9235   1333    188   -194       N  
ATOM    477  CA  ILE A 122     -45.793  -0.688 100.126  1.00 65.05           C  
ANISOU  477  CA  ILE A 122     9118   6323   9276   1196    234   -309       C  
ATOM    478  C   ILE A 122     -45.893  -0.050 101.530  1.00 68.55           C  
ANISOU  478  C   ILE A 122     9548   6602   9894   1210    173   -257       C  
ATOM    479  O   ILE A 122     -45.724  -0.777 102.511  1.00 68.18           O  
ANISOU  479  O   ILE A 122     9407   6505   9992   1127    110   -343       O  
ATOM    480  CB  ILE A 122     -44.334  -0.696  99.576  1.00 68.76           C  
ANISOU  480  CB  ILE A 122     9611   6679   9837   1129    429   -303       C  
ATOM    481  CG1 ILE A 122     -43.496  -1.804 100.237  1.00 68.42           C  
ANISOU  481  CG1 ILE A 122     9433   6519  10043   1042    450   -434       C  
ATOM    482  CG2 ILE A 122     -43.641   0.678  99.641  1.00 69.70           C  
ANISOU  482  CG2 ILE A 122     9810   6631  10043   1125    545   -114       C  
ATOM    483  CD1 ILE A 122     -42.336  -2.329  99.395  1.00 78.86           C  
ANISOU  483  CD1 ILE A 122    10720   7831  11412   1032    666   -489       C  
ATOM    484  N   GLN A 123     -46.190   1.272 101.628  1.00 64.88           N  
ANISOU  484  N   GLN A 123     9203   6049   9401   1326    209   -118       N  
ATOM    485  CA  GLN A 123     -46.300   2.011 102.890  1.00 63.91           C  
ANISOU  485  CA  GLN A 123     9133   5749   9401   1341    190   -132       C  
ATOM    486  C   GLN A 123     -47.224   1.314 103.916  1.00 67.35           C  
ANISOU  486  C   GLN A 123     9447   6326   9817   1365     66   -222       C  
ATOM    487  O   GLN A 123     -46.741   1.092 105.027  1.00 66.13           O  
ANISOU  487  O   GLN A 123     9267   6097   9761   1256     29   -305       O  
ATOM    488  CB  GLN A 123     -46.759   3.452 102.657  1.00 67.03           C  
ANISOU  488  CB  GLN A 123     9718   5989   9763   1524    290     20       C  
ATOM    489  CG  GLN A 123     -45.631   4.394 102.304  1.00 76.16           C  
ANISOU  489  CG  GLN A 123    11038   6853  11048   1410    454     97       C  
ATOM    490  CD  GLN A 123     -46.102   5.825 102.200  1.00 92.33           C  
ANISOU  490  CD  GLN A 123    13329   8630  13122   1598    593    259       C  
ATOM    491  OE1 GLN A 123     -45.889   6.639 103.104  1.00 89.98           O  
ANISOU  491  OE1 GLN A 123    13186   8018  12985   1534    659    155       O  
ATOM    492  NE2 GLN A 123     -46.730   6.171 101.081  1.00 79.67           N  
ANISOU  492  NE2 GLN A 123    11782   7134  11353   1842    648    519       N  
ATOM    493  N   PRO A 124     -48.495   0.913 103.601  1.00 64.97           N  
ANISOU  493  N   PRO A 124     9037   6270   9378   1478     -4   -192       N  
ATOM    494  CA  PRO A 124     -49.325   0.241 104.621  1.00 64.60           C  
ANISOU  494  CA  PRO A 124     8847   6357   9340   1457    -76   -249       C  
ATOM    495  C   PRO A 124     -48.816  -1.143 105.008  1.00 68.15           C  
ANISOU  495  C   PRO A 124     9207   6795   9893   1247   -120   -338       C  
ATOM    496  O   PRO A 124     -49.028  -1.553 106.148  1.00 67.71           O  
ANISOU  496  O   PRO A 124     9095   6753   9877   1204   -139   -341       O  
ATOM    497  CB  PRO A 124     -50.702   0.126 103.957  1.00 67.91           C  
ANISOU  497  CB  PRO A 124     9108   7084   9610   1577   -140   -183       C  
ATOM    498  CG  PRO A 124     -50.671   1.049 102.809  1.00 73.96           C  
ANISOU  498  CG  PRO A 124     9976   7866  10258   1748   -111    -51       C  
ATOM    499  CD  PRO A 124     -49.256   1.072 102.347  1.00 68.36           C  
ANISOU  499  CD  PRO A 124     9434   6923   9618   1611    -31    -87       C  
ATOM    500  N   LEU A 125     -48.158  -1.860 104.070  1.00 64.23           N  
ANISOU  500  N   LEU A 125     8712   6263   9428   1144   -106   -395       N  
ATOM    501  CA  LEU A 125     -47.607  -3.194 104.307  1.00 63.64           C  
ANISOU  501  CA  LEU A 125     8584   6096   9500   1001    -99   -465       C  
ATOM    502  C   LEU A 125     -46.442  -3.141 105.293  1.00 67.97           C  
ANISOU  502  C   LEU A 125     9138   6489  10198    987    -87   -412       C  
ATOM    503  O   LEU A 125     -46.392  -3.965 106.208  1.00 67.80           O  
ANISOU  503  O   LEU A 125     9054   6439  10268    944   -116   -367       O  
ATOM    504  CB  LEU A 125     -47.163  -3.846 102.983  1.00 64.39           C  
ANISOU  504  CB  LEU A 125     8716   6173   9577    943    -34   -580       C  
ATOM    505  CG  LEU A 125     -46.512  -5.236 103.060  1.00 69.15           C  
ANISOU  505  CG  LEU A 125     9307   6591  10376    851     39   -670       C  
ATOM    506  CD1 LEU A 125     -47.508  -6.302 103.485  1.00 69.82           C  
ANISOU  506  CD1 LEU A 125     9339   6668  10520    718     -6   -723       C  
ATOM    507  CD2 LEU A 125     -45.884  -5.608 101.741  1.00 73.38           C  
ANISOU  507  CD2 LEU A 125     9923   7092  10865    843    165   -818       C  
ATOM    508  N   LEU A 126     -45.521  -2.171 105.115  1.00 65.05           N  
ANISOU  508  N   LEU A 126     8827   6043   9847   1006    -48   -392       N  
ATOM    509  CA  LEU A 126     -44.334  -2.000 105.957  1.00 65.21           C  
ANISOU  509  CA  LEU A 126     8795   5992   9990    945    -76   -361       C  
ATOM    510  C   LEU A 126     -44.705  -1.636 107.397  1.00 69.34           C  
ANISOU  510  C   LEU A 126     9334   6576  10436    934   -180   -352       C  
ATOM    511  O   LEU A 126     -44.107  -2.192 108.316  1.00 70.23           O  
ANISOU  511  O   LEU A 126     9352   6740  10594    892   -261   -298       O  
ATOM    512  CB  LEU A 126     -43.365  -0.961 105.371  1.00 65.89           C  
ANISOU  512  CB  LEU A 126     8920   5991  10123    893      2   -359       C  
ATOM    513  CG  LEU A 126     -42.713  -1.323 104.028  1.00 70.77           C  
ANISOU  513  CG  LEU A 126     9506   6592  10791    902    149   -350       C  
ATOM    514  CD1 LEU A 126     -42.184  -0.092 103.333  1.00 72.17           C  
ANISOU  514  CD1 LEU A 126     9769   6695  10959    852    270   -296       C  
ATOM    515  CD2 LEU A 126     -41.617  -2.347 104.190  1.00 73.04           C  
ANISOU  515  CD2 LEU A 126     9607   6878  11268    892    180   -336       C  
ATOM    516  N   CYS A 127     -45.698  -0.743 107.603  1.00 64.98           N  
ANISOU  516  N   CYS A 127     8898   6044   9746   1006   -163   -390       N  
ATOM    517  CA  CYS A 127     -46.147  -0.379 108.948  1.00 65.31           C  
ANISOU  517  CA  CYS A 127     8987   6160   9666   1021   -208   -426       C  
ATOM    518  C   CYS A 127     -46.785  -1.584 109.609  1.00 65.93           C  
ANISOU  518  C   CYS A 127     8951   6394   9706   1029   -241   -335       C  
ATOM    519  O   CYS A 127     -46.485  -1.853 110.762  1.00 65.90           O  
ANISOU  519  O   CYS A 127     8929   6485   9626    988   -307   -296       O  
ATOM    520  CB  CYS A 127     -47.093   0.819 108.927  1.00 67.28           C  
ANISOU  520  CB  CYS A 127     9389   6363   9813   1162   -118   -486       C  
ATOM    521  SG  CYS A 127     -46.253   2.424 108.815  1.00 73.48           S  
ANISOU  521  SG  CYS A 127    10400   6861  10657   1102    -49   -601       S  
ATOM    522  N   ALA A 128     -47.581  -2.362 108.850  1.00 61.07           N  
ANISOU  522  N   ALA A 128     8256   5810   9137   1047   -200   -293       N  
ATOM    523  CA  ALA A 128     -48.258  -3.581 109.310  1.00 61.02           C  
ANISOU  523  CA  ALA A 128     8144   5886   9155    993   -192   -200       C  
ATOM    524  C   ALA A 128     -47.285  -4.708 109.707  1.00 65.59           C  
ANISOU  524  C   ALA A 128     8683   6358   9878    928   -218    -88       C  
ATOM    525  O   ALA A 128     -47.698  -5.623 110.422  1.00 65.51           O  
ANISOU  525  O   ALA A 128     8629   6374   9888    890   -193     51       O  
ATOM    526  CB  ALA A 128     -49.197  -4.086 108.233  1.00 61.72           C  
ANISOU  526  CB  ALA A 128     8155   6016   9281    952   -161   -242       C  
ATOM    527  N   VAL A 129     -46.012  -4.650 109.246  1.00 62.93           N  
ANISOU  527  N   VAL A 129     8346   5906   9659    935   -243   -109       N  
ATOM    528  CA  VAL A 129     -44.990  -5.659 109.546  1.00 63.90           C  
ANISOU  528  CA  VAL A 129     8388   5938   9952    954   -254     31       C  
ATOM    529  C   VAL A 129     -43.992  -5.124 110.603  1.00 69.72           C  
ANISOU  529  C   VAL A 129     9060   6827  10603    968   -393    115       C  
ATOM    530  O   VAL A 129     -43.777  -5.783 111.622  1.00 71.70           O  
ANISOU  530  O   VAL A 129     9251   7172  10822   1009   -460    315       O  
ATOM    531  CB  VAL A 129     -44.273  -6.145 108.256  1.00 67.62           C  
ANISOU  531  CB  VAL A 129     8842   6225  10626    977   -153    -47       C  
ATOM    532  CG1 VAL A 129     -43.066  -7.023 108.579  1.00 69.46           C  
ANISOU  532  CG1 VAL A 129     8957   6367  11069   1078   -138    118       C  
ATOM    533  CG2 VAL A 129     -45.238  -6.894 107.341  1.00 67.44           C  
ANISOU  533  CG2 VAL A 129     8891   6087  10645    912    -49   -166       C  
ATOM    534  N   TYR A 130     -43.399  -3.940 110.355  1.00 65.35           N  
ANISOU  534  N   TYR A 130     8520   6309  10003    912   -439    -27       N  
ATOM    535  CA  TYR A 130     -42.396  -3.326 111.223  1.00 66.20           C  
ANISOU  535  CA  TYR A 130     8544   6579  10029    837   -596    -24       C  
ATOM    536  C   TYR A 130     -42.978  -2.721 112.507  1.00 70.75           C  
ANISOU  536  C   TYR A 130     9235   7343  10304    790   -692    -84       C  
ATOM    537  O   TYR A 130     -42.429  -2.981 113.579  1.00 72.44           O  
ANISOU  537  O   TYR A 130     9358   7787  10380    769   -851     24       O  
ATOM    538  CB  TYR A 130     -41.568  -2.286 110.464  1.00 66.91           C  
ANISOU  538  CB  TYR A 130     8617   6593  10214    722   -574   -172       C  
ATOM    539  CG  TYR A 130     -40.578  -2.927 109.520  1.00 68.30           C  
ANISOU  539  CG  TYR A 130     8606   6700  10646    771   -491    -82       C  
ATOM    540  CD1 TYR A 130     -40.856  -3.048 108.164  1.00 68.90           C  
ANISOU  540  CD1 TYR A 130     8762   6598  10820    825   -299   -139       C  
ATOM    541  CD2 TYR A 130     -39.359  -3.403 109.979  1.00 71.53           C  
ANISOU  541  CD2 TYR A 130     8740   7265  11171    786   -596     62       C  
ATOM    542  CE1 TYR A 130     -39.967  -3.686 107.297  1.00 70.79           C  
ANISOU  542  CE1 TYR A 130     8854   6781  11262    897   -168    -90       C  
ATOM    543  CE2 TYR A 130     -38.477  -4.067 109.131  1.00 73.49           C  
ANISOU  543  CE2 TYR A 130     8794   7452  11675    896   -465    154       C  
ATOM    544  CZ  TYR A 130     -38.769  -4.177 107.781  1.00 78.69           C  
ANISOU  544  CZ  TYR A 130     9577   7899  12422    945   -229     54       C  
ATOM    545  OH  TYR A 130     -37.886  -4.785 106.924  1.00 79.37           O  
ANISOU  545  OH  TYR A 130     9497   7932  12726   1066    -50    102       O  
ATOM    546  N   MET A 131     -44.069  -1.943 112.420  1.00 66.15           N  
ANISOU  546  N   MET A 131     8840   6697   9596    804   -591   -240       N  
ATOM    547  CA  MET A 131     -44.692  -1.352 113.610  1.00 67.80           C  
ANISOU  547  CA  MET A 131     9183   7071   9506    799   -613   -337       C  
ATOM    548  C   MET A 131     -46.154  -1.843 113.743  1.00 71.52           C  
ANISOU  548  C   MET A 131     9687   7587   9898    929   -466   -249       C  
ATOM    549  O   MET A 131     -47.066  -1.030 113.586  1.00 70.52           O  
ANISOU  549  O   MET A 131     9676   7416   9702   1007   -344   -387       O  
ATOM    550  CB  MET A 131     -44.614   0.186 113.555  1.00 71.12           C  
ANISOU  550  CB  MET A 131     9796   7362   9864    720   -579   -624       C  
ATOM    551  CG  MET A 131     -43.235   0.724 113.862  1.00 77.21           C  
ANISOU  551  CG  MET A 131    10518   8173  10644    496   -746   -743       C  
ATOM    552  SD  MET A 131     -43.000   2.435 113.325  1.00 83.26           S  
ANISOU  552  SD  MET A 131    11523   8600  11512    341   -637  -1048       S  
ATOM    553  CE  MET A 131     -43.712   3.304 114.672  1.00 83.01           C  
ANISOU  553  CE  MET A 131    11785   8624  11131    331   -609  -1344       C  
ATOM    554  N   PRO A 132     -46.422  -3.159 113.973  1.00 68.74           N  
ANISOU  554  N   PRO A 132     9220   7304   9596    957   -452     -3       N  
ATOM    555  CA  PRO A 132     -47.824  -3.610 114.037  1.00 68.78           C  
ANISOU  555  CA  PRO A 132     9208   7361   9565   1007   -299     76       C  
ATOM    556  C   PRO A 132     -48.478  -3.370 115.389  1.00 75.47           C  
ANISOU  556  C   PRO A 132    10116   8474  10085   1047   -240    106       C  
ATOM    557  O   PRO A 132     -47.789  -3.129 116.376  1.00 76.55           O  
ANISOU  557  O   PRO A 132    10320   8779   9985   1023   -351    100       O  
ATOM    558  CB  PRO A 132     -47.735  -5.104 113.727  1.00 70.64           C  
ANISOU  558  CB  PRO A 132     9330   7482  10027    964   -276    311       C  
ATOM    559  CG  PRO A 132     -46.341  -5.495 114.064  1.00 76.00           C  
ANISOU  559  CG  PRO A 132     9970   8146  10758    977   -415    438       C  
ATOM    560  CD  PRO A 132     -45.487  -4.283 114.181  1.00 71.30           C  
ANISOU  560  CD  PRO A 132     9413   7636  10041    949   -549    236       C  
ATOM    561  N   LYS A 133     -49.818  -3.446 115.428  1.00 73.33           N  
ANISOU  561  N   LYS A 133     9796   8293   9774   1102    -63    136       N  
ATOM    562  CA  LYS A 133     -50.589  -3.247 116.650  1.00 76.07           C  
ANISOU  562  CA  LYS A 133    10181   8921   9801   1166     70    172       C  
ATOM    563  C   LYS A 133     -50.496  -4.471 117.554  1.00 83.37           C  
ANISOU  563  C   LYS A 133    11050   9999  10629   1094     79    509       C  
ATOM    564  O   LYS A 133     -50.789  -5.591 117.126  1.00 82.59           O  
ANISOU  564  O   LYS A 133    10825   9773  10784   1008    133    734       O  
ATOM    565  CB  LYS A 133     -52.064  -2.919 116.329  1.00 78.79           C  
ANISOU  565  CB  LYS A 133    10414   9351  10172   1271    284    128       C  
ATOM    566  CG  LYS A 133     -52.926  -2.621 117.563  1.00 91.32           C  
ANISOU  566  CG  LYS A 133    12021  11252  11423   1381    495    144       C  
ATOM    567  CD  LYS A 133     -54.364  -2.329 117.193  1.00 98.20           C  
ANISOU  567  CD  LYS A 133    12691  12251  12368   1518    716    136       C  
ATOM    568  CE  LYS A 133     -55.205  -2.033 118.400  1.00108.17           C  
ANISOU  568  CE  LYS A 133    13953  13843  13302   1658    984    149       C  
ATOM    569  NZ  LYS A 133     -56.591  -1.670 118.012  1.00120.08           N  
ANISOU  569  NZ  LYS A 133    15196  15516  14914   1842   1210    155       N  
ATOM    570  N   CYS A 134     -50.095  -4.240 118.810  1.00 83.83           N  
ANISOU  570  N   CYS A 134    11224  10323  10304   1120     33    540       N  
ATOM    571  CA  CYS A 134     -50.031  -5.262 119.844  1.00 87.35           C  
ANISOU  571  CA  CYS A 134    11648  10985  10554   1099     54    918       C  
ATOM    572  C   CYS A 134     -50.981  -4.861 120.973  1.00 94.81           C  
ANISOU  572  C   CYS A 134    12666  12298  11060   1166    269    907       C  
ATOM    573  O   CYS A 134     -50.875  -3.752 121.504  1.00 95.66           O  
ANISOU  573  O   CYS A 134    12937  12576  10832   1228    254    586       O  
ATOM    574  CB  CYS A 134     -48.605  -5.466 120.346  1.00 89.48           C  
ANISOU  574  CB  CYS A 134    11956  11351  10692   1090   -225   1034       C  
ATOM    575  SG  CYS A 134     -48.327  -7.066 121.152  1.00 97.17           S  
ANISOU  575  SG  CYS A 134    12861  12431  11628   1125   -222   1662       S  
ATOM    576  N   GLU A 135     -51.938  -5.741 121.309  1.00 93.07           N  
ANISOU  576  N   GLU A 135    12330  12179  10855   1138    508   1231       N  
ATOM    577  CA  GLU A 135     -52.905  -5.472 122.368  1.00 96.27           C  
ANISOU  577  CA  GLU A 135    12761  12970  10846   1210    781   1271       C  
ATOM    578  C   GLU A 135     -53.209  -6.751 123.134  1.00102.02           C  
ANISOU  578  C   GLU A 135    13424  13853  11487   1129    936   1807       C  
ATOM    579  O   GLU A 135     -53.591  -7.760 122.530  1.00100.65           O  
ANISOU  579  O   GLU A 135    13089  13416  11736    991   1024   2071       O  
ATOM    580  CB  GLU A 135     -54.185  -4.845 121.792  1.00 97.06           C  
ANISOU  580  CB  GLU A 135    12714  13058  11105   1284   1031   1048       C  
ATOM    581  CG  GLU A 135     -54.863  -3.869 122.741  1.00111.82           C  
ANISOU  581  CG  GLU A 135    14690  15282  12514   1472   1281    832       C  
ATOM    582  CD  GLU A 135     -55.905  -2.958 122.115  1.00132.25           C  
ANISOU  582  CD  GLU A 135    17147  17831  15271   1655   1491    561       C  
ATOM    583  OE1 GLU A 135     -56.898  -3.476 121.554  1.00121.21           O  
ANISOU  583  OE1 GLU A 135    15425  16457  14172   1614   1645    747       O  
ATOM    584  OE2 GLU A 135     -55.748  -1.721 122.227  1.00129.23           O  
ANISOU  584  OE2 GLU A 135    16980  17404  14718   1841   1510    169       O  
ATOM    585  N   ASN A 136     -52.983  -6.702 124.466  1.00102.32           N  
ANISOU  585  N   ASN A 136    13614  14307  10954   1198    964   1961       N  
ATOM    586  CA  ASN A 136     -53.194  -7.776 125.436  1.00106.83           C  
ANISOU  586  CA  ASN A 136    14184  15111  11296   1164   1129   2528       C  
ATOM    587  C   ASN A 136     -52.491  -9.084 124.988  1.00110.45           C  
ANISOU  587  C   ASN A 136    14588  15188  12191   1081    986   2979       C  
ATOM    588  O   ASN A 136     -53.136 -10.110 124.747  1.00110.45           O  
ANISOU  588  O   ASN A 136    14474  14949  12542    947   1218   3332       O  
ATOM    589  CB  ASN A 136     -54.692  -7.970 125.701  1.00111.06           C  
ANISOU  589  CB  ASN A 136    14564  15818  11816   1118   1579   2667       C  
ATOM    590  CG  ASN A 136     -55.369  -6.778 126.369  1.00138.78           C  
ANISOU  590  CG  ASN A 136    18148  19752  14830   1282   1797   2294       C  
ATOM    591  OD1 ASN A 136     -54.796  -6.074 127.215  1.00136.65           O  
ANISOU  591  OD1 ASN A 136    18128  19797  13994   1398   1688   2084       O  
ATOM    592  ND2 ASN A 136     -56.618  -6.525 126.000  1.00129.52           N  
ANISOU  592  ND2 ASN A 136    16746  18607  13860   1296   2117   2186       N  
ATOM    593  N   ASP A 137     -51.142  -9.005 124.867  1.00106.96           N  
ANISOU  593  N   ASP A 137    14220  14676  11745   1158    616   2939       N  
ATOM    594  CA  ASP A 137     -50.214 -10.073 124.458  1.00107.13           C  
ANISOU  594  CA  ASP A 137    14202  14347  12157   1180    449   3311       C  
ATOM    595  C   ASP A 137     -50.632 -10.730 123.116  1.00108.05           C  
ANISOU  595  C   ASP A 137    14205  13856  12994   1041    581   3261       C  
ATOM    596  O   ASP A 137     -50.458 -11.938 122.927  1.00109.68           O  
ANISOU  596  O   ASP A 137    14408  13704  13561   1015    665   3666       O  
ATOM    597  CB  ASP A 137     -50.041 -11.129 125.574  1.00115.06           C  
ANISOU  597  CB  ASP A 137    15267  15554  12896   1265    527   4007       C  
ATOM    598  CG  ASP A 137     -49.005 -10.791 126.639  1.00130.90           C  
ANISOU  598  CG  ASP A 137    17351  18104  14280   1434    212   4142       C  
ATOM    599  OD1 ASP A 137     -48.539  -9.624 126.674  1.00129.72           O  
ANISOU  599  OD1 ASP A 137    17230  18223  13835   1428    -36   3624       O  
ATOM    600  OD2 ASP A 137     -48.669 -11.689 127.445  1.00143.04           O  
ANISOU  600  OD2 ASP A 137    18923  19807  15619   1559    212   4775       O  
ATOM    601  N   ARG A 138     -51.157  -9.913 122.180  1.00100.22           N  
ANISOU  601  N   ARG A 138    13142  12747  12191    961    597   2753       N  
ATOM    602  CA  ARG A 138     -51.584 -10.359 120.856  1.00 97.10           C  
ANISOU  602  CA  ARG A 138    12636  11888  12371    807    673   2610       C  
ATOM    603  C   ARG A 138     -51.232  -9.309 119.809  1.00 97.39           C  
ANISOU  603  C   ARG A 138    12653  11826  12525    845    480   2088       C  
ATOM    604  O   ARG A 138     -51.662  -8.161 119.927  1.00 96.02           O  
ANISOU  604  O   ARG A 138    12486  11903  12096    904    488   1774       O  
ATOM    605  CB  ARG A 138     -53.095 -10.665 120.832  1.00 97.34           C  
ANISOU  605  CB  ARG A 138    12523  11962  12499    616    995   2670       C  
ATOM    606  CG  ARG A 138     -53.599 -11.116 119.459  1.00 99.47           C  
ANISOU  606  CG  ARG A 138    12656  11834  13305    399   1031   2475       C  
ATOM    607  CD  ARG A 138     -55.128 -11.177 119.337  1.00103.63           C  
ANISOU  607  CD  ARG A 138    12942  12523  13911    184   1286   2448       C  
ATOM    608  NE  ARG A 138     -55.668 -10.202 118.370  1.00101.51           N  
ANISOU  608  NE  ARG A 138    12508  12366  13697    209   1196   2000       N  
ATOM    609  CZ  ARG A 138     -56.165 -10.503 117.173  1.00109.67           C  
ANISOU  609  CZ  ARG A 138    13374  13209  15087     -2   1158   1805       C  
ATOM    610  NH1 ARG A 138     -56.294 -11.769 116.800  1.00 97.52           N  
ANISOU  610  NH1 ARG A 138    11819  11321  13913   -311   1237   1954       N  
ATOM    611  NH2 ARG A 138     -56.569  -9.540 116.355  1.00 90.21           N  
ANISOU  611  NH2 ARG A 138    10769  10906  12601     91   1049   1464       N  
ATOM    612  N   VAL A 139     -50.478  -9.713 118.776  1.00 92.52           N  
ANISOU  612  N   VAL A 139    12030  10823  12302    828    349   2013       N  
ATOM    613  CA  VAL A 139     -50.089  -8.832 117.680  1.00 88.91           C  
ANISOU  613  CA  VAL A 139    11558  10245  11977    851    197   1586       C  
ATOM    614  C   VAL A 139     -50.981  -9.127 116.451  1.00 92.44           C  
ANISOU  614  C   VAL A 139    11904  10447  12771    690    313   1409       C  
ATOM    615  O   VAL A 139     -51.212 -10.290 116.115  1.00 92.65           O  
ANISOU  615  O   VAL A 139    11908  10194  13100    544    424   1575       O  
ATOM    616  CB  VAL A 139     -48.565  -8.912 117.375  1.00 92.21           C  
ANISOU  616  CB  VAL A 139    12009  10509  12518    956    -24   1591       C  
ATOM    617  CG1 VAL A 139     -48.129 -10.297 116.887  1.00 93.35           C  
ANISOU  617  CG1 VAL A 139    12144  10252  13074    952     43   1850       C  
ATOM    618  CG2 VAL A 139     -48.120  -7.815 116.411  1.00 88.67           C  
ANISOU  618  CG2 VAL A 139    11559  10005  12127    967   -154   1178       C  
ATOM    619  N   GLU A 140     -51.521  -8.067 115.826  1.00 89.05           N  
ANISOU  619  N   GLU A 140    11421  10136  12278    713    290   1079       N  
ATOM    620  CA  GLU A 140     -52.392  -8.175 114.655  1.00 89.10           C  
ANISOU  620  CA  GLU A 140    11290  10046  12516    580    339    901       C  
ATOM    621  C   GLU A 140     -51.566  -8.436 113.382  1.00 92.22           C  
ANISOU  621  C   GLU A 140    11744  10118  13175    546    216    729       C  
ATOM    622  O   GLU A 140     -50.681  -7.645 113.029  1.00 89.53           O  
ANISOU  622  O   GLU A 140    11489   9750  12778    682     87    575       O  
ATOM    623  CB  GLU A 140     -53.257  -6.913 114.492  1.00 90.12           C  
ANISOU  623  CB  GLU A 140    11327  10458  12459    699    363    687       C  
ATOM    624  CG  GLU A 140     -54.478  -6.878 115.397  1.00107.25           C  
ANISOU  624  CG  GLU A 140    13343  12951  14455    698    570    825       C  
ATOM    625  CD  GLU A 140     -55.457  -5.739 115.170  1.00136.52           C  
ANISOU  625  CD  GLU A 140    16905  16924  18042    874    643    648       C  
ATOM    626  OE1 GLU A 140     -55.512  -5.203 114.038  1.00124.59           O  
ANISOU  626  OE1 GLU A 140    15347  15344  16648    933    527    461       O  
ATOM    627  OE2 GLU A 140     -56.205  -5.410 116.122  1.00138.99           O  
ANISOU  627  OE2 GLU A 140    17143  17531  18136    979    841    725       O  
ATOM    628  N   LEU A 141     -51.861  -9.561 112.706  1.00 90.68           N  
ANISOU  628  N   LEU A 141    11514   9673  13268    339    285    741       N  
ATOM    629  CA  LEU A 141     -51.199  -9.982 111.469  1.00 89.55           C  
ANISOU  629  CA  LEU A 141    11447   9220  13358    290    230    547       C  
ATOM    630  C   LEU A 141     -51.752  -9.218 110.254  1.00 93.16           C  
ANISOU  630  C   LEU A 141    11819   9832  13746    255    144    236       C  
ATOM    631  O   LEU A 141     -52.964  -8.961 110.202  1.00 94.29           O  
ANISOU  631  O   LEU A 141    11783  10238  13805    160    160    201       O  
ATOM    632  CB  LEU A 141     -51.385 -11.495 111.240  1.00 92.30           C  
ANISOU  632  CB  LEU A 141    11840   9200  14029     56    372    624       C  
ATOM    633  CG  LEU A 141     -50.623 -12.450 112.145  1.00 98.99           C  
ANISOU  633  CG  LEU A 141    12816   9764  15032    143    475    978       C  
ATOM    634  CD1 LEU A 141     -51.342 -13.779 112.236  1.00103.25           C  
ANISOU  634  CD1 LEU A 141    13387   9981  15861   -143    682   1117       C  
ATOM    635  CD2 LEU A 141     -49.215 -12.675 111.642  1.00100.81           C  
ANISOU  635  CD2 LEU A 141    13168   9712  15423    349    432    937       C  
ATOM    636  N   PRO A 142     -50.906  -8.879 109.247  1.00 87.87           N  
ANISOU  636  N   PRO A 142    11245   9041  13101    341     64     45       N  
ATOM    637  CA  PRO A 142     -51.435  -8.203 108.049  1.00 86.76           C  
ANISOU  637  CA  PRO A 142    11040   9076  12849    324    -18   -188       C  
ATOM    638  C   PRO A 142     -52.157  -9.196 107.130  1.00 91.84           C  
ANISOU  638  C   PRO A 142    11621   9664  13611     34     -5   -363       C  
ATOM    639  O   PRO A 142     -51.786 -10.372 107.096  1.00 92.71           O  
ANISOU  639  O   PRO A 142    11841   9434  13951   -120     93   -382       O  
ATOM    640  CB  PRO A 142     -50.177  -7.628 107.380  1.00 86.66           C  
ANISOU  640  CB  PRO A 142    11170   8939  12818    489    -60   -284       C  
ATOM    641  CG  PRO A 142     -49.013  -7.965 108.292  1.00 90.64           C  
ANISOU  641  CG  PRO A 142    11754   9248  13435    588    -27   -113       C  
ATOM    642  CD  PRO A 142     -49.452  -9.110 109.124  1.00 88.39           C  
ANISOU  642  CD  PRO A 142    11448   8850  13286    470     59     67       C  
ATOM    643  N   SER A 143     -53.186  -8.735 106.393  1.00 88.92           N  
ANISOU  643  N   SER A 143    11074   9624  13086    -42   -104   -493       N  
ATOM    644  CA  SER A 143     -53.944  -9.608 105.491  1.00 91.82           C  
ANISOU  644  CA  SER A 143    11346  10034  13509   -383   -145   -713       C  
ATOM    645  C   SER A 143     -53.160  -9.932 104.207  1.00 96.05           C  
ANISOU  645  C   SER A 143    12088  10383  14023   -427   -170   -995       C  
ATOM    646  O   SER A 143     -52.199  -9.234 103.868  1.00 93.17           O  
ANISOU  646  O   SER A 143    11868   9971  13560   -164   -171   -986       O  
ATOM    647  CB  SER A 143     -55.303  -9.000 105.149  1.00 97.13           C  
ANISOU  647  CB  SER A 143    11688  11228  13989   -433   -282   -727       C  
ATOM    648  OG  SER A 143     -55.189  -7.829 104.360  1.00106.09           O  
ANISOU  648  OG  SER A 143    12820  12621  14868   -156   -411   -754       O  
ATOM    649  N   ARG A 144     -53.563 -11.014 103.516  1.00 96.55           N  
ANISOU  649  N   ARG A 144    12174  10331  14179   -788   -161  -1262       N  
ATOM    650  CA  ARG A 144     -52.947 -11.467 102.268  1.00 98.34           C  
ANISOU  650  CA  ARG A 144    12621  10395  14350   -871   -146  -1604       C  
ATOM    651  C   ARG A 144     -53.113 -10.400 101.164  1.00101.96           C  
ANISOU  651  C   ARG A 144    13007  11329  14403   -728   -332  -1702       C  
ATOM    652  O   ARG A 144     -52.145 -10.104 100.456  1.00100.59           O  
ANISOU  652  O   ARG A 144    13037  11070  14114   -541   -276  -1787       O  
ATOM    653  CB  ARG A 144     -53.552 -12.817 101.827  1.00104.44           C  
ANISOU  653  CB  ARG A 144    13437  10961  15285  -1354   -102  -1928       C  
ATOM    654  CG  ARG A 144     -52.866 -13.446 100.605  1.00119.11           C  
ANISOU  654  CG  ARG A 144    15594  12572  17091  -1450    -22  -2353       C  
ATOM    655  CD  ARG A 144     -53.749 -14.425  99.845  1.00135.87           C  
ANISOU  655  CD  ARG A 144    17722  14699  19203  -1995    -78  -2799       C  
ATOM    656  NE  ARG A 144     -55.024 -13.835  99.418  1.00150.21           N  
ANISOU  656  NE  ARG A 144    19167  17219  20688  -2208   -393  -2848       N  
ATOM    657  CZ  ARG A 144     -55.223 -13.197  98.265  1.00168.27           C  
ANISOU  657  CZ  ARG A 144    21390  20033  22512  -2173   -616  -3041       C  
ATOM    658  NH1 ARG A 144     -56.418 -12.698  97.975  1.00157.71           N  
ANISOU  658  NH1 ARG A 144    19656  19365  20902  -2326   -915  -3012       N  
ATOM    659  NH2 ARG A 144     -54.229 -13.052  97.396  1.00155.86           N  
ANISOU  659  NH2 ARG A 144    20125  18360  20734  -1962   -531  -3226       N  
ATOM    660  N   THR A 145     -54.329  -9.807 101.058  1.00 99.41           N  
ANISOU  660  N   THR A 145    12374  11522  13874   -783   -531  -1634       N  
ATOM    661  CA  THR A 145     -54.701  -8.776 100.075  1.00 99.66           C  
ANISOU  661  CA  THR A 145    12289  12067  13512   -613   -729  -1629       C  
ATOM    662  C   THR A 145     -53.799  -7.533 100.173  1.00 98.90           C  
ANISOU  662  C   THR A 145    12342  11911  13327   -156   -661  -1377       C  
ATOM    663  O   THR A 145     -53.583  -6.864  99.161  1.00 99.30           O  
ANISOU  663  O   THR A 145    12460  12187  13083     -4   -732  -1388       O  
ATOM    664  CB  THR A 145     -56.182  -8.378 100.222  1.00112.81           C  
ANISOU  664  CB  THR A 145    13524  14283  15057   -677   -927  -1502       C  
ATOM    665  OG1 THR A 145     -56.451  -8.005 101.574  1.00113.33           O  
ANISOU  665  OG1 THR A 145    13454  14273  15333   -506   -815  -1199       O  
ATOM    666  CG2 THR A 145     -57.140  -9.483  99.782  1.00115.92           C  
ANISOU  666  CG2 THR A 145    13711  14872  15460  -1210  -1056  -1803       C  
ATOM    667  N   LEU A 146     -53.274  -7.235 101.379  1.00 91.21           N  
ANISOU  667  N   LEU A 146    11424  10644  12587     29   -524  -1151       N  
ATOM    668  CA  LEU A 146     -52.366  -6.115 101.638  1.00 87.58           C  
ANISOU  668  CA  LEU A 146    11109  10064  12103    372   -449   -954       C  
ATOM    669  C   LEU A 146     -50.973  -6.427 101.085  1.00 91.00           C  
ANISOU  669  C   LEU A 146    11799  10188  12589    390   -319  -1074       C  
ATOM    670  O   LEU A 146     -50.309  -5.534 100.551  1.00 89.20           O  
ANISOU  670  O   LEU A 146    11676   9986  12229    585   -284   -996       O  
ATOM    671  CB  LEU A 146     -52.299  -5.835 103.153  1.00 85.18           C  
ANISOU  671  CB  LEU A 146    10771   9602  11990    488   -369   -746       C  
ATOM    672  CG  LEU A 146     -51.538  -4.589 103.607  1.00 86.89           C  
ANISOU  672  CG  LEU A 146    11115   9714  12185    776   -313   -584       C  
ATOM    673  CD1 LEU A 146     -52.399  -3.344 103.504  1.00 87.69           C  
ANISOU  673  CD1 LEU A 146    11117  10087  12113   1011   -366   -447       C  
ATOM    674  CD2 LEU A 146     -51.065  -4.747 105.019  1.00 86.75           C  
ANISOU  674  CD2 LEU A 146    11138   9489  12336    791   -236   -485       C  
ATOM    675  N   CYS A 147     -50.547  -7.697 101.217  1.00 89.46           N  
ANISOU  675  N   CYS A 147    11694   9683  12612    199   -214  -1240       N  
ATOM    676  CA  CYS A 147     -49.259  -8.213 100.760  1.00 90.15           C  
ANISOU  676  CA  CYS A 147    11985   9458  12808    242    -42  -1363       C  
ATOM    677  C   CYS A 147     -49.238  -8.345  99.232  1.00 95.23           C  
ANISOU  677  C   CYS A 147    12741  10271  13170    164    -36  -1641       C  
ATOM    678  O   CYS A 147     -48.302  -7.862  98.595  1.00 93.94           O  
ANISOU  678  O   CYS A 147    12691  10102  12899    331     75  -1629       O  
ATOM    679  CB  CYS A 147     -48.958  -9.548 101.439  1.00 92.36           C  
ANISOU  679  CB  CYS A 147    12330   9326  13436    117     93  -1414       C  
ATOM    680  SG  CYS A 147     -47.370 -10.295 100.970  1.00 97.99           S  
ANISOU  680  SG  CYS A 147    13249   9627  14356    256    356  -1536       S  
ATOM    681  N   GLN A 148     -50.251  -9.029  98.660  1.00 94.52           N  
ANISOU  681  N   GLN A 148    12610  10356  12946   -120   -149  -1900       N  
ATOM    682  CA  GLN A 148     -50.395  -9.314  97.229  1.00 97.79           C  
ANISOU  682  CA  GLN A 148    13137  11001  13017   -268   -183  -2237       C  
ATOM    683  C   GLN A 148     -50.465  -8.038  96.369  1.00100.38           C  
ANISOU  683  C   GLN A 148    13430  11799  12911    -52   -300  -2075       C  
ATOM    684  O   GLN A 148     -50.015  -8.064  95.222  1.00102.31           O  
ANISOU  684  O   GLN A 148    13843  12178  12851    -43   -231  -2260       O  
ATOM    685  CB  GLN A 148     -51.646 -10.179  96.997  1.00103.31           C  
ANISOU  685  CB  GLN A 148    13723  11871  13659   -681   -352  -2526       C  
ATOM    686  CG  GLN A 148     -51.650 -10.986  95.690  1.00129.95           C  
ANISOU  686  CG  GLN A 148    17297  15315  16762   -956   -338  -3032       C  
ATOM    687  CD  GLN A 148     -50.655 -12.131  95.615  1.00155.85           C  
ANISOU  687  CD  GLN A 148    20906  17975  20335  -1012    -10  -3334       C  
ATOM    688  OE1 GLN A 148     -49.768 -12.150  94.750  1.00153.74           O  
ANISOU  688  OE1 GLN A 148    20873  17661  19881   -868    173  -3522       O  
ATOM    689  NE2 GLN A 148     -50.795 -13.120  96.492  1.00149.92           N  
ANISOU  689  NE2 GLN A 148    20182  16736  20045  -1198    104  -3368       N  
ATOM    690  N   ALA A 149     -50.994  -6.937  96.928  1.00 94.20           N  
ANISOU  690  N   ALA A 149    12458  11234  12102    145   -435  -1718       N  
ATOM    691  CA  ALA A 149     -51.136  -5.647  96.251  1.00 94.34           C  
ANISOU  691  CA  ALA A 149    12450  11621  11773    401   -522  -1469       C  
ATOM    692  C   ALA A 149     -49.786  -5.003  95.897  1.00 96.09           C  
ANISOU  692  C   ALA A 149    12894  11633  11984    621   -292  -1336       C  
ATOM    693  O   ALA A 149     -49.748  -4.169  94.993  1.00 97.66           O  
ANISOU  693  O   ALA A 149    13154  12110  11843    778   -305  -1180       O  
ATOM    694  CB  ALA A 149     -51.946  -4.695  97.115  1.00 93.66           C  
ANISOU  694  CB  ALA A 149    12144  11670  11773    595   -642  -1132       C  
ATOM    695  N   THR A 150     -48.691  -5.384  96.590  1.00 89.50           N  
ANISOU  695  N   THR A 150    12151  10343  11510    632    -82  -1361       N  
ATOM    696  CA  THR A 150     -47.351  -4.833  96.348  1.00 87.99           C  
ANISOU  696  CA  THR A 150    12091   9972  11371    794    148  -1235       C  
ATOM    697  C   THR A 150     -46.577  -5.603  95.275  1.00 93.31           C  
ANISOU  697  C   THR A 150    12928  10626  11899    734    353  -1512       C  
ATOM    698  O   THR A 150     -45.853  -4.974  94.513  1.00 94.42           O  
ANISOU  698  O   THR A 150    13161  10863  11852    855    516  -1402       O  
ATOM    699  CB  THR A 150     -46.510  -4.772  97.630  1.00 93.72           C  
ANISOU  699  CB  THR A 150    12763  10317  12530    853    246  -1097       C  
ATOM    700  OG1 THR A 150     -46.304  -6.091  98.141  1.00 95.02           O  
ANISOU  700  OG1 THR A 150    12918  10223  12961    734    302  -1297       O  
ATOM    701  CG2 THR A 150     -47.118  -3.878  98.691  1.00 89.11           C  
ANISOU  701  CG2 THR A 150    12073   9739  12044    934    102   -857       C  
ATOM    702  N   ARG A 151     -46.726  -6.946  95.210  1.00 90.10           N  
ANISOU  702  N   ARG A 151    12576  10072  11585    547    386  -1871       N  
ATOM    703  CA  ARG A 151     -46.031  -7.851  94.274  1.00 92.64           C  
ANISOU  703  CA  ARG A 151    13094  10297  11807    497    630  -2223       C  
ATOM    704  C   ARG A 151     -45.883  -7.275  92.851  1.00 98.64           C  
ANISOU  704  C   ARG A 151    13985  11469  12023    557    697  -2263       C  
ATOM    705  O   ARG A 151     -44.798  -7.357  92.264  1.00 98.95           O  
ANISOU  705  O   ARG A 151    14145  11431  12022    674   1007  -2323       O  
ATOM    706  CB  ARG A 151     -46.742  -9.219  94.193  1.00 95.03           C  
ANISOU  706  CB  ARG A 151    13479  10465  12161    212    578  -2654       C  
ATOM    707  CG  ARG A 151     -46.995  -9.938  95.526  1.00 99.95           C  
ANISOU  707  CG  ARG A 151    14005  10681  13292    123    542  -2596       C  
ATOM    708  CD  ARG A 151     -45.733 -10.293  96.292  1.00 99.64           C  
ANISOU  708  CD  ARG A 151    13978  10175  13705    342    803  -2446       C  
ATOM    709  NE  ARG A 151     -45.400  -9.250  97.260  1.00 97.17           N  
ANISOU  709  NE  ARG A 151    13471   9915  13535    530    711  -2006       N  
ATOM    710  CZ  ARG A 151     -44.479  -9.372  98.207  1.00111.86           C  
ANISOU  710  CZ  ARG A 151    15244  11492  15763    695    819  -1791       C  
ATOM    711  NH1 ARG A 151     -43.789 -10.498  98.332  1.00 99.36           N  
ANISOU  711  NH1 ARG A 151    13734   9534  14484    763   1042  -1906       N  
ATOM    712  NH2 ARG A 151     -44.244  -8.369  99.042  1.00101.36           N  
ANISOU  712  NH2 ARG A 151    13757  10259  14496    801    704  -1462       N  
ATOM    713  N   GLY A 152     -46.967  -6.689  92.340  1.00 96.35           N  
ANISOU  713  N   GLY A 152    13645  11646  11317    502    418  -2185       N  
ATOM    714  CA  GLY A 152     -47.039  -6.084  91.015  1.00 99.39           C  
ANISOU  714  CA  GLY A 152    14142  12519  11102    571    415  -2142       C  
ATOM    715  C   GLY A 152     -46.209  -4.826  90.844  1.00101.06           C  
ANISOU  715  C   GLY A 152    14379  12745  11276    840    604  -1687       C  
ATOM    716  O   GLY A 152     -45.186  -4.874  90.158  1.00102.70           O  
ANISOU  716  O   GLY A 152    14730  12928  11362    909    922  -1736       O  
ATOM    717  N   PRO A 153     -46.610  -3.673  91.442  1.00 94.52           N  
ANISOU  717  N   PRO A 153    13420  11931  10562    990    454  -1244       N  
ATOM    718  CA  PRO A 153     -45.825  -2.436  91.250  1.00 94.07           C  
ANISOU  718  CA  PRO A 153    13426  11815  10502   1194    661   -815       C  
ATOM    719  C   PRO A 153     -44.445  -2.450  91.918  1.00 95.19           C  
ANISOU  719  C   PRO A 153    13545  11497  11127   1199    962   -781       C  
ATOM    720  O   PRO A 153     -43.543  -1.769  91.428  1.00 96.30           O  
ANISOU  720  O   PRO A 153    13750  11623  11216   1276   1227   -555       O  
ATOM    721  CB  PRO A 153     -46.714  -1.346  91.851  1.00 94.28           C  
ANISOU  721  CB  PRO A 153    13344  11878  10601   1341    431   -434       C  
ATOM    722  CG  PRO A 153     -47.604  -2.042  92.777  1.00 96.39           C  
ANISOU  722  CG  PRO A 153    13436  12088  11100   1220    180   -648       C  
ATOM    723  CD  PRO A 153     -47.818  -3.422  92.252  1.00 94.06           C  
ANISOU  723  CD  PRO A 153    13165  11943  10629    982    129  -1122       C  
ATOM    724  N   CYS A 154     -44.273  -3.226  93.009  1.00 88.50           N  
ANISOU  724  N   CYS A 154    12580  10313  10733   1112    923   -973       N  
ATOM    725  CA  CYS A 154     -42.995  -3.355  93.719  1.00 86.74           C  
ANISOU  725  CA  CYS A 154    12265   9730  10962   1126   1148   -937       C  
ATOM    726  C   CYS A 154     -42.193  -4.553  93.165  1.00 93.92           C  
ANISOU  726  C   CYS A 154    13224  10569  11892   1117   1415  -1266       C  
ATOM    727  O   CYS A 154     -41.573  -5.297  93.926  1.00 92.13           O  
ANISOU  727  O   CYS A 154    12888  10042  12075   1130   1499  -1363       O  
ATOM    728  CB  CYS A 154     -43.208  -3.462  95.230  1.00 83.26           C  
ANISOU  728  CB  CYS A 154    11671   9012  10953   1090    961   -891       C  
ATOM    729  SG  CYS A 154     -43.983  -2.006  95.985  1.00 84.88           S  
ANISOU  729  SG  CYS A 154    11845   9222  11183   1147    743   -551       S  
ATOM    730  N   ALA A 155     -42.190  -4.703  91.821  1.00 95.10           N  
ANISOU  730  N   ALA A 155    13548  11010  11575   1127   1570  -1418       N  
ATOM    731  CA  ALA A 155     -41.471  -5.742  91.083  1.00 98.46           C  
ANISOU  731  CA  ALA A 155    14084  11402  11925   1150   1889  -1775       C  
ATOM    732  C   ALA A 155     -39.970  -5.478  91.121  1.00103.51           C  
ANISOU  732  C   ALA A 155    14586  11901  12841   1289   2270  -1590       C  
ATOM    733  O   ALA A 155     -39.183  -6.413  90.968  1.00105.08           O  
ANISOU  733  O   ALA A 155    14776  11937  13213   1379   2564  -1836       O  
ATOM    734  CB  ALA A 155     -41.960  -5.794  89.646  1.00103.74           C  
ANISOU  734  CB  ALA A 155    14990  12511  11914   1109   1925  -1976       C  
ATOM    735  N   ILE A 156     -39.584  -4.199  91.344  1.00 99.49           N  
ANISOU  735  N   ILE A 156    13955  11441  12407   1303   2278  -1156       N  
ATOM    736  CA  ILE A 156     -38.203  -3.712  91.471  1.00100.56           C  
ANISOU  736  CA  ILE A 156    13883  11490  12836   1354   2593   -914       C  
ATOM    737  C   ILE A 156     -37.479  -4.424  92.637  1.00102.54           C  
ANISOU  737  C   ILE A 156    13862  11425  13674   1397   2592   -976       C  
ATOM    738  O   ILE A 156     -36.274  -4.655  92.543  1.00104.31           O  
ANISOU  738  O   ILE A 156    13881  11626  14128   1492   2910   -941       O  
ATOM    739  CB  ILE A 156     -38.153  -2.162  91.648  1.00103.16           C  
ANISOU  739  CB  ILE A 156    14169  11847  13179   1274   2534   -461       C  
ATOM    740  CG1 ILE A 156     -39.184  -1.656  92.697  1.00100.40           C  
ANISOU  740  CG1 ILE A 156    13829  11343  12975   1210   2109   -359       C  
ATOM    741  CG2 ILE A 156     -38.318  -1.439  90.316  1.00107.63           C  
ANISOU  741  CG2 ILE A 156    14955  12735  13206   1303   2716   -272       C  
ATOM    742  CD1 ILE A 156     -38.947  -0.225  93.256  1.00111.28           C  
ANISOU  742  CD1 ILE A 156    15154  12566  14563   1124   2077     18       C  
ATOM    743  N   VAL A 157     -38.225  -4.782  93.714  1.00 95.58           N  
ANISOU  743  N   VAL A 157    12959  10346  13012   1348   2244  -1035       N  
ATOM    744  CA  VAL A 157     -37.733  -5.455  94.927  1.00 93.60           C  
ANISOU  744  CA  VAL A 157    12478   9830  13257   1404   2172  -1032       C  
ATOM    745  C   VAL A 157     -37.259  -6.884  94.608  1.00101.24           C  
ANISOU  745  C   VAL A 157    13468  10638  14361   1576   2436  -1320       C  
ATOM    746  O   VAL A 157     -36.141  -7.233  94.983  1.00102.32           O  
ANISOU  746  O   VAL A 157    13343  10680  14855   1734   2630  -1224       O  
ATOM    747  CB  VAL A 157     -38.785  -5.462  96.074  1.00 93.14           C  
ANISOU  747  CB  VAL A 157    12443   9643  13305   1307   1768  -1002       C  
ATOM    748  CG1 VAL A 157     -38.181  -5.959  97.388  1.00 91.61           C  
ANISOU  748  CG1 VAL A 157    12000   9246  13563   1370   1684   -897       C  
ATOM    749  CG2 VAL A 157     -39.403  -4.085  96.266  1.00 90.74           C  
ANISOU  749  CG2 VAL A 157    12184   9459  12835   1190   1557   -776       C  
ATOM    750  N   GLU A 158     -38.094  -7.702  93.928  1.00100.03           N  
ANISOU  750  N   GLU A 158    13615  10452  13939   1546   2448  -1677       N  
ATOM    751  CA  GLU A 158     -37.754  -9.089  93.589  1.00103.93           C  
ANISOU  751  CA  GLU A 158    14223  10697  14569   1693   2731  -2021       C  
ATOM    752  C   GLU A 158     -36.696  -9.179  92.473  1.00113.65           C  
ANISOU  752  C   GLU A 158    15459  12067  15657   1874   3215  -2132       C  
ATOM    753  O   GLU A 158     -36.059 -10.228  92.331  1.00116.50           O  
ANISOU  753  O   GLU A 158    15834  12179  16251   2092   3541  -2348       O  
ATOM    754  CB  GLU A 158     -39.002  -9.889  93.196  1.00106.44           C  
ANISOU  754  CB  GLU A 158    14876  10930  14636   1515   2589  -2427       C  
ATOM    755  CG  GLU A 158     -38.930 -11.336  93.652  1.00121.26           C  
ANISOU  755  CG  GLU A 158    16845  12320  16909   1600   2722  -2676       C  
ATOM    756  CD  GLU A 158     -39.967 -12.254  93.039  1.00153.88           C  
ANISOU  756  CD  GLU A 158    21334  16325  20807   1371   2689  -3181       C  
ATOM    757  OE1 GLU A 158     -41.168 -12.091  93.353  1.00155.28           O  
ANISOU  757  OE1 GLU A 158    21547  16604  20849   1094   2316  -3191       O  
ATOM    758  OE2 GLU A 158     -39.575 -13.156  92.264  1.00154.78           O  
ANISOU  758  OE2 GLU A 158    21683  16237  20890   1459   3049  -3588       O  
ATOM    759  N   ARG A 159     -36.521  -8.101  91.676  1.00111.70           N  
ANISOU  759  N   ARG A 159    15213  12198  15031   1808   3300  -1968       N  
ATOM    760  CA  ARG A 159     -35.524  -8.065  90.600  1.00116.50           C  
ANISOU  760  CA  ARG A 159    15806  13008  15450   1963   3794  -2018       C  
ATOM    761  C   ARG A 159     -34.124  -7.749  91.122  1.00121.23           C  
ANISOU  761  C   ARG A 159    15952  13591  16518   2121   4031  -1680       C  
ATOM    762  O   ARG A 159     -33.150  -8.279  90.580  1.00125.73           O  
ANISOU  762  O   ARG A 159    16415  14183  17173   2355   4496  -1784       O  
ATOM    763  CB  ARG A 159     -35.893  -7.047  89.496  1.00118.82           C  
ANISOU  763  CB  ARG A 159    16291  13738  15118   1828   3824  -1915       C  
ATOM    764  CG  ARG A 159     -37.158  -7.350  88.681  1.00134.35           C  
ANISOU  764  CG  ARG A 159    18663  15895  16489   1690   3630  -2262       C  
ATOM    765  CD  ARG A 159     -37.119  -8.655  87.890  1.00153.67           C  
ANISOU  765  CD  ARG A 159    21387  18270  18729   1766   3923  -2848       C  
ATOM    766  NE  ARG A 159     -38.406  -8.941  87.251  1.00168.97           N  
ANISOU  766  NE  ARG A 159    23664  20422  20114   1545   3640  -3208       N  
ATOM    767  CZ  ARG A 159     -39.441  -9.526  87.851  1.00184.44           C  
ANISOU  767  CZ  ARG A 159    25695  22168  22213   1356   3259  -3427       C  
ATOM    768  NH1 ARG A 159     -39.362  -9.885  89.128  1.00167.95           N  
ANISOU  768  NH1 ARG A 159    23409  19628  20777   1388   3129  -3294       N  
ATOM    769  NH2 ARG A 159     -40.565  -9.744  87.184  1.00175.85           N  
ANISOU  769  NH2 ARG A 159    24853  21366  20595   1119   3001  -3755       N  
ATOM    770  N   GLU A 160     -34.010  -6.897  92.155  1.00113.97           N  
ANISOU  770  N   GLU A 160    14750  12661  15893   1990   3727  -1300       N  
ATOM    771  CA  GLU A 160     -32.706  -6.482  92.659  1.00115.07           C  
ANISOU  771  CA  GLU A 160    14407  12869  16445   2052   3886   -981       C  
ATOM    772  C   GLU A 160     -32.226  -7.278  93.906  1.00119.45           C  
ANISOU  772  C   GLU A 160    14643  13188  17555   2227   3747   -917       C  
ATOM    773  O   GLU A 160     -31.196  -7.946  93.802  1.00123.00           O  
ANISOU  773  O   GLU A 160    14819  13633  18285   2508   4087   -915       O  
ATOM    774  CB  GLU A 160     -32.668  -4.962  92.919  1.00114.23           C  
ANISOU  774  CB  GLU A 160    14174  12927  16302   1761   3700   -617       C  
ATOM    775  CG  GLU A 160     -32.720  -4.101  91.658  1.00127.14           C  
ANISOU  775  CG  GLU A 160    16016  14820  17472   1655   3962   -522       C  
ATOM    776  CD  GLU A 160     -31.685  -4.335  90.565  1.00159.66           C  
ANISOU  776  CD  GLU A 160    20021  19170  21471   1811   4544   -542       C  
ATOM    777  OE1 GLU A 160     -30.484  -4.488  90.888  1.00158.16           O  
ANISOU  777  OE1 GLU A 160    19376  19022  21697   1902   4784   -412       O  
ATOM    778  OE2 GLU A 160     -32.075  -4.329  89.374  1.00159.04           O  
ANISOU  778  OE2 GLU A 160    20288  19288  20854   1843   4763   -672       O  
ATOM    779  N   ARG A 161     -32.924  -7.207  95.064  1.00112.63           N  
ANISOU  779  N   ARG A 161    13792  12165  16836   2101   3281   -832       N  
ATOM    780  CA  ARG A 161     -32.443  -7.927  96.261  1.00113.01           C  
ANISOU  780  CA  ARG A 161    13537  12051  17351   2283   3141   -699       C  
ATOM    781  C   ARG A 161     -33.340  -9.130  96.628  1.00117.01           C  
ANISOU  781  C   ARG A 161    14353  12193  17913   2400   3022   -920       C  
ATOM    782  O   ARG A 161     -32.967  -9.932  97.490  1.00117.28           O  
ANISOU  782  O   ARG A 161    14202  12040  18318   2621   2980   -797       O  
ATOM    783  CB  ARG A 161     -32.290  -6.982  97.471  1.00110.88           C  
ANISOU  783  CB  ARG A 161    12970  11915  17244   2060   2742   -388       C  
ATOM    784  CG  ARG A 161     -31.050  -7.271  98.322  1.00126.30           C  
ANISOU  784  CG  ARG A 161    14369  13988  19631   2237   2737   -130       C  
ATOM    785  CD  ARG A 161     -31.050  -6.516  99.643  1.00136.21           C  
ANISOU  785  CD  ARG A 161    15397  15377  20982   1992   2275     92       C  
ATOM    786  NE  ARG A 161     -30.847  -7.406 100.796  1.00146.86           N  
ANISOU  786  NE  ARG A 161    16530  16674  22596   2225   2060    247       N  
ATOM    787  CZ  ARG A 161     -30.192  -7.079 101.910  1.00160.87           C  
ANISOU  787  CZ  ARG A 161    17876  18707  24540   2156   1762    498       C  
ATOM    788  NH1 ARG A 161     -29.642  -5.875 102.036  1.00148.59           N  
ANISOU  788  NH1 ARG A 161    16053  17442  22964   1810   1650    571       N  
ATOM    789  NH2 ARG A 161     -30.069  -7.955 102.898  1.00146.53           N  
ANISOU  789  NH2 ARG A 161    15900  16867  22905   2415   1576    684       N  
ATOM    790  N   GLY A 162     -34.498  -9.254  95.982  1.00113.63           N  
ANISOU  790  N   GLY A 162    14370  11683  17123   2243   2969  -1215       N  
ATOM    791  CA  GLY A 162     -35.455 -10.313  96.281  1.00113.71           C  
ANISOU  791  CA  GLY A 162    14678  11351  17178   2244   2851  -1446       C  
ATOM    792  C   GLY A 162     -36.286 -10.009  97.516  1.00114.45           C  
ANISOU  792  C   GLY A 162    14744  11403  17340   2060   2393  -1249       C  
ATOM    793  O   GLY A 162     -35.825  -9.322  98.438  1.00112.15           O  
ANISOU  793  O   GLY A 162    14150  11258  17204   2041   2191   -927       O  
ATOM    794  N   TRP A 163     -37.526 -10.526  97.546  1.00110.33           N  
ANISOU  794  N   TRP A 163    14528  10706  16687   1899   2234  -1465       N  
ATOM    795  CA  TRP A 163     -38.425 -10.320  98.683  1.00106.55           C  
ANISOU  795  CA  TRP A 163    14035  10201  16247   1734   1853  -1296       C  
ATOM    796  C   TRP A 163     -37.969 -11.126  99.901  1.00110.56           C  
ANISOU  796  C   TRP A 163    14376  10453  17179   1923   1820  -1054       C  
ATOM    797  O   TRP A 163     -37.666 -12.314  99.752  1.00113.65           O  
ANISOU  797  O   TRP A 163    14861  10498  17825   2118   2070  -1158       O  
ATOM    798  CB  TRP A 163     -39.874 -10.688  98.327  1.00104.87           C  
ANISOU  798  CB  TRP A 163    14129   9923  15793   1489   1719  -1578       C  
ATOM    799  CG  TRP A 163     -40.608  -9.637  97.554  1.00104.24           C  
ANISOU  799  CG  TRP A 163    14140  10207  15258   1297   1575  -1656       C  
ATOM    800  CD1 TRP A 163     -41.026  -9.717  96.258  1.00109.53           C  
ANISOU  800  CD1 TRP A 163    15030  11028  15559   1203   1676  -1968       C  
ATOM    801  CD2 TRP A 163     -41.034  -8.354  98.036  1.00100.53           C  
ANISOU  801  CD2 TRP A 163    13560   9997  14641   1205   1307  -1403       C  
ATOM    802  NE1 TRP A 163     -41.680  -8.563  95.900  1.00107.37           N  
ANISOU  802  NE1 TRP A 163    14759  11119  14917   1089   1472  -1858       N  
ATOM    803  CE2 TRP A 163     -41.697  -7.707  96.972  1.00105.09           C  
ANISOU  803  CE2 TRP A 163    14282  10856  14790   1101   1268  -1517       C  
ATOM    804  CE3 TRP A 163     -40.919  -7.685  99.267  1.00 98.83           C  
ANISOU  804  CE3 TRP A 163    13157   9801  14594   1210   1107  -1104       C  
ATOM    805  CZ2 TRP A 163     -42.242  -6.426  97.099  1.00101.98           C  
ANISOU  805  CZ2 TRP A 163    13852  10699  14197   1049   1066  -1300       C  
ATOM    806  CZ3 TRP A 163     -41.458  -6.415  99.388  1.00 97.98           C  
ANISOU  806  CZ3 TRP A 163    13044   9907  14277   1119    922   -968       C  
ATOM    807  CH2 TRP A 163     -42.111  -5.800  98.314  1.00 99.14           C  
ANISOU  807  CH2 TRP A 163    13338  10268  14061   1062    917  -1046       C  
ATOM    808  N   PRO A 164     -37.918 -10.514 101.110  1.00104.07           N  
ANISOU  808  N   PRO A 164    13333   9788  16422   1885   1527   -729       N  
ATOM    809  CA  PRO A 164     -37.512 -11.279 102.301  1.00105.10           C  
ANISOU  809  CA  PRO A 164    13301   9751  16880   2080   1464   -443       C  
ATOM    810  C   PRO A 164     -38.558 -12.329 102.669  1.00109.18           C  
ANISOU  810  C   PRO A 164    14091   9910  17482   2015   1450   -510       C  
ATOM    811  O   PRO A 164     -39.737 -12.160 102.349  1.00106.75           O  
ANISOU  811  O   PRO A 164    14006   9613  16940   1739   1350   -729       O  
ATOM    812  CB  PRO A 164     -37.373 -10.207 103.389  1.00104.19           C  
ANISOU  812  CB  PRO A 164    12941   9977  16670   1969   1127   -166       C  
ATOM    813  CG  PRO A 164     -37.373  -8.897 102.664  1.00106.61           C  
ANISOU  813  CG  PRO A 164    13246  10549  16713   1770   1102   -294       C  
ATOM    814  CD  PRO A 164     -38.230  -9.118 101.466  1.00101.98           C  
ANISOU  814  CD  PRO A 164    12983   9846  15919   1675   1256   -613       C  
ATOM    815  N   ASP A 165     -38.112 -13.433 103.299  1.00108.95           N  
ANISOU  815  N   ASP A 165    14026   9563  17806   2274   1569   -299       N  
ATOM    816  CA  ASP A 165     -38.931 -14.584 103.709  1.00110.58           C  
ANISOU  816  CA  ASP A 165    14493   9327  18195   2230   1630   -296       C  
ATOM    817  C   ASP A 165     -40.226 -14.176 104.449  1.00109.55           C  
ANISOU  817  C   ASP A 165    14441   9348  17837   1894   1332   -237       C  
ATOM    818  O   ASP A 165     -41.279 -14.761 104.187  1.00109.72           O  
ANISOU  818  O   ASP A 165    14716   9120  17854   1652   1383   -452       O  
ATOM    819  CB  ASP A 165     -38.107 -15.550 104.586  1.00116.79           C  
ANISOU  819  CB  ASP A 165    15150   9837  19387   2623   1745    116       C  
ATOM    820  CG  ASP A 165     -37.484 -14.906 105.813  1.00128.54           C  
ANISOU  820  CG  ASP A 165    16259  11756  20823   2757   1440    590       C  
ATOM    821  OD1 ASP A 165     -36.452 -14.214 105.661  1.00128.56           O  
ANISOU  821  OD1 ASP A 165    15936  12112  20797   2892   1399    658       O  
ATOM    822  OD2 ASP A 165     -38.054 -15.062 106.919  1.00136.27           O  
ANISOU  822  OD2 ASP A 165    17264  12756  21758   2686   1242    874       O  
ATOM    823  N   PHE A 166     -40.143 -13.161 105.338  1.00101.51           N  
ANISOU  823  N   PHE A 166    13195   8749  16627   1861   1039     20       N  
ATOM    824  CA  PHE A 166     -41.268 -12.657 106.123  1.00 97.51           C  
ANISOU  824  CA  PHE A 166    12726   8437  15886   1610    792     93       C  
ATOM    825  C   PHE A 166     -42.140 -11.679 105.326  1.00 97.42           C  
ANISOU  825  C   PHE A 166    12797   8666  15551   1342    697   -225       C  
ATOM    826  O   PHE A 166     -43.247 -11.365 105.773  1.00 95.83           O  
ANISOU  826  O   PHE A 166    12637   8595  15177   1146    551   -221       O  
ATOM    827  CB  PHE A 166     -40.784 -12.011 107.437  1.00 97.76           C  
ANISOU  827  CB  PHE A 166    12520   8806  15818   1705    546    455       C  
ATOM    828  CG  PHE A 166     -39.923 -10.781 107.288  1.00 96.63           C  
ANISOU  828  CG  PHE A 166    12159   9028  15527   1719    416    423       C  
ATOM    829  CD1 PHE A 166     -38.552 -10.891 107.100  1.00101.41           C  
ANISOU  829  CD1 PHE A 166    12523   9680  16326   1950    495    539       C  
ATOM    830  CD2 PHE A 166     -40.475  -9.513 107.385  1.00 94.74           C  
ANISOU  830  CD2 PHE A 166    11938   9071  14987   1503    237    299       C  
ATOM    831  CE1 PHE A 166     -37.756  -9.755 106.978  1.00101.17           C  
ANISOU  831  CE1 PHE A 166    12264   9985  16192   1890    388    513       C  
ATOM    832  CE2 PHE A 166     -39.676  -8.378 107.265  1.00 96.53           C  
ANISOU  832  CE2 PHE A 166    12000   9554  15123   1466    148    268       C  
ATOM    833  CZ  PHE A 166     -38.327  -8.506 107.047  1.00 96.81           C  
ANISOU  833  CZ  PHE A 166    11787   9643  15354   1622    220    368       C  
ATOM    834  N   LEU A 167     -41.658 -11.205 104.160  1.00 92.85           N  
ANISOU  834  N   LEU A 167    12228   8168  14882   1362    799   -459       N  
ATOM    835  CA  LEU A 167     -42.424 -10.282 103.322  1.00 90.49           C  
ANISOU  835  CA  LEU A 167    12010   8112  14258   1166    717   -692       C  
ATOM    836  C   LEU A 167     -43.001 -10.976 102.070  1.00 96.56           C  
ANISOU  836  C   LEU A 167    12997   8737  14956   1036    870  -1058       C  
ATOM    837  O   LEU A 167     -43.673 -10.321 101.270  1.00 95.02           O  
ANISOU  837  O   LEU A 167    12860   8788  14454    892    790  -1236       O  
ATOM    838  CB  LEU A 167     -41.610  -9.034 102.950  1.00 88.92           C  
ANISOU  838  CB  LEU A 167    11685   8180  13920   1229    694   -649       C  
ATOM    839  CG  LEU A 167     -41.611  -7.931 104.015  1.00 90.70           C  
ANISOU  839  CG  LEU A 167    11775   8631  14055   1192    464   -434       C  
ATOM    840  CD1 LEU A 167     -40.416  -7.035 103.872  1.00 91.17           C  
ANISOU  840  CD1 LEU A 167    11668   8834  14137   1242    488   -353       C  
ATOM    841  CD2 LEU A 167     -42.888  -7.109 103.969  1.00 89.90           C  
ANISOU  841  CD2 LEU A 167    11781   8690  13685   1042    321   -508       C  
ATOM    842  N   ARG A 168     -42.792 -12.305 101.933  1.00 96.89           N  
ANISOU  842  N   ARG A 168    13170   8377  15268   1083   1084  -1170       N  
ATOM    843  CA  ARG A 168     -43.388 -13.097 100.852  1.00 99.90           C  
ANISOU  843  CA  ARG A 168    13798   8571  15586    895   1228  -1591       C  
ATOM    844  C   ARG A 168     -44.811 -13.447 101.291  1.00104.45           C  
ANISOU  844  C   ARG A 168    14422   9128  16134    569   1059  -1637       C  
ATOM    845  O   ARG A 168     -45.020 -13.729 102.474  1.00103.86           O  
ANISOU  845  O   ARG A 168    14270   8926  16265    580   1000  -1336       O  
ATOM    846  CB  ARG A 168     -42.553 -14.347 100.527  1.00104.58           C  
ANISOU  846  CB  ARG A 168    14551   8667  16517   1083   1578  -1729       C  
ATOM    847  CG  ARG A 168     -41.257 -14.025  99.796  1.00116.42           C  
ANISOU  847  CG  ARG A 168    15980  10258  17996   1379   1799  -1768       C  
ATOM    848  CD  ARG A 168     -40.769 -15.171  98.939  1.00132.01           C  
ANISOU  848  CD  ARG A 168    18202  11807  20149   1507   2195  -2117       C  
ATOM    849  NE  ARG A 168     -39.312 -15.160  98.856  1.00141.74           N  
ANISOU  849  NE  ARG A 168    19252  13016  21587   1928   2457  -1946       N  
ATOM    850  CZ  ARG A 168     -38.514 -16.019  99.485  1.00159.83           C  
ANISOU  850  CZ  ARG A 168    21469  14921  24339   2275   2663  -1713       C  
ATOM    851  NH1 ARG A 168     -39.025 -16.968 100.257  1.00152.14           N  
ANISOU  851  NH1 ARG A 168    20642  13496  23669   2245   2657  -1603       N  
ATOM    852  NH2 ARG A 168     -37.196 -15.917  99.365  1.00146.14           N  
ANISOU  852  NH2 ARG A 168    19482  13272  22774   2665   2884  -1540       N  
ATOM    853  N   CYS A 169     -45.795 -13.391 100.371  1.00102.24           N  
ANISOU  853  N   CYS A 169    14231   9042  15572    275    971  -1982       N  
ATOM    854  CA  CYS A 169     -47.205 -13.636 100.708  1.00102.68           C  
ANISOU  854  CA  CYS A 169    14242   9185  15588    -73    795  -2029       C  
ATOM    855  C   CYS A 169     -47.506 -15.138 100.948  1.00111.65           C  
ANISOU  855  C   CYS A 169    15561   9769  17091   -295    981  -2177       C  
ATOM    856  O   CYS A 169     -48.131 -15.828 100.138  1.00114.70           O  
ANISOU  856  O   CYS A 169    16105  10045  17432   -629   1021  -2601       O  
ATOM    857  CB  CYS A 169     -48.142 -13.017  99.674  1.00103.23           C  
ANISOU  857  CB  CYS A 169    14266   9738  15219   -300    592  -2300       C  
ATOM    858  SG  CYS A 169     -47.740 -11.301  99.232  1.00103.14           S  
ANISOU  858  SG  CYS A 169    14122  10252  14813    -17    450  -2102       S  
ATOM    859  N   THR A 170     -47.047 -15.608 102.122  1.00109.58           N  
ANISOU  859  N   THR A 170    15282   9167  17187   -112   1090  -1797       N  
ATOM    860  CA  THR A 170     -47.230 -16.953 102.665  1.00114.37           C  
ANISOU  860  CA  THR A 170    16059   9181  18216   -242   1299  -1747       C  
ATOM    861  C   THR A 170     -48.640 -16.996 103.281  1.00121.35           C  
ANISOU  861  C   THR A 170    16808  10234  19064   -641   1137  -1655       C  
ATOM    862  O   THR A 170     -49.003 -16.049 103.990  1.00117.48           O  
ANISOU  862  O   THR A 170    16068  10202  18366   -570    927  -1358       O  
ATOM    863  CB  THR A 170     -46.102 -17.253 103.692  1.00118.23           C  
ANISOU  863  CB  THR A 170    16528   9371  19025    197   1445  -1266       C  
ATOM    864  OG1 THR A 170     -44.857 -17.365 103.012  1.00115.44           O  
ANISOU  864  OG1 THR A 170    16257   8850  18756    540   1641  -1390       O  
ATOM    865  CG2 THR A 170     -46.346 -18.518 104.521  1.00120.77           C  
ANISOU  865  CG2 THR A 170    17006   9102  19780    123   1650  -1026       C  
ATOM    866  N   PRO A 171     -49.442 -18.070 103.058  1.00124.33           N  
ANISOU  866  N   PRO A 171    17339  10244  19658  -1071   1256  -1909       N  
ATOM    867  CA  PRO A 171     -50.788 -18.122 103.667  1.00125.44           C  
ANISOU  867  CA  PRO A 171    17281  10588  19791  -1479   1129  -1789       C  
ATOM    868  C   PRO A 171     -50.767 -18.006 105.197  1.00128.20           C  
ANISOU  868  C   PRO A 171    17493  10943  20276  -1280   1154  -1170       C  
ATOM    869  O   PRO A 171     -51.757 -17.567 105.789  1.00126.73           O  
ANISOU  869  O   PRO A 171    17051  11155  19947  -1469   1017   -993       O  
ATOM    870  CB  PRO A 171     -51.325 -19.490 103.226  1.00133.99           C  
ANISOU  870  CB  PRO A 171    18611  11098  21202  -1968   1335  -2149       C  
ATOM    871  CG  PRO A 171     -50.113 -20.282 102.826  1.00141.01           C  
ANISOU  871  CG  PRO A 171    19879  11317  22380  -1680   1647  -2291       C  
ATOM    872  CD  PRO A 171     -49.179 -19.277 102.245  1.00131.90           C  
ANISOU  872  CD  PRO A 171    18655  10573  20886  -1236   1536  -2342       C  
ATOM    873  N   ASP A 172     -49.633 -18.370 105.828  1.00125.65           N  
ANISOU  873  N   ASP A 172    17313  10239  20189   -872   1326   -832       N  
ATOM    874  CA  ASP A 172     -49.459 -18.294 107.275  1.00125.22           C  
ANISOU  874  CA  ASP A 172    17154  10231  20192   -642   1336   -230       C  
ATOM    875  C   ASP A 172     -49.094 -16.874 107.726  1.00124.37           C  
ANISOU  875  C   ASP A 172    16802  10763  19688   -327   1077    -40       C  
ATOM    876  O   ASP A 172     -49.732 -16.352 108.643  1.00122.64           O  
ANISOU  876  O   ASP A 172    16406  10910  19283   -370    971    227       O  
ATOM    877  CB  ASP A 172     -48.387 -19.292 107.752  1.00130.71           C  
ANISOU  877  CB  ASP A 172    18075  10303  21286   -309   1599     90       C  
ATOM    878  CG  ASP A 172     -48.309 -19.435 109.263  1.00143.35           C  
ANISOU  878  CG  ASP A 172    19600  11938  22930   -118   1619    751       C  
ATOM    879  OD1 ASP A 172     -47.990 -18.432 109.942  1.00140.68           O  
ANISOU  879  OD1 ASP A 172    19045  12150  22257    133   1397   1000       O  
ATOM    880  OD2 ASP A 172     -48.553 -20.552 109.766  1.00154.00           O  
ANISOU  880  OD2 ASP A 172    21127  12754  24631   -227   1870   1020       O  
ATOM    881  N   ARG A 173     -48.042 -16.283 107.121  1.00118.87           N  
ANISOU  881  N   ARG A 173    16112  10169  18884    -20   1015   -177       N  
ATOM    882  CA  ARG A 173     -47.502 -14.954 107.451  1.00114.47           C  
ANISOU  882  CA  ARG A 173    15366  10116  18011    252    800    -42       C  
ATOM    883  C   ARG A 173     -48.495 -13.814 107.159  1.00115.61           C  
ANISOU  883  C   ARG A 173    15350  10782  17795     72    593   -226       C  
ATOM    884  O   ARG A 173     -48.452 -12.762 107.808  1.00111.81           O  
ANISOU  884  O   ARG A 173    14732  10676  17075    220    444    -56       O  
ATOM    885  CB  ARG A 173     -46.200 -14.709 106.677  1.00114.12           C  
ANISOU  885  CB  ARG A 173    15357  10009  17995    538    839   -183       C  
ATOM    886  CG  ARG A 173     -45.097 -15.713 106.991  1.00128.33           C  
ANISOU  886  CG  ARG A 173    17247  11353  20159    833   1047     50       C  
ATOM    887  CD  ARG A 173     -43.847 -15.392 106.200  1.00137.56           C  
ANISOU  887  CD  ARG A 173    18375  12547  21346   1117   1108    -92       C  
ATOM    888  NE  ARG A 173     -42.745 -16.319 106.468  1.00150.45           N  
ANISOU  888  NE  ARG A 173    20031  13785  23346   1477   1322    154       N  
ATOM    889  CZ  ARG A 173     -41.870 -16.190 107.462  1.00167.24           C  
ANISOU  889  CZ  ARG A 173    21950  16066  25529   1797   1231    611       C  
ATOM    890  NH1 ARG A 173     -41.975 -15.184 108.324  1.00149.26           N  
ANISOU  890  NH1 ARG A 173    19469  14300  22943   1754    936    819       N  
ATOM    891  NH2 ARG A 173     -40.896 -17.076 107.616  1.00162.12           N  
ANISOU  891  NH2 ARG A 173    21292  15074  25234   2172   1435    859       N  
ATOM    892  N   PHE A 174     -49.363 -14.025 106.162  1.00113.97           N  
ANISOU  892  N   PHE A 174    15163  10596  17546   -234    586   -584       N  
ATOM    893  CA  PHE A 174     -50.385 -13.086 105.723  1.00112.25           C  
ANISOU  893  CA  PHE A 174    14764  10874  17014   -382    396   -744       C  
ATOM    894  C   PHE A 174     -51.703 -13.859 105.506  1.00119.14           C  
ANISOU  894  C   PHE A 174    15563  11736  17970   -826    412   -907       C  
ATOM    895  O   PHE A 174     -51.958 -14.342 104.393  1.00121.10           O  
ANISOU  895  O   PHE A 174    15891  11905  18217  -1078    409  -1290       O  
ATOM    896  CB  PHE A 174     -49.925 -12.350 104.450  1.00112.74           C  
ANISOU  896  CB  PHE A 174    14867  11122  16846   -273    310  -1031       C  
ATOM    897  CG  PHE A 174     -48.643 -11.567 104.614  1.00111.72           C  
ANISOU  897  CG  PHE A 174    14767  11012  16667     89    311   -879       C  
ATOM    898  CD1 PHE A 174     -48.660 -10.277 105.126  1.00112.01           C  
ANISOU  898  CD1 PHE A 174    14679  11388  16492    256    173   -703       C  
ATOM    899  CD2 PHE A 174     -47.416 -12.120 104.253  1.00115.19           C  
ANISOU  899  CD2 PHE A 174    15347  11124  17295    252    472   -927       C  
ATOM    900  CE1 PHE A 174     -47.473  -9.554 105.280  1.00111.25           C  
ANISOU  900  CE1 PHE A 174    14595  11301  16373    504    168   -594       C  
ATOM    901  CE2 PHE A 174     -46.229 -11.394 104.407  1.00116.06           C  
ANISOU  901  CE2 PHE A 174    15409  11310  17379    540    467   -778       C  
ATOM    902  CZ  PHE A 174     -46.265 -10.117 104.917  1.00111.30           C  
ANISOU  902  CZ  PHE A 174    14678  11045  16565    626    301   -622       C  
ATOM    903  N   PRO A 175     -52.528 -14.038 106.572  1.00116.06           N  
ANISOU  903  N   PRO A 175    15019  11433  17647   -961    446   -630       N  
ATOM    904  CA  PRO A 175     -53.780 -14.795 106.412  1.00119.72           C  
ANISOU  904  CA  PRO A 175    15355  11902  18233  -1444    479   -762       C  
ATOM    905  C   PRO A 175     -54.822 -14.007 105.628  1.00123.20           C  
ANISOU  905  C   PRO A 175    15501  12936  18373  -1597    248   -996       C  
ATOM    906  O   PRO A 175     -54.727 -12.785 105.542  1.00119.36           O  
ANISOU  906  O   PRO A 175    14903  12850  17598  -1278    101   -932       O  
ATOM    907  CB  PRO A 175     -54.236 -15.050 107.855  1.00122.46           C  
ANISOU  907  CB  PRO A 175    15594  12240  18695  -1469    615   -318       C  
ATOM    908  CG  PRO A 175     -53.106 -14.594 108.739  1.00123.72           C  
ANISOU  908  CG  PRO A 175    15885  12336  18787  -1001    641     12       C  
ATOM    909  CD  PRO A 175     -52.378 -13.560 107.960  1.00115.52           C  
ANISOU  909  CD  PRO A 175    14873  11505  17515   -714    466   -203       C  
ATOM    910  N   GLU A 176     -55.812 -14.704 105.055  1.00124.16           N  
ANISOU  910  N   GLU A 176    15490  13114  18572  -2089    214  -1258       N  
ATOM    911  CA  GLU A 176     -56.853 -14.070 104.248  1.00125.17           C  
ANISOU  911  CA  GLU A 176    15276  13876  18407  -2254    -44  -1465       C  
ATOM    912  C   GLU A 176     -57.902 -13.328 105.086  1.00127.81           C  
ANISOU  912  C   GLU A 176    15182  14743  18637  -2180    -94  -1144       C  
ATOM    913  O   GLU A 176     -58.263 -13.773 106.178  1.00128.65           O  
ANISOU  913  O   GLU A 176    15206  14724  18952  -2293     94   -866       O  
ATOM    914  CB  GLU A 176     -57.551 -15.103 103.352  1.00132.59           C  
ANISOU  914  CB  GLU A 176    16179  14753  19445  -2866    -96  -1895       C  
ATOM    915  CG  GLU A 176     -57.361 -14.850 101.865  1.00145.70           C  
ANISOU  915  CG  GLU A 176    17927  16653  20779  -2899   -312  -2337       C  
ATOM    916  CD  GLU A 176     -57.982 -13.570 101.336  1.00167.17           C  
ANISOU  916  CD  GLU A 176    20287  20173  23057  -2674   -618  -2270       C  
ATOM    917  OE1 GLU A 176     -59.219 -13.543 101.145  1.00166.10           O  
ANISOU  917  OE1 GLU A 176    19722  20565  22823  -2989   -811  -2321       O  
ATOM    918  OE2 GLU A 176     -57.232 -12.591 101.124  1.00157.90           O  
ANISOU  918  OE2 GLU A 176    19244  19095  21658  -2179   -652  -2138       O  
ATOM    919  N   GLY A 177     -58.373 -12.207 104.530  1.00122.38           N  
ANISOU  919  N   GLY A 177    14236  14644  17620  -1961   -319  -1169       N  
ATOM    920  CA  GLY A 177     -59.421 -11.349 105.078  1.00122.06           C  
ANISOU  920  CA  GLY A 177    13755  15177  17445  -1806   -372   -914       C  
ATOM    921  C   GLY A 177     -59.255 -10.847 106.497  1.00121.73           C  
ANISOU  921  C   GLY A 177    13736  15071  17445  -1465   -163   -534       C  
ATOM    922  O   GLY A 177     -60.217 -10.866 107.270  1.00123.49           O  
ANISOU  922  O   GLY A 177    13627  15576  17718  -1556    -57   -332       O  
ATOM    923  N   CYS A 178     -58.049 -10.376 106.845  1.00112.79           N  
ANISOU  923  N   CYS A 178    12971  13620  16265  -1087   -101   -448       N  
ATOM    924  CA  CYS A 178     -57.776  -9.833 108.175  1.00109.84           C  
ANISOU  924  CA  CYS A 178    12665  13219  15852   -769     62   -145       C  
ATOM    925  C   CYS A 178     -58.066  -8.344 108.218  1.00111.71           C  
ANISOU  925  C   CYS A 178    12771  13846  15828   -343     -5    -82       C  
ATOM    926  O   CYS A 178     -57.865  -7.638 107.224  1.00109.96           O  
ANISOU  926  O   CYS A 178    12580  13732  15466   -173   -170   -220       O  
ATOM    927  CB  CYS A 178     -56.340 -10.120 108.605  1.00107.22           C  
ANISOU  927  CB  CYS A 178    12747  12388  15604   -620    140    -84       C  
ATOM    928  SG  CYS A 178     -55.980 -11.870 108.881  1.00113.90           S  
ANISOU  928  SG  CYS A 178    13785  12676  16814   -996    313    -32       S  
ATOM    929  N   THR A 179     -58.537  -7.864 109.387  1.00108.88           N  
ANISOU  929  N   THR A 179    12293  13679  15397   -154    158    138       N  
ATOM    930  CA  THR A 179     -58.787  -6.444 109.641  1.00107.88           C  
ANISOU  930  CA  THR A 179    12108  13823  15059    293    177    194       C  
ATOM    931  C   THR A 179     -57.391  -5.848 109.841  1.00107.32           C  
ANISOU  931  C   THR A 179    12474  13390  14913    541    158    147       C  
ATOM    932  O   THR A 179     -56.760  -6.051 110.881  1.00106.08           O  
ANISOU  932  O   THR A 179    12520  13044  14740    561    268    243       O  
ATOM    933  CB  THR A 179     -59.779  -6.239 110.811  1.00122.47           C  
ANISOU  933  CB  THR A 179    13691  15994  16848    388    407    393       C  
ATOM    934  OG1 THR A 179     -59.246  -6.801 112.013  1.00125.01           O  
ANISOU  934  OG1 THR A 179    14238  16089  17170    308    584    535       O  
ATOM    935  CG2 THR A 179     -61.167  -6.817 110.527  1.00125.31           C  
ANISOU  935  CG2 THR A 179    13527  16768  17315    101    420    448       C  
ATOM    936  N   ASN A 180     -56.849  -5.288 108.754  1.00101.98           N  
ANISOU  936  N   ASN A 180    11925  12628  14194    660      1      8       N  
ATOM    937  CA  ASN A 180     -55.480  -4.785 108.635  1.00 99.04           C  
ANISOU  937  CA  ASN A 180    11912  11924  13796    811    -37    -59       C  
ATOM    938  C   ASN A 180     -55.042  -3.758 109.701  1.00100.42           C  
ANISOU  938  C   ASN A 180    12271  12033  13851   1089     67     -9       C  
ATOM    939  O   ASN A 180     -53.883  -3.818 110.133  1.00 98.63           O  
ANISOU  939  O   ASN A 180    12287  11551  13638   1071     55    -28       O  
ATOM    940  CB  ASN A 180     -55.270  -4.180 107.246  1.00102.70           C  
ANISOU  940  CB  ASN A 180    12417  12412  14193    914   -176   -167       C  
ATOM    941  CG  ASN A 180     -55.015  -5.197 106.158  1.00133.92           C  
ANISOU  941  CG  ASN A 180    16379  16289  18216    625   -284   -317       C  
ATOM    942  OD1 ASN A 180     -54.059  -5.987 106.212  1.00127.61           O  
ANISOU  942  OD1 ASN A 180    15776  15161  17549    475   -248   -382       O  
ATOM    943  ND2 ASN A 180     -55.847  -5.174 105.123  1.00128.33           N  
ANISOU  943  ND2 ASN A 180    15459  15901  17399    563   -417   -383       N  
ATOM    944  N   GLU A 181     -55.938  -2.808 110.086  1.00 96.62           N  
ANISOU  944  N   GLU A 181    11670  11789  13252   1350    169     33       N  
ATOM    945  CA  GLU A 181     -55.710  -1.692 111.030  1.00 95.72           C  
ANISOU  945  CA  GLU A 181    11758  11610  13000   1626    303      2       C  
ATOM    946  C   GLU A 181     -54.998  -0.538 110.298  1.00 96.18           C  
ANISOU  946  C   GLU A 181    12058  11425  13060   1822    246    -96       C  
ATOM    947  O   GLU A 181     -55.262   0.625 110.597  1.00 97.05           O  
ANISOU  947  O   GLU A 181    12278  11496  13103   2113    372   -132       O  
ATOM    948  CB  GLU A 181     -54.944  -2.123 112.309  1.00 96.67           C  
ANISOU  948  CB  GLU A 181    12073  11622  13038   1503    355      9       C  
ATOM    949  CG  GLU A 181     -54.752  -1.042 113.370  1.00108.21           C  
ANISOU  949  CG  GLU A 181    13758  13066  14290   1721    484    -97       C  
ATOM    950  CD  GLU A 181     -55.989  -0.576 114.114  1.00137.45           C  
ANISOU  950  CD  GLU A 181    17321  17053  17849   1949    727    -72       C  
ATOM    951  OE1 GLU A 181     -56.906  -1.400 114.338  1.00140.19           O  
ANISOU  951  OE1 GLU A 181    17369  17681  18216   1852    816     96       O  
ATOM    952  OE2 GLU A 181     -56.022   0.610 114.512  1.00135.16           O  
ANISOU  952  OE2 GLU A 181    17228  16688  17439   2215    860   -228       O  
ATOM    953  N   VAL A 182     -54.127  -0.870 109.319  1.00 89.23           N  
ANISOU  953  N   VAL A 182    11271  10363  12270   1667     96   -132       N  
ATOM    954  CA  VAL A 182     -53.397   0.085 108.473  1.00 87.39           C  
ANISOU  954  CA  VAL A 182    11247   9905  12053   1791     61   -175       C  
ATOM    955  C   VAL A 182     -54.350   0.692 107.426  1.00 92.31           C  
ANISOU  955  C   VAL A 182    11720  10720  12635   2027     46    -69       C  
ATOM    956  O   VAL A 182     -54.018   1.707 106.809  1.00 92.37           O  
ANISOU  956  O   VAL A 182    11903  10555  12637   2219     75    -28       O  
ATOM    957  CB  VAL A 182     -52.137  -0.522 107.817  1.00 88.58           C  
ANISOU  957  CB  VAL A 182    11513   9851  12291   1562    -45   -228       C  
ATOM    958  CG1 VAL A 182     -51.070  -0.808 108.863  1.00 87.54           C  
ANISOU  958  CG1 VAL A 182    11518   9549  12195   1423    -45   -282       C  
ATOM    959  CG2 VAL A 182     -52.462  -1.775 107.006  1.00 87.99           C  
ANISOU  959  CG2 VAL A 182    11254   9919  12261   1360   -138   -228       C  
ATOM    960  N   GLN A 183     -55.534   0.067 107.241  1.00 89.75           N  
ANISOU  960  N   GLN A 183    11048  10770  12281   2002      0      5       N  
ATOM    961  CA  GLN A 183     -56.601   0.539 106.362  1.00 92.03           C  
ANISOU  961  CA  GLN A 183    11081  11387  12498   2236    -57    144       C  
ATOM    962  C   GLN A 183     -57.179   1.834 106.954  1.00 96.85           C  
ANISOU  962  C   GLN A 183    11726  11972  13101   2687    139    244       C  
ATOM    963  O   GLN A 183     -57.633   2.705 106.209  1.00 99.00           O  
ANISOU  963  O   GLN A 183    11951  12327  13339   3025    138    407       O  
ATOM    964  CB  GLN A 183     -57.682  -0.546 106.208  1.00 95.49           C  
ANISOU  964  CB  GLN A 183    11085  12267  12930   2009   -163    162       C  
ATOM    965  CG  GLN A 183     -58.633  -0.338 105.020  1.00120.88           C  
ANISOU  965  CG  GLN A 183    13970  15932  16028   2137   -337    284       C  
ATOM    966  CD  GLN A 183     -58.059  -0.751 103.676  1.00140.33           C  
ANISOU  966  CD  GLN A 183    16537  18405  18376   1930   -547    199       C  
ATOM    967  OE1 GLN A 183     -57.322  -1.739 103.549  1.00133.45           O  
ANISOU  967  OE1 GLN A 183    15820  17328  17557   1557   -587      3       O  
ATOM    968  NE2 GLN A 183     -58.443  -0.034 102.628  1.00133.58           N  
ANISOU  968  NE2 GLN A 183    15589  17822  17342   2193   -669    360       N  
ATOM    969  N   ASN A 184     -57.124   1.959 108.303  1.00 91.89           N  
ANISOU  969  N   ASN A 184    11210  11216  12487   2711    326    148       N  
ATOM    970  CA  ASN A 184     -57.565   3.125 109.076  1.00 93.53           C  
ANISOU  970  CA  ASN A 184    11533  11324  12681   3115    578    147       C  
ATOM    971  C   ASN A 184     -56.511   4.240 109.049  1.00 94.08           C  
ANISOU  971  C   ASN A 184    12087  10866  12794   3226    659     40       C  
ATOM    972  O   ASN A 184     -56.834   5.385 109.352  1.00 96.84           O  
ANISOU  972  O   ASN A 184    12602  11020  13171   3598    876     35       O  
ATOM    973  CB  ASN A 184     -57.866   2.737 110.535  1.00 96.10           C  
ANISOU  973  CB  ASN A 184    11820  11760  12932   3043    753     45       C  
ATOM    974  CG  ASN A 184     -59.058   1.833 110.759  1.00120.30           C  
ANISOU  974  CG  ASN A 184    14396  15328  15985   2963    775    179       C  
ATOM    975  OD1 ASN A 184     -59.769   1.419 109.831  1.00111.78           O  
ANISOU  975  OD1 ASN A 184    12943  14571  14958   2925    624    321       O  
ATOM    976  ND2 ASN A 184     -59.305   1.512 112.022  1.00114.56           N  
ANISOU  976  ND2 ASN A 184    13653  14712  15164   2907    967    136       N  
ATOM    977  N   ILE A 185     -55.260   3.908 108.699  1.00 85.21           N  
ANISOU  977  N   ILE A 185    11180   9495  11702   2900    514    -50       N  
ATOM    978  CA  ILE A 185     -54.168   4.876 108.636  1.00 84.30           C  
ANISOU  978  CA  ILE A 185    11474   8899  11655   2896    579   -153       C  
ATOM    979  C   ILE A 185     -54.059   5.410 107.201  1.00 90.32           C  
ANISOU  979  C   ILE A 185    12277   9566  12475   3040    532     54       C  
ATOM    980  O   ILE A 185     -53.974   4.637 106.245  1.00 88.77           O  
ANISOU  980  O   ILE A 185    11900   9597  12232   2883    350    153       O  
ATOM    981  CB  ILE A 185     -52.842   4.250 109.149  1.00 84.08           C  
ANISOU  981  CB  ILE A 185    11594   8723  11630   2476    465   -335       C  
ATOM    982  CG1 ILE A 185     -52.988   3.772 110.611  1.00 84.31           C  
ANISOU  982  CG1 ILE A 185    11599   8900  11533   2375    508   -478       C  
ATOM    983  CG2 ILE A 185     -51.669   5.226 109.009  1.00 84.94           C  
ANISOU  983  CG2 ILE A 185    12054   8382  11835   2389    513   -444       C  
ATOM    984  CD1 ILE A 185     -52.128   2.595 110.996  1.00 86.44           C  
ANISOU  984  CD1 ILE A 185    11806   9256  11780   2017    339   -505       C  
ATOM    985  N   LYS A 186     -54.075   6.738 107.067  1.00 90.89           N  
ANISOU  985  N   LYS A 186    12615   9286  12632   3344    721    118       N  
ATOM    986  CA  LYS A 186     -53.977   7.439 105.789  1.00 93.14           C  
ANISOU  986  CA  LYS A 186    12998   9431  12958   3541    733    386       C  
ATOM    987  C   LYS A 186     -52.505   7.763 105.480  1.00 99.36           C  
ANISOU  987  C   LYS A 186    14117   9790  13844   3226    751    303       C  
ATOM    988  O   LYS A 186     -51.858   8.477 106.252  1.00100.20           O  
ANISOU  988  O   LYS A 186    14535   9462  14076   3125    901     99       O  
ATOM    989  CB  LYS A 186     -54.837   8.721 105.837  1.00 99.38           C  
ANISOU  989  CB  LYS A 186    13908  10015  13835   4090    980    562       C  
ATOM    990  CG  LYS A 186     -54.816   9.575 104.576  1.00 99.37           C  
ANISOU  990  CG  LYS A 186    14042   9839  13875   4379   1032    932       C  
ATOM    991  CD  LYS A 186     -55.523  10.916 104.792  1.00106.08           C  
ANISOU  991  CD  LYS A 186    15093  10330  14884   4955   1340   1104       C  
ATOM    992  CE  LYS A 186     -54.704  11.949 105.531  1.00112.60           C  
ANISOU  992  CE  LYS A 186    16466  10379  15937   4871   1633    848       C  
ATOM    993  NZ  LYS A 186     -54.689  13.239 104.794  1.00123.72           N  
ANISOU  993  NZ  LYS A 186    18212  11260  17535   5252   1881   1188       N  
ATOM    994  N   PHE A 187     -51.983   7.224 104.356  1.00 96.47           N  
ANISOU  994  N   PHE A 187    13665   9579  13409   3049    607    439       N  
ATOM    995  CA  PHE A 187     -50.610   7.454 103.900  1.00 96.42           C  
ANISOU  995  CA  PHE A 187    13887   9255  13494   2758    647    415       C  
ATOM    996  C   PHE A 187     -50.632   8.458 102.749  1.00106.60           C  
ANISOU  996  C   PHE A 187    15361  10350  14792   3010    785    759       C  
ATOM    997  O   PHE A 187     -50.734   8.086 101.579  1.00105.59           O  
ANISOU  997  O   PHE A 187    15107  10527  14484   3056    688    982       O  
ATOM    998  CB  PHE A 187     -49.923   6.134 103.513  1.00 94.72           C  
ANISOU  998  CB  PHE A 187    13470   9325  13194   2407    460    317       C  
ATOM    999  CG  PHE A 187     -49.644   5.232 104.692  1.00 93.72           C  
ANISOU  999  CG  PHE A 187    13227   9282  13103   2153    360     43       C  
ATOM   1000  CD1 PHE A 187     -48.453   5.333 105.400  1.00 96.03           C  
ANISOU 1000  CD1 PHE A 187    13644   9323  13519   1870    379   -141       C  
ATOM   1001  CD2 PHE A 187     -50.574   4.281 105.097  1.00 95.07           C  
ANISOU 1001  CD2 PHE A 187    13139   9809  13175   2186    244      0       C  
ATOM   1002  CE1 PHE A 187     -48.199   4.503 106.493  1.00 95.18           C  
ANISOU 1002  CE1 PHE A 187    13421   9346  13398   1679    268   -327       C  
ATOM   1003  CE2 PHE A 187     -50.316   3.447 106.188  1.00 96.16           C  
ANISOU 1003  CE2 PHE A 187    13194  10011  13332   1973    179   -178       C  
ATOM   1004  CZ  PHE A 187     -49.130   3.563 106.878  1.00 93.43           C  
ANISOU 1004  CZ  PHE A 187    12990   9439  13072   1749    183   -324       C  
ATOM   1005  N   ASN A 188     -50.585   9.748 103.121  1.00110.31           N  
ANISOU 1005  N   ASN A 188    16157  10300  15454   3186   1028    800       N  
ATOM   1006  CA  ASN A 188     -50.650  10.937 102.263  1.00116.16           C  
ANISOU 1006  CA  ASN A 188    17165  10692  16279   3483   1242   1170       C  
ATOM   1007  C   ASN A 188     -49.562  10.984 101.184  1.00122.26           C  
ANISOU 1007  C   ASN A 188    18046  11373  17034   3220   1280   1359       C  
ATOM   1008  O   ASN A 188     -49.801  11.560 100.118  1.00124.95           O  
ANISOU 1008  O   ASN A 188    18485  11697  17296   3498   1377   1785       O  
ATOM   1009  CB  ASN A 188     -50.535  12.196 103.134  1.00123.48           C  
ANISOU 1009  CB  ASN A 188    18493  10930  17494   3575   1536   1035       C  
ATOM   1010  CG  ASN A 188     -51.580  13.264 102.908  1.00169.82           C  
ANISOU 1010  CG  ASN A 188    24523  16550  23451   4192   1763   1360       C  
ATOM   1011  OD1 ASN A 188     -52.759  12.971 102.633  1.00163.77           O  
ANISOU 1011  OD1 ASN A 188    23451  16254  22519   4624   1660   1586       O  
ATOM   1012  ND2 ASN A 188     -51.127  14.533 103.064  1.00179.28           N  
ANISOU 1012  ND2 ASN A 188    26198  16975  24945   4224   2091   1378       N  
ATOM   1013  N   SER A 189     -48.365  10.420 101.466  1.00117.65           N  
ANISOU 1013  N   SER A 189    17433  10751  16516   2716   1225   1082       N  
ATOM   1014  CA  SER A 189     -47.224  10.438 100.541  1.00118.68           C  
ANISOU 1014  CA  SER A 189    17626  10810  16657   2437   1310   1228       C  
ATOM   1015  C   SER A 189     -47.468   9.588  99.296  1.00122.48           C  
ANISOU 1015  C   SER A 189    17883  11851  16802   2535   1173   1446       C  
ATOM   1016  O   SER A 189     -47.697   8.380  99.399  1.00118.92           O  
ANISOU 1016  O   SER A 189    17150  11845  16188   2444    945   1238       O  
ATOM   1017  CB  SER A 189     -45.948   9.978 101.238  1.00120.39           C  
ANISOU 1017  CB  SER A 189    17773  10934  17037   1921   1269    875       C  
ATOM   1018  OG  SER A 189     -45.321  11.034 101.951  1.00132.09           O  
ANISOU 1018  OG  SER A 189    19532  11842  18816   1704   1451    736       O  
ATOM   1019  N   SER A 190     -47.432  10.235  98.120  1.00122.67           N  
ANISOU 1019  N   SER A 190    18063  11838  16708   2714   1326   1867       N  
ATOM   1020  CA  SER A 190     -47.647   9.583  96.825  1.00122.80           C  
ANISOU 1020  CA  SER A 190    17928  12408  16322   2813   1217   2084       C  
ATOM   1021  C   SER A 190     -46.329   9.167  96.202  1.00125.88           C  
ANISOU 1021  C   SER A 190    18322  12829  16677   2442   1337   2035       C  
ATOM   1022  O   SER A 190     -46.236   8.065  95.653  1.00123.98           O  
ANISOU 1022  O   SER A 190    17882  13058  16167   2340   1198   1891       O  
ATOM   1023  CB  SER A 190     -48.417  10.499  95.878  1.00131.25           C  
ANISOU 1023  CB  SER A 190    19146  13524  17199   3273   1304   2626       C  
ATOM   1024  OG  SER A 190     -47.697  11.676  95.547  1.00142.22           O  
ANISOU 1024  OG  SER A 190    20888  14357  18793   3260   1646   2952       O  
ATOM   1025  N   GLY A 191     -45.313  10.006  96.346  1.00102.53           N  
ANISOU 1025  N   GLY A 191    11787  14276  12893    262   1302    224       N  
ATOM   1026  CA  GLY A 191     -43.994   9.721  95.806  1.00101.63           C  
ANISOU 1026  CA  GLY A 191    11692  14181  12740    287   1273    246       C  
ATOM   1027  C   GLY A 191     -43.577  10.640  94.680  1.00104.11           C  
ANISOU 1027  C   GLY A 191    12009  14504  13044    347   1280    258       C  
ATOM   1028  O   GLY A 191     -44.410  11.286  94.032  1.00103.74           O  
ANISOU 1028  O   GLY A 191    11944  14446  13026    387   1292    253       O  
ATOM   1029  N   GLN A 192     -42.264  10.674  94.444  1.00 99.52           N  
ANISOU 1029  N   GLN A 192    11446  13949  12418    352   1269    278       N  
ATOM   1030  CA  GLN A 192     -41.592  11.489  93.438  1.00 98.66           C  
ANISOU 1030  CA  GLN A 192    11346  13857  12282    395   1269    287       C  
ATOM   1031  C   GLN A 192     -40.506  10.675  92.744  1.00 99.00           C  
ANISOU 1031  C   GLN A 192    11391  13933  12292    429   1219    302       C  
ATOM   1032  O   GLN A 192     -40.066   9.655  93.270  1.00 97.64           O  
ANISOU 1032  O   GLN A 192    11218  13771  12109    416   1201    316       O  
ATOM   1033  CB  GLN A 192     -41.004  12.763  94.076  1.00100.42           C  
ANISOU 1033  CB  GLN A 192    11602  14088  12463    344   1331    296       C  
ATOM   1034  CG  GLN A 192     -39.876  12.522  95.082  1.00127.43           C  
ANISOU 1034  CG  GLN A 192    15038  17551  15827    272   1342    322       C  
ATOM   1035  CD  GLN A 192     -40.334  11.842  96.355  1.00158.81           C  
ANISOU 1035  CD  GLN A 192    19003  21511  19826    208   1353    320       C  
ATOM   1036  OE1 GLN A 192     -41.101  12.395  97.155  1.00156.63           O  
ANISOU 1036  OE1 GLN A 192    18738  21200  19572    156   1405    303       O  
ATOM   1037  NE2 GLN A 192     -39.884  10.613  96.556  1.00154.83           N  
ANISOU 1037  NE2 GLN A 192    18481  21030  19318    212   1306    338       N  
ATOM   1038  N   CYS A 193     -40.060  11.151  91.581  1.00 94.17           N  
ANISOU 1038  N   CYS A 193    10781  13336  11662    474   1203    302       N  
ATOM   1039  CA  CYS A 193     -39.067  10.500  90.735  1.00 93.29           C  
ANISOU 1039  CA  CYS A 193    10670  13255  11520    515   1162    313       C  
ATOM   1040  C   CYS A 193     -37.689  11.143  90.880  1.00 93.94           C  
ANISOU 1040  C   CYS A 193    10765  13396  11534    496   1175    336       C  
ATOM   1041  O   CYS A 193     -37.563  12.370  90.838  1.00 93.33           O  
ANISOU 1041  O   CYS A 193    10705  13328  11426    472   1203    332       O  
ATOM   1042  CB  CYS A 193     -39.535  10.518  89.284  1.00 93.99           C  
ANISOU 1042  CB  CYS A 193    10751  13328  11632    564   1130    295       C  
ATOM   1043  SG  CYS A 193     -41.021   9.530  88.977  1.00 98.37           S  
ANISOU 1043  SG  CYS A 193    11291  13841  12243    572   1107    279       S  
ATOM   1044  N   GLU A 194     -36.659  10.294  91.038  1.00 88.55           N  
ANISOU 1044  N   GLU A 194    10074  12754  10817    508   1157    364       N  
ATOM   1045  CA  GLU A 194     -35.259  10.695  91.180  1.00 87.87           C  
ANISOU 1045  CA  GLU A 194     9986  12748  10653    490   1163    398       C  
ATOM   1046  C   GLU A 194     -34.610  10.875  89.796  1.00 90.39           C  
ANISOU 1046  C   GLU A 194    10304  13094  10945    543   1132    388       C  
ATOM   1047  O   GLU A 194     -34.962  10.158  88.854  1.00 90.38           O  
ANISOU 1047  O   GLU A 194    10299  13054  10985    600   1103    367       O  
ATOM   1048  CB  GLU A 194     -34.501   9.640  92.003  1.00 89.57           C  
ANISOU 1048  CB  GLU A 194    10181  13003  10849    488   1159    446       C  
ATOM   1049  CG  GLU A 194     -33.218  10.135  92.658  1.00102.65           C  
ANISOU 1049  CG  GLU A 194    11825  14761  12417    435   1177    498       C  
ATOM   1050  CD  GLU A 194     -33.347  11.116  93.813  1.00128.03           C  
ANISOU 1050  CD  GLU A 194    15058  17994  15594    325   1224    508       C  
ATOM   1051  OE1 GLU A 194     -34.321  11.007  94.594  1.00124.56           O  
ANISOU 1051  OE1 GLU A 194    14628  17493  15208    287   1244    489       O  
ATOM   1052  OE2 GLU A 194     -32.445  11.971  93.963  1.00124.19           O  
ANISOU 1052  OE2 GLU A 194    14580  17588  15018    268   1244    534       O  
ATOM   1053  N   VAL A 195     -33.664  11.831  89.684  1.00 84.87           N  
ANISOU 1053  N   VAL A 195     9614  12464  10167    512   1141    400       N  
ATOM   1054  CA  VAL A 195     -32.915  12.171  88.463  1.00 83.65           C  
ANISOU 1054  CA  VAL A 195     9461  12352   9970    545   1112    388       C  
ATOM   1055  C   VAL A 195     -32.259  10.890  87.883  1.00 85.80           C  
ANISOU 1055  C   VAL A 195     9706  12643  10252    616   1082    404       C  
ATOM   1056  O   VAL A 195     -31.732  10.097  88.657  1.00 85.14           O  
ANISOU 1056  O   VAL A 195     9601  12592  10157    624   1091    449       O  
ATOM   1057  CB  VAL A 195     -31.881  13.296  88.776  1.00 87.50           C  
ANISOU 1057  CB  VAL A 195     9967  12931  10348    479   1131    409       C  
ATOM   1058  CG1 VAL A 195     -30.774  13.386  87.728  1.00 87.24           C  
ANISOU 1058  CG1 VAL A 195     9925  12974  10250    507   1097    409       C  
ATOM   1059  CG2 VAL A 195     -32.574  14.646  88.942  1.00 87.18           C  
ANISOU 1059  CG2 VAL A 195     9977  12848  10298    424   1167    380       C  
ATOM   1060  N   PRO A 196     -32.358  10.604  86.563  1.00 82.17           N  
ANISOU 1060  N   PRO A 196     9249  12155   9818    667   1051    372       N  
ATOM   1061  CA  PRO A 196     -32.913  11.426  85.473  1.00 81.77           C  
ANISOU 1061  CA  PRO A 196     9216  12072   9783    661   1031    327       C  
ATOM   1062  C   PRO A 196     -34.378  11.135  85.106  1.00 85.83           C  
ANISOU 1062  C   PRO A 196     9735  12495  10383    672   1025    299       C  
ATOM   1063  O   PRO A 196     -34.777  11.369  83.959  1.00 85.00           O  
ANISOU 1063  O   PRO A 196     9632  12366  10298    681   1000    271       O  
ATOM   1064  CB  PRO A 196     -31.993  11.067  84.309  1.00 83.32           C  
ANISOU 1064  CB  PRO A 196     9403  12306   9948    700   1002    318       C  
ATOM   1065  CG  PRO A 196     -31.683   9.607  84.523  1.00 87.86           C  
ANISOU 1065  CG  PRO A 196     9967  12870  10548    755   1010    344       C  
ATOM   1066  CD  PRO A 196     -31.727   9.380  86.026  1.00 83.76           C  
ANISOU 1066  CD  PRO A 196     9437  12363  10026    734   1039    386       C  
ATOM   1067  N   LEU A 197     -35.181  10.643  86.063  1.00 82.18           N  
ANISOU 1067  N   LEU A 197     9269  11991   9963    662   1046    309       N  
ATOM   1068  CA  LEU A 197     -36.583  10.352  85.788  1.00 81.88           C  
ANISOU 1068  CA  LEU A 197     9231  11886   9994    664   1041    289       C  
ATOM   1069  C   LEU A 197     -37.460  11.515  86.242  1.00 87.59           C  
ANISOU 1069  C   LEU A 197     9953  12591  10735    633   1065    283       C  
ATOM   1070  O   LEU A 197     -37.069  12.277  87.128  1.00 86.98           O  
ANISOU 1070  O   LEU A 197     9888  12537  10624    600   1097    295       O  
ATOM   1071  CB  LEU A 197     -37.030   9.029  86.437  1.00 81.79           C  
ANISOU 1071  CB  LEU A 197     9222  11839  10015    672   1047    298       C  
ATOM   1072  CG  LEU A 197     -36.281   7.759  86.006  1.00 86.26           C  
ANISOU 1072  CG  LEU A 197     9803  12403  10568    714   1037    306       C  
ATOM   1073  CD1 LEU A 197     -36.454   6.669  87.016  1.00 86.78           C  
ANISOU 1073  CD1 LEU A 197     9881  12443  10647    716   1052    325       C  
ATOM   1074  CD2 LEU A 197     -36.727   7.269  84.643  1.00 87.77           C  
ANISOU 1074  CD2 LEU A 197    10011  12559  10779    728   1017    280       C  
ATOM   1075  N   VAL A 198     -38.625  11.675  85.594  1.00 85.94           N  
ANISOU 1075  N   VAL A 198     9732  12345  10576    640   1054    270       N  
ATOM   1076  CA  VAL A 198     -39.608  12.719  85.894  1.00 86.40           C  
ANISOU 1076  CA  VAL A 198     9784  12380  10662    629   1082    271       C  
ATOM   1077  C   VAL A 198     -40.969  12.050  86.216  1.00 91.67           C  
ANISOU 1077  C   VAL A 198    10427  13017  11388    628   1085    274       C  
ATOM   1078  O   VAL A 198     -41.285  10.984  85.676  1.00 90.88           O  
ANISOU 1078  O   VAL A 198    10317  12911  11301    632   1054    270       O  
ATOM   1079  CB  VAL A 198     -39.691  13.790  84.769  1.00 90.11           C  
ANISOU 1079  CB  VAL A 198    10257  12854  11128    643   1068    266       C  
ATOM   1080  CG1 VAL A 198     -40.221  13.212  83.466  1.00 89.82           C  
ANISOU 1080  CG1 VAL A 198    10193  12813  11121    657   1021    262       C  
ATOM   1081  CG2 VAL A 198     -40.502  15.014  85.193  1.00 90.18           C  
ANISOU 1081  CG2 VAL A 198    10272  12837  11158    643   1113    275       C  
ATOM   1082  N   ARG A 199     -41.734  12.662  87.137  1.00 89.76           N  
ANISOU 1082  N   ARG A 199    10179  12756  11170    615   1127    279       N  
ATOM   1083  CA  ARG A 199     -43.038  12.192  87.592  1.00 90.66           C  
ANISOU 1083  CA  ARG A 199    10264  12852  11330    608   1136    282       C  
ATOM   1084  C   ARG A 199     -44.067  12.250  86.462  1.00 96.20           C  
ANISOU 1084  C   ARG A 199    10927  13561  12062    630   1109    294       C  
ATOM   1085  O   ARG A 199     -44.265  13.300  85.853  1.00 95.89           O  
ANISOU 1085  O   ARG A 199    10877  13523  12033    655   1117    307       O  
ATOM   1086  CB  ARG A 199     -43.505  13.015  88.811  1.00 92.67           C  
ANISOU 1086  CB  ARG A 199    10524  13087  11600    589   1197    284       C  
ATOM   1087  CG  ARG A 199     -44.773  12.503  89.505  1.00107.72           C  
ANISOU 1087  CG  ARG A 199    12399  14983  13547    574   1209    284       C  
ATOM   1088  CD  ARG A 199     -44.517  11.319  90.425  1.00118.20           C  
ANISOU 1088  CD  ARG A 199    13739  16309  14861    531   1197    271       C  
ATOM   1089  NE  ARG A 199     -45.728  10.916  91.146  1.00126.63           N  
ANISOU 1089  NE  ARG A 199    14782  17371  15960    506   1208    264       N  
ATOM   1090  CZ  ARG A 199     -46.632  10.052  90.690  1.00140.82           C  
ANISOU 1090  CZ  ARG A 199    16555  19186  17766    504   1171    264       C  
ATOM   1091  NH1 ARG A 199     -46.476   9.484  89.498  1.00124.77           N  
ANISOU 1091  NH1 ARG A 199    14524  17168  15716    523   1126    270       N  
ATOM   1092  NH2 ARG A 199     -47.695   9.748  91.419  1.00129.69           N  
ANISOU 1092  NH2 ARG A 199    15123  17782  16373    474   1182    257       N  
ATOM   1093  N   THR A 200     -44.702  11.103  86.183  1.00 94.09           N  
ANISOU 1093  N   THR A 200    10644  13303  11803    614   1078    294       N  
ATOM   1094  CA  THR A 200     -45.730  10.958  85.152  1.00 94.83           C  
ANISOU 1094  CA  THR A 200    10697  13421  11913    613   1050    313       C  
ATOM   1095  C   THR A 200     -46.784   9.937  85.592  1.00100.60           C  
ANISOU 1095  C   THR A 200    11412  14165  12645    577   1044    316       C  
ATOM   1096  O   THR A 200     -46.461   8.953  86.260  1.00 99.94           O  
ANISOU 1096  O   THR A 200    11366  14065  12543    552   1042    294       O  
ATOM   1097  CB  THR A 200     -45.116  10.605  83.777  1.00102.58           C  
ANISOU 1097  CB  THR A 200    11692  14413  12870    609   1008    310       C  
ATOM   1098  OG1 THR A 200     -46.159  10.500  82.805  1.00102.01           O  
ANISOU 1098  OG1 THR A 200    11578  14374  12807    589    983    337       O  
ATOM   1099  CG2 THR A 200     -44.270   9.321  83.786  1.00101.16           C  
ANISOU 1099  CG2 THR A 200    11562  14216  12657    591    993    286       C  
ATOM   1100  N   ASP A 201     -48.043  10.185  85.218  1.00 98.91           N  
ANISOU 1100  N   ASP A 201    11142  13989  12449    574   1041    346       N  
ATOM   1101  CA  ASP A 201     -49.148   9.291  85.545  1.00 99.73           C  
ANISOU 1101  CA  ASP A 201    11226  14126  12542    529   1032    352       C  
ATOM   1102  C   ASP A 201     -49.572   8.486  84.302  1.00104.13           C  
ANISOU 1102  C   ASP A 201    11778  14724  13061    483    990    370       C  
ATOM   1103  O   ASP A 201     -50.341   7.533  84.434  1.00104.05           O  
ANISOU 1103  O   ASP A 201    11773  14745  13018    427    978    371       O  
ATOM   1104  CB  ASP A 201     -50.324  10.071  86.157  1.00102.62           C  
ANISOU 1104  CB  ASP A 201    11527  14521  12943    550   1065    380       C  
ATOM   1105  CG  ASP A 201     -50.020  10.670  87.526  1.00117.37           C  
ANISOU 1105  CG  ASP A 201    13414  16343  14839    570   1117    357       C  
ATOM   1106  OD1 ASP A 201     -49.683   9.894  88.458  1.00118.22           O  
ANISOU 1106  OD1 ASP A 201    13562  16427  14930    532   1118    323       O  
ATOM   1107  OD2 ASP A 201     -50.138  11.909  87.674  1.00124.75           O  
ANISOU 1107  OD2 ASP A 201    14328  17263  15807    619   1161    374       O  
ATOM   1108  N   ASN A 202     -49.027   8.834  83.111  1.00100.75           N  
ANISOU 1108  N   ASN A 202    11351  14297  12631    493    969    380       N  
ATOM   1109  CA  ASN A 202     -49.283   8.131  81.847  1.00100.73           C  
ANISOU 1109  CA  ASN A 202    11353  14328  12589    434    935    395       C  
ATOM   1110  C   ASN A 202     -48.513   6.789  81.834  1.00104.90           C  
ANISOU 1110  C   ASN A 202    11972  14812  13072    396    931    353       C  
ATOM   1111  O   ASN A 202     -47.286   6.793  81.990  1.00104.26           O  
ANISOU 1111  O   ASN A 202    11937  14679  12997    434    939    323       O  
ATOM   1112  CB  ASN A 202     -48.907   9.008  80.643  1.00100.70           C  
ANISOU 1112  CB  ASN A 202    11323  14336  12602    453    915    416       C  
ATOM   1113  CG  ASN A 202     -49.117   8.362  79.288  1.00120.35           C  
ANISOU 1113  CG  ASN A 202    13818  16861  15051    377    883    433       C  
ATOM   1114  OD1 ASN A 202     -48.172   8.187  78.508  1.00112.00           O  
ANISOU 1114  OD1 ASN A 202    12804  15771  13978    366    870    408       O  
ATOM   1115  ND2 ASN A 202     -50.357   8.008  78.965  1.00112.92           N  
ANISOU 1115  ND2 ASN A 202    12830  15991  14083    316    872    478       N  
ATOM   1116  N   PRO A 203     -49.216   5.638  81.667  1.00102.18           N  
ANISOU 1116  N   PRO A 203    11658  14490  12675    320    924    355       N  
ATOM   1117  CA  PRO A 203     -48.530   4.328  81.727  1.00102.24           C  
ANISOU 1117  CA  PRO A 203    11767  14442  12637    290    933    317       C  
ATOM   1118  C   PRO A 203     -47.635   3.988  80.531  1.00106.19           C  
ANISOU 1118  C   PRO A 203    12321  14911  13117    278    930    305       C  
ATOM   1119  O   PRO A 203     -46.778   3.111  80.650  1.00105.34           O  
ANISOU 1119  O   PRO A 203    12296  14742  12986    287    949    275       O  
ATOM   1120  CB  PRO A 203     -49.686   3.322  81.814  1.00104.58           C  
ANISOU 1120  CB  PRO A 203    12088  14779  12871    199    930    326       C  
ATOM   1121  CG  PRO A 203     -50.909   4.133  82.144  1.00109.11           C  
ANISOU 1121  CG  PRO A 203    12559  15433  13467    197    920    366       C  
ATOM   1122  CD  PRO A 203     -50.673   5.463  81.512  1.00104.31           C  
ANISOU 1122  CD  PRO A 203    11877  14841  12917    257    913    395       C  
ATOM   1123  N   LYS A 204     -47.835   4.662  79.390  1.00103.84           N  
ANISOU 1123  N   LYS A 204    11974  14654  12826    257    909    331       N  
ATOM   1124  CA  LYS A 204     -47.059   4.434  78.168  1.00104.40           C  
ANISOU 1124  CA  LYS A 204    12088  14702  12879    232    904    318       C  
ATOM   1125  C   LYS A 204     -45.641   5.034  78.273  1.00108.48           C  
ANISOU 1125  C   LYS A 204    12613  15172  13432    319    908    290       C  
ATOM   1126  O   LYS A 204     -44.752   4.649  77.505  1.00107.96           O  
ANISOU 1126  O   LYS A 204    12598  15074  13349    313    913    267       O  
ATOM   1127  CB  LYS A 204     -47.794   5.022  76.946  1.00107.99           C  
ANISOU 1127  CB  LYS A 204    12478  15224  13328    170    875    361       C  
ATOM   1128  CG  LYS A 204     -49.155   4.377  76.660  1.00133.01           C  
ANISOU 1128  CG  LYS A 204    15635  18462  16441     63    870    400       C  
ATOM   1129  CD  LYS A 204     -49.757   4.802  75.313  1.00148.70           C  
ANISOU 1129  CD  LYS A 204    17564  20523  18411    -17    841    451       C  
ATOM   1130  CE  LYS A 204     -50.604   6.054  75.386  1.00163.15           C  
ANISOU 1130  CE  LYS A 204    19267  22432  20289     24    816    512       C  
ATOM   1131  NZ  LYS A 204     -49.801   7.283  75.148  1.00172.81           N  
ANISOU 1131  NZ  LYS A 204    20454  23625  21579    112    802    506       N  
ATOM   1132  N   SER A 205     -45.440   5.967  79.226  1.00105.20           N  
ANISOU 1132  N   SER A 205    12152  14759  13060    392    910    292       N  
ATOM   1133  CA  SER A 205     -44.187   6.689  79.445  1.00104.81           C  
ANISOU 1133  CA  SER A 205    12104  14687  13032    462    913    273       C  
ATOM   1134  C   SER A 205     -43.310   6.090  80.575  1.00107.94           C  
ANISOU 1134  C   SER A 205    12547  15043  13422    507    940    252       C  
ATOM   1135  O   SER A 205     -42.149   6.485  80.698  1.00107.12           O  
ANISOU 1135  O   SER A 205    12451  14932  13319    554    944    240       O  
ATOM   1136  CB  SER A 205     -44.489   8.155  79.760  1.00108.87           C  
ANISOU 1136  CB  SER A 205    12551  15230  13585    500    907    294       C  
ATOM   1137  OG  SER A 205     -45.339   8.750  78.792  1.00118.26           O  
ANISOU 1137  OG  SER A 205    13687  16461  14785    468    883    326       O  
ATOM   1138  N   TRP A 206     -43.850   5.154  81.386  1.00104.34           N  
ANISOU 1138  N   TRP A 206    12121  14569  12953    487    956    250       N  
ATOM   1139  CA  TRP A 206     -43.141   4.554  82.530  1.00103.67           C  
ANISOU 1139  CA  TRP A 206    12077  14450  12864    523    979    239       C  
ATOM   1140  C   TRP A 206     -41.932   3.724  82.127  1.00107.57           C  
ANISOU 1140  C   TRP A 206    12633  14906  13332    554    994    227       C  
ATOM   1141  O   TRP A 206     -42.029   2.878  81.240  1.00107.66           O  
ANISOU 1141  O   TRP A 206    12698  14893  13316    521   1002    218       O  
ATOM   1142  CB  TRP A 206     -44.077   3.696  83.392  1.00102.46           C  
ANISOU 1142  CB  TRP A 206    11947  14286  12698    484    987    239       C  
ATOM   1143  CG  TRP A 206     -45.204   4.439  84.039  1.00103.24           C  
ANISOU 1143  CG  TRP A 206    11981  14423  12822    465    981    251       C  
ATOM   1144  CD1 TRP A 206     -45.283   5.780  84.287  1.00105.90           C  
ANISOU 1144  CD1 TRP A 206    12253  14786  13199    496    982    264       C  
ATOM   1145  CD2 TRP A 206     -46.391   3.862  84.570  1.00103.35           C  
ANISOU 1145  CD2 TRP A 206    11996  14452  12819    411    979    253       C  
ATOM   1146  NE1 TRP A 206     -46.472   6.077  84.903  1.00105.52           N  
ANISOU 1146  NE1 TRP A 206    12160  14765  13166    473    986    275       N  
ATOM   1147  CE2 TRP A 206     -47.170   4.917  85.096  1.00107.17           C  
ANISOU 1147  CE2 TRP A 206    12404  14976  13341    420    980    268       C  
ATOM   1148  CE3 TRP A 206     -46.893   2.551  84.623  1.00104.92           C  
ANISOU 1148  CE3 TRP A 206    12261  14638  12967    353    980    242       C  
ATOM   1149  CZ2 TRP A 206     -48.417   4.701  85.677  1.00106.64           C  
ANISOU 1149  CZ2 TRP A 206    12310  14942  13265    376    979    275       C  
ATOM   1150  CZ3 TRP A 206     -48.131   2.338  85.199  1.00106.59           C  
ANISOU 1150  CZ3 TRP A 206    12452  14887  13161    299    974    245       C  
ATOM   1151  CH2 TRP A 206     -48.886   3.406  85.704  1.00107.10           C  
ANISOU 1151  CH2 TRP A 206    12427  15000  13268    311    971    262       C  
ATOM   1152  N   TYR A 207     -40.801   3.970  82.806  1.00104.18           N  
ANISOU 1152  N   TYR A 207    12199  14478  12908    612   1005    232       N  
ATOM   1153  CA  TYR A 207     -39.518   3.313  82.587  1.00104.48           C  
ANISOU 1153  CA  TYR A 207    12279  14495  12925    662   1024    232       C  
ATOM   1154  C   TYR A 207     -39.469   1.921  83.265  1.00108.55           C  
ANISOU 1154  C   TYR A 207    12862  14960  13423    673   1053    237       C  
ATOM   1155  O   TYR A 207     -39.321   1.825  84.482  1.00107.39           O  
ANISOU 1155  O   TYR A 207    12705  14815  13282    691   1059    253       O  
ATOM   1156  CB  TYR A 207     -38.374   4.222  83.081  1.00105.84           C  
ANISOU 1156  CB  TYR A 207    12407  14711  13098    711   1021    246       C  
ATOM   1157  CG  TYR A 207     -37.008   3.575  83.054  1.00108.89           C  
ANISOU 1157  CG  TYR A 207    12819  15096  13459    771   1043    260       C  
ATOM   1158  CD1 TYR A 207     -36.368   3.303  81.848  1.00111.30           C  
ANISOU 1158  CD1 TYR A 207    13148  15393  13747    791   1047    246       C  
ATOM   1159  CD2 TYR A 207     -36.339   3.263  84.234  1.00110.07           C  
ANISOU 1159  CD2 TYR A 207    12963  15259  13600    808   1060    292       C  
ATOM   1160  CE1 TYR A 207     -35.108   2.712  81.814  1.00112.55           C  
ANISOU 1160  CE1 TYR A 207    13325  15556  13884    858   1074    264       C  
ATOM   1161  CE2 TYR A 207     -35.073   2.676  84.213  1.00111.48           C  
ANISOU 1161  CE2 TYR A 207    13154  15449  13755    874   1082    318       C  
ATOM   1162  CZ  TYR A 207     -34.461   2.404  82.998  1.00119.44           C  
ANISOU 1162  CZ  TYR A 207    14185  16449  14748    905   1091    305       C  
ATOM   1163  OH  TYR A 207     -33.213   1.829  82.947  1.00121.44           O  
ANISOU 1163  OH  TYR A 207    14445  16717  14978    980   1119    335       O  
ATOM   1164  N   GLU A 208     -39.522   0.854  82.442  1.00106.66           N  
ANISOU 1164  N   GLU A 208    12699  14671  13157    660   1076    225       N  
ATOM   1165  CA  GLU A 208     -39.494  -0.579  82.790  1.00107.44           C  
ANISOU 1165  CA  GLU A 208    12890  14704  13227    668   1114    227       C  
ATOM   1166  C   GLU A 208     -40.247  -0.883  84.121  1.00111.72           C  
ANISOU 1166  C   GLU A 208    13434  15242  13772    642   1106    233       C  
ATOM   1167  O   GLU A 208     -41.422  -0.520  84.215  1.00111.61           O  
ANISOU 1167  O   GLU A 208    13392  15253  13760    574   1082    222       O  
ATOM   1168  CB  GLU A 208     -38.066  -1.180  82.775  1.00109.27           C  
ANISOU 1168  CB  GLU A 208    13158  14908  13451    759   1152    245       C  
ATOM   1169  CG  GLU A 208     -36.974  -0.403  83.494  1.00121.27           C  
ANISOU 1169  CG  GLU A 208    14600  16488  14991    827   1139    276       C  
ATOM   1170  CD  GLU A 208     -35.568  -0.915  83.250  1.00144.92           C  
ANISOU 1170  CD  GLU A 208    17613  19477  17971    918   1175    302       C  
ATOM   1171  OE1 GLU A 208     -34.920  -1.340  84.234  1.00140.74           O  
ANISOU 1171  OE1 GLU A 208    17079  18954  17440    975   1192    344       O  
ATOM   1172  OE2 GLU A 208     -35.117  -0.901  82.081  1.00137.14           O  
ANISOU 1172  OE2 GLU A 208    16645  18486  16977    931   1188    285       O  
ATOM   1173  N   ASP A 209     -39.606  -1.542  85.121  1.00108.17           N  
ANISOU 1173  N   ASP A 209    13013  14766  13320    691   1126    254       N  
ATOM   1174  CA  ASP A 209     -40.251  -1.930  86.391  1.00107.86           C  
ANISOU 1174  CA  ASP A 209    12984  14718  13280    659   1118    257       C  
ATOM   1175  C   ASP A 209     -40.597  -0.721  87.293  1.00110.49           C  
ANISOU 1175  C   ASP A 209    13217  15114  13649    635   1085    262       C  
ATOM   1176  O   ASP A 209     -41.490  -0.840  88.142  1.00110.87           O  
ANISOU 1176  O   ASP A 209    13264  15164  13699    582   1073    252       O  
ATOM   1177  CB  ASP A 209     -39.401  -2.964  87.176  1.00110.14           C  
ANISOU 1177  CB  ASP A 209    13330  14962  13557    719   1148    286       C  
ATOM   1178  CG  ASP A 209     -37.894  -2.744  87.180  1.00121.57           C  
ANISOU 1178  CG  ASP A 209    14739  16433  15017    815   1166    327       C  
ATOM   1179  OD1 ASP A 209     -37.460  -1.580  87.004  1.00122.02           O  
ANISOU 1179  OD1 ASP A 209    14710  16557  15094    825   1145    333       O  
ATOM   1180  OD2 ASP A 209     -37.150  -3.724  87.426  1.00128.26           O  
ANISOU 1180  OD2 ASP A 209    15644  17239  15852    879   1201    359       O  
ATOM   1181  N   VAL A 210     -39.921   0.436  87.082  1.00104.60           N  
ANISOU 1181  N   VAL A 210    12398  14418  12926    668   1076    273       N  
ATOM   1182  CA  VAL A 210     -40.144   1.679  87.835  1.00102.79           C  
ANISOU 1182  CA  VAL A 210    12091  14240  12725    645   1060    278       C  
ATOM   1183  C   VAL A 210     -41.408   2.367  87.274  1.00105.71           C  
ANISOU 1183  C   VAL A 210    12430  14625  13109    595   1042    254       C  
ATOM   1184  O   VAL A 210     -41.331   3.102  86.288  1.00105.57           O  
ANISOU 1184  O   VAL A 210    12385  14629  13098    604   1033    250       O  
ATOM   1185  CB  VAL A 210     -38.893   2.607  87.810  1.00105.54           C  
ANISOU 1185  CB  VAL A 210    12391  14637  13074    691   1063    301       C  
ATOM   1186  CG1 VAL A 210     -39.108   3.840  88.669  1.00104.61           C  
ANISOU 1186  CG1 VAL A 210    12215  14561  12972    656   1061    306       C  
ATOM   1187  CG2 VAL A 210     -37.644   1.871  88.273  1.00105.53           C  
ANISOU 1187  CG2 VAL A 210    12407  14637  13052    746   1081    339       C  
ATOM   1188  N   GLU A 211     -42.568   2.107  87.891  1.00101.44           N  
ANISOU 1188  N   GLU A 211    11891  14080  12571    541   1036    242       N  
ATOM   1189  CA  GLU A 211     -43.842   2.684  87.459  1.00100.97           C  
ANISOU 1189  CA  GLU A 211    11792  14049  12522    496   1022    232       C  
ATOM   1190  C   GLU A 211     -44.073   4.031  88.140  1.00102.70           C  
ANISOU 1190  C   GLU A 211    11940  14302  12780    500   1027    238       C  
ATOM   1191  O   GLU A 211     -43.781   4.191  89.323  1.00101.77           O  
ANISOU 1191  O   GLU A 211    11815  14181  12674    495   1041    241       O  
ATOM   1192  CB  GLU A 211     -45.007   1.724  87.728  1.00102.92           C  
ANISOU 1192  CB  GLU A 211    12077  14289  12740    432   1016    218       C  
ATOM   1193  CG  GLU A 211     -44.933   0.435  86.927  1.00116.03           C  
ANISOU 1193  CG  GLU A 211    13828  15910  14348    414   1022    210       C  
ATOM   1194  CD  GLU A 211     -45.894  -0.670  87.326  1.00142.66           C  
ANISOU 1194  CD  GLU A 211    17263  19270  17671    342   1020    195       C  
ATOM   1195  OE1 GLU A 211     -46.907  -0.392  88.011  1.00133.02           O  
ANISOU 1195  OE1 GLU A 211    16000  18088  16453    295   1005    189       O  
ATOM   1196  OE2 GLU A 211     -45.636  -1.826  86.921  1.00143.63           O  
ANISOU 1196  OE2 GLU A 211    17485  19342  17744    330   1038    187       O  
ATOM   1197  N   GLY A 212     -44.579   4.987  87.373  1.00 98.44           N  
ANISOU 1197  N   GLY A 212    11354  13791  12259    504   1021    244       N  
ATOM   1198  CA  GLY A 212     -44.819   6.345  87.840  1.00 97.80           C  
ANISOU 1198  CA  GLY A 212    11217  13731  12212    515   1038    252       C  
ATOM   1199  C   GLY A 212     -43.714   7.297  87.428  1.00100.78           C  
ANISOU 1199  C   GLY A 212    11587  14113  12590    556   1044    259       C  
ATOM   1200  O   GLY A 212     -43.864   8.514  87.568  1.00100.87           O  
ANISOU 1200  O   GLY A 212    11569  14137  12621    566   1063    266       O  
ATOM   1201  N   CYS A 213     -42.601   6.747  86.901  1.00 95.61           N  
ANISOU 1201  N   CYS A 213    10967  13451  11908    579   1033    258       N  
ATOM   1202  CA  CYS A 213     -41.429   7.500  86.460  1.00 94.60           C  
ANISOU 1202  CA  CYS A 213    10836  13341  11765    612   1034    263       C  
ATOM   1203  C   CYS A 213     -41.128   7.258  84.987  1.00 98.10           C  
ANISOU 1203  C   CYS A 213    11292  13787  12196    627   1010    256       C  
ATOM   1204  O   CYS A 213     -41.161   6.119  84.526  1.00 98.76           O  
ANISOU 1204  O   CYS A 213    11409  13847  12266    622   1003    250       O  
ATOM   1205  CB  CYS A 213     -40.219   7.150  87.319  1.00 94.73           C  
ANISOU 1205  CB  CYS A 213    10871  13365  11756    625   1048    275       C  
ATOM   1206  SG  CYS A 213     -40.381   7.606  89.061  1.00 98.52           S  
ANISOU 1206  SG  CYS A 213    11339  13851  12243    585   1080    285       S  
ATOM   1207  N   GLY A 214     -40.779   8.327  84.286  1.00 92.81           N  
ANISOU 1207  N   GLY A 214    10601  13139  11523    639   1001    256       N  
ATOM   1208  CA  GLY A 214     -40.401   8.284  82.882  1.00 92.02           C  
ANISOU 1208  CA  GLY A 214    10507  13045  11410    643    976    246       C  
ATOM   1209  C   GLY A 214     -39.128   9.068  82.649  1.00 94.47           C  
ANISOU 1209  C   GLY A 214    10819  13385  11690    667    972    242       C  
ATOM   1210  O   GLY A 214     -38.885  10.048  83.359  1.00 94.57           O  
ANISOU 1210  O   GLY A 214    10822  13417  11694    668    988    250       O  
ATOM   1211  N   ILE A 215     -38.292   8.641  81.673  1.00 88.89           N  
ANISOU 1211  N   ILE A 215    10131  12686  10959    679    956    230       N  
ATOM   1212  CA  ILE A 215     -37.025   9.326  81.370  1.00 87.71           C  
ANISOU 1212  CA  ILE A 215     9980  12578  10767    696    948    225       C  
ATOM   1213  C   ILE A 215     -37.338  10.732  80.866  1.00 90.95           C  
ANISOU 1213  C   ILE A 215    10373  13006  11178    675    930    218       C  
ATOM   1214  O   ILE A 215     -38.178  10.873  79.988  1.00 89.41           O  
ANISOU 1214  O   ILE A 215    10165  12795  11011    655    909    214       O  
ATOM   1215  CB  ILE A 215     -36.120   8.540  80.371  1.00 90.58           C  
ANISOU 1215  CB  ILE A 215    10364  12944  11107    714    938    211       C  
ATOM   1216  CG1 ILE A 215     -36.096   7.019  80.682  1.00 91.36           C  
ANISOU 1216  CG1 ILE A 215    10497  13002  11214    738    965    220       C  
ATOM   1217  CG2 ILE A 215     -34.695   9.127  80.351  1.00 90.31           C  
ANISOU 1217  CG2 ILE A 215    10324  12973  11018    735    934    212       C  
ATOM   1218  CD1 ILE A 215     -35.765   6.118  79.497  1.00 97.88           C  
ANISOU 1218  CD1 ILE A 215    11360  13799  12032    741    969    201       C  
ATOM   1219  N   GLN A 216     -36.691  11.764  81.445  1.00 89.36           N  
ANISOU 1219  N   GLN A 216    10174  12839  10939    674    942    223       N  
ATOM   1220  CA  GLN A 216     -36.894  13.174  81.080  1.00 90.53           C  
ANISOU 1220  CA  GLN A 216    10325  12997  11076    658    935    217       C  
ATOM   1221  C   GLN A 216     -36.605  13.402  79.593  1.00 99.03           C  
ANISOU 1221  C   GLN A 216    11400  14087  12140    647    891    196       C  
ATOM   1222  O   GLN A 216     -35.782  12.692  79.013  1.00 99.18           O  
ANISOU 1222  O   GLN A 216    11424  14125  12135    652    873    181       O  
ATOM   1223  CB  GLN A 216     -36.053  14.126  81.959  1.00 91.72           C  
ANISOU 1223  CB  GLN A 216    10501  13186  11164    643    964    223       C  
ATOM   1224  CG  GLN A 216     -34.533  13.924  81.894  1.00101.81           C  
ANISOU 1224  CG  GLN A 216    11787  14530  12365    641    952    221       C  
ATOM   1225  CD  GLN A 216     -33.727  14.938  82.678  1.00115.98           C  
ANISOU 1225  CD  GLN A 216    13610  16379  14078    604    979    232       C  
ATOM   1226  OE1 GLN A 216     -34.207  16.003  83.083  1.00111.44           O  
ANISOU 1226  OE1 GLN A 216    13066  15783  13495    577   1008    232       O  
ATOM   1227  NE2 GLN A 216     -32.451  14.644  82.868  1.00106.05           N  
ANISOU 1227  NE2 GLN A 216    12347  15197  12748    599    975    245       N  
ATOM   1228  N   CYS A 217     -37.302  14.383  78.984  1.00103.91           N  
ANISOU 1228  N   CYS A 217    12812  16557  10114   1957   1152   1672       N  
ATOM   1229  CA  CYS A 217     -37.213  14.725  77.561  1.00104.65           C  
ANISOU 1229  CA  CYS A 217    12867  16642  10252   1970   1133   1667       C  
ATOM   1230  C   CYS A 217     -35.782  15.066  77.128  1.00105.44           C  
ANISOU 1230  C   CYS A 217    13199  16376  10487   1832   1057   1548       C  
ATOM   1231  O   CYS A 217     -35.330  14.557  76.097  1.00103.86           O  
ANISOU 1231  O   CYS A 217    12893  16159  10411   1654    984   1518       O  
ATOM   1232  CB  CYS A 217     -38.172  15.857  77.216  1.00108.28           C  
ANISOU 1232  CB  CYS A 217    13354  17262  10525   2337   1248   1754       C  
ATOM   1233  SG  CYS A 217     -38.029  16.429  75.509  1.00113.04           S  
ANISOU 1233  SG  CYS A 217    13952  17840  11158   2390   1232   1762       S  
ATOM   1234  N   GLN A 218     -35.091  15.941  77.886  1.00101.02           N  
ANISOU 1234  N   GLN A 218    12951  15548   9884   1906   1076   1482       N  
ATOM   1235  CA  GLN A 218     -33.710  16.325  77.590  1.00 99.03           C  
ANISOU 1235  CA  GLN A 218    12912  14987   9728   1744   1004   1376       C  
ATOM   1236  C   GLN A 218     -32.791  15.154  77.931  1.00 98.69           C  
ANISOU 1236  C   GLN A 218    12764  14898   9837   1453    893   1318       C  
ATOM   1237  O   GLN A 218     -32.843  14.654  79.055  1.00 97.37           O  
ANISOU 1237  O   GLN A 218    12585  14760   9649   1421    887   1321       O  
ATOM   1238  CB  GLN A 218     -33.313  17.594  78.363  1.00101.59           C  
ANISOU 1238  CB  GLN A 218    13614  15058   9927   1873   1057   1321       C  
ATOM   1239  CG  GLN A 218     -32.157  18.350  77.734  1.00113.58           C  
ANISOU 1239  CG  GLN A 218    15367  16301  11487   1741   1012   1243       C  
ATOM   1240  CD  GLN A 218     -31.370  19.097  78.772  1.00133.25           C  
ANISOU 1240  CD  GLN A 218    18197  18538  13896   1682   1007   1151       C  
ATOM   1241  OE1 GLN A 218     -30.485  18.542  79.431  1.00127.53           O  
ANISOU 1241  OE1 GLN A 218    17446  17774  13235   1456    919   1086       O  
ATOM   1242  NE2 GLN A 218     -31.687  20.369  78.953  1.00127.77           N  
ANISOU 1242  NE2 GLN A 218    17841  17669  13037   1890   1104   1146       N  
ATOM   1243  N   ASN A 219     -31.994  14.696  76.947  1.00 93.39           N  
ANISOU 1243  N   ASN A 219    12011  14172   9301   1269    813   1276       N  
ATOM   1244  CA  ASN A 219     -31.068  13.570  77.060  1.00 91.61           C  
ANISOU 1244  CA  ASN A 219    11689  13907   9212   1037    714   1227       C  
ATOM   1245  C   ASN A 219     -30.224  13.685  78.338  1.00 95.07           C  
ANISOU 1245  C   ASN A 219    12288  14208   9625    977    680   1176       C  
ATOM   1246  O   ASN A 219     -29.432  14.625  78.466  1.00 95.05           O  
ANISOU 1246  O   ASN A 219    12491  14044   9579    955    668   1116       O  
ATOM   1247  CB  ASN A 219     -30.174  13.478  75.823  1.00 91.59           C  
ANISOU 1247  CB  ASN A 219    11649  13837   9313    909    653   1177       C  
ATOM   1248  CG  ASN A 219     -29.661  12.091  75.523  1.00120.79           C  
ANISOU 1248  CG  ASN A 219    15182  17573  13139    740    576   1155       C  
ATOM   1249  OD1 ASN A 219     -29.397  11.273  76.417  1.00116.30           O  
ANISOU 1249  OD1 ASN A 219    14596  16992  12600    674    542   1154       O  
ATOM   1250  ND2 ASN A 219     -29.475  11.805  74.244  1.00115.07           N  
ANISOU 1250  ND2 ASN A 219    14356  16883  12481    680    551   1136       N  
ATOM   1251  N   PRO A 220     -30.446  12.780  79.326  1.00 90.74           N  
ANISOU 1251  N   PRO A 220    11661  13734   9081    942    667   1207       N  
ATOM   1252  CA  PRO A 220     -29.709  12.882  80.601  1.00 90.14           C  
ANISOU 1252  CA  PRO A 220    11727  13566   8959    899    633   1168       C  
ATOM   1253  C   PRO A 220     -28.222  12.551  80.493  1.00 91.41           C  
ANISOU 1253  C   PRO A 220    11897  13632   9202    723    529   1103       C  
ATOM   1254  O   PRO A 220     -27.450  12.985  81.347  1.00 92.46           O  
ANISOU 1254  O   PRO A 220    12167  13695   9269    674    494   1057       O  
ATOM   1255  CB  PRO A 220     -30.410  11.870  81.497  1.00 92.16           C  
ANISOU 1255  CB  PRO A 220    11863  13952   9201    907    650   1241       C  
ATOM   1256  CG  PRO A 220     -31.025  10.896  80.579  1.00 96.39           C  
ANISOU 1256  CG  PRO A 220    12189  14606   9828    848    649   1294       C  
ATOM   1257  CD  PRO A 220     -31.391  11.645  79.338  1.00 92.14           C  
ANISOU 1257  CD  PRO A 220    11630  14092   9288    921    683   1284       C  
ATOM   1258  N   LEU A 221     -27.828  11.798  79.447  1.00 84.32           N  
ANISOU 1258  N   LEU A 221    10851  12758   8429    636    482   1100       N  
ATOM   1259  CA  LEU A 221     -26.445  11.393  79.196  1.00 82.68           C  
ANISOU 1259  CA  LEU A 221    10610  12514   8291    507    393   1053       C  
ATOM   1260  C   LEU A 221     -25.557  12.545  78.738  1.00 84.40           C  
ANISOU 1260  C   LEU A 221    10945  12656   8468    438    371    989       C  
ATOM   1261  O   LEU A 221     -24.346  12.370  78.685  1.00 83.38           O  
ANISOU 1261  O   LEU A 221    10779  12541   8358    323    298    955       O  
ATOM   1262  CB  LEU A 221     -26.394  10.286  78.130  1.00 82.15           C  
ANISOU 1262  CB  LEU A 221    10376  12492   8346    467    369   1064       C  
ATOM   1263  CG  LEU A 221     -27.076   8.965  78.444  1.00 87.38           C  
ANISOU 1263  CG  LEU A 221    10948  13200   9053    469    377   1121       C  
ATOM   1264  CD1 LEU A 221     -27.182   8.125  77.192  1.00 87.25           C  
ANISOU 1264  CD1 LEU A 221    10824  13199   9129    422    368   1111       C  
ATOM   1265  CD2 LEU A 221     -26.334   8.192  79.534  1.00 90.81           C  
ANISOU 1265  CD2 LEU A 221    11407  13612   9484    449    327   1140       C  
ATOM   1266  N   PHE A 222     -26.137  13.697  78.370  1.00 80.60           N  
ANISOU 1266  N   PHE A 222    10601  12105   7918    507    437    984       N  
ATOM   1267  CA  PHE A 222     -25.372  14.834  77.861  1.00 80.55           C  
ANISOU 1267  CA  PHE A 222    10748  11996   7862    418    427    933       C  
ATOM   1268  C   PHE A 222     -25.799  16.146  78.508  1.00 84.91           C  
ANISOU 1268  C   PHE A 222    11591  12408   8265    491    494    914       C  
ATOM   1269  O   PHE A 222     -26.984  16.349  78.778  1.00 84.57           O  
ANISOU 1269  O   PHE A 222    11595  12369   8168    686    578    956       O  
ATOM   1270  CB  PHE A 222     -25.514  14.930  76.332  1.00 82.06           C  
ANISOU 1270  CB  PHE A 222    10853  12206   8121    428    447    950       C  
ATOM   1271  CG  PHE A 222     -25.127  13.673  75.588  1.00 82.87           C  
ANISOU 1271  CG  PHE A 222    10709  12426   8353    372    393    954       C  
ATOM   1272  CD1 PHE A 222     -23.795  13.377  75.335  1.00 86.02           C  
ANISOU 1272  CD1 PHE A 222    11035  12863   8787    232    318    917       C  
ATOM   1273  CD2 PHE A 222     -26.095  12.776  75.155  1.00 85.09           C  
ANISOU 1273  CD2 PHE A 222    10839  12794   8699    457    420    995       C  
ATOM   1274  CE1 PHE A 222     -23.435  12.203  74.669  1.00 86.44           C  
ANISOU 1274  CE1 PHE A 222    10895  13011   8940    224    280    917       C  
ATOM   1275  CE2 PHE A 222     -25.733  11.602  74.486  1.00 87.67           C  
ANISOU 1275  CE2 PHE A 222    10995  13189   9126    402    375    985       C  
ATOM   1276  CZ  PHE A 222     -24.405  11.330  74.240  1.00 85.47           C  
ANISOU 1276  CZ  PHE A 222    10673  12918   8882    309    311    944       C  
ATOM   1277  N   THR A 223     -24.819  17.037  78.744  1.00 82.70           N  
ANISOU 1277  N   THR A 223    11510  12011   7900    330    458    850       N  
ATOM   1278  CA  THR A 223     -25.015  18.356  79.360  1.00 84.85           C  
ANISOU 1278  CA  THR A 223    12137  12094   8008    359    516    808       C  
ATOM   1279  C   THR A 223     -25.648  19.347  78.370  1.00 90.47           C  
ANISOU 1279  C   THR A 223    13026  12669   8680    488    609    837       C  
ATOM   1280  O   THR A 223     -25.652  19.083  77.164  1.00 89.21           O  
ANISOU 1280  O   THR A 223    12702  12576   8618    486    605    878       O  
ATOM   1281  CB  THR A 223     -23.676  18.904  79.886  1.00 97.16           C  
ANISOU 1281  CB  THR A 223    13851  13588   9477     78    435    727       C  
ATOM   1282  OG1 THR A 223     -22.752  19.031  78.806  1.00100.95           O  
ANISOU 1282  OG1 THR A 223    14251  14094  10011   -115    385    723       O  
ATOM   1283  CG2 THR A 223     -23.073  18.040  80.984  1.00 95.97           C  
ANISOU 1283  CG2 THR A 223    13548  13590   9326    -15    347    708       C  
ATOM   1284  N   GLU A 224     -26.162  20.493  78.882  1.00 90.00           N  
ANISOU 1284  N   GLU A 224    13321  12414   8460    615    695    817       N  
ATOM   1285  CA  GLU A 224     -26.766  21.561  78.070  1.00 91.98           C  
ANISOU 1285  CA  GLU A 224    13813  12502   8635    782    797    854       C  
ATOM   1286  C   GLU A 224     -25.697  22.187  77.140  1.00 97.93           C  
ANISOU 1286  C   GLU A 224    14688  13126   9396    523    754    829       C  
ATOM   1287  O   GLU A 224     -26.011  22.567  76.004  1.00 97.30           O  
ANISOU 1287  O   GLU A 224    14626  13011   9334    614    804    891       O  
ATOM   1288  CB  GLU A 224     -27.443  22.625  78.966  1.00 95.72           C  
ANISOU 1288  CB  GLU A 224    14691  12769   8910    992    904    829       C  
ATOM   1289  CG  GLU A 224     -27.891  23.906  78.262  1.00110.58           C  
ANISOU 1289  CG  GLU A 224    16933  14413  10671   1170   1016    863       C  
ATOM   1290  CD  GLU A 224     -29.108  23.865  77.351  1.00140.96           C  
ANISOU 1290  CD  GLU A 224    20632  18390  14535   1518   1111    986       C  
ATOM   1291  OE1 GLU A 224     -29.933  24.801  77.439  1.00145.95           O  
ANISOU 1291  OE1 GLU A 224    21566  18881  15006   1832   1237   1025       O  
ATOM   1292  OE2 GLU A 224     -29.208  22.948  76.504  1.00136.32           O  
ANISOU 1292  OE2 GLU A 224    19649  18043  14102   1481   1060   1044       O  
ATOM   1293  N   ALA A 225     -24.432  22.249  77.616  1.00 95.91           N  
ANISOU 1293  N   ALA A 225    14484  12842   9115    193    658    750       N  
ATOM   1294  CA  ALA A 225     -23.286  22.745  76.854  1.00 96.71           C  
ANISOU 1294  CA  ALA A 225    14653  12886   9208   -115    604    729       C  
ATOM   1295  C   ALA A 225     -23.072  21.878  75.619  1.00 99.94           C  
ANISOU 1295  C   ALA A 225    14676  13513   9785   -130    564    791       C  
ATOM   1296  O   ALA A 225     -22.846  22.413  74.534  1.00100.33           O  
ANISOU 1296  O   ALA A 225    14789  13499   9831   -195    587    826       O  
ATOM   1297  CB  ALA A 225     -22.039  22.749  77.723  1.00 98.28           C  
ANISOU 1297  CB  ALA A 225    14881  13124   9337   -459    497    643       C  
ATOM   1298  N   GLU A 226     -23.209  20.546  75.783  1.00 95.23           N  
ANISOU 1298  N   GLU A 226    13709  13154   9321    -55    513    806       N  
ATOM   1299  CA  GLU A 226     -23.081  19.556  74.712  1.00 93.84           C  
ANISOU 1299  CA  GLU A 226    13179  13180   9297    -44    478    850       C  
ATOM   1300  C   GLU A 226     -24.301  19.586  73.790  1.00 99.38           C  
ANISOU 1300  C   GLU A 226    13840  13882  10036    214    564    921       C  
ATOM   1301  O   GLU A 226     -24.160  19.331  72.590  1.00 97.73           O  
ANISOU 1301  O   GLU A 226    13470  13763   9899    194    557    953       O  
ATOM   1302  CB  GLU A 226     -22.877  18.158  75.296  1.00 93.68           C  
ANISOU 1302  CB  GLU A 226    12857  13361   9378    -39    406    840       C  
ATOM   1303  CG  GLU A 226     -21.479  17.974  75.856  1.00106.08           C  
ANISOU 1303  CG  GLU A 226    14367  15022  10916   -291    306    791       C  
ATOM   1304  CD  GLU A 226     -21.254  16.763  76.736  1.00131.38           C  
ANISOU 1304  CD  GLU A 226    17359  18386  14174   -258    242    789       C  
ATOM   1305  OE1 GLU A 226     -22.205  16.322  77.421  1.00127.53           O  
ANISOU 1305  OE1 GLU A 226    16875  17877  13704    -82    280    809       O  
ATOM   1306  OE2 GLU A 226     -20.096  16.291  76.784  1.00130.03           O  
ANISOU 1306  OE2 GLU A 226    17023  18375  14008   -408    158    777       O  
ATOM   1307  N   HIS A 227     -25.487  19.916  74.347  1.00 98.83           N  
ANISOU 1307  N   HIS A 227    13908  13744   9899    461    648    950       N  
ATOM   1308  CA  HIS A 227     -26.743  20.038  73.604  1.00 99.80           C  
ANISOU 1308  CA  HIS A 227    13988  13915  10015    733    736   1032       C  
ATOM   1309  C   HIS A 227     -26.647  21.186  72.596  1.00106.45           C  
ANISOU 1309  C   HIS A 227    15060  14603  10784    749    791   1069       C  
ATOM   1310  O   HIS A 227     -26.852  20.955  71.405  1.00105.35           O  
ANISOU 1310  O   HIS A 227    14748  14578  10700    791    796   1123       O  
ATOM   1311  CB  HIS A 227     -27.932  20.254  74.560  1.00101.74           C  
ANISOU 1311  CB  HIS A 227    14341  14152  10164   1001    819   1061       C  
ATOM   1312  CG  HIS A 227     -28.600  18.994  75.008  1.00104.07           C  
ANISOU 1312  CG  HIS A 227    14322  14680  10538   1071    798   1085       C  
ATOM   1313  ND1 HIS A 227     -28.061  18.211  76.010  1.00105.18           N  
ANISOU 1313  ND1 HIS A 227    14376  14859  10727    929    728   1034       N  
ATOM   1314  CD2 HIS A 227     -29.764  18.442  74.598  1.00105.67           C  
ANISOU 1314  CD2 HIS A 227    14300  15090  10758   1254    841   1163       C  
ATOM   1315  CE1 HIS A 227     -28.900  17.201  76.165  1.00103.98           C  
ANISOU 1315  CE1 HIS A 227    13976  14902  10629   1022    735   1083       C  
ATOM   1316  NE2 HIS A 227     -29.938  17.296  75.332  1.00104.57           N  
ANISOU 1316  NE2 HIS A 227    13953  15095  10685   1197    799   1158       N  
ATOM   1317  N   GLN A 228     -26.279  22.402  73.067  1.00106.24           N  
ANISOU 1317  N   GLN A 228    15440  14308  10620    692    830   1038       N  
ATOM   1318  CA  GLN A 228     -26.128  23.616  72.256  1.00108.37           C  
ANISOU 1318  CA  GLN A 228    16024  14363  10790    686    892   1077       C  
ATOM   1319  C   GLN A 228     -25.023  23.470  71.204  1.00112.96           C  
ANISOU 1319  C   GLN A 228    16466  15008  11448    394    820   1077       C  
ATOM   1320  O   GLN A 228     -25.158  24.012  70.106  1.00112.83           O  
ANISOU 1320  O   GLN A 228    16524  14943  11403    446    868   1148       O  
ATOM   1321  CB  GLN A 228     -25.833  24.827  73.150  1.00112.14           C  
ANISOU 1321  CB  GLN A 228    17002  14510  11094    620    937   1021       C  
ATOM   1322  CG  GLN A 228     -27.068  25.392  73.841  1.00130.89           C  
ANISOU 1322  CG  GLN A 228    19631  16763  13337   1001   1057   1049       C  
ATOM   1323  CD  GLN A 228     -26.736  26.484  74.833  1.00156.99           C  
ANISOU 1323  CD  GLN A 228    23459  19729  16462    925   1098    966       C  
ATOM   1324  OE1 GLN A 228     -27.016  26.372  76.029  1.00153.82           O  
ANISOU 1324  OE1 GLN A 228    23130  19317  15999   1004   1107    906       O  
ATOM   1325  NE2 GLN A 228     -26.164  27.585  74.359  1.00151.68           N  
ANISOU 1325  NE2 GLN A 228    23188  18760  15682    766   1129    963       N  
ATOM   1326  N   ASP A 229     -23.942  22.739  71.544  1.00109.92           N  
ANISOU 1326  N   ASP A 229    15870  14754  11141    111    711   1007       N  
ATOM   1327  CA  ASP A 229     -22.802  22.467  70.665  1.00109.96           C  
ANISOU 1327  CA  ASP A 229    15689  14886  11207   -160    639   1003       C  
ATOM   1328  C   ASP A 229     -23.215  21.552  69.501  1.00111.66           C  
ANISOU 1328  C   ASP A 229    15548  15330  11548    -21    635   1055       C  
ATOM   1329  O   ASP A 229     -22.805  21.796  68.367  1.00111.11           O  
ANISOU 1329  O   ASP A 229    15440  15298  11480   -109    638   1094       O  
ATOM   1330  CB  ASP A 229     -21.644  21.846  71.471  1.00112.14           C  
ANISOU 1330  CB  ASP A 229    15805  15294  11509   -429    529    925       C  
ATOM   1331  CG  ASP A 229     -20.546  21.229  70.631  1.00127.68           C  
ANISOU 1331  CG  ASP A 229    17470  17493  13548   -635    454    928       C  
ATOM   1332  OD1 ASP A 229     -19.706  21.989  70.099  1.00130.28           O  
ANISOU 1332  OD1 ASP A 229    17917  17786  13799   -881    447    940       O  
ATOM   1333  OD2 ASP A 229     -20.526  19.984  70.508  1.00134.48           O  
ANISOU 1333  OD2 ASP A 229    17991  18574  14531   -550    409    921       O  
ATOM   1334  N   MET A 230     -24.016  20.509  69.782  1.00107.11           N  
ANISOU 1334  N   MET A 230    14728  14907  11062    171    627   1054       N  
ATOM   1335  CA  MET A 230     -24.505  19.586  68.760  1.00105.89           C  
ANISOU 1335  CA  MET A 230    14264  14962  11008    283    621   1088       C  
ATOM   1336  C   MET A 230     -25.571  20.276  67.896  1.00109.97           C  
ANISOU 1336  C   MET A 230    14877  15448  11458    510    711   1177       C  
ATOM   1337  O   MET A 230     -25.631  20.011  66.696  1.00109.04           O  
ANISOU 1337  O   MET A 230    14593  15462  11374    523    708   1212       O  
ATOM   1338  CB  MET A 230     -25.046  18.290  69.395  1.00107.17           C  
ANISOU 1338  CB  MET A 230    14182  15276  11263    375    587   1062       C  
ATOM   1339  CG  MET A 230     -25.360  17.176  68.384  1.00109.89           C  
ANISOU 1339  CG  MET A 230    14220  15827  11705    416    563   1070       C  
ATOM   1340  SD  MET A 230     -23.986  16.685  67.302  1.00113.67           S  
ANISOU 1340  SD  MET A 230    14526  16416  12249    214    497   1030       S  
ATOM   1341  CE  MET A 230     -23.044  15.685  68.406  1.00109.62           C  
ANISOU 1341  CE  MET A 230    13903  15949  11799     96    416    961       C  
ATOM   1342  N   HIS A 231     -26.381  21.181  68.493  1.00107.62           N  
ANISOU 1342  N   HIS A 231    14855  14987  11047    703    793   1217       N  
ATOM   1343  CA  HIS A 231     -27.407  21.936  67.771  1.00108.60           C  
ANISOU 1343  CA  HIS A 231    15099  15089  11075    973    890   1319       C  
ATOM   1344  C   HIS A 231     -26.759  22.935  66.807  1.00112.82           C  
ANISOU 1344  C   HIS A 231    15856  15468  11543    868    917   1363       C  
ATOM   1345  O   HIS A 231     -27.210  23.042  65.670  1.00112.75           O  
ANISOU 1345  O   HIS A 231    15761  15563  11515    993    950   1445       O  
ATOM   1346  CB  HIS A 231     -28.373  22.645  68.729  1.00111.17           C  
ANISOU 1346  CB  HIS A 231    15682  15284  11274   1244    982   1352       C  
ATOM   1347  CG  HIS A 231     -29.247  21.709  69.510  1.00114.02           C  
ANISOU 1347  CG  HIS A 231    15798  15851  11675   1385    975   1344       C  
ATOM   1348  ND1 HIS A 231     -29.439  21.871  70.873  1.00116.47           N  
ANISOU 1348  ND1 HIS A 231    16268  16058  11927   1446    998   1303       N  
ATOM   1349  CD2 HIS A 231     -29.941  20.619  69.100  1.00114.81           C  
ANISOU 1349  CD2 HIS A 231    15521  16249  11852   1446    946   1372       C  
ATOM   1350  CE1 HIS A 231     -30.242  20.885  71.244  1.00115.00           C  
ANISOU 1350  CE1 HIS A 231    15788  16119  11789   1546    988   1320       C  
ATOM   1351  NE2 HIS A 231     -30.569  20.106  70.212  1.00114.40           N  
ANISOU 1351  NE2 HIS A 231    15392  16282  11793   1534    955   1360       N  
ATOM   1352  N   SER A 232     -25.672  23.618  67.238  1.00109.37           N  
ANISOU 1352  N   SER A 232    15688  14808  11060    608    897   1312       N  
ATOM   1353  CA  SER A 232     -24.917  24.563  66.402  1.00110.09           C  
ANISOU 1353  CA  SER A 232    16009  14743  11076    430    918   1354       C  
ATOM   1354  C   SER A 232     -24.261  23.833  65.227  1.00110.93           C  
ANISOU 1354  C   SER A 232    15769  15098  11283    267    854   1362       C  
ATOM   1355  O   SER A 232     -24.151  24.403  64.140  1.00112.06           O  
ANISOU 1355  O   SER A 232    15991  15216  11373    255    892   1441       O  
ATOM   1356  CB  SER A 232     -23.859  25.290  67.226  1.00115.50           C  
ANISOU 1356  CB  SER A 232    17013  15188  11683    119    893   1284       C  
ATOM   1357  OG  SER A 232     -24.432  25.991  68.318  1.00126.56           O  
ANISOU 1357  OG  SER A 232    18776  16339  12973    268    956   1261       O  
ATOM   1358  N   TYR A 233     -23.851  22.565  65.447  1.00103.70           N  
ANISOU 1358  N   TYR A 233    14488  14416  10499    165    764   1285       N  
ATOM   1359  CA  TYR A 233     -23.242  21.689  64.447  1.00101.62           C  
ANISOU 1359  CA  TYR A 233    13884  14402  10327     48    705   1273       C  
ATOM   1360  C   TYR A 233     -24.284  21.290  63.403  1.00103.37           C  
ANISOU 1360  C   TYR A 233    13923  14784  10570    292    740   1334       C  
ATOM   1361  O   TYR A 233     -23.995  21.342  62.207  1.00103.22           O  
ANISOU 1361  O   TYR A 233    13813  14867  10540    245    743   1375       O  
ATOM   1362  CB  TYR A 233     -22.632  20.440  65.118  1.00101.40           C  
ANISOU 1362  CB  TYR A 233    13576  14540  10411    -64    613   1176       C  
ATOM   1363  CG  TYR A 233     -21.776  19.595  64.199  1.00102.76           C  
ANISOU 1363  CG  TYR A 233    13448  14946  10651   -189    558   1151       C  
ATOM   1364  CD1 TYR A 233     -20.435  19.904  63.982  1.00105.76           C  
ANISOU 1364  CD1 TYR A 233    13820  15375  10989   -455    522   1142       C  
ATOM   1365  CD2 TYR A 233     -22.295  18.469  63.568  1.00102.26           C  
ANISOU 1365  CD2 TYR A 233    13111  15068  10674    -49    543   1133       C  
ATOM   1366  CE1 TYR A 233     -19.642  19.134  63.133  1.00105.69           C  
ANISOU 1366  CE1 TYR A 233    13527  15609  11021   -531    483   1124       C  
ATOM   1367  CE2 TYR A 233     -21.514  17.695  62.712  1.00102.72           C  
ANISOU 1367  CE2 TYR A 233    12929  15325  10776   -133    503   1100       C  
ATOM   1368  CZ  TYR A 233     -20.184  18.028  62.503  1.00109.71           C  
ANISOU 1368  CZ  TYR A 233    13798  16269  11617   -351    477   1098       C  
ATOM   1369  OH  TYR A 233     -19.398  17.265  61.676  1.00108.71           O  
ANISOU 1369  OH  TYR A 233    13426  16366  11514   -399    448   1070       O  
ATOM   1370  N   ILE A 234     -25.496  20.903  63.861  1.00 98.38           N  
ANISOU 1370  N   ILE A 234    13227  14203   9950    537    765   1345       N  
ATOM   1371  CA  ILE A 234     -26.613  20.497  63.005  1.00 97.75           C  
ANISOU 1371  CA  ILE A 234    12952  14323   9865    757    791   1405       C  
ATOM   1372  C   ILE A 234     -27.117  21.726  62.229  1.00104.27           C  
ANISOU 1372  C   ILE A 234    14006  15058  10555    928    880   1528       C  
ATOM   1373  O   ILE A 234     -27.406  21.601  61.038  1.00104.62           O  
ANISOU 1373  O   ILE A 234    13900  15272  10577    992    886   1584       O  
ATOM   1374  CB  ILE A 234     -27.730  19.777  63.822  1.00100.09           C  
ANISOU 1374  CB  ILE A 234    13110  14731  10188    932    793   1392       C  
ATOM   1375  CG1 ILE A 234     -27.249  18.376  64.278  1.00 99.06           C  
ANISOU 1375  CG1 ILE A 234    12731  14713  10193    765    705   1286       C  
ATOM   1376  CG2 ILE A 234     -29.050  19.654  63.033  1.00100.61           C  
ANISOU 1376  CG2 ILE A 234    13016  15021  10190   1170    834   1480       C  
ATOM   1377  CD1 ILE A 234     -27.920  17.806  65.559  1.00106.67           C  
ANISOU 1377  CD1 ILE A 234    13657  15690  11182    841    702   1261       C  
ATOM   1378  N   ALA A 235     -27.162  22.911  62.877  1.00102.49           N  
ANISOU 1378  N   ALA A 235    14165  14553  10224    996    949   1569       N  
ATOM   1379  CA  ALA A 235     -27.594  24.167  62.250  1.00104.62           C  
ANISOU 1379  CA  ALA A 235    14737  14671  10345   1183   1047   1696       C  
ATOM   1380  C   ALA A 235     -26.687  24.551  61.086  1.00109.70           C  
ANISOU 1380  C   ALA A 235    15419  15292  10970    978   1037   1735       C  
ATOM   1381  O   ALA A 235     -27.194  24.918  60.028  1.00110.85           O  
ANISOU 1381  O   ALA A 235    15561  15518  11039   1146   1086   1846       O  
ATOM   1382  CB  ALA A 235     -27.623  25.293  63.272  1.00107.27           C  
ANISOU 1382  CB  ALA A 235    15537  14654  10567   1249   1119   1704       C  
ATOM   1383  N   ALA A 236     -25.356  24.424  61.270  1.00105.59           N  
ANISOU 1383  N   ALA A 236    14903  14708  10509    620    974   1653       N  
ATOM   1384  CA  ALA A 236     -24.349  24.755  60.263  1.00106.05           C  
ANISOU 1384  CA  ALA A 236    14974  14778  10542    376    962   1687       C  
ATOM   1385  C   ALA A 236     -24.414  23.817  59.048  1.00108.34           C  
ANISOU 1385  C   ALA A 236    14862  15404  10898    405    922   1693       C  
ATOM   1386  O   ALA A 236     -24.540  24.305  57.925  1.00108.88           O  
ANISOU 1386  O   ALA A 236    14970  15513  10887    463    966   1794       O  
ATOM   1387  CB  ALA A 236     -22.960  24.725  60.882  1.00106.81           C  
ANISOU 1387  CB  ALA A 236    15105  14809  10670     -6    897   1596       C  
ATOM   1388  N   PHE A 237     -24.357  22.487  59.269  1.00102.87           N  
ANISOU 1388  N   PHE A 237    13813  14938  10333    373    844   1586       N  
ATOM   1389  CA  PHE A 237     -24.394  21.493  58.194  1.00101.72           C  
ANISOU 1389  CA  PHE A 237    13316  15090  10242    386    804   1562       C  
ATOM   1390  C   PHE A 237     -25.763  21.402  57.527  1.00104.87           C  
ANISOU 1390  C   PHE A 237    13620  15637  10590    673    840   1636       C  
ATOM   1391  O   PHE A 237     -25.820  21.223  56.313  1.00104.83           O  
ANISOU 1391  O   PHE A 237    13464  15817  10548    692    840   1672       O  
ATOM   1392  CB  PHE A 237     -23.963  20.112  58.700  1.00102.07           C  
ANISOU 1392  CB  PHE A 237    13080  15283  10420    284    720   1427       C  
ATOM   1393  CG  PHE A 237     -22.469  19.917  58.627  1.00104.16           C  
ANISOU 1393  CG  PHE A 237    13275  15589  10713     15    674   1371       C  
ATOM   1394  CD1 PHE A 237     -21.646  20.319  59.673  1.00108.24           C  
ANISOU 1394  CD1 PHE A 237    13942  15957  11227   -167    653   1341       C  
ATOM   1395  CD2 PHE A 237     -21.880  19.356  57.499  1.00106.30           C  
ANISOU 1395  CD2 PHE A 237    13323  16078  10989    -54    653   1353       C  
ATOM   1396  CE1 PHE A 237     -20.257  20.163  59.594  1.00109.56           C  
ANISOU 1396  CE1 PHE A 237    14006  16230  11392   -418    609   1306       C  
ATOM   1397  CE2 PHE A 237     -20.492  19.194  57.423  1.00109.47           C  
ANISOU 1397  CE2 PHE A 237    13632  16571  11391   -277    619   1316       C  
ATOM   1398  CZ  PHE A 237     -19.690  19.602  58.469  1.00108.20           C  
ANISOU 1398  CZ  PHE A 237    13593  16296  11224   -460    596   1299       C  
ATOM   1399  N   GLY A 238     -26.831  21.540  58.310  1.00100.41           N  
ANISOU 1399  N   GLY A 238    13129  15021  10000    890    873   1663       N  
ATOM   1400  CA  GLY A 238     -28.206  21.483  57.825  1.00100.52           C  
ANISOU 1400  CA  GLY A 238    13027  15228   9939   1173    908   1746       C  
ATOM   1401  C   GLY A 238     -28.575  22.595  56.865  1.00106.51           C  
ANISOU 1401  C   GLY A 238    13962  15962  10544   1350    986   1902       C  
ATOM   1402  O   GLY A 238     -29.188  22.334  55.824  1.00106.61           O  
ANISOU 1402  O   GLY A 238    13771  16238  10498   1468    984   1959       O  
ATOM   1403  N   ALA A 239     -28.194  23.845  57.209  1.00104.51           N  
ANISOU 1403  N   ALA A 239    14111  15387  10213   1361   1056   1971       N  
ATOM   1404  CA  ALA A 239     -28.475  25.034  56.402  1.00106.77           C  
ANISOU 1404  CA  ALA A 239    14660  15569  10338   1539   1146   2135       C  
ATOM   1405  C   ALA A 239     -27.668  25.051  55.099  1.00111.49           C  
ANISOU 1405  C   ALA A 239    15175  16263  10924   1346   1126   2166       C  
ATOM   1406  O   ALA A 239     -28.247  25.335  54.047  1.00112.29           O  
ANISOU 1406  O   ALA A 239    15229  16521  10916   1534   1163   2288       O  
ATOM   1407  CB  ALA A 239     -28.199  26.296  57.202  1.00109.27           C  
ANISOU 1407  CB  ALA A 239    15485  15463  10570   1556   1226   2180       C  
ATOM   1408  N   VAL A 240     -26.351  24.738  55.153  1.00107.29           N  
ANISOU 1408  N   VAL A 240    14602  15677  10485    986   1069   2066       N  
ATOM   1409  CA  VAL A 240     -25.510  24.740  53.951  1.00107.64           C  
ANISOU 1409  CA  VAL A 240    14551  15841  10505    794   1055   2095       C  
ATOM   1410  C   VAL A 240     -25.987  23.653  52.983  1.00111.70           C  
ANISOU 1410  C   VAL A 240    14650  16743  11049    881   1004   2060       C  
ATOM   1411  O   VAL A 240     -26.110  23.953  51.801  1.00112.66           O  
ANISOU 1411  O   VAL A 240    14738  16997  11071    945   1032   2159       O  
ATOM   1412  CB  VAL A 240     -23.974  24.683  54.190  1.00111.12           C  
ANISOU 1412  CB  VAL A 240    15012  16201  11007    400   1012   2013       C  
ATOM   1413  CG1 VAL A 240     -23.478  25.941  54.893  1.00112.75           C  
ANISOU 1413  CG1 VAL A 240    15678  16030  11134    261   1067   2067       C  
ATOM   1414  CG2 VAL A 240     -23.544  23.431  54.947  1.00108.83           C  
ANISOU 1414  CG2 VAL A 240    14432  16046  10872    272    920   1841       C  
ATOM   1415  N   THR A 241     -26.338  22.439  53.483  1.00107.22           N  
ANISOU 1415  N   THR A 241    13798  16345  10596    892    934   1928       N  
ATOM   1416  CA  THR A 241     -26.865  21.350  52.644  1.00106.68           C  
ANISOU 1416  CA  THR A 241    13373  16620  10541    947    883   1875       C  
ATOM   1417  C   THR A 241     -28.200  21.785  52.036  1.00113.02           C  
ANISOU 1417  C   THR A 241    14159  17582  11204   1246    928   2012       C  
ATOM   1418  O   THR A 241     -28.432  21.548  50.853  1.00113.45           O  
ANISOU 1418  O   THR A 241    14036  17888  11181   1282    916   2045       O  
ATOM   1419  CB  THR A 241     -26.999  20.038  53.439  1.00113.35           C  
ANISOU 1419  CB  THR A 241    13996  17550  11522    880    809   1716       C  
ATOM   1420  OG1 THR A 241     -25.752  19.739  54.067  1.00113.49           O  
ANISOU 1420  OG1 THR A 241    14045  17427  11647    647    774   1614       O  
ATOM   1421  CG2 THR A 241     -27.426  18.853  52.566  1.00110.91           C  
ANISOU 1421  CG2 THR A 241    13366  17557  11216    875    753   1638       C  
ATOM   1422  N   GLY A 242     -29.027  22.452  52.844  1.00110.98           N  
ANISOU 1422  N   GLY A 242    14085  17188  10892   1469    983   2094       N  
ATOM   1423  CA  GLY A 242     -30.325  22.976  52.436  1.00112.95           C  
ANISOU 1423  CA  GLY A 242    14333  17600  10984   1809   1039   2247       C  
ATOM   1424  C   GLY A 242     -30.236  23.976  51.301  1.00119.97           C  
ANISOU 1424  C   GLY A 242    15388  18477  11721   1920   1103   2412       C  
ATOM   1425  O   GLY A 242     -31.048  23.927  50.375  1.00120.52           O  
ANISOU 1425  O   GLY A 242    15279  18850  11665   2110   1107   2506       O  
ATOM   1426  N   LEU A 243     -29.225  24.865  51.354  1.00118.16           N  
ANISOU 1426  N   LEU A 243    15495  17912  11488   1776   1150   2450       N  
ATOM   1427  CA  LEU A 243     -28.974  25.895  50.342  1.00120.61           C  
ANISOU 1427  CA  LEU A 243    16031  18141  11652   1831   1221   2616       C  
ATOM   1428  C   LEU A 243     -28.295  25.318  49.093  1.00125.86           C  
ANISOU 1428  C   LEU A 243    16436  19058  12326   1619   1168   2581       C  
ATOM   1429  O   LEU A 243     -28.585  25.767  47.982  1.00126.56           O  
ANISOU 1429  O   LEU A 243    16527  19289  12270   1754   1205   2721       O  
ATOM   1430  CB  LEU A 243     -28.113  27.023  50.930  1.00121.83           C  
ANISOU 1430  CB  LEU A 243    16666  17832  11790   1691   1288   2660       C  
ATOM   1431  CG  LEU A 243     -28.766  27.897  51.996  1.00127.69           C  
ANISOU 1431  CG  LEU A 243    17787  18264  12466   1943   1371   2724       C  
ATOM   1432  CD1 LEU A 243     -27.724  28.500  52.909  1.00128.20           C  
ANISOU 1432  CD1 LEU A 243    18228  17905  12576   1657   1387   2660       C  
ATOM   1433  CD2 LEU A 243     -29.647  28.975  51.377  1.00132.73           C  
ANISOU 1433  CD2 LEU A 243    18689  18852  12891   2340   1482   2949       C  
ATOM   1434  N   CYS A 244     -27.391  24.333  49.282  1.00122.52           N  
ANISOU 1434  N   CYS A 244    15799  18698  12056   1313   1087   2400       N  
ATOM   1435  CA  CYS A 244     -26.647  23.663  48.212  1.00122.93           C  
ANISOU 1435  CA  CYS A 244    15599  18990  12119   1115   1040   2336       C  
ATOM   1436  C   CYS A 244     -27.575  22.819  47.346  1.00127.41           C  
ANISOU 1436  C   CYS A 244    15828  19951  12630   1266    994   2313       C  
ATOM   1437  O   CYS A 244     -27.488  22.896  46.119  1.00128.06           O  
ANISOU 1437  O   CYS A 244    15818  20235  12603   1273   1001   2377       O  
ATOM   1438  CB  CYS A 244     -25.517  22.818  48.788  1.00121.91           C  
ANISOU 1438  CB  CYS A 244    15346  18825  12151    815    975   2153       C  
ATOM   1439  SG  CYS A 244     -24.059  23.766  49.293  1.00126.96           S  
ANISOU 1439  SG  CYS A 244    16297  19140  12801    517   1013   2186       S  
ATOM   1440  N   THR A 245     -28.447  22.009  47.983  1.00123.34           N  
ANISOU 1440  N   THR A 245    15129  19557  12176   1359    945   2222       N  
ATOM   1441  CA  THR A 245     -29.406  21.135  47.298  1.00123.44           C  
ANISOU 1441  CA  THR A 245    14820  19957  12125   1452    890   2185       C  
ATOM   1442  C   THR A 245     -30.478  21.959  46.588  1.00129.48           C  
ANISOU 1442  C   THR A 245    15608  20903  12686   1756    942   2388       C  
ATOM   1443  O   THR A 245     -30.809  21.645  45.449  1.00129.66           O  
ANISOU 1443  O   THR A 245    15424  21248  12593   1783    914   2410       O  
ATOM   1444  CB  THR A 245     -30.043  20.118  48.260  1.00133.24           C  
ANISOU 1444  CB  THR A 245    15892  21264  13471   1433    830   2050       C  
ATOM   1445  OG1 THR A 245     -30.591  20.794  49.395  1.00135.44           O  
ANISOU 1445  OG1 THR A 245    16360  21344  13758   1605    880   2130       O  
ATOM   1446  CG2 THR A 245     -29.070  19.031  48.701  1.00130.44           C  
ANISOU 1446  CG2 THR A 245    15451  20819  13290   1158    767   1843       C  
ATOM   1447  N   LEU A 246     -30.998  23.018  47.247  1.00127.55           N  
ANISOU 1447  N   LEU A 246    15627  20455  12380   1998   1022   2538       N  
ATOM   1448  CA  LEU A 246     -32.015  23.914  46.694  1.00130.00           C  
ANISOU 1448  CA  LEU A 246    16005  20910  12479   2356   1089   2759       C  
ATOM   1449  C   LEU A 246     -31.498  24.585  45.421  1.00135.62           C  
ANISOU 1449  C   LEU A 246    16822  21641  13064   2354   1130   2888       C  
ATOM   1450  O   LEU A 246     -32.219  24.605  44.424  1.00136.58           O  
ANISOU 1450  O   LEU A 246    16767  22109  13017   2533   1125   2995       O  
ATOM   1451  CB  LEU A 246     -32.431  24.969  47.738  1.00131.31           C  
ANISOU 1451  CB  LEU A 246    16522  20763  12608   2615   1184   2880       C  
ATOM   1452  CG  LEU A 246     -33.476  26.013  47.330  1.00139.10           C  
ANISOU 1452  CG  LEU A 246    17647  21846  13360   3063   1278   3128       C  
ATOM   1453  CD1 LEU A 246     -34.861  25.399  47.213  1.00139.82           C  
ANISOU 1453  CD1 LEU A 246    17348  22436  13340   3297   1237   3160       C  
ATOM   1454  CD2 LEU A 246     -33.503  27.159  48.321  1.00143.22           C  
ANISOU 1454  CD2 LEU A 246    18639  21926  13851   3272   1389   3225       C  
ATOM   1455  N   PHE A 247     -30.246  25.094  45.449  1.00132.08           N  
ANISOU 1455  N   PHE A 247    16640  20858  12685   2129   1164   2879       N  
ATOM   1456  CA  PHE A 247     -29.589  25.742  44.311  1.00133.44           C  
ANISOU 1456  CA  PHE A 247    16937  21019  12747   2066   1208   3001       C  
ATOM   1457  C   PHE A 247     -29.473  24.771  43.129  1.00136.34           C  
ANISOU 1457  C   PHE A 247    16919  21802  13082   1941   1132   2914       C  
ATOM   1458  O   PHE A 247     -29.745  25.155  41.989  1.00137.34           O  
ANISOU 1458  O   PHE A 247    17011  22138  13033   2070   1158   3056       O  
ATOM   1459  CB  PHE A 247     -28.198  26.265  44.722  1.00135.09           C  
ANISOU 1459  CB  PHE A 247    17445  20835  13049   1762   1243   2972       C  
ATOM   1460  CG  PHE A 247     -27.355  26.785  43.586  1.00138.20           C  
ANISOU 1460  CG  PHE A 247    17928  21242  13341   1612   1281   3077       C  
ATOM   1461  CD1 PHE A 247     -27.529  28.075  43.106  1.00144.40           C  
ANISOU 1461  CD1 PHE A 247    19067  21848  13951   1780   1384   3317       C  
ATOM   1462  CD2 PHE A 247     -26.380  25.988  43.000  1.00139.40           C  
ANISOU 1462  CD2 PHE A 247    17824  21583  13558   1314   1224   2946       C  
ATOM   1463  CE1 PHE A 247     -26.746  28.558  42.056  1.00146.98           C  
ANISOU 1463  CE1 PHE A 247    19481  22193  14173   1620   1424   3427       C  
ATOM   1464  CE2 PHE A 247     -25.609  26.465  41.936  1.00143.89           C  
ANISOU 1464  CE2 PHE A 247    18452  22203  14015   1175   1265   3052       C  
ATOM   1465  CZ  PHE A 247     -25.798  27.748  41.470  1.00144.73           C  
ANISOU 1465  CZ  PHE A 247    18902  22136  13951   1312   1363   3295       C  
ATOM   1466  N   THR A 248     -29.062  23.519  43.418  1.00130.65           N  
ANISOU 1466  N   THR A 248    15937  21186  12517   1701   1043   2681       N  
ATOM   1467  CA  THR A 248     -28.889  22.428  42.458  1.00129.73           C  
ANISOU 1467  CA  THR A 248    15487  21419  12385   1559    968   2547       C  
ATOM   1468  C   THR A 248     -30.253  22.048  41.865  1.00135.00           C  
ANISOU 1468  C   THR A 248    15901  22489  12903   1772    927   2587       C  
ATOM   1469  O   THR A 248     -30.353  21.911  40.647  1.00135.60           O  
ANISOU 1469  O   THR A 248    15825  22864  12835   1784    911   2622       O  
ATOM   1470  CB  THR A 248     -28.177  21.250  43.144  1.00134.58           C  
ANISOU 1470  CB  THR A 248    15966  21970  13199   1299    898   2298       C  
ATOM   1471  OG1 THR A 248     -26.892  21.703  43.567  1.00133.65           O  
ANISOU 1471  OG1 THR A 248    16052  21554  13176   1108    936   2290       O  
ATOM   1472  CG2 THR A 248     -28.014  20.033  42.229  1.00132.66           C  
ANISOU 1472  CG2 THR A 248    15424  22047  12934   1168    826   2133       C  
ATOM   1473  N   LEU A 249     -31.291  21.911  42.707  1.00131.89           N  
ANISOU 1473  N   LEU A 249    15456  22134  12524   1931    912   2593       N  
ATOM   1474  CA  LEU A 249     -32.646  21.586  42.257  1.00133.08           C  
ANISOU 1474  CA  LEU A 249    15339  22713  12511   2121    872   2646       C  
ATOM   1475  C   LEU A 249     -33.203  22.701  41.368  1.00140.26           C  
ANISOU 1475  C   LEU A 249    16331  23778  13184   2429    940   2909       C  
ATOM   1476  O   LEU A 249     -33.832  22.403  40.351  1.00141.19           O  
ANISOU 1476  O   LEU A 249    16196  24323  13125   2495    897   2948       O  
ATOM   1477  CB  LEU A 249     -33.589  21.346  43.450  1.00132.62           C  
ANISOU 1477  CB  LEU A 249    15224  22661  12505   2235    859   2627       C  
ATOM   1478  CG  LEU A 249     -33.329  20.122  44.327  1.00134.67           C  
ANISOU 1478  CG  LEU A 249    15364  22840  12965   1963    784   2385       C  
ATOM   1479  CD1 LEU A 249     -34.056  20.251  45.632  1.00134.33           C  
ANISOU 1479  CD1 LEU A 249    15367  22698  12974   2100    805   2414       C  
ATOM   1480  CD2 LEU A 249     -33.721  18.839  43.633  1.00137.20           C  
ANISOU 1480  CD2 LEU A 249    15352  23540  13236   1776    682   2230       C  
ATOM   1481  N   ALA A 250     -32.939  23.979  41.745  1.00138.22           N  
ANISOU 1481  N   ALA A 250    16448  23161  12908   2607   1047   3087       N  
ATOM   1482  CA  ALA A 250     -33.373  25.188  41.037  1.00141.12           C  
ANISOU 1482  CA  ALA A 250    17001  23566  13052   2934   1136   3363       C  
ATOM   1483  C   ALA A 250     -32.821  25.255  39.596  1.00146.31           C  
ANISOU 1483  C   ALA A 250    17596  24407  13590   2833   1131   3416       C  
ATOM   1484  O   ALA A 250     -33.564  25.664  38.701  1.00148.29           O  
ANISOU 1484  O   ALA A 250    17763  24969  13612   3094   1149   3598       O  
ATOM   1485  CB  ALA A 250     -32.960  26.428  41.812  1.00142.68           C  
ANISOU 1485  CB  ALA A 250    17691  23240  13283   3056   1253   3495       C  
ATOM   1486  N   THR A 251     -31.535  24.857  39.377  1.00141.04           N  
ANISOU 1486  N   THR A 251    16953  23578  13057   2476   1110   3268       N  
ATOM   1487  CA  THR A 251     -30.893  24.822  38.054  1.00141.44           C  
ANISOU 1487  CA  THR A 251    16927  23811  13002   2347   1107   3294       C  
ATOM   1488  C   THR A 251     -31.533  23.758  37.178  1.00146.35           C  
ANISOU 1488  C   THR A 251    17129  24958  13518   2327   1007   3184       C  
ATOM   1489  O   THR A 251     -31.735  23.994  35.988  1.00148.03           O  
ANISOU 1489  O   THR A 251    17254  25464  13528   2422   1013   3303       O  
ATOM   1490  CB  THR A 251     -29.378  24.572  38.140  1.00145.19           C  
ANISOU 1490  CB  THR A 251    17490  24037  13639   1981   1109   3152       C  
ATOM   1491  OG1 THR A 251     -29.057  23.824  39.306  1.00141.93           O  
ANISOU 1491  OG1 THR A 251    17036  23439  13451   1802   1060   2940       O  
ATOM   1492  CG2 THR A 251     -28.589  25.834  38.134  1.00144.81           C  
ANISOU 1492  CG2 THR A 251    17837  23627  13559   1951   1215   3335       C  
ATOM   1493  N   PHE A 252     -31.863  22.598  37.769  1.00141.90           N  
ANISOU 1493  N   PHE A 252    16328  24511  13077   2191    917   2961       N  
ATOM   1494  CA  PHE A 252     -32.480  21.467  37.084  1.00142.44           C  
ANISOU 1494  CA  PHE A 252    16030  25041  13052   2106    813   2817       C  
ATOM   1495  C   PHE A 252     -33.878  21.811  36.574  1.00150.55           C  
ANISOU 1495  C   PHE A 252    16883  26490  13828   2403    800   3000       C  
ATOM   1496  O   PHE A 252     -34.189  21.494  35.433  1.00151.52           O  
ANISOU 1496  O   PHE A 252    16789  27020  13762   2394    752   3005       O  
ATOM   1497  CB  PHE A 252     -32.548  20.247  38.013  1.00142.20           C  
ANISOU 1497  CB  PHE A 252    15860  24960  13208   1891    733   2559       C  
ATOM   1498  CG  PHE A 252     -31.353  19.317  37.977  1.00142.06           C  
ANISOU 1498  CG  PHE A 252    15835  24791  13352   1574    699   2315       C  
ATOM   1499  CD1 PHE A 252     -31.172  18.427  36.924  1.00145.43           C  
ANISOU 1499  CD1 PHE A 252    16068  25507  13682   1419    639   2167       C  
ATOM   1500  CD2 PHE A 252     -30.447  19.279  39.030  1.00142.46           C  
ANISOU 1500  CD2 PHE A 252    16067  24431  13631   1446    726   2227       C  
ATOM   1501  CE1 PHE A 252     -30.077  17.554  36.901  1.00144.89           C  
ANISOU 1501  CE1 PHE A 252    16006  25304  13742   1180    621   1945       C  
ATOM   1502  CE2 PHE A 252     -29.352  18.404  39.007  1.00143.73           C  
ANISOU 1502  CE2 PHE A 252    16203  24492  13918   1199    700   2016       C  
ATOM   1503  CZ  PHE A 252     -29.176  17.548  37.944  1.00142.20           C  
ANISOU 1503  CZ  PHE A 252    15830  24575  13624   1086    653   1879       C  
ATOM   1504  N   VAL A 253     -34.702  22.488  37.400  1.00149.61           N  
ANISOU 1504  N   VAL A 253    16858  26299  13688   2684    847   3157       N  
ATOM   1505  CA  VAL A 253     -36.074  22.858  37.039  1.00153.09           C  
ANISOU 1505  CA  VAL A 253    17116  27175  13875   3019    844   3354       C  
ATOM   1506  C   VAL A 253     -36.092  24.059  36.047  1.00162.54           C  
ANISOU 1506  C   VAL A 253    18478  28432  14847   3316    930   3640       C  
ATOM   1507  O   VAL A 253     -37.024  24.151  35.243  1.00164.59           O  
ANISOU 1507  O   VAL A 253    18506  29183  14848   3531    903   3780       O  
ATOM   1508  CB  VAL A 253     -36.966  23.088  38.294  1.00157.07           C  
ANISOU 1508  CB  VAL A 253    17642  27621  14417   3242    871   3417       C  
ATOM   1509  CG1 VAL A 253     -36.685  24.423  38.984  1.00157.54           C  
ANISOU 1509  CG1 VAL A 253    18142  27199  14516   3520   1008   3609       C  
ATOM   1510  CG2 VAL A 253     -38.449  22.930  37.967  1.00159.28           C  
ANISOU 1510  CG2 VAL A 253    17566  28513  14441   3479    824   3535       C  
ATOM   1511  N   ALA A 254     -35.062  24.940  36.081  1.00161.00           N  
ANISOU 1511  N   ALA A 254    18674  27764  14733   3305   1029   3728       N  
ATOM   1512  CA  ALA A 254     -34.956  26.105  35.190  1.00164.40           C  
ANISOU 1512  CA  ALA A 254    19332  28169  14962   3551   1122   4005       C  
ATOM   1513  C   ALA A 254     -34.696  25.685  33.738  1.00171.33           C  
ANISOU 1513  C   ALA A 254    19979  29433  15686   3412   1068   3985       C  
ATOM   1514  O   ALA A 254     -35.149  26.364  32.813  1.00173.78           O  
ANISOU 1514  O   ALA A 254    20295  29991  15743   3680   1107   4222       O  
ATOM   1515  CB  ALA A 254     -33.856  27.037  35.669  1.00164.76           C  
ANISOU 1515  CB  ALA A 254    19863  27596  15143   3477   1233   4073       C  
ATOM   1516  N   ASP A 255     -33.984  24.558  33.548  1.00167.39           N  
ANISOU 1516  N   ASP A 255    19286  28990  15324   3017    983   3704       N  
ATOM   1517  CA  ASP A 255     -33.630  23.974  32.250  1.00168.65           C  
ANISOU 1517  CA  ASP A 255    19226  29495  15356   2839    927   3622       C  
ATOM   1518  C   ASP A 255     -34.126  22.513  32.211  1.00174.16           C  
ANISOU 1518  C   ASP A 255    19541  30561  16071   2622    790   3345       C  
ATOM   1519  O   ASP A 255     -33.423  21.607  31.748  1.00172.77           O  
ANISOU 1519  O   ASP A 255    19255  30440  15948   2325    736   3118       O  
ATOM   1520  CB  ASP A 255     -32.098  24.096  32.064  1.00169.10           C  
ANISOU 1520  CB  ASP A 255    19500  29200  15552   2568    981   3551       C  
ATOM   1521  CG  ASP A 255     -31.558  23.730  30.698  1.00177.48           C  
ANISOU 1521  CG  ASP A 255    20408  30562  16466   2422    958   3507       C  
ATOM   1522  OD1 ASP A 255     -31.927  24.405  29.710  1.00179.84           O  
ANISOU 1522  OD1 ASP A 255    20707  31107  16516   2627    992   3732       O  
ATOM   1523  OD2 ASP A 255     -30.734  22.803  30.625  1.00180.89           O  
ANISOU 1523  OD2 ASP A 255    20736  30975  17019   2123    915   3256       O  
ATOM   1524  N   TRP A 256     -35.390  22.317  32.662  1.00173.50           N  
ANISOU 1524  N   TRP A 256    19262  30751  15908   2786    740   3379       N  
ATOM   1525  CA  TRP A 256     -36.094  21.048  32.880  1.00173.63           C  
ANISOU 1525  CA  TRP A 256    18950  31093  15930   2588    615   3152       C  
ATOM   1526  C   TRP A 256     -36.110  20.028  31.728  1.00178.99           C  
ANISOU 1526  C   TRP A 256    19355  32197  16455   2339    511   2969       C  
ATOM   1527  O   TRP A 256     -35.921  18.849  32.021  1.00177.19           O  
ANISOU 1527  O   TRP A 256    19030  31944  16351   2026    434   2687       O  
ATOM   1528  CB  TRP A 256     -37.548  21.279  33.333  1.00174.51           C  
ANISOU 1528  CB  TRP A 256    18875  31539  15893   2862    595   3306       C  
ATOM   1529  CG  TRP A 256     -38.236  20.021  33.795  1.00175.10           C  
ANISOU 1529  CG  TRP A 256    18652  31880  15999   2610    477   3080       C  
ATOM   1530  CD1 TRP A 256     -39.359  19.467  33.260  1.00180.23           C  
ANISOU 1530  CD1 TRP A 256    18932  33146  16402   2583    377   3076       C  
ATOM   1531  CD2 TRP A 256     -37.795  19.117  34.821  1.00172.29           C  
ANISOU 1531  CD2 TRP A 256    18353  31193  15918   2310    443   2822       C  
ATOM   1532  NE1 TRP A 256     -39.672  18.294  33.913  1.00178.61           N  
ANISOU 1532  NE1 TRP A 256    18567  32994  16302   2265    286   2835       N  
ATOM   1533  CE2 TRP A 256     -38.725  18.052  34.871  1.00177.01           C  
ANISOU 1533  CE2 TRP A 256    18631  32204  16422   2109    328   2679       C  
ATOM   1534  CE3 TRP A 256     -36.711  19.111  35.719  1.00170.84           C  
ANISOU 1534  CE3 TRP A 256    18458  30418  16036   2186    498   2708       C  
ATOM   1535  CZ2 TRP A 256     -38.605  16.997  35.781  1.00174.43           C  
ANISOU 1535  CZ2 TRP A 256    18297  31679  16298   1803    275   2434       C  
ATOM   1536  CZ3 TRP A 256     -36.590  18.061  36.615  1.00170.38           C  
ANISOU 1536  CZ3 TRP A 256    18366  30193  16176   1912    442   2467       C  
ATOM   1537  CH2 TRP A 256     -37.527  17.023  36.642  1.00171.78           C  
ANISOU 1537  CH2 TRP A 256    18257  30751  16262   1730    336   2336       C  
ATOM   1538  N   ARG A 257     -36.382  20.430  30.467  1.00178.37           N  
ANISOU 1538  N   ARG A 257    19166  32507  16099   2476    508   3121       N  
ATOM   1539  CA  ARG A 257     -36.409  19.448  29.375  1.00179.15           C  
ANISOU 1539  CA  ARG A 257    19020  33017  16032   2229    407   2930       C  
ATOM   1540  C   ARG A 257     -35.001  18.910  29.002  1.00180.88           C  
ANISOU 1540  C   ARG A 257    19387  32944  16396   1951    426   2710       C  
ATOM   1541  O   ARG A 257     -34.872  17.748  28.593  1.00180.11           O  
ANISOU 1541  O   ARG A 257    19154  33008  16272   1670    341   2438       O  
ATOM   1542  CB  ARG A 257     -37.091  19.983  28.111  1.00183.46           C  
ANISOU 1542  CB  ARG A 257    19386  34101  16218   2448    391   3148       C  
ATOM   1543  CG  ARG A 257     -37.607  18.804  27.263  1.00196.58           C  
ANISOU 1543  CG  ARG A 257    20722  36295  17674   2177    251   2927       C  
ATOM   1544  CD  ARG A 257     -38.402  19.217  26.033  1.00205.06           C  
ANISOU 1544  CD  ARG A 257    21944  37233  18737   2208    188   2948       C  
ATOM   1545  NE  ARG A 257     -38.420  18.174  25.000  1.00210.43           N  
ANISOU 1545  NE  ARG A 257    22858  37435  19660   1767     60   2541       N  
ATOM   1546  CZ  ARG A 257     -39.291  17.168  24.942  1.00218.81           C  
ANISOU 1546  CZ  ARG A 257    24309  37589  21238   1368    -91   2133       C  
ATOM   1547  NH1 ARG A 257     -40.254  17.060  25.851  1.00208.55           N  
ANISOU 1547  NH1 ARG A 257    22295  37535  19409   1568   -111   2389       N  
ATOM   1548  NH2 ARG A 257     -39.210  16.267  23.973  1.00209.41           N  
ANISOU 1548  NH2 ARG A 257    22519  37650  19398   1273   -155   2128       N  
ATOM   1549  N   ASN A 258     -33.970  19.752  29.155  1.00176.23           N  
ANISOU 1549  N   ASN A 258    19081  31937  15940   2029    539   2830       N  
ATOM   1550  CA  ASN A 258     -32.603  19.305  28.897  1.00174.34           C  
ANISOU 1550  CA  ASN A 258    18959  31450  15832   1789    568   2646       C  
ATOM   1551  C   ASN A 258     -32.064  18.543  30.121  1.00174.36           C  
ANISOU 1551  C   ASN A 258    19052  31054  16142   1582    554   2408       C  
ATOM   1552  O   ASN A 258     -31.392  17.525  29.952  1.00172.74           O  
ANISOU 1552  O   ASN A 258    18813  30815  16006   1345    519   2147       O  
ATOM   1553  CB  ASN A 258     -31.670  20.438  28.492  1.00176.65           C  
ANISOU 1553  CB  ASN A 258    19486  31519  16112   1896    688   2864       C  
ATOM   1554  CG  ASN A 258     -30.302  19.976  28.032  1.00203.37           C  
ANISOU 1554  CG  ASN A 258    22923  34782  19567   1661    718   2697       C  
ATOM   1555  OD1 ASN A 258     -30.119  19.498  26.906  1.00200.44           O  
ANISOU 1555  OD1 ASN A 258    22410  34733  19016   1585    690   2610       O  
ATOM   1556  ND2 ASN A 258     -29.300  20.106  28.895  1.00193.70           N  
ANISOU 1556  ND2 ASN A 258    21892  33117  18588   1548    777   2648       N  
ATOM   1557  N   SER A 259     -32.377  19.024  31.341  1.00169.42           N  
ANISOU 1557  N   SER A 259    18550  30140  15682   1692    585   2502       N  
ATOM   1558  CA  SER A 259     -31.941  18.426  32.607  1.00166.55           C  
ANISOU 1558  CA  SER A 259    18281  29398  15603   1529    575   2315       C  
ATOM   1559  C   SER A 259     -32.531  17.023  32.840  1.00168.92           C  
ANISOU 1559  C   SER A 259    18382  29878  15922   1325    463   2049       C  
ATOM   1560  O   SER A 259     -31.822  16.144  33.337  1.00167.05           O  
ANISOU 1560  O   SER A 259    18204  29401  15866   1116    446   1817       O  
ATOM   1561  CB  SER A 259     -32.320  19.324  33.777  1.00169.99           C  
ANISOU 1561  CB  SER A 259    18885  29546  16158   1722    632   2494       C  
ATOM   1562  OG  SER A 259     -33.679  19.122  34.113  1.00180.32           O  
ANISOU 1562  OG  SER A 259    20011  31127  17375   1838    574   2530       O  
ATOM   1563  N   ASN A 260     -33.833  16.829  32.512  1.00165.94           N  
ANISOU 1563  N   ASN A 260    17778  29928  15345   1383    389   2093       N  
ATOM   1564  CA  ASN A 260     -34.568  15.570  32.692  1.00165.19           C  
ANISOU 1564  CA  ASN A 260    17493  30051  15220   1157    278   1869       C  
ATOM   1565  C   ASN A 260     -34.118  14.528  31.647  1.00167.33           C  
ANISOU 1565  C   ASN A 260    17701  30497  15380    909    219   1621       C  
ATOM   1566  O   ASN A 260     -34.884  14.137  30.761  1.00169.29           O  
ANISOU 1566  O   ASN A 260    17746  31201  15374    839    140   1586       O  
ATOM   1567  CB  ASN A 260     -36.093  15.811  32.643  1.00168.60           C  
ANISOU 1567  CB  ASN A 260    17679  30943  15437   1293    222   2026       C  
ATOM   1568  CG  ASN A 260     -36.946  14.682  33.172  1.00190.20           C  
ANISOU 1568  CG  ASN A 260    20239  33860  18168   1047    118   1841       C  
ATOM   1569  OD1 ASN A 260     -36.940  14.371  34.366  1.00183.72           O  
ANISOU 1569  OD1 ASN A 260    19502  32745  17560    977    125   1770       O  
ATOM   1570  ND2 ASN A 260     -37.755  14.091  32.305  1.00182.83           N  
ANISOU 1570  ND2 ASN A 260    19056  33441  16970    904     19   1776       N  
ATOM   1571  N   ARG A 261     -32.855  14.088  31.768  1.00160.08           N  
ANISOU 1571  N   ARG A 261    16962  29225  14638    786    261   1451       N  
ATOM   1572  CA  ARG A 261     -32.208  13.099  30.911  1.00159.50           C  
ANISOU 1572  CA  ARG A 261    16894  29222  14488    592    232   1200       C  
ATOM   1573  C   ARG A 261     -31.181  12.306  31.723  1.00158.90           C  
ANISOU 1573  C   ARG A 261    17001  28707  14668    455    258    981       C  
ATOM   1574  O   ARG A 261     -30.349  12.902  32.416  1.00156.50           O  
ANISOU 1574  O   ARG A 261    16836  28064  14562    549    337   1073       O  
ATOM   1575  CB  ARG A 261     -31.544  13.771  29.692  1.00161.41           C  
ANISOU 1575  CB  ARG A 261    17138  29621  14567    708    292   1316       C  
ATOM   1576  CG  ARG A 261     -32.476  13.956  28.495  1.00175.54           C  
ANISOU 1576  CG  ARG A 261    18722  31947  16026    757    234   1408       C  
ATOM   1577  CD  ARG A 261     -31.757  14.515  27.282  1.00188.09           C  
ANISOU 1577  CD  ARG A 261    20327  33686  17452    853    296   1506       C  
ATOM   1578  NE  ARG A 261     -32.026  15.944  27.097  1.00200.87           N  
ANISOU 1578  NE  ARG A 261    21950  35381  18989   1124    361   1861       N  
ATOM   1579  CZ  ARG A 261     -31.971  16.572  25.927  1.00219.45           C  
ANISOU 1579  CZ  ARG A 261    24439  37652  21289   1195    384   1958       C  
ATOM   1580  NH1 ARG A 261     -31.603  15.918  24.827  1.00211.41           N  
ANISOU 1580  NH1 ARG A 261    23157  37260  19908   1119    363   1859       N  
ATOM   1581  NH2 ARG A 261     -32.233  17.872  25.855  1.00210.73           N  
ANISOU 1581  NH2 ARG A 261    23202  36934  19933   1509    458   2359       N  
ATOM   1582  N   TYR A 262     -31.256  10.962  31.648  1.00154.30           N  
ANISOU 1582  N   TYR A 262    16432  28133  14064    232    192    695       N  
ATOM   1583  CA  TYR A 262     -30.356  10.041  32.348  1.00151.79           C  
ANISOU 1583  CA  TYR A 262    16295  27427  13951    121    213    471       C  
ATOM   1584  C   TYR A 262     -28.931  10.116  31.767  1.00153.62           C  
ANISOU 1584  C   TYR A 262    16625  27547  14198    197    297    425       C  
ATOM   1585  O   TYR A 262     -28.792  10.255  30.549  1.00154.87           O  
ANISOU 1585  O   TYR A 262    16715  27985  14144    225    306    431       O  
ATOM   1586  CB  TYR A 262     -30.894   8.601  32.270  1.00154.11           C  
ANISOU 1586  CB  TYR A 262    16618  27773  14165   -132    124    187       C  
ATOM   1587  CG  TYR A 262     -32.022   8.328  33.240  1.00155.91           C  
ANISOU 1587  CG  TYR A 262    16789  27996  14454   -254     55    202       C  
ATOM   1588  CD1 TYR A 262     -33.345   8.571  32.887  1.00159.80           C  
ANISOU 1588  CD1 TYR A 262    17064  28909  14745   -305    -21    308       C  
ATOM   1589  CD2 TYR A 262     -31.767   7.820  34.511  1.00154.97           C  
ANISOU 1589  CD2 TYR A 262    16815  27488  14577   -313     67    121       C  
ATOM   1590  CE1 TYR A 262     -34.387   8.335  33.783  1.00160.85           C  
ANISOU 1590  CE1 TYR A 262    17111  29089  14914   -418    -79    336       C  
ATOM   1591  CE2 TYR A 262     -32.800   7.575  35.414  1.00155.84           C  
ANISOU 1591  CE2 TYR A 262    16866  27612  14733   -432      9    145       C  
ATOM   1592  CZ  TYR A 262     -34.111   7.830  35.045  1.00166.05           C  
ANISOU 1592  CZ  TYR A 262    17929  29342  15821   -489    -61    252       C  
ATOM   1593  OH  TYR A 262     -35.131   7.584  35.935  1.00168.66           O  
ANISOU 1593  OH  TYR A 262    18171  29735  16178   -610   -113    286       O  
ATOM   1594  N   PRO A 263     -27.855  10.071  32.593  1.00146.79           N  
ANISOU 1594  N   PRO A 263    15897  26318  13559    237    362    394       N  
ATOM   1595  CA  PRO A 263     -27.824   9.883  34.055  1.00143.87           C  
ANISOU 1595  CA  PRO A 263    15624  25598  13442    212    360    380       C  
ATOM   1596  C   PRO A 263     -27.806  11.190  34.866  1.00143.51           C  
ANISOU 1596  C   PRO A 263    15584  25406  13537    344    408    647       C  
ATOM   1597  O   PRO A 263     -27.736  11.123  36.094  1.00141.60           O  
ANISOU 1597  O   PRO A 263    15424  24881  13497    333    410    645       O  
ATOM   1598  CB  PRO A 263     -26.526   9.089  34.249  1.00145.24           C  
ANISOU 1598  CB  PRO A 263    15932  25530  13721    204    408    193       C  
ATOM   1599  CG  PRO A 263     -25.601   9.648  33.187  1.00150.87           C  
ANISOU 1599  CG  PRO A 263    16598  26418  14308    303    480    264       C  
ATOM   1600  CD  PRO A 263     -26.485  10.126  32.042  1.00148.29           C  
ANISOU 1600  CD  PRO A 263    16138  26466  13738    307    445    361       C  
ATOM   1601  N   ALA A 264     -27.872  12.361  34.196  1.00138.61           N  
ANISOU 1601  N   ALA A 264    14905  24962  12799    469    448    874       N  
ATOM   1602  CA  ALA A 264     -27.857  13.681  34.841  1.00136.63           C  
ANISOU 1602  CA  ALA A 264    14718  24553  12642    601    505   1133       C  
ATOM   1603  C   ALA A 264     -29.059  13.880  35.779  1.00137.52           C  
ANISOU 1603  C   ALA A 264    14811  24628  12814    646    463   1215       C  
ATOM   1604  O   ALA A 264     -28.903  14.482  36.842  1.00135.64           O  
ANISOU 1604  O   ALA A 264    14687  24111  12740    707    501   1318       O  
ATOM   1605  CB  ALA A 264     -27.831  14.779  33.790  1.00138.90           C  
ANISOU 1605  CB  ALA A 264    14975  25056  12746    724    554   1354       C  
ATOM   1606  N   VAL A 265     -30.233  13.333  35.408  1.00133.50           N  
ANISOU 1606  N   VAL A 265    14150  24416  12157    602    384   1160       N  
ATOM   1607  CA  VAL A 265     -31.480  13.422  36.174  1.00132.39           C  
ANISOU 1607  CA  VAL A 265    13932  24347  12022    638    340   1237       C  
ATOM   1608  C   VAL A 265     -31.392  12.625  37.509  1.00132.22           C  
ANISOU 1608  C   VAL A 265    13997  24014  12226    509    317   1084       C  
ATOM   1609  O   VAL A 265     -32.126  12.958  38.440  1.00131.66           O  
ANISOU 1609  O   VAL A 265    13912  23893  12219    577    314   1186       O  
ATOM   1610  CB  VAL A 265     -32.710  13.002  35.315  1.00138.44           C  
ANISOU 1610  CB  VAL A 265    14475  25594  12532    584    254   1218       C  
ATOM   1611  CG1 VAL A 265     -32.800  11.487  35.123  1.00138.65           C  
ANISOU 1611  CG1 VAL A 265    14473  25679  12529    300    172    919       C  
ATOM   1612  CG2 VAL A 265     -34.010  13.565  35.880  1.00138.94           C  
ANISOU 1612  CG2 VAL A 265    14410  25847  12533    719    235   1405       C  
ATOM   1613  N   ILE A 266     -30.498  11.606  37.606  1.00125.81           N  
ANISOU 1613  N   ILE A 266    13281  23000  11520    353    310    854       N  
ATOM   1614  CA  ILE A 266     -30.328  10.795  38.824  1.00123.05           C  
ANISOU 1614  CA  ILE A 266    13036  22346  11372    242    293    713       C  
ATOM   1615  C   ILE A 266     -29.903  11.701  39.987  1.00122.88           C  
ANISOU 1615  C   ILE A 266    13124  22021  11544    371    354    866       C  
ATOM   1616  O   ILE A 266     -30.518  11.639  41.054  1.00122.15           O  
ANISOU 1616  O   ILE A 266    13042  21821  11549    365    337    892       O  
ATOM   1617  CB  ILE A 266     -29.343   9.604  38.614  1.00125.70           C  
ANISOU 1617  CB  ILE A 266    13482  22520  11756    113    290    458       C  
ATOM   1618  CG1 ILE A 266     -29.964   8.546  37.688  1.00127.95           C  
ANISOU 1618  CG1 ILE A 266    13714  23054  11848    -58    219    270       C  
ATOM   1619  CG2 ILE A 266     -28.923   8.962  39.946  1.00124.55           C  
ANISOU 1619  CG2 ILE A 266    13478  22012  11835     58    294    358       C  
ATOM   1620  CD1 ILE A 266     -28.988   7.677  36.996  1.00135.84           C  
ANISOU 1620  CD1 ILE A 266    14826  23984  12804   -105    238     58       C  
ATOM   1621  N   LEU A 267     -28.910  12.580  39.754  1.00116.65           N  
ANISOU 1621  N   LEU A 267    12416  21120  10787    473    426    976       N  
ATOM   1622  CA  LEU A 267     -28.393  13.500  40.764  1.00114.25           C  
ANISOU 1622  CA  LEU A 267    12248  20524  10640    559    485   1113       C  
ATOM   1623  C   LEU A 267     -29.423  14.545  41.203  1.00117.33           C  
ANISOU 1623  C   LEU A 267    12644  20947  10989    718    502   1327       C  
ATOM   1624  O   LEU A 267     -29.318  15.035  42.327  1.00116.38           O  
ANISOU 1624  O   LEU A 267    12649  20566  11004    767    533   1395       O  
ATOM   1625  CB  LEU A 267     -27.112  14.170  40.289  1.00114.13           C  
ANISOU 1625  CB  LEU A 267    12312  20425  10626    577    553   1179       C  
ATOM   1626  CG  LEU A 267     -25.895  13.264  40.421  1.00117.74           C  
ANISOU 1626  CG  LEU A 267    12794  20758  11182    468    556    992       C  
ATOM   1627  CD1 LEU A 267     -25.396  12.813  39.068  1.00119.20           C  
ANISOU 1627  CD1 LEU A 267    12897  21181  11214    444    564    902       C  
ATOM   1628  CD2 LEU A 267     -24.817  13.903  41.266  1.00118.26           C  
ANISOU 1628  CD2 LEU A 267    12979  20567  11389    457    609   1066       C  
ATOM   1629  N   PHE A 268     -30.435  14.846  40.356  1.00114.06           N  
ANISOU 1629  N   PHE A 268    12096  20868  10375    812    483   1430       N  
ATOM   1630  CA  PHE A 268     -31.527  15.763  40.706  1.00114.06           C  
ANISOU 1630  CA  PHE A 268    12078  20962  10297   1017    504   1641       C  
ATOM   1631  C   PHE A 268     -32.361  15.132  41.819  1.00117.13           C  
ANISOU 1631  C   PHE A 268    12404  21330  10770    969    458   1571       C  
ATOM   1632  O   PHE A 268     -32.599  15.771  42.847  1.00116.35           O  
ANISOU 1632  O   PHE A 268    12411  21042  10755   1099    500   1680       O  
ATOM   1633  CB  PHE A 268     -32.392  16.095  39.474  1.00117.60           C  
ANISOU 1633  CB  PHE A 268    12358  21842  10485   1135    486   1762       C  
ATOM   1634  CG  PHE A 268     -33.796  16.574  39.770  1.00119.73           C  
ANISOU 1634  CG  PHE A 268    12510  22355  10628   1334    479   1930       C  
ATOM   1635  CD1 PHE A 268     -34.037  17.894  40.129  1.00122.90           C  
ANISOU 1635  CD1 PHE A 268    13057  22642  10999   1622    563   2175       C  
ATOM   1636  CD2 PHE A 268     -34.877  15.706  39.681  1.00122.21           C  
ANISOU 1636  CD2 PHE A 268    12576  23027  10831   1234    392   1848       C  
ATOM   1637  CE1 PHE A 268     -35.335  18.337  40.395  1.00125.19           C  
ANISOU 1637  CE1 PHE A 268    13231  23188  11148   1860    568   2340       C  
ATOM   1638  CE2 PHE A 268     -36.173  16.146  39.959  1.00126.31           C  
ANISOU 1638  CE2 PHE A 268    12944  23839  11211   1429    389   2018       C  
ATOM   1639  CZ  PHE A 268     -36.394  17.460  40.310  1.00124.96           C  
ANISOU 1639  CZ  PHE A 268    12903  23567  11007   1767    480   2266       C  
ATOM   1640  N   TYR A 269     -32.763  13.857  41.618  1.00113.47           N  
ANISOU 1640  N   TYR A 269    11793  21044  10275    766    376   1382       N  
ATOM   1641  CA  TYR A 269     -33.543  13.074  42.575  1.00112.77           C  
ANISOU 1641  CA  TYR A 269    11635  20964  10247    655    326   1298       C  
ATOM   1642  C   TYR A 269     -32.725  12.749  43.824  1.00111.95           C  
ANISOU 1642  C   TYR A 269    11715  20429  10392    584    349   1202       C  
ATOM   1643  O   TYR A 269     -33.309  12.616  44.895  1.00110.64           O  
ANISOU 1643  O   TYR A 269    11545  20196  10299    584    343   1220       O  
ATOM   1644  CB  TYR A 269     -34.083  11.797  41.928  1.00115.78           C  
ANISOU 1644  CB  TYR A 269    11862  21621  10510    408    235   1115       C  
ATOM   1645  CG  TYR A 269     -35.223  12.044  40.963  1.00120.72           C  
ANISOU 1645  CG  TYR A 269    12250  22753  10866    456    193   1221       C  
ATOM   1646  CD1 TYR A 269     -36.515  12.285  41.424  1.00124.12           C  
ANISOU 1646  CD1 TYR A 269    12500  23468  11191    531    172   1355       C  
ATOM   1647  CD2 TYR A 269     -35.019  12.004  39.589  1.00123.03           C  
ANISOU 1647  CD2 TYR A 269    12477  23280  10988    430    172   1189       C  
ATOM   1648  CE1 TYR A 269     -37.570  12.507  40.540  1.00127.73           C  
ANISOU 1648  CE1 TYR A 269    12703  24452  11375    587    129   1466       C  
ATOM   1649  CE2 TYR A 269     -36.068  12.219  38.695  1.00126.65           C  
ANISOU 1649  CE2 TYR A 269    12700  24242  11178    473    126   1292       C  
ATOM   1650  CZ  TYR A 269     -37.342  12.473  39.175  1.00136.31           C  
ANISOU 1650  CZ  TYR A 269    13732  25764  12297    554    102   1434       C  
ATOM   1651  OH  TYR A 269     -38.375  12.687  38.295  1.00141.61           O  
ANISOU 1651  OH  TYR A 269    14138  26987  12680    609     54   1548       O  
ATOM   1652  N   VAL A 270     -31.383  12.649  43.693  1.00106.28           N  
ANISOU 1652  N   VAL A 270    11140  19455   9786    534    378   1114       N  
ATOM   1653  CA  VAL A 270     -30.457  12.435  44.812  1.00103.75           C  
ANISOU 1653  CA  VAL A 270    10982  18757   9681    487    401   1041       C  
ATOM   1654  C   VAL A 270     -30.483  13.710  45.675  1.00106.85           C  
ANISOU 1654  C   VAL A 270    11492  18971  10137    661    464   1232       C  
ATOM   1655  O   VAL A 270     -30.683  13.619  46.885  1.00105.46           O  
ANISOU 1655  O   VAL A 270    11377  18618  10076    662    465   1227       O  
ATOM   1656  CB  VAL A 270     -29.020  12.057  44.340  1.00106.43           C  
ANISOU 1656  CB  VAL A 270    11402  18956  10079    413    419    920       C  
ATOM   1657  CG1 VAL A 270     -27.986  12.260  45.445  1.00104.50           C  
ANISOU 1657  CG1 VAL A 270    11307  18377  10023    415    455    917       C  
ATOM   1658  CG2 VAL A 270     -28.970  10.624  43.821  1.00106.61           C  
ANISOU 1658  CG2 VAL A 270    11383  19059  10064    254    365    697       C  
ATOM   1659  N   ASN A 271     -30.352  14.892  45.027  1.00104.03           N  
ANISOU 1659  N   ASN A 271    11183  18662   9681    810    518   1401       N  
ATOM   1660  CA  ASN A 271     -30.388  16.204  45.674  1.00103.82           C  
ANISOU 1660  CA  ASN A 271    11329  18447   9673    986    589   1588       C  
ATOM   1661  C   ASN A 271     -31.762  16.509  46.263  1.00108.64           C  
ANISOU 1661  C   ASN A 271    11881  19183  10215   1157    593   1699       C  
ATOM   1662  O   ASN A 271     -31.839  17.202  47.280  1.00108.25           O  
ANISOU 1662  O   ASN A 271    11992  18909  10229   1273    641   1785       O  
ATOM   1663  CB  ASN A 271     -29.978  17.296  44.704  1.00105.44           C  
ANISOU 1663  CB  ASN A 271    11622  18680   9759   1090    648   1743       C  
ATOM   1664  CG  ASN A 271     -28.507  17.597  44.780  1.00129.67           C  
ANISOU 1664  CG  ASN A 271    14852  21490  12928    965    685   1715       C  
ATOM   1665  OD1 ASN A 271     -28.082  18.535  45.455  1.00124.30           O  
ANISOU 1665  OD1 ASN A 271    14389  20541  12299   1000    740   1816       O  
ATOM   1666  ND2 ASN A 271     -27.691  16.795  44.109  1.00122.26           N  
ANISOU 1666  ND2 ASN A 271    13811  20639  12002    811    656   1574       N  
ATOM   1667  N   ALA A 272     -32.837  15.973  45.645  1.00105.97           N  
ANISOU 1667  N   ALA A 272    11309  19225   9732   1163    541   1694       N  
ATOM   1668  CA  ALA A 272     -34.214  16.123  46.117  1.00106.97           C  
ANISOU 1668  CA  ALA A 272    11306  19581   9759   1313    537   1800       C  
ATOM   1669  C   ALA A 272     -34.385  15.473  47.498  1.00110.25           C  
ANISOU 1669  C   ALA A 272    11740  19825  10326   1210    518   1703       C  
ATOM   1670  O   ALA A 272     -35.013  16.060  48.383  1.00110.08           O  
ANISOU 1670  O   ALA A 272    11761  19770  10296   1392    563   1820       O  
ATOM   1671  CB  ALA A 272     -35.176  15.500  45.118  1.00109.35           C  
ANISOU 1671  CB  ALA A 272    11320  20364   9863   1255    468   1783       C  
ATOM   1672  N   CYS A 273     -33.778  14.285  47.681  1.00105.90           N  
ANISOU 1672  N   CYS A 273    11181  19152   9905    940    461   1495       N  
ATOM   1673  CA  CYS A 273     -33.797  13.508  48.915  1.00104.70           C  
ANISOU 1673  CA  CYS A 273    11062  18820   9901    809    438   1389       C  
ATOM   1674  C   CYS A 273     -33.059  14.245  50.031  1.00108.58           C  
ANISOU 1674  C   CYS A 273    11786  18927  10544    911    500   1437       C  
ATOM   1675  O   CYS A 273     -33.616  14.400  51.119  1.00108.17           O  
ANISOU 1675  O   CYS A 273    11759  18817  10525    987    519   1487       O  
ATOM   1676  CB  CYS A 273     -33.206  12.123  48.678  1.00104.18           C  
ANISOU 1676  CB  CYS A 273    10984  18687   9912    534    374   1166       C  
ATOM   1677  SG  CYS A 273     -34.204  11.069  47.596  1.00109.85           S  
ANISOU 1677  SG  CYS A 273    11468  19831  10441    338    290   1071       S  
ATOM   1678  N   PHE A 274     -31.826  14.726  49.754  1.00105.36           N  
ANISOU 1678  N   PHE A 274    11542  18285  10206    903    530   1426       N  
ATOM   1679  CA  PHE A 274     -31.021  15.460  50.729  1.00104.76           C  
ANISOU 1679  CA  PHE A 274    11695  17860  10250    949    581   1464       C  
ATOM   1680  C   PHE A 274     -31.631  16.835  51.050  1.00110.72           C  
ANISOU 1680  C   PHE A 274    12583  18571  10913   1204    656   1660       C  
ATOM   1681  O   PHE A 274     -31.344  17.374  52.120  1.00110.73           O  
ANISOU 1681  O   PHE A 274    12778  18304  10992   1251    695   1687       O  
ATOM   1682  CB  PHE A 274     -29.564  15.595  50.272  1.00106.08           C  
ANISOU 1682  CB  PHE A 274    11969  17855  10481    838    590   1410       C  
ATOM   1683  CG  PHE A 274     -28.797  14.297  50.336  1.00107.20           C  
ANISOU 1683  CG  PHE A 274    12044  17955  10731    642    535   1218       C  
ATOM   1684  CD1 PHE A 274     -28.254  13.849  51.535  1.00109.52           C  
ANISOU 1684  CD1 PHE A 274    12420  18022  11172    567    523   1139       C  
ATOM   1685  CD2 PHE A 274     -28.601  13.528  49.196  1.00110.91           C  
ANISOU 1685  CD2 PHE A 274    12390  18610  11141    555    502   1119       C  
ATOM   1686  CE1 PHE A 274     -27.541  12.645  51.594  1.00110.17           C  
ANISOU 1686  CE1 PHE A 274    12464  18058  11338    433    481    976       C  
ATOM   1687  CE2 PHE A 274     -27.889  12.324  49.255  1.00113.43           C  
ANISOU 1687  CE2 PHE A 274    12691  18865  11542    418    464    941       C  
ATOM   1688  CZ  PHE A 274     -27.369  11.888  50.454  1.00110.31           C  
ANISOU 1688  CZ  PHE A 274    12382  18239  11291    370    456    877       C  
ATOM   1689  N   PHE A 275     -32.502  17.375  50.166  1.00108.35           N  
ANISOU 1689  N   PHE A 275    12192  18542  10434   1384    678   1795       N  
ATOM   1690  CA  PHE A 275     -33.178  18.645  50.424  1.00109.51           C  
ANISOU 1690  CA  PHE A 275    12481  18664  10466   1686    760   1993       C  
ATOM   1691  C   PHE A 275     -34.340  18.438  51.396  1.00114.03           C  
ANISOU 1691  C   PHE A 275    12950  19369  11008   1816    765   2026       C  
ATOM   1692  O   PHE A 275     -34.453  19.188  52.366  1.00113.69           O  
ANISOU 1692  O   PHE A 275    13112  19109  10978   1984    830   2100       O  
ATOM   1693  CB  PHE A 275     -33.667  19.310  49.131  1.00113.26           C  
ANISOU 1693  CB  PHE A 275    12896  19398  10740   1871    788   2147       C  
ATOM   1694  CG  PHE A 275     -34.462  20.574  49.369  1.00116.97           C  
ANISOU 1694  CG  PHE A 275    13523  19859  11062   2240    882   2365       C  
ATOM   1695  CD1 PHE A 275     -33.830  21.751  49.754  1.00120.71           C  
ANISOU 1695  CD1 PHE A 275    14376  19936  11551   2351    970   2457       C  
ATOM   1696  CD2 PHE A 275     -35.845  20.581  49.228  1.00120.99           C  
ANISOU 1696  CD2 PHE A 275    13812  20761  11396   2477    886   2480       C  
ATOM   1697  CE1 PHE A 275     -34.569  22.912  49.998  1.00123.87           C  
ANISOU 1697  CE1 PHE A 275    14980  20286  11801   2723   1069   2654       C  
ATOM   1698  CE2 PHE A 275     -36.582  21.743  49.465  1.00126.03           C  
ANISOU 1698  CE2 PHE A 275    14606  21402  11879   2876    985   2690       C  
ATOM   1699  CZ  PHE A 275     -35.939  22.901  49.848  1.00124.64           C  
ANISOU 1699  CZ  PHE A 275    14854  20780  11725   3012   1080   2772       C  
ATOM   1700  N   VAL A 276     -35.205  17.431  51.122  1.00111.28           N  
ANISOU 1700  N   VAL A 276    12293  19389  10601   1725    697   1972       N  
ATOM   1701  CA  VAL A 276     -36.370  17.056  51.941  1.00111.77           C  
ANISOU 1701  CA  VAL A 276    12187  19671  10611   1792    691   2002       C  
ATOM   1702  C   VAL A 276     -35.877  16.651  53.342  1.00114.11           C  
ANISOU 1702  C   VAL A 276    12622  19638  11095   1666    690   1894       C  
ATOM   1703  O   VAL A 276     -36.456  17.083  54.342  1.00114.03           O  
ANISOU 1703  O   VAL A 276    12668  19598  11062   1843    742   1973       O  
ATOM   1704  CB  VAL A 276     -37.212  15.942  51.249  1.00116.44           C  
ANISOU 1704  CB  VAL A 276    12428  20716  11097   1611    603   1942       C  
ATOM   1705  CG1 VAL A 276     -38.172  15.253  52.216  1.00116.61           C  
ANISOU 1705  CG1 VAL A 276    12276  20927  11105   1545    581   1927       C  
ATOM   1706  CG2 VAL A 276     -37.976  16.500  50.054  1.00118.50           C  
ANISOU 1706  CG2 VAL A 276    12519  21382  11122   1806    611   2092       C  
ATOM   1707  N   GLY A 277     -34.788  15.878  53.383  1.00109.09           N  
ANISOU 1707  N   GLY A 277    12051  18771  10628   1391    638   1724       N  
ATOM   1708  CA  GLY A 277     -34.145  15.430  54.614  1.00107.41           C  
ANISOU 1708  CA  GLY A 277    11969  18250  10591   1259    629   1618       C  
ATOM   1709  C   GLY A 277     -33.638  16.572  55.476  1.00110.65           C  
ANISOU 1709  C   GLY A 277    12665  18332  11046   1420    703   1691       C  
ATOM   1710  O   GLY A 277     -33.784  16.529  56.702  1.00109.53           O  
ANISOU 1710  O   GLY A 277    12598  18056  10962   1443    720   1679       O  
ATOM   1711  N   SER A 278     -33.060  17.619  54.829  1.00107.17           N  
ANISOU 1711  N   SER A 278    12403  17759  10558   1521    750   1770       N  
ATOM   1712  CA  SER A 278     -32.538  18.820  55.489  1.00106.84           C  
ANISOU 1712  CA  SER A 278    12688  17381  10524   1643    824   1841       C  
ATOM   1713  C   SER A 278     -33.654  19.623  56.153  1.00111.54           C  
ANISOU 1713  C   SER A 278    13369  18017  10994   1960    903   1980       C  
ATOM   1714  O   SER A 278     -33.431  20.184  57.225  1.00110.91           O  
ANISOU 1714  O   SER A 278    13534  17661  10947   2023    950   1984       O  
ATOM   1715  CB  SER A 278     -31.785  19.699  54.500  1.00110.63           C  
ANISOU 1715  CB  SER A 278    13334  17748  10952   1650    858   1909       C  
ATOM   1716  OG  SER A 278     -30.570  19.075  54.121  1.00119.45           O  
ANISOU 1716  OG  SER A 278    14411  18790  12186   1370    801   1780       O  
ATOM   1717  N   ILE A 279     -34.855  19.656  55.528  1.00109.10           N  
ANISOU 1717  N   ILE A 279    12852  18078  10525   2164    917   2092       N  
ATOM   1718  CA  ILE A 279     -36.050  20.343  56.035  1.00110.61           C  
ANISOU 1718  CA  ILE A 279    13058  18413  10557   2519    997   2243       C  
ATOM   1719  C   ILE A 279     -36.440  19.719  57.389  1.00113.43           C  
ANISOU 1719  C   ILE A 279    13344  18768  10985   2469    986   2173       C  
ATOM   1720  O   ILE A 279     -36.718  20.452  58.342  1.00113.80           O  
ANISOU 1720  O   ILE A 279    13598  18657  10984   2694   1066   2236       O  
ATOM   1721  CB  ILE A 279     -37.211  20.300  54.986  1.00115.73           C  
ANISOU 1721  CB  ILE A 279    13407  19560  11004   2707    994   2373       C  
ATOM   1722  CG1 ILE A 279     -36.828  20.993  53.642  1.00117.18           C  
ANISOU 1722  CG1 ILE A 279    13681  19743  11098   2784   1013   2462       C  
ATOM   1723  CG2 ILE A 279     -38.541  20.838  55.535  1.00119.07           C  
ANISOU 1723  CG2 ILE A 279    13763  20238  11239   3092   1074   2535       C  
ATOM   1724  CD1 ILE A 279     -36.411  22.529  53.667  1.00125.80           C  
ANISOU 1724  CD1 ILE A 279    15216  20464  12119   3050   1128   2599       C  
ATOM   1725  N   GLY A 280     -36.391  18.385  57.463  1.00108.36           N  
ANISOU 1725  N   GLY A 280    12452  18270  10451   2169    893   2040       N  
ATOM   1726  CA  GLY A 280     -36.679  17.621  58.672  1.00107.40           C  
ANISOU 1726  CA  GLY A 280    12251  18149  10405   2062    872   1969       C  
ATOM   1727  C   GLY A 280     -35.664  17.842  59.776  1.00110.34           C  
ANISOU 1727  C   GLY A 280    12916  18081  10927   1980    886   1883       C  
ATOM   1728  O   GLY A 280     -36.039  17.958  60.945  1.00110.44           O  
ANISOU 1728  O   GLY A 280    12995  18035  10932   2078    925   1899       O  
ATOM   1729  N   TRP A 281     -34.373  17.917  59.408  1.00105.88           N  
ANISOU 1729  N   TRP A 281    12513  17237  10479   1800    854   1797       N  
ATOM   1730  CA  TRP A 281     -33.272  18.143  60.345  1.00104.68           C  
ANISOU 1730  CA  TRP A 281    12620  16703  10451   1684    855   1715       C  
ATOM   1731  C   TRP A 281     -33.249  19.585  60.868  1.00109.75           C  
ANISOU 1731  C   TRP A 281    13604  17093  11002   1917    951   1808       C  
ATOM   1732  O   TRP A 281     -32.795  19.805  61.989  1.00109.51           O  
ANISOU 1732  O   TRP A 281    13774  16812  11023   1877    964   1757       O  
ATOM   1733  CB  TRP A 281     -31.927  17.806  59.693  1.00102.34           C  
ANISOU 1733  CB  TRP A 281    12352  16263  10271   1426    795   1613       C  
ATOM   1734  CG  TRP A 281     -31.537  16.365  59.822  1.00101.95           C  
ANISOU 1734  CG  TRP A 281    12110  16275  10351   1179    709   1475       C  
ATOM   1735  CD1 TRP A 281     -31.658  15.392  58.873  1.00104.68           C  
ANISOU 1735  CD1 TRP A 281    12234  16834  10707   1054    653   1416       C  
ATOM   1736  CD2 TRP A 281     -30.964  15.734  60.974  1.00100.56           C  
ANISOU 1736  CD2 TRP A 281    11981  15930  10296   1041    675   1380       C  
ATOM   1737  NE1 TRP A 281     -31.192  14.193  59.361  1.00102.96           N  
ANISOU 1737  NE1 TRP A 281    11951  16559  10609    857    593   1290       N  
ATOM   1738  CE2 TRP A 281     -30.760  14.374  60.649  1.00103.59           C  
ANISOU 1738  CE2 TRP A 281    12182  16417  10761    855    604   1275       C  
ATOM   1739  CE3 TRP A 281     -30.591  16.188  62.249  1.00101.53           C  
ANISOU 1739  CE3 TRP A 281    12301  15824  10453   1060    697   1374       C  
ATOM   1740  CZ2 TRP A 281     -30.209  13.463  61.554  1.00101.77           C  
ANISOU 1740  CZ2 TRP A 281    11960  16063  10644    715    561   1181       C  
ATOM   1741  CZ3 TRP A 281     -30.043  15.285  63.145  1.00101.86           C  
ANISOU 1741  CZ3 TRP A 281    12317  15778  10607    906    646   1278       C  
ATOM   1742  CH2 TRP A 281     -29.861  13.940  62.797  1.00101.73           C  
ANISOU 1742  CH2 TRP A 281    12117  15863  10670    749    581   1192       C  
ATOM   1743  N   LEU A 282     -33.727  20.558  60.067  1.00107.42           N  
ANISOU 1743  N   LEU A 282    13401  16855  10557   2161   1019   1943       N  
ATOM   1744  CA  LEU A 282     -33.755  21.979  60.437  1.00108.62           C  
ANISOU 1744  CA  LEU A 282    13940  16736  10594   2410   1125   2041       C  
ATOM   1745  C   LEU A 282     -35.061  22.398  61.129  1.00113.11           C  
ANISOU 1745  C   LEU A 282    14520  17446  11010   2782   1212   2149       C  
ATOM   1746  O   LEU A 282     -35.135  23.522  61.636  1.00114.57           O  
ANISOU 1746  O   LEU A 282    15068  17374  11090   3019   1309   2215       O  
ATOM   1747  CB  LEU A 282     -33.538  22.869  59.198  1.00110.06           C  
ANISOU 1747  CB  LEU A 282    14270  16870  10676   2506   1167   2149       C  
ATOM   1748  CG  LEU A 282     -32.113  22.986  58.665  1.00113.53           C  
ANISOU 1748  CG  LEU A 282    14847  17072  11215   2192   1124   2077       C  
ATOM   1749  CD1 LEU A 282     -32.123  23.370  57.206  1.00114.52           C  
ANISOU 1749  CD1 LEU A 282    14936  17326  11250   2252   1139   2180       C  
ATOM   1750  CD2 LEU A 282     -31.293  23.993  59.468  1.00116.63           C  
ANISOU 1750  CD2 LEU A 282    15690  17020  11603   2130   1175   2061       C  
ATOM   1751  N   ALA A 283     -36.080  21.508  61.145  1.00108.71           N  
ANISOU 1751  N   ALA A 283    13579  17302  10424   2829   1181   2169       N  
ATOM   1752  CA  ALA A 283     -37.404  21.742  61.742  1.00110.13           C  
ANISOU 1752  CA  ALA A 283    13667  17738  10440   3173   1258   2282       C  
ATOM   1753  C   ALA A 283     -37.325  22.170  63.213  1.00112.60           C  
ANISOU 1753  C   ALA A 283    14255  17774  10754   3275   1321   2247       C  
ATOM   1754  O   ALA A 283     -37.996  23.122  63.604  1.00113.68           O  
ANISOU 1754  O   ALA A 283    14590  17885  10717   3661   1435   2358       O  
ATOM   1755  CB  ALA A 283     -38.257  20.489  61.621  1.00110.55           C  
ANISOU 1755  CB  ALA A 283    13244  18266  10493   3049   1187   2272       C  
ATOM   1756  N   GLN A 284     -36.470  21.488  63.995  1.00106.78           N  
ANISOU 1756  N   GLN A 284    13546  16828  10196   2945   1249   2093       N  
ATOM   1757  CA  GLN A 284     -36.210  21.700  65.423  1.00106.35           C  
ANISOU 1757  CA  GLN A 284    13728  16515  10166   2951   1281   2027       C  
ATOM   1758  C   GLN A 284     -35.799  23.146  65.775  1.00113.25           C  
ANISOU 1758  C   GLN A 284    15114  16977  10940   3149   1379   2054       C  
ATOM   1759  O   GLN A 284     -36.023  23.576  66.910  1.00113.92           O  
ANISOU 1759  O   GLN A 284    15414  16916  10954   3305   1444   2042       O  
ATOM   1760  CB  GLN A 284     -35.106  20.735  65.904  1.00104.66           C  
ANISOU 1760  CB  GLN A 284    13461  16141  10164   2529   1170   1863       C  
ATOM   1761  CG  GLN A 284     -33.829  20.784  65.061  1.00103.12           C  
ANISOU 1761  CG  GLN A 284    13361  15735  10083   2262   1105   1792       C  
ATOM   1762  CD  GLN A 284     -32.646  20.106  65.688  1.00110.81           C  
ANISOU 1762  CD  GLN A 284    14356  16523  11226   1922   1018   1648       C  
ATOM   1763  OE1 GLN A 284     -32.234  20.410  66.810  1.00105.78           O  
ANISOU 1763  OE1 GLN A 284    13936  15662  10595   1890   1030   1596       O  
ATOM   1764  NE2 GLN A 284     -32.019  19.233  64.929  1.00 99.17           N  
ANISOU 1764  NE2 GLN A 284    12673  15137   9872   1676    931   1583       N  
ATOM   1765  N   PHE A 285     -35.198  23.880  64.819  1.00111.44           N  
ANISOU 1765  N   PHE A 285    15098  16552  10693   3128   1391   2087       N  
ATOM   1766  CA  PHE A 285     -34.700  25.240  65.026  1.00114.04           C  
ANISOU 1766  CA  PHE A 285    15961  16444  10923   3244   1479   2109       C  
ATOM   1767  C   PHE A 285     -35.808  26.300  65.015  1.00123.44           C  
ANISOU 1767  C   PHE A 285    17373  17655  11874   3770   1626   2269       C  
ATOM   1768  O   PHE A 285     -35.526  27.472  65.288  1.00125.04           O  
ANISOU 1768  O   PHE A 285    18084  17461  11964   3914   1719   2290       O  
ATOM   1769  CB  PHE A 285     -33.599  25.574  64.011  1.00115.62           C  
ANISOU 1769  CB  PHE A 285    16304  16439  11188   2982   1436   2093       C  
ATOM   1770  CG  PHE A 285     -32.397  24.686  64.207  1.00114.67           C  
ANISOU 1770  CG  PHE A 285    16034  16261  11273   2510   1309   1935       C  
ATOM   1771  CD1 PHE A 285     -31.499  24.923  65.242  1.00117.44           C  
ANISOU 1771  CD1 PHE A 285    16655  16297  11670   2293   1290   1823       C  
ATOM   1772  CD2 PHE A 285     -32.195  23.578  63.398  1.00115.13           C  
ANISOU 1772  CD2 PHE A 285    15682  16604  11460   2300   1211   1898       C  
ATOM   1773  CE1 PHE A 285     -30.414  24.076  65.452  1.00116.26           C  
ANISOU 1773  CE1 PHE A 285    16336  16149  11688   1899   1175   1694       C  
ATOM   1774  CE2 PHE A 285     -31.105  22.733  63.605  1.00116.00           C  
ANISOU 1774  CE2 PHE A 285    15661  16674  11739   1923   1106   1761       C  
ATOM   1775  CZ  PHE A 285     -30.226  22.985  64.634  1.00113.77           C  
ANISOU 1775  CZ  PHE A 285    15619  16110  11498   1738   1089   1669       C  
ATOM   1776  N   MET A 286     -37.065  25.891  64.758  1.00122.55           N  
ANISOU 1776  N   MET A 286    16894  18007  11664   4059   1653   2381       N  
ATOM   1777  CA  MET A 286     -38.223  26.780  64.848  1.00126.34           C  
ANISOU 1777  CA  MET A 286    17513  18599  11893   4616   1798   2546       C  
ATOM   1778  C   MET A 286     -38.574  26.974  66.327  1.00132.57           C  
ANISOU 1778  C   MET A 286    18480  19277  12611   4790   1870   2500       C  
ATOM   1779  O   MET A 286     -38.307  26.084  67.147  1.00129.80           O  
ANISOU 1779  O   MET A 286    17938  18977  12402   4502   1791   2374       O  
ATOM   1780  CB  MET A 286     -39.414  26.213  64.078  1.00129.44           C  
ANISOU 1780  CB  MET A 286    17392  19603  12186   4827   1790   2685       C  
ATOM   1781  CG  MET A 286     -39.391  26.525  62.611  1.00134.07           C  
ANISOU 1781  CG  MET A 286    17928  20292  12720   4883   1781   2794       C  
ATOM   1782  SD  MET A 286     -40.822  25.812  61.765  1.00139.77           S  
ANISOU 1782  SD  MET A 286    18013  21797  13296   5095   1756   2949       S  
ATOM   1783  CE  MET A 286     -42.154  26.894  62.367  1.00140.81           C  
ANISOU 1783  CE  MET A 286    18305  22093  13101   5827   1946   3154       C  
ATOM   1784  N   ASP A 287     -39.161  28.136  66.669  1.00133.55           N  
ANISOU 1784  N   ASP A 287    18993  19243  12506   5276   2026   2603       N  
ATOM   1785  CA  ASP A 287     -39.525  28.514  68.039  1.00135.22           C  
ANISOU 1785  CA  ASP A 287    19455  19320  12605   5515   2121   2565       C  
ATOM   1786  C   ASP A 287     -40.365  27.426  68.741  1.00137.23           C  
ANISOU 1786  C   ASP A 287    19188  20079  12876   5521   2086   2562       C  
ATOM   1787  O   ASP A 287     -41.532  27.215  68.405  1.00138.11           O  
ANISOU 1787  O   ASP A 287    18934  20696  12844   5838   2131   2712       O  
ATOM   1788  CB  ASP A 287     -40.260  29.865  68.047  1.00141.93           C  
ANISOU 1788  CB  ASP A 287    20742  20024  13162   6136   2309   2713       C  
ATOM   1789  CG  ASP A 287     -39.393  31.038  67.624  1.00158.08           C  
ANISOU 1789  CG  ASP A 287    23432  21465  15166   6112   2362   2703       C  
ATOM   1790  OD1 ASP A 287     -38.989  31.084  66.432  1.00159.41           O  
ANISOU 1790  OD1 ASP A 287    23545  21625  15397   5956   2311   2760       O  
ATOM   1791  OD2 ASP A 287     -39.128  31.917  68.476  1.00165.42           O  
ANISOU 1791  OD2 ASP A 287    24936  21931  15986   6236   2458   2640       O  
ATOM   1792  N   GLY A 288     -39.716  26.718  69.666  1.00131.11           N  
ANISOU 1792  N   GLY A 288    18369  19176  12270   5137   2000   2399       N  
ATOM   1793  CA  GLY A 288     -40.306  25.649  70.468  1.00129.61           C  
ANISOU 1793  CA  GLY A 288    17755  19373  12119   5053   1959   2377       C  
ATOM   1794  C   GLY A 288     -40.690  24.377  69.733  1.00130.96           C  
ANISOU 1794  C   GLY A 288    17319  20039  12402   4804   1846   2412       C  
ATOM   1795  O   GLY A 288     -41.424  23.549  70.285  1.00130.29           O  
ANISOU 1795  O   GLY A 288    16866  20341  12297   4784   1832   2436       O  
ATOM   1796  N   ALA A 289     -40.185  24.197  68.495  1.00125.68           N  
ANISOU 1796  N   ALA A 289    16557  19355  11840   4588   1764   2411       N  
ATOM   1797  CA  ALA A 289     -40.482  23.030  67.661  1.00123.63           C  
ANISOU 1797  CA  ALA A 289    15776  19524  11674   4331   1654   2427       C  
ATOM   1798  C   ALA A 289     -39.784  21.767  68.151  1.00123.55           C  
ANISOU 1798  C   ALA A 289    15582  19467  11895   3833   1523   2271       C  
ATOM   1799  O   ALA A 289     -40.391  20.698  68.119  1.00122.24           O  
ANISOU 1799  O   ALA A 289    15001  19693  11751   3681   1466   2286       O  
ATOM   1800  CB  ALA A 289     -40.095  23.301  66.224  1.00124.16           C  
ANISOU 1800  CB  ALA A 289    15853  19555  11766   4277   1616   2465       C  
ATOM   1801  N   ARG A 290     -38.521  21.885  68.609  1.00118.30           N  
ANISOU 1801  N   ARG A 290    15230  18335  11384   3578   1478   2129       N  
ATOM   1802  CA  ARG A 290     -37.721  20.762  69.112  1.00115.43           C  
ANISOU 1802  CA  ARG A 290    14742  17887  11229   3145   1361   1986       C  
ATOM   1803  C   ARG A 290     -38.446  20.025  70.243  1.00119.57           C  
ANISOU 1803  C   ARG A 290    15059  18648  11726   3153   1371   1992       C  
ATOM   1804  O   ARG A 290     -38.482  18.797  70.242  1.00117.83           O  
ANISOU 1804  O   ARG A 290    14533  18621  11616   2868   1284   1953       O  
ATOM   1805  CB  ARG A 290     -36.339  21.246  69.586  1.00113.60           C  
ANISOU 1805  CB  ARG A 290    14904  17157  11102   2952   1333   1860       C  
ATOM   1806  CG  ARG A 290     -35.300  20.133  69.688  1.00116.29           C  
ANISOU 1806  CG  ARG A 290    15104  17421  11660   2514   1201   1728       C  
ATOM   1807  CD  ARG A 290     -33.997  20.621  70.291  1.00118.27           C  
ANISOU 1807  CD  ARG A 290    15701  17260  11976   2330   1174   1616       C  
ATOM   1808  NE  ARG A 290     -33.147  21.281  69.302  1.00120.06           N  
ANISOU 1808  NE  ARG A 290    16109  17281  12226   2232   1159   1606       N  
ATOM   1809  CZ  ARG A 290     -32.970  22.595  69.214  1.00132.56           C  
ANISOU 1809  CZ  ARG A 290    18083  18595  13690   2381   1238   1638       C  
ATOM   1810  NH1 ARG A 290     -33.579  23.414  70.063  1.00117.62           N  
ANISOU 1810  NH1 ARG A 290    16463  16586  11641   2666   1341   1672       N  
ATOM   1811  NH2 ARG A 290     -32.176  23.101  68.280  1.00120.77           N  
ANISOU 1811  NH2 ARG A 290    16731  16937  12219   2246   1219   1638       N  
ATOM   1812  N   ARG A 291     -39.063  20.778  71.166  1.00118.08           N  
ANISOU 1812  N   ARG A 291    15047  18449  11369   3488   1486   2049       N  
ATOM   1813  CA  ARG A 291     -39.801  20.231  72.303  1.00118.43           C  
ANISOU 1813  CA  ARG A 291    14916  18732  11349   3540   1517   2072       C  
ATOM   1814  C   ARG A 291     -41.158  19.657  71.858  1.00122.96           C  
ANISOU 1814  C   ARG A 291    15028  19891  11799   3657   1537   2213       C  
ATOM   1815  O   ARG A 291     -41.675  18.760  72.516  1.00122.36           O  
ANISOU 1815  O   ARG A 291    14686  20084  11722   3523   1518   2227       O  
ATOM   1816  CB  ARG A 291     -39.974  21.287  73.405  1.00121.81           C  
ANISOU 1816  CB  ARG A 291    15712  18955  11615   3881   1642   2078       C  
ATOM   1817  CG  ARG A 291     -38.639  21.782  73.956  1.00136.05           C  
ANISOU 1817  CG  ARG A 291    17959  20212  13520   3697   1609   1928       C  
ATOM   1818  CD  ARG A 291     -38.798  22.628  75.200  1.00155.09           C  
ANISOU 1818  CD  ARG A 291    20731  22427  15771   3965   1718   1905       C  
ATOM   1819  NE  ARG A 291     -37.643  23.508  75.390  1.00169.80           N  
ANISOU 1819  NE  ARG A 291    23095  23763  17660   3857   1710   1787       N  
ATOM   1820  CZ  ARG A 291     -37.473  24.320  76.429  1.00188.63           C  
ANISOU 1820  CZ  ARG A 291    25896  25860  19915   4002   1786   1723       C  
ATOM   1821  NH1 ARG A 291     -38.380  24.368  77.398  1.00178.93           N  
ANISOU 1821  NH1 ARG A 291    24641  24819  18524   4299   1883   1766       N  
ATOM   1822  NH2 ARG A 291     -36.392  25.084  76.511  1.00176.27           N  
ANISOU 1822  NH2 ARG A 291    24778  23832  18364   3834   1766   1613       N  
ATOM   1823  N   GLU A 292     -41.715  20.148  70.736  1.00120.60           N  
ANISOU 1823  N   GLU A 292    14629  19809  11386   3879   1572   2324       N  
ATOM   1824  CA  GLU A 292     -42.978  19.653  70.173  1.00121.77           C  
ANISOU 1824  CA  GLU A 292    14313  20566  11390   3969   1580   2465       C  
ATOM   1825  C   GLU A 292     -42.741  18.281  69.496  1.00122.00           C  
ANISOU 1825  C   GLU A 292    14010  20755  11587   3472   1433   2395       C  
ATOM   1826  O   GLU A 292     -43.636  17.431  69.502  1.00122.29           O  
ANISOU 1826  O   GLU A 292    13656  21257  11552   3351   1408   2460       O  
ATOM   1827  CB  GLU A 292     -43.561  20.692  69.181  1.00125.62           C  
ANISOU 1827  CB  GLU A 292    14830  21217  11684   4391   1662   2609       C  
ATOM   1828  CG  GLU A 292     -44.803  20.273  68.397  1.00138.73           C  
ANISOU 1828  CG  GLU A 292    15990  23549  13170   4485   1659   2764       C  
ATOM   1829  CD  GLU A 292     -46.072  19.976  69.179  1.00163.46           C  
ANISOU 1829  CD  GLU A 292    18787  27220  16099   4668   1728   2887       C  
ATOM   1830  OE1 GLU A 292     -46.370  20.717  70.144  1.00164.95           O  
ANISOU 1830  OE1 GLU A 292    19186  27333  16154   5043   1854   2933       O  
ATOM   1831  OE2 GLU A 292     -46.793  19.027  68.795  1.00157.39           O  
ANISOU 1831  OE2 GLU A 292    17549  26970  15283   4436   1661   2942       O  
ATOM   1832  N   ILE A 293     -41.524  18.068  68.950  1.00114.56           N  
ANISOU 1832  N   ILE A 293    13245  19429  10855   3180   1340   2262       N  
ATOM   1833  CA  ILE A 293     -41.137  16.842  68.245  1.00111.94           C  
ANISOU 1833  CA  ILE A 293    12686  19165  10681   2742   1210   2176       C  
ATOM   1834  C   ILE A 293     -40.527  15.801  69.207  1.00113.32           C  
ANISOU 1834  C   ILE A 293    12884  19145  11028   2396   1142   2056       C  
ATOM   1835  O   ILE A 293     -40.837  14.618  69.075  1.00112.58           O  
ANISOU 1835  O   ILE A 293    12529  19271  10976   2102   1072   2036       O  
ATOM   1836  CB  ILE A 293     -40.162  17.173  67.071  1.00113.65           C  
ANISOU 1836  CB  ILE A 293    13063  19115  11005   2652   1158   2111       C  
ATOM   1837  CG1 ILE A 293     -40.812  18.137  66.049  1.00116.19           C  
ANISOU 1837  CG1 ILE A 293    13352  19653  11144   2992   1223   2249       C  
ATOM   1838  CG2 ILE A 293     -39.651  15.901  66.364  1.00112.36           C  
ANISOU 1838  CG2 ILE A 293    12714  18976  11001   2221   1031   2001       C  
ATOM   1839  CD1 ILE A 293     -39.824  19.064  65.303  1.00123.59           C  
ANISOU 1839  CD1 ILE A 293    14620  20205  12135   3057   1232   2221       C  
ATOM   1840  N   VAL A 294     -39.670  16.226  70.153  1.00108.55           N  
ANISOU 1840  N   VAL A 294    12603  18135  10506   2423   1161   1978       N  
ATOM   1841  CA  VAL A 294     -38.963  15.302  71.048  1.00106.72           C  
ANISOU 1841  CA  VAL A 294    12417  17700  10431   2123   1095   1871       C  
ATOM   1842  C   VAL A 294     -39.732  15.010  72.363  1.00111.94           C  
ANISOU 1842  C   VAL A 294    12994  18538  11000   2190   1149   1927       C  
ATOM   1843  O   VAL A 294     -39.774  13.844  72.767  1.00110.74           O  
ANISOU 1843  O   VAL A 294    12689  18465  10922   1910   1092   1901       O  
ATOM   1844  CB  VAL A 294     -37.522  15.806  71.332  1.00109.25           C  
ANISOU 1844  CB  VAL A 294    13094  17531  10884   2058   1067   1753       C  
ATOM   1845  CG1 VAL A 294     -36.774  14.894  72.305  1.00107.99           C  
ANISOU 1845  CG1 VAL A 294    12976  17191  10864   1794   1000   1658       C  
ATOM   1846  CG2 VAL A 294     -36.734  15.950  70.036  1.00107.93           C  
ANISOU 1846  CG2 VAL A 294    12971  17230  10808   1948   1010   1702       C  
ATOM   1847  N   CYS A 295     -40.302  16.032  73.034  1.00110.69           N  
ANISOU 1847  N   CYS A 295    12959  18425  10672   2555   1264   2004       N  
ATOM   1848  CA  CYS A 295     -40.988  15.834  74.319  1.00111.95           C  
ANISOU 1848  CA  CYS A 295    13053  18757  10726   2646   1327   2057       C  
ATOM   1849  C   CYS A 295     -42.407  15.291  74.173  1.00116.77           C  
ANISOU 1849  C   CYS A 295    13250  19941  11176   2681   1361   2199       C  
ATOM   1850  O   CYS A 295     -43.123  15.624  73.228  1.00118.00           O  
ANISOU 1850  O   CYS A 295    13220  20402  11211   2842   1387   2292       O  
ATOM   1851  CB  CYS A 295     -41.002  17.112  75.158  1.00114.02           C  
ANISOU 1851  CB  CYS A 295    13639  18832  10852   3029   1442   2069       C  
ATOM   1852  SG  CYS A 295     -39.393  17.926  75.351  1.00116.49           S  
ANISOU 1852  SG  CYS A 295    14460  18504  11299   2966   1408   1910       S  
ATOM   1853  N   ARG A 296     -42.821  14.506  75.179  1.00112.56           N  
ANISOU 1853  N   ARG A 296    12576  19574  10620   2538   1365   2225       N  
ATOM   1854  CA  ARG A 296     -44.169  13.978  75.344  1.00114.09           C  
ANISOU 1854  CA  ARG A 296    12380  20334  10634   2537   1407   2368       C  
ATOM   1855  C   ARG A 296     -45.000  15.024  76.095  1.00119.66           C  
ANISOU 1855  C   ARG A 296    13111  21257  11095   3025   1558   2481       C  
ATOM   1856  O   ARG A 296     -44.433  16.005  76.589  1.00118.87           O  
ANISOU 1856  O   ARG A 296    13379  20794  10993   3297   1618   2423       O  
ATOM   1857  CB  ARG A 296     -44.134  12.651  76.108  1.00113.35           C  
ANISOU 1857  CB  ARG A 296    12171  20272  10626   2135   1347   2347       C  
ATOM   1858  CG  ARG A 296     -44.177  11.430  75.219  1.00123.63           C  
ANISOU 1858  CG  ARG A 296    13252  21697  12023   1695   1236   2323       C  
ATOM   1859  CD  ARG A 296     -44.240  10.184  76.065  1.00137.40           C  
ANISOU 1859  CD  ARG A 296    14930  23459  13818   1332   1198   2324       C  
ATOM   1860  NE  ARG A 296     -44.134   8.967  75.267  1.00151.06           N  
ANISOU 1860  NE  ARG A 296    16549  25199  15648    887   1092   2276       N  
ATOM   1861  CZ  ARG A 296     -45.109   8.075  75.130  1.00172.18           C  
ANISOU 1861  CZ  ARG A 296    18928  28286  18206    600   1077   2362       C  
ATOM   1862  NH1 ARG A 296     -46.273   8.253  75.744  1.00164.60           N  
ANISOU 1862  NH1 ARG A 296    17706  27810  17024    714   1161   2516       N  
ATOM   1863  NH2 ARG A 296     -44.925   6.994  74.386  1.00160.26           N  
ANISOU 1863  NH2 ARG A 296    17392  26715  16785    186    979   2294       N  
ATOM   1864  N   ALA A 297     -46.335  14.823  76.186  1.00118.23           N  
ANISOU 1864  N   ALA A 297    12551  21679  10693   3134   1623   2642       N  
ATOM   1865  CA  ALA A 297     -47.248  15.744  76.864  1.00120.55           C  
ANISOU 1865  CA  ALA A 297    12817  22268  10717   3637   1779   2769       C  
ATOM   1866  C   ALA A 297     -46.873  15.938  78.336  1.00123.62           C  
ANISOU 1866  C   ALA A 297    13482  22381  11109   3728   1839   2711       C  
ATOM   1867  O   ALA A 297     -46.928  17.067  78.830  1.00124.54           O  
ANISOU 1867  O   ALA A 297    13866  22366  11087   4181   1957   2718       O  
ATOM   1868  CB  ALA A 297     -48.677  15.238  76.752  1.00124.16           C  
ANISOU 1868  CB  ALA A 297    12751  23482  10942   3637   1817   2953       C  
ATOM   1869  N   ASP A 298     -46.456  14.846  79.016  1.00118.17           N  
ANISOU 1869  N   ASP A 298    12758  21576  10565   3302   1759   2649       N  
ATOM   1870  CA  ASP A 298     -46.078  14.838  80.431  1.00117.25           C  
ANISOU 1870  CA  ASP A 298    12863  21232  10454   3320   1798   2597       C  
ATOM   1871  C   ASP A 298     -44.706  15.486  80.693  1.00119.45           C  
ANISOU 1871  C   ASP A 298    13639  20850  10895   3356   1763   2423       C  
ATOM   1872  O   ASP A 298     -44.520  16.103  81.741  1.00119.56           O  
ANISOU 1872  O   ASP A 298    13917  20686  10825   3579   1838   2385       O  
ATOM   1873  CB  ASP A 298     -46.109  13.404  81.002  1.00117.78           C  
ANISOU 1873  CB  ASP A 298    12725  21414  10611   2847   1722   2611       C  
ATOM   1874  CG  ASP A 298     -45.611  12.304  80.081  1.00121.44           C  
ANISOU 1874  CG  ASP A 298    13086  21764  11291   2360   1575   2551       C  
ATOM   1875  OD1 ASP A 298     -44.554  12.488  79.460  1.00120.59           O  
ANISOU 1875  OD1 ASP A 298    13223  21222  11374   2288   1497   2420       O  
ATOM   1876  OD2 ASP A 298     -46.266  11.245  80.014  1.00124.33           O  
ANISOU 1876  OD2 ASP A 298    13144  22473  11623   2039   1541   2633       O  
ATOM   1877  N   GLY A 299     -43.780  15.353  79.748  1.00114.36           N  
ANISOU 1877  N   GLY A 299    13112  19879  10460   3131   1654   2320       N  
ATOM   1878  CA  GLY A 299     -42.438  15.915  79.863  1.00112.43           C  
ANISOU 1878  CA  GLY A 299    13294  19061  10365   3103   1607   2163       C  
ATOM   1879  C   GLY A 299     -41.332  14.892  79.712  1.00113.78           C  
ANISOU 1879  C   GLY A 299    13489  18949  10793   2644   1460   2052       C  
ATOM   1880  O   GLY A 299     -40.175  15.179  80.027  1.00111.54           O  
ANISOU 1880  O   GLY A 299    13511  18245  10622   2569   1412   1929       O  
ATOM   1881  N   THR A 300     -41.686  13.689  79.229  1.00110.85           N  
ANISOU 1881  N   THR A 300    12802  18821  10496   2336   1391   2098       N  
ATOM   1882  CA  THR A 300     -40.753  12.587  78.989  1.00108.98           C  
ANISOU 1882  CA  THR A 300    12576  18350  10482   1925   1261   2007       C  
ATOM   1883  C   THR A 300     -40.329  12.550  77.510  1.00113.83           C  
ANISOU 1883  C   THR A 300    13158  18879  11213   1813   1188   1956       C  
ATOM   1884  O   THR A 300     -40.808  13.355  76.714  1.00114.38           O  
ANISOU 1884  O   THR A 300    13184  19090  11187   2041   1236   2002       O  
ATOM   1885  CB  THR A 300     -41.368  11.237  79.412  1.00113.19           C  
ANISOU 1885  CB  THR A 300    12850  19146  11010   1633   1236   2081       C  
ATOM   1886  OG1 THR A 300     -42.495  10.938  78.600  1.00112.02           O  
ANISOU 1886  OG1 THR A 300    12373  19437  10754   1591   1253   2186       O  
ATOM   1887  CG2 THR A 300     -41.752  11.192  80.866  1.00111.74           C  
ANISOU 1887  CG2 THR A 300    12686  19059  10710   1718   1306   2141       C  
ATOM   1888  N   MET A 301     -39.416  11.626  77.158  1.00109.82           N  
ANISOU 1888  N   MET A 301    12686  18144  10899   1488   1079   1865       N  
ATOM   1889  CA  MET A 301     -38.958  11.415  75.788  1.00109.25           C  
ANISOU 1889  CA  MET A 301    12576  17996  10937   1349   1006   1806       C  
ATOM   1890  C   MET A 301     -40.029  10.718  74.977  1.00113.69           C  
ANISOU 1890  C   MET A 301    12819  18952  11427   1212    996   1885       C  
ATOM   1891  O   MET A 301     -40.697   9.825  75.507  1.00114.58           O  
ANISOU 1891  O   MET A 301    12766  19279  11491   1033    998   1946       O  
ATOM   1892  CB  MET A 301     -37.705  10.543  75.777  1.00110.28           C  
ANISOU 1892  CB  MET A 301    12837  17798  11267   1071    904   1692       C  
ATOM   1893  CG  MET A 301     -36.456  11.244  76.191  1.00113.74           C  
ANISOU 1893  CG  MET A 301    13559  17875  11782   1152    886   1600       C  
ATOM   1894  SD  MET A 301     -34.995  10.327  75.644  1.00117.18           S  
ANISOU 1894  SD  MET A 301    14075  18022  12427    879    767   1480       S  
ATOM   1895  CE  MET A 301     -35.135   8.825  76.648  1.00114.25           C  
ANISOU 1895  CE  MET A 301    13647  17669  12094    661    737   1509       C  
ATOM   1896  N   ARG A 302     -40.174  11.070  73.689  1.00109.60           N  
ANISOU 1896  N   ARG A 302    12214  18536  10891   1259    981   1885       N  
ATOM   1897  CA  ARG A 302     -41.146  10.387  72.839  1.00110.55           C  
ANISOU 1897  CA  ARG A 302    12023  19053  10928   1091    957   1948       C  
ATOM   1898  C   ARG A 302     -40.563   9.043  72.422  1.00113.55           C  
ANISOU 1898  C   ARG A 302    12413  19269  11460    683    853   1849       C  
ATOM   1899  O   ARG A 302     -39.617   9.003  71.647  1.00111.54           O  
ANISOU 1899  O   ARG A 302    12292  18750  11337    619    795   1744       O  
ATOM   1900  CB  ARG A 302     -41.550  11.237  71.624  1.00110.70           C  
ANISOU 1900  CB  ARG A 302    11940  19273  10849   1301    978   1993       C  
ATOM   1901  CG  ARG A 302     -42.581  12.296  71.971  1.00118.66           C  
ANISOU 1901  CG  ARG A 302    12849  20600  11635   1701   1094   2136       C  
ATOM   1902  CD  ARG A 302     -43.231  12.877  70.744  1.00118.30           C  
ANISOU 1902  CD  ARG A 302    12623  20871  11454   1882   1111   2217       C  
ATOM   1903  NE  ARG A 302     -44.015  14.064  71.062  1.00123.34           N  
ANISOU 1903  NE  ARG A 302    13251  21731  11882   2357   1235   2350       N  
ATOM   1904  CZ  ARG A 302     -44.934  14.596  70.264  1.00143.54           C  
ANISOU 1904  CZ  ARG A 302    15588  24707  14245   2603   1280   2479       C  
ATOM   1905  NH1 ARG A 302     -45.593  15.682  70.633  1.00137.46           N  
ANISOU 1905  NH1 ARG A 302    14851  24105  13274   3085   1406   2603       N  
ATOM   1906  NH2 ARG A 302     -45.203  14.038  69.089  1.00133.57           N  
ANISOU 1906  NH2 ARG A 302    14075  23707  12968   2383   1200   2485       N  
ATOM   1907  N   LEU A 303     -41.063   7.953  73.013  1.00111.51           N  
ANISOU 1907  N   LEU A 303    12050  19140  11179    417    838   1883       N  
ATOM   1908  CA  LEU A 303     -40.580   6.598  72.731  1.00111.23           C  
ANISOU 1908  CA  LEU A 303    12078  18918  11265     36    753   1796       C  
ATOM   1909  C   LEU A 303     -41.747   5.678  72.401  1.00119.03           C  
ANISOU 1909  C   LEU A 303    12810  20293  12120   -269    738   1865       C  
ATOM   1910  O   LEU A 303     -42.829   5.819  72.975  1.00120.90           O  
ANISOU 1910  O   LEU A 303    12835  20911  12191   -233    796   1995       O  
ATOM   1911  CB  LEU A 303     -39.787   6.031  73.923  1.00110.28           C  
ANISOU 1911  CB  LEU A 303    12184  18455  11262    -40    744   1760       C  
ATOM   1912  CG  LEU A 303     -38.681   6.909  74.507  1.00113.31           C  
ANISOU 1912  CG  LEU A 303    12804  18505  11743    221    758   1703       C  
ATOM   1913  CD1 LEU A 303     -38.798   6.991  76.015  1.00114.03           C  
ANISOU 1913  CD1 LEU A 303    12962  18575  11790    306    808   1765       C  
ATOM   1914  CD2 LEU A 303     -37.311   6.424  74.088  1.00113.96           C  
ANISOU 1914  CD2 LEU A 303    13090  18205  12005    114    681   1574       C  
ATOM   1915  N   GLY A 304     -41.515   4.751  71.479  1.00116.19           N  
ANISOU 1915  N   GLY A 304    12478  19850  11818   -574    661   1775       N  
ATOM   1916  CA  GLY A 304     -42.512   3.776  71.048  1.00118.59           C  
ANISOU 1916  CA  GLY A 304    12586  20479  11994   -948    629   1812       C  
ATOM   1917  C   GLY A 304     -43.665   4.336  70.236  1.00124.63           C  
ANISOU 1917  C   GLY A 304    13003  21795  12555   -892    643   1904       C  
ATOM   1918  O   GLY A 304     -44.727   3.712  70.176  1.00127.01           O  
ANISOU 1918  O   GLY A 304    13070  22497  12692  -1176    633   1981       O  
ATOM   1919  N   GLU A 305     -43.455   5.502  69.581  1.00120.07           N  
ANISOU 1919  N   GLU A 305    12393  21255  11972   -537    663   1904       N  
ATOM   1920  CA  GLU A 305     -44.436   6.191  68.727  1.00121.65           C  
ANISOU 1920  CA  GLU A 305    12281  21966  11974   -392    681   2002       C  
ATOM   1921  C   GLU A 305     -44.770   5.338  67.472  1.00127.22           C  
ANISOU 1921  C   GLU A 305    12850  22872  12615   -769    591   1939       C  
ATOM   1922  O   GLU A 305     -43.956   4.472  67.143  1.00125.18           O  
ANISOU 1922  O   GLU A 305    12824  22234  12505  -1035    525   1792       O  
ATOM   1923  CB  GLU A 305     -43.900   7.575  68.327  1.00121.49           C  
ANISOU 1923  CB  GLU A 305    12363  21806  11991     66    724   2002       C  
ATOM   1924  CG  GLU A 305     -44.062   8.624  69.416  1.00130.39           C  
ANISOU 1924  CG  GLU A 305    13540  22933  13068    471    830   2103       C  
ATOM   1925  CD  GLU A 305     -45.135   9.674  69.193  1.00151.60           C  
ANISOU 1925  CD  GLU A 305    15978  26104  15519    840    911   2264       C  
ATOM   1926  OE1 GLU A 305     -45.310  10.525  70.094  1.00135.29           O  
ANISOU 1926  OE1 GLU A 305    13983  24033  13389   1194   1009   2342       O  
ATOM   1927  OE2 GLU A 305     -45.794   9.660  68.126  1.00151.42           O  
ANISOU 1927  OE2 GLU A 305    15701  26471  15360    797    881   2314       O  
ATOM   1928  N   PRO A 306     -45.943   5.460  66.783  1.00127.12           N  
ANISOU 1928  N   PRO A 306    12475  23456  12368   -823    583   2041       N  
ATOM   1929  CA  PRO A 306     -47.037   6.461  66.882  1.00129.33           C  
ANISOU 1929  CA  PRO A 306    12422  24301  12418   -483    659   2230       C  
ATOM   1930  C   PRO A 306     -47.845   6.558  68.181  1.00136.59           C  
ANISOU 1930  C   PRO A 306    13184  25504  13211   -393    743   2380       C  
ATOM   1931  O   PRO A 306     -48.390   7.633  68.430  1.00137.21           O  
ANISOU 1931  O   PRO A 306    13111  25875  13148     47    833   2516       O  
ATOM   1932  CB  PRO A 306     -48.002   6.022  65.773  1.00133.63           C  
ANISOU 1932  CB  PRO A 306    12618  25411  12744   -760    592   2269       C  
ATOM   1933  CG  PRO A 306     -47.131   5.354  64.772  1.00136.32           C  
ANISOU 1933  CG  PRO A 306    13184  25378  13234  -1044    495   2078       C  
ATOM   1934  CD  PRO A 306     -46.138   4.599  65.599  1.00129.66           C  
ANISOU 1934  CD  PRO A 306    12715  23920  12629  -1224    486   1953       C  
ATOM   1935  N   THR A 307     -47.953   5.467  68.976  1.00135.54           N  
ANISOU 1935  N   THR A 307    13092  25298  13108   -786    724   2365       N  
ATOM   1936  CA  THR A 307     -48.753   5.350  70.221  1.00138.31           C  
ANISOU 1936  CA  THR A 307    13279  25948  13327   -791    799   2509       C  
ATOM   1937  C   THR A 307     -50.238   5.693  69.931  1.00148.41           C  
ANISOU 1937  C   THR A 307    14053  28060  14275   -727    836   2700       C  
ATOM   1938  O   THR A 307     -50.800   5.130  68.984  1.00149.85           O  
ANISOU 1938  O   THR A 307    14004  28602  14329  -1067    759   2699       O  
ATOM   1939  CB  THR A 307     -48.191   6.146  71.426  1.00144.86           C  
ANISOU 1939  CB  THR A 307    14339  26440  14260   -368    894   2529       C  
ATOM   1940  OG1 THR A 307     -48.176   7.544  71.141  1.00145.67           O  
ANISOU 1940  OG1 THR A 307    14430  26607  14310    177    961   2576       O  
ATOM   1941  CG2 THR A 307     -46.834   5.656  71.889  1.00140.15           C  
ANISOU 1941  CG2 THR A 307    14177  25125  13947   -486    854   2369       C  
ATOM   1942  N   SER A 308     -50.868   6.609  70.716  1.00147.18           N  
ANISOU 1942  N   SER A 308    13725  28232  13964   -286    953   2860       N  
ATOM   1943  CA  SER A 308     -52.281   6.945  70.516  1.00150.51           C  
ANISOU 1943  CA  SER A 308    13642  29497  14048   -173   1000   3061       C  
ATOM   1944  C   SER A 308     -52.647   8.429  70.781  1.00154.39           C  
ANISOU 1944  C   SER A 308    14046  30220  14394    552   1132   3198       C  
ATOM   1945  O   SER A 308     -53.051   9.123  69.839  1.00156.30           O  
ANISOU 1945  O   SER A 308    14097  30799  14492    828   1137   3267       O  
ATOM   1946  CB  SER A 308     -53.162   6.046  71.383  1.00155.50           C  
ANISOU 1946  CB  SER A 308    14019  30545  14518   -563   1017   3174       C  
ATOM   1947  OG  SER A 308     -52.740   6.061  72.737  1.00162.30           O  
ANISOU 1947  OG  SER A 308    15125  31046  15495   -443   1091   3172       O  
ATOM   1948  N   ASN A 309     -52.538   8.895  72.051  1.00148.11           N  
ANISOU 1948  N   ASN A 309    13403  29256  13616    861   1241   3242       N  
ATOM   1949  CA  ASN A 309     -52.959  10.231  72.493  1.00148.12           C  
ANISOU 1949  CA  ASN A 309    13365  29467  13448   1545   1385   3373       C  
ATOM   1950  C   ASN A 309     -51.938  11.375  72.258  1.00147.42           C  
ANISOU 1950  C   ASN A 309    13716  28767  13529   2018   1421   3269       C  
ATOM   1951  O   ASN A 309     -52.211  12.512  72.654  1.00148.36           O  
ANISOU 1951  O   ASN A 309    13892  28967  13510   2595   1548   3362       O  
ATOM   1952  CB  ASN A 309     -53.340  10.184  73.975  1.00149.43           C  
ANISOU 1952  CB  ASN A 309    13506  29746  13525   1642   1489   3459       C  
ATOM   1953  CG  ASN A 309     -54.589   9.381  74.265  1.00172.28           C  
ANISOU 1953  CG  ASN A 309    15900  33402  16158   1312   1496   3625       C  
ATOM   1954  OD1 ASN A 309     -55.632   9.530  73.614  1.00167.99           O  
ANISOU 1954  OD1 ASN A 309    14907  33581  15340   1376   1505   3776       O  
ATOM   1955  ND2 ASN A 309     -54.522   8.534  75.282  1.00162.15           N  
ANISOU 1955  ND2 ASN A 309    14674  32001  14933    957   1495   3614       N  
ATOM   1956  N   GLU A 310     -50.813  11.102  71.584  1.00139.32           N  
ANISOU 1956  N   GLU A 310    12997  27165  12773   1784   1317   3088       N  
ATOM   1957  CA  GLU A 310     -49.807  12.131  71.303  1.00136.30           C  
ANISOU 1957  CA  GLU A 310    13022  26220  12546   2153   1342   2992       C  
ATOM   1958  C   GLU A 310     -49.994  12.728  69.895  1.00139.87           C  
ANISOU 1958  C   GLU A 310    13362  26873  12909   2344   1319   3032       C  
ATOM   1959  O   GLU A 310     -50.682  12.126  69.063  1.00141.58           O  
ANISOU 1959  O   GLU A 310    13217  27576  13001   2081   1250   3086       O  
ATOM   1960  CB  GLU A 310     -48.387  11.563  71.467  1.00133.98           C  
ANISOU 1960  CB  GLU A 310    13130  25192  12584   1827   1253   2782       C  
ATOM   1961  CG  GLU A 310     -48.008  11.250  72.911  1.00143.36           C  
ANISOU 1961  CG  GLU A 310    14516  26089  13867   1759   1288   2742       C  
ATOM   1962  CD  GLU A 310     -47.783  12.418  73.856  1.00162.27           C  
ANISOU 1962  CD  GLU A 310    17175  28258  16222   2257   1409   2763       C  
ATOM   1963  OE1 GLU A 310     -47.616  13.566  73.380  1.00158.89           O  
ANISOU 1963  OE1 GLU A 310    16905  27716  15751   2664   1463   2773       O  
ATOM   1964  OE2 GLU A 310     -47.742  12.174  75.084  1.00151.71           O  
ANISOU 1964  OE2 GLU A 310    15920  26830  14892   2226   1450   2763       O  
ATOM   1965  N   THR A 311     -49.398  13.922  69.638  1.00133.65           N  
ANISOU 1965  N   THR A 311    12893  25721  12166   2789   1378   3012       N  
ATOM   1966  CA  THR A 311     -49.472  14.608  68.335  1.00133.02           C  
ANISOU 1966  CA  THR A 311    12772  25764  12007   3020   1369   3059       C  
ATOM   1967  C   THR A 311     -48.590  13.891  67.309  1.00132.36           C  
ANISOU 1967  C   THR A 311    12778  25370  12142   2574   1227   2897       C  
ATOM   1968  O   THR A 311     -47.646  13.196  67.686  1.00128.98           O  
ANISOU 1968  O   THR A 311    12585  24463  11960   2226   1160   2734       O  
ATOM   1969  CB  THR A 311     -49.096  16.100  68.443  1.00138.62           C  
ANISOU 1969  CB  THR A 311    13850  26135  12686   3614   1487   3095       C  
ATOM   1970  OG1 THR A 311     -47.759  16.235  68.920  1.00133.14           O  
ANISOU 1970  OG1 THR A 311    13633  24692  12262   3510   1467   2918       O  
ATOM   1971  CG2 THR A 311     -50.058  16.896  69.314  1.00140.60           C  
ANISOU 1971  CG2 THR A 311    14020  26731  12671   4138   1645   3265       C  
ATOM   1972  N   LEU A 312     -48.890  14.076  66.015  1.00129.09           N  
ANISOU 1972  N   LEU A 312    12182  25243  11623   2613   1185   2946       N  
ATOM   1973  CA  LEU A 312     -48.157  13.448  64.913  1.00126.61           C  
ANISOU 1973  CA  LEU A 312    11925  24709  11471   2230   1058   2802       C  
ATOM   1974  C   LEU A 312     -46.786  14.107  64.633  1.00126.62           C  
ANISOU 1974  C   LEU A 312    12390  24020  11700   2360   1059   2677       C  
ATOM   1975  O   LEU A 312     -45.985  13.526  63.900  1.00123.99           O  
ANISOU 1975  O   LEU A 312    12154  23423  11533   2035    961   2535       O  
ATOM   1976  CB  LEU A 312     -49.008  13.447  63.627  1.00128.86           C  
ANISOU 1976  CB  LEU A 312    11835  25596  11531   2234   1014   2907       C  
ATOM   1977  CG  LEU A 312     -50.331  12.672  63.661  1.00136.37           C  
ANISOU 1977  CG  LEU A 312    12276  27302  12235   1993    983   3021       C  
ATOM   1978  CD1 LEU A 312     -51.099  12.871  62.371  1.00139.30           C  
ANISOU 1978  CD1 LEU A 312    12293  28272  12362   2063    943   3133       C  
ATOM   1979  CD2 LEU A 312     -50.116  11.176  63.914  1.00137.00           C  
ANISOU 1979  CD2 LEU A 312    12329  27272  12453   1326    874   2872       C  
ATOM   1980  N   SER A 313     -46.504  15.281  65.243  1.00122.32           N  
ANISOU 1980  N   SER A 313    12141  23187  11150   2810   1171   2725       N  
ATOM   1981  CA  SER A 313     -45.267  16.060  65.084  1.00119.62           C  
ANISOU 1981  CA  SER A 313    12249  22220  10982   2942   1187   2630       C  
ATOM   1982  C   SER A 313     -43.982  15.211  65.078  1.00119.75           C  
ANISOU 1982  C   SER A 313    12467  21744  11288   2491   1081   2422       C  
ATOM   1983  O   SER A 313     -43.049  15.551  64.352  1.00117.96           O  
ANISOU 1983  O   SER A 313    12459  21183  11179   2469   1050   2346       O  
ATOM   1984  CB  SER A 313     -45.162  17.122  66.171  1.00123.51           C  
ANISOU 1984  CB  SER A 313    13055  22437  11436   3353   1314   2675       C  
ATOM   1985  OG  SER A 313     -46.156  18.117  65.991  1.00135.68           O  
ANISOU 1985  OG  SER A 313    14505  24341  12707   3866   1428   2865       O  
ATOM   1986  N   CYS A 314     -43.942  14.109  65.852  1.00114.90           N  
ANISOU 1986  N   CYS A 314    11776  21108  10772   2145   1030   2343       N  
ATOM   1987  CA  CYS A 314     -42.787  13.209  65.928  1.00111.79           C  
ANISOU 1987  CA  CYS A 314    11564  20284  10629   1751    937   2161       C  
ATOM   1988  C   CYS A 314     -42.714  12.293  64.682  1.00114.77           C  
ANISOU 1988  C   CYS A 314    11769  20800  11036   1406    830   2086       C  
ATOM   1989  O   CYS A 314     -41.683  12.281  64.007  1.00111.95           O  
ANISOU 1989  O   CYS A 314    11598  20116  10824   1313    782   1975       O  
ATOM   1990  CB  CYS A 314     -42.832  12.398  67.222  1.00111.48           C  
ANISOU 1990  CB  CYS A 314    11529  20173  10654   1550    934   2126       C  
ATOM   1991  SG  CYS A 314     -41.503  11.174  67.407  1.00112.51           S  
ANISOU 1991  SG  CYS A 314    11870  19817  11061   1106    828   1927       S  
ATOM   1992  N   VAL A 315     -43.801  11.540  64.378  1.00113.03           N  
ANISOU 1992  N   VAL A 315    11200  21082  10664   1207    794   2145       N  
ATOM   1993  CA  VAL A 315     -43.847  10.608  63.240  1.00112.47           C  
ANISOU 1993  CA  VAL A 315    10975  21171  10587    844    691   2064       C  
ATOM   1994  C   VAL A 315     -43.746  11.369  61.907  1.00115.13           C  
ANISOU 1994  C   VAL A 315    11283  21611  10851   1042    684   2094       C  
ATOM   1995  O   VAL A 315     -43.135  10.845  60.974  1.00114.50           O  
ANISOU 1995  O   VAL A 315    11257  21395  10854    806    607   1972       O  
ATOM   1996  CB  VAL A 315     -45.053   9.625  63.246  1.00118.88           C  
ANISOU 1996  CB  VAL A 315    11431  22511  11225    528    649   2119       C  
ATOM   1997  CG1 VAL A 315     -44.959   8.637  64.406  1.00118.23           C  
ANISOU 1997  CG1 VAL A 315    11430  22247  11243    230    638   2063       C  
ATOM   1998  CG2 VAL A 315     -46.395  10.350  63.255  1.00121.65           C  
ANISOU 1998  CG2 VAL A 315    11439  23486  11294    823    716   2328       C  
ATOM   1999  N   ILE A 316     -44.299  12.605  61.833  1.00110.83           N  
ANISOU 1999  N   ILE A 316    10684  21281  10147   1492    772   2256       N  
ATOM   2000  CA  ILE A 316     -44.244  13.459  60.640  1.00110.03           C  
ANISOU 2000  CA  ILE A 316    10581  21271   9954   1738    783   2317       C  
ATOM   2001  C   ILE A 316     -42.773  13.735  60.301  1.00108.07           C  
ANISOU 2001  C   ILE A 316    10702  20431   9930   1707    766   2183       C  
ATOM   2002  O   ILE A 316     -42.360  13.451  59.179  1.00107.09           O  
ANISOU 2002  O   ILE A 316    10557  20301   9831   1545    700   2111       O  
ATOM   2003  CB  ILE A 316     -45.081  14.767  60.824  1.00115.37           C  
ANISOU 2003  CB  ILE A 316    11199  22224  10412   2282    902   2530       C  
ATOM   2004  CG1 ILE A 316     -46.616  14.490  60.806  1.00119.20           C  
ANISOU 2004  CG1 ILE A 316    11217  23455  10617   2321    909   2688       C  
ATOM   2005  CG2 ILE A 316     -44.693  15.884  59.839  1.00115.91           C  
ANISOU 2005  CG2 ILE A 316    11437  22168  10434   2607    941   2594       C  
ATOM   2006  CD1 ILE A 316     -47.245  13.819  59.514  1.00128.65           C  
ANISOU 2006  CD1 ILE A 316    12042  25182  11657   2052    806   2701       C  
ATOM   2007  N   ILE A 317     -41.982  14.214  61.283  1.00101.06           N  
ANISOU 2007  N   ILE A 317    10132  19076   9189   1828    819   2142       N  
ATOM   2008  CA  ILE A 317     -40.555  14.507  61.113  1.00 97.85           C  
ANISOU 2008  CA  ILE A 317    10062  18138   8980   1781    806   2025       C  
ATOM   2009  C   ILE A 317     -39.788  13.203  60.828  1.00 98.58           C  
ANISOU 2009  C   ILE A 317    10148  18065   9242   1346    700   1845       C  
ATOM   2010  O   ILE A 317     -38.894  13.219  59.982  1.00 96.99           O  
ANISOU 2010  O   ILE A 317    10060  17667   9126   1264    664   1763       O  
ATOM   2011  CB  ILE A 317     -39.981  15.304  62.328  1.00 99.99           C  
ANISOU 2011  CB  ILE A 317    10655  18004   9332   1982    883   2027       C  
ATOM   2012  CG1 ILE A 317     -40.679  16.684  62.501  1.00102.52           C  
ANISOU 2012  CG1 ILE A 317    11059  18430   9463   2458   1002   2198       C  
ATOM   2013  CG2 ILE A 317     -38.453  15.462  62.288  1.00 98.16           C  
ANISOU 2013  CG2 ILE A 317    10736  17262   9298   1854    855   1898       C  
ATOM   2014  CD1 ILE A 317     -40.688  17.667  61.287  1.00110.93           C  
ANISOU 2014  CD1 ILE A 317    12187  19546  10415   2707   1037   2296       C  
ATOM   2015  N   PHE A 318     -40.177  12.080  61.471  1.00 94.54           N  
ANISOU 2015  N   PHE A 318     9510  17653   8758   1081    659   1793       N  
ATOM   2016  CA  PHE A 318     -39.547  10.778  61.241  1.00 93.15           C  
ANISOU 2016  CA  PHE A 318     9365  17311   8718    692    570   1629       C  
ATOM   2017  C   PHE A 318     -39.659  10.368  59.782  1.00 96.93           C  
ANISOU 2017  C   PHE A 318     9703  18003   9124    535    506   1580       C  
ATOM   2018  O   PHE A 318     -38.644  10.013  59.188  1.00 94.83           O  
ANISOU 2018  O   PHE A 318     9583  17471   8976    406    463   1452       O  
ATOM   2019  CB  PHE A 318     -40.147   9.677  62.134  1.00 96.01           C  
ANISOU 2019  CB  PHE A 318     9624  17780   9077    435    546   1612       C  
ATOM   2020  CG  PHE A 318     -39.877   8.268  61.640  1.00 97.79           C  
ANISOU 2020  CG  PHE A 318     9850  17942   9362     29    458   1466       C  
ATOM   2021  CD1 PHE A 318     -38.613   7.698  61.765  1.00 98.75           C  
ANISOU 2021  CD1 PHE A 318    10228  17615   9677    -93    427   1321       C  
ATOM   2022  CD2 PHE A 318     -40.882   7.520  61.029  1.00102.22           C  
ANISOU 2022  CD2 PHE A 318    10168  18903   9767   -226    409   1475       C  
ATOM   2023  CE1 PHE A 318     -38.359   6.408  61.294  1.00 99.75           C  
ANISOU 2023  CE1 PHE A 318    10405  17654   9841   -423    359   1186       C  
ATOM   2024  CE2 PHE A 318     -40.626   6.228  60.556  1.00105.22           C  
ANISOU 2024  CE2 PHE A 318    10612  19180  10186   -610    333   1327       C  
ATOM   2025  CZ  PHE A 318     -39.363   5.686  60.683  1.00101.25           C  
ANISOU 2025  CZ  PHE A 318    10402  18191   9879   -685    314   1182       C  
ATOM   2026  N   VAL A 319     -40.891  10.388  59.222  1.00 95.92           N  
ANISOU 2026  N   VAL A 319     9279  18384   8784    543    498   1683       N  
ATOM   2027  CA  VAL A 319     -41.158  10.013  57.828  1.00 97.08           C  
ANISOU 2027  CA  VAL A 319     9258  18810   8816    385    431   1645       C  
ATOM   2028  C   VAL A 319     -40.331  10.928  56.889  1.00100.03           C  
ANISOU 2028  C   VAL A 319     9776  19008   9224    609    451   1646       C  
ATOM   2029  O   VAL A 319     -39.610  10.409  56.039  1.00 98.70           O  
ANISOU 2029  O   VAL A 319     9680  18701   9119    423    395   1515       O  
ATOM   2030  CB  VAL A 319     -42.675  10.009  57.491  1.00103.76           C  
ANISOU 2030  CB  VAL A 319     9727  20300   9395    383    421   1783       C  
ATOM   2031  CG1 VAL A 319     -42.918   9.770  56.002  1.00104.90           C  
ANISOU 2031  CG1 VAL A 319     9703  20754   9399    247    351   1751       C  
ATOM   2032  CG2 VAL A 319     -43.417   8.960  58.318  1.00104.59           C  
ANISOU 2032  CG2 VAL A 319     9691  20586   9461     68    393   1769       C  
ATOM   2033  N   ILE A 320     -40.366  12.263  57.113  1.00 96.42           N  
ANISOU 2033  N   ILE A 320     9398  18512   8726   1001    536   1789       N  
ATOM   2034  CA  ILE A 320     -39.624  13.269  56.342  1.00 95.28           C  
ANISOU 2034  CA  ILE A 320     9424  18181   8597   1222    571   1821       C  
ATOM   2035  C   ILE A 320     -38.113  12.937  56.316  1.00 97.94           C  
ANISOU 2035  C   ILE A 320    10025  18031   9156   1046    542   1656       C  
ATOM   2036  O   ILE A 320     -37.518  12.945  55.239  1.00 97.46           O  
ANISOU 2036  O   ILE A 320     9992  17938   9100    990    514   1603       O  
ATOM   2037  CB  ILE A 320     -39.896  14.706  56.889  1.00 98.44           C  
ANISOU 2037  CB  ILE A 320     9954  18527   8922   1657    681   1994       C  
ATOM   2038  CG1 ILE A 320     -41.328  15.156  56.542  1.00101.10           C  
ANISOU 2038  CG1 ILE A 320    10006  19415   8994   1908    715   2181       C  
ATOM   2039  CG2 ILE A 320     -38.875  15.726  56.362  1.00 98.30           C  
ANISOU 2039  CG2 ILE A 320    10222  18166   8963   1823    724   2009       C  
ATOM   2040  CD1 ILE A 320     -41.860  16.335  57.355  1.00106.36           C  
ANISOU 2040  CD1 ILE A 320    10779  20079   9555   2352    834   2351       C  
ATOM   2041  N   VAL A 321     -37.518  12.614  57.479  1.00 93.71           N  
ANISOU 2041  N   VAL A 321     9659  17164   8784    964    550   1581       N  
ATOM   2042  CA  VAL A 321     -36.087  12.321  57.598  1.00 92.05           C  
ANISOU 2042  CA  VAL A 321     9674  16537   8766    830    527   1444       C  
ATOM   2043  C   VAL A 321     -35.755  10.912  57.055  1.00 96.38           C  
ANISOU 2043  C   VAL A 321    10160  17089   9371    508    445   1281       C  
ATOM   2044  O   VAL A 321     -34.941  10.818  56.136  1.00 95.55           O  
ANISOU 2044  O   VAL A 321    10110  16895   9298    452    422   1203       O  
ATOM   2045  CB  VAL A 321     -35.572  12.530  59.054  1.00 95.03           C  
ANISOU 2045  CB  VAL A 321    10247  16589   9270    879    563   1434       C  
ATOM   2046  CG1 VAL A 321     -34.180  11.937  59.266  1.00 93.16           C  
ANISOU 2046  CG1 VAL A 321    10177  16006   9212    701    524   1290       C  
ATOM   2047  CG2 VAL A 321     -35.574  14.012  59.425  1.00 95.30           C  
ANISOU 2047  CG2 VAL A 321    10444  16514   9252   1187    648   1561       C  
ATOM   2048  N   TYR A 322     -36.366   9.842  57.613  1.00 93.74           N  
ANISOU 2048  N   TYR A 322     9735  16846   9035    302    408   1232       N  
ATOM   2049  CA  TYR A 322     -36.081   8.451  57.247  1.00 93.86           C  
ANISOU 2049  CA  TYR A 322     9765  16802   9095     -7    340   1071       C  
ATOM   2050  C   TYR A 322     -36.420   8.120  55.787  1.00100.83           C  
ANISOU 2050  C   TYR A 322    10511  17956   9844   -127    292   1023       C  
ATOM   2051  O   TYR A 322     -35.588   7.487  55.133  1.00 99.65           O  
ANISOU 2051  O   TYR A 322    10472  17641   9751   -252    260    882       O  
ATOM   2052  CB  TYR A 322     -36.788   7.466  58.188  1.00 95.38           C  
ANISOU 2052  CB  TYR A 322     9917  17039   9286   -215    320   1055       C  
ATOM   2053  CG  TYR A 322     -36.468   6.012  57.915  1.00 97.18           C  
ANISOU 2053  CG  TYR A 322    10239  17130   9555   -531    261    890       C  
ATOM   2054  CD1 TYR A 322     -35.373   5.394  58.512  1.00 97.41           C  
ANISOU 2054  CD1 TYR A 322    10506  16756   9749   -572    260    787       C  
ATOM   2055  CD2 TYR A 322     -37.275   5.245  57.080  1.00100.32           C  
ANISOU 2055  CD2 TYR A 322    10506  17805   9805   -788    207    838       C  
ATOM   2056  CE1 TYR A 322     -35.080   4.052  58.272  1.00 98.76           C  
ANISOU 2056  CE1 TYR A 322    10814  16770   9942   -821    219    640       C  
ATOM   2057  CE2 TYR A 322     -36.981   3.911  56.815  1.00102.14           C  
ANISOU 2057  CE2 TYR A 322    10888  17866  10056  -1081    159    675       C  
ATOM   2058  CZ  TYR A 322     -35.885   3.316  57.416  1.00108.92           C  
ANISOU 2058  CZ  TYR A 322    12015  18288  11084  -1079    171    578       C  
ATOM   2059  OH  TYR A 322     -35.621   1.995  57.159  1.00112.06           O  
ANISOU 2059  OH  TYR A 322    12602  18492  11482  -1332    137    423       O  
ATOM   2060  N   TYR A 323     -37.626   8.490  55.289  1.00100.98           N  
ANISOU 2060  N   TYR A 323    10288  18410   9671    -87    288   1135       N  
ATOM   2061  CA  TYR A 323     -38.010   8.189  53.901  1.00103.15           C  
ANISOU 2061  CA  TYR A 323    10412  18990   9790   -213    234   1093       C  
ATOM   2062  C   TYR A 323     -37.007   8.814  52.938  1.00106.90           C  
ANISOU 2062  C   TYR A 323    10997  19320  10301    -61    250   1066       C  
ATOM   2063  O   TYR A 323     -36.491   8.103  52.075  1.00106.63           O  
ANISOU 2063  O   TYR A 323    11013  19237  10264   -233    206    922       O  
ATOM   2064  CB  TYR A 323     -39.448   8.643  53.573  1.00107.11           C  
ANISOU 2064  CB  TYR A 323    10604  20036  10056   -143    231   1250       C  
ATOM   2065  CG  TYR A 323     -39.906   8.301  52.169  1.00111.35           C  
ANISOU 2065  CG  TYR A 323    10964  20939  10406   -298    165   1209       C  
ATOM   2066  CD1 TYR A 323     -40.501   7.075  51.887  1.00115.15           C  
ANISOU 2066  CD1 TYR A 323    11345  21622  10784   -692     85   1095       C  
ATOM   2067  CD2 TYR A 323     -39.776   9.218  51.129  1.00112.75           C  
ANISOU 2067  CD2 TYR A 323    11084  21267  10488    -66    182   1289       C  
ATOM   2068  CE1 TYR A 323     -40.921   6.754  50.596  1.00118.27           C  
ANISOU 2068  CE1 TYR A 323    11586  22365  10986   -860     18   1043       C  
ATOM   2069  CE2 TYR A 323     -40.182   8.905  49.833  1.00115.71           C  
ANISOU 2069  CE2 TYR A 323    11292  21998  10676   -207    118   1250       C  
ATOM   2070  CZ  TYR A 323     -40.757   7.672  49.571  1.00125.48           C  
ANISOU 2070  CZ  TYR A 323    12425  23442  11809   -607     33   1121       C  
ATOM   2071  OH  TYR A 323     -41.181   7.368  48.300  1.00128.97           O  
ANISOU 2071  OH  TYR A 323    12706  24254  12043   -768    -36   1073       O  
ATOM   2072  N   ALA A 324     -36.691  10.117  53.121  1.00103.18           N  
ANISOU 2072  N   ALA A 324    10590  18756   9857    251    318   1200       N  
ATOM   2073  CA  ALA A 324     -35.728  10.849  52.293  1.00102.66           C  
ANISOU 2073  CA  ALA A 324    10638  18549   9817    389    345   1205       C  
ATOM   2074  C   ALA A 324     -34.317  10.249  52.390  1.00106.31           C  
ANISOU 2074  C   ALA A 324    11305  18630  10458    261    333   1043       C  
ATOM   2075  O   ALA A 324     -33.601  10.228  51.389  1.00105.75           O  
ANISOU 2075  O   ALA A 324    11267  18541  10374    240    324    981       O  
ATOM   2076  CB  ALA A 324     -35.697  12.313  52.695  1.00103.08           C  
ANISOU 2076  CB  ALA A 324    10782  18520   9865    710    426   1381       C  
ATOM   2077  N   LEU A 325     -33.935   9.742  53.583  1.00102.69           N  
ANISOU 2077  N   LEU A 325    10968  17900  10148    190    335    984       N  
ATOM   2078  CA  LEU A 325     -32.636   9.115  53.840  1.00101.23           C  
ANISOU 2078  CA  LEU A 325    10960  17384  10118    101    327    847       C  
ATOM   2079  C   LEU A 325     -32.484   7.829  53.017  1.00106.41           C  
ANISOU 2079  C   LEU A 325    11613  18078  10741   -113    273    677       C  
ATOM   2080  O   LEU A 325     -31.522   7.707  52.251  1.00105.89           O  
ANISOU 2080  O   LEU A 325    11613  17929  10692   -105    274    595       O  
ATOM   2081  CB  LEU A 325     -32.478   8.818  55.349  1.00100.05           C  
ANISOU 2081  CB  LEU A 325    10920  16994  10101     84    337    841       C  
ATOM   2082  CG  LEU A 325     -31.146   8.233  55.816  1.00103.31           C  
ANISOU 2082  CG  LEU A 325    11504  17086  10663     38    332    729       C  
ATOM   2083  CD1 LEU A 325     -30.120   9.321  56.068  1.00102.56           C  
ANISOU 2083  CD1 LEU A 325    11505  16828  10636    192    373    791       C  
ATOM   2084  CD2 LEU A 325     -31.328   7.419  57.068  1.00104.88           C  
ANISOU 2084  CD2 LEU A 325    11773  17134  10944    -54    320    697       C  
ATOM   2085  N   MET A 326     -33.454   6.897  53.152  1.00103.81           N  
ANISOU 2085  N   MET A 326    11213  17887  10343   -311    230    628       N  
ATOM   2086  CA  MET A 326     -33.457   5.605  52.468  1.00104.50           C  
ANISOU 2086  CA  MET A 326    11348  17982  10375   -553    179    457       C  
ATOM   2087  C   MET A 326     -33.687   5.742  50.966  1.00109.78           C  
ANISOU 2087  C   MET A 326    11901  18931  10880   -581    153    426       C  
ATOM   2088  O   MET A 326     -33.149   4.929  50.212  1.00109.92           O  
ANISOU 2088  O   MET A 326    12023  18870  10872   -696    131    267       O  
ATOM   2089  CB  MET A 326     -34.480   4.648  53.091  1.00107.94           C  
ANISOU 2089  CB  MET A 326    11761  18489  10765   -801    142    428       C  
ATOM   2090  CG  MET A 326     -34.079   4.175  54.474  1.00110.43           C  
ANISOU 2090  CG  MET A 326    12243  18479  11238   -814    162    417       C  
ATOM   2091  SD  MET A 326     -32.400   3.494  54.543  1.00113.49           S  
ANISOU 2091  SD  MET A 326    12914  18428  11780   -752    179    266       S  
ATOM   2092  CE  MET A 326     -32.007   3.770  56.252  1.00108.70           C  
ANISOU 2092  CE  MET A 326    12394  17569  11340   -627    215    359       C  
ATOM   2093  N   ALA A 327     -34.446   6.769  50.526  1.00106.96           N  
ANISOU 2093  N   ALA A 327    11344  18896  10402   -452    161    581       N  
ATOM   2094  CA  ALA A 327     -34.675   7.028  49.101  1.00107.98           C  
ANISOU 2094  CA  ALA A 327    11346  19323  10359   -447    139    580       C  
ATOM   2095  C   ALA A 327     -33.381   7.536  48.445  1.00110.64           C  
ANISOU 2095  C   ALA A 327    11797  19483  10759   -289    179    555       C  
ATOM   2096  O   ALA A 327     -33.115   7.220  47.286  1.00110.76           O  
ANISOU 2096  O   ALA A 327    11801  19611  10673   -351    157    462       O  
ATOM   2097  CB  ALA A 327     -35.807   8.027  48.913  1.00109.75           C  
ANISOU 2097  CB  ALA A 327    11334  19936  10429   -300    146    779       C  
ATOM   2098  N   GLY A 328     -32.579   8.273  49.218  1.00105.76           N  
ANISOU 2098  N   GLY A 328    11290  18601  10294   -111    235    633       N  
ATOM   2099  CA  GLY A 328     -31.289   8.809  48.798  1.00104.60           C  
ANISOU 2099  CA  GLY A 328    11244  18287  10210     12    277    629       C  
ATOM   2100  C   GLY A 328     -30.249   7.730  48.576  1.00108.41           C  
ANISOU 2100  C   GLY A 328    11855  18576  10758    -94    266    438       C  
ATOM   2101  O   GLY A 328     -29.410   7.861  47.685  1.00107.75           O  
ANISOU 2101  O   GLY A 328    11789  18512  10640    -45    285    398       O  
ATOM   2102  N   PHE A 329     -30.309   6.647  49.376  1.00105.92           N  
ANISOU 2102  N   PHE A 329    11638  18083  10522   -223    241    326       N  
ATOM   2103  CA  PHE A 329     -29.384   5.516  49.274  1.00106.39           C  
ANISOU 2103  CA  PHE A 329    11860  17932  10632   -287    239    145       C  
ATOM   2104  C   PHE A 329     -29.696   4.626  48.077  1.00112.12           C  
ANISOU 2104  C   PHE A 329    12596  18804  11202   -434    203     -8       C  
ATOM   2105  O   PHE A 329     -28.763   4.108  47.463  1.00112.01           O  
ANISOU 2105  O   PHE A 329    12688  18699  11173   -396    222   -133       O  
ATOM   2106  CB  PHE A 329     -29.390   4.668  50.553  1.00108.14           C  
ANISOU 2106  CB  PHE A 329    12220  17893  10975   -362    230     94       C  
ATOM   2107  CG  PHE A 329     -28.758   5.320  51.758  1.00108.36           C  
ANISOU 2107  CG  PHE A 329    12286  17729  11158   -221    265    199       C  
ATOM   2108  CD1 PHE A 329     -27.457   5.810  51.702  1.00110.68           C  
ANISOU 2108  CD1 PHE A 329    12613  17925  11515    -74    302    214       C  
ATOM   2109  CD2 PHE A 329     -29.438   5.387  52.967  1.00110.35           C  
ANISOU 2109  CD2 PHE A 329    12538  17914  11474   -253    259    277       C  
ATOM   2110  CE1 PHE A 329     -26.872   6.407  52.818  1.00110.54           C  
ANISOU 2110  CE1 PHE A 329    12632  17751  11619     17    325    302       C  
ATOM   2111  CE2 PHE A 329     -28.852   5.983  54.084  1.00111.88           C  
ANISOU 2111  CE2 PHE A 329    12781  17935  11794   -133    288    361       C  
ATOM   2112  CZ  PHE A 329     -27.571   6.484  54.005  1.00109.29           C  
ANISOU 2112  CZ  PHE A 329    12492  17510  11523    -10    316    369       C  
ATOM   2113  N   VAL A 330     -30.992   4.423  47.759  1.00110.26           N  
ANISOU 2113  N   VAL A 330    12251  18811  10833   -603    152     -2       N  
ATOM   2114  CA  VAL A 330     -31.395   3.590  46.618  1.00112.10           C  
ANISOU 2114  CA  VAL A 330    12495  19210  10887   -791    107   -154       C  
ATOM   2115  C   VAL A 330     -31.175   4.367  45.306  1.00115.18           C  
ANISOU 2115  C   VAL A 330    12751  19863  11148   -673    118   -112       C  
ATOM   2116  O   VAL A 330     -30.862   3.744  44.290  1.00116.12           O  
ANISOU 2116  O   VAL A 330    12939  20030  11151   -741    106   -265       O  
ATOM   2117  CB  VAL A 330     -32.818   2.977  46.715  1.00117.97           C  
ANISOU 2117  CB  VAL A 330    13165  20155  11504  -1073     40   -177       C  
ATOM   2118  CG1 VAL A 330     -32.847   1.799  47.684  1.00118.18           C  
ANISOU 2118  CG1 VAL A 330    13411  19874  11617  -1257     30   -288       C  
ATOM   2119  CG2 VAL A 330     -33.866   4.013  47.093  1.00117.54           C  
ANISOU 2119  CG2 VAL A 330    12848  20401  11410  -1009     32     39       C  
ATOM   2120  N   TRP A 331     -31.281   5.720  45.341  1.00109.51           N  
ANISOU 2120  N   TRP A 331    11875  19291  10445   -485    147     93       N  
ATOM   2121  CA  TRP A 331     -31.005   6.570  44.177  1.00109.00           C  
ANISOU 2121  CA  TRP A 331    11703  19447  10264   -353    169    167       C  
ATOM   2122  C   TRP A 331     -29.502   6.568  43.891  1.00110.36           C  
ANISOU 2122  C   TRP A 331    12002  19413  10515   -236    224    101       C  
ATOM   2123  O   TRP A 331     -29.103   6.720  42.738  1.00110.71           O  
ANISOU 2123  O   TRP A 331    12009  19617  10440   -196    237     72       O  
ATOM   2124  CB  TRP A 331     -31.529   8.005  44.361  1.00107.36           C  
ANISOU 2124  CB  TRP A 331    11351  19400  10041   -172    196    415       C  
ATOM   2125  CG  TRP A 331     -32.920   8.223  43.834  1.00110.23           C  
ANISOU 2125  CG  TRP A 331    11507  20167  10207   -217    148    502       C  
ATOM   2126  CD1 TRP A 331     -34.041   8.487  44.565  1.00113.51           C  
ANISOU 2126  CD1 TRP A 331    11801  20728  10598   -211    132    623       C  
ATOM   2127  CD2 TRP A 331     -33.336   8.191  42.460  1.00112.03           C  
ANISOU 2127  CD2 TRP A 331    11603  20751  10211   -265    111    482       C  
ATOM   2128  NE1 TRP A 331     -35.129   8.622  43.735  1.00114.96           N  
ANISOU 2128  NE1 TRP A 331    11767  21361  10553   -247     85    687       N  
ATOM   2129  CE2 TRP A 331     -34.729   8.424  42.439  1.00117.39           C  
ANISOU 2129  CE2 TRP A 331    12068  21800  10735   -293     67    598       C  
ATOM   2130  CE3 TRP A 331     -32.669   7.964  41.240  1.00113.97           C  
ANISOU 2130  CE3 TRP A 331    11880  21068  10356   -283    112    377       C  
ATOM   2131  CZ2 TRP A 331     -35.465   8.455  41.247  1.00118.86           C  
ANISOU 2131  CZ2 TRP A 331    12063  22431  10666   -346     15    617       C  
ATOM   2132  CZ3 TRP A 331     -33.400   7.992  40.061  1.00117.37           C  
ANISOU 2132  CZ3 TRP A 331    12144  21910  10541   -340     64    386       C  
ATOM   2133  CH2 TRP A 331     -34.780   8.239  40.071  1.00119.45           C  
ANISOU 2133  CH2 TRP A 331    12189  22544  10651   -375     12    507       C  
ATOM   2134  N   PHE A 332     -28.677   6.356  44.941  1.00104.53           N  
ANISOU 2134  N   PHE A 332    11399  18358   9962   -183    256     78       N  
ATOM   2135  CA  PHE A 332     -27.222   6.232  44.841  1.00103.25           C  
ANISOU 2135  CA  PHE A 332    11333  18027   9869    -75    307     16       C  
ATOM   2136  C   PHE A 332     -26.890   4.929  44.122  1.00107.67           C  
ANISOU 2136  C   PHE A 332    12012  18559  10339   -147    297   -209       C  
ATOM   2137  O   PHE A 332     -25.978   4.905  43.299  1.00108.14           O  
ANISOU 2137  O   PHE A 332    12080  18674  10334    -53    336   -264       O  
ATOM   2138  CB  PHE A 332     -26.554   6.291  46.236  1.00103.41           C  
ANISOU 2138  CB  PHE A 332    11446  17760  10086     -9    332     57       C  
ATOM   2139  CG  PHE A 332     -25.231   5.564  46.376  1.00105.01           C  
ANISOU 2139  CG  PHE A 332    11766  17783  10348     66    366    -62       C  
ATOM   2140  CD1 PHE A 332     -24.054   6.126  45.895  1.00107.82           C  
ANISOU 2140  CD1 PHE A 332    12071  18205  10690    188    417    -19       C  
ATOM   2141  CD2 PHE A 332     -25.163   4.321  46.998  1.00107.72           C  
ANISOU 2141  CD2 PHE A 332    12274  17910  10747     23    353   -203       C  
ATOM   2142  CE1 PHE A 332     -22.832   5.456  46.028  1.00108.99           C  
ANISOU 2142  CE1 PHE A 332    12292  18250  10868    288    452   -114       C  
ATOM   2143  CE2 PHE A 332     -23.942   3.649  47.126  1.00110.87           C  
ANISOU 2143  CE2 PHE A 332    12783  18163  11179    148    392   -297       C  
ATOM   2144  CZ  PHE A 332     -22.785   4.223  46.641  1.00108.71           C  
ANISOU 2144  CZ  PHE A 332    12420  18003  10883    291    441   -251       C  
ATOM   2145  N   VAL A 333     -27.634   3.848  44.435  1.00103.98           N  
ANISOU 2145  N   VAL A 333    11654  18002   9852   -318    250   -339       N  
ATOM   2146  CA  VAL A 333     -27.456   2.533  43.817  1.00105.22           C  
ANISOU 2146  CA  VAL A 333    11996  18078   9906   -412    241   -568       C  
ATOM   2147  C   VAL A 333     -27.831   2.638  42.324  1.00110.50           C  
ANISOU 2147  C   VAL A 333    12569  19062  10354   -474    219   -623       C  
ATOM   2148  O   VAL A 333     -27.140   2.057  41.485  1.00111.65           O  
ANISOU 2148  O   VAL A 333    12826  19195  10400   -425    247   -775       O  
ATOM   2149  CB  VAL A 333     -28.240   1.431  44.571  1.00109.66           C  
ANISOU 2149  CB  VAL A 333    12727  18451  10489   -627    195   -673       C  
ATOM   2150  CG1 VAL A 333     -28.239   0.109  43.809  1.00112.03           C  
ANISOU 2150  CG1 VAL A 333    13263  18664  10639   -766    183   -918       C  
ATOM   2151  CG2 VAL A 333     -27.666   1.229  45.964  1.00107.87           C  
ANISOU 2151  CG2 VAL A 333    12620  17903  10464   -530    226   -632       C  
ATOM   2152  N   VAL A 334     -28.868   3.444  41.997  1.00106.68           N  
ANISOU 2152  N   VAL A 334    11871  18879   9784   -545    176   -486       N  
ATOM   2153  CA  VAL A 334     -29.312   3.708  40.621  1.00107.89           C  
ANISOU 2153  CA  VAL A 334    11892  19386   9716   -591    149   -497       C  
ATOM   2154  C   VAL A 334     -28.163   4.428  39.871  1.00110.51           C  
ANISOU 2154  C   VAL A 334    12177  19779  10032   -367    219   -440       C  
ATOM   2155  O   VAL A 334     -27.905   4.121  38.703  1.00111.04           O  
ANISOU 2155  O   VAL A 334    12256  20003   9929   -373    223   -552       O  
ATOM   2156  CB  VAL A 334     -30.659   4.491  40.602  1.00111.99           C  
ANISOU 2156  CB  VAL A 334    12173  20230  10148   -662     95   -321       C  
ATOM   2157  CG1 VAL A 334     -30.965   5.083  39.227  1.00113.30           C  
ANISOU 2157  CG1 VAL A 334    12165  20788  10094   -629     79   -266       C  
ATOM   2158  CG2 VAL A 334     -31.807   3.600  41.058  1.00112.97           C  
ANISOU 2158  CG2 VAL A 334    12319  20388  10218   -942     20   -408       C  
ATOM   2159  N   LEU A 335     -27.434   5.317  40.580  1.00105.07           N  
ANISOU 2159  N   LEU A 335    11453  18959   9511   -193    274   -279       N  
ATOM   2160  CA  LEU A 335     -26.276   6.042  40.060  1.00104.38           C  
ANISOU 2160  CA  LEU A 335    11321  18917   9423    -18    344   -202       C  
ATOM   2161  C   LEU A 335     -25.130   5.064  39.778  1.00109.31           C  
ANISOU 2161  C   LEU A 335    12090  19407  10035     45    388   -394       C  
ATOM   2162  O   LEU A 335     -24.529   5.145  38.706  1.00109.91           O  
ANISOU 2162  O   LEU A 335    12128  19657   9976    119    425   -430       O  
ATOM   2163  CB  LEU A 335     -25.832   7.129  41.057  1.00102.38           C  
ANISOU 2163  CB  LEU A 335    11030  18523   9345     91    384      0       C  
ATOM   2164  CG  LEU A 335     -24.892   8.207  40.533  1.00106.64           C  
ANISOU 2164  CG  LEU A 335    11496  19161   9860    213    449    144       C  
ATOM   2165  CD1 LEU A 335     -25.306   9.563  41.038  1.00105.78           C  
ANISOU 2165  CD1 LEU A 335    11336  19048   9808    256    461    381       C  
ATOM   2166  CD2 LEU A 335     -23.457   7.932  40.937  1.00108.27           C  
ANISOU 2166  CD2 LEU A 335    11765  19209  10163    290    503     91       C  
ATOM   2167  N   THR A 336     -24.845   4.135  40.726  1.00106.07           N  
ANISOU 2167  N   THR A 336    11852  18702   9749     37    388   -510       N  
ATOM   2168  CA  THR A 336     -23.781   3.129  40.585  1.00107.14           C  
ANISOU 2168  CA  THR A 336    12155  18686   9866    148    438   -687       C  
ATOM   2169  C   THR A 336     -24.117   2.169  39.443  1.00114.56           C  
ANISOU 2169  C   THR A 336    13218  19715  10596     67    422   -902       C  
ATOM   2170  O   THR A 336     -23.207   1.762  38.720  1.00115.30           O  
ANISOU 2170  O   THR A 336    13377  19845  10586    210    481  -1012       O  
ATOM   2171  CB  THR A 336     -23.496   2.367  41.898  1.00111.98           C  
ANISOU 2171  CB  THR A 336    12945  18958  10646    175    442   -741       C  
ATOM   2172  OG1 THR A 336     -24.602   1.541  42.255  1.00109.98           O  
ANISOU 2172  OG1 THR A 336    12834  18569  10383    -28    380   -843       O  
ATOM   2173  CG2 THR A 336     -23.115   3.282  43.050  1.00107.10           C  
ANISOU 2173  CG2 THR A 336    12218  18258  10218    245    455   -546       C  
ATOM   2174  N   TYR A 337     -25.420   1.835  39.266  1.00113.38           N  
ANISOU 2174  N   TYR A 337    13090  19628  10361   -168    344   -958       N  
ATOM   2175  CA  TYR A 337     -25.899   0.964  38.191  1.00116.80           C  
ANISOU 2175  CA  TYR A 337    13646  20165  10569   -312    312  -1167       C  
ATOM   2176  C   TYR A 337     -25.792   1.681  36.832  1.00124.47           C  
ANISOU 2176  C   TYR A 337    14430  21507  11356   -253    323  -1119       C  
ATOM   2177  O   TYR A 337     -25.453   1.034  35.835  1.00126.09           O  
ANISOU 2177  O   TYR A 337    14752  21778  11378   -235    345  -1300       O  
ATOM   2178  CB  TYR A 337     -27.342   0.485  38.453  1.00118.74           C  
ANISOU 2178  CB  TYR A 337    13926  20427  10762   -625    216  -1216       C  
ATOM   2179  CG  TYR A 337     -27.913  -0.383  37.348  1.00123.93           C  
ANISOU 2179  CG  TYR A 337    14713  21214  11162   -837    169  -1434       C  
ATOM   2180  CD1 TYR A 337     -27.555  -1.724  37.231  1.00128.01           C  
ANISOU 2180  CD1 TYR A 337    15590  21444  11605   -889    191  -1693       C  
ATOM   2181  CD2 TYR A 337     -28.802   0.141  36.411  1.00125.96           C  
ANISOU 2181  CD2 TYR A 337    14750  21882  11228   -978    105  -1383       C  
ATOM   2182  CE1 TYR A 337     -28.062  -2.521  36.202  1.00132.06           C  
ANISOU 2182  CE1 TYR A 337    16262  22055  11860  -1107    148  -1912       C  
ATOM   2183  CE2 TYR A 337     -29.314  -0.645  35.377  1.00129.94           C  
ANISOU 2183  CE2 TYR A 337    15367  22532  11471  -1198     55  -1591       C  
ATOM   2184  CZ  TYR A 337     -28.949  -1.978  35.281  1.00139.93           C  
ANISOU 2184  CZ  TYR A 337    17013  23487  12667  -1280     74  -1864       C  
ATOM   2185  OH  TYR A 337     -29.452  -2.753  34.261  1.00144.40           O  
ANISOU 2185  OH  TYR A 337    17731  24179  12958  -1521     24  -2086       O  
ATOM   2186  N   ALA A 338     -26.088   3.006  36.798  1.00121.35           N  
ANISOU 2186  N   ALA A 338    13771  21341  10995   -213    315   -876       N  
ATOM   2187  CA  ALA A 338     -26.009   3.839  35.589  1.00122.53           C  
ANISOU 2187  CA  ALA A 338    13737  21841  10976   -145    331   -781       C  
ATOM   2188  C   ALA A 338     -24.571   3.909  35.078  1.00129.45           C  
ANISOU 2188  C   ALA A 338    14636  22717  11831     67    427   -806       C  
ATOM   2189  O   ALA A 338     -24.329   3.751  33.878  1.00131.23           O  
ANISOU 2189  O   ALA A 338    14849  23161  11853     99    448   -893       O  
ATOM   2190  CB  ALA A 338     -26.532   5.237  35.877  1.00121.65           C  
ANISOU 2190  CB  ALA A 338    13405  21885  10930   -109    319   -497       C  
ATOM   2191  N   TRP A 339     -23.619   4.093  36.009  1.00126.36           N  
ANISOU 2191  N   TRP A 339    14272  22107  11634    207    484   -736       N  
ATOM   2192  CA  TRP A 339     -22.196   4.160  35.716  1.00127.48           C  
ANISOU 2192  CA  TRP A 339    14399  22275  11762    408    578   -738       C  
ATOM   2193  C   TRP A 339     -21.657   2.785  35.276  1.00135.01           C  
ANISOU 2193  C   TRP A 339    15569  23131  12599    491    614  -1009       C  
ATOM   2194  O   TRP A 339     -20.739   2.728  34.458  1.00136.63           O  
ANISOU 2194  O   TRP A 339    15744  23499  12672    650    687  -1053       O  
ATOM   2195  CB  TRP A 339     -21.420   4.705  36.923  1.00124.55           C  
ANISOU 2195  CB  TRP A 339    13985  21726  11613    500    614   -587       C  
ATOM   2196  CG  TRP A 339     -19.973   4.928  36.621  1.00126.31           C  
ANISOU 2196  CG  TRP A 339    14130  22060  11801    680    706   -550       C  
ATOM   2197  CD1 TRP A 339     -19.449   5.810  35.723  1.00129.90           C  
ANISOU 2197  CD1 TRP A 339    14415  22802  12138    720    755   -421       C  
ATOM   2198  CD2 TRP A 339     -18.878   4.158  37.113  1.00126.68           C  
ANISOU 2198  CD2 TRP A 339    14263  21977  11894    850    763   -649       C  
ATOM   2199  NE1 TRP A 339     -18.085   5.665  35.655  1.00130.10           N  
ANISOU 2199  NE1 TRP A 339    14390  22907  12134    882    838   -430       N  
ATOM   2200  CE2 TRP A 339     -17.706   4.654  36.496  1.00131.51           C  
ANISOU 2200  CE2 TRP A 339    14715  22846  12408    983    845   -568       C  
ATOM   2201  CE3 TRP A 339     -18.767   3.103  38.031  1.00128.03           C  
ANISOU 2201  CE3 TRP A 339    14628  21851  12166    912    757   -784       C  
ATOM   2202  CZ2 TRP A 339     -16.439   4.146  36.785  1.00131.70           C  
ANISOU 2202  CZ2 TRP A 339    14734  22880  12427   1189    918   -614       C  
ATOM   2203  CZ3 TRP A 339     -17.510   2.615  38.328  1.00130.44           C  
ANISOU 2203  CZ3 TRP A 339    14954  22133  12473   1138    830   -824       C  
ATOM   2204  CH2 TRP A 339     -16.366   3.125  37.700  1.00132.00           C  
ANISOU 2204  CH2 TRP A 339    14960  22630  12565   1281    909   -742       C  
ATOM   2205  N   HIS A 340     -22.248   1.692  35.790  1.00132.64           N  
ANISOU 2205  N   HIS A 340    15500  22568  12327    385    568  -1185       N  
ATOM   2206  CA  HIS A 340     -21.902   0.316  35.436  1.00135.14           C  
ANISOU 2206  CA  HIS A 340    16106  22720  12520    449    601  -1456       C  
ATOM   2207  C   HIS A 340     -22.324  -0.002  34.003  1.00141.83           C  
ANISOU 2207  C   HIS A 340    16994  23802  13093    363    585  -1610       C  
ATOM   2208  O   HIS A 340     -21.542  -0.589  33.251  1.00143.11           O  
ANISOU 2208  O   HIS A 340    17281  23998  13097    535    658  -1764       O  
ATOM   2209  CB  HIS A 340     -22.570  -0.662  36.416  1.00136.13           C  
ANISOU 2209  CB  HIS A 340    16493  22483  12748    300    550  -1575       C  
ATOM   2210  CG  HIS A 340     -22.618  -2.089  35.947  1.00142.51           C  
ANISOU 2210  CG  HIS A 340    17666  23092  13388    272    563  -1867       C  
ATOM   2211  ND1 HIS A 340     -21.505  -2.905  36.005  1.00145.68           N  
ANISOU 2211  ND1 HIS A 340    18296  23293  13761    552    659  -1997       N  
ATOM   2212  CD2 HIS A 340     -23.654  -2.802  35.442  1.00146.24           C  
ANISOU 2212  CD2 HIS A 340    18322  23541  13702     -6    493  -2044       C  
ATOM   2213  CE1 HIS A 340     -21.892  -4.078  35.530  1.00147.88           C  
ANISOU 2213  CE1 HIS A 340    18930  23388  13868    450    652  -2255       C  
ATOM   2214  NE2 HIS A 340     -23.178  -4.068  35.186  1.00148.66           N  
ANISOU 2214  NE2 HIS A 340    19019  23582  13884     88    549  -2297       N  
ATOM   2215  N   THR A 341     -23.569   0.386  33.640  1.00138.97           N  
ANISOU 2215  N   THR A 341    16518  23626  12658    108    491  -1563       N  
ATOM   2216  CA  THR A 341     -24.182   0.134  32.333  1.00141.25           C  
ANISOU 2216  CA  THR A 341    16818  24179  12671    -31    450  -1697       C  
ATOM   2217  C   THR A 341     -23.759   1.156  31.267  1.00144.98           C  
ANISOU 2217  C   THR A 341    17030  25044  13014     99    491  -1553       C  
ATOM   2218  O   THR A 341     -23.973   0.896  30.081  1.00146.71           O  
ANISOU 2218  O   THR A 341    17268  25496  12979     47    479  -1678       O  
ATOM   2219  CB  THR A 341     -25.710   0.075  32.453  1.00149.73           C  
ANISOU 2219  CB  THR A 341    17856  25335  13701   -364    327  -1695       C  
ATOM   2220  OG1 THR A 341     -26.181   1.235  33.143  1.00147.45           O  
ANISOU 2220  OG1 THR A 341    17295  25148  13580   -373    295  -1414       O  
ATOM   2221  CG2 THR A 341     -26.190  -1.193  33.152  1.00148.73           C  
ANISOU 2221  CG2 THR A 341    18050  24856  13606   -562    287  -1901       C  
ATOM   2222  N   SER A 342     -23.143   2.289  31.666  1.00139.36           N  
ANISOU 2222  N   SER A 342    16095  24399  12454    251    540  -1298       N  
ATOM   2223  CA  SER A 342     -22.669   3.303  30.718  1.00139.50           C  
ANISOU 2223  CA  SER A 342    15887  24761  12354    362    589  -1136       C  
ATOM   2224  C   SER A 342     -21.537   2.739  29.838  1.00145.94           C  
ANISOU 2224  C   SER A 342    16784  25670  12998    556    685  -1291       C  
ATOM   2225  O   SER A 342     -21.416   3.116  28.672  1.00146.74           O  
ANISOU 2225  O   SER A 342    16770  26095  12890    590    710  -1268       O  
ATOM   2226  CB  SER A 342     -22.206   4.556  31.457  1.00140.47           C  
ANISOU 2226  CB  SER A 342    15821  24871  12678    446    624   -844       C  
ATOM   2227  OG  SER A 342     -21.065   4.316  32.265  1.00147.52           O  
ANISOU 2227  OG  SER A 342    16775  25547  13728    600    696   -852       O  
ATOM   2228  N   PHE A 343     -20.736   1.813  30.403  1.00143.58           N  
ANISOU 2228  N   PHE A 343    16686  25098  12770    703    744  -1447       N  
ATOM   2229  CA  PHE A 343     -19.638   1.128  29.716  1.00145.87           C  
ANISOU 2229  CA  PHE A 343    17085  25446  12895    941    848  -1611       C  
ATOM   2230  C   PHE A 343     -20.149   0.004  28.810  1.00153.82           C  
ANISOU 2230  C   PHE A 343    18358  26437  13650    870    826  -1913       C  
ATOM   2231  O   PHE A 343     -19.425  -0.445  27.920  1.00155.83           O  
ANISOU 2231  O   PHE A 343    18690  26823  13694   1057    910  -2053       O  
ATOM   2232  CB  PHE A 343     -18.646   0.539  30.725  1.00147.11           C  
ANISOU 2232  CB  PHE A 343    17370  25319  13207   1159    920  -1651       C  
ATOM   2233  CG  PHE A 343     -17.826   1.546  31.485  1.00146.34           C  
ANISOU 2233  CG  PHE A 343    17016  25285  13300   1257    961  -1386       C  
ATOM   2234  CD1 PHE A 343     -16.873   2.321  30.839  1.00149.76           C  
ANISOU 2234  CD1 PHE A 343    17208  26058  13637   1391   1043  -1241       C  
ATOM   2235  CD2 PHE A 343     -17.971   1.687  32.855  1.00146.23           C  
ANISOU 2235  CD2 PHE A 343    17015  25000  13544   1201    921  -1287       C  
ATOM   2236  CE1 PHE A 343     -16.110   3.253  31.546  1.00148.99           C  
ANISOU 2236  CE1 PHE A 343    16891  26024  13695   1427   1077  -1000       C  
ATOM   2237  CE2 PHE A 343     -17.201   2.614  33.562  1.00147.30           C  
ANISOU 2237  CE2 PHE A 343    16935  25197  13835   1262    955  -1055       C  
ATOM   2238  CZ  PHE A 343     -16.274   3.390  32.902  1.00145.95           C  
ANISOU 2238  CZ  PHE A 343    16533  25360  13561   1360   1030   -916       C  
ATOM   2239  N   LYS A 344     -21.382  -0.478  29.057  1.00151.09           N  
ANISOU 2239  N   LYS A 344    18164  25934  13310    591    717  -2019       N  
ATOM   2240  CA  LYS A 344     -21.994  -1.544  28.263  1.00154.09           C  
ANISOU 2240  CA  LYS A 344    18824  26283  13441    440    678  -2313       C  
ATOM   2241  C   LYS A 344     -22.602  -0.970  26.964  1.00160.22           C  
ANISOU 2241  C   LYS A 344    19403  27503  13969    303    627  -2283       C  
ATOM   2242  O   LYS A 344     -22.990  -1.737  26.080  1.00162.85           O  
ANISOU 2242  O   LYS A 344    19934  27899  14042    187    601  -2525       O  
ATOM   2243  CB  LYS A 344     -23.031  -2.323  29.092  1.00156.29           C  
ANISOU 2243  CB  LYS A 344    19341  26233  13809    155    581  -2432       C  
ATOM   2244  CG  LYS A 344     -22.378  -3.274  30.092  1.00165.70           C  
ANISOU 2244  CG  LYS A 344    20852  26958  15148    311    644  -2550       C  
ATOM   2245  CD  LYS A 344     -23.377  -3.973  30.991  1.00172.23           C  
ANISOU 2245  CD  LYS A 344    21908  27456  16076     13    555  -2634       C  
ATOM   2246  CE  LYS A 344     -22.679  -4.955  31.897  1.00179.93           C  
ANISOU 2246  CE  LYS A 344    23235  27963  17167    199    628  -2749       C  
ATOM   2247  NZ  LYS A 344     -23.627  -5.608  32.834  1.00187.51           N  
ANISOU 2247  NZ  LYS A 344    24422  28593  18231   -105    547  -2806       N  
ATOM   2248  N   ALA A 345     -22.627   0.378  26.834  1.00155.37           N  
ANISOU 2248  N   ALA A 345    18423  27190  13418    331    621  -1986       N  
ATOM   2249  CA  ALA A 345     -23.114   1.104  25.662  1.00156.36           C  
ANISOU 2249  CA  ALA A 345    18328  27759  13323    253    585  -1893       C  
ATOM   2250  C   ALA A 345     -22.075   1.069  24.532  1.00162.25           C  
ANISOU 2250  C   ALA A 345    19061  28738  13847    483    694  -1961       C  
ATOM   2251  O   ALA A 345     -22.451   1.175  23.362  1.00163.97           O  
ANISOU 2251  O   ALA A 345    19215  29288  13798    415    668  -2007       O  
ATOM   2252  CB  ALA A 345     -23.445   2.543  26.036  1.00154.63           C  
ANISOU 2252  CB  ALA A 345    17783  27710  13259    238    557  -1539       C  
ATOM   2253  N   LEU A 346     -20.776   0.880  24.883  1.00158.38           N  
ANISOU 2253  N   LEU A 346    18624  28104  13448    761    817  -1969       N  
ATOM   2254  CA  LEU A 346     -19.652   0.812  23.938  1.00191.73           C  
ANISOU 2254  CA  LEU A 346    22819  32561  17470   1021    941  -2021       C  
ATOM   2255  C   LEU A 346     -19.759  -0.425  23.048  1.00207.72           C  
ANISOU 2255  C   LEU A 346    25158  34564  19202   1033    953  -2375       C  
ATOM   2256  O   LEU A 346     -19.316  -0.399  21.903  1.00166.44           O  
ANISOU 2256  O   LEU A 346    19885  29642  13711   1157   1017  -2434       O  
ATOM   2257  CB  LEU A 346     -18.278   0.807  24.657  1.00191.02           C  
ANISOU 2257  CB  LEU A 346    22701  32340  17538   1313   1063  -1948       C  
ATOM   2258  CG  LEU A 346     -18.082   1.630  25.947  1.00192.59           C  
ANISOU 2258  CG  LEU A 346    22723  32385  18067   1292   1050  -1681       C  
ATOM   2259  CD1 LEU A 346     -16.801   1.237  26.646  1.00192.77           C  
ANISOU 2259  CD1 LEU A 346    22784  32265  18194   1568   1157  -1693       C  
ATOM   2260  CD2 LEU A 346     -18.070   3.117  25.687  1.00193.64           C  
ANISOU 2260  CD2 LEU A 346    22520  32821  18233   1221   1047  -1358       C  
ATOM   2261  N   GLN A 351     -28.080  -0.132  24.808  1.00175.75           N  
ANISOU 2261  N   GLN A 351    20823  30713  15240   -957     99  -2217       N  
ATOM   2262  CA  GLN A 351     -28.940  -0.271  25.984  1.00174.42           C  
ANISOU 2262  CA  GLN A 351    20652  30357  15263  -1169     21  -2158       C  
ATOM   2263  C   GLN A 351     -29.142   1.101  26.686  1.00175.36           C  
ANISOU 2263  C   GLN A 351    20426  30595  15608  -1023     23  -1782       C  
ATOM   2264  O   GLN A 351     -28.379   1.442  27.599  1.00172.24           O  
ANISOU 2264  O   GLN A 351    20051  29902  15490   -816    102  -1664       O  
ATOM   2265  CB  GLN A 351     -28.371  -1.318  26.965  1.00175.32           C  
ANISOU 2265  CB  GLN A 351    21138  29911  15566  -1156     73  -2347       C  
ATOM   2266  CG  GLN A 351     -28.502  -2.769  26.493  1.00191.85           C  
ANISOU 2266  CG  GLN A 351    23646  31813  17435  -1376     52  -2723       C  
ATOM   2267  CD  GLN A 351     -27.865  -3.779  27.429  1.00207.21           C  
ANISOU 2267  CD  GLN A 351    25994  33183  19553  -1305    121  -2890       C  
ATOM   2268  OE1 GLN A 351     -27.275  -3.446  28.465  1.00198.67           O  
ANISOU 2268  OE1 GLN A 351    24869  31855  18764  -1087    183  -2732       O  
ATOM   2269  NE2 GLN A 351     -27.967  -5.050  27.074  1.00201.87           N  
ANISOU 2269  NE2 GLN A 351    25744  32276  18681  -1486    113  -3215       N  
ATOM   2270  N   PRO A 352     -30.150   1.909  26.264  1.00172.44           N  
ANISOU 2270  N   PRO A 352    19749  30665  15106  -1115    -59  -1591       N  
ATOM   2271  CA  PRO A 352     -30.368   3.214  26.921  1.00169.48           C  
ANISOU 2271  CA  PRO A 352    19099  30372  14923   -948    -46  -1238       C  
ATOM   2272  C   PRO A 352     -31.008   3.079  28.299  1.00170.84           C  
ANISOU 2272  C   PRO A 352    19283  30306  15322  -1069    -90  -1180       C  
ATOM   2273  O   PRO A 352     -31.735   2.115  28.541  1.00171.83           O  
ANISOU 2273  O   PRO A 352    19528  30381  15379  -1364   -170  -1365       O  
ATOM   2274  CB  PRO A 352     -31.293   3.955  25.956  1.00172.98           C  
ANISOU 2274  CB  PRO A 352    19250  31374  15102   -988   -119  -1078       C  
ATOM   2275  CG  PRO A 352     -31.972   2.905  25.168  1.00180.86           C  
ANISOU 2275  CG  PRO A 352    20333  32585  15802  -1302   -217  -1351       C  
ATOM   2276  CD  PRO A 352     -31.153   1.655  25.208  1.00177.19           C  
ANISOU 2276  CD  PRO A 352    20252  31712  15361  -1368   -168  -1684       C  
ATOM   2277  N   LEU A 353     -30.742   4.058  29.190  1.00163.90           N  
ANISOU 2277  N   LEU A 353    18291  29287  14696   -858    -35   -921       N  
ATOM   2278  CA  LEU A 353     -31.260   4.098  30.563  1.00161.59           C  
ANISOU 2278  CA  LEU A 353    17993  28771  14631   -919    -59   -831       C  
ATOM   2279  C   LEU A 353     -32.686   4.675  30.635  1.00165.86           C  
ANISOU 2279  C   LEU A 353    18259  29697  15062  -1022   -150   -645       C  
ATOM   2280  O   LEU A 353     -33.386   4.427  31.620  1.00165.11           O  
ANISOU 2280  O   LEU A 353    18153  29508  15074  -1158   -194   -625       O  
ATOM   2281  CB  LEU A 353     -30.325   4.917  31.481  1.00158.39           C  
ANISOU 2281  CB  LEU A 353    17604  28056  14521   -647     40   -644       C  
ATOM   2282  CG  LEU A 353     -28.920   4.355  31.735  1.00161.83           C  
ANISOU 2282  CG  LEU A 353    18276  28112  15101   -527    131   -794       C  
ATOM   2283  CD1 LEU A 353     -27.999   5.426  32.286  1.00159.46           C  
ANISOU 2283  CD1 LEU A 353    17913  27668  15006   -275    222   -570       C  
ATOM   2284  CD2 LEU A 353     -28.956   3.160  32.675  1.00163.91           C  
ANISOU 2284  CD2 LEU A 353    18782  28004  15491   -677    110   -998       C  
ATOM   2285  N   SER A 354     -33.114   5.424  29.589  1.00163.18           N  
ANISOU 2285  N   SER A 354    17693  29815  14492   -946   -174   -502       N  
ATOM   2286  CA  SER A 354     -34.428   6.083  29.477  1.00163.80           C  
ANISOU 2286  CA  SER A 354    17473  30351  14413   -972   -251   -292       C  
ATOM   2287  C   SER A 354     -35.615   5.105  29.537  1.00168.90           C  
ANISOU 2287  C   SER A 354    18062  31225  14887  -1351   -377   -452       C  
ATOM   2288  O   SER A 354     -36.707   5.504  29.945  1.00168.94           O  
ANISOU 2288  O   SER A 354    17829  31523  14838  -1387   -434   -280       O  
ATOM   2289  CB  SER A 354     -34.514   6.901  28.190  1.00168.97           C  
ANISOU 2289  CB  SER A 354    17938  31447  14816   -813   -249   -142       C  
ATOM   2290  OG  SER A 354     -34.068   8.232  28.406  1.00175.77           O  
ANISOU 2290  OG  SER A 354    18739  32236  15810   -472   -156    155       O  
ATOM   2291  N   GLY A 355     -35.391   3.858  29.122  1.00166.30           N  
ANISOU 2291  N   GLY A 355    17958  30774  14455  -1626   -413   -772       N  
ATOM   2292  CA  GLY A 355     -36.397   2.803  29.155  1.00168.28           C  
ANISOU 2292  CA  GLY A 355    18228  31181  14531  -2057   -530   -963       C  
ATOM   2293  C   GLY A 355     -36.571   2.214  30.540  1.00169.59           C  
ANISOU 2293  C   GLY A 355    18544  30960  14933  -2209   -530  -1013       C  
ATOM   2294  O   GLY A 355     -37.701   1.958  30.966  1.00170.86           O  
ANISOU 2294  O   GLY A 355    18555  31357  15006  -2476   -617   -981       O  
ATOM   2295  N   LYS A 356     -35.444   2.043  31.271  1.00161.82           N  
ANISOU 2295  N   LYS A 356    17831  29413  14241  -2027   -428  -1069       N  
ATOM   2296  CA  LYS A 356     -35.363   1.472  32.621  1.00159.11           C  
ANISOU 2296  CA  LYS A 356    17679  28626  14148  -2117   -408  -1119       C  
ATOM   2297  C   LYS A 356     -35.877   2.424  33.737  1.00158.33           C  
ANISOU 2297  C   LYS A 356    17345  28574  14240  -1957   -394   -825       C  
ATOM   2298  O   LYS A 356     -35.748   2.084  34.917  1.00156.44           O  
ANISOU 2298  O   LYS A 356    17247  27972  14223  -1989   -368   -835       O  
ATOM   2299  CB  LYS A 356     -33.911   1.054  32.926  1.00159.72           C  
ANISOU 2299  CB  LYS A 356    18096  28150  14441  -1920   -301  -1257       C  
ATOM   2300  CG  LYS A 356     -33.437  -0.176  32.159  1.00172.25           C  
ANISOU 2300  CG  LYS A 356    20016  29565  15866  -2090   -302  -1590       C  
ATOM   2301  CD  LYS A 356     -31.967  -0.475  32.444  1.00178.01           C  
ANISOU 2301  CD  LYS A 356    21032  29815  16790  -1813   -183  -1687       C  
ATOM   2302  CE  LYS A 356     -31.467  -1.696  31.717  1.00188.27           C  
ANISOU 2302  CE  LYS A 356    22698  30919  17918  -1920   -166  -2015       C  
ATOM   2303  NZ  LYS A 356     -32.003  -2.954  32.303  1.00197.41           N  
ANISOU 2303  NZ  LYS A 356    24172  31779  19054  -2265   -216  -2223       N  
ATOM   2304  N   THR A 357     -36.486   3.580  33.366  1.00153.11           N  
ANISOU 2304  N   THR A 357    16345  28359  13472  -1779   -409   -565       N  
ATOM   2305  CA  THR A 357     -37.049   4.593  34.275  1.00150.58           C  
ANISOU 2305  CA  THR A 357    15802  28137  13276  -1579   -388   -274       C  
ATOM   2306  C   THR A 357     -38.134   3.964  35.177  1.00154.39           C  
ANISOU 2306  C   THR A 357    16212  28702  13747  -1877   -460   -293       C  
ATOM   2307  O   THR A 357     -38.223   4.317  36.359  1.00151.67           O  
ANISOU 2307  O   THR A 357    15857  28162  13611  -1759   -418   -159       O  
ATOM   2308  CB  THR A 357     -37.589   5.791  33.464  1.00156.98           C  
ANISOU 2308  CB  THR A 357    16297  29458  13891  -1345   -395    -19       C  
ATOM   2309  OG1 THR A 357     -36.578   6.245  32.561  1.00154.04           O  
ANISOU 2309  OG1 THR A 357    16012  29012  13503  -1130   -332    -20       O  
ATOM   2310  CG2 THR A 357     -38.029   6.958  34.344  1.00154.30           C  
ANISOU 2310  CG2 THR A 357    15785  29170  13673  -1051   -347    291       C  
ATOM   2311  N   SER A 358     -38.922   3.015  34.618  1.00153.59           N  
ANISOU 2311  N   SER A 358    16078  28887  13391  -2284   -565   -467       N  
ATOM   2312  CA  SER A 358     -39.986   2.279  35.309  1.00154.72           C  
ANISOU 2312  CA  SER A 358    16154  29167  13466  -2662   -645   -509       C  
ATOM   2313  C   SER A 358     -39.427   1.506  36.509  1.00155.81           C  
ANISOU 2313  C   SER A 358    16626  28693  13881  -2759   -596   -636       C  
ATOM   2314  O   SER A 358     -39.985   1.620  37.597  1.00154.66           O  
ANISOU 2314  O   SER A 358    16381  28537  13844  -2788   -594   -508       O  
ATOM   2315  CB  SER A 358     -40.695   1.313  34.359  1.00162.48           C  
ANISOU 2315  CB  SER A 358    17122  30501  14112  -3130   -764   -720       C  
ATOM   2316  OG  SER A 358     -40.914   1.833  33.057  1.00173.97           O  
ANISOU 2316  OG  SER A 358    18355  32447  15299  -3047   -805   -670       O  
ATOM   2317  N   TYR A 359     -38.317   0.750  36.316  1.00151.27           N  
ANISOU 2317  N   TYR A 359    16440  27628  13410  -2774   -551   -873       N  
ATOM   2318  CA  TYR A 359     -37.655  -0.037  37.367  1.00149.48           C  
ANISOU 2318  CA  TYR A 359    16565  26800  13430  -2823   -497  -1000       C  
ATOM   2319  C   TYR A 359     -37.049   0.856  38.454  1.00149.46           C  
ANISOU 2319  C   TYR A 359    16525  26524  13738  -2434   -404   -792       C  
ATOM   2320  O   TYR A 359     -37.061   0.473  39.625  1.00148.24           O  
ANISOU 2320  O   TYR A 359    16497  26066  13761  -2498   -384   -787       O  
ATOM   2321  CB  TYR A 359     -36.541  -0.938  36.791  1.00151.10           C  
ANISOU 2321  CB  TYR A 359    17178  26593  13640  -2834   -456  -1279       C  
ATOM   2322  CG  TYR A 359     -36.977  -1.969  35.770  1.00156.60           C  
ANISOU 2322  CG  TYR A 359    18029  27439  14034  -3230   -537  -1539       C  
ATOM   2323  CD1 TYR A 359     -37.732  -3.078  36.146  1.00161.25           C  
ANISOU 2323  CD1 TYR A 359    18796  27951  14519  -3701   -606  -1692       C  
ATOM   2324  CD2 TYR A 359     -36.541  -1.899  34.450  1.00158.36           C  
ANISOU 2324  CD2 TYR A 359    18271  27828  14071  -3147   -536  -1649       C  
ATOM   2325  CE1 TYR A 359     -38.114  -4.044  35.214  1.00165.83           C  
ANISOU 2325  CE1 TYR A 359    19568  28638  14804  -4105   -682  -1948       C  
ATOM   2326  CE2 TYR A 359     -36.907  -2.864  33.512  1.00162.73           C  
ANISOU 2326  CE2 TYR A 359    19003  28498  14329  -3518   -609  -1908       C  
ATOM   2327  CZ  TYR A 359     -37.694  -3.935  33.899  1.00172.16           C  
ANISOU 2327  CZ  TYR A 359    20383  29614  15416  -4005   -683  -2063       C  
ATOM   2328  OH  TYR A 359     -38.059  -4.886  32.978  1.00176.35           O  
ANISOU 2328  OH  TYR A 359    21125  30241  15637  -4408   -758  -2331       O  
ATOM   2329  N   PHE A 360     -36.499   2.032  38.063  1.00143.46           N  
ANISOU 2329  N   PHE A 360    15616  25860  13033  -2051   -345   -624       N  
ATOM   2330  CA  PHE A 360     -35.854   2.977  38.979  1.00139.42           C  
ANISOU 2330  CA  PHE A 360    15090  25095  12787  -1695   -256   -432       C  
ATOM   2331  C   PHE A 360     -36.870   3.635  39.913  1.00141.80           C  
ANISOU 2331  C   PHE A 360    15149  25603  13124  -1659   -270   -204       C  
ATOM   2332  O   PHE A 360     -36.765   3.451  41.124  1.00139.44           O  
ANISOU 2332  O   PHE A 360    14955  25002  13022  -1657   -241   -182       O  
ATOM   2333  CB  PHE A 360     -35.044   4.047  38.218  1.00139.73           C  
ANISOU 2333  CB  PHE A 360    15060  25199  12834  -1352   -193   -315       C  
ATOM   2334  CG  PHE A 360     -33.929   3.529  37.331  1.00141.15           C  
ANISOU 2334  CG  PHE A 360    15451  25199  12982  -1323   -159   -512       C  
ATOM   2335  CD1 PHE A 360     -33.136   2.458  37.730  1.00143.67           C  
ANISOU 2335  CD1 PHE A 360    16085  25087  13418  -1403   -131   -730       C  
ATOM   2336  CD2 PHE A 360     -33.637   4.149  36.123  1.00143.39           C  
ANISOU 2336  CD2 PHE A 360    15624  25748  13112  -1178   -144   -464       C  
ATOM   2337  CE1 PHE A 360     -32.106   1.986  36.913  1.00144.86           C  
ANISOU 2337  CE1 PHE A 360    16426  25098  13516  -1330    -88   -906       C  
ATOM   2338  CE2 PHE A 360     -32.603   3.679  35.308  1.00146.31           C  
ANISOU 2338  CE2 PHE A 360    16174  25983  13434  -1134   -104   -642       C  
ATOM   2339  CZ  PHE A 360     -31.843   2.601  35.710  1.00144.20           C  
ANISOU 2339  CZ  PHE A 360    16210  25306  13274  -1199    -74   -864       C  
ATOM   2340  N   HIS A 361     -37.871   4.351  39.355  1.00139.39           N  
ANISOU 2340  N   HIS A 361    14521  25831  12610  -1622   -313    -35       N  
ATOM   2341  CA  HIS A 361     -38.919   5.048  40.113  1.00138.95           C  
ANISOU 2341  CA  HIS A 361    14200  26060  12535  -1534   -319    200       C  
ATOM   2342  C   HIS A 361     -39.790   4.095  40.947  1.00141.98           C  
ANISOU 2342  C   HIS A 361    14565  26485  12895  -1893   -378    128       C  
ATOM   2343  O   HIS A 361     -40.361   4.530  41.946  1.00141.14           O  
ANISOU 2343  O   HIS A 361    14326  26442  12858  -1798   -355    297       O  
ATOM   2344  CB  HIS A 361     -39.794   5.897  39.187  1.00141.98           C  
ANISOU 2344  CB  HIS A 361    14243  27052  12649  -1406   -355    385       C  
ATOM   2345  CG  HIS A 361     -39.186   7.230  38.889  1.00144.03           C  
ANISOU 2345  CG  HIS A 361    14490  27262  12974   -963   -269    581       C  
ATOM   2346  ND1 HIS A 361     -39.494   8.348  39.646  1.00144.85           N  
ANISOU 2346  ND1 HIS A 361    14494  27388  13156   -636   -204    838       N  
ATOM   2347  CD2 HIS A 361     -38.266   7.571  37.956  1.00145.41           C  
ANISOU 2347  CD2 HIS A 361    14772  27336  13141   -818   -233    548       C  
ATOM   2348  CE1 HIS A 361     -38.774   9.334  39.134  1.00143.39           C  
ANISOU 2348  CE1 HIS A 361    14378  27101  13004   -325   -135    954       C  
ATOM   2349  NE2 HIS A 361     -38.019   8.915  38.115  1.00143.95           N  
ANISOU 2349  NE2 HIS A 361    14556  27112  13026   -429   -150    794       N  
ATOM   2350  N   LEU A 362     -39.875   2.805  40.562  1.00138.42           N  
ANISOU 2350  N   LEU A 362    14274  25981  12339  -2305   -446   -120       N  
ATOM   2351  CA  LEU A 362     -40.610   1.808  41.337  1.00138.60           C  
ANISOU 2351  CA  LEU A 362    14340  25985  12335  -2701   -498   -202       C  
ATOM   2352  C   LEU A 362     -39.835   1.518  42.618  1.00138.17           C  
ANISOU 2352  C   LEU A 362    14573  25333  12592  -2611   -423   -232       C  
ATOM   2353  O   LEU A 362     -40.344   1.779  43.699  1.00137.42           O  
ANISOU 2353  O   LEU A 362    14367  25263  12585  -2575   -404    -85       O  
ATOM   2354  CB  LEU A 362     -40.840   0.516  40.523  1.00141.53           C  
ANISOU 2354  CB  LEU A 362    14876  26406  12493  -3182   -585   -471       C  
ATOM   2355  CG  LEU A 362     -41.387  -0.700  41.278  1.00147.67           C  
ANISOU 2355  CG  LEU A 362    15823  27032  13251  -3652   -631   -601       C  
ATOM   2356  CD1 LEU A 362     -42.896  -0.623  41.431  1.00150.55           C  
ANISOU 2356  CD1 LEU A 362    15796  28024  13380  -3936   -714   -458       C  
ATOM   2357  CD2 LEU A 362     -40.999  -1.982  40.583  1.00151.89           C  
ANISOU 2357  CD2 LEU A 362    16741  27295  13677  -4011   -670   -916       C  
ATOM   2358  N   LEU A 363     -38.583   1.048  42.486  1.00131.77           N  
ANISOU 2358  N   LEU A 363    14112  24020  11933  -2533   -376   -407       N  
ATOM   2359  CA  LEU A 363     -37.695   0.678  43.587  1.00128.79           C  
ANISOU 2359  CA  LEU A 363    14029  23074  11830  -2434   -308   -455       C  
ATOM   2360  C   LEU A 363     -37.289   1.857  44.482  1.00128.53           C  
ANISOU 2360  C   LEU A 363    13890  22928  12016  -2033   -230   -233       C  
ATOM   2361  O   LEU A 363     -37.223   1.680  45.697  1.00126.94           O  
ANISOU 2361  O   LEU A 363    13785  22464  11983  -2027   -200   -193       O  
ATOM   2362  CB  LEU A 363     -36.437   0.015  43.017  1.00128.59           C  
ANISOU 2362  CB  LEU A 363    14350  22644  11862  -2382   -272   -676       C  
ATOM   2363  CG  LEU A 363     -36.431  -1.514  42.966  1.00135.83           C  
ANISOU 2363  CG  LEU A 363    15617  23285  12707  -2748   -304   -934       C  
ATOM   2364  CD1 LEU A 363     -37.343  -2.053  41.871  1.00139.56           C  
ANISOU 2364  CD1 LEU A 363    16022  24137  12866  -3128   -398  -1060       C  
ATOM   2365  CD2 LEU A 363     -35.025  -2.030  42.755  1.00137.95           C  
ANISOU 2365  CD2 LEU A 363    16244  23084  13088  -2556   -235  -1105       C  
ATOM   2366  N   THR A 364     -37.020   3.042  43.903  1.00123.15           N  
ANISOU 2366  N   THR A 364    13040  22431  11321  -1714   -197    -91       N  
ATOM   2367  CA  THR A 364     -36.575   4.205  44.684  1.00119.91           C  
ANISOU 2367  CA  THR A 364    12583  21879  11097  -1350   -119    106       C  
ATOM   2368  C   THR A 364     -37.664   4.830  45.552  1.00123.08           C  
ANISOU 2368  C   THR A 364    12755  22531  11478  -1293   -119    314       C  
ATOM   2369  O   THR A 364     -37.332   5.501  46.531  1.00120.93           O  
ANISOU 2369  O   THR A 364    12527  22041  11381  -1061    -55    436       O  
ATOM   2370  CB  THR A 364     -35.959   5.289  43.808  1.00125.83           C  
ANISOU 2370  CB  THR A 364    13267  22720  11823  -1051    -76    203       C  
ATOM   2371  OG1 THR A 364     -36.853   5.621  42.747  1.00126.85           O  
ANISOU 2371  OG1 THR A 364    13148  23353  11695  -1088   -127    270       O  
ATOM   2372  CG2 THR A 364     -34.594   4.901  43.282  1.00123.78           C  
ANISOU 2372  CG2 THR A 364    13242  22141  11647  -1003    -42     40       C  
ATOM   2373  N   TRP A 365     -38.942   4.640  45.208  1.00121.20           N  
ANISOU 2373  N   TRP A 365    12269  22769  11013  -1494   -186    358       N  
ATOM   2374  CA  TRP A 365     -40.007   5.246  46.003  1.00120.90           C  
ANISOU 2374  CA  TRP A 365    11981  23032  10925  -1404   -177    569       C  
ATOM   2375  C   TRP A 365     -40.811   4.200  46.790  1.00123.98           C  
ANISOU 2375  C   TRP A 365    12350  23479  11277  -1778   -225    507       C  
ATOM   2376  O   TRP A 365     -41.282   4.526  47.880  1.00122.75           O  
ANISOU 2376  O   TRP A 365    12106  23349  11183  -1686   -189    646       O  
ATOM   2377  CB  TRP A 365     -40.924   6.136  45.136  1.00121.56           C  
ANISOU 2377  CB  TRP A 365    11723  23708  10755  -1246   -198    749       C  
ATOM   2378  CG  TRP A 365     -40.183   7.200  44.365  1.00121.35           C  
ANISOU 2378  CG  TRP A 365    11736  23624  10749   -888   -144    834       C  
ATOM   2379  CD1 TRP A 365     -40.045   7.277  43.011  1.00125.39           C  
ANISOU 2379  CD1 TRP A 365    12190  24357  11097   -897   -178    791       C  
ATOM   2380  CD2 TRP A 365     -39.391   8.270  44.908  1.00118.79           C  
ANISOU 2380  CD2 TRP A 365    11555  22963  10617   -510    -46    961       C  
ATOM   2381  NE1 TRP A 365     -39.245   8.344  42.673  1.00123.27           N  
ANISOU 2381  NE1 TRP A 365    12008  23924  10906   -543   -104    900       N  
ATOM   2382  CE2 TRP A 365     -38.825   8.968  43.818  1.00122.50           C  
ANISOU 2382  CE2 TRP A 365    12043  23475  11025   -317    -23   1002       C  
ATOM   2383  CE3 TRP A 365     -39.117   8.719  46.213  1.00118.15           C  
ANISOU 2383  CE3 TRP A 365    11596  22557  10737   -333     24   1045       C  
ATOM   2384  CZ2 TRP A 365     -38.018  10.098  43.989  1.00120.01           C  
ANISOU 2384  CZ2 TRP A 365    11873  22887  10840     19     67   1130       C  
ATOM   2385  CZ3 TRP A 365     -38.307   9.831  46.382  1.00117.84           C  
ANISOU 2385  CZ3 TRP A 365    11706  22245  10824     -1    108   1155       C  
ATOM   2386  CH2 TRP A 365     -37.765  10.506  45.279  1.00118.58           C  
ANISOU 2386  CH2 TRP A 365    11824  22379  10851    158    129   1198       C  
ATOM   2387  N   SER A 366     -40.912   2.947  46.289  1.00121.02           N  
ANISOU 2387  N   SER A 366    12095  23087  10802  -2199   -297    295       N  
ATOM   2388  CA  SER A 366     -41.663   1.892  46.975  1.00121.99           C  
ANISOU 2388  CA  SER A 366    12238  23243  10869  -2615   -344    231       C  
ATOM   2389  C   SER A 366     -40.865   1.293  48.143  1.00122.85           C  
ANISOU 2389  C   SER A 366    12689  22746  11242  -2628   -291    150       C  
ATOM   2390  O   SER A 366     -41.426   1.157  49.232  1.00122.65           O  
ANISOU 2390  O   SER A 366    12606  22739  11256  -2714   -279    242       O  
ATOM   2391  CB  SER A 366     -42.117   0.805  45.998  1.00128.03           C  
ANISOU 2391  CB  SER A 366    13041  24207  11399  -3089   -441     37       C  
ATOM   2392  OG  SER A 366     -42.270  -0.480  46.582  1.00137.17           O  
ANISOU 2392  OG  SER A 366    14443  25107  12568  -3519   -470   -113       O  
ATOM   2393  N   LEU A 367     -39.583   0.913  47.926  1.00116.66           N  
ANISOU 2393  N   LEU A 367    12246  21460  10617  -2539   -259    -14       N  
ATOM   2394  CA  LEU A 367     -38.736   0.298  48.967  1.00114.36           C  
ANISOU 2394  CA  LEU A 367    12289  20605  10559  -2522   -210    -93       C  
ATOM   2395  C   LEU A 367     -38.594   1.159  50.243  1.00115.62           C  
ANISOU 2395  C   LEU A 367    12373  20650  10908  -2216   -142     98       C  
ATOM   2396  O   LEU A 367     -38.711   0.574  51.319  1.00115.49           O  
ANISOU 2396  O   LEU A 367    12479  20420  10980  -2349   -130     98       O  
ATOM   2397  CB  LEU A 367     -37.341  -0.090  48.459  1.00113.04           C  
ANISOU 2397  CB  LEU A 367    12445  19998  10505  -2390   -177   -270       C  
ATOM   2398  CG  LEU A 367     -37.215  -1.508  47.901  1.00119.87           C  
ANISOU 2398  CG  LEU A 367    13619  20659  11267  -2736   -216   -518       C  
ATOM   2399  CD1 LEU A 367     -36.277  -1.527  46.768  1.00119.98           C  
ANISOU 2399  CD1 LEU A 367    13765  20570  11251  -2584   -201   -658       C  
ATOM   2400  CD2 LEU A 367     -36.782  -2.534  48.989  1.00122.06           C  
ANISOU 2400  CD2 LEU A 367    14252  20432  11691  -2847   -184   -601       C  
ATOM   2401  N   PRO A 368     -38.401   2.509  50.205  1.00109.70           N  
ANISOU 2401  N   PRO A 368    11446  20028  10208  -1832    -96    263       N  
ATOM   2402  CA  PRO A 368     -38.318   3.254  51.476  1.00106.95           C  
ANISOU 2402  CA  PRO A 368    11073  19548  10017  -1580    -33    422       C  
ATOM   2403  C   PRO A 368     -39.682   3.307  52.181  1.00109.67           C  
ANISOU 2403  C   PRO A 368    11170  20258  10241  -1702    -46    565       C  
ATOM   2404  O   PRO A 368     -39.728   3.246  53.413  1.00108.07           O  
ANISOU 2404  O   PRO A 368    11026  19885  10152  -1675    -10    626       O  
ATOM   2405  CB  PRO A 368     -37.823   4.646  51.056  1.00107.34           C  
ANISOU 2405  CB  PRO A 368    11037  19648  10100  -1183     17    545       C  
ATOM   2406  CG  PRO A 368     -37.409   4.507  49.625  1.00112.81           C  
ANISOU 2406  CG  PRO A 368    11747  20421  10694  -1223    -15    434       C  
ATOM   2407  CD  PRO A 368     -38.228   3.421  49.055  1.00111.10           C  
ANISOU 2407  CD  PRO A 368    11478  20443  10293  -1611    -93    313       C  
ATOM   2408  N   PHE A 369     -40.789   3.358  51.386  1.00106.61           N  
ANISOU 2408  N   PHE A 369    10496  20405   9605  -1851   -100    616       N  
ATOM   2409  CA  PHE A 369     -42.176   3.361  51.865  1.00107.41           C  
ANISOU 2409  CA  PHE A 369    10297  20980   9533  -1994   -120    757       C  
ATOM   2410  C   PHE A 369     -42.458   2.088  52.662  1.00111.90           C  
ANISOU 2410  C   PHE A 369    11007  21386  10123  -2411   -148    662       C  
ATOM   2411  O   PHE A 369     -43.021   2.187  53.751  1.00112.18           O  
ANISOU 2411  O   PHE A 369    10942  21509  10173  -2402   -116    788       O  
ATOM   2412  CB  PHE A 369     -43.168   3.508  50.693  1.00111.51           C  
ANISOU 2412  CB  PHE A 369    10490  22121   9758  -2115   -187    803       C  
ATOM   2413  CG  PHE A 369     -44.601   3.121  50.988  1.00115.72           C  
ANISOU 2413  CG  PHE A 369    10707  23202  10060  -2413   -234    899       C  
ATOM   2414  CD1 PHE A 369     -45.080   1.857  50.662  1.00121.06           C  
ANISOU 2414  CD1 PHE A 369    11413  23992  10591  -2965   -320    751       C  
ATOM   2415  CD2 PHE A 369     -45.481   4.031  51.562  1.00118.39           C  
ANISOU 2415  CD2 PHE A 369    10721  23962  10300  -2144   -188   1141       C  
ATOM   2416  CE1 PHE A 369     -46.403   1.498  50.932  1.00124.99           C  
ANISOU 2416  CE1 PHE A 369    11597  25039  10854  -3288   -367    848       C  
ATOM   2417  CE2 PHE A 369     -46.810   3.676  51.817  1.00124.22           C  
ANISOU 2417  CE2 PHE A 369    11123  25277  10799  -2417   -229   1243       C  
ATOM   2418  CZ  PHE A 369     -47.260   2.410  51.505  1.00124.64           C  
ANISOU 2418  CZ  PHE A 369    11185  25461  10713  -3008   -321   1099       C  
ATOM   2419  N   VAL A 370     -42.068   0.905  52.123  1.00108.47           N  
ANISOU 2419  N   VAL A 370    10829  20707   9677  -2764   -201    445       N  
ATOM   2420  CA  VAL A 370     -42.248  -0.407  52.765  1.00109.44           C  
ANISOU 2420  CA  VAL A 370    11174  20599   9807  -3190   -226    337       C  
ATOM   2421  C   VAL A 370     -41.556  -0.399  54.140  1.00110.75           C  
ANISOU 2421  C   VAL A 370    11560  20295  10227  -2994   -152    380       C  
ATOM   2422  O   VAL A 370     -42.186  -0.776  55.130  1.00111.03           O  
ANISOU 2422  O   VAL A 370    11557  20381  10246  -3177   -143    458       O  
ATOM   2423  CB  VAL A 370     -41.758  -1.575  51.864  1.00114.58           C  
ANISOU 2423  CB  VAL A 370    12150  20979  10408  -3517   -278     82       C  
ATOM   2424  CG1 VAL A 370     -41.679  -2.894  52.632  1.00115.47           C  
ANISOU 2424  CG1 VAL A 370    12614  20690  10571  -3880   -279    -31       C  
ATOM   2425  CG2 VAL A 370     -42.656  -1.729  50.641  1.00117.55           C  
ANISOU 2425  CG2 VAL A 370    12295  21879  10489  -3815   -365     38       C  
ATOM   2426  N   LEU A 371     -40.296   0.087  54.199  1.00104.49           N  
ANISOU 2426  N   LEU A 371    10962  19096   9643  -2626   -100    344       N  
ATOM   2427  CA  LEU A 371     -39.509   0.180  55.433  1.00102.05           C  
ANISOU 2427  CA  LEU A 371    10852  18359   9563  -2412    -36    381       C  
ATOM   2428  C   LEU A 371     -40.114   1.181  56.426  1.00105.52           C  
ANISOU 2428  C   LEU A 371    11042  19031  10019  -2182     12    597       C  
ATOM   2429  O   LEU A 371     -40.168   0.873  57.619  1.00104.78           O  
ANISOU 2429  O   LEU A 371    11036  18766  10010  -2222     42    646       O  
ATOM   2430  CB  LEU A 371     -38.046   0.541  55.139  1.00 99.40           C  
ANISOU 2430  CB  LEU A 371    10729  17633   9406  -2092      1    300       C  
ATOM   2431  CG  LEU A 371     -37.209  -0.552  54.478  1.00104.81           C  
ANISOU 2431  CG  LEU A 371    11738  17973  10112  -2244    -20     83       C  
ATOM   2432  CD1 LEU A 371     -35.943   0.022  53.895  1.00103.33           C  
ANISOU 2432  CD1 LEU A 371    11634  17593  10032  -1914     13     33       C  
ATOM   2433  CD2 LEU A 371     -36.879  -1.672  55.450  1.00107.35           C  
ANISOU 2433  CD2 LEU A 371    12377  17881  10531  -2403     -4     14       C  
ATOM   2434  N   THR A 372     -40.594   2.352  55.936  1.00101.65           N  
ANISOU 2434  N   THR A 372    10261  18932   9431  -1931     24    730       N  
ATOM   2435  CA  THR A 372     -41.234   3.390  56.758  1.00100.66           C  
ANISOU 2435  CA  THR A 372     9909  19057   9280  -1660     80    937       C  
ATOM   2436  C   THR A 372     -42.497   2.810  57.412  1.00106.23           C  
ANISOU 2436  C   THR A 372    10418  20110   9834  -1952     64   1020       C  
ATOM   2437  O   THR A 372     -42.668   2.945  58.627  1.00105.02           O  
ANISOU 2437  O   THR A 372    10269  19890   9745  -1868    114   1116       O  
ATOM   2438  CB  THR A 372     -41.538   4.645  55.917  1.00107.10           C  
ANISOU 2438  CB  THR A 372    10490  20225   9980  -1342     97   1056       C  
ATOM   2439  OG1 THR A 372     -40.333   5.104  55.306  1.00103.98           O  
ANISOU 2439  OG1 THR A 372    10292  19500   9718  -1129    112    978       O  
ATOM   2440  CG2 THR A 372     -42.142   5.777  56.740  1.00105.36           C  
ANISOU 2440  CG2 THR A 372    10091  20221   9720   -998    171   1267       C  
ATOM   2441  N   VAL A 373     -43.346   2.132  56.606  1.00105.04           N  
ANISOU 2441  N   VAL A 373    10102  20336   9472  -2321     -9    979       N  
ATOM   2442  CA  VAL A 373     -44.590   1.485  57.036  1.00107.22           C  
ANISOU 2442  CA  VAL A 373    10164  21017   9559  -2692    -39   1050       C  
ATOM   2443  C   VAL A 373     -44.266   0.377  58.061  1.00110.78           C  
ANISOU 2443  C   VAL A 373    10918  21033  10139  -2982    -31    970       C  
ATOM   2444  O   VAL A 373     -44.898   0.345  59.119  1.00110.60           O  
ANISOU 2444  O   VAL A 373    10779  21160  10085  -3032      5   1098       O  
ATOM   2445  CB  VAL A 373     -45.399   0.960  55.816  1.00113.58           C  
ANISOU 2445  CB  VAL A 373    10767  22286  10101  -3070   -132    992       C  
ATOM   2446  CG1 VAL A 373     -46.474  -0.047  56.220  1.00116.64           C  
ANISOU 2446  CG1 VAL A 373    11032  22983  10303  -3605   -178   1011       C  
ATOM   2447  CG2 VAL A 373     -46.018   2.118  55.044  1.00113.93           C  
ANISOU 2447  CG2 VAL A 373    10426  22894   9969  -2760   -131   1141       C  
ATOM   2448  N   ALA A 374     -43.253  -0.481  57.767  1.00106.64           N  
ANISOU 2448  N   ALA A 374    10791  19976   9753  -3128    -53    771       N  
ATOM   2449  CA  ALA A 374     -42.813  -1.582  58.636  1.00106.48           C  
ANISOU 2449  CA  ALA A 374    11124  19482   9853  -3366    -42    687       C  
ATOM   2450  C   ALA A 374     -42.384  -1.090  60.028  1.00108.31           C  
ANISOU 2450  C   ALA A 374    11416  19467  10268  -3052     36    803       C  
ATOM   2451  O   ALA A 374     -42.641  -1.788  61.009  1.00108.56           O  
ANISOU 2451  O   ALA A 374    11557  19377  10313  -3267     52    838       O  
ATOM   2452  CB  ALA A 374     -41.676  -2.349  57.984  1.00106.49           C  
ANISOU 2452  CB  ALA A 374    11533  18966   9964  -3424    -62    468       C  
ATOM   2453  N   ILE A 375     -41.758   0.108  60.117  1.00102.43           N  
ANISOU 2453  N   ILE A 375    10613  18658   9647  -2568     83    865       N  
ATOM   2454  CA  ILE A 375     -41.328   0.710  61.386  1.00100.21           C  
ANISOU 2454  CA  ILE A 375    10389  18165   9519  -2255    153    967       C  
ATOM   2455  C   ILE A 375     -42.555   1.214  62.156  1.00105.76           C  
ANISOU 2455  C   ILE A 375    10772  19332  10082  -2230    189   1161       C  
ATOM   2456  O   ILE A 375     -42.696   0.907  63.340  1.00104.69           O  
ANISOU 2456  O   ILE A 375    10697  19094   9987  -2282    225   1225       O  
ATOM   2457  CB  ILE A 375     -40.281   1.841  61.176  1.00100.35           C  
ANISOU 2457  CB  ILE A 375    10470  17975   9686  -1798    189    963       C  
ATOM   2458  CG1 ILE A 375     -38.953   1.271  60.652  1.00 99.23           C  
ANISOU 2458  CG1 ILE A 375    10648  17365   9690  -1803    167    784       C  
ATOM   2459  CG2 ILE A 375     -40.060   2.644  62.476  1.00 99.77           C  
ANISOU 2459  CG2 ILE A 375    10408  17785   9716  -1488    259   1083       C  
ATOM   2460  CD1 ILE A 375     -38.124   2.237  59.881  1.00102.83           C  
ANISOU 2460  CD1 ILE A 375    11100  17761  10210  -1487    179    761       C  
ATOM   2461  N   LEU A 376     -43.433   1.984  61.481  1.00104.38           N  
ANISOU 2461  N   LEU A 376    10251  19683   9725  -2126    185   1261       N  
ATOM   2462  CA  LEU A 376     -44.645   2.549  62.075  1.00106.03           C  
ANISOU 2462  CA  LEU A 376    10112  20416   9760  -2040    227   1459       C  
ATOM   2463  C   LEU A 376     -45.609   1.450  62.545  1.00114.83           C  
ANISOU 2463  C   LEU A 376    11118  21784  10727  -2525    198   1492       C  
ATOM   2464  O   LEU A 376     -46.365   1.685  63.488  1.00116.52           O  
ANISOU 2464  O   LEU A 376    11136  22284  10853  -2475    250   1648       O  
ATOM   2465  CB  LEU A 376     -45.345   3.508  61.099  1.00106.96           C  
ANISOU 2465  CB  LEU A 376     9892  21059   9688  -1820    223   1558       C  
ATOM   2466  CG  LEU A 376     -44.564   4.775  60.721  1.00108.93           C  
ANISOU 2466  CG  LEU A 376    10228  21114  10044  -1316    269   1574       C  
ATOM   2467  CD1 LEU A 376     -45.037   5.325  59.400  1.00110.63           C  
ANISOU 2467  CD1 LEU A 376    10204  21747  10082  -1221    237   1614       C  
ATOM   2468  CD2 LEU A 376     -44.648   5.840  61.805  1.00109.44           C  
ANISOU 2468  CD2 LEU A 376    10274  21168  10142   -888    369   1722       C  
ATOM   2469  N   ALA A 377     -45.545   0.247  61.932  1.00113.49           N  
ANISOU 2469  N   ALA A 377    11108  21486  10526  -2999    122   1345       N  
ATOM   2470  CA  ALA A 377     -46.360  -0.912  62.317  1.00116.92           C  
ANISOU 2470  CA  ALA A 377    11521  22084  10820  -3541     90   1356       C  
ATOM   2471  C   ALA A 377     -45.849  -1.520  63.636  1.00120.88           C  
ANISOU 2471  C   ALA A 377    12331  22110  11488  -3598    137   1356       C  
ATOM   2472  O   ALA A 377     -46.651  -1.758  64.548  1.00121.97           O  
ANISOU 2472  O   ALA A 377    12321  22499  11523  -3770    168   1490       O  
ATOM   2473  CB  ALA A 377     -46.353  -1.958  61.212  1.00119.64           C  
ANISOU 2473  CB  ALA A 377    12018  22365  11075  -4013     -1   1178       C  
ATOM   2474  N   VAL A 378     -44.511  -1.729  63.752  1.00115.34           N  
ANISOU 2474  N   VAL A 378    12037  20758  11030  -3427    147   1222       N  
ATOM   2475  CA  VAL A 378     -43.877  -2.273  64.966  1.00114.13           C  
ANISOU 2475  CA  VAL A 378    12197  20128  11040  -3422    190   1222       C  
ATOM   2476  C   VAL A 378     -43.744  -1.161  66.033  1.00115.92           C  
ANISOU 2476  C   VAL A 378    12293  20398  11352  -2959    268   1366       C  
ATOM   2477  O   VAL A 378     -43.414  -1.456  67.185  1.00114.89           O  
ANISOU 2477  O   VAL A 378    12340  19994  11320  -2931    309   1406       O  
ATOM   2478  CB  VAL A 378     -42.518  -2.996  64.708  1.00116.39           C  
ANISOU 2478  CB  VAL A 378    12954  19751  11518  -3410    173   1035       C  
ATOM   2479  CG1 VAL A 378     -42.702  -4.252  63.860  1.00119.01           C  
ANISOU 2479  CG1 VAL A 378    13496  19977  11744  -3898    110    889       C  
ATOM   2480  CG2 VAL A 378     -41.471  -2.068  64.096  1.00113.05           C  
ANISOU 2480  CG2 VAL A 378    12562  19150  11240  -2960    179    964       C  
ATOM   2481  N   ALA A 379     -44.034   0.104  65.636  1.00111.70           N  
ANISOU 2481  N   ALA A 379    11469  20211  10762  -2603    290   1444       N  
ATOM   2482  CA  ALA A 379     -44.002   1.334  66.432  1.00109.97           C  
ANISOU 2482  CA  ALA A 379    11129  20073  10581  -2136    368   1571       C  
ATOM   2483  C   ALA A 379     -42.671   1.483  67.170  1.00111.19           C  
ANISOU 2483  C   ALA A 379    11625  19645  10977  -1886    396   1503       C  
ATOM   2484  O   ALA A 379     -42.577   1.215  68.369  1.00110.22           O  
ANISOU 2484  O   ALA A 379    11609  19363  10906  -1891    434   1556       O  
ATOM   2485  CB  ALA A 379     -45.176   1.381  67.402  1.00112.92           C  
ANISOU 2485  CB  ALA A 379    11236  20880  10787  -2203    419   1750       C  
ATOM   2486  N   GLN A 380     -41.628   1.871  66.425  1.00106.75           N  
ANISOU 2486  N   GLN A 380    11224  18790  10547  -1687    374   1389       N  
ATOM   2487  CA  GLN A 380     -40.283   2.043  66.974  1.00104.22           C  
ANISOU 2487  CA  GLN A 380    11197  17967  10436  -1461    391   1319       C  
ATOM   2488  C   GLN A 380     -39.738   3.454  66.696  1.00106.33           C  
ANISOU 2488  C   GLN A 380    11429  18215  10756  -1043    422   1336       C  
ATOM   2489  O   GLN A 380     -38.520   3.649  66.643  1.00104.89           O  
ANISOU 2489  O   GLN A 380    11461  17668  10726   -894    415   1250       O  
ATOM   2490  CB  GLN A 380     -39.326   0.958  66.435  1.00105.18           C  
ANISOU 2490  CB  GLN A 380    11612  17682  10671  -1662    338   1154       C  
ATOM   2491  CG  GLN A 380     -39.629  -0.458  66.943  1.00117.89           C  
ANISOU 2491  CG  GLN A 380    13384  19157  12253  -2046    321   1135       C  
ATOM   2492  CD  GLN A 380     -39.536  -0.630  68.445  1.00131.37           C  
ANISOU 2492  CD  GLN A 380    15190  20707  14016  -1999    366   1226       C  
ATOM   2493  OE1 GLN A 380     -40.391  -1.259  69.072  1.00126.70           O  
ANISOU 2493  OE1 GLN A 380    14552  20264  13325  -2265    378   1309       O  
ATOM   2494  NE2 GLN A 380     -38.496  -0.087  69.056  1.00121.83           N  
ANISOU 2494  NE2 GLN A 380    14119  19217  12955  -1680    390   1218       N  
ATOM   2495  N   VAL A 381     -40.643   4.444  66.563  1.00102.54           N  
ANISOU 2495  N   VAL A 381    10690  18137  10133   -850    462   1458       N  
ATOM   2496  CA  VAL A 381     -40.266   5.843  66.351  1.00100.59           C  
ANISOU 2496  CA  VAL A 381    10445  17871   9905   -451    505   1495       C  
ATOM   2497  C   VAL A 381     -39.957   6.450  67.730  1.00102.64           C  
ANISOU 2497  C   VAL A 381    10829  17945  10225   -215    569   1554       C  
ATOM   2498  O   VAL A 381     -40.825   6.480  68.605  1.00103.91           O  
ANISOU 2498  O   VAL A 381    10862  18337  10281   -194    616   1663       O  
ATOM   2499  CB  VAL A 381     -41.338   6.647  65.569  1.00106.08           C  
ANISOU 2499  CB  VAL A 381    10848  19057  10403   -300    528   1607       C  
ATOM   2500  CG1 VAL A 381     -40.881   8.082  65.322  1.00104.73           C  
ANISOU 2500  CG1 VAL A 381    10751  18793  10248    113    580   1646       C  
ATOM   2501  CG2 VAL A 381     -41.686   5.964  64.248  1.00107.25           C  
ANISOU 2501  CG2 VAL A 381    10860  19422  10467   -577    454   1544       C  
ATOM   2502  N   ASP A 382     -38.707   6.890  67.926  1.00 95.70           N  
ANISOU 2502  N   ASP A 382    10193  16669   9499    -60    569   1479       N  
ATOM   2503  CA  ASP A 382     -38.234   7.457  69.189  1.00 93.74           C  
ANISOU 2503  CA  ASP A 382    10102  16207   9308    134    617   1507       C  
ATOM   2504  C   ASP A 382     -37.572   8.820  68.950  1.00 96.23           C  
ANISOU 2504  C   ASP A 382    10542  16374   9649    438    650   1502       C  
ATOM   2505  O   ASP A 382     -36.986   9.030  67.896  1.00 95.34           O  
ANISOU 2505  O   ASP A 382    10466  16177   9582    440    618   1440       O  
ATOM   2506  CB  ASP A 382     -37.254   6.486  69.882  1.00 94.02           C  
ANISOU 2506  CB  ASP A 382    10343  15884   9494    -40    575   1419       C  
ATOM   2507  CG  ASP A 382     -37.668   5.016  69.903  1.00100.45           C  
ANISOU 2507  CG  ASP A 382    11129  16736  10303   -379    536   1399       C  
ATOM   2508  OD1 ASP A 382     -38.838   4.728  70.249  1.00101.44           O  
ANISOU 2508  OD1 ASP A 382    11079  17164  10299   -494    560   1493       O  
ATOM   2509  OD2 ASP A 382     -36.809   4.153  69.614  1.00104.70           O  
ANISOU 2509  OD2 ASP A 382    11834  16998  10951   -527    486   1294       O  
ATOM   2510  N   GLY A 383     -37.671   9.725  69.918  1.00 92.77           N  
ANISOU 2510  N   GLY A 383    10186  15897   9165    677    717   1566       N  
ATOM   2511  CA  GLY A 383     -37.113  11.070  69.818  1.00 92.03           C  
ANISOU 2511  CA  GLY A 383    10265  15635   9068    946    759   1566       C  
ATOM   2512  C   GLY A 383     -35.904  11.312  70.698  1.00 94.01           C  
ANISOU 2512  C   GLY A 383    10777  15510   9432    956    748   1492       C  
ATOM   2513  O   GLY A 383     -35.823  10.782  71.812  1.00 93.51           O  
ANISOU 2513  O   GLY A 383    10756  15376   9399    884    745   1487       O  
ATOM   2514  N   ASP A 384     -34.965  12.140  70.203  1.00 88.94           N  
ANISOU 2514  N   ASP A 384    10306  14649   8837   1034    742   1443       N  
ATOM   2515  CA  ASP A 384     -33.736  12.507  70.907  1.00 87.69           C  
ANISOU 2515  CA  ASP A 384    10385  14172   8762   1021    724   1372       C  
ATOM   2516  C   ASP A 384     -33.563  14.025  70.888  1.00 92.17           C  
ANISOU 2516  C   ASP A 384    11158  14615   9247   1238    786   1398       C  
ATOM   2517  O   ASP A 384     -33.738  14.651  69.841  1.00 92.12           O  
ANISOU 2517  O   ASP A 384    11145  14664   9193   1332    808   1431       O  
ATOM   2518  CB  ASP A 384     -32.530  11.794  70.270  1.00 88.37           C  
ANISOU 2518  CB  ASP A 384    10483  14104   8988    815    640   1271       C  
ATOM   2519  CG  ASP A 384     -31.154  12.081  70.855  1.00 97.01           C  
ANISOU 2519  CG  ASP A 384    11767  14937  10155    768    607   1202       C  
ATOM   2520  OD1 ASP A 384     -31.077  12.485  72.037  1.00 97.41           O  
ANISOU 2520  OD1 ASP A 384    11945  14898  10170    829    629   1213       O  
ATOM   2521  OD2 ASP A 384     -30.153  11.842  70.149  1.00103.37           O  
ANISOU 2521  OD2 ASP A 384    12578  15659  11038    662    556   1138       O  
ATOM   2522  N   SER A 385     -33.225  14.608  72.052  1.00 89.06           N  
ANISOU 2522  N   SER A 385    10972  14045   8823   1311    815   1383       N  
ATOM   2523  CA  SER A 385     -33.062  16.051  72.236  1.00 89.82           C  
ANISOU 2523  CA  SER A 385    11341  13967   8819   1501    881   1397       C  
ATOM   2524  C   SER A 385     -31.779  16.612  71.615  1.00 94.34           C  
ANISOU 2524  C   SER A 385    12091  14300   9453   1376    839   1329       C  
ATOM   2525  O   SER A 385     -31.804  17.759  71.167  1.00 95.13           O  
ANISOU 2525  O   SER A 385    12384  14294   9465   1513    896   1362       O  
ATOM   2526  CB  SER A 385     -33.094  16.404  73.715  1.00 93.08           C  
ANISOU 2526  CB  SER A 385    11932  14269   9163   1582    920   1384       C  
ATOM   2527  OG  SER A 385     -32.051  15.725  74.390  1.00 98.81           O  
ANISOU 2527  OG  SER A 385    12683  14862   9999   1352    837   1300       O  
ATOM   2528  N   VAL A 386     -30.664  15.835  71.600  1.00 90.40           N  
ANISOU 2528  N   VAL A 386    11538  13725   9086   1128    748   1246       N  
ATOM   2529  CA  VAL A 386     -29.388  16.304  71.033  1.00 90.37           C  
ANISOU 2529  CA  VAL A 386    11658  13554   9126    985    705   1190       C  
ATOM   2530  C   VAL A 386     -29.475  16.360  69.493  1.00 95.31           C  
ANISOU 2530  C   VAL A 386    12172  14275   9766    988    706   1218       C  
ATOM   2531  O   VAL A 386     -29.071  17.365  68.901  1.00 95.28           O  
ANISOU 2531  O   VAL A 386    12334  14155   9711   1005    732   1234       O  
ATOM   2532  CB  VAL A 386     -28.114  15.547  71.519  1.00 93.29           C  
ANISOU 2532  CB  VAL A 386    11991  13858   9597    760    614   1107       C  
ATOM   2533  CG1 VAL A 386     -27.890  15.738  73.015  1.00 93.54           C  
ANISOU 2533  CG1 VAL A 386    12172  13784   9584    752    612   1081       C  
ATOM   2534  CG2 VAL A 386     -28.130  14.064  71.161  1.00 92.06           C  
ANISOU 2534  CG2 VAL A 386    11580  13847   9552    672    558   1087       C  
ATOM   2535  N   SER A 387     -30.029  15.303  68.860  1.00 92.26           N  
ANISOU 2535  N   SER A 387    11525  14096   9433    961    679   1226       N  
ATOM   2536  CA  SER A 387     -30.205  15.230  67.410  1.00 92.25           C  
ANISOU 2536  CA  SER A 387    11395  14226   9431    959    674   1246       C  
ATOM   2537  C   SER A 387     -31.340  16.156  66.985  1.00 99.06           C  
ANISOU 2537  C   SER A 387    12285  15197  10157   1199    756   1353       C  
ATOM   2538  O   SER A 387     -31.279  16.731  65.901  1.00 99.65           O  
ANISOU 2538  O   SER A 387    12380  15294  10189   1247    773   1390       O  
ATOM   2539  CB  SER A 387     -30.474  13.796  66.960  1.00 94.22           C  
ANISOU 2539  CB  SER A 387    11395  14650   9754    836    618   1208       C  
ATOM   2540  OG  SER A 387     -31.754  13.334  67.358  1.00102.83           O  
ANISOU 2540  OG  SER A 387    12353  15928  10790    902    644   1262       O  
ATOM   2541  N   GLY A 388     -32.344  16.293  67.855  1.00 96.81           N  
ANISOU 2541  N   GLY A 388    11999  14994   9790   1363    810   1411       N  
ATOM   2542  CA  GLY A 388     -33.511  17.143  67.645  1.00 98.64           C  
ANISOU 2542  CA  GLY A 388    12247  15370   9864   1653    900   1528       C  
ATOM   2543  C   GLY A 388     -34.510  16.609  66.637  1.00103.71           C  
ANISOU 2543  C   GLY A 388    12588  16364  10452   1694    894   1594       C  
ATOM   2544  O   GLY A 388     -35.332  17.374  66.125  1.00104.97           O  
ANISOU 2544  O   GLY A 388    12737  16677  10469   1944    962   1703       O  
ATOM   2545  N   ILE A 389     -34.444  15.296  66.337  1.00 99.56           N  
ANISOU 2545  N   ILE A 389    11831  15973  10023   1451    814   1530       N  
ATOM   2546  CA  ILE A 389     -35.336  14.628  65.380  1.00100.19           C  
ANISOU 2546  CA  ILE A 389    11624  16397  10047   1409    789   1568       C  
ATOM   2547  C   ILE A 389     -35.809  13.265  65.924  1.00104.62           C  
ANISOU 2547  C   ILE A 389    11991  17110  10650   1201    742   1530       C  
ATOM   2548  O   ILE A 389     -35.137  12.667  66.770  1.00103.70           O  
ANISOU 2548  O   ILE A 389    11967  16788  10648   1055    709   1454       O  
ATOM   2549  CB  ILE A 389     -34.685  14.464  63.966  1.00102.53           C  
ANISOU 2549  CB  ILE A 389    11879  16686  10391   1284    737   1516       C  
ATOM   2550  CG1 ILE A 389     -33.391  13.615  63.996  1.00101.14           C  
ANISOU 2550  CG1 ILE A 389    11764  16280  10384   1023    662   1376       C  
ATOM   2551  CG2 ILE A 389     -34.456  15.807  63.264  1.00103.94           C  
ANISOU 2551  CG2 ILE A 389    12222  16780  10492   1487    792   1588       C  
ATOM   2552  CD1 ILE A 389     -33.538  12.256  63.343  1.00105.99           C  
ANISOU 2552  CD1 ILE A 389    12184  17048  11040    803    593   1302       C  
ATOM   2553  N   CYS A 390     -36.949  12.774  65.404  1.00101.87           N  
ANISOU 2553  N   CYS A 390    11379  17132  10194   1173    736   1591       N  
ATOM   2554  CA  CYS A 390     -37.506  11.465  65.734  1.00101.71           C  
ANISOU 2554  CA  CYS A 390    11178  17285  10184    925    691   1565       C  
ATOM   2555  C   CYS A 390     -36.977  10.437  64.735  1.00103.14           C  
ANISOU 2555  C   CYS A 390    11313  17426  10450    644    605   1450       C  
ATOM   2556  O   CYS A 390     -37.018  10.683  63.531  1.00103.38           O  
ANISOU 2556  O   CYS A 390    11270  17581  10429    664    589   1449       O  
ATOM   2557  CB  CYS A 390     -39.028  11.508  65.736  1.00104.68           C  
ANISOU 2557  CB  CYS A 390    11286  18119  10367   1012    730   1695       C  
ATOM   2558  SG  CYS A 390     -39.756  12.199  67.246  1.00109.80           S  
ANISOU 2558  SG  CYS A 390    11963  18845  10910   1285    832   1813       S  
ATOM   2559  N   PHE A 391     -36.462   9.302  65.227  1.00 97.52           N  
ANISOU 2559  N   PHE A 391    10668  16532   9854    405    556   1355       N  
ATOM   2560  CA  PHE A 391     -35.877   8.263  64.385  1.00 96.45           C  
ANISOU 2560  CA  PHE A 391    10550  16304   9793    164    486   1232       C  
ATOM   2561  C   PHE A 391     -36.133   6.852  64.937  1.00 99.74           C  
ANISOU 2561  C   PHE A 391    10967  16692  10239   -109    450   1183       C  
ATOM   2562  O   PHE A 391     -36.526   6.688  66.088  1.00 98.78           O  
ANISOU 2562  O   PHE A 391    10852  16571  10111   -116    476   1241       O  
ATOM   2563  CB  PHE A 391     -34.368   8.517  64.244  1.00 96.76           C  
ANISOU 2563  CB  PHE A 391    10792  16002   9969    216    472   1143       C  
ATOM   2564  CG  PHE A 391     -33.745   8.027  62.962  1.00 98.47           C  
ANISOU 2564  CG  PHE A 391    11011  16189  10215    104    425   1041       C  
ATOM   2565  CD1 PHE A 391     -33.969   8.693  61.760  1.00102.20           C  
ANISOU 2565  CD1 PHE A 391    11389  16841  10603    184    430   1069       C  
ATOM   2566  CD2 PHE A 391     -32.889   6.933  62.961  1.00100.53           C  
ANISOU 2566  CD2 PHE A 391    11384  16237  10575    -49    383    923       C  
ATOM   2567  CE1 PHE A 391     -33.380   8.247  60.574  1.00103.09           C  
ANISOU 2567  CE1 PHE A 391    11503  16937  10727     87    392    971       C  
ATOM   2568  CE2 PHE A 391     -32.293   6.494  61.776  1.00103.58           C  
ANISOU 2568  CE2 PHE A 391    11786  16600  10971   -120    351    823       C  
ATOM   2569  CZ  PHE A 391     -32.543   7.152  60.590  1.00102.00           C  
ANISOU 2569  CZ  PHE A 391    11477  16592  10685    -62    354    844       C  
ATOM   2570  N   VAL A 392     -35.909   5.840  64.092  1.00 97.44           N  
ANISOU 2570  N   VAL A 392    10694  16364   9965   -334    395   1077       N  
ATOM   2571  CA  VAL A 392     -36.104   4.423  64.401  1.00 98.73           C  
ANISOU 2571  CA  VAL A 392    10919  16453  10141   -623    361   1017       C  
ATOM   2572  C   VAL A 392     -34.920   3.856  65.213  1.00103.05           C  
ANISOU 2572  C   VAL A 392    11715  16598  10841   -613    356    949       C  
ATOM   2573  O   VAL A 392     -33.758   4.139  64.920  1.00101.33           O  
ANISOU 2573  O   VAL A 392    11612  16172  10716   -481    349    884       O  
ATOM   2574  CB  VAL A 392     -36.370   3.587  63.105  1.00103.99           C  
ANISOU 2574  CB  VAL A 392    11548  17229  10734   -867    308    919       C  
ATOM   2575  CG1 VAL A 392     -35.336   3.861  62.010  1.00102.84           C  
ANISOU 2575  CG1 VAL A 392    11484  16946  10646   -758    290    819       C  
ATOM   2576  CG2 VAL A 392     -36.481   2.088  63.390  1.00105.03           C  
ANISOU 2576  CG2 VAL A 392    11826  17208  10871  -1185    277    841       C  
ATOM   2577  N   GLY A 393     -35.261   3.052  66.218  1.00101.49           N  
ANISOU 2577  N   GLY A 393    11582  16332  10649   -755    360    978       N  
ATOM   2578  CA  GLY A 393     -34.324   2.315  67.055  1.00101.05           C  
ANISOU 2578  CA  GLY A 393    11756  15932  10706   -764    355    934       C  
ATOM   2579  C   GLY A 393     -33.419   3.080  67.994  1.00103.82           C  
ANISOU 2579  C   GLY A 393    12184  16117  11148   -520    377    968       C  
ATOM   2580  O   GLY A 393     -32.303   2.620  68.260  1.00103.23           O  
ANISOU 2580  O   GLY A 393    12278  15778  11165   -474    360    909       O  
ATOM   2581  N   TYR A 394     -33.885   4.227  68.535  1.00 99.50           N  
ANISOU 2581  N   TYR A 394    11523  15727  10556   -357    416   1063       N  
ATOM   2582  CA  TYR A 394     -33.090   4.975  69.513  1.00 97.99           C  
ANISOU 2582  CA  TYR A 394    11429  15378  10425   -162    435   1088       C  
ATOM   2583  C   TYR A 394     -33.094   4.209  70.844  1.00104.96           C  
ANISOU 2583  C   TYR A 394    12409  16142  11330   -230    439   1126       C  
ATOM   2584  O   TYR A 394     -32.037   4.026  71.455  1.00104.05           O  
ANISOU 2584  O   TYR A 394    12435  15806  11292   -167    422   1096       O  
ATOM   2585  CB  TYR A 394     -33.610   6.414  69.703  1.00 98.03           C  
ANISOU 2585  CB  TYR A 394    11346  15548  10355     40    484   1169       C  
ATOM   2586  CG  TYR A 394     -33.093   7.454  68.727  1.00 97.88           C  
ANISOU 2586  CG  TYR A 394    11328  15524  10339    178    487   1141       C  
ATOM   2587  CD1 TYR A 394     -31.796   7.389  68.226  1.00 98.62           C  
ANISOU 2587  CD1 TYR A 394    11525  15423  10525    173    449   1054       C  
ATOM   2588  CD2 TYR A 394     -33.856   8.571  68.402  1.00 98.86           C  
ANISOU 2588  CD2 TYR A 394    11364  15841  10359    339    535   1218       C  
ATOM   2589  CE1 TYR A 394     -31.306   8.360  67.350  1.00 98.49           C  
ANISOU 2589  CE1 TYR A 394    11513  15408  10500    274    455   1041       C  
ATOM   2590  CE2 TYR A 394     -33.374   9.555  67.538  1.00 99.09           C  
ANISOU 2590  CE2 TYR A 394    11430  15838  10381    464    544   1208       C  
ATOM   2591  CZ  TYR A 394     -32.098   9.445  67.012  1.00104.11           C  
ANISOU 2591  CZ  TYR A 394    12164  16280  11114    411    502   1119       C  
ATOM   2592  OH  TYR A 394     -31.621  10.415  66.162  1.00103.06           O  
ANISOU 2592  OH  TYR A 394    12069  16126  10964    506    515   1120       O  
ATOM   2593  N   LYS A 395     -34.287   3.729  71.260  1.00104.69           N  
ANISOU 2593  N   LYS A 395    12284  16283  11209   -369    462   1201       N  
ATOM   2594  CA  LYS A 395     -34.493   2.947  72.479  1.00105.86           C  
ANISOU 2594  CA  LYS A 395    12512  16356  11353   -468    474   1258       C  
ATOM   2595  C   LYS A 395     -34.099   1.489  72.208  1.00112.13           C  
ANISOU 2595  C   LYS A 395    13472  16934  12199   -679    436   1193       C  
ATOM   2596  O   LYS A 395     -33.159   0.992  72.833  1.00111.49           O  
ANISOU 2596  O   LYS A 395    13572  16595  12192   -626    423   1174       O  
ATOM   2597  CB  LYS A 395     -35.954   3.067  72.961  1.00109.60           C  
ANISOU 2597  CB  LYS A 395    12804  17149  11691   -544    520   1375       C  
ATOM   2598  CG  LYS A 395     -36.237   2.412  74.312  1.00124.98           C  
ANISOU 2598  CG  LYS A 395    14817  19056  13614   -635    545   1457       C  
ATOM   2599  CD  LYS A 395     -37.703   2.563  74.707  1.00136.75           C  
ANISOU 2599  CD  LYS A 395    16087  20925  14947   -710    597   1581       C  
ATOM   2600  CE  LYS A 395     -38.122   1.623  75.814  1.00146.48           C  
ANISOU 2600  CE  LYS A 395    17374  22148  16136   -902    617   1667       C  
ATOM   2601  NZ  LYS A 395     -38.315   0.234  75.310  1.00156.30           N  
ANISOU 2601  NZ  LYS A 395    18708  23298  17379  -1262    578   1637       N  
ATOM   2602  N   ASN A 396     -34.792   0.819  71.264  1.00111.07           N  
ANISOU 2602  N   ASN A 396    13290  16904  12006   -908    420   1159       N  
ATOM   2603  CA  ASN A 396     -34.512  -0.572  70.904  1.00112.74           C  
ANISOU 2603  CA  ASN A 396    13710  16885  12239  -1124    392   1084       C  
ATOM   2604  C   ASN A 396     -33.564  -0.596  69.705  1.00116.59           C  
ANISOU 2604  C   ASN A 396    14277  17231  12789  -1039    359    951       C  
ATOM   2605  O   ASN A 396     -34.008  -0.597  68.554  1.00116.89           O  
ANISOU 2605  O   ASN A 396    14227  17414  12771  -1152    341    893       O  
ATOM   2606  CB  ASN A 396     -35.810  -1.350  70.629  1.00117.69           C  
ANISOU 2606  CB  ASN A 396    14274  17701  12742  -1474    390   1115       C  
ATOM   2607  CG  ASN A 396     -36.819  -1.299  71.758  1.00148.35           C  
ANISOU 2607  CG  ASN A 396    18034  21795  16537  -1568    429   1260       C  
ATOM   2608  OD1 ASN A 396     -37.802  -0.550  71.717  1.00142.83           O  
ANISOU 2608  OD1 ASN A 396    17061  21472  15734  -1556    451   1340       O  
ATOM   2609  ND2 ASN A 396     -36.603  -2.097  72.794  1.00143.13           N  
ANISOU 2609  ND2 ASN A 396    17569  20913  15900  -1645    444   1308       N  
ATOM   2610  N   TYR A 397     -32.244  -0.600  69.994  1.00112.31           N  
ANISOU 2610  N   TYR A 397    13884  16439  12347   -833    353    911       N  
ATOM   2611  CA  TYR A 397     -31.150  -0.576  69.018  1.00111.44           C  
ANISOU 2611  CA  TYR A 397    13842  16208  12294   -703    331    799       C  
ATOM   2612  C   TYR A 397     -31.160  -1.783  68.064  1.00115.83           C  
ANISOU 2612  C   TYR A 397    14571  16622  12817   -877    317    691       C  
ATOM   2613  O   TYR A 397     -30.574  -1.698  66.980  1.00115.73           O  
ANISOU 2613  O   TYR A 397    14563  16596  12813   -804    304    592       O  
ATOM   2614  CB  TYR A 397     -29.785  -0.462  69.724  1.00112.14           C  
ANISOU 2614  CB  TYR A 397    14035  16107  12465   -467    329    803       C  
ATOM   2615  CG  TYR A 397     -29.291  -1.713  70.424  1.00115.70           C  
ANISOU 2615  CG  TYR A 397    14735  16290  12935   -473    333    808       C  
ATOM   2616  CD1 TYR A 397     -28.296  -2.505  69.858  1.00118.36           C  
ANISOU 2616  CD1 TYR A 397    15254  16425  13294   -376    328    721       C  
ATOM   2617  CD2 TYR A 397     -29.768  -2.065  71.684  1.00117.45           C  
ANISOU 2617  CD2 TYR A 397    15018  16466  13140   -539    350    911       C  
ATOM   2618  CE1 TYR A 397     -27.822  -3.645  70.505  1.00120.79           C  
ANISOU 2618  CE1 TYR A 397    15821  16471  13602   -332    342    739       C  
ATOM   2619  CE2 TYR A 397     -29.299  -3.201  72.343  1.00120.01           C  
ANISOU 2619  CE2 TYR A 397    15595  16531  13471   -525    358    934       C  
ATOM   2620  CZ  TYR A 397     -28.326  -3.989  71.747  1.00129.83           C  
ANISOU 2620  CZ  TYR A 397    17039  17558  14734   -411    355    849       C  
ATOM   2621  OH  TYR A 397     -27.857  -5.112  72.383  1.00135.01           O  
ANISOU 2621  OH  TYR A 397    17973  17943  15381   -354    373    883       O  
ATOM   2622  N   ARG A 398     -31.822  -2.890  68.453  1.00112.75           N  
ANISOU 2622  N   ARG A 398    14341  16123  12376  -1115    324    707       N  
ATOM   2623  CA  ARG A 398     -31.935  -4.089  67.623  1.00114.00           C  
ANISOU 2623  CA  ARG A 398    14725  16111  12479  -1324    315    598       C  
ATOM   2624  C   ARG A 398     -32.811  -3.805  66.392  1.00116.67           C  
ANISOU 2624  C   ARG A 398    14885  16722  12724  -1520    289    537       C  
ATOM   2625  O   ARG A 398     -32.618  -4.440  65.356  1.00117.44           O  
ANISOU 2625  O   ARG A 398    15127  16716  12778  -1613    275    409       O  
ATOM   2626  CB  ARG A 398     -32.472  -5.274  68.436  1.00117.00           C  
ANISOU 2626  CB  ARG A 398    15346  16296  12812  -1566    331    647       C  
ATOM   2627  CG  ARG A 398     -31.460  -5.808  69.458  1.00128.20           C  
ANISOU 2627  CG  ARG A 398    17011  17396  14305  -1353    356    690       C  
ATOM   2628  CD  ARG A 398     -31.938  -7.064  70.144  1.00143.10           C  
ANISOU 2628  CD  ARG A 398    19197  19043  16134  -1594    379    738       C  
ATOM   2629  NE  ARG A 398     -31.669  -8.259  69.342  1.00155.59           N  
ANISOU 2629  NE  ARG A 398    21140  20311  17664  -1707    386    612       N  
ATOM   2630  CZ  ARG A 398     -31.215  -9.401  69.841  1.00172.44           C  
ANISOU 2630  CZ  ARG A 398    23676  22059  19786  -1686    419    622       C  
ATOM   2631  NH1 ARG A 398     -30.972  -9.515  71.140  1.00160.68           N  
ANISOU 2631  NH1 ARG A 398    22248  20472  18332  -1565    442    760       N  
ATOM   2632  NH2 ARG A 398     -30.998 -10.439  69.044  1.00161.43           N  
ANISOU 2632  NH2 ARG A 398    22644  20364  18327  -1774    433    495       N  
ATOM   2633  N   TYR A 399     -33.731  -2.817  66.497  1.00111.20           N  
ANISOU 2633  N   TYR A 399    13878  16388  11986  -1550    287    631       N  
ATOM   2634  CA  TYR A 399     -34.588  -2.365  65.399  1.00111.01           C  
ANISOU 2634  CA  TYR A 399    13626  16695  11856  -1683    263    607       C  
ATOM   2635  C   TYR A 399     -33.827  -1.402  64.495  1.00111.54           C  
ANISOU 2635  C   TYR A 399    13582  16827  11971  -1418    257    554       C  
ATOM   2636  O   TYR A 399     -34.123  -1.319  63.306  1.00111.62           O  
ANISOU 2636  O   TYR A 399    13504  17002  11903  -1502    232    485       O  
ATOM   2637  CB  TYR A 399     -35.869  -1.706  65.924  1.00112.86           C  
ANISOU 2637  CB  TYR A 399    13571  17311  12001  -1769    275    750       C  
ATOM   2638  CG  TYR A 399     -36.949  -2.702  66.281  1.00117.82           C  
ANISOU 2638  CG  TYR A 399    14233  18022  12512  -2157    268    788       C  
ATOM   2639  CD1 TYR A 399     -37.784  -3.236  65.304  1.00121.95           C  
ANISOU 2639  CD1 TYR A 399    14698  18747  12889  -2490    230    729       C  
ATOM   2640  CD2 TYR A 399     -37.145  -3.104  67.599  1.00119.41           C  
ANISOU 2640  CD2 TYR A 399    14521  18119  12730  -2217    299    889       C  
ATOM   2641  CE1 TYR A 399     -38.779  -4.158  65.627  1.00125.57           C  
ANISOU 2641  CE1 TYR A 399    15191  19299  13219  -2904    221    766       C  
ATOM   2642  CE2 TYR A 399     -38.141  -4.019  67.936  1.00123.12           C  
ANISOU 2642  CE2 TYR A 399    15026  18675  13079  -2609    298    937       C  
ATOM   2643  CZ  TYR A 399     -38.955  -4.546  66.946  1.00133.28           C  
ANISOU 2643  CZ  TYR A 399    16259  20162  14219  -2967    258    875       C  
ATOM   2644  OH  TYR A 399     -39.935  -5.450  67.280  1.00137.78           O  
ANISOU 2644  OH  TYR A 399    16867  20833  14652  -3405    253    925       O  
ATOM   2645  N   ARG A 400     -32.837  -0.686  65.056  1.00105.45           N  
ANISOU 2645  N   ARG A 400    12819  15935  11313  -1120    277    588       N  
ATOM   2646  CA  ARG A 400     -31.973   0.238  64.319  1.00103.44           C  
ANISOU 2646  CA  ARG A 400    12485  15714  11104   -884    276    551       C  
ATOM   2647  C   ARG A 400     -31.026  -0.564  63.409  1.00106.83           C  
ANISOU 2647  C   ARG A 400    13102  15940  11550   -870    263    407       C  
ATOM   2648  O   ARG A 400     -30.660  -0.081  62.343  1.00106.22           O  
ANISOU 2648  O   ARG A 400    12944  15961  11454   -788    256    351       O  
ATOM   2649  CB  ARG A 400     -31.189   1.135  65.295  1.00102.21           C  
ANISOU 2649  CB  ARG A 400    12309  15484  11042   -632    297    627       C  
ATOM   2650  CG  ARG A 400     -30.510   2.351  64.660  1.00112.41           C  
ANISOU 2650  CG  ARG A 400    13490  16864  12357   -431    301    625       C  
ATOM   2651  CD  ARG A 400     -30.243   3.434  65.691  1.00121.26           C  
ANISOU 2651  CD  ARG A 400    14567  17987  13519   -264    322    721       C  
ATOM   2652  NE  ARG A 400     -29.257   4.432  65.269  1.00126.61           N  
ANISOU 2652  NE  ARG A 400    15220  18658  14228   -101    325    711       N  
ATOM   2653  CZ  ARG A 400     -27.942   4.325  65.429  1.00134.52           C  
ANISOU 2653  CZ  ARG A 400    16306  19514  15293    -11    314    670       C  
ATOM   2654  NH1 ARG A 400     -27.416   3.218  65.941  1.00117.78           N  
ANISOU 2654  NH1 ARG A 400    14313  17227  13212    -23    302    632       N  
ATOM   2655  NH2 ARG A 400     -27.142   5.316  65.068  1.00119.16           N  
ANISOU 2655  NH2 ARG A 400    14319  17603  13354     91    317    675       N  
ATOM   2656  N   ALA A 401     -30.666  -1.799  63.811  1.00103.38           N  
ANISOU 2656  N   ALA A 401    12928  15220  11130   -938    268    353       N  
ATOM   2657  CA  ALA A 401     -29.795  -2.683  63.030  1.00103.48           C  
ANISOU 2657  CA  ALA A 401    13169  15014  11137   -891    271    216       C  
ATOM   2658  C   ALA A 401     -30.498  -3.223  61.778  1.00107.22           C  
ANISOU 2658  C   ALA A 401    13678  15570  11491  -1132    249    102       C  
ATOM   2659  O   ALA A 401     -29.864  -3.351  60.734  1.00107.01           O  
ANISOU 2659  O   ALA A 401    13708  15514  11437  -1046    250    -11       O  
ATOM   2660  CB  ALA A 401     -29.324  -3.844  63.889  1.00105.39           C  
ANISOU 2660  CB  ALA A 401    13717  14919  11408   -875    291    209       C  
ATOM   2661  N   GLY A 402     -31.787  -3.535  61.901  1.00103.76           N  
ANISOU 2661  N   GLY A 402    13196  15261  10966  -1440    230    133       N  
ATOM   2662  CA  GLY A 402     -32.587  -4.091  60.815  1.00104.99           C  
ANISOU 2662  CA  GLY A 402    13377  15534  10980  -1737    199     31       C  
ATOM   2663  C   GLY A 402     -33.228  -3.082  59.886  1.00106.73           C  
ANISOU 2663  C   GLY A 402    13265  16166  11123  -1756    170     54       C  
ATOM   2664  O   GLY A 402     -33.650  -3.452  58.785  1.00107.92           O  
ANISOU 2664  O   GLY A 402    13423  16434  11149  -1951    139    -50       O  
ATOM   2665  N   PHE A 403     -33.319  -1.809  60.312  1.00100.25           N  
ANISOU 2665  N   PHE A 403    12171  15561  10357  -1552    183    190       N  
ATOM   2666  CA  PHE A 403     -33.941  -0.766  59.500  1.00 99.52           C  
ANISOU 2666  CA  PHE A 403    11776  15854  10182  -1519    166    241       C  
ATOM   2667  C   PHE A 403     -32.970   0.362  59.124  1.00101.85           C  
ANISOU 2667  C   PHE A 403    11983  16157  10558  -1186    188    263       C  
ATOM   2668  O   PHE A 403     -33.325   1.211  58.308  1.00101.38           O  
ANISOU 2668  O   PHE A 403    11720  16372  10426  -1127    181    300       O  
ATOM   2669  CB  PHE A 403     -35.181  -0.200  60.203  1.00101.40           C  
ANISOU 2669  CB  PHE A 403    11769  16402  10358  -1595    169    399       C  
ATOM   2670  CG  PHE A 403     -36.344  -1.167  60.232  1.00105.31           C  
ANISOU 2670  CG  PHE A 403    12261  17038  10714  -1989    138    388       C  
ATOM   2671  CD1 PHE A 403     -37.076  -1.435  59.082  1.00110.11           C  
ANISOU 2671  CD1 PHE A 403    12762  17919  11155  -2231     91    322       C  
ATOM   2672  CD2 PHE A 403     -36.716  -1.799  61.411  1.00107.74           C  
ANISOU 2672  CD2 PHE A 403    12668  17227  11041  -2143    153    448       C  
ATOM   2673  CE1 PHE A 403     -38.146  -2.332  59.108  1.00113.48           C  
ANISOU 2673  CE1 PHE A 403    13185  18501  11432  -2650     56    311       C  
ATOM   2674  CE2 PHE A 403     -37.787  -2.695  61.436  1.00113.02           C  
ANISOU 2674  CE2 PHE A 403    13340  18037  11566  -2554    125    446       C  
ATOM   2675  CZ  PHE A 403     -38.496  -2.953  60.285  1.00113.09           C  
ANISOU 2675  CZ  PHE A 403    13241  18323  11404  -2819     75    375       C  
ATOM   2676  N   VAL A 404     -31.749   0.373  59.688  1.00 97.44           N  
ANISOU 2676  N   VAL A 404    11575  15318  10132   -979    215    249       N  
ATOM   2677  CA  VAL A 404     -30.754   1.397  59.358  1.00 95.80           C  
ANISOU 2677  CA  VAL A 404    11294  15121   9987   -713    234    270       C  
ATOM   2678  C   VAL A 404     -29.461   0.708  58.905  1.00101.41           C  
ANISOU 2678  C   VAL A 404    12193  15600  10737   -616    242    146       C  
ATOM   2679  O   VAL A 404     -29.007   0.995  57.801  1.00101.45           O  
ANISOU 2679  O   VAL A 404    12149  15697  10700   -548    243     87       O  
ATOM   2680  CB  VAL A 404     -30.497   2.427  60.492  1.00 97.88           C  
ANISOU 2680  CB  VAL A 404    11487  15366  10339   -531    260    402       C  
ATOM   2681  CG1 VAL A 404     -29.679   3.607  59.996  1.00 96.40           C  
ANISOU 2681  CG1 VAL A 404    11215  15235  10176   -329    277    433       C  
ATOM   2682  CG2 VAL A 404     -31.799   2.922  61.104  1.00 98.03           C  
ANISOU 2682  CG2 VAL A 404    11355  15589  10302   -598    266    523       C  
ATOM   2683  N   LEU A 405     -28.888  -0.209  59.721  1.00 98.92           N  
ANISOU 2683  N   LEU A 405    12093  15008  10486   -592    254    112       N  
ATOM   2684  CA  LEU A 405     -27.646  -0.903  59.364  1.00 99.53           C  
ANISOU 2684  CA  LEU A 405    12352  14883  10581   -444    272      8       C  
ATOM   2685  C   LEU A 405     -27.827  -1.898  58.214  1.00105.08           C  
ANISOU 2685  C   LEU A 405    13216  15533  11176   -573    267   -148       C  
ATOM   2686  O   LEU A 405     -26.920  -2.016  57.394  1.00105.18           O  
ANISOU 2686  O   LEU A 405    13276  15525  11163   -421    286   -235       O  
ATOM   2687  CB  LEU A 405     -27.014  -1.625  60.563  1.00100.02           C  
ANISOU 2687  CB  LEU A 405    12610  14676  10718   -345    290     31       C  
ATOM   2688  CG  LEU A 405     -25.982  -0.851  61.394  1.00103.54           C  
ANISOU 2688  CG  LEU A 405    12960  15126  11253   -109    301    124       C  
ATOM   2689  CD1 LEU A 405     -25.490  -1.694  62.542  1.00104.65           C  
ANISOU 2689  CD1 LEU A 405    13295  15028  11440    -24    313    151       C  
ATOM   2690  CD2 LEU A 405     -24.774  -0.426  60.563  1.00105.13           C  
ANISOU 2690  CD2 LEU A 405    13084  15413  11445     88    315     80       C  
ATOM   2691  N   ALA A 406     -28.967  -2.613  58.154  1.00102.77           N  
ANISOU 2691  N   ALA A 406    13011  15233  10805   -862    244   -186       N  
ATOM   2692  CA  ALA A 406     -29.242  -3.582  57.090  1.00104.91           C  
ANISOU 2692  CA  ALA A 406    13469  15445  10948  -1042    233   -347       C  
ATOM   2693  C   ALA A 406     -29.372  -2.886  55.713  1.00108.64           C  
ANISOU 2693  C   ALA A 406    13736  16214  11330  -1041    214   -394       C  
ATOM   2694  O   ALA A 406     -28.622  -3.284  54.823  1.00108.69           O  
ANISOU 2694  O   ALA A 406    13871  16143  11285   -937    233   -521       O  
ATOM   2695  CB  ALA A 406     -30.488  -4.397  57.407  1.00107.66           C  
ANISOU 2695  CB  ALA A 406    13932  15760  11215  -1410    204   -360       C  
ATOM   2696  N   PRO A 407     -30.217  -1.829  55.505  1.00104.56           N  
ANISOU 2696  N   PRO A 407    12908  16037  10782  -1108    186   -287       N  
ATOM   2697  CA  PRO A 407     -30.276  -1.195  54.172  1.00104.27           C  
ANISOU 2697  CA  PRO A 407    12696  16273  10647  -1081    172   -321       C  
ATOM   2698  C   PRO A 407     -28.983  -0.477  53.777  1.00105.53           C  
ANISOU 2698  C   PRO A 407    12802  16424  10872   -774    210   -310       C  
ATOM   2699  O   PRO A 407     -28.657  -0.484  52.594  1.00105.92           O  
ANISOU 2699  O   PRO A 407    12841  16574  10831   -741    212   -400       O  
ATOM   2700  CB  PRO A 407     -31.438  -0.208  54.289  1.00105.61           C  
ANISOU 2700  CB  PRO A 407    12567  16786  10775  -1164    145   -172       C  
ATOM   2701  CG  PRO A 407     -31.572   0.055  55.730  1.00108.95           C  
ANISOU 2701  CG  PRO A 407    12974  17107  11316  -1110    163    -45       C  
ATOM   2702  CD  PRO A 407     -31.195  -1.207  56.422  1.00105.39           C  
ANISOU 2702  CD  PRO A 407    12820  16308  10915  -1194    172   -130       C  
ATOM   2703  N   ILE A 408     -28.244   0.114  54.744  1.00 99.79           N  
ANISOU 2703  N   ILE A 408    12039  15594  10281   -571    238   -205       N  
ATOM   2704  CA  ILE A 408     -26.970   0.793  54.462  1.00 98.63           C  
ANISOU 2704  CA  ILE A 408    11829  15461  10183   -320    272   -183       C  
ATOM   2705  C   ILE A 408     -25.893  -0.279  54.173  1.00104.28           C  
ANISOU 2705  C   ILE A 408    12768  15970  10885   -202    302   -322       C  
ATOM   2706  O   ILE A 408     -25.025  -0.058  53.327  1.00104.02           O  
ANISOU 2706  O   ILE A 408    12691  16024  10810    -55    328   -365       O  
ATOM   2707  CB  ILE A 408     -26.557   1.810  55.566  1.00 99.88           C  
ANISOU 2707  CB  ILE A 408    11880  15607  10463   -184    285    -30       C  
ATOM   2708  CG1 ILE A 408     -27.577   2.974  55.612  1.00 99.68           C  
ANISOU 2708  CG1 ILE A 408    11658  15800  10417   -241    273    100       C  
ATOM   2709  CG2 ILE A 408     -25.132   2.358  55.342  1.00 99.44           C  
ANISOU 2709  CG2 ILE A 408    11777  15564  10439     25    316    -16       C  
ATOM   2710  CD1 ILE A 408     -27.513   3.889  56.851  1.00107.69           C  
ANISOU 2710  CD1 ILE A 408    12621  16770  11527   -151    286    240       C  
ATOM   2711  N   GLY A 409     -26.003  -1.438  54.822  1.00102.44           N  
ANISOU 2711  N   GLY A 409    12780  15477  10666   -263    304   -386       N  
ATOM   2712  CA  GLY A 409     -25.117  -2.572  54.589  1.00103.98           C  
ANISOU 2712  CA  GLY A 409    13243  15440  10823   -128    342   -518       C  
ATOM   2713  C   GLY A 409     -25.321  -3.116  53.192  1.00109.59           C  
ANISOU 2713  C   GLY A 409    14055  16201  11384   -215    343   -680       C  
ATOM   2714  O   GLY A 409     -24.349  -3.401  52.490  1.00110.22           O  
ANISOU 2714  O   GLY A 409    14211  16262  11406    -12    386   -769       O  
ATOM   2715  N   LEU A 410     -26.599  -3.193  52.767  1.00106.28           N  
ANISOU 2715  N   LEU A 410    13607  15891  10882   -518    296   -711       N  
ATOM   2716  CA  LEU A 410     -27.028  -3.654  51.450  1.00107.69           C  
ANISOU 2716  CA  LEU A 410    13862  16163  10893   -675    280   -864       C  
ATOM   2717  C   LEU A 410     -26.587  -2.688  50.344  1.00110.24           C  
ANISOU 2717  C   LEU A 410    13936  16787  11163   -533    287   -849       C  
ATOM   2718  O   LEU A 410     -26.006  -3.157  49.369  1.00111.45           O  
ANISOU 2718  O   LEU A 410    14212  16926  11209   -443    316   -987       O  
ATOM   2719  CB  LEU A 410     -28.552  -3.849  51.412  1.00108.82           C  
ANISOU 2719  CB  LEU A 410    13969  16424  10951  -1059    216   -866       C  
ATOM   2720  CG  LEU A 410     -29.123  -4.447  50.130  1.00116.27           C  
ANISOU 2720  CG  LEU A 410    15014  17469  11694  -1293    184  -1036       C  
ATOM   2721  CD1 LEU A 410     -29.066  -5.965  50.159  1.00119.34           C  
ANISOU 2721  CD1 LEU A 410    15860  17483  12003  -1435    201  -1218       C  
ATOM   2722  CD2 LEU A 410     -30.560  -4.022  49.942  1.00119.70           C  
ANISOU 2722  CD2 LEU A 410    15205  18239  12037  -1611    113   -968       C  
ATOM   2723  N   VAL A 411     -26.822  -1.353  50.498  1.00104.13           N  
ANISOU 2723  N   VAL A 411    12843  16271  10453   -497    271   -679       N  
ATOM   2724  CA  VAL A 411     -26.434  -0.352  49.482  1.00102.91           C  
ANISOU 2724  CA  VAL A 411    12464  16393  10242   -376    282   -636       C  
ATOM   2725  C   VAL A 411     -24.902  -0.334  49.299  1.00106.44           C  
ANISOU 2725  C   VAL A 411    12950  16773  10721    -91    344   -662       C  
ATOM   2726  O   VAL A 411     -24.437  -0.040  48.199  1.00106.62           O  
ANISOU 2726  O   VAL A 411    12892  16974  10645     -7    366   -701       O  
ATOM   2727  CB  VAL A 411     -27.003   1.087  49.671  1.00104.74           C  
ANISOU 2727  CB  VAL A 411    12403  16876  10516   -381    263   -442       C  
ATOM   2728  CG1 VAL A 411     -28.528   1.092  49.653  1.00105.05           C  
ANISOU 2728  CG1 VAL A 411    12355  17081  10479   -627    207   -410       C  
ATOM   2729  CG2 VAL A 411     -26.461   1.775  50.917  1.00102.70           C  
ANISOU 2729  CG2 VAL A 411    12093  16504  10423   -237    285   -298       C  
ATOM   2730  N   LEU A 412     -24.132  -0.691  50.348  1.00102.40           N  
ANISOU 2730  N   LEU A 412    12549  16037  10322     57    373   -637       N  
ATOM   2731  CA  LEU A 412     -22.676  -0.780  50.265  1.00102.39           C  
ANISOU 2731  CA  LEU A 412    12565  16012  10327    335    431   -653       C  
ATOM   2732  C   LEU A 412     -22.259  -1.979  49.428  1.00107.90           C  
ANISOU 2732  C   LEU A 412    13509  16597  10891    424    470   -846       C  
ATOM   2733  O   LEU A 412     -21.275  -1.889  48.699  1.00108.23           O  
ANISOU 2733  O   LEU A 412    13497  16768  10859    629    520   -881       O  
ATOM   2734  CB  LEU A 412     -22.035  -0.880  51.652  1.00101.77           C  
ANISOU 2734  CB  LEU A 412    12528  15758  10381    470    444   -566       C  
ATOM   2735  CG  LEU A 412     -21.803   0.418  52.415  1.00104.42           C  
ANISOU 2735  CG  LEU A 412    12622  16224  10828    488    430   -383       C  
ATOM   2736  CD1 LEU A 412     -21.301   0.114  53.793  1.00104.12           C  
ANISOU 2736  CD1 LEU A 412    12660  16007  10895    589    433   -323       C  
ATOM   2737  CD2 LEU A 412     -20.791   1.315  51.715  1.00106.57           C  
ANISOU 2737  CD2 LEU A 412    12691  16745  11058    619    461   -328       C  
ATOM   2738  N   ILE A 413     -23.006  -3.099  49.532  1.00105.37           N  
ANISOU 2738  N   ILE A 413    13476  16036  10524    264    453   -972       N  
ATOM   2739  CA  ILE A 413     -22.727  -4.324  48.782  1.00107.61           C  
ANISOU 2739  CA  ILE A 413    14080  16145  10662    326    494  -1176       C  
ATOM   2740  C   ILE A 413     -23.121  -4.123  47.312  1.00112.71           C  
ANISOU 2740  C   ILE A 413    14651  17029  11145    208    479  -1279       C  
ATOM   2741  O   ILE A 413     -22.282  -4.338  46.440  1.00113.28           O  
ANISOU 2741  O   ILE A 413    14770  17167  11105    416    536  -1374       O  
ATOM   2742  CB  ILE A 413     -23.412  -5.573  49.415  1.00112.07           C  
ANISOU 2742  CB  ILE A 413    15023  16340  11217    150    481  -1272       C  
ATOM   2743  CG1 ILE A 413     -22.874  -5.843  50.832  1.00111.61           C  
ANISOU 2743  CG1 ILE A 413    15060  16046  11302    320    506  -1167       C  
ATOM   2744  CG2 ILE A 413     -23.241  -6.819  48.529  1.00115.82           C  
ANISOU 2744  CG2 ILE A 413    15893  16604  11511    177    524  -1503       C  
ATOM   2745  CD1 ILE A 413     -23.820  -6.654  51.738  1.00119.25           C  
ANISOU 2745  CD1 ILE A 413    16290  16715  12303     64    475  -1175       C  
ATOM   2746  N   VAL A 414     -24.378  -3.697  47.046  1.00109.20           N  
ANISOU 2746  N   VAL A 414    14074  16748  10671   -106    407  -1251       N  
ATOM   2747  CA  VAL A 414     -24.922  -3.497  45.697  1.00110.29           C  
ANISOU 2747  CA  VAL A 414    14123  17145  10637   -254    378  -1335       C  
ATOM   2748  C   VAL A 414     -24.198  -2.337  44.990  1.00114.14           C  
ANISOU 2748  C   VAL A 414    14303  17952  11115    -51    408  -1231       C  
ATOM   2749  O   VAL A 414     -23.678  -2.537  43.889  1.00115.19           O  
ANISOU 2749  O   VAL A 414    14473  18193  11103     55    444  -1344       O  
ATOM   2750  CB  VAL A 414     -26.466  -3.305  45.677  1.00114.01           C  
ANISOU 2750  CB  VAL A 414    14487  17768  11062   -626    290  -1302       C  
ATOM   2751  CG1 VAL A 414     -27.005  -3.368  44.254  1.00115.62           C  
ANISOU 2751  CG1 VAL A 414    14655  18225  11048   -789    256  -1422       C  
ATOM   2752  CG2 VAL A 414     -27.174  -4.341  46.549  1.00114.99           C  
ANISOU 2752  CG2 VAL A 414    14885  17596  11209   -863    262  -1365       C  
ATOM   2753  N   GLY A 415     -24.166  -1.161  45.625  1.00109.19           N  
ANISOU 2753  N   GLY A 415    13402  17458  10627     -7    396  -1022       N  
ATOM   2754  CA  GLY A 415     -23.504   0.033  45.099  1.00108.15           C  
ANISOU 2754  CA  GLY A 415    13000  17598  10495    145    425   -895       C  
ATOM   2755  C   GLY A 415     -22.032  -0.196  44.829  1.00113.06           C  
ANISOU 2755  C   GLY A 415    13659  18208  11091    426    503   -939       C  
ATOM   2756  O   GLY A 415     -21.527   0.178  43.766  1.00113.37           O  
ANISOU 2756  O   GLY A 415    13584  18478  11012    516    537   -952       O  
ATOM   2757  N   GLY A 416     -21.373  -0.857  45.781  1.00109.64           N  
ANISOU 2757  N   GLY A 416    13381  17529  10748    571    533   -960       N  
ATOM   2758  CA  GLY A 416     -19.967  -1.225  45.714  1.00110.24           C  
ANISOU 2758  CA  GLY A 416    13496  17600  10792    874    611   -994       C  
ATOM   2759  C   GLY A 416     -19.665  -2.147  44.559  1.00116.53           C  
ANISOU 2759  C   GLY A 416    14484  18397  11394    984    660  -1195       C  
ATOM   2760  O   GLY A 416     -18.700  -1.909  43.836  1.00116.81           O  
ANISOU 2760  O   GLY A 416    14401  18650  11333   1190    722  -1195       O  
ATOM   2761  N   TYR A 417     -20.514  -3.178  44.349  1.00114.73           N  
ANISOU 2761  N   TYR A 417    14559  17944  11090    827    635  -1367       N  
ATOM   2762  CA  TYR A 417     -20.377  -4.146  43.257  1.00117.54           C  
ANISOU 2762  CA  TYR A 417    15175  18248  11239    892    678  -1590       C  
ATOM   2763  C   TYR A 417     -20.365  -3.447  41.900  1.00121.25           C  
ANISOU 2763  C   TYR A 417    15423  19084  11563    867    681  -1599       C  
ATOM   2764  O   TYR A 417     -19.495  -3.750  41.088  1.00122.76           O  
ANISOU 2764  O   TYR A 417    15660  19374  11609   1104    757  -1693       O  
ATOM   2765  CB  TYR A 417     -21.496  -5.204  43.304  1.00120.81           C  
ANISOU 2765  CB  TYR A 417    15943  18368  11592    614    630  -1758       C  
ATOM   2766  CG  TYR A 417     -21.504  -6.160  42.130  1.00126.07           C  
ANISOU 2766  CG  TYR A 417    16914  18966  12020    618    665  -2007       C  
ATOM   2767  CD1 TYR A 417     -20.603  -7.218  42.061  1.00130.68           C  
ANISOU 2767  CD1 TYR A 417    17849  19294  12509    922    759  -2154       C  
ATOM   2768  CD2 TYR A 417     -22.432  -6.023  41.101  1.00127.75           C  
ANISOU 2768  CD2 TYR A 417    17083  19374  12083    327    604  -2097       C  
ATOM   2769  CE1 TYR A 417     -20.608  -8.104  40.987  1.00135.18           C  
ANISOU 2769  CE1 TYR A 417    18746  19773  12842    938    799  -2398       C  
ATOM   2770  CE2 TYR A 417     -22.441  -6.897  40.016  1.00132.08           C  
ANISOU 2770  CE2 TYR A 417    17930  19861  12393    311    632  -2340       C  
ATOM   2771  CZ  TYR A 417     -21.529  -7.939  39.964  1.00142.75           C  
ANISOU 2771  CZ  TYR A 417    19661  20924  13655    614    732  -2498       C  
ATOM   2772  OH  TYR A 417     -21.539  -8.815  38.902  1.00147.04           O  
ANISOU 2772  OH  TYR A 417    20546  21377  13946    610    768  -2753       O  
ATOM   2773  N   PHE A 418     -21.309  -2.514  41.665  1.00115.92           N  
ANISOU 2773  N   PHE A 418    14508  18624  10912    607    606  -1492       N  
ATOM   2774  CA  PHE A 418     -21.408  -1.780  40.407  1.00115.94           C  
ANISOU 2774  CA  PHE A 418    14295  18983  10772    569    603  -1473       C  
ATOM   2775  C   PHE A 418     -20.236  -0.814  40.220  1.00118.73           C  
ANISOU 2775  C   PHE A 418    14375  19587  11152    806    667  -1317       C  
ATOM   2776  O   PHE A 418     -19.798  -0.619  39.085  1.00119.50           O  
ANISOU 2776  O   PHE A 418    14386  19932  11087    896    709  -1354       O  
ATOM   2777  CB  PHE A 418     -22.748  -1.043  40.305  1.00116.64           C  
ANISOU 2777  CB  PHE A 418    14207  19238  10873    265    509  -1374       C  
ATOM   2778  CG  PHE A 418     -23.949  -1.956  40.204  1.00120.05           C  
ANISOU 2778  CG  PHE A 418    14859  19541  11214    -24    440  -1534       C  
ATOM   2779  CD1 PHE A 418     -23.894  -3.128  39.460  1.00126.38           C  
ANISOU 2779  CD1 PHE A 418    15970  20218  11831    -51    459  -1784       C  
ATOM   2780  CD2 PHE A 418     -25.146  -1.628  40.824  1.00121.35           C  
ANISOU 2780  CD2 PHE A 418    14924  19729  11454   -283    358  -1433       C  
ATOM   2781  CE1 PHE A 418     -25.001  -3.973  39.367  1.00129.30           C  
ANISOU 2781  CE1 PHE A 418    16563  20469  12097   -376    390  -1935       C  
ATOM   2782  CE2 PHE A 418     -26.259  -2.469  40.720  1.00126.11           C  
ANISOU 2782  CE2 PHE A 418    15703  20264  11951   -594    291  -1571       C  
ATOM   2783  CZ  PHE A 418     -26.178  -3.637  39.994  1.00127.19           C  
ANISOU 2783  CZ  PHE A 418    16160  20262  11906   -663    303  -1823       C  
ATOM   2784  N   LEU A 419     -19.706  -0.252  41.320  1.00113.33           N  
ANISOU 2784  N   LEU A 419    13563  18846  10651    891    676  -1148       N  
ATOM   2785  CA  LEU A 419     -18.552   0.647  41.284  1.00112.39           C  
ANISOU 2785  CA  LEU A 419    13192  18959  10553   1067    732   -993       C  
ATOM   2786  C   LEU A 419     -17.265  -0.128  41.016  1.00118.62           C  
ANISOU 2786  C   LEU A 419    14062  19772  11237   1378    826  -1095       C  
ATOM   2787  O   LEU A 419     -16.427   0.361  40.268  1.00119.03           O  
ANISOU 2787  O   LEU A 419    13925  20121  11180   1506    884  -1043       O  
ATOM   2788  CB  LEU A 419     -18.421   1.457  42.578  1.00110.13           C  
ANISOU 2788  CB  LEU A 419    12768  18605  10473   1026    705   -796       C  
ATOM   2789  CG  LEU A 419     -19.344   2.665  42.712  1.00112.95           C  
ANISOU 2789  CG  LEU A 419    12961  19049  10906    803    644   -630       C  
ATOM   2790  CD1 LEU A 419     -19.492   3.054  44.149  1.00111.17           C  
ANISOU 2790  CD1 LEU A 419    12724  18641  10876    750    611   -507       C  
ATOM   2791  CD2 LEU A 419     -18.835   3.856  41.910  1.00115.45           C  
ANISOU 2791  CD2 LEU A 419    13042  19677  11147    814    678   -487       C  
ATOM   2792  N   ILE A 420     -17.110  -1.334  41.606  1.00116.90           N  
ANISOU 2792  N   ILE A 420    14129  19254  11034   1512    847  -1230       N  
ATOM   2793  CA  ILE A 420     -15.940  -2.194  41.404  1.00119.70           C  
ANISOU 2793  CA  ILE A 420    14606  19606  11269   1866    945  -1332       C  
ATOM   2794  C   ILE A 420     -15.979  -2.754  39.974  1.00127.48           C  
ANISOU 2794  C   ILE A 420    15730  20691  12016   1931    992  -1525       C  
ATOM   2795  O   ILE A 420     -14.980  -2.634  39.268  1.00128.67           O  
ANISOU 2795  O   ILE A 420    15746  21118  12026   2172   1075  -1521       O  
ATOM   2796  CB  ILE A 420     -15.823  -3.318  42.479  1.00123.88           C  
ANISOU 2796  CB  ILE A 420    15446  19751  11873   2012    959  -1407       C  
ATOM   2797  CG1 ILE A 420     -15.535  -2.724  43.876  1.00122.30           C  
ANISOU 2797  CG1 ILE A 420    15068  19520  11880   2002    924  -1207       C  
ATOM   2798  CG2 ILE A 420     -14.744  -4.356  42.111  1.00127.86           C  
ANISOU 2798  CG2 ILE A 420    16148  20229  12206   2424   1072  -1540       C  
ATOM   2799  CD1 ILE A 420     -15.960  -3.621  45.069  1.00130.06           C  
ANISOU 2799  CD1 ILE A 420    16351  20088  12980   1995    898  -1247       C  
ATOM   2800  N   ARG A 421     -17.131  -3.316  39.537  1.00125.58           N  
ANISOU 2800  N   ARG A 421    15737  20265  11714   1696    937  -1686       N  
ATOM   2801  CA  ARG A 421     -17.291  -3.867  38.183  1.00128.27           C  
ANISOU 2801  CA  ARG A 421    16240  20686  11810   1708    968  -1889       C  
ATOM   2802  C   ARG A 421     -17.159  -2.769  37.111  1.00131.21           C  
ANISOU 2802  C   ARG A 421    16264  21506  12082   1659    971  -1786       C  
ATOM   2803  O   ARG A 421     -16.703  -3.059  36.008  1.00132.74           O  
ANISOU 2803  O   ARG A 421    16498  21877  12061   1812   1037  -1906       O  
ATOM   2804  CB  ARG A 421     -18.624  -4.616  38.030  1.00130.32           C  
ANISOU 2804  CB  ARG A 421    16814  20682  12020   1391    890  -2066       C  
ATOM   2805  CG  ARG A 421     -18.537  -5.786  37.056  1.00147.07           C  
ANISOU 2805  CG  ARG A 421    19316  22677  13887   1488    946  -2348       C  
ATOM   2806  CD  ARG A 421     -19.812  -6.602  37.030  1.00161.15           C  
ANISOU 2806  CD  ARG A 421    21443  24173  15612   1127    866  -2527       C  
ATOM   2807  NE  ARG A 421     -19.856  -7.508  35.880  1.00175.91           N  
ANISOU 2807  NE  ARG A 421    23649  25987  17202   1142    905  -2800       N  
ATOM   2808  CZ  ARG A 421     -20.966  -8.068  35.406  1.00193.41           C  
ANISOU 2808  CZ  ARG A 421    26112  28094  19282    772    828  -2979       C  
ATOM   2809  NH1 ARG A 421     -22.140  -7.817  35.975  1.00180.17           N  
ANISOU 2809  NH1 ARG A 421    24348  26385  17721    368    711  -2899       N  
ATOM   2810  NH2 ARG A 421     -20.913  -8.875  34.355  1.00183.32           N  
ANISOU 2810  NH2 ARG A 421    25161  26762  17731    796    869  -3238       N  
ATOM   2811  N   GLY A 422     -17.516  -1.533  37.468  1.00124.80           N  
ANISOU 2811  N   GLY A 422    15140  20860  11417   1470    910  -1563       N  
ATOM   2812  CA  GLY A 422     -17.409  -0.364  36.607  1.00123.74           C  
ANISOU 2812  CA  GLY A 422    14688  21117  11211   1412    913  -1420       C  
ATOM   2813  C   GLY A 422     -15.974  -0.016  36.244  1.00127.91           C  
ANISOU 2813  C   GLY A 422    15018  21926  11658   1689   1017  -1338       C  
ATOM   2814  O   GLY A 422     -15.664   0.103  35.058  1.00129.43           O  
ANISOU 2814  O   GLY A 422    15132  22396  11650   1760   1067  -1381       O  
ATOM   2815  N   VAL A 423     -15.079   0.142  37.254  1.00122.84           N  
ANISOU 2815  N   VAL A 423    14277  21249  11149   1841   1051  -1217       N  
ATOM   2816  CA  VAL A 423     -13.657   0.450  37.025  1.00123.49           C  
ANISOU 2816  CA  VAL A 423    14133  21647  11142   2093   1148  -1123       C  
ATOM   2817  C   VAL A 423     -12.967  -0.753  36.403  1.00130.32           C  
ANISOU 2817  C   VAL A 423    15192  22522  11800   2429   1246  -1330       C  
ATOM   2818  O   VAL A 423     -12.039  -0.568  35.621  1.00131.23           O  
ANISOU 2818  O   VAL A 423    15130  22990  11741   2621   1335  -1304       O  
ATOM   2819  CB  VAL A 423     -12.860   0.960  38.255  1.00126.10           C  
ANISOU 2819  CB  VAL A 423    14278  21997  11638   2145   1151   -934       C  
ATOM   2820  CG1 VAL A 423     -13.186   2.411  38.570  1.00123.44           C  
ANISOU 2820  CG1 VAL A 423    13700  21768  11433   1855   1089   -703       C  
ATOM   2821  CG2 VAL A 423     -13.037   0.067  39.481  1.00125.59           C  
ANISOU 2821  CG2 VAL A 423    14454  21546  11717   2227   1123  -1007       C  
ATOM   2822  N   MET A 424     -13.434  -1.980  36.736  1.00128.54           N  
ANISOU 2822  N   MET A 424    15352  21910  11578   2499   1238  -1534       N  
ATOM   2823  CA  MET A 424     -12.909  -3.227  36.188  1.00132.14           C  
ANISOU 2823  CA  MET A 424    16098  22282  11827   2829   1335  -1757       C  
ATOM   2824  C   MET A 424     -13.125  -3.260  34.684  1.00139.03           C  
ANISOU 2824  C   MET A 424    16995  23371  12458   2802   1365  -1891       C  
ATOM   2825  O   MET A 424     -12.223  -3.668  33.968  1.00141.25           O  
ANISOU 2825  O   MET A 424    17286  23855  12528   3125   1477  -1971       O  
ATOM   2826  CB  MET A 424     -13.539  -4.452  36.856  1.00135.29           C  
ANISOU 2826  CB  MET A 424    16959  22165  12282   2830   1309  -1939       C  
ATOM   2827  CG  MET A 424     -12.830  -4.850  38.127  1.00138.83           C  
ANISOU 2827  CG  MET A 424    17456  22436  12859   3076   1341  -1859       C  
ATOM   2828  SD  MET A 424     -13.563  -6.295  38.915  1.00144.44           S  
ANISOU 2828  SD  MET A 424    18747  22512  13621   3068   1320  -2053       S  
ATOM   2829  CE  MET A 424     -12.318  -7.518  38.546  1.00145.51           C  
ANISOU 2829  CE  MET A 424    19176  22600  13512   3665   1486  -2209       C  
ATOM   2830  N   THR A 425     -14.291  -2.779  34.206  1.00135.43           N  
ANISOU 2830  N   THR A 425    16520  22919  12018   2434   1268  -1898       N  
ATOM   2831  CA  THR A 425     -14.628  -2.695  32.783  1.00137.38           C  
ANISOU 2831  CA  THR A 425    16761  23403  12033   2358   1276  -2006       C  
ATOM   2832  C   THR A 425     -13.760  -1.619  32.119  1.00141.83           C  
ANISOU 2832  C   THR A 425    16914  24461  12512   2453   1338  -1812       C  
ATOM   2833  O   THR A 425     -13.247  -1.859  31.028  1.00143.58           O  
ANISOU 2833  O   THR A 425    17133  24933  12489   2635   1422  -1911       O  
ATOM   2834  CB  THR A 425     -16.134  -2.418  32.598  1.00147.02           C  
ANISOU 2834  CB  THR A 425    18031  24531  13298   1938   1145  -2029       C  
ATOM   2835  OG1 THR A 425     -16.886  -3.355  33.370  1.00148.58           O  
ANISOU 2835  OG1 THR A 425    18577  24287  13589   1813   1087  -2173       O  
ATOM   2836  CG2 THR A 425     -16.575  -2.519  31.153  1.00147.65           C  
ANISOU 2836  CG2 THR A 425    18155  24832  13113   1850   1142  -2173       C  
ATOM   2837  N   LEU A 426     -13.568  -0.464  32.796  1.00136.90           N  
ANISOU 2837  N   LEU A 426    15968  23969  12078   2326   1304  -1542       N  
ATOM   2838  CA  LEU A 426     -12.769   0.658  32.303  1.00137.17           C  
ANISOU 2838  CA  LEU A 426    15624  24446  12050   2346   1356  -1326       C  
ATOM   2839  C   LEU A 426     -11.291   0.274  32.153  1.00146.32           C  
ANISOU 2839  C   LEU A 426    16677  25856  13064   2724   1489  -1331       C  
ATOM   2840  O   LEU A 426     -10.743   0.414  31.061  1.00148.29           O  
ANISOU 2840  O   LEU A 426    16794  26463  13086   2846   1570  -1339       O  
ATOM   2841  CB  LEU A 426     -12.909   1.891  33.222  1.00133.98           C  
ANISOU 2841  CB  LEU A 426    14981  24043  11883   2110   1289  -1054       C  
ATOM   2842  CG  LEU A 426     -11.990   3.091  32.924  1.00138.23           C  
ANISOU 2842  CG  LEU A 426    15157  24991  12374   2087   1343   -807       C  
ATOM   2843  CD1 LEU A 426     -12.440   3.848  31.701  1.00138.77           C  
ANISOU 2843  CD1 LEU A 426    15114  25318  12293   1930   1339   -741       C  
ATOM   2844  CD2 LEU A 426     -11.939   4.037  34.094  1.00138.14           C  
ANISOU 2844  CD2 LEU A 426    15002  24888  12595   1902   1289   -583       C  
ATOM   2845  N   PHE A 427     -10.655  -0.203  33.238  1.00144.60           N  
ANISOU 2845  N   PHE A 427    16500  25483  12959   2919   1514  -1316       N  
ATOM   2846  CA  PHE A 427      -9.239  -0.567  33.255  1.00147.52           C  
ANISOU 2846  CA  PHE A 427    16735  26123  13191   3307   1638  -1293       C  
ATOM   2847  C   PHE A 427      -8.929  -1.806  32.410  1.00156.09           C  
ANISOU 2847  C   PHE A 427    18096  27196  14017   3672   1742  -1551       C  
ATOM   2848  O   PHE A 427      -7.806  -1.914  31.911  1.00157.13           O  
ANISOU 2848  O   PHE A 427    18052  27704  13945   3992   1863  -1527       O  
ATOM   2849  CB  PHE A 427      -8.721  -0.746  34.689  1.00148.62           C  
ANISOU 2849  CB  PHE A 427    16847  26109  13512   3420   1625  -1199       C  
ATOM   2850  CG  PHE A 427      -8.417   0.576  35.354  1.00148.16           C  
ANISOU 2850  CG  PHE A 427    16421  26260  13613   3163   1574   -916       C  
ATOM   2851  CD1 PHE A 427      -7.216   1.237  35.111  1.00152.67           C  
ANISOU 2851  CD1 PHE A 427    16613  27335  14061   3248   1648   -739       C  
ATOM   2852  CD2 PHE A 427      -9.335   1.168  36.213  1.00147.53           C  
ANISOU 2852  CD2 PHE A 427    16385  25884  13785   2825   1454   -828       C  
ATOM   2853  CE1 PHE A 427      -6.949   2.478  35.702  1.00151.94           C  
ANISOU 2853  CE1 PHE A 427    16223  27414  14095   2959   1598   -487       C  
ATOM   2854  CE2 PHE A 427      -9.062   2.401  36.816  1.00148.68           C  
ANISOU 2854  CE2 PHE A 427    16244  26188  14058   2585   1412   -581       C  
ATOM   2855  CZ  PHE A 427      -7.876   3.053  36.548  1.00148.13           C  
ANISOU 2855  CZ  PHE A 427    15833  26588  13864   2635   1481   -416       C  
ATOM   2856  N   SER A 428      -9.910  -2.712  32.214  1.00155.64           N  
ANISOU 2856  N   SER A 428    18466  26729  13943   3616   1701  -1795       N  
ATOM   2857  CA  SER A 428      -9.721  -3.893  31.371  1.00159.68           C  
ANISOU 2857  CA  SER A 428    19316  27167  14189   3928   1798  -2067       C  
ATOM   2858  C   SER A 428      -9.692  -3.472  29.914  1.00164.76           C  
ANISOU 2858  C   SER A 428    19811  28199  14589   3888   1839  -2100       C  
ATOM   2859  O   SER A 428      -8.763  -3.856  29.204  1.00166.16           O  
ANISOU 2859  O   SER A 428    19959  28657  14517   4254   1972  -2167       O  
ATOM   2860  CB  SER A 428     -10.816  -4.930  31.602  1.00163.65           C  
ANISOU 2860  CB  SER A 428    20338  27109  14733   3800   1732  -2314       C  
ATOM   2861  OG  SER A 428     -10.635  -6.087  30.801  1.00176.60           O  
ANISOU 2861  OG  SER A 428    22369  28631  16102   4088   1829  -2592       O  
ATOM   2862  N   ALA A1011     -10.685  -2.655  29.478  1.00135.67           N  
ANISOU 2862  N   ALA A1011    14950  22433  14167   1223   2438  -1548       N  
ATOM   2863  CA  ALA A1011     -10.805  -2.136  28.113  1.00134.36           C  
ANISOU 2863  CA  ALA A1011    14808  22086  14158   1155   2303  -1648       C  
ATOM   2864  C   ALA A1011      -9.657  -1.199  27.763  1.00136.12           C  
ANISOU 2864  C   ALA A1011    15186  22077  14457   1248   2104  -1716       C  
ATOM   2865  O   ALA A1011      -9.209  -1.203  26.614  1.00133.13           O  
ANISOU 2865  O   ALA A1011    14898  21465  14220   1132   2054  -1695       O  
ATOM   2866  CB  ALA A1011     -12.136  -1.419  27.943  1.00136.34           C  
ANISOU 2866  CB  ALA A1011    14898  22547  14359   1248   2238  -1828       C  
ATOM   2867  N   ARG A1012      -9.184  -0.400  28.738  1.00134.42           N  
ANISOU 2867  N   ARG A1012    14992  21930  14152   1453   1995  -1804       N  
ATOM   2868  CA  ARG A1012      -8.067   0.513  28.529  1.00133.94           C  
ANISOU 2868  CA  ARG A1012    15060  21650  14182   1523   1812  -1884       C  
ATOM   2869  C   ARG A1012      -6.763  -0.250  28.423  1.00137.47           C  
ANISOU 2869  C   ARG A1012    15611  21917  14703   1402   1877  -1748       C  
ATOM   2870  O   ARG A1012      -5.900   0.169  27.653  1.00135.91           O  
ANISOU 2870  O   ARG A1012    15510  21486  14643   1336   1784  -1768       O  
ATOM   2871  CB  ARG A1012      -7.972   1.559  29.637  1.00136.45           C  
ANISOU 2871  CB  ARG A1012    15353  22097  14394   1783   1661  -2049       C  
ATOM   2872  CG  ARG A1012      -8.752   2.816  29.356  1.00148.15           C  
ANISOU 2872  CG  ARG A1012    16813  23602  15875   1927   1481  -2243       C  
ATOM   2873  CD  ARG A1012      -8.764   3.697  30.574  1.00163.95           C  
ANISOU 2873  CD  ARG A1012    18772  25770  17752   2202   1339  -2414       C  
ATOM   2874  NE  ARG A1012      -7.956   4.886  30.344  1.00173.20           N  
ANISOU 2874  NE  ARG A1012    20069  26690  19051   2276   1113  -2554       N  
ATOM   2875  CZ  ARG A1012      -6.779   5.148  30.913  1.00187.10           C  
ANISOU 2875  CZ  ARG A1012    21883  28345  20862   2322   1033  -2598       C  
ATOM   2876  NH1 ARG A1012      -6.233   4.272  31.760  1.00174.82           N  
ANISOU 2876  NH1 ARG A1012    20284  26925  19216   2336   1154  -2508       N  
ATOM   2877  NH2 ARG A1012      -6.129   6.262  30.625  1.00173.23           N  
ANISOU 2877  NH2 ARG A1012    20229  26340  19250   2354    835  -2733       N  
ATOM   2878  N   ARG A1013      -6.612  -1.374  29.167  1.00135.21           N  
ANISOU 2878  N   ARG A1013    15313  21740  14321   1377   2039  -1609       N  
ATOM   2879  CA  ARG A1013      -5.383  -2.168  29.094  1.00134.61           C  
ANISOU 2879  CA  ARG A1013    15342  21508  14295   1294   2089  -1493       C  
ATOM   2880  C   ARG A1013      -5.348  -2.990  27.810  1.00137.92           C  
ANISOU 2880  C   ARG A1013    15808  21745  14851   1060   2173  -1377       C  
ATOM   2881  O   ARG A1013      -4.297  -3.050  27.174  1.00136.82           O  
ANISOU 2881  O   ARG A1013    15752  21415  14818    991   2125  -1363       O  
ATOM   2882  CB  ARG A1013      -5.165  -3.080  30.315  1.00136.68           C  
ANISOU 2882  CB  ARG A1013    15619  21921  14392   1381   2217  -1379       C  
ATOM   2883  CG  ARG A1013      -3.703  -3.524  30.406  1.00150.10           C  
ANISOU 2883  CG  ARG A1013    17430  23478  16122   1394   2188  -1340       C  
ATOM   2884  CD  ARG A1013      -3.404  -4.596  31.434  1.00163.07           C  
ANISOU 2884  CD  ARG A1013    19139  25223  17597   1481   2317  -1201       C  
ATOM   2885  NE  ARG A1013      -2.027  -5.095  31.288  1.00172.79           N  
ANISOU 2885  NE  ARG A1013    20475  26304  18873   1486   2277  -1180       N  
ATOM   2886  CZ  ARG A1013      -1.212  -5.425  32.289  1.00188.71           C  
ANISOU 2886  CZ  ARG A1013    22555  28396  20748   1678   2261  -1180       C  
ATOM   2887  NH1 ARG A1013      -1.617  -5.324  33.549  1.00179.93           N  
ANISOU 2887  NH1 ARG A1013    21429  27508  19430   1889   2292  -1180       N  
ATOM   2888  NH2 ARG A1013       0.019  -5.854  32.036  1.00172.88           N  
ANISOU 2888  NH2 ARG A1013    20627  26266  18795   1682   2210  -1191       N  
ATOM   2889  N   GLN A1014      -6.481  -3.618  27.430  1.00135.01           N  
ANISOU 2889  N   GLN A1014    15370  21447  14481    943   2293  -1313       N  
ATOM   2890  CA  GLN A1014      -6.577  -4.450  26.229  1.00134.13           C  
ANISOU 2890  CA  GLN A1014    15288  21180  14495    737   2363  -1227       C  
ATOM   2891  C   GLN A1014      -6.246  -3.658  24.961  1.00136.44           C  
ANISOU 2891  C   GLN A1014    15628  21296  14918    704   2225  -1314       C  
ATOM   2892  O   GLN A1014      -5.621  -4.220  24.063  1.00134.92           O  
ANISOU 2892  O   GLN A1014    15507  20935  14821    583   2243  -1247       O  
ATOM   2893  CB  GLN A1014      -7.946  -5.114  26.118  1.00136.73           C  
ANISOU 2893  CB  GLN A1014    15500  21640  14813    627   2498  -1191       C  
ATOM   2894  CG  GLN A1014      -8.037  -6.392  26.954  1.00159.80           C  
ANISOU 2894  CG  GLN A1014    18434  24623  17659    553   2694  -1021       C  
ATOM   2895  CD  GLN A1014      -9.446  -6.798  27.326  1.00189.90           C  
ANISOU 2895  CD  GLN A1014    22093  28641  21421    475   2845  -1003       C  
ATOM   2896  OE1 GLN A1014     -10.413  -6.021  27.241  1.00188.30           O  
ANISOU 2896  OE1 GLN A1014    21743  28606  21195    531   2794  -1147       O  
ATOM   2897  NE2 GLN A1014      -9.581  -8.030  27.788  1.00185.61           N  
ANISOU 2897  NE2 GLN A1014    21581  28090  20853    348   3038   -829       N  
ATOM   2898  N   LEU A1015      -6.613  -2.352  24.910  1.00132.98           N  
ANISOU 2898  N   LEU A1015    15166  20891  14471    825   2085  -1459       N  
ATOM   2899  CA  LEU A1015      -6.291  -1.456  23.799  1.00131.83           C  
ANISOU 2899  CA  LEU A1015    15099  20563  14426    815   1956  -1527       C  
ATOM   2900  C   LEU A1015      -4.792  -1.166  23.804  1.00135.63           C  
ANISOU 2900  C   LEU A1015    15682  20878  14974    804   1901  -1510       C  
ATOM   2901  O   LEU A1015      -4.153  -1.282  22.758  1.00134.26           O  
ANISOU 2901  O   LEU A1015    15582  20533  14896    694   1901  -1461       O  
ATOM   2902  CB  LEU A1015      -7.101  -0.147  23.892  1.00132.54           C  
ANISOU 2902  CB  LEU A1015    15163  20722  14474    973   1815  -1686       C  
ATOM   2903  CG  LEU A1015      -6.746   0.937  22.874  1.00136.67           C  
ANISOU 2903  CG  LEU A1015    15812  21032  15084    990   1674  -1745       C  
ATOM   2904  CD1 LEU A1015      -7.594   0.825  21.629  1.00136.66           C  
ANISOU 2904  CD1 LEU A1015    15818  21002  15103    947   1674  -1750       C  
ATOM   2905  CD2 LEU A1015      -6.859   2.320  23.467  1.00140.11           C  
ANISOU 2905  CD2 LEU A1015    16277  21470  15486   1174   1507  -1895       C  
ATOM   2906  N   ALA A1016      -4.244  -0.806  24.987  1.00133.76           N  
ANISOU 2906  N   ALA A1016    15431  20712  14679    926   1855  -1564       N  
ATOM   2907  CA  ALA A1016      -2.837  -0.489  25.215  1.00134.02           C  
ANISOU 2907  CA  ALA A1016    15518  20630  14772    935   1792  -1594       C  
ATOM   2908  C   ALA A1016      -1.919  -1.657  24.845  1.00139.31           C  
ANISOU 2908  C   ALA A1016    16224  21228  15479    812   1896  -1472       C  
ATOM   2909  O   ALA A1016      -0.855  -1.428  24.267  1.00138.65           O  
ANISOU 2909  O   ALA A1016    16184  21003  15495    741   1859  -1485       O  
ATOM   2910  CB  ALA A1016      -2.623  -0.102  26.667  1.00135.77           C  
ANISOU 2910  CB  ALA A1016    15692  20998  14896   1121   1730  -1691       C  
ATOM   2911  N   ASP A1017      -2.341  -2.900  25.147  1.00137.56           N  
ANISOU 2911  N   ASP A1017    15986  21100  15179    782   2027  -1356       N  
ATOM   2912  CA  ASP A1017      -1.586  -4.115  24.832  1.00137.73           C  
ANISOU 2912  CA  ASP A1017    16061  21050  15220    690   2115  -1243       C  
ATOM   2913  C   ASP A1017      -1.616  -4.411  23.342  1.00142.53           C  
ANISOU 2913  C   ASP A1017    16701  21514  15938    533   2137  -1195       C  
ATOM   2914  O   ASP A1017      -0.614  -4.877  22.797  1.00141.85           O  
ANISOU 2914  O   ASP A1017    16661  21330  15904    472   2145  -1162       O  
ATOM   2915  CB  ASP A1017      -2.125  -5.319  25.618  1.00140.51           C  
ANISOU 2915  CB  ASP A1017    16416  21513  15459    703   2249  -1124       C  
ATOM   2916  CG  ASP A1017      -1.880  -5.239  27.113  1.00153.91           C  
ANISOU 2916  CG  ASP A1017    18108  23361  17011    886   2245  -1144       C  
ATOM   2917  OD1 ASP A1017      -0.756  -4.862  27.512  1.00154.54           O  
ANISOU 2917  OD1 ASP A1017    18208  23424  17087    988   2153  -1226       O  
ATOM   2918  OD2 ASP A1017      -2.799  -5.590  27.885  1.00162.73           O  
ANISOU 2918  OD2 ASP A1017    19193  24625  18010    931   2339  -1083       O  
ATOM   2919  N   LEU A1018      -2.761  -4.147  22.689  1.00140.18           N  
ANISOU 2919  N   LEU A1018    16373  21226  15662    489   2139  -1208       N  
ATOM   2920  CA  LEU A1018      -2.951  -4.350  21.250  1.00139.80           C  
ANISOU 2920  CA  LEU A1018    16353  21066  15697    378   2145  -1183       C  
ATOM   2921  C   LEU A1018      -2.133  -3.338  20.469  1.00145.07           C  
ANISOU 2921  C   LEU A1018    17082  21602  16435    371   2056  -1229       C  
ATOM   2922  O   LEU A1018      -1.505  -3.700  19.476  1.00144.18           O  
ANISOU 2922  O   LEU A1018    17015  21390  16376    288   2078  -1182       O  
ATOM   2923  CB  LEU A1018      -4.434  -4.226  20.863  1.00140.13           C  
ANISOU 2923  CB  LEU A1018    16330  21183  15727    373   2149  -1222       C  
ATOM   2924  CG  LEU A1018      -5.285  -5.496  20.737  1.00145.09           C  
ANISOU 2924  CG  LEU A1018    16898  21868  16360    275   2262  -1162       C  
ATOM   2925  CD1 LEU A1018      -6.710  -5.164  21.018  1.00146.08           C  
ANISOU 2925  CD1 LEU A1018    16908  22152  16444    311   2268  -1240       C  
ATOM   2926  CD2 LEU A1018      -5.144  -6.157  19.363  1.00147.37           C  
ANISOU 2926  CD2 LEU A1018    17226  22033  16735    173   2268  -1135       C  
ATOM   2927  N   GLU A1019      -2.122  -2.069  20.937  1.00143.59           N  
ANISOU 2927  N   GLU A1019    16899  21413  16246    458   1960  -1321       N  
ATOM   2928  CA  GLU A1019      -1.361  -0.967  20.341  1.00144.35           C  
ANISOU 2928  CA  GLU A1019    17066  21360  16420    437   1882  -1362       C  
ATOM   2929  C   GLU A1019       0.134  -1.247  20.440  1.00150.64           C  
ANISOU 2929  C   GLU A1019    17862  22102  17270    374   1906  -1347       C  
ATOM   2930  O   GLU A1019       0.871  -0.949  19.502  1.00150.11           O  
ANISOU 2930  O   GLU A1019    17843  21915  17277    281   1915  -1322       O  
ATOM   2931  CB  GLU A1019      -1.697   0.366  21.022  1.00146.55           C  
ANISOU 2931  CB  GLU A1019    17351  21637  16692    554   1762  -1480       C  
ATOM   2932  CG  GLU A1019      -1.733   1.544  20.058  1.00156.99           C  
ANISOU 2932  CG  GLU A1019    18785  22784  18079    538   1683  -1503       C  
ATOM   2933  CD  GLU A1019      -3.010   1.700  19.247  1.00177.45           C  
ANISOU 2933  CD  GLU A1019    21417  25388  20618    590   1661  -1500       C  
ATOM   2934  OE1 GLU A1019      -4.096   1.347  19.758  1.00175.36           O  
ANISOU 2934  OE1 GLU A1019    21064  25293  20272    674   1662  -1545       O  
ATOM   2935  OE2 GLU A1019      -2.928   2.213  18.108  1.00170.19           O  
ANISOU 2935  OE2 GLU A1019    20615  24319  19731    556   1643  -1461       O  
ATOM   2936  N   ASP A1020       0.566  -1.848  21.574  1.00149.39           N  
ANISOU 2936  N   ASP A1020    17649  22051  17061    436   1924  -1363       N  
ATOM   2937  CA  ASP A1020       1.947  -2.247  21.863  1.00150.19           C  
ANISOU 2937  CA  ASP A1020    17729  22149  17187    420   1934  -1381       C  
ATOM   2938  C   ASP A1020       2.409  -3.307  20.856  1.00154.62           C  
ANISOU 2938  C   ASP A1020    18316  22668  17766    318   2017  -1285       C  
ATOM   2939  O   ASP A1020       3.487  -3.167  20.279  1.00154.14           O  
ANISOU 2939  O   ASP A1020    18248  22550  17770    248   2019  -1304       O  
ATOM   2940  CB  ASP A1020       2.049  -2.790  23.307  1.00152.82           C  
ANISOU 2940  CB  ASP A1020    18022  22627  17416    560   1932  -1410       C  
ATOM   2941  CG  ASP A1020       3.433  -2.768  23.942  1.00165.22           C  
ANISOU 2941  CG  ASP A1020    19553  24226  18999    618   1883  -1505       C  
ATOM   2942  OD1 ASP A1020       4.395  -3.259  23.300  1.00166.08           O  
ANISOU 2942  OD1 ASP A1020    19658  24289  19156    539   1914  -1490       O  
ATOM   2943  OD2 ASP A1020       3.541  -2.335  25.112  1.00171.71           O  
ANISOU 2943  OD2 ASP A1020    20335  25140  19767    762   1812  -1608       O  
ATOM   2944  N   ASN A1021       1.576  -4.346  20.635  1.00151.96           N  
ANISOU 2944  N   ASN A1021    18000  22364  17376    306   2085  -1194       N  
ATOM   2945  CA  ASN A1021       1.839  -5.452  19.714  1.00151.94           C  
ANISOU 2945  CA  ASN A1021    18027  22318  17384    231   2147  -1117       C  
ATOM   2946  C   ASN A1021       1.795  -4.983  18.262  1.00157.87           C  
ANISOU 2946  C   ASN A1021    18807  22981  18198    145   2145  -1103       C  
ATOM   2947  O   ASN A1021       2.608  -5.442  17.461  1.00157.27           O  
ANISOU 2947  O   ASN A1021    18741  22872  18142     96   2171  -1081       O  
ATOM   2948  CB  ASN A1021       0.841  -6.584  19.938  1.00151.50           C  
ANISOU 2948  CB  ASN A1021    17985  22300  17280    230   2212  -1041       C  
ATOM   2949  CG  ASN A1021       0.978  -7.275  21.270  1.00171.61           C  
ANISOU 2949  CG  ASN A1021    20541  24922  19741    314   2244  -1012       C  
ATOM   2950  OD1 ASN A1021       2.082  -7.602  21.729  1.00163.66           O  
ANISOU 2950  OD1 ASN A1021    19554  23927  18702    378   2227  -1029       O  
ATOM   2951  ND2 ASN A1021      -0.153  -7.547  21.903  1.00165.08           N  
ANISOU 2951  ND2 ASN A1021    19699  24161  18862    325   2298   -968       N  
ATOM   2952  N   TRP A1022       0.855  -4.058  17.935  1.00156.30           N  
ANISOU 2952  N   TRP A1022    18625  22754  18009    151   2109  -1122       N  
ATOM   2953  CA  TRP A1022       0.688  -3.436  16.610  1.00156.91           C  
ANISOU 2953  CA  TRP A1022    18761  22742  18116    108   2097  -1104       C  
ATOM   2954  C   TRP A1022       1.930  -2.618  16.274  1.00161.58           C  
ANISOU 2954  C   TRP A1022    19377  23252  18764     50   2094  -1112       C  
ATOM   2955  O   TRP A1022       2.380  -2.621  15.124  1.00161.23           O  
ANISOU 2955  O   TRP A1022    19374  23155  18730    -11   2134  -1061       O  
ATOM   2956  CB  TRP A1022      -0.578  -2.541  16.587  1.00156.32           C  
ANISOU 2956  CB  TRP A1022    18710  22663  18019    173   2037  -1145       C  
ATOM   2957  CG  TRP A1022      -0.729  -1.633  15.391  1.00157.82           C  
ANISOU 2957  CG  TRP A1022    19001  22747  18219    172   2005  -1130       C  
ATOM   2958  CD1 TRP A1022      -0.266  -0.355  15.268  1.00161.47           C  
ANISOU 2958  CD1 TRP A1022    19543  23090  18717    166   1962  -1140       C  
ATOM   2959  CD2 TRP A1022      -1.458  -1.912  14.187  1.00157.73           C  
ANISOU 2959  CD2 TRP A1022    19032  22729  18169    194   2009  -1106       C  
ATOM   2960  NE1 TRP A1022      -0.621   0.164  14.044  1.00161.40           N  
ANISOU 2960  NE1 TRP A1022    19650  22993  18681    183   1953  -1096       N  
ATOM   2961  CE2 TRP A1022      -1.355  -0.770  13.360  1.00162.41           C  
ANISOU 2961  CE2 TRP A1022    19751  23202  18753    217   1974  -1084       C  
ATOM   2962  CE3 TRP A1022      -2.174  -3.026  13.715  1.00158.71           C  
ANISOU 2962  CE3 TRP A1022    19103  22929  18269    199   2034  -1110       C  
ATOM   2963  CZ2 TRP A1022      -1.938  -0.711  12.088  1.00162.18           C  
ANISOU 2963  CZ2 TRP A1022    19806  23151  18665    276   1962  -1061       C  
ATOM   2964  CZ3 TRP A1022      -2.760  -2.961  12.460  1.00160.58           C  
ANISOU 2964  CZ3 TRP A1022    19396  23150  18469    249   2008  -1116       C  
ATOM   2965  CH2 TRP A1022      -2.629  -1.821  11.656  1.00161.95           C  
ANISOU 2965  CH2 TRP A1022    19703  23225  18606    302   1972  -1090       C  
ATOM   2966  N   GLU A1023       2.477  -1.917  17.284  1.00158.82           N  
ANISOU 2966  N   GLU A1023    18992  22901  18450     68   2050  -1183       N  
ATOM   2967  CA  GLU A1023       3.653  -1.081  17.115  1.00159.52           C  
ANISOU 2967  CA  GLU A1023    19076  22911  18622    -12   2047  -1217       C  
ATOM   2968  C   GLU A1023       4.903  -1.940  17.007  1.00163.73           C  
ANISOU 2968  C   GLU A1023    19535  23510  19164    -63   2106  -1220       C  
ATOM   2969  O   GLU A1023       5.819  -1.548  16.296  1.00163.94           O  
ANISOU 2969  O   GLU A1023    19552  23490  19249   -167   2150  -1212       O  
ATOM   2970  CB  GLU A1023       3.780  -0.042  18.239  1.00161.73           C  
ANISOU 2970  CB  GLU A1023    19330  23167  18954     33   1957  -1329       C  
ATOM   2971  CG  GLU A1023       4.530   1.219  17.827  1.00173.95           C  
ANISOU 2971  CG  GLU A1023    20915  24561  20620    -75   1941  -1360       C  
ATOM   2972  CD  GLU A1023       4.123   1.860  16.510  1.00193.68           C  
ANISOU 2972  CD  GLU A1023    23552  26911  23126   -143   1977  -1254       C  
ATOM   2973  OE1 GLU A1023       2.927   2.198  16.353  1.00185.57           O  
ANISOU 2973  OE1 GLU A1023    22616  25851  22041    -49   1923  -1236       O  
ATOM   2974  OE2 GLU A1023       5.003   2.027  15.635  1.00188.04           O  
ANISOU 2974  OE2 GLU A1023    22855  26128  22463   -277   2060  -1194       O  
ATOM   2975  N   THR A1024       4.926  -3.125  17.659  1.00160.37           N  
ANISOU 2975  N   THR A1024    19065  23194  18673     13   2112  -1226       N  
ATOM   2976  CA  THR A1024       6.047  -4.076  17.593  1.00160.60           C  
ANISOU 2976  CA  THR A1024    19039  23297  18686     10   2146  -1243       C  
ATOM   2977  C   THR A1024       6.143  -4.643  16.162  1.00164.75           C  
ANISOU 2977  C   THR A1024    19598  23802  19197    -55   2211  -1162       C  
ATOM   2978  O   THR A1024       7.249  -4.819  15.646  1.00165.02           O  
ANISOU 2978  O   THR A1024    19578  23876  19245   -101   2247  -1186       O  
ATOM   2979  CB  THR A1024       5.886  -5.185  18.655  1.00170.01           C  
ANISOU 2979  CB  THR A1024    20226  24577  19793    133   2130  -1250       C  
ATOM   2980  OG1 THR A1024       5.758  -4.587  19.947  1.00171.63           O  
ANISOU 2980  OG1 THR A1024    20402  24823  19987    218   2070  -1327       O  
ATOM   2981  CG2 THR A1024       7.058  -6.176  18.667  1.00168.66           C  
ANISOU 2981  CG2 THR A1024    20018  24479  19588    173   2139  -1286       C  
ATOM   2982  N   LEU A1025       4.978  -4.895  15.524  1.00160.80           N  
ANISOU 2982  N   LEU A1025    19171  23260  18665    -46   2220  -1087       N  
ATOM   2983  CA  LEU A1025       4.883  -5.407  14.156  1.00160.35           C  
ANISOU 2983  CA  LEU A1025    19152  23192  18582    -73   2262  -1026       C  
ATOM   2984  C   LEU A1025       5.407  -4.376  13.150  1.00165.42           C  
ANISOU 2984  C   LEU A1025    19820  23782  19250   -154   2304   -995       C  
ATOM   2985  O   LEU A1025       6.221  -4.737  12.302  1.00165.54           O  
ANISOU 2985  O   LEU A1025    19812  23842  19244   -186   2359   -977       O  
ATOM   2986  CB  LEU A1025       3.438  -5.810  13.808  1.00159.72           C  
ANISOU 2986  CB  LEU A1025    19126  23089  18472    -33   2244   -990       C  
ATOM   2987  CG  LEU A1025       2.882  -7.058  14.502  1.00163.65           C  
ANISOU 2987  CG  LEU A1025    19609  23621  18948     10   2237   -991       C  
ATOM   2988  CD1 LEU A1025       1.379  -6.992  14.609  1.00163.64           C  
ANISOU 2988  CD1 LEU A1025    19617  23612  18946     24   2221   -988       C  
ATOM   2989  CD2 LEU A1025       3.296  -8.333  13.787  1.00165.62           C  
ANISOU 2989  CD2 LEU A1025    19869  23880  19180     20   2251   -979       C  
ATOM   2990  N   ASN A1026       4.974  -3.095  13.270  1.00162.47           N  
ANISOU 2990  N   ASN A1026    19500  23314  18916   -182   2282   -988       N  
ATOM   2991  CA  ASN A1026       5.374  -1.980  12.400  1.00163.38           C  
ANISOU 2991  CA  ASN A1026    19681  23335  19060   -268   2330   -935       C  
ATOM   2992  C   ASN A1026       6.862  -1.641  12.523  1.00169.21           C  
ANISOU 2992  C   ASN A1026    20329  24093  19872   -387   2390   -970       C  
ATOM   2993  O   ASN A1026       7.500  -1.339  11.514  1.00169.98           O  
ANISOU 2993  O   ASN A1026    20444  24175  19966   -476   2481   -904       O  
ATOM   2994  CB  ASN A1026       4.543  -0.733  12.703  1.00162.74           C  
ANISOU 2994  CB  ASN A1026    19697  23125  19011   -249   2267   -936       C  
ATOM   2995  CG  ASN A1026       3.162  -0.734  12.099  1.00179.67           C  
ANISOU 2995  CG  ASN A1026    21944  25246  21075   -145   2225   -898       C  
ATOM   2996  OD1 ASN A1026       2.588  -1.778  11.755  1.00172.27           O  
ANISOU 2996  OD1 ASN A1026    20982  24397  20077    -82   2224   -895       O  
ATOM   2997  ND2 ASN A1026       2.584   0.449  11.983  1.00171.58           N  
ANISOU 2997  ND2 ASN A1026    21038  24098  20057   -116   2176   -887       N  
ATOM   2998  N   ASP A1027       7.408  -1.689  13.751  1.00166.24           N  
ANISOU 2998  N   ASP A1027    19846  23765  19554   -381   2342  -1082       N  
ATOM   2999  CA  ASP A1027       8.813  -1.392  14.027  1.00167.41           C  
ANISOU 2999  CA  ASP A1027    19868  23958  19785   -481   2377  -1167       C  
ATOM   3000  C   ASP A1027       9.718  -2.491  13.495  1.00171.35           C  
ANISOU 3000  C   ASP A1027    20270  24610  20224   -476   2439  -1178       C  
ATOM   3001  O   ASP A1027      10.767  -2.178  12.931  1.00172.17           O  
ANISOU 3001  O   ASP A1027    20293  24754  20369   -595   2524  -1191       O  
ATOM   3002  CB  ASP A1027       9.060  -1.188  15.532  1.00169.54           C  
ANISOU 3002  CB  ASP A1027    20049  24258  20112   -426   2281  -1313       C  
ATOM   3003  CG  ASP A1027       8.432   0.056  16.145  1.00182.20           C  
ANISOU 3003  CG  ASP A1027    21717  25721  21791   -431   2205  -1345       C  
ATOM   3004  OD1 ASP A1027       8.251   1.059  15.414  1.00183.78           O  
ANISOU 3004  OD1 ASP A1027    22015  25766  22047   -533   2239  -1274       O  
ATOM   3005  OD2 ASP A1027       8.138   0.034  17.360  1.00188.84           O  
ANISOU 3005  OD2 ASP A1027    22522  26606  22624   -316   2109  -1443       O  
ATOM   3006  N   ASN A1028       9.319  -3.768  13.653  1.00166.93           N  
ANISOU 3006  N   ASN A1028    19722  24135  19571   -343   2400  -1177       N  
ATOM   3007  CA  ASN A1028      10.125  -4.888  13.177  1.00167.00           C  
ANISOU 3007  CA  ASN A1028    19658  24281  19513   -301   2430  -1205       C  
ATOM   3008  C   ASN A1028      10.067  -5.032  11.651  1.00171.62           C  
ANISOU 3008  C   ASN A1028    20293  24876  20039   -337   2513  -1104       C  
ATOM   3009  O   ASN A1028      11.006  -5.578  11.075  1.00172.03           O  
ANISOU 3009  O   ASN A1028    20260  25057  20047   -337   2560  -1137       O  
ATOM   3010  CB  ASN A1028       9.747  -6.185  13.864  1.00167.11           C  
ANISOU 3010  CB  ASN A1028    19696  24343  19455   -148   2355  -1233       C  
ATOM   3011  CG  ASN A1028      10.367  -6.315  15.234  1.00194.38           C  
ANISOU 3011  CG  ASN A1028    23072  27863  22920    -74   2290  -1355       C  
ATOM   3012  OD1 ASN A1028      11.595  -6.344  15.397  1.00190.68           O  
ANISOU 3012  OD1 ASN A1028    22478  27506  22464    -75   2291  -1469       O  
ATOM   3013  ND2 ASN A1028       9.531  -6.372  16.257  1.00186.62           N  
ANISOU 3013  ND2 ASN A1028    22152  26833  21924      4   2232  -1345       N  
ATOM   3014  N   LEU A1029       9.009  -4.503  10.996  1.00168.19           N  
ANISOU 3014  N   LEU A1029    19990  24326  19588   -349   2525   -995       N  
ATOM   3015  CA  LEU A1029       8.895  -4.513   9.536  1.00168.78           C  
ANISOU 3015  CA  LEU A1029    20131  24412  19586   -355   2598   -898       C  
ATOM   3016  C   LEU A1029       9.989  -3.642   8.928  1.00175.78           C  
ANISOU 3016  C   LEU A1029    20967  25321  20500   -501   2723   -863       C  
ATOM   3017  O   LEU A1029      10.607  -4.044   7.940  1.00176.02           O  
ANISOU 3017  O   LEU A1029    20958  25469  20451   -501   2805   -833       O  
ATOM   3018  CB  LEU A1029       7.508  -4.032   9.076  1.00168.31           C  
ANISOU 3018  CB  LEU A1029    20227  24228  19496   -308   2566   -813       C  
ATOM   3019  CG  LEU A1029       6.414  -5.097   8.988  1.00171.67           C  
ANISOU 3019  CG  LEU A1029    20690  24671  19866   -176   2484   -832       C  
ATOM   3020  CD1 LEU A1029       5.053  -4.462   8.865  1.00171.55           C  
ANISOU 3020  CD1 LEU A1029    20786  24552  19842   -130   2434   -796       C  
ATOM   3021  CD2 LEU A1029       6.641  -6.048   7.824  1.00174.27           C  
ANISOU 3021  CD2 LEU A1029    21014  25100  20102   -104   2506   -823       C  
ATOM   3022  N   LYS A1030      10.252  -2.467   9.554  1.00174.43           N  
ANISOU 3022  N   LYS A1030    20787  25041  20446   -628   2738   -875       N  
ATOM   3023  CA  LYS A1030      11.294  -1.513   9.161  1.00176.88           C  
ANISOU 3023  CA  LYS A1030    21041  25337  20829   -815   2865   -849       C  
ATOM   3024  C   LYS A1030      12.671  -2.173   9.271  1.00183.45           C  
ANISOU 3024  C   LYS A1030    21655  26380  21667   -854   2915   -968       C  
ATOM   3025  O   LYS A1030      13.504  -1.985   8.383  1.00184.73           O  
ANISOU 3025  O   LYS A1030    21752  26631  21806   -962   3055   -923       O  
ATOM   3026  CB  LYS A1030      11.240  -0.239  10.029  1.00179.78           C  
ANISOU 3026  CB  LYS A1030    21434  25524  21350   -930   2831   -883       C  
ATOM   3027  CG  LYS A1030       9.942   0.557   9.933  1.00189.10           C  
ANISOU 3027  CG  LYS A1030    22830  26497  22521   -880   2771   -784       C  
ATOM   3028  CD  LYS A1030       9.993   1.815  10.807  1.00196.73           C  
ANISOU 3028  CD  LYS A1030    23819  27284  23645   -981   2720   -842       C  
ATOM   3029  CE  LYS A1030       8.689   2.582  10.831  1.00203.29           C  
ANISOU 3029  CE  LYS A1030    24860  27924  24455   -893   2631   -778       C  
ATOM   3030  NZ  LYS A1030       8.452   3.343   9.575  1.00211.18           N  
ANISOU 3030  NZ  LYS A1030    26061  28776  25402   -945   2728   -599       N  
ATOM   3031  N   VAL A1031      12.883  -2.976  10.347  1.00180.29           N  
ANISOU 3031  N   VAL A1031    21147  26074  21280   -746   2801  -1120       N  
ATOM   3032  CA  VAL A1031      14.117  -3.724  10.632  1.00181.24           C  
ANISOU 3032  CA  VAL A1031    21067  26409  21389   -719   2802  -1273       C  
ATOM   3033  C   VAL A1031      14.381  -4.721   9.485  1.00186.45           C  
ANISOU 3033  C   VAL A1031    21713  27228  21901   -634   2857  -1232       C  
ATOM   3034  O   VAL A1031      15.520  -4.801   9.021  1.00187.50           O  
ANISOU 3034  O   VAL A1031    21686  27538  22018   -696   2947  -1295       O  
ATOM   3035  CB  VAL A1031      14.082  -4.417  12.029  1.00183.95           C  
ANISOU 3035  CB  VAL A1031    21362  26792  21737   -566   2650  -1420       C  
ATOM   3036  CG1 VAL A1031      15.331  -5.265  12.273  1.00184.55           C  
ANISOU 3036  CG1 VAL A1031    21252  27097  21771   -487   2630  -1590       C  
ATOM   3037  CG2 VAL A1031      13.916  -3.394  13.150  1.00183.94           C  
ANISOU 3037  CG2 VAL A1031    21353  26668  21868   -628   2591  -1485       C  
ATOM   3038  N   ILE A1032      13.328  -5.434   9.008  1.00182.53           N  
ANISOU 3038  N   ILE A1032    21371  26679  21305   -494   2801  -1143       N  
ATOM   3039  CA  ILE A1032      13.424  -6.407   7.907  1.00182.83           C  
ANISOU 3039  CA  ILE A1032    21416  26849  21203   -382   2822  -1119       C  
ATOM   3040  C   ILE A1032      13.722  -5.670   6.586  1.00188.92           C  
ANISOU 3040  C   ILE A1032    22200  27658  21922   -493   2986   -996       C  
ATOM   3041  O   ILE A1032      14.514  -6.169   5.783  1.00189.62           O  
ANISOU 3041  O   ILE A1032    22190  27944  21912   -459   3055  -1023       O  
ATOM   3042  CB  ILE A1032      12.171  -7.335   7.794  1.00184.37           C  
ANISOU 3042  CB  ILE A1032    21762  26958  21334   -217   2708  -1082       C  
ATOM   3043  CG1 ILE A1032      11.931  -8.106   9.108  1.00183.71           C  
ANISOU 3043  CG1 ILE A1032    21678  26834  21288   -121   2577  -1177       C  
ATOM   3044  CG2 ILE A1032      12.312  -8.332   6.621  1.00185.54           C  
ANISOU 3044  CG2 ILE A1032    21912  27238  21346    -88   2709  -1087       C  
ATOM   3045  CD1 ILE A1032      10.490  -8.484   9.382  1.00189.74           C  
ANISOU 3045  CD1 ILE A1032    22588  27446  22059    -52   2494  -1118       C  
ATOM   3046  N   GLU A1033      13.119  -4.479   6.384  1.00186.20           N  
ANISOU 3046  N   GLU A1033    21986  27133  21631   -611   3048   -862       N  
ATOM   3047  CA  GLU A1033      13.333  -3.650   5.192  1.00188.04           C  
ANISOU 3047  CA  GLU A1033    22281  27360  21808   -719   3216   -709       C  
ATOM   3048  C   GLU A1033      14.799  -3.205   5.082  1.00194.22           C  
ANISOU 3048  C   GLU A1033    22868  28286  22642   -907   3372   -749       C  
ATOM   3049  O   GLU A1033      15.383  -3.292   4.004  1.00195.42           O  
ANISOU 3049  O   GLU A1033    22975  28595  22681   -928   3514   -684       O  
ATOM   3050  CB  GLU A1033      12.406  -2.422   5.202  1.00189.66           C  
ANISOU 3050  CB  GLU A1033    22687  27304  22071   -795   3225   -572       C  
ATOM   3051  CG  GLU A1033      11.069  -2.655   4.490  1.00201.20           C  
ANISOU 3051  CG  GLU A1033    24351  28687  23408   -618   3155   -478       C  
ATOM   3052  CD  GLU A1033      10.037  -1.549   4.632  1.00227.18           C  
ANISOU 3052  CD  GLU A1033    27842  31733  26742   -636   3120   -382       C  
ATOM   3053  OE1 GLU A1033       9.937  -0.960   5.734  1.00225.03           O  
ANISOU 3053  OE1 GLU A1033    27555  31332  26614   -719   3057   -440       O  
ATOM   3054  OE2 GLU A1033       9.262  -1.342   3.667  1.00223.32           O  
ANISOU 3054  OE2 GLU A1033    27527  31195  26129   -530   3130   -270       O  
ATOM   3055  N   LYS A1034      15.388  -2.762   6.206  1.00191.10           N  
ANISOU 3055  N   LYS A1034    22339  27857  22413  -1034   3345   -874       N  
ATOM   3056  CA  LYS A1034      16.757  -2.254   6.308  1.00193.27           C  
ANISOU 3056  CA  LYS A1034    22392  28257  22784  -1239   3476   -959       C  
ATOM   3057  C   LYS A1034      17.826  -3.347   6.486  1.00197.96           C  
ANISOU 3057  C   LYS A1034    22735  29159  23320  -1141   3446  -1160       C  
ATOM   3058  O   LYS A1034      19.015  -3.063   6.299  1.00199.67           O  
ANISOU 3058  O   LYS A1034    22735  29550  23580  -1295   3578  -1239       O  
ATOM   3059  CB  LYS A1034      16.850  -1.291   7.494  1.00195.75           C  
ANISOU 3059  CB  LYS A1034    22668  28394  23312  -1389   3423  -1045       C  
ATOM   3060  CG  LYS A1034      16.081   0.008   7.300  1.00204.86           C  
ANISOU 3060  CG  LYS A1034    24044  29245  24548  -1524   3471   -868       C  
ATOM   3061  CD  LYS A1034      15.906   0.775   8.610  1.00211.10           C  
ANISOU 3061  CD  LYS A1034    24827  29849  25531  -1591   3350   -983       C  
ATOM   3062  CE  LYS A1034      17.174   1.345   9.217  1.00221.01           C  
ANISOU 3062  CE  LYS A1034    25836  31163  26976  -1805   3403  -1156       C  
ATOM   3063  NZ  LYS A1034      16.866   2.246  10.352  1.00228.73           N  
ANISOU 3063  NZ  LYS A1034    26847  31922  28137  -1860   3278  -1252       N  
ATOM   3064  N   ALA A1035      17.410  -4.560   6.902  1.00193.12           N  
ANISOU 3064  N   ALA A1035    22152  28605  22619   -893   3272  -1252       N  
ATOM   3065  CA  ALA A1035      18.268  -5.712   7.184  1.00193.39           C  
ANISOU 3065  CA  ALA A1035    22005  28895  22581   -736   3194  -1452       C  
ATOM   3066  C   ALA A1035      19.181  -6.080   6.020  1.00200.18           C  
ANISOU 3066  C   ALA A1035    22719  30029  23310   -735   3329  -1464       C  
ATOM   3067  O   ALA A1035      18.714  -6.350   4.908  1.00199.59           O  
ANISOU 3067  O   ALA A1035    22765  29973  23098   -662   3383  -1326       O  
ATOM   3068  CB  ALA A1035      17.422  -6.912   7.560  1.00191.80           C  
ANISOU 3068  CB  ALA A1035    21945  28639  22293   -478   3006  -1477       C  
ATOM   3069  N   ASP A1036      20.493  -6.082   6.300  1.00199.51           N  
ANISOU 3069  N   ASP A1036    22361  30180  23263   -803   3378  -1650       N  
ATOM   3070  CA  ASP A1036      21.551  -6.429   5.353  1.00201.88           C  
ANISOU 3070  CA  ASP A1036    22458  30804  23443   -804   3510  -1712       C  
ATOM   3071  C   ASP A1036      21.942  -7.911   5.522  1.00205.91           C  
ANISOU 3071  C   ASP A1036    22890  31538  23810   -496   3336  -1914       C  
ATOM   3072  O   ASP A1036      22.776  -8.419   4.766  1.00207.12           O  
ANISOU 3072  O   ASP A1036    22875  31992  23829   -423   3402  -2001       O  
ATOM   3073  CB  ASP A1036      22.772  -5.502   5.548  1.00206.51           C  
ANISOU 3073  CB  ASP A1036    22763  31533  24170  -1079   3674  -1819       C  
ATOM   3074  CG  ASP A1036      22.470  -4.009   5.526  1.00216.29           C  
ANISOU 3074  CG  ASP A1036    24088  32509  25585  -1397   3829  -1641       C  
ATOM   3075  OD1 ASP A1036      21.566  -3.592   4.765  1.00216.05           O  
ANISOU 3075  OD1 ASP A1036    24308  32283  25498  -1429   3905  -1385       O  
ATOM   3076  OD2 ASP A1036      23.161  -3.256   6.242  1.00223.38           O  
ANISOU 3076  OD2 ASP A1036    24802  33398  26674  -1604   3867  -1771       O  
ATOM   3077  N   ASN A1037      21.317  -8.604   6.504  1.00200.82           N  
ANISOU 3077  N   ASN A1037    22381  30741  23182   -307   3118  -1981       N  
ATOM   3078  CA  ASN A1037      21.571 -10.013   6.799  1.00200.27           C  
ANISOU 3078  CA  ASN A1037    22300  30805  22987     -4   2932  -2154       C  
ATOM   3079  C   ASN A1037      20.307 -10.732   7.348  1.00201.97           C  
ANISOU 3079  C   ASN A1037    22799  30747  23195    167   2751  -2073       C  
ATOM   3080  O   ASN A1037      19.403 -10.080   7.866  1.00200.10           O  
ANISOU 3080  O   ASN A1037    22706  30255  23069     56   2750  -1945       O  
ATOM   3081  CB  ASN A1037      22.748 -10.132   7.769  1.00202.13           C  
ANISOU 3081  CB  ASN A1037    22293  31241  23265     40   2863  -2425       C  
ATOM   3082  CG  ASN A1037      23.034 -11.539   8.191  1.00223.05           C  
ANISOU 3082  CG  ASN A1037    24964  34004  25781    374   2655  -2607       C  
ATOM   3083  OD1 ASN A1037      22.701 -11.934   9.305  1.00214.54           O  
ANISOU 3083  OD1 ASN A1037    24003  32782  24731    509   2493  -2662       O  
ATOM   3084  ND2 ASN A1037      23.500 -12.363   7.260  1.00216.40           N  
ANISOU 3084  ND2 ASN A1037    24061  33387  24775    535   2649  -2674       N  
ATOM   3085  N   ALA A1038      20.254 -12.081   7.201  1.00198.56           N  
ANISOU 3085  N   ALA A1038    22442  30371  22631    435   2603  -2154       N  
ATOM   3086  CA  ALA A1038      19.145 -12.955   7.605  1.00196.62           C  
ANISOU 3086  CA  ALA A1038    22450  29883  22372    595   2443  -2089       C  
ATOM   3087  C   ALA A1038      18.931 -13.062   9.135  1.00199.82           C  
ANISOU 3087  C   ALA A1038    22929  30138  22857    644   2323  -2141       C  
ATOM   3088  O   ALA A1038      17.790 -13.286   9.544  1.00197.79           O  
ANISOU 3088  O   ALA A1038    22879  29633  22639    661   2261  -2019       O  
ATOM   3089  CB  ALA A1038      19.336 -14.343   7.021  1.00197.76           C  
ANISOU 3089  CB  ALA A1038    22640  30132  22367    858   2319  -2186       C  
ATOM   3090  N   ALA A1039      19.998 -12.928   9.970  1.00197.66           N  
ANISOU 3090  N   ALA A1039    22478  30027  22596    680   2290  -2329       N  
ATOM   3091  CA  ALA A1039      19.894 -12.965  11.440  1.00196.91           C  
ANISOU 3091  CA  ALA A1039    22441  29825  22550    755   2178  -2393       C  
ATOM   3092  C   ALA A1039      19.060 -11.779  11.960  1.00199.51           C  
ANISOU 3092  C   ALA A1039    22830  29945  23029    537   2252  -2249       C  
ATOM   3093  O   ALA A1039      18.360 -11.923  12.965  1.00197.91           O  
ANISOU 3093  O   ALA A1039    22777  29572  22849    603   2168  -2205       O  
ATOM   3094  CB  ALA A1039      21.274 -12.959  12.079  1.00199.50           C  
ANISOU 3094  CB  ALA A1039    22535  30411  22856    848   2128  -2655       C  
ATOM   3095  N   GLN A1040      19.113 -10.627  11.248  1.00196.41           N  
ANISOU 3095  N   GLN A1040    22339  29564  22726    288   2412  -2169       N  
ATOM   3096  CA  GLN A1040      18.343  -9.409  11.541  1.00195.34           C  
ANISOU 3096  CA  GLN A1040    22268  29223  22728     80   2483  -2033       C  
ATOM   3097  C   GLN A1040      16.861  -9.628  11.183  1.00196.67           C  
ANISOU 3097  C   GLN A1040    22689  29161  22878     95   2469  -1824       C  
ATOM   3098  O   GLN A1040      15.978  -9.160  11.907  1.00195.26           O  
ANISOU 3098  O   GLN A1040    22623  28796  22770     54   2437  -1748       O  
ATOM   3099  CB  GLN A1040      18.903  -8.197  10.768  1.00198.28           C  
ANISOU 3099  CB  GLN A1040    22488  29660  23189   -180   2661  -2001       C  
ATOM   3100  CG  GLN A1040      20.336  -7.804  11.123  1.00217.22           C  
ANISOU 3100  CG  GLN A1040    24599  32287  25649   -255   2698  -2221       C  
ATOM   3101  CD  GLN A1040      20.873  -6.768  10.165  1.00239.57           C  
ANISOU 3101  CD  GLN A1040    27292  35179  28555   -531   2907  -2157       C  
ATOM   3102  OE1 GLN A1040      21.336  -7.083   9.063  1.00235.95           O  
ANISOU 3102  OE1 GLN A1040    26759  34898  27994   -539   3014  -2129       O  
ATOM   3103  NE2 GLN A1040      20.822  -5.506  10.564  1.00233.30           N  
ANISOU 3103  NE2 GLN A1040    26470  34236  27936   -759   2972  -2130       N  
ATOM   3104  N   VAL A1041      16.605 -10.343  10.058  1.00192.21           N  
ANISOU 3104  N   VAL A1041    22191  28628  22211    165   2485  -1756       N  
ATOM   3105  CA  VAL A1041      15.283 -10.706   9.528  1.00190.08           C  
ANISOU 3105  CA  VAL A1041    22125  28180  21915    199   2461  -1601       C  
ATOM   3106  C   VAL A1041      14.629 -11.734  10.476  1.00191.57           C  
ANISOU 3106  C   VAL A1041    22455  28242  22090    358   2317  -1619       C  
ATOM   3107  O   VAL A1041      13.461 -11.570  10.832  1.00189.92           O  
ANISOU 3107  O   VAL A1041    22382  27847  21933    321   2300  -1510       O  
ATOM   3108  CB  VAL A1041      15.387 -11.241   8.063  1.00194.51           C  
ANISOU 3108  CB  VAL A1041    22688  28853  22365    260   2501  -1573       C  
ATOM   3109  CG1 VAL A1041      14.036 -11.695   7.523  1.00193.06           C  
ANISOU 3109  CG1 VAL A1041    22694  28499  22161    317   2451  -1457       C  
ATOM   3110  CG2 VAL A1041      16.002 -10.205   7.130  1.00195.78           C  
ANISOU 3110  CG2 VAL A1041    22729  29139  22521     96   2674  -1521       C  
ATOM   3111  N   LYS A1042      15.397 -12.768  10.898  1.00187.67           N  
ANISOU 3111  N   LYS A1042    21931  27855  21520    539   2219  -1756       N  
ATOM   3112  CA  LYS A1042      14.963 -13.844  11.797  1.00186.34           C  
ANISOU 3112  CA  LYS A1042    21916  27566  21318    705   2091  -1767       C  
ATOM   3113  C   LYS A1042      14.553 -13.295  13.173  1.00188.10           C  
ANISOU 3113  C   LYS A1042    22181  27682  21606    667   2078  -1738       C  
ATOM   3114  O   LYS A1042      13.496 -13.672  13.684  1.00186.91           O  
ANISOU 3114  O   LYS A1042    22193  27354  21469    685   2047  -1634       O  
ATOM   3115  CB  LYS A1042      16.065 -14.907  11.956  1.00190.07           C  
ANISOU 3115  CB  LYS A1042    22347  28191  21680    925   1987  -1936       C  
ATOM   3116  CG  LYS A1042      15.518 -16.326  12.039  1.00203.03           C  
ANISOU 3116  CG  LYS A1042    24199  29683  23261   1102   1867  -1910       C  
ATOM   3117  CD  LYS A1042      16.084 -17.119  13.213  1.00212.99           C  
ANISOU 3117  CD  LYS A1042    25536  30947  24445   1316   1746  -2010       C  
ATOM   3118  CE  LYS A1042      15.169 -18.258  13.596  1.00222.14           C  
ANISOU 3118  CE  LYS A1042    26961  31853  25590   1412   1666  -1906       C  
ATOM   3119  NZ  LYS A1042      15.833 -19.230  14.506  1.00231.66           N  
ANISOU 3119  NZ  LYS A1042    28282  33057  26681   1670   1537  -2001       N  
ATOM   3120  N   ASP A1043      15.374 -12.388  13.746  1.00184.06           N  
ANISOU 3120  N   ASP A1043    21510  27288  21136    611   2105  -1839       N  
ATOM   3121  CA  ASP A1043      15.136 -11.759  15.048  1.00183.04           C  
ANISOU 3121  CA  ASP A1043    21390  27096  21060    598   2080  -1850       C  
ATOM   3122  C   ASP A1043      13.893 -10.868  15.021  1.00184.50           C  
ANISOU 3122  C   ASP A1043    21658  27106  21337    433   2144  -1692       C  
ATOM   3123  O   ASP A1043      13.134 -10.876  15.990  1.00183.67           O  
ANISOU 3123  O   ASP A1043    21654  26897  21236    476   2107  -1640       O  
ATOM   3124  CB  ASP A1043      16.364 -10.949  15.496  1.00186.10           C  
ANISOU 3124  CB  ASP A1043    21557  27661  21493    564   2085  -2033       C  
ATOM   3125  CG  ASP A1043      16.189 -10.201  16.806  1.00195.23           C  
ANISOU 3125  CG  ASP A1043    22701  28769  22708    565   2043  -2078       C  
ATOM   3126  OD1 ASP A1043      16.094 -10.865  17.862  1.00195.68           O  
ANISOU 3126  OD1 ASP A1043    22853  28816  22679    763   1946  -2113       O  
ATOM   3127  OD2 ASP A1043      16.150  -8.954  16.774  1.00200.97           O  
ANISOU 3127  OD2 ASP A1043    23338  29463  23559    381   2105  -2078       O  
ATOM   3128  N   ALA A1044      13.684 -10.112  13.928  1.00179.68           N  
ANISOU 3128  N   ALA A1044    21011  26476  20783    266   2240  -1617       N  
ATOM   3129  CA  ALA A1044      12.529  -9.225  13.787  1.00178.02           C  
ANISOU 3129  CA  ALA A1044    20885  26108  20645    136   2288  -1482       C  
ATOM   3130  C   ALA A1044      11.227 -10.015  13.602  1.00179.23           C  
ANISOU 3130  C   ALA A1044    21206  26132  20763    193   2258  -1366       C  
ATOM   3131  O   ALA A1044      10.205  -9.634  14.175  1.00178.08           O  
ANISOU 3131  O   ALA A1044    21135  25875  20654    164   2250  -1298       O  
ATOM   3132  CB  ALA A1044      12.736  -8.277  12.623  1.00179.30           C  
ANISOU 3132  CB  ALA A1044    20992  26282  20852    -27   2396  -1429       C  
ATOM   3133  N   LEU A1045      11.277 -11.127  12.836  1.00174.62           N  
ANISOU 3133  N   LEU A1045    20665  25572  20111    276   2236  -1362       N  
ATOM   3134  CA  LEU A1045      10.125 -11.992  12.577  1.00173.17           C  
ANISOU 3134  CA  LEU A1045    20620  25263  19915    318   2201  -1282       C  
ATOM   3135  C   LEU A1045       9.670 -12.732  13.835  1.00176.28           C  
ANISOU 3135  C   LEU A1045    21110  25570  20298    401   2144  -1267       C  
ATOM   3136  O   LEU A1045       8.464 -12.819  14.054  1.00175.35           O  
ANISOU 3136  O   LEU A1045    21077  25334  20216    358   2153  -1182       O  
ATOM   3137  CB  LEU A1045      10.415 -12.994  11.456  1.00173.47           C  
ANISOU 3137  CB  LEU A1045    20673  25347  19892    400   2173  -1313       C  
ATOM   3138  CG  LEU A1045      10.337 -12.467  10.027  1.00177.99           C  
ANISOU 3138  CG  LEU A1045    21206  25972  20450    337   2235  -1279       C  
ATOM   3139  CD1 LEU A1045      11.075 -13.382   9.082  1.00178.92           C  
ANISOU 3139  CD1 LEU A1045    21292  26209  20480    454   2202  -1356       C  
ATOM   3140  CD2 LEU A1045       8.896 -12.281   9.573  1.00179.33           C  
ANISOU 3140  CD2 LEU A1045    21470  26009  20659    287   2238  -1189       C  
ATOM   3141  N   THR A1046      10.612 -13.255  14.661  1.00173.02           N  
ANISOU 3141  N   THR A1046    20686  25227  19827    527   2091  -1352       N  
ATOM   3142  CA  THR A1046      10.282 -13.955  15.915  1.00172.85           C  
ANISOU 3142  CA  THR A1046    20783  25128  19763    632   2048  -1322       C  
ATOM   3143  C   THR A1046       9.570 -12.992  16.877  1.00175.40           C  
ANISOU 3143  C   THR A1046    21098  25420  20126    563   2086  -1269       C  
ATOM   3144  O   THR A1046       8.578 -13.377  17.500  1.00174.47           O  
ANISOU 3144  O   THR A1046    21088  25201  20003    565   2100  -1173       O  
ATOM   3145  CB  THR A1046      11.523 -14.596  16.571  1.00183.09           C  
ANISOU 3145  CB  THR A1046    22075  26528  20964    821   1971  -1441       C  
ATOM   3146  OG1 THR A1046      12.606 -13.666  16.587  1.00184.14           O  
ANISOU 3146  OG1 THR A1046    22022  26834  21108    804   1976  -1573       O  
ATOM   3147  CG2 THR A1046      11.946 -15.888  15.893  1.00182.25           C  
ANISOU 3147  CG2 THR A1046    22044  26408  20795    944   1905  -1479       C  
ATOM   3148  N   LYS A1047      10.051 -11.730  16.948  1.00171.77           N  
ANISOU 3148  N   LYS A1047    20506  25046  19714    493   2105  -1335       N  
ATOM   3149  CA  LYS A1047       9.471 -10.651  17.755  1.00171.25           C  
ANISOU 3149  CA  LYS A1047    20416  24958  19692    438   2121  -1317       C  
ATOM   3150  C   LYS A1047       8.072 -10.297  17.248  1.00174.84           C  
ANISOU 3150  C   LYS A1047    20928  25304  20200    323   2169  -1201       C  
ATOM   3151  O   LYS A1047       7.200  -9.961  18.048  1.00174.09           O  
ANISOU 3151  O   LYS A1047    20866  25175  20105    324   2174  -1158       O  
ATOM   3152  CB  LYS A1047      10.365  -9.406  17.728  1.00173.84           C  
ANISOU 3152  CB  LYS A1047    20594  25370  20086    369   2123  -1428       C  
ATOM   3153  CG  LYS A1047      11.621  -9.501  18.576  1.00184.64           C  
ANISOU 3153  CG  LYS A1047    21869  26871  21415    492   2061  -1587       C  
ATOM   3154  CD  LYS A1047      12.448  -8.244  18.402  1.00192.29           C  
ANISOU 3154  CD  LYS A1047    22668  27905  22489    372   2076  -1705       C  
ATOM   3155  CE  LYS A1047      13.772  -8.315  19.113  1.00199.93           C  
ANISOU 3155  CE  LYS A1047    23496  29033  23434    485   2008  -1906       C  
ATOM   3156  NZ  LYS A1047      14.574  -7.087  18.878  1.00206.72           N  
ANISOU 3156  NZ  LYS A1047    24171  29943  24429    325   2036  -2030       N  
ATOM   3157  N   MET A1048       7.868 -10.371  15.916  1.00171.80           N  
ANISOU 3157  N   MET A1048    20545  24888  19844    245   2198  -1166       N  
ATOM   3158  CA  MET A1048       6.587 -10.122  15.253  1.00171.46           C  
ANISOU 3158  CA  MET A1048    20548  24760  19839    165   2225  -1085       C  
ATOM   3159  C   MET A1048       5.611 -11.260  15.527  1.00175.92           C  
ANISOU 3159  C   MET A1048    21201  25250  20389    195   2220  -1026       C  
ATOM   3160  O   MET A1048       4.419 -11.003  15.702  1.00175.32           O  
ANISOU 3160  O   MET A1048    21143  25130  20342    146   2239   -980       O  
ATOM   3161  CB  MET A1048       6.777  -9.961  13.740  1.00173.90           C  
ANISOU 3161  CB  MET A1048    20839  25078  20156    114   2250  -1078       C  
ATOM   3162  CG  MET A1048       7.142  -8.564  13.328  1.00177.90           C  
ANISOU 3162  CG  MET A1048    21294  25601  20699     28   2289  -1082       C  
ATOM   3163  SD  MET A1048       7.525  -8.437  11.564  1.00182.55           S  
ANISOU 3163  SD  MET A1048    21879  26226  21257    -10   2343  -1051       S  
ATOM   3164  CE  MET A1048       5.882  -8.303  10.891  1.00178.67           C  
ANISOU 3164  CE  MET A1048    21486  25639  20763     -4   2326   -983       C  
ATOM   3165  N   ARG A1049       6.118 -12.518  15.552  1.00173.35           N  
ANISOU 3165  N   ARG A1049    20932  24910  20024    272   2193  -1034       N  
ATOM   3166  CA  ARG A1049       5.333 -13.727  15.813  1.00173.79           C  
ANISOU 3166  CA  ARG A1049    21092  24859  20081    285   2192   -973       C  
ATOM   3167  C   ARG A1049       4.785 -13.693  17.242  1.00179.43           C  
ANISOU 3167  C   ARG A1049    21850  25559  20767    300   2227   -912       C  
ATOM   3168  O   ARG A1049       3.601 -13.968  17.442  1.00179.38           O  
ANISOU 3168  O   ARG A1049    21875  25486  20795    229   2272   -843       O  
ATOM   3169  CB  ARG A1049       6.172 -14.995  15.576  1.00173.80           C  
ANISOU 3169  CB  ARG A1049    21167  24831  20038    389   2138  -1006       C  
ATOM   3170  CG  ARG A1049       5.320 -16.235  15.356  1.00181.55           C  
ANISOU 3170  CG  ARG A1049    22262  25660  21061    365   2130   -953       C  
ATOM   3171  CD  ARG A1049       6.110 -17.517  15.492  1.00188.16           C  
ANISOU 3171  CD  ARG A1049    23219  26432  21843    496   2064   -975       C  
ATOM   3172  NE  ARG A1049       5.220 -18.670  15.609  1.00193.04           N  
ANISOU 3172  NE  ARG A1049    23972  26856  22518    450   2070   -903       N  
ATOM   3173  CZ  ARG A1049       5.620 -19.936  15.669  1.00206.22           C  
ANISOU 3173  CZ  ARG A1049    25793  28398  24162    548   2006   -904       C  
ATOM   3174  NH1 ARG A1049       6.913 -20.235  15.613  1.00193.53           N  
ANISOU 3174  NH1 ARG A1049    24212  26865  22456    726   1921   -990       N  
ATOM   3175  NH2 ARG A1049       4.732 -20.912  15.776  1.00192.78           N  
ANISOU 3175  NH2 ARG A1049    24217  26492  22541    467   2025   -831       N  
ATOM   3176  N   ALA A1050       5.636 -13.313  18.221  1.00177.04           N  
ANISOU 3176  N   ALA A1050    21532  25338  20397    398   2208   -949       N  
ATOM   3177  CA  ALA A1050       5.272 -13.178  19.634  1.00177.51           C  
ANISOU 3177  CA  ALA A1050    21629  25422  20396    456   2235   -904       C  
ATOM   3178  C   ALA A1050       4.233 -12.072  19.821  1.00181.17           C  
ANISOU 3178  C   ALA A1050    22017  25917  20903    367   2272   -888       C  
ATOM   3179  O   ALA A1050       3.308 -12.245  20.611  1.00181.20           O  
ANISOU 3179  O   ALA A1050    22055  25915  20876    361   2325   -814       O  
ATOM   3180  CB  ALA A1050       6.508 -12.884  20.469  1.00178.72           C  
ANISOU 3180  CB  ALA A1050    21755  25681  20468    605   2179   -995       C  
ATOM   3181  N   ALA A1051       4.371 -10.958  19.069  1.00177.37           N  
ANISOU 3181  N   ALA A1051    21440  25466  20486    302   2249   -954       N  
ATOM   3182  CA  ALA A1051       3.455  -9.816  19.100  1.00177.00           C  
ANISOU 3182  CA  ALA A1051    21337  25436  20477    242   2258   -960       C  
ATOM   3183  C   ALA A1051       2.097 -10.170  18.485  1.00181.15           C  
ANISOU 3183  C   ALA A1051    21876  25910  21045    155   2298   -903       C  
ATOM   3184  O   ALA A1051       1.067  -9.795  19.045  1.00181.14           O  
ANISOU 3184  O   ALA A1051    21848  25943  21034    143   2322   -887       O  
ATOM   3185  CB  ALA A1051       4.068  -8.630  18.374  1.00177.35           C  
ANISOU 3185  CB  ALA A1051    21317  25489  20578    199   2223  -1031       C  
ATOM   3186  N   ALA A1052       2.094 -10.901  17.351  1.00177.62           N  
ANISOU 3186  N   ALA A1052    21453  25397  20637    107   2296   -893       N  
ATOM   3187  CA  ALA A1052       0.871 -11.314  16.655  1.00177.63           C  
ANISOU 3187  CA  ALA A1052    21447  25352  20691     30   2315   -877       C  
ATOM   3188  C   ALA A1052       0.044 -12.308  17.492  1.00182.54           C  
ANISOU 3188  C   ALA A1052    22103  25941  21314     -5   2377   -810       C  
ATOM   3189  O   ALA A1052      -1.169 -12.131  17.606  1.00182.52           O  
ANISOU 3189  O   ALA A1052    22043  25965  21341    -67   2413   -810       O  
ATOM   3190  CB  ALA A1052       1.214 -11.919  15.302  1.00178.25           C  
ANISOU 3190  CB  ALA A1052    21545  25378  20803     18   2282   -904       C  
ATOM   3191  N   LEU A1053       0.701 -13.324  18.094  1.00179.78           N  
ANISOU 3191  N   LEU A1053    21846  25537  20924     40   2394   -755       N  
ATOM   3192  CA  LEU A1053       0.067 -14.353  18.928  1.00180.88           C  
ANISOU 3192  CA  LEU A1053    22059  25613  21054      2   2471   -659       C  
ATOM   3193  C   LEU A1053      -0.497 -13.774  20.227  1.00185.33           C  
ANISOU 3193  C   LEU A1053    22591  26281  21544     25   2540   -610       C  
ATOM   3194  O   LEU A1053      -1.528 -14.251  20.704  1.00185.79           O  
ANISOU 3194  O   LEU A1053    22647  26329  21615    -60   2634   -539       O  
ATOM   3195  CB  LEU A1053       1.059 -15.480  19.246  1.00181.62           C  
ANISOU 3195  CB  LEU A1053    22299  25612  21096     88   2454   -611       C  
ATOM   3196  CG  LEU A1053       1.346 -16.455  18.105  1.00186.42           C  
ANISOU 3196  CG  LEU A1053    22962  26095  21776     65   2397   -646       C  
ATOM   3197  CD1 LEU A1053       2.690 -17.124  18.288  1.00186.96           C  
ANISOU 3197  CD1 LEU A1053    23144  26129  21762    214   2332   -656       C  
ATOM   3198  CD2 LEU A1053       0.242 -17.496  17.971  1.00190.08           C  
ANISOU 3198  CD2 LEU A1053    23473  26413  22337    -71   2453   -587       C  
ATOM   3199  N   ASP A1054       0.179 -12.749  20.789  1.00181.54           N  
ANISOU 3199  N   ASP A1054    22077  25909  20991    136   2495   -659       N  
ATOM   3200  CA  ASP A1054      -0.227 -12.042  22.005  1.00181.93           C  
ANISOU 3200  CA  ASP A1054    22087  26082  20955    202   2529   -647       C  
ATOM   3201  C   ASP A1054      -1.459 -11.191  21.713  1.00186.33           C  
ANISOU 3201  C   ASP A1054    22523  26713  21562    125   2542   -695       C  
ATOM   3202  O   ASP A1054      -2.409 -11.216  22.496  1.00186.90           O  
ANISOU 3202  O   ASP A1054    22557  26869  21588    110   2621   -652       O  
ATOM   3203  CB  ASP A1054       0.938 -11.171  22.524  1.00183.17           C  
ANISOU 3203  CB  ASP A1054    22230  26318  21050    346   2444   -731       C  
ATOM   3204  CG  ASP A1054       0.767 -10.483  23.876  1.00192.82           C  
ANISOU 3204  CG  ASP A1054    23422  27675  22163    467   2449   -746       C  
ATOM   3205  OD1 ASP A1054      -0.210 -10.800  24.594  1.00194.30           O  
ANISOU 3205  OD1 ASP A1054    23617  27918  22290    457   2542   -662       O  
ATOM   3206  OD2 ASP A1054       1.615  -9.627  24.220  1.00197.82           O  
ANISOU 3206  OD2 ASP A1054    24016  28369  22776    571   2361   -852       O  
ATOM   3207  N   ALA A1055      -1.455 -10.463  20.573  1.00182.45           N  
ANISOU 3207  N   ALA A1055    21975  26199  21149     88   2467   -783       N  
ATOM   3208  CA  ALA A1055      -2.563  -9.614  20.132  1.00182.56           C  
ANISOU 3208  CA  ALA A1055    21892  26272  21199     50   2450   -850       C  
ATOM   3209  C   ALA A1055      -3.766 -10.454  19.677  1.00188.65           C  
ANISOU 3209  C   ALA A1055    22616  27027  22033    -70   2516   -832       C  
ATOM   3210  O   ALA A1055      -4.888  -9.945  19.664  1.00188.69           O  
ANISOU 3210  O   ALA A1055    22520  27127  22045    -89   2523   -891       O  
ATOM   3211  CB  ALA A1055      -2.110  -8.693  19.015  1.00182.25           C  
ANISOU 3211  CB  ALA A1055    21850  26191  21208     63   2357   -927       C  
ATOM   3212  N   GLN A1056      -3.530 -11.739  19.322  1.00186.65           N  
ANISOU 3212  N   GLN A1056    22431  26657  21831   -144   2555   -771       N  
ATOM   3213  CA  GLN A1056      -4.555 -12.708  18.913  1.00188.01           C  
ANISOU 3213  CA  GLN A1056    22563  26778  22094   -281   2616   -763       C  
ATOM   3214  C   GLN A1056      -5.423 -13.090  20.124  1.00194.73           C  
ANISOU 3214  C   GLN A1056    23377  27702  22908   -344   2750   -682       C  
ATOM   3215  O   GLN A1056      -6.628 -13.317  19.976  1.00195.53           O  
ANISOU 3215  O   GLN A1056    23364  27851  23078   -462   2810   -718       O  
ATOM   3216  CB  GLN A1056      -3.888 -13.956  18.300  1.00189.50           C  
ANISOU 3216  CB  GLN A1056    22861  26795  22344   -322   2602   -724       C  
ATOM   3217  CG  GLN A1056      -4.853 -14.956  17.665  1.00205.20           C  
ANISOU 3217  CG  GLN A1056    24809  28696  24464   -471   2635   -751       C  
ATOM   3218  CD  GLN A1056      -4.149 -16.174  17.112  1.00224.11           C  
ANISOU 3218  CD  GLN A1056    27329  30905  26916   -486   2599   -725       C  
ATOM   3219  OE1 GLN A1056      -3.463 -16.917  17.827  1.00219.77           O  
ANISOU 3219  OE1 GLN A1056    26922  30260  26319   -457   2636   -616       O  
ATOM   3220  NE2 GLN A1056      -4.347 -16.434  15.827  1.00216.22           N  
ANISOU 3220  NE2 GLN A1056    26287  29856  26010   -509   2515   -837       N  
ATOM   3221  N   LYS A1057      -4.802 -13.139  21.321  1.00192.31           N  
ANISOU 3221  N   LYS A1057    23160  27425  22486   -257   2799   -582       N  
ATOM   3222  CA  LYS A1057      -5.443 -13.479  22.594  1.00194.06           C  
ANISOU 3222  CA  LYS A1057    23377  27731  22627   -282   2942   -474       C  
ATOM   3223  C   LYS A1057      -6.411 -12.379  23.086  1.00199.09           C  
ANISOU 3223  C   LYS A1057    23848  28590  23205   -247   2958   -552       C  
ATOM   3224  O   LYS A1057      -7.335 -12.688  23.843  1.00200.30           O  
ANISOU 3224  O   LYS A1057    23935  28848  23321   -317   3096   -491       O  
ATOM   3225  CB  LYS A1057      -4.376 -13.754  23.664  1.00196.66           C  
ANISOU 3225  CB  LYS A1057    23864  28042  22815   -139   2960   -365       C  
ATOM   3226  CG  LYS A1057      -3.567 -15.020  23.413  1.00208.64           C  
ANISOU 3226  CG  LYS A1057    25561  29351  24361   -157   2961   -275       C  
ATOM   3227  CD  LYS A1057      -2.256 -15.020  24.185  1.00216.57           C  
ANISOU 3227  CD  LYS A1057    26704  30359  25223     47   2909   -238       C  
ATOM   3228  CE  LYS A1057      -1.408 -16.218  23.836  1.00226.35           C  
ANISOU 3228  CE  LYS A1057    28122  31400  26481     65   2879   -181       C  
ATOM   3229  NZ  LYS A1057      -0.053 -16.120  24.433  1.00234.57           N  
ANISOU 3229  NZ  LYS A1057    29267  32475  27385    290   2795   -199       N  
ATOM   3230  N   ALA A1058      -6.203 -11.113  22.650  1.00194.90           N  
ANISOU 3230  N   ALA A1058    23257  28129  22666   -138   2822   -686       N  
ATOM   3231  CA  ALA A1058      -7.001  -9.936  23.022  1.00195.13           C  
ANISOU 3231  CA  ALA A1058    23152  28352  22635    -59   2790   -790       C  
ATOM   3232  C   ALA A1058      -8.488 -10.067  22.647  1.00200.46           C  
ANISOU 3232  C   ALA A1058    23662  29131  23374   -178   2850   -860       C  
ATOM   3233  O   ALA A1058      -8.819 -10.583  21.579  1.00199.95           O  
ANISOU 3233  O   ALA A1058    23569  28970  23434   -295   2835   -904       O  
ATOM   3234  CB  ALA A1058      -6.419  -8.686  22.380  1.00194.33           C  
ANISOU 3234  CB  ALA A1058    23063  28228  22546     57   2623   -911       C  
ATOM   3235  N   THR A1059      -9.371  -9.581  23.537  1.00198.51           N  
ANISOU 3235  N   THR A1059    23290  29101  23032   -132   2910   -893       N  
ATOM   3236  CA  THR A1059     -10.835  -9.620  23.409  1.00199.93           C  
ANISOU 3236  CA  THR A1059    23270  29448  23248   -227   2979   -984       C  
ATOM   3237  C   THR A1059     -11.454  -8.246  23.788  1.00203.53           C  
ANISOU 3237  C   THR A1059    23601  30135  23595    -49   2887  -1138       C  
ATOM   3238  O   THR A1059     -11.055  -7.685  24.811  1.00203.21           O  
ANISOU 3238  O   THR A1059    23602  30189  23421     99   2878  -1108       O  
ATOM   3239  CB  THR A1059     -11.409 -10.741  24.321  1.00211.38           C  
ANISOU 3239  CB  THR A1059    24679  30957  24677   -385   3207   -837       C  
ATOM   3240  OG1 THR A1059     -10.529 -11.870  24.347  1.00211.42           O  
ANISOU 3240  OG1 THR A1059    24874  30730  24727   -473   3273   -663       O  
ATOM   3241  CG2 THR A1059     -12.813 -11.182  23.914  1.00211.72           C  
ANISOU 3241  CG2 THR A1059    24507  31109  24828   -572   3303   -926       C  
ATOM   3242  N   PRO A1060     -12.444  -7.700  23.028  1.00199.79           N  
ANISOU 3242  N   PRO A1060    22979  29765  23166    -37   2808  -1319       N  
ATOM   3243  CA  PRO A1060     -13.054  -6.414  23.429  1.00199.65           C  
ANISOU 3243  CA  PRO A1060    22859  29966  23033    159   2706  -1476       C  
ATOM   3244  C   PRO A1060     -14.018  -6.583  24.619  1.00204.69           C  
ANISOU 3244  C   PRO A1060    23317  30895  23561    149   2861  -1474       C  
ATOM   3245  O   PRO A1060     -14.415  -7.720  24.896  1.00205.72           O  
ANISOU 3245  O   PRO A1060    23381  31046  23736    -53   3057  -1363       O  
ATOM   3246  CB  PRO A1060     -13.802  -5.957  22.161  1.00201.34           C  
ANISOU 3246  CB  PRO A1060    22987  30189  23323    183   2575  -1667       C  
ATOM   3247  CG  PRO A1060     -13.455  -6.951  21.085  1.00205.23           C  
ANISOU 3247  CG  PRO A1060    23545  30464  23969     11   2599  -1608       C  
ATOM   3248  CD  PRO A1060     -13.060  -8.205  21.787  1.00201.45           C  
ANISOU 3248  CD  PRO A1060    23109  29910  23522   -168   2787  -1411       C  
ATOM   3249  N   PRO A1061     -14.422  -5.504  25.343  1.00200.95           N  
ANISOU 3249  N   PRO A1061    22763  30649  22941    359   2786  -1593       N  
ATOM   3250  CA  PRO A1061     -15.338  -5.692  26.485  1.00204.52           C  
ANISOU 3250  CA  PRO A1061    23030  31416  23265    358   2950  -1588       C  
ATOM   3251  C   PRO A1061     -16.765  -6.020  26.048  1.00206.13           C  
ANISOU 3251  C   PRO A1061    22970  31822  23528    226   3032  -1725       C  
ATOM   3252  O   PRO A1061     -17.290  -7.075  26.394  1.00160.76           O  
ANISOU 3252  O   PRO A1061    17112  26149  17820      5   3259  -1620       O  
ATOM   3253  CB  PRO A1061     -15.280  -4.344  27.205  1.00206.00           C  
ANISOU 3253  CB  PRO A1061    23215  31770  23285    657   2795  -1718       C  
ATOM   3254  CG  PRO A1061     -14.991  -3.366  26.128  1.00208.30           C  
ANISOU 3254  CG  PRO A1061    23603  31890  23654    777   2547  -1869       C  
ATOM   3255  CD  PRO A1061     -14.054  -4.080  25.186  1.00201.76           C  
ANISOU 3255  CD  PRO A1061    22946  30728  22984    606   2554  -1734       C  
ATOM   3256  N   SER A1070     -17.902 -16.108  19.106  1.00244.39           N  
ANISOU 3256  N   SER A1070    27716  34952  30189  -1892   3513  -1625       N  
ATOM   3257  CA  SER A1070     -18.422 -14.878  18.512  1.00243.17           C  
ANISOU 3257  CA  SER A1070    27394  35051  29948  -1663   3332  -1882       C  
ATOM   3258  C   SER A1070     -17.941 -14.722  17.055  1.00244.94           C  
ANISOU 3258  C   SER A1070    27711  35126  30230  -1510   3085  -2033       C  
ATOM   3259  O   SER A1070     -16.771 -15.006  16.787  1.00242.37           O  
ANISOU 3259  O   SER A1070    27646  34552  29891  -1453   3027  -1882       O  
ATOM   3260  CB  SER A1070     -18.002 -13.669  19.342  1.00244.90           C  
ANISOU 3260  CB  SER A1070    27699  35437  29916  -1416   3307  -1795       C  
ATOM   3261  OG  SER A1070     -18.607 -12.475  18.872  1.00253.11           O  
ANISOU 3261  OG  SER A1070    28588  36716  30867  -1195   3140  -2040       O  
ATOM   3262  N   PRO A1071     -18.805 -14.262  16.106  1.00241.88           N  
ANISOU 3262  N   PRO A1071    27114  34904  29886  -1418   2936  -2334       N  
ATOM   3263  CA  PRO A1071     -18.358 -14.111  14.704  1.00239.89           C  
ANISOU 3263  CA  PRO A1071    26962  34526  29657  -1245   2708  -2468       C  
ATOM   3264  C   PRO A1071     -17.340 -12.985  14.505  1.00240.26           C  
ANISOU 3264  C   PRO A1071    27249  34538  29499   -951   2569  -2375       C  
ATOM   3265  O   PRO A1071     -16.564 -13.036  13.549  1.00238.43           O  
ANISOU 3265  O   PRO A1071    27185  34138  29269   -841   2438  -2370       O  
ATOM   3266  CB  PRO A1071     -19.654 -13.814  13.937  1.00243.44           C  
ANISOU 3266  CB  PRO A1071    27114  35213  30168  -1193   2598  -2819       C  
ATOM   3267  CG  PRO A1071     -20.769 -14.143  14.882  1.00250.24           C  
ANISOU 3267  CG  PRO A1071    27757  36185  31137  -1375   2769  -2779       C  
ATOM   3268  CD  PRO A1071     -20.226 -13.886  16.247  1.00245.67           C  
ANISOU 3268  CD  PRO A1071    27251  35710  30380  -1448   2965  -2578       C  
ATOM   3269  N   GLU A1072     -17.347 -11.975  15.401  1.00236.30           N  
ANISOU 3269  N   GLU A1072    26758  34198  28827   -827   2600  -2310       N  
ATOM   3270  CA  GLU A1072     -16.410 -10.844  15.387  1.00233.68           C  
ANISOU 3270  CA  GLU A1072    26644  33825  28318   -578   2485  -2220       C  
ATOM   3271  C   GLU A1072     -15.024 -11.312  15.848  1.00235.60           C  
ANISOU 3271  C   GLU A1072    27138  33830  28549   -636   2558  -1948       C  
ATOM   3272  O   GLU A1072     -14.008 -10.854  15.321  1.00233.32           O  
ANISOU 3272  O   GLU A1072    27046  33409  28197   -494   2451  -1885       O  
ATOM   3273  CB  GLU A1072     -16.917  -9.698  16.287  1.00235.35           C  
ANISOU 3273  CB  GLU A1072    26772  34279  28372   -437   2488  -2261       C  
ATOM   3274  CG  GLU A1072     -18.256  -9.102  15.873  1.00247.14           C  
ANISOU 3274  CG  GLU A1072    28021  36038  29843   -326   2393  -2552       C  
ATOM   3275  CD  GLU A1072     -18.260  -8.055  14.773  1.00258.91           C  
ANISOU 3275  CD  GLU A1072    29902  37048  31425     39   2127  -2396       C  
ATOM   3276  OE1 GLU A1072     -17.253  -7.931  14.038  1.00250.52           O  
ANISOU 3276  OE1 GLU A1072    28773  36251  30161     41   2072  -2612       O  
ATOM   3277  OE2 GLU A1072     -19.294  -7.362  14.637  1.00253.30           O  
ANISOU 3277  OE2 GLU A1072    28834  36878  30529    135   2055  -2825       O  
ATOM   3278  N   MET A1073     -15.005 -12.236  16.834  1.00232.74           N  
ANISOU 3278  N   MET A1073    26766  33423  28241   -841   2745  -1792       N  
ATOM   3279  CA  MET A1073     -13.817 -12.850  17.431  1.00231.28           C  
ANISOU 3279  CA  MET A1073    26805  33033  28039   -896   2829  -1544       C  
ATOM   3280  C   MET A1073     -13.188 -13.876  16.468  1.00233.72           C  
ANISOU 3280  C   MET A1073    27233  33088  28481   -974   2777  -1525       C  
ATOM   3281  O   MET A1073     -11.962 -13.981  16.416  1.00231.64           O  
ANISOU 3281  O   MET A1073    27180  32664  28170   -901   2740  -1393       O  
ATOM   3282  CB  MET A1073     -14.197 -13.517  18.770  1.00235.52           C  
ANISOU 3282  CB  MET A1073    27293  33620  28573  -1073   3051  -1393       C  
ATOM   3283  CG  MET A1073     -13.014 -13.897  19.642  1.00238.37           C  
ANISOU 3283  CG  MET A1073    27893  33828  28849  -1055   3130  -1142       C  
ATOM   3284  SD  MET A1073     -12.224 -12.496  20.465  1.00240.61           S  
ANISOU 3284  SD  MET A1073    28277  34240  28906   -788   3059  -1088       S  
ATOM   3285  CE  MET A1073     -10.869 -13.326  21.261  1.00236.89           C  
ANISOU 3285  CE  MET A1073    28067  33563  28379   -792   3140   -835       C  
ATOM   3286  N   LYS A1074     -14.031 -14.622  15.712  1.00231.03           N  
ANISOU 3286  N   LYS A1074    26744  32727  28308  -1111   2765  -1680       N  
ATOM   3287  CA  LYS A1074     -13.624 -15.648  14.741  1.00230.45           C  
ANISOU 3287  CA  LYS A1074    26751  32429  28378  -1179   2697  -1711       C  
ATOM   3288  C   LYS A1074     -12.747 -15.064  13.624  1.00230.98           C  
ANISOU 3288  C   LYS A1074    26952  32444  28364   -951   2509  -1763       C  
ATOM   3289  O   LYS A1074     -11.689 -15.624  13.340  1.00229.55           O  
ANISOU 3289  O   LYS A1074    26953  32074  28190   -931   2479  -1659       O  
ATOM   3290  CB  LYS A1074     -14.853 -16.344  14.129  1.00235.25           C  
ANISOU 3290  CB  LYS A1074    27128  33073  29184  -1345   2694  -1928       C  
ATOM   3291  CG  LYS A1074     -15.436 -17.457  14.988  1.00249.34           C  
ANISOU 3291  CG  LYS A1074    28837  34780  31120  -1650   2898  -1838       C  
ATOM   3292  CD  LYS A1074     -16.750 -17.965  14.418  1.00259.17           C  
ANISOU 3292  CD  LYS A1074    29843  36036  32593  -1767   2861  -2013       C  
ATOM   3293  CE  LYS A1074     -17.389 -19.005  15.302  1.00266.45           C  
ANISOU 3293  CE  LYS A1074    30990  36423  33826  -1614   2784  -1276       C  
ATOM   3294  NZ  LYS A1074     -18.695 -19.458  14.759  1.00272.51           N  
ANISOU 3294  NZ  LYS A1074    31800  36821  34920  -1323   2456   -845       N  
ATOM   3295  N   ASP A1075     -13.180 -13.943  13.006  1.00226.15           N  
ANISOU 3295  N   ASP A1075    26260  32003  27665   -770   2388  -1919       N  
ATOM   3296  CA  ASP A1075     -12.451 -13.268  11.929  1.00223.94           C  
ANISOU 3296  CA  ASP A1075    26109  31690  27289   -552   2231  -1957       C  
ATOM   3297  C   ASP A1075     -11.212 -12.535  12.456  1.00225.01           C  
ANISOU 3297  C   ASP A1075    26442  31772  27279   -448   2247  -1762       C  
ATOM   3298  O   ASP A1075     -10.236 -12.398  11.716  1.00223.26           O  
ANISOU 3298  O   ASP A1075    26366  31456  27007   -342   2172  -1719       O  
ATOM   3299  CB  ASP A1075     -13.364 -12.289  11.180  1.00226.19           C  
ANISOU 3299  CB  ASP A1075    26272  32161  27510   -381   2105  -2172       C  
ATOM   3300  CG  ASP A1075     -14.345 -12.947  10.234  1.00238.22           C  
ANISOU 3300  CG  ASP A1075    27618  33732  29164   -413   2026  -2417       C  
ATOM   3301  OD1 ASP A1075     -13.905 -13.450   9.176  1.00238.56           O  
ANISOU 3301  OD1 ASP A1075    27734  33665  29242   -354   1929  -2469       O  
ATOM   3302  OD2 ASP A1075     -15.560 -12.913  10.522  1.00246.01           O  
ANISOU 3302  OD2 ASP A1075    28377  34886  30209   -479   2050  -2578       O  
ATOM   3303  N   PHE A1076     -11.252 -12.066  13.722  1.00221.01           N  
ANISOU 3303  N   PHE A1076    25926  31342  26705   -474   2345  -1658       N  
ATOM   3304  CA  PHE A1076     -10.132 -11.374  14.368  1.00219.02           C  
ANISOU 3304  CA  PHE A1076    25833  31052  26333   -383   2356  -1502       C  
ATOM   3305  C   PHE A1076      -9.006 -12.369  14.681  1.00222.20           C  
ANISOU 3305  C   PHE A1076    26380  31279  26766   -462   2419  -1341       C  
ATOM   3306  O   PHE A1076      -7.844 -12.066  14.402  1.00220.52           O  
ANISOU 3306  O   PHE A1076    26305  30991  26494   -370   2368  -1275       O  
ATOM   3307  CB  PHE A1076     -10.593 -10.633  15.642  1.00221.04           C  
ANISOU 3307  CB  PHE A1076    26021  31461  26504   -364   2425  -1472       C  
ATOM   3308  CG  PHE A1076      -9.505  -9.928  16.424  1.00221.07           C  
ANISOU 3308  CG  PHE A1076    26164  31436  26399   -269   2427  -1343       C  
ATOM   3309  CD1 PHE A1076      -8.968  -8.727  15.975  1.00222.74           C  
ANISOU 3309  CD1 PHE A1076    26459  31638  26535   -114   2313  -1374       C  
ATOM   3310  CD2 PHE A1076      -9.044 -10.448  17.629  1.00223.27           C  
ANISOU 3310  CD2 PHE A1076    26490  31694  26648   -330   2542  -1199       C  
ATOM   3311  CE1 PHE A1076      -7.972  -8.070  16.705  1.00222.63           C  
ANISOU 3311  CE1 PHE A1076    26549  31592  26447    -45   2309  -1284       C  
ATOM   3312  CE2 PHE A1076      -8.048  -9.790  18.358  1.00224.99           C  
ANISOU 3312  CE2 PHE A1076    26815  31903  26768   -225   2525  -1118       C  
ATOM   3313  CZ  PHE A1076      -7.521  -8.605  17.892  1.00221.87           C  
ANISOU 3313  CZ  PHE A1076    26475  31498  26327    -93   2407  -1172       C  
ATOM   3314  N   ARG A1077      -9.354 -13.553  15.243  1.00219.71           N  
ANISOU 3314  N   ARG A1077    26037  30899  26545   -631   2529  -1284       N  
ATOM   3315  CA  ARG A1077      -8.399 -14.619  15.574  1.00219.34           C  
ANISOU 3315  CA  ARG A1077    26146  30669  26524   -691   2580  -1139       C  
ATOM   3316  C   ARG A1077      -7.822 -15.251  14.311  1.00223.10           C  
ANISOU 3316  C   ARG A1077    26693  31005  27068   -662   2473  -1201       C  
ATOM   3317  O   ARG A1077      -6.642 -15.603  14.298  1.00221.91           O  
ANISOU 3317  O   ARG A1077    26692  30746  26876   -603   2450  -1113       O  
ATOM   3318  CB  ARG A1077      -9.050 -15.707  16.436  1.00220.59           C  
ANISOU 3318  CB  ARG A1077    26277  30770  26768   -885   2731  -1056       C  
ATOM   3319  CG  ARG A1077      -9.267 -15.317  17.890  1.00228.48           C  
ANISOU 3319  CG  ARG A1077    27263  31891  27659   -893   2865   -934       C  
ATOM   3320  CD  ARG A1077     -10.071 -16.375  18.619  1.00238.87           C  
ANISOU 3320  CD  ARG A1077    28538  33161  29060  -1107   3040   -848       C  
ATOM   3321  NE  ARG A1077     -11.429 -16.503  18.081  1.00247.17           N  
ANISOU 3321  NE  ARG A1077    29362  34302  30251  -1254   3059  -1013       N  
ATOM   3322  CZ  ARG A1077     -12.278 -17.476  18.399  1.00262.92           C  
ANISOU 3322  CZ  ARG A1077    31274  36243  32378  -1491   3204   -986       C  
ATOM   3323  NH1 ARG A1077     -11.919 -18.427  19.252  1.00251.56           N  
ANISOU 3323  NH1 ARG A1077    29999  34641  30942  -1604   3350   -773       N  
ATOM   3324  NH2 ARG A1077     -13.489 -17.509  17.861  1.00250.89           N  
ANISOU 3324  NH2 ARG A1077    29509  34829  30989  -1615   3205  -1178       N  
ATOM   3325  N   HIS A1078      -8.651 -15.395  13.255  1.00220.50           N  
ANISOU 3325  N   HIS A1078    26246  30701  26833   -682   2398  -1372       N  
ATOM   3326  CA  HIS A1078      -8.232 -15.963  11.973  1.00220.28           C  
ANISOU 3326  CA  HIS A1078    26265  30572  26858   -625   2280  -1463       C  
ATOM   3327  C   HIS A1078      -7.302 -14.995  11.226  1.00222.16           C  
ANISOU 3327  C   HIS A1078    26588  30865  26957   -428   2186  -1462       C  
ATOM   3328  O   HIS A1078      -6.387 -15.450  10.539  1.00221.51           O  
ANISOU 3328  O   HIS A1078    26604  30699  26860   -360   2125  -1453       O  
ATOM   3329  CB  HIS A1078      -9.441 -16.344  11.101  1.00222.69           C  
ANISOU 3329  CB  HIS A1078    26404  30912  27295   -681   2217  -1672       C  
ATOM   3330  CG  HIS A1078      -9.067 -17.043   9.830  1.00226.41           C  
ANISOU 3330  CG  HIS A1078    26918  31284  27823   -611   2088  -1783       C  
ATOM   3331  ND1 HIS A1078      -8.484 -18.299   9.840  1.00228.91           N  
ANISOU 3331  ND1 HIS A1078    27343  31400  28232   -687   2089  -1733       N  
ATOM   3332  CD2 HIS A1078      -9.196 -16.632   8.548  1.00227.97           C  
ANISOU 3332  CD2 HIS A1078    27076  31563  27978   -449   1951  -1943       C  
ATOM   3333  CE1 HIS A1078      -8.275 -18.607   8.570  1.00228.43           C  
ANISOU 3333  CE1 HIS A1078    27287  31318  28187   -569   1947  -1876       C  
ATOM   3334  NE2 HIS A1078      -8.687 -17.634   7.757  1.00228.23           N  
ANISOU 3334  NE2 HIS A1078    27174  31466  28076   -422   1867  -2000       N  
ATOM   3335  N   GLY A1079      -7.534 -13.688  11.393  1.00217.39           N  
ANISOU 3335  N   GLY A1079    25949  30398  26253   -341   2179  -1469       N  
ATOM   3336  CA  GLY A1079      -6.731 -12.621  10.798  1.00215.52           C  
ANISOU 3336  CA  GLY A1079    25799  30198  25890   -183   2116  -1446       C  
ATOM   3337  C   GLY A1079      -5.269 -12.702  11.192  1.00217.30           C  
ANISOU 3337  C   GLY A1079    26157  30348  26059   -166   2150  -1305       C  
ATOM   3338  O   GLY A1079      -4.387 -12.424  10.374  1.00216.21           O  
ANISOU 3338  O   GLY A1079    26091  30199  25858    -73   2103  -1295       O  
ATOM   3339  N   PHE A1080      -5.010 -13.108  12.455  1.00213.07           N  
ANISOU 3339  N   PHE A1080    25646  29775  25535   -247   2236  -1201       N  
ATOM   3340  CA  PHE A1080      -3.672 -13.304  13.011  1.00211.73           C  
ANISOU 3340  CA  PHE A1080    25588  29549  25312   -219   2262  -1091       C  
ATOM   3341  C   PHE A1080      -3.136 -14.700  12.668  1.00214.55           C  
ANISOU 3341  C   PHE A1080    26017  29780  25722   -242   2245  -1081       C  
ATOM   3342  O   PHE A1080      -1.922 -14.860  12.565  1.00213.44           O  
ANISOU 3342  O   PHE A1080    25958  29613  25526   -169   2222  -1044       O  
ATOM   3343  CB  PHE A1080      -3.660 -13.080  14.530  1.00213.66           C  
ANISOU 3343  CB  PHE A1080    25840  29826  25516   -248   2346   -997       C  
ATOM   3344  CG  PHE A1080      -3.656 -11.627  14.943  1.00214.56           C  
ANISOU 3344  CG  PHE A1080    25921  30047  25554   -180   2335  -1005       C  
ATOM   3345  CD1 PHE A1080      -2.490 -10.872  14.881  1.00216.85           C  
ANISOU 3345  CD1 PHE A1080    26269  30340  25784   -102   2301   -984       C  
ATOM   3346  CD2 PHE A1080      -4.812 -11.019  15.417  1.00217.21           C  
ANISOU 3346  CD2 PHE A1080    26163  30482  25886   -194   2356  -1046       C  
ATOM   3347  CE1 PHE A1080      -2.485  -9.530  15.268  1.00217.42           C  
ANISOU 3347  CE1 PHE A1080    26324  30476  25809    -49   2281  -1000       C  
ATOM   3348  CE2 PHE A1080      -4.806  -9.677  15.806  1.00219.60           C  
ANISOU 3348  CE2 PHE A1080    26452  30866  26120   -111   2324  -1068       C  
ATOM   3349  CZ  PHE A1080      -3.643  -8.942  15.730  1.00216.86           C  
ANISOU 3349  CZ  PHE A1080    26183  30485  25730    -44   2283  -1042       C  
ATOM   3350  N   ASP A1081      -4.035 -15.699  12.474  1.00211.26           N  
ANISOU 3350  N   ASP A1081    25563  29285  25420   -340   2249  -1131       N  
ATOM   3351  CA  ASP A1081      -3.678 -17.073  12.094  1.00211.41           C  
ANISOU 3351  CA  ASP A1081    25662  29152  25515   -364   2213  -1143       C  
ATOM   3352  C   ASP A1081      -3.018 -17.078  10.714  1.00213.93           C  
ANISOU 3352  C   ASP A1081    25996  29488  25800   -236   2098  -1239       C  
ATOM   3353  O   ASP A1081      -2.064 -17.827  10.496  1.00213.55           O  
ANISOU 3353  O   ASP A1081    26044  29363  25732   -173   2054  -1228       O  
ATOM   3354  CB  ASP A1081      -4.905 -18.004  12.110  1.00214.83           C  
ANISOU 3354  CB  ASP A1081    26029  29490  26106   -521   2240  -1200       C  
ATOM   3355  CG  ASP A1081      -5.287 -18.540  13.479  1.00223.78           C  
ANISOU 3355  CG  ASP A1081    27203  30548  27276   -662   2375  -1066       C  
ATOM   3356  OD1 ASP A1081      -4.392 -19.053  14.188  1.00223.95           O  
ANISOU 3356  OD1 ASP A1081    27380  30472  27239   -627   2407   -940       O  
ATOM   3357  OD2 ASP A1081      -6.490 -18.508  13.813  1.00230.05           O  
ANISOU 3357  OD2 ASP A1081    27872  31385  28150   -800   2451  -1095       O  
ATOM   3358  N   ILE A1082      -3.508 -16.208   9.804  1.00209.58           N  
ANISOU 3358  N   ILE A1082    25359  29053  25220   -175   2049  -1332       N  
ATOM   3359  CA  ILE A1082      -2.968 -16.022   8.455  1.00208.88           C  
ANISOU 3359  CA  ILE A1082    25283  29018  25063    -35   1958  -1410       C  
ATOM   3360  C   ILE A1082      -1.590 -15.353   8.579  1.00211.04           C  
ANISOU 3360  C   ILE A1082    25628  29349  25207     47   1988  -1311       C  
ATOM   3361  O   ILE A1082      -0.625 -15.827   7.977  1.00210.61           O  
ANISOU 3361  O   ILE A1082    25623  29296  25105    131   1946  -1326       O  
ATOM   3362  CB  ILE A1082      -3.930 -15.193   7.542  1.00212.13           C  
ANISOU 3362  CB  ILE A1082    25608  29539  25453     29   1907  -1522       C  
ATOM   3363  CG1 ILE A1082      -5.344 -15.807   7.476  1.00213.86           C  
ANISOU 3363  CG1 ILE A1082    25712  29732  25814    -60   1876  -1657       C  
ATOM   3364  CG2 ILE A1082      -3.349 -15.023   6.129  1.00212.85           C  
ANISOU 3364  CG2 ILE A1082    25734  29696  25444    196   1826  -1582       C  
ATOM   3365  CD1 ILE A1082      -6.470 -14.800   7.128  1.00220.85           C  
ANISOU 3365  CD1 ILE A1082    26491  30752  26670     -9   1846  -1759       C  
ATOM   3366  N   LEU A1083      -1.512 -14.272   9.384  1.00206.28           N  
ANISOU 3366  N   LEU A1083    25018  28803  24555     20   2056  -1228       N  
ATOM   3367  CA  LEU A1083      -0.309 -13.471   9.622  1.00204.90           C  
ANISOU 3367  CA  LEU A1083    24883  28683  24286     65   2091  -1152       C  
ATOM   3368  C   LEU A1083       0.839 -14.305  10.224  1.00208.50           C  
ANISOU 3368  C   LEU A1083    25396  29098  24729     78   2101  -1111       C  
ATOM   3369  O   LEU A1083       1.945 -14.243   9.689  1.00208.14           O  
ANISOU 3369  O   LEU A1083    25363  29106  24615    150   2087  -1119       O  
ATOM   3370  CB  LEU A1083      -0.642 -12.272  10.530  1.00204.28           C  
ANISOU 3370  CB  LEU A1083    24781  28645  24190     26   2143  -1099       C  
ATOM   3371  CG  LEU A1083       0.329 -11.086  10.487  1.00208.16           C  
ANISOU 3371  CG  LEU A1083    25295  29188  24608     59   2166  -1053       C  
ATOM   3372  CD1 LEU A1083       0.017 -10.156   9.325  1.00208.33           C  
ANISOU 3372  CD1 LEU A1083    25330  29245  24581    113   2143  -1073       C  
ATOM   3373  CD2 LEU A1083       0.282 -10.301  11.781  1.00210.22           C  
ANISOU 3373  CD2 LEU A1083    25543  29459  24872     23   2202  -1012       C  
ATOM   3374  N   VAL A1084       0.575 -15.093  11.302  1.00204.91           N  
ANISOU 3374  N   VAL A1084    24976  28556  24325     21   2128  -1069       N  
ATOM   3375  CA  VAL A1084       1.577 -15.957  11.960  1.00204.69           C  
ANISOU 3375  CA  VAL A1084    25032  28473  24267     66   2123  -1032       C  
ATOM   3376  C   VAL A1084       2.047 -17.024  10.953  1.00208.12           C  
ANISOU 3376  C   VAL A1084    25509  28857  24709    140   2039  -1107       C  
ATOM   3377  O   VAL A1084       3.252 -17.246  10.829  1.00207.82           O  
ANISOU 3377  O   VAL A1084    25500  28864  24596    241   2007  -1126       O  
ATOM   3378  CB  VAL A1084       1.079 -16.579  13.301  1.00209.27           C  
ANISOU 3378  CB  VAL A1084    25675  28958  24881      1   2180   -949       C  
ATOM   3379  CG1 VAL A1084       2.098 -17.558  13.883  1.00209.71           C  
ANISOU 3379  CG1 VAL A1084    25854  28939  24886     87   2157   -916       C  
ATOM   3380  CG2 VAL A1084       0.755 -15.496  14.324  1.00208.55           C  
ANISOU 3380  CG2 VAL A1084    25534  28953  24753    -31   2251   -893       C  
ATOM   3381  N   GLY A1085       1.101 -17.609  10.210  1.00204.17           N  
ANISOU 3381  N   GLY A1085    24994  28285  24298    101   1995  -1173       N  
ATOM   3382  CA  GLY A1085       1.368 -18.591   9.161  1.00204.11           C  
ANISOU 3382  CA  GLY A1085    25017  28228  24308    184   1893  -1274       C  
ATOM   3383  C   GLY A1085       2.263 -18.042   8.065  1.00205.57           C  
ANISOU 3383  C   GLY A1085    25158  28570  24377    314   1856  -1329       C  
ATOM   3384  O   GLY A1085       3.099 -18.771   7.528  1.00205.62           O  
ANISOU 3384  O   GLY A1085    25201  28588  24337    430   1785  -1392       O  
ATOM   3385  N   GLN A1086       2.116 -16.735   7.760  1.00199.88           N  
ANISOU 3385  N   GLN A1086    24369  27974  23602    301   1911  -1300       N  
ATOM   3386  CA  GLN A1086       2.915 -16.001   6.780  1.00198.81           C  
ANISOU 3386  CA  GLN A1086    24200  27990  23350    394   1919  -1312       C  
ATOM   3387  C   GLN A1086       4.286 -15.615   7.362  1.00201.73           C  
ANISOU 3387  C   GLN A1086    24564  28439  23643    408   1975  -1258       C  
ATOM   3388  O   GLN A1086       5.263 -15.545   6.612  1.00201.41           O  
ANISOU 3388  O   GLN A1086    24495  28521  23510    493   1975  -1288       O  
ATOM   3389  CB  GLN A1086       2.167 -14.753   6.317  1.00199.49           C  
ANISOU 3389  CB  GLN A1086    24250  28136  23412    368   1958  -1287       C  
ATOM   3390  CG  GLN A1086       1.126 -15.005   5.237  1.00207.37           C  
ANISOU 3390  CG  GLN A1086    25230  29135  24428    430   1882  -1388       C  
ATOM   3391  CD  GLN A1086       0.451 -13.732   4.791  1.00218.98           C  
ANISOU 3391  CD  GLN A1086    26689  30669  25844    446   1909  -1365       C  
ATOM   3392  OE1 GLN A1086       0.974 -12.619   4.950  1.00212.17           O  
ANISOU 3392  OE1 GLN A1086    25850  29853  24911    428   1986  -1267       O  
ATOM   3393  NE2 GLN A1086      -0.721 -13.869   4.193  1.00209.92           N  
ANISOU 3393  NE2 GLN A1086    25511  29519  24731    489   1837  -1468       N  
ATOM   3394  N   ILE A1087       4.350 -15.351   8.693  1.00197.77           N  
ANISOU 3394  N   ILE A1087    24075  27891  23175    333   2023  -1192       N  
ATOM   3395  CA  ILE A1087       5.585 -15.028   9.425  1.00197.44           C  
ANISOU 3395  CA  ILE A1087    24014  27925  23078    353   2059  -1172       C  
ATOM   3396  C   ILE A1087       6.458 -16.298   9.456  1.00201.83           C  
ANISOU 3396  C   ILE A1087    24615  28475  23597    469   1987  -1237       C  
ATOM   3397  O   ILE A1087       7.661 -16.210   9.208  1.00201.86           O  
ANISOU 3397  O   ILE A1087    24565  28611  23521    544   1986  -1286       O  
ATOM   3398  CB  ILE A1087       5.291 -14.454  10.857  1.00200.16           C  
ANISOU 3398  CB  ILE A1087    24365  28226  23459    276   2108  -1105       C  
ATOM   3399  CG1 ILE A1087       4.782 -12.999  10.781  1.00199.96           C  
ANISOU 3399  CG1 ILE A1087    24291  28236  23449    195   2165  -1065       C  
ATOM   3400  CG2 ILE A1087       6.521 -14.527  11.782  1.00201.30           C  
ANISOU 3400  CG2 ILE A1087    24502  28431  23553    335   2108  -1123       C  
ATOM   3401  CD1 ILE A1087       3.950 -12.528  11.994  1.00206.54           C  
ANISOU 3401  CD1 ILE A1087    25132  29018  24326    132   2192  -1017       C  
ATOM   3402  N   ASP A1088       5.833 -17.475   9.726  1.00198.57           N  
ANISOU 3402  N   ASP A1088    24299  27906  23243    483   1926  -1245       N  
ATOM   3403  CA  ASP A1088       6.483 -18.794   9.773  1.00199.18           C  
ANISOU 3403  CA  ASP A1088    24464  27922  23294    607   1834  -1306       C  
ATOM   3404  C   ASP A1088       7.105 -19.157   8.417  1.00203.15           C  
ANISOU 3404  C   ASP A1088    24923  28532  23731    732   1761  -1418       C  
ATOM   3405  O   ASP A1088       8.178 -19.764   8.387  1.00203.52           O  
ANISOU 3405  O   ASP A1088    24986  28644  23698    873   1698  -1492       O  
ATOM   3406  CB  ASP A1088       5.489 -19.894  10.203  1.00201.75           C  
ANISOU 3406  CB  ASP A1088    24916  28015  23725    557   1797  -1276       C  
ATOM   3407  CG  ASP A1088       4.871 -19.737  11.586  1.00211.14           C  
ANISOU 3407  CG  ASP A1088    26161  29106  24957    450   1880  -1155       C  
ATOM   3408  OD1 ASP A1088       5.521 -19.132  12.468  1.00211.22           O  
ANISOU 3408  OD1 ASP A1088    26157  29205  24892    480   1926  -1113       O  
ATOM   3409  OD2 ASP A1088       3.742 -20.231  11.789  1.00217.14           O  
ANISOU 3409  OD2 ASP A1088    26969  29712  25824    338   1901  -1114       O  
ATOM   3410  N   ASP A1089       6.432 -18.778   7.303  1.00198.98           N  
ANISOU 3410  N   ASP A1089    24338  28043  23220    705   1764  -1442       N  
ATOM   3411  CA  ASP A1089       6.915 -18.997   5.936  1.00199.10           C  
ANISOU 3411  CA  ASP A1089    24306  28193  23151    837   1707  -1543       C  
ATOM   3412  C   ASP A1089       8.109 -18.087   5.651  1.00202.35           C  
ANISOU 3412  C   ASP A1089    24613  28836  23436    869   1790  -1531       C  
ATOM   3413  O   ASP A1089       9.055 -18.514   4.989  1.00203.02           O  
ANISOU 3413  O   ASP A1089    24656  29065  23419   1008   1748  -1621       O  
ATOM   3414  CB  ASP A1089       5.796 -18.754   4.903  1.00200.81           C  
ANISOU 3414  CB  ASP A1089    24500  28397  23403    818   1689  -1569       C  
ATOM   3415  CG  ASP A1089       4.642 -19.739   4.950  1.00210.39           C  
ANISOU 3415  CG  ASP A1089    25776  29404  24757    783   1596  -1628       C  
ATOM   3416  OD1 ASP A1089       4.892 -20.942   5.199  1.00211.44           O  
ANISOU 3416  OD1 ASP A1089    25992  29411  24933    840   1504  -1687       O  
ATOM   3417  OD2 ASP A1089       3.498 -19.321   4.682  1.00216.26           O  
ANISOU 3417  OD2 ASP A1089    26486  30112  25569    704   1610  -1628       O  
ATOM   3418  N   ALA A1090       8.064 -16.836   6.168  1.00197.30           N  
ANISOU 3418  N   ALA A1090    23924  28231  22809    736   1908  -1431       N  
ATOM   3419  CA  ALA A1090       9.128 -15.836   6.028  1.00196.72           C  
ANISOU 3419  CA  ALA A1090    23745  28343  22655    709   2009  -1409       C  
ATOM   3420  C   ALA A1090      10.358 -16.216   6.876  1.00199.45           C  
ANISOU 3420  C   ALA A1090    24049  28766  22968    766   1991  -1472       C  
ATOM   3421  O   ALA A1090      11.492 -15.963   6.457  1.00199.83           O  
ANISOU 3421  O   ALA A1090    23985  29012  22930    808   2032  -1528       O  
ATOM   3422  CB  ALA A1090       8.610 -14.463   6.426  1.00196.67           C  
ANISOU 3422  CB  ALA A1090    23726  28298  22703    551   2113  -1298       C  
ATOM   3423  N   LEU A1091      10.123 -16.838   8.056  1.00194.39           N  
ANISOU 3423  N   LEU A1091    23495  27980  22384    778   1932  -1469       N  
ATOM   3424  CA  LEU A1091      11.153 -17.324   8.981  1.00194.02           C  
ANISOU 3424  CA  LEU A1091    23444  27983  22292    877   1886  -1539       C  
ATOM   3425  C   LEU A1091      11.912 -18.489   8.367  1.00197.46           C  
ANISOU 3425  C   LEU A1091    23894  28493  22638   1073   1775  -1668       C  
ATOM   3426  O   LEU A1091      13.131 -18.570   8.530  1.00197.87           O  
ANISOU 3426  O   LEU A1091    23858  28720  22603   1178   1756  -1771       O  
ATOM   3427  CB  LEU A1091      10.529 -17.763  10.318  1.00193.67           C  
ANISOU 3427  CB  LEU A1091    23533  27744  22308    862   1854  -1476       C  
ATOM   3428  CG  LEU A1091      10.401 -16.704  11.398  1.00197.45           C  
ANISOU 3428  CG  LEU A1091    23971  28225  22825    751   1935  -1407       C  
ATOM   3429  CD1 LEU A1091       9.288 -17.050  12.359  1.00197.27           C  
ANISOU 3429  CD1 LEU A1091    24082  28006  22864    702   1935  -1307       C  
ATOM   3430  CD2 LEU A1091      11.706 -16.530  12.154  1.00200.31           C  
ANISOU 3430  CD2 LEU A1091    24254  28735  23119    843   1919  -1500       C  
ATOM   3431  N   LYS A1092      11.187 -19.387   7.659  1.00192.90           N  
ANISOU 3431  N   LYS A1092    23418  27792  22085   1130   1691  -1684       N  
ATOM   3432  CA  LYS A1092      11.750 -20.538   6.970  1.00193.35           C  
ANISOU 3432  CA  LYS A1092    23507  27892  22064   1333   1560  -1820       C  
ATOM   3433  C   LYS A1092      12.730 -20.069   5.896  1.00196.86           C  
ANISOU 3433  C   LYS A1092    23778  28638  22384   1405   1603  -1905       C  
ATOM   3434  O   LYS A1092      13.810 -20.652   5.768  1.00197.52           O  
ANISOU 3434  O   LYS A1092    23813  28876  22360   1581   1530  -2040       O  
ATOM   3435  CB  LYS A1092      10.638 -21.403   6.369  1.00195.76           C  
ANISOU 3435  CB  LYS A1092    23935  27993  22453   1345   1467  -1829       C  
ATOM   3436  CG  LYS A1092      11.092 -22.818   6.100  1.00206.24           C  
ANISOU 3436  CG  LYS A1092    25364  29260  23737   1560   1294  -1967       C  
ATOM   3437  CD  LYS A1092      10.965 -23.778   7.297  1.00212.87           C  
ANISOU 3437  CD  LYS A1092    26403  29843  24634   1593   1216  -1936       C  
ATOM   3438  CE  LYS A1092      12.020 -24.855   7.252  1.00220.18           C  
ANISOU 3438  CE  LYS A1092    27406  30803  25450   1857   1057  -2086       C  
ATOM   3439  NZ  LYS A1092      11.662 -25.964   6.324  1.00227.49           N  
ANISOU 3439  NZ  LYS A1092    28427  31597  26411   1978    898  -2201       N  
ATOM   3440  N   LEU A1093      12.367 -18.994   5.156  1.00192.25           N  
ANISOU 3440  N   LEU A1093    23103  28141  21800   1275   1728  -1824       N  
ATOM   3441  CA  LEU A1093      13.198 -18.380   4.120  1.00192.59           C  
ANISOU 3441  CA  LEU A1093    22990  28465  21721   1302   1818  -1858       C  
ATOM   3442  C   LEU A1093      14.466 -17.777   4.735  1.00196.51           C  
ANISOU 3442  C   LEU A1093    23335  29153  22175   1262   1904  -1895       C  
ATOM   3443  O   LEU A1093      15.546 -17.907   4.151  1.00197.55           O  
ANISOU 3443  O   LEU A1093    23331  29543  22186   1366   1919  -2003       O  
ATOM   3444  CB  LEU A1093      12.412 -17.298   3.350  1.00191.99           C  
ANISOU 3444  CB  LEU A1093    22902  28386  21658   1164   1942  -1728       C  
ATOM   3445  CG  LEU A1093      11.331 -17.766   2.364  1.00196.51           C  
ANISOU 3445  CG  LEU A1093    23565  28869  22231   1242   1862  -1737       C  
ATOM   3446  CD1 LEU A1093      10.394 -16.628   2.012  1.00195.89           C  
ANISOU 3446  CD1 LEU A1093    23511  28735  22185   1104   1968  -1601       C  
ATOM   3447  CD2 LEU A1093      11.940 -18.338   1.088  1.00200.27           C  
ANISOU 3447  CD2 LEU A1093    23982  29561  22549   1446   1812  -1854       C  
ATOM   3448  N   ALA A1094      14.329 -17.135   5.918  1.00191.55           N  
ANISOU 3448  N   ALA A1094    22717  28416  21646   1119   1955  -1824       N  
ATOM   3449  CA  ALA A1094      15.431 -16.526   6.666  1.00191.61           C  
ANISOU 3449  CA  ALA A1094    22578  28579  21647   1071   2017  -1882       C  
ATOM   3450  C   ALA A1094      16.387 -17.600   7.201  1.00195.76           C  
ANISOU 3450  C   ALA A1094    23089  29199  22092   1290   1881  -2057       C  
ATOM   3451  O   ALA A1094      17.600 -17.384   7.210  1.00196.54           O  
ANISOU 3451  O   ALA A1094    23006  29549  22123   1332   1911  -2185       O  
ATOM   3452  CB  ALA A1094      14.885 -15.686   7.811  1.00191.19           C  
ANISOU 3452  CB  ALA A1094    22565  28361  21716    905   2068  -1781       C  
ATOM   3453  N   ASN A1095      15.835 -18.763   7.617  1.00191.43           N  
ANISOU 3453  N   ASN A1095    22735  28447  21551   1431   1731  -2069       N  
ATOM   3454  CA  ASN A1095      16.597 -19.910   8.117  1.00192.07           C  
ANISOU 3454  CA  ASN A1095    22873  28560  21546   1677   1574  -2222       C  
ATOM   3455  C   ASN A1095      17.406 -20.551   6.986  1.00197.09           C  
ANISOU 3455  C   ASN A1095    23415  29424  22048   1867   1507  -2381       C  
ATOM   3456  O   ASN A1095      18.521 -21.020   7.228  1.00198.00           O  
ANISOU 3456  O   ASN A1095    23450  29725  22055   2057   1425  -2556       O  
ATOM   3457  CB  ASN A1095      15.672 -20.940   8.766  1.00191.77           C  
ANISOU 3457  CB  ASN A1095    23102  28197  21564   1745   1454  -2156       C  
ATOM   3458  CG  ASN A1095      15.191 -20.555  10.143  1.00211.78           C  
ANISOU 3458  CG  ASN A1095    25728  30564  24176   1643   1495  -2042       C  
ATOM   3459  OD1 ASN A1095      15.980 -20.291  11.058  1.00204.97           O  
ANISOU 3459  OD1 ASN A1095    24805  29808  23266   1705   1489  -2108       O  
ATOM   3460  ND2 ASN A1095      13.881 -20.571  10.337  1.00203.61           N  
ANISOU 3460  ND2 ASN A1095    24834  29278  23252   1504   1527  -1886       N  
ATOM   3461  N   GLU A1096      16.855 -20.541   5.749  1.00193.32           N  
ANISOU 3461  N   GLU A1096    22936  28957  21562   1837   1537  -2337       N  
ATOM   3462  CA  GLU A1096      17.513 -21.061   4.542  1.00194.43           C  
ANISOU 3462  CA  GLU A1096    22979  29338  21559   2021   1487  -2479       C  
ATOM   3463  C   GLU A1096      18.574 -20.066   4.038  1.00198.37           C  
ANISOU 3463  C   GLU A1096    23203  30200  21969   1943   1656  -2519       C  
ATOM   3464  O   GLU A1096      19.428 -20.439   3.233  1.00199.59           O  
ANISOU 3464  O   GLU A1096    23223  30635  21975   2110   1632  -2665       O  
ATOM   3465  CB  GLU A1096      16.494 -21.374   3.421  1.00195.59           C  
ANISOU 3465  CB  GLU A1096    23224  29371  21719   2034   1454  -2424       C  
ATOM   3466  CG  GLU A1096      15.566 -22.544   3.713  1.00206.39           C  
ANISOU 3466  CG  GLU A1096    24834  30406  23177   2124   1273  -2433       C  
ATOM   3467  CD  GLU A1096      14.799 -23.143   2.548  1.00227.20           C  
ANISOU 3467  CD  GLU A1096    27540  32971  25814   2213   1180  -2474       C  
ATOM   3468  OE1 GLU A1096      15.330 -23.189   1.413  1.00220.75           O  
ANISOU 3468  OE1 GLU A1096    26605  32415  24856   2356   1173  -2577       O  
ATOM   3469  OE2 GLU A1096      13.674 -23.632   2.796  1.00221.65           O  
ANISOU 3469  OE2 GLU A1096    27007  31958  25253   2150   1107  -2419       O  
ATOM   3470  N   GLY A1097      18.508 -18.824   4.527  1.00193.40           N  
ANISOU 3470  N   GLY A1097    22491  29560  21433   1690   1825  -2395       N  
ATOM   3471  CA  GLY A1097      19.438 -17.753   4.185  1.00193.86           C  
ANISOU 3471  CA  GLY A1097    22298  29906  21453   1549   2011  -2407       C  
ATOM   3472  C   GLY A1097      18.970 -16.832   3.077  1.00196.44           C  
ANISOU 3472  C   GLY A1097    22596  30271  21770   1380   2191  -2242       C  
ATOM   3473  O   GLY A1097      19.701 -15.916   2.691  1.00197.28           O  
ANISOU 3473  O   GLY A1097    22514  30596  21848   1236   2373  -2222       O  
ATOM   3474  N   LYS A1098      17.749 -17.064   2.557  1.00190.70           N  
ANISOU 3474  N   LYS A1098    22059  29331  21067   1397   2143  -2127       N  
ATOM   3475  CA  LYS A1098      17.156 -16.269   1.480  1.00189.99           C  
ANISOU 3475  CA  LYS A1098    21988  29254  20944   1290   2284  -1971       C  
ATOM   3476  C   LYS A1098      16.620 -14.951   2.057  1.00191.82           C  
ANISOU 3476  C   LYS A1098    22256  29311  21316   1015   2424  -1792       C  
ATOM   3477  O   LYS A1098      15.441 -14.860   2.407  1.00189.99           O  
ANISOU 3477  O   LYS A1098    22189  28813  21186    962   2372  -1695       O  
ATOM   3478  CB  LYS A1098      16.053 -17.072   0.761  1.00191.76           C  
ANISOU 3478  CB  LYS A1098    22388  29328  21143   1444   2147  -1965       C  
ATOM   3479  CG  LYS A1098      16.554 -18.337   0.069  1.00205.53           C  
ANISOU 3479  CG  LYS A1098    24108  31237  22747   1731   1994  -2153       C  
ATOM   3480  CD  LYS A1098      15.441 -19.357  -0.106  1.00213.83           C  
ANISOU 3480  CD  LYS A1098    25352  32040  23855   1868   1797  -2194       C  
ATOM   3481  CE  LYS A1098      15.939 -20.643  -0.714  1.00224.99           C  
ANISOU 3481  CE  LYS A1098    26760  33578  25147   2164   1615  -2401       C  
ATOM   3482  NZ  LYS A1098      14.836 -21.619  -0.904  1.00233.40           N  
ANISOU 3482  NZ  LYS A1098    28009  34374  26298   2271   1421  -2453       N  
ATOM   3483  N   VAL A1099      17.509 -13.943   2.186  1.00188.60           N  
ANISOU 3483  N   VAL A1099    21680  29057  20920    841   2597  -1767       N  
ATOM   3484  CA  VAL A1099      17.197 -12.622   2.754  1.00187.48           C  
ANISOU 3484  CA  VAL A1099    21556  28759  20918    579   2726  -1623       C  
ATOM   3485  C   VAL A1099      16.215 -11.876   1.840  1.00190.39           C  
ANISOU 3485  C   VAL A1099    22067  29008  21264    503   2823  -1425       C  
ATOM   3486  O   VAL A1099      15.189 -11.403   2.327  1.00188.66           O  
ANISOU 3486  O   VAL A1099    21992  28538  21154    418   2794  -1324       O  
ATOM   3487  CB  VAL A1099      18.465 -11.763   3.042  1.00192.98           C  
ANISOU 3487  CB  VAL A1099    22025  29650  21651    401   2883  -1671       C  
ATOM   3488  CG1 VAL A1099      18.116 -10.512   3.850  1.00192.10           C  
ANISOU 3488  CG1 VAL A1099    21948  29328  21715    152   2965  -1561       C  
ATOM   3489  CG2 VAL A1099      19.540 -12.573   3.759  1.00193.49           C  
ANISOU 3489  CG2 VAL A1099    21923  29901  21694    534   2776  -1907       C  
ATOM   3490  N   LYS A1100      16.523 -11.799   0.527  1.00187.63           N  
ANISOU 3490  N   LYS A1100    21680  28857  20755    559   2929  -1381       N  
ATOM   3491  CA  LYS A1100      15.712 -11.124  -0.497  1.00187.28           C  
ANISOU 3491  CA  LYS A1100    21778  28744  20637    539   3024  -1200       C  
ATOM   3492  C   LYS A1100      14.301 -11.725  -0.599  1.00188.66           C  
ANISOU 3492  C   LYS A1100    22147  28708  20829    687   2847  -1197       C  
ATOM   3493  O   LYS A1100      13.332 -10.982  -0.780  1.00187.39           O  
ANISOU 3493  O   LYS A1100    22130  28373  20698    624   2878  -1060       O  
ATOM   3494  CB  LYS A1100      16.416 -11.184  -1.863  1.00191.81           C  
ANISOU 3494  CB  LYS A1100    22266  29619  20996    634   3153  -1184       C  
ATOM   3495  CG  LYS A1100      17.558 -10.182  -2.006  1.00204.17           C  
ANISOU 3495  CG  LYS A1100    23666  31361  22550    412   3405  -1109       C  
ATOM   3496  CD  LYS A1100      18.590 -10.628  -3.037  1.00213.66           C  
ANISOU 3496  CD  LYS A1100    24694  32947  23540    533   3506  -1178       C  
ATOM   3497  CE  LYS A1100      19.780  -9.700  -3.088  1.00222.73           C  
ANISOU 3497  CE  LYS A1100    25640  34287  24701    280   3768  -1126       C  
ATOM   3498  NZ  LYS A1100      20.909 -10.295  -3.851  1.00231.85           N  
ANISOU 3498  NZ  LYS A1100    26565  35864  25661    407   3845  -1252       N  
ATOM   3499  N   GLU A1101      14.192 -13.061  -0.463  1.00184.31           N  
ANISOU 3499  N   GLU A1101    21597  28168  20266    882   2658  -1358       N  
ATOM   3500  CA  GLU A1101      12.924 -13.791  -0.514  1.00182.72           C  
ANISOU 3500  CA  GLU A1101    21547  27771  20107   1006   2482  -1391       C  
ATOM   3501  C   GLU A1101      12.115 -13.586   0.771  1.00184.58           C  
ANISOU 3501  C   GLU A1101    21867  27731  20535    870   2423  -1353       C  
ATOM   3502  O   GLU A1101      10.887 -13.509   0.701  1.00183.01           O  
ANISOU 3502  O   GLU A1101    21789  27357  20391    872   2364  -1307       O  
ATOM   3503  CB  GLU A1101      13.159 -15.286  -0.765  1.00184.43           C  
ANISOU 3503  CB  GLU A1101    21745  28066  20266   1240   2304  -1579       C  
ATOM   3504  CG  GLU A1101      13.643 -15.602  -2.171  1.00195.68           C  
ANISOU 3504  CG  GLU A1101    23110  29758  21481   1433   2323  -1635       C  
ATOM   3505  CD  GLU A1101      13.560 -17.060  -2.578  1.00212.03           C  
ANISOU 3505  CD  GLU A1101    25204  31858  23502   1695   2108  -1829       C  
ATOM   3506  OE1 GLU A1101      14.611 -17.632  -2.947  1.00202.64           O  
ANISOU 3506  OE1 GLU A1101    23898  30914  22182   1845   2087  -1956       O  
ATOM   3507  OE2 GLU A1101      12.443 -17.627  -2.553  1.00204.50           O  
ANISOU 3507  OE2 GLU A1101    24377  30686  22640   1751   1957  -1868       O  
ATOM   3508  N   ALA A1102      12.799 -13.500   1.937  1.00181.06           N  
ANISOU 3508  N   ALA A1102    21346  27269  20180    769   2436  -1387       N  
ATOM   3509  CA  ALA A1102      12.167 -13.271   3.243  1.00179.49           C  
ANISOU 3509  CA  ALA A1102    21212  26846  20139    654   2392  -1353       C  
ATOM   3510  C   ALA A1102      11.706 -11.820   3.376  1.00183.37           C  
ANISOU 3510  C   ALA A1102    21740  27241  20693    468   2516  -1205       C  
ATOM   3511  O   ALA A1102      10.690 -11.566   4.026  1.00181.74           O  
ANISOU 3511  O   ALA A1102    21627  26841  20584    412   2471  -1157       O  
ATOM   3512  CB  ALA A1102      13.125 -13.623   4.371  1.00180.25           C  
ANISOU 3512  CB  ALA A1102    21218  26989  20278    649   2358  -1452       C  
ATOM   3513  N   GLN A1103      12.449 -10.875   2.755  1.00181.59           N  
ANISOU 3513  N   GLN A1103    21443  27146  20406    375   2675  -1134       N  
ATOM   3514  CA  GLN A1103      12.129  -9.443   2.737  1.00181.83           C  
ANISOU 3514  CA  GLN A1103    21532  27071  20486    202   2800   -986       C  
ATOM   3515  C   GLN A1103      10.888  -9.178   1.888  1.00186.02           C  
ANISOU 3515  C   GLN A1103    22227  27496  20958    275   2780   -888       C  
ATOM   3516  O   GLN A1103      10.072  -8.331   2.250  1.00185.00           O  
ANISOU 3516  O   GLN A1103    22200  27191  20901    193   2784   -804       O  
ATOM   3517  CB  GLN A1103      13.307  -8.627   2.195  1.00185.22           C  
ANISOU 3517  CB  GLN A1103    21849  27663  20864     76   2989   -931       C  
ATOM   3518  CG  GLN A1103      14.398  -8.363   3.219  1.00202.21           C  
ANISOU 3518  CG  GLN A1103    23831  29875  23125    -63   3027  -1022       C  
ATOM   3519  CD  GLN A1103      15.541  -7.585   2.623  1.00225.26           C  
ANISOU 3519  CD  GLN A1103    26613  32965  26010   -216   3229   -979       C  
ATOM   3520  OE1 GLN A1103      16.136  -7.970   1.607  1.00222.22           O  
ANISOU 3520  OE1 GLN A1103    26153  32804  25476   -141   3308   -985       O  
ATOM   3521  NE2 GLN A1103      15.890  -6.479   3.257  1.00219.00           N  
ANISOU 3521  NE2 GLN A1103    25775  32076  25358   -439   3321   -943       N  
ATOM   3522  N   ALA A1104      10.763  -9.897   0.752  1.00183.76           N  
ANISOU 3522  N   ALA A1104    21960  27331  20529    451   2745   -919       N  
ATOM   3523  CA  ALA A1104       9.637  -9.809  -0.180  1.00183.86           C  
ANISOU 3523  CA  ALA A1104    22111  27288  20459    575   2702   -871       C  
ATOM   3524  C   ALA A1104       8.369 -10.389   0.455  1.00186.60           C  
ANISOU 3524  C   ALA A1104    22522  27455  20920    622   2532   -948       C  
ATOM   3525  O   ALA A1104       7.284  -9.827   0.282  1.00185.90           O  
ANISOU 3525  O   ALA A1104    22540  27251  20841    635   2507   -897       O  
ATOM   3526  CB  ALA A1104       9.971 -10.548  -1.469  1.00185.88           C  
ANISOU 3526  CB  ALA A1104    22341  27752  20533    774   2690   -926       C  
ATOM   3527  N   ALA A1105       8.523 -11.499   1.216  1.00182.53           N  
ANISOU 3527  N   ALA A1105    21944  26919  20489    647   2423  -1071       N  
ATOM   3528  CA  ALA A1105       7.449 -12.173   1.951  1.00181.11           C  
ANISOU 3528  CA  ALA A1105    21809  26570  20434    657   2288  -1138       C  
ATOM   3529  C   ALA A1105       6.939 -11.282   3.084  1.00184.27           C  
ANISOU 3529  C   ALA A1105    22239  26821  20954    499   2323  -1061       C  
ATOM   3530  O   ALA A1105       5.766 -11.368   3.454  1.00182.96           O  
ANISOU 3530  O   ALA A1105    22123  26530  20864    492   2253  -1076       O  
ATOM   3531  CB  ALA A1105       7.948 -13.497   2.510  1.00181.62           C  
ANISOU 3531  CB  ALA A1105    21827  26638  20543    714   2190  -1256       C  
ATOM   3532  N   ALA A1106       7.833 -10.427   3.628  1.00181.39           N  
ANISOU 3532  N   ALA A1106    21828  26485  20608    374   2430   -998       N  
ATOM   3533  CA  ALA A1106       7.545  -9.469   4.695  1.00180.60           C  
ANISOU 3533  CA  ALA A1106    21747  26262  20613    237   2462   -940       C  
ATOM   3534  C   ALA A1106       6.693  -8.302   4.182  1.00184.47           C  
ANISOU 3534  C   ALA A1106    22342  26669  21080    213   2500   -842       C  
ATOM   3535  O   ALA A1106       5.908  -7.744   4.956  1.00183.40           O  
ANISOU 3535  O   ALA A1106    22249  26411  21025    161   2468   -827       O  
ATOM   3536  CB  ALA A1106       8.838  -8.952   5.304  1.00181.87           C  
ANISOU 3536  CB  ALA A1106    21810  26488  20805    124   2548   -937       C  
ATOM   3537  N   GLU A1107       6.827  -7.948   2.879  1.00181.85           N  
ANISOU 3537  N   GLU A1107    22062  26412  20622    276   2563   -780       N  
ATOM   3538  CA  GLU A1107       6.038  -6.878   2.252  1.00182.10           C  
ANISOU 3538  CA  GLU A1107    22230  26363  20596    299   2592   -682       C  
ATOM   3539  C   GLU A1107       4.573  -7.298   2.166  1.00184.89           C  
ANISOU 3539  C   GLU A1107    22638  26654  20958    423   2455   -758       C  
ATOM   3540  O   GLU A1107       3.682  -6.453   2.242  1.00184.44           O  
ANISOU 3540  O   GLU A1107    22674  26498  20906    435   2431   -722       O  
ATOM   3541  CB  GLU A1107       6.562  -6.511   0.845  1.00185.25           C  
ANISOU 3541  CB  GLU A1107    22688  26873  20825    366   2701   -588       C  
ATOM   3542  CG  GLU A1107       8.068  -6.315   0.688  1.00197.45           C  
ANISOU 3542  CG  GLU A1107    24140  28542  22343    251   2854   -534       C  
ATOM   3543  CD  GLU A1107       8.785  -5.269   1.528  1.00220.30           C  
ANISOU 3543  CD  GLU A1107    27001  31347  25357     26   2961   -467       C  
ATOM   3544  OE1 GLU A1107       8.127  -4.316   1.998  1.00216.01           O  
ANISOU 3544  OE1 GLU A1107    26567  30621  24886    -38   2945   -407       O  
ATOM   3545  OE2 GLU A1107      10.025  -5.375   1.670  1.00214.90           O  
ANISOU 3545  OE2 GLU A1107    26176  30785  24691    -77   3055   -489       O  
ATOM   3546  N   GLN A1108       4.332  -8.620   2.022  1.00180.83           N  
ANISOU 3546  N   GLN A1108    22057  26197  20453    516   2358   -878       N  
ATOM   3547  CA  GLN A1108       3.004  -9.233   1.950  1.00180.08           C  
ANISOU 3547  CA  GLN A1108    21970  26056  20396    609   2227   -985       C  
ATOM   3548  C   GLN A1108       2.302  -9.211   3.311  1.00182.48           C  
ANISOU 3548  C   GLN A1108    22242  26244  20850    498   2187  -1012       C  
ATOM   3549  O   GLN A1108       1.070  -9.236   3.349  1.00181.97           O  
ANISOU 3549  O   GLN A1108    22183  26137  20820    540   2110  -1078       O  
ATOM   3550  CB  GLN A1108       3.095 -10.679   1.431  1.00181.59           C  
ANISOU 3550  CB  GLN A1108    22100  26317  20578    715   2139  -1111       C  
ATOM   3551  CG  GLN A1108       3.492 -10.806  -0.042  1.00196.40           C  
ANISOU 3551  CG  GLN A1108    24003  28337  22282    883   2146  -1120       C  
ATOM   3552  CD  GLN A1108       2.393 -10.440  -1.016  1.00213.86           C  
ANISOU 3552  CD  GLN A1108    26290  30564  24402   1041   2081  -1156       C  
ATOM   3553  OE1 GLN A1108       1.226 -10.823  -0.866  1.00207.69           O  
ANISOU 3553  OE1 GLN A1108    25489  29721  23704   1078   1964  -1274       O  
ATOM   3554  NE2 GLN A1108       2.759  -9.733  -2.071  1.00207.83           N  
ANISOU 3554  NE2 GLN A1108    25612  29899  23456   1148   2158  -1063       N  
ATOM   3555  N   LEU A1109       3.075  -9.171   4.421  1.00178.05           N  
ANISOU 3555  N   LEU A1109    21634  25653  20365    372   2238   -976       N  
ATOM   3556  CA  LEU A1109       2.522  -9.122   5.780  1.00176.75           C  
ANISOU 3556  CA  LEU A1109    21442  25402  20314    283   2215   -990       C  
ATOM   3557  C   LEU A1109       1.817  -7.790   6.004  1.00180.05           C  
ANISOU 3557  C   LEU A1109    21917  25761  20732    263   2225   -943       C  
ATOM   3558  O   LEU A1109       0.799  -7.746   6.697  1.00179.14           O  
ANISOU 3558  O   LEU A1109    21785  25605  20676    253   2176   -985       O  
ATOM   3559  CB  LEU A1109       3.601  -9.347   6.865  1.00176.42           C  
ANISOU 3559  CB  LEU A1109    21346  25363  20323    197   2256   -974       C  
ATOM   3560  CG  LEU A1109       4.616 -10.496   6.669  1.00181.50           C  
ANISOU 3560  CG  LEU A1109    21944  26076  20942    239   2247  -1020       C  
ATOM   3561  CD1 LEU A1109       5.596 -10.576   7.832  1.00181.45           C  
ANISOU 3561  CD1 LEU A1109    21888  26082  20973    182   2273  -1023       C  
ATOM   3562  CD2 LEU A1109       3.931 -11.831   6.487  1.00184.12           C  
ANISOU 3562  CD2 LEU A1109    22282  26370  21303    305   2157  -1098       C  
ATOM   3563  N   LYS A1110       2.352  -6.712   5.382  1.00177.15           N  
ANISOU 3563  N   LYS A1110    21626  25391  20294    261   2290   -856       N  
ATOM   3564  CA  LYS A1110       1.801  -5.354   5.423  1.00177.39           C  
ANISOU 3564  CA  LYS A1110    21755  25337  20309    262   2293   -802       C  
ATOM   3565  C   LYS A1110       0.336  -5.344   4.945  1.00181.61           C  
ANISOU 3565  C   LYS A1110    22332  25871  20800    397   2196   -872       C  
ATOM   3566  O   LYS A1110      -0.496  -4.714   5.595  1.00181.02           O  
ANISOU 3566  O   LYS A1110    22274  25745  20762    403   2147   -901       O  
ATOM   3567  CB  LYS A1110       2.639  -4.387   4.563  1.00181.16           C  
ANISOU 3567  CB  LYS A1110    22334  25795  20704    243   2393   -680       C  
ATOM   3568  CG  LYS A1110       4.016  -4.056   5.119  1.00196.38           C  
ANISOU 3568  CG  LYS A1110    24202  27718  22696     83   2494   -628       C  
ATOM   3569  CD  LYS A1110       4.785  -3.196   4.140  1.00208.36           C  
ANISOU 3569  CD  LYS A1110    25811  29224  24134     41   2618   -500       C  
ATOM   3570  CE  LYS A1110       5.866  -2.382   4.824  1.00219.90           C  
ANISOU 3570  CE  LYS A1110    27230  30624  25699   -148   2710   -458       C  
ATOM   3571  NZ  LYS A1110       6.449  -1.356   3.928  1.00230.87           N  
ANISOU 3571  NZ  LYS A1110    28734  31956  27031   -224   2847   -311       N  
ATOM   3572  N   THR A1111       0.007  -6.057   3.845  1.00178.78           N  
ANISOU 3572  N   THR A1111    21976  25588  20366    520   2155   -925       N  
ATOM   3573  CA  THR A1111      -1.372  -6.093   3.343  1.00179.11           C  
ANISOU 3573  CA  THR A1111    22031  25653  20369    662   2048  -1030       C  
ATOM   3574  C   THR A1111      -2.248  -7.051   4.172  1.00182.13           C  
ANISOU 3574  C   THR A1111    22272  26050  20880    613   1979  -1163       C  
ATOM   3575  O   THR A1111      -3.436  -6.774   4.311  1.00182.07           O  
ANISOU 3575  O   THR A1111    22240  26054  20883    671   1907  -1253       O  
ATOM   3576  CB  THR A1111      -1.466  -6.392   1.842  1.00189.21           C  
ANISOU 3576  CB  THR A1111    23366  27015  21511    838   2016  -1061       C  
ATOM   3577  OG1 THR A1111      -0.333  -7.148   1.403  1.00188.70           O  
ANISOU 3577  OG1 THR A1111    23266  27011  21419    812   2077  -1024       O  
ATOM   3578  CG2 THR A1111      -1.639  -5.114   1.005  1.00189.58           C  
ANISOU 3578  CG2 THR A1111    23596  27036  21402    970   2031   -970       C  
ATOM   3579  N   THR A1112      -1.673  -8.137   4.754  1.00177.79           N  
ANISOU 3579  N   THR A1112    21633  25498  20420    506   2006  -1172       N  
ATOM   3580  CA  THR A1112      -2.409  -9.069   5.633  1.00177.07           C  
ANISOU 3580  CA  THR A1112    21431  25391  20455    428   1971  -1260       C  
ATOM   3581  C   THR A1112      -2.783  -8.327   6.929  1.00179.82           C  
ANISOU 3581  C   THR A1112    21761  25711  20853    345   2001  -1225       C  
ATOM   3582  O   THR A1112      -3.793  -8.644   7.564  1.00179.61           O  
ANISOU 3582  O   THR A1112    21649  25699  20895    308   1977  -1298       O  
ATOM   3583  CB  THR A1112      -1.591 -10.348   5.909  1.00185.31           C  
ANISOU 3583  CB  THR A1112    22437  26413  21560    359   1992  -1255       C  
ATOM   3584  OG1 THR A1112      -1.111 -10.890   4.677  1.00186.29           O  
ANISOU 3584  OG1 THR A1112    22583  26582  21615    462   1958  -1292       O  
ATOM   3585  CG2 THR A1112      -2.394 -11.415   6.658  1.00183.54           C  
ANISOU 3585  CG2 THR A1112    22129  26144  21463    274   1967  -1329       C  
ATOM   3586  N   ARG A1113      -1.965  -7.327   7.294  1.00175.51           N  
ANISOU 3586  N   ARG A1113    21284  25130  20271    316   2054  -1122       N  
ATOM   3587  CA  ARG A1113      -2.169  -6.444   8.435  1.00174.77           C  
ANISOU 3587  CA  ARG A1113    21189  25008  20207    269   2066  -1097       C  
ATOM   3588  C   ARG A1113      -3.256  -5.415   8.099  1.00178.61           C  
ANISOU 3588  C   ARG A1113    21723  25501  20640    375   1999  -1148       C  
ATOM   3589  O   ARG A1113      -4.137  -5.185   8.922  1.00178.07           O  
ANISOU 3589  O   ARG A1113    21594  25464  20602    377   1967  -1210       O  
ATOM   3590  CB  ARG A1113      -0.847  -5.747   8.806  1.00174.88           C  
ANISOU 3590  CB  ARG A1113    21256  24973  20218    204   2129   -999       C  
ATOM   3591  CG  ARG A1113      -0.918  -4.835  10.029  1.00185.31           C  
ANISOU 3591  CG  ARG A1113    22573  26260  21577    167   2125   -994       C  
ATOM   3592  CD  ARG A1113       0.213  -3.818  10.060  1.00194.37           C  
ANISOU 3592  CD  ARG A1113    23786  27337  22729    115   2167   -925       C  
ATOM   3593  NE  ARG A1113       0.116  -2.845   8.968  1.00202.90           N  
ANISOU 3593  NE  ARG A1113    24997  28351  23746    166   2166   -873       N  
ATOM   3594  CZ  ARG A1113       1.142  -2.150   8.487  1.00216.92           C  
ANISOU 3594  CZ  ARG A1113    26846  30060  25514    103   2234   -787       C  
ATOM   3595  NH1 ARG A1113       2.357  -2.309   8.995  1.00203.03           N  
ANISOU 3595  NH1 ARG A1113    25012  28313  23817    -13   2298   -772       N  
ATOM   3596  NH2 ARG A1113       0.961  -1.293   7.492  1.00204.92           N  
ANISOU 3596  NH2 ARG A1113    25475  28466  23919    158   2244   -718       N  
ATOM   3597  N   ASN A1114      -3.196  -4.805   6.898  1.00175.47           N  
ANISOU 3597  N   ASN A1114    21440  25086  20146    482   1978  -1122       N  
ATOM   3598  CA  ASN A1114      -4.157  -3.790   6.462  1.00175.94           C  
ANISOU 3598  CA  ASN A1114    21585  25140  20125    626   1900  -1169       C  
ATOM   3599  C   ASN A1114      -5.541  -4.377   6.172  1.00179.87           C  
ANISOU 3599  C   ASN A1114    21978  25744  20622    725   1808  -1336       C  
ATOM   3600  O   ASN A1114      -6.540  -3.735   6.490  1.00179.93           O  
ANISOU 3600  O   ASN A1114    21972  25786  20608    810   1736  -1424       O  
ATOM   3601  CB  ASN A1114      -3.643  -3.044   5.227  1.00176.94           C  
ANISOU 3601  CB  ASN A1114    21891  25209  20127    724   1917  -1073       C  
ATOM   3602  CG  ASN A1114      -2.428  -2.178   5.471  1.00194.65           C  
ANISOU 3602  CG  ASN A1114    24241  27337  22381    615   2011   -919       C  
ATOM   3603  OD1 ASN A1114      -2.295  -1.502   6.495  1.00188.01           O  
ANISOU 3603  OD1 ASN A1114    23400  26425  21611    538   2012   -906       O  
ATOM   3604  ND2 ASN A1114      -1.524  -2.150   4.508  1.00185.09           N  
ANISOU 3604  ND2 ASN A1114    23114  26112  21098    610   2092   -812       N  
ATOM   3605  N   ALA A1115      -5.602  -5.585   5.579  1.00176.16           N  
ANISOU 3605  N   ALA A1115    21423  25330  20180    719   1801  -1400       N  
ATOM   3606  CA  ALA A1115      -6.853  -6.246   5.202  1.00176.63           C  
ANISOU 3606  CA  ALA A1115    21359  25488  20265    794   1711  -1585       C  
ATOM   3607  C   ALA A1115      -7.647  -6.795   6.392  1.00180.34           C  
ANISOU 3607  C   ALA A1115    21652  26004  20864    664   1725  -1669       C  
ATOM   3608  O   ALA A1115      -8.877  -6.723   6.367  1.00180.72           O  
ANISOU 3608  O   ALA A1115    21596  26149  20920    731   1653  -1827       O  
ATOM   3609  CB  ALA A1115      -6.575  -7.375   4.222  1.00177.61           C  
ANISOU 3609  CB  ALA A1115    21452  25636  20397    820   1693  -1635       C  
ATOM   3610  N   TYR A1116      -6.969  -7.356   7.410  1.00176.16           N  
ANISOU 3610  N   TYR A1116    21087  25422  20424    490   1818  -1571       N  
ATOM   3611  CA  TYR A1116      -7.664  -7.971   8.540  1.00176.20           C  
ANISOU 3611  CA  TYR A1116    20943  25469  20535    361   1858  -1619       C  
ATOM   3612  C   TYR A1116      -7.482  -7.223   9.867  1.00179.77           C  
ANISOU 3612  C   TYR A1116    21405  25922  20977    311   1913  -1536       C  
ATOM   3613  O   TYR A1116      -8.477  -6.825  10.473  1.00179.96           O  
ANISOU 3613  O   TYR A1116    21337  26041  20999    330   1896  -1618       O  
ATOM   3614  CB  TYR A1116      -7.215  -9.439   8.718  1.00177.29           C  
ANISOU 3614  CB  TYR A1116    21035  25546  20781    220   1916  -1589       C  
ATOM   3615  CG  TYR A1116      -7.338 -10.291   7.472  1.00179.79           C  
ANISOU 3615  CG  TYR A1116    21334  25855  21123    270   1847  -1691       C  
ATOM   3616  CD1 TYR A1116      -8.565 -10.821   7.084  1.00183.06           C  
ANISOU 3616  CD1 TYR A1116    21609  26334  21612    273   1785  -1874       C  
ATOM   3617  CD2 TYR A1116      -6.221 -10.600   6.702  1.00180.18           C  
ANISOU 3617  CD2 TYR A1116    21488  25847  21125    319   1842  -1626       C  
ATOM   3618  CE1 TYR A1116      -8.685 -11.605   5.937  1.00184.74           C  
ANISOU 3618  CE1 TYR A1116    21798  26541  21855    338   1701  -1998       C  
ATOM   3619  CE2 TYR A1116      -6.327 -11.386   5.556  1.00181.93           C  
ANISOU 3619  CE2 TYR A1116    21692  26075  21356    395   1765  -1736       C  
ATOM   3620  CZ  TYR A1116      -7.562 -11.888   5.178  1.00190.87           C  
ANISOU 3620  CZ  TYR A1116    22696  27259  22569    408   1687  -1926       C  
ATOM   3621  OH  TYR A1116      -7.676 -12.658   4.045  1.00193.08           O  
ANISOU 3621  OH  TYR A1116    22951  27548  22864    500   1591  -2063       O  
ATOM   3622  N   ILE A1117      -6.224  -7.058  10.319  1.00175.53           N  
ANISOU 3622  N   ILE A1117    20963  25301  20430    260   1971  -1396       N  
ATOM   3623  CA  ILE A1117      -5.836  -6.480  11.616  1.00174.86           C  
ANISOU 3623  CA  ILE A1117    20887  25211  20342    218   2015  -1326       C  
ATOM   3624  C   ILE A1117      -6.246  -4.993  11.774  1.00178.85           C  
ANISOU 3624  C   ILE A1117    21442  25735  20779    330   1949  -1361       C  
ATOM   3625  O   ILE A1117      -6.858  -4.661  12.793  1.00178.68           O  
ANISOU 3625  O   ILE A1117    21348  25789  20754    339   1947  -1404       O  
ATOM   3626  CB  ILE A1117      -4.306  -6.672  11.887  1.00177.14           C  
ANISOU 3626  CB  ILE A1117    21252  25414  20638    156   2072  -1205       C  
ATOM   3627  CG1 ILE A1117      -3.787  -8.101  11.507  1.00177.44           C  
ANISOU 3627  CG1 ILE A1117    21278  25418  20723     90   2109  -1180       C  
ATOM   3628  CG2 ILE A1117      -3.918  -6.298  13.322  1.00177.47           C  
ANISOU 3628  CG2 ILE A1117    21281  25468  20683    125   2108  -1161       C  
ATOM   3629  CD1 ILE A1117      -4.506  -9.362  12.127  1.00184.86           C  
ANISOU 3629  CD1 ILE A1117    22128  26373  21738      1   2148  -1205       C  
ATOM   3630  N   GLN A1118      -5.896  -4.114  10.802  1.00175.26           N  
ANISOU 3630  N   GLN A1118    21122  25207  20262    423   1898  -1339       N  
ATOM   3631  CA  GLN A1118      -6.167  -2.667  10.837  1.00175.35           C  
ANISOU 3631  CA  GLN A1118    21234  25182  20210    539   1825  -1358       C  
ATOM   3632  C   GLN A1118      -7.654  -2.342  11.043  1.00179.29           C  
ANISOU 3632  C   GLN A1118    21648  25805  20670    657   1740  -1510       C  
ATOM   3633  O   GLN A1118      -7.963  -1.418  11.796  1.00179.30           O  
ANISOU 3633  O   GLN A1118    21663  25818  20643    723   1690  -1548       O  
ATOM   3634  CB  GLN A1118      -5.661  -1.984   9.565  1.00177.23           C  
ANISOU 3634  CB  GLN A1118    21650  25312  20378    617   1802  -1293       C  
ATOM   3635  CG  GLN A1118      -5.815  -0.465   9.600  1.00195.79           C  
ANISOU 3635  CG  GLN A1118    24152  27568  22669    727   1729  -1288       C  
ATOM   3636  CD  GLN A1118      -5.463   0.248   8.333  1.00218.76           C  
ANISOU 3636  CD  GLN A1118    27267  30359  25491    814   1718  -1205       C  
ATOM   3637  OE1 GLN A1118      -5.327  -0.324   7.245  1.00214.67           O  
ANISOU 3637  OE1 GLN A1118    26776  29867  24921    844   1745  -1176       O  
ATOM   3638  NE2 GLN A1118      -5.348   1.557   8.440  1.00212.82           N  
ANISOU 3638  NE2 GLN A1118    26682  29470  24711    871   1673  -1166       N  
ATOM   3639  N   LYS A1119      -8.563  -3.110  10.400  1.00175.48           N  
ANISOU 3639  N   LYS A1119    21060  25424  20189    689   1715  -1618       N  
ATOM   3640  CA  LYS A1119     -10.020  -2.933  10.483  1.00175.81           C  
ANISOU 3640  CA  LYS A1119    20978  25623  20200    798   1635  -1799       C  
ATOM   3641  C   LYS A1119     -10.552  -3.084  11.919  1.00178.58           C  
ANISOU 3641  C   LYS A1119    21164  26097  20592    721   1684  -1841       C  
ATOM   3642  O   LYS A1119     -11.509  -2.395  12.282  1.00179.08           O  
ANISOU 3642  O   LYS A1119    21162  26283  20597    842   1610  -1970       O  
ATOM   3643  CB  LYS A1119     -10.744  -3.920   9.552  1.00178.77           C  
ANISOU 3643  CB  LYS A1119    21237  26084  20605    807   1612  -1922       C  
ATOM   3644  CG  LYS A1119     -10.645  -3.546   8.078  1.00191.22           C  
ANISOU 3644  CG  LYS A1119    22962  27607  22085    979   1523  -1942       C  
ATOM   3645  CD  LYS A1119     -11.564  -4.386   7.208  1.00200.30           C  
ANISOU 3645  CD  LYS A1119    23973  28876  23255   1037   1461  -2126       C  
ATOM   3646  CE  LYS A1119     -11.560  -3.904   5.778  1.00210.38           C  
ANISOU 3646  CE  LYS A1119    25410  30130  24397   1265   1358  -2159       C  
ATOM   3647  NZ  LYS A1119     -12.564  -4.621   4.949  1.00219.93           N  
ANISOU 3647  NZ  LYS A1119    26466  31480  25617   1364   1264  -2389       N  
ATOM   3648  N   TYR A1120      -9.925  -3.962  12.730  1.00173.43           N  
ANISOU 3648  N   TYR A1120    20456  25422  20018    542   1805  -1733       N  
ATOM   3649  CA  TYR A1120     -10.327  -4.201  14.117  1.00173.05           C  
ANISOU 3649  CA  TYR A1120    20271  25492  19987    469   1878  -1739       C  
ATOM   3650  C   TYR A1120      -9.612  -3.260  15.104  1.00175.25           C  
ANISOU 3650  C   TYR A1120    20640  25727  20218    516   1869  -1667       C  
ATOM   3651  O   TYR A1120     -10.168  -2.987  16.172  1.00175.14           O  
ANISOU 3651  O   TYR A1120    20530  25850  20168    549   1880  -1717       O  
ATOM   3652  CB  TYR A1120     -10.111  -5.673  14.506  1.00174.05           C  
ANISOU 3652  CB  TYR A1120    20313  25610  20207    275   2012  -1660       C  
ATOM   3653  CG  TYR A1120     -11.064  -6.616  13.800  1.00176.70           C  
ANISOU 3653  CG  TYR A1120    20511  26011  20617    210   2019  -1772       C  
ATOM   3654  CD1 TYR A1120     -12.412  -6.668  14.148  1.00180.19           C  
ANISOU 3654  CD1 TYR A1120    20754  26642  21067    204   2028  -1920       C  
ATOM   3655  CD2 TYR A1120     -10.622  -7.449  12.777  1.00177.06           C  
ANISOU 3655  CD2 TYR A1120    20606  25942  20728    158   2012  -1754       C  
ATOM   3656  CE1 TYR A1120     -13.298  -7.515  13.486  1.00182.10           C  
ANISOU 3656  CE1 TYR A1120    20844  26947  21401    131   2028  -2055       C  
ATOM   3657  CE2 TYR A1120     -11.499  -8.304  12.110  1.00179.05           C  
ANISOU 3657  CE2 TYR A1120    20722  26244  21064    104   1998  -1889       C  
ATOM   3658  CZ  TYR A1120     -12.837  -8.335  12.471  1.00187.43           C  
ANISOU 3658  CZ  TYR A1120    21579  27483  22153     80   2007  -2042       C  
ATOM   3659  OH  TYR A1120     -13.714  -9.167  11.820  1.00188.87           O  
ANISOU 3659  OH  TYR A1120    21602  27719  22441     13   1990  -2204       O  
ATOM   3660  N   LEU A1121      -8.408  -2.752  14.747  1.00170.41           N  
ANISOU 3660  N   LEU A1121    20199  24942  19608    522   1847  -1566       N  
ATOM   3661  CA  LEU A1121      -7.648  -1.812  15.583  1.00169.75           C  
ANISOU 3661  CA  LEU A1121    20197  24793  19505    559   1821  -1524       C  
ATOM   3662  C   LEU A1121      -8.341  -0.438  15.613  1.00174.09           C  
ANISOU 3662  C   LEU A1121    20799  25361  19986    735   1688  -1635       C  
ATOM   3663  O   LEU A1121      -8.383   0.192  16.672  1.00174.02           O  
ANISOU 3663  O   LEU A1121    20768  25401  19952    797   1652  -1677       O  
ATOM   3664  CB  LEU A1121      -6.192  -1.674  15.110  1.00169.01           C  
ANISOU 3664  CB  LEU A1121    20244  24518  19453    491   1843  -1405       C  
ATOM   3665  CG  LEU A1121      -5.268  -0.928  16.079  1.00173.53           C  
ANISOU 3665  CG  LEU A1121    20864  25028  20043    490   1829  -1379       C  
ATOM   3666  CD1 LEU A1121      -4.234  -1.858  16.683  1.00172.91           C  
ANISOU 3666  CD1 LEU A1121    20742  24949  20005    377   1924  -1298       C  
ATOM   3667  CD2 LEU A1121      -4.631   0.275  15.418  1.00176.40           C  
ANISOU 3667  CD2 LEU A1121    21389  25214  20419    521   1763  -1357       C  
ATOM   3668  N   GLU A1122      -8.914  -0.002  14.464  1.00170.84           N  
ANISOU 3668  N   GLU A1122    20463  24918  19533    842   1605  -1695       N  
ATOM   3669  CA  GLU A1122      -9.659   1.258  14.346  1.00171.58           C  
ANISOU 3669  CA  GLU A1122    20633  25016  19542   1045   1459  -1812       C  
ATOM   3670  C   GLU A1122     -10.924   1.193  15.209  1.00175.51           C  
ANISOU 3670  C   GLU A1122    20933  25762  19991   1130   1428  -1972       C  
ATOM   3671  O   GLU A1122     -11.250   2.172  15.882  1.00175.83           O  
ANISOU 3671  O   GLU A1122    20995  25840  19975   1272   1330  -2060       O  
ATOM   3672  CB  GLU A1122     -10.020   1.547  12.879  1.00173.63           C  
ANISOU 3672  CB  GLU A1122    21021  25207  19744   1161   1384  -1838       C  
ATOM   3673  CG  GLU A1122      -8.823   1.826  11.982  1.00183.83           C  
ANISOU 3673  CG  GLU A1122    22527  26267  21054   1103   1419  -1674       C  
ATOM   3674  CD  GLU A1122      -9.054   1.661  10.489  1.00203.42           C  
ANISOU 3674  CD  GLU A1122    25106  28718  23467   1190   1394  -1667       C  
ATOM   3675  OE1 GLU A1122      -9.857   0.785  10.090  1.00198.51           O  
ANISOU 3675  OE1 GLU A1122    24336  28253  22835   1214   1391  -1770       O  
ATOM   3676  OE2 GLU A1122      -8.407   2.401   9.714  1.00195.47           O  
ANISOU 3676  OE2 GLU A1122    24324  27528  22418   1231   1383  -1558       O  
ATOM   3677  N   ARG A1123     -11.608   0.020  15.212  1.00171.50           N  
ANISOU 3677  N   ARG A1123    20226  25425  19512   1034   1518  -2015       N  
ATOM   3678  CA  ARG A1123     -12.824  -0.249  15.990  1.00172.07           C  
ANISOU 3678  CA  ARG A1123    20066  25762  19549   1065   1535  -2158       C  
ATOM   3679  C   ARG A1123     -12.555  -0.189  17.496  1.00174.37           C  
ANISOU 3679  C   ARG A1123    20290  26138  19825   1028   1602  -2112       C  
ATOM   3680  O   ARG A1123     -13.377   0.353  18.235  1.00175.33           O  
ANISOU 3680  O   ARG A1123    20302  26450  19865   1157   1551  -2242       O  
ATOM   3681  CB  ARG A1123     -13.413  -1.625  15.638  1.00173.00           C  
ANISOU 3681  CB  ARG A1123    19998  25992  19741    908   1646  -2183       C  
ATOM   3682  CG  ARG A1123     -14.225  -1.680  14.352  1.00185.01           C  
ANISOU 3682  CG  ARG A1123    21488  27557  21252   1003   1552  -2332       C  
ATOM   3683  CD  ARG A1123     -14.921  -3.025  14.242  1.00196.96           C  
ANISOU 3683  CD  ARG A1123    22771  29201  22862    832   1658  -2395       C  
ATOM   3684  NE  ARG A1123     -15.274  -3.364  12.860  1.00207.03           N  
ANISOU 3684  NE  ARG A1123    24047  30453  24163    883   1580  -2502       N  
ATOM   3685  CZ  ARG A1123     -15.798  -4.528  12.482  1.00222.36           C  
ANISOU 3685  CZ  ARG A1123    25811  32460  26213    741   1641  -2581       C  
ATOM   3686  NH1 ARG A1123     -16.036  -5.480  13.376  1.00211.01           N  
ANISOU 3686  NH1 ARG A1123    24200  31097  24876    516   1797  -2541       N  
ATOM   3687  NH2 ARG A1123     -16.085  -4.748  11.206  1.00208.96           N  
ANISOU 3687  NH2 ARG A1123    24121  30748  24525    828   1543  -2702       N  
ATOM   3688  N   ALA A1124     -11.414  -0.758  17.948  1.00167.95           N  
ANISOU 3688  N   ALA A1124    19537  25204  19074    877   1710  -1941       N  
ATOM   3689  CA  ALA A1124     -11.010  -0.783  19.355  1.00166.77           C  
ANISOU 3689  CA  ALA A1124    19344  25126  18896    861   1773  -1888       C  
ATOM   3690  C   ALA A1124     -10.749   0.628  19.873  1.00168.54           C  
ANISOU 3690  C   ALA A1124    19667  25309  19060   1042   1628  -1961       C  
ATOM   3691  O   ALA A1124     -11.097   0.930  21.013  1.00168.83           O  
ANISOU 3691  O   ALA A1124    19612  25513  19022   1134   1620  -2025       O  
ATOM   3692  CB  ALA A1124      -9.772  -1.645  19.531  1.00166.33           C  
ANISOU 3692  CB  ALA A1124    19358  24929  18910    699   1886  -1712       C  
ATOM   3693  N   ARG A1125     -10.171   1.493  19.023  1.00163.01           N  
ANISOU 3693  N   ARG A1125    19158  24387  18391   1096   1515  -1953       N  
ATOM   3694  CA  ARG A1125      -9.861   2.882  19.341  1.00162.62           C  
ANISOU 3694  CA  ARG A1125    19241  24229  18318   1249   1364  -2020       C  
ATOM   3695  C   ARG A1125     -11.134   3.725  19.456  1.00165.65           C  
ANISOU 3695  C   ARG A1125    19580  24764  18596   1475   1223  -2211       C  
ATOM   3696  O   ARG A1125     -11.238   4.524  20.386  1.00165.89           O  
ANISOU 3696  O   ARG A1125    19603  24853  18574   1618   1127  -2309       O  
ATOM   3697  CB  ARG A1125      -8.911   3.473  18.291  1.00163.08           C  
ANISOU 3697  CB  ARG A1125    19526  23989  18447   1207   1316  -1932       C  
ATOM   3698  CG  ARG A1125      -7.451   3.087  18.527  1.00174.79           C  
ANISOU 3698  CG  ARG A1125    21054  25332  20028   1035   1409  -1794       C  
ATOM   3699  CD  ARG A1125      -6.643   2.972  17.248  1.00187.15           C  
ANISOU 3699  CD  ARG A1125    22761  26691  21657    919   1454  -1670       C  
ATOM   3700  NE  ARG A1125      -6.386   4.275  16.635  1.00199.48           N  
ANISOU 3700  NE  ARG A1125    24528  28035  23231    991   1345  -1675       N  
ATOM   3701  CZ  ARG A1125      -5.288   4.584  15.951  1.00214.79           C  
ANISOU 3701  CZ  ARG A1125    26610  29757  25243    877   1384  -1561       C  
ATOM   3702  NH1 ARG A1125      -4.323   3.686  15.791  1.00201.08           N  
ANISOU 3702  NH1 ARG A1125    24817  28018  23567    705   1514  -1455       N  
ATOM   3703  NH2 ARG A1125      -5.144   5.793  15.426  1.00203.44           N  
ANISOU 3703  NH2 ARG A1125    25376  28106  23814    935   1296  -1552       N  
ATOM   3704  N   SER A1126     -12.105   3.527  18.536  1.00160.93           N  
ANISOU 3704  N   SER A1126    18938  24247  17959   1527   1198  -2286       N  
ATOM   3705  CA  SER A1126     -13.375   4.262  18.493  1.00161.36           C  
ANISOU 3705  CA  SER A1126    18938  24469  17902   1764   1053  -2495       C  
ATOM   3706  C   SER A1126     -14.284   3.971  19.692  1.00163.79           C  
ANISOU 3706  C   SER A1126    18983  25118  18131   1815   1097  -2619       C  
ATOM   3707  O   SER A1126     -14.919   4.899  20.198  1.00164.51           O  
ANISOU 3707  O   SER A1126    19053  25331  18121   2042    955  -2787       O  
ATOM   3708  CB  SER A1126     -14.132   3.958  17.205  1.00165.03           C  
ANISOU 3708  CB  SER A1126    19393  24964  18347   1802   1025  -2559       C  
ATOM   3709  OG  SER A1126     -14.399   2.575  17.050  1.00172.57           O  
ANISOU 3709  OG  SER A1126    20150  26056  19362   1607   1189  -2519       O  
ATOM   3710  N   THR A1127     -14.356   2.693  20.131  1.00158.40           N  
ANISOU 3710  N   THR A1127    18109  24586  17488   1612   1296  -2533       N  
ATOM   3711  CA  THR A1127     -15.185   2.252  21.263  1.00158.71           C  
ANISOU 3711  CA  THR A1127    17894  24957  17452   1616   1394  -2608       C  
ATOM   3712  C   THR A1127     -14.710   2.893  22.570  1.00161.12           C  
ANISOU 3712  C   THR A1127    18227  25307  17685   1730   1357  -2607       C  
ATOM   3713  O   THR A1127     -15.540   3.295  23.384  1.00162.24           O  
ANISOU 3713  O   THR A1127    18218  25720  17705   1892   1318  -2756       O  
ATOM   3714  CB  THR A1127     -15.215   0.720  21.381  1.00166.30           C  
ANISOU 3714  CB  THR A1127    18703  25995  18487   1347   1630  -2474       C  
ATOM   3715  OG1 THR A1127     -13.882   0.208  21.324  1.00163.00           O  
ANISOU 3715  OG1 THR A1127    18446  25324  18162   1187   1708  -2263       O  
ATOM   3716  CG2 THR A1127     -16.086   0.062  20.312  1.00166.20           C  
ANISOU 3716  CG2 THR A1127    18568  26047  18532   1264   1657  -2556       C  
ATOM   3717  N   LEU A1128     -13.384   3.013  22.755  1.00154.97           N  
ANISOU 3717  N   LEU A1128    17625  24280  16976   1661   1358  -2465       N  
ATOM   3718  CA  LEU A1128     -12.793   3.631  23.943  1.00154.37           C  
ANISOU 3718  CA  LEU A1128    17585  24219  16849   1776   1301  -2483       C  
ATOM   3719  C   LEU A1128     -12.864   5.165  23.882  1.00157.98           C  
ANISOU 3719  C   LEU A1128    18180  24573  17273   2022   1052  -2650       C  
ATOM   3720  O   LEU A1128     -12.833   5.817  24.928  1.00158.10           O  
ANISOU 3720  O   LEU A1128    18170  24689  17212   2191    962  -2752       O  
ATOM   3721  CB  LEU A1128     -11.344   3.164  24.123  1.00152.85           C  
ANISOU 3721  CB  LEU A1128    17510  23811  16754   1614   1384  -2301       C  
ATOM   3722  CG  LEU A1128     -11.168   2.014  25.092  1.00157.24           C  
ANISOU 3722  CG  LEU A1128    17942  24535  17268   1505   1580  -2181       C  
ATOM   3723  CD1 LEU A1128     -11.258   0.679  24.387  1.00156.65           C  
ANISOU 3723  CD1 LEU A1128    17824  24427  17267   1269   1758  -2036       C  
ATOM   3724  CD2 LEU A1128      -9.853   2.110  25.790  1.00158.84           C  
ANISOU 3724  CD2 LEU A1128    18244  24610  17496   1507   1568  -2111       C  
ATOM   3725  N   SER A1129     -12.981   5.733  22.666  1.00154.04           N  
ANISOU 3725  N   SER A1129    17837  23872  16820   2059    936  -2680       N  
ATOM   3726  CA  SER A1129     -13.093   7.177  22.449  1.00154.63           C  
ANISOU 3726  CA  SER A1129    18090  23796  16866   2289    697  -2822       C  
ATOM   3727  C   SER A1129     -14.494   7.674  22.813  1.00159.27           C  
ANISOU 3727  C   SER A1129    18535  24683  17296   2553    575  -3058       C  
ATOM   3728  O   SER A1129     -14.667   8.853  23.131  1.00159.89           O  
ANISOU 3728  O   SER A1129    18718  24717  17317   2796    366  -3214       O  
ATOM   3729  CB  SER A1129     -12.769   7.525  21.001  1.00157.68           C  
ANISOU 3729  CB  SER A1129    18710  23873  17328   2245    640  -2747       C  
ATOM   3730  OG  SER A1129     -11.404   7.267  20.714  1.00164.55           O  
ANISOU 3730  OG  SER A1129    19714  24472  18337   2026    732  -2553       O  
ATOM   3731  N   LYS A1130     -15.480   6.757  22.789  1.00155.65           N  
ANISOU 3731  N   LYS A1130    17831  24535  16775   2502    707  -3096       N  
ATOM   3732  CA  LYS A1130     -16.892   6.972  23.115  1.00157.25           C  
ANISOU 3732  CA  LYS A1130    17821  25101  16828   2711    641  -3327       C  
ATOM   3733  C   LYS A1130     -17.058   7.333  24.621  1.00161.65           C  
ANISOU 3733  C   LYS A1130    18242  25912  17266   2866    618  -3429       C  
ATOM   3734  O   LYS A1130     -18.081   7.916  24.996  1.00163.17           O  
ANISOU 3734  O   LYS A1130    18306  26378  17315   3119    496  -3658       O  
ATOM   3735  CB  LYS A1130     -17.694   5.709  22.704  1.00159.91           C  
ANISOU 3735  CB  LYS A1130    17908  25673  17178   2527    837  -3308       C  
ATOM   3736  CG  LYS A1130     -19.077   5.481  23.319  1.00177.11           C  
ANISOU 3736  CG  LYS A1130    19757  28312  19223   2629    881  -3508       C  
ATOM   3737  CD  LYS A1130     -20.175   6.372  22.787  1.00188.75           C  
ANISOU 3737  CD  LYS A1130    21200  29933  20585   2929    659  -3791       C  
ATOM   3738  CE  LYS A1130     -21.469   5.964  23.437  1.00199.95           C  
ANISOU 3738  CE  LYS A1130    22240  31846  21887   2976    749  -3979       C  
ATOM   3739  NZ  LYS A1130     -22.449   7.072  23.452  1.00210.08           N  
ANISOU 3739  NZ  LYS A1130    23474  33342  23004   3356    500  -4294       N  
ATOM   3740  N   ILE A1131     -16.026   7.054  25.455  1.00156.51           N  
ANISOU 3740  N   ILE A1131    17630  25175  16663   2751    712  -3280       N  
ATOM   3741  CA  ILE A1131     -16.032   7.364  26.894  1.00156.95           C  
ANISOU 3741  CA  ILE A1131    17579  25459  16597   2913    689  -3364       C  
ATOM   3742  C   ILE A1131     -15.861   8.889  27.079  1.00160.99           C  
ANISOU 3742  C   ILE A1131    18271  25818  17081   3207    387  -3553       C  
ATOM   3743  O   ILE A1131     -14.752   9.408  26.934  1.00159.74           O  
ANISOU 3743  O   ILE A1131    18341  25307  17048   3164    296  -3484       O  
ATOM   3744  CB  ILE A1131     -14.964   6.555  27.694  1.00158.79           C  
ANISOU 3744  CB  ILE A1131    17808  25649  16876   2726    871  -3157       C  
ATOM   3745  CG1 ILE A1131     -15.034   5.043  27.389  1.00158.18           C  
ANISOU 3745  CG1 ILE A1131    17612  25639  16851   2424   1155  -2951       C  
ATOM   3746  CG2 ILE A1131     -15.106   6.808  29.203  1.00161.05           C  
ANISOU 3746  CG2 ILE A1131    17964  26232  16997   2931    857  -3255       C  
ATOM   3747  CD1 ILE A1131     -13.751   4.235  27.748  1.00163.53           C  
ANISOU 3747  CD1 ILE A1131    18380  26143  17612   2224   1304  -2721       C  
ATOM   3748  N   ASN A 446     -16.969   9.584  27.407  1.00158.11           N  
ANISOU 3748  N   ASN A 446    17120  28641  14314    907   1121    152       N  
ATOM   3749  CA  ASN A 446     -17.010  11.036  27.614  1.00156.64           C  
ANISOU 3749  CA  ASN A 446    16859  28462  14194    793   1132    468       C  
ATOM   3750  C   ASN A 446     -16.684  11.417  29.075  1.00157.46           C  
ANISOU 3750  C   ASN A 446    17003  28257  14568    728   1122    565       C  
ATOM   3751  O   ASN A 446     -16.550  10.536  29.933  1.00156.00           O  
ANISOU 3751  O   ASN A 446    16889  27860  14524    778   1097    394       O  
ATOM   3752  CB  ASN A 446     -18.374  11.604  27.193  1.00156.49           C  
ANISOU 3752  CB  ASN A 446    16871  28473  14116    724   1058    570       C  
ATOM   3753  CG  ASN A 446     -19.559  10.918  27.820  1.00172.84           C  
ANISOU 3753  CG  ASN A 446    19051  30323  16297    693    951    415       C  
ATOM   3754  OD1 ASN A 446     -19.915  11.171  28.973  1.00165.13           O  
ANISOU 3754  OD1 ASN A 446    18137  29065  15538    643    912    478       O  
ATOM   3755  ND2 ASN A 446     -20.214  10.057  27.060  1.00164.97           N  
ANISOU 3755  ND2 ASN A 446    18080  29467  15134    700    902    213       N  
ATOM   3756  N   GLU A 447     -16.527  12.731  29.344  1.00152.60           N  
ANISOU 3756  N   GLU A 447    16364  27611  14007    614   1147    841       N  
ATOM   3757  CA  GLU A 447     -16.187  13.248  30.675  1.00150.17           C  
ANISOU 3757  CA  GLU A 447    16106  27028  13924    523   1141    950       C  
ATOM   3758  C   GLU A 447     -17.344  13.066  31.675  1.00150.38           C  
ANISOU 3758  C   GLU A 447    16272  26722  14143    511   1047    895       C  
ATOM   3759  O   GLU A 447     -17.078  12.702  32.819  1.00148.65           O  
ANISOU 3759  O   GLU A 447    16100  26273  14108    502   1026    828       O  
ATOM   3760  CB  GLU A 447     -15.785  14.727  30.594  1.00152.14           C  
ANISOU 3760  CB  GLU A 447    16348  27314  14144    379   1194   1252       C  
ATOM   3761  CG  GLU A 447     -14.852  15.176  31.711  1.00162.80           C  
ANISOU 3761  CG  GLU A 447    17700  28511  15644    254   1219   1344       C  
ATOM   3762  CD  GLU A 447     -14.139  16.504  31.520  1.00186.94           C  
ANISOU 3762  CD  GLU A 447    20752  31652  18626     63   1288   1617       C  
ATOM   3763  OE1 GLU A 447     -13.701  16.795  30.383  1.00183.08           O  
ANISOU 3763  OE1 GLU A 447    20162  31471  17929     47   1354   1705       O  
ATOM   3764  OE2 GLU A 447     -13.963  17.228  32.528  1.00181.94           O  
ANISOU 3764  OE2 GLU A 447    20225  30776  18129    -87   1279   1737       O  
ATOM   3765  N   THR A 448     -18.614  13.278  31.233  1.00145.39           N  
ANISOU 3765  N   THR A 448    15687  26105  13450    520    992    927       N  
ATOM   3766  CA  THR A 448     -19.826  13.127  32.058  1.00142.79           C  
ANISOU 3766  CA  THR A 448    15454  25538  13260    511    907    892       C  
ATOM   3767  C   THR A 448     -19.944  11.695  32.609  1.00143.63           C  
ANISOU 3767  C   THR A 448    15604  25510  13458    540    857    612       C  
ATOM   3768  O   THR A 448     -20.416  11.514  33.729  1.00141.54           O  
ANISOU 3768  O   THR A 448    15419  24984  13374    511    808    584       O  
ATOM   3769  CB  THR A 448     -21.084  13.495  31.255  1.00151.82           C  
ANISOU 3769  CB  THR A 448    16583  26847  14254    536    863    969       C  
ATOM   3770  OG1 THR A 448     -20.813  14.630  30.434  1.00154.45           O  
ANISOU 3770  OG1 THR A 448    16885  27356  14442    541    925   1205       O  
ATOM   3771  CG2 THR A 448     -22.240  13.841  32.153  1.00148.55           C  
ANISOU 3771  CG2 THR A 448    16242  26231  13967    534    799   1045       C  
ATOM   3772  N   MET A 449     -19.482  10.697  31.821  1.00139.96           N  
ANISOU 3772  N   MET A 449    15109  25213  12855    603    877    411       N  
ATOM   3773  CA  MET A 449     -19.450   9.271  32.147  1.00138.95           C  
ANISOU 3773  CA  MET A 449    15073  24956  12766    650    850    134       C  
ATOM   3774  C   MET A 449     -18.495   9.028  33.321  1.00138.45           C  
ANISOU 3774  C   MET A 449    15041  24671  12892    692    882    118       C  
ATOM   3775  O   MET A 449     -18.907   8.433  34.314  1.00136.63           O  
ANISOU 3775  O   MET A 449    14921  24175  12819    675    832     22       O  
ATOM   3776  CB  MET A 449     -19.007   8.463  30.904  1.00143.73           C  
ANISOU 3776  CB  MET A 449    15663  25810  13138    739    892    -47       C  
ATOM   3777  CG  MET A 449     -19.348   6.986  30.963  1.00148.20           C  
ANISOU 3777  CG  MET A 449    16393  26237  13678    767    853   -348       C  
ATOM   3778  SD  MET A 449     -18.783   6.068  29.511  1.00155.33           S  
ANISOU 3778  SD  MET A 449    17330  27406  14283    896    915   -575       S  
ATOM   3779  CE  MET A 449     -20.095   6.467  28.334  1.00153.17           C  
ANISOU 3779  CE  MET A 449    16999  27404  13795    752    839   -545       C  
ATOM   3780  N   LEU A 450     -17.234   9.515  33.214  1.00132.98           N  
ANISOU 3780  N   LEU A 450    14238  24117  12171    734    963    226       N  
ATOM   3781  CA  LEU A 450     -16.209   9.358  34.248  1.00130.70           C  
ANISOU 3781  CA  LEU A 450    13931  23705  12022    774    995    233       C  
ATOM   3782  C   LEU A 450     -16.510  10.215  35.472  1.00129.25           C  
ANISOU 3782  C   LEU A 450    13788  23275  12046    646    954    398       C  
ATOM   3783  O   LEU A 450     -16.215   9.784  36.585  1.00127.56           O  
ANISOU 3783  O   LEU A 450    13621  22859  11986    668    936    344       O  
ATOM   3784  CB  LEU A 450     -14.815   9.683  33.700  1.00132.27           C  
ANISOU 3784  CB  LEU A 450    13961  24205  12091    826   1091    316       C  
ATOM   3785  CG  LEU A 450     -14.254   8.719  32.645  1.00138.99           C  
ANISOU 3785  CG  LEU A 450    14771  25307  12731   1010   1152    136       C  
ATOM   3786  CD1 LEU A 450     -12.994   9.272  32.034  1.00140.93           C  
ANISOU 3786  CD1 LEU A 450    14809  25914  12825   1035   1250    271       C  
ATOM   3787  CD2 LEU A 450     -13.995   7.314  33.224  1.00141.19           C  
ANISOU 3787  CD2 LEU A 450    15173  25411  13063   1195   1152   -103       C  
ATOM   3788  N   ARG A 451     -17.118  11.405  35.268  1.00123.37           N  
ANISOU 3788  N   ARG A 451    13044  22540  11290    533    943    597       N  
ATOM   3789  CA  ARG A 451     -17.522  12.328  36.333  1.00120.73           C  
ANISOU 3789  CA  ARG A 451    12790  21960  11120    428    912    759       C  
ATOM   3790  C   ARG A 451     -18.591  11.672  37.211  1.00120.39           C  
ANISOU 3790  C   ARG A 451    12860  21659  11223    446    834    641       C  
ATOM   3791  O   ARG A 451     -18.563  11.834  38.432  1.00118.23           O  
ANISOU 3791  O   ARG A 451    12652  21150  11119    407    812    675       O  
ATOM   3792  CB  ARG A 451     -18.040  13.654  35.745  1.00121.64           C  
ANISOU 3792  CB  ARG A 451    12926  22143  11149    357    929    988       C  
ATOM   3793  CG  ARG A 451     -17.933  14.831  36.712  1.00130.90           C  
ANISOU 3793  CG  ARG A 451    14202  23092  12443    245    939   1187       C  
ATOM   3794  CD  ARG A 451     -18.710  16.038  36.228  1.00138.86           C  
ANISOU 3794  CD  ARG A 451    15302  24092  13367    228    954   1401       C  
ATOM   3795  NE  ARG A 451     -18.709  17.130  37.208  1.00140.51           N  
ANISOU 3795  NE  ARG A 451    15676  24029  13683    136    966   1572       N  
ATOM   3796  CZ  ARG A 451     -19.656  18.058  37.293  1.00149.07           C  
ANISOU 3796  CZ  ARG A 451    16912  24974  14752    178    967   1732       C  
ATOM   3797  NH1 ARG A 451     -20.696  18.032  36.471  1.00133.14           N  
ANISOU 3797  NH1 ARG A 451    14865  23103  12619    309    949   1757       N  
ATOM   3798  NH2 ARG A 451     -19.576  19.014  38.209  1.00134.57           N  
ANISOU 3798  NH2 ARG A 451    15266  22862  13000    101    987   1868       N  
ATOM   3799  N   LEU A 452     -19.502  10.895  36.584  1.00115.73           N  
ANISOU 3799  N   LEU A 452    12290  21134  10549    487    791    497       N  
ATOM   3800  CA  LEU A 452     -20.554  10.143  37.264  1.00113.81           C  
ANISOU 3800  CA  LEU A 452    12140  20699  10403    470    717    372       C  
ATOM   3801  C   LEU A 452     -19.933   9.122  38.226  1.00116.24           C  
ANISOU 3801  C   LEU A 452    12522  20800  10846    510    714    215       C  
ATOM   3802  O   LEU A 452     -20.418   8.979  39.346  1.00115.10           O  
ANISOU 3802  O   LEU A 452    12456  20420  10858    472    671    212       O  
ATOM   3803  CB  LEU A 452     -21.470   9.448  36.241  1.00114.88           C  
ANISOU 3803  CB  LEU A 452    12272  21005  10374    462    674    234       C  
ATOM   3804  CG  LEU A 452     -22.760   8.832  36.776  1.00118.71           C  
ANISOU 3804  CG  LEU A 452    12827  21366  10912    386    591    141       C  
ATOM   3805  CD1 LEU A 452     -23.814   9.901  37.039  1.00118.21           C  
ANISOU 3805  CD1 LEU A 452    12714  21334  10868    357    559    347       C  
ATOM   3806  CD2 LEU A 452     -23.302   7.807  35.805  1.00122.50           C  
ANISOU 3806  CD2 LEU A 452    13330  22001  11214    341    552    -64       C  
ATOM   3807  N   GLY A 453     -18.851   8.469  37.795  1.00112.66           N  
ANISOU 3807  N   GLY A 453    12039  20448  10317    607    767    105       N  
ATOM   3808  CA  GLY A 453     -18.109   7.499  38.592  1.00111.81           C  
ANISOU 3808  CA  GLY A 453    12000  20184  10300    702    781    -28       C  
ATOM   3809  C   GLY A 453     -17.371   8.128  39.755  1.00113.23           C  
ANISOU 3809  C   GLY A 453    12133  20256  10633    682    793    112       C  
ATOM   3810  O   GLY A 453     -17.323   7.542  40.841  1.00112.01           O  
ANISOU 3810  O   GLY A 453    12064  19880  10614    713    768     50       O  
ATOM   3811  N   ILE A 454     -16.797   9.337  39.536  1.00108.65           N  
ANISOU 3811  N   ILE A 454    11433  19831  10019    611    831    307       N  
ATOM   3812  CA  ILE A 454     -16.075  10.116  40.552  1.00106.92           C  
ANISOU 3812  CA  ILE A 454    11173  19541   9911    533    840    454       C  
ATOM   3813  C   ILE A 454     -17.055  10.440  41.681  1.00107.21           C  
ANISOU 3813  C   ILE A 454    11339  19277  10118    451    777    500       C  
ATOM   3814  O   ILE A 454     -16.737  10.212  42.848  1.00105.49           O  
ANISOU 3814  O   ILE A 454    11157  18894  10030    451    757    486       O  
ATOM   3815  CB  ILE A 454     -15.417  11.386  39.932  1.00110.87           C  
ANISOU 3815  CB  ILE A 454    11562  20258  10305    420    893    654       C  
ATOM   3816  CG1 ILE A 454     -14.255  10.997  38.992  1.00113.05           C  
ANISOU 3816  CG1 ILE A 454    11673  20870  10409    510    964    614       C  
ATOM   3817  CG2 ILE A 454     -14.937  12.372  41.017  1.00110.89           C  
ANISOU 3817  CG2 ILE A 454    11581  20139  10415    265    888    816       C  
ATOM   3818  CD1 ILE A 454     -13.992  11.980  37.881  1.00122.31           C  
ANISOU 3818  CD1 ILE A 454    12754  22298  11419    414   1017    770       C  
ATOM   3819  N   PHE A 455     -18.267  10.897  41.312  1.00102.94           N  
ANISOU 3819  N   PHE A 455    10857  18697   9558    404    747    551       N  
ATOM   3820  CA  PHE A 455     -19.355  11.208  42.236  1.00101.22           C  
ANISOU 3820  CA  PHE A 455    10745  18247   9465    358    696    599       C  
ATOM   3821  C   PHE A 455     -19.842   9.942  42.936  1.00103.92           C  
ANISOU 3821  C   PHE A 455    11161  18422   9902    400    647    422       C  
ATOM   3822  O   PHE A 455     -20.115   9.991  44.130  1.00101.80           O  
ANISOU 3822  O   PHE A 455    10963  17943   9773    372    619    446       O  
ATOM   3823  CB  PHE A 455     -20.504  11.902  41.494  1.00103.26           C  
ANISOU 3823  CB  PHE A 455    11013  18589   9632    343    684    698       C  
ATOM   3824  CG  PHE A 455     -20.367  13.405  41.443  1.00105.11           C  
ANISOU 3824  CG  PHE A 455    11278  18819   9838    292    724    926       C  
ATOM   3825  CD1 PHE A 455     -19.377  14.005  40.669  1.00109.51           C  
ANISOU 3825  CD1 PHE A 455    11775  19546  10286    249    783   1018       C  
ATOM   3826  CD2 PHE A 455     -21.229  14.222  42.163  1.00106.94           C  
ANISOU 3826  CD2 PHE A 455    11621  18874  10136    290    710   1052       C  
ATOM   3827  CE1 PHE A 455     -19.245  15.395  40.630  1.00111.10           C  
ANISOU 3827  CE1 PHE A 455    12057  19706  10450    172    825   1233       C  
ATOM   3828  CE2 PHE A 455     -21.110  15.612  42.107  1.00110.44           C  
ANISOU 3828  CE2 PHE A 455    12158  19267  10537    255    756   1259       C  
ATOM   3829  CZ  PHE A 455     -20.108  16.189  41.354  1.00109.77           C  
ANISOU 3829  CZ  PHE A 455    12042  19315  10349    180    812   1348       C  
ATOM   3830  N   GLY A 456     -19.886   8.830  42.195  1.00101.69           N  
ANISOU 3830  N   GLY A 456    10882  18224   9530    459    644    247       N  
ATOM   3831  CA  GLY A 456     -20.274   7.511  42.683  1.00101.76           C  
ANISOU 3831  CA  GLY A 456    11007  18065   9594    483    608     63       C  
ATOM   3832  C   GLY A 456     -19.381   7.020  43.801  1.00106.63           C  
ANISOU 3832  C   GLY A 456    11671  18511  10334    554    621     30       C  
ATOM   3833  O   GLY A 456     -19.880   6.582  44.840  1.00105.88           O  
ANISOU 3833  O   GLY A 456    11677  18193  10360    526    582     -3       O  
ATOM   3834  N   PHE A 457     -18.053   7.122  43.607  1.00104.83           N  
ANISOU 3834  N   PHE A 457    11352  18419  10061    646    675     53       N  
ATOM   3835  CA  PHE A 457     -17.073   6.737  44.621  1.00105.22           C  
ANISOU 3835  CA  PHE A 457    11402  18382  10196    734    689     45       C  
ATOM   3836  C   PHE A 457     -17.091   7.733  45.771  1.00107.90           C  
ANISOU 3836  C   PHE A 457    11719  18609  10669    618    662    205       C  
ATOM   3837  O   PHE A 457     -16.970   7.320  46.927  1.00107.23           O  
ANISOU 3837  O   PHE A 457    11697  18348  10697    645    638    186       O  
ATOM   3838  CB  PHE A 457     -15.661   6.616  44.032  1.00109.06           C  
ANISOU 3838  CB  PHE A 457    11752  19126  10562    868    757     42       C  
ATOM   3839  CG  PHE A 457     -15.393   5.298  43.350  1.00112.95           C  
ANISOU 3839  CG  PHE A 457    12324  19650  10940   1064    795   -151       C  
ATOM   3840  CD1 PHE A 457     -15.146   4.148  44.094  1.00116.82           C  
ANISOU 3840  CD1 PHE A 457    12956  19949  11481   1221    796   -269       C  
ATOM   3841  CD2 PHE A 457     -15.362   5.210  41.966  1.00117.16           C  
ANISOU 3841  CD2 PHE A 457    12820  20396  11301   1105    834   -213       C  
ATOM   3842  CE1 PHE A 457     -14.906   2.928  43.468  1.00119.93           C  
ANISOU 3842  CE1 PHE A 457    13486  20328  11754   1420    841   -452       C  
ATOM   3843  CE2 PHE A 457     -15.114   3.989  41.336  1.00122.14           C  
ANISOU 3843  CE2 PHE A 457    13567  21034  11808   1296    875   -407       C  
ATOM   3844  CZ  PHE A 457     -14.884   2.856  42.093  1.00120.82           C  
ANISOU 3844  CZ  PHE A 457    13572  20643  11692   1457    882   -528       C  
ATOM   3845  N   LEU A 458     -17.286   9.037  45.456  1.00103.65           N  
ANISOU 3845  N   LEU A 458    11122  18155  10105    492    668    361       N  
ATOM   3846  CA  LEU A 458     -17.366  10.124  46.438  1.00102.05           C  
ANISOU 3846  CA  LEU A 458    10948  17826  10000    370    650    512       C  
ATOM   3847  C   LEU A 458     -18.556   9.912  47.368  1.00102.71           C  
ANISOU 3847  C   LEU A 458    11163  17656  10207    353    599    488       C  
ATOM   3848  O   LEU A 458     -18.428  10.107  48.577  1.00100.89           O  
ANISOU 3848  O   LEU A 458    10982  17268  10083    320    578    529       O  
ATOM   3849  CB  LEU A 458     -17.460  11.492  45.742  1.00102.66           C  
ANISOU 3849  CB  LEU A 458    11001  18010   9996    261    679    676       C  
ATOM   3850  CG  LEU A 458     -16.930  12.699  46.526  1.00107.55           C  
ANISOU 3850  CG  LEU A 458    11654  18555  10654    118    687    834       C  
ATOM   3851  CD1 LEU A 458     -15.398  12.689  46.618  1.00108.83           C  
ANISOU 3851  CD1 LEU A 458    11678  18907  10765     70    714    853       C  
ATOM   3852  CD2 LEU A 458     -17.367  13.989  45.877  1.00110.90           C  
ANISOU 3852  CD2 LEU A 458    12144  18994  11000     29    717    992       C  
ATOM   3853  N   ALA A 459     -19.689   9.463  46.803  1.00 98.82           N  
ANISOU 3853  N   ALA A 459    10712  17156   9681    367    577    419       N  
ATOM   3854  CA  ALA A 459     -20.906   9.145  47.544  1.00 97.64           C  
ANISOU 3854  CA  ALA A 459    10654  16830   9615    340    531    393       C  
ATOM   3855  C   ALA A 459     -20.708   7.856  48.338  1.00101.56           C  
ANISOU 3855  C   ALA A 459    11228  17167  10192    385    510    254       C  
ATOM   3856  O   ALA A 459     -21.141   7.787  49.490  1.00100.95           O  
ANISOU 3856  O   ALA A 459    11221  16911  10224    357    482    276       O  
ATOM   3857  CB  ALA A 459     -22.088   9.012  46.597  1.00 98.78           C  
ANISOU 3857  CB  ALA A 459    10784  17089   9661    316    511    363       C  
ATOM   3858  N   PHE A 460     -20.006   6.856  47.740  1.00 98.04           N  
ANISOU 3858  N   PHE A 460    10789  16782   9681    474    531    120       N  
ATOM   3859  CA  PHE A 460     -19.702   5.571  48.376  1.00 97.79           C  
ANISOU 3859  CA  PHE A 460    10873  16585   9698    559    526    -10       C  
ATOM   3860  C   PHE A 460     -18.902   5.762  49.662  1.00101.84           C  
ANISOU 3860  C   PHE A 460    11374  17001  10320    603    526     65       C  
ATOM   3861  O   PHE A 460     -19.170   5.069  50.647  1.00102.15           O  
ANISOU 3861  O   PHE A 460    11528  16837  10446    619    502     24       O  
ATOM   3862  CB  PHE A 460     -18.939   4.639  47.428  1.00100.84           C  
ANISOU 3862  CB  PHE A 460    11281  17069   9963    697    568   -149       C  
ATOM   3863  CG  PHE A 460     -18.671   3.270  48.006  1.00102.93           C  
ANISOU 3863  CG  PHE A 460    11722  17131  10255    818    575   -283       C  
ATOM   3864  CD1 PHE A 460     -17.493   3.005  48.694  1.00106.26           C  
ANISOU 3864  CD1 PHE A 460    12122  17546  10707    987    605   -260       C  
ATOM   3865  CD2 PHE A 460     -19.607   2.251  47.887  1.00105.92           C  
ANISOU 3865  CD2 PHE A 460    12300  17330  10614    756    550   -423       C  
ATOM   3866  CE1 PHE A 460     -17.259   1.747  49.253  1.00108.28           C  
ANISOU 3866  CE1 PHE A 460    12568  17598  10977   1136    618   -366       C  
ATOM   3867  CE2 PHE A 460     -19.366   0.991  48.439  1.00109.87           C  
ANISOU 3867  CE2 PHE A 460    13019  17596  11130    865    564   -537       C  
ATOM   3868  CZ  PHE A 460     -18.191   0.745  49.112  1.00108.23           C  
ANISOU 3868  CZ  PHE A 460    12802  17364  10955   1077    601   -504       C  
ATOM   3869  N   GLY A 461     -17.926   6.673  49.627  1.00 97.70           N  
ANISOU 3869  N   GLY A 461    10714  16634   9772    604    551    174       N  
ATOM   3870  CA  GLY A 461     -17.077   6.994  50.767  1.00 97.25           C  
ANISOU 3870  CA  GLY A 461    10615  16549   9785    611    544    254       C  
ATOM   3871  C   GLY A 461     -17.884   7.379  51.987  1.00100.07           C  
ANISOU 3871  C   GLY A 461    11066  16691  10267    514    501    315       C  
ATOM   3872  O   GLY A 461     -17.786   6.726  53.031  1.00 99.13           O  
ANISOU 3872  O   GLY A 461    11015  16427  10223    567    480    284       O  
ATOM   3873  N   PHE A 462     -18.748   8.396  51.824  1.00 96.57           N  
ANISOU 3873  N   PHE A 462    10636  16226   9829    396    493    402       N  
ATOM   3874  CA  PHE A 462     -19.634   8.911  52.867  1.00 95.76           C  
ANISOU 3874  CA  PHE A 462    10622  15945   9817    325    465    470       C  
ATOM   3875  C   PHE A 462     -20.613   7.845  53.387  1.00 98.71           C  
ANISOU 3875  C   PHE A 462    11092  16161  10252    349    435    380       C  
ATOM   3876  O   PHE A 462     -20.924   7.851  54.579  1.00 97.41           O  
ANISOU 3876  O   PHE A 462    10993  15847  10172    330    414    411       O  
ATOM   3877  CB  PHE A 462     -20.421  10.127  52.358  1.00 97.75           C  
ANISOU 3877  CB  PHE A 462    10883  16233  10026    255    478    579       C  
ATOM   3878  CG  PHE A 462     -19.634  11.404  52.152  1.00 99.87           C  
ANISOU 3878  CG  PHE A 462    11128  16576  10243    181    507    701       C  
ATOM   3879  CD1 PHE A 462     -18.888  11.958  53.188  1.00102.67           C  
ANISOU 3879  CD1 PHE A 462    11516  16854  10638    108    501    760       C  
ATOM   3880  CD2 PHE A 462     -19.703  12.095  50.950  1.00102.88           C  
ANISOU 3880  CD2 PHE A 462    11472  17099  10520    159    540    764       C  
ATOM   3881  CE1 PHE A 462     -18.186  13.151  53.007  1.00104.11           C  
ANISOU 3881  CE1 PHE A 462    11709  17092  10756    -15    526    871       C  
ATOM   3882  CE2 PHE A 462     -19.003  13.291  50.773  1.00106.38           C  
ANISOU 3882  CE2 PHE A 462    11929  17585  10904     58    572    888       C  
ATOM   3883  CZ  PHE A 462     -18.251  13.811  51.803  1.00104.20           C  
ANISOU 3883  CZ  PHE A 462    11702  17221  10668    -44    565    937       C  
ATOM   3884  N   VAL A 463     -21.092   6.940  52.501  1.00 95.48           N  
ANISOU 3884  N   VAL A 463    10702  15790   9786    369    434    269       N  
ATOM   3885  CA  VAL A 463     -22.005   5.844  52.861  1.00 95.16           C  
ANISOU 3885  CA  VAL A 463    10772  15608   9776    341    407    176       C  
ATOM   3886  C   VAL A 463     -21.224   4.838  53.738  1.00 98.09           C  
ANISOU 3886  C   VAL A 463    11239  15822  10207    432    408    112       C  
ATOM   3887  O   VAL A 463     -21.757   4.376  54.754  1.00 97.19           O  
ANISOU 3887  O   VAL A 463    11221  15538  10167    398    386    112       O  
ATOM   3888  CB  VAL A 463     -22.664   5.187  51.609  1.00100.23           C  
ANISOU 3888  CB  VAL A 463    11429  16342  10310    298    403     66       C  
ATOM   3889  CG1 VAL A 463     -23.432   3.915  51.969  1.00100.74           C  
ANISOU 3889  CG1 VAL A 463    11644  16246  10386    226    376    -48       C  
ATOM   3890  CG2 VAL A 463     -23.595   6.169  50.903  1.00 99.83           C  
ANISOU 3890  CG2 VAL A 463    11275  16464  10193    224    395    153       C  
ATOM   3891  N   LEU A 464     -19.944   4.564  53.377  1.00 94.24           N  
ANISOU 3891  N   LEU A 464    10713  15418   9676    563    439     76       N  
ATOM   3892  CA  LEU A 464     -19.057   3.668  54.122  1.00 94.33           C  
ANISOU 3892  CA  LEU A 464    10796  15331   9716    709    449     36       C  
ATOM   3893  C   LEU A 464     -18.779   4.221  55.529  1.00 95.53           C  
ANISOU 3893  C   LEU A 464    10915  15420   9960    688    424    147       C  
ATOM   3894  O   LEU A 464     -18.710   3.442  56.482  1.00 95.27           O  
ANISOU 3894  O   LEU A 464    10991  15230   9979    755    413    130       O  
ATOM   3895  CB  LEU A 464     -17.746   3.438  53.353  1.00 95.99           C  
ANISOU 3895  CB  LEU A 464    10918  15727   9826    878    494     -1       C  
ATOM   3896  CG  LEU A 464     -16.791   2.362  53.896  1.00102.78           C  
ANISOU 3896  CG  LEU A 464    11854  16527  10671   1102    518    -50       C  
ATOM   3897  CD1 LEU A 464     -17.386   0.959  53.766  1.00104.40           C  
ANISOU 3897  CD1 LEU A 464    12324  16483  10859   1168    530   -192       C  
ATOM   3898  CD2 LEU A 464     -15.453   2.423  53.190  1.00107.08           C  
ANISOU 3898  CD2 LEU A 464    12241  17347  11098   1277    567    -46       C  
ATOM   3899  N   ILE A 465     -18.662   5.560  55.653  1.00 89.81           N  
ANISOU 3899  N   ILE A 465    10072  14805   9245    589    417    261       N  
ATOM   3900  CA  ILE A 465     -18.443   6.260  56.923  1.00 88.08           C  
ANISOU 3900  CA  ILE A 465     9840  14534   9092    534    392    360       C  
ATOM   3901  C   ILE A 465     -19.729   6.192  57.764  1.00 91.47           C  
ANISOU 3901  C   ILE A 465    10388  14765   9600    461    367    373       C  
ATOM   3902  O   ILE A 465     -19.648   5.858  58.946  1.00 90.83           O  
ANISOU 3902  O   ILE A 465    10367  14568   9577    484    348    391       O  
ATOM   3903  CB  ILE A 465     -17.958   7.729  56.700  1.00 90.52           C  
ANISOU 3903  CB  ILE A 465    10043  14989   9361    423    399    466       C  
ATOM   3904  CG1 ILE A 465     -16.639   7.815  55.873  1.00 91.94           C  
ANISOU 3904  CG1 ILE A 465    10072  15418   9442    468    426    469       C  
ATOM   3905  CG2 ILE A 465     -17.847   8.513  58.010  1.00 90.18           C  
ANISOU 3905  CG2 ILE A 465    10034  14864   9367    335    371    552       C  
ATOM   3906  CD1 ILE A 465     -15.376   7.025  56.383  1.00101.35           C  
ANISOU 3906  CD1 ILE A 465    11181  16722  10603    612    425    448       C  
ATOM   3907  N   THR A 466     -20.906   6.487  57.148  1.00 88.53           N  
ANISOU 3907  N   THR A 466    10032  14391   9213    381    369    373       N  
ATOM   3908  CA  THR A 466     -22.232   6.455  57.794  1.00 88.11           C  
ANISOU 3908  CA  THR A 466    10050  14224   9204    311    353    397       C  
ATOM   3909  C   THR A 466     -22.463   5.076  58.416  1.00 92.95           C  
ANISOU 3909  C   THR A 466    10777  14682   9857    329    339    320       C  
ATOM   3910  O   THR A 466     -22.860   4.995  59.580  1.00 92.07           O  
ANISOU 3910  O   THR A 466    10723  14455   9804    306    325    364       O  
ATOM   3911  CB  THR A 466     -23.351   6.833  56.792  1.00 96.29           C  
ANISOU 3911  CB  THR A 466    11043  15366  10177    248    358    405       C  
ATOM   3912  OG1 THR A 466     -23.074   8.119  56.240  1.00 97.71           O  
ANISOU 3912  OG1 THR A 466    11154  15661  10312    251    380    491       O  
ATOM   3913  CG2 THR A 466     -24.735   6.865  57.429  1.00 93.06           C  
ANISOU 3913  CG2 THR A 466    10659  14914   9784    185    346    448       C  
ATOM   3914  N   PHE A 467     -22.162   4.005  57.654  1.00 91.03           N  
ANISOU 3914  N   PHE A 467    10590  14425   9571    376    348    209       N  
ATOM   3915  CA  PHE A 467     -22.289   2.623  58.103  1.00 91.90           C  
ANISOU 3915  CA  PHE A 467    10870  14349   9698    399    345    129       C  
ATOM   3916  C   PHE A 467     -21.451   2.377  59.358  1.00 96.52           C  
ANISOU 3916  C   PHE A 467    11500  14830  10342    513    343    177       C  
ATOM   3917  O   PHE A 467     -21.977   1.852  60.340  1.00 96.40           O  
ANISOU 3917  O   PHE A 467    11597  14656  10375    474    331    196       O  
ATOM   3918  CB  PHE A 467     -21.871   1.657  56.990  1.00 95.00           C  
ANISOU 3918  CB  PHE A 467    11349  14738  10009    471    369     -3       C  
ATOM   3919  CG  PHE A 467     -21.968   0.199  57.370  1.00 97.78           C  
ANISOU 3919  CG  PHE A 467    11944  14850  10357    501    377    -93       C  
ATOM   3920  CD1 PHE A 467     -23.170  -0.487  57.257  1.00101.54           C  
ANISOU 3920  CD1 PHE A 467    12562  15209  10810    311    360   -154       C  
ATOM   3921  CD2 PHE A 467     -20.853  -0.491  57.836  1.00100.65           C  
ANISOU 3921  CD2 PHE A 467    12405  15116  10721    716    403   -107       C  
ATOM   3922  CE1 PHE A 467     -23.259  -1.835  57.613  1.00104.14           C  
ANISOU 3922  CE1 PHE A 467    13167  15278  11123    309    373   -233       C  
ATOM   3923  CE2 PHE A 467     -20.944  -1.836  58.199  1.00105.17           C  
ANISOU 3923  CE2 PHE A 467    13253  15428  11278    766    420   -178       C  
ATOM   3924  CZ  PHE A 467     -22.145  -2.500  58.080  1.00104.20           C  
ANISOU 3924  CZ  PHE A 467    13309  15143  11138    549    406   -244       C  
ATOM   3925  N   SER A 468     -20.160   2.776  59.321  1.00 93.19           N  
ANISOU 3925  N   SER A 468    10974  14531   9902    642    354    206       N  
ATOM   3926  CA  SER A 468     -19.190   2.625  60.408  1.00 93.06           C  
ANISOU 3926  CA  SER A 468    10950  14498   9909    764    346    260       C  
ATOM   3927  C   SER A 468     -19.655   3.312  61.699  1.00 96.31           C  
ANISOU 3927  C   SER A 468    11355  14850  10389    663    315    356       C  
ATOM   3928  O   SER A 468     -19.398   2.791  62.787  1.00 96.17           O  
ANISOU 3928  O   SER A 468    11406  14734  10399    731    302    386       O  
ATOM   3929  CB  SER A 468     -17.832   3.179  59.988  1.00 96.47           C  
ANISOU 3929  CB  SER A 468    11209  15167  10279    861    357    289       C  
ATOM   3930  OG  SER A 468     -17.377   2.557  58.798  1.00106.31           O  
ANISOU 3930  OG  SER A 468    12455  16491  11446    981    395    201       O  
ATOM   3931  N   CYS A 469     -20.354   4.459  61.575  1.00 92.21           N  
ANISOU 3931  N   CYS A 469    10769  14386   9882    524    308    407       N  
ATOM   3932  CA  CYS A 469     -20.876   5.208  62.717  1.00 91.49           C  
ANISOU 3932  CA  CYS A 469    10692  14236   9833    445    290    489       C  
ATOM   3933  C   CYS A 469     -22.064   4.482  63.338  1.00 97.73           C  
ANISOU 3933  C   CYS A 469    11597  14873  10663    398    287    483       C  
ATOM   3934  O   CYS A 469     -22.098   4.353  64.563  1.00 97.65           O  
ANISOU 3934  O   CYS A 469    11641  14776  10685    408    275    530       O  
ATOM   3935  CB  CYS A 469     -21.239   6.631  62.319  1.00 90.87           C  
ANISOU 3935  CB  CYS A 469    10548  14246   9731    354    298    546       C  
ATOM   3936  SG  CYS A 469     -19.820   7.672  61.903  1.00 94.93           S  
ANISOU 3936  SG  CYS A 469    10951  14929  10189    338    299    585       S  
ATOM   3937  N   HIS A 470     -23.030   4.000  62.512  1.00 95.86           N  
ANISOU 3937  N   HIS A 470    11391  14625  10406    328    298    430       N  
ATOM   3938  CA  HIS A 470     -24.192   3.255  63.013  1.00 96.64           C  
ANISOU 3938  CA  HIS A 470    11585  14616  10518    233    295    427       C  
ATOM   3939  C   HIS A 470     -23.756   1.901  63.568  1.00103.21           C  
ANISOU 3939  C   HIS A 470    12580  15267  11369    289    294    384       C  
ATOM   3940  O   HIS A 470     -24.370   1.413  64.519  1.00103.25           O  
ANISOU 3940  O   HIS A 470    12676  15158  11397    228    291    422       O  
ATOM   3941  CB  HIS A 470     -25.279   3.060  61.950  1.00 97.85           C  
ANISOU 3941  CB  HIS A 470    11715  14846  10617    109    297    379       C  
ATOM   3942  CG  HIS A 470     -25.934   4.314  61.467  1.00100.54           C  
ANISOU 3942  CG  HIS A 470    11912  15367  10922     78    303    443       C  
ATOM   3943  ND1 HIS A 470     -26.221   4.478  60.144  1.00102.69           N  
ANISOU 3943  ND1 HIS A 470    12112  15778  11127     43    305    402       N  
ATOM   3944  CD2 HIS A 470     -26.363   5.405  62.145  1.00101.50           C  
ANISOU 3944  CD2 HIS A 470    11977  15538  11051     97    312    546       C  
ATOM   3945  CE1 HIS A 470     -26.805   5.659  60.041  1.00101.59           C  
ANISOU 3945  CE1 HIS A 470    11870  15772  10957     55    316    493       C  
ATOM   3946  NE2 HIS A 470     -26.910   6.257  61.220  1.00101.27           N  
ANISOU 3946  NE2 HIS A 470    11849  15671  10958     95    325    578       N  
ATOM   3947  N   PHE A 471     -22.682   1.314  62.995  1.00101.49           N  
ANISOU 3947  N   PHE A 471    12405  15030  11127    424    305    317       N  
ATOM   3948  CA  PHE A 471     -22.123   0.044  63.452  1.00103.33           C  
ANISOU 3948  CA  PHE A 471    12820  15083  11356    543    317    284       C  
ATOM   3949  C   PHE A 471     -21.494   0.208  64.837  1.00107.43           C  
ANISOU 3949  C   PHE A 471    13326  15581  11913    646    303    380       C  
ATOM   3950  O   PHE A 471     -21.647  -0.687  65.669  1.00108.01           O  
ANISOU 3950  O   PHE A 471    13565  15477  11998    673    307    401       O  
ATOM   3951  CB  PHE A 471     -21.095  -0.511  62.457  1.00106.69           C  
ANISOU 3951  CB  PHE A 471    13280  15536  11723    716    343    196       C  
ATOM   3952  CG  PHE A 471     -20.730  -1.952  62.718  1.00110.73           C  
ANISOU 3952  CG  PHE A 471    14048  15820  12204    859    371    148       C  
ATOM   3953  CD1 PHE A 471     -19.644  -2.277  63.526  1.00115.03           C  
ANISOU 3953  CD1 PHE A 471    14613  16352  12743   1094    379    206       C  
ATOM   3954  CD2 PHE A 471     -21.482  -2.986  62.172  1.00114.71           C  
ANISOU 3954  CD2 PHE A 471    14792  16124  12669    757    389     48       C  
ATOM   3955  CE1 PHE A 471     -19.319  -3.612  63.786  1.00118.20           C  
ANISOU 3955  CE1 PHE A 471    15285  16522  13102   1268    415    176       C  
ATOM   3956  CE2 PHE A 471     -21.153  -4.321  62.428  1.00119.97           C  
ANISOU 3956  CE2 PHE A 471    15760  16528  13294    893    425      5       C  
ATOM   3957  CZ  PHE A 471     -20.075  -4.624  63.235  1.00118.86           C  
ANISOU 3957  CZ  PHE A 471    15652  16358  13152   1169    441     74       C  
ATOM   3958  N   TYR A 472     -20.801   1.347  65.084  1.00103.09           N  
ANISOU 3958  N   TYR A 472    12594  15210  11368    682    285    440       N  
ATOM   3959  CA  TYR A 472     -20.176   1.662  66.374  1.00102.82           C  
ANISOU 3959  CA  TYR A 472    12520  15201  11345    747    261    526       C  
ATOM   3960  C   TYR A 472     -21.248   1.846  67.452  1.00106.10           C  
ANISOU 3960  C   TYR A 472    12998  15515  11802    622    251    587       C  
ATOM   3961  O   TYR A 472     -21.093   1.327  68.561  1.00106.33           O  
ANISOU 3961  O   TYR A 472    13108  15455  11836    680    242    638       O  
ATOM   3962  CB  TYR A 472     -19.282   2.916  66.272  1.00103.56           C  
ANISOU 3962  CB  TYR A 472    12422  15515  11410    742    241    564       C  
ATOM   3963  CG  TYR A 472     -18.756   3.413  67.607  1.00105.55           C  
ANISOU 3963  CG  TYR A 472    12631  15820  11655    748    206    644       C  
ATOM   3964  CD1 TYR A 472     -17.611   2.862  68.181  1.00108.73           C  
ANISOU 3964  CD1 TYR A 472    13000  16301  12011    908    189    676       C  
ATOM   3965  CD2 TYR A 472     -19.400   4.440  68.294  1.00105.43           C  
ANISOU 3965  CD2 TYR A 472    12613  15789  11656    607    193    690       C  
ATOM   3966  CE1 TYR A 472     -17.129   3.313  69.411  1.00109.44           C  
ANISOU 3966  CE1 TYR A 472    13040  16471  12073    896    149    748       C  
ATOM   3967  CE2 TYR A 472     -18.933   4.892  69.528  1.00106.36           C  
ANISOU 3967  CE2 TYR A 472    12713  15949  11748    596    159    750       C  
ATOM   3968  CZ  TYR A 472     -17.794   4.330  70.080  1.00114.24           C  
ANISOU 3968  CZ  TYR A 472    13663  17044  12701    724    131    777       C  
ATOM   3969  OH  TYR A 472     -17.336   4.789  71.291  1.00114.64           O  
ANISOU 3969  OH  TYR A 472    13684  17167  12706    694     90    834       O  
ATOM   3970  N   ASP A 473     -22.322   2.590  67.124  1.00101.83           N  
ANISOU 3970  N   ASP A 473    12410  15010  11272    473    257    591       N  
ATOM   3971  CA  ASP A 473     -23.444   2.857  68.023  1.00101.34           C  
ANISOU 3971  CA  ASP A 473    12377  14903  11226    369    259    652       C  
ATOM   3972  C   ASP A 473     -24.181   1.575  68.380  1.00106.26           C  
ANISOU 3972  C   ASP A 473    13150  15370  11855    313    271    647       C  
ATOM   3973  O   ASP A 473     -24.601   1.411  69.523  1.00105.66           O  
ANISOU 3973  O   ASP A 473    13127  15233  11786    286    271    714       O  
ATOM   3974  CB  ASP A 473     -24.420   3.858  67.389  1.00102.56           C  
ANISOU 3974  CB  ASP A 473    12438  15167  11363    270    273    661       C  
ATOM   3975  CG  ASP A 473     -24.002   5.315  67.445  1.00111.09           C  
ANISOU 3975  CG  ASP A 473    13434  16348  12426    293    272    700       C  
ATOM   3976  OD1 ASP A 473     -23.090   5.648  68.245  1.00110.79           O  
ANISOU 3976  OD1 ASP A 473    13401  16306  12388    339    252    726       O  
ATOM   3977  OD2 ASP A 473     -24.613   6.132  66.723  1.00117.33           O  
ANISOU 3977  OD2 ASP A 473    14169  17222  13190    256    290    709       O  
ATOM   3978  N   PHE A 474     -24.322   0.669  67.403  1.00104.42           N  
ANISOU 3978  N   PHE A 474    13002  15066  11606    282    282    566       N  
ATOM   3979  CA  PHE A 474     -24.985  -0.617  67.565  1.00106.15           C  
ANISOU 3979  CA  PHE A 474    13413  15107  11812    185    295    546       C  
ATOM   3980  C   PHE A 474     -24.146  -1.559  68.446  1.00112.61           C  
ANISOU 3980  C   PHE A 474    14407  15743  12637    336    301    574       C  
ATOM   3981  O   PHE A 474     -24.704  -2.215  69.329  1.00113.50           O  
ANISOU 3981  O   PHE A 474    14657  15720  12748    261    309    629       O  
ATOM   3982  CB  PHE A 474     -25.251  -1.238  66.184  1.00108.86           C  
ANISOU 3982  CB  PHE A 474    13826  15422  12113    105    305    432       C  
ATOM   3983  CG  PHE A 474     -25.591  -2.707  66.168  1.00112.33           C  
ANISOU 3983  CG  PHE A 474    14539  15623  12518     15    321    380       C  
ATOM   3984  CD1 PHE A 474     -26.840  -3.154  66.582  1.00116.19           C  
ANISOU 3984  CD1 PHE A 474    15100  16063  12982   -232    321    413       C  
ATOM   3985  CD2 PHE A 474     -24.667  -3.644  65.721  1.00115.79           C  
ANISOU 3985  CD2 PHE A 474    15178  15887  12930    176    343    301       C  
ATOM   3986  CE1 PHE A 474     -27.148  -4.515  66.579  1.00119.30           C  
ANISOU 3986  CE1 PHE A 474    15789  16209  13331   -359    338    367       C  
ATOM   3987  CE2 PHE A 474     -24.980  -5.004  65.706  1.00120.86           C  
ANISOU 3987  CE2 PHE A 474    16140  16256  13525     94    366    249       C  
ATOM   3988  CZ  PHE A 474     -26.220  -5.429  66.128  1.00119.80           C  
ANISOU 3988  CZ  PHE A 474    16100  16049  13371   -196    362    280       C  
ATOM   3989  N   PHE A 475     -22.818  -1.610  68.211  1.00109.88           N  
ANISOU 3989  N   PHE A 475    14046  15422  12283    555    300    551       N  
ATOM   3990  CA  PHE A 475     -21.864  -2.453  68.938  1.00111.33           C  
ANISOU 3990  CA  PHE A 475    14367  15484  12447    766    308    588       C  
ATOM   3991  C   PHE A 475     -21.742  -2.066  70.423  1.00113.04           C  
ANISOU 3991  C   PHE A 475    14532  15740  12679    796    284    706       C  
ATOM   3992  O   PHE A 475     -21.528  -2.949  71.257  1.00114.18           O  
ANISOU 3992  O   PHE A 475    14845  15734  12806    895    294    763       O  
ATOM   3993  CB  PHE A 475     -20.478  -2.377  68.266  1.00114.28           C  
ANISOU 3993  CB  PHE A 475    14654  15985  12784   1003    311    549       C  
ATOM   3994  CG  PHE A 475     -19.371  -3.201  68.888  1.00118.45           C  
ANISOU 3994  CG  PHE A 475    15286  16457  13264   1284    324    596       C  
ATOM   3995  CD1 PHE A 475     -18.479  -2.632  69.791  1.00122.04           C  
ANISOU 3995  CD1 PHE A 475    15570  17101  13700   1409    290    689       C  
ATOM   3996  CD2 PHE A 475     -19.193  -4.534  68.537  1.00123.41           C  
ANISOU 3996  CD2 PHE A 475    16191  16854  13843   1435    370    549       C  
ATOM   3997  CE1 PHE A 475     -17.451  -3.393  70.362  1.00124.95           C  
ANISOU 3997  CE1 PHE A 475    16005  17470  14001   1695    299    749       C  
ATOM   3998  CE2 PHE A 475     -18.159  -5.293  69.101  1.00128.35           C  
ANISOU 3998  CE2 PHE A 475    16922  17439  14405   1751    391    608       C  
ATOM   3999  CZ  PHE A 475     -17.295  -4.717  70.009  1.00126.16           C  
ANISOU 3999  CZ  PHE A 475    16432  17394  14108   1888    353    715       C  
ATOM   4000  N   ASN A 476     -21.852  -0.765  70.750  1.00106.17           N  
ANISOU 4000  N   ASN A 476    13455  15057  11827    720    257    743       N  
ATOM   4001  CA  ASN A 476     -21.674  -0.294  72.122  1.00104.63           C  
ANISOU 4001  CA  ASN A 476    13213  14916  11627    744    232    838       C  
ATOM   4002  C   ASN A 476     -22.978   0.135  72.837  1.00105.49           C  
ANISOU 4002  C   ASN A 476    13324  15007  11751    564    240    887       C  
ATOM   4003  O   ASN A 476     -22.888   0.522  74.003  1.00105.16           O  
ANISOU 4003  O   ASN A 476    13260  15005  11691    583    224    959       O  
ATOM   4004  CB  ASN A 476     -20.664   0.855  72.154  1.00104.74           C  
ANISOU 4004  CB  ASN A 476    13030  15151  11617    802    197    844       C  
ATOM   4005  CG  ASN A 476     -19.262   0.436  71.800  1.00134.33           C  
ANISOU 4005  CG  ASN A 476    16729  18991  15318   1004    187    832       C  
ATOM   4006  OD1 ASN A 476     -18.511  -0.077  72.635  1.00133.90           O  
ANISOU 4006  OD1 ASN A 476    16700  18956  15220   1161    172    895       O  
ATOM   4007  ND2 ASN A 476     -18.878   0.646  70.550  1.00126.64           N  
ANISOU 4007  ND2 ASN A 476    15674  18107  14338   1021    199    762       N  
ATOM   4008  N   GLN A 477     -24.175   0.032  72.198  1.00 99.98           N  
ANISOU 4008  N   GLN A 477    12646  14276  11065    397    265    855       N  
ATOM   4009  CA  GLN A 477     -25.436   0.422  72.869  1.00 98.55           C  
ANISOU 4009  CA  GLN A 477    12434  14136  10873    251    280    916       C  
ATOM   4010  C   GLN A 477     -25.712  -0.469  74.088  1.00101.58           C  
ANISOU 4010  C   GLN A 477    12964  14392  11241    234    291    999       C  
ATOM   4011  O   GLN A 477     -26.142   0.037  75.129  1.00100.00           O  
ANISOU 4011  O   GLN A 477    12720  14259  11019    213    295   1074       O  
ATOM   4012  CB  GLN A 477     -26.646   0.415  71.914  1.00 99.80           C  
ANISOU 4012  CB  GLN A 477    12551  14348  11020     76    301    878       C  
ATOM   4013  CG  GLN A 477     -27.927   0.998  72.542  1.00112.45           C  
ANISOU 4013  CG  GLN A 477    14063  16077  12585    -36    323    954       C  
ATOM   4014  CD  GLN A 477     -28.575   2.140  71.783  1.00131.52           C  
ANISOU 4014  CD  GLN A 477    16309  18688  14975    -57    334    942       C  
ATOM   4015  OE1 GLN A 477     -28.285   2.413  70.610  1.00126.98           O  
ANISOU 4015  OE1 GLN A 477    15682  18156  14409    -43    324    874       O  
ATOM   4016  NE2 GLN A 477     -29.523   2.803  72.433  1.00123.78           N  
ANISOU 4016  NE2 GLN A 477    15246  17841  13946    -76    361   1018       N  
ATOM   4017  N   ALA A 478     -25.411  -1.777  73.962  1.00 98.86           N  
ANISOU 4017  N   ALA A 478    12815  13854  10895    261    301    987       N  
ATOM   4018  CA  ALA A 478     -25.586  -2.785  75.008  1.00 99.54           C  
ANISOU 4018  CA  ALA A 478    13093  13773  10956    251    317   1073       C  
ATOM   4019  C   ALA A 478     -25.000  -2.320  76.347  1.00101.06           C  
ANISOU 4019  C   ALA A 478    13229  14039  11130    390    297   1165       C  
ATOM   4020  O   ALA A 478     -25.686  -2.402  77.366  1.00100.18           O  
ANISOU 4020  O   ALA A 478    13150  13925  10990    307    312   1254       O  
ATOM   4021  CB  ALA A 478     -24.941  -4.094  74.577  1.00102.19           C  
ANISOU 4021  CB  ALA A 478    13677  13871  11282    352    333   1038       C  
ATOM   4022  N   GLU A 479     -23.761  -1.786  76.331  1.00 96.73           N  
ANISOU 4022  N   GLU A 479    12581  13591  10581    580    262   1145       N  
ATOM   4023  CA  GLU A 479     -23.100  -1.284  77.532  1.00 96.17           C  
ANISOU 4023  CA  GLU A 479    12442  13628  10471    692    231   1218       C  
ATOM   4024  C   GLU A 479     -23.662   0.078  77.942  1.00 98.36           C  
ANISOU 4024  C   GLU A 479    12565  14069  10737    585    222   1219       C  
ATOM   4025  O   GLU A 479     -23.774   0.329  79.143  1.00 98.55           O  
ANISOU 4025  O   GLU A 479    12592  14137  10715    593    215   1290       O  
ATOM   4026  CB  GLU A 479     -21.573  -1.205  77.355  1.00 97.73           C  
ANISOU 4026  CB  GLU A 479    12565  13924  10642    902    192   1202       C  
ATOM   4027  CG  GLU A 479     -20.803  -2.230  78.180  1.00109.45           C  
ANISOU 4027  CG  GLU A 479    14178  15337  12071   1105    187   1290       C  
ATOM   4028  CD  GLU A 479     -20.806  -2.046  79.690  1.00130.93           C  
ANISOU 4028  CD  GLU A 479    16892  18123  14733   1120    164   1397       C  
ATOM   4029  OE1 GLU A 479     -21.266  -2.972  80.398  1.00126.59           O  
ANISOU 4029  OE1 GLU A 479    16528  17407  14164   1131    193   1483       O  
ATOM   4030  OE2 GLU A 479     -20.337  -0.988  80.168  1.00122.92           O  
ANISOU 4030  OE2 GLU A 479    15705  17319  13679   1108    117   1394       O  
ATOM   4031  N   TRP A 480     -24.031   0.945  76.962  1.00 92.60           N  
ANISOU 4031  N   TRP A 480    11724  13423  10037    502    229   1145       N  
ATOM   4032  CA  TRP A 480     -24.584   2.279  77.231  1.00 90.93           C  
ANISOU 4032  CA  TRP A 480    11410  13339   9802    436    234   1143       C  
ATOM   4033  C   TRP A 480     -25.915   2.196  77.982  1.00 95.98           C  
ANISOU 4033  C   TRP A 480    12081  13977  10411    343    277   1211       C  
ATOM   4034  O   TRP A 480     -26.174   3.048  78.833  1.00 95.37           O  
ANISOU 4034  O   TRP A 480    11975  13981  10281    356    284   1242       O  
ATOM   4035  CB  TRP A 480     -24.753   3.094  75.943  1.00 88.42           C  
ANISOU 4035  CB  TRP A 480    10996  13090   9510    390    242   1067       C  
ATOM   4036  CG  TRP A 480     -23.478   3.416  75.213  1.00 88.98           C  
ANISOU 4036  CG  TRP A 480    11005  13213   9591    461    206   1009       C  
ATOM   4037  CD1 TRP A 480     -22.225   3.520  75.745  1.00 92.34           C  
ANISOU 4037  CD1 TRP A 480    11403  13698   9982    548    163   1021       C  
ATOM   4038  CD2 TRP A 480     -23.350   3.736  73.822  1.00 88.16           C  
ANISOU 4038  CD2 TRP A 480    10833  13151   9513    439    212    940       C  
ATOM   4039  NE1 TRP A 480     -21.317   3.836  74.759  1.00 91.78           N  
ANISOU 4039  NE1 TRP A 480    11244  13715   9915    575    144    966       N  
ATOM   4040  CE2 TRP A 480     -21.982   3.982  73.570  1.00 92.39           C  
ANISOU 4040  CE2 TRP A 480    11304  13769  10031    513    176    915       C  
ATOM   4041  CE3 TRP A 480     -24.260   3.834  72.760  1.00 88.93           C  
ANISOU 4041  CE3 TRP A 480    10904  13256   9631    361    242    904       C  
ATOM   4042  CZ2 TRP A 480     -21.500   4.303  72.299  1.00 91.54           C  
ANISOU 4042  CZ2 TRP A 480    11116  13733   9931    512    177    857       C  
ATOM   4043  CZ3 TRP A 480     -23.783   4.150  71.501  1.00 90.37           C  
ANISOU 4043  CZ3 TRP A 480    11017  13497   9822    369    239    842       C  
ATOM   4044  CH2 TRP A 480     -22.417   4.380  71.278  1.00 91.27           C  
ANISOU 4044  CH2 TRP A 480    11079  13676   9924    444    209    819       C  
ATOM   4045  N   GLU A 481     -26.737   1.163  77.690  1.00 93.66           N  
ANISOU 4045  N   GLU A 481    11855  13601  10132    240    307   1233       N  
ATOM   4046  CA  GLU A 481     -28.016   0.920  78.367  1.00 94.09           C  
ANISOU 4046  CA  GLU A 481    11919  13691  10140    120    350   1312       C  
ATOM   4047  C   GLU A 481     -27.768   0.365  79.769  1.00 99.10           C  
ANISOU 4047  C   GLU A 481    12658  14261  10735    166    349   1405       C  
ATOM   4048  O   GLU A 481     -28.483   0.731  80.710  1.00 98.67           O  
ANISOU 4048  O   GLU A 481    12570  14303  10617    138    378   1475       O  
ATOM   4049  CB  GLU A 481     -28.908  -0.032  77.559  1.00 96.47           C  
ANISOU 4049  CB  GLU A 481    12262  13941  10449    -59    374   1304       C  
ATOM   4050  CG  GLU A 481     -29.551   0.629  76.352  1.00108.44           C  
ANISOU 4050  CG  GLU A 481    13635  15598  11968   -129    382   1240       C  
ATOM   4051  CD  GLU A 481     -30.802  -0.043  75.821  1.00135.26           C  
ANISOU 4051  CD  GLU A 481    17013  19056  15324   -355    408   1255       C  
ATOM   4052  OE1 GLU A 481     -30.725  -1.227  75.417  1.00137.03           O  
ANISOU 4052  OE1 GLU A 481    17392  19114  15561   -476    401   1227       O  
ATOM   4053  OE2 GLU A 481     -31.858   0.629  75.782  1.00129.29           O  
ANISOU 4053  OE2 GLU A 481    16093  18526  14505   -411    436   1295       O  
ATOM   4054  N   ARG A 482     -26.744  -0.513  79.900  1.00 97.04           N  
ANISOU 4054  N   ARG A 482    12524  13853  10495    262    320   1413       N  
ATOM   4055  CA  ARG A 482     -26.313  -1.116  81.167  1.00 98.17           C  
ANISOU 4055  CA  ARG A 482    12777  13931  10591    346    313   1511       C  
ATOM   4056  C   ARG A 482     -25.799  -0.035  82.122  1.00101.08           C  
ANISOU 4056  C   ARG A 482    13044  14456  10905    448    283   1524       C  
ATOM   4057  O   ARG A 482     -26.147  -0.057  83.301  1.00101.14           O  
ANISOU 4057  O   ARG A 482    13082  14500  10845    444    297   1609       O  
ATOM   4058  CB  ARG A 482     -25.223  -2.186  80.940  1.00100.18           C  
ANISOU 4058  CB  ARG A 482    13181  14019  10863    488    292   1514       C  
ATOM   4059  CG  ARG A 482     -25.724  -3.536  80.414  1.00114.09           C  
ANISOU 4059  CG  ARG A 482    15158  15550  12643    389    332   1526       C  
ATOM   4060  CD  ARG A 482     -26.507  -4.371  81.426  1.00126.46           C  
ANISOU 4060  CD  ARG A 482    16887  17006  14154    272    371   1652       C  
ATOM   4061  NE  ARG A 482     -25.704  -4.790  82.578  1.00135.25           N  
ANISOU 4061  NE  ARG A 482    18102  18071  15214    462    358   1758       N  
ATOM   4062  CZ  ARG A 482     -25.903  -4.370  83.824  1.00149.49           C  
ANISOU 4062  CZ  ARG A 482    19840  20003  16956    471    355   1851       C  
ATOM   4063  NH1 ARG A 482     -25.137  -4.813  84.809  1.00135.22           N  
ANISOU 4063  NH1 ARG A 482    18125  18164  15087    650    339   1950       N  
ATOM   4064  NH2 ARG A 482     -26.879  -3.512  84.096  1.00138.53           N  
ANISOU 4064  NH2 ARG A 482    18295  18789  15551    320    373   1848       N  
ATOM   4065  N   SER A 483     -25.002   0.929  81.596  1.00 96.18           N  
ANISOU 4065  N   SER A 483    12314  13930  10299    514    243   1438       N  
ATOM   4066  CA  SER A 483     -24.421   2.059  82.330  1.00 95.08           C  
ANISOU 4066  CA  SER A 483    12103  13929  10095    566    207   1423       C  
ATOM   4067  C   SER A 483     -25.502   3.036  82.786  1.00 97.11           C  
ANISOU 4067  C   SER A 483    12332  14263  10303    494    250   1425       C  
ATOM   4068  O   SER A 483     -25.308   3.712  83.796  1.00 96.86           O  
ANISOU 4068  O   SER A 483    12309  14307  10185    526    237   1437       O  
ATOM   4069  CB  SER A 483     -23.398   2.786  81.463  1.00 97.82           C  
ANISOU 4069  CB  SER A 483    12358  14346  10464    599    162   1332       C  
ATOM   4070  OG  SER A 483     -22.369   1.905  81.043  1.00107.44           O  
ANISOU 4070  OG  SER A 483    13583  15535  11706    705    130   1335       O  
ATOM   4071  N   PHE A 484     -26.641   3.094  82.043  1.00 92.13           N  
ANISOU 4071  N   PHE A 484    11668  13632   9707    409    304   1413       N  
ATOM   4072  CA  PHE A 484     -27.798   3.944  82.337  1.00 91.11           C  
ANISOU 4072  CA  PHE A 484    11495  13607   9516    383    361   1429       C  
ATOM   4073  C   PHE A 484     -28.638   3.324  83.437  1.00 95.96           C  
ANISOU 4073  C   PHE A 484    12143  14255  10063    348    403   1537       C  
ATOM   4074  O   PHE A 484     -28.917   4.005  84.426  1.00 95.59           O  
ANISOU 4074  O   PHE A 484    12103  14294   9921    403    427   1563       O  
ATOM   4075  CB  PHE A 484     -28.663   4.201  81.087  1.00 92.10           C  
ANISOU 4075  CB  PHE A 484    11536  13778   9679    322    398   1393       C  
ATOM   4076  CG  PHE A 484     -29.814   5.155  81.320  1.00 93.48           C  
ANISOU 4076  CG  PHE A 484    11651  14098   9769    352    464   1419       C  
ATOM   4077  CD1 PHE A 484     -29.607   6.529  81.351  1.00 95.94           C  
ANISOU 4077  CD1 PHE A 484    11985  14436  10030    455    473   1368       C  
ATOM   4078  CD2 PHE A 484     -31.106   4.680  81.504  1.00 96.29           C  
ANISOU 4078  CD2 PHE A 484    11939  14572  10076    281    521   1501       C  
ATOM   4079  CE1 PHE A 484     -30.671   7.412  81.572  1.00 97.07           C  
ANISOU 4079  CE1 PHE A 484    12104  14704  10074    539    547   1397       C  
ATOM   4080  CE2 PHE A 484     -32.171   5.565  81.719  1.00 99.25           C  
ANISOU 4080  CE2 PHE A 484    12236  15128  10348    355    590   1537       C  
ATOM   4081  CZ  PHE A 484     -31.945   6.924  81.755  1.00 96.66           C  
ANISOU 4081  CZ  PHE A 484    11952  14806   9970    509    607   1485       C  
ATOM   4082  N   ARG A 485     -29.055   2.042  83.270  1.00 93.79           N  
ANISOU 4082  N   ARG A 485    11908  13906   9823    246    418   1598       N  
ATOM   4083  CA  ARG A 485     -29.857   1.347  84.281  1.00 95.21           C  
ANISOU 4083  CA  ARG A 485    12128  14115   9932    174    462   1717       C  
ATOM   4084  C   ARG A 485     -29.137   1.381  85.628  1.00101.20           C  
ANISOU 4084  C   ARG A 485    12962  14865  10623    285    437   1768       C  
ATOM   4085  O   ARG A 485     -29.763   1.719  86.630  1.00101.51           O  
ANISOU 4085  O   ARG A 485    12984  15022  10563    294    478   1832       O  
ATOM   4086  CB  ARG A 485     -30.196  -0.096  83.876  1.00 95.70           C  
ANISOU 4086  CB  ARG A 485    12284  14043  10034     19    473   1770       C  
ATOM   4087  CG  ARG A 485     -31.510  -0.551  84.497  1.00106.13           C  
ANISOU 4087  CG  ARG A 485    13584  15472  11269   -143    537   1886       C  
ATOM   4088  CD  ARG A 485     -31.612  -2.039  84.769  1.00118.54           C  
ANISOU 4088  CD  ARG A 485    15337  16866  12838   -292    548   1978       C  
ATOM   4089  NE  ARG A 485     -32.743  -2.322  85.660  1.00128.34           N  
ANISOU 4089  NE  ARG A 485    16545  18251  13968   -442    610   2110       N  
ATOM   4090  CZ  ARG A 485     -33.159  -3.538  86.005  1.00143.90           C  
ANISOU 4090  CZ  ARG A 485    18668  20106  15900   -636    637   2218       C  
ATOM   4091  NH1 ARG A 485     -32.542  -4.617  85.537  1.00133.84           N  
ANISOU 4091  NH1 ARG A 485    17629  18535  14690   -683    612   2203       N  
ATOM   4092  NH2 ARG A 485     -34.194  -3.685  86.822  1.00129.72           N  
ANISOU 4092  NH2 ARG A 485    16809  18491  13989   -783    697   2346       N  
ATOM   4093  N   ASP A 486     -27.812   1.116  85.629  1.00 99.07           N  
ANISOU 4093  N   ASP A 486    12756  14495  10391    382    370   1739       N  
ATOM   4094  CA  ASP A 486     -26.965   1.137  86.822  1.00100.26           C  
ANISOU 4094  CA  ASP A 486    12957  14674  10465    493    330   1784       C  
ATOM   4095  C   ASP A 486     -26.864   2.544  87.428  1.00104.31           C  
ANISOU 4095  C   ASP A 486    13413  15332  10890    542    320   1726       C  
ATOM   4096  O   ASP A 486     -26.738   2.659  88.650  1.00104.98           O  
ANISOU 4096  O   ASP A 486    13534  15485  10867    588    314   1778       O  
ATOM   4097  CB  ASP A 486     -25.562   0.603  86.508  1.00102.70           C  
ANISOU 4097  CB  ASP A 486    13303  14904  10816    601    261   1766       C  
ATOM   4098  CG  ASP A 486     -25.491  -0.902  86.301  1.00117.16           C  
ANISOU 4098  CG  ASP A 486    15273  16553  12689    612    276   1845       C  
ATOM   4099  OD1 ASP A 486     -26.220  -1.642  87.012  1.00118.72           O  
ANISOU 4099  OD1 ASP A 486    15573  16692  12844    546    321   1956       O  
ATOM   4100  OD2 ASP A 486     -24.685  -1.344  85.456  1.00124.65           O  
ANISOU 4100  OD2 ASP A 486    16247  17416  13698    690    247   1799       O  
ATOM   4101  N   TYR A 487     -26.933   3.597  86.587  1.00 99.64           N  
ANISOU 4101  N   TYR A 487    12759  14772  10329    531    323   1618       N  
ATOM   4102  CA  TYR A 487     -26.896   4.991  87.018  1.00 99.41           C  
ANISOU 4102  CA  TYR A 487    12736  14828  10209    567    325   1549       C  
ATOM   4103  C   TYR A 487     -28.211   5.353  87.703  1.00103.82           C  
ANISOU 4103  C   TYR A 487    13301  15474  10673    582    412   1600       C  
ATOM   4104  O   TYR A 487     -28.188   5.997  88.751  1.00104.03           O  
ANISOU 4104  O   TYR A 487    13388  15564  10574    637    420   1595       O  
ATOM   4105  CB  TYR A 487     -26.622   5.921  85.824  1.00100.16           C  
ANISOU 4105  CB  TYR A 487    12797  14897  10361    553    314   1438       C  
ATOM   4106  CG  TYR A 487     -26.783   7.399  86.110  1.00103.05           C  
ANISOU 4106  CG  TYR A 487    13228  15299  10628    583    337   1366       C  
ATOM   4107  CD1 TYR A 487     -25.832   8.094  86.853  1.00105.99           C  
ANISOU 4107  CD1 TYR A 487    13680  15687  10903    575    281   1312       C  
ATOM   4108  CD2 TYR A 487     -27.868   8.111  85.609  1.00103.95           C  
ANISOU 4108  CD2 TYR A 487    13341  15431  10726    621    417   1352       C  
ATOM   4109  CE1 TYR A 487     -25.968   9.458  87.108  1.00107.90           C  
ANISOU 4109  CE1 TYR A 487    14044  15915  11037    585    307   1233       C  
ATOM   4110  CE2 TYR A 487     -28.019   9.474  85.863  1.00105.55           C  
ANISOU 4110  CE2 TYR A 487    13658  15626  10821    683    451   1288       C  
ATOM   4111  CZ  TYR A 487     -27.068  10.143  86.616  1.00115.24           C  
ANISOU 4111  CZ  TYR A 487    15010  16819  11955    656    398   1222       C  
ATOM   4112  OH  TYR A 487     -27.216  11.486  86.866  1.00118.83           O  
ANISOU 4112  OH  TYR A 487    15639  17223  12289    701    438   1148       O  
ATOM   4113  N   VAL A 488     -29.347   4.939  87.101  1.00100.68           N  
ANISOU 4113  N   VAL A 488    12832  15105  10315    529    476   1647       N  
ATOM   4114  CA  VAL A 488     -30.705   5.181  87.602  1.00101.26           C  
ANISOU 4114  CA  VAL A 488    12860  15326  10289    545    568   1715       C  
ATOM   4115  C   VAL A 488     -30.886   4.478  88.967  1.00107.36           C  
ANISOU 4115  C   VAL A 488    13675  16149  10970    535    585   1827       C  
ATOM   4116  O   VAL A 488     -31.291   5.131  89.929  1.00107.71           O  
ANISOU 4116  O   VAL A 488    13741  16307  10877    621    631   1843       O  
ATOM   4117  CB  VAL A 488     -31.769   4.746  86.556  1.00104.63           C  
ANISOU 4117  CB  VAL A 488    13166  15819  10771    451    616   1750       C  
ATOM   4118  CG1 VAL A 488     -33.168   4.695  87.156  1.00105.80           C  
ANISOU 4118  CG1 VAL A 488    13223  16181  10797    440    709   1857       C  
ATOM   4119  CG2 VAL A 488     -31.747   5.667  85.343  1.00103.23           C  
ANISOU 4119  CG2 VAL A 488    12943  15637  10642    499    615   1652       C  
ATOM   4120  N   LEU A 489     -30.532   3.176  89.054  1.00105.18           N  
ANISOU 4120  N   LEU A 489    13436  15774  10755    446    551   1904       N  
ATOM   4121  CA  LEU A 489     -30.624   2.373  90.278  1.00106.85           C  
ANISOU 4121  CA  LEU A 489    13710  16006  10884    429    565   2030       C  
ATOM   4122  C   LEU A 489     -29.707   2.911  91.377  1.00114.75           C  
ANISOU 4122  C   LEU A 489    14781  17031  11787    552    517   2006       C  
ATOM   4123  O   LEU A 489     -30.033   2.772  92.557  1.00115.36           O  
ANISOU 4123  O   LEU A 489    14889  17202  11741    576    548   2093       O  
ATOM   4124  CB  LEU A 489     -30.296   0.898  90.004  1.00107.06           C  
ANISOU 4124  CB  LEU A 489    13818  15864  10995    331    538   2109       C  
ATOM   4125  CG  LEU A 489     -31.360   0.074  89.275  1.00111.73           C  
ANISOU 4125  CG  LEU A 489    14383  16437  11631    141    591   2167       C  
ATOM   4126  CD1 LEU A 489     -30.787  -1.231  88.792  1.00112.29           C  
ANISOU 4126  CD1 LEU A 489    14603  16269  11793     70    557   2197       C  
ATOM   4127  CD2 LEU A 489     -32.565  -0.212  90.163  1.00115.42           C  
ANISOU 4127  CD2 LEU A 489    14809  17071  11973     38    673   2304       C  
ATOM   4128  N   CYS A 490     -28.575   3.534  90.984  1.00113.66           N  
ANISOU 4128  N   CYS A 490    14660  16835  11689    610    439   1890       N  
ATOM   4129  CA  CYS A 490     -27.600   4.139  91.895  1.00115.44           C  
ANISOU 4129  CA  CYS A 490    14941  17112  11810    684    377   1846       C  
ATOM   4130  C   CYS A 490     -28.226   5.323  92.631  1.00120.74           C  
ANISOU 4130  C   CYS A 490    15648  17894  12332    734    431   1797       C  
ATOM   4131  O   CYS A 490     -27.982   5.494  93.826  1.00121.74           O  
ANISOU 4131  O   CYS A 490    15836  18102  12318    776    417   1818       O  
ATOM   4132  CB  CYS A 490     -26.342   4.562  91.139  1.00115.62           C  
ANISOU 4132  CB  CYS A 490    14949  17083  11900    687    287   1736       C  
ATOM   4133  SG  CYS A 490     -25.027   5.238  92.190  1.00120.85           S  
ANISOU 4133  SG  CYS A 490    15652  17856  12410    718    190   1683       S  
ATOM   4134  N   GLN A 491     -29.017   6.138  91.917  1.00116.99           N  
ANISOU 4134  N   GLN A 491    15150  17427  11874    749    495   1732       N  
ATOM   4135  CA  GLN A 491     -29.671   7.334  92.453  1.00117.93           C  
ANISOU 4135  CA  GLN A 491    15335  17627  11845    845    566   1677       C  
ATOM   4136  C   GLN A 491     -30.638   7.016  93.621  1.00125.61           C  
ANISOU 4136  C   GLN A 491    16298  18754  12675    898    648   1790       C  
ATOM   4137  O   GLN A 491     -30.835   7.863  94.495  1.00126.12           O  
ANISOU 4137  O   GLN A 491    16459  18889  12573    999    688   1748       O  
ATOM   4138  CB  GLN A 491     -30.402   8.078  91.332  1.00118.32           C  
ANISOU 4138  CB  GLN A 491    15350  17663  11944    886    628   1620       C  
ATOM   4139  CG  GLN A 491     -29.477   8.542  90.204  1.00124.96           C  
ANISOU 4139  CG  GLN A 491    16214  18364  12901    834    557   1509       C  
ATOM   4140  CD  GLN A 491     -28.641   9.752  90.533  1.00139.80           C  
ANISOU 4140  CD  GLN A 491    18259  20174  14684    850    517   1383       C  
ATOM   4141  OE1 GLN A 491     -29.070  10.682  91.219  1.00137.95           O  
ANISOU 4141  OE1 GLN A 491    18162  19959  14295    945    576   1340       O  
ATOM   4142  NE2 GLN A 491     -27.443   9.799  89.995  1.00128.57           N  
ANISOU 4142  NE2 GLN A 491    16841  18675  13337    750    421   1317       N  
ATOM   4143  N   ALA A 492     -31.201   5.797  93.657  1.00124.28           N  
ANISOU 4143  N   ALA A 492    16032  18631  12556    819    675   1932       N  
ATOM   4144  CA  ALA A 492     -32.096   5.368  94.732  1.00126.38           C  
ANISOU 4144  CA  ALA A 492    16271  19062  12686    834    753   2063       C  
ATOM   4145  C   ALA A 492     -31.344   4.581  95.819  1.00132.49           C  
ANISOU 4145  C   ALA A 492    17118  19816  13407    808    695   2144       C  
ATOM   4146  O   ALA A 492     -31.838   4.469  96.944  1.00133.44           O  
ANISOU 4146  O   ALA A 492    17252  20077  13374    845    748   2232       O  
ATOM   4147  CB  ALA A 492     -33.223   4.529  94.166  1.00127.56           C  
ANISOU 4147  CB  ALA A 492    16281  19295  12890    721    822   2182       C  
ATOM   4148  N   ASN A 493     -30.163   4.029  95.483  1.00129.60           N  
ANISOU 4148  N   ASN A 493    16792  19300  13152    766    591   2126       N  
ATOM   4149  CA  ASN A 493     -29.350   3.265  96.427  1.00131.20           C  
ANISOU 4149  CA  ASN A 493    17058  19493  13297    778    529   2214       C  
ATOM   4150  C   ASN A 493     -28.473   4.206  97.257  1.00135.86           C  
ANISOU 4150  C   ASN A 493    17715  20158  13747    860    464   2115       C  
ATOM   4151  O   ASN A 493     -28.370   4.007  98.466  1.00137.06           O  
ANISOU 4151  O   ASN A 493    17912  20416  13750    900    460   2188       O  
ATOM   4152  CB  ASN A 493     -28.489   2.207  95.693  1.00135.37           C  
ANISOU 4152  CB  ASN A 493    17599  19855  13981    739    456   2253       C  
ATOM   4153  CG  ASN A 493     -27.579   1.338  96.575  1.00178.72           C  
ANISOU 4153  CG  ASN A 493    23160  25337  19408    799    393   2364       C  
ATOM   4154  OD1 ASN A 493     -26.849   1.832  97.441  1.00176.60           O  
ANISOU 4154  OD1 ASN A 493    22907  25182  19010    874    335   2336       O  
ATOM   4155  ND2 ASN A 493     -27.526   0.013  96.395  1.00179.11           N  
ANISOU 4155  ND2 ASN A 493    23273  25253  19529    776    399   2496       N  
ATOM   4156  N   VAL A 494     -27.830   5.209  96.624  1.00131.39           N  
ANISOU 4156  N   VAL A 494    17166  19543  13214    861    412   1951       N  
ATOM   4157  CA  VAL A 494     -26.912   6.129  97.308  1.00131.76           C  
ANISOU 4157  CA  VAL A 494    17294  19653  13118    877    337   1840       C  
ATOM   4158  C   VAL A 494     -27.663   7.044  98.322  1.00137.57           C  
ANISOU 4158  C   VAL A 494    18132  20490  13649    943    414   1796       C  
ATOM   4159  O   VAL A 494     -27.047   7.508  99.286  1.00137.94           O  
ANISOU 4159  O   VAL A 494    18267  20620  13526    947    361   1743       O  
ATOM   4160  CB  VAL A 494     -26.037   6.927  96.298  1.00134.16           C  
ANISOU 4160  CB  VAL A 494    17602  19870  13503    817    265   1686       C  
ATOM   4161  CG1 VAL A 494     -26.784   8.101  95.682  1.00133.16           C  
ANISOU 4161  CG1 VAL A 494    17546  19672  13378    830    342   1568       C  
ATOM   4162  CG2 VAL A 494     -24.721   7.377  96.925  1.00134.87           C  
ANISOU 4162  CG2 VAL A 494    17731  20049  13464    767    148   1613       C  
ATOM   4163  N   THR A 495     -28.986   7.248  98.131  1.00135.08           N  
ANISOU 4163  N   THR A 495    17798  20197  13329   1002    539   1824       N  
ATOM   4164  CA  THR A 495     -29.810   8.063  99.024  1.00136.63           C  
ANISOU 4164  CA  THR A 495    18086  20506  13321   1114    634   1794       C  
ATOM   4165  C   THR A 495     -30.079   7.283 100.348  1.00143.73           C  
ANISOU 4165  C   THR A 495    18965  21566  14079   1138    658   1941       C  
ATOM   4166  O   THR A 495     -30.234   7.915 101.396  1.00144.86           O  
ANISOU 4166  O   THR A 495    19216  21815  14010   1220    692   1899       O  
ATOM   4167  CB  THR A 495     -31.084   8.573  98.296  1.00142.11           C  
ANISOU 4167  CB  THR A 495    18737  21218  14041   1204    761   1786       C  
ATOM   4168  OG1 THR A 495     -31.726   9.577  99.080  1.00143.28           O  
ANISOU 4168  OG1 THR A 495    19012  21459  13971   1362    855   1726       O  
ATOM   4169  CG2 THR A 495     -32.073   7.475  97.939  1.00139.40           C  
ANISOU 4169  CG2 THR A 495    18205  20968  13791   1160    829   1958       C  
ATOM   4170  N   ILE A 496     -30.067   5.924 100.302  1.00141.17           N  
ANISOU 4170  N   ILE A 496    18536  21243  13860   1064    640   2108       N  
ATOM   4171  CA  ILE A 496     -30.274   5.052 101.475  1.00142.89           C  
ANISOU 4171  CA  ILE A 496    18747  21589  13956   1069    661   2276       C  
ATOM   4172  C   ILE A 496     -28.921   4.538 102.011  1.00148.38           C  
ANISOU 4172  C   ILE A 496    19485  22264  14629   1052    531   2303       C  
ATOM   4173  O   ILE A 496     -27.948   4.463 101.256  1.00147.14           O  
ANISOU 4173  O   ILE A 496    19314  21992  14601   1014    434   2240       O  
ATOM   4174  CB  ILE A 496     -31.267   3.877 101.207  1.00146.17           C  
ANISOU 4174  CB  ILE A 496    19058  22023  14458    989    743   2466       C  
ATOM   4175  CG1 ILE A 496     -30.743   2.853 100.166  1.00145.33           C  
ANISOU 4175  CG1 ILE A 496    18925  21718  14576    879    678   2516       C  
ATOM   4176  CG2 ILE A 496     -32.635   4.407 100.825  1.00147.04           C  
ANISOU 4176  CG2 ILE A 496    19080  22251  14538   1016    872   2459       C  
ATOM   4177  CD1 ILE A 496     -31.120   1.397 100.436  1.00152.80           C  
ANISOU 4177  CD1 ILE A 496    19876  22634  15546    780    711   2729       C  
ATOM   4178  N   GLY A 497     -28.888   4.188 103.301  1.00147.28           N  
ANISOU 4178  N   GLY A 497    19383  22267  14309   1093    534   2407       N  
ATOM   4179  CA  GLY A 497     -27.698   3.682 103.984  1.00148.32           C  
ANISOU 4179  CA  GLY A 497    19541  22445  14370   1109    418   2463       C  
ATOM   4180  C   GLY A 497     -26.535   4.654 103.962  1.00152.91           C  
ANISOU 4180  C   GLY A 497    20158  23053  14888   1097    299   2277       C  
ATOM   4181  O   GLY A 497     -25.390   4.255 103.729  1.00152.37           O  
ANISOU 4181  O   GLY A 497    20046  22980  14869   1085    185   2290       O  
ATOM   4182  N   LEU A 498     -26.838   5.944 104.178  1.00150.42           N  
ANISOU 4182  N   LEU A 498    19932  22772  14448   1100    332   2106       N  
ATOM   4183  CA  LEU A 498     -25.877   7.045 104.168  1.00150.76           C  
ANISOU 4183  CA  LEU A 498    20057  22825  14401   1036    234   1907       C  
ATOM   4184  C   LEU A 498     -25.958   7.841 105.490  1.00157.75           C  
ANISOU 4184  C   LEU A 498    21087  23860  14991   1063    243   1826       C  
ATOM   4185  O   LEU A 498     -27.071   8.016 106.004  1.00157.98           O  
ANISOU 4185  O   LEU A 498    21172  23929  14923   1160    370   1856       O  
ATOM   4186  CB  LEU A 498     -26.182   7.954 102.959  1.00149.29           C  
ANISOU 4186  CB  LEU A 498    19914  22459  14349   1000    274   1751       C  
ATOM   4187  CG  LEU A 498     -25.142   9.007 102.578  1.00153.92           C  
ANISOU 4187  CG  LEU A 498    20588  22996  14898    881    172   1555       C  
ATOM   4188  CD1 LEU A 498     -24.035   8.414 101.719  1.00153.13           C  
ANISOU 4188  CD1 LEU A 498    20339  22879  14966    796     56   1586       C  
ATOM   4189  CD2 LEU A 498     -25.789  10.153 101.860  1.00155.65           C  
ANISOU 4189  CD2 LEU A 498    20945  23050  15145    891    256   1404       C  
ATOM   4190  N   PRO A 499     -24.811   8.328 106.059  1.00156.03           N  
ANISOU 4190  N   PRO A 499    20924  23753  14608    973    113   1724       N  
ATOM   4191  CA  PRO A 499     -24.879   9.094 107.323  1.00157.73           C  
ANISOU 4191  CA  PRO A 499    21304  24105  14520    980    119   1629       C  
ATOM   4192  C   PRO A 499     -25.748  10.355 107.205  1.00160.59           C  
ANISOU 4192  C   PRO A 499    21883  24332  14802   1023    236   1450       C  
ATOM   4193  O   PRO A 499     -25.653  11.087 106.213  1.00159.08           O  
ANISOU 4193  O   PRO A 499    21764  23955  14723    962    237   1316       O  
ATOM   4194  CB  PRO A 499     -23.411   9.443 107.611  1.00160.65           C  
ANISOU 4194  CB  PRO A 499    21677  24606  14759    818    -57   1530       C  
ATOM   4195  CG  PRO A 499     -22.613   8.437 106.839  1.00164.03           C  
ANISOU 4195  CG  PRO A 499    21880  25048  15394    801   -147   1663       C  
ATOM   4196  CD  PRO A 499     -23.411   8.190 105.598  1.00157.41           C  
ANISOU 4196  CD  PRO A 499    21001  23969  14839    856    -43   1694       C  
ATOM   4197  N   THR A 500     -26.619  10.578 108.217  1.00157.60           N  
ANISOU 4197  N   THR A 500    21612  24053  14217   1153    344   1463       N  
ATOM   4198  CA  THR A 500     -27.588  11.683 108.315  1.00157.63           C  
ANISOU 4198  CA  THR A 500    21834  23967  14091   1277    484   1324       C  
ATOM   4199  C   THR A 500     -26.956  13.075 108.088  1.00161.14           C  
ANISOU 4199  C   THR A 500    22557  24244  14424   1164    431   1059       C  
ATOM   4200  O   THR A 500     -27.580  13.920 107.444  1.00160.41           O  
ANISOU 4200  O   THR A 500    22623  23963  14364   1251    532    951       O  
ATOM   4201  CB  THR A 500     -28.324  11.657 109.676  1.00166.03           C  
ANISOU 4201  CB  THR A 500    22969  25230  14885   1428    581   1377       C  
ATOM   4202  OG1 THR A 500     -27.381  11.570 110.748  1.00165.23           O  
ANISOU 4202  OG1 THR A 500    22914  25293  14572   1322    456   1353       O  
ATOM   4203  CG2 THR A 500     -29.339  10.523 109.781  1.00164.00           C  
ANISOU 4203  CG2 THR A 500    22487  25106  14721   1549    690   1629       C  
ATOM   4204  N   LYS A 501     -25.729  13.300 108.596  1.00158.04           N  
ANISOU 4204  N   LYS A 501    22226  23930  13891    963    274    964       N  
ATOM   4205  CA  LYS A 501     -25.004  14.572 108.493  1.00158.62           C  
ANISOU 4205  CA  LYS A 501    22581  23865  13822    778    204    715       C  
ATOM   4206  C   LYS A 501     -24.373  14.810 107.096  1.00159.70           C  
ANISOU 4206  C   LYS A 501    22665  23818  14196    615    136    660       C  
ATOM   4207  O   LYS A 501     -24.322  15.956 106.647  1.00159.99           O  
ANISOU 4207  O   LYS A 501    22976  23634  14181    534    159    474       O  
ATOM   4208  CB  LYS A 501     -23.901  14.653 109.570  1.00163.07           C  
ANISOU 4208  CB  LYS A 501    23188  24648  14124    578     49    649       C  
ATOM   4209  CG  LYS A 501     -24.404  14.680 111.015  1.00173.73           C  
ANISOU 4209  CG  LYS A 501    24660  26173  15177    706    107    653       C  
ATOM   4210  CD  LYS A 501     -23.244  14.677 112.008  1.00182.06           C  
ANISOU 4210  CD  LYS A 501    25716  27484  15974    490    -66    602       C  
ATOM   4211  CE  LYS A 501     -23.692  14.770 113.448  1.00191.71           C  
ANISOU 4211  CE  LYS A 501    27080  28886  16877    604    -15    589       C  
ATOM   4212  NZ  LYS A 501     -24.273  13.491 113.940  1.00198.49           N  
ANISOU 4212  NZ  LYS A 501    27665  29950  17803    819     44    863       N  
ATOM   4213  N   GLN A 502     -23.876  13.747 106.436  1.00153.25           N  
ANISOU 4213  N   GLN A 502    21525  23083  13618    572     57    820       N  
ATOM   4214  CA  GLN A 502     -23.188  13.815 105.140  1.00150.91           C  
ANISOU 4214  CA  GLN A 502    21131  22667  13539    424    -16    790       C  
ATOM   4215  C   GLN A 502     -24.141  14.112 103.953  1.00151.35           C  
ANISOU 4215  C   GLN A 502    21230  22467  13810    553    118    782       C  
ATOM   4216  O   GLN A 502     -25.158  13.422 103.830  1.00149.70           O  
ANISOU 4216  O   GLN A 502    20892  22267  13720    755    228    925       O  
ATOM   4217  CB  GLN A 502     -22.449  12.482 104.885  1.00151.14           C  
ANISOU 4217  CB  GLN A 502    20813  22880  13733    403   -122    978       C  
ATOM   4218  CG  GLN A 502     -21.408  12.521 103.760  1.00165.58           C  
ANISOU 4218  CG  GLN A 502    22514  24680  15719    226   -231    942       C  
ATOM   4219  CD  GLN A 502     -21.087  11.163 103.170  1.00182.47           C  
ANISOU 4219  CD  GLN A 502    24343  26904  18081    313   -269   1139       C  
ATOM   4220  OE1 GLN A 502     -21.306  10.106 103.780  1.00177.24           O  
ANISOU 4220  OE1 GLN A 502    23556  26366  17421    458   -257   1311       O  
ATOM   4221  NE2 GLN A 502     -20.537  11.163 101.964  1.00173.72           N  
ANISOU 4221  NE2 GLN A 502    23128  25722  17154    229   -312   1118       N  
ATOM   4222  N   PRO A 503     -23.799  15.068 103.033  1.00146.53           N  
ANISOU 4222  N   PRO A 503    20776  21651  13249    421    104    634       N  
ATOM   4223  CA  PRO A 503     -24.658  15.291 101.851  1.00144.19           C  
ANISOU 4223  CA  PRO A 503    20492  21141  13154    557    222    647       C  
ATOM   4224  C   PRO A 503     -24.608  14.090 100.902  1.00144.43           C  
ANISOU 4224  C   PRO A 503    20174  21225  13477    582    196    817       C  
ATOM   4225  O   PRO A 503     -23.613  13.359 100.899  1.00143.64           O  
ANISOU 4225  O   PRO A 503    19878  21268  13433    456     69    881       O  
ATOM   4226  CB  PRO A 503     -24.064  16.547 101.202  1.00146.68           C  
ANISOU 4226  CB  PRO A 503    21070  21241  13422    368    188    458       C  
ATOM   4227  CG  PRO A 503     -22.647  16.560 101.627  1.00152.43           C  
ANISOU 4227  CG  PRO A 503    21760  22122  14035     70     12    398       C  
ATOM   4228  CD  PRO A 503     -22.618  15.961 103.010  1.00149.38           C  
ANISOU 4228  CD  PRO A 503    21302  21982  13472    124    -22    462       C  
ATOM   4229  N   ILE A 504     -25.678  13.878 100.111  1.00138.60           N  
ANISOU 4229  N   ILE A 504    19367  20390  12906    754    317    891       N  
ATOM   4230  CA  ILE A 504     -25.790  12.731  99.201  1.00135.61           C  
ANISOU 4230  CA  ILE A 504    18698  20039  12789    777    309   1042       C  
ATOM   4231  C   ILE A 504     -24.804  12.872  98.018  1.00136.02           C  
ANISOU 4231  C   ILE A 504    18686  20000  12997    609    213    984       C  
ATOM   4232  O   ILE A 504     -24.889  13.842  97.256  1.00135.13           O  
ANISOU 4232  O   ILE A 504    18722  19718  12902    577    246    873       O  
ATOM   4233  CB  ILE A 504     -27.254  12.473  98.721  1.00137.92           C  
ANISOU 4233  CB  ILE A 504    18921  20300  13181    974    460   1136       C  
ATOM   4234  CG1 ILE A 504     -28.234  12.405  99.921  1.00139.78           C  
ANISOU 4234  CG1 ILE A 504    19207  20670  13231   1139    565   1198       C  
ATOM   4235  CG2 ILE A 504     -27.338  11.185  97.884  1.00137.05           C  
ANISOU 4235  CG2 ILE A 504    18539  20218  13315    953    442   1287       C  
ATOM   4236  CD1 ILE A 504     -29.708  12.744  99.606  1.00146.88           C  
ANISOU 4236  CD1 ILE A 504    20114  21575  14119   1350    733   1234       C  
ATOM   4237  N   PRO A 505     -23.860  11.905  97.866  1.00130.54           N  
ANISOU 4237  N   PRO A 505    17775  19424  12399    521    100   1069       N  
ATOM   4238  CA  PRO A 505     -22.921  11.978  96.735  1.00128.80           C  
ANISOU 4238  CA  PRO A 505    17462  19161  12314    381     16   1026       C  
ATOM   4239  C   PRO A 505     -23.594  11.534  95.440  1.00128.82           C  
ANISOU 4239  C   PRO A 505    17351  19039  12556    468     89   1087       C  
ATOM   4240  O   PRO A 505     -24.336  10.550  95.420  1.00127.36           O  
ANISOU 4240  O   PRO A 505    17046  18875  12472    591    147   1216       O  
ATOM   4241  CB  PRO A 505     -21.772  11.051  97.146  1.00131.13           C  
ANISOU 4241  CB  PRO A 505    17563  19668  12592    321   -112   1112       C  
ATOM   4242  CG  PRO A 505     -22.334  10.147  98.186  1.00136.27           C  
ANISOU 4242  CG  PRO A 505    18169  20419  13187    468    -76   1247       C  
ATOM   4243  CD  PRO A 505     -23.639  10.691  98.683  1.00132.27           C  
ANISOU 4243  CD  PRO A 505    17834  19824  12600    573     55   1219       C  
ATOM   4244  N   ASP A 506     -23.360  12.293  94.370  1.00123.94           N  
ANISOU 4244  N   ASP A 506    16788  18293  12010    384     88    993       N  
ATOM   4245  CA  ASP A 506     -23.941  12.041  93.055  1.00121.76           C  
ANISOU 4245  CA  ASP A 506    16417  17908  11938    449    150   1029       C  
ATOM   4246  C   ASP A 506     -23.330  10.806  92.392  1.00122.38           C  
ANISOU 4246  C   ASP A 506    16253  18056  12188    432     84   1125       C  
ATOM   4247  O   ASP A 506     -22.162  10.495  92.626  1.00122.06           O  
ANISOU 4247  O   ASP A 506    16127  18139  12112    346    -23   1130       O  
ATOM   4248  CB  ASP A 506     -23.767  13.275  92.149  1.00123.93           C  
ANISOU 4248  CB  ASP A 506    16845  18028  12214    361    163    904       C  
ATOM   4249  CG  ASP A 506     -22.334  13.681  91.859  1.00135.46           C  
ANISOU 4249  CG  ASP A 506    18300  19529  13640    134     42    826       C  
ATOM   4250  OD1 ASP A 506     -21.531  13.762  92.820  1.00137.69           O  
ANISOU 4250  OD1 ASP A 506    18608  19942  13767     18    -44    796       O  
ATOM   4251  OD2 ASP A 506     -22.029  13.969  90.681  1.00140.31           O  
ANISOU 4251  OD2 ASP A 506    18880  20069  14361     61     35    797       O  
ATOM   4252  N   CYS A 507     -24.131  10.108  91.568  1.00116.77           N  
ANISOU 4252  N   CYS A 507    15439  17283  11643    522    151   1200       N  
ATOM   4253  CA  CYS A 507     -23.706   8.917  90.831  1.00115.30           C  
ANISOU 4253  CA  CYS A 507    15076  17114  11619    527    111   1281       C  
ATOM   4254  C   CYS A 507     -23.172   9.314  89.457  1.00115.66           C  
ANISOU 4254  C   CYS A 507    15073  17097  11774    454     84   1208       C  
ATOM   4255  O   CYS A 507     -23.414  10.432  88.995  1.00114.91           O  
ANISOU 4255  O   CYS A 507    15085  16921  11655    411    118   1118       O  
ATOM   4256  CB  CYS A 507     -24.844   7.906  90.716  1.00115.48           C  
ANISOU 4256  CB  CYS A 507    15039  17102  11735    618    193   1395       C  
ATOM   4257  SG  CYS A 507     -25.412   7.237  92.300  1.00120.84           S  
ANISOU 4257  SG  CYS A 507    15752  17876  12285    688    226   1514       S  
ATOM   4258  N   GLU A 508     -22.444   8.392  88.809  1.00109.97           N  
ANISOU 4258  N   GLU A 508    14209  16411  11162    456     30   1253       N  
ATOM   4259  CA  GLU A 508     -21.839   8.613  87.501  1.00108.49           C  
ANISOU 4259  CA  GLU A 508    13947  16200  11073    396      3   1197       C  
ATOM   4260  C   GLU A 508     -22.282   7.559  86.476  1.00110.22           C  
ANISOU 4260  C   GLU A 508    14074  16344  11460    470     42   1253       C  
ATOM   4261  O   GLU A 508     -22.788   6.498  86.852  1.00109.65           O  
ANISOU 4261  O   GLU A 508    13994  16247  11423    546     70   1344       O  
ATOM   4262  CB  GLU A 508     -20.309   8.610  87.622  1.00110.86           C  
ANISOU 4262  CB  GLU A 508    14153  16664  11305    324   -107   1181       C  
ATOM   4263  CG  GLU A 508     -19.765   9.711  88.516  1.00125.74           C  
ANISOU 4263  CG  GLU A 508    16134  18638  13005    186   -161   1107       C  
ATOM   4264  CD  GLU A 508     -18.276   9.989  88.430  1.00157.07           C  
ANISOU 4264  CD  GLU A 508    19987  22810  16882     47   -271   1075       C  
ATOM   4265  OE1 GLU A 508     -17.593   9.433  87.537  1.00151.91           O  
ANISOU 4265  OE1 GLU A 508    19165  22240  16314     76   -301   1106       O  
ATOM   4266  OE2 GLU A 508     -17.794  10.794  89.257  1.00156.81           O  
ANISOU 4266  OE2 GLU A 508    20035  22872  16673   -102   -327   1016       O  
ATOM   4267  N   ILE A 509     -22.073   7.866  85.177  1.00105.37           N  
ANISOU 4267  N   ILE A 509    13411  15690  10935    428     44   1196       N  
ATOM   4268  CA  ILE A 509     -22.382   6.997  84.036  1.00103.74           C  
ANISOU 4268  CA  ILE A 509    13129  15416  10871    472     74   1220       C  
ATOM   4269  C   ILE A 509     -21.060   6.425  83.512  1.00106.33           C  
ANISOU 4269  C   ILE A 509    13348  15826  11226    495      5   1219       C  
ATOM   4270  O   ILE A 509     -20.179   7.205  83.135  1.00105.70           O  
ANISOU 4270  O   ILE A 509    13218  15838  11106    417    -41   1160       O  
ATOM   4271  CB  ILE A 509     -23.172   7.754  82.919  1.00105.77           C  
ANISOU 4271  CB  ILE A 509    13402  15597  11189    434    134   1162       C  
ATOM   4272  CG1 ILE A 509     -24.390   8.529  83.469  1.00105.99           C  
ANISOU 4272  CG1 ILE A 509    13531  15590  11149    454    208   1165       C  
ATOM   4273  CG2 ILE A 509     -23.587   6.810  81.786  1.00105.91           C  
ANISOU 4273  CG2 ILE A 509    13347  15561  11333    459    162   1181       C  
ATOM   4274  CD1 ILE A 509     -24.223  10.026  83.437  1.00110.96           C  
ANISOU 4274  CD1 ILE A 509    14275  16192  11691    411    215   1086       C  
ATOM   4275  N   LYS A 510     -20.921   5.073  83.502  1.00102.39           N  
ANISOU 4275  N   LYS A 510    12826  15299  10779    605      4   1291       N  
ATOM   4276  CA  LYS A 510     -19.715   4.360  83.040  1.00102.43           C  
ANISOU 4276  CA  LYS A 510    12737  15389  10792    698    -45   1308       C  
ATOM   4277  C   LYS A 510     -19.301   4.797  81.637  1.00104.38           C  
ANISOU 4277  C   LYS A 510    12899  15662  11100    653    -47   1229       C  
ATOM   4278  O   LYS A 510     -18.174   5.259  81.448  1.00104.90           O  
ANISOU 4278  O   LYS A 510    12852  15902  11103    628   -103   1204       O  
ATOM   4279  CB  LYS A 510     -19.926   2.832  83.038  1.00105.55           C  
ANISOU 4279  CB  LYS A 510    13199  15662  11242    840    -15   1389       C  
ATOM   4280  CG  LYS A 510     -20.040   2.183  84.392  1.00120.44           C  
ANISOU 4280  CG  LYS A 510    15164  17543  13055    916    -20   1495       C  
ATOM   4281  CD  LYS A 510     -20.040   0.675  84.246  1.00130.30           C  
ANISOU 4281  CD  LYS A 510    16518  18645  14345   1060     11   1577       C  
ATOM   4282  CE  LYS A 510     -19.918   0.052  85.603  1.00141.69           C  
ANISOU 4282  CE  LYS A 510    18036  20107  15693   1159     -2   1700       C  
ATOM   4283  NZ  LYS A 510     -21.211   0.041  86.341  1.00148.82           N  
ANISOU 4283  NZ  LYS A 510    19044  20906  16594   1042     52   1746       N  
ATOM   4284  N   ASN A 511     -20.218   4.650  80.665  1.00 98.41           N  
ANISOU 4284  N   ASN A 511    12183  14762  10447    628     14   1196       N  
ATOM   4285  CA  ASN A 511     -20.002   4.998  79.263  1.00 96.86           C  
ANISOU 4285  CA  ASN A 511    11917  14577  10308    591     23   1127       C  
ATOM   4286  C   ASN A 511     -21.285   5.518  78.626  1.00 97.89           C  
ANISOU 4286  C   ASN A 511    12099  14596  10497    507     85   1090       C  
ATOM   4287  O   ASN A 511     -22.387   5.142  79.027  1.00 97.59           O  
ANISOU 4287  O   ASN A 511    12133  14468  10479    504    128   1127       O  
ATOM   4288  CB  ASN A 511     -19.440   3.810  78.466  1.00 98.07           C  
ANISOU 4288  CB  ASN A 511    12038  14715  10510    721     26   1133       C  
ATOM   4289  CG  ASN A 511     -20.000   2.460  78.846  1.00111.73           C  
ANISOU 4289  CG  ASN A 511    13893  16284  12273    818     59   1193       C  
ATOM   4290  OD1 ASN A 511     -21.088   2.070  78.419  1.00103.34           O  
ANISOU 4290  OD1 ASN A 511    12917  15072  11275    757    109   1182       O  
ATOM   4291  ND2 ASN A 511     -19.251   1.706  79.640  1.00101.43           N  
ANISOU 4291  ND2 ASN A 511    12608  15019  10911    962     31   1266       N  
ATOM   4292  N   ARG A 512     -21.126   6.400  77.639  1.00 92.53           N  
ANISOU 4292  N   ARG A 512    11373  13953   9830    440     89   1031       N  
ATOM   4293  CA  ARG A 512     -22.216   7.051  76.912  1.00 90.88           C  
ANISOU 4293  CA  ARG A 512    11195  13680   9654    387    144   1004       C  
ATOM   4294  C   ARG A 512     -21.865   7.176  75.411  1.00 93.48           C  
ANISOU 4294  C   ARG A 512    11449  14041  10029    368    148    954       C  
ATOM   4295  O   ARG A 512     -20.693   6.991  75.058  1.00 93.36           O  
ANISOU 4295  O   ARG A 512    11355  14114  10003    383    108    937       O  
ATOM   4296  CB  ARG A 512     -22.507   8.436  77.530  1.00 90.19           C  
ANISOU 4296  CB  ARG A 512    11191  13590   9486    329    157    995       C  
ATOM   4297  CG  ARG A 512     -21.323   9.392  77.520  1.00 96.99           C  
ANISOU 4297  CG  ARG A 512    12051  14523  10277    238    108    956       C  
ATOM   4298  CD  ARG A 512     -21.780  10.817  77.636  1.00100.03           C  
ANISOU 4298  CD  ARG A 512    12578  14839  10591    173    143    929       C  
ATOM   4299  NE  ARG A 512     -20.652  11.742  77.696  1.00107.38           N  
ANISOU 4299  NE  ARG A 512    13544  15822  11434     28     94    890       N  
ATOM   4300  CZ  ARG A 512     -20.770  13.054  77.859  1.00122.42           C  
ANISOU 4300  CZ  ARG A 512    15629  17637  13249    -62    116    858       C  
ATOM   4301  NH1 ARG A 512     -19.692  13.819  77.912  1.00110.58           N  
ANISOU 4301  NH1 ARG A 512    14168  16190  11655   -246     65    823       N  
ATOM   4302  NH2 ARG A 512     -21.967  13.609  77.987  1.00111.83           N  
ANISOU 4302  NH2 ARG A 512    14439  16161  11890     30    193    864       N  
ATOM   4303  N   PRO A 513     -22.831   7.500  74.512  1.00 88.97           N  
ANISOU 4303  N   PRO A 513    10880  13435   9489    345    195    938       N  
ATOM   4304  CA  PRO A 513     -22.488   7.614  73.084  1.00 88.77           C  
ANISOU 4304  CA  PRO A 513    10782  13452   9493    329    198    894       C  
ATOM   4305  C   PRO A 513     -21.491   8.738  72.798  1.00 93.36           C  
ANISOU 4305  C   PRO A 513    11342  14108  10023    264    175    874       C  
ATOM   4306  O   PRO A 513     -21.538   9.786  73.445  1.00 94.04           O  
ANISOU 4306  O   PRO A 513    11515  14171  10047    207    176    884       O  
ATOM   4307  CB  PRO A 513     -23.840   7.884  72.413  1.00 89.97           C  
ANISOU 4307  CB  PRO A 513    10943  13583   9659    318    252    899       C  
ATOM   4308  CG  PRO A 513     -24.857   7.418  73.392  1.00 94.25           C  
ANISOU 4308  CG  PRO A 513    11532  14084  10195    333    275    946       C  
ATOM   4309  CD  PRO A 513     -24.272   7.738  74.723  1.00 89.94           C  
ANISOU 4309  CD  PRO A 513    11049  13519   9604    346    249    968       C  
ATOM   4310  N   SER A 514     -20.567   8.498  71.853  1.00 89.11           N  
ANISOU 4310  N   SER A 514    10704  13662   9493    262    155    846       N  
ATOM   4311  CA  SER A 514     -19.561   9.485  71.478  1.00 88.93           C  
ANISOU 4311  CA  SER A 514    10639  13744   9408    163    133    837       C  
ATOM   4312  C   SER A 514     -20.179  10.539  70.567  1.00 92.15           C  
ANISOU 4312  C   SER A 514    11104  14103   9806    101    178    833       C  
ATOM   4313  O   SER A 514     -20.720  10.205  69.506  1.00 91.71           O  
ANISOU 4313  O   SER A 514    11005  14046   9793    149    209    820       O  
ATOM   4314  CB  SER A 514     -18.364   8.819  70.806  1.00 92.19           C  
ANISOU 4314  CB  SER A 514    10899  14318   9812    204    105    823       C  
ATOM   4315  OG  SER A 514     -17.417   9.773  70.352  1.00 99.82           O  
ANISOU 4315  OG  SER A 514    11798  15425  10704     74     87    824       O  
ATOM   4316  N   LEU A 515     -20.105  11.815  70.997  1.00 87.90           N  
ANISOU 4316  N   LEU A 515    10687  13517   9195     -4    182    846       N  
ATOM   4317  CA  LEU A 515     -20.617  12.969  70.250  1.00 87.11           C  
ANISOU 4317  CA  LEU A 515    10695  13343   9061    -46    231    858       C  
ATOM   4318  C   LEU A 515     -19.764  13.218  68.999  1.00 90.01           C  
ANISOU 4318  C   LEU A 515    10965  13823   9410   -130    226    854       C  
ATOM   4319  O   LEU A 515     -20.258  13.796  68.032  1.00 89.45           O  
ANISOU 4319  O   LEU A 515    10937  13718   9331   -121    271    872       O  
ATOM   4320  CB  LEU A 515     -20.657  14.226  71.132  1.00 87.77           C  
ANISOU 4320  CB  LEU A 515    10994  13304   9049   -134    242    867       C  
ATOM   4321  CG  LEU A 515     -21.598  14.182  72.324  1.00 92.13           C  
ANISOU 4321  CG  LEU A 515    11662  13751   9591    -34    264    874       C  
ATOM   4322  CD1 LEU A 515     -20.974  14.839  73.536  1.00 93.57           C  
ANISOU 4322  CD1 LEU A 515    11989  13887   9676   -153    230    853       C  
ATOM   4323  CD2 LEU A 515     -22.932  14.812  72.002  1.00 93.90           C  
ANISOU 4323  CD2 LEU A 515    12010  13870   9797     95    345    907       C  
ATOM   4324  N   LEU A 516     -18.491  12.767  69.022  1.00 85.71           N  
ANISOU 4324  N   LEU A 516    10276  13443   8846   -194    174    841       N  
ATOM   4325  CA  LEU A 516     -17.564  12.866  67.899  1.00 85.53           C  
ANISOU 4325  CA  LEU A 516    10120  13587   8791   -266    169    842       C  
ATOM   4326  C   LEU A 516     -18.026  11.934  66.775  1.00 87.88           C  
ANISOU 4326  C   LEU A 516    10310  13918   9162   -115    199    819       C  
ATOM   4327  O   LEU A 516     -18.068  12.358  65.620  1.00 87.66           O  
ANISOU 4327  O   LEU A 516    10260  13930   9116   -144    231    827       O  
ATOM   4328  CB  LEU A 516     -16.135  12.523  68.346  1.00 86.52           C  
ANISOU 4328  CB  LEU A 516    10086  13935   8854   -336    108    844       C  
ATOM   4329  CG  LEU A 516     -15.020  12.796  67.340  1.00 92.10           C  
ANISOU 4329  CG  LEU A 516    10632  14874   9487   -445    103    860       C  
ATOM   4330  CD1 LEU A 516     -14.472  14.207  67.495  1.00 93.38           C  
ANISOU 4330  CD1 LEU A 516    10894  15052   9534   -730     90    890       C  
ATOM   4331  CD2 LEU A 516     -13.907  11.782  67.492  1.00 96.06           C  
ANISOU 4331  CD2 LEU A 516    10899  15643   9955   -351     62    862       C  
ATOM   4332  N   VAL A 517     -18.410  10.682  67.126  1.00 82.88           N  
ANISOU 4332  N   VAL A 517     9638  13254   8598     33    192    792       N  
ATOM   4333  CA  VAL A 517     -18.917   9.669  66.193  1.00 81.57           C  
ANISOU 4333  CA  VAL A 517     9417  13088   8488    154    216    753       C  
ATOM   4334  C   VAL A 517     -20.217  10.207  65.560  1.00 85.40           C  
ANISOU 4334  C   VAL A 517     9979  13480   8988    145    260    763       C  
ATOM   4335  O   VAL A 517     -20.386  10.099  64.344  1.00 85.72           O  
ANISOU 4335  O   VAL A 517     9963  13583   9023    163    282    744       O  
ATOM   4336  CB  VAL A 517     -19.101   8.281  66.878  1.00 84.28           C  
ANISOU 4336  CB  VAL A 517     9770  13368   8885    278    201    729       C  
ATOM   4337  CG1 VAL A 517     -19.769   7.274  65.945  1.00 83.58           C  
ANISOU 4337  CG1 VAL A 517     9685  13233   8836    357    229    677       C  
ATOM   4338  CG2 VAL A 517     -17.765   7.730  67.365  1.00 84.86           C  
ANISOU 4338  CG2 VAL A 517     9750  13571   8919    340    165    735       C  
ATOM   4339  N   GLU A 518     -21.086  10.848  66.377  1.00 81.14           N  
ANISOU 4339  N   GLU A 518     9562  12821   8446    132    274    800       N  
ATOM   4340  CA  GLU A 518     -22.337  11.467  65.925  1.00 80.62           C  
ANISOU 4340  CA  GLU A 518     9562  12705   8367    163    321    832       C  
ATOM   4341  C   GLU A 518     -22.044  12.598  64.938  1.00 83.92           C  
ANISOU 4341  C   GLU A 518    10007  13157   8723    109    347    864       C  
ATOM   4342  O   GLU A 518     -22.662  12.647  63.877  1.00 83.20           O  
ANISOU 4342  O   GLU A 518     9874  13118   8619    153    376    874       O  
ATOM   4343  CB  GLU A 518     -23.172  11.985  67.113  1.00 82.14           C  
ANISOU 4343  CB  GLU A 518     9884  12784   8542    195    340    872       C  
ATOM   4344  CG  GLU A 518     -23.685  10.915  68.071  1.00 95.34           C  
ANISOU 4344  CG  GLU A 518    11535  14426  10262    242    325    861       C  
ATOM   4345  CD  GLU A 518     -24.148   9.606  67.455  1.00122.83           C  
ANISOU 4345  CD  GLU A 518    14919  17956  13796    267    319    827       C  
ATOM   4346  OE1 GLU A 518     -23.288   8.718  67.257  1.00116.38           O  
ANISOU 4346  OE1 GLU A 518    14052  17156  13013    264    288    781       O  
ATOM   4347  OE2 GLU A 518     -25.354   9.477  67.143  1.00123.93           O  
ANISOU 4347  OE2 GLU A 518    15035  18127  13924    289    347    847       O  
ATOM   4348  N   LYS A 519     -21.062  13.463  65.265  1.00 81.01           N  
ANISOU 4348  N   LYS A 519     9705  12772   8301     -7    335    882       N  
ATOM   4349  CA  LYS A 519     -20.631  14.573  64.416  1.00 81.80           C  
ANISOU 4349  CA  LYS A 519     9865  12888   8329   -102    361    922       C  
ATOM   4350  C   LYS A 519     -20.052  14.060  63.087  1.00 86.62           C  
ANISOU 4350  C   LYS A 519    10297  13672   8940   -110    358    903       C  
ATOM   4351  O   LYS A 519     -20.349  14.635  62.036  1.00 86.48           O  
ANISOU 4351  O   LYS A 519    10300  13677   8881   -107    396    941       O  
ATOM   4352  CB  LYS A 519     -19.610  15.452  65.146  1.00 85.29           C  
ANISOU 4352  CB  LYS A 519    10415  13291   8699   -284    338    935       C  
ATOM   4353  CG  LYS A 519     -20.245  16.492  66.062  1.00 97.94           C  
ANISOU 4353  CG  LYS A 519    12284  14681  10250   -292    368    963       C  
ATOM   4354  CD  LYS A 519     -19.200  17.174  66.924  1.00107.42           C  
ANISOU 4354  CD  LYS A 519    13596  15849  11368   -508    330    952       C  
ATOM   4355  CE  LYS A 519     -19.778  18.292  67.742  1.00115.79           C  
ANISOU 4355  CE  LYS A 519    14977  16667  12351   -522    369    966       C  
ATOM   4356  NZ  LYS A 519     -18.729  18.974  68.544  1.00124.97           N  
ANISOU 4356  NZ  LYS A 519    16271  17801  13412   -783    325    943       N  
ATOM   4357  N   ILE A 520     -19.268  12.957  63.132  1.00 83.63           N  
ANISOU 4357  N   ILE A 520     9758  13420   8597    -89    320    849       N  
ATOM   4358  CA  ILE A 520     -18.678  12.310  61.954  1.00 83.97           C  
ANISOU 4358  CA  ILE A 520     9638  13638   8630    -57    323    816       C  
ATOM   4359  C   ILE A 520     -19.821  11.735  61.084  1.00 88.99           C  
ANISOU 4359  C   ILE A 520    10261  14253   9298     57    349    785       C  
ATOM   4360  O   ILE A 520     -19.767  11.856  59.858  1.00 89.45           O  
ANISOU 4360  O   ILE A 520    10257  14416   9314     59    373    785       O  
ATOM   4361  CB  ILE A 520     -17.609  11.245  62.373  1.00 87.29           C  
ANISOU 4361  CB  ILE A 520     9921  14185   9060     -7    285    770       C  
ATOM   4362  CG1 ILE A 520     -16.317  11.935  62.873  1.00 88.60           C  
ANISOU 4362  CG1 ILE A 520    10032  14485   9147   -157    256    813       C  
ATOM   4363  CG2 ILE A 520     -17.267  10.281  61.232  1.00 88.48           C  
ANISOU 4363  CG2 ILE A 520     9940  14476   9201    106    301    715       C  
ATOM   4364  CD1 ILE A 520     -15.421  11.089  63.792  1.00 93.74           C  
ANISOU 4364  CD1 ILE A 520    10574  15252   9792    -94    210    797       C  
ATOM   4365  N   ASN A 521     -20.868  11.167  61.720  1.00 86.04           N  
ANISOU 4365  N   ASN A 521     9943  13767   8983    130    345    766       N  
ATOM   4366  CA  ASN A 521     -22.032  10.621  61.020  1.00 86.49           C  
ANISOU 4366  CA  ASN A 521     9980  13834   9049    193    361    741       C  
ATOM   4367  C   ASN A 521     -22.792  11.741  60.312  1.00 94.55           C  
ANISOU 4367  C   ASN A 521    11039  14879  10009    194    398    813       C  
ATOM   4368  O   ASN A 521     -23.171  11.572  59.150  1.00 95.16           O  
ANISOU 4368  O   ASN A 521    11045  15064  10047    216    411    800       O  
ATOM   4369  CB  ASN A 521     -22.956   9.867  61.980  1.00 84.38           C  
ANISOU 4369  CB  ASN A 521     9758  13467   8836    228    348    725       C  
ATOM   4370  CG  ASN A 521     -23.968   8.958  61.305  1.00105.13           C  
ANISOU 4370  CG  ASN A 521    12344  16138  11462    241    350    678       C  
ATOM   4371  OD1 ASN A 521     -24.698   9.344  60.377  1.00 99.14           O  
ANISOU 4371  OD1 ASN A 521    11542  15477  10649    241    368    699       O  
ATOM   4372  ND2 ASN A 521     -24.083   7.737  61.799  1.00 96.56           N  
ANISOU 4372  ND2 ASN A 521    11284  14984  10421    239    330    621       N  
ATOM   4373  N   LEU A 522     -22.997  12.887  61.003  1.00 93.22           N  
ANISOU 4373  N   LEU A 522    10999  14606   9813    183    420    889       N  
ATOM   4374  CA  LEU A 522     -23.689  14.059  60.453  1.00 94.39           C  
ANISOU 4374  CA  LEU A 522    11236  14742   9885    226    468    977       C  
ATOM   4375  C   LEU A 522     -22.877  14.667  59.310  1.00101.28           C  
ANISOU 4375  C   LEU A 522    12092  15692  10697    157    484   1005       C  
ATOM   4376  O   LEU A 522     -23.462  15.068  58.303  1.00101.74           O  
ANISOU 4376  O   LEU A 522    12139  15825  10693    216    516   1055       O  
ATOM   4377  CB  LEU A 522     -23.964  15.113  61.538  1.00 94.62           C  
ANISOU 4377  CB  LEU A 522    11465  14600   9885    245    496   1040       C  
ATOM   4378  CG  LEU A 522     -25.064  14.777  62.545  1.00 99.02           C  
ANISOU 4378  CG  LEU A 522    12046  15111  10466    350    502   1044       C  
ATOM   4379  CD1 LEU A 522     -24.818  15.470  63.859  1.00 99.44           C  
ANISOU 4379  CD1 LEU A 522    12286  14992  10505    331    511   1059       C  
ATOM   4380  CD2 LEU A 522     -26.436  15.144  62.017  1.00102.50           C  
ANISOU 4380  CD2 LEU A 522    12475  15632  10839    503    550   1116       C  
ATOM   4381  N   PHE A 523     -21.530  14.688  59.448  1.00 99.21           N  
ANISOU 4381  N   PHE A 523    11806  15452  10438     32    462    981       N  
ATOM   4382  CA  PHE A 523     -20.608  15.185  58.424  1.00100.70           C  
ANISOU 4382  CA  PHE A 523    11950  15754  10558    -66    477   1011       C  
ATOM   4383  C   PHE A 523     -20.694  14.314  57.175  1.00105.01           C  
ANISOU 4383  C   PHE A 523    12320  16481  11096      4    477    961       C  
ATOM   4384  O   PHE A 523     -20.637  14.843  56.070  1.00105.00           O  
ANISOU 4384  O   PHE A 523    12303  16573  11021    -12    508   1010       O  
ATOM   4385  CB  PHE A 523     -19.162  15.234  58.956  1.00103.45           C  
ANISOU 4385  CB  PHE A 523    12258  16155  10895   -221    446    996       C  
ATOM   4386  CG  PHE A 523     -18.099  15.452  57.903  1.00106.61           C  
ANISOU 4386  CG  PHE A 523    12541  16748  11217   -328    458   1019       C  
ATOM   4387  CD1 PHE A 523     -17.848  16.722  57.395  1.00111.35           C  
ANISOU 4387  CD1 PHE A 523    13264  17320  11723   -468    496   1115       C  
ATOM   4388  CD2 PHE A 523     -17.349  14.387  57.417  1.00109.45           C  
ANISOU 4388  CD2 PHE A 523    12685  17319  11584   -279    440    952       C  
ATOM   4389  CE1 PHE A 523     -16.869  16.922  56.419  1.00113.64           C  
ANISOU 4389  CE1 PHE A 523    13432  17816  11928   -587    511   1149       C  
ATOM   4390  CE2 PHE A 523     -16.373  14.587  56.437  1.00113.70           C  
ANISOU 4390  CE2 PHE A 523    13093  18077  12031   -362    460    980       C  
ATOM   4391  CZ  PHE A 523     -16.138  15.853  55.946  1.00112.89           C  
ANISOU 4391  CZ  PHE A 523    13086  17971  11838   -529    493   1081       C  
ATOM   4392  N   ALA A 524     -20.819  12.987  57.354  1.00101.81           N  
ANISOU 4392  N   ALA A 524    11811  16115  10756     75    446    862       N  
ATOM   4393  CA  ALA A 524     -20.935  12.029  56.261  1.00102.26           C  
ANISOU 4393  CA  ALA A 524    11745  16312  10796    136    444    787       C  
ATOM   4394  C   ALA A 524     -22.299  12.150  55.573  1.00107.94           C  
ANISOU 4394  C   ALA A 524    12474  17060  11479    193    459    810       C  
ATOM   4395  O   ALA A 524     -22.346  12.179  54.345  1.00107.80           O  
ANISOU 4395  O   ALA A 524    12387  17185  11388    205    475    808       O  
ATOM   4396  CB  ALA A 524     -20.723  10.614  56.776  1.00102.66           C  
ANISOU 4396  CB  ALA A 524    11755  16338  10912    191    412    679       C  
ATOM   4397  N   MET A 525     -23.397  12.251  56.363  1.00105.89           N  
ANISOU 4397  N   MET A 525    12283  16700  11251    233    455    840       N  
ATOM   4398  CA  MET A 525     -24.770  12.381  55.865  1.00106.82           C  
ANISOU 4398  CA  MET A 525    12378  16897  11314    297    467    879       C  
ATOM   4399  C   MET A 525     -24.932  13.691  55.076  1.00111.22           C  
ANISOU 4399  C   MET A 525    12979  17507  11771    340    511   1000       C  
ATOM   4400  O   MET A 525     -25.272  13.641  53.893  1.00111.48           O  
ANISOU 4400  O   MET A 525    12926  17707  11724    366    517   1007       O  
ATOM   4401  CB  MET A 525     -25.784  12.310  57.026  1.00109.38           C  
ANISOU 4401  CB  MET A 525    12751  17132  11675    339    462    906       C  
ATOM   4402  CG  MET A 525     -27.232  12.174  56.568  1.00114.66           C  
ANISOU 4402  CG  MET A 525    13337  17958  12272    396    465    940       C  
ATOM   4403  SD  MET A 525     -28.451  12.838  57.741  1.00120.13           S  
ANISOU 4403  SD  MET A 525    14091  18611  12944    510    497   1048       S  
ATOM   4404  CE  MET A 525     -28.622  11.451  58.870  1.00116.28           C  
ANISOU 4404  CE  MET A 525    13575  18052  12555    410    453    951       C  
ATOM   4405  N   PHE A 526     -24.656  14.847  55.722  1.00107.56           N  
ANISOU 4405  N   PHE A 526    12676  16892  11301    342    544   1092       N  
ATOM   4406  CA  PHE A 526     -24.767  16.173  55.105  1.00107.98           C  
ANISOU 4406  CA  PHE A 526    12847  16929  11252    386    598   1220       C  
ATOM   4407  C   PHE A 526     -23.675  16.428  54.064  1.00110.60           C  
ANISOU 4407  C   PHE A 526    13142  17346  11535    281    608   1230       C  
ATOM   4408  O   PHE A 526     -23.895  17.217  53.144  1.00110.94           O  
ANISOU 4408  O   PHE A 526    13231  17445  11476    324    649   1329       O  
ATOM   4409  CB  PHE A 526     -24.761  17.283  56.166  1.00110.26           C  
ANISOU 4409  CB  PHE A 526    13376  16983  11533    401    634   1299       C  
ATOM   4410  CG  PHE A 526     -26.048  17.355  56.951  1.00111.89           C  
ANISOU 4410  CG  PHE A 526    13632  17147  11734    566    651   1334       C  
ATOM   4411  CD1 PHE A 526     -27.213  17.842  56.367  1.00116.42           C  
ANISOU 4411  CD1 PHE A 526    14203  17827  12204    753    693   1435       C  
ATOM   4412  CD2 PHE A 526     -26.100  16.930  58.271  1.00113.38           C  
ANISOU 4412  CD2 PHE A 526    13851  17225  12003    547    628   1277       C  
ATOM   4413  CE1 PHE A 526     -28.410  17.893  57.087  1.00117.81           C  
ANISOU 4413  CE1 PHE A 526    14387  18023  12353    923    715   1479       C  
ATOM   4414  CE2 PHE A 526     -27.296  16.985  58.992  1.00116.69           C  
ANISOU 4414  CE2 PHE A 526    14295  17642  12401    702    651   1316       C  
ATOM   4415  CZ  PHE A 526     -28.442  17.470  58.398  1.00116.03           C  
ANISOU 4415  CZ  PHE A 526    14191  17686  12209    891    696   1417       C  
ATOM   4416  N   GLY A 527     -22.536  15.751  54.208  1.00105.91           N  
ANISOU 4416  N   GLY A 527    12459  16785  10997    163    576   1139       N  
ATOM   4417  CA  GLY A 527     -21.413  15.847  53.278  1.00106.33           C  
ANISOU 4417  CA  GLY A 527    12433  16975  10994     63    586   1141       C  
ATOM   4418  C   GLY A 527     -21.767  15.362  51.888  1.00109.65           C  
ANISOU 4418  C   GLY A 527    12712  17603  11345    131    593   1116       C  
ATOM   4419  O   GLY A 527     -21.371  15.986  50.901  1.00109.43           O  
ANISOU 4419  O   GLY A 527    12677  17679  11221     94    627   1189       O  
ATOM   4420  N   THR A 528     -22.554  14.262  51.812  1.00105.62           N  
ANISOU 4420  N   THR A 528    12105  17156  10869    213    559   1016       N  
ATOM   4421  CA  THR A 528     -23.051  13.685  50.561  1.00105.81           C  
ANISOU 4421  CA  THR A 528    12009  17381  10814    261    554    969       C  
ATOM   4422  C   THR A 528     -23.967  14.702  49.881  1.00109.63           C  
ANISOU 4422  C   THR A 528    12532  17933  11190    335    586   1106       C  
ATOM   4423  O   THR A 528     -23.776  14.981  48.707  1.00110.62           O  
ANISOU 4423  O   THR A 528    12604  18216  11211    339    608   1145       O  
ATOM   4424  CB  THR A 528     -23.775  12.345  50.791  1.00115.74           C  
ANISOU 4424  CB  THR A 528    13202  18655  12118    283    507    834       C  
ATOM   4425  OG1 THR A 528     -23.165  11.619  51.852  1.00114.73           O  
ANISOU 4425  OG1 THR A 528    13106  18384  12102    254    485    751       O  
ATOM   4426  CG2 THR A 528     -23.806  11.480  49.546  1.00116.44           C  
ANISOU 4426  CG2 THR A 528    13185  18934  12123    282    495    729       C  
ATOM   4427  N   GLY A 529     -24.894  15.287  50.645  1.00104.90           N  
ANISOU 4427  N   GLY A 529    12032  17220  10604    413    596   1190       N  
ATOM   4428  CA  GLY A 529     -25.830  16.306  50.173  1.00105.32           C  
ANISOU 4428  CA  GLY A 529    12147  17327  10544    544    636   1342       C  
ATOM   4429  C   GLY A 529     -25.174  17.534  49.568  1.00109.49           C  
ANISOU 4429  C   GLY A 529    12810  17803  10987    530    694   1476       C  
ATOM   4430  O   GLY A 529     -25.730  18.140  48.648  1.00110.21           O  
ANISOU 4430  O   GLY A 529    12907  18016  10950    636    726   1589       O  
ATOM   4431  N   ILE A 530     -23.982  17.903  50.076  1.00105.29           N  
ANISOU 4431  N   ILE A 530    12388  17109  10511    386    707   1471       N  
ATOM   4432  CA  ILE A 530     -23.207  19.038  49.577  1.00106.04           C  
ANISOU 4432  CA  ILE A 530    12630  17141  10520    300    761   1594       C  
ATOM   4433  C   ILE A 530     -22.388  18.570  48.365  1.00110.46           C  
ANISOU 4433  C   ILE A 530    13008  17940  11023    210    756   1554       C  
ATOM   4434  O   ILE A 530     -22.381  19.257  47.343  1.00111.42           O  
ANISOU 4434  O   ILE A 530    13164  18150  11021    224    800   1668       O  
ATOM   4435  CB  ILE A 530     -22.325  19.684  50.689  1.00108.99           C  
ANISOU 4435  CB  ILE A 530    13199  17264  10948    141    772   1611       C  
ATOM   4436  CG1 ILE A 530     -23.199  20.249  51.836  1.00109.24           C  
ANISOU 4436  CG1 ILE A 530    13446  17051  11007    260    789   1655       C  
ATOM   4437  CG2 ILE A 530     -21.416  20.788  50.117  1.00110.96           C  
ANISOU 4437  CG2 ILE A 530    13601  17465  11093    -21    824   1732       C  
ATOM   4438  CD1 ILE A 530     -22.502  20.346  53.195  1.00114.57           C  
ANISOU 4438  CD1 ILE A 530    14244  17520  11766    112    768   1597       C  
ATOM   4439  N   ALA A 531     -21.717  17.402  48.474  1.00106.27           N  
ANISOU 4439  N   ALA A 531    12297  17515  10567    140    711   1398       N  
ATOM   4440  CA  ALA A 531     -20.885  16.847  47.399  1.00106.66           C  
ANISOU 4440  CA  ALA A 531    12171  17802  10552     87    714   1340       C  
ATOM   4441  C   ALA A 531     -21.695  16.523  46.143  1.00111.00           C  
ANISOU 4441  C   ALA A 531    12615  18562  10997    201    715   1333       C  
ATOM   4442  O   ALA A 531     -21.209  16.778  45.047  1.00111.89           O  
ANISOU 4442  O   ALA A 531    12668  18849  10996    172    747   1380       O  
ATOM   4443  CB  ALA A 531     -20.152  15.606  47.877  1.00106.58           C  
ANISOU 4443  CB  ALA A 531    12025  17838  10632     57    674   1174       C  
ATOM   4444  N   MET A 532     -22.926  16.003  46.293  1.00106.86           N  
ANISOU 4444  N   MET A 532    12061  18049  10492    314    679   1284       N  
ATOM   4445  CA  MET A 532     -23.789  15.671  45.158  1.00107.67           C  
ANISOU 4445  CA  MET A 532    12050  18386  10475    399    666   1273       C  
ATOM   4446  C   MET A 532     -24.362  16.942  44.520  1.00115.17           C  
ANISOU 4446  C   MET A 532    13084  19382  11293    491    713   1476       C  
ATOM   4447  O   MET A 532     -24.728  16.916  43.343  1.00116.49           O  
ANISOU 4447  O   MET A 532    13153  19785  11322    544    715   1504       O  
ATOM   4448  CB  MET A 532     -24.917  14.701  45.564  1.00109.13           C  
ANISOU 4448  CB  MET A 532    12162  18602  10700    445    607   1163       C  
ATOM   4449  CG  MET A 532     -24.430  13.366  46.130  1.00111.53           C  
ANISOU 4449  CG  MET A 532    12423  18835  11116    369    566    967       C  
ATOM   4450  SD  MET A 532     -23.226  12.464  45.125  1.00116.15           S  
ANISOU 4450  SD  MET A 532    12916  19570  11647    323    573    820       S  
ATOM   4451  CE  MET A 532     -21.749  12.703  46.089  1.00112.14           C  
ANISOU 4451  CE  MET A 532    12460  18894  11255    270    600    835       C  
ATOM   4452  N   SER A 533     -24.384  18.061  45.277  1.00112.76           N  
ANISOU 4452  N   SER A 533    12983  18846  11015    515    755   1617       N  
ATOM   4453  CA  SER A 533     -24.868  19.355  44.800  1.00114.70           C  
ANISOU 4453  CA  SER A 533    13383  19065  11131    630    816   1826       C  
ATOM   4454  C   SER A 533     -23.824  20.068  43.903  1.00121.76           C  
ANISOU 4454  C   SER A 533    14341  19992  11930    517    870   1926       C  
ATOM   4455  O   SER A 533     -24.167  21.053  43.245  1.00122.83           O  
ANISOU 4455  O   SER A 533    14602  20137  11930    610    924   2104       O  
ATOM   4456  CB  SER A 533     -25.263  20.245  45.976  1.00117.81           C  
ANISOU 4456  CB  SER A 533    14025  19163  11575    705    850   1925       C  
ATOM   4457  OG  SER A 533     -24.182  21.037  46.442  1.00126.14           O  
ANISOU 4457  OG  SER A 533    15294  19973  12661    545    891   1978       O  
ATOM   4458  N   THR A 534     -22.567  19.571  43.871  1.00119.37           N  
ANISOU 4458  N   THR A 534    13950  19727  11680    327    860   1823       N  
ATOM   4459  CA  THR A 534     -21.487  20.167  43.071  1.00121.27           C  
ANISOU 4459  CA  THR A 534    14212  20045  11822    184    911   1914       C  
ATOM   4460  C   THR A 534     -21.483  19.635  41.615  1.00127.69           C  
ANISOU 4460  C   THR A 534    14816  21196  12503    231    911   1884       C  
ATOM   4461  O   THR A 534     -20.581  19.972  40.841  1.00128.34           O  
ANISOU 4461  O   THR A 534    14869  21407  12488    118    954   1948       O  
ATOM   4462  CB  THR A 534     -20.115  19.975  43.741  1.00129.38           C  
ANISOU 4462  CB  THR A 534    15216  21009  12933    -35    906   1842       C  
ATOM   4463  OG1 THR A 534     -19.748  18.598  43.707  1.00129.00           O  
ANISOU 4463  OG1 THR A 534    14927  21140  12950    -23    857   1646       O  
ATOM   4464  CG2 THR A 534     -20.059  20.525  45.166  1.00127.20           C  
ANISOU 4464  CG2 THR A 534    15153  20414  12765   -109    902   1865       C  
ATOM   4465  N   TRP A 535     -22.502  18.837  41.241  1.00125.51           N  
ANISOU 4465  N   TRP A 535    14401  21081  12206    379    863   1792       N  
ATOM   4466  CA  TRP A 535     -22.681  18.289  39.893  1.00127.05           C  
ANISOU 4466  CA  TRP A 535    14416  21599  12258    429    853   1744       C  
ATOM   4467  C   TRP A 535     -23.075  19.410  38.921  1.00134.66           C  
ANISOU 4467  C   TRP A 535    15462  22661  13043    513    907   1966       C  
ATOM   4468  O   TRP A 535     -22.798  19.330  37.724  1.00135.28           O  
ANISOU 4468  O   TRP A 535    15433  22993  12976    506    925   1983       O  
ATOM   4469  CB  TRP A 535     -23.753  17.188  39.928  1.00125.12           C  
ANISOU 4469  CB  TRP A 535    14037  21473  12032    520    778   1587       C  
ATOM   4470  CG  TRP A 535     -24.023  16.523  38.609  1.00127.23           C  
ANISOU 4470  CG  TRP A 535    14134  22069  12141    548    755   1506       C  
ATOM   4471  CD1 TRP A 535     -25.037  16.808  37.744  1.00131.48           C  
ANISOU 4471  CD1 TRP A 535    14612  22832  12513    657    743   1597       C  
ATOM   4472  CD2 TRP A 535     -23.265  15.459  38.004  1.00127.25           C  
ANISOU 4472  CD2 TRP A 535    14013  22224  12113    479    743   1316       C  
ATOM   4473  NE1 TRP A 535     -24.961  15.990  36.638  1.00131.91           N  
ANISOU 4473  NE1 TRP A 535    14515  23170  12437    629    717   1466       N  
ATOM   4474  CE2 TRP A 535     -23.882  15.151  36.772  1.00132.59           C  
ANISOU 4474  CE2 TRP A 535    14576  23200  12603    528    722   1287       C  
ATOM   4475  CE3 TRP A 535     -22.129  14.724  38.390  1.00127.87           C  
ANISOU 4475  CE3 TRP A 535    14069  22230  12287    403    752   1169       C  
ATOM   4476  CZ2 TRP A 535     -23.397  14.145  35.919  1.00132.49           C  
ANISOU 4476  CZ2 TRP A 535    14460  23382  12497    494    712   1102       C  
ATOM   4477  CZ3 TRP A 535     -21.650  13.730  37.546  1.00130.02           C  
ANISOU 4477  CZ3 TRP A 535    14234  22701  12467    405    750    998       C  
ATOM   4478  CH2 TRP A 535     -22.280  13.448  36.328  1.00131.92           C  
ANISOU 4478  CH2 TRP A 535    14394  23205  12524    445    732    958       C  
ATOM   4479  N   VAL A 536     -23.705  20.454  39.463  1.00133.21           N  
ANISOU 4479  N   VAL A 536    15488  22265  12858    609    939   2139       N  
ATOM   4480  CA  VAL A 536     -24.186  21.642  38.763  1.00135.52           C  
ANISOU 4480  CA  VAL A 536    15934  22574  12985    738   1000   2380       C  
ATOM   4481  C   VAL A 536     -23.206  22.829  38.991  1.00142.38           C  
ANISOU 4481  C   VAL A 536    17078  23176  13844    590   1082   2541       C  
ATOM   4482  O   VAL A 536     -23.563  23.980  38.746  1.00143.34           O  
ANISOU 4482  O   VAL A 536    17440  23173  13852    692   1148   2759       O  
ATOM   4483  CB  VAL A 536     -25.634  21.979  39.206  1.00139.49           C  
ANISOU 4483  CB  VAL A 536    16505  23032  13461    990    990   2468       C  
ATOM   4484  CG1 VAL A 536     -26.598  20.868  38.814  1.00138.66           C  
ANISOU 4484  CG1 VAL A 536    16112  23254  13318   1081    908   2331       C  
ATOM   4485  CG2 VAL A 536     -25.688  22.295  40.686  1.00138.31           C  
ANISOU 4485  CG2 VAL A 536    16554  22527  13470    986    999   2458       C  
ATOM   4486  N   TRP A 537     -21.969  22.549  39.445  1.00140.46           N  
ANISOU 4486  N   TRP A 537    16810  22857  13703    344   1080   2442       N  
ATOM   4487  CA  TRP A 537     -20.965  23.601  39.646  1.00142.92           C  
ANISOU 4487  CA  TRP A 537    17355  22961  13985    130   1147   2581       C  
ATOM   4488  C   TRP A 537     -20.055  23.632  38.403  1.00151.59           C  
ANISOU 4488  C   TRP A 537    18319  24337  14940    -10   1186   2635       C  
ATOM   4489  O   TRP A 537     -18.835  23.463  38.492  1.00151.37           O  
ANISOU 4489  O   TRP A 537    18205  24375  14932   -249   1194   2586       O  
ATOM   4490  CB  TRP A 537     -20.184  23.386  40.960  1.00140.41           C  
ANISOU 4490  CB  TRP A 537    17081  22434  13836    -67   1119   2465       C  
ATOM   4491  CG  TRP A 537     -20.964  23.639  42.226  1.00140.44           C  
ANISOU 4491  CG  TRP A 537    17285  22124  13953     42   1102   2452       C  
ATOM   4492  CD1 TRP A 537     -22.321  23.628  42.377  1.00142.99           C  
ANISOU 4492  CD1 TRP A 537    17646  22410  14274    321   1090   2475       C  
ATOM   4493  CD2 TRP A 537     -20.418  23.850  43.536  1.00139.71           C  
ANISOU 4493  CD2 TRP A 537    17345  21759  13979   -123   1091   2402       C  
ATOM   4494  NE1 TRP A 537     -22.654  23.849  43.693  1.00141.67           N  
ANISOU 4494  NE1 TRP A 537    17659  21953  14218    353   1082   2447       N  
ATOM   4495  CE2 TRP A 537     -21.506  23.991  44.427  1.00142.89           C  
ANISOU 4495  CE2 TRP A 537    17899  21944  14449     80   1080   2397       C  
ATOM   4496  CE3 TRP A 537     -19.111  23.949  44.044  1.00141.22           C  
ANISOU 4496  CE3 TRP A 537    17547  21902  14207   -429   1088   2367       C  
ATOM   4497  CZ2 TRP A 537     -21.329  24.231  45.795  1.00141.62           C  
ANISOU 4497  CZ2 TRP A 537    17922  21494  14394     -7   1070   2351       C  
ATOM   4498  CZ3 TRP A 537     -18.936  24.182  45.400  1.00142.15           C  
ANISOU 4498  CZ3 TRP A 537    17838  21746  14426   -531   1068   2321       C  
ATOM   4499  CH2 TRP A 537     -20.035  24.322  46.259  1.00141.96           C  
ANISOU 4499  CH2 TRP A 537    17985  21481  14471   -320   1061   2309       C  
ATOM   4500  N   THR A 538     -20.688  23.834  37.231  1.00151.94           N  
ANISOU 4500  N   THR A 538    18325  24584  14822    154   1209   2743       N  
ATOM   4501  CA  THR A 538     -20.055  23.843  35.911  1.00154.49           C  
ANISOU 4501  CA  THR A 538    18509  25212  14977     76   1248   2804       C  
ATOM   4502  C   THR A 538     -20.262  25.188  35.191  1.00163.98           C  
ANISOU 4502  C   THR A 538    19976  26333  15995    108   1334   3092       C  
ATOM   4503  O   THR A 538     -20.912  26.085  35.731  1.00164.45           O  
ANISOU 4503  O   THR A 538    20342  26084  16057    215   1365   3235       O  
ATOM   4504  CB  THR A 538     -20.605  22.672  35.068  1.00161.15           C  
ANISOU 4504  CB  THR A 538    19041  26420  15768    242   1190   2644       C  
ATOM   4505  OG1 THR A 538     -22.035  22.722  35.044  1.00159.29           O  
ANISOU 4505  OG1 THR A 538    18838  26182  15502    496   1156   2682       O  
ATOM   4506  CG2 THR A 538     -20.131  21.313  35.570  1.00157.73           C  
ANISOU 4506  CG2 THR A 538    18376  26075  15478    181   1125   2367       C  
ATOM   4507  N   LYS A 539     -19.692  25.319  33.974  1.00164.05           N  
ANISOU 4507  N   LYS A 539    19882  26617  15831     29   1379   3181       N  
ATOM   4508  CA  LYS A 539     -19.770  26.507  33.113  1.00167.46           C  
ANISOU 4508  CA  LYS A 539    20546  27020  16061     43   1467   3463       C  
ATOM   4509  C   LYS A 539     -21.200  26.740  32.613  1.00174.13           C  
ANISOU 4509  C   LYS A 539    21445  27920  16799    402   1460   3571       C  
ATOM   4510  O   LYS A 539     -21.664  27.880  32.596  1.00175.34           O  
ANISOU 4510  O   LYS A 539    21931  27836  16855    515   1526   3809       O  
ATOM   4511  CB  LYS A 539     -18.825  26.363  31.900  1.00171.53           C  
ANISOU 4511  CB  LYS A 539    20864  27896  16413   -120   1509   3501       C  
ATOM   4512  CG  LYS A 539     -17.351  26.147  32.238  1.00187.58           C  
ANISOU 4512  CG  LYS A 539    22788  29982  18502   -465   1525   3423       C  
ATOM   4513  CD  LYS A 539     -16.641  25.283  31.181  1.00198.11           C  
ANISOU 4513  CD  LYS A 539    23753  31798  19722   -502   1528   3319       C  
ATOM   4514  CE  LYS A 539     -15.934  26.086  30.115  1.00212.43           C  
ANISOU 4514  CE  LYS A 539    25611  33792  21310   -674   1623   3546       C  
ATOM   4515  NZ  LYS A 539     -14.617  26.584  30.589  1.00223.76           N  
ANISOU 4515  NZ  LYS A 539    27099  35169  22749  -1055   1672   3618       N  
ATOM   4516  N   ALA A 540     -21.878  25.651  32.197  1.00171.68           N  
ANISOU 4516  N   ALA A 540    20813  27934  16485    578   1380   3399       N  
ATOM   4517  CA  ALA A 540     -23.230  25.625  31.633  1.00173.40           C  
ANISOU 4517  CA  ALA A 540    20966  28341  16576    897   1350   3466       C  
ATOM   4518  C   ALA A 540     -24.312  26.118  32.600  1.00179.60           C  
ANISOU 4518  C   ALA A 540    21959  28850  17432   1126   1344   3541       C  
ATOM   4519  O   ALA A 540     -25.329  26.639  32.144  1.00180.62           O  
ANISOU 4519  O   ALA A 540    22150  29070  17405   1408   1361   3715       O  
ATOM   4520  CB  ALA A 540     -23.569  24.216  31.178  1.00172.83           C  
ANISOU 4520  CB  ALA A 540    20511  28652  16506    939   1254   3213       C  
ATOM   4521  N   THR A 541     -24.113  25.932  33.911  1.00176.65           N  
ANISOU 4521  N   THR A 541    21673  28174  17273   1028   1321   3414       N  
ATOM   4522  CA  THR A 541     -25.085  26.335  34.930  1.00177.29           C  
ANISOU 4522  CA  THR A 541    21942  27996  17425   1242   1320   3463       C  
ATOM   4523  C   THR A 541     -25.006  27.840  35.215  1.00185.56           C  
ANISOU 4523  C   THR A 541    23460  28646  18400   1296   1429   3726       C  
ATOM   4524  O   THR A 541     -26.007  28.428  35.634  1.00185.96           O  
ANISOU 4524  O   THR A 541    23703  28549  18405   1590   1458   3851       O  
ATOM   4525  CB  THR A 541     -24.902  25.510  36.193  1.00183.91           C  
ANISOU 4525  CB  THR A 541    22691  28683  18504   1117   1254   3222       C  
ATOM   4526  OG1 THR A 541     -23.532  25.585  36.594  1.00183.36           O  
ANISOU 4526  OG1 THR A 541    22707  28425  18538    793   1277   3162       O  
ATOM   4527  CG2 THR A 541     -25.323  24.054  35.995  1.00180.99           C  
ANISOU 4527  CG2 THR A 541    21927  28657  18186   1134   1150   2981       C  
ATOM   4528  N   LEU A 542     -23.830  28.462  34.968  1.00185.02           N  
ANISOU 4528  N   LEU A 542    23585  28417  18299   1013   1495   3815       N  
ATOM   4529  CA  LEU A 542     -23.628  29.906  35.123  1.00188.28           C  
ANISOU 4529  CA  LEU A 542    24496  28427  18614    996   1606   4066       C  
ATOM   4530  C   LEU A 542     -24.459  30.638  34.070  1.00197.48           C  
ANISOU 4530  C   LEU A 542    25786  29712  19537   1319   1669   4329       C  
ATOM   4531  O   LEU A 542     -25.014  31.701  34.353  1.00199.21           O  
ANISOU 4531  O   LEU A 542    26415  29611  19665   1540   1750   4534       O  
ATOM   4532  CB  LEU A 542     -22.139  30.281  35.000  1.00189.13           C  
ANISOU 4532  CB  LEU A 542    24723  28417  18720    555   1651   4093       C  
ATOM   4533  CG  LEU A 542     -21.204  29.789  36.108  1.00191.83           C  
ANISOU 4533  CG  LEU A 542    25002  28617  19269    224   1603   3881       C  
ATOM   4534  CD1 LEU A 542     -19.761  29.837  35.659  1.00192.95           C  
ANISOU 4534  CD1 LEU A 542    25068  28878  19366   -191   1628   3891       C  
ATOM   4535  CD2 LEU A 542     -21.379  30.594  37.390  1.00194.68           C  
ANISOU 4535  CD2 LEU A 542    25795  28469  19707    212   1637   3920       C  
ATOM   4536  N   LEU A 543     -24.579  30.022  32.871  1.00196.11           N  
ANISOU 4536  N   LEU A 543    25258  30011  19245   1373   1631   4314       N  
ATOM   4537  CA  LEU A 543     -25.352  30.483  31.716  1.00199.33           C  
ANISOU 4537  CA  LEU A 543    25669  30665  19403   1676   1668   4539       C  
ATOM   4538  C   LEU A 543     -26.841  30.567  32.060  1.00205.98           C  
ANISOU 4538  C   LEU A 543    26511  31556  20197   2124   1648   4601       C  
ATOM   4539  O   LEU A 543     -27.475  31.559  31.709  1.00208.79           O  
ANISOU 4539  O   LEU A 543    27145  31823  20364   2430   1729   4873       O  
ATOM   4540  CB  LEU A 543     -25.127  29.519  30.530  1.00198.79           C  
ANISOU 4540  CB  LEU A 543    25149  31135  19249   1594   1604   4425       C  
ATOM   4541  CG  LEU A 543     -25.739  29.884  29.174  1.00205.90           C  
ANISOU 4541  CG  LEU A 543    25992  32375  19867   1845   1632   4642       C  
ATOM   4542  CD1 LEU A 543     -24.750  29.634  28.061  1.00206.68           C  
ANISOU 4542  CD1 LEU A 543    25921  32749  19858   1590   1648   4634       C  
ATOM   4543  CD2 LEU A 543     -27.021  29.099  28.913  1.00207.35           C  
ANISOU 4543  CD2 LEU A 543    25826  32972  19986   2147   1535   4551       C  
ATOM   4544  N   ILE A 544     -27.389  29.530  32.740  1.00201.61           N  
ANISOU 4544  N   ILE A 544    25649  31156  19797   2167   1546   4361       N  
ATOM   4545  CA  ILE A 544     -28.803  29.435  33.126  1.00202.28           C  
ANISOU 4545  CA  ILE A 544    25645  31373  19839   2553   1513   4391       C  
ATOM   4546  C   ILE A 544     -29.184  30.582  34.079  1.00209.21           C  
ANISOU 4546  C   ILE A 544    26998  31774  20718   2783   1611   4568       C  
ATOM   4547  O   ILE A 544     -30.267  31.151  33.928  1.00211.63           O  
ANISOU 4547  O   ILE A 544    27393  32164  20852   3206   1653   4767       O  
ATOM   4548  CB  ILE A 544     -29.184  28.049  33.737  1.00202.24           C  
ANISOU 4548  CB  ILE A 544    25234  31599  20008   2470   1386   4086       C  
ATOM   4549  CG1 ILE A 544     -28.442  26.847  33.067  1.00200.60           C  
ANISOU 4549  CG1 ILE A 544    24661  31704  19855   2151   1301   3846       C  
ATOM   4550  CG2 ILE A 544     -30.704  27.836  33.743  1.00203.90           C  
ANISOU 4550  CG2 ILE A 544    25235  32138  20098   2841   1341   4138       C  
ATOM   4551  CD1 ILE A 544     -28.732  26.525  31.535  1.00209.53           C  
ANISOU 4551  CD1 ILE A 544    25516  33348  20749   2222   1269   3895       C  
ATOM   4552  N   TRP A 545     -28.302  30.932  35.037  1.00205.63           N  
ANISOU 4552  N   TRP A 545    26854  30841  20435   2519   1650   4501       N  
ATOM   4553  CA  TRP A 545     -28.601  32.016  35.973  1.00208.48           C  
ANISOU 4553  CA  TRP A 545    27717  30710  20788   2710   1747   4644       C  
ATOM   4554  C   TRP A 545     -28.415  33.399  35.337  1.00220.45           C  
ANISOU 4554  C   TRP A 545    29725  31947  22089   2822   1882   4958       C  
ATOM   4555  O   TRP A 545     -29.200  34.294  35.650  1.00221.64           O  
ANISOU 4555  O   TRP A 545    30235  31863  22116   3208   1969   5151       O  
ATOM   4556  CB  TRP A 545     -27.800  31.901  37.275  1.00205.17           C  
ANISOU 4556  CB  TRP A 545    27465  29886  20604   2385   1734   4454       C  
ATOM   4557  CG  TRP A 545     -28.214  30.731  38.121  1.00202.77           C  
ANISOU 4557  CG  TRP A 545    26788  29763  20493   2377   1625   4192       C  
ATOM   4558  CD1 TRP A 545     -27.453  29.648  38.442  1.00202.74           C  
ANISOU 4558  CD1 TRP A 545    26479  29868  20687   2023   1531   3929       C  
ATOM   4559  CD2 TRP A 545     -29.503  30.506  38.718  1.00202.18           C  
ANISOU 4559  CD2 TRP A 545    26602  29806  20410   2747   1603   4183       C  
ATOM   4560  NE1 TRP A 545     -28.175  28.774  39.218  1.00200.00           N  
ANISOU 4560  NE1 TRP A 545    25873  29654  20463   2131   1453   3756       N  
ATOM   4561  CE2 TRP A 545     -29.441  29.266  39.389  1.00202.72           C  
ANISOU 4561  CE2 TRP A 545    26310  30030  20685   2556   1492   3906       C  
ATOM   4562  CE3 TRP A 545     -30.708  31.232  38.749  1.00205.62           C  
ANISOU 4562  CE3 TRP A 545    27203  30253  20668   3237   1672   4392       C  
ATOM   4563  CZ2 TRP A 545     -30.533  28.736  40.086  1.00200.85           C  
ANISOU 4563  CZ2 TRP A 545    25873  29956  20485   2792   1446   3832       C  
ATOM   4564  CZ3 TRP A 545     -31.790  30.702  39.434  1.00205.94           C  
ANISOU 4564  CZ3 TRP A 545    27010  30498  20739   3494   1626   4319       C  
ATOM   4565  CH2 TRP A 545     -31.696  29.472  40.096  1.00203.24           C  
ANISOU 4565  CH2 TRP A 545    26309  30304  20607   3250   1513   4042       C  
ATOM   4566  N   ARG A 546     -27.418  33.571  34.437  1.00221.19           N  
ANISOU 4566  N   ARG A 546    29844  32079  22120   2511   1905   5019       N  
ATOM   4567  CA  ARG A 546     -27.182  34.847  33.745  1.00226.56           C  
ANISOU 4567  CA  ARG A 546    30996  32503  22582   2570   2034   5328       C  
ATOM   4568  C   ARG A 546     -28.278  35.138  32.700  1.00234.88           C  
ANISOU 4568  C   ARG A 546    32019  33736  23488   2845   1966   5409       C  
ATOM   4569  O   ARG A 546     -28.659  36.301  32.557  1.00236.10           O  
ANISOU 4569  O   ARG A 546    32669  33426  23612   2811   1928   5481       O  
ATOM   4570  CB  ARG A 546     -25.791  34.883  33.077  1.00229.51           C  
ANISOU 4570  CB  ARG A 546    31368  32883  22951   2069   2048   5327       C  
ATOM   4571  CG  ARG A 546     -24.631  34.983  34.065  1.00245.11           C  
ANISOU 4571  CG  ARG A 546    33553  34468  25111   1586   2051   5180       C  
ATOM   4572  CD  ARG A 546     -23.316  35.246  33.389  1.00248.44           C  
ANISOU 4572  CD  ARG A 546    34054  34838  25503   1054   2056   5181       C  
ATOM   4573  NE  ARG A 546     -22.222  35.244  34.357  1.00254.09           N  
ANISOU 4573  NE  ARG A 546    34933  35194  26416    507   2003   4950       N  
ATOM   4574  CZ  ARG A 546     -21.123  35.978  34.238  1.00270.26           C  
ANISOU 4574  CZ  ARG A 546    37710  36155  28821   -725   1619   4109       C  
ATOM   4575  NH1 ARG A 546     -20.963  36.781  33.194  1.00262.88           N  
ANISOU 4575  NH1 ARG A 546    36838  35604  27440   -439   1891   4793       N  
ATOM   4576  NH2 ARG A 546     -20.176  35.920  35.165  1.00262.74           N  
ANISOU 4576  NH2 ARG A 546    36527  35671  27632   -468   1982   4721       N  
ATOM   4577  N   ARG A 547     -28.770  34.099  31.973  1.00232.74           N  
ANISOU 4577  N   ARG A 547    31182  34069  23179   2968   1879   5318       N  
ATOM   4578  CA  ARG A 547     -29.818  34.252  30.950  1.00233.17           C  
ANISOU 4578  CA  ARG A 547    31218  34169  23208   3004   1719   5222       C  
ATOM   4579  C   ARG A 547     -31.184  34.581  31.589  1.00236.86           C  
ANISOU 4579  C   ARG A 547    31881  34198  23918   2966   1506   4955       C  
ATOM   4580  O   ARG A 547     -31.974  35.307  30.984  1.00237.34           O  
ANISOU 4580  O   ARG A 547    32135  34097  23945   2994   1402   4984       O  
ATOM   4581  CB  ARG A 547     -29.921  33.020  30.016  1.00232.25           C  
ANISOU 4581  CB  ARG A 547    30536  34628  23081   2929   1620   5047       C  
ATOM   4582  CG  ARG A 547     -30.537  31.755  30.620  1.00237.55           C  
ANISOU 4582  CG  ARG A 547    30942  35169  24147   2624   1384   4497       C  
ATOM   4583  CD  ARG A 547     -30.860  30.707  29.568  1.00245.30           C  
ANISOU 4583  CD  ARG A 547    31853  35844  25506   2051   1107   3875       C  
ATOM   4584  NE  ARG A 547     -31.996  31.094  28.725  1.00255.35           N  
ANISOU 4584  NE  ARG A 547    33590  36227  27202   1525    792   3360       N  
ATOM   4585  CZ  ARG A 547     -33.272  30.866  29.026  1.00264.86           C  
ANISOU 4585  CZ  ARG A 547    35044  36631  28960   1053    494   2799       C  
ATOM   4586  NH1 ARG A 547     -34.233  31.254  28.198  1.00256.44           N  
ANISOU 4586  NH1 ARG A 547    33711  36262  27462   1607    566   3227       N  
ATOM   4587  NH2 ARG A 547     -33.597  30.254  30.158  1.00254.06           N  
ANISOU 4587  NH2 ARG A 547    33091  36215  27225   1774    706   3231       N  
ATOM   4588  N   THR A 548     -31.449  34.062  32.804  1.00235.20           N  
ANISOU 4588  N   THR A 548    31505  34086  23776   3191   1560   4925       N  
ATOM   4589  CA  THR A 548     -32.693  34.329  33.528  1.00235.44           C  
ANISOU 4589  CA  THR A 548    31610  33934  23914   3366   1461   4837       C  
ATOM   4590  C   THR A 548     -32.627  35.724  34.162  1.00241.63           C  
ANISOU 4590  C   THR A 548    33011  33871  24925   2951   1318   4720       C  
ATOM   4591  O   THR A 548     -33.660  36.384  34.261  1.00241.63           O  
ANISOU 4591  O   THR A 548    33135  33709  24966   3056   1209   4727       O  
ATOM   4592  CB  THR A 548     -32.995  33.235  34.552  1.00238.64           C  
ANISOU 4592  CB  THR A 548    31718  34346  24609   3183   1342   4484       C  
ATOM   4593  OG1 THR A 548     -31.812  32.933  35.292  1.00238.62           O  
ANISOU 4593  OG1 THR A 548    31728  34322  24615   3115   1479   4528       O  
ATOM   4594  CG2 THR A 548     -33.554  31.972  33.908  1.00235.89           C  
ANISOU 4594  CG2 THR A 548    30792  34637  24197   3307   1292   4403       C  
ATOM   4595  N   TRP A 549     -31.414  36.178  34.561  1.00242.07           N  
ANISOU 4595  N   TRP A 549    33369  33677  24931   2812   1456   4850       N  
ATOM   4596  CA  TRP A 549     -31.171  37.512  35.126  1.00244.40           C  
ANISOU 4596  CA  TRP A 549    34180  33395  25285   2593   1412   4922       C  
ATOM   4597  C   TRP A 549     -31.341  38.578  34.032  1.00249.28           C  
ANISOU 4597  C   TRP A 549    35000  33736  25978   2104   1141   4876       C  
ATOM   4598  O   TRP A 549     -31.905  39.640  34.302  1.00249.81           O  
ANISOU 4598  O   TRP A 549    35295  33517  26104   2083   1025   4957       O  
ATOM   4599  CB  TRP A 549     -29.769  37.595  35.762  1.00244.78           C  
ANISOU 4599  CB  TRP A 549    34460  33245  25302   2417   1588   5008       C  
ATOM   4600  CG  TRP A 549     -29.409  38.953  36.294  1.00247.45           C  
ANISOU 4600  CG  TRP A 549    35274  33027  25720   2079   1504   5071       C  
ATOM   4601  CD1 TRP A 549     -29.679  39.445  37.537  1.00249.49           C  
ANISOU 4601  CD1 TRP A 549    35660  32947  26186   1954   1390   4959       C  
ATOM   4602  CD2 TRP A 549     -28.710  39.993  35.593  1.00249.41           C  
ANISOU 4602  CD2 TRP A 549    35807  33053  25905   1697   1448   5231       C  
ATOM   4603  NE1 TRP A 549     -29.199  40.729  37.653  1.00251.13           N  
ANISOU 4603  NE1 TRP A 549    36192  32788  26436   1633   1312   5100       N  
ATOM   4604  CE2 TRP A 549     -28.603  41.092  36.473  1.00253.39           C  
ANISOU 4604  CE2 TRP A 549    36481  33147  26651   1281   1234   5196       C  
ATOM   4605  CE3 TRP A 549     -28.175  40.107  34.297  1.00251.12           C  
ANISOU 4605  CE3 TRP A 549    35995  33404  26013   1414   1404   5292       C  
ATOM   4606  CZ2 TRP A 549     -27.973  42.288  36.103  1.00254.92           C  
ANISOU 4606  CZ2 TRP A 549    36888  33132  26839    926   1158   5410       C  
ATOM   4607  CZ3 TRP A 549     -27.553  41.292  33.933  1.00254.14           C  
ANISOU 4607  CZ3 TRP A 549    36621  33533  26408    937   1275   5438       C  
ATOM   4608  CH2 TRP A 549     -27.456  42.365  34.829  1.00255.61           C  
ANISOU 4608  CH2 TRP A 549    36980  33379  26762    730   1164   5528       C  
ATOM   4609  N   CYS A 550     -30.851  38.286  32.802  1.00247.82           N  
ANISOU 4609  N   CYS A 550    34737  33822  25600   2116   1230   4981       N  
ATOM   4610  CA  CYS A 550     -30.954  39.155  31.623  1.00249.13           C  
ANISOU 4610  CA  CYS A 550    35094  33885  25679   1916   1109   5084       C  
ATOM   4611  C   CYS A 550     -32.420  39.270  31.173  1.00250.85           C  
ANISOU 4611  C   CYS A 550    35166  34108  26038   1924    854   4912       C  
ATOM   4612  O   CYS A 550     -32.819  40.312  30.648  1.00251.55           O  
ANISOU 4612  O   CYS A 550    35464  34016  26099   1835    725   5040       O  
ATOM   4613  CB  CYS A 550     -30.066  38.646  30.490  1.00249.57           C  
ANISOU 4613  CB  CYS A 550    35048  34174  25603   1735   1183   5081       C  
ATOM   4614  SG  CYS A 550     -28.312  39.071  30.667  1.00254.01           S  
ANISOU 4614  SG  CYS A 550    35886  34442  26182   1122   1215   5087       S  
ATOM   4615  N   ARG A 551     -33.211  38.193  31.385  1.00246.70           N  
ANISOU 4615  N   ARG A 551    34268  33997  25470   2404    958   4865       N  
ATOM   4616  CA  ARG A 551     -34.639  38.112  31.068  1.00245.80           C  
ANISOU 4616  CA  ARG A 551    33965  34027  25400   2607    824   4792       C  
ATOM   4617  C   ARG A 551     -35.441  38.991  32.041  1.00248.74           C  
ANISOU 4617  C   ARG A 551    34511  33986  26012   2480    638   4707       C  
ATOM   4618  O   ARG A 551     -36.415  39.622  31.629  1.00249.03           O  
ANISOU 4618  O   ARG A 551    34583  33956  26083   2512    489   4733       O  
ATOM   4619  CB  ARG A 551     -35.117  36.648  31.122  1.00244.62           C  
ANISOU 4619  CB  ARG A 551    33335  34300  25310   2759    842   4586       C  
ATOM   4620  CG  ARG A 551     -36.477  36.403  30.468  1.00250.77           C  
ANISOU 4620  CG  ARG A 551    33977  34884  26418   2354    499   4174       C  
ATOM   4621  CD  ARG A 551     -36.749  34.929  30.217  1.00256.92           C  
ANISOU 4621  CD  ARG A 551    34478  35576  27563   1892    329   3642       C  
ATOM   4622  NE  ARG A 551     -37.002  34.184  31.453  1.00263.60           N  
ANISOU 4622  NE  ARG A 551    35271  36014  28873   1471    180   3191       N  
ATOM   4623  CZ  ARG A 551     -37.334  32.897  31.502  1.00272.08           C  
ANISOU 4623  CZ  ARG A 551    36277  36642  30460    894    -11   2593       C  
ATOM   4624  NH1 ARG A 551     -37.465  32.194  30.383  1.00262.62           N  
ANISOU 4624  NH1 ARG A 551    34686  36297  28800   1520    201   2939       N  
ATOM   4625  NH2 ARG A 551     -37.543  32.304  32.669  1.00261.83           N  
ANISOU 4625  NH2 ARG A 551    34554  36123  28806   1679    265   2979       N  
ATOM   4626  N   LEU A 552     -35.018  39.037  33.323  1.00245.93           N  
ANISOU 4626  N   LEU A 552    34265  33562  25615   2738    825   4831       N  
ATOM   4627  CA  LEU A 552     -35.654  39.848  34.363  1.00245.78           C  
ANISOU 4627  CA  LEU A 552    34416  33257  25713   2846    767   4867       C  
ATOM   4628  C   LEU A 552     -35.297  41.328  34.190  1.00249.60           C  
ANISOU 4628  C   LEU A 552    35240  33290  26305   2417    582   4959       C  
ATOM   4629  O   LEU A 552     -36.179  42.181  34.296  1.00249.41           O  
ANISOU 4629  O   LEU A 552    35289  33119  26355   2501    456   5024       O  
ATOM   4630  CB  LEU A 552     -35.257  39.365  35.773  1.00245.07           C  
ANISOU 4630  CB  LEU A 552    34317  33105  25694   2952    899   4798       C  
ATOM   4631  CG  LEU A 552     -35.775  37.992  36.217  1.00246.38           C  
ANISOU 4631  CG  LEU A 552    34047  33550  26018   2950    855   4503       C  
ATOM   4632  CD1 LEU A 552     -34.945  37.447  37.359  1.00246.05           C  
ANISOU 4632  CD1 LEU A 552    34019  33463  26005   2971   1003   4461       C  
ATOM   4633  CD2 LEU A 552     -37.248  38.041  36.602  1.00247.57           C  
ANISOU 4633  CD2 LEU A 552    34021  33689  26356   2998    679   4342       C  
ATOM   4634  N   THR A 553     -34.008  41.628  33.920  1.00248.65           N  
ANISOU 4634  N   THR A 553    35376  33086  26013   2314    735   5158       N  
ATOM   4635  CA  THR A 553     -33.508  42.991  33.719  1.00273.85           C  
ANISOU 4635  CA  THR A 553    37984  35624  30444    165   -294   4231       C  
ATOM   4636  C   THR A 553     -32.467  43.004  32.592  1.00282.91           C  
ANISOU 4636  C   THR A 553    37993  36480  33019     59   -106   2746       C  
ATOM   4637  O   THR A 553     -32.293  44.023  31.926  1.00270.15           O  
ANISOU 4637  O   THR A 553    37992  35247  29406    104   -184   4859       O  
ATOM   4638  CB  THR A 553     -32.960  43.587  35.034  1.00276.19           C  
ANISOU 4638  CB  THR A 553    37987  35703  31249    135   -232   3932       C  
ATOM   4639  OG1 THR A 553     -32.612  44.956  34.820  1.00276.12           O  
ANISOU 4639  OG1 THR A 553    37988  35546  31379    135   -221   4025       O  
ATOM   4640  CG2 THR A 553     -31.759  42.816  35.603  1.00275.15           C  
ANISOU 4640  CG2 THR A 553    37994  35664  30885     54    -94   4071       C  
TER    4641      THR A 553                                                      
ATOM   4642  N   PRO B  58      39.917  22.187 -16.837  1.00217.29           N  
ANISOU 4642  N   PRO B  58    25178  33278  24102   -867   2643   2908       N  
ATOM   4643  CA  PRO B  58      40.760  20.983 -16.794  1.00216.51           C  
ANISOU 4643  CA  PRO B  58    24962  33600  23703   -682   2595   2809       C  
ATOM   4644  C   PRO B  58      39.946  19.688 -16.894  1.00217.99           C  
ANISOU 4644  C   PRO B  58    25304  33779  23743   -338   2547   2494       C  
ATOM   4645  O   PRO B  58      38.776  19.698 -16.505  1.00215.68           O  
ANISOU 4645  O   PRO B  58    25229  33111  23606   -345   2521   2286       O  
ATOM   4646  CB  PRO B  58      41.462  21.093 -15.442  1.00218.24           C  
ANISOU 4646  CB  PRO B  58    25177  33733  24011   -991   2557   2690       C  
ATOM   4647  CG  PRO B  58      40.564  21.918 -14.598  1.00222.00           C  
ANISOU 4647  CG  PRO B  58    25873  33667  24812  -1247   2549   2525       C  
ATOM   4648  CD  PRO B  58      39.695  22.757 -15.494  1.00218.31           C  
ANISOU 4648  CD  PRO B  58    25476  32963  24508  -1198   2617   2705       C  
ATOM   4649  N   PRO B  59      40.522  18.560 -17.386  1.00215.05           N  
ANISOU 4649  N   PRO B  59    24828  33797  23084    -40   2541   2443       N  
ATOM   4650  CA  PRO B  59      39.734  17.322 -17.468  1.00213.26           C  
ANISOU 4650  CA  PRO B  59    24767  33488  22773    250   2507   2111       C  
ATOM   4651  C   PRO B  59      39.461  16.743 -16.071  1.00215.37           C  
ANISOU 4651  C   PRO B  59    25221  33425  23186    153   2463   1853       C  
ATOM   4652  O   PRO B  59      40.323  16.847 -15.186  1.00215.31           O  
ANISOU 4652  O   PRO B  59    25134  33483  23190    -10   2463   1920       O  
ATOM   4653  CB  PRO B  59      40.611  16.393 -18.323  1.00216.62           C  
ANISOU 4653  CB  PRO B  59    25021  34404  22881    580   2534   2139       C  
ATOM   4654  CG  PRO B  59      41.668  17.276 -18.931  1.00223.55           C  
ANISOU 4654  CG  PRO B  59    25614  35679  23644    489   2579   2541       C  
ATOM   4655  CD  PRO B  59      41.886  18.341 -17.907  1.00218.89           C  
ANISOU 4655  CD  PRO B  59    25042  34810  23316     60   2573   2674       C  
ATOM   4656  N   PRO B  60      38.251  16.186 -15.817  1.00210.29           N  
ANISOU 4656  N   PRO B  60    24793  32461  22644    231   2427   1579       N  
ATOM   4657  CA  PRO B  60      37.985  15.637 -14.475  1.00208.52           C  
ANISOU 4657  CA  PRO B  60    24712  31963  22554    150   2393   1387       C  
ATOM   4658  C   PRO B  60      38.750  14.343 -14.218  1.00212.83           C  
ANISOU 4658  C   PRO B  60    25219  32684  22964    378   2421   1319       C  
ATOM   4659  O   PRO B  60      38.935  13.539 -15.134  1.00213.31           O  
ANISOU 4659  O   PRO B  60    25253  32928  22868    662   2451   1260       O  
ATOM   4660  CB  PRO B  60      36.472  15.407 -14.453  1.00208.68           C  
ANISOU 4660  CB  PRO B  60    24938  31647  22704    181   2354   1162       C  
ATOM   4661  CG  PRO B  60      36.028  15.446 -15.855  1.00214.01           C  
ANISOU 4661  CG  PRO B  60    25573  32487  23254    352   2367   1172       C  
ATOM   4662  CD  PRO B  60      37.106  15.991 -16.734  1.00211.56           C  
ANISOU 4662  CD  PRO B  60    25040  32565  22778    394   2416   1447       C  
ATOM   4663  N   LEU B  61      39.209  14.165 -12.964  1.00209.15           N  
ANISOU 4663  N   LEU B  61    24732  32185  22549    270   2420   1331       N  
ATOM   4664  CA  LEU B  61      39.970  13.002 -12.495  1.00209.72           C  
ANISOU 4664  CA  LEU B  61    24750  32419  22515    490   2471   1333       C  
ATOM   4665  C   LEU B  61      39.213  11.711 -12.776  1.00213.57           C  
ANISOU 4665  C   LEU B  61    25421  32666  23059    770   2494   1106       C  
ATOM   4666  O   LEU B  61      37.995  11.678 -12.588  1.00211.81           O  
ANISOU 4666  O   LEU B  61    25373  32098  23009    688   2448    930       O  
ATOM   4667  CB  LEU B  61      40.268  13.109 -10.982  1.00209.26           C  
ANISOU 4667  CB  LEU B  61    24637  32355  22519    308   2462   1374       C  
ATOM   4668  CG  LEU B  61      40.891  14.411 -10.452  1.00214.46           C  
ANISOU 4668  CG  LEU B  61    25131  33186  23167    -52   2428   1509       C  
ATOM   4669  CD1 LEU B  61      40.735  14.493  -8.951  1.00213.94           C  
ANISOU 4669  CD1 LEU B  61    25054  33055  23180   -232   2399   1434       C  
ATOM   4670  CD2 LEU B  61      42.363  14.530 -10.828  1.00219.09           C  
ANISOU 4670  CD2 LEU B  61    25451  34272  23520    -29   2473   1747       C  
ATOM   4671  N   SER B  62      39.937  10.654 -13.208  1.00211.72           N  
ANISOU 4671  N   SER B  62    25143  32612  22687   1095   2573   1105       N  
ATOM   4672  CA  SER B  62      39.385   9.340 -13.565  1.00212.00           C  
ANISOU 4672  CA  SER B  62    25353  32402  22796   1373   2618    863       C  
ATOM   4673  C   SER B  62      38.573   8.707 -12.419  1.00214.46           C  
ANISOU 4673  C   SER B  62    25826  32302  23359   1311   2620    764       C  
ATOM   4674  O   SER B  62      37.635   7.950 -12.686  1.00214.24           O  
ANISOU 4674  O   SER B  62    25977  31944  23478   1385   2620    526       O  
ATOM   4675  CB  SER B  62      40.495   8.394 -14.009  1.00217.82           C  
ANISOU 4675  CB  SER B  62    26004  33402  23356   1742   2727    912       C  
ATOM   4676  OG  SER B  62      41.403   8.103 -12.958  1.00226.29           O  
ANISOU 4676  OG  SER B  62    26961  34622  24396   1799   2798   1138       O  
ATOM   4677  N   HIS B  63      38.917   9.053 -11.159  1.00209.80           N  
ANISOU 4677  N   HIS B  63    25143  31769  22802   1157   2618    948       N  
ATOM   4678  CA  HIS B  63      38.263   8.569  -9.941  1.00208.41           C  
ANISOU 4678  CA  HIS B  63    25051  31312  22824   1098   2624    931       C  
ATOM   4679  C   HIS B  63      37.115   9.489  -9.479  1.00208.64           C  
ANISOU 4679  C   HIS B  63    25159  31129  22987    779   2511    839       C  
ATOM   4680  O   HIS B  63      36.228   9.025  -8.761  1.00207.35           O  
ANISOU 4680  O   HIS B  63    25098  30688  22997    745   2500    770       O  
ATOM   4681  CB  HIS B  63      39.293   8.404  -8.821  1.00210.21           C  
ANISOU 4681  CB  HIS B  63    25085  31826  22959   1147   2691   1182       C  
ATOM   4682  CG  HIS B  63      40.287   7.323  -9.109  1.00216.18           C  
ANISOU 4682  CG  HIS B  63    25780  32747  23610   1524   2830   1297       C  
ATOM   4683  ND1 HIS B  63      40.092   6.024  -8.668  1.00219.27           N  
ANISOU 4683  ND1 HIS B  63    26272  32876  24166   1785   2945   1311       N  
ATOM   4684  CD2 HIS B  63      41.436   7.374  -9.822  1.00219.68           C  
ANISOU 4684  CD2 HIS B  63    26077  33578  23815   1694   2880   1413       C  
ATOM   4685  CE1 HIS B  63      41.132   5.335  -9.110  1.00221.18           C  
ANISOU 4685  CE1 HIS B  63    26440  33330  24268   2126   3070   1420       C  
ATOM   4686  NE2 HIS B  63      41.968   6.105  -9.809  1.00221.76           N  
ANISOU 4686  NE2 HIS B  63    26355  33828  24075   2090   3030   1482       N  
ATOM   4687  N   CYS B  64      37.117  10.774  -9.918  1.00203.57           N  
ANISOU 4687  N   CYS B  64    24466  30609  22273    565   2440    857       N  
ATOM   4688  CA  CYS B  64      36.091  11.781  -9.591  1.00201.29           C  
ANISOU 4688  CA  CYS B  64    24254  30124  22101    298   2353    781       C  
ATOM   4689  C   CYS B  64      34.912  11.752 -10.596  1.00204.06           C  
ANISOU 4689  C   CYS B  64    24760  30256  22516    329   2315    607       C  
ATOM   4690  O   CYS B  64      34.075  12.659 -10.594  1.00202.50           O  
ANISOU 4690  O   CYS B  64    24618  29937  22384    157   2259    572       O  
ATOM   4691  CB  CYS B  64      36.707  13.177  -9.508  1.00201.65           C  
ANISOU 4691  CB  CYS B  64    24172  30363  22082     57   2325    904       C  
ATOM   4692  SG  CYS B  64      37.240  13.667  -7.845  1.00205.54           S  
ANISOU 4692  SG  CYS B  64    24524  30998  22574   -167   2307    967       S  
ATOM   4693  N   GLY B  65      34.864  10.711 -11.425  1.00201.36           N  
ANISOU 4693  N   GLY B  65    24476  29887  22144    555   2354    488       N  
ATOM   4694  CA  GLY B  65      33.828  10.499 -12.430  1.00201.08           C  
ANISOU 4694  CA  GLY B  65    24548  29731  22123    597   2320    283       C  
ATOM   4695  C   GLY B  65      33.618   9.028 -12.721  1.00205.91           C  
ANISOU 4695  C   GLY B  65    25260  30175  22799    797   2366     77       C  
ATOM   4696  O   GLY B  65      34.479   8.205 -12.396  1.00206.57           O  
ANISOU 4696  O   GLY B  65    25326  30270  22892    971   2448    133       O  
ATOM   4697  N   ARG B  66      32.466   8.679 -13.325  1.00202.51           N  
ANISOU 4697  N   ARG B  66    24933  29588  22422    772   2324   -165       N  
ATOM   4698  CA  ARG B  66      32.175   7.283 -13.645  1.00204.10           C  
ANISOU 4698  CA  ARG B  66    25248  29572  22729    912   2368   -422       C  
ATOM   4699  C   ARG B  66      31.567   7.136 -15.039  1.00209.14           C  
ANISOU 4699  C   ARG B  66    25893  30330  23239    957   2331   -713       C  
ATOM   4700  O   ARG B  66      30.786   7.988 -15.471  1.00207.73           O  
ANISOU 4700  O   ARG B  66    25667  30293  22967    823   2255   -719       O  
ATOM   4701  CB  ARG B  66      31.244   6.676 -12.591  1.00203.61           C  
ANISOU 4701  CB  ARG B  66    25299  29132  22930    780   2358   -457       C  
ATOM   4702  CG  ARG B  66      31.484   5.192 -12.354  1.00215.42           C  
ANISOU 4702  CG  ARG B  66    26897  30328  24623    943   2462   -557       C  
ATOM   4703  CD  ARG B  66      30.572   4.639 -11.279  1.00222.86           C  
ANISOU 4703  CD  ARG B  66    27918  30919  25839    798   2461   -519       C  
ATOM   4704  NE  ARG B  66      30.999   5.029  -9.934  1.00227.83           N  
ANISOU 4704  NE  ARG B  66    28456  31612  26497    769   2480   -183       N  
ATOM   4705  CZ  ARG B  66      30.342   4.723  -8.820  1.00240.49           C  
ANISOU 4705  CZ  ARG B  66    30065  33020  28289    664   2481    -58       C  
ATOM   4706  NH1 ARG B  66      29.217   4.020  -8.875  1.00228.40           N  
ANISOU 4706  NH1 ARG B  66    28638  31181  26964    553   2464   -218       N  
ATOM   4707  NH2 ARG B  66      30.804   5.116  -7.642  1.00225.88           N  
ANISOU 4707  NH2 ARG B  66    28092  31324  26407    659   2497    225       N  
ATOM   4708  N   ALA B  67      31.923   6.038 -15.734  1.00208.05           N  
ANISOU 4708  N   ALA B  67    25804  30157  23089   1165   2394   -961       N  
ATOM   4709  CA  ALA B  67      31.423   5.727 -17.071  1.00209.71           C  
ANISOU 4709  CA  ALA B  67    26000  30530  23151   1228   2363  -1311       C  
ATOM   4710  C   ALA B  67      29.960   5.284 -16.996  1.00213.60           C  
ANISOU 4710  C   ALA B  67    26596  30756  23808   1013   2299  -1581       C  
ATOM   4711  O   ALA B  67      29.650   4.262 -16.374  1.00214.23           O  
ANISOU 4711  O   ALA B  67    26821  30413  24165    970   2340  -1708       O  
ATOM   4712  CB  ALA B  67      32.282   4.649 -17.718  1.00213.62           C  
ANISOU 4712  CB  ALA B  67    26529  31037  23601   1524   2460  -1535       C  
ATOM   4713  N   ALA B  68      29.059   6.096 -17.582  1.00209.18           N  
ANISOU 4713  N   ALA B  68    25940  30460  23081    876   2206  -1618       N  
ATOM   4714  CA  ALA B  68      27.612   5.860 -17.611  1.00209.18           C  
ANISOU 4714  CA  ALA B  68    25977  30341  23159    657   2131  -1844       C  
ATOM   4715  C   ALA B  68      26.966   6.520 -18.842  1.00213.46           C  
ANISOU 4715  C   ALA B  68    26350  31370  23385    649   2063  -1967       C  
ATOM   4716  O   ALA B  68      27.312   7.665 -19.151  1.00211.79           O  
ANISOU 4716  O   ALA B  68    26003  31492  22975    719   2061  -1678       O  
ATOM   4717  CB  ALA B  68      26.964   6.389 -16.336  1.00207.09           C  
ANISOU 4717  CB  ALA B  68    25760  29845  23079    451   2093  -1572       C  
ATOM   4718  N   PRO B  69      26.022   5.841 -19.547  1.00211.99           N  
ANISOU 4718  N   PRO B  69    26147  31253  23147    558   2015  -2376       N  
ATOM   4719  CA  PRO B  69      25.393   6.470 -20.727  1.00212.59           C  
ANISOU 4719  CA  PRO B  69    26010  31896  22870    573   1956  -2471       C  
ATOM   4720  C   PRO B  69      24.495   7.650 -20.341  1.00212.74           C  
ANISOU 4720  C   PRO B  69    25946  32053  22835    436   1907  -2140       C  
ATOM   4721  O   PRO B  69      23.666   7.533 -19.433  1.00210.97           O  
ANISOU 4721  O   PRO B  69    25818  31524  22817    233   1870  -2105       O  
ATOM   4722  CB  PRO B  69      24.603   5.326 -21.368  1.00218.02           C  
ANISOU 4722  CB  PRO B  69    26708  32579  23552    462   1916  -3031       C  
ATOM   4723  CG  PRO B  69      24.360   4.359 -20.273  1.00222.57           C  
ANISOU 4723  CG  PRO B  69    27515  32502  24549    285   1936  -3125       C  
ATOM   4724  CD  PRO B  69      25.505   4.474 -19.317  1.00215.91           C  
ANISOU 4724  CD  PRO B  69    26796  31334  23904    429   2021  -2763       C  
ATOM   4725  N   CYS B  70      24.693   8.799 -21.016  1.00207.99           N  
ANISOU 4725  N   CYS B  70    25158  31906  21962    571   1920  -1865       N  
ATOM   4726  CA  CYS B  70      23.977  10.046 -20.742  1.00205.49           C  
ANISOU 4726  CA  CYS B  70    24765  31718  21595    509   1909  -1506       C  
ATOM   4727  C   CYS B  70      22.636  10.114 -21.459  1.00210.73           C  
ANISOU 4727  C   CYS B  70    25262  32779  22028    442   1852  -1666       C  
ATOM   4728  O   CYS B  70      22.522   9.716 -22.618  1.00213.33           O  
ANISOU 4728  O   CYS B  70    25420  33552  22084    524   1835  -1942       O  
ATOM   4729  CB  CYS B  70      24.839  11.255 -21.098  1.00204.84           C  
ANISOU 4729  CB  CYS B  70    24564  31880  21384    681   1977  -1091       C  
ATOM   4730  SG  CYS B  70      26.462  11.289 -20.290  1.00206.94           S  
ANISOU 4730  SG  CYS B  70    24966  31798  21866    735   2039   -878       S  
ATOM   4731  N   GLU B  71      21.636  10.675 -20.767  1.00205.19           N  
ANISOU 4731  N   GLU B  71    24583  31976  21404    311   1826  -1480       N  
ATOM   4732  CA  GLU B  71      20.284  10.903 -21.275  1.00206.18           C  
ANISOU 4732  CA  GLU B  71    24531  32507  21301    250   1780  -1537       C  
ATOM   4733  C   GLU B  71      19.892  12.373 -21.015  1.00207.76           C  
ANISOU 4733  C   GLU B  71    24667  32822  21450    346   1835  -1046       C  
ATOM   4734  O   GLU B  71      20.274  12.911 -19.971  1.00204.76           O  
ANISOU 4734  O   GLU B  71    24460  32016  21325    325   1868   -788       O  
ATOM   4735  CB  GLU B  71      19.263   9.912 -20.667  1.00208.12           C  
ANISOU 4735  CB  GLU B  71    24865  32511  21702    -20   1697  -1850       C  
ATOM   4736  CG  GLU B  71      19.188   9.881 -19.148  1.00217.03           C  
ANISOU 4736  CG  GLU B  71    26214  33061  23187   -155   1692  -1675       C  
ATOM   4737  CD  GLU B  71      18.173   8.906 -18.587  1.00241.05           C  
ANISOU 4737  CD  GLU B  71    29306  35901  26382   -424   1619  -1926       C  
ATOM   4738  OE1 GLU B  71      18.567   7.765 -18.254  1.00237.82           O  
ANISOU 4738  OE1 GLU B  71    29041  35098  26222   -533   1616  -2180       O  
ATOM   4739  OE2 GLU B  71      16.984   9.283 -18.473  1.00236.52           O  
ANISOU 4739  OE2 GLU B  71    28617  35561  25687   -517   1574  -1843       O  
ATOM   4740  N   PRO B  72      19.176  13.054 -21.946  1.00205.69           N  
ANISOU 4740  N   PRO B  72    24152  33138  20863    471   1858   -906       N  
ATOM   4741  CA  PRO B  72      18.825  14.468 -21.710  1.00204.37           C  
ANISOU 4741  CA  PRO B  72    23943  33022  20686    602   1943   -412       C  
ATOM   4742  C   PRO B  72      17.898  14.665 -20.509  1.00206.10           C  
ANISOU 4742  C   PRO B  72    24308  32903  21098    465   1913   -334       C  
ATOM   4743  O   PRO B  72      17.062  13.806 -20.227  1.00206.01           O  
ANISOU 4743  O   PRO B  72    24301  32892  21081    280   1821   -621       O  
ATOM   4744  CB  PRO B  72      18.137  14.887 -23.011  1.00209.10           C  
ANISOU 4744  CB  PRO B  72    24206  34376  20866    775   1976   -320       C  
ATOM   4745  CG  PRO B  72      17.647  13.617 -23.612  1.00215.82           C  
ANISOU 4745  CG  PRO B  72    24939  35546  21516    632   1865   -849       C  
ATOM   4746  CD  PRO B  72      18.665  12.586 -23.251  1.00210.57           C  
ANISOU 4746  CD  PRO B  72    24496  34412  21100    516   1821  -1185       C  
ATOM   4747  N   LEU B  73      18.066  15.796 -19.800  1.00200.81           N  
ANISOU 4747  N   LEU B  73    23750  31947  20603    550   1995     45       N  
ATOM   4748  CA  LEU B  73      17.285  16.158 -18.616  1.00198.87           C  
ANISOU 4748  CA  LEU B  73    23639  31397  20525    475   1984    151       C  
ATOM   4749  C   LEU B  73      15.826  16.437 -18.964  1.00203.94           C  
ANISOU 4749  C   LEU B  73    24094  32484  20908    538   1981    229       C  
ATOM   4750  O   LEU B  73      15.546  17.265 -19.833  1.00205.10           O  
ANISOU 4750  O   LEU B  73    24053  33046  20831    755   2073    495       O  
ATOM   4751  CB  LEU B  73      17.895  17.393 -17.928  1.00197.54           C  
ANISOU 4751  CB  LEU B  73    23619  30853  20585    574   2088    497       C  
ATOM   4752  CG  LEU B  73      18.968  17.135 -16.877  1.00200.09           C  
ANISOU 4752  CG  LEU B  73    24165  30645  21216    436   2064    412       C  
ATOM   4753  CD1 LEU B  73      19.876  18.332 -16.732  1.00200.02           C  
ANISOU 4753  CD1 LEU B  73    24226  30409  21364    522   2176    711       C  
ATOM   4754  CD2 LEU B  73      18.348  16.821 -15.532  1.00200.98           C  
ANISOU 4754  CD2 LEU B  73    24416  30456  21492    297   1997    309       C  
ATOM   4755  N   ARG B  74      14.899  15.742 -18.290  1.00200.20           N  
ANISOU 4755  N   ARG B  74    23647  31963  20459    356   1884     33       N  
ATOM   4756  CA  ARG B  74      13.460  15.932 -18.477  1.00201.59           C  
ANISOU 4756  CA  ARG B  74    23632  32585  20379    387   1868    104       C  
ATOM   4757  C   ARG B  74      13.003  17.160 -17.672  1.00203.77           C  
ANISOU 4757  C   ARG B  74    23993  32688  20742    568   1962    483       C  
ATOM   4758  O   ARG B  74      12.042  17.830 -18.058  1.00205.04           O  
ANISOU 4758  O   ARG B  74    23979  33265  20662    749   2024    714       O  
ATOM   4759  CB  ARG B  74      12.685  14.663 -18.058  1.00203.04           C  
ANISOU 4759  CB  ARG B  74    23796  32777  20572     87   1727   -249       C  
ATOM   4760  CG  ARG B  74      11.207  14.660 -18.455  1.00217.52           C  
ANISOU 4760  CG  ARG B  74    25366  35207  22075     68   1690   -236       C  
ATOM   4761  CD  ARG B  74      10.551  13.305 -18.264  1.00230.00           C  
ANISOU 4761  CD  ARG B  74    26894  36824  23671   -286   1549   -626       C  
ATOM   4762  NE  ARG B  74      10.695  12.454 -19.448  1.00239.66           N  
ANISOU 4762  NE  ARG B  74    28205  37902  24953   -374   1493   -951       N  
ATOM   4763  CZ  ARG B  74       9.792  12.352 -20.421  1.00249.00           C  
ANISOU 4763  CZ  ARG B  74    30018  37916  26677   -267   1448   -837       C  
ATOM   4764  NH1 ARG B  74      10.011  11.554 -21.456  1.00240.91           N  
ANISOU 4764  NH1 ARG B  74    28533  37839  25163   -407   1394  -1262       N  
ATOM   4765  NH2 ARG B  74       8.662  13.048 -20.364  1.00239.25           N  
ANISOU 4765  NH2 ARG B  74    28175  37947  24783   -252   1479   -704       N  
ATOM   4766  N   TYR B  75      13.723  17.463 -16.572  1.00197.19           N  
ANISOU 4766  N   TYR B  75    23418  31266  20241    536   1981    538       N  
ATOM   4767  CA  TYR B  75      13.427  18.573 -15.668  1.00195.78           C  
ANISOU 4767  CA  TYR B  75    23362  30830  20194    685   2066    808       C  
ATOM   4768  C   TYR B  75      14.562  19.585 -15.693  1.00198.53           C  
ANISOU 4768  C   TYR B  75    23848  30837  20749    815   2191   1017       C  
ATOM   4769  O   TYR B  75      15.714  19.228 -15.436  1.00196.60           O  
ANISOU 4769  O   TYR B  75    23729  30272  20699    681   2161    885       O  
ATOM   4770  CB  TYR B  75      13.182  18.066 -14.230  1.00194.89           C  
ANISOU 4770  CB  TYR B  75    23400  30376  20274    510   1973    658       C  
ATOM   4771  CG  TYR B  75      12.371  16.791 -14.164  1.00196.55           C  
ANISOU 4771  CG  TYR B  75    23494  30814  20372    286   1836    412       C  
ATOM   4772  CD1 TYR B  75      10.980  16.823 -14.205  1.00199.87           C  
ANISOU 4772  CD1 TYR B  75    23740  31647  20555    316   1809    483       C  
ATOM   4773  CD2 TYR B  75      12.994  15.549 -14.087  1.00196.50           C  
ANISOU 4773  CD2 TYR B  75    23543  30611  20506     42   1744    121       C  
ATOM   4774  CE1 TYR B  75      10.230  15.651 -14.171  1.00201.40           C  
ANISOU 4774  CE1 TYR B  75    23809  32051  20663     60   1683    256       C  
ATOM   4775  CE2 TYR B  75      12.255  14.370 -14.061  1.00198.24           C  
ANISOU 4775  CE2 TYR B  75    23666  30979  20678   -193   1634   -109       C  
ATOM   4776  CZ  TYR B  75      10.873  14.426 -14.097  1.00206.83           C  
ANISOU 4776  CZ  TYR B  75    24573  32474  21540   -208   1598    -46       C  
ATOM   4777  OH  TYR B  75      10.144  13.268 -14.059  1.00208.90           O  
ANISOU 4777  OH  TYR B  75    24727  32871  21776   -488   1489   -273       O  
ATOM   4778  N   ASN B  76      14.235  20.842 -16.018  1.00196.27           N  
ANISOU 4778  N   ASN B  76    23526  30625  20423   1076   2342   1361       N  
ATOM   4779  CA  ASN B  76      15.202  21.937 -16.091  1.00196.30           C  
ANISOU 4779  CA  ASN B  76    23646  30287  20651   1189   2486   1605       C  
ATOM   4780  C   ASN B  76      15.593  22.439 -14.693  1.00197.63           C  
ANISOU 4780  C   ASN B  76    24078  29865  21147   1109   2496   1547       C  
ATOM   4781  O   ASN B  76      16.612  23.117 -14.555  1.00197.35           O  
ANISOU 4781  O   ASN B  76    24166  29466  21351   1087   2577   1637       O  
ATOM   4782  CB  ASN B  76      14.646  23.100 -16.941  1.00200.52           C  
ANISOU 4782  CB  ASN B  76    24043  31084  21060   1514   2672   2028       C  
ATOM   4783  CG  ASN B  76      13.304  23.672 -16.510  1.00224.18           C  
ANISOU 4783  CG  ASN B  76    27022  34198  23958   1718   2735   2186       C  
ATOM   4784  OD1 ASN B  76      12.555  23.085 -15.718  1.00216.44           O  
ANISOU 4784  OD1 ASN B  76    26069  33255  22915   1615   2617   1973       O  
ATOM   4785  ND2 ASN B  76      12.951  24.827 -17.062  1.00218.75           N  
ANISOU 4785  ND2 ASN B  76    26266  33605  23244   2037   2937   2600       N  
ATOM   4786  N   VAL B  77      14.796  22.091 -13.666  1.00192.14           N  
ANISOU 4786  N   VAL B  77    23442  29119  20444   1052   2411   1391       N  
ATOM   4787  CA  VAL B  77      14.983  22.542 -12.289  1.00190.43           C  
ANISOU 4787  CA  VAL B  77    23431  28457  20468   1005   2412   1306       C  
ATOM   4788  C   VAL B  77      15.191  21.343 -11.319  1.00190.87           C  
ANISOU 4788  C   VAL B  77    23526  28429  20569    749   2241    997       C  
ATOM   4789  O   VAL B  77      14.575  20.287 -11.484  1.00189.95           O  
ANISOU 4789  O   VAL B  77    23288  28599  20286    655   2132    879       O  
ATOM   4790  CB  VAL B  77      13.779  23.451 -11.890  1.00195.71           C  
ANISOU 4790  CB  VAL B  77    24113  29173  21075   1260   2507   1479       C  
ATOM   4791  CG1 VAL B  77      12.457  22.681 -11.799  1.00195.37           C  
ANISOU 4791  CG1 VAL B  77    23906  29580  20747   1275   2403   1426       C  
ATOM   4792  CG2 VAL B  77      14.050  24.245 -10.623  1.00195.43           C  
ANISOU 4792  CG2 VAL B  77    24294  28665  21297   1274   2553   1401       C  
ATOM   4793  N   CYS B  78      16.095  21.521 -10.333  1.00185.49           N  
ANISOU 4793  N   CYS B  78    22996  27362  20118    630   2230    880       N  
ATOM   4794  CA  CYS B  78      16.413  20.531  -9.300  1.00183.01           C  
ANISOU 4794  CA  CYS B  78    22708  26958  19868    429   2101    655       C  
ATOM   4795  C   CYS B  78      16.201  21.168  -7.924  1.00186.05           C  
ANISOU 4795  C   CYS B  78    23194  27143  20356    464   2110    599       C  
ATOM   4796  O   CYS B  78      16.959  22.061  -7.534  1.00186.35           O  
ANISOU 4796  O   CYS B  78    23348  26888  20566    462   2183    583       O  
ATOM   4797  CB  CYS B  78      17.838  20.003  -9.465  1.00182.23           C  
ANISOU 4797  CB  CYS B  78    22640  26708  19892    262   2076    559       C  
ATOM   4798  SG  CYS B  78      18.244  18.576  -8.423  1.00184.26           S  
ANISOU 4798  SG  CYS B  78    22887  26917  20208     59   1945    350       S  
ATOM   4799  N   LEU B  79      15.127  20.741  -7.229  1.00181.51           N  
ANISOU 4799  N   LEU B  79    22552  26756  19658    496   2039    565       N  
ATOM   4800  CA  LEU B  79      14.704  21.191  -5.894  1.00181.17           C  
ANISOU 4800  CA  LEU B  79    22552  26647  19636    564   2030    500       C  
ATOM   4801  C   LEU B  79      14.594  22.736  -5.786  1.00186.19           C  
ANISOU 4801  C   LEU B  79    23321  27064  20358    775   2173    559       C  
ATOM   4802  O   LEU B  79      15.005  23.319  -4.781  1.00186.00           O  
ANISOU 4802  O   LEU B  79    23395  26818  20458    766   2191    414       O  
ATOM   4803  CB  LEU B  79      15.639  20.636  -4.794  1.00180.02           C  
ANISOU 4803  CB  LEU B  79    22423  26366  19610    377   1952    325       C  
ATOM   4804  CG  LEU B  79      15.663  19.114  -4.588  1.00183.35           C  
ANISOU 4804  CG  LEU B  79    22726  26945  19994    205   1835    289       C  
ATOM   4805  CD1 LEU B  79      16.954  18.683  -3.924  1.00182.65           C  
ANISOU 4805  CD1 LEU B  79    22655  26704  20041     55   1809    184       C  
ATOM   4806  CD2 LEU B  79      14.468  18.638  -3.775  1.00185.78           C  
ANISOU 4806  CD2 LEU B  79    22913  27503  20170    242   1764    324       C  
ATOM   4807  N   GLY B  80      14.031  23.367  -6.817  1.00184.10           N  
ANISOU 4807  N   GLY B  80    23046  26877  20026    967   2282    768       N  
ATOM   4808  CA  GLY B  80      13.813  24.811  -6.858  1.00186.31           C  
ANISOU 4808  CA  GLY B  80    23454  26923  20414   1210   2453    884       C  
ATOM   4809  C   GLY B  80      14.898  25.658  -7.496  1.00191.43           C  
ANISOU 4809  C   GLY B  80    24221  27206  21308   1176   2583    965       C  
ATOM   4810  O   GLY B  80      14.724  26.876  -7.616  1.00193.41           O  
ANISOU 4810  O   GLY B  80    24588  27202  21699   1376   2753   1094       O  
ATOM   4811  N   SER B  81      16.016  25.029  -7.923  1.00186.83           N  
ANISOU 4811  N   SER B  81    23607  26591  20790    935   2518    911       N  
ATOM   4812  CA  SER B  81      17.152  25.709  -8.561  1.00187.94           C  
ANISOU 4812  CA  SER B  81    23818  26444  21146    860   2625   1011       C  
ATOM   4813  C   SER B  81      17.415  25.160  -9.981  1.00192.06           C  
ANISOU 4813  C   SER B  81    24191  27246  21536    856   2624   1206       C  
ATOM   4814  O   SER B  81      17.560  23.946 -10.147  1.00189.87           O  
ANISOU 4814  O   SER B  81    23808  27226  21110    722   2487   1085       O  
ATOM   4815  CB  SER B  81      18.409  25.566  -7.705  1.00190.43           C  
ANISOU 4815  CB  SER B  81    24207  26509  21640    583   2556    763       C  
ATOM   4816  OG  SER B  81      18.208  25.979  -6.363  1.00199.20           O  
ANISOU 4816  OG  SER B  81    25415  27445  22825    573   2539    532       O  
ATOM   4817  N   VAL B  82      17.467  26.055 -11.001  1.00191.04           N  
ANISOU 4817  N   VAL B  82    24045  27075  21466   1020   2789   1509       N  
ATOM   4818  CA  VAL B  82      17.711  25.690 -12.410  1.00191.11           C  
ANISOU 4818  CA  VAL B  82    23877  27416  21319   1061   2809   1720       C  
ATOM   4819  C   VAL B  82      19.156  25.131 -12.558  1.00194.07           C  
ANISOU 4819  C   VAL B  82    24242  27715  21782    802   2734   1601       C  
ATOM   4820  O   VAL B  82      20.062  25.565 -11.842  1.00193.61           O  
ANISOU 4820  O   VAL B  82    24312  27285  21968    634   2747   1500       O  
ATOM   4821  CB  VAL B  82      17.388  26.855 -13.399  1.00198.04           C  
ANISOU 4821  CB  VAL B  82    24708  28305  22235   1337   3027   2140       C  
ATOM   4822  CG1 VAL B  82      18.335  28.046 -13.238  1.00199.95           C  
ANISOU 4822  CG1 VAL B  82    25107  28009  22856   1283   3183   2274       C  
ATOM   4823  CG2 VAL B  82      17.342  26.376 -14.849  1.00198.34           C  
ANISOU 4823  CG2 VAL B  82    24493  28867  22000   1435   3033   2353       C  
ATOM   4824  N   LEU B  83      19.338  24.141 -13.455  1.00190.23           N  
ANISOU 4824  N   LEU B  83    23590  27615  21076    775   2653   1586       N  
ATOM   4825  CA  LEU B  83      20.604  23.435 -13.671  1.00189.18           C  
ANISOU 4825  CA  LEU B  83    23421  27497  20963    585   2579   1470       C  
ATOM   4826  C   LEU B  83      21.467  24.033 -14.794  1.00195.57           C  
ANISOU 4826  C   LEU B  83    24129  28375  21802    638   2695   1758       C  
ATOM   4827  O   LEU B  83      20.947  24.377 -15.862  1.00196.98           O  
ANISOU 4827  O   LEU B  83    24163  28848  21831    846   2786   2019       O  
ATOM   4828  CB  LEU B  83      20.359  21.940 -13.949  1.00187.57           C  
ANISOU 4828  CB  LEU B  83    23109  27635  20524    530   2430   1240       C  
ATOM   4829  CG  LEU B  83      19.845  21.118 -12.777  1.00190.33           C  
ANISOU 4829  CG  LEU B  83    23537  27894  20885    411   2303    967       C  
ATOM   4830  CD1 LEU B  83      20.584  21.419 -11.489  1.00189.63           C  
ANISOU 4830  CD1 LEU B  83    23595  27430  21026    264   2290    859       C  
ATOM   4831  CD2 LEU B  83      18.376  20.929 -12.806  1.00192.95           C  
ANISOU 4831  CD2 LEU B  83    23805  28463  21043    519   2275    964       C  
ATOM   4832  N   PRO B  84      22.806  24.118 -14.571  1.00192.22           N  
ANISOU 4832  N   PRO B  84    23744  27747  21544    453   2692   1732       N  
ATOM   4833  CA  PRO B  84      23.694  24.693 -15.604  1.00194.11           C  
ANISOU 4833  CA  PRO B  84    23863  28072  21818    484   2802   2040       C  
ATOM   4834  C   PRO B  84      24.058  23.729 -16.745  1.00197.59           C  
ANISOU 4834  C   PRO B  84    24095  29014  21968    557   2742   2043       C  
ATOM   4835  O   PRO B  84      24.730  24.140 -17.696  1.00198.90           O  
ANISOU 4835  O   PRO B  84    24113  29358  22103    620   2829   2324       O  
ATOM   4836  CB  PRO B  84      24.946  25.081 -14.814  1.00195.93           C  
ANISOU 4836  CB  PRO B  84    24198  27936  22312    225   2803   1972       C  
ATOM   4837  CG  PRO B  84      24.959  24.180 -13.631  1.00197.71           C  
ANISOU 4837  CG  PRO B  84    24522  28080  22517     75   2651   1586       C  
ATOM   4838  CD  PRO B  84      23.554  23.756 -13.346  1.00192.10           C  
ANISOU 4838  CD  PRO B  84    23852  27463  21676    214   2597   1456       C  
ATOM   4839  N   TYR B  85      23.623  22.461 -16.651  1.00192.19           N  
ANISOU 4839  N   TYR B  85    23390  28553  21081    548   2600   1731       N  
ATOM   4840  CA  TYR B  85      23.913  21.408 -17.626  1.00191.92           C  
ANISOU 4840  CA  TYR B  85    23185  28956  20778    608   2532   1621       C  
ATOM   4841  C   TYR B  85      22.613  20.835 -18.218  1.00195.90           C  
ANISOU 4841  C   TYR B  85    23580  29840  21015    744   2487   1510       C  
ATOM   4842  O   TYR B  85      21.527  21.158 -17.731  1.00195.40           O  
ANISOU 4842  O   TYR B  85    23579  29689  20975    778   2494   1520       O  
ATOM   4843  CB  TYR B  85      24.775  20.312 -16.974  1.00191.14           C  
ANISOU 4843  CB  TYR B  85    23167  28736  20721    441   2417   1312       C  
ATOM   4844  CG  TYR B  85      24.279  19.856 -15.618  1.00190.62           C  
ANISOU 4844  CG  TYR B  85    23278  28360  20791    304   2331   1060       C  
ATOM   4845  CD1 TYR B  85      23.401  18.785 -15.500  1.00191.71           C  
ANISOU 4845  CD1 TYR B  85    23420  28611  20812    305   2234    806       C  
ATOM   4846  CD2 TYR B  85      24.709  20.481 -14.448  1.00190.58           C  
ANISOU 4846  CD2 TYR B  85    23411  27977  21025    162   2347   1073       C  
ATOM   4847  CE1 TYR B  85      22.943  18.361 -14.256  1.00190.87           C  
ANISOU 4847  CE1 TYR B  85    23441  28257  20825    188   2163    631       C  
ATOM   4848  CE2 TYR B  85      24.243  20.076 -13.199  1.00189.77           C  
ANISOU 4848  CE2 TYR B  85    23427  27669  21007     65   2270    864       C  
ATOM   4849  CZ  TYR B  85      23.370  19.008 -13.108  1.00195.53           C  
ANISOU 4849  CZ  TYR B  85    24147  28526  21619     88   2182    672       C  
ATOM   4850  OH  TYR B  85      22.936  18.600 -11.875  1.00194.04           O  
ANISOU 4850  OH  TYR B  85    24044  28168  21513     -2   2114    520       O  
ATOM   4851  N   GLY B  86      22.741  20.014 -19.264  1.00193.06           N  
ANISOU 4851  N   GLY B  86    23040  29928  20386    821   2442   1395       N  
ATOM   4852  CA  GLY B  86      21.605  19.439 -19.980  1.00193.79           C  
ANISOU 4852  CA  GLY B  86    22976  30471  20184    920   2395   1254       C  
ATOM   4853  C   GLY B  86      21.396  17.935 -19.950  1.00196.83           C  
ANISOU 4853  C   GLY B  86    23372  30958  20457    801   2251    790       C  
ATOM   4854  O   GLY B  86      20.313  17.476 -20.323  1.00197.04           O  
ANISOU 4854  O   GLY B  86    23290  31297  20280    814   2199    631       O  
ATOM   4855  N   ALA B  87      22.407  17.147 -19.531  1.00192.51           N  
ANISOU 4855  N   ALA B  87    22942  30161  20042    685   2196    575       N  
ATOM   4856  CA  ALA B  87      22.268  15.685 -19.486  1.00192.34           C  
ANISOU 4856  CA  ALA B  87    22958  30147  19976    583   2087    143       C  
ATOM   4857  C   ALA B  87      22.506  15.127 -18.080  1.00194.21           C  
ANISOU 4857  C   ALA B  87    23426  29861  20506    405   2035      3       C  
ATOM   4858  O   ALA B  87      23.297  15.686 -17.315  1.00192.34           O  
ANISOU 4858  O   ALA B  87    23295  29325  20461    369   2074    179       O  
ATOM   4859  CB  ALA B  87      23.210  15.030 -20.480  1.00194.65           C  
ANISOU 4859  CB  ALA B  87    23137  30719  20104    681   2087     -6       C  
ATOM   4860  N   THR B  88      21.806  14.023 -17.745  1.00191.07           N  
ANISOU 4860  N   THR B  88    23081  29383  20136    282   1951   -307       N  
ATOM   4861  CA  THR B  88      21.879  13.374 -16.433  1.00189.37           C  
ANISOU 4861  CA  THR B  88    23043  28728  20180    130   1908   -411       C  
ATOM   4862  C   THR B  88      21.983  11.834 -16.545  1.00194.80           C  
ANISOU 4862  C   THR B  88    23773  29320  20921     51   1859   -769       C  
ATOM   4863  O   THR B  88      21.883  11.280 -17.641  1.00196.51           O  
ANISOU 4863  O   THR B  88    23889  29815  20960     96   1845   -998       O  
ATOM   4864  CB  THR B  88      20.672  13.798 -15.567  1.00195.56           C  
ANISOU 4864  CB  THR B  88    23864  29416  21026     44   1877   -322       C  
ATOM   4865  OG1 THR B  88      20.869  13.352 -14.226  1.00193.38           O  
ANISOU 4865  OG1 THR B  88    23726  28761  20987    -73   1850   -348       O  
ATOM   4866  CG2 THR B  88      19.344  13.277 -16.096  1.00195.29           C  
ANISOU 4866  CG2 THR B  88    23717  29662  20823    -14   1816   -500       C  
ATOM   4867  N   SER B  89      22.186  11.160 -15.390  1.00190.60           N  
ANISOU 4867  N   SER B  89    23384  28396  20640    -56   1845   -812       N  
ATOM   4868  CA  SER B  89      22.287   9.704 -15.267  1.00191.77           C  
ANISOU 4868  CA  SER B  89    23608  28325  20933   -130   1829  -1094       C  
ATOM   4869  C   SER B  89      21.724   9.230 -13.912  1.00194.66           C  
ANISOU 4869  C   SER B  89    24065  28354  21542   -285   1803  -1045       C  
ATOM   4870  O   SER B  89      22.073   9.787 -12.867  1.00192.23           O  
ANISOU 4870  O   SER B  89    23801  27902  21336   -276   1821   -807       O  
ATOM   4871  CB  SER B  89      23.735   9.249 -15.433  1.00195.84           C  
ANISOU 4871  CB  SER B  89    24173  28737  21499      4   1893  -1120       C  
ATOM   4872  OG  SER B  89      23.822   7.842 -15.591  1.00206.81           O  
ANISOU 4872  OG  SER B  89    25637  29928  23016    -16   1903  -1422       O  
ATOM   4873  N   THR B  90      20.852   8.199 -13.938  1.00192.75           N  
ANISOU 4873  N   THR B  90    23832  28017  21389   -438   1761  -1276       N  
ATOM   4874  CA  THR B  90      20.219   7.617 -12.743  1.00192.05           C  
ANISOU 4874  CA  THR B  90    23793  27643  21532   -596   1740  -1212       C  
ATOM   4875  C   THR B  90      21.059   6.427 -12.217  1.00196.58           C  
ANISOU 4875  C   THR B  90    24484  27820  22389   -582   1808  -1264       C  
ATOM   4876  O   THR B  90      20.518   5.479 -11.635  1.00197.14           O  
ANISOU 4876  O   THR B  90    24590  27627  22688   -728   1809  -1308       O  
ATOM   4877  CB  THR B  90      18.755   7.218 -13.034  1.00201.11           C  
ANISOU 4877  CB  THR B  90    24858  28922  22632   -798   1664  -1383       C  
ATOM   4878  OG1 THR B  90      18.699   6.392 -14.198  1.00203.59           O  
ANISOU 4878  OG1 THR B  90    25152  29310  22892   -852   1655  -1757       O  
ATOM   4879  CG2 THR B  90      17.835   8.422 -13.193  1.00198.23           C  
ANISOU 4879  CG2 THR B  90    24369  28939  22010   -777   1616  -1224       C  
ATOM   4880  N   LEU B  91      22.386   6.502 -12.417  1.00193.06           N  
ANISOU 4880  N   LEU B  91    24080  27346  21927   -395   1878  -1220       N  
ATOM   4881  CA  LEU B  91      23.368   5.504 -12.003  1.00194.11           C  
ANISOU 4881  CA  LEU B  91    24308  27166  22281   -301   1971  -1219       C  
ATOM   4882  C   LEU B  91      23.799   5.745 -10.557  1.00196.41           C  
ANISOU 4882  C   LEU B  91    24594  27334  22698   -273   2006   -876       C  
ATOM   4883  O   LEU B  91      24.052   4.781  -9.831  1.00197.07           O  
ANISOU 4883  O   LEU B  91    24724  27130  23021   -256   2076   -803       O  
ATOM   4884  CB  LEU B  91      24.584   5.565 -12.946  1.00194.92           C  
ANISOU 4884  CB  LEU B  91    24414  27411  22237    -87   2027  -1309       C  
ATOM   4885  CG  LEU B  91      25.687   4.533 -12.729  1.00201.40           C  
ANISOU 4885  CG  LEU B  91    25322  27963  23237     78   2142  -1323       C  
ATOM   4886  CD1 LEU B  91      25.650   3.460 -13.797  1.00205.04           C  
ANISOU 4886  CD1 LEU B  91    25855  28309  23743    122   2176  -1727       C  
ATOM   4887  CD2 LEU B  91      27.042   5.200 -12.688  1.00202.71           C  
ANISOU 4887  CD2 LEU B  91    25435  28336  23250    278   2191  -1100       C  
ATOM   4888  N   LEU B  92      23.887   7.026 -10.146  1.00190.81           N  
ANISOU 4888  N   LEU B  92    23819  26850  21831   -260   1967   -670       N  
ATOM   4889  CA  LEU B  92      24.319   7.411  -8.800  1.00189.23           C  
ANISOU 4889  CA  LEU B  92    23581  26627  21690   -241   1988   -395       C  
ATOM   4890  C   LEU B  92      23.229   7.130  -7.760  1.00193.50           C  
ANISOU 4890  C   LEU B  92    24091  27073  22359   -373   1949   -297       C  
ATOM   4891  O   LEU B  92      23.552   6.819  -6.611  1.00192.95           O  
ANISOU 4891  O   LEU B  92    23978  26932  22402   -344   1990    -97       O  
ATOM   4892  CB  LEU B  92      24.773   8.882  -8.747  1.00187.31           C  
ANISOU 4892  CB  LEU B  92    23287  26623  21259   -210   1964   -269       C  
ATOM   4893  CG  LEU B  92      25.932   9.305  -9.686  1.00192.00           C  
ANISOU 4893  CG  LEU B  92    23871  27363  21718    -90   2005   -287       C  
ATOM   4894  CD1 LEU B  92      26.528  10.620  -9.241  1.00190.75           C  
ANISOU 4894  CD1 LEU B  92    23658  27351  21468   -105   2003   -112       C  
ATOM   4895  CD2 LEU B  92      27.052   8.264  -9.735  1.00195.56           C  
ANISOU 4895  CD2 LEU B  92    24338  27721  22243     47   2090   -296       C  
ATOM   4896  N   ALA B  93      21.951   7.202  -8.169  1.00190.80           N  
ANISOU 4896  N   ALA B  93    23738  26783  21975   -508   1875   -417       N  
ATOM   4897  CA  ALA B  93      20.818   6.879  -7.307  1.00191.11           C  
ANISOU 4897  CA  ALA B  93    23722  26776  22114   -645   1833   -322       C  
ATOM   4898  C   ALA B  93      20.466   5.396  -7.490  1.00198.23           C  
ANISOU 4898  C   ALA B  93    24666  27388  23266   -757   1867   -443       C  
ATOM   4899  O   ALA B  93      20.049   4.987  -8.577  1.00199.38           O  
ANISOU 4899  O   ALA B  93    24848  27512  23395   -845   1844   -720       O  
ATOM   4900  CB  ALA B  93      19.629   7.772  -7.634  1.00191.09           C  
ANISOU 4900  CB  ALA B  93    23662  27028  21917   -724   1743   -360       C  
ATOM   4901  N   GLY B  94      20.711   4.602  -6.449  1.00196.15           N  
ANISOU 4901  N   GLY B  94    24387  26906  23234   -745   1936   -239       N  
ATOM   4902  CA  GLY B  94      20.460   3.163  -6.449  1.00199.27           C  
ANISOU 4902  CA  GLY B  94    24833  26933  23947   -845   2004   -293       C  
ATOM   4903  C   GLY B  94      18.989   2.799  -6.440  1.00205.09           C  
ANISOU 4903  C   GLY B  94    25511  27654  24761  -1110   1928   -355       C  
ATOM   4904  O   GLY B  94      18.595   1.780  -7.015  1.00207.75           O  
ANISOU 4904  O   GLY B  94    25910  27717  25310  -1270   1951   -573       O  
ATOM   4905  N   ASP B  95      18.173   3.637  -5.783  1.00200.17           N  
ANISOU 4905  N   ASP B  95    24758  27335  23962  -1161   1840   -176       N  
ATOM   4906  CA  ASP B  95      16.724   3.476  -5.659  1.00201.26           C  
ANISOU 4906  CA  ASP B  95    24790  27579  24101  -1396   1757   -171       C  
ATOM   4907  C   ASP B  95      15.989   3.825  -6.963  1.00205.38           C  
ANISOU 4907  C   ASP B  95    25313  28312  24411  -1521   1667   -502       C  
ATOM   4908  O   ASP B  95      14.854   3.383  -7.154  1.00206.91           O  
ANISOU 4908  O   ASP B  95    25423  28559  24635  -1763   1608   -587       O  
ATOM   4909  CB  ASP B  95      16.190   4.350  -4.502  1.00201.27           C  
ANISOU 4909  CB  ASP B  95    24641  27899  23934  -1338   1702    137       C  
ATOM   4910  CG  ASP B  95      16.462   5.850  -4.588  1.00209.92           C  
ANISOU 4910  CG  ASP B  95    25738  29318  24704  -1157   1656    130       C  
ATOM   4911  OD1 ASP B  95      17.331   6.259  -5.393  1.00209.66           O  
ANISOU 4911  OD1 ASP B  95    25812  29259  24589  -1046   1681    -33       O  
ATOM   4912  OD2 ASP B  95      15.848   6.606  -3.809  1.00215.58           O  
ANISOU 4912  OD2 ASP B  95    26345  30301  25264  -1117   1606    298       O  
ATOM   4913  N   SER B  96      16.632   4.614  -7.848  1.00200.21           N  
ANISOU 4913  N   SER B  96    24720  27822  23529  -1361   1661   -663       N  
ATOM   4914  CA  SER B  96      16.047   5.068  -9.108  1.00200.35           C  
ANISOU 4914  CA  SER B  96    24698  28136  23291  -1418   1592   -928       C  
ATOM   4915  C   SER B  96      16.679   4.410 -10.334  1.00205.99           C  
ANISOU 4915  C   SER B  96    25505  28722  24041  -1414   1628  -1284       C  
ATOM   4916  O   SER B  96      17.885   4.150 -10.363  1.00205.26           O  
ANISOU 4916  O   SER B  96    25526  28405  24060  -1249   1712  -1292       O  
ATOM   4917  CB  SER B  96      16.175   6.583  -9.232  1.00201.03           C  
ANISOU 4917  CB  SER B  96    24747  28567  23067  -1220   1567   -797       C  
ATOM   4918  OG  SER B  96      15.622   7.232  -8.100  1.00208.06           O  
ANISOU 4918  OG  SER B  96    25563  29577  23912  -1192   1540   -515       O  
ATOM   4919  N   ASP B  97      15.842   4.161 -11.353  1.00204.66           N  
ANISOU 4919  N   ASP B  97    25261  28758  23743  -1586   1564  -1588       N  
ATOM   4920  CA  ASP B  97      16.214   3.593 -12.651  1.00206.83           C  
ANISOU 4920  CA  ASP B  97    25577  29033  23975  -1599   1578  -2004       C  
ATOM   4921  C   ASP B  97      15.801   4.561 -13.763  1.00209.54           C  
ANISOU 4921  C   ASP B  97    25774  29950  23890  -1529   1512  -2117       C  
ATOM   4922  O   ASP B  97      16.466   4.636 -14.797  1.00209.88           O  
ANISOU 4922  O   ASP B  97    25824  30142  23779  -1390   1534  -2332       O  
ATOM   4923  CB  ASP B  97      15.565   2.210 -12.858  1.00212.91           C  
ANISOU 4923  CB  ASP B  97    26363  29522  25009  -1911   1571  -2326       C  
ATOM   4924  CG  ASP B  97      15.972   1.145 -11.853  1.00224.02           C  
ANISOU 4924  CG  ASP B  97    27910  30322  26884  -1965   1669  -2190       C  
ATOM   4925  OD1 ASP B  97      17.133   1.181 -11.379  1.00222.85           O  
ANISOU 4925  OD1 ASP B  97    27878  29945  26850  -1710   1765  -1994       O  
ATOM   4926  OD2 ASP B  97      15.146   0.249 -11.572  1.00232.81           O  
ANISOU 4926  OD2 ASP B  97    29001  31204  28253  -2265   1659  -2267       O  
ATOM   4927  N   SER B  98      14.707   5.310 -13.524  1.00204.42           N  
ANISOU 4927  N   SER B  98    24975  29654  23040  -1595   1442  -1934       N  
ATOM   4928  CA  SER B  98      14.146   6.315 -14.425  1.00203.60           C  
ANISOU 4928  CA  SER B  98    24699  30132  22527  -1502   1398  -1933       C  
ATOM   4929  C   SER B  98      14.339   7.720 -13.863  1.00202.85           C  
ANISOU 4929  C   SER B  98    24607  30166  22302  -1253   1429  -1523       C  
ATOM   4930  O   SER B  98      14.502   7.880 -12.651  1.00200.56           O  
ANISOU 4930  O   SER B  98    24403  29603  22199  -1228   1447  -1271       O  
ATOM   4931  CB  SER B  98      12.658   6.048 -14.640  1.00209.49           C  
ANISOU 4931  CB  SER B  98    25252  31217  23129  -1763   1309  -2050       C  
ATOM   4932  OG  SER B  98      12.076   7.007 -15.509  1.00218.53           O  
ANISOU 4932  OG  SER B  98    26197  32983  23852  -1641   1283  -2008       O  
ATOM   4933  N   GLN B  99      14.295   8.742 -14.742  1.00198.03           N  
ANISOU 4933  N   GLN B  99    23886  29982  21372  -1066   1442  -1456       N  
ATOM   4934  CA  GLN B  99      14.386  10.150 -14.348  1.00194.88           C  
ANISOU 4934  CA  GLN B  99    23490  29690  20864   -835   1489  -1088       C  
ATOM   4935  C   GLN B  99      13.129  10.555 -13.579  1.00197.97           C  
ANISOU 4935  C   GLN B  99    23793  30237  21188   -887   1449   -891       C  
ATOM   4936  O   GLN B  99      13.192  11.398 -12.683  1.00195.50           O  
ANISOU 4936  O   GLN B  99    23547  29807  20927   -753   1483   -619       O  
ATOM   4937  CB  GLN B  99      14.562  11.043 -15.579  1.00196.61           C  
ANISOU 4937  CB  GLN B  99    23591  30332  20782   -625   1534  -1039       C  
ATOM   4938  CG  GLN B  99      15.997  11.444 -15.839  1.00205.45           C  
ANISOU 4938  CG  GLN B  99    24819  31271  21972   -445   1610   -966       C  
ATOM   4939  CD  GLN B  99      16.065  12.513 -16.894  1.00222.07           C  
ANISOU 4939  CD  GLN B  99    26780  33798  23796   -222   1672   -794       C  
ATOM   4940  OE1 GLN B  99      15.888  13.705 -16.621  1.00215.99           O  
ANISOU 4940  OE1 GLN B  99    26006  33071  22989    -68   1733   -468       O  
ATOM   4941  NE2 GLN B  99      16.363  12.115 -18.116  1.00215.47           N  
ANISOU 4941  NE2 GLN B  99    25821  33278  22770   -182   1670  -1002       N  
ATOM   4942  N   GLU B 100      11.990   9.932 -13.938  1.00196.52           N  
ANISOU 4942  N   GLU B 100    23446  30343  20878  -1091   1376  -1052       N  
ATOM   4943  CA  GLU B 100      10.676  10.125 -13.330  1.00196.53           C  
ANISOU 4943  CA  GLU B 100    23312  30585  20773  -1172   1326   -890       C  
ATOM   4944  C   GLU B 100      10.676   9.563 -11.912  1.00198.54           C  
ANISOU 4944  C   GLU B 100    23672  30427  21336  -1303   1305   -784       C  
ATOM   4945  O   GLU B 100      10.110  10.185 -11.012  1.00196.89           O  
ANISOU 4945  O   GLU B 100    23429  30296  21082  -1215   1303   -519       O  
ATOM   4946  CB  GLU B 100       9.584   9.464 -14.188  1.00201.32           C  
ANISOU 4946  CB  GLU B 100    23688  31641  21162  -1407   1248  -1134       C  
ATOM   4947  CG  GLU B 100       9.305  10.191 -15.498  1.00213.59           C  
ANISOU 4947  CG  GLU B 100    25050  33793  22313  -1234   1271  -1153       C  
ATOM   4948  CD  GLU B 100      10.120   9.816 -16.724  1.00234.59           C  
ANISOU 4948  CD  GLU B 100    27702  36532  24901  -1216   1287  -1462       C  
ATOM   4949  OE1 GLU B 100      11.294   9.402 -16.579  1.00229.77           O  
ANISOU 4949  OE1 GLU B 100    27302  35443  24558  -1198   1320  -1574       O  
ATOM   4950  OE2 GLU B 100       9.586   9.974 -17.846  1.00228.94           O  
ANISOU 4950  OE2 GLU B 100    26742  36421  23824  -1191   1272  -1576       O  
ATOM   4951  N   GLU B 101      11.345   8.405 -11.715  1.00195.32           N  
ANISOU 4951  N   GLU B 101    23385  29594  21236  -1480   1304   -974       N  
ATOM   4952  CA  GLU B 101      11.504   7.742 -10.420  1.00194.44           C  
ANISOU 4952  CA  GLU B 101    23356  29079  21442  -1586   1307   -843       C  
ATOM   4953  C   GLU B 101      12.389   8.598  -9.513  1.00195.21           C  
ANISOU 4953  C   GLU B 101    23578  28989  21604  -1328   1368   -584       C  
ATOM   4954  O   GLU B 101      12.055   8.784  -8.343  1.00193.80           O  
ANISOU 4954  O   GLU B 101    23371  28781  21482  -1308   1360   -354       O  
ATOM   4955  CB  GLU B 101      12.097   6.332 -10.598  1.00197.74           C  
ANISOU 4955  CB  GLU B 101    23878  29074  22179  -1786   1327  -1099       C  
ATOM   4956  CG  GLU B 101      12.142   5.513  -9.314  1.00207.85           C  
ANISOU 4956  CG  GLU B 101    25204  29965  23804  -1905   1349   -917       C  
ATOM   4957  CD  GLU B 101      12.517   4.048  -9.445  1.00229.37           C  
ANISOU 4957  CD  GLU B 101    28025  32232  26892  -2113   1392  -1133       C  
ATOM   4958  OE1 GLU B 101      13.171   3.675 -10.446  1.00225.56           O  
ANISOU 4958  OE1 GLU B 101    27640  31633  26430  -2094   1422  -1451       O  
ATOM   4959  OE2 GLU B 101      12.175   3.274  -8.522  1.00222.07           O  
ANISOU 4959  OE2 GLU B 101    27075  31057  26243  -2275   1407   -966       O  
ATOM   4960  N   ALA B 102      13.496   9.136 -10.070  1.00190.55           N  
ANISOU 4960  N   ALA B 102    23099  28319  20983  -1142   1427   -631       N  
ATOM   4961  CA  ALA B 102      14.445  10.005  -9.373  1.00187.86           C  
ANISOU 4961  CA  ALA B 102    22866  27821  20691   -933   1486   -438       C  
ATOM   4962  C   ALA B 102      13.747  11.260  -8.855  1.00190.31           C  
ANISOU 4962  C   ALA B 102    23120  28366  20823   -786   1484   -220       C  
ATOM   4963  O   ALA B 102      13.942  11.625  -7.694  1.00188.50           O  
ANISOU 4963  O   ALA B 102    22927  28021  20676   -718   1496    -64       O  
ATOM   4964  CB  ALA B 102      15.592  10.378 -10.301  1.00188.16           C  
ANISOU 4964  CB  ALA B 102    22986  27818  20687   -796   1543   -529       C  
ATOM   4965  N   HIS B 103      12.886  11.874  -9.698  1.00187.58           N  
ANISOU 4965  N   HIS B 103    22668  28382  20221   -725   1475   -213       N  
ATOM   4966  CA  HIS B 103      12.108  13.070  -9.376  1.00186.88           C  
ANISOU 4966  CA  HIS B 103    22523  28535  19946   -543   1496     -5       C  
ATOM   4967  C   HIS B 103      11.136  12.804  -8.219  1.00189.76           C  
ANISOU 4967  C   HIS B 103    22802  28981  20319   -615   1439    112       C  
ATOM   4968  O   HIS B 103      10.998  13.654  -7.341  1.00188.33           O  
ANISOU 4968  O   HIS B 103    22647  28802  20110   -447   1466    272       O  
ATOM   4969  CB  HIS B 103      11.346  13.571 -10.611  1.00189.37           C  
ANISOU 4969  CB  HIS B 103    22700  29280  19971   -456   1510      2       C  
ATOM   4970  CG  HIS B 103      10.492  14.768 -10.337  1.00193.04           C  
ANISOU 4970  CG  HIS B 103    23104  29994  20247   -226   1557    244       C  
ATOM   4971  ND1 HIS B 103       9.125  14.652 -10.161  1.00196.20           N  
ANISOU 4971  ND1 HIS B 103    23327  30771  20450   -257   1508    322       N  
ATOM   4972  CD2 HIS B 103      10.845  16.064 -10.174  1.00194.14           C  
ANISOU 4972  CD2 HIS B 103    23345  30030  20388     36   1659    418       C  
ATOM   4973  CE1 HIS B 103       8.689  15.878  -9.919  1.00195.63           C  
ANISOU 4973  CE1 HIS B 103    23255  30828  20247     28   1587    546       C  
ATOM   4974  NE2 HIS B 103       9.689  16.760  -9.914  1.00194.87           N  
ANISOU 4974  NE2 HIS B 103    23337  30416  20286    206   1684    600       N  
ATOM   4975  N   GLY B 104      10.496  11.633  -8.234  1.00186.93           N  
ANISOU 4975  N   GLY B 104    22334  28687  20003   -866   1366     23       N  
ATOM   4976  CA  GLY B 104       9.560  11.195  -7.202  1.00186.91           C  
ANISOU 4976  CA  GLY B 104    22208  28791  20019   -978   1308    160       C  
ATOM   4977  C   GLY B 104      10.223  10.990  -5.854  1.00188.19           C  
ANISOU 4977  C   GLY B 104    22447  28653  20405   -951   1324    279       C  
ATOM   4978  O   GLY B 104       9.630  11.303  -4.817  1.00187.52           O  
ANISOU 4978  O   GLY B 104    22273  28722  20255   -876   1305    464       O  
ATOM   4979  N   LYS B 105      11.472  10.474  -5.867  1.00182.99           N  
ANISOU 4979  N   LYS B 105    21929  27619  19980   -988   1363    180       N  
ATOM   4980  CA  LYS B 105      12.273  10.245  -4.664  1.00181.15           C  
ANISOU 4980  CA  LYS B 105    21744  27146  19939   -945   1392    298       C  
ATOM   4981  C   LYS B 105      12.708  11.593  -4.071  1.00182.20           C  
ANISOU 4981  C   LYS B 105    21935  27336  19955   -696   1429    376       C  
ATOM   4982  O   LYS B 105      12.759  11.722  -2.851  1.00181.39           O  
ANISOU 4982  O   LYS B 105    21781  27268  19873   -631   1426    506       O  
ATOM   4983  CB  LYS B 105      13.485   9.340  -4.959  1.00183.46           C  
ANISOU 4983  CB  LYS B 105    22155  27071  20481  -1022   1440    181       C  
ATOM   4984  CG  LYS B 105      13.146   7.910  -5.411  1.00196.53           C  
ANISOU 4984  CG  LYS B 105    23783  28562  22328  -1275   1425     69       C  
ATOM   4985  CD  LYS B 105      12.565   7.028  -4.299  1.00205.62           C  
ANISOU 4985  CD  LYS B 105    24811  29657  23657  -1416   1413    279       C  
ATOM   4986  CE  LYS B 105      12.336   5.601  -4.740  1.00216.68           C  
ANISOU 4986  CE  LYS B 105    26215  30789  25326  -1689   1422    158       C  
ATOM   4987  NZ  LYS B 105      11.128   5.461  -5.596  1.00226.31           N  
ANISOU 4987  NZ  LYS B 105    27332  32249  26407  -1907   1343    -12       N  
ATOM   4988  N   LEU B 106      12.956  12.606  -4.939  1.00177.27           N  
ANISOU 4988  N   LEU B 106    21401  26746  19206   -561   1467    298       N  
ATOM   4989  CA  LEU B 106      13.298  13.980  -4.559  1.00175.68           C  
ANISOU 4989  CA  LEU B 106    21278  26544  18929   -347   1518    342       C  
ATOM   4990  C   LEU B 106      12.122  14.649  -3.850  1.00179.29           C  
ANISOU 4990  C   LEU B 106    21640  27271  19213   -216   1500    462       C  
ATOM   4991  O   LEU B 106      12.347  15.472  -2.965  1.00178.61           O  
ANISOU 4991  O   LEU B 106    21592  27159  19112    -70   1528    483       O  
ATOM   4992  CB  LEU B 106      13.727  14.815  -5.778  1.00175.56           C  
ANISOU 4992  CB  LEU B 106    21360  26493  18852   -246   1582    284       C  
ATOM   4993  CG  LEU B 106      15.127  14.537  -6.337  1.00179.51           C  
ANISOU 4993  CG  LEU B 106    21963  26747  19494   -299   1618    184       C  
ATOM   4994  CD1 LEU B 106      15.278  15.104  -7.726  1.00180.06           C  
ANISOU 4994  CD1 LEU B 106    22059  26892  19465   -221   1668    164       C  
ATOM   4995  CD2 LEU B 106      16.219  15.094  -5.423  1.00181.08           C  
ANISOU 4995  CD2 LEU B 106    22246  26748  19808   -250   1656    196       C  
ATOM   4996  N   VAL B 107      10.876  14.276  -4.221  1.00176.28           N  
ANISOU 4996  N   VAL B 107    21118  27174  18685   -273   1453    523       N  
ATOM   4997  CA  VAL B 107       9.635  14.764  -3.605  1.00176.58           C  
ANISOU 4997  CA  VAL B 107    21024  27546  18520   -143   1431    666       C  
ATOM   4998  C   VAL B 107       9.534  14.147  -2.188  1.00179.51           C  
ANISOU 4998  C   VAL B 107    21288  27954  18962   -205   1380    761       C  
ATOM   4999  O   VAL B 107       9.061  14.813  -1.265  1.00179.28           O  
ANISOU 4999  O   VAL B 107    21200  28117  18802    -21   1382    847       O  
ATOM   5000  CB  VAL B 107       8.391  14.467  -4.499  1.00182.03           C  
ANISOU 5000  CB  VAL B 107    21556  28599  19010   -215   1393    712       C  
ATOM   5001  CG1 VAL B 107       7.080  14.803  -3.792  1.00182.93           C  
ANISOU 5001  CG1 VAL B 107    21494  29116  18896    -91   1365    893       C  
ATOM   5002  CG2 VAL B 107       8.479  15.222  -5.822  1.00182.17           C  
ANISOU 5002  CG2 VAL B 107    21634  28674  18907    -87   1461    667       C  
ATOM   5003  N   LEU B 108      10.029  12.899  -2.015  1.00175.31           N  
ANISOU 5003  N   LEU B 108    20729  27240  18639   -435   1348    755       N  
ATOM   5004  CA  LEU B 108      10.055  12.214  -0.718  1.00175.04           C  
ANISOU 5004  CA  LEU B 108    20569  27240  18698   -488   1321    903       C  
ATOM   5005  C   LEU B 108      11.125  12.830   0.184  1.00176.56           C  
ANISOU 5005  C   LEU B 108    20838  27316  18931   -326   1364    870       C  
ATOM   5006  O   LEU B 108      10.880  13.036   1.373  1.00176.36           O  
ANISOU 5006  O   LEU B 108    20684  27510  18815   -216   1349    978       O  
ATOM   5007  CB  LEU B 108      10.299  10.700  -0.877  1.00176.05           C  
ANISOU 5007  CB  LEU B 108    20659  27152  19080   -763   1308    933       C  
ATOM   5008  CG  LEU B 108       9.220   9.883  -1.594  1.00182.74           C  
ANISOU 5008  CG  LEU B 108    21395  28114  19926  -1004   1255    938       C  
ATOM   5009  CD1 LEU B 108       9.758   8.529  -2.007  1.00184.21           C  
ANISOU 5009  CD1 LEU B 108    21633  27933  20425  -1260   1273    860       C  
ATOM   5010  CD2 LEU B 108       7.974   9.708  -0.724  1.00186.39           C  
ANISOU 5010  CD2 LEU B 108    21610  28951  20259  -1036   1198   1183       C  
ATOM   5011  N   TRP B 109      12.300  13.148  -0.391  1.00171.34           N  
ANISOU 5011  N   TRP B 109    20360  26364  18380   -315   1416    712       N  
ATOM   5012  CA  TRP B 109      13.408  13.770   0.329  1.00170.08           C  
ANISOU 5012  CA  TRP B 109    20266  26105  18253   -208   1456    642       C  
ATOM   5013  C   TRP B 109      13.119  15.239   0.646  1.00171.71           C  
ANISOU 5013  C   TRP B 109    20526  26423  18294      2   1478    557       C  
ATOM   5014  O   TRP B 109      13.662  15.756   1.622  1.00171.55           O  
ANISOU 5014  O   TRP B 109    20488  26443  18248     88   1490    492       O  
ATOM   5015  CB  TRP B 109      14.713  13.646  -0.460  1.00168.34           C  
ANISOU 5015  CB  TRP B 109    20201  25571  18188   -279   1504    519       C  
ATOM   5016  CG  TRP B 109      15.384  12.312  -0.316  1.00169.80           C  
ANISOU 5016  CG  TRP B 109    20342  25613  18560   -413   1513    590       C  
ATOM   5017  CD1 TRP B 109      15.470  11.333  -1.260  1.00173.16           C  
ANISOU 5017  CD1 TRP B 109    20818  25849  19125   -549   1521    559       C  
ATOM   5018  CD2 TRP B 109      16.087  11.823   0.834  1.00170.03           C  
ANISOU 5018  CD2 TRP B 109    20263  25685  18656   -395   1532    705       C  
ATOM   5019  NE1 TRP B 109      16.172  10.257  -0.766  1.00173.23           N  
ANISOU 5019  NE1 TRP B 109    20784  25717  19319   -606   1556    657       N  
ATOM   5020  CE2 TRP B 109      16.559  10.528   0.519  1.00174.58           C  
ANISOU 5020  CE2 TRP B 109    20842  26050  19440   -506   1567    779       C  
ATOM   5021  CE3 TRP B 109      16.361  12.351   2.107  1.00171.55           C  
ANISOU 5021  CE3 TRP B 109    20337  26105  18738   -284   1530    745       C  
ATOM   5022  CZ2 TRP B 109      17.283   9.750   1.431  1.00174.66           C  
ANISOU 5022  CZ2 TRP B 109    20739  26065  19559   -484   1615    952       C  
ATOM   5023  CZ3 TRP B 109      17.083  11.582   3.009  1.00173.70           C  
ANISOU 5023  CZ3 TRP B 109    20467  26452  19080   -280   1561    898       C  
ATOM   5024  CH2 TRP B 109      17.543  10.301   2.665  1.00174.87           C  
ANISOU 5024  CH2 TRP B 109    20620  26381  19443   -367   1610   1029       C  
ATOM   5025  N   SER B 110      12.238  15.905  -0.138  1.00166.70           N  
ANISOU 5025  N   SER B 110    19940  25860  17539     97   1493    554       N  
ATOM   5026  CA  SER B 110      11.868  17.305   0.102  1.00166.29           C  
ANISOU 5026  CA  SER B 110    19959  25865  17360    334   1543    493       C  
ATOM   5027  C   SER B 110      10.979  17.455   1.362  1.00168.89           C  
ANISOU 5027  C   SER B 110    20124  26533  17512    479   1504    562       C  
ATOM   5028  O   SER B 110      10.517  18.556   1.668  1.00169.58           O  
ANISOU 5028  O   SER B 110    20258  26697  17478    711   1549    502       O  
ATOM   5029  CB  SER B 110      11.193  17.920  -1.123  1.00170.55           C  
ANISOU 5029  CB  SER B 110    20571  26416  17815    434   1595    532       C  
ATOM   5030  OG  SER B 110       9.900  17.391  -1.363  1.00180.65           O  
ANISOU 5030  OG  SER B 110    21685  28028  18926    426   1544    679       O  
ATOM   5031  N   GLY B 111      10.793  16.352   2.092  1.00163.53           N  
ANISOU 5031  N   GLY B 111    19253  26050  16833    359   1434    696       N  
ATOM   5032  CA  GLY B 111      10.057  16.305   3.349  1.00163.55           C  
ANISOU 5032  CA  GLY B 111    19045  26438  16660    480   1390    805       C  
ATOM   5033  C   GLY B 111      10.934  16.729   4.509  1.00165.23           C  
ANISOU 5033  C   GLY B 111    19236  26679  16865    568   1401    667       C  
ATOM   5034  O   GLY B 111      10.468  16.832   5.647  1.00166.05           O  
ANISOU 5034  O   GLY B 111    19153  27146  16792    708   1370    715       O  
ATOM   5035  N   LEU B 112      12.224  16.979   4.212  1.00158.93           N  
ANISOU 5035  N   LEU B 112    18603  25548  16234    482   1444    491       N  
ATOM   5036  CA  LEU B 112      13.234  17.437   5.155  1.00158.34           C  
ANISOU 5036  CA  LEU B 112    18513  25492  16155    515   1457    310       C  
ATOM   5037  C   LEU B 112      13.346  18.963   5.085  1.00162.30           C  
ANISOU 5037  C   LEU B 112    19207  25830  16629    665   1518     30       C  
ATOM   5038  O   LEU B 112      14.270  19.545   5.654  1.00162.32           O  
ANISOU 5038  O   LEU B 112    19245  25772  16658    650   1538   -200       O  
ATOM   5039  CB  LEU B 112      14.579  16.744   4.889  1.00157.06           C  
ANISOU 5039  CB  LEU B 112    18386  25106  16185    316   1472    310       C  
ATOM   5040  CG  LEU B 112      14.699  15.333   5.465  1.00161.54           C  
ANISOU 5040  CG  LEU B 112    18729  25858  16789    223   1441    567       C  
ATOM   5041  CD1 LEU B 112      14.260  14.276   4.473  1.00160.97           C  
ANISOU 5041  CD1 LEU B 112    18695  25597  16870     76   1435    752       C  
ATOM   5042  CD2 LEU B 112      16.102  15.047   5.867  1.00163.70           C  
ANISOU 5042  CD2 LEU B 112    18964  26094  17140    151   1470    525       C  
ATOM   5043  N   ARG B 113      12.361  19.604   4.416  1.00159.19           N  
ANISOU 5043  N   ARG B 113    18921  25384  16181    814   1555     59       N  
ATOM   5044  CA  ARG B 113      12.200  21.051   4.294  1.00160.64           C  
ANISOU 5044  CA  ARG B 113    19294  25382  16359   1012   1643   -143       C  
ATOM   5045  C   ARG B 113      12.029  21.668   5.675  1.00167.32           C  
ANISOU 5045  C   ARG B 113    20046  26485  17043   1191   1633   -348       C  
ATOM   5046  O   ARG B 113      12.557  22.744   5.937  1.00168.24           O  
ANISOU 5046  O   ARG B 113    20316  26377  17232   1251   1698   -644       O  
ATOM   5047  CB  ARG B 113      10.957  21.368   3.439  1.00161.65           C  
ANISOU 5047  CB  ARG B 113    19469  25554  16398   1188   1687     30       C  
ATOM   5048  CG  ARG B 113      11.256  21.912   2.053  1.00173.35           C  
ANISOU 5048  CG  ARG B 113    21166  26655  18043   1167   1782     53       C  
ATOM   5049  CD  ARG B 113       9.997  22.424   1.383  1.00187.01           C  
ANISOU 5049  CD  ARG B 113    22908  28516  19633   1412   1847    224       C  
ATOM   5050  NE  ARG B 113       9.574  21.568   0.274  1.00196.63           N  
ANISOU 5050  NE  ARG B 113    24039  29862  20808   1282   1809    445       N  
ATOM   5051  CZ  ARG B 113       9.905  21.766  -1.000  1.00212.62           C  
ANISOU 5051  CZ  ARG B 113    26174  31676  22935   1239   1876    505       C  
ATOM   5052  NH1 ARG B 113       9.469  20.938  -1.940  1.00200.40           N  
ANISOU 5052  NH1 ARG B 113    24515  30320  21308   1117   1830    654       N  
ATOM   5053  NH2 ARG B 113      10.677  22.792  -1.343  1.00200.99           N  
ANISOU 5053  NH2 ARG B 113    24907  29818  21642   1306   1992    410       N  
ATOM   5054  N   ASN B 114      11.273  20.982   6.555  1.00165.19           N  
ANISOU 5054  N   ASN B 114    19511  26700  16555   1272   1553   -196       N  
ATOM   5055  CA  ASN B 114      10.917  21.417   7.905  1.00167.55           C  
ANISOU 5055  CA  ASN B 114    19647  27391  16622   1483   1529   -350       C  
ATOM   5056  C   ASN B 114      12.123  21.604   8.851  1.00173.15           C  
ANISOU 5056  C   ASN B 114    20298  28144  17345   1386   1513   -641       C  
ATOM   5057  O   ASN B 114      12.016  22.404   9.781  1.00175.06           O  
ANISOU 5057  O   ASN B 114    20499  28584  17432   1568   1522   -927       O  
ATOM   5058  CB  ASN B 114       9.898  20.456   8.518  1.00168.35           C  
ANISOU 5058  CB  ASN B 114    19430  28042  16494   1553   1445    -31       C  
ATOM   5059  CG  ASN B 114       8.588  20.390   7.751  1.00188.77           C  
ANISOU 5059  CG  ASN B 114    22021  30708  18995   1662   1454    220       C  
ATOM   5060  OD1 ASN B 114       8.077  21.394   7.231  1.00182.10           O  
ANISOU 5060  OD1 ASN B 114    21359  29704  18125   1869   1535    123       O  
ATOM   5061  ND2 ASN B 114       8.001  19.204   7.679  1.00179.65           N  
ANISOU 5061  ND2 ASN B 114    20646  29820  17794   1527   1382    561       N  
ATOM   5062  N   ALA B 115      13.257  20.904   8.611  1.00168.88           N  
ANISOU 5062  N   ALA B 115    19746  27453  16969   1116   1493   -591       N  
ATOM   5063  CA  ALA B 115      14.479  21.042   9.417  1.00169.94           C  
ANISOU 5063  CA  ALA B 115    19794  27679  17095   1001   1480   -842       C  
ATOM   5064  C   ALA B 115      15.451  22.027   8.726  1.00175.35           C  
ANISOU 5064  C   ALA B 115    20777  27834  18016    861   1555  -1145       C  
ATOM   5065  O   ALA B 115      16.058  21.655   7.721  1.00173.08           O  
ANISOU 5065  O   ALA B 115    20617  27211  17934    677   1578  -1009       O  
ATOM   5066  CB  ALA B 115      15.134  19.681   9.628  1.00169.14           C  
ANISOU 5066  CB  ALA B 115    19471  27784  17013    826   1433   -561       C  
ATOM   5067  N   PRO B 116      15.590  23.289   9.215  1.00175.64           N  
ANISOU 5067  N   PRO B 116    20924  27772  18038    944   1600  -1556       N  
ATOM   5068  CA  PRO B 116      16.453  24.264   8.518  1.00176.66           C  
ANISOU 5068  CA  PRO B 116    21339  27346  18438    788   1686  -1810       C  
ATOM   5069  C   PRO B 116      17.942  23.933   8.472  1.00181.15           C  
ANISOU 5069  C   PRO B 116    21855  27859  19114    476   1665  -1877       C  
ATOM   5070  O   PRO B 116      18.589  24.246   7.471  1.00179.72           O  
ANISOU 5070  O   PRO B 116    21880  27226  19180    312   1725  -1859       O  
ATOM   5071  CB  PRO B 116      16.241  25.562   9.309  1.00182.15           C  
ANISOU 5071  CB  PRO B 116    22118  28005  19084    938   1735  -2267       C  
ATOM   5072  CG  PRO B 116      14.971  25.371  10.052  1.00187.20           C  
ANISOU 5072  CG  PRO B 116    22586  29107  19433   1254   1695  -2187       C  
ATOM   5073  CD  PRO B 116      14.917  23.913  10.372  1.00180.24           C  
ANISOU 5073  CD  PRO B 116    21389  28720  18375   1192   1587  -1813       C  
ATOM   5074  N   ARG B 117      18.486  23.344   9.547  1.00179.66           N  
ANISOU 5074  N   ARG B 117    21370  28170  18722    414   1588  -1935       N  
ATOM   5075  CA  ARG B 117      19.916  23.043   9.639  1.00180.03           C  
ANISOU 5075  CA  ARG B 117    21316  28273  18813    146   1572  -1997       C  
ATOM   5076  C   ARG B 117      20.316  21.855   8.753  1.00182.55           C  
ANISOU 5076  C   ARG B 117    21621  28495  19246     41   1568  -1571       C  
ATOM   5077  O   ARG B 117      21.432  21.839   8.233  1.00181.69           O  
ANISOU 5077  O   ARG B 117    21567  28195  19272   -168   1592  -1586       O  
ATOM   5078  CB  ARG B 117      20.338  22.802  11.106  1.00181.98           C  
ANISOU 5078  CB  ARG B 117    21205  29177  18761    154   1505  -2172       C  
ATOM   5079  CG  ARG B 117      20.586  24.079  11.944  1.00194.47           C  
ANISOU 5079  CG  ARG B 117    22797  30831  20261    126   1511  -2753       C  
ATOM   5080  CD  ARG B 117      21.929  24.743  11.692  1.00203.19           C  
ANISOU 5080  CD  ARG B 117    23997  31671  21537   -201   1542  -3062       C  
ATOM   5081  NE  ARG B 117      22.757  24.770  12.905  1.00210.17           N  
ANISOU 5081  NE  ARG B 117    24549  33155  22152   -320   1482  -3374       N  
ATOM   5082  CZ  ARG B 117      23.998  25.254  12.962  1.00222.02           C  
ANISOU 5082  CZ  ARG B 117    26019  34626  23710   -634   1487  -3672       C  
ATOM   5083  NH1 ARG B 117      24.562  25.792  11.879  1.00208.21           N  
ANISOU 5083  NH1 ARG B 117    24568  32238  22306   -861   1554  -3687       N  
ATOM   5084  NH2 ARG B 117      24.672  25.221  14.106  1.00208.04           N  
ANISOU 5084  NH2 ARG B 117    23894  33514  21637   -727   1426  -3949       N  
ATOM   5085  N   CYS B 118      19.410  20.884   8.567  1.00178.82           N  
ANISOU 5085  N   CYS B 118    21075  28147  18723    178   1542  -1211       N  
ATOM   5086  CA  CYS B 118      19.656  19.708   7.728  1.00177.05           C  
ANISOU 5086  CA  CYS B 118    20852  27797  18623     93   1545   -846       C  
ATOM   5087  C   CYS B 118      19.346  20.009   6.248  1.00180.70           C  
ANISOU 5087  C   CYS B 118    21612  27744  19300     64   1594   -778       C  
ATOM   5088  O   CYS B 118      20.122  19.605   5.375  1.00179.28           O  
ANISOU 5088  O   CYS B 118    21514  27337  19269    -74   1620   -673       O  
ATOM   5089  CB  CYS B 118      18.863  18.505   8.236  1.00177.07           C  
ANISOU 5089  CB  CYS B 118    20622  28153  18504    210   1501   -509       C  
ATOM   5090  SG  CYS B 118      18.695  17.150   7.040  1.00178.75           S  
ANISOU 5090  SG  CYS B 118    20910  28086  18921    129   1516   -116       S  
ATOM   5091  N   TRP B 119      18.221  20.715   5.971  1.00178.22           N  
ANISOU 5091  N   TRP B 119    21436  27302  18978    220   1616   -822       N  
ATOM   5092  CA  TRP B 119      17.770  21.065   4.611  1.00177.30           C  
ANISOU 5092  CA  TRP B 119    21556  26796  19015    243   1673   -724       C  
ATOM   5093  C   TRP B 119      18.811  21.885   3.846  1.00180.77           C  
ANISOU 5093  C   TRP B 119    22193  26834  19657     99   1747   -867       C  
ATOM   5094  O   TRP B 119      18.962  21.692   2.636  1.00179.02           O  
ANISOU 5094  O   TRP B 119    22085  26374  19560     46   1783   -705       O  
ATOM   5095  CB  TRP B 119      16.428  21.823   4.648  1.00177.50           C  
ANISOU 5095  CB  TRP B 119    21657  26832  18955    482   1702   -749       C  
ATOM   5096  CG  TRP B 119      15.794  22.111   3.310  1.00178.06           C  
ANISOU 5096  CG  TRP B 119    21906  26629  19120    555   1767   -587       C  
ATOM   5097  CD1 TRP B 119      15.444  23.337   2.822  1.00182.58           C  
ANISOU 5097  CD1 TRP B 119    22677  26920  19776    699   1872   -669       C  
ATOM   5098  CD2 TRP B 119      15.391  21.153   2.312  1.00176.09           C  
ANISOU 5098  CD2 TRP B 119    21626  26404  18876    505   1742   -313       C  
ATOM   5099  NE1 TRP B 119      14.869  23.206   1.577  1.00181.16           N  
ANISOU 5099  NE1 TRP B 119    22564  26646  19623    757   1914   -426       N  
ATOM   5100  CE2 TRP B 119      14.813  21.877   1.245  1.00180.44           C  
ANISOU 5100  CE2 TRP B 119    22331  26756  19470    627   1826   -238       C  
ATOM   5101  CE3 TRP B 119      15.470  19.751   2.210  1.00175.73           C  
ANISOU 5101  CE3 TRP B 119    21435  26520  18815    369   1667   -134       C  
ATOM   5102  CZ2 TRP B 119      14.325  21.252   0.091  1.00178.54           C  
ANISOU 5102  CZ2 TRP B 119    22075  26550  19211    605   1820    -22       C  
ATOM   5103  CZ3 TRP B 119      14.991  19.134   1.063  1.00176.14           C  
ANISOU 5103  CZ3 TRP B 119    21508  26525  18892    327   1664     42       C  
ATOM   5104  CH2 TRP B 119      14.429  19.881   0.020  1.00177.17           C  
ANISOU 5104  CH2 TRP B 119    21766  26532  19020    438   1731     82       C  
ATOM   5105  N   ALA B 120      19.535  22.773   4.556  1.00178.79           N  
ANISOU 5105  N   ALA B 120    21959  26544  19431     22   1767  -1174       N  
ATOM   5106  CA  ALA B 120      20.563  23.641   3.983  1.00179.37           C  
ANISOU 5106  CA  ALA B 120    22194  26245  19713   -156   1840  -1324       C  
ATOM   5107  C   ALA B 120      21.732  22.852   3.367  1.00180.81           C  
ANISOU 5107  C   ALA B 120    22315  26426  19958   -359   1823  -1164       C  
ATOM   5108  O   ALA B 120      22.260  23.274   2.337  1.00180.40           O  
ANISOU 5108  O   ALA B 120    22407  26053  20083   -455   1888  -1104       O  
ATOM   5109  CB  ALA B 120      21.085  24.593   5.050  1.00183.15           C  
ANISOU 5109  CB  ALA B 120    22652  26756  20181   -242   1847  -1728       C  
ATOM   5110  N   VAL B 121      22.121  21.715   3.980  1.00175.81           N  
ANISOU 5110  N   VAL B 121    21459  26162  19181   -396   1751  -1064       N  
ATOM   5111  CA  VAL B 121      23.247  20.906   3.497  1.00174.33           C  
ANISOU 5111  CA  VAL B 121    21198  26008  19031   -540   1748   -910       C  
ATOM   5112  C   VAL B 121      22.802  19.686   2.663  1.00176.48           C  
ANISOU 5112  C   VAL B 121    21474  26257  19322   -458   1737   -599       C  
ATOM   5113  O   VAL B 121      23.608  19.188   1.870  1.00175.35           O  
ANISOU 5113  O   VAL B 121    21351  26022  19253   -539   1760   -481       O  
ATOM   5114  CB  VAL B 121      24.211  20.456   4.631  1.00178.87           C  
ANISOU 5114  CB  VAL B 121    21516  26992  19455   -634   1706   -984       C  
ATOM   5115  CG1 VAL B 121      24.989  21.635   5.204  1.00181.29           C  
ANISOU 5115  CG1 VAL B 121    21813  27304  19764   -807   1718  -1336       C  
ATOM   5116  CG2 VAL B 121      23.483  19.692   5.732  1.00178.61           C  
ANISOU 5116  CG2 VAL B 121    21265  27369  19228   -478   1651   -896       C  
ATOM   5117  N   ILE B 122      21.559  19.191   2.847  1.00172.61           N  
ANISOU 5117  N   ILE B 122    20952  25870  18760   -310   1704   -483       N  
ATOM   5118  CA  ILE B 122      21.103  18.006   2.115  1.00170.91           C  
ANISOU 5118  CA  ILE B 122    20730  25630  18580   -278   1690   -238       C  
ATOM   5119  C   ILE B 122      20.753  18.342   0.644  1.00174.59           C  
ANISOU 5119  C   ILE B 122    21388  25803  19145   -267   1731   -195       C  
ATOM   5120  O   ILE B 122      21.009  17.506  -0.227  1.00173.30           O  
ANISOU 5120  O   ILE B 122    21240  25567  19038   -306   1736    -76       O  
ATOM   5121  CB  ILE B 122      19.958  17.242   2.841  1.00173.83           C  
ANISOU 5121  CB  ILE B 122    20954  26249  18844   -172   1638   -101       C  
ATOM   5122  CG1 ILE B 122      19.921  15.754   2.405  1.00173.25           C  
ANISOU 5122  CG1 ILE B 122    20819  26160  18847   -211   1631    131       C  
ATOM   5123  CG2 ILE B 122      18.588  17.929   2.721  1.00174.78           C  
ANISOU 5123  CG2 ILE B 122    21148  26364  18898    -43   1629   -130       C  
ATOM   5124  CD1 ILE B 122      19.336  14.788   3.426  1.00181.33           C  
ANISOU 5124  CD1 ILE B 122    21627  27462  19809   -163   1597    320       C  
ATOM   5125  N   GLN B 123      20.204  19.555   0.373  1.00172.20           N  
ANISOU 5125  N   GLN B 123    21218  25353  18859   -194   1771   -288       N  
ATOM   5126  CA  GLN B 123      19.808  20.010  -0.967  1.00171.96           C  
ANISOU 5126  CA  GLN B 123    21330  25113  18892   -142   1828   -205       C  
ATOM   5127  C   GLN B 123      20.922  19.825  -2.028  1.00176.02           C  
ANISOU 5127  C   GLN B 123    21891  25481  19507   -255   1865   -148       C  
ATOM   5128  O   GLN B 123      20.624  19.191  -3.044  1.00174.81           O  
ANISOU 5128  O   GLN B 123    21742  25341  19337   -229   1863    -29       O  
ATOM   5129  CB  GLN B 123      19.335  21.470  -0.948  1.00174.86           C  
ANISOU 5129  CB  GLN B 123    21829  25306  19301    -31   1904   -295       C  
ATOM   5130  CG  GLN B 123      17.885  21.624  -0.554  1.00190.49           C  
ANISOU 5130  CG  GLN B 123    23787  27438  21151    165   1891   -264       C  
ATOM   5131  CD  GLN B 123      17.422  23.052  -0.667  1.00212.98           C  
ANISOU 5131  CD  GLN B 123    26788  30071  24062    324   1996   -327       C  
ATOM   5132  OE1 GLN B 123      16.739  23.426  -1.624  1.00209.81           O  
ANISOU 5132  OE1 GLN B 123    26455  29603  23662    465   2067   -164       O  
ATOM   5133  NE2 GLN B 123      17.756  23.876   0.321  1.00206.65           N  
ANISOU 5133  NE2 GLN B 123    26032  29174  23310    320   2020   -569       N  
ATOM   5134  N   PRO B 124      22.192  20.296  -1.832  1.00173.68           N  
ANISOU 5134  N   PRO B 124    21603  25096  19291   -385   1895   -236       N  
ATOM   5135  CA  PRO B 124      23.216  20.079  -2.873  1.00173.27           C  
ANISOU 5135  CA  PRO B 124    21566  24965  19302   -470   1929   -146       C  
ATOM   5136  C   PRO B 124      23.611  18.614  -3.048  1.00176.04           C  
ANISOU 5136  C   PRO B 124    21818  25470  19599   -483   1884    -63       C  
ATOM   5137  O   PRO B 124      23.975  18.226  -4.156  1.00175.21           O  
ANISOU 5137  O   PRO B 124    21732  25333  19505   -475   1907     21       O  
ATOM   5138  CB  PRO B 124      24.417  20.895  -2.378  1.00176.41           C  
ANISOU 5138  CB  PRO B 124    21956  25294  19778   -631   1960   -266       C  
ATOM   5139  CG  PRO B 124      23.884  21.804  -1.333  1.00182.23           C  
ANISOU 5139  CG  PRO B 124    22729  25983  20526   -619   1962   -455       C  
ATOM   5140  CD  PRO B 124      22.756  21.068  -0.704  1.00176.73           C  
ANISOU 5140  CD  PRO B 124    21965  25487  19695   -473   1897   -436       C  
ATOM   5141  N   LEU B 125      23.547  17.812  -1.966  1.00172.63           N  
ANISOU 5141  N   LEU B 125    21271  25209  19111   -484   1832    -78       N  
ATOM   5142  CA  LEU B 125      23.892  16.391  -1.989  1.00172.03           C  
ANISOU 5142  CA  LEU B 125    21108  25228  19028   -474   1816     23       C  
ATOM   5143  C   LEU B 125      22.885  15.590  -2.824  1.00176.28           C  
ANISOU 5143  C   LEU B 125    21692  25706  19579   -414   1799     87       C  
ATOM   5144  O   LEU B 125      23.297  14.758  -3.636  1.00175.60           O  
ANISOU 5144  O   LEU B 125    21620  25571  19530   -411   1816    120       O  
ATOM   5145  CB  LEU B 125      23.979  15.829  -0.553  1.00172.33           C  
ANISOU 5145  CB  LEU B 125    20985  25481  19011   -468   1786     47       C  
ATOM   5146  CG  LEU B 125      24.279  14.326  -0.403  1.00176.84           C  
ANISOU 5146  CG  LEU B 125    21458  26117  19615   -429   1798    203       C  
ATOM   5147  CD1 LEU B 125      25.697  13.988  -0.837  1.00177.25           C  
ANISOU 5147  CD1 LEU B 125    21490  26174  19685   -444   1851    243       C  
ATOM   5148  CD2 LEU B 125      24.050  13.869   1.011  1.00179.88           C  
ANISOU 5148  CD2 LEU B 125    21661  26749  19938   -388   1779    290       C  
ATOM   5149  N   LEU B 126      21.577  15.855  -2.632  1.00173.80           N  
ANISOU 5149  N   LEU B 126    21390  25425  19222   -365   1766     83       N  
ATOM   5150  CA  LEU B 126      20.489  15.164  -3.329  1.00173.95           C  
ANISOU 5150  CA  LEU B 126    21416  25453  19224   -344   1739    125       C  
ATOM   5151  C   LEU B 126      20.510  15.435  -4.836  1.00178.88           C  
ANISOU 5151  C   LEU B 126    22122  26013  19832   -325   1770    105       C  
ATOM   5152  O   LEU B 126      20.325  14.492  -5.606  1.00178.35           O  
ANISOU 5152  O   LEU B 126    22044  25951  19771   -350   1757     87       O  
ATOM   5153  CB  LEU B 126      19.118  15.531  -2.734  1.00174.26           C  
ANISOU 5153  CB  LEU B 126    21415  25618  19177   -286   1700    149       C  
ATOM   5154  CG  LEU B 126      18.863  15.077  -1.290  1.00179.08           C  
ANISOU 5154  CG  LEU B 126    21894  26383  19767   -284   1660    202       C  
ATOM   5155  CD1 LEU B 126      17.736  15.861  -0.668  1.00179.78           C  
ANISOU 5155  CD1 LEU B 126    21949  26626  19733   -184   1635    197       C  
ATOM   5156  CD2 LEU B 126      18.592  13.578  -1.211  1.00181.42           C  
ANISOU 5156  CD2 LEU B 126    22099  26693  20138   -353   1636    315       C  
ATOM   5157  N   CYS B 127      20.765  16.694  -5.258  1.00176.85           N  
ANISOU 5157  N   CYS B 127    21933  25700  19561   -280   1821    107       N  
ATOM   5158  CA  CYS B 127      20.852  17.032  -6.683  1.00177.56           C  
ANISOU 5158  CA  CYS B 127    22059  25788  19617   -235   1867    146       C  
ATOM   5159  C   CYS B 127      22.063  16.334  -7.295  1.00181.09           C  
ANISOU 5159  C   CYS B 127    22491  26217  20097   -282   1880    127       C  
ATOM   5160  O   CYS B 127      21.939  15.763  -8.371  1.00181.09           O  
ANISOU 5160  O   CYS B 127    22471  26296  20037   -253   1879    107       O  
ATOM   5161  CB  CYS B 127      20.901  18.542  -6.906  1.00179.03           C  
ANISOU 5161  CB  CYS B 127    22313  25882  19827   -170   1944    211       C  
ATOM   5162  SG  CYS B 127      19.281  19.359  -6.857  1.00183.88           S  
ANISOU 5162  SG  CYS B 127    22947  26564  20357    -13   1966    276       S  
ATOM   5163  N   ALA B 128      23.195  16.298  -6.563  1.00177.16           N  
ANISOU 5163  N   ALA B 128    21982  25663  19668   -345   1891    119       N  
ATOM   5164  CA  ALA B 128      24.444  15.649  -6.976  1.00176.95           C  
ANISOU 5164  CA  ALA B 128    21925  25654  19655   -361   1914    126       C  
ATOM   5165  C   ALA B 128      24.318  14.118  -7.127  1.00180.85           C  
ANISOU 5165  C   ALA B 128    22396  26154  20165   -336   1891     78       C  
ATOM   5166  O   ALA B 128      25.163  13.510  -7.789  1.00180.70           O  
ANISOU 5166  O   ALA B 128    22368  26150  20140   -296   1922     63       O  
ATOM   5167  CB  ALA B 128      25.541  15.969  -5.978  1.00177.76           C  
ANISOU 5167  CB  ALA B 128    21982  25764  19795   -435   1928    139       C  
ATOM   5168  N   VAL B 129      23.280  13.499  -6.519  1.00177.62           N  
ANISOU 5168  N   VAL B 129    21976  25725  19788   -356   1846     56       N  
ATOM   5169  CA  VAL B 129      23.052  12.049  -6.579  1.00178.14           C  
ANISOU 5169  CA  VAL B 129    22032  25723  19931   -366   1838     15       C  
ATOM   5170  C   VAL B 129      21.889  11.722  -7.549  1.00183.49           C  
ANISOU 5170  C   VAL B 129    22725  26431  20562   -394   1801    -93       C  
ATOM   5171  O   VAL B 129      22.068  10.907  -8.457  1.00183.97           O  
ANISOU 5171  O   VAL B 129    22806  26458  20637   -389   1814   -215       O  
ATOM   5172  CB  VAL B 129      22.818  11.446  -5.161  1.00181.74           C  
ANISOU 5172  CB  VAL B 129    22422  26154  20476   -395   1826    109       C  
ATOM   5173  CG1 VAL B 129      22.365   9.987  -5.234  1.00182.61           C  
ANISOU 5173  CG1 VAL B 129    22531  26129  20725   -428   1832     96       C  
ATOM   5174  CG2 VAL B 129      24.071  11.568  -4.296  1.00181.36           C  
ANISOU 5174  CG2 VAL B 129    22312  26162  20436   -360   1868    202       C  
ATOM   5175  N   TYR B 130      20.720  12.362  -7.353  1.00180.56           N  
ANISOU 5175  N   TYR B 130    22330  26159  20115   -414   1759    -64       N  
ATOM   5176  CA  TYR B 130      19.514  12.127  -8.141  1.00181.52           C  
ANISOU 5176  CA  TYR B 130    22420  26402  20149   -452   1718   -144       C  
ATOM   5177  C   TYR B 130      19.565  12.740  -9.544  1.00186.25           C  
ANISOU 5177  C   TYR B 130    23012  27161  20593   -377   1742   -192       C  
ATOM   5178  O   TYR B 130      19.234  12.040 -10.504  1.00187.04           O  
ANISOU 5178  O   TYR B 130    23075  27360  20632   -412   1722   -341       O  
ATOM   5179  CB  TYR B 130      18.264  12.594  -7.391  1.00182.64           C  
ANISOU 5179  CB  TYR B 130    22507  26657  20229   -465   1675    -55       C  
ATOM   5180  CG  TYR B 130      17.890  11.650  -6.271  1.00184.80           C  
ANISOU 5180  CG  TYR B 130    22730  26858  20628   -559   1640     -5       C  
ATOM   5181  CD1 TYR B 130      17.356  10.395  -6.543  1.00188.19           C  
ANISOU 5181  CD1 TYR B 130    23124  27231  21147   -694   1613    -81       C  
ATOM   5182  CD2 TYR B 130      18.165  11.965  -4.945  1.00184.92           C  
ANISOU 5182  CD2 TYR B 130    22717  26860  20682   -519   1645    117       C  
ATOM   5183  CE1 TYR B 130      17.035   9.509  -5.519  1.00189.74           C  
ANISOU 5183  CE1 TYR B 130    23260  27336  21495   -782   1601     23       C  
ATOM   5184  CE2 TYR B 130      17.811  11.103  -3.908  1.00186.40           C  
ANISOU 5184  CE2 TYR B 130    22817  27039  20967   -580   1625    220       C  
ATOM   5185  CZ  TYR B 130      17.259   9.869  -4.201  1.00195.82           C  
ANISOU 5185  CZ  TYR B 130    23978  28146  22278   -710   1609    202       C  
ATOM   5186  OH  TYR B 130      16.950   9.009  -3.177  1.00198.71           O  
ANISOU 5186  OH  TYR B 130    24245  28479  22776   -772   1608    361       O  
ATOM   5187  N   MET B 131      19.983  14.009  -9.682  1.00182.66           N  
ANISOU 5187  N   MET B 131    22578  26742  20082   -278   1790    -72       N  
ATOM   5188  CA  MET B 131      20.082  14.651 -11.000  1.00183.55           C  
ANISOU 5188  CA  MET B 131    22653  27034  20053   -181   1833    -40       C  
ATOM   5189  C   MET B 131      21.542  15.092 -11.266  1.00187.80           C  
ANISOU 5189  C   MET B 131    23223  27492  20641   -138   1895     28       C  
ATOM   5190  O   MET B 131      21.799  16.294 -11.309  1.00187.38           O  
ANISOU 5190  O   MET B 131    23183  27419  20593    -84   1954    183       O  
ATOM   5191  CB  MET B 131      19.106  15.836 -11.092  1.00186.22           C  
ANISOU 5191  CB  MET B 131    22964  27505  20288    -86   1862    109       C  
ATOM   5192  CG  MET B 131      17.664  15.418 -11.272  1.00190.70           C  
ANISOU 5192  CG  MET B 131    23441  28298  20718   -106   1807     60       C  
ATOM   5193  SD  MET B 131      16.477  16.729 -10.891  1.00195.29           S  
ANISOU 5193  SD  MET B 131    24002  29001  21200     44   1850    264       S  
ATOM   5194  CE  MET B 131      16.491  17.634 -12.404  1.00193.58           C  
ANISOU 5194  CE  MET B 131    23699  29041  20812    229   1949    426       C  
ATOM   5195  N   PRO B 132      22.529  14.163 -11.391  1.00184.93           N  
ANISOU 5195  N   PRO B 132    22867  27069  20328   -160   1894    -69       N  
ATOM   5196  CA  PRO B 132      23.920  14.608 -11.588  1.00185.01           C  
ANISOU 5196  CA  PRO B 132    22876  27064  20357   -122   1951     25       C  
ATOM   5197  C   PRO B 132      24.244  14.964 -13.035  1.00191.06           C  
ANISOU 5197  C   PRO B 132    23561  28063  20970    -16   1993     73       C  
ATOM   5198  O   PRO B 132      23.506  14.594 -13.943  1.00191.60           O  
ANISOU 5198  O   PRO B 132    23567  28332  20900     36   1973    -26       O  
ATOM   5199  CB  PRO B 132      24.749  13.413 -11.116  1.00186.60           C  
ANISOU 5199  CB  PRO B 132    23098  27155  20647   -142   1945    -71       C  
ATOM   5200  CG  PRO B 132      23.852  12.237 -11.228  1.00191.45           C  
ANISOU 5200  CG  PRO B 132    23728  27731  21285   -172   1901   -248       C  
ATOM   5201  CD  PRO B 132      22.438  12.688 -11.359  1.00186.94           C  
ANISOU 5201  CD  PRO B 132    23132  27257  20640   -212   1857   -254       C  
ATOM   5202  N   LYS B 133      25.361  15.678 -13.244  1.00188.64           N  
ANISOU 5202  N   LYS B 133    23226  27775  20673      8   2051    230       N  
ATOM   5203  CA  LYS B 133      25.807  16.088 -14.571  1.00190.14           C  
ANISOU 5203  CA  LYS B 133    23305  28226  20716    121   2103    342       C  
ATOM   5204  C   LYS B 133      26.433  14.914 -15.321  1.00195.76           C  
ANISOU 5204  C   LYS B 133    23959  29112  21310    206   2088    171       C  
ATOM   5205  O   LYS B 133      27.352  14.262 -14.817  1.00194.84           O  
ANISOU 5205  O   LYS B 133    23880  28886  21266    190   2089    114       O  
ATOM   5206  CB  LYS B 133      26.797  17.267 -14.484  1.00192.96           C  
ANISOU 5206  CB  LYS B 133    23638  28528  21151     85   2176    596       C  
ATOM   5207  CG  LYS B 133      27.256  17.804 -15.839  1.00208.02           C  
ANISOU 5207  CG  LYS B 133    25396  30729  22915    207   2245    797       C  
ATOM   5208  CD  LYS B 133      28.250  18.938 -15.689  1.00218.83           C  
ANISOU 5208  CD  LYS B 133    26737  31999  24408    123   2322   1064       C  
ATOM   5209  CE  LYS B 133      28.706  19.463 -17.025  1.00231.64           C  
ANISOU 5209  CE  LYS B 133    28180  33937  25894    249   2400   1326       C  
ATOM   5210  NZ  LYS B 133      29.624  20.619 -16.867  1.00241.97           N  
ANISOU 5210  NZ  LYS B 133    29457  35109  27370    124   2484   1615       N  
ATOM   5211  N   CYS B 134      25.924  14.659 -16.532  1.00194.72           N  
ANISOU 5211  N   CYS B 134    23723  29284  20980    315   2084     84       N  
ATOM   5212  CA  CYS B 134      26.436  13.638 -17.436  1.00196.47           C  
ANISOU 5212  CA  CYS B 134    23875  29721  21055    426   2077   -124       C  
ATOM   5213  C   CYS B 134      26.911  14.326 -18.713  1.00202.06           C  
ANISOU 5213  C   CYS B 134    24392  30845  21536    583   2132     58       C  
ATOM   5214  O   CYS B 134      26.144  15.061 -19.337  1.00202.36           O  
ANISOU 5214  O   CYS B 134    24321  31118  21448    632   2151    194       O  
ATOM   5215  CB  CYS B 134      25.390  12.565 -17.724  1.00197.89           C  
ANISOU 5215  CB  CYS B 134    24071  29935  21181    397   2013   -466       C  
ATOM   5216  SG  CYS B 134      26.080  10.994 -18.313  1.00203.93           S  
ANISOU 5216  SG  CYS B 134    24854  30724  21905    491   2010   -840       S  
ATOM   5217  N   GLU B 135      28.184  14.124 -19.079  1.00199.47           N  
ANISOU 5217  N   GLU B 135    24001  30644  21146    678   2168    108       N  
ATOM   5218  CA  GLU B 135      28.755  14.731 -20.277  1.00201.21           C  
ANISOU 5218  CA  GLU B 135    24006  31303  21140    838   2224    322       C  
ATOM   5219  C   GLU B 135      29.730  13.763 -20.946  1.00207.27           C  
ANISOU 5219  C   GLU B 135    24696  32319  21739   1004   2228    138       C  
ATOM   5220  O   GLU B 135      30.675  13.283 -20.308  1.00206.35           O  
ANISOU 5220  O   GLU B 135    24665  32005  21733    992   2238    114       O  
ATOM   5221  CB  GLU B 135      29.433  16.072 -19.940  1.00202.07           C  
ANISOU 5221  CB  GLU B 135    24081  31322  21375    764   2295    750       C  
ATOM   5222  CG  GLU B 135      29.355  17.088 -21.068  1.00213.01           C  
ANISOU 5222  CG  GLU B 135    25248  33092  22595    888   2370   1082       C  
ATOM   5223  CD  GLU B 135      29.665  18.522 -20.682  1.00228.35           C  
ANISOU 5223  CD  GLU B 135    27193  34824  24744    774   2456   1501       C  
ATOM   5224  OE1 GLU B 135      30.790  18.782 -20.198  1.00220.28           O  
ANISOU 5224  OE1 GLU B 135    26186  33660  23849    661   2477   1631       O  
ATOM   5225  OE2 GLU B 135      28.795  19.395 -20.903  1.00220.00           O  
ANISOU 5225  OE2 GLU B 135    26109  33760  23720    802   2513   1704       O  
ATOM   5226  N   ASN B 136      29.467  13.454 -22.236  1.00206.51           N  
ANISOU 5226  N   ASN B 136    24420  32695  21348   1181   2224     -5       N  
ATOM   5227  CA  ASN B 136      30.264  12.567 -23.094  1.00208.75           C  
ANISOU 5227  CA  ASN B 136    24599  33310  21409   1393   2232   -227       C  
ATOM   5228  C   ASN B 136      30.460  11.179 -22.431  1.00212.67           C  
ANISOU 5228  C   ASN B 136    25315  33418  22072   1374   2206   -625       C  
ATOM   5229  O   ASN B 136      31.592  10.763 -22.160  1.00212.27           O  
ANISOU 5229  O   ASN B 136    25299  33295  22058   1471   2247   -592       O  
ATOM   5230  CB  ASN B 136      31.614  13.240 -23.437  1.00210.55           C  
ANISOU 5230  CB  ASN B 136    24658  33807  21534   1511   2302    157       C  
ATOM   5231  CG  ASN B 136      32.548  12.452 -24.305  1.00237.00           C  
ANISOU 5231  CG  ASN B 136    27872  37557  24622   1771   2321     -9       C  
ATOM   5232  OD1 ASN B 136      32.144  11.812 -25.277  1.00234.01           O  
ANISOU 5232  OD1 ASN B 136    27386  37534  23992   1936   2298   -333       O  
ATOM   5233  ND2 ASN B 136      33.822  12.469 -23.952  1.00228.82           N  
ANISOU 5233  ND2 ASN B 136    26823  36497  23622   1817   2365    189       N  
ATOM   5234  N   ASP B 137      29.329  10.487 -22.150  1.00209.56           N  
ANISOU 5234  N   ASP B 137    25055  32779  21788   1248   2149   -963       N  
ATOM   5235  CA  ASP B 137      29.235   9.160 -21.515  1.00209.84           C  
ANISOU 5235  CA  ASP B 137    25306  32381  22042   1196   2136  -1329       C  
ATOM   5236  C   ASP B 137      30.019   9.092 -20.175  1.00212.40           C  
ANISOU 5236  C   ASP B 137    25794  32260  22650   1135   2176  -1110       C  
ATOM   5237  O   ASP B 137      30.605   8.057 -19.840  1.00212.94           O  
ANISOU 5237  O   ASP B 137    25978  32093  22839   1225   2219  -1278       O  
ATOM   5238  CB  ASP B 137      29.675   8.036 -22.484  1.00214.92           C  
ANISOU 5238  CB  ASP B 137    25912  33231  22516   1411   2157  -1742       C  
ATOM   5239  CG  ASP B 137      28.597   7.537 -23.437  1.00225.95           C  
ANISOU 5239  CG  ASP B 137    27227  34889  23735   1382   2098  -2180       C  
ATOM   5240  OD1 ASP B 137      27.530   8.189 -23.529  1.00225.45           O  
ANISOU 5240  OD1 ASP B 137    27078  34977  23604   1231   2043  -2097       O  
ATOM   5241  OD2 ASP B 137      28.825   6.502 -24.099  1.00234.38           O  
ANISOU 5241  OD2 ASP B 137    28305  36033  24717   1518   2111  -2617       O  
ATOM   5242  N   ARG B 138      29.991  10.195 -19.402  1.00206.97           N  
ANISOU 5242  N   ARG B 138    25106  31469  22065    989   2172   -744       N  
ATOM   5243  CA  ARG B 138      30.659  10.303 -18.106  1.00205.06           C  
ANISOU 5243  CA  ARG B 138    24967  30903  22043    903   2199   -534       C  
ATOM   5244  C   ARG B 138      29.809  11.115 -17.136  1.00207.27           C  
ANISOU 5244  C   ARG B 138    25317  30942  22493    676   2158   -376       C  
ATOM   5245  O   ARG B 138      29.472  12.264 -17.425  1.00206.51           O  
ANISOU 5245  O   ARG B 138    25140  30997  22328    623   2153   -175       O  
ATOM   5246  CB  ARG B 138      32.056  10.932 -18.254  1.00205.18           C  
ANISOU 5246  CB  ARG B 138    24850  31165  21945    999   2254   -233       C  
ATOM   5247  CG  ARG B 138      32.775  11.093 -16.929  1.00212.46           C  
ANISOU 5247  CG  ARG B 138    25831  31847  23046    891   2277    -31       C  
ATOM   5248  CD  ARG B 138      34.100  11.746 -17.068  1.00220.17           C  
ANISOU 5248  CD  ARG B 138    26651  33101  23902    934   2323    259       C  
ATOM   5249  NE  ARG B 138      34.937  11.211 -16.013  1.00224.59           N  
ANISOU 5249  NE  ARG B 138    27248  33528  24559    940   2358    317       N  
ATOM   5250  CZ  ARG B 138      36.251  11.377 -15.946  1.00236.64           C  
ANISOU 5250  CZ  ARG B 138    28633  35306  25972   1004   2407    529       C  
ATOM   5251  NH1 ARG B 138      36.890  12.071 -16.876  1.00224.44           N  
ANISOU 5251  NH1 ARG B 138    26910  34134  24234   1051   2423    712       N  
ATOM   5252  NH2 ARG B 138      36.935  10.861 -14.944  1.00221.56           N  
ANISOU 5252  NH2 ARG B 138    26733  33325  24127   1023   2445    592       N  
ATOM   5253  N   VAL B 139      29.496  10.524 -15.974  1.00203.00           N  
ANISOU 5253  N   VAL B 139    24919  30035  22177    569   2144   -444       N  
ATOM   5254  CA  VAL B 139      28.705  11.179 -14.935  1.00200.91           C  
ANISOU 5254  CA  VAL B 139    24716  29560  22061    380   2105   -323       C  
ATOM   5255  C   VAL B 139      29.656  11.665 -13.811  1.00203.51           C  
ANISOU 5255  C   VAL B 139    25045  29788  22492    319   2134    -90       C  
ATOM   5256  O   VAL B 139      30.561  10.931 -13.395  1.00203.63           O  
ANISOU 5256  O   VAL B 139    25064  29759  22546    397   2177    -83       O  
ATOM   5257  CB  VAL B 139      27.534  10.277 -14.428  1.00204.79           C  
ANISOU 5257  CB  VAL B 139    25315  29796  22699    284   2060   -538       C  
ATOM   5258  CG1 VAL B 139      28.023   8.997 -13.746  1.00205.25           C  
ANISOU 5258  CG1 VAL B 139    25462  29588  22935    326   2101   -631       C  
ATOM   5259  CG2 VAL B 139      26.567  11.048 -13.536  1.00202.89           C  
ANISOU 5259  CG2 VAL B 139    25103  29440  22545    125   2014   -415       C  
ATOM   5260  N   GLU B 140      29.468  12.922 -13.364  1.00198.75           N  
ANISOU 5260  N   GLU B 140    24424  29174  21919    190   2122     92       N  
ATOM   5261  CA  GLU B 140      30.272  13.534 -12.304  1.00197.70           C  
ANISOU 5261  CA  GLU B 140    24270  28980  21867     83   2139    261       C  
ATOM   5262  C   GLU B 140      29.824  13.040 -10.917  1.00200.24           C  
ANISOU 5262  C   GLU B 140    24663  29085  22334      1   2110    204       C  
ATOM   5263  O   GLU B 140      28.658  13.210 -10.540  1.00199.13           O  
ANISOU 5263  O   GLU B 140    24586  28813  22259    -70   2066    144       O  
ATOM   5264  CB  GLU B 140      30.202  15.070 -12.376  1.00198.90           C  
ANISOU 5264  CB  GLU B 140    24391  29151  22031    -35   2149    432       C  
ATOM   5265  CG  GLU B 140      31.122  15.687 -13.418  1.00210.00           C  
ANISOU 5265  CG  GLU B 140    25673  30796  23322     15   2200    607       C  
ATOM   5266  CD  GLU B 140      31.211  17.206 -13.419  1.00228.60           C  
ANISOU 5266  CD  GLU B 140    28000  33101  25757   -123   2238    817       C  
ATOM   5267  OE1 GLU B 140      30.953  17.832 -12.365  1.00217.08           O  
ANISOU 5267  OE1 GLU B 140    26617  31413  24449   -283   2227    803       O  
ATOM   5268  OE2 GLU B 140      31.572  17.771 -14.476  1.00224.90           O  
ANISOU 5268  OE2 GLU B 140    27424  32822  25205    -65   2289   1000       O  
ATOM   5269  N   LEU B 141      30.759  12.423 -10.168  1.00196.43           N  
ANISOU 5269  N   LEU B 141    24139  28618  21876     34   2142    255       N  
ATOM   5270  CA  LEU B 141      30.525  11.897  -8.819  1.00195.26           C  
ANISOU 5270  CA  LEU B 141    24004  28347  21840     -8   2134    263       C  
ATOM   5271  C   LEU B 141      30.563  13.014  -7.764  1.00197.45           C  
ANISOU 5271  C   LEU B 141    24231  28660  22131   -177   2104    339       C  
ATOM   5272  O   LEU B 141      31.385  13.926  -7.895  1.00197.47           O  
ANISOU 5272  O   LEU B 141    24164  28792  22072   -257   2118    416       O  
ATOM   5273  CB  LEU B 141      31.581  10.829  -8.463  1.00196.35           C  
ANISOU 5273  CB  LEU B 141    24081  28548  21975    136   2205    334       C  
ATOM   5274  CG  LEU B 141      31.486   9.473  -9.164  1.00202.30           C  
ANISOU 5274  CG  LEU B 141    24912  29170  22782    320   2255    217       C  
ATOM   5275  CD1 LEU B 141      32.826   8.803  -9.195  1.00203.99           C  
ANISOU 5275  CD1 LEU B 141    25053  29522  22934    514   2350    321       C  
ATOM   5276  CD2 LEU B 141      30.506   8.557  -8.464  1.00204.66           C  
ANISOU 5276  CD2 LEU B 141    25291  29200  23271    300   2253    162       C  
ATOM   5277  N   PRO B 142      29.725  12.959  -6.698  1.00192.44           N  
ANISOU 5277  N   PRO B 142    23617  27929  21574   -240   2066    310       N  
ATOM   5278  CA  PRO B 142      29.798  14.003  -5.655  1.00191.66           C  
ANISOU 5278  CA  PRO B 142    23463  27891  21468   -385   2039    324       C  
ATOM   5279  C   PRO B 142      30.999  13.784  -4.731  1.00195.01           C  
ANISOU 5279  C   PRO B 142    23730  28537  21827   -401   2069    409       C  
ATOM   5280  O   PRO B 142      31.398  12.640  -4.525  1.00194.99           O  
ANISOU 5280  O   PRO B 142    23673  28595  21819   -265   2112    492       O  
ATOM   5281  CB  PRO B 142      28.472  13.849  -4.893  1.00192.76           C  
ANISOU 5281  CB  PRO B 142    23647  27923  21669   -398   1991    267       C  
ATOM   5282  CG  PRO B 142      27.699  12.754  -5.608  1.00197.21           C  
ANISOU 5282  CG  PRO B 142    24288  28354  22288   -300   1990    235       C  
ATOM   5283  CD  PRO B 142      28.697  11.955  -6.369  1.00193.62           C  
ANISOU 5283  CD  PRO B 142    23821  27929  21816   -192   2048    259       C  
ATOM   5284  N   SER B 143      31.580  14.867  -4.178  1.00191.09           N  
ANISOU 5284  N   SER B 143    23152  28170  21284   -565   2055    389       N  
ATOM   5285  CA  SER B 143      32.747  14.758  -3.292  1.00191.47           C  
ANISOU 5285  CA  SER B 143    23003  28525  21222   -610   2077    456       C  
ATOM   5286  C   SER B 143      32.363  14.254  -1.885  1.00193.64           C  
ANISOU 5286  C   SER B 143    23170  28936  21467   -574   2060    461       C  
ATOM   5287  O   SER B 143      31.191  14.309  -1.505  1.00192.26           O  
ANISOU 5287  O   SER B 143    23078  28611  21363   -569   2018    387       O  
ATOM   5288  CB  SER B 143      33.492  16.089  -3.201  1.00196.44           C  
ANISOU 5288  CB  SER B 143    23564  29257  21818   -846   2065    394       C  
ATOM   5289  OG  SER B 143      32.739  17.088  -2.534  1.00206.03           O  
ANISOU 5289  OG  SER B 143    24837  30341  23102   -998   2019    222       O  
ATOM   5290  N   ARG B 144      33.367  13.757  -1.123  1.00190.21           N  
ANISOU 5290  N   ARG B 144    22522  28848  20904   -530   2100    581       N  
ATOM   5291  CA  ARG B 144      33.227  13.231   0.241  1.00190.09           C  
ANISOU 5291  CA  ARG B 144    22327  29085  20812   -464   2104    654       C  
ATOM   5292  C   ARG B 144      32.818  14.337   1.228  1.00193.61           C  
ANISOU 5292  C   ARG B 144    22704  29661  21196   -657   2027    452       C  
ATOM   5293  O   ARG B 144      32.021  14.077   2.132  1.00193.19           O  
ANISOU 5293  O   ARG B 144    22594  29680  21130   -597   2002    454       O  
ATOM   5294  CB  ARG B 144      34.542  12.569   0.693  1.00191.27           C  
ANISOU 5294  CB  ARG B 144    22227  29648  20797   -356   2181    858       C  
ATOM   5295  CG  ARG B 144      34.435  11.762   1.987  1.00200.84           C  
ANISOU 5295  CG  ARG B 144    23223  31157  21929   -208   2221   1034       C  
ATOM   5296  CD  ARG B 144      35.327  10.537   1.973  1.00210.28           C  
ANISOU 5296  CD  ARG B 144    24284  32535  23078     56   2351   1340       C  
ATOM   5297  NE  ARG B 144      34.756   9.463   1.157  1.00218.55           N  
ANISOU 5297  NE  ARG B 144    25556  33123  24358    255   2417   1434       N  
ATOM   5298  CZ  ARG B 144      35.354   8.300   0.913  1.00235.46           C  
ANISOU 5298  CZ  ARG B 144    27673  35248  26545    522   2551   1669       C  
ATOM   5299  NH1 ARG B 144      36.553   8.041   1.421  1.00225.49           N  
ANISOU 5299  NH1 ARG B 144    26149  34446  25081    655   2640   1888       N  
ATOM   5300  NH2 ARG B 144      34.758   7.389   0.156  1.00222.54           N  
ANISOU 5300  NH2 ARG B 144    26263  33143  25148    660   2605   1675       N  
ATOM   5301  N   THR B 145      33.357  15.559   1.045  1.00190.22           N  
ANISOU 5301  N   THR B 145    22278  29257  20739   -887   1996    277       N  
ATOM   5302  CA  THR B 145      33.085  16.746   1.868  1.00190.69           C  
ANISOU 5302  CA  THR B 145    22304  29382  20769  -1095   1935     14       C  
ATOM   5303  C   THR B 145      31.613  17.196   1.760  1.00192.27           C  
ANISOU 5303  C   THR B 145    22727  29212  21114  -1064   1896   -119       C  
ATOM   5304  O   THR B 145      31.082  17.764   2.717  1.00192.54           O  
ANISOU 5304  O   THR B 145    22714  29342  21100  -1118   1852   -306       O  
ATOM   5305  CB  THR B 145      34.030  17.899   1.492  1.00200.53           C  
ANISOU 5305  CB  THR B 145    23536  30632  22024  -1369   1933   -127       C  
ATOM   5306  OG1 THR B 145      33.972  18.128   0.082  1.00199.59           O  
ANISOU 5306  OG1 THR B 145    23626  30143  22065  -1363   1964    -44       O  
ATOM   5307  CG2 THR B 145      35.470  17.647   1.929  1.00200.92           C  
ANISOU 5307  CG2 THR B 145    23290  31185  21865  -1448   1955    -42       C  
ATOM   5308  N   LEU B 146      30.967  16.940   0.602  1.00186.34           N  
ANISOU 5308  N   LEU B 146    22194  28097  20509   -963   1914    -29       N  
ATOM   5309  CA  LEU B 146      29.561  17.264   0.345  1.00184.59           C  
ANISOU 5309  CA  LEU B 146    22164  27575  20398   -904   1887   -103       C  
ATOM   5310  C   LEU B 146      28.648  16.294   1.104  1.00186.97           C  
ANISOU 5310  C   LEU B 146    22397  27985  20657   -745   1862    -16       C  
ATOM   5311  O   LEU B 146      27.604  16.700   1.620  1.00186.21           O  
ANISOU 5311  O   LEU B 146    22339  27853  20559   -721   1823   -115       O  
ATOM   5312  CB  LEU B 146      29.281  17.201  -1.170  1.00183.49           C  
ANISOU 5312  CB  LEU B 146    22213  27130  20375   -847   1917    -15       C  
ATOM   5313  CG  LEU B 146      27.908  17.678  -1.651  1.00187.33           C  
ANISOU 5313  CG  LEU B 146    22878  27351  20949   -790   1902    -66       C  
ATOM   5314  CD1 LEU B 146      27.860  19.198  -1.780  1.00188.72           C  
ANISOU 5314  CD1 LEU B 146    23154  27344  21206   -910   1924   -198       C  
ATOM   5315  CD2 LEU B 146      27.563  17.045  -2.974  1.00188.63           C  
ANISOU 5315  CD2 LEU B 146    23142  27375  21154   -681   1923     50       C  
ATOM   5316  N   CYS B 147      29.055  15.014   1.164  1.00183.11           N  
ANISOU 5316  N   CYS B 147    21804  27627  20145   -624   1897    190       N  
ATOM   5317  CA  CYS B 147      28.348  13.924   1.831  1.00182.64           C  
ANISOU 5317  CA  CYS B 147    21657  27650  20088   -480   1900    348       C  
ATOM   5318  C   CYS B 147      28.469  14.052   3.356  1.00185.79           C  
ANISOU 5318  C   CYS B 147    21804  28466  20322   -476   1879    346       C  
ATOM   5319  O   CYS B 147      27.455  13.993   4.051  1.00185.30           O  
ANISOU 5319  O   CYS B 147    21697  28474  20236   -421   1842    351       O  
ATOM   5320  CB  CYS B 147      28.879  12.576   1.339  1.00183.43           C  
ANISOU 5320  CB  CYS B 147    21741  27694  20260   -347   1976    571       C  
ATOM   5321  SG  CYS B 147      28.072  11.131   2.082  1.00188.03           S  
ANISOU 5321  SG  CYS B 147    22225  28288  20930   -186   2013    823       S  
ATOM   5322  N   GLN B 148      29.714  14.191   3.868  1.00182.12           N  
ANISOU 5322  N   GLN B 148    21142  28343  19713   -526   1904    349       N  
ATOM   5323  CA  GLN B 148      30.055  14.279   5.292  1.00182.92           C  
ANISOU 5323  CA  GLN B 148    20940  28964  19598   -521   1891    340       C  
ATOM   5324  C   GLN B 148      29.385  15.468   5.997  1.00185.40           C  
ANISOU 5324  C   GLN B 148    21254  29359  19831   -634   1810     24       C  
ATOM   5325  O   GLN B 148      29.074  15.369   7.185  1.00185.94           O  
ANISOU 5325  O   GLN B 148    21094  29824  19730   -564   1785     24       O  
ATOM   5326  CB  GLN B 148      31.577  14.373   5.452  1.00185.84           C  
ANISOU 5326  CB  GLN B 148    21111  29688  19813   -597   1929    359       C  
ATOM   5327  CG  GLN B 148      32.108  13.907   6.801  1.00202.21           C  
ANISOU 5327  CG  GLN B 148    22797  32400  21632   -505   1953    498       C  
ATOM   5328  CD  GLN B 148      33.605  14.025   6.866  1.00221.47           C  
ANISOU 5328  CD  GLN B 148    25024  35231  23892   -589   1991    521       C  
ATOM   5329  OE1 GLN B 148      34.331  13.747   5.900  1.00216.02           O  
ANISOU 5329  OE1 GLN B 148    24435  34362  23282   -580   2044    637       O  
ATOM   5330  NE2 GLN B 148      34.112  14.413   8.023  1.00215.16           N  
ANISOU 5330  NE2 GLN B 148    23893  35043  22815   -664   1964    413       N  
ATOM   5331  N   ALA B 149      29.129  16.567   5.258  1.00180.28           N  
ANISOU 5331  N   ALA B 149    20854  28338  19305   -780   1781   -227       N  
ATOM   5332  CA  ALA B 149      28.495  17.787   5.770  1.00180.55           C  
ANISOU 5332  CA  ALA B 149    20950  28336  19317   -868   1729   -555       C  
ATOM   5333  C   ALA B 149      27.039  17.567   6.227  1.00182.31           C  
ANISOU 5333  C   ALA B 149    21198  28545  19525   -695   1695   -518       C  
ATOM   5334  O   ALA B 149      26.544  18.351   7.040  1.00183.34           O  
ANISOU 5334  O   ALA B 149    21283  28823  19555   -698   1655   -765       O  
ATOM   5335  CB  ALA B 149      28.541  18.876   4.710  1.00181.14           C  
ANISOU 5335  CB  ALA B 149    21303  27940  19583  -1019   1745   -731       C  
ATOM   5336  N   THR B 150      26.363  16.512   5.721  1.00175.94           N  
ANISOU 5336  N   THR B 150    20453  27582  18813   -551   1712   -229       N  
ATOM   5337  CA  THR B 150      24.970  16.210   6.071  1.00174.66           C  
ANISOU 5337  CA  THR B 150    20293  27429  18641   -410   1679   -145       C  
ATOM   5338  C   THR B 150      24.848  15.319   7.306  1.00178.46           C  
ANISOU 5338  C   THR B 150    20459  28385  18962   -283   1675     67       C  
ATOM   5339  O   THR B 150      23.920  15.520   8.082  1.00178.47           O  
ANISOU 5339  O   THR B 150    20363  28599  18849   -193   1632     32       O  
ATOM   5340  CB  THR B 150      24.212  15.561   4.902  1.00179.70           C  
ANISOU 5340  CB  THR B 150    21136  27675  19465   -364   1695     35       C  
ATOM   5341  OG1 THR B 150      24.812  14.309   4.563  1.00178.48           O  
ANISOU 5341  OG1 THR B 150    20926  27497  19392   -334   1745    290       O  
ATOM   5342  CG2 THR B 150      24.124  16.462   3.689  1.00177.02           C  
ANISOU 5342  CG2 THR B 150    21071  26938  19252   -442   1705   -125       C  
ATOM   5343  N   ARG B 151      25.768  14.343   7.488  1.00174.86           N  
ANISOU 5343  N   ARG B 151    19829  28122  18490   -248   1731    315       N  
ATOM   5344  CA  ARG B 151      25.788  13.366   8.594  1.00175.74           C  
ANISOU 5344  CA  ARG B 151    19611  28691  18472    -98   1763    617       C  
ATOM   5345  C   ARG B 151      25.381  13.964   9.953  1.00181.38           C  
ANISOU 5345  C   ARG B 151    20064  29938  18914    -43   1704    476       C  
ATOM   5346  O   ARG B 151      24.584  13.357  10.671  1.00181.52           O  
ANISOU 5346  O   ARG B 151    19896  30207  18867    102   1701    715       O  
ATOM   5347  CB  ARG B 151      27.177  12.704   8.730  1.00176.34           C  
ANISOU 5347  CB  ARG B 151    19504  29003  18496    -69   1845    811       C  
ATOM   5348  CG  ARG B 151      27.765  12.067   7.462  1.00182.92           C  
ANISOU 5348  CG  ARG B 151    20556  29390  19556    -82   1916    940       C  
ATOM   5349  CD  ARG B 151      26.943  10.922   6.900  1.00188.68           C  
ANISOU 5349  CD  ARG B 151    21420  29737  20532     18   1963   1206       C  
ATOM   5350  NE  ARG B 151      26.015  11.397   5.876  1.00192.29           N  
ANISOU 5350  NE  ARG B 151    22187  29732  21140    -85   1900   1001       N  
ATOM   5351  CZ  ARG B 151      25.314  10.610   5.069  1.00203.26           C  
ANISOU 5351  CZ  ARG B 151    23748  30735  22748    -71   1920   1113       C  
ATOM   5352  NH1 ARG B 151      25.431   9.289   5.149  1.00189.95           N  
ANISOU 5352  NH1 ARG B 151    21990  28973  21208     32   2011   1417       N  
ATOM   5353  NH2 ARG B 151      24.496  11.136   4.168  1.00188.40           N  
ANISOU 5353  NH2 ARG B 151    22100  28542  20943   -159   1861    921       N  
ATOM   5354  N   GLY B 152      25.919  15.145  10.265  1.00179.21           N  
ANISOU 5354  N   GLY B 152    19774  29827  18491   -167   1660     83       N  
ATOM   5355  CA  GLY B 152      25.664  15.874  11.501  1.00181.37           C  
ANISOU 5355  CA  GLY B 152    19815  30610  18488   -135   1601   -173       C  
ATOM   5356  C   GLY B 152      24.249  16.408  11.643  1.00185.10           C  
ANISOU 5356  C   GLY B 152    20410  30959  18960    -45   1545   -312       C  
ATOM   5357  O   GLY B 152      23.483  15.865  12.445  1.00185.58           O  
ANISOU 5357  O   GLY B 152    20243  31388  18881    131   1530    -97       O  
ATOM   5358  N   PRO B 153      23.856  17.474  10.895  1.00180.75           N  
ANISOU 5358  N   PRO B 153    20196  29925  18556   -140   1525   -634       N  
ATOM   5359  CA  PRO B 153      22.492  18.024  11.059  1.00180.72           C  
ANISOU 5359  CA  PRO B 153    20295  29848  18523     -9   1486   -754       C  
ATOM   5360  C   PRO B 153      21.370  17.103  10.553  1.00183.05           C  
ANISOU 5360  C   PRO B 153    20654  29964  18934    115   1490   -366       C  
ATOM   5361  O   PRO B 153      20.254  17.183  11.075  1.00183.11           O  
ANISOU 5361  O   PRO B 153    20580  30174  18819    269   1455   -334       O  
ATOM   5362  CB  PRO B 153      22.533  19.331  10.270  1.00182.39           C  
ANISOU 5362  CB  PRO B 153    20853  29546  18902   -133   1500  -1130       C  
ATOM   5363  CG  PRO B 153      23.624  19.149   9.292  1.00185.43           C  
ANISOU 5363  CG  PRO B 153    21372  29603  19479   -321   1543  -1057       C  
ATOM   5364  CD  PRO B 153      24.639  18.260   9.919  1.00181.61           C  
ANISOU 5364  CD  PRO B 153    20577  29576  18850   -348   1549   -873       C  
ATOM   5365  N   CYS B 154      21.663  16.216   9.577  1.00178.15           N  
ANISOU 5365  N   CYS B 154    20153  29003  18532     45   1533    -88       N  
ATOM   5366  CA  CYS B 154      20.690  15.256   9.040  1.00176.80           C  
ANISOU 5366  CA  CYS B 154    20035  28642  18497    104   1538    245       C  
ATOM   5367  C   CYS B 154      20.785  13.915   9.799  1.00182.44           C  
ANISOU 5367  C   CYS B 154    20443  29702  19175    185   1567    651       C  
ATOM   5368  O   CYS B 154      20.714  12.837   9.196  1.00181.18           O  
ANISOU 5368  O   CYS B 154    20334  29286  19220    158   1611    943       O  
ATOM   5369  CB  CYS B 154      20.867  15.067   7.534  1.00174.99           C  
ANISOU 5369  CB  CYS B 154    20110  27853  18526    -11   1571    269       C  
ATOM   5370  SG  CYS B 154      20.587  16.570   6.560  1.00178.13           S  
ANISOU 5370  SG  CYS B 154    20843  27844  18993    -65   1566    -83       S  
ATOM   5371  N   ALA B 155      20.918  14.002  11.142  1.00181.74           N  
ANISOU 5371  N   ALA B 155    20022  30207  18824    295   1551    665       N  
ATOM   5372  CA  ALA B 155      20.993  12.862  12.058  1.00183.25           C  
ANISOU 5372  CA  ALA B 155    19855  30836  18937    415   1593   1090       C  
ATOM   5373  C   ALA B 155      19.632  12.177  12.168  1.00187.67           C  
ANISOU 5373  C   ALA B 155    20347  31402  19558    494   1579   1410       C  
ATOM   5374  O   ALA B 155      19.569  10.994  12.510  1.00188.14           O  
ANISOU 5374  O   ALA B 155    20202  31577  19706    549   1641   1856       O  
ATOM   5375  CB  ALA B 155      21.464  13.322  13.429  1.00186.48           C  
ANISOU 5375  CB  ALA B 155    19901  31961  18991    518   1572    970       C  
ATOM   5376  N   ILE B 156      18.549  12.927  11.849  1.00183.96           N  
ANISOU 5376  N   ILE B 156    20047  30797  19055    497   1509   1202       N  
ATOM   5377  CA  ILE B 156      17.148  12.486  11.825  1.00184.04           C  
ANISOU 5377  CA  ILE B 156    20012  30823  19092    543   1479   1447       C  
ATOM   5378  C   ILE B 156      16.957  11.319  10.852  1.00186.75           C  
ANISOU 5378  C   ILE B 156    20497  30687  19772    402   1527   1744       C  
ATOM   5379  O   ILE B 156      16.128  10.451  11.114  1.00187.18           O  
ANISOU 5379  O   ILE B 156    20388  30840  19891    408   1533   2101       O  
ATOM   5380  CB  ILE B 156      16.165  13.647  11.475  1.00186.74           C  
ANISOU 5380  CB  ILE B 156    20551  31075  19328    586   1411   1127       C  
ATOM   5381  CG1 ILE B 156      16.661  14.509  10.293  1.00185.54           C  
ANISOU 5381  CG1 ILE B 156    20790  30379  19328    468   1422    765       C  
ATOM   5382  CG2 ILE B 156      15.881  14.510  12.687  1.00189.54           C  
ANISOU 5382  CG2 ILE B 156    20683  31998  19337    778   1365    927       C  
ATOM   5383  CD1 ILE B 156      15.596  15.415   9.630  1.00192.90           C  
ANISOU 5383  CD1 ILE B 156    21950  31104  20241    518   1393    576       C  
ATOM   5384  N   VAL B 157      17.734  11.304   9.745  1.00181.67           N  
ANISOU 5384  N   VAL B 157    20143  29541  19341    271   1563   1586       N  
ATOM   5385  CA  VAL B 157      17.693  10.295   8.682  1.00180.63           C  
ANISOU 5385  CA  VAL B 157    20189  28917  19527    134   1610   1751       C  
ATOM   5386  C   VAL B 157      18.166   8.930   9.207  1.00186.36           C  
ANISOU 5386  C   VAL B 157    20703  29696  20409    163   1706   2170       C  
ATOM   5387  O   VAL B 157      17.460   7.943   8.999  1.00186.81           O  
ANISOU 5387  O   VAL B 157    20738  29567  20676     90   1734   2443       O  
ATOM   5388  CB  VAL B 157      18.506  10.728   7.431  1.00182.55           C  
ANISOU 5388  CB  VAL B 157    20757  28705  19900     30   1627   1456       C  
ATOM   5389  CG1 VAL B 157      18.273   9.770   6.265  1.00181.92           C  
ANISOU 5389  CG1 VAL B 157    20862  28154  20106   -100   1661   1549       C  
ATOM   5390  CG2 VAL B 157      18.174  12.162   7.020  1.00181.21           C  
ANISOU 5390  CG2 VAL B 157    20772  28492  19590     33   1563   1090       C  
ATOM   5391  N   GLU B 158      19.343   8.869   9.873  1.00183.91           N  
ANISOU 5391  N   GLU B 158    20229  29642  20005    264   1768   2233       N  
ATOM   5392  CA  GLU B 158      19.894   7.614  10.398  1.00185.82           C  
ANISOU 5392  CA  GLU B 158    20255  29961  20387    348   1891   2675       C  
ATOM   5393  C   GLU B 158      19.110   7.092  11.624  1.00192.55           C  
ANISOU 5393  C   GLU B 158    20729  31294  21139    466   1903   3087       C  
ATOM   5394  O   GLU B 158      19.230   5.913  11.963  1.00194.23           O  
ANISOU 5394  O   GLU B 158    20774  31478  21548    522   2021   3544       O  
ATOM   5395  CB  GLU B 158      21.382   7.763  10.733  1.00187.62           C  
ANISOU 5395  CB  GLU B 158    20383  30412  20491    442   1957   2638       C  
ATOM   5396  CG  GLU B 158      22.167   6.496  10.443  1.00199.64           C  
ANISOU 5396  CG  GLU B 158    21908  31659  22287    497   2112   2978       C  
ATOM   5397  CD  GLU B 158      23.566   6.456  11.023  1.00221.98           C  
ANISOU 5397  CD  GLU B 158    24525  34871  24947    644   2199   3080       C  
ATOM   5398  OE1 GLU B 158      24.421   7.257  10.580  1.00216.52           O  
ANISOU 5398  OE1 GLU B 158    23963  34175  24130    582   2160   2732       O  
ATOM   5399  OE2 GLU B 158      23.813   5.607  11.909  1.00218.66           O  
ANISOU 5399  OE2 GLU B 158    23786  34776  24518    822   2316   3539       O  
ATOM   5400  N   ARG B 159      18.271   7.951  12.238  1.00189.49           N  
ANISOU 5400  N   ARG B 159    20211  31322  20464    515   1794   2944       N  
ATOM   5401  CA  ARG B 159      17.410   7.616  13.377  1.00191.70           C  
ANISOU 5401  CA  ARG B 159    20113  32139  20587    640   1785   3306       C  
ATOM   5402  C   ARG B 159      16.018   7.172  12.872  1.00196.54           C  
ANISOU 5402  C   ARG B 159    20814  32474  21388    505   1744   3458       C  
ATOM   5403  O   ARG B 159      15.436   6.243  13.436  1.00198.39           O  
ANISOU 5403  O   ARG B 159    20788  32869  21722    523   1795   3936       O  
ATOM   5404  CB  ARG B 159      17.291   8.831  14.330  1.00191.57           C  
ANISOU 5404  CB  ARG B 159    19895  32777  20117    792   1689   3020       C  
ATOM   5405  CG  ARG B 159      16.349   8.669  15.537  1.00202.54           C  
ANISOU 5405  CG  ARG B 159    20864  34836  21255    960   1661   3339       C  
ATOM   5406  CD  ARG B 159      16.835   7.641  16.551  1.00215.86           C  
ANISOU 5406  CD  ARG B 159    22185  36858  22973   1092   1771   3846       C  
ATOM   5407  NE  ARG B 159      15.863   7.404  17.622  1.00221.78           N  
ANISOU 5407  NE  ARG B 159    23261  36894  24112   1032   1691   3635       N  
ATOM   5408  CZ  ARG B 159      14.893   6.494  17.578  1.00230.75           C  
ANISOU 5408  CZ  ARG B 159    24922  36841  25911    802   1666   3520       C  
ATOM   5409  NH1 ARG B 159      14.737   5.729  16.503  1.00223.28           N  
ANISOU 5409  NH1 ARG B 159    23526  36503  24806    796   1781   4236       N  
ATOM   5410  NH2 ARG B 159      14.066   6.347  18.604  1.00219.57           N  
ANISOU 5410  NH2 ARG B 159    22783  36623  24022   1037   1669   4124       N  
ATOM   5411  N   GLU B 160      15.507   7.823  11.804  1.00191.60           N  
ANISOU 5411  N   GLU B 160    20529  31460  20809    364   1661   3079       N  
ATOM   5412  CA  GLU B 160      14.202   7.562  11.200  1.00191.73           C  
ANISOU 5412  CA  GLU B 160    20635  31266  20948    216   1608   3144       C  
ATOM   5413  C   GLU B 160      14.161   6.237  10.401  1.00197.08           C  
ANISOU 5413  C   GLU B 160    21438  31381  22064      5   1689   3379       C  
ATOM   5414  O   GLU B 160      13.506   5.292  10.848  1.00199.03           O  
ANISOU 5414  O   GLU B 160    21467  31697  22458    -52   1728   3800       O  
ATOM   5415  CB  GLU B 160      13.813   8.753  10.284  1.00190.86           C  
ANISOU 5415  CB  GLU B 160    20832  30969  20716    172   1514   2661       C  
ATOM   5416  CG  GLU B 160      12.408   8.716   9.692  1.00202.24           C  
ANISOU 5416  CG  GLU B 160    22326  32340  22175     54   1446   2688       C  
ATOM   5417  CD  GLU B 160      12.128   9.717   8.580  1.00221.52           C  
ANISOU 5417  CD  GLU B 160    25082  34530  24553     17   1391   2279       C  
ATOM   5418  OE1 GLU B 160      12.994  10.580   8.293  1.00211.58           O  
ANISOU 5418  OE1 GLU B 160    24017  33133  23240     85   1402   1955       O  
ATOM   5419  OE2 GLU B 160      11.022   9.635   7.997  1.00217.84           O  
ANISOU 5419  OE2 GLU B 160    24645  34035  24088    -83   1344   2309       O  
ATOM   5420  N   ARG B 161      14.830   6.186   9.229  1.00192.50           N  
ANISOU 5420  N   ARG B 161    21198  30253  21691   -114   1716   3100       N  
ATOM   5421  CA  ARG B 161      14.845   5.032   8.323  1.00193.30           C  
ANISOU 5421  CA  ARG B 161    21470  29774  22201   -312   1790   3193       C  
ATOM   5422  C   ARG B 161      16.242   4.562   7.909  1.00197.02           C  
ANISOU 5422  C   ARG B 161    22100  29884  22874   -267   1906   3146       C  
ATOM   5423  O   ARG B 161      16.358   3.637   7.097  1.00197.49           O  
ANISOU 5423  O   ARG B 161    22335  29427  23276   -404   1978   3157       O  
ATOM   5424  CB  ARG B 161      14.047   5.394   7.056  1.00192.27           C  
ANISOU 5424  CB  ARG B 161    21601  29355  22098   -510   1697   2853       C  
ATOM   5425  CG  ARG B 161      12.546   5.354   7.259  1.00203.99           C  
ANISOU 5425  CG  ARG B 161    22922  31085  23498   -618   1615   2998       C  
ATOM   5426  CD  ARG B 161      11.864   4.230   6.511  1.00216.72           C  
ANISOU 5426  CD  ARG B 161    24595  32300  25449   -913   1635   3090       C  
ATOM   5427  NE  ARG B 161      10.425   4.258   6.763  1.00228.19           N  
ANISOU 5427  NE  ARG B 161    25846  34080  26775  -1026   1547   3248       N  
ATOM   5428  CZ  ARG B 161       9.538   3.453   6.187  1.00245.90           C  
ANISOU 5428  CZ  ARG B 161    28080  36112  29237  -1327   1531   3309       C  
ATOM   5429  NH1 ARG B 161       9.932   2.539   5.308  1.00235.09           N  
ANISOU 5429  NH1 ARG B 161    26916  34163  28245  -1544   1600   3184       N  
ATOM   5430  NH2 ARG B 161       8.250   3.559   6.479  1.00234.35           N  
ANISOU 5430  NH2 ARG B 161    26397  35039  27608  -1418   1447   3474       N  
ATOM   5431  N   GLY B 162      17.274   5.209   8.441  1.00192.74           N  
ANISOU 5431  N   GLY B 162    21491  29632  22110    -80   1922   3068       N  
ATOM   5432  CA  GLY B 162      18.665   4.885   8.144  1.00192.47           C  
ANISOU 5432  CA  GLY B 162    21560  29380  22191     -2   2029   3041       C  
ATOM   5433  C   GLY B 162      19.131   5.415   6.804  1.00193.97           C  
ANISOU 5433  C   GLY B 162    22102  29181  22418    -99   1991   2603       C  
ATOM   5434  O   GLY B 162      18.326   5.554   5.877  1.00192.67           O  
ANISOU 5434  O   GLY B 162    22131  28748  22325   -260   1920   2389       O  
ATOM   5435  N   TRP B 163      20.440   5.718   6.687  1.00189.81           N  
ANISOU 5435  N   TRP B 163    21628  28675  21818      1   2040   2486       N  
ATOM   5436  CA  TRP B 163      21.017   6.227   5.441  1.00187.72           C  
ANISOU 5436  CA  TRP B 163    21659  28094  21572    -70   2015   2118       C  
ATOM   5437  C   TRP B 163      21.094   5.120   4.389  1.00192.93           C  
ANISOU 5437  C   TRP B 163    22523  28215  22568   -144   2096   2127       C  
ATOM   5438  O   TRP B 163      21.569   4.022   4.703  1.00194.63           O  
ANISOU 5438  O   TRP B 163    22663  28292  22994    -56   2230   2415       O  
ATOM   5439  CB  TRP B 163      22.411   6.838   5.658  1.00185.66           C  
ANISOU 5439  CB  TRP B 163    21358  28055  21130     39   2046   2020       C  
ATOM   5440  CG  TRP B 163      22.400   8.229   6.218  1.00185.35           C  
ANISOU 5440  CG  TRP B 163    21239  28408  20777     40   1945   1794       C  
ATOM   5441  CD1 TRP B 163      22.824   8.614   7.455  1.00189.23           C  
ANISOU 5441  CD1 TRP B 163    21452  29419  21028    143   1943   1872       C  
ATOM   5442  CD2 TRP B 163      21.962   9.425   5.552  1.00183.32           C  
ANISOU 5442  CD2 TRP B 163    21180  28053  20423    -59   1844   1436       C  
ATOM   5443  NE1 TRP B 163      22.676   9.974   7.606  1.00187.72           N  
ANISOU 5443  NE1 TRP B 163    21295  29412  20615     94   1844   1537       N  
ATOM   5444  CE2 TRP B 163      22.145  10.498   6.454  1.00187.36           C  
ANISOU 5444  CE2 TRP B 163    21550  28967  20671    -19   1791   1291       C  
ATOM   5445  CE3 TRP B 163      21.421   9.696   4.281  1.00183.18           C  
ANISOU 5445  CE3 TRP B 163    21428  27664  20507   -166   1803   1231       C  
ATOM   5446  CZ2 TRP B 163      21.816  11.821   6.125  1.00185.57           C  
ANISOU 5446  CZ2 TRP B 163    21474  28699  20335    -77   1716    959       C  
ATOM   5447  CZ3 TRP B 163      21.089  11.006   3.960  1.00183.44           C  
ANISOU 5447  CZ3 TRP B 163    21579  27718  20401   -202   1731    957       C  
ATOM   5448  CH2 TRP B 163      21.289  12.051   4.874  1.00184.33           C  
ANISOU 5448  CH2 TRP B 163    21581  28152  20304   -155   1696    828       C  
ATOM   5449  N   PRO B 164      20.641   5.380   3.138  1.00188.58           N  
ANISOU 5449  N   PRO B 164    22217  27366  22067   -288   2030   1812       N  
ATOM   5450  CA  PRO B 164      20.733   4.340   2.099  1.00189.80           C  
ANISOU 5450  CA  PRO B 164    22561  27037  22519   -362   2102   1742       C  
ATOM   5451  C   PRO B 164      22.190   4.062   1.719  1.00194.32           C  
ANISOU 5451  C   PRO B 164    23218  27476  23139   -212   2210   1715       C  
ATOM   5452  O   PRO B 164      23.041   4.944   1.866  1.00192.52           O  
ANISOU 5452  O   PRO B 164    22958  27513  22679   -120   2189   1640       O  
ATOM   5453  CB  PRO B 164      19.935   4.931   0.928  1.00190.14           C  
ANISOU 5453  CB  PRO B 164    22783  26973  22491   -525   1988   1392       C  
ATOM   5454  CG  PRO B 164      19.172   6.099   1.503  1.00192.92           C  
ANISOU 5454  CG  PRO B 164    23025  27709  22567   -531   1874   1373       C  
ATOM   5455  CD  PRO B 164      20.040   6.615   2.597  1.00187.99           C  
ANISOU 5455  CD  PRO B 164    22247  27401  21780   -367   1902   1510       C  
ATOM   5456  N   ASP B 165      22.470   2.829   1.259  1.00193.18           N  
ANISOU 5456  N   ASP B 165    23175  26924  23301   -189   2332   1779       N  
ATOM   5457  CA  ASP B 165      23.802   2.339   0.869  1.00193.86           C  
ANISOU 5457  CA  ASP B 165    23342  26853  23464     -6   2463   1788       C  
ATOM   5458  C   ASP B 165      24.557   3.305  -0.067  1.00194.70           C  
ANISOU 5458  C   ASP B 165    23575  27070  23332     16   2397   1466       C  
ATOM   5459  O   ASP B 165      25.761   3.507   0.117  1.00194.18           O  
ANISOU 5459  O   ASP B 165    23449  27189  23142    182   2460   1544       O  
ATOM   5460  CB  ASP B 165      23.699   0.949   0.214  1.00198.92           C  
ANISOU 5460  CB  ASP B 165    24144  26939  24497    -21   2588   1773       C  
ATOM   5461  CG  ASP B 165      22.760   0.890  -0.979  1.00209.77           C  
ANISOU 5461  CG  ASP B 165    25714  28031  25958   -260   2491   1384       C  
ATOM   5462  OD1 ASP B 165      21.529   0.846  -0.764  1.00210.96           O  
ANISOU 5462  OD1 ASP B 165    25810  28178  26167   -468   2411   1402       O  
ATOM   5463  OD2 ASP B 165      23.256   0.921  -2.125  1.00215.02           O  
ANISOU 5463  OD2 ASP B 165    26555  28549  26596   -233   2492   1067       O  
ATOM   5464  N   PHE B 166      23.845   3.915  -1.038  1.00189.01           N  
ANISOU 5464  N   PHE B 166    22995  26286  22534   -148   2277   1143       N  
ATOM   5465  CA  PHE B 166      24.408   4.850  -2.009  1.00186.65           C  
ANISOU 5465  CA  PHE B 166    22802  26086  22029   -139   2219    875       C  
ATOM   5466  C   PHE B 166      24.549   6.269  -1.432  1.00187.83           C  
ANISOU 5466  C   PHE B 166    22848  26619  21901   -153   2131    880       C  
ATOM   5467  O   PHE B 166      25.224   7.098  -2.043  1.00186.21           O  
ANISOU 5467  O   PHE B 166    22696  26513  21543   -137   2107    735       O  
ATOM   5468  CB  PHE B 166      23.578   4.865  -3.309  1.00188.31           C  
ANISOU 5468  CB  PHE B 166    23172  26110  22265   -283   2147    562       C  
ATOM   5469  CG  PHE B 166      22.157   5.359  -3.179  1.00189.04           C  
ANISOU 5469  CG  PHE B 166    23227  26305  22294   -457   2031    516       C  
ATOM   5470  CD1 PHE B 166      21.135   4.494  -2.804  1.00193.82           C  
ANISOU 5470  CD1 PHE B 166    23792  26758  23094   -585   2031    605       C  
ATOM   5471  CD2 PHE B 166      21.833   6.678  -3.474  1.00189.25           C  
ANISOU 5471  CD2 PHE B 166    23255  26575  22075   -488   1934    399       C  
ATOM   5472  CE1 PHE B 166      19.819   4.950  -2.693  1.00194.27           C  
ANISOU 5472  CE1 PHE B 166    23785  26973  23056   -735   1923    582       C  
ATOM   5473  CE2 PHE B 166      20.516   7.132  -3.366  1.00191.72           C  
ANISOU 5473  CE2 PHE B 166    23525  27013  22308   -604   1843    377       C  
ATOM   5474  CZ  PHE B 166      19.522   6.269  -2.961  1.00191.31           C  
ANISOU 5474  CZ  PHE B 166    23410  26874  22407   -724   1832    470       C  
ATOM   5475  N   LEU B 167      23.927   6.547  -0.267  1.00183.96           N  
ANISOU 5475  N   LEU B 167    22203  26341  21353   -182   2090   1042       N  
ATOM   5476  CA  LEU B 167      24.017   7.863   0.369  1.00182.19           C  
ANISOU 5476  CA  LEU B 167    21884  26456  20883   -193   2016    998       C  
ATOM   5477  C   LEU B 167      24.942   7.850   1.606  1.00187.36           C  
ANISOU 5477  C   LEU B 167    22320  27432  21436    -79   2071   1207       C  
ATOM   5478  O   LEU B 167      25.117   8.893   2.243  1.00186.41           O  
ANISOU 5478  O   LEU B 167    22101  27614  21112    -99   2015   1135       O  
ATOM   5479  CB  LEU B 167      22.632   8.431   0.707  1.00181.42           C  
ANISOU 5479  CB  LEU B 167    21760  26455  20716   -284   1916    955       C  
ATOM   5480  CG  LEU B 167      21.928   9.139  -0.456  1.00184.74           C  
ANISOU 5480  CG  LEU B 167    22351  26753  21089   -375   1845    712       C  
ATOM   5481  CD1 LEU B 167      20.437   9.170  -0.258  1.00184.94           C  
ANISOU 5481  CD1 LEU B 167    22338  26832  21097   -447   1775    732       C  
ATOM   5482  CD2 LEU B 167      22.458  10.556  -0.654  1.00185.77           C  
ANISOU 5482  CD2 LEU B 167    22531  27006  21048   -362   1816    558       C  
ATOM   5483  N   ARG B 168      25.580   6.699   1.904  1.00185.86           N  
ANISOU 5483  N   ARG B 168    22052  27188  21380     49   2192   1450       N  
ATOM   5484  CA  ARG B 168      26.573   6.595   2.979  1.00186.82           C  
ANISOU 5484  CA  ARG B 168    21930  27678  21373    191   2266   1683       C  
ATOM   5485  C   ARG B 168      27.909   7.071   2.406  1.00190.93           C  
ANISOU 5485  C   ARG B 168    22489  28288  21766    226   2292   1560       C  
ATOM   5486  O   ARG B 168      28.193   6.779   1.244  1.00190.35           O  
ANISOU 5486  O   ARG B 168    22611  27910  21803    235   2321   1440       O  
ATOM   5487  CB  ARG B 168      26.664   5.162   3.537  1.00188.60           C  
ANISOU 5487  CB  ARG B 168    22038  27816  21806    350   2412   2060       C  
ATOM   5488  CG  ARG B 168      25.460   4.762   4.389  1.00196.25           C  
ANISOU 5488  CG  ARG B 168    22875  28829  22864    313   2393   2271       C  
ATOM   5489  CD  ARG B 168      25.790   3.697   5.422  1.00203.47           C  
ANISOU 5489  CD  ARG B 168    23540  29890  23878    507   2547   2742       C  
ATOM   5490  NE  ARG B 168      25.511   2.339   4.941  1.00208.39           N  
ANISOU 5490  NE  ARG B 168    24299  29979  24902    537   2677   2920       N  
ATOM   5491  CZ  ARG B 168      24.451   1.617   5.286  1.00220.01           C  
ANISOU 5491  CZ  ARG B 168    25726  31258  26608    462   2701   3133       C  
ATOM   5492  NH1 ARG B 168      23.576   2.082   6.167  1.00205.21           N  
ANISOU 5492  NH1 ARG B 168    23646  29746  24576    394   2604   3241       N  
ATOM   5493  NH2 ARG B 168      24.290   0.396   4.795  1.00207.32           N  
ANISOU 5493  NH2 ARG B 168    24264  29105  25403    462   2832   3251       N  
ATOM   5494  N   CYS B 169      28.698   7.844   3.181  1.00187.99           N  
ANISOU 5494  N   CYS B 169    21918  28363  21146    229   2273   1564       N  
ATOM   5495  CA  CYS B 169      29.961   8.419   2.703  1.00187.81           C  
ANISOU 5495  CA  CYS B 169    21894  28486  20980    214   2284   1453       C  
ATOM   5496  C   CYS B 169      31.099   7.403   2.658  1.00194.93           C  
ANISOU 5496  C   CYS B 169    22699  29463  21902    427   2432   1710       C  
ATOM   5497  O   CYS B 169      32.125   7.708   2.053  1.00194.30           O  
ANISOU 5497  O   CYS B 169    22636  29469  21722    435   2452   1641       O  
ATOM   5498  CB  CYS B 169      30.367   9.631   3.538  1.00187.84           C  
ANISOU 5498  CB  CYS B 169    21712  28936  20721     92   2208   1321       C  
ATOM   5499  SG  CYS B 169      29.035  10.820   3.850  1.00190.20           S  
ANISOU 5499  SG  CYS B 169    22097  29184  20987    -88   2064   1043       S  
ATOM   5500  N   THR B 170      30.971   6.255   3.359  1.00194.81           N  
ANISOU 5500  N   THR B 170    22557  29461  22002    614   2547   2037       N  
ATOM   5501  CA  THR B 170      32.012   5.220   3.459  1.00197.57           C  
ANISOU 5501  CA  THR B 170    22794  29889  22385    878   2723   2346       C  
ATOM   5502  C   THR B 170      32.357   4.578   2.069  1.00203.14           C  
ANISOU 5502  C   THR B 170    23775  30122  23287    970   2797   2245       C  
ATOM   5503  O   THR B 170      33.554   4.537   1.768  1.00203.71           O  
ANISOU 5503  O   THR B 170    23784  30390  23225   1106   2871   2302       O  
ATOM   5504  CB  THR B 170      31.649   4.159   4.529  1.00207.39           C  
ANISOU 5504  CB  THR B 170    23843  31202  23755   1064   2847   2760       C  
ATOM   5505  OG1 THR B 170      31.283   4.821   5.743  1.00205.50           O  
ANISOU 5505  OG1 THR B 170    23333  31459  23287    985   2762   2810       O  
ATOM   5506  CG2 THR B 170      32.796   3.185   4.814  1.00209.05           C  
ANISOU 5506  CG2 THR B 170    23884  31582  23964   1386   3056   3144       C  
ATOM   5507  N   PRO B 171      31.406   4.112   1.199  1.00200.14           N  
ANISOU 5507  N   PRO B 171    23671  29193  23180    901   2777   2075       N  
ATOM   5508  CA  PRO B 171      31.824   3.507  -0.086  1.00201.01           C  
ANISOU 5508  CA  PRO B 171    24007  28936  23430   1008   2850   1935       C  
ATOM   5509  C   PRO B 171      32.516   4.478  -1.062  1.00203.90           C  
ANISOU 5509  C   PRO B 171    24441  29457  23575    932   2766   1673       C  
ATOM   5510  O   PRO B 171      32.530   5.692  -0.843  1.00201.67           O  
ANISOU 5510  O   PRO B 171    24078  29463  23084    746   2642   1561       O  
ATOM   5511  CB  PRO B 171      30.508   2.988  -0.678  1.00202.72           C  
ANISOU 5511  CB  PRO B 171    24454  28635  23937    877   2812   1754       C  
ATOM   5512  CG  PRO B 171      29.452   3.811  -0.039  1.00205.18           C  
ANISOU 5512  CG  PRO B 171    24694  29098  24167    648   2664   1705       C  
ATOM   5513  CD  PRO B 171      29.938   4.032   1.357  1.00201.12           C  
ANISOU 5513  CD  PRO B 171    23884  29053  23480    734   2697   2006       C  
ATOM   5514  N   ASP B 172      33.080   3.917  -2.154  1.00201.97           N  
ANISOU 5514  N   ASP B 172    24343  29003  23393   1085   2844   1578       N  
ATOM   5515  CA  ASP B 172      33.819   4.610  -3.219  1.00201.19           C  
ANISOU 5515  CA  ASP B 172    24293  29050  23101   1069   2796   1386       C  
ATOM   5516  C   ASP B 172      32.968   5.634  -4.014  1.00203.43           C  
ANISOU 5516  C   ASP B 172    24711  29238  23344    805   2631   1077       C  
ATOM   5517  O   ASP B 172      33.520   6.342  -4.862  1.00202.60           O  
ANISOU 5517  O   ASP B 172    24618  29284  23077    773   2589    960       O  
ATOM   5518  CB  ASP B 172      34.417   3.570  -4.195  1.00205.20           C  
ANISOU 5518  CB  ASP B 172    24930  29327  23708   1338   2930   1344       C  
ATOM   5519  CG  ASP B 172      33.406   2.743  -4.978  1.00215.03           C  
ANISOU 5519  CG  ASP B 172    26427  30038  25238   1321   2940   1099       C  
ATOM   5520  OD1 ASP B 172      32.388   2.320  -4.381  1.00215.73           O  
ANISOU 5520  OD1 ASP B 172    26555  29865  25549   1211   2932   1140       O  
ATOM   5521  OD2 ASP B 172      33.653   2.484  -6.175  1.00220.80           O  
ANISOU 5521  OD2 ASP B 172    27291  30643  25958   1416   2959    867       O  
ATOM   5522  N   ARG B 173      31.650   5.717  -3.734  1.00199.15           N  
ANISOU 5522  N   ARG B 173    24245  28485  22937    636   2551    989       N  
ATOM   5523  CA  ARG B 173      30.696   6.606  -4.407  1.00197.16           C  
ANISOU 5523  CA  ARG B 173    24107  28152  22653    424   2415    742       C  
ATOM   5524  C   ARG B 173      30.966   8.108  -4.157  1.00199.30           C  
ANISOU 5524  C   ARG B 173    24283  28726  22714    268   2323    722       C  
ATOM   5525  O   ARG B 173      30.586   8.924  -5.002  1.00197.57           O  
ANISOU 5525  O   ARG B 173    24153  28474  22442    158   2250    556       O  
ATOM   5526  CB  ARG B 173      29.258   6.251  -4.005  1.00197.39           C  
ANISOU 5526  CB  ARG B 173    24198  27945  22857    305   2367    706       C  
ATOM   5527  CG  ARG B 173      28.732   5.017  -4.729  1.00209.83           C  
ANISOU 5527  CG  ARG B 173    25926  29135  24665    355   2424    587       C  
ATOM   5528  CD  ARG B 173      27.407   4.548  -4.167  1.00218.93           C  
ANISOU 5528  CD  ARG B 173    27094  30085  26007    218   2391    616       C  
ATOM   5529  NE  ARG B 173      26.823   3.463  -4.957  1.00227.42           N  
ANISOU 5529  NE  ARG B 173    28320  30773  27315    192   2431    434       N  
ATOM   5530  CZ  ARG B 173      25.945   3.635  -5.941  1.00238.96           C  
ANISOU 5530  CZ  ARG B 173    29882  32154  28759     39   2340    141       C  
ATOM   5531  NH1 ARG B 173      25.538   4.855  -6.273  1.00222.03           N  
ANISOU 5531  NH1 ARG B 173    27709  30271  26382    -66   2219     46       N  
ATOM   5532  NH2 ARG B 173      25.467   2.589  -6.602  1.00227.67           N  
ANISOU 5532  NH2 ARG B 173    28572  30390  27544     -9   2379    -63       N  
ATOM   5533  N   PHE B 174      31.622   8.474  -3.028  1.00196.25           N  
ANISOU 5533  N   PHE B 174    23709  28641  22215    257   2336    885       N  
ATOM   5534  CA  PHE B 174      31.948   9.876  -2.731  1.00195.19           C  
ANISOU 5534  CA  PHE B 174    23488  28762  21915     79   2259    823       C  
ATOM   5535  C   PHE B 174      33.475  10.051  -2.594  1.00200.15           C  
ANISOU 5535  C   PHE B 174    23941  29737  22369    125   2314    943       C  
ATOM   5536  O   PHE B 174      33.996   9.978  -1.479  1.00200.46           O  
ANISOU 5536  O   PHE B 174    23776  30083  22307    142   2342   1081       O  
ATOM   5537  CB  PHE B 174      31.204  10.396  -1.480  1.00196.48           C  
ANISOU 5537  CB  PHE B 174    23563  29032  22060    -41   2194    819       C  
ATOM   5538  CG  PHE B 174      29.703  10.261  -1.548  1.00197.13           C  
ANISOU 5538  CG  PHE B 174    23779  28845  22276    -84   2137    734       C  
ATOM   5539  CD1 PHE B 174      28.927  11.225  -2.183  1.00199.12           C  
ANISOU 5539  CD1 PHE B 174    24166  28963  22529   -210   2059    553       C  
ATOM   5540  CD2 PHE B 174      29.064   9.168  -0.982  1.00199.82           C  
ANISOU 5540  CD2 PHE B 174    24092  29086  22744      5   2174    870       C  
ATOM   5541  CE1 PHE B 174      27.537  11.091  -2.257  1.00199.38           C  
ANISOU 5541  CE1 PHE B 174    24291  28817  22648   -239   2010    494       C  
ATOM   5542  CE2 PHE B 174      27.677   9.036  -1.054  1.00202.03           C  
ANISOU 5542  CE2 PHE B 174    24466  29161  23133    -62   2117    805       C  
ATOM   5543  CZ  PHE B 174      26.921   9.999  -1.690  1.00198.88           C  
ANISOU 5543  CZ  PHE B 174    24187  28684  22693   -181   2031    610       C  
ATOM   5544  N   PRO B 175      34.215  10.264  -3.715  1.00197.09           N  
ANISOU 5544  N   PRO B 175    23595  29372  21918    153   2334    910       N  
ATOM   5545  CA  PRO B 175      35.681  10.415  -3.611  1.00198.25           C  
ANISOU 5545  CA  PRO B 175    23547  29901  21878    190   2386   1049       C  
ATOM   5546  C   PRO B 175      36.084  11.713  -2.902  1.00202.10           C  
ANISOU 5546  C   PRO B 175    23880  30671  22237    -79   2316   1005       C  
ATOM   5547  O   PRO B 175      35.298  12.659  -2.849  1.00200.69           O  
ANISOU 5547  O   PRO B 175    23798  30324  22130   -281   2234    839       O  
ATOM   5548  CB  PRO B 175      36.156  10.372  -5.068  1.00200.26           C  
ANISOU 5548  CB  PRO B 175    23891  30099  22100    281   2412   1013       C  
ATOM   5549  CG  PRO B 175      34.973   9.883  -5.861  1.00203.78           C  
ANISOU 5549  CG  PRO B 175    24568  30142  22718    342   2392    853       C  
ATOM   5550  CD  PRO B 175      33.775  10.355  -5.120  1.00197.98           C  
ANISOU 5550  CD  PRO B 175    23892  29240  22089    164   2311    766       C  
ATOM   5551  N   GLU B 176      37.308  11.727  -2.333  1.00200.04           N  
ANISOU 5551  N   GLU B 176    23371  30850  21785    -76   2359   1146       N  
ATOM   5552  CA  GLU B 176      37.904  12.780  -1.496  1.00200.72           C  
ANISOU 5552  CA  GLU B 176    23247  31297  21719   -342   2305   1091       C  
ATOM   5553  C   GLU B 176      37.657  14.229  -2.005  1.00204.10           C  
ANISOU 5553  C   GLU B 176    23787  31538  22223   -656   2221    883       C  
ATOM   5554  O   GLU B 176      36.773  14.903  -1.469  1.00202.98           O  
ANISOU 5554  O   GLU B 176    23728  31219  22175   -811   2155    701       O  
ATOM   5555  CB  GLU B 176      39.412  12.530  -1.282  1.00204.17           C  
ANISOU 5555  CB  GLU B 176    23397  32266  21912   -281   2373   1288       C  
ATOM   5556  CG  GLU B 176      39.756  11.205  -0.603  1.00214.60           C  
ANISOU 5556  CG  GLU B 176    24562  33831  23145     47   2485   1543       C  
ATOM   5557  CD  GLU B 176      39.313  10.976   0.834  1.00232.35           C  
ANISOU 5557  CD  GLU B 176    26648  36285  25349     59   2481   1584       C  
ATOM   5558  OE1 GLU B 176      39.077  11.966   1.565  1.00228.08           O  
ANISOU 5558  OE1 GLU B 176    26018  35899  24743   -222   2383   1387       O  
ATOM   5559  OE2 GLU B 176      39.243   9.794   1.241  1.00223.55           O  
ANISOU 5559  OE2 GLU B 176    25479  35197  24262    364   2588   1824       O  
ATOM   5560  N   GLY B 177      38.426  14.691  -2.990  1.00201.42           N  
ANISOU 5560  N   GLY B 177    23437  31246  21846   -728   2235    934       N  
ATOM   5561  CA  GLY B 177      38.296  16.047  -3.514  1.00201.58           C  
ANISOU 5561  CA  GLY B 177    23544  31077  21970  -1013   2186    809       C  
ATOM   5562  C   GLY B 177      37.787  16.111  -4.936  1.00205.06           C  
ANISOU 5562  C   GLY B 177    24190  31192  22531   -911   2200    840       C  
ATOM   5563  O   GLY B 177      38.585  16.059  -5.876  1.00205.56           O  
ANISOU 5563  O   GLY B 177    24188  31403  22513   -855   2239    984       O  
ATOM   5564  N   CYS B 178      36.455  16.243  -5.107  1.00200.51           N  
ANISOU 5564  N   CYS B 178    23831  30234  22118   -879   2169    716       N  
ATOM   5565  CA  CYS B 178      35.845  16.306  -6.433  1.00199.80           C  
ANISOU 5565  CA  CYS B 178    23907  29898  22110   -773   2181    737       C  
ATOM   5566  C   CYS B 178      35.196  17.652  -6.693  1.00203.37           C  
ANISOU 5566  C   CYS B 178    24472  30089  22711   -968   2162    669       C  
ATOM   5567  O   CYS B 178      34.675  18.286  -5.775  1.00202.66           O  
ANISOU 5567  O   CYS B 178    24424  29869  22709  -1119   2129    529       O  
ATOM   5568  CB  CYS B 178      34.845  15.174  -6.637  1.00198.93           C  
ANISOU 5568  CB  CYS B 178    23935  29607  22044   -532   2179    682       C  
ATOM   5569  SG  CYS B 178      35.580  13.515  -6.677  1.00203.62           S  
ANISOU 5569  SG  CYS B 178    24449  30386  22531   -240   2245    785       S  
ATOM   5570  N   THR B 179      35.215  18.067  -7.965  1.00200.41           N  
ANISOU 5570  N   THR B 179    24134  29653  22358   -933   2195    781       N  
ATOM   5571  CA  THR B 179      34.617  19.313  -8.415  1.00200.67           C  
ANISOU 5571  CA  THR B 179    24269  29429  22548  -1060   2213    795       C  
ATOM   5572  C   THR B 179      33.105  19.101  -8.451  1.00202.26           C  
ANISOU 5572  C   THR B 179    24647  29387  22818   -918   2189    684       C  
ATOM   5573  O   THR B 179      32.587  18.353  -9.287  1.00201.02           O  
ANISOU 5573  O   THR B 179    24530  29258  22592   -712   2189    705       O  
ATOM   5574  CB  THR B 179      35.240  19.817  -9.748  1.00210.31           C  
ANISOU 5574  CB  THR B 179    25413  30750  23746  -1052   2272   1024       C  
ATOM   5575  OG1 THR B 179      34.524  20.961 -10.211  1.00210.76           O  
ANISOU 5575  OG1 THR B 179    25573  30530  23977  -1123   2315   1088       O  
ATOM   5576  CG2 THR B 179      35.315  18.746 -10.840  1.00208.01           C  
ANISOU 5576  CG2 THR B 179    25082  30673  23278   -763   2282   1101       C  
ATOM   5577  N   ASN B 180      32.408  19.767  -7.523  1.00198.06           N  
ANISOU 5577  N   ASN B 180    24202  28647  22405  -1036   2168    546       N  
ATOM   5578  CA  ASN B 180      30.958  19.719  -7.415  1.00196.25           C  
ANISOU 5578  CA  ASN B 180    24116  28222  22229   -921   2146    456       C  
ATOM   5579  C   ASN B 180      30.336  20.762  -8.325  1.00200.52           C  
ANISOU 5579  C   ASN B 180    24749  28566  22875   -898   2207    562       C  
ATOM   5580  O   ASN B 180      30.661  21.948  -8.221  1.00201.67           O  
ANISOU 5580  O   ASN B 180    24915  28546  23165  -1058   2261    598       O  
ATOM   5581  CB  ASN B 180      30.513  19.944  -5.964  1.00195.72           C  
ANISOU 5581  CB  ASN B 180    24075  28085  22206  -1014   2102    269       C  
ATOM   5582  CG  ASN B 180      30.705  18.761  -5.052  1.00212.00           C  
ANISOU 5582  CG  ASN B 180    26040  30359  24154   -957   2051    212       C  
ATOM   5583  OD1 ASN B 180      30.346  17.621  -5.371  1.00204.35           O  
ANISOU 5583  OD1 ASN B 180    25079  29437  23130   -788   2038    258       O  
ATOM   5584  ND2 ASN B 180      31.210  19.025  -3.859  1.00203.10           N  
ANISOU 5584  ND2 ASN B 180    24811  29360  22997  -1096   2028    106       N  
ATOM   5585  N   GLU B 181      29.445  20.321  -9.224  1.00196.24           N  
ANISOU 5585  N   GLU B 181    24249  28049  22266   -701   2210    618       N  
ATOM   5586  CA  GLU B 181      28.713  21.213 -10.124  1.00197.06           C  
ANISOU 5586  CA  GLU B 181    24406  28041  22426   -619   2280    763       C  
ATOM   5587  C   GLU B 181      27.604  21.917  -9.316  1.00200.78           C  
ANISOU 5587  C   GLU B 181    25007  28267  23012   -621   2286    663       C  
ATOM   5588  O   GLU B 181      27.129  22.981  -9.718  1.00201.90           O  
ANISOU 5588  O   GLU B 181    25212  28233  23267   -580   2374    789       O  
ATOM   5589  CB  GLU B 181      28.149  20.429 -11.326  1.00197.89           C  
ANISOU 5589  CB  GLU B 181    24464  28363  22362   -409   2272    825       C  
ATOM   5590  CG  GLU B 181      27.690  21.290 -12.498  1.00209.15           C  
ANISOU 5590  CG  GLU B 181    25861  29823  23783   -292   2363   1055       C  
ATOM   5591  CD  GLU B 181      28.735  21.926 -13.401  1.00226.57           C  
ANISOU 5591  CD  GLU B 181    27952  32129  26005   -317   2447   1313       C  
ATOM   5592  OE1 GLU B 181      29.946  21.662 -13.220  1.00216.96           O  
ANISOU 5592  OE1 GLU B 181    26663  30994  24779   -435   2428   1308       O  
ATOM   5593  OE2 GLU B 181      28.330  22.681 -14.313  1.00220.39           O  
ANISOU 5593  OE2 GLU B 181    27125  31385  25230   -203   2540   1555       O  
ATOM   5594  N   VAL B 182      27.246  21.335  -8.144  1.00195.60           N  
ANISOU 5594  N   VAL B 182    24376  27614  22327   -650   2206    460       N  
ATOM   5595  CA  VAL B 182      26.246  21.842  -7.195  1.00195.07           C  
ANISOU 5595  CA  VAL B 182    24405  27391  22323   -634   2195    331       C  
ATOM   5596  C   VAL B 182      26.815  23.029  -6.379  1.00199.96           C  
ANISOU 5596  C   VAL B 182    25072  27793  23111   -815   2239    227       C  
ATOM   5597  O   VAL B 182      26.045  23.736  -5.725  1.00200.25           O  
ANISOU 5597  O   VAL B 182    25206  27655  23226   -785   2260    114       O  
ATOM   5598  CB  VAL B 182      25.660  20.735  -6.270  1.00197.16           C  
ANISOU 5598  CB  VAL B 182    24636  27799  22476   -589   2096    188       C  
ATOM   5599  CG1 VAL B 182      24.758  19.784  -7.050  1.00195.72           C  
ANISOU 5599  CG1 VAL B 182    24441  27745  22180   -437   2064    248       C  
ATOM   5600  CG2 VAL B 182      26.754  19.967  -5.525  1.00196.56           C  
ANISOU 5600  CG2 VAL B 182    24453  27875  22357   -702   2047    118       C  
ATOM   5601  N   GLN B 183      28.153  23.243  -6.428  1.00196.85           N  
ANISOU 5601  N   GLN B 183    24600  27427  22767  -1007   2256    250       N  
ATOM   5602  CA  GLN B 183      28.842  24.352  -5.759  1.00198.66           C  
ANISOU 5602  CA  GLN B 183    24851  27464  23168  -1246   2297    126       C  
ATOM   5603  C   GLN B 183      28.529  25.658  -6.498  1.00204.15           C  
ANISOU 5603  C   GLN B 183    25671  27802  24093  -1237   2430    274       C  
ATOM   5604  O   GLN B 183      28.414  26.711  -5.868  1.00205.99           O  
ANISOU 5604  O   GLN B 183    26010  27732  24523  -1352   2486    119       O  
ATOM   5605  CB  GLN B 183      30.359  24.098  -5.699  1.00200.53           C  
ANISOU 5605  CB  GLN B 183    24927  27908  23357  -1461   2274    145       C  
ATOM   5606  CG  GLN B 183      31.109  24.949  -4.668  1.00215.08           C  
ANISOU 5606  CG  GLN B 183    26736  29675  25311  -1764   2275    -83       C  
ATOM   5607  CD  GLN B 183      30.996  24.448  -3.242  1.00229.86           C  
ANISOU 5607  CD  GLN B 183    28532  31766  27036  -1791   2180   -362       C  
ATOM   5608  OE1 GLN B 183      30.968  23.240  -2.964  1.00222.43           O  
ANISOU 5608  OE1 GLN B 183    27487  31136  25892  -1654   2111   -325       O  
ATOM   5609  NE2 GLN B 183      30.984  25.376  -2.296  1.00222.74           N  
ANISOU 5609  NE2 GLN B 183    27667  30721  26242  -1973   2186   -646       N  
ATOM   5610  N   ASN B 184      28.384  25.573  -7.835  1.00199.92           N  
ANISOU 5610  N   ASN B 184    25113  27315  23531  -1085   2490    572       N  
ATOM   5611  CA  ASN B 184      28.019  26.689  -8.705  1.00201.78           C  
ANISOU 5611  CA  ASN B 184    25429  27278  23960  -1007   2638    818       C  
ATOM   5612  C   ASN B 184      26.533  27.010  -8.529  1.00204.97           C  
ANISOU 5612  C   ASN B 184    25969  27531  24378   -766   2678    788       C  
ATOM   5613  O   ASN B 184      26.141  28.172  -8.634  1.00207.12           O  
ANISOU 5613  O   ASN B 184    26363  27456  24878   -720   2815    880       O  
ATOM   5614  CB  ASN B 184      28.328  26.354 -10.175  1.00202.23           C  
ANISOU 5614  CB  ASN B 184    25355  27577  23905   -883   2680   1157       C  
ATOM   5615  CG  ASN B 184      29.790  26.121 -10.507  1.00223.78           C  
ANISOU 5615  CG  ASN B 184    27930  30493  26604  -1076   2661   1249       C  
ATOM   5616  OD1 ASN B 184      30.705  26.422  -9.730  1.00218.83           O  
ANISOU 5616  OD1 ASN B 184    27282  29782  26080  -1351   2639   1106       O  
ATOM   5617  ND2 ASN B 184      30.044  25.599 -11.699  1.00214.33           N  
ANISOU 5617  ND2 ASN B 184    26594  29603  25237   -931   2671   1490       N  
ATOM   5618  N   ILE B 185      25.717  25.972  -8.248  1.00198.54           N  
ANISOU 5618  N   ILE B 185    25129  26977  23331   -611   2568    674       N  
ATOM   5619  CA  ILE B 185      24.268  26.066  -8.046  1.00197.91           C  
ANISOU 5619  CA  ILE B 185    25132  26874  23192   -379   2580    651       C  
ATOM   5620  C   ILE B 185      23.980  26.647  -6.646  1.00202.74           C  
ANISOU 5620  C   ILE B 185    25860  27259  23915   -444   2570    361       C  
ATOM   5621  O   ILE B 185      24.565  26.209  -5.652  1.00201.47           O  
ANISOU 5621  O   ILE B 185    25652  27188  23711   -620   2469    114       O  
ATOM   5622  CB  ILE B 185      23.574  24.684  -8.272  1.00198.15           C  
ANISOU 5622  CB  ILE B 185    25063  27285  22941   -246   2460    635       C  
ATOM   5623  CG1 ILE B 185      23.941  24.090  -9.655  1.00198.05           C  
ANISOU 5623  CG1 ILE B 185    24926  27523  22801   -188   2466    846       C  
ATOM   5624  CG2 ILE B 185      22.048  24.789  -8.120  1.00198.81           C  
ANISOU 5624  CG2 ILE B 185    25192  27411  22934    -20   2470    645       C  
ATOM   5625  CD1 ILE B 185      23.738  22.569  -9.815  1.00202.57           C  
ANISOU 5625  CD1 ILE B 185    25401  28417  23148   -159   2339    743       C  
ATOM   5626  N   LYS B 186      23.075  27.638  -6.589  1.00201.34           N  
ANISOU 5626  N   LYS B 186    25816  26822  23862   -272   2684    398       N  
ATOM   5627  CA  LYS B 186      22.654  28.329  -5.372  1.00202.66           C  
ANISOU 5627  CA  LYS B 186    26108  26761  24133   -269   2701    112       C  
ATOM   5628  C   LYS B 186      21.280  27.800  -4.920  1.00204.34           C  
ANISOU 5628  C   LYS B 186    26305  27218  24116    -13   2635     64       C  
ATOM   5629  O   LYS B 186      20.306  27.891  -5.673  1.00203.98           O  
ANISOU 5629  O   LYS B 186    26266  27242  23995    242   2703    304       O  
ATOM   5630  CB  LYS B 186      22.621  29.848  -5.634  1.00209.27           C  
ANISOU 5630  CB  LYS B 186    27121  27092  25302   -229   2902    193       C  
ATOM   5631  CG  LYS B 186      22.141  30.719  -4.466  1.00224.97           C  
ANISOU 5631  CG  LYS B 186    29272  28777  27431   -188   2951   -137       C  
ATOM   5632  CD  LYS B 186      21.946  32.174  -4.859  1.00237.64           C  
ANISOU 5632  CD  LYS B 186    31074  29822  29396    -86   3185    -13       C  
ATOM   5633  CE  LYS B 186      20.670  32.436  -5.625  1.00247.33           C  
ANISOU 5633  CE  LYS B 186    32344  31067  30563    337   3316    336       C  
ATOM   5634  NZ  LYS B 186      20.586  33.860  -6.018  1.00260.46           N  
ANISOU 5634  NZ  LYS B 186    34198  32146  32618    452   3575    507       N  
ATOM   5635  N   PHE B 187      21.221  27.241  -3.695  1.00199.16           N  
ANISOU 5635  N   PHE B 187    25595  26748  23328    -84   2506   -220       N  
ATOM   5636  CA  PHE B 187      20.000  26.704  -3.095  1.00197.42           C  
ANISOU 5636  CA  PHE B 187    25326  26796  22888    120   2432   -268       C  
ATOM   5637  C   PHE B 187      19.470  27.707  -2.067  1.00203.37           C  
ANISOU 5637  C   PHE B 187    26198  27356  23717    232   2491   -514       C  
ATOM   5638  O   PHE B 187      19.808  27.650  -0.880  1.00203.37           O  
ANISOU 5638  O   PHE B 187    26157  27438  23677    115   2414   -820       O  
ATOM   5639  CB  PHE B 187      20.243  25.312  -2.487  1.00196.38           C  
ANISOU 5639  CB  PHE B 187    25020  27045  22550      0   2262   -351       C  
ATOM   5640  CG  PHE B 187      20.508  24.239  -3.516  1.00195.53           C  
ANISOU 5640  CG  PHE B 187    24815  27121  22356    -45   2214   -136       C  
ATOM   5641  CD1 PHE B 187      19.462  23.513  -4.073  1.00197.13           C  
ANISOU 5641  CD1 PHE B 187    24954  27553  22394    108   2178     23       C  
ATOM   5642  CD2 PHE B 187      21.804  23.954  -3.931  1.00197.10           C  
ANISOU 5642  CD2 PHE B 187    24974  27289  22626   -241   2205   -114       C  
ATOM   5643  CE1 PHE B 187      19.706  22.524  -5.030  1.00196.46           C  
ANISOU 5643  CE1 PHE B 187    24784  27628  22235     58   2135    154       C  
ATOM   5644  CE2 PHE B 187      22.047  22.963  -4.886  1.00198.21           C  
ANISOU 5644  CE2 PHE B 187    25031  27603  22678   -250   2168     47       C  
ATOM   5645  CZ  PHE B 187      20.997  22.254  -5.428  1.00195.17           C  
ANISOU 5645  CZ  PHE B 187    24600  27409  22147   -104   2134    156       C  
ATOM   5646  N   ASN B 188      18.658  28.656  -2.570  1.00201.64           N  
ANISOU 5646  N   ASN B 188    26116  26896  23601    482   2644   -371       N  
ATOM   5647  CA  ASN B 188      18.035  29.776  -1.857  1.00204.46           C  
ANISOU 5647  CA  ASN B 188    26630  26985  24070    671   2754   -560       C  
ATOM   5648  C   ASN B 188      17.156  29.342  -0.681  1.00207.19           C  
ANISOU 5648  C   ASN B 188    26889  27680  24152    822   2644   -768       C  
ATOM   5649  O   ASN B 188      17.041  30.099   0.282  1.00209.55           O  
ANISOU 5649  O   ASN B 188    27281  27822  24516    881   2683  -1083       O  
ATOM   5650  CB  ASN B 188      17.184  30.600  -2.837  1.00207.08           C  
ANISOU 5650  CB  ASN B 188    27080  27099  24503    990   2948   -235       C  
ATOM   5651  CG  ASN B 188      17.424  32.095  -2.813  1.00232.71           C  
ANISOU 5651  CG  ASN B 188    30561  29733  28124   1041   3161   -312       C  
ATOM   5652  OD1 ASN B 188      18.552  32.577  -2.655  1.00227.87           O  
ANISOU 5652  OD1 ASN B 188    30027  28771  27781    742   3190   -492       O  
ATOM   5653  ND2 ASN B 188      16.364  32.864  -3.026  1.00226.94           N  
ANISOU 5653  ND2 ASN B 188    29943  28853  27431   1422   3330   -150       N  
ATOM   5654  N   SER B 189      16.521  28.156  -0.770  1.00200.10           N  
ANISOU 5654  N   SER B 189    25807  27255  22966    884   2514   -598       N  
ATOM   5655  CA  SER B 189      15.614  27.641   0.252  1.00198.99           C  
ANISOU 5655  CA  SER B 189    25539  27508  22559   1030   2409   -703       C  
ATOM   5656  C   SER B 189      16.316  27.317   1.579  1.00201.75           C  
ANISOU 5656  C   SER B 189    25788  28018  22850    836   2290  -1042       C  
ATOM   5657  O   SER B 189      17.223  26.480   1.634  1.00199.41           O  
ANISOU 5657  O   SER B 189    25374  27856  22538    579   2191  -1044       O  
ATOM   5658  CB  SER B 189      14.864  26.407  -0.249  1.00199.76           C  
ANISOU 5658  CB  SER B 189    25453  28035  22412   1074   2306   -418       C  
ATOM   5659  OG  SER B 189      13.692  26.771  -0.958  1.00209.44           O  
ANISOU 5659  OG  SER B 189    26701  29327  23548   1363   2397   -173       O  
ATOM   5660  N   SER B 190      15.886  28.026   2.637  1.00199.91           N  
ANISOU 5660  N   SER B 190    25591  27797  22570    991   2315  -1326       N  
ATOM   5661  CA  SER B 190      16.244  27.823   4.037  1.00199.90           C  
ANISOU 5661  CA  SER B 190    25447  28079  22426    900   2208  -1663       C  
ATOM   5662  C   SER B 190      15.022  27.136   4.659  1.00201.33           C  
ANISOU 5662  C   SER B 190    25438  28777  22283   1147   2121  -1540       C  
ATOM   5663  O   SER B 190      13.920  27.310   4.133  1.00201.23           O  
ANISOU 5663  O   SER B 190    25475  28778  22207   1409   2182  -1319       O  
ATOM   5664  CB  SER B 190      16.584  29.147   4.722  1.00207.67           C  
ANISOU 5664  CB  SER B 190    26597  28733  23577    908   2304  -2102       C  
ATOM   5665  OG  SER B 190      15.448  29.984   4.872  1.00219.39           O  
ANISOU 5665  OG  SER B 190    28213  30103  25042   1273   2414  -2152       O  
ATOM   5666  N   GLY B 191      15.185  26.403   5.752  1.00177.54           N  
ANISOU 5666  N   GLY B 191    22188  24901  20367   -258   1099    879       N  
ATOM   5667  CA  GLY B 191      14.058  25.706   6.368  1.00176.49           C  
ANISOU 5667  CA  GLY B 191    22082  24778  20199   -303   1081    830       C  
ATOM   5668  C   GLY B 191      13.073  26.566   7.138  1.00178.34           C  
ANISOU 5668  C   GLY B 191    22314  25009  20438   -319   1096    832       C  
ATOM   5669  O   GLY B 191      13.409  27.673   7.570  1.00177.84           O  
ANISOU 5669  O   GLY B 191    22253  24904  20415   -312   1120    858       O  
ATOM   5670  N   GLN B 192      11.835  26.044   7.301  1.00173.43           N  
ANISOU 5670  N   GLN B 192    21692  24435  19769   -343   1086    806       N  
ATOM   5671  CA  GLN B 192      10.711  26.653   8.037  1.00172.54           C  
ANISOU 5671  CA  GLN B 192    21577  24342  19640   -349   1099    815       C  
ATOM   5672  C   GLN B 192      10.144  25.611   9.004  1.00173.99           C  
ANISOU 5672  C   GLN B 192    21786  24517  19805   -410   1063    776       C  
ATOM   5673  O   GLN B 192       9.879  24.488   8.567  1.00173.63           O  
ANISOU 5673  O   GLN B 192    21743  24503  19727   -444   1042    744       O  
ATOM   5674  CB  GLN B 192       9.607  27.158   7.078  1.00174.35           C  
ANISOU 5674  CB  GLN B 192    21754  24680  19811   -302   1133    847       C  
ATOM   5675  CG  GLN B 192      10.060  28.164   6.011  1.00193.76           C  
ANISOU 5675  CG  GLN B 192    24181  27157  22283   -226   1182    895       C  
ATOM   5676  CD  GLN B 192      10.486  27.527   4.701  1.00215.45           C  
ANISOU 5676  CD  GLN B 192    26894  29957  25011   -204   1172    886       C  
ATOM   5677  OE1 GLN B 192      10.612  26.301   4.567  1.00211.18           O  
ANISOU 5677  OE1 GLN B 192    26369  29420  24449   -250   1129    838       O  
ATOM   5678  NE2 GLN B 192      10.727  28.356   3.696  1.00208.46           N  
ANISOU 5678  NE2 GLN B 192    25967  29109  24130   -125   1219    936       N  
ATOM   5679  N   CYS B 193       9.962  25.953  10.304  1.00168.63           N  
ANISOU 5679  N   CYS B 193    21131  23794  19145   -423   1058    777       N  
ATOM   5680  CA  CYS B 193       9.473  24.966  11.275  1.00167.47           C  
ANISOU 5680  CA  CYS B 193    21005  23639  18988   -471   1028    748       C  
ATOM   5681  C   CYS B 193       7.977  24.718  11.150  1.00171.40           C  
ANISOU 5681  C   CYS B 193    21471  24227  19424   -487   1026    758       C  
ATOM   5682  O   CYS B 193       7.176  25.656  11.142  1.00171.21           O  
ANISOU 5682  O   CYS B 193    21422  24258  19370   -447   1050    799       O  
ATOM   5683  CB  CYS B 193       9.851  25.343  12.702  1.00166.97           C  
ANISOU 5683  CB  CYS B 193    20971  23510  18961   -471   1021    746       C  
ATOM   5684  SG  CYS B 193      11.636  25.377  12.996  1.00170.21           S  
ANISOU 5684  SG  CYS B 193    21402  23845  19426   -474   1015    732       S  
ATOM   5685  N   GLU B 194       7.620  23.428  11.057  1.00167.68           N  
ANISOU 5685  N   GLU B 194    21007  23775  18931   -548   1003    724       N  
ATOM   5686  CA  GLU B 194       6.250  22.936  10.946  1.00167.67           C  
ANISOU 5686  CA  GLU B 194    20972  23867  18866   -594    993    727       C  
ATOM   5687  C   GLU B 194       5.626  22.793  12.342  1.00169.95           C  
ANISOU 5687  C   GLU B 194    21269  24144  19161   -609    981    743       C  
ATOM   5688  O   GLU B 194       6.330  22.454  13.298  1.00169.38           O  
ANISOU 5688  O   GLU B 194    21239  23980  19139   -609    974    726       O  
ATOM   5689  CB  GLU B 194       6.244  21.586  10.203  1.00169.59           C  
ANISOU 5689  CB  GLU B 194    21234  24118  19086   -667    976    674       C  
ATOM   5690  CG  GLU B 194       4.915  21.202   9.572  1.00183.53           C  
ANISOU 5690  CG  GLU B 194    22948  26012  20772   -728    966    670       C  
ATOM   5691  CD  GLU B 194       4.448  22.002   8.370  1.00213.46           C  
ANISOU 5691  CD  GLU B 194    26670  29933  24505   -685    982    697       C  
ATOM   5692  OE1 GLU B 194       5.300  22.438   7.561  1.00213.95           O  
ANISOU 5692  OE1 GLU B 194    26735  29970  24587   -627    998    695       O  
ATOM   5693  OE2 GLU B 194       3.214  22.152   8.216  1.00211.03           O  
ANISOU 5693  OE2 GLU B 194    26295  29763  24123   -707    981    725       O  
ATOM   5694  N   VAL B 195       4.303  23.052  12.446  1.00165.38           N  
ANISOU 5694  N   VAL B 195    20641  23673  18522   -612    982    783       N  
ATOM   5695  CA  VAL B 195       3.498  22.963  13.675  1.00164.53           C  
ANISOU 5695  CA  VAL B 195    20527  23583  18404   -615    971    815       C  
ATOM   5696  C   VAL B 195       3.696  21.561  14.313  1.00167.00           C  
ANISOU 5696  C   VAL B 195    20875  23827  18750   -691    949    772       C  
ATOM   5697  O   VAL B 195       3.715  20.577  13.571  1.00166.68           O  
ANISOU 5697  O   VAL B 195    20845  23788  18697   -766    943    730       O  
ATOM   5698  CB  VAL B 195       2.008  23.283  13.352  1.00168.92           C  
ANISOU 5698  CB  VAL B 195    21011  24302  18869   -614    977    873       C  
ATOM   5699  CG1 VAL B 195       1.046  22.757  14.419  1.00168.95           C  
ANISOU 5699  CG1 VAL B 195    20996  24348  18850   -646    957    906       C  
ATOM   5700  CG2 VAL B 195       1.808  24.780  13.140  1.00168.70           C  
ANISOU 5700  CG2 VAL B 195    20968  24323  18809   -506   1017    934       C  
ATOM   5701  N   PRO B 196       3.951  21.433  15.639  1.00162.32           N  
ANISOU 5701  N   PRO B 196    20310  23165  18200   -668    945    780       N  
ATOM   5702  CA  PRO B 196       3.935  22.463  16.692  1.00161.32           C  
ANISOU 5702  CA  PRO B 196    20186  23025  18085   -586    950    820       C  
ATOM   5703  C   PRO B 196       5.304  23.078  17.030  1.00163.33           C  
ANISOU 5703  C   PRO B 196    20483  23177  18396   -537    957    793       C  
ATOM   5704  O   PRO B 196       5.501  23.547  18.157  1.00162.56           O  
ANISOU 5704  O   PRO B 196    20403  23043  18318   -491    955    803       O  
ATOM   5705  CB  PRO B 196       3.381  21.681  17.879  1.00163.17           C  
ANISOU 5705  CB  PRO B 196    20417  23257  18325   -603    936    836       C  
ATOM   5706  CG  PRO B 196       3.962  20.300  17.711  1.00167.84           C  
ANISOU 5706  CG  PRO B 196    21042  23780  18950   -675    937    784       C  
ATOM   5707  CD  PRO B 196       4.140  20.089  16.224  1.00163.78           C  
ANISOU 5707  CD  PRO B 196    20529  23285  18413   -726    940    749       C  
ATOM   5708  N   LEU B 197       6.240  23.091  16.071  1.00158.84           N  
ANISOU 5708  N   LEU B 197    19929  22574  17849   -549    965    761       N  
ATOM   5709  CA  LEU B 197       7.558  23.669  16.313  1.00157.82           C  
ANISOU 5709  CA  LEU B 197    19829  22368  17767   -517    971    743       C  
ATOM   5710  C   LEU B 197       7.605  25.103  15.792  1.00161.74           C  
ANISOU 5710  C   LEU B 197    20322  22873  18257   -472    993    767       C  
ATOM   5711  O   LEU B 197       6.854  25.459  14.881  1.00161.32           O  
ANISOU 5711  O   LEU B 197    20243  22889  18165   -460   1009    794       O  
ATOM   5712  CB  LEU B 197       8.680  22.814  15.694  1.00157.58           C  
ANISOU 5712  CB  LEU B 197    19819  22293  17762   -545    971    707       C  
ATOM   5713  CG  LEU B 197       8.805  21.362  16.195  1.00162.06           C  
ANISOU 5713  CG  LEU B 197    20411  22830  18335   -579    969    685       C  
ATOM   5714  CD1 LEU B 197       9.581  20.511  15.213  1.00162.37           C  
ANISOU 5714  CD1 LEU B 197    20480  22842  18373   -599    981    659       C  
ATOM   5715  CD2 LEU B 197       9.464  21.290  17.562  1.00163.86           C  
ANISOU 5715  CD2 LEU B 197    20651  23017  18592   -548    969    684       C  
ATOM   5716  N   VAL B 198       8.460  25.931  16.403  1.00158.80           N  
ANISOU 5716  N   VAL B 198    19980  22437  17921   -447    998    759       N  
ATOM   5717  CA  VAL B 198       8.650  27.336  16.042  1.00159.32           C  
ANISOU 5717  CA  VAL B 198    20063  22482  17991   -411   1029    778       C  
ATOM   5718  C   VAL B 198      10.139  27.552  15.679  1.00164.92           C  
ANISOU 5718  C   VAL B 198    20781  23132  18749   -433   1029    753       C  
ATOM   5719  O   VAL B 198      11.024  26.892  16.240  1.00164.57           O  
ANISOU 5719  O   VAL B 198    20738  23062  18729   -462   1004    724       O  
ATOM   5720  CB  VAL B 198       8.120  28.312  17.150  1.00163.30           C  
ANISOU 5720  CB  VAL B 198    20605  22963  18478   -366   1041    796       C  
ATOM   5721  CG1 VAL B 198       8.897  28.203  18.461  1.00163.06           C  
ANISOU 5721  CG1 VAL B 198    20601  22875  18480   -383   1014    757       C  
ATOM   5722  CG2 VAL B 198       8.066  29.758  16.663  1.00163.39           C  
ANISOU 5722  CG2 VAL B 198    20651  22948  18480   -322   1093    825       C  
ATOM   5723  N   ARG B 199      10.391  28.448  14.704  1.00162.69           N  
ANISOU 5723  N   ARG B 199    20497  22842  18473   -414   1063    774       N  
ATOM   5724  CA  ARG B 199      11.720  28.792  14.208  1.00163.01           C  
ANISOU 5724  CA  ARG B 199    20538  22841  18558   -433   1068    767       C  
ATOM   5725  C   ARG B 199      12.536  29.493  15.296  1.00168.20           C  
ANISOU 5725  C   ARG B 199    21231  23433  19246   -462   1061    742       C  
ATOM   5726  O   ARG B 199      12.093  30.496  15.871  1.00168.04           O  
ANISOU 5726  O   ARG B 199    21254  23373  19218   -446   1084    745       O  
ATOM   5727  CB  ARG B 199      11.609  29.670  12.944  1.00163.63           C  
ANISOU 5727  CB  ARG B 199    20606  22932  18636   -396   1115    806       C  
ATOM   5728  CG  ARG B 199      12.929  29.954  12.220  1.00174.43           C  
ANISOU 5728  CG  ARG B 199    21959  24269  20046   -411   1123    812       C  
ATOM   5729  CD  ARG B 199      13.408  28.800  11.351  1.00183.54           C  
ANISOU 5729  CD  ARG B 199    23073  25471  21195   -413   1097    810       C  
ATOM   5730  NE  ARG B 199      14.616  29.144  10.599  1.00191.16           N  
ANISOU 5730  NE  ARG B 199    24017  26423  22194   -411   1108    833       N  
ATOM   5731  CZ  ARG B 199      15.857  28.983  11.050  1.00204.60           C  
ANISOU 5731  CZ  ARG B 199    25715  28102  23920   -449   1085    827       C  
ATOM   5732  NH1 ARG B 199      16.074  28.481  12.261  1.00192.10           N  
ANISOU 5732  NH1 ARG B 199    24149  26508  22333   -487   1053    793       N  
ATOM   5733  NH2 ARG B 199      16.892  29.327  10.295  1.00190.35           N  
ANISOU 5733  NH2 ARG B 199    23883  26301  22141   -445   1096    861       N  
ATOM   5734  N   THR B 200      13.719  28.933  15.590  1.00165.64           N  
ANISOU 5734  N   THR B 200    20888  23103  18943   -502   1032    719       N  
ATOM   5735  CA  THR B 200      14.647  29.464  16.589  1.00166.24           C  
ANISOU 5735  CA  THR B 200    20980  23145  19040   -544   1018    691       C  
ATOM   5736  C   THR B 200      16.085  29.223  16.130  1.00170.20           C  
ANISOU 5736  C   THR B 200    21442  23665  19560   -580   1007    697       C  
ATOM   5737  O   THR B 200      16.387  28.202  15.504  1.00169.40           O  
ANISOU 5737  O   THR B 200    21310  23606  19450   -562    999    714       O  
ATOM   5738  CB  THR B 200      14.368  28.893  18.001  1.00178.90           C  
ANISOU 5738  CB  THR B 200    22590  24760  20623   -543    988    660       C  
ATOM   5739  OG1 THR B 200      15.290  29.466  18.933  1.00181.52           O  
ANISOU 5739  OG1 THR B 200    22931  25076  20964   -588    973    627       O  
ATOM   5740  CG2 THR B 200      14.430  27.356  18.061  1.00177.95           C  
ANISOU 5740  CG2 THR B 200    22435  24690  20488   -531    968    661       C  
ATOM   5741  N   ASP B 201      16.964  30.181  16.441  1.00167.40           N  
ANISOU 5741  N   ASP B 201    21096  23281  19227   -632   1009    686       N  
ATOM   5742  CA  ASP B 201      18.375  30.096  16.088  1.00167.59           C  
ANISOU 5742  CA  ASP B 201    21073  23340  19263   -673    998    703       C  
ATOM   5743  C   ASP B 201      19.213  29.733  17.323  1.00171.11           C  
ANISOU 5743  C   ASP B 201    21493  23833  19687   -716    962    671       C  
ATOM   5744  O   ASP B 201      20.391  29.400  17.177  1.00171.00           O  
ANISOU 5744  O   ASP B 201    21426  23882  19663   -741    950    693       O  
ATOM   5745  CB  ASP B 201      18.849  31.405  15.428  1.00170.24           C  
ANISOU 5745  CB  ASP B 201    21422  23625  19636   -713   1029    722       C  
ATOM   5746  CG  ASP B 201      18.234  31.656  14.056  1.00181.95           C  
ANISOU 5746  CG  ASP B 201    22908  25090  21134   -652   1071    767       C  
ATOM   5747  OD1 ASP B 201      18.415  30.802  13.154  1.00182.49           O  
ANISOU 5747  OD1 ASP B 201    22932  25212  21193   -610   1065    800       O  
ATOM   5748  OD2 ASP B 201      17.593  32.713  13.877  1.00188.24           O  
ANISOU 5748  OD2 ASP B 201    23755  25823  21946   -641   1116    772       O  
ATOM   5749  N   ASN B 202      18.590  29.748  18.528  1.00167.13           N  
ANISOU 5749  N   ASN B 202    21019  23315  19167   -714    949    628       N  
ATOM   5750  CA  ASN B 202      19.235  29.389  19.793  1.00166.98           C  
ANISOU 5750  CA  ASN B 202    20971  23355  19118   -740    918    596       C  
ATOM   5751  C   ASN B 202      19.399  27.852  19.867  1.00171.01           C  
ANISOU 5751  C   ASN B 202    21437  23939  19598   -681    913    621       C  
ATOM   5752  O   ASN B 202      18.401  27.134  19.764  1.00169.95           O  
ANISOU 5752  O   ASN B 202    21326  23786  19462   -625    922    628       O  
ATOM   5753  CB  ASN B 202      18.441  29.941  20.991  1.00165.76           C  
ANISOU 5753  CB  ASN B 202    20868  23160  18954   -740    910    546       C  
ATOM   5754  CG  ASN B 202      19.026  29.608  22.345  1.00179.75           C  
ANISOU 5754  CG  ASN B 202    22605  25003  20690   -757    879    509       C  
ATOM   5755  OD1 ASN B 202      18.386  28.957  23.175  1.00171.77           O  
ANISOU 5755  OD1 ASN B 202    21594  24013  19657   -700    871    499       O  
ATOM   5756  ND2 ASN B 202      20.246  30.058  22.611  1.00170.02           N  
ANISOU 5756  ND2 ASN B 202    21334  23821  19444   -837    862    490       N  
ATOM   5757  N   PRO B 203      20.647  27.334  20.022  1.00168.37           N  
ANISOU 5757  N   PRO B 203    21043  23695  19234   -693    905    641       N  
ATOM   5758  CA  PRO B 203      20.854  25.870  20.025  1.00167.81           C  
ANISOU 5758  CA  PRO B 203    20948  23686  19128   -622    919    675       C  
ATOM   5759  C   PRO B 203      20.352  25.135  21.272  1.00170.87           C  
ANISOU 5759  C   PRO B 203    21337  24096  19490   -578    919    652       C  
ATOM   5760  O   PRO B 203      20.168  23.917  21.211  1.00169.99           O  
ANISOU 5760  O   PRO B 203    21232  23998  19359   -514    944    678       O  
ATOM   5761  CB  PRO B 203      22.378  25.722  19.903  1.00170.12           C  
ANISOU 5761  CB  PRO B 203    21173  24082  19382   -639    918    715       C  
ATOM   5762  CG  PRO B 203      22.886  27.078  19.503  1.00175.19           C  
ANISOU 5762  CG  PRO B 203    21803  24706  20055   -729    901    707       C  
ATOM   5763  CD  PRO B 203      21.934  28.046  20.115  1.00170.79           C  
ANISOU 5763  CD  PRO B 203    21303  24058  19531   -769    891    643       C  
ATOM   5764  N   LYS B 204      20.144  25.853  22.390  1.00167.34           N  
ANISOU 5764  N   LYS B 204    20891  23651  19041   -609    896    605       N  
ATOM   5765  CA  LYS B 204      19.674  25.279  23.658  1.00166.84           C  
ANISOU 5765  CA  LYS B 204    20821  23617  18953   -559    895    586       C  
ATOM   5766  C   LYS B 204      18.171  24.946  23.615  1.00169.63           C  
ANISOU 5766  C   LYS B 204    21228  23890  19332   -513    904    586       C  
ATOM   5767  O   LYS B 204      17.692  24.159  24.436  1.00168.71           O  
ANISOU 5767  O   LYS B 204    21106  23794  19201   -457    914    589       O  
ATOM   5768  CB  LYS B 204      19.965  26.243  24.825  1.00169.80           C  
ANISOU 5768  CB  LYS B 204    21182  24024  19310   -606    864    532       C  
ATOM   5769  CG  LYS B 204      21.457  26.515  25.057  1.00182.77           C  
ANISOU 5769  CG  LYS B 204    22755  25778  20913   -665    850    530       C  
ATOM   5770  CD  LYS B 204      21.744  27.279  26.353  1.00192.06           C  
ANISOU 5770  CD  LYS B 204    23912  27005  22056   -715    817    466       C  
ATOM   5771  CE  LYS B 204      21.721  28.780  26.183  1.00201.83           C  
ANISOU 5771  CE  LYS B 204    25206  28158  23324   -821    796    412       C  
ATOM   5772  NZ  LYS B 204      20.373  29.341  26.448  1.00210.16           N  
ANISOU 5772  NZ  LYS B 204    26355  29088  24409   -791    798    380       N  
ATOM   5773  N   SER B 205      17.440  25.539  22.649  1.00165.96           N  
ANISOU 5773  N   SER B 205    20808  23347  18901   -535    906    588       N  
ATOM   5774  CA  SER B 205      15.992  25.388  22.470  1.00165.36           C  
ANISOU 5774  CA  SER B 205    20773  23218  18839   -503    913    595       C  
ATOM   5775  C   SER B 205      15.600  24.353  21.396  1.00168.63           C  
ANISOU 5775  C   SER B 205    21194  23620  19257   -484    935    628       C  
ATOM   5776  O   SER B 205      14.419  24.000  21.317  1.00167.88           O  
ANISOU 5776  O   SER B 205    21119  23503  19163   -466    939    636       O  
ATOM   5777  CB  SER B 205      15.370  26.734  22.106  1.00169.06           C  
ANISOU 5777  CB  SER B 205    21285  23626  19325   -528    911    584       C  
ATOM   5778  OG  SER B 205      15.735  27.752  23.024  1.00178.54           O  
ANISOU 5778  OG  SER B 205    22501  24818  20519   -556    895    545       O  
ATOM   5779  N   TRP B 206      16.571  23.865  20.581  1.00165.17           N  
ANISOU 5779  N   TRP B 206    20740  23203  18814   -489    947    647       N  
ATOM   5780  CA  TRP B 206      16.325  22.908  19.497  1.00164.71           C  
ANISOU 5780  CA  TRP B 206    20702  23129  18751   -473    969    670       C  
ATOM   5781  C   TRP B 206      15.812  21.558  20.010  1.00168.31           C  
ANISOU 5781  C   TRP B 206    21177  23582  19190   -439    991    675       C  
ATOM   5782  O   TRP B 206      16.400  20.972  20.922  1.00168.03           O  
ANISOU 5782  O   TRP B 206    21126  23582  19136   -405   1006    682       O  
ATOM   5783  CB  TRP B 206      17.574  22.698  18.626  1.00163.53           C  
ANISOU 5783  CB  TRP B 206    20537  23007  18589   -469    981    696       C  
ATOM   5784  CG  TRP B 206      18.048  23.921  17.884  1.00164.54           C  
ANISOU 5784  CG  TRP B 206    20646  23131  18739   -506    967    702       C  
ATOM   5785  CD1 TRP B 206      17.324  25.040  17.590  1.00167.40           C  
ANISOU 5785  CD1 TRP B 206    21023  23451  19130   -533    959    688       C  
ATOM   5786  CD2 TRP B 206      19.347  24.117  17.293  1.00164.63           C  
ANISOU 5786  CD2 TRP B 206    20625  23184  18743   -512    969    734       C  
ATOM   5787  NE1 TRP B 206      18.104  25.942  16.898  1.00167.09           N  
ANISOU 5787  NE1 TRP B 206    20966  23412  19110   -560    960    704       N  
ATOM   5788  CE2 TRP B 206      19.347  25.396  16.692  1.00168.70           C  
ANISOU 5788  CE2 TRP B 206    21135  23670  19292   -553    962    733       C  
ATOM   5789  CE3 TRP B 206      20.528  23.354  17.250  1.00166.04           C  
ANISOU 5789  CE3 TRP B 206    20777  23430  18882   -480    983    772       C  
ATOM   5790  CZ2 TRP B 206      20.477  25.921  16.038  1.00168.31           C  
ANISOU 5790  CZ2 TRP B 206    21049  23653  19249   -574    962    768       C  
ATOM   5791  CZ3 TRP B 206      21.640  23.870  16.593  1.00167.79           C  
ANISOU 5791  CZ3 TRP B 206    20957  23697  19098   -495    979    811       C  
ATOM   5792  CH2 TRP B 206      21.609  25.139  16.001  1.00168.55           C  
ANISOU 5792  CH2 TRP B 206    21044  23760  19239   -547    966    808       C  
ATOM   5793  N   TYR B 207      14.710  21.075  19.400  1.00164.56           N  
ANISOU 5793  N   TYR B 207    20733  23073  18719   -450    997    673       N  
ATOM   5794  CA  TYR B 207      14.028  19.827  19.732  1.00164.40           C  
ANISOU 5794  CA  TYR B 207    20740  23033  18689   -439   1021    676       C  
ATOM   5795  C   TYR B 207      14.798  18.647  19.169  1.00168.08           C  
ANISOU 5795  C   TYR B 207    21245  23486  19133   -417   1062    689       C  
ATOM   5796  O   TYR B 207      14.750  18.386  17.963  1.00167.56           O  
ANISOU 5796  O   TYR B 207    21210  23398  19058   -436   1067    685       O  
ATOM   5797  CB  TYR B 207      12.572  19.853  19.220  1.00165.69           C  
ANISOU 5797  CB  TYR B 207    20917  23182  18856   -477   1009    670       C  
ATOM   5798  CG  TYR B 207      11.838  18.531  19.315  1.00167.97           C  
ANISOU 5798  CG  TYR B 207    21240  23446  19136   -494   1034    670       C  
ATOM   5799  CD1 TYR B 207      11.488  17.988  20.549  1.00170.15           C  
ANISOU 5799  CD1 TYR B 207    21512  23720  19416   -470   1048    682       C  
ATOM   5800  CD2 TYR B 207      11.468  17.835  18.170  1.00168.98           C  
ANISOU 5800  CD2 TYR B 207    21406  23552  19248   -537   1046    657       C  
ATOM   5801  CE1 TYR B 207      10.810  16.771  20.639  1.00171.38           C  
ANISOU 5801  CE1 TYR B 207    21704  23844  19569   -494   1079    686       C  
ATOM   5802  CE2 TYR B 207      10.785  16.623  18.247  1.00170.30           C  
ANISOU 5802  CE2 TYR B 207    21615  23685  19404   -572   1072    651       C  
ATOM   5803  CZ  TYR B 207      10.460  16.093  19.483  1.00177.98           C  
ANISOU 5803  CZ  TYR B 207    22586  24648  20389   -553   1091    667       C  
ATOM   5804  OH  TYR B 207       9.796  14.893  19.550  1.00179.32           O  
ANISOU 5804  OH  TYR B 207    22803  24775  20555   -596   1124    664       O  
ATOM   5805  N   GLU B 208      15.518  17.944  20.078  1.00164.82           N  
ANISOU 5805  N   GLU B 208    20831  23092  18702   -366   1096    707       N  
ATOM   5806  CA  GLU B 208      16.385  16.769  19.895  1.00164.94           C  
ANISOU 5806  CA  GLU B 208    20888  23103  18680   -315   1154    734       C  
ATOM   5807  C   GLU B 208      17.240  16.868  18.604  1.00168.88           C  
ANISOU 5807  C   GLU B 208    21403  23607  19158   -311   1156    748       C  
ATOM   5808  O   GLU B 208      18.045  17.799  18.493  1.00168.55           O  
ANISOU 5808  O   GLU B 208    21306  23619  19115   -311   1128    760       O  
ATOM   5809  CB  GLU B 208      15.613  15.422  19.988  1.00166.58           C  
ANISOU 5809  CB  GLU B 208    21168  23242  18883   -313   1205    732       C  
ATOM   5810  CG  GLU B 208      14.257  15.336  19.301  1.00176.98           C  
ANISOU 5810  CG  GLU B 208    22517  24507  20222   -392   1181    699       C  
ATOM   5811  CD  GLU B 208      13.534  14.029  19.547  1.00198.54           C  
ANISOU 5811  CD  GLU B 208    25315  27172  22948   -408   1232    697       C  
ATOM   5812  OE1 GLU B 208      13.873  13.029  18.876  1.00196.13           O  
ANISOU 5812  OE1 GLU B 208    25095  26811  22616   -403   1283    695       O  
ATOM   5813  OE2 GLU B 208      12.632  14.002  20.415  1.00191.27           O  
ANISOU 5813  OE2 GLU B 208    24369  26254  22051   -425   1223    699       O  
ATOM   5814  N   ASP B 209      17.071  15.917  17.657  1.00165.26           N  
ANISOU 5814  N   ASP B 209    21020  23091  18678   -308   1191    746       N  
ATOM   5815  CA  ASP B 209      17.796  15.827  16.390  1.00164.75           C  
ANISOU 5815  CA  ASP B 209    20984  23027  18585   -288   1198    762       C  
ATOM   5816  C   ASP B 209      17.315  16.866  15.336  1.00167.25           C  
ANISOU 5816  C   ASP B 209    21268  23349  18931   -343   1143    739       C  
ATOM   5817  O   ASP B 209      18.083  17.182  14.424  1.00166.72           O  
ANISOU 5817  O   ASP B 209    21190  23306  18849   -318   1138    762       O  
ATOM   5818  CB  ASP B 209      17.726  14.393  15.829  1.00166.85           C  
ANISOU 5818  CB  ASP B 209    21362  23224  18811   -262   1261    762       C  
ATOM   5819  CG  ASP B 209      16.390  13.668  15.961  1.00174.40           C  
ANISOU 5819  CG  ASP B 209    22377  24102  19784   -326   1272    717       C  
ATOM   5820  OD1 ASP B 209      15.340  14.350  16.001  1.00174.60           O  
ANISOU 5820  OD1 ASP B 209    22356  24137  19849   -398   1220    684       O  
ATOM   5821  OD2 ASP B 209      16.392  12.419  15.943  1.00178.58           O  
ANISOU 5821  OD2 ASP B 209    23005  24564  20283   -305   1339    718       O  
ATOM   5822  N   VAL B 210      16.084  17.412  15.477  1.00162.77           N  
ANISOU 5822  N   VAL B 210    20679  22767  18398   -405   1108    703       N  
ATOM   5823  CA  VAL B 210      15.524  18.450  14.591  1.00161.93           C  
ANISOU 5823  CA  VAL B 210    20537  22678  18313   -443   1068    689       C  
ATOM   5824  C   VAL B 210      16.119  19.813  15.004  1.00165.99           C  
ANISOU 5824  C   VAL B 210    20984  23230  18854   -437   1041    707       C  
ATOM   5825  O   VAL B 210      15.627  20.454  15.940  1.00165.55           O  
ANISOU 5825  O   VAL B 210    20902  23180  18821   -456   1023    696       O  
ATOM   5826  CB  VAL B 210      13.967  18.464  14.605  1.00165.20           C  
ANISOU 5826  CB  VAL B 210    20952  23081  18735   -500   1051    658       C  
ATOM   5827  CG1 VAL B 210      13.391  19.540  13.671  1.00164.69           C  
ANISOU 5827  CG1 VAL B 210    20846  23052  18676   -520   1023    656       C  
ATOM   5828  CG2 VAL B 210      13.404  17.083  14.281  1.00165.27           C  
ANISOU 5828  CG2 VAL B 210    21032  23048  18716   -529   1078    634       C  
ATOM   5829  N   GLU B 211      17.196  20.230  14.323  1.00162.91           N  
ANISOU 5829  N   GLU B 211    20572  22866  18459   -413   1041    736       N  
ATOM   5830  CA  GLU B 211      17.895  21.480  14.630  1.00162.87           C  
ANISOU 5830  CA  GLU B 211    20510  22894  18480   -424   1021    753       C  
ATOM   5831  C   GLU B 211      17.276  22.655  13.868  1.00166.49           C  
ANISOU 5831  C   GLU B 211    20950  23341  18970   -450   1005    747       C  
ATOM   5832  O   GLU B 211      16.920  22.516  12.695  1.00166.07           O  
ANISOU 5832  O   GLU B 211    20905  23285  18908   -438   1011    751       O  
ATOM   5833  CB  GLU B 211      19.396  21.349  14.327  1.00164.63           C  
ANISOU 5833  CB  GLU B 211    20710  23165  18678   -389   1032    799       C  
ATOM   5834  CG  GLU B 211      20.121  20.336  15.207  1.00176.65           C  
ANISOU 5834  CG  GLU B 211    22241  24720  20156   -347   1059    819       C  
ATOM   5835  CD  GLU B 211      21.536  19.949  14.812  1.00200.04           C  
ANISOU 5835  CD  GLU B 211    25186  27749  23069   -290   1082    882       C  
ATOM   5836  OE1 GLU B 211      22.153  20.673  13.996  1.00199.36           O  
ANISOU 5836  OE1 GLU B 211    25063  27694  22992   -296   1066    913       O  
ATOM   5837  OE2 GLU B 211      22.036  18.927  15.334  1.00194.09           O  
ANISOU 5837  OE2 GLU B 211    24456  27025  22265   -232   1122    909       O  
ATOM   5838  N   GLY B 212      17.157  23.790  14.555  1.00163.05           N  
ANISOU 5838  N   GLY B 212    20491  22899  18562   -480    992    738       N  
ATOM   5839  CA  GLY B 212      16.553  25.013  14.037  1.00162.97           C  
ANISOU 5839  CA  GLY B 212    20474  22871  18578   -494    993    739       C  
ATOM   5840  C   GLY B 212      15.114  25.186  14.492  1.00167.25           C  
ANISOU 5840  C   GLY B 212    21035  23397  19116   -498    992    718       C  
ATOM   5841  O   GLY B 212      14.531  26.261  14.315  1.00166.85           O  
ANISOU 5841  O   GLY B 212    20985  23333  19075   -497   1003    724       O  
ATOM   5842  N   CYS B 213      14.536  24.120  15.089  1.00164.31           N  
ANISOU 5842  N   CYS B 213    20679  23029  18723   -498    985    700       N  
ATOM   5843  CA  CYS B 213      13.152  24.080  15.562  1.00164.39           C  
ANISOU 5843  CA  CYS B 213    20699  23042  18721   -502    982    691       C  
ATOM   5844  C   CYS B 213      13.065  23.795  17.057  1.00166.46           C  
ANISOU 5844  C   CYS B 213    20967  23296  18984   -501    971    678       C  
ATOM   5845  O   CYS B 213      13.758  22.914  17.552  1.00166.17           O  
ANISOU 5845  O   CYS B 213    20933  23260  18944   -494    974    673       O  
ATOM   5846  CB  CYS B 213      12.362  23.042  14.772  1.00165.40           C  
ANISOU 5846  CB  CYS B 213    20835  23190  18821   -512    986    686       C  
ATOM   5847  SG  CYS B 213      12.202  23.418  13.012  1.00169.91           S  
ANISOU 5847  SG  CYS B 213    21389  23795  19377   -503    997    699       S  
ATOM   5848  N   GLY B 214      12.164  24.501  17.738  1.00161.30           N  
ANISOU 5848  N   GLY B 214    20316  22642  18327   -493    965    680       N  
ATOM   5849  CA  GLY B 214      11.889  24.327  19.162  1.00160.18           C  
ANISOU 5849  CA  GLY B 214    20177  22500  18182   -478    954    671       C  
ATOM   5850  C   GLY B 214      10.397  24.237  19.415  1.00161.53           C  
ANISOU 5850  C   GLY B 214    20349  22694  18330   -465    952    691       C  
ATOM   5851  O   GLY B 214       9.626  24.862  18.684  1.00161.36           O  
ANISOU 5851  O   GLY B 214    20327  22692  18292   -461    961    711       O  
ATOM   5852  N   ILE B 215       9.964  23.448  20.430  1.00155.50           N  
ANISOU 5852  N   ILE B 215    19581  21941  17561   -452    946    694       N  
ATOM   5853  CA  ILE B 215       8.535  23.281  20.749  1.00153.95           C  
ANISOU 5853  CA  ILE B 215    19374  21780  17339   -442    942    724       C  
ATOM   5854  C   ILE B 215       7.982  24.628  21.208  1.00155.39           C  
ANISOU 5854  C   ILE B 215    19568  21972  17503   -397    939    744       C  
ATOM   5855  O   ILE B 215       8.589  25.256  22.071  1.00154.68           O  
ANISOU 5855  O   ILE B 215    19496  21853  17424   -372    933    725       O  
ATOM   5856  CB  ILE B 215       8.245  22.158  21.792  1.00156.73           C  
ANISOU 5856  CB  ILE B 215    19717  22138  17695   -432    941    732       C  
ATOM   5857  CG1 ILE B 215       9.105  20.902  21.551  1.00157.03           C  
ANISOU 5857  CG1 ILE B 215    19768  22145  17750   -457    961    711       C  
ATOM   5858  CG2 ILE B 215       6.745  21.804  21.812  1.00157.37           C  
ANISOU 5858  CG2 ILE B 215    19778  22268  17746   -443    937    771       C  
ATOM   5859  CD1 ILE B 215       9.370  20.040  22.794  1.00164.36           C  
ANISOU 5859  CD1 ILE B 215    20693  23067  18689   -420    976    717       C  
ATOM   5860  N   GLN B 216       6.854  25.077  20.619  1.00150.66           N  
ANISOU 5860  N   GLN B 216    18960  21419  16865   -386    949    783       N  
ATOM   5861  CA  GLN B 216       6.204  26.353  20.954  1.00150.01           C  
ANISOU 5861  CA  GLN B 216    18901  21347  16748   -325    963    817       C  
ATOM   5862  C   GLN B 216       5.835  26.413  22.450  1.00153.21           C  
ANISOU 5862  C   GLN B 216    19318  21753  17142   -273    948    829       C  
ATOM   5863  O   GLN B 216       5.570  25.371  23.059  1.00152.96           O  
ANISOU 5863  O   GLN B 216    19256  21746  17117   -281    931    836       O  
ATOM   5864  CB  GLN B 216       4.964  26.609  20.068  1.00151.34           C  
ANISOU 5864  CB  GLN B 216    19043  21598  16859   -310    983    873       C  
ATOM   5865  CG  GLN B 216       3.838  25.566  20.178  1.00159.75           C  
ANISOU 5865  CG  GLN B 216    20057  22750  17890   -333    966    909       C  
ATOM   5866  CD  GLN B 216       2.593  25.903  19.388  1.00172.24           C  
ANISOU 5866  CD  GLN B 216    21599  24446  19397   -317    985    972       C  
ATOM   5867  OE1 GLN B 216       2.376  27.040  18.942  1.00165.74           O  
ANISOU 5867  OE1 GLN B 216    20793  23643  18538   -257   1020   1005       O  
ATOM   5868  NE2 GLN B 216       1.724  24.916  19.230  1.00163.43           N  
ANISOU 5868  NE2 GLN B 216    20429  23415  18251   -369    967    995       N  
ATOM   5869  N   CYS B 217       5.842  27.630  23.029  1.00173.81           N  
ANISOU 5869  N   CYS B 217    19211  31817  15012  -2406   1909   2423       N  
ATOM   5870  CA  CYS B 217       5.567  27.891  24.446  1.00170.76           C  
ANISOU 5870  CA  CYS B 217    19018  30967  14897  -2341   1855   2482       C  
ATOM   5871  C   CYS B 217       4.193  27.352  24.898  1.00171.86           C  
ANISOU 5871  C   CYS B 217    19146  31006  15149  -2098   1745   2411       C  
ATOM   5872  O   CYS B 217       4.110  26.705  25.950  1.00169.43           O  
ANISOU 5872  O   CYS B 217    18808  30464  15106  -2049   1690   2246       O  
ATOM   5873  CB  CYS B 217       5.699  29.376  24.756  1.00171.98           C  
ANISOU 5873  CB  CYS B 217    19503  30847  14994  -2415   1903   2838       C  
ATOM   5874  SG  CYS B 217       5.226  29.813  26.448  1.00173.42           S  
ANISOU 5874  SG  CYS B 217    19944  30476  15472  -2319   1840   2920       S  
ATOM   5875  N   GLN B 218       3.125  27.643  24.130  1.00168.40           N  
ANISOU 5875  N   GLN B 218    18730  30753  14501  -1951   1712   2547       N  
ATOM   5876  CA  GLN B 218       1.774  27.173  24.440  1.00166.38           C  
ANISOU 5876  CA  GLN B 218    18439  30465  14314  -1730   1611   2486       C  
ATOM   5877  C   GLN B 218       1.698  25.681  24.139  1.00168.13           C  
ANISOU 5877  C   GLN B 218    18349  30932  14602  -1721   1576   2110       C  
ATOM   5878  O   GLN B 218       2.036  25.266  23.029  1.00169.30           O  
ANISOU 5878  O   GLN B 218    18308  31457  14562  -1791   1614   1988       O  
ATOM   5879  CB  GLN B 218       0.721  27.959  23.643  1.00169.56           C  
ANISOU 5879  CB  GLN B 218    18938  31038  14449  -1575   1587   2749       C  
ATOM   5880  CG  GLN B 218      -0.667  27.922  24.263  1.00178.94           C  
ANISOU 5880  CG  GLN B 218    20180  32084  15724  -1341   1491   2786       C  
ATOM   5881  CD  GLN B 218      -1.736  28.050  23.215  1.00197.73           C  
ANISOU 5881  CD  GLN B 218    22480  34822  17828  -1180   1446   2886       C  
ATOM   5882  OE1 GLN B 218      -2.134  27.067  22.582  1.00192.86           O  
ANISOU 5882  OE1 GLN B 218    21600  34544  17134  -1160   1407   2648       O  
ATOM   5883  NE2 GLN B 218      -2.216  29.266  23.002  1.00191.63           N  
ANISOU 5883  NE2 GLN B 218    21933  33984  16895  -1060   1450   3238       N  
ATOM   5884  N   ASN B 219       1.305  24.879  25.150  1.00161.34           N  
ANISOU 5884  N   ASN B 219    17444  29848  14012  -1648   1512   1925       N  
ATOM   5885  CA  ASN B 219       1.195  23.421  25.087  1.00159.84           C  
ANISOU 5885  CA  ASN B 219    16996  29790  13944  -1638   1478   1565       C  
ATOM   5886  C   ASN B 219       0.449  22.990  23.815  1.00164.01           C  
ANISOU 5886  C   ASN B 219    17338  30752  14227  -1581   1459   1463       C  
ATOM   5887  O   ASN B 219      -0.739  23.290  23.673  1.00163.86           O  
ANISOU 5887  O   ASN B 219    17359  30800  14101  -1440   1400   1584       O  
ATOM   5888  CB  ASN B 219       0.504  22.870  26.336  1.00159.13           C  
ANISOU 5888  CB  ASN B 219    16943  29387  14134  -1537   1403   1477       C  
ATOM   5889  CG  ASN B 219       0.882  21.453  26.686  1.00185.05           C  
ANISOU 5889  CG  ASN B 219    20032  32636  17641  -1577   1389   1132       C  
ATOM   5890  OD1 ASN B 219       1.147  20.606  25.824  1.00181.53           O  
ANISOU 5890  OD1 ASN B 219    19373  32469  17129  -1624   1412    889       O  
ATOM   5891  ND2 ASN B 219       0.888  21.157  27.975  1.00175.79           N  
ANISOU 5891  ND2 ASN B 219    18936  31115  16741  -1553   1353   1102       N  
ATOM   5892  N   PRO B 220       1.156  22.340  22.855  1.00160.79           N  
ANISOU 5892  N   PRO B 220    16721  30667  13707  -1688   1512   1245       N  
ATOM   5893  CA  PRO B 220       0.502  21.965  21.589  1.00162.02           C  
ANISOU 5893  CA  PRO B 220    16693  31272  13597  -1652   1498   1138       C  
ATOM   5894  C   PRO B 220      -0.522  20.842  21.702  1.00164.08           C  
ANISOU 5894  C   PRO B 220    16793  31589  13961  -1564   1422    868       C  
ATOM   5895  O   PRO B 220      -1.393  20.745  20.836  1.00165.24           O  
ANISOU 5895  O   PRO B 220    16829  32073  13882  -1505   1386    842       O  
ATOM   5896  CB  PRO B 220       1.664  21.527  20.708  1.00165.21           C  
ANISOU 5896  CB  PRO B 220    16921  31960  13892  -1803   1586    944       C  
ATOM   5897  CG  PRO B 220       2.726  21.109  21.638  1.00168.16           C  
ANISOU 5897  CG  PRO B 220    17304  32030  14560  -1884   1620    813       C  
ATOM   5898  CD  PRO B 220       2.585  21.959  22.856  1.00162.16           C  
ANISOU 5898  CD  PRO B 220    16806  30839  13969  -1843   1589   1085       C  
ATOM   5899  N   LEU B 221      -0.426  19.996  22.738  1.00157.68           N  
ANISOU 5899  N   LEU B 221    15967  30468  13477  -1564   1397    671       N  
ATOM   5900  CA  LEU B 221      -1.352  18.879  22.908  1.00156.70           C  
ANISOU 5900  CA  LEU B 221    15702  30362  13474  -1510   1334    408       C  
ATOM   5901  C   LEU B 221      -2.731  19.332  23.423  1.00159.41           C  
ANISOU 5901  C   LEU B 221    16147  30610  13810  -1371   1252    594       C  
ATOM   5902  O   LEU B 221      -3.648  18.516  23.433  1.00158.80           O  
ANISOU 5902  O   LEU B 221    15945  30614  13780  -1337   1199    403       O  
ATOM   5903  CB  LEU B 221      -0.764  17.805  23.844  1.00155.06           C  
ANISOU 5903  CB  LEU B 221    15454  29842  13619  -1555   1339    153       C  
ATOM   5904  CG  LEU B 221       0.592  17.196  23.451  1.00160.48           C  
ANISOU 5904  CG  LEU B 221    16015  30604  14356  -1663   1417    -73       C  
ATOM   5905  CD1 LEU B 221       1.088  16.239  24.518  1.00159.11           C  
ANISOU 5905  CD1 LEU B 221    15834  30079  14543  -1666   1409   -267       C  
ATOM   5906  CD2 LEU B 221       0.530  16.495  22.093  1.00165.09           C  
ANISOU 5906  CD2 LEU B 221    16368  31624  14733  -1707   1448   -346       C  
ATOM   5907  N   PHE B 222      -2.895  20.616  23.815  1.00155.62           N  
ANISOU 5907  N   PHE B 222    15888  29975  13265  -1295   1245    955       N  
ATOM   5908  CA  PHE B 222      -4.176  21.126  24.318  1.00155.04           C  
ANISOU 5908  CA  PHE B 222    15914  29815  13178  -1138   1174   1142       C  
ATOM   5909  C   PHE B 222      -4.582  22.422  23.622  1.00161.16           C  
ANISOU 5909  C   PHE B 222    16806  30775  13653  -1037   1172   1480       C  
ATOM   5910  O   PHE B 222      -3.732  23.267  23.332  1.00161.54           O  
ANISOU 5910  O   PHE B 222    16986  30792  13600  -1093   1234   1676       O  
ATOM   5911  CB  PHE B 222      -4.136  21.334  25.841  1.00154.39           C  
ANISOU 5911  CB  PHE B 222    16018  29253  13388  -1103   1158   1237       C  
ATOM   5912  CG  PHE B 222      -3.729  20.105  26.620  1.00154.26           C  
ANISOU 5912  CG  PHE B 222    15913  29024  13674  -1187   1156    948       C  
ATOM   5913  CD1 PHE B 222      -4.650  19.102  26.900  1.00156.82           C  
ANISOU 5913  CD1 PHE B 222    16106  29364  14113  -1159   1103    738       C  
ATOM   5914  CD2 PHE B 222      -2.423  19.949  27.069  1.00155.49           C  
ANISOU 5914  CD2 PHE B 222    16113  28970  13996  -1296   1208    891       C  
ATOM   5915  CE1 PHE B 222      -4.269  17.957  27.603  1.00156.42           C  
ANISOU 5915  CE1 PHE B 222    15992  29097  14344  -1233   1104    489       C  
ATOM   5916  CE2 PHE B 222      -2.044  18.807  27.781  1.00156.99           C  
ANISOU 5916  CE2 PHE B 222    16224  28963  14463  -1349   1202    642       C  
ATOM   5917  CZ  PHE B 222      -2.973  17.823  28.050  1.00154.65           C  
ANISOU 5917  CZ  PHE B 222    15821  28655  14283  -1314   1151    451       C  
ATOM   5918  N   THR B 223      -5.891  22.576  23.373  1.00158.89           N  
ANISOU 5918  N   THR B 223    16469  30679  13225   -886   1102   1554       N  
ATOM   5919  CA  THR B 223      -6.486  23.743  22.710  1.00160.89           C  
ANISOU 5919  CA  THR B 223    16818  31126  13185   -741   1084   1881       C  
ATOM   5920  C   THR B 223      -6.555  24.945  23.661  1.00163.75           C  
ANISOU 5920  C   THR B 223    17484  31086  13646   -625   1091   2214       C  
ATOM   5921  O   THR B 223      -6.417  24.771  24.875  1.00161.34           O  
ANISOU 5921  O   THR B 223    17277  30400  13624   -640   1090   2163       O  
ATOM   5922  CB  THR B 223      -7.894  23.395  22.178  1.00172.28           C  
ANISOU 5922  CB  THR B 223    18072  32933  14454   -607    998   1817       C  
ATOM   5923  OG1 THR B 223      -8.736  22.999  23.261  1.00171.02           O  
ANISOU 5923  OG1 THR B 223    17911  32550  14521   -527    944   1739       O  
ATOM   5924  CG2 THR B 223      -7.871  22.309  21.106  1.00172.53           C  
ANISOU 5924  CG2 THR B 223    17809  33400  14342   -727    994   1492       C  
ATOM   5925  N   GLU B 224      -6.789  26.161  23.108  1.00162.06           N  
ANISOU 5925  N   GLU B 224    17425  30958  13194   -505   1098   2554       N  
ATOM   5926  CA  GLU B 224      -6.930  27.406  23.877  1.00161.75           C  
ANISOU 5926  CA  GLU B 224    17694  30549  13217   -376   1109   2883       C  
ATOM   5927  C   GLU B 224      -8.176  27.327  24.797  1.00163.56           C  
ANISOU 5927  C   GLU B 224    17927  30639  13578   -179   1034   2879       C  
ATOM   5928  O   GLU B 224      -8.150  27.854  25.915  1.00161.26           O  
ANISOU 5928  O   GLU B 224    17849  29939  13483   -127   1047   2989       O  
ATOM   5929  CB  GLU B 224      -6.984  28.631  22.933  1.00166.21           C  
ANISOU 5929  CB  GLU B 224    18408  31269  13476   -278   1133   3241       C  
ATOM   5930  CG  GLU B 224      -7.377  29.960  23.577  1.00180.13           C  
ANISOU 5930  CG  GLU B 224    20492  32682  15268    -94   1138   3594       C  
ATOM   5931  CD  GLU B 224      -6.380  30.664  24.483  1.00205.04           C  
ANISOU 5931  CD  GLU B 224    23937  35340  18628   -214   1218   3710       C  
ATOM   5932  OE1 GLU B 224      -6.245  31.900  24.338  1.00201.75           O  
ANISOU 5932  OE1 GLU B 224    23790  34756  18109   -151   1262   4038       O  
ATOM   5933  OE2 GLU B 224      -5.777  30.007  25.365  1.00197.15           O  
ANISOU 5933  OE2 GLU B 224    22906  34113  17891   -365   1234   3482       O  
ATOM   5934  N   ALA B 225      -9.239  26.634  24.332  1.00160.52           N  
ANISOU 5934  N   ALA B 225    17295  30614  13081    -88    960   2732       N  
ATOM   5935  CA  ALA B 225     -10.469  26.404  25.088  1.00159.38           C  
ANISOU 5935  CA  ALA B 225    17093  30427  13037     76    889   2689       C  
ATOM   5936  C   ALA B 225     -10.157  25.603  26.351  1.00160.15           C  
ANISOU 5936  C   ALA B 225    17195  30174  13481    -48    901   2461       C  
ATOM   5937  O   ALA B 225     -10.668  25.928  27.422  1.00158.54           O  
ANISOU 5937  O   ALA B 225    17115  29692  13432     65    885   2541       O  
ATOM   5938  CB  ALA B 225     -11.480  25.663  24.227  1.00161.60           C  
ANISOU 5938  CB  ALA B 225    17069  31212  13122    127    816   2524       C  
ATOM   5939  N   GLU B 226      -9.270  24.594  26.227  1.00155.69           N  
ANISOU 5939  N   GLU B 226    16505  29620  13032   -271    933   2187       N  
ATOM   5940  CA  GLU B 226      -8.818  23.746  27.330  1.00153.07           C  
ANISOU 5940  CA  GLU B 226    16169  28970  13021   -399    946   1970       C  
ATOM   5941  C   GLU B 226      -7.849  24.506  28.240  1.00155.78           C  
ANISOU 5941  C   GLU B 226    16783  28875  13531   -443   1001   2135       C  
ATOM   5942  O   GLU B 226      -7.828  24.252  29.448  1.00153.59           O  
ANISOU 5942  O   GLU B 226    16578  28280  13499   -458    996   2078       O  
ATOM   5943  CB  GLU B 226      -8.168  22.468  26.792  1.00154.22           C  
ANISOU 5943  CB  GLU B 226    16098  29282  13218   -595    964   1637       C  
ATOM   5944  CG  GLU B 226      -9.196  21.492  26.246  1.00165.17           C  
ANISOU 5944  CG  GLU B 226    17218  31016  14522   -585    907   1403       C  
ATOM   5945  CD  GLU B 226      -8.668  20.346  25.407  1.00184.27           C  
ANISOU 5945  CD  GLU B 226    19418  33676  16920   -757    928   1077       C  
ATOM   5946  OE1 GLU B 226      -7.623  20.515  24.737  1.00177.05           O  
ANISOU 5946  OE1 GLU B 226    18517  32837  15917   -847    985   1079       O  
ATOM   5947  OE2 GLU B 226      -9.343  19.293  25.373  1.00178.11           O  
ANISOU 5947  OE2 GLU B 226    18447  33029  16196   -803    892    816       O  
ATOM   5948  N   HIS B 227      -7.065  25.446  27.660  1.00153.27           N  
ANISOU 5948  N   HIS B 227    16613  28554  13069   -474   1056   2341       N  
ATOM   5949  CA  HIS B 227      -6.119  26.297  28.387  1.00152.21           C  
ANISOU 5949  CA  HIS B 227    16742  28038  13054   -539   1115   2510       C  
ATOM   5950  C   HIS B 227      -6.874  27.206  29.361  1.00155.44           C  
ANISOU 5950  C   HIS B 227    17374  28154  13534   -359   1096   2725       C  
ATOM   5951  O   HIS B 227      -6.588  27.171  30.556  1.00153.40           O  
ANISOU 5951  O   HIS B 227    17226  27554  13505   -400   1104   2687       O  
ATOM   5952  CB  HIS B 227      -5.266  27.133  27.414  1.00154.90           C  
ANISOU 5952  CB  HIS B 227    17183  28487  13186   -618   1181   2697       C  
ATOM   5953  CG  HIS B 227      -3.985  26.478  26.999  1.00158.10           C  
ANISOU 5953  CG  HIS B 227    17466  28981  13623   -847   1236   2505       C  
ATOM   5954  ND1 HIS B 227      -3.958  25.491  26.030  1.00160.63           N  
ANISOU 5954  ND1 HIS B 227    17517  29681  13836   -911   1226   2270       N  
ATOM   5955  CD2 HIS B 227      -2.718  26.714  27.414  1.00159.13           C  
ANISOU 5955  CD2 HIS B 227    17705  28887  13870  -1018   1301   2514       C  
ATOM   5956  CE1 HIS B 227      -2.686  25.151  25.897  1.00159.72           C  
ANISOU 5956  CE1 HIS B 227    17355  29552  13781  -1100   1289   2144       C  
ATOM   5957  NE2 HIS B 227      -1.904  25.855  26.712  1.00159.17           N  
ANISOU 5957  NE2 HIS B 227    17498  29136  13845  -1172   1333   2286       N  
ATOM   5958  N   GLN B 228      -7.873  27.968  28.856  1.00153.44           N  
ANISOU 5958  N   GLN B 228    17169  28054  13078   -147   1066   2937       N  
ATOM   5959  CA  GLN B 228      -8.711  28.892  29.631  1.00153.27           C  
ANISOU 5959  CA  GLN B 228    17348  27800  13089     70   1049   3147       C  
ATOM   5960  C   GLN B 228      -9.539  28.165  30.695  1.00154.74           C  
ANISOU 5960  C   GLN B 228    17431  27897  13467    135    998   2973       C  
ATOM   5961  O   GLN B 228      -9.756  28.719  31.774  1.00153.55           O  
ANISOU 5961  O   GLN B 228    17465  27424  13452    222   1007   3064       O  
ATOM   5962  CB  GLN B 228      -9.645  29.678  28.703  1.00157.45           C  
ANISOU 5962  CB  GLN B 228    17892  28592  13340    303   1019   3385       C  
ATOM   5963  CG  GLN B 228      -8.961  30.830  27.971  1.00179.13           C  
ANISOU 5963  CG  GLN B 228    20862  31287  15914    292   1081   3671       C  
ATOM   5964  CD  GLN B 228      -9.848  31.499  26.943  1.00209.41           C  
ANISOU 5964  CD  GLN B 228    24689  35424  19453    526   1044   3910       C  
ATOM   5965  OE1 GLN B 228     -11.086  31.433  26.986  1.00207.46           O  
ANISOU 5965  OE1 GLN B 228    24333  35349  19143    756    974   3925       O  
ATOM   5966  NE2 GLN B 228      -9.226  32.169  25.984  1.00206.74           N  
ANISOU 5966  NE2 GLN B 228    24459  35177  18917    472   1093   4114       N  
ATOM   5967  N   ASP B 229      -9.992  26.931  30.389  1.00150.34           N  
ANISOU 5967  N   ASP B 229    16583  27623  12915     82    950   2717       N  
ATOM   5968  CA  ASP B 229     -10.775  26.077  31.286  1.00148.36           C  
ANISOU 5968  CA  ASP B 229    16202  27332  12835    104    906   2531       C  
ATOM   5969  C   ASP B 229      -9.923  25.609  32.477  1.00148.17           C  
ANISOU 5969  C   ASP B 229    16264  26935  13098    -60    937   2404       C  
ATOM   5970  O   ASP B 229     -10.413  25.604  33.608  1.00146.27           O  
ANISOU 5970  O   ASP B 229    16086  26482  13009      2    924   2402       O  
ATOM   5971  CB  ASP B 229     -11.350  24.874  30.515  1.00150.99           C  
ANISOU 5971  CB  ASP B 229    16215  28065  13091     47    857   2283       C  
ATOM   5972  CG  ASP B 229     -11.897  23.763  31.390  1.00161.39           C  
ANISOU 5972  CG  ASP B 229    17387  29321  14611    -15    827   2047       C  
ATOM   5973  OD1 ASP B 229     -13.026  23.917  31.914  1.00162.09           O  
ANISOU 5973  OD1 ASP B 229    17449  29440  14696    136    790   2095       O  
ATOM   5974  OD2 ASP B 229     -11.197  22.743  31.556  1.00166.90           O  
ANISOU 5974  OD2 ASP B 229    18000  29941  15472   -210    843   1820       O  
ATOM   5975  N   MET B 230      -8.660  25.215  32.220  1.00143.26           N  
ANISOU 5975  N   MET B 230    15633  26260  12540   -262    977   2301       N  
ATOM   5976  CA  MET B 230      -7.735  24.779  33.265  1.00140.59           C  
ANISOU 5976  CA  MET B 230    15362  25600  12454   -413   1002   2192       C  
ATOM   5977  C   MET B 230      -7.276  25.985  34.098  1.00142.96           C  
ANISOU 5977  C   MET B 230    15957  25549  12811   -382   1041   2412       C  
ATOM   5978  O   MET B 230      -7.088  25.840  35.305  1.00140.96           O  
ANISOU 5978  O   MET B 230    15786  25019  12755   -419   1041   2370       O  
ATOM   5979  CB  MET B 230      -6.537  24.018  32.669  1.00142.74           C  
ANISOU 5979  CB  MET B 230    15515  25960  12761   -614   1032   2013       C  
ATOM   5980  CG  MET B 230      -5.651  23.324  33.709  1.00144.53           C  
ANISOU 5980  CG  MET B 230    15754  25909  13252   -754   1043   1866       C  
ATOM   5981  SD  MET B 230      -6.503  22.164  34.822  1.00147.19           S  
ANISOU 5981  SD  MET B 230    15982  26131  13814   -732    989   1682       S  
ATOM   5982  CE  MET B 230      -6.684  20.765  33.754  1.00144.72           C  
ANISOU 5982  CE  MET B 230    15374  26144  13467   -811    972   1395       C  
ATOM   5983  N   HIS B 231      -7.136  27.172  33.467  1.00140.46           N  
ANISOU 5983  N   HIS B 231    15807  25245  12317   -316   1075   2647       N  
ATOM   5984  CA  HIS B 231      -6.745  28.405  34.156  1.00140.14           C  
ANISOU 5984  CA  HIS B 231    16069  24863  12314   -292   1121   2860       C  
ATOM   5985  C   HIS B 231      -7.863  28.873  35.092  1.00143.24           C  
ANISOU 5985  C   HIS B 231    16572  25093  12760    -84   1094   2946       C  
ATOM   5986  O   HIS B 231      -7.568  29.257  36.221  1.00141.85           O  
ANISOU 5986  O   HIS B 231    16569  24592  12734   -111   1116   2971       O  
ATOM   5987  CB  HIS B 231      -6.356  29.515  33.165  1.00143.12           C  
ANISOU 5987  CB  HIS B 231    16602  25293  12483   -279   1170   3096       C  
ATOM   5988  CG  HIS B 231      -5.092  29.235  32.405  1.00146.77           C  
ANISOU 5988  CG  HIS B 231    16995  25872  12899   -506   1215   3030       C  
ATOM   5989  ND1 HIS B 231      -5.016  29.432  31.038  1.00150.48           N  
ANISOU 5989  ND1 HIS B 231    17397  26648  13132   -509   1232   3114       N  
ATOM   5990  CD2 HIS B 231      -3.901  28.762  32.843  1.00147.15           C  
ANISOU 5990  CD2 HIS B 231    17017  25796  13099   -724   1246   2885       C  
ATOM   5991  CE1 HIS B 231      -3.788  29.084  30.692  1.00149.69           C  
ANISOU 5991  CE1 HIS B 231    17231  26595  13047   -733   1279   3012       C  
ATOM   5992  NE2 HIS B 231      -3.081  28.673  31.744  1.00148.07           N  
ANISOU 5992  NE2 HIS B 231    17045  26141  13076   -862   1287   2872       N  
ATOM   5993  N   SER B 232      -9.139  28.784  34.652  1.00140.43           N  
ANISOU 5993  N   SER B 232    16092  24986  12279    115   1046   2972       N  
ATOM   5994  CA  SER B 232     -10.310  29.140  35.464  1.00140.17           C  
ANISOU 5994  CA  SER B 232    16113  24866  12278    332   1020   3034       C  
ATOM   5995  C   SER B 232     -10.437  28.198  36.670  1.00140.68           C  
ANISOU 5995  C   SER B 232    16084  24804  12565    248    999   2829       C  
ATOM   5996  O   SER B 232     -10.870  28.629  37.738  1.00139.86           O  
ANISOU 5996  O   SER B 232    16110  24479  12551    347   1006   2877       O  
ATOM   5997  CB  SER B 232     -11.585  29.094  34.628  1.00146.11           C  
ANISOU 5997  CB  SER B 232    16694  25987  12835    542    968   3078       C  
ATOM   5998  OG  SER B 232     -11.508  29.968  33.513  1.00158.85           O  
ANISOU 5998  OG  SER B 232    18396  27732  14228    637    982   3292       O  
ATOM   5999  N   TYR B 233     -10.033  26.919  36.491  1.00135.00           N  
ANISOU 5999  N   TYR B 233    15148  24217  11929     66    978   2602       N  
ATOM   6000  CA  TYR B 233     -10.030  25.883  37.525  1.00132.25           C  
ANISOU 6000  CA  TYR B 233    14702  23754  11792    -40    959   2409       C  
ATOM   6001  C   TYR B 233      -8.961  26.194  38.570  1.00133.28           C  
ANISOU 6001  C   TYR B 233    15030  23520  12090   -161    996   2431       C  
ATOM   6002  O   TYR B 233      -9.240  26.105  39.767  1.00131.42           O  
ANISOU 6002  O   TYR B 233    14851  23094  11987   -143    991   2407       O  
ATOM   6003  CB  TYR B 233      -9.794  24.491  36.902  1.00132.94           C  
ANISOU 6003  CB  TYR B 233    14530  24064  11917   -196    935   2171       C  
ATOM   6004  CG  TYR B 233     -10.009  23.336  37.861  1.00132.89           C  
ANISOU 6004  CG  TYR B 233    14412  23967  12115   -284    912   1983       C  
ATOM   6005  CD1 TYR B 233     -11.281  22.815  38.083  1.00135.19           C  
ANISOU 6005  CD1 TYR B 233    14557  24410  12399   -205    876   1912       C  
ATOM   6006  CD2 TYR B 233      -8.937  22.740  38.519  1.00131.95           C  
ANISOU 6006  CD2 TYR B 233    14322  23626  12187   -450    926   1881       C  
ATOM   6007  CE1 TYR B 233     -11.485  21.750  38.960  1.00134.71           C  
ANISOU 6007  CE1 TYR B 233    14405  24257  12522   -303    862   1755       C  
ATOM   6008  CE2 TYR B 233      -9.129  21.679  39.405  1.00131.59           C  
ANISOU 6008  CE2 TYR B 233    14189  23484  12327   -524    905   1733       C  
ATOM   6009  CZ  TYR B 233     -10.406  21.182  39.617  1.00139.09           C  
ANISOU 6009  CZ  TYR B 233    15012  24565  13270   -459    876   1673       C  
ATOM   6010  OH  TYR B 233     -10.609  20.127  40.475  1.00138.54           O  
ANISOU 6010  OH  TYR B 233    14866  24394  13378   -548    862   1541       O  
ATOM   6011  N   ILE B 234      -7.745  26.569  38.113  1.00129.63           N  
ANISOU 6011  N   ILE B 234    14661  22986  11607   -292   1035   2476       N  
ATOM   6012  CA  ILE B 234      -6.607  26.915  38.969  1.00128.34           C  
ANISOU 6012  CA  ILE B 234    14669  22519  11576   -432   1070   2494       C  
ATOM   6013  C   ILE B 234      -6.921  28.232  39.707  1.00132.82           C  
ANISOU 6013  C   ILE B 234    15511  22830  12125   -312   1100   2684       C  
ATOM   6014  O   ILE B 234      -6.626  28.333  40.897  1.00131.19           O  
ANISOU 6014  O   ILE B 234    15414  22376  12055   -363   1107   2660       O  
ATOM   6015  CB  ILE B 234      -5.270  26.955  38.159  1.00131.72           C  
ANISOU 6015  CB  ILE B 234    15090  22996  11961   -611   1108   2484       C  
ATOM   6016  CG1 ILE B 234      -4.844  25.522  37.758  1.00131.42           C  
ANISOU 6016  CG1 ILE B 234    14789  23146  11999   -734   1082   2249       C  
ATOM   6017  CG2 ILE B 234      -4.134  27.646  38.936  1.00131.80           C  
ANISOU 6017  CG2 ILE B 234    15306  22714  12059   -748   1151   2548       C  
ATOM   6018  CD1 ILE B 234      -3.953  25.407  36.490  1.00141.24           C  
ANISOU 6018  CD1 ILE B 234    15938  24600  13126   -850   1115   2214       C  
ATOM   6019  N   ALA B 235      -7.565  29.204  39.019  1.00131.12           N  
ANISOU 6019  N   ALA B 235    15402  22679  11740   -140   1116   2865       N  
ATOM   6020  CA  ALA B 235      -7.949  30.494  39.603  1.00131.74           C  
ANISOU 6020  CA  ALA B 235    15753  22508  11794      8   1150   3047       C  
ATOM   6021  C   ALA B 235      -8.926  30.311  40.763  1.00134.43           C  
ANISOU 6021  C   ALA B 235    16083  22764  12231    144   1125   2989       C  
ATOM   6022  O   ALA B 235      -8.742  30.937  41.804  1.00134.09           O  
ANISOU 6022  O   ALA B 235    16241  22434  12273    145   1156   3025       O  
ATOM   6023  CB  ALA B 235      -8.565  31.395  38.544  1.00134.79           C  
ANISOU 6023  CB  ALA B 235    16219  23020  11976    199   1163   3251       C  
ATOM   6024  N   ALA B 236      -9.933  29.428  40.596  1.00129.96           N  
ANISOU 6024  N   ALA B 236    15274  22459  11646    238   1073   2887       N  
ATOM   6025  CA  ALA B 236     -10.957  29.141  41.602  1.00128.73           C  
ANISOU 6025  CA  ALA B 236    15063  22289  11561    358   1051   2826       C  
ATOM   6026  C   ALA B 236     -10.373  28.451  42.842  1.00129.21           C  
ANISOU 6026  C   ALA B 236    15119  22158  11817    182   1049   2684       C  
ATOM   6027  O   ALA B 236     -10.565  28.953  43.947  1.00128.38           O  
ANISOU 6027  O   ALA B 236    15162  21841  11775    237   1070   2714       O  
ATOM   6028  CB  ALA B 236     -12.064  28.289  40.996  1.00129.85           C  
ANISOU 6028  CB  ALA B 236    14924  22789  11625    450    999   2739       C  
ATOM   6029  N   PHE B 237      -9.647  27.329  42.662  1.00123.83           N  
ANISOU 6029  N   PHE B 237    14274  21550  11225    -20   1026   2535       N  
ATOM   6030  CA  PHE B 237      -9.051  26.576  43.767  1.00121.77           C  
ANISOU 6030  CA  PHE B 237    13993  21130  11146   -179   1016   2413       C  
ATOM   6031  C   PHE B 237      -7.891  27.316  44.426  1.00124.89           C  
ANISOU 6031  C   PHE B 237    14611  21241  11602   -292   1052   2471       C  
ATOM   6032  O   PHE B 237      -7.755  27.241  45.644  1.00123.69           O  
ANISOU 6032  O   PHE B 237    14525  20914  11556   -335   1050   2437       O  
ATOM   6033  CB  PHE B 237      -8.594  25.187  43.311  1.00122.78           C  
ANISOU 6033  CB  PHE B 237    13891  21406  11352   -336    983   2243       C  
ATOM   6034  CG  PHE B 237      -9.694  24.161  43.407  1.00124.29           C  
ANISOU 6034  CG  PHE B 237    13875  21778  11573   -293    947   2129       C  
ATOM   6035  CD1 PHE B 237     -10.590  23.980  42.360  1.00128.80           C  
ANISOU 6035  CD1 PHE B 237    14291  22637  12011   -199    929   2111       C  
ATOM   6036  CD2 PHE B 237      -9.851  23.392  44.554  1.00125.65           C  
ANISOU 6036  CD2 PHE B 237    14006  21843  11894   -357    932   2045       C  
ATOM   6037  CE1 PHE B 237     -11.621  23.041  42.458  1.00130.02           C  
ANISOU 6037  CE1 PHE B 237    14246  22969  12188   -186    900   1995       C  
ATOM   6038  CE2 PHE B 237     -10.882  22.452  44.650  1.00128.72           C  
ANISOU 6038  CE2 PHE B 237    14209  22392  12308   -343    907   1945       C  
ATOM   6039  CZ  PHE B 237     -11.762  22.285  43.603  1.00128.13           C  
ANISOU 6039  CZ  PHE B 237    13976  22601  12106   -265    892   1913       C  
ATOM   6040  N   GLY B 238      -7.092  28.026  43.630  1.00121.69           N  
ANISOU 6040  N   GLY B 238    14313  20806  11117   -347   1084   2558       N  
ATOM   6041  CA  GLY B 238      -5.946  28.796  44.103  1.00121.17           C  
ANISOU 6041  CA  GLY B 238    14454  20496  11090   -483   1124   2612       C  
ATOM   6042  C   GLY B 238      -6.303  29.946  45.024  1.00124.46           C  
ANISOU 6042  C   GLY B 238    15127  20662  11502   -384   1160   2715       C  
ATOM   6043  O   GLY B 238      -5.666  30.122  46.068  1.00123.22           O  
ANISOU 6043  O   GLY B 238    15080  20302  11436   -499   1171   2678       O  
ATOM   6044  N   ALA B 239      -7.333  30.734  44.644  1.00121.48           N  
ANISOU 6044  N   ALA B 239    14841  20304  11011   -162   1179   2838       N  
ATOM   6045  CA  ALA B 239      -7.803  31.890  45.409  1.00121.73           C  
ANISOU 6045  CA  ALA B 239    15125  20097  11028    -23   1221   2935       C  
ATOM   6046  C   ALA B 239      -8.491  31.469  46.705  1.00123.24           C  
ANISOU 6046  C   ALA B 239    15269  20247  11309     41   1201   2836       C  
ATOM   6047  O   ALA B 239      -8.212  32.064  47.747  1.00122.65           O  
ANISOU 6047  O   ALA B 239    15381  19932  11288      7   1232   2830       O  
ATOM   6048  CB  ALA B 239      -8.748  32.733  44.568  1.00124.44           C  
ANISOU 6048  CB  ALA B 239    15550  20505  11226    229   1240   3096       C  
ATOM   6049  N   VAL B 240      -9.368  30.438  46.643  1.00118.25           N  
ANISOU 6049  N   VAL B 240    14388  19857  10686    116   1152   2753       N  
ATOM   6050  CA  VAL B 240     -10.107  29.906  47.796  1.00116.74           C  
ANISOU 6050  CA  VAL B 240    14117  19675  10565    165   1135   2663       C  
ATOM   6051  C   VAL B 240      -9.102  29.388  48.843  1.00118.50           C  
ANISOU 6051  C   VAL B 240    14356  19745  10922    -59   1125   2565       C  
ATOM   6052  O   VAL B 240      -9.222  29.766  50.010  1.00118.18           O  
ANISOU 6052  O   VAL B 240    14438  19548  10918    -42   1145   2551       O  
ATOM   6053  CB  VAL B 240     -11.164  28.838  47.387  1.00119.89           C  
ANISOU 6053  CB  VAL B 240    14232  20380  10943    243   1089   2591       C  
ATOM   6054  CG1 VAL B 240     -11.697  28.070  48.596  1.00118.56           C  
ANISOU 6054  CG1 VAL B 240    13961  20223  10864    217   1073   2488       C  
ATOM   6055  CG2 VAL B 240     -12.319  29.483  46.629  1.00121.36           C  
ANISOU 6055  CG2 VAL B 240    14405  20726  10980    502   1096   2693       C  
ATOM   6056  N   THR B 241      -8.084  28.596  48.414  1.00113.12           N  
ANISOU 6056  N   THR B 241    13561  19116  10304   -256   1096   2500       N  
ATOM   6057  CA  THR B 241      -7.033  28.052  49.290  1.00111.41           C  
ANISOU 6057  CA  THR B 241    13337  18786  10207   -458   1077   2417       C  
ATOM   6058  C   THR B 241      -6.213  29.202  49.876  1.00115.62           C  
ANISOU 6058  C   THR B 241    14127  19073  10732   -534   1120   2471       C  
ATOM   6059  O   THR B 241      -5.905  29.178  51.065  1.00114.33           O  
ANISOU 6059  O   THR B 241    14022  18787  10630   -609   1114   2425       O  
ATOM   6060  CB  THR B 241      -6.144  27.042  48.540  1.00117.36           C  
ANISOU 6060  CB  THR B 241    13910  19663  11017   -614   1043   2340       C  
ATOM   6061  OG1 THR B 241      -6.968  26.052  47.931  1.00116.36           O  
ANISOU 6061  OG1 THR B 241    13565  19754  10891   -547   1012   2278       O  
ATOM   6062  CG2 THR B 241      -5.122  26.354  49.450  1.00114.18           C  
ANISOU 6062  CG2 THR B 241    13468  19172  10742   -790   1013   2258       C  
ATOM   6063  N   GLY B 242      -5.914  30.202  49.042  1.00113.59           N  
ANISOU 6063  N   GLY B 242    14020  18750  10389   -517   1163   2570       N  
ATOM   6064  CA  GLY B 242      -5.170  31.398  49.423  1.00114.22           C  
ANISOU 6064  CA  GLY B 242    14364  18582  10450   -602   1216   2627       C  
ATOM   6065  C   GLY B 242      -5.846  32.189  50.524  1.00117.78           C  
ANISOU 6065  C   GLY B 242    15006  18849  10897   -481   1249   2638       C  
ATOM   6066  O   GLY B 242      -5.173  32.650  51.446  1.00117.10           O  
ANISOU 6066  O   GLY B 242    15067  18580  10847   -610   1269   2600       O  
ATOM   6067  N   LEU B 243      -7.186  32.319  50.447  1.00114.57           N  
ANISOU 6067  N   LEU B 243    14579  18513  10438   -234   1255   2677       N  
ATOM   6068  CA  LEU B 243      -8.010  33.039  51.421  1.00115.13           C  
ANISOU 6068  CA  LEU B 243    14806  18446  10493    -71   1291   2679       C  
ATOM   6069  C   LEU B 243      -8.248  32.212  52.691  1.00117.40           C  
ANISOU 6069  C   LEU B 243    14970  18787  10850   -118   1258   2560       C  
ATOM   6070  O   LEU B 243      -8.291  32.780  53.784  1.00117.41           O  
ANISOU 6070  O   LEU B 243    15126  18629  10858   -111   1290   2522       O  
ATOM   6071  CB  LEU B 243      -9.356  33.439  50.798  1.00116.36           C  
ANISOU 6071  CB  LEU B 243    14952  18702  10557    228   1307   2768       C  
ATOM   6072  CG  LEU B 243      -9.305  34.510  49.709  1.00122.82           C  
ANISOU 6072  CG  LEU B 243    15953  19427  11287    331   1350   2921       C  
ATOM   6073  CD1 LEU B 243     -10.482  34.381  48.775  1.00123.90           C  
ANISOU 6073  CD1 LEU B 243    15948  19801  11326    586   1329   3001       C  
ATOM   6074  CD2 LEU B 243      -9.234  35.912  50.301  1.00126.95           C  
ANISOU 6074  CD2 LEU B 243    16816  19618  11800    401   1426   2974       C  
ATOM   6075  N   CYS B 244      -8.406  30.881  52.542  1.00111.94           N  
ANISOU 6075  N   CYS B 244    14009  18316  10205   -169   1198   2500       N  
ATOM   6076  CA  CYS B 244      -8.635  29.936  53.637  1.00110.19           C  
ANISOU 6076  CA  CYS B 244    13651  18165  10051   -225   1164   2409       C  
ATOM   6077  C   CYS B 244      -7.405  29.821  54.525  1.00112.02           C  
ANISOU 6077  C   CYS B 244    13948  18264  10350   -448   1148   2354       C  
ATOM   6078  O   CYS B 244      -7.542  29.873  55.746  1.00111.32           O  
ANISOU 6078  O   CYS B 244    13911  18116  10271   -463   1152   2310       O  
ATOM   6079  CB  CYS B 244      -9.046  28.571  53.094  1.00109.70           C  
ANISOU 6079  CB  CYS B 244    13309  18343  10029   -238   1110   2368       C  
ATOM   6080  SG  CYS B 244     -10.773  28.473  52.559  1.00114.57           S  
ANISOU 6080  SG  CYS B 244    13789  19181  10560     15   1118   2393       S  
ATOM   6081  N   THR B 245      -6.210  29.654  53.914  1.00107.91           N  
ANISOU 6081  N   THR B 245    13409  17726   9865   -619   1128   2354       N  
ATOM   6082  CA  THR B 245      -4.932  29.526  54.621  1.00107.28           C  
ANISOU 6082  CA  THR B 245    13360  17560   9840   -836   1105   2303       C  
ATOM   6083  C   THR B 245      -4.555  30.842  55.298  1.00111.23           C  
ANISOU 6083  C   THR B 245    14128  17841  10292   -880   1159   2310       C  
ATOM   6084  O   THR B 245      -4.121  30.814  56.445  1.00110.16           O  
ANISOU 6084  O   THR B 245    14031  17650  10175   -986   1144   2250       O  
ATOM   6085  CB  THR B 245      -3.803  29.043  53.689  1.00119.05           C  
ANISOU 6085  CB  THR B 245    14743  19122  11371   -989   1078   2297       C  
ATOM   6086  OG1 THR B 245      -3.734  29.877  52.529  1.00120.26           O  
ANISOU 6086  OG1 THR B 245    14998  19243  11452   -954   1125   2371       O  
ATOM   6087  CG2 THR B 245      -3.951  27.579  53.289  1.00117.78           C  
ANISOU 6087  CG2 THR B 245    14317  19150  11285   -987   1021   2249       C  
ATOM   6088  N   LEU B 246      -4.739  31.983  54.601  1.00109.25           N  
ANISOU 6088  N   LEU B 246    14067  17467   9976   -800   1221   2383       N  
ATOM   6089  CA  LEU B 246      -4.444  33.321  55.118  1.00110.71           C  
ANISOU 6089  CA  LEU B 246    14540  17405  10120   -836   1285   2388       C  
ATOM   6090  C   LEU B 246      -5.275  33.604  56.367  1.00115.01           C  
ANISOU 6090  C   LEU B 246    15169  17882  10647   -716   1306   2331       C  
ATOM   6091  O   LEU B 246      -4.718  34.071  57.360  1.00115.39           O  
ANISOU 6091  O   LEU B 246    15351  17800  10693   -844   1321   2261       O  
ATOM   6092  CB  LEU B 246      -4.703  34.388  54.037  1.00112.53           C  
ANISOU 6092  CB  LEU B 246    14954  17515  10288   -725   1350   2503       C  
ATOM   6093  CG  LEU B 246      -4.468  35.855  54.404  1.00119.74           C  
ANISOU 6093  CG  LEU B 246    16203  18127  11166   -747   1431   2522       C  
ATOM   6094  CD1 LEU B 246      -2.986  36.166  54.530  1.00120.59           C  
ANISOU 6094  CD1 LEU B 246    16397  18130  11293  -1058   1440   2483       C  
ATOM   6095  CD2 LEU B 246      -5.094  36.773  53.374  1.00124.36           C  
ANISOU 6095  CD2 LEU B 246    16954  18608  11689   -553   1490   2662       C  
ATOM   6096  N   PHE B 247      -6.588  33.288  56.325  1.00111.16           N  
ANISOU 6096  N   PHE B 247    14586  17513  10139   -483   1305   2351       N  
ATOM   6097  CA  PHE B 247      -7.518  33.468  57.444  1.00111.34           C  
ANISOU 6097  CA  PHE B 247    14651  17523  10132   -346   1330   2296       C  
ATOM   6098  C   PHE B 247      -7.069  32.645  58.655  1.00113.70           C  
ANISOU 6098  C   PHE B 247    14836  17897  10466   -511   1282   2205       C  
ATOM   6099  O   PHE B 247      -7.088  33.151  59.775  1.00113.90           O  
ANISOU 6099  O   PHE B 247    14990  17826  10459   -530   1311   2136       O  
ATOM   6100  CB  PHE B 247      -8.950  33.081  57.026  1.00113.21           C  
ANISOU 6100  CB  PHE B 247    14739  17940  10337    -90   1329   2336       C  
ATOM   6101  CG  PHE B 247      -9.953  33.040  58.157  1.00115.29           C  
ANISOU 6101  CG  PHE B 247    14980  18259  10566     43   1352   2273       C  
ATOM   6102  CD1 PHE B 247     -10.547  34.208  58.628  1.00120.43           C  
ANISOU 6102  CD1 PHE B 247    15846  18755  11158    219   1427   2258       C  
ATOM   6103  CD2 PHE B 247     -10.307  31.833  58.750  1.00116.26           C  
ANISOU 6103  CD2 PHE B 247    14871  18587  10715     -8   1304   2228       C  
ATOM   6104  CE1 PHE B 247     -11.467  34.170  59.684  1.00121.68           C  
ANISOU 6104  CE1 PHE B 247    15970  18989  11273    343   1454   2187       C  
ATOM   6105  CE2 PHE B 247     -11.224  31.795  59.806  1.00119.46           C  
ANISOU 6105  CE2 PHE B 247    15249  19066  11075     99   1332   2174       C  
ATOM   6106  CZ  PHE B 247     -11.800  32.962  60.264  1.00119.25           C  
ANISOU 6106  CZ  PHE B 247    15419  18912  10979    275   1407   2149       C  
ATOM   6107  N   THR B 248      -6.671  31.380  58.410  1.00108.71           N  
ANISOU 6107  N   THR B 248    13969  17437   9898   -623   1209   2205       N  
ATOM   6108  CA  THR B 248      -6.194  30.421  59.407  1.00107.32           C  
ANISOU 6108  CA  THR B 248    13662  17351   9765   -771   1151   2150       C  
ATOM   6109  C   THR B 248      -4.883  30.919  60.018  1.00112.33           C  
ANISOU 6109  C   THR B 248    14424  17861  10396   -983   1143   2103       C  
ATOM   6110  O   THR B 248      -4.750  30.905  61.239  1.00112.58           O  
ANISOU 6110  O   THR B 248    14486  17890  10401  -1050   1133   2046       O  
ATOM   6111  CB  THR B 248      -6.076  29.028  58.772  1.00108.50           C  
ANISOU 6111  CB  THR B 248    13554  17676   9994   -814   1084   2171       C  
ATOM   6112  OG1 THR B 248      -7.374  28.634  58.325  1.00103.23           O  
ANISOU 6112  OG1 THR B 248    12773  17135   9313   -634   1096   2196       O  
ATOM   6113  CG2 THR B 248      -5.514  27.974  59.732  1.00105.05           C  
ANISOU 6113  CG2 THR B 248    12986  17315   9612   -956   1019   2139       C  
ATOM   6114  N   LEU B 249      -3.938  31.391  59.178  1.00109.36           N  
ANISOU 6114  N   LEU B 249    14118  17399  10033  -1096   1152   2125       N  
ATOM   6115  CA  LEU B 249      -2.657  31.930  59.639  1.00110.22           C  
ANISOU 6115  CA  LEU B 249    14340  17408  10132  -1320   1149   2075       C  
ATOM   6116  C   LEU B 249      -2.872  33.187  60.495  1.00116.70           C  
ANISOU 6116  C   LEU B 249    15424  18036  10880  -1312   1218   2018       C  
ATOM   6117  O   LEU B 249      -2.215  33.342  61.531  1.00116.68           O  
ANISOU 6117  O   LEU B 249    15469  18013  10851  -1469   1202   1938       O  
ATOM   6118  CB  LEU B 249      -1.726  32.255  58.453  1.00110.59           C  
ANISOU 6118  CB  LEU B 249    14411  17414  10194  -1439   1161   2117       C  
ATOM   6119  CG  LEU B 249      -1.208  31.086  57.612  1.00113.96           C  
ANISOU 6119  CG  LEU B 249    14586  18024  10688  -1489   1098   2141       C  
ATOM   6120  CD1 LEU B 249      -0.667  31.576  56.295  1.00114.81           C  
ANISOU 6120  CD1 LEU B 249    14739  18101  10783  -1545   1135   2195       C  
ATOM   6121  CD2 LEU B 249      -0.154  30.299  58.341  1.00115.67           C  
ANISOU 6121  CD2 LEU B 249    14658  18344  10947  -1665   1025   2084       C  
ATOM   6122  N   ALA B 250      -3.821  34.059  60.068  1.00114.73           N  
ANISOU 6122  N   ALA B 250    15340  17656  10597  -1115   1293   2056       N  
ATOM   6123  CA  ALA B 250      -4.183  35.316  60.729  1.00116.47           C  
ANISOU 6123  CA  ALA B 250    15834  17661  10759  -1055   1373   2000       C  
ATOM   6124  C   ALA B 250      -4.709  35.094  62.152  1.00121.00           C  
ANISOU 6124  C   ALA B 250    16383  18301  11290  -1016   1367   1904       C  
ATOM   6125  O   ALA B 250      -4.380  35.879  63.040  1.00122.09           O  
ANISOU 6125  O   ALA B 250    16704  18303  11382  -1108   1406   1806       O  
ATOM   6126  CB  ALA B 250      -5.222  36.060  59.905  1.00118.15           C  
ANISOU 6126  CB  ALA B 250    16177  17762  10951   -796   1442   2081       C  
ATOM   6127  N   THR B 251      -5.496  34.022  62.374  1.00116.48           N  
ANISOU 6127  N   THR B 251    15585  17944  10728   -899   1322   1927       N  
ATOM   6128  CA  THR B 251      -6.058  33.713  63.692  1.00116.48           C  
ANISOU 6128  CA  THR B 251    15538  18043  10677   -863   1319   1854       C  
ATOM   6129  C   THR B 251      -4.942  33.234  64.625  1.00120.48           C  
ANISOU 6129  C   THR B 251    15983  18619  11175  -1115   1254   1796       C  
ATOM   6130  O   THR B 251      -4.920  33.627  65.797  1.00120.66           O  
ANISOU 6130  O   THR B 251    16099  18625  11123  -1165   1273   1702       O  
ATOM   6131  CB  THR B 251      -7.205  32.696  63.587  1.00122.38           C  
ANISOU 6131  CB  THR B 251    16060  19002  11435   -691   1296   1908       C  
ATOM   6132  OG1 THR B 251      -8.081  33.054  62.514  1.00120.43           O  
ANISOU 6132  OG1 THR B 251    15833  18732  11195   -475   1338   1974       O  
ATOM   6133  CG2 THR B 251      -7.999  32.563  64.892  1.00122.77           C  
ANISOU 6133  CG2 THR B 251    16086  19152  11410   -621   1317   1842       C  
ATOM   6134  N   PHE B 252      -4.009  32.412  64.091  1.00116.57           N  
ANISOU 6134  N   PHE B 252    15328  18213  10749  -1263   1178   1847       N  
ATOM   6135  CA  PHE B 252      -2.862  31.873  64.817  1.00116.43           C  
ANISOU 6135  CA  PHE B 252    15219  18288  10729  -1485   1103   1813       C  
ATOM   6136  C   PHE B 252      -1.953  32.985  65.333  1.00123.55           C  
ANISOU 6136  C   PHE B 252    16327  19049  11569  -1667   1134   1714       C  
ATOM   6137  O   PHE B 252      -1.557  32.939  66.494  1.00123.13           O  
ANISOU 6137  O   PHE B 252    16271  19065  11449  -1784   1104   1641       O  
ATOM   6138  CB  PHE B 252      -2.052  30.910  63.930  1.00116.65           C  
ANISOU 6138  CB  PHE B 252    15051  18418  10851  -1573   1030   1882       C  
ATOM   6139  CG  PHE B 252      -2.460  29.458  63.991  1.00116.34           C  
ANISOU 6139  CG  PHE B 252    14770  18560  10873  -1505    964   1945       C  
ATOM   6140  CD1 PHE B 252      -2.108  28.666  65.077  1.00118.83           C  
ANISOU 6140  CD1 PHE B 252    14973  19002  11175  -1588    896   1942       C  
ATOM   6141  CD2 PHE B 252      -3.152  28.869  62.940  1.00116.96           C  
ANISOU 6141  CD2 PHE B 252    14736  18683  11021  -1369    968   2009       C  
ATOM   6142  CE1 PHE B 252      -2.470  27.322  65.127  1.00118.38           C  
ANISOU 6142  CE1 PHE B 252    14716  19080  11185  -1534    841   2011       C  
ATOM   6143  CE2 PHE B 252      -3.520  27.525  62.994  1.00118.41           C  
ANISOU 6143  CE2 PHE B 252    14711  19010  11269  -1329    914   2054       C  
ATOM   6144  CZ  PHE B 252      -3.176  26.761  64.086  1.00116.33           C  
ANISOU 6144  CZ  PHE B 252    14358  18838  11005  -1412    854   2060       C  
ATOM   6145  N   VAL B 253      -1.662  33.997  64.495  1.00122.94           N  
ANISOU 6145  N   VAL B 253    16431  18776  11503  -1695   1196   1713       N  
ATOM   6146  CA  VAL B 253      -0.787  35.107  64.872  1.00125.32           C  
ANISOU 6146  CA  VAL B 253    16946  18916  11754  -1895   1237   1615       C  
ATOM   6147  C   VAL B 253      -1.522  36.114  65.820  1.00133.00           C  
ANISOU 6147  C   VAL B 253    18153  19735  12646  -1811   1319   1505       C  
ATOM   6148  O   VAL B 253      -0.861  36.754  66.640  1.00134.00           O  
ANISOU 6148  O   VAL B 253    18409  19796  12707  -1997   1333   1383       O  
ATOM   6149  CB  VAL B 253      -0.149  35.786  63.622  1.00129.59           C  
ANISOU 6149  CB  VAL B 253    17601  19299  12338  -1983   1280   1665       C  
ATOM   6150  CG1 VAL B 253      -1.134  36.681  62.874  1.00130.33           C  
ANISOU 6150  CG1 VAL B 253    17903  19178  12439  -1769   1376   1721       C  
ATOM   6151  CG2 VAL B 253       1.128  36.541  63.980  1.00130.89           C  
ANISOU 6151  CG2 VAL B 253    17893  19376  12463  -2283   1291   1569       C  
ATOM   6152  N   ALA B 254      -2.871  36.210  65.733  1.00131.06           N  
ANISOU 6152  N   ALA B 254    17944  19458  12397  -1536   1370   1537       N  
ATOM   6153  CA  ALA B 254      -3.679  37.104  66.577  1.00133.45           C  
ANISOU 6153  CA  ALA B 254    18448  19631  12626  -1410   1455   1429       C  
ATOM   6154  C   ALA B 254      -3.714  36.630  68.038  1.00140.02           C  
ANISOU 6154  C   ALA B 254    19186  20647  13370  -1479   1417   1329       C  
ATOM   6155  O   ALA B 254      -3.820  37.458  68.945  1.00141.62           O  
ANISOU 6155  O   ALA B 254    19570  20750  13490  -1502   1476   1188       O  
ATOM   6156  CB  ALA B 254      -5.094  37.205  66.033  1.00134.10           C  
ANISOU 6156  CB  ALA B 254    18540  19686  12724  -1083   1510   1500       C  
ATOM   6157  N   ASP B 255      -3.621  35.307  68.253  1.00136.63           N  
ANISOU 6157  N   ASP B 255    18481  20479  12953  -1510   1322   1402       N  
ATOM   6158  CA  ASP B 255      -3.611  34.650  69.565  1.00137.18           C  
ANISOU 6158  CA  ASP B 255    18425  20762  12937  -1579   1271   1353       C  
ATOM   6159  C   ASP B 255      -2.321  33.789  69.667  1.00142.80           C  
ANISOU 6159  C   ASP B 255    18957  21628  13670  -1812   1156   1396       C  
ATOM   6160  O   ASP B 255      -2.358  32.663  70.170  1.00141.61           O  
ANISOU 6160  O   ASP B 255    18599  21695  13513  -1816   1080   1461       O  
ATOM   6161  CB  ASP B 255      -4.904  33.810  69.712  1.00137.77           C  
ANISOU 6161  CB  ASP B 255    18335  21001  13009  -1358   1272   1428       C  
ATOM   6162  CG  ASP B 255      -5.152  33.212  71.086  1.00147.08           C  
ANISOU 6162  CG  ASP B 255    19408  22395  14082  -1394   1242   1392       C  
ATOM   6163  OD1 ASP B 255      -5.321  33.988  72.050  1.00149.49           O  
ANISOU 6163  OD1 ASP B 255    19858  22669  14271  -1407   1297   1257       O  
ATOM   6164  OD2 ASP B 255      -5.229  31.967  71.187  1.00151.15           O  
ANISOU 6164  OD2 ASP B 255    19700  23105  14626  -1403   1168   1501       O  
ATOM   6165  N   TRP B 256      -1.177  34.332  69.193  1.00141.57           N  
ANISOU 6165  N   TRP B 256    18884  21365  13542  -2003   1148   1363       N  
ATOM   6166  CA  TRP B 256       0.139  33.683  69.101  1.00141.53           C  
ANISOU 6166  CA  TRP B 256    18716  21497  13563  -2215   1049   1395       C  
ATOM   6167  C   TRP B 256       0.694  33.104  70.418  1.00147.16           C  
ANISOU 6167  C   TRP B 256    19301  22435  14177  -2350    964   1353       C  
ATOM   6168  O   TRP B 256       1.352  32.064  70.367  1.00145.68           O  
ANISOU 6168  O   TRP B 256    18897  22427  14029  -2410    864   1438       O  
ATOM   6169  CB  TRP B 256       1.167  34.646  68.496  1.00141.54           C  
ANISOU 6169  CB  TRP B 256    18866  21335  13577  -2411   1082   1335       C  
ATOM   6170  CG  TRP B 256       2.460  34.001  68.090  1.00141.99           C  
ANISOU 6170  CG  TRP B 256    18734  21538  13676  -2597    992   1379       C  
ATOM   6171  CD1 TRP B 256       3.695  34.240  68.618  1.00146.16           C  
ANISOU 6171  CD1 TRP B 256    19243  22152  14140  -2857    947   1293       C  
ATOM   6172  CD2 TRP B 256       2.647  33.015  67.062  1.00140.04           C  
ANISOU 6172  CD2 TRP B 256    18283  21385  13540  -2531    939   1508       C  
ATOM   6173  NE1 TRP B 256       4.643  33.479  67.974  1.00144.78           N  
ANISOU 6173  NE1 TRP B 256    18857  22124  14031  -2945    870   1366       N  
ATOM   6174  CE2 TRP B 256       4.027  32.713  67.018  1.00144.35           C  
ANISOU 6174  CE2 TRP B 256    18692  22067  14087  -2745    866   1494       C  
ATOM   6175  CE3 TRP B 256       1.783  32.359  66.168  1.00139.65           C  
ANISOU 6175  CE3 TRP B 256    18145  21331  13584  -2316    947   1621       C  
ATOM   6176  CZ2 TRP B 256       4.562  31.786  66.116  1.00142.44           C  
ANISOU 6176  CZ2 TRP B 256    18238  21943  13942  -2733    808   1586       C  
ATOM   6177  CZ3 TRP B 256       2.316  31.439  65.277  1.00139.86           C  
ANISOU 6177  CZ3 TRP B 256    17969  21468  13704  -2322    889   1705       C  
ATOM   6178  CH2 TRP B 256       3.688  31.158  65.260  1.00140.83           C  
ANISOU 6178  CH2 TRP B 256    17967  21711  13832  -2521    822   1686       C  
ATOM   6179  N   ARG B 257       0.453  33.752  71.571  1.00146.31           N  
ANISOU 6179  N   ARG B 257    19324  22327  13938  -2391   1001   1225       N  
ATOM   6180  CA  ARG B 257       0.969  33.264  72.854  1.00147.24           C  
ANISOU 6180  CA  ARG B 257    19326  22683  13935  -2522    919   1187       C  
ATOM   6181  C   ARG B 257       0.336  31.931  73.273  1.00150.90           C  
ANISOU 6181  C   ARG B 257    19575  23358  14404  -2381    855   1325       C  
ATOM   6182  O   ARG B 257       0.980  31.161  73.992  1.00150.76           O  
ANISOU 6182  O   ARG B 257    19396  23557  14329  -2480    756   1370       O  
ATOM   6183  CB  ARG B 257       0.788  34.310  73.955  1.00150.17           C  
ANISOU 6183  CB  ARG B 257    19896  23009  14152  -2595    985   1001       C  
ATOM   6184  CG  ARG B 257       1.896  35.343  73.936  1.00163.95           C  
ANISOU 6184  CG  ARG B 257    21792  24640  15860  -2849   1002    855       C  
ATOM   6185  CD  ARG B 257       1.645  36.476  74.900  1.00179.61           C  
ANISOU 6185  CD  ARG B 257    24008  26527  17707  -2916   1086    645       C  
ATOM   6186  NE  ARG B 257       2.579  37.576  74.660  1.00190.72           N  
ANISOU 6186  NE  ARG B 257    25603  27754  19109  -3157   1128    504       N  
ATOM   6187  CZ  ARG B 257       2.503  38.768  75.243  1.00208.01           C  
ANISOU 6187  CZ  ARG B 257    28050  29771  21212  -3250   1220    297       C  
ATOM   6188  NH1 ARG B 257       1.533  39.030  76.111  1.00197.57           N  
ANISOU 6188  NH1 ARG B 257    26821  28449  19796  -3104   1280    199       N  
ATOM   6189  NH2 ARG B 257       3.395  39.708  74.961  1.00197.33           N  
ANISOU 6189  NH2 ARG B 257    26866  28246  19867  -3496   1259    179       N  
ATOM   6190  N   ASN B 258      -0.892  31.647  72.803  1.00147.09           N  
ANISOU 6190  N   ASN B 258    19085  22816  13987  -2158    910   1399       N  
ATOM   6191  CA  ASN B 258      -1.633  30.421  73.085  1.00146.02           C  
ANISOU 6191  CA  ASN B 258    18764  22849  13868  -2031    870   1530       C  
ATOM   6192  C   ASN B 258      -1.572  29.455  71.888  1.00149.24           C  
ANISOU 6192  C   ASN B 258    19013  23246  14446  -1960    825   1674       C  
ATOM   6193  O   ASN B 258      -1.497  28.244  72.090  1.00148.15           O  
ANISOU 6193  O   ASN B 258    18690  23255  14346  -1952    748   1791       O  
ATOM   6194  CB  ASN B 258      -3.082  30.753  73.448  1.00145.48           C  
ANISOU 6194  CB  ASN B 258    18776  22760  13740  -1847    967   1494       C  
ATOM   6195  CG  ASN B 258      -3.875  29.571  73.953  1.00163.20           C  
ANISOU 6195  CG  ASN B 258    20841  25199  15970  -1756    937   1614       C  
ATOM   6196  OD1 ASN B 258      -3.725  29.134  75.099  1.00158.52           O  
ANISOU 6196  OD1 ASN B 258    20181  24788  15260  -1833    893   1627       O  
ATOM   6197  ND2 ASN B 258      -4.740  29.038  73.101  1.00151.99           N  
ANISOU 6197  ND2 ASN B 258    19339  23751  14658  -1600    963   1706       N  
ATOM   6198  N   SER B 259      -1.596  29.998  70.651  1.00145.96           N  
ANISOU 6198  N   SER B 259    18678  22652  14127  -1911    875   1665       N  
ATOM   6199  CA  SER B 259      -1.554  29.235  69.395  1.00144.58           C  
ANISOU 6199  CA  SER B 259    18371  22460  14101  -1845    845   1773       C  
ATOM   6200  C   SER B 259      -0.240  28.463  69.212  1.00148.53           C  
ANISOU 6200  C   SER B 259    18714  23058  14662  -1989    742   1823       C  
ATOM   6201  O   SER B 259      -0.278  27.326  68.736  1.00147.65           O  
ANISOU 6201  O   SER B 259    18429  23018  14653  -1930    690   1924       O  
ATOM   6202  CB  SER B 259      -1.727  30.157  68.189  1.00148.39           C  
ANISOU 6202  CB  SER B 259    18995  22746  14638  -1786    922   1746       C  
ATOM   6203  OG  SER B 259      -2.895  30.962  68.130  1.00158.14           O  
ANISOU 6203  OG  SER B 259    20383  23868  15834  -1620   1020   1707       O  
ATOM   6204  N   ASN B 260       0.919  29.093  69.540  1.00145.38           N  
ANISOU 6204  N   ASN B 260    18373  22663  14202  -2177    717   1743       N  
ATOM   6205  CA  ASN B 260       2.260  28.509  69.385  1.00144.66           C  
ANISOU 6205  CA  ASN B 260    18126  22688  14150  -2316    621   1773       C  
ATOM   6206  C   ASN B 260       2.503  27.434  70.466  1.00147.46           C  
ANISOU 6206  C   ASN B 260    18314  23251  14463  -2327    521   1845       C  
ATOM   6207  O   ASN B 260       3.341  27.603  71.357  1.00148.45           O  
ANISOU 6207  O   ASN B 260    18418  23502  14482  -2470    464   1800       O  
ATOM   6208  CB  ASN B 260       3.340  29.610  69.415  1.00146.82           C  
ANISOU 6208  CB  ASN B 260    18513  22915  14355  -2526    635   1654       C  
ATOM   6209  CG  ASN B 260       4.703  29.190  68.911  1.00167.58           C  
ANISOU 6209  CG  ASN B 260    20983  25654  17036  -2662    559   1673       C  
ATOM   6210  OD1 ASN B 260       4.899  28.889  67.728  1.00161.15           O  
ANISOU 6210  OD1 ASN B 260    20099  24797  16335  -2622    566   1723       O  
ATOM   6211  ND2 ASN B 260       5.695  29.227  69.785  1.00159.82           N  
ANISOU 6211  ND2 ASN B 260    19935  24832  15957  -2830    488   1622       N  
ATOM   6212  N   ARG B 261       1.753  26.321  70.367  1.00141.54           N  
ANISOU 6212  N   ARG B 261    17447  22540  13793  -2179    501   1962       N  
ATOM   6213  CA  ARG B 261       1.804  25.164  71.258  1.00140.68           C  
ANISOU 6213  CA  ARG B 261    17189  22595  13668  -2158    415   2071       C  
ATOM   6214  C   ARG B 261       1.454  23.898  70.479  1.00140.87           C  
ANISOU 6214  C   ARG B 261    17068  22598  13857  -2034    390   2192       C  
ATOM   6215  O   ARG B 261       0.442  23.868  69.775  1.00139.31           O  
ANISOU 6215  O   ARG B 261    16904  22300  13727  -1922    460   2198       O  
ATOM   6216  CB  ARG B 261       0.856  25.346  72.459  1.00142.18           C  
ANISOU 6216  CB  ARG B 261    17456  22846  13719  -2125    451   2065       C  
ATOM   6217  CG  ARG B 261       1.491  26.077  73.638  1.00155.28           C  
ANISOU 6217  CG  ARG B 261    19185  24619  15197  -2272    426   1972       C  
ATOM   6218  CD  ARG B 261       0.583  26.126  74.856  1.00166.15           C  
ANISOU 6218  CD  ARG B 261    20613  26093  16425  -2237    458   1970       C  
ATOM   6219  NE  ARG B 261      -0.142  27.393  74.972  1.00176.41           N  
ANISOU 6219  NE  ARG B 261    22112  27277  17639  -2218    572   1817       N  
ATOM   6220  CZ  ARG B 261      -0.410  28.006  76.125  1.00193.99           C  
ANISOU 6220  CZ  ARG B 261    24432  29589  19686  -2267    605   1719       C  
ATOM   6221  NH1 ARG B 261       0.038  27.501  77.273  1.00182.44           N  
ANISOU 6221  NH1 ARG B 261    22878  28351  18091  -2355    524   1763       N  
ATOM   6222  NH2 ARG B 261      -1.076  29.149  76.138  1.00182.96           N  
ANISOU 6222  NH2 ARG B 261    23224  28058  18233  -2225    716   1573       N  
ATOM   6223  N   TYR B 262       2.303  22.862  70.597  1.00136.00           N  
ANISOU 6223  N   TYR B 262    16290  22081  13304  -2049    291   2281       N  
ATOM   6224  CA  TYR B 262       2.128  21.566  69.936  1.00134.19           C  
ANISOU 6224  CA  TYR B 262    15925  21822  13241  -1943    260   2387       C  
ATOM   6225  C   TYR B 262       0.926  20.807  70.523  1.00135.11           C  
ANISOU 6225  C   TYR B 262    16035  21943  13358  -1856    280   2486       C  
ATOM   6226  O   TYR B 262       0.721  20.872  71.736  1.00135.65           O  
ANISOU 6226  O   TYR B 262    16136  22112  13294  -1890    265   2523       O  
ATOM   6227  CB  TYR B 262       3.410  20.725  70.057  1.00136.45           C  
ANISOU 6227  CB  TYR B 262    16052  22210  13583  -1970    147   2452       C  
ATOM   6228  CG  TYR B 262       4.493  21.135  69.081  1.00138.97           C  
ANISOU 6228  CG  TYR B 262    16323  22523  13957  -2031    137   2366       C  
ATOM   6229  CD1 TYR B 262       5.418  22.124  69.407  1.00142.19           C  
ANISOU 6229  CD1 TYR B 262    16768  23014  14245  -2178    121   2274       C  
ATOM   6230  CD2 TYR B 262       4.597  20.531  67.833  1.00139.02           C  
ANISOU 6230  CD2 TYR B 262    16242  22454  14126  -1956    148   2368       C  
ATOM   6231  CE1 TYR B 262       6.413  22.511  68.507  1.00143.49           C  
ANISOU 6231  CE1 TYR B 262    16881  23189  14451  -2255    120   2198       C  
ATOM   6232  CE2 TYR B 262       5.587  20.908  66.926  1.00140.05           C  
ANISOU 6232  CE2 TYR B 262    16317  22602  14292  -2018    146   2289       C  
ATOM   6233  CZ  TYR B 262       6.497  21.895  67.270  1.00148.56           C  
ANISOU 6233  CZ  TYR B 262    17430  23767  15249  -2171    133   2211       C  
ATOM   6234  OH  TYR B 262       7.478  22.267  66.384  1.00149.31           O  
ANISOU 6234  OH  TYR B 262    17463  23897  15370  -2252    138   2138       O  
ATOM   6235  N   PRO B 263       0.089  20.121  69.708  1.00128.86           N  
ANISOU 6235  N   PRO B 263    15202  21061  12698  -1759    320   2523       N  
ATOM   6236  CA  PRO B 263       0.187  19.912  68.255  1.00126.95           C  
ANISOU 6236  CA  PRO B 263    14909  20720  12605  -1711    341   2482       C  
ATOM   6237  C   PRO B 263      -0.584  20.930  67.401  1.00127.97           C  
ANISOU 6237  C   PRO B 263    15144  20767  12711  -1675    439   2383       C  
ATOM   6238  O   PRO B 263      -0.590  20.797  66.171  1.00127.11           O  
ANISOU 6238  O   PRO B 263    14994  20597  12705  -1634    461   2351       O  
ATOM   6239  CB  PRO B 263      -0.412  18.515  68.093  1.00128.59           C  
ANISOU 6239  CB  PRO B 263    15016  20898  12944  -1637    327   2581       C  
ATOM   6240  CG  PRO B 263      -1.500  18.455  69.146  1.00133.87           C  
ANISOU 6240  CG  PRO B 263    15737  21615  13511  -1631    362   2643       C  
ATOM   6241  CD  PRO B 263      -1.063  19.383  70.270  1.00130.46           C  
ANISOU 6241  CD  PRO B 263    15391  21281  12898  -1704    346   2617       C  
ATOM   6242  N   ALA B 264      -1.231  21.938  68.035  1.00122.43           N  
ANISOU 6242  N   ALA B 264    14577  20069  11871  -1679    498   2335       N  
ATOM   6243  CA  ALA B 264      -2.011  22.971  67.345  1.00120.48           C  
ANISOU 6243  CA  ALA B 264    14447  19737  11591  -1616    592   2255       C  
ATOM   6244  C   ALA B 264      -1.144  23.805  66.390  1.00120.64           C  
ANISOU 6244  C   ALA B 264    14528  19679  11632  -1668    603   2183       C  
ATOM   6245  O   ALA B 264      -1.608  24.162  65.309  1.00119.78           O  
ANISOU 6245  O   ALA B 264    14449  19497  11563  -1598    658   2158       O  
ATOM   6246  CB  ALA B 264      -2.692  23.875  68.357  1.00122.04           C  
ANISOU 6246  CB  ALA B 264    14782  19952  11635  -1607    648   2210       C  
ATOM   6247  N   VAL B 265       0.125  24.063  66.772  1.00115.16           N  
ANISOU 6247  N   VAL B 265    13834  19019  10904  -1798    549   2157       N  
ATOM   6248  CA  VAL B 265       1.093  24.843  65.994  1.00114.05           C  
ANISOU 6248  CA  VAL B 265    13740  18827  10769  -1890    560   2090       C  
ATOM   6249  C   VAL B 265       1.507  24.104  64.684  1.00114.62           C  
ANISOU 6249  C   VAL B 265    13672  18899  10978  -1857    539   2115       C  
ATOM   6250  O   VAL B 265       1.915  24.774  63.736  1.00114.08           O  
ANISOU 6250  O   VAL B 265    13652  18776  10917  -1897    577   2070       O  
ATOM   6251  CB  VAL B 265       2.322  25.252  66.861  1.00118.91           C  
ANISOU 6251  CB  VAL B 265    14365  19519  11295  -2056    504   2047       C  
ATOM   6252  CG1 VAL B 265       3.284  24.089  67.100  1.00118.78           C  
ANISOU 6252  CG1 VAL B 265    14149  19642  11342  -2087    396   2111       C  
ATOM   6253  CG2 VAL B 265       3.050  26.454  66.270  1.00119.31           C  
ANISOU 6253  CG2 VAL B 265    14533  19492  11307  -2181    549   1957       C  
ATOM   6254  N   ILE B 266       1.383  22.753  64.625  1.00108.95           N  
ANISOU 6254  N   ILE B 266    12795  18236  10366  -1788    486   2182       N  
ATOM   6255  CA  ILE B 266       1.737  21.960  63.436  1.00107.41           C  
ANISOU 6255  CA  ILE B 266    12464  18044  10305  -1748    470   2185       C  
ATOM   6256  C   ILE B 266       0.879  22.406  62.246  1.00111.25           C  
ANISOU 6256  C   ILE B 266    13005  18459  10806  -1673    550   2153       C  
ATOM   6257  O   ILE B 266       1.426  22.678  61.175  1.00110.78           O  
ANISOU 6257  O   ILE B 266    12924  18393  10773  -1699    568   2114       O  
ATOM   6258  CB  ILE B 266       1.635  20.427  63.690  1.00109.67           C  
ANISOU 6258  CB  ILE B 266    12598  18365  10707  -1682    408   2258       C  
ATOM   6259  CG1 ILE B 266       2.747  19.969  64.642  1.00110.65           C  
ANISOU 6259  CG1 ILE B 266    12645  18576  10821  -1742    316   2302       C  
ATOM   6260  CG2 ILE B 266       1.686  19.621  62.379  1.00109.20           C  
ANISOU 6260  CG2 ILE B 266    12418  18284  10787  -1620    413   2234       C  
ATOM   6261  CD1 ILE B 266       2.455  18.726  65.370  1.00117.36           C  
ANISOU 6261  CD1 ILE B 266    13416  19439  11735  -1679    262   2406       C  
ATOM   6262  N   LEU B 267      -0.442  22.543  62.456  1.00108.11           N  
ANISOU 6262  N   LEU B 267    12673  18029  10373  -1581    599   2171       N  
ATOM   6263  CA  LEU B 267      -1.384  22.950  61.415  1.00107.75           C  
ANISOU 6263  CA  LEU B 267    12669  17946  10326  -1485    669   2152       C  
ATOM   6264  C   LEU B 267      -1.152  24.385  60.931  1.00112.86           C  
ANISOU 6264  C   LEU B 267    13478  18518  10887  -1511    727   2115       C  
ATOM   6265  O   LEU B 267      -1.507  24.686  59.790  1.00113.09           O  
ANISOU 6265  O   LEU B 267    13519  18529  10922  -1450    770   2110       O  
ATOM   6266  CB  LEU B 267      -2.826  22.765  61.876  1.00107.63           C  
ANISOU 6266  CB  LEU B 267    12667  17946  10280  -1380    704   2179       C  
ATOM   6267  CG  LEU B 267      -3.284  21.328  61.785  1.00111.82           C  
ANISOU 6267  CG  LEU B 267    13037  18531  10918  -1348    671   2214       C  
ATOM   6268  CD1 LEU B 267      -3.440  20.714  63.160  1.00112.48           C  
ANISOU 6268  CD1 LEU B 267    13103  18647  10989  -1379    637   2273       C  
ATOM   6269  CD2 LEU B 267      -4.516  21.193  60.920  1.00113.53           C  
ANISOU 6269  CD2 LEU B 267    13211  18780  11146  -1244    722   2199       C  
ATOM   6270  N   PHE B 268      -0.525  25.249  61.763  1.00109.62           N  
ANISOU 6270  N   PHE B 268    13193  18065  10393  -1612    728   2090       N  
ATOM   6271  CA  PHE B 268      -0.179  26.619  61.377  1.00110.07           C  
ANISOU 6271  CA  PHE B 268    13426  18019  10377  -1670    787   2053       C  
ATOM   6272  C   PHE B 268       0.888  26.564  60.279  1.00113.38           C  
ANISOU 6272  C   PHE B 268    13774  18461  10844  -1762    776   2044       C  
ATOM   6273  O   PHE B 268       0.723  27.188  59.228  1.00113.05           O  
ANISOU 6273  O   PHE B 268    13804  18363  10788  -1733    832   2052       O  
ATOM   6274  CB  PHE B 268       0.302  27.430  62.595  1.00113.06           C  
ANISOU 6274  CB  PHE B 268    13942  18355  10660  -1786    788   2006       C  
ATOM   6275  CG  PHE B 268       1.159  28.632  62.282  1.00116.05           C  
ANISOU 6275  CG  PHE B 268    14473  18634  10986  -1926    829   1957       C  
ATOM   6276  CD1 PHE B 268       0.584  29.833  61.893  1.00120.13           C  
ANISOU 6276  CD1 PHE B 268    15204  18990  11451  -1874    919   1946       C  
ATOM   6277  CD2 PHE B 268       2.542  28.566  62.390  1.00119.23           C  
ANISOU 6277  CD2 PHE B 268    14806  19106  11389  -2112    780   1925       C  
ATOM   6278  CE1 PHE B 268       1.374  30.947  61.616  1.00122.62           C  
ANISOU 6278  CE1 PHE B 268    15683  19186  11722  -2023    965   1908       C  
ATOM   6279  CE2 PHE B 268       3.335  29.674  62.093  1.00123.61           C  
ANISOU 6279  CE2 PHE B 268    15500  19576  11892  -2273    825   1876       C  
ATOM   6280  CZ  PHE B 268       2.745  30.859  61.712  1.00122.58           C  
ANISOU 6280  CZ  PHE B 268    15602  19256  11716  -2237    920   1870       C  
ATOM   6281  N   TYR B 269       1.956  25.773  60.518  1.00109.31           N  
ANISOU 6281  N   TYR B 269    13105  18047  10381  -1859    702   2034       N  
ATOM   6282  CA  TYR B 269       3.060  25.565  59.584  1.00108.85           C  
ANISOU 6282  CA  TYR B 269    12938  18053  10368  -1946    685   2014       C  
ATOM   6283  C   TYR B 269       2.606  24.779  58.351  1.00110.94           C  
ANISOU 6283  C   TYR B 269    13078  18359  10717  -1833    695   2027       C  
ATOM   6284  O   TYR B 269       3.174  24.974  57.281  1.00110.68           O  
ANISOU 6284  O   TYR B 269    13008  18356  10687  -1879    719   2009       O  
ATOM   6285  CB  TYR B 269       4.234  24.867  60.271  1.00110.45           C  
ANISOU 6285  CB  TYR B 269    12992  18372  10601  -2044    600   1999       C  
ATOM   6286  CG  TYR B 269       4.996  25.766  61.221  1.00113.70           C  
ANISOU 6286  CG  TYR B 269    13505  18785  10910  -2207    590   1962       C  
ATOM   6287  CD1 TYR B 269       5.904  26.708  60.745  1.00116.86           C  
ANISOU 6287  CD1 TYR B 269    13968  19178  11255  -2370    626   1914       C  
ATOM   6288  CD2 TYR B 269       4.835  25.654  62.597  1.00114.92           C  
ANISOU 6288  CD2 TYR B 269    13685  18965  11014  -2216    546   1969       C  
ATOM   6289  CE1 TYR B 269       6.611  27.538  61.617  1.00119.04           C  
ANISOU 6289  CE1 TYR B 269    14337  19460  11435  -2546    620   1861       C  
ATOM   6290  CE2 TYR B 269       5.539  26.476  63.479  1.00117.25           C  
ANISOU 6290  CE2 TYR B 269    14065  19282  11201  -2378    536   1915       C  
ATOM   6291  CZ  TYR B 269       6.425  27.419  62.985  1.00125.80           C  
ANISOU 6291  CZ  TYR B 269    15213  20346  12237  -2548    573   1854       C  
ATOM   6292  OH  TYR B 269       7.116  28.230  63.854  1.00128.49           O  
ANISOU 6292  OH  TYR B 269    15638  20712  12470  -2732    565   1783       O  
ATOM   6293  N   VAL B 270       1.576  23.917  58.496  1.00106.46           N  
ANISOU 6293  N   VAL B 270    12444  17801  10206  -1699    681   2053       N  
ATOM   6294  CA  VAL B 270       0.967  23.164  57.391  1.00105.56           C  
ANISOU 6294  CA  VAL B 270    12217  17729  10163  -1596    693   2048       C  
ATOM   6295  C   VAL B 270       0.258  24.186  56.484  1.00109.59           C  
ANISOU 6295  C   VAL B 270    12852  18196  10591  -1539    769   2060       C  
ATOM   6296  O   VAL B 270       0.490  24.190  55.274  1.00108.89           O  
ANISOU 6296  O   VAL B 270    12711  18156  10507  -1538    791   2045       O  
ATOM   6297  CB  VAL B 270       0.016  22.031  57.886  1.00108.69           C  
ANISOU 6297  CB  VAL B 270    12523  18142  10633  -1498    664   2069       C  
ATOM   6298  CG1 VAL B 270      -0.922  21.551  56.780  1.00107.93           C  
ANISOU 6298  CG1 VAL B 270    12351  18084  10574  -1399    695   2050       C  
ATOM   6299  CG2 VAL B 270       0.803  20.857  58.451  1.00108.52           C  
ANISOU 6299  CG2 VAL B 270    12363  18157  10714  -1535    589   2072       C  
ATOM   6300  N   ASN B 271      -0.546  25.088  57.092  1.00106.86           N  
ANISOU 6300  N   ASN B 271    12675  17764  10163  -1487    811   2088       N  
ATOM   6301  CA  ASN B 271      -1.277  26.151  56.400  1.00107.54           C  
ANISOU 6301  CA  ASN B 271    12906  17787  10166  -1402    882   2118       C  
ATOM   6302  C   ASN B 271      -0.331  27.182  55.789  1.00113.58           C  
ANISOU 6302  C   ASN B 271    13790  18488  10878  -1516    920   2124       C  
ATOM   6303  O   ASN B 271      -0.659  27.754  54.747  1.00113.75           O  
ANISOU 6303  O   ASN B 271    13874  18495  10852  -1457    969   2162       O  
ATOM   6304  CB  ASN B 271      -2.264  26.829  57.336  1.00107.68           C  
ANISOU 6304  CB  ASN B 271    13073  17723  10119  -1311    916   2135       C  
ATOM   6305  CG  ASN B 271      -3.633  26.211  57.263  1.00129.86           C  
ANISOU 6305  CG  ASN B 271    15791  20612  12940  -1150    920   2150       C  
ATOM   6306  OD1 ASN B 271      -4.514  26.700  56.558  1.00126.99           O  
ANISOU 6306  OD1 ASN B 271    15470  20255  12525  -1017    964   2177       O  
ATOM   6307  ND2 ASN B 271      -3.837  25.108  57.965  1.00119.96           N  
ANISOU 6307  ND2 ASN B 271    14402  19428  11748  -1161    873   2138       N  
ATOM   6308  N   ALA B 272       0.844  27.397  56.418  1.00111.10           N  
ANISOU 6308  N   ALA B 272    13500  18152  10563  -1684    897   2092       N  
ATOM   6309  CA  ALA B 272       1.882  28.307  55.931  1.00112.28           C  
ANISOU 6309  CA  ALA B 272    13745  18255  10663  -1841    934   2088       C  
ATOM   6310  C   ALA B 272       2.424  27.832  54.575  1.00117.22           C  
ANISOU 6310  C   ALA B 272    14223  19000  11316  -1867    935   2090       C  
ATOM   6311  O   ALA B 272       2.606  28.646  53.666  1.00118.03           O  
ANISOU 6311  O   ALA B 272    14424  19066  11356  -1907    994   2127       O  
ATOM   6312  CB  ALA B 272       3.008  28.402  56.948  1.00113.48           C  
ANISOU 6312  CB  ALA B 272    13894  18414  10808  -2022    894   2036       C  
ATOM   6313  N   CYS B 273       2.626  26.505  54.435  1.00113.35           N  
ANISOU 6313  N   CYS B 273    13504  18648  10916  -1835    874   2051       N  
ATOM   6314  CA  CYS B 273       3.111  25.844  53.226  1.00113.37           C  
ANISOU 6314  CA  CYS B 273    13335  18786  10955  -1843    870   2024       C  
ATOM   6315  C   CYS B 273       2.098  25.976  52.090  1.00118.88           C  
ANISOU 6315  C   CYS B 273    14053  19505  11613  -1712    916   2060       C  
ATOM   6316  O   CYS B 273       2.472  26.389  50.990  1.00119.14           O  
ANISOU 6316  O   CYS B 273    14087  19591  11588  -1756    958   2076       O  
ATOM   6317  CB  CYS B 273       3.437  24.383  53.511  1.00112.72           C  
ANISOU 6317  CB  CYS B 273    13031  18805  10992  -1814    797   1966       C  
ATOM   6318  SG  CYS B 273       4.847  24.148  54.617  1.00116.97           S  
ANISOU 6318  SG  CYS B 273    13497  19382  11563  -1958    732   1932       S  
ATOM   6319  N   PHE B 274       0.815  25.661  52.361  1.00116.16           N  
ANISOU 6319  N   PHE B 274    13716  19138  11283  -1557    909   2078       N  
ATOM   6320  CA  PHE B 274      -0.250  25.754  51.364  1.00116.89           C  
ANISOU 6320  CA  PHE B 274    13805  19282  11325  -1419    942   2110       C  
ATOM   6321  C   PHE B 274      -0.554  27.214  50.992  1.00121.82           C  
ANISOU 6321  C   PHE B 274    14652  19805  11830  -1390   1010   2201       C  
ATOM   6322  O   PHE B 274      -1.085  27.451  49.907  1.00121.80           O  
ANISOU 6322  O   PHE B 274    14647  19871  11760  -1302   1040   2245       O  
ATOM   6323  CB  PHE B 274      -1.518  25.026  51.832  1.00118.69           C  
ANISOU 6323  CB  PHE B 274    13966  19535  11596  -1277    917   2099       C  
ATOM   6324  CG  PHE B 274      -1.383  23.520  51.820  1.00120.33           C  
ANISOU 6324  CG  PHE B 274    13958  19840  11924  -1289    863   2020       C  
ATOM   6325  CD1 PHE B 274      -1.543  22.799  50.642  1.00124.11           C  
ANISOU 6325  CD1 PHE B 274    14284  20451  12422  -1257    862   1965       C  
ATOM   6326  CD2 PHE B 274      -1.112  22.820  52.989  1.00122.46           C  
ANISOU 6326  CD2 PHE B 274    14185  20061  12282  -1329    815   2001       C  
ATOM   6327  CE1 PHE B 274      -1.419  21.404  50.633  1.00124.86           C  
ANISOU 6327  CE1 PHE B 274    14199  20601  12639  -1267    820   1879       C  
ATOM   6328  CE2 PHE B 274      -0.984  21.426  52.980  1.00125.04           C  
ANISOU 6328  CE2 PHE B 274    14336  20442  12731  -1330    769   1940       C  
ATOM   6329  CZ  PHE B 274      -1.135  20.729  51.801  1.00123.38           C  
ANISOU 6329  CZ  PHE B 274    13988  20335  12554  -1300    775   1874       C  
ATOM   6330  N   PHE B 275      -0.179  28.188  51.852  1.00119.23           N  
ANISOU 6330  N   PHE B 275    14517  19315  11471  -1467   1034   2227       N  
ATOM   6331  CA  PHE B 275      -0.366  29.607  51.550  1.00120.52           C  
ANISOU 6331  CA  PHE B 275    14922  19333  11535  -1452   1106   2312       C  
ATOM   6332  C   PHE B 275       0.716  30.088  50.576  1.00125.21           C  
ANISOU 6332  C   PHE B 275    15542  19951  12083  -1609   1143   2341       C  
ATOM   6333  O   PHE B 275       0.386  30.735  49.582  1.00125.50           O  
ANISOU 6333  O   PHE B 275    15669  19979  12038  -1549   1192   2429       O  
ATOM   6334  CB  PHE B 275      -0.377  30.471  52.821  1.00122.98           C  
ANISOU 6334  CB  PHE B 275    15443  19450  11833  -1488   1127   2307       C  
ATOM   6335  CG  PHE B 275      -0.463  31.953  52.541  1.00126.39           C  
ANISOU 6335  CG  PHE B 275    16152  19689  12181  -1485   1208   2386       C  
ATOM   6336  CD1 PHE B 275      -1.656  32.530  52.120  1.00130.36           C  
ANISOU 6336  CD1 PHE B 275    16770  20132  12628  -1266   1249   2468       C  
ATOM   6337  CD2 PHE B 275       0.655  32.768  52.673  1.00129.73           C  
ANISOU 6337  CD2 PHE B 275    16720  19992  12580  -1701   1245   2381       C  
ATOM   6338  CE1 PHE B 275      -1.728  33.896  51.833  1.00133.21           C  
ANISOU 6338  CE1 PHE B 275    17406  20288  12921  -1245   1326   2556       C  
ATOM   6339  CE2 PHE B 275       0.581  34.134  52.392  1.00134.49           C  
ANISOU 6339  CE2 PHE B 275    17602  20382  13115  -1709   1328   2459       C  
ATOM   6340  CZ  PHE B 275      -0.610  34.689  51.975  1.00133.37           C  
ANISOU 6340  CZ  PHE B 275    17590  20156  12928  -1472   1368   2552       C  
ATOM   6341  N   VAL B 276       2.002  29.782  50.878  1.00121.69           N  
ANISOU 6341  N   VAL B 276    15011  19548  11678  -1808   1118   2274       N  
ATOM   6342  CA  VAL B 276       3.177  30.127  50.064  1.00122.46           C  
ANISOU 6342  CA  VAL B 276    15093  19706  11732  -1992   1153   2282       C  
ATOM   6343  C   VAL B 276       3.030  29.469  48.679  1.00127.13           C  
ANISOU 6343  C   VAL B 276    15509  20492  12303  -1921   1155   2289       C  
ATOM   6344  O   VAL B 276       3.264  30.127  47.664  1.00127.87           O  
ANISOU 6344  O   VAL B 276    15672  20608  12304  -1971   1213   2362       O  
ATOM   6345  CB  VAL B 276       4.500  29.732  50.785  1.00125.88           C  
ANISOU 6345  CB  VAL B 276    15412  20198  12218  -2192   1112   2190       C  
ATOM   6346  CG1 VAL B 276       5.694  29.700  49.831  1.00126.35           C  
ANISOU 6346  CG1 VAL B 276    15357  20407  12244  -2361   1137   2172       C  
ATOM   6347  CG2 VAL B 276       4.779  30.666  51.957  1.00126.46           C  
ANISOU 6347  CG2 VAL B 276    15690  20091  12270  -2309   1127   2184       C  
ATOM   6348  N   GLY B 277       2.595  28.206  48.669  1.00123.20           N  
ANISOU 6348  N   GLY B 277    14800  20127  11883  -1808   1095   2215       N  
ATOM   6349  CA  GLY B 277       2.348  27.429  47.458  1.00123.09           C  
ANISOU 6349  CA  GLY B 277    14603  20306  11858  -1733   1090   2186       C  
ATOM   6350  C   GLY B 277       1.283  28.036  46.563  1.00127.93           C  
ANISOU 6350  C   GLY B 277    15313  20930  12363  -1591   1131   2286       C  
ATOM   6351  O   GLY B 277       1.442  28.051  45.337  1.00128.44           O  
ANISOU 6351  O   GLY B 277    15312  21140  12347  -1602   1160   2307       O  
ATOM   6352  N   SER B 278       0.200  28.570  47.178  1.00124.24           N  
ANISOU 6352  N   SER B 278    14999  20327  11881  -1451   1136   2351       N  
ATOM   6353  CA  SER B 278      -0.914  29.222  46.482  1.00124.76           C  
ANISOU 6353  CA  SER B 278    15165  20396  11841  -1277   1169   2460       C  
ATOM   6354  C   SER B 278      -0.465  30.505  45.784  1.00129.93           C  
ANISOU 6354  C   SER B 278    16024  20963  12380  -1343   1240   2590       C  
ATOM   6355  O   SER B 278      -0.957  30.797  44.693  1.00130.22           O  
ANISOU 6355  O   SER B 278    16068  21099  12309  -1245   1264   2679       O  
ATOM   6356  CB  SER B 278      -2.052  29.527  47.448  1.00127.85           C  
ANISOU 6356  CB  SER B 278    15670  20658  12251  -1115   1161   2487       C  
ATOM   6357  OG  SER B 278      -2.679  28.326  47.863  1.00134.66           O  
ANISOU 6357  OG  SER B 278    16336  21634  13196  -1041   1103   2390       O  
ATOM   6358  N   ILE B 279       0.483  31.251  46.402  1.00126.83           N  
ANISOU 6358  N   ILE B 279    15793  20393  12002  -1519   1274   2602       N  
ATOM   6359  CA  ILE B 279       1.064  32.489  45.864  1.00128.28           C  
ANISOU 6359  CA  ILE B 279    16193  20456  12090  -1635   1351   2722       C  
ATOM   6360  C   ILE B 279       1.764  32.167  44.526  1.00132.63           C  
ANISOU 6360  C   ILE B 279    16594  21232  12568  -1739   1370   2735       C  
ATOM   6361  O   ILE B 279       1.580  32.896  43.548  1.00133.53           O  
ANISOU 6361  O   ILE B 279    16821  21354  12562  -1709   1423   2872       O  
ATOM   6362  CB  ILE B 279       2.018  33.163  46.907  1.00131.71           C  
ANISOU 6362  CB  ILE B 279    16791  20683  12570  -1847   1377   2688       C  
ATOM   6363  CG1 ILE B 279       1.284  33.540  48.234  1.00131.89           C  
ANISOU 6363  CG1 ILE B 279    16973  20493  12646  -1740   1366   2666       C  
ATOM   6364  CG2 ILE B 279       2.791  34.358  46.333  1.00134.31           C  
ANISOU 6364  CG2 ILE B 279    17332  20891  12810  -2027   1464   2796       C  
ATOM   6365  CD1 ILE B 279       0.061  34.544  48.165  1.00140.34           C  
ANISOU 6365  CD1 ILE B 279    18289  21379  13656  -1514   1414   2790       C  
ATOM   6366  N   GLY B 280       2.496  31.052  44.496  1.00128.37           N  
ANISOU 6366  N   GLY B 280    15799  20879  12096  -1839   1326   2594       N  
ATOM   6367  CA  GLY B 280       3.189  30.561  43.311  1.00128.92           C  
ANISOU 6367  CA  GLY B 280    15683  21193  12107  -1930   1340   2563       C  
ATOM   6368  C   GLY B 280       2.253  30.113  42.207  1.00133.78           C  
ANISOU 6368  C   GLY B 280    16185  22003  12644  -1751   1329   2588       C  
ATOM   6369  O   GLY B 280       2.510  30.381  41.030  1.00135.02           O  
ANISOU 6369  O   GLY B 280    16320  22307  12674  -1793   1373   2653       O  
ATOM   6370  N   TRP B 281       1.153  29.438  42.581  1.00129.53           N  
ANISOU 6370  N   TRP B 281    15566  21483  12167  -1560   1273   2535       N  
ATOM   6371  CA  TRP B 281       0.142  28.953  41.642  1.00129.69           C  
ANISOU 6371  CA  TRP B 281    15461  21704  12114  -1389   1253   2538       C  
ATOM   6372  C   TRP B 281      -0.702  30.097  41.068  1.00135.32           C  
ANISOU 6372  C   TRP B 281    16370  22367  12677  -1250   1292   2732       C  
ATOM   6373  O   TRP B 281      -1.183  29.977  39.942  1.00135.66           O  
ANISOU 6373  O   TRP B 281    16325  22623  12598  -1162   1293   2772       O  
ATOM   6374  CB  TRP B 281      -0.769  27.920  42.317  1.00127.12           C  
ANISOU 6374  CB  TRP B 281    14995  21403  11902  -1255   1185   2422       C  
ATOM   6375  CG  TRP B 281      -0.249  26.515  42.237  1.00127.20           C  
ANISOU 6375  CG  TRP B 281    14748  21563  12019  -1327   1144   2237       C  
ATOM   6376  CD1 TRP B 281       0.403  25.824  43.215  1.00129.07           C  
ANISOU 6376  CD1 TRP B 281    14918  21714  12410  -1412   1109   2130       C  
ATOM   6377  CD2 TRP B 281      -0.335  25.632  41.110  1.00127.24           C  
ANISOU 6377  CD2 TRP B 281    14535  21825  11983  -1309   1134   2135       C  
ATOM   6378  NE1 TRP B 281       0.726  24.562  42.770  1.00128.09           N  
ANISOU 6378  NE1 TRP B 281    14557  21754  12356  -1434   1081   1974       N  
ATOM   6379  CE2 TRP B 281       0.284  24.417  41.481  1.00130.25           C  
ANISOU 6379  CE2 TRP B 281    14737  22237  12515  -1380   1098   1961       C  
ATOM   6380  CE3 TRP B 281      -0.882  25.746  39.821  1.00129.49           C  
ANISOU 6380  CE3 TRP B 281    14761  22327  12112  -1237   1151   2170       C  
ATOM   6381  CZ2 TRP B 281       0.378  23.327  40.608  1.00129.66           C  
ANISOU 6381  CZ2 TRP B 281    14437  22375  12453  -1382   1087   1807       C  
ATOM   6382  CZ3 TRP B 281      -0.793  24.664  38.959  1.00130.98           C  
ANISOU 6382  CZ3 TRP B 281    14713  22756  12297  -1254   1136   2012       C  
ATOM   6383  CH2 TRP B 281      -0.166  23.474  39.352  1.00130.70           C  
ANISOU 6383  CH2 TRP B 281    14513  22721  12426  -1327   1108   1824       C  
ATOM   6384  N   LEU B 282      -0.887  31.194  41.835  1.00132.88           N  
ANISOU 6384  N   LEU B 282    16328  21784  12374  -1221   1324   2847       N  
ATOM   6385  CA  LEU B 282      -1.682  32.359  41.420  1.00134.54           C  
ANISOU 6385  CA  LEU B 282    16763  21896  12462  -1063   1365   3044       C  
ATOM   6386  C   LEU B 282      -0.849  33.434  40.703  1.00140.96           C  
ANISOU 6386  C   LEU B 282    17768  22627  13164  -1206   1444   3198       C  
ATOM   6387  O   LEU B 282      -1.432  34.376  40.159  1.00142.21           O  
ANISOU 6387  O   LEU B 282    18111  22717  13206  -1074   1481   3384       O  
ATOM   6388  CB  LEU B 282      -2.396  32.994  42.628  1.00134.45           C  
ANISOU 6388  CB  LEU B 282    16954  21613  12520   -934   1366   3078       C  
ATOM   6389  CG  LEU B 282      -3.631  32.270  43.168  1.00137.91           C  
ANISOU 6389  CG  LEU B 282    17254  22134  13011   -725   1305   2998       C  
ATOM   6390  CD1 LEU B 282      -3.868  32.627  44.617  1.00137.77           C  
ANISOU 6390  CD1 LEU B 282    17387  21867  13095   -695   1308   2964       C  
ATOM   6391  CD2 LEU B 282      -4.872  32.588  42.345  1.00140.98           C  
ANISOU 6391  CD2 LEU B 282    17640  22657  13269   -469   1300   3119       C  
ATOM   6392  N   ALA B 283       0.497  33.294  40.702  1.00138.04           N  
ANISOU 6392  N   ALA B 283    17353  22271  12827  -1472   1470   3128       N  
ATOM   6393  CA  ALA B 283       1.456  34.227  40.085  1.00140.03           C  
ANISOU 6393  CA  ALA B 283    17763  22463  12980  -1671   1553   3254       C  
ATOM   6394  C   ALA B 283       1.161  34.483  38.603  1.00145.84           C  
ANISOU 6394  C   ALA B 283    18481  23401  13529  -1600   1583   3403       C  
ATOM   6395  O   ALA B 283       1.170  35.635  38.172  1.00147.41           O  
ANISOU 6395  O   ALA B 283    18930  23455  13623  -1612   1651   3607       O  
ATOM   6396  CB  ALA B 283       2.873  33.699  40.240  1.00140.23           C  
ANISOU 6396  CB  ALA B 283    17635  22581  13064  -1949   1560   3112       C  
ATOM   6397  N   GLN B 284       0.865  33.410  37.849  1.00142.20           N  
ANISOU 6397  N   GLN B 284    17734  23269  13027  -1523   1534   3303       N  
ATOM   6398  CA  GLN B 284       0.544  33.391  36.415  1.00143.77           C  
ANISOU 6398  CA  GLN B 284    17844  23746  13036  -1450   1546   3400       C  
ATOM   6399  C   GLN B 284      -0.624  34.320  36.021  1.00150.67           C  
ANISOU 6399  C   GLN B 284    18919  24545  13785  -1205   1554   3630       C  
ATOM   6400  O   GLN B 284      -0.677  34.765  34.871  1.00152.60           O  
ANISOU 6400  O   GLN B 284    19195  24943  13844  -1184   1588   3790       O  
ATOM   6401  CB  GLN B 284       0.204  31.952  35.975  1.00143.46           C  
ANISOU 6401  CB  GLN B 284    17459  24038  13011  -1380   1477   3198       C  
ATOM   6402  CG  GLN B 284      -0.876  31.280  36.829  1.00149.78           C  
ANISOU 6402  CG  GLN B 284    18180  24790  13940  -1186   1399   3087       C  
ATOM   6403  CD  GLN B 284      -1.440  30.020  36.237  1.00160.12           C  
ANISOU 6403  CD  GLN B 284    19189  26415  15235  -1100   1340   2923       C  
ATOM   6404  OE1 GLN B 284      -1.937  29.995  35.109  1.00153.63           O  
ANISOU 6404  OE1 GLN B 284    18281  25848  14245  -1013   1337   2977       O  
ATOM   6405  NE2 GLN B 284      -1.458  28.966  37.030  1.00150.36           N  
ANISOU 6405  NE2 GLN B 284    17799  25160  14173  -1115   1289   2723       N  
ATOM   6406  N   PHE B 285      -1.548  34.600  36.963  1.00147.17           N  
ANISOU 6406  N   PHE B 285    18601  23884  13433  -1014   1523   3647       N  
ATOM   6407  CA  PHE B 285      -2.738  35.418  36.724  1.00148.93           C  
ANISOU 6407  CA  PHE B 285    18995  24036  13558   -736   1522   3846       C  
ATOM   6408  C   PHE B 285      -2.440  36.924  36.692  1.00156.33           C  
ANISOU 6408  C   PHE B 285    20306  24654  14438   -766   1609   4087       C  
ATOM   6409  O   PHE B 285      -3.341  37.711  36.390  1.00157.78           O  
ANISOU 6409  O   PHE B 285    20659  24761  14528   -525   1617   4284       O  
ATOM   6410  CB  PHE B 285      -3.842  35.085  37.735  1.00149.31           C  
ANISOU 6410  CB  PHE B 285    19007  24003  13721   -517   1462   3754       C  
ATOM   6411  CG  PHE B 285      -4.309  33.657  37.577  1.00149.07           C  
ANISOU 6411  CG  PHE B 285    18625  24296  13720   -472   1382   3552       C  
ATOM   6412  CD1 PHE B 285      -5.169  33.298  36.545  1.00153.00           C  
ANISOU 6412  CD1 PHE B 285    18949  25116  14067   -303   1342   3587       C  
ATOM   6413  CD2 PHE B 285      -3.841  32.659  38.423  1.00149.04           C  
ANISOU 6413  CD2 PHE B 285    18463  24280  13887   -611   1349   3326       C  
ATOM   6414  CE1 PHE B 285      -5.565  31.968  36.375  1.00152.45           C  
ANISOU 6414  CE1 PHE B 285    18562  25334  14027   -293   1275   3381       C  
ATOM   6415  CE2 PHE B 285      -4.241  31.331  38.253  1.00150.46           C  
ANISOU 6415  CE2 PHE B 285    18338  24725  14104   -584   1284   3141       C  
ATOM   6416  CZ  PHE B 285      -5.095  30.995  37.229  1.00149.32           C  
ANISOU 6416  CZ  PHE B 285    18034  24883  13818   -437   1251   3161       C  
ATOM   6417  N   MET B 286      -1.180  37.321  36.941  1.00154.11           N  
ANISOU 6417  N   MET B 286    20149  24201  14205  -1059   1675   4078       N  
ATOM   6418  CA  MET B 286      -0.747  38.710  36.817  1.00157.06           C  
ANISOU 6418  CA  MET B 286    20879  24274  14523  -1150   1770   4298       C  
ATOM   6419  C   MET B 286      -0.557  39.032  35.330  1.00164.18           C  
ANISOU 6419  C   MET B 286    21780  25390  15210  -1179   1811   4497       C  
ATOM   6420  O   MET B 286      -0.255  38.129  34.538  1.00162.87           O  
ANISOU 6420  O   MET B 286    21323  25596  14963  -1253   1782   4402       O  
ATOM   6421  CB  MET B 286       0.549  38.957  37.594  1.00159.19           C  
ANISOU 6421  CB  MET B 286    21251  24327  14909  -1486   1824   4198       C  
ATOM   6422  CG  MET B 286       0.340  39.244  39.050  1.00162.11           C  
ANISOU 6422  CG  MET B 286    21776  24370  15447  -1453   1816   4099       C  
ATOM   6423  SD  MET B 286       1.918  39.538  39.877  1.00166.48           S  
ANISOU 6423  SD  MET B 286    22423  24726  16105  -1872   1875   3978       S  
ATOM   6424  CE  MET B 286       2.291  41.202  39.302  1.00167.07           C  
ANISOU 6424  CE  MET B 286    22923  24484  16072  -1998   2005   4256       C  
ATOM   6425  N   ASP B 287      -0.735  40.311  34.957  1.00164.36           N  
ANISOU 6425  N   ASP B 287    22135  25177  15138  -1117   1881   4771       N  
ATOM   6426  CA  ASP B 287      -0.624  40.805  33.584  1.00167.14           C  
ANISOU 6426  CA  ASP B 287    22546  25692  15270  -1127   1928   5015       C  
ATOM   6427  C   ASP B 287       0.700  40.381  32.914  1.00171.41           C  
ANISOU 6427  C   ASP B 287    22918  26471  15737  -1483   1975   4945       C  
ATOM   6428  O   ASP B 287       1.774  40.880  33.262  1.00171.59           O  
ANISOU 6428  O   ASP B 287    23091  26289  15817  -1781   2054   4942       O  
ATOM   6429  CB  ASP B 287      -0.785  42.335  33.555  1.00172.50           C  
ANISOU 6429  CB  ASP B 287    23668  25967  15905  -1064   2014   5314       C  
ATOM   6430  CG  ASP B 287      -2.185  42.808  33.900  1.00184.96           C  
ANISOU 6430  CG  ASP B 287    25397  27377  17502   -654   1973   5427       C  
ATOM   6431  OD1 ASP B 287      -2.618  42.598  35.061  1.00184.07           O  
ANISOU 6431  OD1 ASP B 287    25283  27093  17562   -551   1935   5255       O  
ATOM   6432  OD2 ASP B 287      -2.837  43.414  33.023  1.00193.43           O  
ANISOU 6432  OD2 ASP B 287    26590  28494  18409   -432   1980   5694       O  
ATOM   6433  N   GLY B 288       0.581  39.411  32.003  1.00167.63           N  
ANISOU 6433  N   GLY B 288    22110  26443  15138  -1445   1924   4862       N  
ATOM   6434  CA  GLY B 288       1.673  38.843  31.215  1.00167.46           C  
ANISOU 6434  CA  GLY B 288    21867  26740  15022  -1723   1959   4773       C  
ATOM   6435  C   GLY B 288       2.704  38.034  31.976  1.00168.34           C  
ANISOU 6435  C   GLY B 288    21786  26871  15305  -1975   1954   4482       C  
ATOM   6436  O   GLY B 288       3.782  37.762  31.437  1.00168.27           O  
ANISOU 6436  O   GLY B 288    21637  27067  15229  -2235   2003   4419       O  
ATOM   6437  N   ALA B 289       2.384  37.632  33.224  1.00162.03           N  
ANISOU 6437  N   ALA B 289    20967  25879  14718  -1892   1893   4305       N  
ATOM   6438  CA  ALA B 289       3.288  36.873  34.085  1.00159.44           C  
ANISOU 6438  CA  ALA B 289    20469  25548  14563  -2096   1875   4042       C  
ATOM   6439  C   ALA B 289       3.448  35.427  33.632  1.00160.94           C  
ANISOU 6439  C   ALA B 289    20259  26136  14753  -2092   1814   3808       C  
ATOM   6440  O   ALA B 289       4.564  34.914  33.684  1.00160.30           O  
ANISOU 6440  O   ALA B 289    20013  26177  14718  -2321   1835   3653       O  
ATOM   6441  CB  ALA B 289       2.804  36.911  35.521  1.00158.48           C  
ANISOU 6441  CB  ALA B 289    20458  25114  14642  -1989   1828   3951       C  
ATOM   6442  N   ARG B 290       2.352  34.776  33.185  1.00155.80           N  
ANISOU 6442  N   ARG B 290    19450  25692  14053  -1835   1743   3774       N  
ATOM   6443  CA  ARG B 290       2.356  33.383  32.728  1.00153.63           C  
ANISOU 6443  CA  ARG B 290    18813  25776  13783  -1813   1686   3540       C  
ATOM   6444  C   ARG B 290       3.387  33.167  31.606  1.00158.79           C  
ANISOU 6444  C   ARG B 290    19308  26739  14285  -2022   1747   3514       C  
ATOM   6445  O   ARG B 290       4.129  32.186  31.643  1.00156.94           O  
ANISOU 6445  O   ARG B 290    18824  26677  14127  -2142   1736   3281       O  
ATOM   6446  CB  ARG B 290       0.954  32.964  32.262  1.00152.32           C  
ANISOU 6446  CB  ARG B 290    18545  25790  13541  -1524   1614   3551       C  
ATOM   6447  CG  ARG B 290       0.754  31.453  32.206  1.00157.01           C  
ANISOU 6447  CG  ARG B 290    18798  26647  14213  -1482   1543   3266       C  
ATOM   6448  CD  ARG B 290      -0.587  31.077  31.605  1.00162.61           C  
ANISOU 6448  CD  ARG B 290    19390  27580  14813  -1237   1479   3274       C  
ATOM   6449  NE  ARG B 290      -1.674  31.156  32.583  1.00165.50           N  
ANISOU 6449  NE  ARG B 290    19844  27737  15301  -1034   1421   3288       N  
ATOM   6450  CZ  ARG B 290      -2.582  32.126  32.634  1.00177.11           C  
ANISOU 6450  CZ  ARG B 290    21522  29079  16693   -838   1419   3511       C  
ATOM   6451  NH1 ARG B 290      -2.553  33.119  31.754  1.00164.02           N  
ANISOU 6451  NH1 ARG B 290    20025  27460  14837   -812   1468   3759       N  
ATOM   6452  NH2 ARG B 290      -3.529  32.109  33.561  1.00162.67           N  
ANISOU 6452  NH2 ARG B 290    19741  27086  14978   -658   1371   3493       N  
ATOM   6453  N   ARG B 291       3.462  34.108  30.648  1.00158.32           N  
ANISOU 6453  N   ARG B 291    19402  26739  14013  -2065   1817   3758       N  
ATOM   6454  CA  ARG B 291       4.395  34.051  29.523  1.00160.02           C  
ANISOU 6454  CA  ARG B 291    19490  27261  14048  -2269   1888   3769       C  
ATOM   6455  C   ARG B 291       5.830  34.388  29.966  1.00164.58           C  
ANISOU 6455  C   ARG B 291    20120  27717  14698  -2588   1967   3733       C  
ATOM   6456  O   ARG B 291       6.780  33.939  29.328  1.00164.73           O  
ANISOU 6456  O   ARG B 291    19933  28021  14638  -2775   2013   3625       O  
ATOM   6457  CB  ARG B 291       3.927  34.975  28.389  1.00163.50           C  
ANISOU 6457  CB  ARG B 291    20094  27803  14226  -2201   1935   4072       C  
ATOM   6458  CG  ARG B 291       2.550  34.576  27.855  1.00174.58           C  
ANISOU 6458  CG  ARG B 291    21395  29407  15529  -1891   1850   4093       C  
ATOM   6459  CD  ARG B 291       2.207  35.161  26.501  1.00188.47           C  
ANISOU 6459  CD  ARG B 291    23205  31420  16987  -1830   1884   4343       C  
ATOM   6460  NE  ARG B 291       1.147  34.381  25.859  1.00195.20           N  
ANISOU 6460  NE  ARG B 291    23824  32613  17729  -1595   1797   4255       N  
ATOM   6461  CZ  ARG B 291       0.768  34.517  24.591  1.00209.83           C  
ANISOU 6461  CZ  ARG B 291    25610  34815  19302  -1521   1800   4395       C  
ATOM   6462  NH1 ARG B 291       1.358  35.411  23.806  1.00201.05           N  
ANISOU 6462  NH1 ARG B 291    24656  33749  17986  -1658   1890   4651       N  
ATOM   6463  NH2 ARG B 291      -0.204  33.762  24.099  1.00194.76           N  
ANISOU 6463  NH2 ARG B 291    23475  33222  17303  -1321   1714   4283       N  
ATOM   6464  N   GLU B 292       5.986  35.147  31.068  1.00161.21           N  
ANISOU 6464  N   GLU B 292    19948  26888  14416  -2652   1982   3804       N  
ATOM   6465  CA  GLU B 292       7.294  35.497  31.634  1.00161.60           C  
ANISOU 6465  CA  GLU B 292    20049  26809  14543  -2962   2048   3757       C  
ATOM   6466  C   GLU B 292       7.892  34.269  32.359  1.00163.28           C  
ANISOU 6466  C   GLU B 292    19966  27134  14940  -3010   1987   3438       C  
ATOM   6467  O   GLU B 292       9.113  34.100  32.379  1.00163.10           O  
ANISOU 6467  O   GLU B 292    19814  27229  14927  -3257   2033   3333       O  
ATOM   6468  CB  GLU B 292       7.150  36.711  32.583  1.00163.73           C  
ANISOU 6468  CB  GLU B 292    20699  26610  14902  -3001   2080   3923       C  
ATOM   6469  CG  GLU B 292       8.386  37.122  33.378  1.00175.48           C  
ANISOU 6469  CG  GLU B 292    22261  27926  16489  -3321   2136   3858       C  
ATOM   6470  CD  GLU B 292       9.593  37.605  32.598  1.00198.81           C  
ANISOU 6470  CD  GLU B 292    25207  31040  19293  -3653   2248   3936       C  
ATOM   6471  OE1 GLU B 292       9.414  38.351  31.607  1.00200.65           O  
ANISOU 6471  OE1 GLU B 292    25598  31304  19336  -3674   2320   4177       O  
ATOM   6472  OE2 GLU B 292      10.726  37.271  33.010  1.00189.65           O  
ANISOU 6472  OE2 GLU B 292    23886  29973  18199  -3897   2266   3766       O  
ATOM   6473  N   ILE B 293       7.023  33.406  32.920  1.00158.04           N  
ANISOU 6473  N   ILE B 293    19188  26447  14413  -2770   1886   3293       N  
ATOM   6474  CA  ILE B 293       7.408  32.209  33.669  1.00155.87           C  
ANISOU 6474  CA  ILE B 293    18661  26236  14326  -2767   1818   3015       C  
ATOM   6475  C   ILE B 293       7.533  30.977  32.745  1.00160.03           C  
ANISOU 6475  C   ILE B 293    18846  27160  14800  -2717   1797   2824       C  
ATOM   6476  O   ILE B 293       8.470  30.201  32.914  1.00159.02           O  
ANISOU 6476  O   ILE B 293    18496  27169  14755  -2829   1795   2624       O  
ATOM   6477  CB  ILE B 293       6.400  31.948  34.842  1.00156.86           C  
ANISOU 6477  CB  ILE B 293    18866  26100  14633  -2552   1728   2968       C  
ATOM   6478  CG1 ILE B 293       6.357  33.139  35.830  1.00157.63           C  
ANISOU 6478  CG1 ILE B 293    19296  25805  14791  -2610   1755   3119       C  
ATOM   6479  CG2 ILE B 293       6.705  30.642  35.596  1.00155.55           C  
ANISOU 6479  CG2 ILE B 293    18446  25996  14658  -2529   1654   2702       C  
ATOM   6480  CD1 ILE B 293       5.012  33.339  36.563  1.00163.38           C  
ANISOU 6480  CD1 ILE B 293    20187  26291  15598  -2350   1696   3178       C  
ATOM   6481  N   VAL B 294       6.602  30.791  31.794  1.00157.83           N  
ANISOU 6481  N   VAL B 294    18519  27067  14383  -2545   1781   2875       N  
ATOM   6482  CA  VAL B 294       6.571  29.600  30.937  1.00157.91           C  
ANISOU 6482  CA  VAL B 294    18215  27441  14342  -2483   1758   2670       C  
ATOM   6483  C   VAL B 294       7.387  29.763  29.621  1.00165.23           C  
ANISOU 6483  C   VAL B 294    19029  28708  15042  -2649   1847   2698       C  
ATOM   6484  O   VAL B 294       8.099  28.825  29.254  1.00164.05           O  
ANISOU 6484  O   VAL B 294    18608  28815  14909  -2716   1857   2471       O  
ATOM   6485  CB  VAL B 294       5.102  29.165  30.655  1.00161.14           C  
ANISOU 6485  CB  VAL B 294    18590  27913  14722  -2217   1683   2664       C  
ATOM   6486  CG1 VAL B 294       5.031  27.956  29.720  1.00161.09           C  
ANISOU 6486  CG1 VAL B 294    18271  28282  14653  -2169   1664   2437       C  
ATOM   6487  CG2 VAL B 294       4.358  28.871  31.960  1.00158.63           C  
ANISOU 6487  CG2 VAL B 294    18342  27301  14628  -2070   1602   2608       C  
ATOM   6488  N   CYS B 295       7.268  30.908  28.910  1.00165.74           N  
ANISOU 6488  N   CYS B 295    19296  28781  14896  -2706   1914   2971       N  
ATOM   6489  CA  CYS B 295       7.957  31.098  27.617  1.00168.76           C  
ANISOU 6489  CA  CYS B 295    19579  29508  15035  -2864   2003   3023       C  
ATOM   6490  C   CYS B 295       9.422  31.494  27.763  1.00172.60           C  
ANISOU 6490  C   CYS B 295    20061  29998  15524  -3168   2094   3018       C  
ATOM   6491  O   CYS B 295       9.797  32.207  28.697  1.00171.91           O  
ANISOU 6491  O   CYS B 295    20177  29590  15553  -3284   2111   3109       O  
ATOM   6492  CB  CYS B 295       7.229  32.111  26.734  1.00172.05           C  
ANISOU 6492  CB  CYS B 295    20204  29958  15208  -2797   2037   3334       C  
ATOM   6493  SG  CYS B 295       5.448  31.829  26.551  1.00175.65           S  
ANISOU 6493  SG  CYS B 295    20674  30434  15630  -2435   1928   3378       S  
ATOM   6494  N   ARG B 296      10.224  31.090  26.757  1.00169.86           N  
ANISOU 6494  N   ARG B 296    19481  30041  15018  -3305   2161   2918       N  
ATOM   6495  CA  ARG B 296      11.638  31.427  26.599  1.00171.03           C  
ANISOU 6495  CA  ARG B 296    19568  30310  15106  -3608   2263   2910       C  
ATOM   6496  C   ARG B 296      11.751  32.765  25.856  1.00177.71           C  
ANISOU 6496  C   ARG B 296    20663  31150  15710  -3774   2365   3243       C  
ATOM   6497  O   ARG B 296      10.726  33.370  25.521  1.00178.18           O  
ANISOU 6497  O   ARG B 296    20936  31099  15667  -3623   2347   3471       O  
ATOM   6498  CB  ARG B 296      12.386  30.314  25.838  1.00171.12           C  
ANISOU 6498  CB  ARG B 296    19196  30767  15054  -3652   2290   2631       C  
ATOM   6499  CG  ARG B 296      12.678  29.084  26.674  1.00176.64           C  
ANISOU 6499  CG  ARG B 296    19663  31440  16013  -3556   2214   2309       C  
ATOM   6500  CD  ARG B 296      13.802  28.239  26.113  1.00184.31           C  
ANISOU 6500  CD  ARG B 296    20291  32793  16944  -3662   2268   2053       C  
ATOM   6501  NE  ARG B 296      15.118  28.795  26.424  1.00191.93           N  
ANISOU 6501  NE  ARG B 296    21243  33778  17902  -3939   2348   2086       N  
ATOM   6502  CZ  ARG B 296      16.180  28.065  26.751  1.00205.81           C  
ANISOU 6502  CZ  ARG B 296    22738  35689  19770  -4007   2356   1845       C  
ATOM   6503  NH1 ARG B 296      17.338  28.653  27.018  1.00197.26           N  
ANISOU 6503  NH1 ARG B 296    21642  34648  18661  -4274   2428   1888       N  
ATOM   6504  NH2 ARG B 296      16.091  26.742  26.818  1.00188.44           N  
ANISOU 6504  NH2 ARG B 296    20289  33600  17710  -3807   2292   1558       N  
ATOM   6505  N   ALA B 297      12.985  33.219  25.582  1.00175.72           N  
ANISOU 6505  N   ALA B 297    20379  31027  15362  -4082   2474   3278       N  
ATOM   6506  CA  ALA B 297      13.242  34.472  24.873  1.00178.47           C  
ANISOU 6506  CA  ALA B 297    20961  31370  15479  -4289   2588   3595       C  
ATOM   6507  C   ALA B 297      12.802  34.393  23.400  1.00184.05           C  
ANISOU 6507  C   ALA B 297    21580  32458  15891  -4213   2622   3698       C  
ATOM   6508  O   ALA B 297      12.205  35.345  22.897  1.00185.67           O  
ANISOU 6508  O   ALA B 297    22052  32562  15932  -4184   2653   4014       O  
ATOM   6509  CB  ALA B 297      14.717  34.832  24.963  1.00180.89           C  
ANISOU 6509  CB  ALA B 297    21204  31766  15758  -4659   2697   3566       C  
ATOM   6510  N   ASP B 298      13.070  33.250  22.731  1.00179.81           N  
ANISOU 6510  N   ASP B 298    20675  32355  15289  -4166   2614   3427       N  
ATOM   6511  CA  ASP B 298      12.730  33.010  21.321  1.00181.23           C  
ANISOU 6511  CA  ASP B 298    20715  32965  15179  -4103   2644   3461       C  
ATOM   6512  C   ASP B 298      11.228  32.750  21.099  1.00182.73           C  
ANISOU 6512  C   ASP B 298    20960  33123  15344  -3768   2535   3509       C  
ATOM   6513  O   ASP B 298      10.702  33.104  20.040  1.00184.73           O  
ANISOU 6513  O   ASP B 298    21256  33606  15328  -3713   2556   3697       O  
ATOM   6514  CB  ASP B 298      13.558  31.846  20.728  1.00183.36           C  
ANISOU 6514  CB  ASP B 298    20567  33705  15398  -4167   2677   3117       C  
ATOM   6515  CG  ASP B 298      13.822  30.685  21.668  1.00189.82           C  
ANISOU 6515  CG  ASP B 298    21162  34442  16519  -4064   2598   2754       C  
ATOM   6516  OD1 ASP B 298      12.866  30.235  22.339  1.00187.63           O  
ANISOU 6516  OD1 ASP B 298    20938  33921  16432  -3818   2482   2684       O  
ATOM   6517  OD2 ASP B 298      14.982  30.216  21.719  1.00195.99           O  
ANISOU 6517  OD2 ASP B 298    21709  35418  17339  -4225   2653   2546       O  
ATOM   6518  N   GLY B 299      10.569  32.133  22.076  1.00174.73           N  
ANISOU 6518  N   GLY B 299    19935  31857  14596  -3557   2420   3344       N  
ATOM   6519  CA  GLY B 299       9.146  31.814  22.004  1.00172.82           C  
ANISOU 6519  CA  GLY B 299    19721  31585  14359  -3248   2312   3357       C  
ATOM   6520  C   GLY B 299       8.839  30.345  22.204  1.00173.10           C  
ANISOU 6520  C   GLY B 299    19455  31765  14551  -3085   2225   2980       C  
ATOM   6521  O   GLY B 299       7.727  29.898  21.903  1.00171.98           O  
ANISOU 6521  O   GLY B 299    19259  31717  14369  -2861   2145   2939       O  
ATOM   6522  N   THR B 300       9.827  29.589  22.716  1.00167.77           N  
ANISOU 6522  N   THR B 300    18583  31108  14055  -3199   2240   2706       N  
ATOM   6523  CA  THR B 300       9.707  28.157  22.994  1.00165.40           C  
ANISOU 6523  CA  THR B 300    18008  30898  13936  -3063   2169   2339       C  
ATOM   6524  C   THR B 300       9.382  27.945  24.496  1.00165.64           C  
ANISOU 6524  C   THR B 300    18150  30489  14297  -2957   2080   2283       C  
ATOM   6525  O   THR B 300       9.304  28.917  25.255  1.00164.68           O  
ANISOU 6525  O   THR B 300    18301  30026  14243  -2999   2080   2510       O  
ATOM   6526  CB  THR B 300      10.996  27.399  22.569  1.00174.95           C  
ANISOU 6526  CB  THR B 300    18917  32425  15129  -3221   2242   2069       C  
ATOM   6527  OG1 THR B 300      12.101  27.839  23.354  1.00174.97           O  
ANISOU 6527  OG1 THR B 300    18977  32246  15258  -3416   2290   2103       O  
ATOM   6528  CG2 THR B 300      11.317  27.539  21.084  1.00176.91           C  
ANISOU 6528  CG2 THR B 300    19034  33145  15040  -3328   2335   2100       C  
ATOM   6529  N   MET B 301       9.198  26.674  24.917  1.00159.78           N  
ANISOU 6529  N   MET B 301    17203  29752  13754  -2826   2008   1979       N  
ATOM   6530  CA  MET B 301       8.931  26.305  26.311  1.00156.69           C  
ANISOU 6530  CA  MET B 301    16879  28989  13666  -2727   1924   1901       C  
ATOM   6531  C   MET B 301      10.211  26.372  27.130  1.00158.30           C  
ANISOU 6531  C   MET B 301    17061  29061  14024  -2899   1959   1843       C  
ATOM   6532  O   MET B 301      11.271  25.990  26.625  1.00159.18           O  
ANISOU 6532  O   MET B 301    16963  29438  14079  -3028   2023   1695       O  
ATOM   6533  CB  MET B 301       8.343  24.888  26.408  1.00157.77           C  
ANISOU 6533  CB  MET B 301    16804  29188  13953  -2547   1846   1604       C  
ATOM   6534  CG  MET B 301       6.878  24.815  26.081  1.00161.57           C  
ANISOU 6534  CG  MET B 301    17339  29689  14361  -2359   1780   1660       C  
ATOM   6535  SD  MET B 301       6.062  23.345  26.743  1.00164.10           S  
ANISOU 6535  SD  MET B 301    17510  29900  14941  -2172   1677   1364       S  
ATOM   6536  CE  MET B 301       6.670  22.084  25.612  1.00162.16           C  
ANISOU 6536  CE  MET B 301    16921  30069  14622  -2207   1721   1011       C  
ATOM   6537  N   ARG B 302      10.119  26.835  28.394  1.00151.50           N  
ANISOU 6537  N   ARG B 302    16399  27818  13348  -2897   1915   1946       N  
ATOM   6538  CA  ARG B 302      11.283  26.895  29.278  1.00149.90           C  
ANISOU 6538  CA  ARG B 302    16171  27493  13291  -3056   1933   1887       C  
ATOM   6539  C   ARG B 302      11.583  25.486  29.748  1.00150.32           C  
ANISOU 6539  C   ARG B 302    15967  27593  13555  -2949   1873   1580       C  
ATOM   6540  O   ARG B 302      10.780  24.889  30.465  1.00148.35           O  
ANISOU 6540  O   ARG B 302    15743  27143  13482  -2772   1784   1510       O  
ATOM   6541  CB  ARG B 302      11.073  27.871  30.447  1.00148.46           C  
ANISOU 6541  CB  ARG B 302    16288  26905  13217  -3095   1908   2087       C  
ATOM   6542  CG  ARG B 302      11.299  29.316  30.036  1.00158.44           C  
ANISOU 6542  CG  ARG B 302    17795  28115  14290  -3279   1998   2371       C  
ATOM   6543  CD  ARG B 302      11.269  30.281  31.192  1.00165.28           C  
ANISOU 6543  CD  ARG B 302    18951  28580  15267  -3350   1988   2532       C  
ATOM   6544  NE  ARG B 302      11.613  31.632  30.757  1.00176.02           N  
ANISOU 6544  NE  ARG B 302    20548  29878  16454  -3554   2088   2789       N  
ATOM   6545  CZ  ARG B 302      11.874  32.645  31.575  1.00190.77           C  
ANISOU 6545  CZ  ARG B 302    22677  31428  18378  -3699   2115   2931       C  
ATOM   6546  NH1 ARG B 302      11.840  32.471  32.890  1.00175.06           N  
ANISOU 6546  NH1 ARG B 302    20734  29178  16601  -3659   2047   2839       N  
ATOM   6547  NH2 ARG B 302      12.171  33.839  31.086  1.00182.65           N  
ANISOU 6547  NH2 ARG B 302    21872  30336  17189  -3891   2214   3166       N  
ATOM   6548  N   LEU B 303      12.687  24.913  29.249  1.00146.13           N  
ANISOU 6548  N   LEU B 303    15181  27349  12993  -3046   1927   1395       N  
ATOM   6549  CA  LEU B 303      13.073  23.542  29.570  1.00144.34           C  
ANISOU 6549  CA  LEU B 303    14700  27186  12958  -2932   1881   1097       C  
ATOM   6550  C   LEU B 303      14.515  23.466  30.051  1.00147.96           C  
ANISOU 6550  C   LEU B 303    15014  27713  13491  -3076   1914   1007       C  
ATOM   6551  O   LEU B 303      15.368  24.213  29.567  1.00149.50           O  
ANISOU 6551  O   LEU B 303    15193  28092  13519  -3288   2003   1094       O  
ATOM   6552  CB  LEU B 303      12.874  22.617  28.352  1.00145.20           C  
ANISOU 6552  CB  LEU B 303    14580  27628  12963  -2838   1908    885       C  
ATOM   6553  CG  LEU B 303      11.446  22.459  27.810  1.00149.05           C  
ANISOU 6553  CG  LEU B 303    15143  28114  13374  -2683   1866    916       C  
ATOM   6554  CD1 LEU B 303      11.457  21.962  26.389  1.00150.99           C  
ANISOU 6554  CD1 LEU B 303    15186  28765  13419  -2677   1924    761       C  
ATOM   6555  CD2 LEU B 303      10.628  21.518  28.664  1.00149.35           C  
ANISOU 6555  CD2 LEU B 303    15183  27902  13663  -2489   1763    783       C  
ATOM   6556  N   GLY B 304      14.763  22.555  30.995  1.00142.41           N  
ANISOU 6556  N   GLY B 304    14203  26874  13032  -2961   1840    840       N  
ATOM   6557  CA  GLY B 304      16.073  22.299  31.584  1.00142.47           C  
ANISOU 6557  CA  GLY B 304    14043  26951  13139  -3046   1846    733       C  
ATOM   6558  C   GLY B 304      16.719  23.473  32.294  1.00146.39           C  
ANISOU 6558  C   GLY B 304    14692  27331  13600  -3270   1868    927       C  
ATOM   6559  O   GLY B 304      17.951  23.534  32.373  1.00147.41           O  
ANISOU 6559  O   GLY B 304    14655  27644  13708  -3416   1910    862       O  
ATOM   6560  N   GLU B 305      15.903  24.411  32.824  1.00141.79           N  
ANISOU 6560  N   GLU B 305    14418  26448  13009  -3300   1842   1154       N  
ATOM   6561  CA  GLU B 305      16.412  25.586  33.554  1.00142.09           C  
ANISOU 6561  CA  GLU B 305    14642  26325  13020  -3520   1865   1335       C  
ATOM   6562  C   GLU B 305      16.934  25.119  34.944  1.00145.07           C  
ANISOU 6562  C   GLU B 305    14953  26551  13616  -3487   1779   1239       C  
ATOM   6563  O   GLU B 305      16.479  24.071  35.406  1.00142.91           O  
ANISOU 6563  O   GLU B 305    14595  26188  13516  -3262   1694   1110       O  
ATOM   6564  CB  GLU B 305      15.317  26.683  33.653  1.00142.86           C  
ANISOU 6564  CB  GLU B 305    15095  26136  13047  -3527   1867   1590       C  
ATOM   6565  CG  GLU B 305      15.844  28.079  33.366  1.00153.81           C  
ANISOU 6565  CG  GLU B 305    16665  27519  14258  -3807   1966   1797       C  
ATOM   6566  CD  GLU B 305      14.840  29.213  33.360  1.00166.53           C  
ANISOU 6566  CD  GLU B 305    18634  28848  15790  -3804   1982   2058       C  
ATOM   6567  OE1 GLU B 305      14.036  29.275  32.406  1.00149.37           O  
ANISOU 6567  OE1 GLU B 305    16510  26756  13488  -3694   2002   2140       O  
ATOM   6568  OE2 GLU B 305      14.910  30.090  34.254  1.00161.36           O  
ANISOU 6568  OE2 GLU B 305    18211  27912  15187  -3921   1981   2181       O  
ATOM   6569  N   PRO B 306      17.953  25.756  35.603  1.00142.97           N  
ANISOU 6569  N   PRO B 306    14691  26288  13344  -3707   1797   1280       N  
ATOM   6570  CA  PRO B 306      18.656  27.013  35.257  1.00145.34           C  
ANISOU 6570  CA  PRO B 306    15094  26668  13462  -4022   1900   1425       C  
ATOM   6571  C   PRO B 306      19.526  26.906  33.991  1.00153.52           C  
ANISOU 6571  C   PRO B 306    15892  28119  14318  -4154   2006   1349       C  
ATOM   6572  O   PRO B 306      20.480  26.129  33.943  1.00153.95           O  
ANISOU 6572  O   PRO B 306    15638  28444  14411  -4146   2006   1155       O  
ATOM   6573  CB  PRO B 306      19.509  27.307  36.508  1.00147.01           C  
ANISOU 6573  CB  PRO B 306    15297  26792  13769  -4174   1860   1408       C  
ATOM   6574  CG  PRO B 306      18.896  26.489  37.609  1.00148.72           C  
ANISOU 6574  CG  PRO B 306    15522  26780  14205  -3921   1731   1334       C  
ATOM   6575  CD  PRO B 306      18.424  25.254  36.911  1.00143.34           C  
ANISOU 6575  CD  PRO B 306    14654  26228  13580  -3657   1705   1188       C  
ATOM   6576  N   THR B 307      19.154  27.696  32.957  1.00152.72           N  
ANISOU 6576  N   THR B 307    15940  28072  14013  -4262   2098   1510       N  
ATOM   6577  CA  THR B 307      19.850  27.811  31.661  1.00155.46           C  
ANISOU 6577  CA  THR B 307    16115  28811  14142  -4418   2216   1489       C  
ATOM   6578  C   THR B 307      20.319  29.241  31.444  1.00162.74           C  
ANISOU 6578  C   THR B 307    17241  29708  14886  -4758   2323   1716       C  
ATOM   6579  O   THR B 307      19.662  30.186  31.890  1.00161.68           O  
ANISOU 6579  O   THR B 307    17445  29228  14759  -4806   2315   1926       O  
ATOM   6580  CB  THR B 307      18.978  27.371  30.468  1.00162.40           C  
ANISOU 6580  CB  THR B 307    16967  29832  14907  -4238   2236   1477       C  
ATOM   6581  OG1 THR B 307      17.662  27.909  30.579  1.00160.63           O  
ANISOU 6581  OG1 THR B 307    17056  29293  14684  -4122   2196   1672       O  
ATOM   6582  CG2 THR B 307      18.940  25.872  30.286  1.00159.40           C  
ANISOU 6582  CG2 THR B 307    16291  29627  14646  -3983   2179   1193       C  
ATOM   6583  N   SER B 308      21.443  29.394  30.727  1.00163.23           N  
ANISOU 6583  N   SER B 308    17098  30136  14786  -4993   2429   1670       N  
ATOM   6584  CA  SER B 308      22.050  30.686  30.407  1.00166.32           C  
ANISOU 6584  CA  SER B 308    17645  30558  14992  -5361   2550   1870       C  
ATOM   6585  C   SER B 308      21.163  31.534  29.474  1.00172.25           C  
ANISOU 6585  C   SER B 308    18685  31205  15556  -5383   2618   2132       C  
ATOM   6586  O   SER B 308      20.334  30.980  28.745  1.00171.35           O  
ANISOU 6586  O   SER B 308    18536  31173  15396  -5142   2593   2112       O  
ATOM   6587  CB  SER B 308      23.432  30.488  29.787  1.00172.77           C  
ANISOU 6587  CB  SER B 308    18124  31850  15670  -5586   2649   1736       C  
ATOM   6588  OG  SER B 308      23.480  29.414  28.862  1.00182.54           O  
ANISOU 6588  OG  SER B 308    19057  33448  16852  -5394   2660   1542       O  
ATOM   6589  N   ASN B 309      21.341  32.882  29.526  1.00170.93           N  
ANISOU 6589  N   ASN B 309    18810  30851  15284  -5673   2702   2379       N  
ATOM   6590  CA  ASN B 309      20.627  33.914  28.751  1.00172.35           C  
ANISOU 6590  CA  ASN B 309    19316  30886  15284  -5735   2777   2680       C  
ATOM   6591  C   ASN B 309      19.106  33.937  29.058  1.00174.01           C  
ANISOU 6591  C   ASN B 309    19793  30726  15598  -5408   2678   2792       C  
ATOM   6592  O   ASN B 309      18.307  34.270  28.174  1.00174.54           O  
ANISOU 6592  O   ASN B 309    20007  30798  15514  -5308   2706   2972       O  
ATOM   6593  CB  ASN B 309      20.864  33.758  27.231  1.00175.76           C  
ANISOU 6593  CB  ASN B 309    19573  31757  15453  -5791   2879   2706       C  
ATOM   6594  CG  ASN B 309      22.274  34.031  26.770  1.00203.80           C  
ANISOU 6594  CG  ASN B 309    23000  35461  18973  -6028   3018   2642       C  
ATOM   6595  OD1 ASN B 309      23.129  33.140  26.750  1.00199.58           O  
ANISOU 6595  OD1 ASN B 309    22007  35482  18341  -6161   3005   2404       O  
ATOM   6596  ND2 ASN B 309      22.529  35.251  26.318  1.00199.25           N  
ANISOU 6596  ND2 ASN B 309    22585  35033  18087  -6467   3130   2935       N  
ATOM   6597  N   GLU B 310      18.708  33.602  30.306  1.00167.61           N  
ANISOU 6597  N   GLU B 310    19038  29617  15030  -5243   2562   2692       N  
ATOM   6598  CA  GLU B 310      17.294  33.582  30.707  1.00164.97           C  
ANISOU 6598  CA  GLU B 310    18930  28948  14803  -4937   2468   2776       C  
ATOM   6599  C   GLU B 310      17.069  34.208  32.092  1.00166.32           C  
ANISOU 6599  C   GLU B 310    19369  28673  15153  -4965   2417   2833       C  
ATOM   6600  O   GLU B 310      17.989  34.248  32.911  1.00165.97           O  
ANISOU 6600  O   GLU B 310    19250  28613  15200  -5156   2414   2725       O  
ATOM   6601  CB  GLU B 310      16.726  32.146  30.685  1.00163.97           C  
ANISOU 6601  CB  GLU B 310    18538  28971  14792  -4605   2360   2545       C  
ATOM   6602  CG  GLU B 310      16.573  31.528  29.299  1.00176.28           C  
ANISOU 6602  CG  GLU B 310    19885  30919  16176  -4511   2397   2489       C  
ATOM   6603  CD  GLU B 310      15.496  32.058  28.365  1.00200.51           C  
ANISOU 6603  CD  GLU B 310    23153  33967  19066  -4396   2420   2712       C  
ATOM   6604  OE1 GLU B 310      15.379  31.508  27.246  1.00197.72           O  
ANISOU 6604  OE1 GLU B 310    22608  33962  18557  -4323   2445   2647       O  
ATOM   6605  OE2 GLU B 310      14.768  33.007  28.739  1.00194.84           O  
ANISOU 6605  OE2 GLU B 310    22775  32899  18357  -4368   2412   2945       O  
ATOM   6606  N   THR B 311      15.834  34.687  32.350  1.00160.85           N  
ANISOU 6606  N   THR B 311    18976  27639  14501  -4766   2375   2995       N  
ATOM   6607  CA  THR B 311      15.460  35.300  33.630  1.00159.23           C  
ANISOU 6607  CA  THR B 311    19045  26999  14454  -4757   2330   3048       C  
ATOM   6608  C   THR B 311      15.136  34.216  34.668  1.00158.89           C  
ANISOU 6608  C   THR B 311    18832  26907  14631  -4525   2197   2826       C  
ATOM   6609  O   THR B 311      14.771  33.091  34.307  1.00157.04           O  
ANISOU 6609  O   THR B 311    18355  26883  14430  -4300   2135   2686       O  
ATOM   6610  CB  THR B 311      14.289  36.286  33.477  1.00166.91           C  
ANISOU 6610  CB  THR B 311    20405  27636  15377  -4625   2347   3311       C  
ATOM   6611  OG1 THR B 311      13.135  35.596  33.002  1.00164.13           O  
ANISOU 6611  OG1 THR B 311    19980  27364  15018  -4280   2275   3305       O  
ATOM   6612  CG2 THR B 311      14.624  37.473  32.577  1.00168.65           C  
ANISOU 6612  CG2 THR B 311    20850  27837  15393  -4867   2482   3567       C  
ATOM   6613  N   LEU B 312      15.254  34.572  35.957  1.00153.40           N  
ANISOU 6613  N   LEU B 312    18278  25928  14079  -4589   2158   2798       N  
ATOM   6614  CA  LEU B 312      15.014  33.665  37.077  1.00149.98           C  
ANISOU 6614  CA  LEU B 312    17716  25423  13846  -4404   2037   2615       C  
ATOM   6615  C   LEU B 312      13.516  33.414  37.349  1.00151.04           C  
ANISOU 6615  C   LEU B 312    17987  25337  14064  -4066   1959   2663       C  
ATOM   6616  O   LEU B 312      13.194  32.499  38.111  1.00148.92           O  
ANISOU 6616  O   LEU B 312    17586  25047  13948  -3884   1859   2516       O  
ATOM   6617  CB  LEU B 312      15.695  34.200  38.353  1.00150.17           C  
ANISOU 6617  CB  LEU B 312    17841  25251  13964  -4613   2026   2572       C  
ATOM   6618  CG  LEU B 312      17.222  34.348  38.327  1.00156.44           C  
ANISOU 6618  CG  LEU B 312    18457  26283  14699  -4955   2085   2487       C  
ATOM   6619  CD1 LEU B 312      17.717  35.015  39.589  1.00157.04           C  
ANISOU 6619  CD1 LEU B 312    18678  26139  14849  -5162   2073   2461       C  
ATOM   6620  CD2 LEU B 312      17.917  33.004  38.135  1.00157.61           C  
ANISOU 6620  CD2 LEU B 312    18177  26816  14890  -4875   2032   2269       C  
ATOM   6621  N   SER B 313      12.610  34.188  36.707  1.00147.11           N  
ANISOU 6621  N   SER B 313    17740  24697  13458  -3977   2003   2870       N  
ATOM   6622  CA  SER B 313      11.149  34.102  36.852  1.00144.90           C  
ANISOU 6622  CA  SER B 313    17597  24235  13225  -3662   1941   2940       C  
ATOM   6623  C   SER B 313      10.600  32.659  36.894  1.00146.28           C  
ANISOU 6623  C   SER B 313    17491  24589  13501  -3406   1840   2753       C  
ATOM   6624  O   SER B 313       9.634  32.414  37.614  1.00144.50           O  
ANISOU 6624  O   SER B 313    17336  24180  13387  -3194   1766   2737       O  
ATOM   6625  CB  SER B 313      10.458  34.869  35.732  1.00149.34           C  
ANISOU 6625  CB  SER B 313    18347  24787  13609  -3596   2005   3172       C  
ATOM   6626  OG  SER B 313      10.681  36.263  35.868  1.00158.50           O  
ANISOU 6626  OG  SER B 313    19841  25671  14708  -3780   2092   3370       O  
ATOM   6627  N   CYS B 314      11.221  31.715  36.159  1.00142.50           N  
ANISOU 6627  N   CYS B 314    16700  24458  12987  -3433   1841   2605       N  
ATOM   6628  CA  CYS B 314      10.809  30.309  36.124  1.00140.38           C  
ANISOU 6628  CA  CYS B 314    16165  24355  12818  -3217   1757   2411       C  
ATOM   6629  C   CYS B 314      11.260  29.566  37.399  1.00141.11           C  
ANISOU 6629  C   CYS B 314    16136  24363  13117  -3207   1680   2237       C  
ATOM   6630  O   CYS B 314      10.416  28.980  38.085  1.00139.01           O  
ANISOU 6630  O   CYS B 314    15874  23961  12983  -3006   1598   2183       O  
ATOM   6631  CB  CYS B 314      11.334  29.629  34.862  1.00142.07           C  
ANISOU 6631  CB  CYS B 314    16109  24956  12914  -3249   1798   2308       C  
ATOM   6632  SG  CYS B 314      10.964  27.855  34.743  1.00144.34           S  
ANISOU 6632  SG  CYS B 314    16070  25439  13332  -3012   1710   2037       S  
ATOM   6633  N   VAL B 315      12.580  29.595  37.716  1.00136.94           N  
ANISOU 6633  N   VAL B 315    15493  23931  12606  -3426   1705   2158       N  
ATOM   6634  CA  VAL B 315      13.144  28.902  38.888  1.00134.73           C  
ANISOU 6634  CA  VAL B 315    15076  23614  12499  -3424   1629   2005       C  
ATOM   6635  C   VAL B 315      12.602  29.503  40.197  1.00135.59           C  
ANISOU 6635  C   VAL B 315    15437  23378  12705  -3402   1583   2085       C  
ATOM   6636  O   VAL B 315      12.394  28.752  41.149  1.00133.75           O  
ANISOU 6636  O   VAL B 315    15129  23069  12623  -3274   1495   1986       O  
ATOM   6637  CB  VAL B 315      14.696  28.806  38.900  1.00140.04           C  
ANISOU 6637  CB  VAL B 315    15542  24516  13152  -3655   1662   1900       C  
ATOM   6638  CG1 VAL B 315      15.202  27.909  37.773  1.00140.57           C  
ANISOU 6638  CG1 VAL B 315    15306  24944  13162  -3618   1692   1764       C  
ATOM   6639  CG2 VAL B 315      15.369  30.177  38.851  1.00141.96           C  
ANISOU 6639  CG2 VAL B 315    15972  24701  13266  -3960   1754   2039       C  
ATOM   6640  N   ILE B 316      12.334  30.831  40.224  1.00131.48           N  
ANISOU 6640  N   ILE B 316    15219  22643  12093  -3515   1645   2263       N  
ATOM   6641  CA  ILE B 316      11.780  31.531  41.389  1.00130.07           C  
ANISOU 6641  CA  ILE B 316    15307  22128  11987  -3496   1618   2336       C  
ATOM   6642  C   ILE B 316      10.417  30.914  41.734  1.00130.80           C  
ANISOU 6642  C   ILE B 316    15423  22103  12172  -3188   1541   2326       C  
ATOM   6643  O   ILE B 316      10.225  30.478  42.870  1.00128.86           O  
ANISOU 6643  O   ILE B 316    15161  21744  12056  -3111   1467   2249       O  
ATOM   6644  CB  ILE B 316      11.706  33.075  41.154  1.00135.09           C  
ANISOU 6644  CB  ILE B 316    16278  22548  12503  -3658   1715   2530       C  
ATOM   6645  CG1 ILE B 316      13.115  33.742  41.162  1.00137.63           C  
ANISOU 6645  CG1 ILE B 316    16597  22940  12757  -4016   1788   2523       C  
ATOM   6646  CG2 ILE B 316      10.736  33.787  42.117  1.00135.15           C  
ANISOU 6646  CG2 ILE B 316    16589  22189  12573  -3546   1695   2615       C  
ATOM   6647  CD1 ILE B 316      14.008  33.605  42.470  1.00145.50           C  
ANISOU 6647  CD1 ILE B 316    17514  23915  13856  -4177   1738   2381       C  
ATOM   6648  N   ILE B 317       9.511  30.818  40.734  1.00126.54           N  
ANISOU 6648  N   ILE B 317    14896  21628  11555  -3021   1557   2399       N  
ATOM   6649  CA  ILE B 317       8.172  30.243  40.879  1.00124.19           C  
ANISOU 6649  CA  ILE B 317    14598  21268  11320  -2742   1493   2391       C  
ATOM   6650  C   ILE B 317       8.287  28.742  41.231  1.00125.11           C  
ANISOU 6650  C   ILE B 317    14429  21530  11577  -2640   1410   2193       C  
ATOM   6651  O   ILE B 317       7.520  28.276  42.079  1.00123.03           O  
ANISOU 6651  O   ILE B 317    14182  21135  11427  -2487   1343   2157       O  
ATOM   6652  CB  ILE B 317       7.305  30.539  39.612  1.00127.95           C  
ANISOU 6652  CB  ILE B 317    15130  21835  11649  -2617   1532   2514       C  
ATOM   6653  CG1 ILE B 317       6.428  31.794  39.828  1.00128.93           C  
ANISOU 6653  CG1 ILE B 317    15589  21684  11716  -2544   1565   2715       C  
ATOM   6654  CG2 ILE B 317       6.437  29.352  39.166  1.00127.39           C  
ANISOU 6654  CG2 ILE B 317    14851  21937  11613  -2394   1470   2408       C  
ATOM   6655  CD1 ILE B 317       7.141  33.166  39.694  1.00136.41           C  
ANISOU 6655  CD1 ILE B 317    16784  22479  12564  -2770   1660   2869       C  
ATOM   6656  N   PHE B 318       9.276  28.020  40.639  1.00120.93           N  
ANISOU 6656  N   PHE B 318    13648  21257  11043  -2729   1420   2068       N  
ATOM   6657  CA  PHE B 318       9.517  26.601  40.919  1.00119.11           C  
ANISOU 6657  CA  PHE B 318    13153  21149  10952  -2632   1350   1879       C  
ATOM   6658  C   PHE B 318       9.827  26.378  42.392  1.00121.21           C  
ANISOU 6658  C   PHE B 318    13433  21254  11365  -2646   1283   1835       C  
ATOM   6659  O   PHE B 318       9.205  25.513  43.008  1.00119.50           O  
ANISOU 6659  O   PHE B 318    13160  20966  11276  -2484   1212   1770       O  
ATOM   6660  CB  PHE B 318      10.654  26.026  40.058  1.00122.04           C  
ANISOU 6660  CB  PHE B 318    13268  21818  11284  -2731   1385   1754       C  
ATOM   6661  CG  PHE B 318      11.248  24.740  40.599  1.00122.99           C  
ANISOU 6661  CG  PHE B 318    13143  22021  11567  -2665   1318   1568       C  
ATOM   6662  CD1 PHE B 318      10.554  23.537  40.502  1.00124.97           C  
ANISOU 6662  CD1 PHE B 318    13267  22287  11928  -2462   1265   1452       C  
ATOM   6663  CD2 PHE B 318      12.489  24.738  41.225  1.00126.04           C  
ANISOU 6663  CD2 PHE B 318    13429  22463  11996  -2804   1308   1514       C  
ATOM   6664  CE1 PHE B 318      11.096  22.356  41.017  1.00125.65           C  
ANISOU 6664  CE1 PHE B 318    13152  22414  12175  -2388   1206   1297       C  
ATOM   6665  CE2 PHE B 318      13.028  23.557  41.741  1.00128.52           C  
ANISOU 6665  CE2 PHE B 318    13522  22849  12460  -2713   1242   1361       C  
ATOM   6666  CZ  PHE B 318      12.323  22.377  41.641  1.00125.58           C  
ANISOU 6666  CZ  PHE B 318    13050  22458  12207  -2499   1192   1260       C  
ATOM   6667  N   VAL B 319      10.807  27.130  42.940  1.00117.71           N  
ANISOU 6667  N   VAL B 319    13056  20773  10894  -2852   1307   1866       N  
ATOM   6668  CA  VAL B 319      11.227  27.022  44.342  1.00116.30           C  
ANISOU 6668  CA  VAL B 319    12885  20479  10824  -2895   1243   1825       C  
ATOM   6669  C   VAL B 319      10.014  27.309  45.257  1.00116.64           C  
ANISOU 6669  C   VAL B 319    13145  20253  10920  -2760   1205   1902       C  
ATOM   6670  O   VAL B 319       9.723  26.494  46.132  1.00114.50           O  
ANISOU 6670  O   VAL B 319    12802  19932  10772  -2640   1127   1841       O  
ATOM   6671  CB  VAL B 319      12.459  27.918  44.667  1.00121.78           C  
ANISOU 6671  CB  VAL B 319    13620  21202  11448  -3172   1285   1842       C  
ATOM   6672  CG1 VAL B 319      12.775  27.922  46.164  1.00121.18           C  
ANISOU 6672  CG1 VAL B 319    13574  21009  11458  -3217   1215   1809       C  
ATOM   6673  CG2 VAL B 319      13.684  27.477  43.869  1.00122.74           C  
ANISOU 6673  CG2 VAL B 319    13478  21632  11527  -3290   1316   1745       C  
ATOM   6674  N   ILE B 320       9.267  28.406  44.988  1.00112.46           N  
ANISOU 6674  N   ILE B 320    12871  19562  10295  -2761   1262   2039       N  
ATOM   6675  CA  ILE B 320       8.075  28.814  45.742  1.00110.91           C  
ANISOU 6675  CA  ILE B 320    12888  19125  10128  -2622   1241   2114       C  
ATOM   6676  C   ILE B 320       7.039  27.665  45.796  1.00113.74           C  
ANISOU 6676  C   ILE B 320    13119  19517  10579  -2381   1176   2058       C  
ATOM   6677  O   ILE B 320       6.537  27.359  46.878  1.00111.99           O  
ANISOU 6677  O   ILE B 320    12931  19174  10446  -2295   1121   2039       O  
ATOM   6678  CB  ILE B 320       7.468  30.124  45.155  1.00114.72           C  
ANISOU 6678  CB  ILE B 320    13642  19462  10486  -2630   1322   2274       C  
ATOM   6679  CG1 ILE B 320       8.374  31.335  45.472  1.00116.79           C  
ANISOU 6679  CG1 ILE B 320    14091  19600  10684  -2885   1386   2329       C  
ATOM   6680  CG2 ILE B 320       6.044  30.372  45.673  1.00114.05           C  
ANISOU 6680  CG2 ILE B 320    13729  19181  10424  -2417   1303   2342       C  
ATOM   6681  CD1 ILE B 320       8.142  32.579  44.615  1.00126.68           C  
ANISOU 6681  CD1 ILE B 320    15586  20741  11803  -2943   1483   2493       C  
ATOM   6682  N   VAL B 321       6.759  27.017  44.649  1.00111.03           N  
ANISOU 6682  N   VAL B 321    12625  19352  10209  -2291   1185   2023       N  
ATOM   6683  CA  VAL B 321       5.768  25.940  44.553  1.00109.87           C  
ANISOU 6683  CA  VAL B 321    12357  19249  10140  -2091   1134   1958       C  
ATOM   6684  C   VAL B 321       6.311  24.617  45.143  1.00111.94           C  
ANISOU 6684  C   VAL B 321    12403  19575  10556  -2072   1066   1813       C  
ATOM   6685  O   VAL B 321       5.693  24.092  46.069  1.00110.03           O  
ANISOU 6685  O   VAL B 321    12171  19221  10416  -1972   1010   1799       O  
ATOM   6686  CB  VAL B 321       5.246  25.765  43.093  1.00114.73           C  
ANISOU 6686  CB  VAL B 321    12895  20042  10655  -2014   1170   1961       C  
ATOM   6687  CG1 VAL B 321       4.461  24.464  42.915  1.00113.65           C  
ANISOU 6687  CG1 VAL B 321    12582  19993  10608  -1854   1118   1845       C  
ATOM   6688  CG2 VAL B 321       4.392  26.958  42.675  1.00115.35           C  
ANISOU 6688  CG2 VAL B 321    13199  20031  10597  -1962   1218   2128       C  
ATOM   6689  N   TYR B 322       7.437  24.089  44.611  1.00108.72           N  
ANISOU 6689  N   TYR B 322    11803  19346  10160  -2157   1073   1715       N  
ATOM   6690  CA  TYR B 322       8.012  22.806  45.024  1.00107.91           C  
ANISOU 6690  CA  TYR B 322    11488  19310  10204  -2112   1013   1580       C  
ATOM   6691  C   TYR B 322       8.463  22.781  46.493  1.00112.40           C  
ANISOU 6691  C   TYR B 322    12092  19753  10861  -2150    952   1595       C  
ATOM   6692  O   TYR B 322       8.151  21.802  47.176  1.00111.50           O  
ANISOU 6692  O   TYR B 322    11906  19580  10879  -2036    888   1550       O  
ATOM   6693  CB  TYR B 322       9.174  22.393  44.108  1.00109.60           C  
ANISOU 6693  CB  TYR B 322    11492  19758  10394  -2188   1044   1471       C  
ATOM   6694  CG  TYR B 322       9.761  21.035  44.431  1.00110.71           C  
ANISOU 6694  CG  TYR B 322    11411  19964  10692  -2107    986   1327       C  
ATOM   6695  CD1 TYR B 322       9.239  19.874  43.868  1.00112.30           C  
ANISOU 6695  CD1 TYR B 322    11481  20209  10978  -1961    972   1211       C  
ATOM   6696  CD2 TYR B 322      10.853  20.912  45.283  1.00111.90           C  
ANISOU 6696  CD2 TYR B 322    11482  20133  10902  -2174    946   1305       C  
ATOM   6697  CE1 TYR B 322       9.783  18.622  44.156  1.00113.34           C  
ANISOU 6697  CE1 TYR B 322    11431  20366  11268  -1873    925   1083       C  
ATOM   6698  CE2 TYR B 322      11.391  19.666  45.595  1.00113.07           C  
ANISOU 6698  CE2 TYR B 322    11434  20331  11198  -2070    889   1191       C  
ATOM   6699  CZ  TYR B 322      10.856  18.523  45.028  1.00121.03           C  
ANISOU 6699  CZ  TYR B 322    12335  21347  12304  -1914    882   1082       C  
ATOM   6700  OH  TYR B 322      11.414  17.305  45.331  1.00123.65           O  
ANISOU 6700  OH  TYR B 322    12493  21697  12792  -1802    832    973       O  
ATOM   6701  N   TYR B 323       9.220  23.803  46.968  1.00109.86           N  
ANISOU 6701  N   TYR B 323    11874  19401  10467  -2319    973   1656       N  
ATOM   6702  CA  TYR B 323       9.692  23.829  48.360  1.00109.56           C  
ANISOU 6702  CA  TYR B 323    11861  19279  10488  -2371    913   1662       C  
ATOM   6703  C   TYR B 323       8.501  23.772  49.310  1.00114.23           C  
ANISOU 6703  C   TYR B 323    12598  19673  11131  -2247    874   1721       C  
ATOM   6704  O   TYR B 323       8.492  22.920  50.196  1.00113.77           O  
ANISOU 6704  O   TYR B 323    12461  19588  11180  -2171    802   1692       O  
ATOM   6705  CB  TYR B 323      10.585  25.053  48.662  1.00111.27           C  
ANISOU 6705  CB  TYR B 323    12187  19493  10599  -2597    951   1706       C  
ATOM   6706  CG  TYR B 323      11.132  25.092  50.074  1.00112.01           C  
ANISOU 6706  CG  TYR B 323    12287  19541  10731  -2668    886   1697       C  
ATOM   6707  CD1 TYR B 323      12.324  24.454  50.399  1.00114.48           C  
ANISOU 6707  CD1 TYR B 323    12379  20031  11088  -2720    834   1618       C  
ATOM   6708  CD2 TYR B 323      10.473  25.795  51.080  1.00111.99           C  
ANISOU 6708  CD2 TYR B 323    12505  19340  10707  -2678    877   1764       C  
ATOM   6709  CE1 TYR B 323      12.826  24.478  51.700  1.00115.21           C  
ANISOU 6709  CE1 TYR B 323    12463  20113  11197  -2780    765   1615       C  
ATOM   6710  CE2 TYR B 323      10.962  25.822  52.384  1.00112.81           C  
ANISOU 6710  CE2 TYR B 323    12609  19428  10827  -2747    815   1748       C  
ATOM   6711  CZ  TYR B 323      12.141  25.167  52.688  1.00119.70           C  
ANISOU 6711  CZ  TYR B 323    13255  20490  11736  -2802    756   1679       C  
ATOM   6712  OH  TYR B 323      12.628  25.211  53.969  1.00119.75           O  
ANISOU 6712  OH  TYR B 323    13251  20510  11738  -2870    688   1669       O  
ATOM   6713  N   ALA B 324       7.483  24.636  49.087  1.00111.70           N  
ANISOU 6713  N   ALA B 324    12482  19227  10731  -2215    922   1808       N  
ATOM   6714  CA  ALA B 324       6.265  24.696  49.902  1.00111.26           C  
ANISOU 6714  CA  ALA B 324    12565  19006  10703  -2092    899   1862       C  
ATOM   6715  C   ALA B 324       5.475  23.384  49.842  1.00115.40           C  
ANISOU 6715  C   ALA B 324    12949  19560  11337  -1922    854   1812       C  
ATOM   6716  O   ALA B 324       4.896  22.984  50.852  1.00114.56           O  
ANISOU 6716  O   ALA B 324    12872  19361  11296  -1850    809   1827       O  
ATOM   6717  CB  ALA B 324       5.389  25.853  49.456  1.00112.36           C  
ANISOU 6717  CB  ALA B 324    12923  19038  10732  -2067    967   1959       C  
ATOM   6718  N   LEU B 325       5.477  22.710  48.671  1.00112.68           N  
ANISOU 6718  N   LEU B 325    12455  19350  11007  -1873    869   1746       N  
ATOM   6719  CA  LEU B 325       4.793  21.434  48.448  1.00112.08           C  
ANISOU 6719  CA  LEU B 325    12243  19306  11037  -1738    836   1673       C  
ATOM   6720  C   LEU B 325       5.415  20.327  49.314  1.00115.82           C  
ANISOU 6720  C   LEU B 325    12586  19763  11658  -1720    767   1613       C  
ATOM   6721  O   LEU B 325       4.700  19.689  50.090  1.00114.94           O  
ANISOU 6721  O   LEU B 325    12486  19553  11632  -1638    726   1628       O  
ATOM   6722  CB  LEU B 325       4.853  21.054  46.952  1.00112.79           C  
ANISOU 6722  CB  LEU B 325    12201  19563  11092  -1718    875   1592       C  
ATOM   6723  CG  LEU B 325       4.118  19.787  46.521  1.00117.42           C  
ANISOU 6723  CG  LEU B 325    12651  20190  11774  -1600    854   1491       C  
ATOM   6724  CD1 LEU B 325       2.649  20.064  46.254  1.00117.30           C  
ANISOU 6724  CD1 LEU B 325    12724  20153  11694  -1513    871   1542       C  
ATOM   6725  CD2 LEU B 325       4.759  19.188  45.290  1.00121.03           C  
ANISOU 6725  CD2 LEU B 325    12929  20828  12227  -1613    881   1362       C  
ATOM   6726  N   MET B 326       6.744  20.137  49.201  1.00113.04           N  
ANISOU 6726  N   MET B 326    12110  19512  11326  -1796    756   1558       N  
ATOM   6727  CA  MET B 326       7.495  19.114  49.927  1.00113.16           C  
ANISOU 6727  CA  MET B 326    11986  19535  11473  -1762    688   1509       C  
ATOM   6728  C   MET B 326       7.588  19.406  51.424  1.00116.57           C  
ANISOU 6728  C   MET B 326    12516  19863  11914  -1794    633   1596       C  
ATOM   6729  O   MET B 326       7.620  18.458  52.211  1.00116.13           O  
ANISOU 6729  O   MET B 326    12393  19759  11971  -1715    569   1598       O  
ATOM   6730  CB  MET B 326       8.890  18.917  49.322  1.00116.80           C  
ANISOU 6730  CB  MET B 326    12272  20172  11934  -1822    695   1422       C  
ATOM   6731  CG  MET B 326       8.856  18.248  47.955  1.00121.13           C  
ANISOU 6731  CG  MET B 326    12680  20838  12505  -1761    738   1303       C  
ATOM   6732  SD  MET B 326       7.892  16.707  47.921  1.00125.09           S  
ANISOU 6732  SD  MET B 326    13113  21236  13181  -1582    705   1224       S  
ATOM   6733  CE  MET B 326       7.436  16.653  46.219  1.00122.13           C  
ANISOU 6733  CE  MET B 326    12672  21004  12729  -1572    780   1115       C  
ATOM   6734  N   ALA B 327       7.597  20.698  51.822  1.00113.11           N  
ANISOU 6734  N   ALA B 327    12242  19382  11351  -1906    660   1668       N  
ATOM   6735  CA  ALA B 327       7.613  21.089  53.235  1.00112.93           C  
ANISOU 6735  CA  ALA B 327    12326  19272  11311  -1949    616   1736       C  
ATOM   6736  C   ALA B 327       6.256  20.768  53.887  1.00117.08           C  
ANISOU 6736  C   ALA B 327    12950  19659  11875  -1833    602   1790       C  
ATOM   6737  O   ALA B 327       6.208  20.398  55.062  1.00116.85           O  
ANISOU 6737  O   ALA B 327    12931  19583  11884  -1811    545   1830       O  
ATOM   6738  CB  ALA B 327       7.943  22.566  53.381  1.00114.10           C  
ANISOU 6738  CB  ALA B 327    12637  19396  11320  -2108    662   1774       C  
ATOM   6739  N   GLY B 328       5.183  20.870  53.093  1.00113.01           N  
ANISOU 6739  N   GLY B 328    12490  19109  11341  -1759    652   1792       N  
ATOM   6740  CA  GLY B 328       3.818  20.565  53.505  1.00111.75           C  
ANISOU 6740  CA  GLY B 328    12398  18857  11207  -1652    651   1831       C  
ATOM   6741  C   GLY B 328       3.606  19.088  53.774  1.00114.94           C  
ANISOU 6741  C   GLY B 328    12664  19251  11755  -1565    600   1801       C  
ATOM   6742  O   GLY B 328       2.835  18.733  54.671  1.00114.52           O  
ANISOU 6742  O   GLY B 328    12657  19120  11734  -1517    577   1852       O  
ATOM   6743  N   PHE B 329       4.302  18.214  53.010  1.00111.15           N  
ANISOU 6743  N   PHE B 329    12021  18847  11365  -1546    588   1717       N  
ATOM   6744  CA  PHE B 329       4.215  16.759  53.160  1.00110.87           C  
ANISOU 6744  CA  PHE B 329    11864  18776  11487  -1462    546   1677       C  
ATOM   6745  C   PHE B 329       4.969  16.263  54.388  1.00114.68           C  
ANISOU 6745  C   PHE B 329    12315  19221  12038  -1460    472   1732       C  
ATOM   6746  O   PHE B 329       4.507  15.318  55.032  1.00114.93           O  
ANISOU 6746  O   PHE B 329    12335  19162  12172  -1394    437   1768       O  
ATOM   6747  CB  PHE B 329       4.733  16.035  51.913  1.00113.26           C  
ANISOU 6747  CB  PHE B 329    12009  19166  11859  -1431    564   1551       C  
ATOM   6748  CG  PHE B 329       3.852  16.152  50.694  1.00114.91           C  
ANISOU 6748  CG  PHE B 329    12217  19427  12017  -1412    625   1487       C  
ATOM   6749  CD1 PHE B 329       2.510  15.790  50.746  1.00117.88           C  
ANISOU 6749  CD1 PHE B 329    12635  19740  12415  -1361    635   1496       C  
ATOM   6750  CD2 PHE B 329       4.376  16.567  49.476  1.00117.95           C  
ANISOU 6750  CD2 PHE B 329    12540  19951  12325  -1449    671   1414       C  
ATOM   6751  CE1 PHE B 329       1.698  15.897  49.614  1.00119.11           C  
ANISOU 6751  CE1 PHE B 329    12769  19980  12508  -1342    683   1434       C  
ATOM   6752  CE2 PHE B 329       3.562  16.673  48.345  1.00120.86           C  
ANISOU 6752  CE2 PHE B 329    12898  20396  12627  -1427    720   1362       C  
ATOM   6753  CZ  PHE B 329       2.231  16.329  48.419  1.00118.58           C  
ANISOU 6753  CZ  PHE B 329    12646  20052  12356  -1369    722   1370       C  
ATOM   6754  N   VAL B 330       6.133  16.870  54.703  1.00110.37           N  
ANISOU 6754  N   VAL B 330    11750  18755  11430  -1537    449   1743       N  
ATOM   6755  CA  VAL B 330       6.922  16.472  55.874  1.00110.24           C  
ANISOU 6755  CA  VAL B 330    11688  18746  11452  -1534    370   1800       C  
ATOM   6756  C   VAL B 330       6.268  17.018  57.157  1.00112.38           C  
ANISOU 6756  C   VAL B 330    12111  18943  11645  -1568    351   1906       C  
ATOM   6757  O   VAL B 330       6.365  16.364  58.198  1.00112.05           O  
ANISOU 6757  O   VAL B 330    12050  18872  11653  -1527    287   1977       O  
ATOM   6758  CB  VAL B 330       8.434  16.807  55.797  1.00114.92           C  
ANISOU 6758  CB  VAL B 330    12170  19491  12005  -1606    344   1761       C  
ATOM   6759  CG1 VAL B 330       9.161  15.831  54.877  1.00115.39           C  
ANISOU 6759  CG1 VAL B 330    12037  19626  12180  -1523    340   1662       C  
ATOM   6760  CG2 VAL B 330       8.681  18.247  55.370  1.00114.70           C  
ANISOU 6760  CG2 VAL B 330    12231  19527  11821  -1756    403   1744       C  
ATOM   6761  N   TRP B 331       5.563  18.176  57.071  1.00107.62           N  
ANISOU 6761  N   TRP B 331    11662  18309  10919  -1631    410   1919       N  
ATOM   6762  CA  TRP B 331       4.826  18.745  58.206  1.00106.84           C  
ANISOU 6762  CA  TRP B 331    11713  18143  10739  -1651    408   1997       C  
ATOM   6763  C   TRP B 331       3.607  17.874  58.499  1.00108.54           C  
ANISOU 6763  C   TRP B 331    11938  18274  11029  -1551    408   2039       C  
ATOM   6764  O   TRP B 331       3.175  17.807  59.650  1.00108.60           O  
ANISOU 6764  O   TRP B 331    12008  18248  11009  -1548    382   2114       O  
ATOM   6765  CB  TRP B 331       4.415  20.209  57.967  1.00105.60           C  
ANISOU 6765  CB  TRP B 331    11723  17957  10443  -1722    478   1990       C  
ATOM   6766  CG  TRP B 331       5.407  21.220  58.478  1.00107.48           C  
ANISOU 6766  CG  TRP B 331    12023  18238  10577  -1861    469   1982       C  
ATOM   6767  CD1 TRP B 331       6.171  22.066  57.728  1.00110.95           C  
ANISOU 6767  CD1 TRP B 331    12479  18722  10954  -1970    509   1936       C  
ATOM   6768  CD2 TRP B 331       5.743  21.485  59.852  1.00107.84           C  
ANISOU 6768  CD2 TRP B 331    12118  18298  10560  -1926    420   2017       C  
ATOM   6769  NE1 TRP B 331       6.959  22.844  58.546  1.00111.39           N  
ANISOU 6769  NE1 TRP B 331    12594  18809  10920  -2110    490   1931       N  
ATOM   6770  CE2 TRP B 331       6.734  22.493  59.854  1.00112.83           C  
ANISOU 6770  CE2 TRP B 331    12790  18983  11097  -2083    432   1974       C  
ATOM   6771  CE3 TRP B 331       5.321  20.952  61.082  1.00108.93           C  
ANISOU 6771  CE3 TRP B 331    12263  18423  10701  -1879    369   2080       C  
ATOM   6772  CZ2 TRP B 331       7.291  22.997  61.040  1.00112.91           C  
ANISOU 6772  CZ2 TRP B 331    12847  19038  11016  -2194    391   1975       C  
ATOM   6773  CZ3 TRP B 331       5.879  21.446  62.254  1.00111.13           C  
ANISOU 6773  CZ3 TRP B 331    12587  18757  10881  -1976    326   2093       C  
ATOM   6774  CH2 TRP B 331       6.847  22.459  62.226  1.00112.62           C  
ANISOU 6774  CH2 TRP B 331    12812  19003  10976  -2132    336   2032       C  
ATOM   6775  N   PHE B 332       3.079  17.180  57.461  1.00103.23           N  
ANISOU 6775  N   PHE B 332    11193  17583  10445  -1483    438   1986       N  
ATOM   6776  CA  PHE B 332       1.968  16.230  57.579  1.00102.19           C  
ANISOU 6776  CA  PHE B 332    11047  17381  10400  -1412    443   2006       C  
ATOM   6777  C   PHE B 332       2.449  15.005  58.355  1.00104.80           C  
ANISOU 6777  C   PHE B 332    11300  17663  10855  -1377    375   2057       C  
ATOM   6778  O   PHE B 332       1.711  14.482  59.188  1.00104.49           O  
ANISOU 6778  O   PHE B 332    11299  17560  10843  -1359    362   2135       O  
ATOM   6779  CB  PHE B 332       1.416  15.832  56.188  1.00103.65           C  
ANISOU 6779  CB  PHE B 332    11164  17581  10638  -1371    492   1910       C  
ATOM   6780  CG  PHE B 332       0.770  14.462  56.090  1.00105.29           C  
ANISOU 6780  CG  PHE B 332    11296  17721  10988  -1320    485   1889       C  
ATOM   6781  CD1 PHE B 332      -0.519  14.244  56.567  1.00107.98           C  
ANISOU 6781  CD1 PHE B 332    11688  18018  11320  -1312    506   1936       C  
ATOM   6782  CD2 PHE B 332       1.448  13.393  55.515  1.00107.86           C  
ANISOU 6782  CD2 PHE B 332    11500  18024  11456  -1286    464   1813       C  
ATOM   6783  CE1 PHE B 332      -1.117  12.980  56.473  1.00109.15           C  
ANISOU 6783  CE1 PHE B 332    11775  18096  11601  -1296    507   1912       C  
ATOM   6784  CE2 PHE B 332       0.851  12.127  55.430  1.00111.06           C  
ANISOU 6784  CE2 PHE B 332    11859  18335  12004  -1252    465   1784       C  
ATOM   6785  CZ  PHE B 332      -0.429  11.931  55.906  1.00108.83           C  
ANISOU 6785  CZ  PHE B 332    11636  18004  11712  -1271    487   1836       C  
ATOM   6786  N   VAL B 333       3.689  14.555  58.078  1.00100.22           N  
ANISOU 6786  N   VAL B 333    10608  17122  10348  -1362    332   2020       N  
ATOM   6787  CA  VAL B 333       4.302  13.408  58.747  1.00100.31           C  
ANISOU 6787  CA  VAL B 333    10541  17090  10482  -1300    261   2076       C  
ATOM   6788  C   VAL B 333       4.522  13.769  60.231  1.00104.17           C  
ANISOU 6788  C   VAL B 333    11095  17604  10879  -1335    205   2204       C  
ATOM   6789  O   VAL B 333       4.288  12.928  61.099  1.00104.15           O  
ANISOU 6789  O   VAL B 333    11100  17533  10939  -1291    162   2306       O  
ATOM   6790  CB  VAL B 333       5.594  12.944  58.024  1.00104.56           C  
ANISOU 6790  CB  VAL B 333    10930  17692  11106  -1254    234   1992       C  
ATOM   6791  CG1 VAL B 333       6.351  11.898  58.837  1.00105.62           C  
ANISOU 6791  CG1 VAL B 333    10988  17792  11352  -1166    151   2070       C  
ATOM   6792  CG2 VAL B 333       5.268  12.393  56.641  1.00104.14           C  
ANISOU 6792  CG2 VAL B 333    10809  17610  11148  -1212    291   1859       C  
ATOM   6793  N   VAL B 334       4.891  15.039  60.515  1.00100.46           N  
ANISOU 6793  N   VAL B 334    10688  17228  10253  -1426    211   2197       N  
ATOM   6794  CA  VAL B 334       5.079  15.567  61.875  1.00100.48           C  
ANISOU 6794  CA  VAL B 334    10760  17280  10137  -1483    165   2287       C  
ATOM   6795  C   VAL B 334       3.715  15.511  62.603  1.00104.18           C  
ANISOU 6795  C   VAL B 334    11345  17670  10569  -1474    195   2363       C  
ATOM   6796  O   VAL B 334       3.673  15.161  63.785  1.00104.18           O  
ANISOU 6796  O   VAL B 334    11364  17680  10539  -1471    146   2469       O  
ATOM   6797  CB  VAL B 334       5.717  16.990  61.856  1.00103.99           C  
ANISOU 6797  CB  VAL B 334    11260  17823  10429  -1604    183   2229       C  
ATOM   6798  CG1 VAL B 334       5.605  17.695  63.207  1.00104.05           C  
ANISOU 6798  CG1 VAL B 334    11374  17868  10292  -1678    159   2290       C  
ATOM   6799  CG2 VAL B 334       7.175  16.922  61.420  1.00104.56           C  
ANISOU 6799  CG2 VAL B 334    11190  18014  10525  -1630    141   2174       C  
ATOM   6800  N   LEU B 335       2.611  15.780  61.866  1.00100.16           N  
ANISOU 6800  N   LEU B 335    10893  17103  10059  -1463    274   2311       N  
ATOM   6801  CA  LEU B 335       1.238  15.712  62.370  1.00 99.78           C  
ANISOU 6801  CA  LEU B 335    10927  17006   9977  -1449    314   2363       C  
ATOM   6802  C   LEU B 335       0.873  14.259  62.706  1.00103.86           C  
ANISOU 6802  C   LEU B 335    11384  17447  10630  -1400    286   2440       C  
ATOM   6803  O   LEU B 335       0.322  14.016  63.782  1.00103.49           O  
ANISOU 6803  O   LEU B 335    11386  17394  10542  -1412    275   2542       O  
ATOM   6804  CB  LEU B 335       0.256  16.294  61.339  1.00 99.04           C  
ANISOU 6804  CB  LEU B 335    10876  16899   9855  -1433    398   2282       C  
ATOM   6805  CG  LEU B 335      -1.141  16.635  61.840  1.00103.66           C  
ANISOU 6805  CG  LEU B 335    11548  17481  10359  -1421    451   2316       C  
ATOM   6806  CD1 LEU B 335      -1.592  17.956  61.293  1.00103.68           C  
ANISOU 6806  CD1 LEU B 335    11644  17506  10244  -1413    515   2256       C  
ATOM   6807  CD2 LEU B 335      -2.138  15.563  61.463  1.00105.47           C  
ANISOU 6807  CD2 LEU B 335    11709  17673  10691  -1385    474   2319       C  
ATOM   6808  N   THR B 336       1.199  13.300  61.800  1.00100.64           N  
ANISOU 6808  N   THR B 336    10877  16979  10382  -1349    278   2388       N  
ATOM   6809  CA  THR B 336       0.925  11.870  62.002  1.00101.31           C  
ANISOU 6809  CA  THR B 336    10919  16951  10622  -1305    257   2449       C  
ATOM   6810  C   THR B 336       1.744  11.341  63.186  1.00106.52           C  
ANISOU 6810  C   THR B 336    11568  17607  11297  -1280    172   2587       C  
ATOM   6811  O   THR B 336       1.236  10.517  63.944  1.00106.81           O  
ANISOU 6811  O   THR B 336    11635  17565  11382  -1273    159   2705       O  
ATOM   6812  CB  THR B 336       1.160  11.031  60.725  1.00110.49           C  
ANISOU 6812  CB  THR B 336    11986  18043  11950  -1254    274   2333       C  
ATOM   6813  OG1 THR B 336       2.545  10.995  60.387  1.00110.75           O  
ANISOU 6813  OG1 THR B 336    11934  18121  12025  -1210    226   2290       O  
ATOM   6814  CG2 THR B 336       0.334  11.504  59.537  1.00108.86           C  
ANISOU 6814  CG2 THR B 336    11777  17872  11713  -1278    351   2203       C  
ATOM   6815  N   TYR B 337       2.990  11.837  63.358  1.00103.80           N  
ANISOU 6815  N   TYR B 337    11179  17363  10898  -1274    115   2579       N  
ATOM   6816  CA  TYR B 337       3.873  11.460  64.466  1.00104.78           C  
ANISOU 6816  CA  TYR B 337    11272  17534  11005  -1244     23   2707       C  
ATOM   6817  C   TYR B 337       3.354  12.047  65.790  1.00109.47           C  
ANISOU 6817  C   TYR B 337    11966  18199  11429  -1314     13   2816       C  
ATOM   6818  O   TYR B 337       3.447  11.379  66.823  1.00110.17           O  
ANISOU 6818  O   TYR B 337    12058  18284  11516  -1287    -44   2967       O  
ATOM   6819  CB  TYR B 337       5.330  11.903  64.203  1.00105.83           C  
ANISOU 6819  CB  TYR B 337    11304  17798  11109  -1234    -32   2645       C  
ATOM   6820  CG  TYR B 337       6.283  11.572  65.335  1.00108.45           C  
ANISOU 6820  CG  TYR B 337    11581  18223  11403  -1196   -137   2773       C  
ATOM   6821  CD1 TYR B 337       6.764  10.278  65.514  1.00111.82           C  
ANISOU 6821  CD1 TYR B 337    11932  18576  11981  -1064   -199   2867       C  
ATOM   6822  CD2 TYR B 337       6.696  12.551  66.234  1.00109.13           C  
ANISOU 6822  CD2 TYR B 337    11694  18474  11297  -1287   -174   2800       C  
ATOM   6823  CE1 TYR B 337       7.624   9.964  66.566  1.00114.01           C  
ANISOU 6823  CE1 TYR B 337    12151  18956  12210  -1009   -304   3004       C  
ATOM   6824  CE2 TYR B 337       7.558  12.248  67.288  1.00111.33           C  
ANISOU 6824  CE2 TYR B 337    11907  18875  11519  -1254   -279   2919       C  
ATOM   6825  CZ  TYR B 337       8.027  10.954  67.443  1.00118.93           C  
ANISOU 6825  CZ  TYR B 337    12784  19779  12626  -1107   -346   3029       C  
ATOM   6826  OH  TYR B 337       8.878  10.639  68.475  1.00119.35           O  
ANISOU 6826  OH  TYR B 337    12764  19970  12615  -1054   -457   3163       O  
ATOM   6827  N   ALA B 338       2.819  13.291  65.754  1.00105.80           N  
ANISOU 6827  N   ALA B 338    11585  17799  10816  -1396     71   2742       N  
ATOM   6828  CA  ALA B 338       2.257  13.978  66.922  1.00106.23           C  
ANISOU 6828  CA  ALA B 338    11739  17927  10696  -1461     80   2807       C  
ATOM   6829  C   ALA B 338       1.043  13.232  67.457  1.00110.92           C  
ANISOU 6829  C   ALA B 338    12378  18450  11317  -1450    113   2910       C  
ATOM   6830  O   ALA B 338       0.928  13.046  68.670  1.00111.12           O  
ANISOU 6830  O   ALA B 338    12436  18531  11255  -1471     79   3036       O  
ATOM   6831  CB  ALA B 338       1.866  15.396  66.560  1.00106.01           C  
ANISOU 6831  CB  ALA B 338    11800  17940  10540  -1525    150   2686       C  
ATOM   6832  N   TRP B 339       0.155  12.788  66.542  1.00107.29           N  
ANISOU 6832  N   TRP B 339    11911  17885  10970  -1429    179   2855       N  
ATOM   6833  CA  TRP B 339      -1.056  12.015  66.828  1.00107.71           C  
ANISOU 6833  CA  TRP B 339    11988  17868  11066  -1440    224   2929       C  
ATOM   6834  C   TRP B 339      -0.678  10.636  67.398  1.00114.96           C  
ANISOU 6834  C   TRP B 339    12876  18694  12110  -1407    163   3081       C  
ATOM   6835  O   TRP B 339      -1.386  10.118  68.260  1.00115.45           O  
ANISOU 6835  O   TRP B 339    12980  18741  12145  -1443    174   3210       O  
ATOM   6836  CB  TRP B 339      -1.913  11.905  65.544  1.00105.18           C  
ANISOU 6836  CB  TRP B 339    11643  17483  10837  -1433    301   2805       C  
ATOM   6837  CG  TRP B 339      -2.577  10.580  65.299  1.00106.42           C  
ANISOU 6837  CG  TRP B 339    11768  17515  11152  -1437    323   2844       C  
ATOM   6838  CD1 TRP B 339      -2.108   9.558  64.527  1.00109.73           C  
ANISOU 6838  CD1 TRP B 339    12126  17805  11762  -1396    304   2807       C  
ATOM   6839  CD2 TRP B 339      -3.847  10.151  65.805  1.00106.54           C  
ANISOU 6839  CD2 TRP B 339    11812  17521  11146  -1497    377   2912       C  
ATOM   6840  NE1 TRP B 339      -2.992   8.507  64.543  1.00109.88           N  
ANISOU 6840  NE1 TRP B 339    12149  17712  11889  -1437    341   2849       N  
ATOM   6841  CE2 TRP B 339      -4.073   8.846  65.314  1.00111.15           C  
ANISOU 6841  CE2 TRP B 339    12358  17953  11919  -1508    387   2918       C  
ATOM   6842  CE3 TRP B 339      -4.805  10.731  66.653  1.00107.58           C  
ANISOU 6842  CE3 TRP B 339    11995  17767  11115  -1547    422   2963       C  
ATOM   6843  CZ2 TRP B 339      -5.230   8.122  65.619  1.00111.10           C  
ANISOU 6843  CZ2 TRP B 339    12365  17904  11943  -1590    441   2977       C  
ATOM   6844  CZ3 TRP B 339      -5.965  10.026  66.928  1.00109.68           C  
ANISOU 6844  CZ3 TRP B 339    12256  18016  11403  -1614    476   3020       C  
ATOM   6845  CH2 TRP B 339      -6.164   8.734  66.424  1.00111.14           C  
ANISOU 6845  CH2 TRP B 339    12404  18048  11777  -1646    485   3032       C  
ATOM   6846  N   HIS B 340       0.440  10.060  66.915  1.00113.68           N  
ANISOU 6846  N   HIS B 340    12641  18473  12080  -1335    102   3068       N  
ATOM   6847  CA  HIS B 340       0.967   8.766  67.342  1.00116.02           C  
ANISOU 6847  CA  HIS B 340    12909  18659  12514  -1267     38   3208       C  
ATOM   6848  C   HIS B 340       1.474   8.845  68.794  1.00121.41           C  
ANISOU 6848  C   HIS B 340    13615  19454  13061  -1267    -41   3385       C  
ATOM   6849  O   HIS B 340       1.172   7.967  69.603  1.00122.53           O  
ANISOU 6849  O   HIS B 340    13795  19528  13233  -1260    -61   3561       O  
ATOM   6850  CB  HIS B 340       2.093   8.313  66.381  1.00117.69           C  
ANISOU 6850  CB  HIS B 340    13023  18811  12883  -1167     -2   3117       C  
ATOM   6851  CG  HIS B 340       2.953   7.213  66.916  1.00123.61           C  
ANISOU 6851  CG  HIS B 340    13736  19481  13748  -1058    -87   3262       C  
ATOM   6852  ND1 HIS B 340       4.148   7.479  67.559  1.00126.50           N  
ANISOU 6852  ND1 HIS B 340    14041  19990  14033  -1001   -183   3331       N  
ATOM   6853  CD2 HIS B 340       2.753   5.878  66.899  1.00127.15           C  
ANISOU 6853  CD2 HIS B 340    14204  19723  14382   -996    -88   3349       C  
ATOM   6854  CE1 HIS B 340       4.634   6.300  67.912  1.00127.96           C  
ANISOU 6854  CE1 HIS B 340    14205  20060  14353   -883   -244   3470       C  
ATOM   6855  NE2 HIS B 340       3.834   5.309  67.527  1.00128.74           N  
ANISOU 6855  NE2 HIS B 340    14363  19928  14623   -875   -187   3487       N  
ATOM   6856  N   THR B 341       2.257   9.892  69.103  1.00117.77           N  
ANISOU 6856  N   THR B 341    13132  19170  12447  -1286    -84   3338       N  
ATOM   6857  CA  THR B 341       2.886  10.121  70.409  1.00118.89           C  
ANISOU 6857  CA  THR B 341    13274  19469  12431  -1296   -168   3471       C  
ATOM   6858  C   THR B 341       1.942  10.789  71.432  1.00123.81           C  
ANISOU 6858  C   THR B 341    13994  20198  12851  -1397   -126   3521       C  
ATOM   6859  O   THR B 341       2.257  10.786  72.628  1.00124.98           O  
ANISOU 6859  O   THR B 341    14151  20475  12863  -1413   -189   3655       O  
ATOM   6860  CB  THR B 341       4.171  10.946  70.251  1.00124.59           C  
ANISOU 6860  CB  THR B 341    13918  20348  13075  -1295   -229   3373       C  
ATOM   6861  OG1 THR B 341       3.893  12.122  69.489  1.00122.58           O  
ANISOU 6861  OG1 THR B 341    13698  20122  12756  -1373   -154   3186       O  
ATOM   6862  CG2 THR B 341       5.299  10.152  69.610  1.00123.17           C  
ANISOU 6862  CG2 THR B 341    13615  20122  13063  -1173   -294   3369       C  
ATOM   6863  N   SER B 342       0.786  11.333  70.981  1.00119.61           N  
ANISOU 6863  N   SER B 342    13524  19629  12292  -1457    -21   3416       N  
ATOM   6864  CA  SER B 342      -0.203  11.951  71.878  1.00119.68           C  
ANISOU 6864  CA  SER B 342    13616  19740  12116  -1536     33   3444       C  
ATOM   6865  C   SER B 342      -0.803  10.907  72.819  1.00125.81           C  
ANISOU 6865  C   SER B 342    14415  20493  12894  -1549     27   3648       C  
ATOM   6866  O   SER B 342      -1.146  11.238  73.953  1.00125.80           O  
ANISOU 6866  O   SER B 342    14458  20631  12708  -1605     29   3729       O  
ATOM   6867  CB  SER B 342      -1.309  12.647  71.092  1.00121.60           C  
ANISOU 6867  CB  SER B 342    13902  19950  12351  -1564    144   3293       C  
ATOM   6868  OG  SER B 342      -2.084  11.729  70.341  1.00129.10           O  
ANISOU 6868  OG  SER B 342    14827  20757  13468  -1547    194   3299       O  
ATOM   6869  N   PHE B 343      -0.899   9.647  72.351  1.00124.46           N  
ANISOU 6869  N   PHE B 343    14219  20141  12928  -1504     24   3729       N  
ATOM   6870  CA  PHE B 343      -1.413   8.515  73.114  1.00126.89           C  
ANISOU 6870  CA  PHE B 343    14561  20378  13275  -1523     23   3939       C  
ATOM   6871  C   PHE B 343      -0.390   7.997  74.133  1.00136.39           C  
ANISOU 6871  C   PHE B 343    15751  21638  14432  -1466    -92   4140       C  
ATOM   6872  O   PHE B 343      -0.784   7.336  75.093  1.00137.32           O  
ANISOU 6872  O   PHE B 343    15914  21762  14499  -1497    -99   4343       O  
ATOM   6873  CB  PHE B 343      -1.848   7.379  72.173  1.00128.52           C  
ANISOU 6873  CB  PHE B 343    14760  20342  13730  -1504     66   3932       C  
ATOM   6874  CG  PHE B 343      -3.095   7.660  71.369  1.00128.27           C  
ANISOU 6874  CG  PHE B 343    14734  20280  13723  -1578    179   3781       C  
ATOM   6875  CD1 PHE B 343      -4.335   7.763  71.992  1.00131.19           C  
ANISOU 6875  CD1 PHE B 343    15143  20731  13974  -1680    256   3833       C  
ATOM   6876  CD2 PHE B 343      -3.037   7.777  69.985  1.00128.83           C  
ANISOU 6876  CD2 PHE B 343    14758  20264  13927  -1543    209   3590       C  
ATOM   6877  CE1 PHE B 343      -5.487   8.014  71.248  1.00131.05           C  
ANISOU 6877  CE1 PHE B 343    15107  20716  13970  -1736    355   3694       C  
ATOM   6878  CE2 PHE B 343      -4.189   8.022  69.242  1.00130.60           C  
ANISOU 6878  CE2 PHE B 343    14972  20489  14159  -1602    305   3459       C  
ATOM   6879  CZ  PHE B 343      -5.406   8.137  69.876  1.00128.92           C  
ANISOU 6879  CZ  PHE B 343    14790  20364  13830  -1694    375   3511       C  
ATOM   6880  N   LYS B 344       0.908   8.292  73.942  1.00136.37           N  
ANISOU 6880  N   LYS B 344    15680  21699  14436  -1386   -182   4092       N  
ATOM   6881  CA  LYS B 344       1.955   7.853  74.874  1.00139.69           C  
ANISOU 6881  CA  LYS B 344    16063  22215  14799  -1313   -303   4275       C  
ATOM   6882  C   LYS B 344       2.009   8.776  76.103  1.00148.16           C  
ANISOU 6882  C   LYS B 344    17153  23562  15581  -1396   -334   4313       C  
ATOM   6883  O   LYS B 344       2.626   8.424  77.113  1.00149.49           O  
ANISOU 6883  O   LYS B 344    17298  23854  15646  -1360   -429   4496       O  
ATOM   6884  CB  LYS B 344       3.330   7.773  74.175  1.00142.03           C  
ANISOU 6884  CB  LYS B 344    16251  22503  15210  -1194   -387   4200       C  
ATOM   6885  CG  LYS B 344       3.420   6.701  73.077  1.00154.03           C  
ANISOU 6885  CG  LYS B 344    17748  23758  17018  -1090   -368   4176       C  
ATOM   6886  CD  LYS B 344       3.488   5.277  73.638  1.00164.16           C  
ANISOU 6886  CD  LYS B 344    19065  24881  18427   -994   -415   4426       C  
ATOM   6887  CE  LYS B 344       3.048   4.240  72.637  1.00169.22           C  
ANISOU 6887  CE  LYS B 344    19739  25216  19343   -949   -351   4385       C  
ATOM   6888  NZ  LYS B 344       2.873   2.910  73.276  1.00175.61           N  
ANISOU 6888  NZ  LYS B 344    20625  25833  20265   -891   -374   4641       N  
ATOM   6889  N   ALA B 345       1.331   9.940  76.017  1.00146.55           N  
ANISOU 6889  N   ALA B 345    16993  23450  15240  -1499   -252   4141       N  
ATOM   6890  CA  ALA B 345       1.257  10.940  77.081  1.00148.26           C  
ANISOU 6890  CA  ALA B 345    17240  23909  15181  -1587   -257   4121       C  
ATOM   6891  C   ALA B 345       0.331  10.525  78.234  1.00157.43           C  
ANISOU 6891  C   ALA B 345    18463  25146  16206  -1647   -225   4303       C  
ATOM   6892  O   ALA B 345       0.632  10.866  79.380  1.00158.48           O  
ANISOU 6892  O   ALA B 345    18598  25500  16118  -1687   -278   4379       O  
ATOM   6893  CB  ALA B 345       0.792  12.267  76.514  1.00147.12           C  
ANISOU 6893  CB  ALA B 345    17139  23793  14966  -1655   -167   3873       C  
ATOM   6894  N   LEU B 346      -0.803   9.838  77.945  1.00156.60           N  
ANISOU 6894  N   LEU B 346    18403  24885  16215  -1668   -136   4360       N  
ATOM   6895  CA  LEU B 346      -1.759   9.419  78.984  1.00158.99           C  
ANISOU 6895  CA  LEU B 346    18758  25264  16388  -1745    -89   4533       C  
ATOM   6896  C   LEU B 346      -1.192   8.285  79.857  1.00167.59           C  
ANISOU 6896  C   LEU B 346    19844  26355  17479  -1702   -185   4828       C  
ATOM   6897  O   LEU B 346      -1.360   8.322  81.077  1.00168.61           O  
ANISOU 6897  O   LEU B 346    19995  26678  17391  -1758   -203   4975       O  
ATOM   6898  CB  LEU B 346      -3.145   9.037  78.410  1.00158.46           C  
ANISOU 6898  CB  LEU B 346    18724  25052  16432  -1802     39   4500       C  
ATOM   6899  CG  LEU B 346      -3.224   7.939  77.351  1.00163.08           C  
ANISOU 6899  CG  LEU B 346    19298  25352  17311  -1758     52   4525       C  
ATOM   6900  CD1 LEU B 346      -3.861   6.687  77.909  1.00164.98           C  
ANISOU 6900  CD1 LEU B 346    19584  25491  17609  -1814     78   4765       C  
ATOM   6901  CD2 LEU B 346      -3.989   8.414  76.147  1.00164.15           C  
ANISOU 6901  CD2 LEU B 346    19420  25404  17546  -1777    150   4294       C  
ATOM   6902  N   GLY B 347      -0.510   7.325  79.232  1.00167.01           N  
ANISOU 6902  N   GLY B 347    19743  26073  17639  -1595   -246   4909       N  
ATOM   6903  CA  GLY B 347       0.107   6.193  79.912  1.00170.56           C  
ANISOU 6903  CA  GLY B 347    20196  26479  18129  -1515   -342   5194       C  
ATOM   6904  C   GLY B 347       1.316   6.600  80.731  1.00178.75           C  
ANISOU 6904  C   GLY B 347    21167  27768  18983  -1453   -476   5261       C  
ATOM   6905  O   GLY B 347       2.355   6.951  80.165  1.00177.68           O  
ANISOU 6905  O   GLY B 347    20948  27656  18907  -1368   -547   5134       O  
ATOM   6906  N   THR B 348       1.171   6.555  82.078  1.00180.25           N  
ANISOU 6906  N   THR B 348    21381  28171  18933  -1506   -510   5458       N  
ATOM   6907  CA  THR B 348       2.158   6.892  83.128  1.00183.21           C  
ANISOU 6907  CA  THR B 348    21692  28848  19070  -1474   -639   5558       C  
ATOM   6908  C   THR B 348       2.690   8.352  82.956  1.00188.04           C  
ANISOU 6908  C   THR B 348    22239  29675  19532  -1530   -653   5264       C  
ATOM   6909  O   THR B 348       1.877   9.281  82.929  1.00186.09           O  
ANISOU 6909  O   THR B 348    22042  29488  19176  -1650   -549   5077       O  
ATOM   6910  CB  THR B 348       3.292   5.836  83.243  1.00196.41           C  
ANISOU 6910  CB  THR B 348    23307  30457  20861  -1295   -778   5790       C  
ATOM   6911  OG1 THR B 348       4.022   5.746  82.016  1.00197.76           O  
ANISOU 6911  OG1 THR B 348    23411  30449  21279  -1180   -803   5631       O  
ATOM   6912  CG2 THR B 348       2.784   4.461  83.671  1.00197.17           C  
ANISOU 6912  CG2 THR B 348    23497  30360  21060  -1255   -768   6114       C  
ATOM   6913  N   THR B 349       4.033   8.543  82.871  1.00186.69           N  
ANISOU 6913  N   THR B 349    21960  29623  19352  -1445   -777   5229       N  
ATOM   6914  CA  THR B 349       4.710   9.847  82.748  1.00186.18           C  
ANISOU 6914  CA  THR B 349    21830  29762  19147  -1513   -802   4971       C  
ATOM   6915  C   THR B 349       4.384  10.552  81.419  1.00188.82           C  
ANISOU 6915  C   THR B 349    22192  29905  19648  -1550   -697   4684       C  
ATOM   6916  O   THR B 349       4.363   9.912  80.364  1.00187.25           O  
ANISOU 6916  O   THR B 349    21984  29449  19712  -1461   -671   4673       O  
ATOM   6917  CB  THR B 349       6.233   9.692  82.910  1.00197.17           C  
ANISOU 6917  CB  THR B 349    23077  31324  20513  -1411   -961   5026       C  
ATOM   6918  OG1 THR B 349       6.718   8.721  81.980  1.00199.51           O  
ANISOU 6918  OG1 THR B 349    23325  31378  21101  -1245   -993   5094       O  
ATOM   6919  CG2 THR B 349       6.641   9.317  84.334  1.00200.86           C  
ANISOU 6919  CG2 THR B 349    23504  32074  20740  -1391  -1078   5277       C  
ATOM   6920  N   TYR B 350       4.149  11.882  81.487  1.00185.81           N  
ANISOU 6920  N   TYR B 350    21847  29651  19102  -1678   -637   4453       N  
ATOM   6921  CA  TYR B 350       3.802  12.738  80.344  1.00183.73           C  
ANISOU 6921  CA  TYR B 350    21625  29238  18948  -1722   -535   4187       C  
ATOM   6922  C   TYR B 350       4.993  12.909  79.388  1.00187.42           C  
ANISOU 6922  C   TYR B 350    21993  29667  19550  -1670   -596   4066       C  
ATOM   6923  O   TYR B 350       6.091  13.265  79.824  1.00188.03           O  
ANISOU 6923  O   TYR B 350    21982  29957  19505  -1690   -697   4047       O  
ATOM   6924  CB  TYR B 350       3.297  14.118  80.822  1.00184.69           C  
ANISOU 6924  CB  TYR B 350    21827  29506  18841  -1860   -460   3993       C  
ATOM   6925  CG  TYR B 350       2.073  14.060  81.714  1.00187.59           C  
ANISOU 6925  CG  TYR B 350    22280  29935  19060  -1913   -383   4076       C  
ATOM   6926  CD1 TYR B 350       0.790  14.048  81.172  1.00188.39           C  
ANISOU 6926  CD1 TYR B 350    22458  29864  19259  -1914   -252   4025       C  
ATOM   6927  CD2 TYR B 350       2.195  14.052  83.101  1.00190.58           C  
ANISOU 6927  CD2 TYR B 350    22650  30577  19184  -1965   -439   4198       C  
ATOM   6928  CE1 TYR B 350      -0.340  14.000  81.987  1.00190.42           C  
ANISOU 6928  CE1 TYR B 350    22773  30206  19370  -1967   -174   4094       C  
ATOM   6929  CE2 TYR B 350       1.072  14.003  83.926  1.00192.31           C  
ANISOU 6929  CE2 TYR B 350    22938  30879  19252  -2020   -360   4271       C  
ATOM   6930  CZ  TYR B 350      -0.194  13.979  83.365  1.00198.87           C  
ANISOU 6930  CZ  TYR B 350    23838  31534  20190  -2022   -225   4217       C  
ATOM   6931  OH  TYR B 350      -1.304  13.934  84.173  1.00201.60           O  
ANISOU 6931  OH  TYR B 350    24232  31988  20380  -2080   -141   4282       O  
ATOM   6932  N   GLN B 351       4.764  12.649  78.085  1.00183.05           N  
ANISOU 6932  N   GLN B 351    21444  28867  19239  -1611   -534   3981       N  
ATOM   6933  CA  GLN B 351       5.784  12.754  77.034  1.00182.49           C  
ANISOU 6933  CA  GLN B 351    21277  28749  19312  -1561   -571   3859       C  
ATOM   6934  C   GLN B 351       5.502  13.998  76.152  1.00185.27           C  
ANISOU 6934  C   GLN B 351    21690  29045  19660  -1659   -471   3599       C  
ATOM   6935  O   GLN B 351       4.551  13.982  75.359  1.00183.35           O  
ANISOU 6935  O   GLN B 351    21518  28610  19537  -1648   -368   3535       O  
ATOM   6936  CB  GLN B 351       5.853  11.460  76.190  1.00183.63           C  
ANISOU 6936  CB  GLN B 351    21374  28665  19732  -1411   -581   3959       C  
ATOM   6937  CG  GLN B 351       6.068  10.163  76.995  1.00195.14           C  
ANISOU 6937  CG  GLN B 351    22800  30119  21224  -1296   -670   4236       C  
ATOM   6938  CD  GLN B 351       7.417  10.044  77.677  1.00213.70           C  
ANISOU 6938  CD  GLN B 351    25021  32704  23471  -1231   -817   4332       C  
ATOM   6939  OE1 GLN B 351       8.443  10.553  77.206  1.00209.79           O  
ANISOU 6939  OE1 GLN B 351    24414  32323  22973  -1227   -865   4194       O  
ATOM   6940  NE2 GLN B 351       7.450   9.323  78.788  1.00206.43           N  
ANISOU 6940  NE2 GLN B 351    24102  31871  22459  -1176   -893   4583       N  
ATOM   6941  N   PRO B 352       6.306  15.089  76.280  1.00182.31           N  
ANISOU 6941  N   PRO B 352    21289  28837  19142  -1760   -499   3450       N  
ATOM   6942  CA  PRO B 352       5.995  16.317  75.525  1.00180.27           C  
ANISOU 6942  CA  PRO B 352    21120  28506  18869  -1858   -398   3224       C  
ATOM   6943  C   PRO B 352       6.681  16.458  74.157  1.00180.96           C  
ANISOU 6943  C   PRO B 352    21140  28497  19119  -1837   -385   3102       C  
ATOM   6944  O   PRO B 352       7.839  16.068  73.972  1.00181.30           O  
ANISOU 6944  O   PRO B 352    21042  28632  19211  -1800   -474   3124       O  
ATOM   6945  CB  PRO B 352       6.447  17.432  76.472  1.00183.37           C  
ANISOU 6945  CB  PRO B 352    21544  29117  19011  -2004   -424   3128       C  
ATOM   6946  CG  PRO B 352       7.549  16.814  77.295  1.00190.06           C  
ANISOU 6946  CG  PRO B 352    22245  30190  19778  -1979   -569   3262       C  
ATOM   6947  CD  PRO B 352       7.430  15.305  77.219  1.00185.95           C  
ANISOU 6947  CD  PRO B 352    21655  29573  19425  -1807   -618   3485       C  
ATOM   6948  N   LEU B 353       5.947  17.068  73.206  1.00174.09           N  
ANISOU 6948  N   LEU B 353    20367  27462  18318  -1860   -272   2970       N  
ATOM   6949  CA  LEU B 353       6.407  17.344  71.840  1.00171.90           C  
ANISOU 6949  CA  LEU B 353    20051  27091  18172  -1857   -237   2844       C  
ATOM   6950  C   LEU B 353       7.148  18.698  71.752  1.00174.38           C  
ANISOU 6950  C   LEU B 353    20395  27504  18356  -2010   -224   2681       C  
ATOM   6951  O   LEU B 353       7.803  18.948  70.736  1.00173.60           O  
ANISOU 6951  O   LEU B 353    20242  27381  18337  -2032   -211   2589       O  
ATOM   6952  CB  LEU B 353       5.229  17.322  70.839  1.00170.06           C  
ANISOU 6952  CB  LEU B 353    19904  26649  18063  -1804   -125   2797       C  
ATOM   6953  CG  LEU B 353       4.616  15.958  70.496  1.00174.02           C  
ANISOU 6953  CG  LEU B 353    20359  27019  18741  -1675   -123   2914       C  
ATOM   6954  CD1 LEU B 353       3.147  16.099  70.155  1.00172.85           C  
ANISOU 6954  CD1 LEU B 353    20317  26743  18615  -1662    -16   2888       C  
ATOM   6955  CD2 LEU B 353       5.352  15.285  69.347  1.00175.53           C  
ANISOU 6955  CD2 LEU B 353    20430  27145  19119  -1597   -147   2882       C  
ATOM   6956  N   SER B 354       7.059  19.559  72.809  1.00170.33           N  
ANISOU 6956  N   SER B 354    19973  27105  17641  -2126   -224   2639       N  
ATOM   6957  CA  SER B 354       7.724  20.872  72.872  1.00170.02           C  
ANISOU 6957  CA  SER B 354    19988  27146  17467  -2299   -207   2476       C  
ATOM   6958  C   SER B 354       9.267  20.761  72.851  1.00173.25           C  
ANISOU 6958  C   SER B 354    20220  27749  17856  -2366   -309   2458       C  
ATOM   6959  O   SER B 354       9.940  21.699  72.417  1.00173.26           O  
ANISOU 6959  O   SER B 354    20236  27782  17814  -2510   -283   2316       O  
ATOM   6960  CB  SER B 354       7.273  21.651  74.104  1.00174.40           C  
ANISOU 6960  CB  SER B 354    20668  27784  17810  -2398   -189   2432       C  
ATOM   6961  OG  SER B 354       6.165  22.507  73.797  1.00181.61           O  
ANISOU 6961  OG  SER B 354    21771  28518  18713  -2405    -61   2335       O  
ATOM   6962  N   GLY B 355       9.796  19.624  73.305  1.00168.67           N  
ANISOU 6962  N   GLY B 355    19479  27299  17311  -2258   -420   2606       N  
ATOM   6963  CA  GLY B 355      11.228  19.350  73.303  1.00168.71           C  
ANISOU 6963  CA  GLY B 355    19283  27515  17305  -2277   -527   2609       C  
ATOM   6964  C   GLY B 355      11.740  18.929  71.937  1.00168.83           C  
ANISOU 6964  C   GLY B 355    19188  27446  17513  -2200   -510   2574       C  
ATOM   6965  O   GLY B 355      12.818  19.361  71.515  1.00169.20           O  
ANISOU 6965  O   GLY B 355    19122  27630  17536  -2296   -533   2475       O  
ATOM   6966  N   LYS B 356      10.940  18.112  71.217  1.00161.45           N  
ANISOU 6966  N   LYS B 356    18285  26295  16764  -2042   -461   2642       N  
ATOM   6967  CA  LYS B 356      11.230  17.562  69.883  1.00159.09           C  
ANISOU 6967  CA  LYS B 356    17891  25894  16660  -1944   -434   2609       C  
ATOM   6968  C   LYS B 356      11.097  18.599  68.735  1.00158.32           C  
ANISOU 6968  C   LYS B 356    17879  25698  16578  -2061   -322   2443       C  
ATOM   6969  O   LYS B 356      11.204  18.213  67.567  1.00157.06           O  
ANISOU 6969  O   LYS B 356    17657  25456  16564  -1989   -285   2405       O  
ATOM   6970  CB  LYS B 356      10.309  16.359  69.599  1.00160.59           C  
ANISOU 6970  CB  LYS B 356    18106  25883  17027  -1759   -415   2726       C  
ATOM   6971  CG  LYS B 356      10.644  15.112  70.407  1.00173.31           C  
ANISOU 6971  CG  LYS B 356    19611  27557  18682  -1611   -525   2907       C  
ATOM   6972  CD  LYS B 356       9.633  14.004  70.159  1.00179.91           C  
ANISOU 6972  CD  LYS B 356    20507  28162  19690  -1467   -488   3015       C  
ATOM   6973  CE  LYS B 356       9.964  12.740  70.919  1.00189.23           C  
ANISOU 6973  CE  LYS B 356    21606  29363  20928  -1315   -591   3213       C  
ATOM   6974  NZ  LYS B 356      11.122  12.013  70.327  1.00197.00           N  
ANISOU 6974  NZ  LYS B 356    22409  30394  22048  -1179   -658   3209       N  
ATOM   6975  N   THR B 357      10.903  19.902  69.065  1.00152.37           N  
ANISOU 6975  N   THR B 357    17270  24953  15669  -2237   -268   2346       N  
ATOM   6976  CA  THR B 357      10.773  21.025  68.118  1.00150.17           C  
ANISOU 6976  CA  THR B 357    17108  24570  15380  -2361   -161   2208       C  
ATOM   6977  C   THR B 357      12.031  21.127  67.230  1.00152.98           C  
ANISOU 6977  C   THR B 357    17304  25047  15772  -2430   -175   2130       C  
ATOM   6978  O   THR B 357      11.914  21.434  66.039  1.00151.65           O  
ANISOU 6978  O   THR B 357    17169  24774  15678  -2444    -93   2065       O  
ATOM   6979  CB  THR B 357      10.506  22.336  68.886  1.00154.49           C  
ANISOU 6979  CB  THR B 357    17837  25116  15746  -2535   -117   2126       C  
ATOM   6980  OG1 THR B 357       9.412  22.135  69.774  1.00151.17           O  
ANISOU 6980  OG1 THR B 357    17529  24629  15282  -2458   -110   2199       O  
ATOM   6981  CG2 THR B 357      10.179  23.513  67.971  1.00151.61           C  
ANISOU 6981  CG2 THR B 357    17639  24589  15376  -2640      4   2010       C  
ATOM   6982  N   SER B 358      13.220  20.836  67.812  1.00149.76           N  
ANISOU 6982  N   SER B 358    16713  24884  15306  -2467   -280   2141       N  
ATOM   6983  CA  SER B 358      14.513  20.850  67.125  1.00149.87           C  
ANISOU 6983  CA  SER B 358    16532  25074  15337  -2531   -306   2069       C  
ATOM   6984  C   SER B 358      14.526  19.862  65.953  1.00151.14           C  
ANISOU 6984  C   SER B 358    16575  25159  15692  -2348   -288   2091       C  
ATOM   6985  O   SER B 358      14.916  20.252  64.857  1.00150.72           O  
ANISOU 6985  O   SER B 358    16485  25109  15671  -2417   -223   1997       O  
ATOM   6986  CB  SER B 358      15.647  20.529  68.094  1.00155.52           C  
ANISOU 6986  CB  SER B 358    17049  26088  15953  -2555   -438   2101       C  
ATOM   6987  OG  SER B 358      16.905  20.647  67.449  1.00164.52           O  
ANISOU 6987  OG  SER B 358    17988  27430  17091  -2635   -456   2015       O  
ATOM   6988  N   TYR B 359      14.074  18.604  66.178  1.00145.93           N  
ANISOU 6988  N   TYR B 359    15868  24423  15157  -2125   -338   2210       N  
ATOM   6989  CA  TYR B 359      14.010  17.554  65.155  1.00144.51           C  
ANISOU 6989  CA  TYR B 359    15589  24148  15171  -1940   -322   2222       C  
ATOM   6990  C   TYR B 359      13.005  17.889  64.049  1.00143.81           C  
ANISOU 6990  C   TYR B 359    15648  23841  15154  -1948   -198   2159       C  
ATOM   6991  O   TYR B 359      13.254  17.556  62.889  1.00142.80           O  
ANISOU 6991  O   TYR B 359    15430  23697  15129  -1893   -157   2093       O  
ATOM   6992  CB  TYR B 359      13.633  16.188  65.766  1.00146.51           C  
ANISOU 6992  CB  TYR B 359    15804  24326  15539  -1722   -395   2371       C  
ATOM   6993  CG  TYR B 359      14.587  15.633  66.803  1.00150.97           C  
ANISOU 6993  CG  TYR B 359    16208  25101  16051  -1655   -529   2468       C  
ATOM   6994  CD1 TYR B 359      15.846  15.158  66.438  1.00154.47           C  
ANISOU 6994  CD1 TYR B 359    16416  25734  16543  -1577   -592   2437       C  
ATOM   6995  CD2 TYR B 359      14.189  15.471  68.128  1.00152.55           C  
ANISOU 6995  CD2 TYR B 359    16481  25323  16159  -1641   -594   2602       C  
ATOM   6996  CE1 TYR B 359      16.713  14.606  67.381  1.00157.48           C  
ANISOU 6996  CE1 TYR B 359    16635  26326  16873  -1486   -723   2540       C  
ATOM   6997  CE2 TYR B 359      15.045  14.915  69.079  1.00155.59           C  
ANISOU 6997  CE2 TYR B 359    16715  25917  16486  -1562   -724   2712       C  
ATOM   6998  CZ  TYR B 359      16.309  14.486  68.701  1.00164.57           C  
ANISOU 6998  CZ  TYR B 359    17616  27244  17670  -1478   -792   2684       C  
ATOM   6999  OH  TYR B 359      17.158  13.938  69.634  1.00167.33           O  
ANISOU 6999  OH  TYR B 359    17802  27820  17954  -1378   -928   2801       O  
ATOM   7000  N   PHE B 360      11.865  18.523  64.411  1.00137.79           N  
ANISOU 7000  N   PHE B 360    15100  22927  14327  -2005   -140   2177       N  
ATOM   7001  CA  PHE B 360      10.797  18.878  63.475  1.00135.42           C  
ANISOU 7001  CA  PHE B 360    14944  22436  14074  -1996    -30   2135       C  
ATOM   7002  C   PHE B 360      11.239  19.977  62.514  1.00137.89           C  
ANISOU 7002  C   PHE B 360    15288  22779  14324  -2147     47   2021       C  
ATOM   7003  O   PHE B 360      11.277  19.727  61.308  1.00137.21           O  
ANISOU 7003  O   PHE B 360    15143  22667  14324  -2101     96   1972       O  
ATOM   7004  CB  PHE B 360       9.506  19.290  64.213  1.00136.41           C  
ANISOU 7004  CB  PHE B 360    15272  22424  14133  -2002      7   2186       C  
ATOM   7005  CG  PHE B 360       8.898  18.247  65.126  1.00138.19           C  
ANISOU 7005  CG  PHE B 360    15490  22607  14410  -1873    -50   2311       C  
ATOM   7006  CD1 PHE B 360       8.885  16.904  64.766  1.00141.45           C  
ANISOU 7006  CD1 PHE B 360    15787  22969  14988  -1716    -83   2368       C  
ATOM   7007  CD2 PHE B 360       8.290  18.615  66.319  1.00140.75           C  
ANISOU 7007  CD2 PHE B 360    15933  22930  14615  -1913    -59   2369       C  
ATOM   7008  CE1 PHE B 360       8.320  15.944  65.608  1.00142.75           C  
ANISOU 7008  CE1 PHE B 360    15962  23075  15202  -1613   -129   2499       C  
ATOM   7009  CE2 PHE B 360       7.721  17.654  67.159  1.00143.89           C  
ANISOU 7009  CE2 PHE B 360    16325  23299  15047  -1810   -105   2499       C  
ATOM   7010  CZ  PHE B 360       7.738  16.326  66.797  1.00142.08           C  
ANISOU 7010  CZ  PHE B 360    15989  23008  14987  -1666   -139   2572       C  
ATOM   7011  N   HIS B 361      11.620  21.165  63.044  1.00133.59           N  
ANISOU 7011  N   HIS B 361    14836  22296  13627  -2336     59   1978       N  
ATOM   7012  CA  HIS B 361      12.059  22.325  62.257  1.00132.79           C  
ANISOU 7012  CA  HIS B 361    14798  22205  13452  -2514    138   1884       C  
ATOM   7013  C   HIS B 361      13.326  22.049  61.436  1.00135.40           C  
ANISOU 7013  C   HIS B 361    14912  22719  13816  -2557    122   1824       C  
ATOM   7014  O   HIS B 361      13.531  22.704  60.414  1.00134.76           O  
ANISOU 7014  O   HIS B 361    14860  22628  13714  -2659    203   1764       O  
ATOM   7015  CB  HIS B 361      12.259  23.548  63.152  1.00134.35           C  
ANISOU 7015  CB  HIS B 361    15139  22420  13487  -2717    148   1844       C  
ATOM   7016  CG  HIS B 361      10.984  24.276  63.415  1.00136.62           C  
ANISOU 7016  CG  HIS B 361    15683  22494  13731  -2707    221   1856       C  
ATOM   7017  ND1 HIS B 361      10.589  25.338  62.626  1.00138.00           N  
ANISOU 7017  ND1 HIS B 361    16038  22522  13876  -2789    329   1811       N  
ATOM   7018  CD2 HIS B 361      10.031  24.040  64.345  1.00137.61           C  
ANISOU 7018  CD2 HIS B 361    15903  22542  13841  -2609    203   1913       C  
ATOM   7019  CE1 HIS B 361       9.424  25.729  63.112  1.00136.72           C  
ANISOU 7019  CE1 HIS B 361    16066  22197  13682  -2724    370   1835       C  
ATOM   7020  NE2 HIS B 361       9.050  24.978  64.148  1.00136.82           N  
ANISOU 7020  NE2 HIS B 361    16031  22256  13700  -2623    300   1890       N  
ATOM   7021  N   LEU B 362      14.153  21.073  61.858  1.00131.44           N  
ANISOU 7021  N   LEU B 362    14189  22390  13361  -2469     22   1848       N  
ATOM   7022  CA  LEU B 362      15.343  20.687  61.108  1.00131.64           C  
ANISOU 7022  CA  LEU B 362    13980  22613  13426  -2473      4   1787       C  
ATOM   7023  C   LEU B 362      14.908  19.953  59.840  1.00133.32           C  
ANISOU 7023  C   LEU B 362    14147  22726  13782  -2315     60   1768       C  
ATOM   7024  O   LEU B 362      15.173  20.436  58.746  1.00133.29           O  
ANISOU 7024  O   LEU B 362    14128  22755  13761  -2403    139   1694       O  
ATOM   7025  CB  LEU B 362      16.290  19.820  61.964  1.00133.09           C  
ANISOU 7025  CB  LEU B 362    13941  23008  13621  -2383   -124   1827       C  
ATOM   7026  CG  LEU B 362      17.458  19.147  61.243  1.00139.10           C  
ANISOU 7026  CG  LEU B 362    14424  23980  14449  -2313   -153   1769       C  
ATOM   7027  CD1 LEU B 362      18.621  20.104  61.063  1.00140.99           C  
ANISOU 7027  CD1 LEU B 362    14557  24464  14549  -2557   -138   1672       C  
ATOM   7028  CD2 LEU B 362      17.902  17.906  61.983  1.00142.57           C  
ANISOU 7028  CD2 LEU B 362    14684  24518  14966  -2097   -277   1852       C  
ATOM   7029  N   LEU B 363      14.178  18.838  60.003  1.00127.58           N  
ANISOU 7029  N   LEU B 363    13417  21872  13187  -2102     26   1834       N  
ATOM   7030  CA  LEU B 363      13.702  17.976  58.928  1.00125.83           C  
ANISOU 7030  CA  LEU B 363    13149  21550  13112  -1943     69   1806       C  
ATOM   7031  C   LEU B 363      12.688  18.641  57.992  1.00126.73           C  
ANISOU 7031  C   LEU B 363    13433  21514  13204  -1993    179   1773       C  
ATOM   7032  O   LEU B 363      12.756  18.401  56.786  1.00125.92           O  
ANISOU 7032  O   LEU B 363    13259  21432  13154  -1958    234   1701       O  
ATOM   7033  CB  LEU B 363      13.091  16.701  59.521  1.00125.59           C  
ANISOU 7033  CB  LEU B 363    13108  21393  13215  -1737      8   1893       C  
ATOM   7034  CG  LEU B 363      14.012  15.484  59.619  1.00131.78           C  
ANISOU 7034  CG  LEU B 363    13673  22280  14118  -1573    -74   1900       C  
ATOM   7035  CD1 LEU B 363      15.033  15.632  60.748  1.00133.48           C  
ANISOU 7035  CD1 LEU B 363    13784  22695  14240  -1614   -176   1956       C  
ATOM   7036  CD2 LEU B 363      13.210  14.229  59.862  1.00134.36           C  
ANISOU 7036  CD2 LEU B 363    14034  22412  14605  -1378   -100   1978       C  
ATOM   7037  N   THR B 364      11.764  19.466  58.523  1.00121.56           N  
ANISOU 7037  N   THR B 364    12995  20725  12465  -2065    212   1823       N  
ATOM   7038  CA  THR B 364      10.720  20.108  57.715  1.00119.82           C  
ANISOU 7038  CA  THR B 364    12941  20364  12219  -2082    308   1811       C  
ATOM   7039  C   THR B 364      11.232  21.253  56.833  1.00123.42           C  
ANISOU 7039  C   THR B 364    13440  20882  12572  -2250    386   1753       C  
ATOM   7040  O   THR B 364      10.553  21.608  55.865  1.00122.68           O  
ANISOU 7040  O   THR B 364    13435  20711  12468  -2236    464   1743       O  
ATOM   7041  CB  THR B 364       9.556  20.610  58.575  1.00125.16           C  
ANISOU 7041  CB  THR B 364    13828  20886  12841  -2078    321   1880       C  
ATOM   7042  OG1 THR B 364      10.039  21.453  59.621  1.00124.79           O  
ANISOU 7042  OG1 THR B 364    13856  20884  12675  -2219    294   1892       O  
ATOM   7043  CG2 THR B 364       8.699  19.483  59.124  1.00122.34           C  
ANISOU 7043  CG2 THR B 364    13456  20439  12589  -1914    278   1945       C  
ATOM   7044  N   TRP B 365      12.402  21.833  57.153  1.00120.12           N  
ANISOU 7044  N   TRP B 365    12960  20611  12069  -2413    367   1720       N  
ATOM   7045  CA  TRP B 365      12.933  22.935  56.353  1.00120.05           C  
ANISOU 7045  CA  TRP B 365    13000  20655  11958  -2603    448   1674       C  
ATOM   7046  C   TRP B 365      14.227  22.554  55.614  1.00122.24           C  
ANISOU 7046  C   TRP B 365    13032  21167  12246  -2653    442   1599       C  
ATOM   7047  O   TRP B 365      14.502  23.150  54.575  1.00122.24           O  
ANISOU 7047  O   TRP B 365    13041  21215  12189  -2763    524   1564       O  
ATOM   7048  CB  TRP B 365      13.137  24.215  57.189  1.00119.94           C  
ANISOU 7048  CB  TRP B 365    13159  20603  11811  -2812    462   1681       C  
ATOM   7049  CG  TRP B 365      11.923  24.701  57.942  1.00120.28           C  
ANISOU 7049  CG  TRP B 365    13443  20430  11826  -2767    478   1737       C  
ATOM   7050  CD1 TRP B 365      11.847  24.957  59.280  1.00123.51           C  
ANISOU 7050  CD1 TRP B 365    13932  20816  12180  -2811    427   1750       C  
ATOM   7051  CD2 TRP B 365      10.631  25.029  57.398  1.00119.14           C  
ANISOU 7051  CD2 TRP B 365    13483  20091  11694  -2668    550   1778       C  
ATOM   7052  NE1 TRP B 365      10.588  25.400  59.610  1.00122.14           N  
ANISOU 7052  NE1 TRP B 365    13977  20441  11989  -2741    470   1791       N  
ATOM   7053  CE2 TRP B 365       9.819  25.452  58.476  1.00122.69           C  
ANISOU 7053  CE2 TRP B 365    14111  20404  12102  -2646    543   1812       C  
ATOM   7054  CE3 TRP B 365      10.075  24.997  56.104  1.00119.85           C  
ANISOU 7054  CE3 TRP B 365    13591  20133  11814  -2589    619   1788       C  
ATOM   7055  CZ2 TRP B 365       8.485  25.842  58.302  1.00121.09           C  
ANISOU 7055  CZ2 TRP B 365    14094  20019  11895  -2539    603   1854       C  
ATOM   7056  CZ3 TRP B 365       8.751  25.379  55.934  1.00120.50           C  
ANISOU 7056  CZ3 TRP B 365    13857  20040  11886  -2485    670   1838       C  
ATOM   7057  CH2 TRP B 365       7.972  25.795  57.024  1.00120.87           C  
ANISOU 7057  CH2 TRP B 365    14072  19955  11900  -2456    663   1870       C  
ATOM   7058  N   SER B 366      14.995  21.562  56.107  1.00117.48           N  
ANISOU 7058  N   SER B 366    12209  20716  11713  -2560    351   1580       N  
ATOM   7059  CA  SER B 366      16.232  21.141  55.444  1.00117.66           C  
ANISOU 7059  CA  SER B 366    11973  20983  11748  -2578    344   1499       C  
ATOM   7060  C   SER B 366      15.974  20.115  54.314  1.00118.40           C  
ANISOU 7060  C   SER B 366    11948  21072  11967  -2387    373   1450       C  
ATOM   7061  O   SER B 366      16.520  20.303  53.224  1.00118.52           O  
ANISOU 7061  O   SER B 366    11862  21224  11946  -2455    439   1376       O  
ATOM   7062  CB  SER B 366      17.240  20.591  56.447  1.00122.75           C  
ANISOU 7062  CB  SER B 366    12423  21816  12402  -2550    233   1498       C  
ATOM   7063  OG  SER B 366      16.858  19.337  56.986  1.00130.99           O  
ANISOU 7063  OG  SER B 366    13404  22785  13581  -2303    151   1550       O  
ATOM   7064  N   LEU B 367      15.127  19.079  54.542  1.00111.95           N  
ANISOU 7064  N   LEU B 367    11151  20101  11284  -2169    333   1485       N  
ATOM   7065  CA  LEU B 367      14.811  18.053  53.531  1.00110.39           C  
ANISOU 7065  CA  LEU B 367    10855  19877  11211  -1994    361   1420       C  
ATOM   7066  C   LEU B 367      14.200  18.633  52.233  1.00109.98           C  
ANISOU 7066  C   LEU B 367    10897  19791  11101  -2058    470   1379       C  
ATOM   7067  O   LEU B 367      14.660  18.197  51.171  1.00109.99           O  
ANISOU 7067  O   LEU B 367    10742  19921  11127  -2019    510   1280       O  
ATOM   7068  CB  LEU B 367      13.902  16.963  54.093  1.00109.73           C  
ANISOU 7068  CB  LEU B 367    10818  19602  11273  -1793    307   1472       C  
ATOM   7069  CG  LEU B 367      14.581  15.733  54.711  1.00115.86           C  
ANISOU 7069  CG  LEU B 367    11418  20426  12179  -1623    214   1477       C  
ATOM   7070  CD1 LEU B 367      15.347  16.059  56.002  1.00117.13           C  
ANISOU 7070  CD1 LEU B 367    11542  20697  12266  -1687    125   1554       C  
ATOM   7071  CD2 LEU B 367      13.547  14.758  55.126  1.00117.83           C  
ANISOU 7071  CD2 LEU B 367    11753  20452  12565  -1459    184   1537       C  
ATOM   7072  N   PRO B 368      13.248  19.614  52.238  1.00102.71           N  
ANISOU 7072  N   PRO B 368    10210  18724  10091  -2147    521   1448       N  
ATOM   7073  CA  PRO B 368      12.770  20.155  50.949  1.00101.13           C  
ANISOU 7073  CA  PRO B 368    10078  18524   9821  -2194    619   1424       C  
ATOM   7074  C   PRO B 368      13.857  20.952  50.236  1.00103.37           C  
ANISOU 7074  C   PRO B 368    10288  19002   9984  -2381    678   1383       C  
ATOM   7075  O   PRO B 368      13.926  20.895  49.012  1.00102.91           O  
ANISOU 7075  O   PRO B 368    10160  19045   9896  -2383    744   1326       O  
ATOM   7076  CB  PRO B 368      11.585  21.048  51.334  1.00101.82           C  
ANISOU 7076  CB  PRO B 368    10434  18411   9844  -2226    647   1524       C  
ATOM   7077  CG  PRO B 368      11.299  20.756  52.756  1.00106.06           C  
ANISOU 7077  CG  PRO B 368    11026  18836  10434  -2172    568   1582       C  
ATOM   7078  CD  PRO B 368      12.578  20.291  53.365  1.00103.00           C  
ANISOU 7078  CD  PRO B 368    10454  18601  10078  -2199    497   1548       C  
ATOM   7079  N   PHE B 369      14.727  21.645  51.004  1.00 99.10           N  
ANISOU 7079  N   PHE B 369     9750  18534   9370  -2548    655   1404       N  
ATOM   7080  CA  PHE B 369      15.852  22.438  50.506  1.00 99.86           C  
ANISOU 7080  CA  PHE B 369     9770  18825   9346  -2767    709   1367       C  
ATOM   7081  C   PHE B 369      16.843  21.547  49.750  1.00105.65           C  
ANISOU 7081  C   PHE B 369    10203  19816  10124  -2704    708   1252       C  
ATOM   7082  O   PHE B 369      17.253  21.918  48.650  1.00106.21           O  
ANISOU 7082  O   PHE B 369    10214  20032  10111  -2808    792   1209       O  
ATOM   7083  CB  PHE B 369      16.550  23.187  51.661  1.00101.89           C  
ANISOU 7083  CB  PHE B 369    10069  19114   9530  -2951    668   1394       C  
ATOM   7084  CG  PHE B 369      17.938  23.714  51.370  1.00104.68           C  
ANISOU 7084  CG  PHE B 369    10267  19725   9781  -3177    699   1333       C  
ATOM   7085  CD1 PHE B 369      19.066  22.986  51.729  1.00108.54           C  
ANISOU 7085  CD1 PHE B 369    10474  20464  10305  -3146    627   1260       C  
ATOM   7086  CD2 PHE B 369      18.117  24.943  50.746  1.00107.06           C  
ANISOU 7086  CD2 PHE B 369    10703  20026   9949  -3422    801   1356       C  
ATOM   7087  CE1 PHE B 369      20.348  23.470  51.452  1.00111.31           C  
ANISOU 7087  CE1 PHE B 369    10655  21088  10551  -3363    658   1196       C  
ATOM   7088  CE2 PHE B 369      19.397  25.429  50.477  1.00111.67           C  
ANISOU 7088  CE2 PHE B 369    11138  20860  10432  -3659    837   1299       C  
ATOM   7089  CZ  PHE B 369      20.504  24.690  50.830  1.00110.92           C  
ANISOU 7089  CZ  PHE B 369    10739  21039  10365  -3633    765   1213       C  
ATOM   7090  N   VAL B 370      17.214  20.380  50.332  1.00102.14           N  
ANISOU 7090  N   VAL B 370     9575  19426   9806  -2526    618   1207       N  
ATOM   7091  CA  VAL B 370      18.138  19.407  49.732  1.00102.73           C  
ANISOU 7091  CA  VAL B 370     9359  19727   9947  -2416    608   1088       C  
ATOM   7092  C   VAL B 370      17.590  18.958  48.364  1.00106.85           C  
ANISOU 7092  C   VAL B 370     9858  20242  10497  -2317    686   1014       C  
ATOM   7093  O   VAL B 370      18.333  18.990  47.379  1.00107.49           O  
ANISOU 7093  O   VAL B 370     9775  20550  10516  -2376    750    921       O  
ATOM   7094  CB  VAL B 370      18.407  18.209  50.684  1.00106.07           C  
ANISOU 7094  CB  VAL B 370     9643  20138  10519  -2200    493   1082       C  
ATOM   7095  CG1 VAL B 370      19.113  17.055  49.969  1.00106.85           C  
ANISOU 7095  CG1 VAL B 370     9471  20405  10721  -2019    491    952       C  
ATOM   7096  CG2 VAL B 370      19.212  18.655  51.898  1.00106.66           C  
ANISOU 7096  CG2 VAL B 370     9675  20319  10530  -2314    415   1135       C  
ATOM   7097  N   LEU B 371      16.281  18.610  48.301  1.00102.03           N  
ANISOU 7097  N   LEU B 371     9411  19396   9960  -2187    685   1052       N  
ATOM   7098  CA  LEU B 371      15.610  18.177  47.073  1.00101.42           C  
ANISOU 7098  CA  LEU B 371     9325  19308   9901  -2096    751    979       C  
ATOM   7099  C   LEU B 371      15.524  19.307  46.041  1.00106.74           C  
ANISOU 7099  C   LEU B 371    10087  20071  10397  -2279    854   1004       C  
ATOM   7100  O   LEU B 371      15.760  19.050  44.858  1.00107.37           O  
ANISOU 7100  O   LEU B 371    10040  20318  10438  -2268    917    906       O  
ATOM   7101  CB  LEU B 371      14.215  17.622  47.371  1.00 99.67           C  
ANISOU 7101  CB  LEU B 371     9254  18829   9784  -1944    720   1022       C  
ATOM   7102  CG  LEU B 371      14.169  16.267  48.078  1.00104.20           C  
ANISOU 7102  CG  LEU B 371     9739  19302  10552  -1740    637    987       C  
ATOM   7103  CD1 LEU B 371      12.795  16.006  48.649  1.00102.97           C  
ANISOU 7103  CD1 LEU B 371     9768  18889  10467  -1658    609   1068       C  
ATOM   7104  CD2 LEU B 371      14.575  15.129  47.143  1.00107.31           C  
ANISOU 7104  CD2 LEU B 371     9925  19802  11046  -1597    659    820       C  
ATOM   7105  N   THR B 372      15.219  20.553  46.484  1.00103.13           N  
ANISOU 7105  N   THR B 372     9849  19506   9830  -2444    873   1134       N  
ATOM   7106  CA  THR B 372      15.135  21.740  45.618  1.00103.27           C  
ANISOU 7106  CA  THR B 372     9992  19568   9678  -2625    971   1194       C  
ATOM   7107  C   THR B 372      16.505  21.990  44.974  1.00109.03           C  
ANISOU 7107  C   THR B 372    10526  20587  10311  -2788   1025   1121       C  
ATOM   7108  O   THR B 372      16.579  22.159  43.758  1.00109.35           O  
ANISOU 7108  O   THR B 372    10519  20773  10256  -2836   1108   1090       O  
ATOM   7109  CB  THR B 372      14.636  22.962  46.419  1.00108.04           C  
ANISOU 7109  CB  THR B 372    10876  19964  10211  -2755    974   1338       C  
ATOM   7110  OG1 THR B 372      13.385  22.650  47.029  1.00103.61           O  
ANISOU 7110  OG1 THR B 372    10462  19169   9736  -2591    926   1392       O  
ATOM   7111  CG2 THR B 372      14.480  24.205  45.559  1.00106.71           C  
ANISOU 7111  CG2 THR B 372    10875  19793   9879  -2925   1077   1423       C  
ATOM   7112  N   VAL B 373      17.579  21.964  45.790  1.00106.97           N  
ANISOU 7112  N   VAL B 373    10136  20438  10068  -2869    976   1091       N  
ATOM   7113  CA  VAL B 373      18.969  22.160  45.369  1.00109.38           C  
ANISOU 7113  CA  VAL B 373    10222  21050  10286  -3031   1017   1015       C  
ATOM   7114  C   VAL B 373      19.371  21.041  44.384  1.00114.72           C  
ANISOU 7114  C   VAL B 373    10627  21945  11015  -2868   1038    862       C  
ATOM   7115  O   VAL B 373      19.910  21.351  43.317  1.00115.57           O  
ANISOU 7115  O   VAL B 373    10630  22278  11002  -2988   1129    812       O  
ATOM   7116  CB  VAL B 373      19.922  22.258  46.599  1.00114.36           C  
ANISOU 7116  CB  VAL B 373    10757  21759  10934  -3119    939   1011       C  
ATOM   7117  CG1 VAL B 373      21.389  22.069  46.212  1.00116.25           C  
ANISOU 7117  CG1 VAL B 373    10685  22367  11118  -3215    960    897       C  
ATOM   7118  CG2 VAL B 373      19.731  23.587  47.325  1.00114.24           C  
ANISOU 7118  CG2 VAL B 373    11001  21584  10821  -3354    952   1130       C  
ATOM   7119  N   ALA B 374      19.053  19.767  44.718  1.00111.15           N  
ANISOU 7119  N   ALA B 374    10081  21413  10738  -2602    962    789       N  
ATOM   7120  CA  ALA B 374      19.353  18.589  43.890  1.00112.19           C  
ANISOU 7120  CA  ALA B 374     9975  21700  10951  -2414    977    624       C  
ATOM   7121  C   ALA B 374      18.735  18.685  42.484  1.00117.04           C  
ANISOU 7121  C   ALA B 374    10628  22363  11478  -2423   1075    579       C  
ATOM   7122  O   ALA B 374      19.367  18.243  41.524  1.00118.04           O  
ANISOU 7122  O   ALA B 374    10541  22738  11569  -2397   1132    438       O  
ATOM   7123  CB  ALA B 374      18.877  17.321  44.578  1.00112.05           C  
ANISOU 7123  CB  ALA B 374     9934  21496  11146  -2142    883    586       C  
ATOM   7124  N   ILE B 375      17.525  19.279  42.364  1.00112.72           N  
ANISOU 7124  N   ILE B 375    10342  21603  10884  -2454   1094    697       N  
ATOM   7125  CA  ILE B 375      16.836  19.472  41.080  1.00112.56           C  
ANISOU 7125  CA  ILE B 375    10377  21635  10756  -2464   1177    683       C  
ATOM   7126  C   ILE B 375      17.538  20.573  40.282  1.00118.36           C  
ANISOU 7126  C   ILE B 375    11102  22592  11279  -2711   1277    731       C  
ATOM   7127  O   ILE B 375      17.838  20.369  39.107  1.00119.03           O  
ANISOU 7127  O   ILE B 375    11042  22913  11272  -2723   1351    634       O  
ATOM   7128  CB  ILE B 375      15.321  19.779  41.263  1.00113.71           C  
ANISOU 7128  CB  ILE B 375    10791  21502  10911  -2404   1159    805       C  
ATOM   7129  CG1 ILE B 375      14.574  18.557  41.820  1.00112.56           C  
ANISOU 7129  CG1 ILE B 375    10631  21171  10966  -2171   1079    737       C  
ATOM   7130  CG2 ILE B 375      14.685  20.259  39.941  1.00114.79           C  
ANISOU 7130  CG2 ILE B 375    10996  21731  10888  -2449   1245    829       C  
ATOM   7131  CD1 ILE B 375      13.329  18.880  42.568  1.00116.50           C  
ANISOU 7131  CD1 ILE B 375    11373  21390  11501  -2129   1035    873       C  
ATOM   7132  N   LEU B 376      17.792  21.734  40.920  1.00115.81           N  
ANISOU 7132  N   LEU B 376    10937  22190  10873  -2916   1283    878       N  
ATOM   7133  CA  LEU B 376      18.442  22.886  40.296  1.00117.90           C  
ANISOU 7133  CA  LEU B 376    11235  22619  10942  -3187   1381    951       C  
ATOM   7134  C   LEU B 376      19.873  22.552  39.841  1.00126.79           C  
ANISOU 7134  C   LEU B 376    12047  24109  12019  -3276   1422    810       C  
ATOM   7135  O   LEU B 376      20.353  23.155  38.877  1.00128.16           O  
ANISOU 7135  O   LEU B 376    12176  24497  12020  -3458   1525    823       O  
ATOM   7136  CB  LEU B 376      18.441  24.099  41.237  1.00117.55           C  
ANISOU 7136  CB  LEU B 376    11433  22378  10853  -3385   1373   1111       C  
ATOM   7137  CG  LEU B 376      17.066  24.680  41.583  1.00120.14           C  
ANISOU 7137  CG  LEU B 376    12087  22368  11191  -3324   1357   1263       C  
ATOM   7138  CD1 LEU B 376      17.114  25.448  42.879  1.00120.11           C  
ANISOU 7138  CD1 LEU B 376    12269  22152  11214  -3441   1314   1355       C  
ATOM   7139  CD2 LEU B 376      16.525  25.550  40.467  1.00122.52           C  
ANISOU 7139  CD2 LEU B 376    12556  22669  11328  -3412   1455   1379       C  
ATOM   7140  N   ALA B 377      20.525  21.564  40.497  1.00125.12           N  
ANISOU 7140  N   ALA B 377    11611  23975  11952  -3134   1345    679       N  
ATOM   7141  CA  ALA B 377      21.867  21.099  40.137  1.00127.63           C  
ANISOU 7141  CA  ALA B 377    11598  24652  12244  -3162   1372    527       C  
ATOM   7142  C   ALA B 377      21.822  20.258  38.842  1.00133.30           C  
ANISOU 7142  C   ALA B 377    12133  25569  12946  -3016   1436    367       C  
ATOM   7143  O   ALA B 377      22.611  20.511  37.926  1.00135.00           O  
ANISOU 7143  O   ALA B 377    12178  26102  13012  -3154   1530    301       O  
ATOM   7144  CB  ALA B 377      22.469  20.293  41.278  1.00128.44           C  
ANISOU 7144  CB  ALA B 377    11536  24752  12511  -3015   1261    456       C  
ATOM   7145  N   VAL B 378      20.869  19.296  38.752  1.00128.86           N  
ANISOU 7145  N   VAL B 378    11613  24824  12525  -2756   1390    301       N  
ATOM   7146  CA  VAL B 378      20.685  18.445  37.565  1.00129.60           C  
ANISOU 7146  CA  VAL B 378    11557  25072  12614  -2609   1445    128       C  
ATOM   7147  C   VAL B 378      19.932  19.232  36.459  1.00134.89           C  
ANISOU 7147  C   VAL B 378    12387  25777  13088  -2740   1536    216       C  
ATOM   7148  O   VAL B 378      19.848  18.760  35.321  1.00135.55           O  
ANISOU 7148  O   VAL B 378    12347  26053  13103  -2679   1600     83       O  
ATOM   7149  CB  VAL B 378      20.009  17.070  37.862  1.00132.10           C  
ANISOU 7149  CB  VAL B 378    11849  25186  13157  -2303   1368      5       C  
ATOM   7150  CG1 VAL B 378      20.889  16.193  38.747  1.00132.57           C  
ANISOU 7150  CG1 VAL B 378    11713  25263  13394  -2147   1290    -90       C  
ATOM   7151  CG2 VAL B 378      18.611  17.223  38.455  1.00129.45           C  
ANISOU 7151  CG2 VAL B 378    11805  24485  12896  -2247   1306    147       C  
ATOM   7152  N   ALA B 379      19.413  20.441  36.812  1.00131.29           N  
ANISOU 7152  N   ALA B 379    12205  25139  12539  -2913   1541    439       N  
ATOM   7153  CA  ALA B 379      18.665  21.406  35.992  1.00131.27           C  
ANISOU 7153  CA  ALA B 379    12410  25114  12351  -3040   1614    588       C  
ATOM   7154  C   ALA B 379      17.496  20.735  35.255  1.00134.23           C  
ANISOU 7154  C   ALA B 379    12821  25437  12743  -2845   1609    525       C  
ATOM   7155  O   ALA B 379      17.556  20.499  34.044  1.00135.10           O  
ANISOU 7155  O   ALA B 379    12804  25800  12728  -2843   1681    427       O  
ATOM   7156  CB  ALA B 379      19.595  22.119  35.017  1.00134.45           C  
ANISOU 7156  CB  ALA B 379    12705  25848  12531  -3278   1733    601       C  
ATOM   7157  N   GLN B 380      16.441  20.411  36.009  1.00128.88           N  
ANISOU 7157  N   GLN B 380    12303  24450  12214  -2689   1523    570       N  
ATOM   7158  CA  GLN B 380      15.260  19.750  35.463  1.00128.03           C  
ANISOU 7158  CA  GLN B 380    12232  24277  12138  -2513   1506    507       C  
ATOM   7159  C   GLN B 380      13.990  20.583  35.694  1.00131.72           C  
ANISOU 7159  C   GLN B 380    12992  24503  12551  -2520   1485    715       C  
ATOM   7160  O   GLN B 380      12.887  20.032  35.749  1.00130.02           O  
ANISOU 7160  O   GLN B 380    12838  24150  12415  -2363   1438    688       O  
ATOM   7161  CB  GLN B 380      15.116  18.331  36.045  1.00128.45           C  
ANISOU 7161  CB  GLN B 380    12163  24209  12434  -2290   1427    328       C  
ATOM   7162  CG  GLN B 380      16.197  17.350  35.579  1.00144.15           C  
ANISOU 7162  CG  GLN B 380    13852  26443  14477  -2222   1455     90       C  
ATOM   7163  CD  GLN B 380      16.235  17.106  34.083  1.00166.50           C  
ANISOU 7163  CD  GLN B 380    16538  29572  17154  -2230   1546    -57       C  
ATOM   7164  OE1 GLN B 380      17.303  17.080  33.466  1.00165.47           O  
ANISOU 7164  OE1 GLN B 380    16202  29738  16931  -2300   1614   -164       O  
ATOM   7165  NE2 GLN B 380      15.078  16.916  33.466  1.00156.88           N  
ANISOU 7165  NE2 GLN B 380    15408  28306  15892  -2162   1549    -73       N  
ATOM   7166  N   VAL B 381      14.146  21.916  35.781  1.00129.76           N  
ANISOU 7166  N   VAL B 381    12924  24217  12163  -2705   1527    918       N  
ATOM   7167  CA  VAL B 381      13.020  22.835  35.955  1.00129.20           C  
ANISOU 7167  CA  VAL B 381    13140  23923  12027  -2705   1519   1126       C  
ATOM   7168  C   VAL B 381      12.428  23.097  34.556  1.00135.46           C  
ANISOU 7168  C   VAL B 381    13944  24904  12621  -2699   1584   1164       C  
ATOM   7169  O   VAL B 381      13.131  23.618  33.682  1.00137.03           O  
ANISOU 7169  O   VAL B 381    14086  25336  12643  -2854   1670   1194       O  
ATOM   7170  CB  VAL B 381      13.418  24.143  36.706  1.00133.16           C  
ANISOU 7170  CB  VAL B 381    13853  24260  12480  -2895   1538   1320       C  
ATOM   7171  CG1 VAL B 381      12.212  25.051  36.914  1.00132.02           C  
ANISOU 7171  CG1 VAL B 381    14012  23864  12285  -2857   1531   1523       C  
ATOM   7172  CG2 VAL B 381      14.085  23.838  38.043  1.00132.25           C  
ANISOU 7172  CG2 VAL B 381    13692  24020  12536  -2911   1470   1265       C  
ATOM   7173  N   ASP B 382      11.164  22.669  34.333  1.00131.47           N  
ANISOU 7173  N   ASP B 382    13488  24329  12137  -2524   1542   1152       N  
ATOM   7174  CA  ASP B 382      10.437  22.842  33.066  1.00132.23           C  
ANISOU 7174  CA  ASP B 382    13588  24614  12041  -2489   1585   1186       C  
ATOM   7175  C   ASP B 382       9.140  23.610  33.293  1.00135.98           C  
ANISOU 7175  C   ASP B 382    14317  24883  12467  -2410   1554   1392       C  
ATOM   7176  O   ASP B 382       8.539  23.489  34.354  1.00133.97           O  
ANISOU 7176  O   ASP B 382    14169  24364  12369  -2316   1486   1420       O  
ATOM   7177  CB  ASP B 382      10.118  21.491  32.400  1.00133.85           C  
ANISOU 7177  CB  ASP B 382    13564  24999  12293  -2348   1566    935       C  
ATOM   7178  CG  ASP B 382      11.275  20.530  32.223  1.00143.19           C  
ANISOU 7178  CG  ASP B 382    14483  26362  13559  -2365   1588    693       C  
ATOM   7179  OD1 ASP B 382      12.268  20.909  31.569  1.00145.43           O  
ANISOU 7179  OD1 ASP B 382    14668  26887  13702  -2507   1666    686       O  
ATOM   7180  OD2 ASP B 382      11.154  19.370  32.669  1.00147.27           O  
ANISOU 7180  OD2 ASP B 382    14888  26793  14275  -2230   1533    507       O  
ATOM   7181  N   GLY B 383       8.710  24.368  32.293  1.00134.37           N  
ANISOU 7181  N   GLY B 383    14199  24816  12041  -2436   1605   1537       N  
ATOM   7182  CA  GLY B 383       7.481  25.147  32.364  1.00134.31           C  
ANISOU 7182  CA  GLY B 383    14420  24650  11961  -2336   1582   1744       C  
ATOM   7183  C   GLY B 383       6.370  24.604  31.490  1.00139.88           C  
ANISOU 7183  C   GLY B 383    15035  25541  12572  -2178   1554   1685       C  
ATOM   7184  O   GLY B 383       6.629  24.086  30.401  1.00141.05           O  
ANISOU 7184  O   GLY B 383    14993  26001  12599  -2200   1589   1557       O  
ATOM   7185  N   ASP B 384       5.120  24.743  31.958  1.00136.24           N  
ANISOU 7185  N   ASP B 384    14702  24908  12153  -2022   1494   1772       N  
ATOM   7186  CA  ASP B 384       3.915  24.300  31.252  1.00136.83           C  
ANISOU 7186  CA  ASP B 384    14700  25153  12137  -1868   1457   1729       C  
ATOM   7187  C   ASP B 384       2.894  25.437  31.222  1.00142.70           C  
ANISOU 7187  C   ASP B 384    15673  25797  12750  -1768   1449   2000       C  
ATOM   7188  O   ASP B 384       2.661  26.083  32.244  1.00141.96           O  
ANISOU 7188  O   ASP B 384    15783  25400  12757  -1738   1431   2135       O  
ATOM   7189  CB  ASP B 384       3.338  23.037  31.922  1.00136.98           C  
ANISOU 7189  CB  ASP B 384    14589  25087  12370  -1758   1383   1512       C  
ATOM   7190  CG  ASP B 384       2.056  22.456  31.342  1.00145.38           C  
ANISOU 7190  CG  ASP B 384    15555  26316  13368  -1619   1338   1432       C  
ATOM   7191  OD1 ASP B 384       1.768  22.707  30.146  1.00147.00           O  
ANISOU 7191  OD1 ASP B 384    15703  26805  13344  -1609   1364   1468       O  
ATOM   7192  OD2 ASP B 384       1.371  21.703  32.067  1.00149.13           O  
ANISOU 7192  OD2 ASP B 384    15993  26655  14012  -1533   1279   1324       O  
ATOM   7193  N   SER B 385       2.294  25.677  30.043  1.00141.24           N  
ANISOU 7193  N   SER B 385    15451  25879  12333  -1707   1461   2074       N  
ATOM   7194  CA  SER B 385       1.328  26.752  29.811  1.00142.13           C  
ANISOU 7194  CA  SER B 385    15763  25951  12289  -1583   1454   2344       C  
ATOM   7195  C   SER B 385      -0.053  26.486  30.434  1.00144.83           C  
ANISOU 7195  C   SER B 385    16124  26185  12719  -1378   1373   2335       C  
ATOM   7196  O   SER B 385      -0.703  27.449  30.844  1.00144.67           O  
ANISOU 7196  O   SER B 385    16321  25977  12670  -1269   1364   2555       O  
ATOM   7197  CB  SER B 385       1.171  27.009  28.318  1.00148.13           C  
ANISOU 7197  CB  SER B 385    16449  27077  12758  -1578   1487   2423       C  
ATOM   7198  OG  SER B 385       0.714  25.834  27.675  1.00156.97           O  
ANISOU 7198  OG  SER B 385    17300  28498  13845  -1523   1447   2179       O  
ATOM   7199  N   VAL B 386      -0.513  25.208  30.482  1.00140.34           N  
ANISOU 7199  N   VAL B 386    15334  25737  12253  -1329   1319   2081       N  
ATOM   7200  CA  VAL B 386      -1.833  24.867  31.049  1.00139.10           C  
ANISOU 7200  CA  VAL B 386    15165  25514  12174  -1160   1246   2055       C  
ATOM   7201  C   VAL B 386      -1.809  25.009  32.585  1.00140.44           C  
ANISOU 7201  C   VAL B 386    15487  25296  12579  -1147   1226   2085       C  
ATOM   7202  O   VAL B 386      -2.726  25.610  33.149  1.00139.61           O  
ANISOU 7202  O   VAL B 386    15523  25046  12475  -1009   1199   2229       O  
ATOM   7203  CB  VAL B 386      -2.427  23.495  30.599  1.00142.97           C  
ANISOU 7203  CB  VAL B 386    15384  26249  12687  -1130   1200   1781       C  
ATOM   7204  CG1 VAL B 386      -2.702  23.474  29.100  1.00144.96           C  
ANISOU 7204  CG1 VAL B 386    15496  26911  12670  -1116   1211   1767       C  
ATOM   7205  CG2 VAL B 386      -1.558  22.308  31.005  1.00141.61           C  
ANISOU 7205  CG2 VAL B 386    15069  26007  12731  -1251   1206   1513       C  
ATOM   7206  N   SER B 387      -0.752  24.487  33.245  1.00135.63           N  
ANISOU 7206  N   SER B 387    14843  24537  12152  -1282   1240   1953       N  
ATOM   7207  CA  SER B 387      -0.581  24.579  34.693  1.00133.77           C  
ANISOU 7207  CA  SER B 387    14737  23965  12125  -1292   1220   1972       C  
ATOM   7208  C   SER B 387      -0.198  26.006  35.078  1.00138.54           C  
ANISOU 7208  C   SER B 387    15609  24356  12673  -1330   1264   2213       C  
ATOM   7209  O   SER B 387      -0.592  26.476  36.142  1.00137.51           O  
ANISOU 7209  O   SER B 387    15643  23967  12638  -1270   1246   2299       O  
ATOM   7210  CB  SER B 387       0.469  23.585  35.183  1.00135.87           C  
ANISOU 7210  CB  SER B 387    14869  24177  12578  -1414   1217   1767       C  
ATOM   7211  OG  SER B 387       1.783  23.943  34.787  1.00143.13           O  
ANISOU 7211  OG  SER B 387    15787  25150  13446  -1569   1275   1781       O  
ATOM   7212  N   GLY B 388       0.550  26.672  34.194  1.00136.66           N  
ANISOU 7212  N   GLY B 388    15414  24234  12277  -1435   1327   2313       N  
ATOM   7213  CA  GLY B 388       1.005  28.048  34.363  1.00137.54           C  
ANISOU 7213  CA  GLY B 388    15787  24155  12317  -1506   1384   2543       C  
ATOM   7214  C   GLY B 388       2.116  28.227  35.377  1.00140.32           C  
ANISOU 7214  C   GLY B 388    16221  24273  12822  -1676   1406   2510       C  
ATOM   7215  O   GLY B 388       2.337  29.343  35.855  1.00140.47           O  
ANISOU 7215  O   GLY B 388    16485  24059  12828  -1730   1444   2678       O  
ATOM   7216  N   ILE B 389       2.818  27.129  35.722  1.00135.42           N  
ANISOU 7216  N   ILE B 389    15397  23711  12346  -1756   1381   2290       N  
ATOM   7217  CA  ILE B 389       3.915  27.136  36.696  1.00134.46           C  
ANISOU 7217  CA  ILE B 389    15303  23420  12367  -1909   1388   2235       C  
ATOM   7218  C   ILE B 389       5.095  26.285  36.195  1.00137.98           C  
ANISOU 7218  C   ILE B 389    15505  24087  12834  -2042   1407   2053       C  
ATOM   7219  O   ILE B 389       4.908  25.380  35.376  1.00137.55           O  
ANISOU 7219  O   ILE B 389    15244  24268  12749  -1983   1396   1913       O  
ATOM   7220  CB  ILE B 389       3.461  26.669  38.125  1.00135.75           C  
ANISOU 7220  CB  ILE B 389    15496  23349  12734  -1824   1319   2167       C  
ATOM   7221  CG1 ILE B 389       2.900  25.226  38.133  1.00134.90           C  
ANISOU 7221  CG1 ILE B 389    15162  23356  12738  -1708   1256   1973       C  
ATOM   7222  CG2 ILE B 389       2.491  27.649  38.789  1.00136.50           C  
ANISOU 7222  CG2 ILE B 389    15847  23204  12813  -1714   1313   2340       C  
ATOM   7223  CD1 ILE B 389       3.799  24.223  38.827  1.00141.28           C  
ANISOU 7223  CD1 ILE B 389    15818  24136  13728  -1779   1224   1798       C  
ATOM   7224  N   CYS B 390       6.299  26.566  36.722  1.00134.52           N  
ANISOU 7224  N   CYS B 390    15085  23577  12451  -2217   1434   2043       N  
ATOM   7225  CA  CYS B 390       7.518  25.817  36.431  1.00134.71           C  
ANISOU 7225  CA  CYS B 390    14875  23799  12510  -2336   1452   1871       C  
ATOM   7226  C   CYS B 390       7.670  24.705  37.467  1.00137.42           C  
ANISOU 7226  C   CYS B 390    15088  24048  13079  -2267   1376   1699       C  
ATOM   7227  O   CYS B 390       7.547  24.969  38.665  1.00136.02           O  
ANISOU 7227  O   CYS B 390    15041  23629  13011  -2261   1336   1752       O  
ATOM   7228  CB  CYS B 390       8.733  26.738  36.415  1.00136.35           C  
ANISOU 7228  CB  CYS B 390    15154  24014  12638  -2569   1523   1958       C  
ATOM   7229  SG  CYS B 390       8.944  27.670  34.878  1.00142.64           S  
ANISOU 7229  SG  CYS B 390    16007  25033  13158  -2690   1628   2112       S  
ATOM   7230  N   PHE B 391       7.912  23.464  37.015  1.00134.22           N  
ANISOU 7230  N   PHE B 391    14434  23826  12739  -2209   1358   1494       N  
ATOM   7231  CA  PHE B 391       8.032  22.304  37.897  1.00132.95           C  
ANISOU 7231  CA  PHE B 391    14148  23573  12795  -2125   1289   1336       C  
ATOM   7232  C   PHE B 391       9.067  21.293  37.390  1.00136.74           C  
ANISOU 7232  C   PHE B 391    14362  24266  13326  -2146   1303   1127       C  
ATOM   7233  O   PHE B 391       9.494  21.353  36.236  1.00137.48           O  
ANISOU 7233  O   PHE B 391    14346  24612  13280  -2207   1367   1076       O  
ATOM   7234  CB  PHE B 391       6.656  21.635  38.044  1.00134.03           C  
ANISOU 7234  CB  PHE B 391    14297  23621  13006  -1948   1234   1299       C  
ATOM   7235  CG  PHE B 391       6.422  20.914  39.349  1.00134.76           C  
ANISOU 7235  CG  PHE B 391    14396  23495  13311  -1870   1160   1250       C  
ATOM   7236  CD1 PHE B 391       6.206  21.624  40.527  1.00137.33           C  
ANISOU 7236  CD1 PHE B 391    14912  23590  13679  -1884   1132   1393       C  
ATOM   7237  CD2 PHE B 391       6.362  19.527  39.395  1.00136.99           C  
ANISOU 7237  CD2 PHE B 391    14505  23798  13745  -1779   1122   1065       C  
ATOM   7238  CE1 PHE B 391       5.978  20.956  41.734  1.00137.13           C  
ANISOU 7238  CE1 PHE B 391    14889  23386  13829  -1816   1065   1360       C  
ATOM   7239  CE2 PHE B 391       6.124  18.860  40.601  1.00138.77           C  
ANISOU 7239  CE2 PHE B 391    14750  23816  14160  -1710   1056   1046       C  
ATOM   7240  CZ  PHE B 391       5.941  19.579  41.763  1.00136.01           C  
ANISOU 7240  CZ  PHE B 391    14577  23268  13834  -1730   1027   1198       C  
ATOM   7241  N   VAL B 392       9.466  20.367  38.271  1.00132.39           N  
ANISOU 7241  N   VAL B 392    13710  23618  12973  -2086   1246   1010       N  
ATOM   7242  CA  VAL B 392      10.454  19.322  38.006  1.00133.15           C  
ANISOU 7242  CA  VAL B 392    13559  23871  13159  -2065   1249    807       C  
ATOM   7243  C   VAL B 392       9.834  18.145  37.223  1.00137.42           C  
ANISOU 7243  C   VAL B 392    13960  24502  13750  -1928   1246    618       C  
ATOM   7244  O   VAL B 392       8.720  17.705  37.514  1.00136.00           O  
ANISOU 7244  O   VAL B 392    13850  24173  13650  -1822   1201    615       O  
ATOM   7245  CB  VAL B 392      11.148  18.845  39.325  1.00136.56           C  
ANISOU 7245  CB  VAL B 392    13953  24153  13781  -2040   1182    782       C  
ATOM   7246  CG1 VAL B 392      10.142  18.500  40.422  1.00134.72           C  
ANISOU 7246  CG1 VAL B 392    13853  23639  13693  -1926   1105    842       C  
ATOM   7247  CG2 VAL B 392      12.118  17.686  39.086  1.00137.43           C  
ANISOU 7247  CG2 VAL B 392    13805  24409  14002  -1972   1180    572       C  
ATOM   7248  N   GLY B 393      10.592  17.660  36.244  1.00135.79           N  
ANISOU 7248  N   GLY B 393    13552  24549  13491  -1944   1299    451       N  
ATOM   7249  CA  GLY B 393      10.270  16.491  35.438  1.00136.43           C  
ANISOU 7249  CA  GLY B 393    13473  24745  13621  -1835   1309    224       C  
ATOM   7250  C   GLY B 393       9.099  16.554  34.483  1.00140.84           C  
ANISOU 7250  C   GLY B 393    14069  25402  14042  -1809   1329    213       C  
ATOM   7251  O   GLY B 393       8.467  15.522  34.243  1.00140.35           O  
ANISOU 7251  O   GLY B 393    13931  25321  14074  -1708   1309     42       O  
ATOM   7252  N   TYR B 394       8.811  17.735  33.901  1.00138.18           N  
ANISOU 7252  N   TYR B 394    13843  25180  13479  -1902   1370    390       N  
ATOM   7253  CA  TYR B 394       7.739  17.844  32.905  1.00138.61           C  
ANISOU 7253  CA  TYR B 394    13914  25382  13370  -1870   1385    391       C  
ATOM   7254  C   TYR B 394       8.204  17.188  31.599  1.00144.36           C  
ANISOU 7254  C   TYR B 394    14420  26438  13994  -1883   1447    165       C  
ATOM   7255  O   TYR B 394       7.459  16.405  31.006  1.00144.17           O  
ANISOU 7255  O   TYR B 394    14309  26502  13967  -1808   1437      1       O  
ATOM   7256  CB  TYR B 394       7.321  19.308  32.662  1.00139.97           C  
ANISOU 7256  CB  TYR B 394    14280  25574  13329  -1943   1410    666       C  
ATOM   7257  CG  TYR B 394       6.288  19.885  33.610  1.00140.20           C  
ANISOU 7257  CG  TYR B 394    14530  25327  13413  -1880   1353    858       C  
ATOM   7258  CD1 TYR B 394       5.269  19.091  34.135  1.00141.05           C  
ANISOU 7258  CD1 TYR B 394    14635  25291  13666  -1756   1287    779       C  
ATOM   7259  CD2 TYR B 394       6.259  21.248  33.890  1.00141.03           C  
ANISOU 7259  CD2 TYR B 394    14848  25330  13409  -1947   1372   1114       C  
ATOM   7260  CE1 TYR B 394       4.292  19.628  34.974  1.00140.74           C  
ANISOU 7260  CE1 TYR B 394    14782  25032  13660  -1694   1242    948       C  
ATOM   7261  CE2 TYR B 394       5.286  21.797  34.724  1.00140.84           C  
ANISOU 7261  CE2 TYR B 394    15023  25062  13427  -1872   1326   1276       C  
ATOM   7262  CZ  TYR B 394       4.305  20.983  35.264  1.00147.26           C  
ANISOU 7262  CZ  TYR B 394    15812  25761  14379  -1742   1261   1191       C  
ATOM   7263  OH  TYR B 394       3.348  21.527  36.086  1.00147.56           O  
ANISOU 7263  OH  TYR B 394    16030  25587  14448  -1665   1222   1342       O  
ATOM   7264  N   LYS B 395       9.456  17.484  31.185  1.00142.34           N  
ANISOU 7264  N   LYS B 395    14061  26369  13652  -1986   1512    143       N  
ATOM   7265  CA  LYS B 395      10.090  16.929  29.989  1.00144.15           C  
ANISOU 7265  CA  LYS B 395    14065  26935  13770  -2008   1583    -77       C  
ATOM   7266  C   LYS B 395      10.616  15.522  30.306  1.00148.05           C  
ANISOU 7266  C   LYS B 395    14380  27369  14503  -1898   1565   -360       C  
ATOM   7267  O   LYS B 395      10.154  14.552  29.699  1.00148.57           O  
ANISOU 7267  O   LYS B 395    14335  27515  14600  -1814   1569   -588       O  
ATOM   7268  CB  LYS B 395      11.216  17.860  29.485  1.00148.01           C  
ANISOU 7268  CB  LYS B 395    14517  27653  14067  -2173   1666     28       C  
ATOM   7269  CG  LYS B 395      11.836  17.446  28.151  1.00162.29           C  
ANISOU 7269  CG  LYS B 395    16094  29860  15709  -2212   1753   -176       C  
ATOM   7270  CD  LYS B 395      12.966  18.388  27.732  1.00172.44           C  
ANISOU 7270  CD  LYS B 395    17342  31372  16804  -2398   1841    -57       C  
ATOM   7271  CE  LYS B 395      13.828  17.811  26.626  1.00182.37           C  
ANISOU 7271  CE  LYS B 395    18329  33024  17941  -2427   1930   -301       C  
ATOM   7272  NZ  LYS B 395      14.739  16.737  27.126  1.00188.97           N  
ANISOU 7272  NZ  LYS B 395    18964  33831  19005  -2332   1921   -555       N  
ATOM   7273  N   ASN B 396      11.565  15.414  31.264  1.00143.53           N  
ANISOU 7273  N   ASN B 396    13785  26651  14097  -1895   1544   -346       N  
ATOM   7274  CA  ASN B 396      12.149  14.139  31.676  1.00143.31           C  
ANISOU 7274  CA  ASN B 396    13603  26541  14308  -1768   1522   -580       C  
ATOM   7275  C   ASN B 396      11.383  13.611  32.888  1.00144.52           C  
ANISOU 7275  C   ASN B 396    13893  26316  14703  -1658   1427   -530       C  
ATOM   7276  O   ASN B 396      11.736  13.905  34.033  1.00142.77           O  
ANISOU 7276  O   ASN B 396    13757  25896  14595  -1661   1376   -385       O  
ATOM   7277  CB  ASN B 396      13.654  14.277  31.961  1.00144.77           C  
ANISOU 7277  CB  ASN B 396    13653  26838  14515  -1814   1551   -597       C  
ATOM   7278  CG  ASN B 396      14.456  14.861  30.820  1.00165.67           C  
ANISOU 7278  CG  ASN B 396    16162  29873  16912  -1949   1654   -628       C  
ATOM   7279  OD1 ASN B 396      14.816  16.044  30.819  1.00158.30           O  
ANISOU 7279  OD1 ASN B 396    15310  29023  15815  -2116   1686   -419       O  
ATOM   7280  ND2 ASN B 396      14.755  14.045  29.820  1.00158.82           N  
ANISOU 7280  ND2 ASN B 396    15087  29250  16006  -1888   1713   -894       N  
ATOM   7281  N   TYR B 397      10.312  12.835  32.614  1.00140.60           N  
ANISOU 7281  N   TYR B 397    13413  25740  14270  -1574   1405   -655       N  
ATOM   7282  CA  TYR B 397       9.398  12.246  33.599  1.00138.59           C  
ANISOU 7282  CA  TYR B 397    13281  25153  14225  -1484   1327   -625       C  
ATOM   7283  C   TYR B 397      10.104  11.297  34.587  1.00141.17           C  
ANISOU 7283  C   TYR B 397    13557  25257  14825  -1373   1285   -708       C  
ATOM   7284  O   TYR B 397       9.573  11.060  35.675  1.00139.39           O  
ANISOU 7284  O   TYR B 397    13457  24742  14761  -1324   1216   -605       O  
ATOM   7285  CB  TYR B 397       8.228  11.525  32.897  1.00140.22           C  
ANISOU 7285  CB  TYR B 397    13470  25385  14423  -1445   1330   -789       C  
ATOM   7286  CG  TYR B 397       8.564  10.204  32.229  1.00144.05           C  
ANISOU 7286  CG  TYR B 397    13777  25941  15016  -1368   1367  -1122       C  
ATOM   7287  CD1 TYR B 397       8.219   8.994  32.823  1.00146.12           C  
ANISOU 7287  CD1 TYR B 397    14050  25928  15540  -1266   1329  -1262       C  
ATOM   7288  CD2 TYR B 397       9.161  10.166  30.972  1.00146.72           C  
ANISOU 7288  CD2 TYR B 397    13944  26616  15186  -1400   1447  -1300       C  
ATOM   7289  CE1 TYR B 397       8.505   7.777  32.207  1.00148.70           C  
ANISOU 7289  CE1 TYR B 397    14235  26286  15979  -1190   1370  -1580       C  
ATOM   7290  CE2 TYR B 397       9.455   8.955  30.347  1.00149.43           C  
ANISOU 7290  CE2 TYR B 397    14128  27022  15629  -1321   1488  -1630       C  
ATOM   7291  CZ  TYR B 397       9.124   7.762  30.969  1.00156.37           C  
ANISOU 7291  CZ  TYR B 397    15033  27594  16786  -1213   1450  -1773       C  
ATOM   7292  OH  TYR B 397       9.406   6.562  30.363  1.00159.03           O  
ANISOU 7292  OH  TYR B 397    15233  27956  17234  -1130   1496  -2108       O  
ATOM   7293  N   ARG B 398      11.293  10.773  34.221  1.00138.18           N  
ANISOU 7293  N   ARG B 398    12991  25023  14488  -1327   1325   -882       N  
ATOM   7294  CA  ARG B 398      12.081   9.887  35.080  1.00137.81           C  
ANISOU 7294  CA  ARG B 398    12875  24799  14687  -1196   1286   -956       C  
ATOM   7295  C   ARG B 398      12.616  10.667  36.297  1.00139.46           C  
ANISOU 7295  C   ARG B 398    13172  24895  14920  -1239   1228   -706       C  
ATOM   7296  O   ARG B 398      12.821  10.070  37.354  1.00138.87           O  
ANISOU 7296  O   ARG B 398    13122  24591  15050  -1134   1163   -676       O  
ATOM   7297  CB  ARG B 398      13.216   9.215  34.293  1.00139.94           C  
ANISOU 7297  CB  ARG B 398    12906  25296  14969  -1122   1350  -1211       C  
ATOM   7298  CG  ARG B 398      12.710   8.217  33.268  1.00149.98           C  
ANISOU 7298  CG  ARG B 398    14095  26624  16268  -1056   1400  -1500       C  
ATOM   7299  CD  ARG B 398      13.807   7.339  32.696  1.00161.33           C  
ANISOU 7299  CD  ARG B 398    15306  28214  17778   -935   1459  -1779       C  
ATOM   7300  NE  ARG B 398      13.263   6.312  31.802  1.00170.61           N  
ANISOU 7300  NE  ARG B 398    16424  29399  19002   -870   1505  -2077       N  
ATOM   7301  CZ  ARG B 398      13.226   5.007  32.068  1.00185.80           C  
ANISOU 7301  CZ  ARG B 398    18335  31073  21188   -707   1493  -2276       C  
ATOM   7302  NH1 ARG B 398      13.720   4.538  33.209  1.00174.39           N  
ANISOU 7302  NH1 ARG B 398    16924  29356  19979   -572   1431  -2192       N  
ATOM   7303  NH2 ARG B 398      12.712   4.158  31.187  1.00172.77           N  
ANISOU 7303  NH2 ARG B 398    16639  29445  19560   -681   1545  -2562       N  
ATOM   7304  N   TYR B 399      12.789  12.002  36.155  1.00134.59           N  
ANISOU 7304  N   TYR B 399    12617  24431  14089  -1399   1253   -524       N  
ATOM   7305  CA  TYR B 399      13.213  12.902  37.231  1.00132.96           C  
ANISOU 7305  CA  TYR B 399    12513  24133  13872  -1479   1207   -294       C  
ATOM   7306  C   TYR B 399      12.026  13.268  38.116  1.00133.11           C  
ANISOU 7306  C   TYR B 399    12769  23874  13934  -1487   1144   -105       C  
ATOM   7307  O   TYR B 399      12.210  13.545  39.302  1.00131.68           O  
ANISOU 7307  O   TYR B 399    12678  23525  13831  -1493   1084     41       O  
ATOM   7308  CB  TYR B 399      13.872  14.169  36.672  1.00134.95           C  
ANISOU 7308  CB  TYR B 399    12749  24642  13883  -1664   1272   -190       C  
ATOM   7309  CG  TYR B 399      15.334  13.981  36.336  1.00138.80           C  
ANISOU 7309  CG  TYR B 399    13003  25388  14349  -1679   1315   -317       C  
ATOM   7310  CD1 TYR B 399      16.314  14.072  37.322  1.00141.01           C  
ANISOU 7310  CD1 TYR B 399    13225  25641  14712  -1683   1270   -257       C  
ATOM   7311  CD2 TYR B 399      15.742  13.728  35.032  1.00141.49           C  
ANISOU 7311  CD2 TYR B 399    13164  26027  14570  -1690   1403   -501       C  
ATOM   7312  CE1 TYR B 399      17.664  13.902  37.019  1.00143.88           C  
ANISOU 7312  CE1 TYR B 399    13347  26274  15047  -1692   1309   -377       C  
ATOM   7313  CE2 TYR B 399      17.090  13.562  34.715  1.00144.51           C  
ANISOU 7313  CE2 TYR B 399    13311  26674  14922  -1700   1450   -626       C  
ATOM   7314  CZ  TYR B 399      18.049  13.648  35.713  1.00152.34           C  
ANISOU 7314  CZ  TYR B 399    14239  27639  16004  -1698   1402   -562       C  
ATOM   7315  OH  TYR B 399      19.380  13.480  35.408  1.00155.14           O  
ANISOU 7315  OH  TYR B 399    14338  28285  16324  -1701   1447   -689       O  
ATOM   7316  N   ARG B 400      10.808  13.255  37.543  1.00128.11           N  
ANISOU 7316  N   ARG B 400    12223  23214  13240  -1485   1159   -116       N  
ATOM   7317  CA  ARG B 400       9.565  13.523  38.266  1.00125.91           C  
ANISOU 7317  CA  ARG B 400    12143  22703  12993  -1477   1107     37       C  
ATOM   7318  C   ARG B 400       9.259  12.352  39.211  1.00128.53           C  
ANISOU 7318  C   ARG B 400    12486  22771  13579  -1349   1042    -20       C  
ATOM   7319  O   ARG B 400       8.667  12.564  40.263  1.00126.91           O  
ANISOU 7319  O   ARG B 400    12429  22354  13437  -1344    987    135       O  
ATOM   7320  CB  ARG B 400       8.413  13.759  37.274  1.00126.25           C  
ANISOU 7320  CB  ARG B 400    12232  22850  12889  -1501   1142     19       C  
ATOM   7321  CG  ARG B 400       7.141  14.362  37.871  1.00135.83           C  
ANISOU 7321  CG  ARG B 400    13643  23894  14070  -1507   1103    204       C  
ATOM   7322  CD  ARG B 400       6.286  15.084  36.827  1.00150.63           C  
ANISOU 7322  CD  ARG B 400    15561  25949  15721  -1550   1142    253       C  
ATOM   7323  NE  ARG B 400       5.963  14.272  35.649  1.00164.93           N  
ANISOU 7323  NE  ARG B 400    17223  27951  17491  -1520   1176     34       N  
ATOM   7324  CZ  ARG B 400       4.941  13.421  35.574  1.00180.85           C  
ANISOU 7324  CZ  ARG B 400    19220  29905  19589  -1461   1151    -83       C  
ATOM   7325  NH1 ARG B 400       4.115  13.273  36.602  1.00162.40           N  
ANISOU 7325  NH1 ARG B 400    17003  27326  17377  -1421   1096     12       N  
ATOM   7326  NH2 ARG B 400       4.737  12.714  34.471  1.00174.00           N  
ANISOU 7326  NH2 ARG B 400    18212  29229  18672  -1453   1186   -303       N  
ATOM   7327  N   ALA B 401       9.684  11.127  38.847  1.00125.68           N  
ANISOU 7327  N   ALA B 401    11974  22419  13360  -1246   1053   -240       N  
ATOM   7328  CA  ALA B 401       9.486   9.925  39.661  1.00125.13           C  
ANISOU 7328  CA  ALA B 401    11916  22085  13542  -1120   1000   -299       C  
ATOM   7329  C   ALA B 401      10.360   9.936  40.923  1.00127.32           C  
ANISOU 7329  C   ALA B 401    12205  22237  13936  -1072    937   -170       C  
ATOM   7330  O   ALA B 401       9.904   9.494  41.978  1.00126.86           O  
ANISOU 7330  O   ALA B 401    12250  21929  14024  -1016    875    -77       O  
ATOM   7331  CB  ALA B 401       9.783   8.682  38.841  1.00127.72           C  
ANISOU 7331  CB  ALA B 401    12089  22455  13985  -1019   1039   -578       C  
ATOM   7332  N   GLY B 402      11.591  10.432  40.799  1.00122.65           N  
ANISOU 7332  N   GLY B 402    11497  21839  13264  -1104    953   -166       N  
ATOM   7333  CA  GLY B 402      12.555  10.485  41.894  1.00121.87           C  
ANISOU 7333  CA  GLY B 402    11370  21692  13245  -1067    893    -62       C  
ATOM   7334  C   GLY B 402      12.476  11.705  42.788  1.00122.53           C  
ANISOU 7334  C   GLY B 402    11599  21742  13216  -1197    856    175       C  
ATOM   7335  O   GLY B 402      13.021  11.686  43.896  1.00122.10           O  
ANISOU 7335  O   GLY B 402    11551  21608  13235  -1168    790    276       O  
ATOM   7336  N   PHE B 403      11.813  12.777  42.321  1.00116.74           N  
ANISOU 7336  N   PHE B 403    10985  21071  12300  -1335    898    263       N  
ATOM   7337  CA  PHE B 403      11.699  14.010  43.096  1.00114.82           C  
ANISOU 7337  CA  PHE B 403    10902  20780  11946  -1462    876    473       C  
ATOM   7338  C   PHE B 403      10.247  14.368  43.450  1.00116.34           C  
ANISOU 7338  C   PHE B 403    11304  20784  12118  -1472    862    593       C  
ATOM   7339  O   PHE B 403      10.032  15.289  44.238  1.00115.04           O  
ANISOU 7339  O   PHE B 403    11290  20533  11886  -1550    840    758       O  
ATOM   7340  CB  PHE B 403      12.379  15.174  42.361  1.00117.03           C  
ANISOU 7340  CB  PHE B 403    11155  21296  12016  -1626    943    504       C  
ATOM   7341  CG  PHE B 403      13.885  15.073  42.349  1.00119.81           C  
ANISOU 7341  CG  PHE B 403    11310  21844  12368  -1652    949    431       C  
ATOM   7342  CD1 PHE B 403      14.625  15.322  43.499  1.00122.82           C  
ANISOU 7342  CD1 PHE B 403    11687  22190  12789  -1684    888    523       C  
ATOM   7343  CD2 PHE B 403      14.567  14.742  41.184  1.00123.18           C  
ANISOU 7343  CD2 PHE B 403    11541  22521  12742  -1647   1016    264       C  
ATOM   7344  CE1 PHE B 403      16.018  15.225  43.487  1.00125.28           C  
ANISOU 7344  CE1 PHE B 403    11792  22718  13090  -1706    889    451       C  
ATOM   7345  CE2 PHE B 403      15.962  14.645  41.174  1.00127.37           C  
ANISOU 7345  CE2 PHE B 403    11866  23261  13266  -1664   1025    190       C  
ATOM   7346  CZ  PHE B 403      16.677  14.889  42.325  1.00125.52           C  
ANISOU 7346  CZ  PHE B 403    11621  22995  13074  -1693    959    286       C  
ATOM   7347  N   VAL B 404       9.254  13.645  42.896  1.00111.94           N  
ANISOU 7347  N   VAL B 404    10748  20170  11613  -1396    875    500       N  
ATOM   7348  CA  VAL B 404       7.844  13.905  43.205  1.00109.89           C  
ANISOU 7348  CA  VAL B 404    10657  19765  11333  -1397    862    599       C  
ATOM   7349  C   VAL B 404       7.192  12.604  43.691  1.00113.24           C  
ANISOU 7349  C   VAL B 404    11072  19999  11957  -1286    821    528       C  
ATOM   7350  O   VAL B 404       6.646  12.599  44.793  1.00112.14           O  
ANISOU 7350  O   VAL B 404    11050  19675  11882  -1271    773    653       O  
ATOM   7351  CB  VAL B 404       7.049  14.560  42.041  1.00113.43           C  
ANISOU 7351  CB  VAL B 404    11141  20359  11600  -1449    921    593       C  
ATOM   7352  CG1 VAL B 404       5.686  15.054  42.505  1.00111.86           C  
ANISOU 7352  CG1 VAL B 404    11114  20031  11358  -1444    903    727       C  
ATOM   7353  CG2 VAL B 404       7.830  15.702  41.401  1.00113.86           C  
ANISOU 7353  CG2 VAL B 404    11191  20607  11465  -1563    974    651       C  
ATOM   7354  N   LEU B 405       7.273  11.504  42.905  1.00110.43           N  
ANISOU 7354  N   LEU B 405    10583  19680  11697  -1216    845    328       N  
ATOM   7355  CA  LEU B 405       6.665  10.226  43.293  1.00110.60           C  
ANISOU 7355  CA  LEU B 405    10609  19497  11917  -1128    817    249       C  
ATOM   7356  C   LEU B 405       7.377   9.553  44.473  1.00114.96           C  
ANISOU 7356  C   LEU B 405    11158  19867  12654  -1042    755    306       C  
ATOM   7357  O   LEU B 405       6.700   8.952  45.307  1.00114.93           O  
ANISOU 7357  O   LEU B 405    11244  19648  12778  -1006    716    369       O  
ATOM   7358  CB  LEU B 405       6.581   9.241  42.118  1.00112.04           C  
ANISOU 7358  CB  LEU B 405    10663  19752  12155  -1085    865     -1       C  
ATOM   7359  CG  LEU B 405       5.299   9.255  41.269  1.00116.61           C  
ANISOU 7359  CG  LEU B 405    11265  20403  12639  -1140    901    -77       C  
ATOM   7360  CD1 LEU B 405       5.398   8.252  40.151  1.00118.60           C  
ANISOU 7360  CD1 LEU B 405    11378  20738  12945  -1106    949   -351       C  
ATOM   7361  CD2 LEU B 405       4.064   8.919  42.091  1.00118.32           C  
ANISOU 7361  CD2 LEU B 405    11605  20407  12943  -1146    865     10       C  
ATOM   7362  N   ALA B 406       8.718   9.642  44.542  1.00111.72           N  
ANISOU 7362  N   ALA B 406    10640  19561  12250  -1011    745    290       N  
ATOM   7363  CA  ALA B 406       9.495   9.047  45.633  1.00112.26           C  
ANISOU 7363  CA  ALA B 406    10683  19500  12472   -912    678    354       C  
ATOM   7364  C   ALA B 406       9.180   9.721  46.998  1.00114.96           C  
ANISOU 7364  C   ALA B 406    11175  19727  12778   -965    616    589       C  
ATOM   7365  O   ALA B 406       8.801   8.983  47.918  1.00114.41           O  
ANISOU 7365  O   ALA B 406    11173  19448  12851   -894    566    660       O  
ATOM   7366  CB  ALA B 406      10.986   9.108  45.330  1.00114.41           C  
ANISOU 7366  CB  ALA B 406    10779  19968  12725   -874    683    280       C  
ATOM   7367  N   PRO B 407       9.250  11.079  47.162  1.00110.85           N  
ANISOU 7367  N   PRO B 407    10724  19323  12071  -1092    623    709       N  
ATOM   7368  CA  PRO B 407       8.914  11.667  48.474  1.00109.66           C  
ANISOU 7368  CA  PRO B 407    10720  19058  11889  -1137    568    904       C  
ATOM   7369  C   PRO B 407       7.441  11.502  48.861  1.00112.34           C  
ANISOU 7369  C   PRO B 407    11207  19220  12255  -1138    567    971       C  
ATOM   7370  O   PRO B 407       7.163  11.342  50.050  1.00111.65           O  
ANISOU 7370  O   PRO B 407    11207  18993  12222  -1119    514   1098       O  
ATOM   7371  CB  PRO B 407       9.278  13.146  48.313  1.00110.95           C  
ANISOU 7371  CB  PRO B 407    10929  19378  11849  -1280    597    974       C  
ATOM   7372  CG  PRO B 407       9.251  13.394  46.866  1.00115.76           C  
ANISOU 7372  CG  PRO B 407    11471  20146  12366  -1319    674    853       C  
ATOM   7373  CD  PRO B 407       9.691  12.129  46.216  1.00112.48           C  
ANISOU 7373  CD  PRO B 407    10888  19761  12090  -1203    682    675       C  
ATOM   7374  N   ILE B 408       6.505  11.521  47.879  1.00108.35           N  
ANISOU 7374  N   ILE B 408    10719  18748  11703  -1161    624    887       N  
ATOM   7375  CA  ILE B 408       5.069  11.337  48.150  1.00107.36           C  
ANISOU 7375  CA  ILE B 408    10704  18495  11594  -1167    628    932       C  
ATOM   7376  C   ILE B 408       4.813   9.848  48.489  1.00111.60           C  
ANISOU 7376  C   ILE B 408    11210  18849  12344  -1084    603    870       C  
ATOM   7377  O   ILE B 408       3.970   9.551  49.339  1.00110.95           O  
ANISOU 7377  O   ILE B 408    11224  18615  12317  -1087    580    966       O  
ATOM   7378  CB  ILE B 408       4.153  11.892  47.018  1.00109.93           C  
ANISOU 7378  CB  ILE B 408    11043  18947  11780  -1217    688    871       C  
ATOM   7379  CG1 ILE B 408       4.302  13.429  46.926  1.00109.70           C  
ANISOU 7379  CG1 ILE B 408    11097  19036  11550  -1293    709    985       C  
ATOM   7380  CG2 ILE B 408       2.674  11.518  47.243  1.00109.79           C  
ANISOU 7380  CG2 ILE B 408    11096  18827  11791  -1215    691    890       C  
ATOM   7381  CD1 ILE B 408       3.729  14.094  45.667  1.00118.19           C  
ANISOU 7381  CD1 ILE B 408    12169  20275  12463  -1328    768    941       C  
ATOM   7382  N   GLY B 409       5.587   8.952  47.877  1.00108.77           N  
ANISOU 7382  N   GLY B 409    10724  18501  12103  -1011    612    718       N  
ATOM   7383  CA  GLY B 409       5.524   7.523  48.160  1.00109.49           C  
ANISOU 7383  CA  GLY B 409    10797  18391  12415   -920    594    654       C  
ATOM   7384  C   GLY B 409       5.984   7.245  49.579  1.00112.97           C  
ANISOU 7384  C   GLY B 409    11292  18682  12949   -861    521    825       C  
ATOM   7385  O   GLY B 409       5.349   6.473  50.307  1.00113.26           O  
ANISOU 7385  O   GLY B 409    11411  18513  13111   -839    499    894       O  
ATOM   7386  N   LEU B 410       7.067   7.943  49.995  1.00108.01           N  
ANISOU 7386  N   LEU B 410    10620  18178  12242   -852    484    905       N  
ATOM   7387  CA  LEU B 410       7.660   7.862  51.327  1.00107.17           C  
ANISOU 7387  CA  LEU B 410    10543  17999  12179   -802    406   1072       C  
ATOM   7388  C   LEU B 410       6.715   8.429  52.404  1.00108.47           C  
ANISOU 7388  C   LEU B 410    10868  18083  12264   -884    382   1255       C  
ATOM   7389  O   LEU B 410       6.498   7.746  53.407  1.00108.74           O  
ANISOU 7389  O   LEU B 410    10962  17954  12400   -835    335   1370       O  
ATOM   7390  CB  LEU B 410       9.019   8.588  51.363  1.00107.31           C  
ANISOU 7390  CB  LEU B 410    10452  18224  12098   -805    380   1082       C  
ATOM   7391  CG  LEU B 410       9.785   8.533  52.694  1.00112.20           C  
ANISOU 7391  CG  LEU B 410    11066  18827  12739   -752    290   1240       C  
ATOM   7392  CD1 LEU B 410      10.579   7.227  52.842  1.00114.24           C  
ANISOU 7392  CD1 LEU B 410    11213  19000  13192   -564    247   1203       C  
ATOM   7393  CD2 LEU B 410      10.679   9.749  52.851  1.00114.06           C  
ANISOU 7393  CD2 LEU B 410    11250  19290  12797   -851    275   1278       C  
ATOM   7394  N   VAL B 411       6.136   9.645  52.197  1.00102.34           N  
ANISOU 7394  N   VAL B 411    10164  17415  11306  -1001    417   1286       N  
ATOM   7395  CA  VAL B 411       5.232  10.266  53.185  1.00100.64           C  
ANISOU 7395  CA  VAL B 411    10095  17140  11002  -1069    403   1441       C  
ATOM   7396  C   VAL B 411       3.975   9.394  53.392  1.00103.09           C  
ANISOU 7396  C   VAL B 411    10471  17282  11415  -1058    419   1453       C  
ATOM   7397  O   VAL B 411       3.418   9.399  54.491  1.00102.57           O  
ANISOU 7397  O   VAL B 411    10502  17130  11340  -1078    391   1594       O  
ATOM   7398  CB  VAL B 411       4.866  11.762  52.933  1.00103.20           C  
ANISOU 7398  CB  VAL B 411    10498  17593  11122  -1173    442   1470       C  
ATOM   7399  CG1 VAL B 411       6.104  12.656  52.938  1.00103.11           C  
ANISOU 7399  CG1 VAL B 411    10444  17725  11007  -1219    428   1480       C  
ATOM   7400  CG2 VAL B 411       4.041  11.962  51.666  1.00102.55           C  
ANISOU 7400  CG2 VAL B 411    10407  17572  10985  -1198    513   1359       C  
ATOM   7401  N   LEU B 412       3.569   8.620  52.362  1.00 98.69           N  
ANISOU 7401  N   LEU B 412     9855  16691  10951  -1039    464   1300       N  
ATOM   7402  CA  LEU B 412       2.437   7.702  52.465  1.00 98.30           C  
ANISOU 7402  CA  LEU B 412     9853  16487  11010  -1053    484   1285       C  
ATOM   7403  C   LEU B 412       2.786   6.515  53.357  1.00102.34           C  
ANISOU 7403  C   LEU B 412    10385  16791  11709   -980    438   1361       C  
ATOM   7404  O   LEU B 412       1.926   6.042  54.102  1.00102.51           O  
ANISOU 7404  O   LEU B 412    10493  16674  11781  -1016    435   1459       O  
ATOM   7405  CB  LEU B 412       1.994   7.199  51.086  1.00 98.84           C  
ANISOU 7405  CB  LEU B 412     9845  16591  11119  -1066    544   1077       C  
ATOM   7406  CG  LEU B 412       1.062   8.092  50.271  1.00102.54           C  
ANISOU 7406  CG  LEU B 412    10317  17229  11413  -1144    594   1025       C  
ATOM   7407  CD1 LEU B 412       0.853   7.506  48.900  1.00103.93           C  
ANISOU 7407  CD1 LEU B 412    10393  17469  11626  -1151    644    806       C  
ATOM   7408  CD2 LEU B 412      -0.288   8.254  50.938  1.00103.43           C  
ANISOU 7408  CD2 LEU B 412    10522  17298  11479  -1207    602   1128       C  
ATOM   7409  N   ILE B 413       4.045   6.039  53.284  1.00 98.48           N  
ANISOU 7409  N   ILE B 413     9813  16287  11318   -873    403   1325       N  
ATOM   7410  CA  ILE B 413       4.522   4.910  54.082  1.00 99.29           C  
ANISOU 7410  CA  ILE B 413     9931  16193  11603   -767    353   1409       C  
ATOM   7411  C   ILE B 413       4.704   5.353  55.546  1.00102.61           C  
ANISOU 7411  C   ILE B 413    10425  16616  11946   -771    284   1644       C  
ATOM   7412  O   ILE B 413       4.135   4.717  56.440  1.00103.18           O  
ANISOU 7412  O   ILE B 413    10591  16521  12093   -775    265   1779       O  
ATOM   7413  CB  ILE B 413       5.819   4.279  53.489  1.00103.67           C  
ANISOU 7413  CB  ILE B 413    10356  16755  12280   -623    339   1285       C  
ATOM   7414  CG1 ILE B 413       5.559   3.698  52.081  1.00104.57           C  
ANISOU 7414  CG1 ILE B 413    10405  16851  12478   -621    414   1035       C  
ATOM   7415  CG2 ILE B 413       6.384   3.194  54.424  1.00106.24           C  
ANISOU 7415  CG2 ILE B 413    10704  16878  12785   -481    276   1407       C  
ATOM   7416  CD1 ILE B 413       6.786   3.545  51.193  1.00111.00           C  
ANISOU 7416  CD1 ILE B 413    11063  17786  13327   -510    424    866       C  
ATOM   7417  N   VAL B 414       5.473   6.441  55.779  1.00 97.95           N  
ANISOU 7417  N   VAL B 414     9795  16223  11200   -787    250   1689       N  
ATOM   7418  CA  VAL B 414       5.780   6.967  57.118  1.00 97.61           C  
ANISOU 7418  CA  VAL B 414     9804  16227  11057   -801    182   1883       C  
ATOM   7419  C   VAL B 414       4.506   7.514  57.800  1.00101.23           C  
ANISOU 7419  C   VAL B 414    10400  16659  11404   -917    205   1990       C  
ATOM   7420  O   VAL B 414       4.192   7.096  58.922  1.00101.56           O  
ANISOU 7420  O   VAL B 414    10516  16604  11467   -911    168   2150       O  
ATOM   7421  CB  VAL B 414       6.913   8.025  57.119  1.00100.93           C  
ANISOU 7421  CB  VAL B 414    10143  16872  11333   -819    150   1873       C  
ATOM   7422  CG1 VAL B 414       7.366   8.331  58.545  1.00100.89           C  
ANISOU 7422  CG1 VAL B 414    10172  16915  11247   -820     67   2056       C  
ATOM   7423  CG2 VAL B 414       8.103   7.564  56.281  1.00102.14           C  
ANISOU 7423  CG2 VAL B 414    10135  17096  11577   -714    143   1739       C  
ATOM   7424  N   GLY B 415       3.803   8.422  57.116  1.00 96.19           N  
ANISOU 7424  N   GLY B 415     9788  16117  10643  -1009    268   1906       N  
ATOM   7425  CA  GLY B 415       2.566   9.018  57.610  1.00 94.66           C  
ANISOU 7425  CA  GLY B 415     9705  15925  10335  -1099    300   1980       C  
ATOM   7426  C   GLY B 415       1.505   7.979  57.912  1.00 98.67           C  
ANISOU 7426  C   GLY B 415    10264  16270  10958  -1111    321   2021       C  
ATOM   7427  O   GLY B 415       0.869   8.030  58.972  1.00 98.49           O  
ANISOU 7427  O   GLY B 415    10325  16213  10883  -1153    311   2162       O  
ATOM   7428  N   GLY B 416       1.366   7.017  56.992  1.00 95.23           N  
ANISOU 7428  N   GLY B 416     9773  15735  10674  -1084    353   1892       N  
ATOM   7429  CA  GLY B 416       0.442   5.892  57.099  1.00 95.66           C  
ANISOU 7429  CA  GLY B 416     9869  15612  10865  -1115    382   1898       C  
ATOM   7430  C   GLY B 416       0.719   5.021  58.308  1.00 99.85           C  
ANISOU 7430  C   GLY B 416    10460  15974  11503  -1071    330   2077       C  
ATOM   7431  O   GLY B 416      -0.210   4.681  59.047  1.00100.21           O  
ANISOU 7431  O   GLY B 416    10587  15937  11551  -1144    346   2189       O  
ATOM   7432  N   TYR B 417       2.012   4.698  58.541  1.00 95.62           N  
ANISOU 7432  N   TYR B 417     9880  15410  11042   -951    266   2115       N  
ATOM   7433  CA  TYR B 417       2.462   3.888  59.677  1.00 96.23           C  
ANISOU 7433  CA  TYR B 417    10006  15346  11213   -875    202   2303       C  
ATOM   7434  C   TYR B 417       2.026   4.507  61.009  1.00 98.45           C  
ANISOU 7434  C   TYR B 417    10370  15704  11332   -946    172   2506       C  
ATOM   7435  O   TYR B 417       1.492   3.794  61.857  1.00 99.06           O  
ANISOU 7435  O   TYR B 417    10531  15644  11462   -969    166   2659       O  
ATOM   7436  CB  TYR B 417       3.993   3.691  59.656  1.00 98.24           C  
ANISOU 7436  CB  TYR B 417    10165  15633  11528   -718    132   2302       C  
ATOM   7437  CG  TYR B 417       4.544   2.968  60.871  1.00101.65           C  
ANISOU 7437  CG  TYR B 417    10637  15959  12029   -615     51   2520       C  
ATOM   7438  CD1 TYR B 417       4.419   1.587  61.003  1.00105.87           C  
ANISOU 7438  CD1 TYR B 417    11228  16220  12777   -536     53   2577       C  
ATOM   7439  CD2 TYR B 417       5.199   3.662  61.884  1.00102.14           C  
ANISOU 7439  CD2 TYR B 417    10681  16191  11936   -598    -28   2671       C  
ATOM   7440  CE1 TYR B 417       4.907   0.919  62.128  1.00108.92           C  
ANISOU 7440  CE1 TYR B 417    11661  16504  13219   -429    -23   2805       C  
ATOM   7441  CE2 TYR B 417       5.696   3.005  63.010  1.00104.87           C  
ANISOU 7441  CE2 TYR B 417    11054  16468  12322   -497   -109   2884       C  
ATOM   7442  CZ  TYR B 417       5.550   1.632  63.127  1.00115.48           C  
ANISOU 7442  CZ  TYR B 417    12460  17538  13878   -404   -108   2963       C  
ATOM   7443  OH  TYR B 417       6.030   0.978  64.238  1.00119.53           O  
ANISOU 7443  OH  TYR B 417    13010  17980  14427   -291   -190   3199       O  
ATOM   7444  N   PHE B 418       2.240   5.824  61.186  1.00 92.65           N  
ANISOU 7444  N   PHE B 418     9620  15186  10398   -988    159   2503       N  
ATOM   7445  CA  PHE B 418       1.876   6.524  62.421  1.00 91.44           C  
ANISOU 7445  CA  PHE B 418     9543  15129  10073  -1054    135   2663       C  
ATOM   7446  C   PHE B 418       0.368   6.629  62.596  1.00 94.43           C  
ANISOU 7446  C   PHE B 418    10001  15485  10395  -1169    206   2681       C  
ATOM   7447  O   PHE B 418      -0.109   6.591  63.733  1.00 94.48           O  
ANISOU 7447  O   PHE B 418    10079  15493  10327  -1213    195   2841       O  
ATOM   7448  CB  PHE B 418       2.524   7.909  62.478  1.00 91.82           C  
ANISOU 7448  CB  PHE B 418     9562  15390   9935  -1077    112   2624       C  
ATOM   7449  CG  PHE B 418       4.029   7.874  62.604  1.00 93.95           C  
ANISOU 7449  CG  PHE B 418     9741  15734  10223   -986     31   2638       C  
ATOM   7450  CD1 PHE B 418       4.658   6.927  63.411  1.00 98.30           C  
ANISOU 7450  CD1 PHE B 418    10274  16210  10864   -887    -45   2784       C  
ATOM   7451  CD2 PHE B 418       4.818   8.806  61.942  1.00 95.13           C  
ANISOU 7451  CD2 PHE B 418     9817  16039  10289  -1001     32   2514       C  
ATOM   7452  CE1 PHE B 418       6.047   6.889  63.515  1.00 99.84           C  
ANISOU 7452  CE1 PHE B 418    10361  16506  11069   -787   -124   2794       C  
ATOM   7453  CE2 PHE B 418       6.208   8.777  62.061  1.00 98.67           C  
ANISOU 7453  CE2 PHE B 418    10158  16589  10744   -928    -40   2519       C  
ATOM   7454  CZ  PHE B 418       6.812   7.821  62.848  1.00 98.29           C  
ANISOU 7454  CZ  PHE B 418    10075  16487  10786   -815   -120   2654       C  
ATOM   7455  N   LEU B 419      -0.381   6.724  61.475  1.00 90.02           N  
ANISOU 7455  N   LEU B 419     9418  14925   9862  -1214    280   2518       N  
ATOM   7456  CA  LEU B 419      -1.843   6.783  61.498  1.00 89.25           C  
ANISOU 7456  CA  LEU B 419     9364  14834   9713  -1317    350   2512       C  
ATOM   7457  C   LEU B 419      -2.435   5.420  61.854  1.00 93.61           C  
ANISOU 7457  C   LEU B 419     9954  15192  10421  -1358    367   2590       C  
ATOM   7458  O   LEU B 419      -3.401   5.371  62.613  1.00 93.13           O  
ANISOU 7458  O   LEU B 419     9949  15142  10294  -1446    398   2694       O  
ATOM   7459  CB  LEU B 419      -2.409   7.287  60.161  1.00 88.29           C  
ANISOU 7459  CB  LEU B 419     9187  14799   9559  -1345    413   2318       C  
ATOM   7460  CG  LEU B 419      -2.368   8.801  59.943  1.00 91.41           C  
ANISOU 7460  CG  LEU B 419     9587  15384   9761  -1342    424   2274       C  
ATOM   7461  CD1 LEU B 419      -2.461   9.138  58.480  1.00 91.14           C  
ANISOU 7461  CD1 LEU B 419     9484  15421   9723  -1333    466   2094       C  
ATOM   7462  CD2 LEU B 419      -3.483   9.506  60.696  1.00 93.09           C  
ANISOU 7462  CD2 LEU B 419     9865  15686   9817  -1401    460   2351       C  
ATOM   7463  N   ILE B 420      -1.849   4.323  61.327  1.00 91.61           N  
ANISOU 7463  N   ILE B 420     9677  14759  10373  -1296    354   2539       N  
ATOM   7464  CA  ILE B 420      -2.289   2.952  61.616  1.00 93.57           C  
ANISOU 7464  CA  ILE B 420     9982  14771  10798  -1334    373   2611       C  
ATOM   7465  C   ILE B 420      -1.935   2.611  63.081  1.00 98.35           C  
ANISOU 7465  C   ILE B 420    10668  15312  11388  -1303    313   2872       C  
ATOM   7466  O   ILE B 420      -2.812   2.162  63.822  1.00 98.66           O  
ANISOU 7466  O   ILE B 420    10782  15285  11420  -1405    344   3004       O  
ATOM   7467  CB  ILE B 420      -1.714   1.913  60.603  1.00 98.15           C  
ANISOU 7467  CB  ILE B 420    10525  15159  11607  -1259    380   2463       C  
ATOM   7468  CG1 ILE B 420      -2.286   2.148  59.182  1.00 97.88           C  
ANISOU 7468  CG1 ILE B 420    10413  15205  11570  -1321    449   2207       C  
ATOM   7469  CG2 ILE B 420      -1.990   0.464  61.070  1.00101.15           C  
ANISOU 7469  CG2 ILE B 420    10998  15244  12188  -1283    393   2569       C  
ATOM   7470  CD1 ILE B 420      -1.416   1.616  58.018  1.00106.40           C  
ANISOU 7470  CD1 ILE B 420    11419  16206  12802  -1219    449   2011       C  
ATOM   7471  N   ARG B 421      -0.670   2.865  63.501  1.00 94.76           N  
ANISOU 7471  N   ARG B 421    10188  14908  10908  -1172    228   2948       N  
ATOM   7472  CA  ARG B 421      -0.182   2.618  64.866  1.00 95.54           C  
ANISOU 7472  CA  ARG B 421    10343  14993  10966  -1123    155   3196       C  
ATOM   7473  C   ARG B 421      -0.979   3.460  65.901  1.00 98.47           C  
ANISOU 7473  C   ARG B 421    10765  15541  11109  -1239    168   3317       C  
ATOM   7474  O   ARG B 421      -1.199   2.997  67.023  1.00 98.83           O  
ANISOU 7474  O   ARG B 421    10883  15543  11125  -1266    147   3528       O  
ATOM   7475  CB  ARG B 421       1.338   2.895  64.957  1.00 94.79           C  
ANISOU 7475  CB  ARG B 421    10172  14986  10859   -966     60   3211       C  
ATOM   7476  CG  ARG B 421       2.038   2.435  66.250  1.00106.90           C  
ANISOU 7476  CG  ARG B 421    11739  16501  12376   -876    -33   3464       C  
ATOM   7477  CD  ARG B 421       2.036   0.931  66.497  1.00122.23           C  
ANISOU 7477  CD  ARG B 421    13756  18152  14535   -804    -41   3603       C  
ATOM   7478  NE  ARG B 421       2.841   0.190  65.522  1.00136.95           N  
ANISOU 7478  NE  ARG B 421    15562  19856  16618   -654    -50   3471       N  
ATOM   7479  CZ  ARG B 421       3.020  -1.128  65.543  1.00158.66           C  
ANISOU 7479  CZ  ARG B 421    18374  22317  19590   -553    -55   3552       C  
ATOM   7480  NH1 ARG B 421       2.460  -1.868  66.495  1.00148.29           N  
ANISOU 7480  NH1 ARG B 421    17192  20839  18312   -598    -54   3786       N  
ATOM   7481  NH2 ARG B 421       3.762  -1.716  64.615  1.00149.73           N  
ANISOU 7481  NH2 ARG B 421    17182  21059  18648   -406    -57   3401       N  
ATOM   7482  N   GLY B 422      -1.441   4.644  65.478  1.00 93.28           N  
ANISOU 7482  N   GLY B 422    10075  15072  10297  -1302    210   3180       N  
ATOM   7483  CA  GLY B 422      -2.228   5.576  66.284  1.00 92.08           C  
ANISOU 7483  CA  GLY B 422     9963  15097   9927  -1395    237   3242       C  
ATOM   7484  C   GLY B 422      -3.585   5.041  66.687  1.00 96.12           C  
ANISOU 7484  C   GLY B 422    10527  15555  10438  -1518    309   3316       C  
ATOM   7485  O   GLY B 422      -3.915   5.030  67.880  1.00 96.67           O  
ANISOU 7485  O   GLY B 422    10652  15680  10396  -1568    302   3491       O  
ATOM   7486  N   VAL B 423      -4.381   4.574  65.692  1.00 91.93           N  
ANISOU 7486  N   VAL B 423     9971  14937  10023  -1579    381   3178       N  
ATOM   7487  CA  VAL B 423      -5.710   3.994  65.941  1.00 92.52           C  
ANISOU 7487  CA  VAL B 423    10075  14970  10109  -1721    458   3223       C  
ATOM   7488  C   VAL B 423      -5.555   2.650  66.654  1.00 98.85           C  
ANISOU 7488  C   VAL B 423    10955  15545  11057  -1745    440   3414       C  
ATOM   7489  O   VAL B 423      -6.415   2.294  67.458  1.00 99.79           O  
ANISOU 7489  O   VAL B 423    11125  15666  11126  -1865    482   3552       O  
ATOM   7490  CB  VAL B 423      -6.644   3.871  64.702  1.00 95.88           C  
ANISOU 7490  CB  VAL B 423    10436  15394  10598  -1798    538   3015       C  
ATOM   7491  CG1 VAL B 423      -7.217   5.222  64.295  1.00 93.86           C  
ANISOU 7491  CG1 VAL B 423    10123  15388  10152  -1796    572   2889       C  
ATOM   7492  CG2 VAL B 423      -5.962   3.182  63.524  1.00 96.07           C  
ANISOU 7492  CG2 VAL B 423    10425  15248  10828  -1734    525   2865       C  
ATOM   7493  N   MET B 424      -4.446   1.925  66.382  1.00 95.75           N  
ANISOU 7493  N   MET B 424    10574  14965  10841  -1625    379   3431       N  
ATOM   7494  CA  MET B 424      -4.139   0.645  67.024  1.00 97.73           C  
ANISOU 7494  CA  MET B 424    10915  14970  11249  -1606    352   3627       C  
ATOM   7495  C   MET B 424      -3.971   0.837  68.535  1.00101.36           C  
ANISOU 7495  C   MET B 424    11433  15531  11548  -1602    300   3894       C  
ATOM   7496  O   MET B 424      -4.464   0.016  69.314  1.00102.75           O  
ANISOU 7496  O   MET B 424    11698  15585  11758  -1685    322   4089       O  
ATOM   7497  CB  MET B 424      -2.883   0.011  66.412  1.00100.88           C  
ANISOU 7497  CB  MET B 424    11297  15186  11847  -1432    291   3575       C  
ATOM   7498  CG  MET B 424      -3.171  -0.796  65.178  1.00105.29           C  
ANISOU 7498  CG  MET B 424    11846  15537  12624  -1460    354   3375       C  
ATOM   7499  SD  MET B 424      -1.676  -1.525  64.473  1.00110.95           S  
ANISOU 7499  SD  MET B 424    12533  16053  13568  -1232    290   3296       S  
ATOM   7500  CE  MET B 424      -1.899  -3.221  64.962  1.00111.35           C  
ANISOU 7500  CE  MET B 424    12740  15701  13867  -1249    312   3472       C  
ATOM   7501  N   THR B 425      -3.325   1.954  68.937  1.00 95.42           N  
ANISOU 7501  N   THR B 425    10633  15015  10609  -1526    238   3895       N  
ATOM   7502  CA  THR B 425      -3.116   2.318  70.340  1.00 94.99           C  
ANISOU 7502  CA  THR B 425    10615  15114  10362  -1525    185   4112       C  
ATOM   7503  C   THR B 425      -4.464   2.708  70.961  1.00 97.57           C  
ANISOU 7503  C   THR B 425    10972  15582  10518  -1694    268   4155       C  
ATOM   7504  O   THR B 425      -4.746   2.307  72.092  1.00 98.90           O  
ANISOU 7504  O   THR B 425    11205  15766  10606  -1753    264   4379       O  
ATOM   7505  CB  THR B 425      -2.066   3.439  70.465  1.00 97.76           C  
ANISOU 7505  CB  THR B 425    10899  15679  10565  -1420    104   4052       C  
ATOM   7506  OG1 THR B 425      -0.902   3.085  69.716  1.00 97.85           O  
ANISOU 7506  OG1 THR B 425    10856  15584  10740  -1272     42   3977       O  
ATOM   7507  CG2 THR B 425      -1.666   3.707  71.912  1.00 95.63           C  
ANISOU 7507  CG2 THR B 425    10660  15572  10104  -1408     33   4269       C  
ATOM   7508  N   LEU B 426      -5.296   3.468  70.213  1.00 91.18           N  
ANISOU 7508  N   LEU B 426    10110  14886   9648  -1765    345   3948       N  
ATOM   7509  CA  LEU B 426      -6.614   3.927  70.665  1.00 90.06           C  
ANISOU 7509  CA  LEU B 426     9969  14909   9341  -1905    431   3951       C  
ATOM   7510  C   LEU B 426      -7.572   2.764  70.888  1.00 96.51           C  
ANISOU 7510  C   LEU B 426    10830  15580  10258  -2051    501   4064       C  
ATOM   7511  O   LEU B 426      -8.107   2.640  71.987  1.00 97.57           O  
ANISOU 7511  O   LEU B 426    11007  15800  10264  -2143    525   4242       O  
ATOM   7512  CB  LEU B 426      -7.224   4.933  69.667  1.00 87.36           C  
ANISOU 7512  CB  LEU B 426     9550  14705   8936  -1912    490   3702       C  
ATOM   7513  CG  LEU B 426      -8.669   5.375  69.928  1.00 90.48           C  
ANISOU 7513  CG  LEU B 426     9920  15276   9181  -2033    587   3671       C  
ATOM   7514  CD1 LEU B 426      -8.761   6.313  71.130  1.00 90.05           C  
ANISOU 7514  CD1 LEU B 426     9892  15446   8876  -2029    581   3761       C  
ATOM   7515  CD2 LEU B 426      -9.269   6.007  68.701  1.00 90.17           C  
ANISOU 7515  CD2 LEU B 426     9801  15314   9145  -2023    641   3435       C  
ATOM   7516  N   PHE B 427      -7.780   1.920  69.860  1.00 94.00           N  
ANISOU 7516  N   PHE B 427    10505  15051  10162  -2085    538   3954       N  
ATOM   7517  CA  PHE B 427      -8.696   0.788  69.920  1.00 96.35           C  
ANISOU 7517  CA  PHE B 427    10848  15184  10577  -2251    614   4027       C  
ATOM   7518  C   PHE B 427      -8.223  -0.309  70.884  1.00103.10           C  
ANISOU 7518  C   PHE B 427    11824  15827  11522  -2253    575   4309       C  
ATOM   7519  O   PHE B 427      -9.075  -1.006  71.433  1.00105.11           O  
ANISOU 7519  O   PHE B 427    12135  16020  11780  -2421    642   4447       O  
ATOM   7520  CB  PHE B 427      -8.972   0.221  68.522  1.00 98.50           C  
ANISOU 7520  CB  PHE B 427    11080  15289  11056  -2290    661   3806       C  
ATOM   7521  CG  PHE B 427      -9.992   1.045  67.762  1.00 98.98           C  
ANISOU 7521  CG  PHE B 427    11027  15578  11004  -2365    731   3585       C  
ATOM   7522  CD1 PHE B 427     -11.354   0.900  68.009  1.00103.27           C  
ANISOU 7522  CD1 PHE B 427    11538  16232  11469  -2556    824   3594       C  
ATOM   7523  CD2 PHE B 427      -9.590   1.997  66.831  1.00 99.23           C  
ANISOU 7523  CD2 PHE B 427    10977  15734  10994  -2241    704   3381       C  
ATOM   7524  CE1 PHE B 427     -12.293   1.675  67.323  1.00102.83           C  
ANISOU 7524  CE1 PHE B 427    11360  16412  11298  -2600    882   3398       C  
ATOM   7525  CE2 PHE B 427     -10.533   2.770  66.145  1.00100.80           C  
ANISOU 7525  CE2 PHE B 427    11074  16147  11079  -2288    764   3200       C  
ATOM   7526  CZ  PHE B 427     -11.877   2.596  66.388  1.00 99.64           C  
ANISOU 7526  CZ  PHE B 427    10886  16113  10859  -2456    849   3208       C  
ATOM   7527  N   SER B 428      -6.895  -0.437  71.126  1.00 99.45           N  
ANISOU 7527  N   SER B 428    11396  15274  11116  -2070    469   4406       N  
ATOM   7528  CA  SER B 428      -6.366  -1.412  72.090  1.00101.50           C  
ANISOU 7528  CA  SER B 428    11769  15353  11442  -2033    418   4700       C  
ATOM   7529  C   SER B 428      -6.694  -0.949  73.511  1.00104.25           C  
ANISOU 7529  C   SER B 428    12143  15940  11529  -2100    411   4921       C  
ATOM   7530  O   SER B 428      -7.242  -1.723  74.303  1.00106.65           O  
ANISOU 7530  O   SER B 428    12536  16160  11828  -2223    450   5145       O  
ATOM   7531  CB  SER B 428      -4.863  -1.606  71.914  1.00105.80           C  
ANISOU 7531  CB  SER B 428    12314  15783  12103  -1799    303   4726       C  
ATOM   7532  OG  SER B 428      -4.360  -2.528  72.867  1.00119.47           O  
ANISOU 7532  OG  SER B 428    14152  17353  13888  -1738    247   5028       O  
ATOM   7533  N   ALA B1011      -6.401   0.337  73.800  1.00 97.25           N  
ANISOU 7533  N   ALA B1011    11584  14355  11010  -2343   -497   1692       N  
ATOM   7534  CA  ALA B1011      -6.656   0.991  75.080  1.00 94.12           C  
ANISOU 7534  CA  ALA B1011    11186  13496  11079  -2145   -542   1756       C  
ATOM   7535  C   ALA B1011      -8.152   0.997  75.413  1.00 95.64           C  
ANISOU 7535  C   ALA B1011    11358  13592  11388  -2147   -656   1872       C  
ATOM   7536  O   ALA B1011      -8.533   0.687  76.543  1.00 93.17           O  
ANISOU 7536  O   ALA B1011    11175  12931  11293  -2012   -636   1662       O  
ATOM   7537  CB  ALA B1011      -6.116   2.414  75.060  1.00 95.74           C  
ANISOU 7537  CB  ALA B1011    11216  13597  11565  -2116   -546   2114       C  
ATOM   7538  N   ARG B1012      -8.988   1.295  74.414  1.00 93.02           N  
ANISOU 7538  N   ARG B1012    10843  13611  10889  -2322   -776   2231       N  
ATOM   7539  CA  ARG B1012     -10.429   1.344  74.573  1.00 92.72           C  
ANISOU 7539  CA  ARG B1012    10706  13556  10969  -2344   -895   2450       C  
ATOM   7540  C   ARG B1012     -11.034  -0.055  74.748  1.00 95.18           C  
ANISOU 7540  C   ARG B1012    11218  13942  11004  -2425   -916   2056       C  
ATOM   7541  O   ARG B1012     -12.040  -0.181  75.450  1.00 93.93           O  
ANISOU 7541  O   ARG B1012    11059  13572  11057  -2346   -962   2075       O  
ATOM   7542  CB  ARG B1012     -11.077   2.067  73.403  1.00 96.57           C  
ANISOU 7542  CB  ARG B1012    10874  14470  11348  -2540  -1045   3045       C  
ATOM   7543  CG  ARG B1012     -12.290   2.849  73.845  1.00110.99           C  
ANISOU 7543  CG  ARG B1012    12468  16072  13633  -2424  -1100   3496       C  
ATOM   7544  CD  ARG B1012     -13.085   3.359  72.655  1.00129.87           C  
ANISOU 7544  CD  ARG B1012    14484  18970  15891  -2648  -1289   4165       C  
ATOM   7545  NE  ARG B1012     -12.655   4.707  72.286  1.00141.64           N  
ANISOU 7545  NE  ARG B1012    15711  20400  17706  -2575  -1241   4685       N  
ATOM   7546  CZ  ARG B1012     -13.340   5.818  72.514  1.00160.47           C  
ANISOU 7546  CZ  ARG B1012    17792  22508  20672  -2412  -1192   5255       C  
ATOM   7547  NH1 ARG B1012     -14.571   5.758  73.012  1.00156.51           N  
ANISOU 7547  NH1 ARG B1012    17166  21836  20465  -2318  -1204   5442       N  
ATOM   7548  NH2 ARG B1012     -12.834   6.993  72.178  1.00144.51           N  
ANISOU 7548  NH2 ARG B1012    15561  20387  18961  -2351  -1109   5686       N  
ATOM   7549  N   ARG B1013     -10.430  -1.096  74.124  1.00 92.20           N  
ANISOU 7549  N   ARG B1013    11013  13830  10189  -2585   -841   1694       N  
ATOM   7550  CA  ARG B1013     -10.936  -2.462  74.284  1.00 91.90           C  
ANISOU 7550  CA  ARG B1013    11191  13805   9921  -2679   -805   1282       C  
ATOM   7551  C   ARG B1013     -10.551  -3.013  75.649  1.00 93.43           C  
ANISOU 7551  C   ARG B1013    11584  13492  10422  -2395   -679    913       C  
ATOM   7552  O   ARG B1013     -11.389  -3.651  76.286  1.00 92.63           O  
ANISOU 7552  O   ARG B1013    11578  13229  10391  -2366   -710    762       O  
ATOM   7553  CB  ARG B1013     -10.469  -3.423  73.178  1.00 95.01           C  
ANISOU 7553  CB  ARG B1013    11730  14586   9782  -2970   -682    979       C  
ATOM   7554  CG  ARG B1013     -11.304  -4.710  73.127  1.00109.95           C  
ANISOU 7554  CG  ARG B1013    13815  16549  11411  -3175   -660    633       C  
ATOM   7555  CD  ARG B1013     -10.710  -5.812  72.278  1.00125.79           C  
ANISOU 7555  CD  ARG B1013    16056  18768  12971  -3435   -407    177       C  
ATOM   7556  NE  ARG B1013     -11.492  -7.038  72.409  1.00134.73           N  
ANISOU 7556  NE  ARG B1013    17400  19853  13939  -3614   -347   -192       N  
ATOM   7557  CZ  ARG B1013     -11.332  -8.107  71.639  1.00151.59           C  
ANISOU 7557  CZ  ARG B1013    19773  22165  15659  -3940   -103   -628       C  
ATOM   7558  NH1 ARG B1013     -10.401  -8.116  70.691  1.00142.77           N  
ANISOU 7558  NH1 ARG B1013    18715  21290  14243  -4106    122   -760       N  
ATOM   7559  NH2 ARG B1013     -12.085  -9.182  71.820  1.00137.02           N  
ANISOU 7559  NH2 ARG B1013    18124  20231  13707  -4115    -42   -959       N  
ATOM   7560  N   GLN B1014      -9.309  -2.754  76.107  1.00 88.75           N  
ANISOU 7560  N   GLN B1014    11028  12687  10006  -2211   -556    814       N  
ATOM   7561  CA  GLN B1014      -8.809  -3.239  77.399  1.00 86.20           C  
ANISOU 7561  CA  GLN B1014    10850  11959   9942  -1984   -463    538       C  
ATOM   7562  C   GLN B1014      -9.668  -2.721  78.575  1.00 87.68           C  
ANISOU 7562  C   GLN B1014    11029  11821  10467  -1859   -558    642       C  
ATOM   7563  O   GLN B1014      -9.908  -3.472  79.527  1.00 85.60           O  
ANISOU 7563  O   GLN B1014    10906  11322  10297  -1766   -527    403       O  
ATOM   7564  CB  GLN B1014      -7.326  -2.891  77.575  1.00 87.57           C  
ANISOU 7564  CB  GLN B1014    10992  12059  10223  -1871   -357    527       C  
ATOM   7565  CG  GLN B1014      -6.429  -3.918  76.881  1.00116.64           C  
ANISOU 7565  CG  GLN B1014    14750  15900  13669  -1905   -152    270       C  
ATOM   7566  CD  GLN B1014      -5.051  -3.424  76.491  1.00153.26           C  
ANISOU 7566  CD  GLN B1014    19273  20633  18326  -1866    -48    375       C  
ATOM   7567  OE1 GLN B1014      -4.761  -2.222  76.462  1.00152.65           O  
ANISOU 7567  OE1 GLN B1014    19051  20584  18365  -1872   -153    667       O  
ATOM   7568  NE2 GLN B1014      -4.154  -4.352  76.180  1.00151.07           N  
ANISOU 7568  NE2 GLN B1014    19047  20382  17970  -1821    197    150       N  
ATOM   7569  N   LEU B1015     -10.190  -1.483  78.465  1.00 84.52           N  
ANISOU 7569  N   LEU B1015    10457  11402  10256  -1869   -638   1010       N  
ATOM   7570  CA  LEU B1015     -11.090  -0.891  79.467  1.00 83.41           C  
ANISOU 7570  CA  LEU B1015    10297  10929  10468  -1764   -648   1122       C  
ATOM   7571  C   LEU B1015     -12.455  -1.578  79.407  1.00 87.76           C  
ANISOU 7571  C   LEU B1015    10844  11558  10943  -1820   -726   1126       C  
ATOM   7572  O   LEU B1015     -12.996  -1.960  80.443  1.00 85.68           O  
ANISOU 7572  O   LEU B1015    10693  11021  10839  -1726   -692    956       O  
ATOM   7573  CB  LEU B1015     -11.246   0.627  79.250  1.00 84.98           C  
ANISOU 7573  CB  LEU B1015    10287  11042  10961  -1748   -633   1546       C  
ATOM   7574  CG  LEU B1015     -12.310   1.336  80.108  1.00 89.39           C  
ANISOU 7574  CG  LEU B1015    10794  11232  11939  -1645   -558   1707       C  
ATOM   7575  CD1 LEU B1015     -11.722   1.847  81.400  1.00 87.86           C  
ANISOU 7575  CD1 LEU B1015    10768  10603  12013  -1568   -398   1482       C  
ATOM   7576  CD2 LEU B1015     -12.965   2.458  79.331  1.00 94.99           C  
ANISOU 7576  CD2 LEU B1015    11199  12009  12885  -1658   -562   2260       C  
ATOM   7577  N   ALA B1016     -12.996  -1.729  78.179  1.00 87.24           N  
ANISOU 7577  N   ALA B1016    10638  11905  10603  -2014   -839   1336       N  
ATOM   7578  CA  ALA B1016     -14.281  -2.366  77.879  1.00 88.71           C  
ANISOU 7578  CA  ALA B1016    10776  12288  10642  -2159   -954   1400       C  
ATOM   7579  C   ALA B1016     -14.322  -3.810  78.379  1.00 92.37           C  
ANISOU 7579  C   ALA B1016    11505  12657  10934  -2174   -899    912       C  
ATOM   7580  O   ALA B1016     -15.359  -4.233  78.885  1.00 92.16           O  
ANISOU 7580  O   ALA B1016    11491  12535  10993  -2173   -945    894       O  
ATOM   7581  CB  ALA B1016     -14.552  -2.325  76.381  1.00 92.93           C  
ANISOU 7581  CB  ALA B1016    11133  13383  10792  -2462  -1094   1681       C  
ATOM   7582  N   ASP B1017     -13.199  -4.554  78.250  1.00 88.64           N  
ANISOU 7582  N   ASP B1017    11222  12189  10270  -2175   -775    551       N  
ATOM   7583  CA  ASP B1017     -13.087  -5.940  78.704  1.00 87.64           C  
ANISOU 7583  CA  ASP B1017    11330  11917  10052  -2161   -663    116       C  
ATOM   7584  C   ASP B1017     -13.031  -6.010  80.224  1.00 88.28           C  
ANISOU 7584  C   ASP B1017    11498  11562  10480  -1906   -619      4       C  
ATOM   7585  O   ASP B1017     -13.591  -6.938  80.808  1.00 86.71           O  
ANISOU 7585  O   ASP B1017    11422  11220  10304  -1892   -596   -199       O  
ATOM   7586  CB  ASP B1017     -11.858  -6.620  78.092  1.00 90.98           C  
ANISOU 7586  CB  ASP B1017    11877  12433  10257  -2203   -478   -164       C  
ATOM   7587  CG  ASP B1017     -11.948  -6.843  76.598  1.00110.85           C  
ANISOU 7587  CG  ASP B1017    14384  15402  12333  -2535   -465   -174       C  
ATOM   7588  OD1 ASP B1017     -13.028  -7.280  76.119  1.00114.60           O  
ANISOU 7588  OD1 ASP B1017    14870  16105  12569  -2799   -564   -175       O  
ATOM   7589  OD2 ASP B1017     -10.939  -6.615  75.909  1.00119.33           O  
ANISOU 7589  OD2 ASP B1017    15440  16629  13270  -2568   -351   -185       O  
ATOM   7590  N   LEU B1018     -12.355  -5.032  80.864  1.00 84.31           N  
ANISOU 7590  N   LEU B1018    10939  10870  10224  -1749   -602    133       N  
ATOM   7591  CA  LEU B1018     -12.236  -4.949  82.316  1.00 82.40           C  
ANISOU 7591  CA  LEU B1018    10784  10276  10249  -1588   -563     40       C  
ATOM   7592  C   LEU B1018     -13.587  -4.581  82.935  1.00 87.25           C  
ANISOU 7592  C   LEU B1018    11364  10732  11056  -1569   -605    163       C  
ATOM   7593  O   LEU B1018     -13.957  -5.154  83.959  1.00 85.85           O  
ANISOU 7593  O   LEU B1018    11305  10347  10969  -1507   -574     -3       O  
ATOM   7594  CB  LEU B1018     -11.169  -3.929  82.686  1.00 81.98           C  
ANISOU 7594  CB  LEU B1018    10684  10121  10343  -1526   -529    139       C  
ATOM   7595  CG  LEU B1018     -10.644  -4.018  84.076  1.00 85.13           C  
ANISOU 7595  CG  LEU B1018    11189  10266  10888  -1452   -490     -2       C  
ATOM   7596  CD1 LEU B1018      -9.403  -4.939  84.180  1.00 85.49           C  
ANISOU 7596  CD1 LEU B1018    11271  10373  10840  -1403   -447   -149       C  
ATOM   7597  CD2 LEU B1018     -10.257  -2.671  84.537  1.00 87.27           C  
ANISOU 7597  CD2 LEU B1018    11419  10400  11340  -1480   -465    134       C  
ATOM   7598  N   GLU B1019     -14.325  -3.644  82.295  1.00 85.88           N  
ANISOU 7598  N   GLU B1019    11000  10665  10964  -1620   -658    496       N  
ATOM   7599  CA  GLU B1019     -15.651  -3.201  82.723  1.00 86.34           C  
ANISOU 7599  CA  GLU B1019    10954  10581  11271  -1584   -656    704       C  
ATOM   7600  C   GLU B1019     -16.635  -4.352  82.627  1.00 91.33           C  
ANISOU 7600  C   GLU B1019    11621  11338  11740  -1671   -738    600       C  
ATOM   7601  O   GLU B1019     -17.491  -4.488  83.496  1.00 90.91           O  
ANISOU 7601  O   GLU B1019    11591  11072  11879  -1601   -696    582       O  
ATOM   7602  CB  GLU B1019     -16.128  -2.022  81.865  1.00 90.19           C  
ANISOU 7602  CB  GLU B1019    11159  11202  11908  -1616   -690   1179       C  
ATOM   7603  CG  GLU B1019     -16.952  -1.002  82.629  1.00103.79           C  
ANISOU 7603  CG  GLU B1019    12765  12570  14101  -1480   -543   1421       C  
ATOM   7604  CD  GLU B1019     -16.155  -0.010  83.453  1.00131.96           C  
ANISOU 7604  CD  GLU B1019    16436  15758  17944  -1385   -340   1329       C  
ATOM   7605  OE1 GLU B1019     -15.022   0.333  83.041  1.00128.72           O  
ANISOU 7605  OE1 GLU B1019    16048  15439  17419  -1427   -361   1302       O  
ATOM   7606  OE2 GLU B1019     -16.677   0.448  84.497  1.00131.92           O  
ANISOU 7606  OE2 GLU B1019    16491  15370  18264  -1299   -139   1281       O  
ATOM   7607  N   ASP B1020     -16.492  -5.189  81.576  1.00 89.46           N  
ANISOU 7607  N   ASP B1020    11406  11444  11140  -1855   -826    505       N  
ATOM   7608  CA  ASP B1020     -17.306  -6.376  81.302  1.00 90.29           C  
ANISOU 7608  CA  ASP B1020    11578  11707  11022  -2024   -890    354       C  
ATOM   7609  C   ASP B1020     -17.133  -7.395  82.426  1.00 91.07           C  
ANISOU 7609  C   ASP B1020    11911  11492  11198  -1902   -785    -19       C  
ATOM   7610  O   ASP B1020     -18.130  -7.892  82.948  1.00 90.69           O  
ANISOU 7610  O   ASP B1020    11879  11356  11225  -1916   -810    -41       O  
ATOM   7611  CB  ASP B1020     -16.905  -6.995  79.942  1.00 94.75           C  
ANISOU 7611  CB  ASP B1020    12180  12671  11149  -2297   -925    241       C  
ATOM   7612  CG  ASP B1020     -17.949  -7.870  79.268  1.00109.97           C  
ANISOU 7612  CG  ASP B1020    14106  14897  12779  -2614  -1029    203       C  
ATOM   7613  OD1 ASP B1020     -18.473  -8.796  79.934  1.00110.65           O  
ANISOU 7613  OD1 ASP B1020    14332  14794  12917  -2605   -990    -33       O  
ATOM   7614  OD2 ASP B1020     -18.187  -7.679  78.050  1.00118.48           O  
ANISOU 7614  OD2 ASP B1020    15054  16429  13536  -2916  -1148    399       O  
ATOM   7615  N   ASN B1021     -15.870  -7.667  82.815  1.00 85.40           N  
ANISOU 7615  N   ASN B1021    11337  10623  10487  -1783   -673   -250       N  
ATOM   7616  CA  ASN B1021     -15.508  -8.607  83.875  1.00 83.47           C  
ANISOU 7616  CA  ASN B1021    11268  10112  10335  -1662   -576   -519       C  
ATOM   7617  C   ASN B1021     -15.918  -8.089  85.254  1.00 85.06           C  
ANISOU 7617  C   ASN B1021    11475  10039  10803  -1524   -572   -449       C  
ATOM   7618  O   ASN B1021     -16.376  -8.877  86.085  1.00 83.65           O  
ANISOU 7618  O   ASN B1021    11395   9705  10685  -1491   -547   -580       O  
ATOM   7619  CB  ASN B1021     -14.012  -8.890  83.846  1.00 84.55           C  
ANISOU 7619  CB  ASN B1021    11471  10213  10443  -1576   -466   -661       C  
ATOM   7620  CG  ASN B1021     -13.548  -9.637  82.614  1.00113.10           C  
ANISOU 7620  CG  ASN B1021    15134  14028  13811  -1709   -368   -823       C  
ATOM   7621  OD1 ASN B1021     -14.166 -10.613  82.159  1.00110.02           O  
ANISOU 7621  OD1 ASN B1021    14840  13692  13271  -1861   -319  -1005       O  
ATOM   7622  ND2 ASN B1021     -12.424  -9.207  82.056  1.00104.30           N  
ANISOU 7622  ND2 ASN B1021    13968  13019  12642  -1682   -303   -786       N  
ATOM   7623  N   TRP B1022     -15.768  -6.770  85.487  1.00 81.41           N  
ANISOU 7623  N   TRP B1022    10921   9511  10500  -1470   -565   -255       N  
ATOM   7624  CA  TRP B1022     -16.134  -6.142  86.755  1.00 80.62           C  
ANISOU 7624  CA  TRP B1022    10858   9138  10637  -1394   -490   -232       C  
ATOM   7625  C   TRP B1022     -17.661  -6.091  86.909  1.00 84.06           C  
ANISOU 7625  C   TRP B1022    11214   9514  11213  -1399   -483   -102       C  
ATOM   7626  O   TRP B1022     -18.151  -6.114  88.038  1.00 83.59           O  
ANISOU 7626  O   TRP B1022    11234   9229  11298  -1352   -391   -176       O  
ATOM   7627  CB  TRP B1022     -15.516  -4.748  86.875  1.00 80.25           C  
ANISOU 7627  CB  TRP B1022    10758   8996  10737  -1377   -421   -102       C  
ATOM   7628  CG  TRP B1022     -15.651  -4.146  88.239  1.00 81.50           C  
ANISOU 7628  CG  TRP B1022    11022   8860  11084  -1368   -281   -178       C  
ATOM   7629  CD1 TRP B1022     -14.920  -4.449  89.350  1.00 83.69           C  
ANISOU 7629  CD1 TRP B1022    11459   9052  11289  -1413   -258   -376       C  
ATOM   7630  CD2 TRP B1022     -16.567  -3.116  88.627  1.00 82.94           C  
ANISOU 7630  CD2 TRP B1022    11152   8804  11555  -1346   -113    -46       C  
ATOM   7631  NE1 TRP B1022     -15.329  -3.675  90.412  1.00 83.98           N  
ANISOU 7631  NE1 TRP B1022    11588   8839  11482  -1471    -90   -431       N  
ATOM   7632  CE2 TRP B1022     -16.342  -2.848  89.996  1.00 86.90           C  
ANISOU 7632  CE2 TRP B1022    11841   9070  12108  -1410     39   -252       C  
ATOM   7633  CE3 TRP B1022     -17.563  -2.389  87.947  1.00 86.24           C  
ANISOU 7633  CE3 TRP B1022    11361   9191  12214  -1290    -52    260       C  
ATOM   7634  CZ2 TRP B1022     -17.090  -1.899  90.707  1.00 88.04           C  
ANISOU 7634  CZ2 TRP B1022    12018   8896  12538  -1419    307   -240       C  
ATOM   7635  CZ3 TRP B1022     -18.290  -1.434  88.646  1.00 89.57           C  
ANISOU 7635  CZ3 TRP B1022    11764   9275  12994  -1243    210    342       C  
ATOM   7636  CH2 TRP B1022     -18.052  -1.195  90.009  1.00 90.13           C  
ANISOU 7636  CH2 TRP B1022    12070   9061  13113  -1307    417     56       C  
ATOM   7637  N   GLU B1023     -18.406  -6.047  85.783  1.00 80.29           N  
ANISOU 7637  N   GLU B1023    10561   9271  10674  -1482   -581    115       N  
ATOM   7638  CA  GLU B1023     -19.861  -6.076  85.800  1.00 80.19           C  
ANISOU 7638  CA  GLU B1023    10406   9270  10792  -1506   -604    314       C  
ATOM   7639  C   GLU B1023     -20.347  -7.512  85.974  1.00 80.30           C  
ANISOU 7639  C   GLU B1023    10542   9338  10629  -1593   -667     88       C  
ATOM   7640  O   GLU B1023     -21.393  -7.710  86.583  1.00 80.12           O  
ANISOU 7640  O   GLU B1023    10481   9205  10755  -1572   -640    145       O  
ATOM   7641  CB  GLU B1023     -20.460  -5.427  84.545  1.00 84.36           C  
ANISOU 7641  CB  GLU B1023    10646  10092  11316  -1607   -717    723       C  
ATOM   7642  CG  GLU B1023     -21.853  -4.851  84.759  1.00102.18           C  
ANISOU 7642  CG  GLU B1023    12652  12273  13899  -1554   -675   1097       C  
ATOM   7643  CD  GLU B1023     -22.079  -4.011  86.008  1.00130.80           C  
ANISOU 7643  CD  GLU B1023    16309  15439  17952  -1344   -405   1101       C  
ATOM   7644  OE1 GLU B1023     -21.345  -3.014  86.205  1.00134.79           O  
ANISOU 7644  OE1 GLU B1023    16846  15744  18626  -1258   -257   1114       O  
ATOM   7645  OE2 GLU B1023     -22.991  -4.359  86.794  1.00123.01           O  
ANISOU 7645  OE2 GLU B1023    15331  14288  17118  -1296   -317   1071       O  
ATOM   7646  N   THR B1024     -19.574  -8.510  85.486  1.00 74.34           N  
ANISOU 7646  N   THR B1024     9935   8712   9599  -1684   -707   -171       N  
ATOM   7647  CA  THR B1024     -19.891  -9.940  85.632  1.00 73.49           C  
ANISOU 7647  CA  THR B1024     9972   8592   9360  -1773   -709   -423       C  
ATOM   7648  C   THR B1024     -19.792 -10.327  87.119  1.00 74.68           C  
ANISOU 7648  C   THR B1024    10262   8419   9692  -1611   -609   -572       C  
ATOM   7649  O   THR B1024     -20.616 -11.107  87.606  1.00 74.61           O  
ANISOU 7649  O   THR B1024    10298   8332   9720  -1644   -606   -636       O  
ATOM   7650  CB  THR B1024     -18.969 -10.800  84.742  1.00 80.69           C  
ANISOU 7650  CB  THR B1024    11010   9643  10005  -1891   -675   -669       C  
ATOM   7651  OG1 THR B1024     -19.091 -10.368  83.388  1.00 84.52           O  
ANISOU 7651  OG1 THR B1024    11371  10480  10263  -2095   -770   -521       O  
ATOM   7652  CG2 THR B1024     -19.293 -12.289  84.806  1.00 78.25           C  
ANISOU 7652  CG2 THR B1024    10863   9263   9605  -2004   -612   -945       C  
ATOM   7653  N   LEU B1025     -18.803  -9.753  87.836  1.00 68.56           N  
ANISOU 7653  N   LEU B1025     9545   7496   9009  -1477   -539   -603       N  
ATOM   7654  CA  LEU B1025     -18.587  -9.993  89.262  1.00 66.47           C  
ANISOU 7654  CA  LEU B1025     9399   7004   8852  -1388   -465   -705       C  
ATOM   7655  C   LEU B1025     -19.747  -9.444  90.093  1.00 69.05           C  
ANISOU 7655  C   LEU B1025     9692   7188   9357  -1369   -403   -605       C  
ATOM   7656  O   LEU B1025     -20.271 -10.166  90.938  1.00 69.09           O  
ANISOU 7656  O   LEU B1025     9773   7085   9393  -1367   -372   -685       O  
ATOM   7657  CB  LEU B1025     -17.253  -9.382  89.738  1.00 65.86           C  
ANISOU 7657  CB  LEU B1025     9364   6884   8776  -1335   -431   -724       C  
ATOM   7658  CG  LEU B1025     -15.979 -10.059  89.239  1.00 70.57           C  
ANISOU 7658  CG  LEU B1025     9981   7571   9260  -1311   -442   -806       C  
ATOM   7659  CD1 LEU B1025     -14.830  -9.070  89.176  1.00 70.54           C  
ANISOU 7659  CD1 LEU B1025     9931   7621   9249  -1300   -445   -730       C  
ATOM   7660  CD2 LEU B1025     -15.625 -11.270  90.090  1.00 73.18           C  
ANISOU 7660  CD2 LEU B1025    10391   7795   9618  -1262   -409   -895       C  
ATOM   7661  N   ASN B1026     -20.167  -8.196  89.831  1.00 64.96           N  
ANISOU 7661  N   ASN B1026     9043   6650   8988  -1350   -351   -411       N  
ATOM   7662  CA  ASN B1026     -21.245  -7.520  90.559  1.00 65.14           C  
ANISOU 7662  CA  ASN B1026     9007   6482   9260  -1306   -203   -293       C  
ATOM   7663  C   ASN B1026     -22.596  -8.184  90.329  1.00 68.67           C  
ANISOU 7663  C   ASN B1026     9334   6999   9756  -1336   -257   -175       C  
ATOM   7664  O   ASN B1026     -23.382  -8.304  91.280  1.00 67.72           O  
ANISOU 7664  O   ASN B1026     9243   6710   9777  -1303   -134   -193       O  
ATOM   7665  CB  ASN B1026     -21.313  -6.045  90.163  1.00 68.07           C  
ANISOU 7665  CB  ASN B1026     9227   6779   9856  -1258    -88    -64       C  
ATOM   7666  CG  ASN B1026     -20.035  -5.273  90.419  1.00 94.69           C  
ANISOU 7666  CG  ASN B1026    12715  10066  13198  -1269    -19   -177       C  
ATOM   7667  OD1 ASN B1026     -19.154  -5.680  91.199  1.00 84.77           O  
ANISOU 7667  OD1 ASN B1026    11648   8783  11779  -1319    -28   -411       O  
ATOM   7668  ND2 ASN B1026     -19.890  -4.150  89.733  1.00 91.07           N  
ANISOU 7668  ND2 ASN B1026    12113   9592  12898  -1242     38     35       N  
ATOM   7669  N   ASP B1027     -22.862  -8.609  89.067  1.00 65.92           N  
ANISOU 7669  N   ASP B1027     8854   6928   9263  -1439   -435    -57       N  
ATOM   7670  CA  ASP B1027     -24.112  -9.266  88.668  1.00 66.54           C  
ANISOU 7670  CA  ASP B1027     8795   7157   9329  -1550   -535     79       C  
ATOM   7671  C   ASP B1027     -24.228 -10.648  89.286  1.00 66.75           C  
ANISOU 7671  C   ASP B1027     9012   7112   9238  -1603   -547   -194       C  
ATOM   7672  O   ASP B1027     -25.311 -11.005  89.748  1.00 66.90           O  
ANISOU 7672  O   ASP B1027     8969   7083   9369  -1624   -528   -119       O  
ATOM   7673  CB  ASP B1027     -24.248  -9.362  87.133  1.00 70.21           C  
ANISOU 7673  CB  ASP B1027     9096   8003   9578  -1746   -733    251       C  
ATOM   7674  CG  ASP B1027     -24.430  -8.044  86.395  1.00 78.81           C  
ANISOU 7674  CG  ASP B1027     9905   9226  10815  -1719   -754    661       C  
ATOM   7675  OD1 ASP B1027     -24.971  -7.086  87.002  1.00 80.48           O  
ANISOU 7675  OD1 ASP B1027     9971   9212  11397  -1548   -593    899       O  
ATOM   7676  OD2 ASP B1027     -24.042  -7.973  85.210  1.00 82.02           O  
ANISOU 7676  OD2 ASP B1027    10234   9948  10982  -1876   -901    754       O  
ATOM   7677  N   ASN B1028     -23.123 -11.412  89.318  1.00 60.55           N  
ANISOU 7677  N   ASN B1028     8433   6300   8274  -1611   -555   -472       N  
ATOM   7678  CA  ASN B1028     -23.143 -12.751  89.897  1.00 60.04           C  
ANISOU 7678  CA  ASN B1028     8530   6124   8158  -1640   -534   -690       C  
ATOM   7679  C   ASN B1028     -23.203 -12.722  91.429  1.00 62.48           C  
ANISOU 7679  C   ASN B1028     8928   6194   8618  -1514   -419   -724       C  
ATOM   7680  O   ASN B1028     -23.685 -13.687  92.018  1.00 62.47           O  
ANISOU 7680  O   ASN B1028     8993   6105   8637  -1542   -402   -797       O  
ATOM   7681  CB  ASN B1028     -21.976 -13.587  89.410  1.00 60.99           C  
ANISOU 7681  CB  ASN B1028     8795   6259   8120  -1667   -523   -915       C  
ATOM   7682  CG  ASN B1028     -22.219 -14.175  88.042  1.00 86.13           C  
ANISOU 7682  CG  ASN B1028    11968   9660  11098  -1892   -584   -992       C  
ATOM   7683  OD1 ASN B1028     -23.146 -14.967  87.828  1.00 72.70           O  
ANISOU 7683  OD1 ASN B1028    10273   8005   9344  -2069   -618  -1037       O  
ATOM   7684  ND2 ASN B1028     -21.401 -13.780  87.079  1.00 83.49           N  
ANISOU 7684  ND2 ASN B1028    11622   9486  10614  -1935   -595  -1013       N  
ATOM   7685  N   LEU B1029     -22.771 -11.615  92.067  1.00 57.74           N  
ANISOU 7685  N   LEU B1029     8334   5498   8105  -1419   -327   -675       N  
ATOM   7686  CA  LEU B1029     -22.855 -11.447  93.521  1.00 56.80           C  
ANISOU 7686  CA  LEU B1029     8317   5199   8064  -1380   -194   -726       C  
ATOM   7687  C   LEU B1029     -24.322 -11.386  93.956  1.00 61.89           C  
ANISOU 7687  C   LEU B1029     8875   5763   8877  -1381    -99   -618       C  
ATOM   7688  O   LEU B1029     -24.693 -11.995  94.963  1.00 61.52           O  
ANISOU 7688  O   LEU B1029     8917   5624   8834  -1397    -35   -684       O  
ATOM   7689  CB  LEU B1029     -22.109 -10.185  93.983  1.00 56.73           C  
ANISOU 7689  CB  LEU B1029     8356   5117   8084  -1359    -82   -737       C  
ATOM   7690  CG  LEU B1029     -20.617 -10.332  94.251  1.00 60.99           C  
ANISOU 7690  CG  LEU B1029     9006   5711   8457  -1383   -145   -842       C  
ATOM   7691  CD1 LEU B1029     -19.958  -8.985  94.363  1.00 61.82           C  
ANISOU 7691  CD1 LEU B1029     9129   5778   8582  -1415    -57   -840       C  
ATOM   7692  CD2 LEU B1029     -20.352 -11.134  95.507  1.00 64.45           C  
ANISOU 7692  CD2 LEU B1029     9565   6122   8803  -1436   -140   -913       C  
ATOM   7693  N   LYS B1030     -25.157 -10.680  93.162  1.00 59.71           N  
ANISOU 7693  N   LYS B1030     8392   5544   8752  -1367    -93   -401       N  
ATOM   7694  CA  LYS B1030     -26.600 -10.537  93.367  1.00 60.92           C  
ANISOU 7694  CA  LYS B1030     8374   5648   9125  -1352      0   -203       C  
ATOM   7695  C   LYS B1030     -27.274 -11.909  93.267  1.00 63.94           C  
ANISOU 7695  C   LYS B1030     8754   6135   9407  -1461   -141   -235       C  
ATOM   7696  O   LYS B1030     -28.159 -12.218  94.068  1.00 64.00           O  
ANISOU 7696  O   LYS B1030     8744   6040   9534  -1453    -38   -201       O  
ATOM   7697  CB  LYS B1030     -27.216  -9.564  92.337  1.00 66.11           C  
ANISOU 7697  CB  LYS B1030     8734   6409   9975  -1324    -12    140       C  
ATOM   7698  CG  LYS B1030     -26.677  -8.130  92.385  1.00 93.24           C  
ANISOU 7698  CG  LYS B1030    12145   9686  13596  -1211    177    213       C  
ATOM   7699  CD  LYS B1030     -27.394  -7.248  91.365  1.00112.70           C  
ANISOU 7699  CD  LYS B1030    14254  12253  16314  -1168    168    654       C  
ATOM   7700  CE  LYS B1030     -26.841  -5.844  91.289  1.00130.09           C  
ANISOU 7700  CE  LYS B1030    16417  14267  18746  -1057    371    755       C  
ATOM   7701  NZ  LYS B1030     -25.588  -5.779  90.489  1.00140.27           N  
ANISOU 7701  NZ  LYS B1030    17795  15741  19760  -1124    173    653       N  
ATOM   7702  N   VAL B1031     -26.821 -12.740  92.297  1.00 59.76           N  
ANISOU 7702  N   VAL B1031     8260   5787   8657  -1582   -339   -328       N  
ATOM   7703  CA  VAL B1031     -27.309 -14.104  92.047  1.00 59.76           C  
ANISOU 7703  CA  VAL B1031     8301   5861   8544  -1741   -446   -420       C  
ATOM   7704  C   VAL B1031     -27.053 -14.970  93.297  1.00 62.98           C  
ANISOU 7704  C   VAL B1031     8906   6053   8969  -1682   -350   -603       C  
ATOM   7705  O   VAL B1031     -27.957 -15.709  93.698  1.00 63.74           O  
ANISOU 7705  O   VAL B1031     8982   6111   9125  -1750   -342   -578       O  
ATOM   7706  CB  VAL B1031     -26.690 -14.731  90.759  1.00 63.58           C  
ANISOU 7706  CB  VAL B1031     8841   6535   8781  -1911   -586   -557       C  
ATOM   7707  CG1 VAL B1031     -27.124 -16.188  90.564  1.00 64.46           C  
ANISOU 7707  CG1 VAL B1031     9050   6649   8793  -2113   -624   -725       C  
ATOM   7708  CG2 VAL B1031     -27.038 -13.905  89.524  1.00 64.80           C  
ANISOU 7708  CG2 VAL B1031     8772   6980   8868  -2027   -713   -318       C  
ATOM   7709  N   ILE B1032     -25.850 -14.845  93.925  1.00 57.45           N  
ANISOU 7709  N   ILE B1032     8363   5245   8219  -1576   -288   -734       N  
ATOM   7710  CA  ILE B1032     -25.469 -15.597  95.133  1.00 56.44           C  
ANISOU 7710  CA  ILE B1032     8383   4975   8088  -1539   -222   -824       C  
ATOM   7711  C   ILE B1032     -26.314 -15.104  96.325  1.00 61.46           C  
ANISOU 7711  C   ILE B1032     9003   5521   8826  -1517    -82   -744       C  
ATOM   7712  O   ILE B1032     -26.733 -15.926  97.142  1.00 61.01           O  
ANISOU 7712  O   ILE B1032     8999   5397   8787  -1548    -48   -748       O  
ATOM   7713  CB  ILE B1032     -23.940 -15.550  95.427  1.00 58.34           C  
ANISOU 7713  CB  ILE B1032     8732   5200   8234  -1473   -225   -902       C  
ATOM   7714  CG1 ILE B1032     -23.124 -16.105  94.242  1.00 58.73           C  
ANISOU 7714  CG1 ILE B1032     8792   5302   8220  -1481   -293   -992       C  
ATOM   7715  CG2 ILE B1032     -23.595 -16.337  96.699  1.00 58.87           C  
ANISOU 7715  CG2 ILE B1032     8890   5183   8296  -1466   -188   -891       C  
ATOM   7716  CD1 ILE B1032     -21.724 -15.529  94.101  1.00 66.16           C  
ANISOU 7716  CD1 ILE B1032     9752   6291   9094  -1407   -301  -1002       C  
ATOM   7717  N   GLU B1033     -26.599 -13.790  96.398  1.00 60.21           N  
ANISOU 7717  N   GLU B1033     8774   5343   8761  -1469     36   -668       N  
ATOM   7718  CA  GLU B1033     -27.426 -13.201  97.464  1.00 61.90           C  
ANISOU 7718  CA  GLU B1033     8983   5429   9106  -1453    264   -625       C  
ATOM   7719  C   GLU B1033     -28.858 -13.759  97.430  1.00 64.07           C  
ANISOU 7719  C   GLU B1033     9107   5702   9534  -1472    279   -481       C  
ATOM   7720  O   GLU B1033     -29.396 -14.133  98.470  1.00 64.57           O  
ANISOU 7720  O   GLU B1033     9227   5685   9623  -1496    407   -499       O  
ATOM   7721  CB  GLU B1033     -27.464 -11.663  97.343  1.00 64.90           C  
ANISOU 7721  CB  GLU B1033     9297   5719   9642  -1387    455   -566       C  
ATOM   7722  CG  GLU B1033     -26.398 -10.941  98.151  1.00 84.72           C  
ANISOU 7722  CG  GLU B1033    12010   8155  12023  -1435    587   -746       C  
ATOM   7723  CD  GLU B1033     -26.268  -9.443  97.914  1.00128.62           C  
ANISOU 7723  CD  GLU B1033    17533  13582  17755  -1391    796   -724       C  
ATOM   7724  OE1 GLU B1033     -26.375  -9.023  96.739  1.00140.52           O  
ANISOU 7724  OE1 GLU B1033    18850  15138  19401  -1302    705   -547       O  
ATOM   7725  OE2 GLU B1033     -26.011  -8.692  98.889  1.00130.32           O  
ANISOU 7725  OE2 GLU B1033    17915  13650  17949  -1478   1059   -884       O  
ATOM   7726  N   LYS B1034     -29.443 -13.846  96.223  1.00 58.68           N  
ANISOU 7726  N   LYS B1034     8225   5152   8921  -1500    133   -324       N  
ATOM   7727  CA  LYS B1034     -30.816 -14.291  95.975  1.00 59.32           C  
ANISOU 7727  CA  LYS B1034     8101   5300   9139  -1566     99   -126       C  
ATOM   7728  C   LYS B1034     -30.969 -15.816  95.892  1.00 62.13           C  
ANISOU 7728  C   LYS B1034     8540   5709   9357  -1716    -61   -233       C  
ATOM   7729  O   LYS B1034     -32.096 -16.319  95.909  1.00 62.31           O  
ANISOU 7729  O   LYS B1034     8425   5776   9475  -1806    -82    -97       O  
ATOM   7730  CB  LYS B1034     -31.321 -13.654  94.673  1.00 62.91           C  
ANISOU 7730  CB  LYS B1034     8272   5946   9684  -1599    -19    145       C  
ATOM   7731  CG  LYS B1034     -31.506 -12.142  94.788  1.00 78.89           C  
ANISOU 7731  CG  LYS B1034    10137   7855  11983  -1429    206    350       C  
ATOM   7732  CD  LYS B1034     -31.694 -11.474  93.453  1.00 92.97           C  
ANISOU 7732  CD  LYS B1034    11636   9854  13835  -1455     60    662       C  
ATOM   7733  CE  LYS B1034     -33.128 -11.590  93.023  1.00111.61           C  
ANISOU 7733  CE  LYS B1034    13629  12386  16390  -1529     -6   1067       C  
ATOM   7734  NZ  LYS B1034     -33.388 -10.850  91.765  1.00128.09           N  
ANISOU 7734  NZ  LYS B1034    15372  14737  18558  -1576   -157   1482       N  
ATOM   7735  N   ALA B1035     -29.846 -16.546  95.837  1.00 57.43           N  
ANISOU 7735  N   ALA B1035     8156   5083   8580  -1740   -142   -457       N  
ATOM   7736  CA  ALA B1035     -29.809 -18.001  95.704  1.00 57.22           C  
ANISOU 7736  CA  ALA B1035     8234   5028   8480  -1867   -228   -582       C  
ATOM   7737  C   ALA B1035     -30.493 -18.772  96.856  1.00 60.04           C  
ANISOU 7737  C   ALA B1035     8625   5257   8931  -1879   -138   -548       C  
ATOM   7738  O   ALA B1035     -30.213 -18.544  98.035  1.00 57.93           O  
ANISOU 7738  O   ALA B1035     8442   4894   8675  -1779    -12   -547       O  
ATOM   7739  CB  ALA B1035     -28.371 -18.473  95.560  1.00 56.90           C  
ANISOU 7739  CB  ALA B1035     8378   4918   8324  -1823   -246   -773       C  
ATOM   7740  N   ASP B1036     -31.392 -19.693  96.476  1.00 58.13           N  
ANISOU 7740  N   ASP B1036     8318   5042   8725  -2050   -206   -520       N  
ATOM   7741  CA  ASP B1036     -32.087 -20.621  97.363  1.00 59.07           C  
ANISOU 7741  CA  ASP B1036     8459   5046   8939  -2102   -143   -481       C  
ATOM   7742  C   ASP B1036     -31.387 -21.980  97.313  1.00 61.19           C  
ANISOU 7742  C   ASP B1036     8910   5155   9186  -2170   -152   -652       C  
ATOM   7743  O   ASP B1036     -31.698 -22.850  98.122  1.00 61.51           O  
ANISOU 7743  O   ASP B1036     8992   5059   9319  -2191    -87   -614       O  
ATOM   7744  CB  ASP B1036     -33.580 -20.773  96.987  1.00 63.90           C  
ANISOU 7744  CB  ASP B1036     8855   5781   9642  -2272   -199   -307       C  
ATOM   7745  CG  ASP B1036     -34.434 -19.510  96.987  1.00 82.90           C  
ANISOU 7745  CG  ASP B1036    11004   8313  12180  -2186   -144    -47       C  
ATOM   7746  OD1 ASP B1036     -33.899 -18.423  97.328  1.00 85.57           O  
ANISOU 7746  OD1 ASP B1036    11364   8603  12546  -1993    -22    -42       O  
ATOM   7747  OD2 ASP B1036     -35.638 -19.607  96.636  1.00 88.47           O  
ANISOU 7747  OD2 ASP B1036    11472   9157  12988  -2323   -204    172       O  
ATOM   7748  N   ASN B1037     -30.463 -22.181  96.355  1.00 56.17           N  
ANISOU 7748  N   ASN B1037     8369   4513   8460  -2202   -195   -825       N  
ATOM   7749  CA  ASN B1037     -29.749 -23.452  96.253  1.00 56.33           C  
ANISOU 7749  CA  ASN B1037     8550   4313   8540  -2238   -118   -984       C  
ATOM   7750  C   ASN B1037     -28.275 -23.263  95.857  1.00 59.24           C  
ANISOU 7750  C   ASN B1037     9013   4633   8861  -2100    -79  -1096       C  
ATOM   7751  O   ASN B1037     -27.885 -22.218  95.331  1.00 56.52           O  
ANISOU 7751  O   ASN B1037     8626   4462   8388  -2049   -149  -1104       O  
ATOM   7752  CB  ASN B1037     -30.454 -24.472  95.338  1.00 55.33           C  
ANISOU 7752  CB  ASN B1037     8462   4148   8413  -2541   -122  -1137       C  
ATOM   7753  CG  ASN B1037     -30.397 -24.210  93.859  1.00 71.68           C  
ANISOU 7753  CG  ASN B1037    10540   6411  10282  -2759   -203  -1303       C  
ATOM   7754  OD1 ASN B1037     -29.441 -24.574  93.170  1.00 68.89           O  
ANISOU 7754  OD1 ASN B1037    10334   5960   9881  -2784   -108  -1525       O  
ATOM   7755  ND2 ASN B1037     -31.472 -23.671  93.316  1.00 61.26           N  
ANISOU 7755  ND2 ASN B1037     9047   5382   8846  -2958   -363  -1177       N  
ATOM   7756  N   ALA B1038     -27.464 -24.303  96.137  1.00 58.06           N  
ANISOU 7756  N   ALA B1038     8966   4232   8863  -2031     54  -1142       N  
ATOM   7757  CA  ALA B1038     -26.021 -24.365  95.907  1.00 58.32           C  
ANISOU 7757  CA  ALA B1038     9051   4169   8938  -1874    139  -1189       C  
ATOM   7758  C   ALA B1038     -25.649 -24.281  94.436  1.00 64.44           C  
ANISOU 7758  C   ALA B1038     9897   4991   9598  -1994    173  -1442       C  
ATOM   7759  O   ALA B1038     -24.697 -23.570  94.108  1.00 63.15           O  
ANISOU 7759  O   ALA B1038     9717   4924   9353  -1872    154  -1447       O  
ATOM   7760  CB  ALA B1038     -25.449 -25.643  96.502  1.00 60.86           C  
ANISOU 7760  CB  ALA B1038     9410   4173   9540  -1780    317  -1109       C  
ATOM   7761  N   ALA B1039     -26.388 -24.990  93.547  1.00 63.33           N  
ANISOU 7761  N   ALA B1039     9837   4809   9418  -2274    224  -1657       N  
ATOM   7762  CA  ALA B1039     -26.089 -25.013  92.110  1.00 64.52           C  
ANISOU 7762  CA  ALA B1039    10083   5040   9392  -2481    280  -1934       C  
ATOM   7763  C   ALA B1039     -26.091 -23.612  91.516  1.00 67.55           C  
ANISOU 7763  C   ALA B1039    10354   5801   9511  -2487     70  -1856       C  
ATOM   7764  O   ALA B1039     -25.331 -23.352  90.581  1.00 69.00           O  
ANISOU 7764  O   ALA B1039    10591   6066   9559  -2526    118  -2005       O  
ATOM   7765  CB  ALA B1039     -27.067 -25.898  91.375  1.00 68.10           C  
ANISOU 7765  CB  ALA B1039    10638   5469   9768  -2880    331  -2161       C  
ATOM   7766  N   GLN B1040     -26.908 -22.706  92.101  1.00 61.02           N  
ANISOU 7766  N   GLN B1040     9362   5173   8651  -2430   -122  -1606       N  
ATOM   7767  CA  GLN B1040     -27.009 -21.293  91.738  1.00 58.73           C  
ANISOU 7767  CA  GLN B1040     8923   5180   8213  -2387   -285  -1451       C  
ATOM   7768  C   GLN B1040     -25.735 -20.571  92.119  1.00 60.98           C  
ANISOU 7768  C   GLN B1040     9222   5418   8529  -2108   -245  -1408       C  
ATOM   7769  O   GLN B1040     -25.188 -19.807  91.323  1.00 59.31           O  
ANISOU 7769  O   GLN B1040     8980   5371   8184  -2108   -293  -1425       O  
ATOM   7770  CB  GLN B1040     -28.189 -20.639  92.465  1.00 58.93           C  
ANISOU 7770  CB  GLN B1040     8771   5310   8311  -2354   -389  -1189       C  
ATOM   7771  CG  GLN B1040     -29.555 -21.089  92.009  1.00 70.61           C  
ANISOU 7771  CG  GLN B1040    10150   6931   9746  -2648   -482  -1135       C  
ATOM   7772  CD  GLN B1040     -30.612 -20.370  92.795  1.00 81.11           C  
ANISOU 7772  CD  GLN B1040    11271   8331  11218  -2549   -526   -836       C  
ATOM   7773  OE1 GLN B1040     -30.836 -20.650  93.973  1.00 70.93           O  
ANISOU 7773  OE1 GLN B1040    10011   6853  10084  -2412   -429   -788       O  
ATOM   7774  NE2 GLN B1040     -31.273 -19.414  92.161  1.00 75.11           N  
ANISOU 7774  NE2 GLN B1040    10277   7841  10421  -2617   -647   -602       N  
ATOM   7775  N   VAL B1041     -25.278 -20.828  93.362  1.00 58.22           N  
ANISOU 7775  N   VAL B1041     8905   4875   8342  -1906   -171  -1324       N  
ATOM   7776  CA  VAL B1041     -24.090 -20.257  93.999  1.00 57.01           C  
ANISOU 7776  CA  VAL B1041     8750   4698   8213  -1688   -151  -1237       C  
ATOM   7777  C   VAL B1041     -22.835 -20.720  93.238  1.00 64.64           C  
ANISOU 7777  C   VAL B1041     9782   5583   9194  -1640    -46  -1370       C  
ATOM   7778  O   VAL B1041     -21.978 -19.889  92.925  1.00 63.50           O  
ANISOU 7778  O   VAL B1041     9604   5555   8968  -1556    -80  -1348       O  
ATOM   7779  CB  VAL B1041     -24.039 -20.628  95.510  1.00 59.53           C  
ANISOU 7779  CB  VAL B1041     9071   4893   8654  -1579   -115  -1079       C  
ATOM   7780  CG1 VAL B1041     -22.771 -20.111  96.174  1.00 58.75           C  
ANISOU 7780  CG1 VAL B1041     8955   4835   8532  -1435   -123   -962       C  
ATOM   7781  CG2 VAL B1041     -25.270 -20.114  96.250  1.00 58.21           C  
ANISOU 7781  CG2 VAL B1041     8850   4797   8469  -1630   -157   -976       C  
ATOM   7782  N   LYS B1042     -22.758 -22.036  92.915  1.00 64.81           N  
ANISOU 7782  N   LYS B1042     9897   5382   9346  -1704    120  -1515       N  
ATOM   7783  CA  LYS B1042     -21.651 -22.671  92.192  1.00 66.81           C  
ANISOU 7783  CA  LYS B1042    10220   5473   9690  -1658    326  -1666       C  
ATOM   7784  C   LYS B1042     -21.492 -22.079  90.775  1.00 71.26           C  
ANISOU 7784  C   LYS B1042    10823   6248  10004  -1815    309  -1865       C  
ATOM   7785  O   LYS B1042     -20.373 -21.751  90.376  1.00 69.64           O  
ANISOU 7785  O   LYS B1042    10603   6063   9794  -1697    383  -1878       O  
ATOM   7786  CB  LYS B1042     -21.846 -24.201  92.122  1.00 71.94           C  
ANISOU 7786  CB  LYS B1042    10983   5779  10571  -1737    578  -1814       C  
ATOM   7787  CG  LYS B1042     -20.535 -24.965  92.268  1.00 90.53           C  
ANISOU 7787  CG  LYS B1042    13327   7829  13240  -1515    854  -1764       C  
ATOM   7788  CD  LYS B1042     -20.342 -26.020  91.190  1.00107.79           C  
ANISOU 7788  CD  LYS B1042    15683   9724  15547  -1661   1215  -2110       C  
ATOM   7789  CE  LYS B1042     -18.879 -26.361  91.000  1.00126.79           C  
ANISOU 7789  CE  LYS B1042    18040  11898  18235  -1416   1514  -2062       C  
ATOM   7790  NZ  LYS B1042     -18.688 -27.602  90.201  1.00143.14           N  
ANISOU 7790  NZ  LYS B1042    20289  13545  20552  -1526   1992  -2393       N  
ATOM   7791  N   ASP B1043     -22.615 -21.914  90.047  1.00 69.93           N  
ANISOU 7791  N   ASP B1043    10673   6277   9620  -2097    194  -1969       N  
ATOM   7792  CA  ASP B1043     -22.654 -21.366  88.691  1.00 71.34           C  
ANISOU 7792  CA  ASP B1043    10861   6740   9506  -2323    134  -2100       C  
ATOM   7793  C   ASP B1043     -22.231 -19.901  88.667  1.00 70.65           C  
ANISOU 7793  C   ASP B1043    10626   6898   9320  -2168    -43  -1886       C  
ATOM   7794  O   ASP B1043     -21.514 -19.506  87.751  1.00 70.50           O  
ANISOU 7794  O   ASP B1043    10618   7017   9151  -2209    -10  -1966       O  
ATOM   7795  CB  ASP B1043     -24.058 -21.526  88.075  1.00 76.24           C  
ANISOU 7795  CB  ASP B1043    11469   7579   9919  -2696     -1  -2148       C  
ATOM   7796  CG  ASP B1043     -24.217 -20.918  86.688  1.00 97.80           C  
ANISOU 7796  CG  ASP B1043    14163  10702  12294  -2995   -118  -2197       C  
ATOM   7797  OD1 ASP B1043     -23.599 -21.451  85.725  1.00101.65           O  
ANISOU 7797  OD1 ASP B1043    14816  11182  12623  -3190     70  -2497       O  
ATOM   7798  OD2 ASP B1043     -24.956 -19.912  86.563  1.00105.97           O  
ANISOU 7798  OD2 ASP B1043    14993  12050  13222  -3042   -370  -1916       O  
ATOM   7799  N   ALA B1044     -22.665 -19.104  89.661  1.00 64.39           N  
ANISOU 7799  N   ALA B1044     9708   6139   8617  -2009   -190  -1634       N  
ATOM   7800  CA  ALA B1044     -22.320 -17.682  89.744  1.00 62.29           C  
ANISOU 7800  CA  ALA B1044     9320   6038   8309  -1876   -306  -1445       C  
ATOM   7801  C   ALA B1044     -20.837 -17.481  90.096  1.00 65.63           C  
ANISOU 7801  C   ALA B1044     9772   6360   8803  -1663   -221  -1444       C  
ATOM   7802  O   ALA B1044     -20.194 -16.594  89.530  1.00 64.82           O  
ANISOU 7802  O   ALA B1044     9617   6405   8607  -1633   -261  -1402       O  
ATOM   7803  CB  ALA B1044     -23.204 -16.983  90.762  1.00 61.49           C  
ANISOU 7803  CB  ALA B1044     9115   5931   8316  -1796   -389  -1234       C  
ATOM   7804  N   LEU B1045     -20.292 -18.330  90.997  1.00 61.78           N  
ANISOU 7804  N   LEU B1045     9338   5644   8492  -1530   -112  -1444       N  
ATOM   7805  CA  LEU B1045     -18.894 -18.271  91.428  1.00 60.48           C  
ANISOU 7805  CA  LEU B1045     9145   5413   8422  -1345    -48  -1361       C  
ATOM   7806  C   LEU B1045     -17.937 -18.658  90.305  1.00 65.56           C  
ANISOU 7806  C   LEU B1045     9820   6035   9057  -1341    111  -1509       C  
ATOM   7807  O   LEU B1045     -16.915 -17.993  90.163  1.00 65.73           O  
ANISOU 7807  O   LEU B1045     9770   6148   9055  -1242     99  -1427       O  
ATOM   7808  CB  LEU B1045     -18.649 -19.156  92.656  1.00 60.74           C  
ANISOU 7808  CB  LEU B1045     9169   5249   8661  -1230     16  -1231       C  
ATOM   7809  CG  LEU B1045     -19.092 -18.598  94.004  1.00 63.73           C  
ANISOU 7809  CG  LEU B1045     9511   5691   9014  -1219   -115  -1050       C  
ATOM   7810  CD1 LEU B1045     -19.223 -19.701  95.019  1.00 64.12           C  
ANISOU 7810  CD1 LEU B1045     9556   5574   9231  -1178    -56   -927       C  
ATOM   7811  CD2 LEU B1045     -18.136 -17.518  94.501  1.00 66.55           C  
ANISOU 7811  CD2 LEU B1045     9803   6203   9280  -1171   -202   -911       C  
ATOM   7812  N   THR B1046     -18.252 -19.712  89.508  1.00 63.22           N  
ANISOU 7812  N   THR B1046     9637   5612   8771  -1477    289  -1745       N  
ATOM   7813  CA  THR B1046     -17.413 -20.148  88.377  1.00 64.84           C  
ANISOU 7813  CA  THR B1046     9912   5768   8955  -1518    526  -1955       C  
ATOM   7814  C   THR B1046     -17.321 -19.020  87.337  1.00 67.79           C  
ANISOU 7814  C   THR B1046    10253   6477   9026  -1645    395  -1983       C  
ATOM   7815  O   THR B1046     -16.232 -18.750  86.825  1.00 67.46           O  
ANISOU 7815  O   THR B1046    10182   6474   8976  -1561    503  -1995       O  
ATOM   7816  CB  THR B1046     -17.912 -21.464  87.745  1.00 73.57           C  
ANISOU 7816  CB  THR B1046    11196   6661  10097  -1724    785  -2266       C  
ATOM   7817  OG1 THR B1046     -19.325 -21.410  87.549  1.00 76.19           O  
ANISOU 7817  OG1 THR B1046    11575   7155  10219  -1999    604  -2335       O  
ATOM   7818  CG2 THR B1046     -17.542 -22.687  88.562  1.00 71.53           C  
ANISOU 7818  CG2 THR B1046    10952   5986  10239  -1541   1037  -2224       C  
ATOM   7819  N   LYS B1047     -18.458 -18.337  87.074  1.00 63.85           N  
ANISOU 7819  N   LYS B1047     9721   6225   8314  -1832    164  -1933       N  
ATOM   7820  CA  LYS B1047     -18.559 -17.197  86.161  1.00 63.82           C  
ANISOU 7820  CA  LYS B1047     9632   6560   8055  -1957      5  -1854       C  
ATOM   7821  C   LYS B1047     -17.738 -16.020  86.687  1.00 67.38           C  
ANISOU 7821  C   LYS B1047     9956   7055   8590  -1722    -92  -1623       C  
ATOM   7822  O   LYS B1047     -17.157 -15.280  85.895  1.00 67.22           O  
ANISOU 7822  O   LYS B1047     9881   7225   8435  -1749   -114  -1586       O  
ATOM   7823  CB  LYS B1047     -20.024 -16.773  85.982  1.00 65.87           C  
ANISOU 7823  CB  LYS B1047     9812   7039   8178  -2165   -213  -1733       C  
ATOM   7824  CG  LYS B1047     -20.848 -17.677  85.086  1.00 76.73           C  
ANISOU 7824  CG  LYS B1047    11287   8529   9338  -2533   -178  -1945       C  
ATOM   7825  CD  LYS B1047     -22.279 -17.186  85.049  1.00 85.97           C  
ANISOU 7825  CD  LYS B1047    12297   9945  10422  -2711   -427  -1710       C  
ATOM   7826  CE  LYS B1047     -23.195 -18.103  84.291  1.00105.48           C  
ANISOU 7826  CE  LYS B1047    14848  12571  12659  -3138   -436  -1887       C  
ATOM   7827  NZ  LYS B1047     -24.597 -17.612  84.334  1.00119.19           N  
ANISOU 7827  NZ  LYS B1047    16360  14568  14359  -3292   -696  -1568       N  
ATOM   7828  N   MET B1048     -17.700 -15.851  88.026  1.00 63.73           N  
ANISOU 7828  N   MET B1048     9456   6436   8325  -1535   -143  -1475       N  
ATOM   7829  CA  MET B1048     -16.930 -14.813  88.711  1.00 62.75           C  
ANISOU 7829  CA  MET B1048     9243   6335   8263  -1378   -217  -1291       C  
ATOM   7830  C   MET B1048     -15.439 -15.119  88.641  1.00 68.35           C  
ANISOU 7830  C   MET B1048     9935   6990   9046  -1250    -93  -1295       C  
ATOM   7831  O   MET B1048     -14.639 -14.193  88.496  1.00 67.68           O  
ANISOU 7831  O   MET B1048     9772   7023   8921  -1205   -143  -1191       O  
ATOM   7832  CB  MET B1048     -17.365 -14.693  90.175  1.00 64.08           C  
ANISOU 7832  CB  MET B1048     9410   6383   8556  -1306   -277  -1174       C  
ATOM   7833  CG  MET B1048     -18.552 -13.803  90.379  1.00 67.49           C  
ANISOU 7833  CG  MET B1048     9800   6874   8969  -1373   -371  -1087       C  
ATOM   7834  SD  MET B1048     -19.150 -13.818  92.086  1.00 71.44           S  
ANISOU 7834  SD  MET B1048    10340   7222   9584  -1333   -363  -1017       S  
ATOM   7835  CE  MET B1048     -18.022 -12.645  92.821  1.00 67.61           C  
ANISOU 7835  CE  MET B1048     9847   6769   9073  -1299   -369   -935       C  
ATOM   7836  N   ARG B1049     -15.068 -16.418  88.761  1.00 66.71           N  
ANISOU 7836  N   ARG B1049     9777   6581   8990  -1185     92  -1385       N  
ATOM   7837  CA  ARG B1049     -13.685 -16.898  88.710  1.00 67.83           C  
ANISOU 7837  CA  ARG B1049     9854   6624   9296  -1028    271  -1335       C  
ATOM   7838  C   ARG B1049     -13.092 -16.637  87.324  1.00 72.50           C  
ANISOU 7838  C   ARG B1049    10458   7339   9749  -1090    396  -1479       C  
ATOM   7839  O   ARG B1049     -11.974 -16.128  87.227  1.00 71.77           O  
ANISOU 7839  O   ARG B1049    10252   7324   9694   -983    415  -1349       O  
ATOM   7840  CB  ARG B1049     -13.599 -18.392  89.077  1.00 69.88           C  
ANISOU 7840  CB  ARG B1049    10148   6578   9826   -938    505  -1376       C  
ATOM   7841  CG  ARG B1049     -12.201 -18.806  89.516  1.00 84.50           C  
ANISOU 7841  CG  ARG B1049    11834   8313  11960   -713    655  -1145       C  
ATOM   7842  CD  ARG B1049     -12.017 -20.303  89.513  1.00102.45           C  
ANISOU 7842  CD  ARG B1049    14124  10226  14575   -604    996  -1191       C  
ATOM   7843  NE  ARG B1049     -10.601 -20.661  89.606  1.00119.09           N  
ANISOU 7843  NE  ARG B1049    16026  12223  17001   -372   1207   -943       N  
ATOM   7844  CZ  ARG B1049     -10.142 -21.908  89.680  1.00141.13           C  
ANISOU 7844  CZ  ARG B1049    18751  14654  20217   -201   1569   -870       C  
ATOM   7845  NH1 ARG B1049      -8.838 -22.134  89.761  1.00134.25           N  
ANISOU 7845  NH1 ARG B1049    17629  13704  19674     30   1761   -567       N  
ATOM   7846  NH2 ARG B1049     -10.983 -22.937  89.681  1.00128.45           N  
ANISOU 7846  NH2 ARG B1049    17307  12749  18751   -261   1762  -1071       N  
ATOM   7847  N   ALA B1050     -13.865 -16.945  86.261  1.00 70.57           N  
ANISOU 7847  N   ALA B1050    10346   7157   9311  -1305    467  -1732       N  
ATOM   7848  CA  ALA B1050     -13.483 -16.723  84.867  1.00 72.46           C  
ANISOU 7848  CA  ALA B1050    10625   7577   9328  -1452    585  -1895       C  
ATOM   7849  C   ALA B1050     -13.316 -15.230  84.583  1.00 75.63           C  
ANISOU 7849  C   ALA B1050    10902   8281   9553  -1471    343  -1694       C  
ATOM   7850  O   ALA B1050     -12.382 -14.848  83.883  1.00 75.92           O  
ANISOU 7850  O   ALA B1050    10890   8434   9523  -1453    432  -1688       O  
ATOM   7851  CB  ALA B1050     -14.530 -17.320  83.935  1.00 75.25           C  
ANISOU 7851  CB  ALA B1050    11144   8010   9437  -1777    648  -2176       C  
ATOM   7852  N   ALA B1051     -14.201 -14.393  85.161  1.00 71.41           N  
ANISOU 7852  N   ALA B1051    10308   7838   8988  -1494     77  -1520       N  
ATOM   7853  CA  ALA B1051     -14.180 -12.936  85.020  1.00 70.43           C  
ANISOU 7853  CA  ALA B1051    10060   7920   8781  -1500   -115  -1304       C  
ATOM   7854  C   ALA B1051     -12.980 -12.320  85.751  1.00 74.00           C  
ANISOU 7854  C   ALA B1051    10423   8309   9386  -1312   -124  -1148       C  
ATOM   7855  O   ALA B1051     -12.337 -11.433  85.200  1.00 73.76           O  
ANISOU 7855  O   ALA B1051    10310   8431   9285  -1320   -155  -1049       O  
ATOM   7856  CB  ALA B1051     -15.477 -12.335  85.552  1.00 69.91           C  
ANISOU 7856  CB  ALA B1051     9952   7873   8736  -1551   -300  -1165       C  
ATOM   7857  N   ALA B1052     -12.676 -12.795  86.975  1.00 70.50           N  
ANISOU 7857  N   ALA B1052     9981   7674   9131  -1179   -109  -1099       N  
ATOM   7858  CA  ALA B1052     -11.563 -12.298  87.784  1.00 70.00           C  
ANISOU 7858  CA  ALA B1052     9817   7606   9173  -1073   -151   -920       C  
ATOM   7859  C   ALA B1052     -10.201 -12.616  87.141  1.00 76.38           C  
ANISOU 7859  C   ALA B1052    10535   8451  10035   -982      5   -896       C  
ATOM   7860  O   ALA B1052      -9.349 -11.727  87.067  1.00 75.45           O  
ANISOU 7860  O   ALA B1052    10311   8463   9893   -977    -56   -756       O  
ATOM   7861  CB  ALA B1052     -11.634 -12.881  89.184  1.00 70.22           C  
ANISOU 7861  CB  ALA B1052     9850   7491   9342  -1012   -183   -837       C  
ATOM   7862  N   LEU B1053     -10.015 -13.864  86.650  1.00 75.95           N  
ANISOU 7862  N   LEU B1053    10523   8260  10072   -923    245  -1039       N  
ATOM   7863  CA  LEU B1053      -8.781 -14.334  86.007  1.00 78.37           C  
ANISOU 7863  CA  LEU B1053    10745   8538  10495   -812    496  -1036       C  
ATOM   7864  C   LEU B1053      -8.525 -13.624  84.668  1.00 85.98           C  
ANISOU 7864  C   LEU B1053    11722   9721  11227   -928    539  -1136       C  
ATOM   7865  O   LEU B1053      -7.369 -13.377  84.311  1.00 86.23           O  
ANISOU 7865  O   LEU B1053    11625   9821  11318   -844    646  -1031       O  
ATOM   7866  CB  LEU B1053      -8.830 -15.853  85.801  1.00 80.44           C  
ANISOU 7866  CB  LEU B1053    11088   8523  10953   -742    825  -1215       C  
ATOM   7867  CG  LEU B1053      -8.603 -16.697  87.044  1.00 85.44           C  
ANISOU 7867  CG  LEU B1053    11622   8925  11915   -564    860  -1008       C  
ATOM   7868  CD1 LEU B1053      -9.221 -18.068  86.888  1.00 87.87           C  
ANISOU 7868  CD1 LEU B1053    12076   8925  12384   -563   1138  -1234       C  
ATOM   7869  CD2 LEU B1053      -7.123 -16.804  87.377  1.00 90.11           C  
ANISOU 7869  CD2 LEU B1053    11953   9501  12785   -356    972   -689       C  
ATOM   7870  N   ASP B1054      -9.607 -13.299  83.942  1.00 85.18           N  
ANISOU 7870  N   ASP B1054    11743   9760  10862  -1134    446  -1289       N  
ATOM   7871  CA  ASP B1054      -9.569 -12.586  82.665  1.00 87.36           C  
ANISOU 7871  CA  ASP B1054    12018  10310  10865  -1301    438  -1331       C  
ATOM   7872  C   ASP B1054      -9.172 -11.119  82.912  1.00 90.30           C  
ANISOU 7872  C   ASP B1054    12240  10841  11230  -1267    207  -1053       C  
ATOM   7873  O   ASP B1054      -8.317 -10.597  82.195  1.00 91.29           O  
ANISOU 7873  O   ASP B1054    12280  11122  11283  -1276    265   -986       O  
ATOM   7874  CB  ASP B1054     -10.941 -12.688  81.965  1.00 90.81           C  
ANISOU 7874  CB  ASP B1054    12577  10896  11033  -1565    353  -1478       C  
ATOM   7875  CG  ASP B1054     -11.033 -12.192  80.532  1.00113.39           C  
ANISOU 7875  CG  ASP B1054    15436  14101  13545  -1817    351  -1512       C  
ATOM   7876  OD1 ASP B1054     -10.280 -11.256  80.169  1.00115.69           O  
ANISOU 7876  OD1 ASP B1054    15602  14553  13800  -1776    304  -1333       O  
ATOM   7877  OD2 ASP B1054     -11.879 -12.716  79.784  1.00124.41           O  
ANISOU 7877  OD2 ASP B1054    16947  15638  14684  -2092    380  -1694       O  
ATOM   7878  N   ALA B1055      -9.775 -10.469  83.941  1.00 84.89           N  
ANISOU 7878  N   ALA B1055    11531  10090  10632  -1242    -13   -908       N  
ATOM   7879  CA  ALA B1055      -9.501  -9.075  84.318  1.00 83.64           C  
ANISOU 7879  CA  ALA B1055    11270  10002  10508  -1244   -179   -689       C  
ATOM   7880  C   ALA B1055      -8.079  -8.920  84.839  1.00 88.45           C  
ANISOU 7880  C   ALA B1055    11769  10594  11244  -1140   -147   -565       C  
ATOM   7881  O   ALA B1055      -7.488  -7.850  84.692  1.00 88.56           O  
ANISOU 7881  O   ALA B1055    11691  10715  11244  -1180   -216   -418       O  
ATOM   7882  CB  ALA B1055     -10.492  -8.601  85.368  1.00 82.72           C  
ANISOU 7882  CB  ALA B1055    11196   9758  10477  -1262   -320   -634       C  
ATOM   7883  N   GLN B1056      -7.527  -9.992  85.423  1.00 85.70           N  
ANISOU 7883  N   GLN B1056    11402  10118  11040  -1019    -37   -584       N  
ATOM   7884  CA  GLN B1056      -6.165 -10.059  85.939  1.00 86.92           C  
ANISOU 7884  CA  GLN B1056    11390  10289  11347   -921     -6   -390       C  
ATOM   7885  C   GLN B1056      -5.128  -9.929  84.804  1.00 95.83           C  
ANISOU 7885  C   GLN B1056    12407  11548  12456   -881    158   -360       C  
ATOM   7886  O   GLN B1056      -4.071  -9.336  85.017  1.00 97.42           O  
ANISOU 7886  O   GLN B1056    12440  11858  12718   -869    105   -146       O  
ATOM   7887  CB  GLN B1056      -5.979 -11.391  86.670  1.00 88.83           C  
ANISOU 7887  CB  GLN B1056    11599  10353  11797   -781    112   -361       C  
ATOM   7888  CG  GLN B1056      -4.747 -11.494  87.549  1.00 95.78           C  
ANISOU 7888  CG  GLN B1056    12248  11281  12862   -701     73    -42       C  
ATOM   7889  CD  GLN B1056      -4.726 -12.808  88.279  1.00111.86           C  
ANISOU 7889  CD  GLN B1056    14224  13136  15141   -558    185     57       C  
ATOM   7890  OE1 GLN B1056      -4.956 -13.881  87.705  1.00108.46           O  
ANISOU 7890  OE1 GLN B1056    13857  12499  14853   -433    459   -105       O  
ATOM   7891  NE2 GLN B1056      -4.464 -12.751  89.568  1.00103.09           N  
ANISOU 7891  NE2 GLN B1056    12994  12102  14075   -608    -11    328       N  
ATOM   7892  N   LYS B1057      -5.440 -10.478  83.610  1.00 94.23           N  
ANISOU 7892  N   LYS B1057    12304  11358  12142   -903    364   -580       N  
ATOM   7893  CA  LYS B1057      -4.578 -10.496  82.421  1.00 96.64           C  
ANISOU 7893  CA  LYS B1057    12545  11787  12385   -896    591   -617       C  
ATOM   7894  C   LYS B1057      -4.411  -9.116  81.753  1.00103.02           C  
ANISOU 7894  C   LYS B1057    13292  12854  12997  -1029    433   -493       C  
ATOM   7895  O   LYS B1057      -3.420  -8.917  81.042  1.00104.54           O  
ANISOU 7895  O   LYS B1057    13372  13173  13176  -1007    578   -427       O  
ATOM   7896  CB  LYS B1057      -5.132 -11.493  81.387  1.00100.21           C  
ANISOU 7896  CB  LYS B1057    13181  12194  12700   -979    871   -950       C  
ATOM   7897  CG  LYS B1057      -4.991 -12.952  81.807  1.00110.18           C  
ANISOU 7897  CG  LYS B1057    14487  13143  14234   -826   1163  -1078       C  
ATOM   7898  CD  LYS B1057      -5.912 -13.843  81.007  1.00120.15           C  
ANISOU 7898  CD  LYS B1057    16000  14334  15318  -1003   1379  -1463       C  
ATOM   7899  CE  LYS B1057      -5.876 -15.264  81.506  1.00132.87           C  
ANISOU 7899  CE  LYS B1057    17667  15564  17253   -855   1687  -1588       C  
ATOM   7900  NZ  LYS B1057      -6.911 -16.109  80.852  1.00144.77           N  
ANISOU 7900  NZ  LYS B1057    19449  16986  18569  -1092   1869  -1991       N  
ATOM   7901  N   ALA B1058      -5.371  -8.185  81.967  1.00100.08           N  
ANISOU 7901  N   ALA B1058    12975  12538  12514  -1154    176   -439       N  
ATOM   7902  CA  ALA B1058      -5.408  -6.832  81.382  1.00101.20           C  
ANISOU 7902  CA  ALA B1058    13047  12872  12532  -1275     36   -277       C  
ATOM   7903  C   ALA B1058      -4.147  -5.995  81.683  1.00108.80           C  
ANISOU 7903  C   ALA B1058    13841  13885  13614  -1239     -5    -55       C  
ATOM   7904  O   ALA B1058      -3.610  -6.052  82.797  1.00108.25           O  
ANISOU 7904  O   ALA B1058    13714  13703  13713  -1179    -67     31       O  
ATOM   7905  CB  ALA B1058      -6.637  -6.092  81.867  1.00100.31           C  
ANISOU 7905  CB  ALA B1058    12991  12696  12426  -1355   -169   -216       C  
ATOM   7906  N   THR B1059      -3.687  -5.221  80.666  1.00108.46           N  
ANISOU 7906  N   THR B1059    13708  14048  13455  -1317     17     59       N  
ATOM   7907  CA  THR B1059      -2.483  -4.377  80.722  1.00109.63           C  
ANISOU 7907  CA  THR B1059    13684  14280  13692  -1320     -9    277       C  
ATOM   7908  C   THR B1059      -2.769  -2.967  80.143  1.00115.73           C  
ANISOU 7908  C   THR B1059    14411  15167  14396  -1461   -130    456       C  
ATOM   7909  O   THR B1059      -3.386  -2.885  79.079  1.00116.27           O  
ANISOU 7909  O   THR B1059    14501  15399  14278  -1539   -106    455       O  
ATOM   7910  CB  THR B1059      -1.328  -5.058  79.942  1.00118.19           C  
ANISOU 7910  CB  THR B1059    14656  15488  14761  -1233    242    266       C  
ATOM   7911  OG1 THR B1059      -1.384  -6.477  80.106  1.00117.57           O  
ANISOU 7911  OG1 THR B1059    14648  15267  14755  -1102    446     69       O  
ATOM   7912  CG2 THR B1059       0.051  -4.539  80.338  1.00116.98           C  
ANISOU 7912  CG2 THR B1059    14282  15393  14772  -1198    220    515       C  
ATOM   7913  N   PRO B1060      -2.312  -1.850  80.775  1.00113.39           N  
ANISOU 7913  N   PRO B1060    14037  14800  14245  -1526   -245    634       N  
ATOM   7914  CA  PRO B1060      -2.568  -0.522  80.187  1.00114.33           C  
ANISOU 7914  CA  PRO B1060    14097  14970  14375  -1641   -305    833       C  
ATOM   7915  C   PRO B1060      -1.636  -0.237  78.993  1.00121.53           C  
ANISOU 7915  C   PRO B1060    14856  16153  15170  -1673   -221    987       C  
ATOM   7916  O   PRO B1060      -0.639  -0.951  78.840  1.00122.16           O  
ANISOU 7916  O   PRO B1060    14868  16335  15214  -1600   -103    934       O  
ATOM   7917  CB  PRO B1060      -2.307   0.448  81.357  1.00115.52           C  
ANISOU 7917  CB  PRO B1060    14259  14901  14733  -1734   -388    900       C  
ATOM   7918  CG  PRO B1060      -2.029  -0.403  82.559  1.00118.83           C  
ANISOU 7918  CG  PRO B1060    14744  15225  15182  -1701   -419    747       C  
ATOM   7919  CD  PRO B1060      -1.561  -1.720  82.037  1.00114.70           C  
ANISOU 7919  CD  PRO B1060    14165  14852  14564  -1546   -318    676       C  
ATOM   7920  N   PRO B1061      -1.919   0.777  78.127  1.00119.89           N  
ANISOU 7920  N   PRO B1061    14565  16064  14924  -1772   -255   1211       N  
ATOM   7921  CA  PRO B1061      -1.016   1.036  76.990  1.00126.06           C  
ANISOU 7921  CA  PRO B1061    15198  17135  15564  -1824   -170   1367       C  
ATOM   7922  C   PRO B1061       0.310   1.664  77.427  1.00162.13           C  
ANISOU 7922  C   PRO B1061    19635  21667  20302  -1840   -165   1501       C  
ATOM   7923  O   PRO B1061       1.376   1.108  77.170  1.00126.10           O  
ANISOU 7923  O   PRO B1061    14977  17248  15686  -1785    -47   1479       O  
ATOM   7924  CB  PRO B1061      -1.821   2.000  76.119  1.00128.45           C  
ANISOU 7924  CB  PRO B1061    15426  17564  15817  -1939   -245   1641       C  
ATOM   7925  CG  PRO B1061      -2.694   2.725  77.080  1.00130.32           C  
ANISOU 7925  CG  PRO B1061    15714  17460  16342  -1926   -341   1704       C  
ATOM   7926  CD  PRO B1061      -3.062   1.718  78.128  1.00122.74           C  
ANISOU 7926  CD  PRO B1061    14929  16302  15403  -1833   -346   1381       C  
ATOM   7927  N   SER B1067       3.927  -0.356  82.263  1.00149.59           N  
ANISOU 7927  N   SER B1067    17732  19871  19235  -1780   -357   1525       N  
ATOM   7928  CA  SER B1067       4.872  -1.468  82.225  1.00150.85           C  
ANISOU 7928  CA  SER B1067    17666  20153  19498  -1592   -227   1658       C  
ATOM   7929  C   SER B1067       4.203  -2.777  82.698  1.00153.48           C  
ANISOU 7929  C   SER B1067    18107  20333  19875  -1405   -155   1491       C  
ATOM   7930  O   SER B1067       3.402  -2.731  83.637  1.00151.67           O  
ANISOU 7930  O   SER B1067    18049  19973  19608  -1501   -316   1375       O  
ATOM   7931  CB  SER B1067       6.093  -1.152  83.087  1.00156.10           C  
ANISOU 7931  CB  SER B1067    18066  20983  20264  -1754   -382   1972       C  
ATOM   7932  OG  SER B1067       7.120  -2.118  82.933  1.00166.74           O  
ANISOU 7932  OG  SER B1067    19108  22458  21788  -1546   -224   2209       O  
ATOM   7933  N   PRO B1068       4.492  -3.953  82.076  1.00150.53           N  
ANISOU 7933  N   PRO B1068    17650  19946  19599  -1151    124   1459       N  
ATOM   7934  CA  PRO B1068       3.861  -5.204  82.557  1.00149.21           C  
ANISOU 7934  CA  PRO B1068    17587  19589  19518   -985    217   1308       C  
ATOM   7935  C   PRO B1068       4.475  -5.690  83.880  1.00151.75           C  
ANISOU 7935  C   PRO B1068    17695  19925  20038   -971     85   1591       C  
ATOM   7936  O   PRO B1068       3.839  -6.423  84.642  1.00150.29           O  
ANISOU 7936  O   PRO B1068    17607  19597  19900   -919     44   1518       O  
ATOM   7937  CB  PRO B1068       4.115  -6.195  81.417  1.00153.08           C  
ANISOU 7937  CB  PRO B1068    18053  20033  20078   -763    626   1182       C  
ATOM   7938  CG  PRO B1068       5.340  -5.688  80.731  1.00160.04           C  
ANISOU 7938  CG  PRO B1068    18682  21115  21012   -759    743   1412       C  
ATOM   7939  CD  PRO B1068       5.405  -4.200  80.935  1.00154.41           C  
ANISOU 7939  CD  PRO B1068    17960  20561  20147  -1017    414   1545       C  
ATOM   7940  N   ASP B1069       5.712  -5.250  84.144  1.00148.68           N  
ANISOU 7940  N   ASP B1069    16994  19749  19749  -1050     -1   1953       N  
ATOM   7941  CA  ASP B1069       6.516  -5.560  85.321  1.00149.61           C  
ANISOU 7941  CA  ASP B1069    16815  20007  20024  -1110   -172   2349       C  
ATOM   7942  C   ASP B1069       6.203  -4.594  86.482  1.00149.71           C  
ANISOU 7942  C   ASP B1069    16947  20130  19804  -1505   -562   2356       C  
ATOM   7943  O   ASP B1069       6.506  -4.918  87.633  1.00150.73           O  
ANISOU 7943  O   ASP B1069    16921  20391  19959  -1634   -753   2613       O  
ATOM   7944  CB  ASP B1069       8.016  -5.483  84.953  1.00154.99           C  
ANISOU 7944  CB  ASP B1069    17070  20913  20908  -1052    -76   2768       C  
ATOM   7945  CG  ASP B1069       8.340  -5.856  83.512  1.00166.39           C  
ANISOU 7945  CG  ASP B1069    18475  22272  22473   -776    345   2656       C  
ATOM   7946  OD1 ASP B1069       8.290  -7.062  83.184  1.00168.54           O  
ANISOU 7946  OD1 ASP B1069    18716  22345  22978   -472    694   2598       O  
ATOM   7947  OD2 ASP B1069       8.625  -4.937  82.709  1.00171.43           O  
ANISOU 7947  OD2 ASP B1069    19132  23033  22969   -888    354   2610       O  
ATOM   7948  N   SER B1070       5.590  -3.417  86.166  1.00141.87           N  
ANISOU 7948  N   SER B1070    16227  19081  18596  -1713   -646   2084       N  
ATOM   7949  CA  SER B1070       5.222  -2.296  87.054  1.00139.57           C  
ANISOU 7949  CA  SER B1070    16121  18806  18103  -2111   -899   1988       C  
ATOM   7950  C   SER B1070       4.667  -2.728  88.431  1.00140.47           C  
ANISOU 7950  C   SER B1070    16345  18899  18127  -2264  -1066   1950       C  
ATOM   7951  O   SER B1070       3.875  -3.675  88.493  1.00138.79           O  
ANISOU 7951  O   SER B1070    16245  18517  17971  -2031   -971   1811       O  
ATOM   7952  CB  SER B1070       4.197  -1.397  86.369  1.00139.93           C  
ANISOU 7952  CB  SER B1070    16482  18634  18052  -2143   -828   1653       C  
ATOM   7953  OG  SER B1070       4.033  -0.162  87.044  1.00147.42           O  
ANISOU 7953  OG  SER B1070    17583  19545  18886  -2520   -970   1573       O  
ATOM   7954  N   PRO B1071       5.058  -2.030  89.537  1.00136.14           N  
ANISOU 7954  N   PRO B1071    15781  18538  17410  -2701  -1305   2059       N  
ATOM   7955  CA  PRO B1071       4.546  -2.408  90.872  1.00135.08           C  
ANISOU 7955  CA  PRO B1071    15761  18438  17126  -2911  -1460   2024       C  
ATOM   7956  C   PRO B1071       3.043  -2.183  91.024  1.00132.84           C  
ANISOU 7956  C   PRO B1071    15898  17821  16753  -2899  -1367   1572       C  
ATOM   7957  O   PRO B1071       2.420  -2.881  91.820  1.00132.15           O  
ANISOU 7957  O   PRO B1071    15904  17696  16611  -2892  -1408   1518       O  
ATOM   7958  CB  PRO B1071       5.326  -1.510  91.840  1.00140.01           C  
ANISOU 7958  CB  PRO B1071    16312  19366  17518  -3478  -1704   2183       C  
ATOM   7959  CG  PRO B1071       6.412  -0.902  91.045  1.00146.43           C  
ANISOU 7959  CG  PRO B1071    16881  20329  18425  -3502  -1696   2400       C  
ATOM   7960  CD  PRO B1071       5.980  -0.880  89.626  1.00139.57           C  
ANISOU 7960  CD  PRO B1071    16105  19178  17749  -3076  -1434   2204       C  
ATOM   7961  N   GLU B1072       2.466  -1.216  90.269  1.00124.90           N  
ANISOU 7961  N   GLU B1072    15113  16582  15762  -2892  -1236   1299       N  
ATOM   7962  CA  GLU B1072       1.028  -0.927  90.270  1.00120.89           C  
ANISOU 7962  CA  GLU B1072    14945  15747  15243  -2843  -1114    938       C  
ATOM   7963  C   GLU B1072       0.290  -2.125  89.714  1.00119.14           C  
ANISOU 7963  C   GLU B1072    14734  15404  15131  -2428  -1008    876       C  
ATOM   7964  O   GLU B1072      -0.712  -2.547  90.290  1.00117.20           O  
ANISOU 7964  O   GLU B1072    14670  15009  14851  -2401   -993    701       O  
ATOM   7965  CB  GLU B1072       0.697   0.334  89.450  1.00121.86           C  
ANISOU 7965  CB  GLU B1072    15198  15669  15435  -2885   -986    795       C  
ATOM   7966  CG  GLU B1072       1.166   1.638  90.077  1.00136.05           C  
ANISOU 7966  CG  GLU B1072    17079  17465  17150  -3343  -1020    754       C  
ATOM   7967  CD  GLU B1072       2.577   2.093  89.748  1.00161.30           C  
ANISOU 7967  CD  GLU B1072    20023  20928  20338  -3508  -1118   1021       C  
ATOM   7968  OE1 GLU B1072       3.396   1.265  89.286  1.00152.95           O  
ANISOU 7968  OE1 GLU B1072    18671  20119  19325  -3287  -1186   1297       O  
ATOM   7969  OE2 GLU B1072       2.868   3.291  89.969  1.00160.57           O  
ANISOU 7969  OE2 GLU B1072    20021  20771  20216  -3869  -1095    955       O  
ATOM   7970  N   MET B1073       0.826  -2.706  88.624  1.00113.89           N  
ANISOU 7970  N   MET B1073    13875  14809  14589  -2136   -911   1010       N  
ATOM   7971  CA  MET B1073       0.275  -3.889  87.970  1.00112.01           C  
ANISOU 7971  CA  MET B1073    13651  14461  14447  -1789   -760    925       C  
ATOM   7972  C   MET B1073       0.403  -5.122  88.867  1.00114.68           C  
ANISOU 7972  C   MET B1073    13890  14829  14853  -1704   -797   1054       C  
ATOM   7973  O   MET B1073      -0.506  -5.954  88.881  1.00112.97           O  
ANISOU 7973  O   MET B1073    13808  14441  14673  -1538   -712    890       O  
ATOM   7974  CB  MET B1073       0.949  -4.127  86.608  1.00115.26           C  
ANISOU 7974  CB  MET B1073    13897  14948  14947  -1573   -589   1008       C  
ATOM   7975  CG  MET B1073       0.324  -3.329  85.473  1.00117.91           C  
ANISOU 7975  CG  MET B1073    14372  15222  15207  -1569   -509    844       C  
ATOM   7976  SD  MET B1073      -1.341  -3.892  85.020  1.00120.16           S  
ANISOU 7976  SD  MET B1073    14914  15309  15431  -1438   -421    546       S  
ATOM   7977  CE  MET B1073      -2.341  -2.526  85.671  1.00115.65           C  
ANISOU 7977  CE  MET B1073    14531  14578  14834  -1661   -545    465       C  
ATOM   7978  N   LYS B1074       1.509  -5.218  89.636  1.00112.14           N  
ANISOU 7978  N   LYS B1074    13313  14745  14551  -1842   -936   1386       N  
ATOM   7979  CA  LYS B1074       1.772  -6.311  90.576  1.00112.83           C  
ANISOU 7979  CA  LYS B1074    13225  14917  14726  -1794  -1002   1642       C  
ATOM   7980  C   LYS B1074       0.696  -6.339  91.683  1.00114.24           C  
ANISOU 7980  C   LYS B1074    13661  15015  14730  -1982  -1122   1453       C  
ATOM   7981  O   LYS B1074       0.167  -7.414  91.974  1.00113.49           O  
ANISOU 7981  O   LYS B1074    13581  14802  14738  -1794  -1061   1457       O  
ATOM   7982  CB  LYS B1074       3.186  -6.179  91.177  1.00118.51           C  
ANISOU 7982  CB  LYS B1074    13573  15990  15465  -1987  -1179   2115       C  
ATOM   7983  CG  LYS B1074       3.727  -7.466  91.801  1.00131.30           C  
ANISOU 7983  CG  LYS B1074    14863  17720  17305  -1824  -1191   2547       C  
ATOM   7984  CD  LYS B1074       5.252  -7.493  91.801  1.00140.74           C  
ANISOU 7984  CD  LYS B1074    15579  19233  18663  -1849  -1256   3093       C  
ATOM   7985  CE  LYS B1074       5.822  -8.703  92.504  1.00148.41           C  
ANISOU 7985  CE  LYS B1074    16149  20331  19908  -1699  -1274   3639       C  
ATOM   7986  NZ  LYS B1074       5.820  -8.544  93.982  1.00155.66           N  
ANISOU 7986  NZ  LYS B1074    17009  21591  20543  -2139  -1645   3894       N  
ATOM   7987  N   ASP B1075       0.352  -5.156  92.259  1.00109.19           N  
ANISOU 7987  N   ASP B1075    13236  14403  13848  -2352  -1242   1268       N  
ATOM   7988  CA  ASP B1075      -0.668  -4.987  93.308  1.00107.54           C  
ANISOU 7988  CA  ASP B1075    13301  14105  13454  -2580  -1298   1042       C  
ATOM   7989  C   ASP B1075      -2.067  -5.209  92.740  1.00105.32           C  
ANISOU 7989  C   ASP B1075    13277  13482  13259  -2321  -1119    703       C  
ATOM   7990  O   ASP B1075      -2.970  -5.622  93.474  1.00104.32           O  
ANISOU 7990  O   ASP B1075    13309  13255  13073  -2351  -1118    576       O  
ATOM   7991  CB  ASP B1075      -0.582  -3.590  93.955  1.00111.07           C  
ANISOU 7991  CB  ASP B1075    13922  14618  13661  -3061  -1375    894       C  
ATOM   7992  CG  ASP B1075       0.781  -3.190  94.506  1.00130.11           C  
ANISOU 7992  CG  ASP B1075    16098  17415  15924  -3431  -1579   1207       C  
ATOM   7993  OD1 ASP B1075       1.534  -4.089  94.953  1.00134.10           O  
ANISOU 7993  OD1 ASP B1075    16295  18207  16449  -3408  -1732   1607       O  
ATOM   7994  OD2 ASP B1075       1.086  -1.976  94.510  1.00137.90           O  
ANISOU 7994  OD2 ASP B1075    17188  18415  16792  -3762  -1582   1084       O  
ATOM   7995  N   PHE B1076      -2.240  -4.921  91.432  1.00 97.65           N  
ANISOU 7995  N   PHE B1076    12326  12372  12405  -2101   -979    589       N  
ATOM   7996  CA  PHE B1076      -3.490  -5.110  90.705  1.00 93.81           C  
ANISOU 7996  CA  PHE B1076    12023  11639  11984  -1887   -836    338       C  
ATOM   7997  C   PHE B1076      -3.728  -6.606  90.500  1.00 95.35           C  
ANISOU 7997  C   PHE B1076    12157  11778  12293  -1609   -761    363       C  
ATOM   7998  O   PHE B1076      -4.804  -7.094  90.841  1.00 93.60           O  
ANISOU 7998  O   PHE B1076    12091  11405  12067  -1562   -732    208       O  
ATOM   7999  CB  PHE B1076      -3.462  -4.347  89.366  1.00 94.73           C  
ANISOU 7999  CB  PHE B1076    12130  11718  12143  -1804   -742    288       C  
ATOM   8000  CG  PHE B1076      -4.548  -4.724  88.384  1.00 94.51           C  
ANISOU 8000  CG  PHE B1076    12203  11551  12154  -1599   -624    126       C  
ATOM   8001  CD1 PHE B1076      -5.832  -4.205  88.510  1.00 96.19           C  
ANISOU 8001  CD1 PHE B1076    12592  11589  12368  -1645   -599    -25       C  
ATOM   8002  CD2 PHE B1076      -4.284  -5.589  87.326  1.00 96.66           C  
ANISOU 8002  CD2 PHE B1076    12385  11882  12460  -1393   -516    135       C  
ATOM   8003  CE1 PHE B1076      -6.835  -4.551  87.600  1.00 96.00           C  
ANISOU 8003  CE1 PHE B1076    12614  11505  12355  -1506   -531   -111       C  
ATOM   8004  CE2 PHE B1076      -5.290  -5.939  86.419  1.00 98.48           C  
ANISOU 8004  CE2 PHE B1076    12718  12046  12654  -1299   -426    -22       C  
ATOM   8005  CZ  PHE B1076      -6.557  -5.415  86.561  1.00 95.35           C  
ANISOU 8005  CZ  PHE B1076    12459  11533  12236  -1365   -467   -117       C  
ATOM   8006  N   ARG B1077      -2.719  -7.331  89.961  1.00 92.14           N  
ANISOU 8006  N   ARG B1077    11521  11468  12020  -1431   -690    561       N  
ATOM   8007  CA  ARG B1077      -2.783  -8.777  89.728  1.00 92.10           C  
ANISOU 8007  CA  ARG B1077    11448  11353  12195  -1166   -535    589       C  
ATOM   8008  C   ARG B1077      -2.967  -9.531  91.048  1.00 95.73           C  
ANISOU 8008  C   ARG B1077    11873  11809  12691  -1207   -635    737       C  
ATOM   8009  O   ARG B1077      -3.738 -10.491  91.084  1.00 94.99           O  
ANISOU 8009  O   ARG B1077    11872  11528  12691  -1061   -530    624       O  
ATOM   8010  CB  ARG B1077      -1.534  -9.285  88.993  1.00 95.01           C  
ANISOU 8010  CB  ARG B1077    11550  11793  12757   -979   -373    804       C  
ATOM   8011  CG  ARG B1077      -1.504  -8.935  87.508  1.00108.34           C  
ANISOU 8011  CG  ARG B1077    13296  13462  14406   -898   -195    616       C  
ATOM   8012  CD  ARG B1077      -0.377  -9.638  86.767  1.00127.45           C  
ANISOU 8012  CD  ARG B1077    15482  15898  17045   -687     63    774       C  
ATOM   8013  NE  ARG B1077       0.951  -9.143  87.150  1.00143.40           N  
ANISOU 8013  NE  ARG B1077    17198  18143  19146   -744    -46   1153       N  
ATOM   8014  CZ  ARG B1077       1.637  -8.220  86.479  1.00158.69           C  
ANISOU 8014  CZ  ARG B1077    19047  20244  21004   -824    -60   1213       C  
ATOM   8015  NH1 ARG B1077       1.129  -7.672  85.382  1.00147.06           N  
ANISOU 8015  NH1 ARG B1077    17761  18748  19367   -850     27    942       N  
ATOM   8016  NH2 ARG B1077       2.835  -7.839  86.902  1.00144.70           N  
ANISOU 8016  NH2 ARG B1077    16977  18691  19312   -903   -174   1583       N  
ATOM   8017  N   HIS B1078      -2.292  -9.072  92.134  1.00 92.58           N  
ANISOU 8017  N   HIS B1078    11345  11643  12188  -1453   -847    993       N  
ATOM   8018  CA  HIS B1078      -2.387  -9.669  93.472  1.00 92.57           C  
ANISOU 8018  CA  HIS B1078    11285  11736  12150  -1574   -986   1196       C  
ATOM   8019  C   HIS B1078      -3.797  -9.503  94.054  1.00 91.83           C  
ANISOU 8019  C   HIS B1078    11513  11490  11888  -1695  -1007    879       C  
ATOM   8020  O   HIS B1078      -4.263 -10.398  94.757  1.00 92.09           O  
ANISOU 8020  O   HIS B1078    11549  11476  11965  -1652  -1017    954       O  
ATOM   8021  CB  HIS B1078      -1.334  -9.087  94.432  1.00 95.82           C  
ANISOU 8021  CB  HIS B1078    11492  12518  12397  -1915  -1231   1537       C  
ATOM   8022  CG  HIS B1078      -1.298  -9.767  95.767  1.00101.33           C  
ANISOU 8022  CG  HIS B1078    12070  13405  13027  -2076  -1396   1839       C  
ATOM   8023  ND1 HIS B1078      -0.917 -11.093  95.894  1.00105.13           N  
ANISOU 8023  ND1 HIS B1078    12263  13870  13813  -1803  -1335   2221       N  
ATOM   8024  CD2 HIS B1078      -1.615  -9.286  96.991  1.00103.96           C  
ANISOU 8024  CD2 HIS B1078    12536  13939  13024  -2495  -1588   1814       C  
ATOM   8025  CE1 HIS B1078      -1.013 -11.374  97.183  1.00106.37           C  
ANISOU 8025  CE1 HIS B1078    12357  14254  13804  -2057  -1536   2468       C  
ATOM   8026  NE2 HIS B1078      -1.435 -10.319  97.883  1.00106.10           N  
ANISOU 8026  NE2 HIS B1078    12587  14378  13349  -2498  -1695   2213       N  
ATOM   8027  N   GLY B1079      -4.467  -8.395  93.723  1.00 84.31           N  
ANISOU 8027  N   GLY B1079    10801  10442  10793  -1822   -983    563       N  
ATOM   8028  CA  GLY B1079      -5.833  -8.109  94.159  1.00 81.60           C  
ANISOU 8028  CA  GLY B1079    10737   9920  10348  -1910   -945    273       C  
ATOM   8029  C   GLY B1079      -6.836  -9.154  93.706  1.00 81.27           C  
ANISOU 8029  C   GLY B1079    10769   9657  10454  -1636   -821    145       C  
ATOM   8030  O   GLY B1079      -7.795  -9.453  94.420  1.00 78.87           O  
ANISOU 8030  O   GLY B1079    10604   9259  10104  -1686   -819     42       O  
ATOM   8031  N   PHE B1080      -6.600  -9.725  92.514  1.00 77.61           N  
ANISOU 8031  N   PHE B1080    10218   9117  10152  -1381   -699    138       N  
ATOM   8032  CA  PHE B1080      -7.417 -10.780  91.930  1.00 76.73           C  
ANISOU 8032  CA  PHE B1080    10179   8808  10165  -1173   -554     -7       C  
ATOM   8033  C   PHE B1080      -6.949 -12.136  92.417  1.00 83.20           C  
ANISOU 8033  C   PHE B1080    10848   9587  11176  -1030   -498    205       C  
ATOM   8034  O   PHE B1080      -7.761 -13.053  92.497  1.00 82.65           O  
ANISOU 8034  O   PHE B1080    10867   9339  11198   -937   -408    105       O  
ATOM   8035  CB  PHE B1080      -7.398 -10.716  90.399  1.00 78.05           C  
ANISOU 8035  CB  PHE B1080    10359   8935  10364  -1049   -412   -154       C  
ATOM   8036  CG  PHE B1080      -8.264  -9.607  89.854  1.00 78.09           C  
ANISOU 8036  CG  PHE B1080    10502   8937  10233  -1154   -450   -325       C  
ATOM   8037  CD1 PHE B1080      -9.637  -9.777  89.717  1.00 80.41           C  
ANISOU 8037  CD1 PHE B1080    10939   9113  10501  -1161   -430   -493       C  
ATOM   8038  CD2 PHE B1080      -7.712  -8.383  89.501  1.00 79.88           C  
ANISOU 8038  CD2 PHE B1080    10681   9276  10394  -1250   -501   -267       C  
ATOM   8039  CE1 PHE B1080     -10.441  -8.746  89.227  1.00 80.38           C  
ANISOU 8039  CE1 PHE B1080    10993   9111  10436  -1238   -455   -553       C  
ATOM   8040  CE2 PHE B1080      -8.516  -7.352  89.016  1.00 81.98           C  
ANISOU 8040  CE2 PHE B1080    11033   9508  10610  -1324   -507   -352       C  
ATOM   8041  CZ  PHE B1080      -9.873  -7.542  88.873  1.00 79.41           C  
ANISOU 8041  CZ  PHE B1080    10813   9072  10288  -1306   -482   -470       C  
ATOM   8042  N   ASP B1081      -5.646 -12.265  92.762  1.00 82.19           N  
ANISOU 8042  N   ASP B1081    10465   9623  11141  -1018   -544    541       N  
ATOM   8043  CA  ASP B1081      -5.088 -13.505  93.307  1.00 84.37           C  
ANISOU 8043  CA  ASP B1081    10517   9867  11672   -868   -483    869       C  
ATOM   8044  C   ASP B1081      -5.776 -13.830  94.634  1.00 86.94           C  
ANISOU 8044  C   ASP B1081    10902  10228  11903  -1012   -633    959       C  
ATOM   8045  O   ASP B1081      -6.082 -14.997  94.894  1.00 88.36           O  
ANISOU 8045  O   ASP B1081    11035  10237  12300   -856   -524   1060       O  
ATOM   8046  CB  ASP B1081      -3.558 -13.404  93.489  1.00 89.36           C  
ANISOU 8046  CB  ASP B1081    10800  10734  12418   -864   -543   1304       C  
ATOM   8047  CG  ASP B1081      -2.750 -13.664  92.228  1.00106.00           C  
ANISOU 8047  CG  ASP B1081    12768  12740  14768   -617   -283   1312       C  
ATOM   8048  OD1 ASP B1081      -3.025 -14.679  91.539  1.00108.81           O  
ANISOU 8048  OD1 ASP B1081    13169  12801  15374   -372     21   1171       O  
ATOM   8049  OD2 ASP B1081      -1.817 -12.876  91.947  1.00112.97           O  
ANISOU 8049  OD2 ASP B1081    13501  13833  15590   -692   -356   1452       O  
ATOM   8050  N   ILE B1082      -6.062 -12.782  95.443  1.00 80.38           N  
ANISOU 8050  N   ILE B1082    10197   9593  10750  -1327   -843    893       N  
ATOM   8051  CA  ILE B1082      -6.768 -12.890  96.721  1.00 79.53           C  
ANISOU 8051  CA  ILE B1082    10192   9557  10466  -1537   -966    919       C  
ATOM   8052  C   ILE B1082      -8.226 -13.251  96.434  1.00 80.14           C  
ANISOU 8052  C   ILE B1082    10524   9341  10584  -1421   -830    573       C  
ATOM   8053  O   ILE B1082      -8.761 -14.176  97.048  1.00 80.94           O  
ANISOU 8053  O   ILE B1082    10627   9362  10766  -1375   -813    658       O  
ATOM   8054  CB  ILE B1082      -6.650 -11.580  97.569  1.00 82.78           C  
ANISOU 8054  CB  ILE B1082    10715  10229  10508  -1956  -1143    860       C  
ATOM   8055  CG1 ILE B1082      -5.174 -11.160  97.790  1.00 85.77           C  
ANISOU 8055  CG1 ILE B1082    10830  10947  10813  -2135  -1307   1210       C  
ATOM   8056  CG2 ILE B1082      -7.398 -11.714  98.910  1.00 83.82           C  
ANISOU 8056  CG2 ILE B1082    10981  10451  10417  -2214  -1224    852       C  
ATOM   8057  CD1 ILE B1082      -4.971  -9.684  98.109  1.00 91.76           C  
ANISOU 8057  CD1 ILE B1082    11741  11875  11247  -2537  -1400   1028       C  
ATOM   8058  N   LEU B1083      -8.847 -12.528  95.479  1.00 73.10           N  
ANISOU 8058  N   LEU B1083     9813   8312   9650  -1384   -743    233       N  
ATOM   8059  CA  LEU B1083     -10.243 -12.677  95.070  1.00 70.35           C  
ANISOU 8059  CA  LEU B1083     9667   7741   9320  -1314   -640    -62       C  
ATOM   8060  C   LEU B1083     -10.545 -14.091  94.534  1.00 73.20           C  
ANISOU 8060  C   LEU B1083     9998   7899   9915  -1084   -494    -74       C  
ATOM   8061  O   LEU B1083     -11.515 -14.693  94.996  1.00 71.68           O  
ANISOU 8061  O   LEU B1083     9901   7586   9749  -1087   -471   -140       O  
ATOM   8062  CB  LEU B1083     -10.608 -11.607  94.030  1.00 68.65           C  
ANISOU 8062  CB  LEU B1083     9554   7486   9042  -1324   -596   -292       C  
ATOM   8063  CG  LEU B1083     -12.086 -11.287  93.864  1.00 71.25           C  
ANISOU 8063  CG  LEU B1083    10053   7672   9346  -1346   -543   -514       C  
ATOM   8064  CD1 LEU B1083     -12.541 -10.268  94.881  1.00 71.25           C  
ANISOU 8064  CD1 LEU B1083    10168   7683   9222  -1554   -563   -567       C  
ATOM   8065  CD2 LEU B1083     -12.348 -10.739  92.489  1.00 72.84           C  
ANISOU 8065  CD2 LEU B1083    10259   7853   9564  -1282   -491   -626       C  
ATOM   8066  N   VAL B1084      -9.711 -14.625  93.598  1.00 70.48           N  
ANISOU 8066  N   VAL B1084     9529   7499   9750   -907   -360    -22       N  
ATOM   8067  CA  VAL B1084      -9.872 -15.973  93.019  1.00 71.20           C  
ANISOU 8067  CA  VAL B1084     9616   7344  10094   -719   -133    -81       C  
ATOM   8068  C   VAL B1084      -9.712 -17.007  94.143  1.00 77.33           C  
ANISOU 8068  C   VAL B1084    10261   8052  11070   -656   -131    220       C  
ATOM   8069  O   VAL B1084     -10.525 -17.928  94.238  1.00 77.18           O  
ANISOU 8069  O   VAL B1084    10332   7816  11177   -606    -20    126       O  
ATOM   8070  CB  VAL B1084      -8.934 -16.257  91.816  1.00 76.01           C  
ANISOU 8070  CB  VAL B1084    10133   7891  10859   -567     86   -111       C  
ATOM   8071  CG1 VAL B1084      -9.071 -17.703  91.326  1.00 77.76           C  
ANISOU 8071  CG1 VAL B1084    10378   7795  11371   -409    404   -208       C  
ATOM   8072  CG2 VAL B1084      -9.219 -15.296  90.672  1.00 74.28           C  
ANISOU 8072  CG2 VAL B1084    10042   7770  10411   -660     73   -384       C  
ATOM   8073  N   GLY B1085      -8.726 -16.787  95.014  1.00 75.33           N  
ANISOU 8073  N   GLY B1085     9787   8018  10816   -703   -278    601       N  
ATOM   8074  CA  GLY B1085      -8.470 -17.624  96.179  1.00 77.29           C  
ANISOU 8074  CA  GLY B1085     9848   8305  11213   -691   -336   1005       C  
ATOM   8075  C   GLY B1085      -9.669 -17.693  97.102  1.00 79.50           C  
ANISOU 8075  C   GLY B1085    10306   8588  11314   -852   -448    906       C  
ATOM   8076  O   GLY B1085      -9.980 -18.757  97.640  1.00 80.73           O  
ANISOU 8076  O   GLY B1085    10400   8606  11669   -772   -382   1086       O  
ATOM   8077  N   GLN B1086     -10.368 -16.559  97.251  1.00 73.24           N  
ANISOU 8077  N   GLN B1086     9730   7917  10182  -1067   -575    625       N  
ATOM   8078  CA  GLN B1086     -11.570 -16.426  98.070  1.00 72.06           C  
ANISOU 8078  CA  GLN B1086     9767   7764   9847  -1231   -636    483       C  
ATOM   8079  C   GLN B1086     -12.786 -17.045  97.367  1.00 76.42           C  
ANISOU 8079  C   GLN B1086    10483   8012  10539  -1096   -474    188       C  
ATOM   8080  O   GLN B1086     -13.678 -17.555  98.047  1.00 75.97           O  
ANISOU 8080  O   GLN B1086    10498   7884  10481  -1142   -471    186       O  
ATOM   8081  CB  GLN B1086     -11.834 -14.952  98.381  1.00 71.58           C  
ANISOU 8081  CB  GLN B1086     9867   7876   9455  -1489   -738    282       C  
ATOM   8082  CG  GLN B1086     -11.019 -14.396  99.536  1.00 79.21           C  
ANISOU 8082  CG  GLN B1086    10748   9181  10167  -1783   -915    527       C  
ATOM   8083  CD  GLN B1086     -11.346 -12.947  99.807  1.00 93.86           C  
ANISOU 8083  CD  GLN B1086    12814  11120  11730  -2062   -925    249       C  
ATOM   8084  OE1 GLN B1086     -12.413 -12.432  99.451  1.00 86.42           O  
ANISOU 8084  OE1 GLN B1086    12069   9972  10794  -2031   -796    -70       O  
ATOM   8085  NE2 GLN B1086     -10.441 -12.255 100.473  1.00 89.61           N  
ANISOU 8085  NE2 GLN B1086    12222  10878  10947  -2364  -1058    387       N  
ATOM   8086  N   ILE B1087     -12.824 -16.986  96.009  1.00 73.43           N  
ANISOU 8086  N   ILE B1087    10160   7494  10247   -973   -348    -51       N  
ATOM   8087  CA  ILE B1087     -13.890 -17.568  95.176  1.00 73.09           C  
ANISOU 8087  CA  ILE B1087    10259   7223  10287   -917   -208   -330       C  
ATOM   8088  C   ILE B1087     -13.785 -19.098  95.275  1.00 81.76           C  
ANISOU 8088  C   ILE B1087    11294   8079  11693   -777    -35   -216       C  
ATOM   8089  O   ILE B1087     -14.802 -19.769  95.448  1.00 81.75           O  
ANISOU 8089  O   ILE B1087    11393   7921  11750   -806     18   -318       O  
ATOM   8090  CB  ILE B1087     -13.832 -17.051  93.698  1.00 74.97           C  
ANISOU 8090  CB  ILE B1087    10557   7462  10464   -900   -136   -578       C  
ATOM   8091  CG1 ILE B1087     -14.331 -15.600  93.594  1.00 73.25           C  
ANISOU 8091  CG1 ILE B1087    10409   7411  10010  -1033   -274   -680       C  
ATOM   8092  CG2 ILE B1087     -14.630 -17.944  92.738  1.00 75.85           C  
ANISOU 8092  CG2 ILE B1087    10784   7379  10656   -895     32   -829       C  
ATOM   8093  CD1 ILE B1087     -13.816 -14.805  92.389  1.00 78.83           C  
ANISOU 8093  CD1 ILE B1087    11096   8219  10638  -1029   -261   -769       C  
ATOM   8094  N   ASP B1088     -12.547 -19.632  95.203  1.00 82.03           N  
ANISOU 8094  N   ASP B1088    11137   8068  11963   -624     74     29       N  
ATOM   8095  CA  ASP B1088     -12.247 -21.061  95.301  1.00 85.38           C  
ANISOU 8095  CA  ASP B1088    11451   8205  12786   -449    309    207       C  
ATOM   8096  C   ASP B1088     -12.701 -21.618  96.654  1.00 90.28           C  
ANISOU 8096  C   ASP B1088    12003   8838  13462   -492    198    498       C  
ATOM   8097  O   ASP B1088     -13.259 -22.716  96.696  1.00 91.64           O  
ANISOU 8097  O   ASP B1088    12215   8719  13885   -425    376    478       O  
ATOM   8098  CB  ASP B1088     -10.741 -21.321  95.077  1.00 90.34           C  
ANISOU 8098  CB  ASP B1088    11816   8817  13692   -260    448    515       C  
ATOM   8099  CG  ASP B1088     -10.202 -20.897  93.711  1.00103.04           C  
ANISOU 8099  CG  ASP B1088    13480  10399  15273   -209    613    243       C  
ATOM   8100  OD1 ASP B1088     -10.926 -21.070  92.701  1.00103.72           O  
ANISOU 8100  OD1 ASP B1088    13799  10324  15288   -267    776   -186       O  
ATOM   8101  OD2 ASP B1088      -9.055 -20.400  93.654  1.00108.76           O  
ANISOU 8101  OD2 ASP B1088    14003  11297  16023   -145    573    478       O  
ATOM   8102  N   ASP B1089     -12.503 -20.842  97.744  1.00 86.06           N  
ANISOU 8102  N   ASP B1089    11388   8647  12662   -647    -81    741       N  
ATOM   8103  CA  ASP B1089     -12.913 -21.206  99.102  1.00 86.90           C  
ANISOU 8103  CA  ASP B1089    11437   8866  12714   -760   -216   1025       C  
ATOM   8104  C   ASP B1089     -14.435 -21.223  99.206  1.00 87.38           C  
ANISOU 8104  C   ASP B1089    11751   8815  12635   -868   -209    696       C  
ATOM   8105  O   ASP B1089     -14.987 -22.105  99.870  1.00 88.29           O  
ANISOU 8105  O   ASP B1089    11846   8816  12884   -864   -171    847       O  
ATOM   8106  CB  ASP B1089     -12.308 -20.246 100.142  1.00 89.85           C  
ANISOU 8106  CB  ASP B1089    11709   9685  12744   -996   -496   1287       C  
ATOM   8107  CG  ASP B1089     -10.790 -20.286 100.262  1.00109.55           C  
ANISOU 8107  CG  ASP B1089    13881  12374  15368   -939   -559   1740       C  
ATOM   8108  OD1 ASP B1089     -10.204 -21.394 100.135  1.00114.18           O  
ANISOU 8108  OD1 ASP B1089    14225  12766  16391   -698   -398   2083       O  
ATOM   8109  OD2 ASP B1089     -10.186 -19.217 100.514  1.00116.63           O  
ANISOU 8109  OD2 ASP B1089    14750  13607  15956  -1144   -751   1779       O  
ATOM   8110  N   ALA B1090     -15.103 -20.274  98.515  1.00 80.24           N  
ANISOU 8110  N   ALA B1090    11049   7939  11501   -953   -233    295       N  
ATOM   8111  CA  ALA B1090     -16.562 -20.157  98.464  1.00 78.28           C  
ANISOU 8111  CA  ALA B1090    10994   7606  11143  -1048   -221     11       C  
ATOM   8112  C   ALA B1090     -17.181 -21.287  97.618  1.00 82.51           C  
ANISOU 8112  C   ALA B1090    11595   7818  11935   -952    -27   -166       C  
ATOM   8113  O   ALA B1090     -18.272 -21.767  97.943  1.00 81.76           O  
ANISOU 8113  O   ALA B1090    11581   7621  11863  -1018     -7   -231       O  
ATOM   8114  CB  ALA B1090     -16.958 -18.801  97.908  1.00 76.67           C  
ANISOU 8114  CB  ALA B1090    10911   7528  10693  -1145   -286   -261       C  
ATOM   8115  N   LEU B1091     -16.470 -21.711  96.547  1.00 79.98           N  
ANISOU 8115  N   LEU B1091    11250   7339  11800   -829    140   -257       N  
ATOM   8116  CA  LEU B1091     -16.861 -22.800  95.646  1.00 81.20           C  
ANISOU 8116  CA  LEU B1091    11498   7170  12183   -795    391   -481       C  
ATOM   8117  C   LEU B1091     -16.806 -24.128  96.370  1.00 88.44           C  
ANISOU 8117  C   LEU B1091    12329   7819  13456   -695    546   -235       C  
ATOM   8118  O   LEU B1091     -17.680 -24.969  96.156  1.00 89.77           O  
ANISOU 8118  O   LEU B1091    12615   7742  13750   -759    686   -408       O  
ATOM   8119  CB  LEU B1091     -15.951 -22.853  94.412  1.00 82.22           C  
ANISOU 8119  CB  LEU B1091    11628   7208  12404   -712    588   -641       C  
ATOM   8120  CG  LEU B1091     -16.375 -22.030  93.204  1.00 84.78           C  
ANISOU 8120  CG  LEU B1091    12096   7683  12435   -859    542   -994       C  
ATOM   8121  CD1 LEU B1091     -15.182 -21.682  92.357  1.00 85.56           C  
ANISOU 8121  CD1 LEU B1091    12136   7828  12546   -769    654  -1024       C  
ATOM   8122  CD2 LEU B1091     -17.412 -22.762  92.369  1.00 87.27           C  
ANISOU 8122  CD2 LEU B1091    12595   7830  12735  -1033    689  -1332       C  
ATOM   8123  N   LYS B1092     -15.775 -24.318  97.226  1.00 86.41           N  
ANISOU 8123  N   LYS B1092    11842   7622  13369   -560    515    208       N  
ATOM   8124  CA  LYS B1092     -15.580 -25.519  98.048  1.00 89.52           C  
ANISOU 8124  CA  LYS B1092    12071   7800  14142   -442    641    593       C  
ATOM   8125  C   LYS B1092     -16.774 -25.692  98.988  1.00 93.37           C  
ANISOU 8125  C   LYS B1092    12638   8348  14491   -594    497    630       C  
ATOM   8126  O   LYS B1092     -17.284 -26.798  99.123  1.00 95.06           O  
ANISOU 8126  O   LYS B1092    12867   8253  14997   -560    676    669       O  
ATOM   8127  CB  LYS B1092     -14.278 -25.436  98.863  1.00 93.86           C  
ANISOU 8127  CB  LYS B1092    12298   8555  14807   -328    538   1158       C  
ATOM   8128  CG  LYS B1092     -13.122 -26.354  98.439  1.00112.04           C  
ANISOU 8128  CG  LYS B1092    14366  10550  17653    -55    859   1440       C  
ATOM   8129  CD  LYS B1092     -11.823 -25.622  98.713  1.00122.09           C  
ANISOU 8129  CD  LYS B1092    15367  12175  18847    -10    681   1821       C  
ATOM   8130  CE  LYS B1092     -10.884 -25.564  97.530  1.00132.65           C  
ANISOU 8130  CE  LYS B1092    16657  13343  20401    170    946   1680       C  
ATOM   8131  NZ  LYS B1092      -9.772 -24.608  97.773  1.00140.84           N  
ANISOU 8131  NZ  LYS B1092    17463  14799  21249    145    702   1989       N  
ATOM   8132  N   LEU B1093     -17.239 -24.575  99.598  1.00 87.53           N  
ANISOU 8132  N   LEU B1093    11962   7978  13319   -771    216    589       N  
ATOM   8133  CA  LEU B1093     -18.404 -24.536 100.493  1.00 86.71           C  
ANISOU 8133  CA  LEU B1093    11943   7970  13031   -932    100    589       C  
ATOM   8134  C   LEU B1093     -19.686 -24.905  99.735  1.00 89.36           C  
ANISOU 8134  C   LEU B1093    12474   8068  13411   -993    219    201       C  
ATOM   8135  O   LEU B1093     -20.522 -25.635 100.274  1.00 89.89           O  
ANISOU 8135  O   LEU B1093    12561   8011  13581  -1046    259    267       O  
ATOM   8136  CB  LEU B1093     -18.560 -23.145 101.145  1.00 84.87           C  
ANISOU 8136  CB  LEU B1093    11766   8132  12351  -1115   -128    550       C  
ATOM   8137  CG  LEU B1093     -17.560 -22.756 102.245  1.00 91.14           C  
ANISOU 8137  CG  LEU B1093    12392   9263  12973  -1204   -298    947       C  
ATOM   8138  CD1 LEU B1093     -17.572 -21.255 102.483  1.00 89.35           C  
ANISOU 8138  CD1 LEU B1093    12283   9343  12324  -1406   -436    755       C  
ATOM   8139  CD2 LEU B1093     -17.848 -23.489 103.556  1.00 95.60           C  
ANISOU 8139  CD2 LEU B1093    12857   9923  13544  -1302   -352   1322       C  
ATOM   8140  N   ALA B1094     -19.824 -24.408  98.482  1.00 84.14           N  
ANISOU 8140  N   ALA B1094    11935   7379  12657  -1017    261   -168       N  
ATOM   8141  CA  ALA B1094     -20.965 -24.675  97.603  1.00 83.50           C  
ANISOU 8141  CA  ALA B1094    12011   7158  12557  -1143    337   -517       C  
ATOM   8142  C   ALA B1094     -20.983 -26.143  97.173  1.00 90.67           C  
ANISOU 8142  C   ALA B1094    12960   7668  13824  -1116    610   -583       C  
ATOM   8143  O   ALA B1094     -22.061 -26.735  97.072  1.00 90.48           O  
ANISOU 8143  O   ALA B1094    13031   7508  13838  -1261    661   -729       O  
ATOM   8144  CB  ALA B1094     -20.923 -23.765  96.386  1.00 82.66           C  
ANISOU 8144  CB  ALA B1094    11981   7192  12236  -1205    296   -808       C  
ATOM   8145  N   ASN B1095     -19.789 -26.734  96.949  1.00 90.60           N  
ANISOU 8145  N   ASN B1095    12866   7448  14108   -938    816   -461       N  
ATOM   8146  CA  ASN B1095     -19.619 -28.139  96.569  1.00 94.95           C  
ANISOU 8146  CA  ASN B1095    13449   7532  15097   -879   1179   -509       C  
ATOM   8147  C   ASN B1095     -20.002 -29.059  97.730  1.00102.47           C  
ANISOU 8147  C   ASN B1095    14299   8311  16324   -833   1209   -163       C  
ATOM   8148  O   ASN B1095     -20.555 -30.136  97.495  1.00104.85           O  
ANISOU 8148  O   ASN B1095    14699   8240  16901   -899   1457   -297       O  
ATOM   8149  CB  ASN B1095     -18.183 -28.412  96.114  1.00 98.99           C  
ANISOU 8149  CB  ASN B1095    13845   7861  15907   -656   1431   -399       C  
ATOM   8150  CG  ASN B1095     -17.878 -27.912  94.721  1.00125.14           C  
ANISOU 8150  CG  ASN B1095    17305  11211  19032   -734   1539   -821       C  
ATOM   8151  OD1 ASN B1095     -18.548 -28.262  93.739  1.00123.62           O  
ANISOU 8151  OD1 ASN B1095    17338  10874  18758   -949   1704  -1261       O  
ATOM   8152  ND2 ASN B1095     -16.826 -27.120  94.592  1.00114.16           N  
ANISOU 8152  ND2 ASN B1095    15784  10036  17557   -597   1456   -682       N  
ATOM   8153  N   GLU B1096     -19.736 -28.614  98.983  1.00 98.94           N  
ANISOU 8153  N   GLU B1096    13666   8156  15771   -766    959    274       N  
ATOM   8154  CA  GLU B1096     -20.089 -29.343 100.209  1.00100.64           C  
ANISOU 8154  CA  GLU B1096    13756   8320  16163   -754    930    673       C  
ATOM   8155  C   GLU B1096     -21.590 -29.185 100.517  1.00101.14           C  
ANISOU 8155  C   GLU B1096    13973   8488  15968   -976    792    471       C  
ATOM   8156  O   GLU B1096     -22.137 -29.948 101.321  1.00102.98           O  
ANISOU 8156  O   GLU B1096    14155   8610  16364  -1005    822    703       O  
ATOM   8157  CB  GLU B1096     -19.238 -28.888 101.420  1.00102.64           C  
ANISOU 8157  CB  GLU B1096    13756   8934  16309   -687    699   1218       C  
ATOM   8158  CG  GLU B1096     -17.741 -29.186 101.347  1.00119.96           C  
ANISOU 8158  CG  GLU B1096    15695  11054  18832   -459    817   1596       C  
ATOM   8159  CD  GLU B1096     -17.268 -30.488 100.722  1.00157.51           C  
ANISOU 8159  CD  GLU B1096    20377  15239  24232   -240   1252   1662       C  
ATOM   8160  OE1 GLU B1096     -17.680 -31.564 101.214  1.00164.82           O  
ANISOU 8160  OE1 GLU B1096    21242  15866  25518   -203   1415   1889       O  
ATOM   8161  OE2 GLU B1096     -16.474 -30.435  99.753  1.00157.91           O  
ANISOU 8161  OE2 GLU B1096    20431  15120  24449   -108   1465   1489       O  
ATOM   8162  N   GLY B1097     -22.230 -28.211  99.863  1.00 92.35           N  
ANISOU 8162  N   GLY B1097    13014   7585  14489  -1120    657     89       N  
ATOM   8163  CA  GLY B1097     -23.653 -27.933 100.006  1.00 89.85           C  
ANISOU 8163  CA  GLY B1097    12803   7385  13953  -1316    543    -88       C  
ATOM   8164  C   GLY B1097     -23.995 -26.847 101.001  1.00 89.82           C  
ANISOU 8164  C   GLY B1097    12754   7765  13607  -1372    312     56       C  
ATOM   8165  O   GLY B1097     -25.176 -26.565 101.222  1.00 87.99           O  
ANISOU 8165  O   GLY B1097    12574   7626  13231  -1506    253    -42       O  
ATOM   8166  N   LYS B1098     -22.966 -26.230 101.607  1.00 85.70           N  
ANISOU 8166  N   LYS B1098    12134   7469  12959  -1295    207    287       N  
ATOM   8167  CA  LYS B1098     -23.128 -25.160 102.595  1.00 84.13           C  
ANISOU 8167  CA  LYS B1098    11930   7629  12405  -1403     41    383       C  
ATOM   8168  C   LYS B1098     -23.447 -23.843 101.869  1.00 84.53           C  
ANISOU 8168  C   LYS B1098    12084   7823  12209  -1454    -15     52       C  
ATOM   8169  O   LYS B1098     -22.541 -23.065 101.574  1.00 82.98           O  
ANISOU 8169  O   LYS B1098    11875   7760  11895  -1415    -73     24       O  
ATOM   8170  CB  LYS B1098     -21.869 -25.041 103.478  1.00 88.09           C  
ANISOU 8170  CB  LYS B1098    12283   8349  12836  -1381    -56    761       C  
ATOM   8171  CG  LYS B1098     -21.575 -26.287 104.310  1.00108.05           C  
ANISOU 8171  CG  LYS B1098    14644  10783  15628  -1333    -17   1212       C  
ATOM   8172  CD  LYS B1098     -20.106 -26.378 104.686  1.00120.25           C  
ANISOU 8172  CD  LYS B1098    15965  12483  17243  -1255    -91   1637       C  
ATOM   8173  CE  LYS B1098     -19.783 -27.644 105.437  1.00131.07           C  
ANISOU 8173  CE  LYS B1098    17103  13741  18955  -1177    -36   2179       C  
ATOM   8174  NZ  LYS B1098     -18.350 -27.694 105.827  1.00140.32           N  
ANISOU 8174  NZ  LYS B1098    17985  15118  20211  -1109   -130   2693       N  
ATOM   8175  N   VAL B1099     -24.741 -23.623 101.549  1.00 79.86           N  
ANISOU 8175  N   VAL B1099    11565   7200  11578  -1540      9   -153       N  
ATOM   8176  CA  VAL B1099     -25.239 -22.444 100.826  1.00 77.72           C  
ANISOU 8176  CA  VAL B1099    11338   7040  11152  -1578    -23   -386       C  
ATOM   8177  C   VAL B1099     -25.051 -21.189 101.684  1.00 81.93           C  
ANISOU 8177  C   VAL B1099    11890   7795  11443  -1626    -48   -348       C  
ATOM   8178  O   VAL B1099     -24.480 -20.215 101.196  1.00 80.45           O  
ANISOU 8178  O   VAL B1099    11717   7696  11153  -1601    -79   -447       O  
ATOM   8179  CB  VAL B1099     -26.717 -22.594 100.362  1.00 81.30           C  
ANISOU 8179  CB  VAL B1099    11793   7433  11666  -1670      6   -506       C  
ATOM   8180  CG1 VAL B1099     -27.126 -21.460  99.423  1.00 79.72           C  
ANISOU 8180  CG1 VAL B1099    11569   7350  11370  -1691    -34   -652       C  
ATOM   8181  CG2 VAL B1099     -26.960 -23.947  99.697  1.00 82.53           C  
ANISOU 8181  CG2 VAL B1099    11967   7363  12027  -1713     58   -569       C  
ATOM   8182  N   LYS B1100     -25.504 -21.228 102.959  1.00 80.36           N  
ANISOU 8182  N   LYS B1100    11706   7682  11146  -1726    -10   -219       N  
ATOM   8183  CA  LYS B1100     -25.413 -20.120 103.921  1.00 80.78           C  
ANISOU 8183  CA  LYS B1100    11825   7933  10936  -1853     34   -232       C  
ATOM   8184  C   LYS B1100     -23.956 -19.697 104.180  1.00 84.67           C  
ANISOU 8184  C   LYS B1100    12317   8601  11252  -1895    -66   -148       C  
ATOM   8185  O   LYS B1100     -23.680 -18.500 104.309  1.00 83.33           O  
ANISOU 8185  O   LYS B1100    12223   8545  10894  -1988    -29   -282       O  
ATOM   8186  CB  LYS B1100     -26.096 -20.503 105.244  1.00 85.52           C  
ANISOU 8186  CB  LYS B1100    12448   8609  11436  -1997    110   -100       C  
ATOM   8187  CG  LYS B1100     -27.613 -20.407 105.193  1.00104.00           C  
ANISOU 8187  CG  LYS B1100    14790  10835  13890  -1998    256   -203       C  
ATOM   8188  CD  LYS B1100     -28.282 -21.310 106.218  1.00116.93           C  
ANISOU 8188  CD  LYS B1100    16412  12490  15528  -2093    305    -25       C  
ATOM   8189  CE  LYS B1100     -29.781 -21.139 106.184  1.00126.42           C  
ANISOU 8189  CE  LYS B1100    17585  13595  16854  -2096    464   -103       C  
ATOM   8190  NZ  LYS B1100     -30.467 -22.071 107.114  1.00134.52           N  
ANISOU 8190  NZ  LYS B1100    18584  14630  17897  -2187    515     76       N  
ATOM   8191  N   GLU B1101     -23.036 -20.679 104.232  1.00 82.69           N  
ANISOU 8191  N   GLU B1101    11961   8355  11102  -1830   -170     94       N  
ATOM   8192  CA  GLU B1101     -21.609 -20.450 104.452  1.00 83.87           C  
ANISOU 8192  CA  GLU B1101    12038   8696  11134  -1863   -287    272       C  
ATOM   8193  C   GLU B1101     -20.939 -19.880 103.193  1.00 86.28           C  
ANISOU 8193  C   GLU B1101    12336   8927  11518  -1724   -305     98       C  
ATOM   8194  O   GLU B1101     -20.035 -19.048 103.316  1.00 86.14           O  
ANISOU 8194  O   GLU B1101    12313   9100  11317  -1808   -376    114       O  
ATOM   8195  CB  GLU B1101     -20.908 -21.740 104.896  1.00 87.81           C  
ANISOU 8195  CB  GLU B1101    12359   9194  11809  -1799   -355    677       C  
ATOM   8196  CG  GLU B1101     -21.276 -22.181 106.302  1.00105.65           C  
ANISOU 8196  CG  GLU B1101    14589  11641  13911  -1991   -385    950       C  
ATOM   8197  CD  GLU B1101     -20.369 -23.229 106.918  1.00147.76           C  
ANISOU 8197  CD  GLU B1101    19686  17073  19383  -1968   -486   1479       C  
ATOM   8198  OE1 GLU B1101     -20.886 -24.300 107.313  1.00149.07           O  
ANISOU 8198  OE1 GLU B1101    19779  17104  19758  -1920   -434   1699       O  
ATOM   8199  OE2 GLU B1101     -19.148 -22.971 107.031  1.00154.47           O  
ANISOU 8199  OE2 GLU B1101    20394  18144  20152  -2004   -613   1718       O  
ATOM   8200  N   ALA B1102     -21.380 -20.327 101.990  1.00 81.24           N  
ANISOU 8200  N   ALA B1102    11703   8042  11123  -1557   -241    -69       N  
ATOM   8201  CA  ALA B1102     -20.862 -19.854 100.702  1.00 79.53           C  
ANISOU 8201  CA  ALA B1102    11486   7772  10959  -1452   -242   -242       C  
ATOM   8202  C   ALA B1102     -21.379 -18.447 100.395  1.00 81.51           C  
ANISOU 8202  C   ALA B1102    11821   8105  11045  -1522   -230   -460       C  
ATOM   8203  O   ALA B1102     -20.660 -17.662  99.770  1.00 80.64           O  
ANISOU 8203  O   ALA B1102    11703   8060  10877  -1496   -262   -528       O  
ATOM   8204  CB  ALA B1102     -21.249 -20.810  99.587  1.00 80.28           C  
ANISOU 8204  CB  ALA B1102    11583   7622  11296  -1344   -158   -366       C  
ATOM   8205  N   GLN B1103     -22.619 -18.131 100.845  1.00 76.80           N  
ANISOU 8205  N   GLN B1103    11283   7484  10414  -1601   -155   -536       N  
ATOM   8206  CA  GLN B1103     -23.250 -16.817 100.687  1.00 75.53           C  
ANISOU 8206  CA  GLN B1103    11167   7339  10190  -1645    -70   -685       C  
ATOM   8207  C   GLN B1103     -22.549 -15.773 101.551  1.00 81.31           C  
ANISOU 8207  C   GLN B1103    11980   8210  10705  -1787    -33   -705       C  
ATOM   8208  O   GLN B1103     -22.388 -14.632 101.119  1.00 79.44           O  
ANISOU 8208  O   GLN B1103    11770   7966  10450  -1794     25   -819       O  
ATOM   8209  CB  GLN B1103     -24.734 -16.880 101.058  1.00 76.74           C  
ANISOU 8209  CB  GLN B1103    11324   7409  10424  -1678     49   -706       C  
ATOM   8210  CG  GLN B1103     -25.622 -17.419  99.956  1.00 78.95           C  
ANISOU 8210  CG  GLN B1103    11516   7593  10888  -1606     17   -726       C  
ATOM   8211  CD  GLN B1103     -27.062 -17.478 100.380  1.00 89.97           C  
ANISOU 8211  CD  GLN B1103    12869   8936  12379  -1646    124   -688       C  
ATOM   8212  OE1 GLN B1103     -27.414 -18.083 101.395  1.00 85.29           O  
ANISOU 8212  OE1 GLN B1103    12313   8328  11766  -1705    178   -624       O  
ATOM   8213  NE2 GLN B1103     -27.937 -16.878  99.588  1.00 81.26           N  
ANISOU 8213  NE2 GLN B1103    11653   7824  11396  -1621    155   -679       N  
ATOM   8214  N   ALA B1104     -22.152 -16.171 102.781  1.00 81.72           N  
ANISOU 8214  N   ALA B1104    12066   8401  10582  -1940    -61   -579       N  
ATOM   8215  CA  ALA B1104     -21.441 -15.333 103.749  1.00 84.09           C  
ANISOU 8215  CA  ALA B1104    12458   8904  10589  -2187    -45   -592       C  
ATOM   8216  C   ALA B1104     -20.022 -15.038 103.261  1.00 90.88           C  
ANISOU 8216  C   ALA B1104    13250   9889  11390  -2179   -198   -520       C  
ATOM   8217  O   ALA B1104     -19.544 -13.909 103.409  1.00 91.65           O  
ANISOU 8217  O   ALA B1104    13431  10071  11320  -2341   -153   -643       O  
ATOM   8218  CB  ALA B1104     -21.405 -16.019 105.104  1.00 86.93           C  
ANISOU 8218  CB  ALA B1104    12831   9454  10745  -2391    -82   -407       C  
ATOM   8219  N   ALA B1105     -19.368 -16.048 102.648  1.00 88.51           N  
ANISOU 8219  N   ALA B1105    12798   9572  11262  -1992   -338   -329       N  
ATOM   8220  CA  ALA B1105     -18.029 -15.950 102.061  1.00 89.00           C  
ANISOU 8220  CA  ALA B1105    12748   9726  11343  -1929   -457   -218       C  
ATOM   8221  C   ALA B1105     -18.047 -15.022 100.842  1.00 91.24           C  
ANISOU 8221  C   ALA B1105    13069   9895  11702  -1821   -402   -447       C  
ATOM   8222  O   ALA B1105     -17.035 -14.384 100.539  1.00 91.01           O  
ANISOU 8222  O   ALA B1105    13001   9977  11601  -1856   -464   -426       O  
ATOM   8223  CB  ALA B1105     -17.534 -17.332 101.660  1.00 90.50           C  
ANISOU 8223  CB  ALA B1105    12769   9830  11787  -1720   -510     18       C  
ATOM   8224  N   ALA B1106     -19.216 -14.940 100.163  1.00 86.19           N  
ANISOU 8224  N   ALA B1106    12479   9065  11205  -1712   -297   -621       N  
ATOM   8225  CA  ALA B1106     -19.448 -14.091  98.997  1.00 84.59           C  
ANISOU 8225  CA  ALA B1106    12276   8781  11084  -1625   -252   -770       C  
ATOM   8226  C   ALA B1106     -19.584 -12.625  99.400  1.00 88.72           C  
ANISOU 8226  C   ALA B1106    12890   9311  11507  -1764   -137   -886       C  
ATOM   8227  O   ALA B1106     -19.266 -11.749  98.597  1.00 87.99           O  
ANISOU 8227  O   ALA B1106    12775   9200  11458  -1725   -122   -937       O  
ATOM   8228  CB  ALA B1106     -20.688 -14.549  98.255  1.00 84.63           C  
ANISOU 8228  CB  ALA B1106    12256   8645  11254  -1521   -204   -832       C  
ATOM   8229  N   GLU B1107     -20.030 -12.351 100.644  1.00 86.25           N  
ANISOU 8229  N   GLU B1107    12691   9012  11068  -1947    -21   -933       N  
ATOM   8230  CA  GLU B1107     -20.146 -10.983 101.158  1.00 87.32           C  
ANISOU 8230  CA  GLU B1107    12959   9100  11121  -2126    179  -1097       C  
ATOM   8231  C   GLU B1107     -18.746 -10.392 101.376  1.00 90.38           C  
ANISOU 8231  C   GLU B1107    13380   9665  11294  -2315     85  -1095       C  
ATOM   8232  O   GLU B1107     -18.581  -9.178 101.261  1.00 90.71           O  
ANISOU 8232  O   GLU B1107    13504   9627  11336  -2416    231  -1237       O  
ATOM   8233  CB  GLU B1107     -20.982 -10.933 102.449  1.00 90.88           C  
ANISOU 8233  CB  GLU B1107    13550   9521  11460  -2316    381  -1189       C  
ATOM   8234  CG  GLU B1107     -21.785  -9.647 102.612  1.00108.38           C  
ANISOU 8234  CG  GLU B1107    15878  11505  13797  -2375    736  -1392       C  
ATOM   8235  CD  GLU B1107     -22.977  -9.405 101.695  1.00138.54           C  
ANISOU 8235  CD  GLU B1107    19561  15079  17996  -2102    874  -1346       C  
ATOM   8236  OE1 GLU B1107     -23.414 -10.344 100.990  1.00132.88           O  
ANISOU 8236  OE1 GLU B1107    18692  14394  17404  -1910    689  -1194       O  
ATOM   8237  OE2 GLU B1107     -23.471  -8.254 101.677  1.00139.74           O  
ANISOU 8237  OE2 GLU B1107    19749  15008  18337  -2104   1185  -1443       O  
ATOM   8238  N   GLN B1108     -17.740 -11.257 101.631  1.00 85.76           N  
ANISOU 8238  N   GLN B1108    12702   9309  10573  -2354   -147   -896       N  
ATOM   8239  CA  GLN B1108     -16.345 -10.868 101.833  1.00 85.82           C  
ANISOU 8239  CA  GLN B1108    12673   9550  10383  -2540   -288   -804       C  
ATOM   8240  C   GLN B1108     -15.640 -10.610 100.501  1.00 86.49           C  
ANISOU 8240  C   GLN B1108    12633   9588  10639  -2326   -365   -768       C  
ATOM   8241  O   GLN B1108     -14.616  -9.925 100.477  1.00 87.08           O  
ANISOU 8241  O   GLN B1108    12689   9804  10594  -2475   -430   -742       O  
ATOM   8242  CB  GLN B1108     -15.594 -11.910 102.675  1.00 88.73           C  
ANISOU 8242  CB  GLN B1108    12922  10203  10587  -2657   -495   -504       C  
ATOM   8243  CG  GLN B1108     -16.064 -11.962 104.138  1.00112.70           C  
ANISOU 8243  CG  GLN B1108    16092  13396  13333  -2991   -440   -519       C  
ATOM   8244  CD  GLN B1108     -16.352 -10.594 104.735  1.00139.96           C  
ANISOU 8244  CD  GLN B1108    19799  16826  16552  -3334   -215   -849       C  
ATOM   8245  OE1 GLN B1108     -15.493  -9.696 104.784  1.00137.92           O  
ANISOU 8245  OE1 GLN B1108    19591  16694  16118  -3579   -234   -920       O  
ATOM   8246  NE2 GLN B1108     -17.589 -10.394 105.164  1.00133.54           N  
ANISOU 8246  NE2 GLN B1108    19152  15815  15770  -3359     47  -1068       N  
ATOM   8247  N   LEU B1109     -16.216 -11.102  99.390  1.00 80.04           N  
ANISOU 8247  N   LEU B1109    11741   8597  10075  -2024   -349   -779       N  
ATOM   8248  CA  LEU B1109     -15.688 -10.846  98.051  1.00 78.36           C  
ANISOU 8248  CA  LEU B1109    11428   8355   9990  -1850   -390   -770       C  
ATOM   8249  C   LEU B1109     -15.917  -9.388  97.686  1.00 82.33           C  
ANISOU 8249  C   LEU B1109    12003   8760  10518  -1916   -262   -914       C  
ATOM   8250  O   LEU B1109     -15.137  -8.824  96.922  1.00 81.89           O  
ANISOU 8250  O   LEU B1109    11882   8751  10480  -1887   -304   -885       O  
ATOM   8251  CB  LEU B1109     -16.337 -11.761  97.003  1.00 77.03           C  
ANISOU 8251  CB  LEU B1109    11190   8065  10012  -1606   -389   -773       C  
ATOM   8252  CG  LEU B1109     -15.848 -13.197  96.955  1.00 82.04           C  
ANISOU 8252  CG  LEU B1109    11732   8720  10720  -1491   -458   -637       C  
ATOM   8253  CD1 LEU B1109     -16.806 -14.070  96.168  1.00 81.56           C  
ANISOU 8253  CD1 LEU B1109    11678   8504  10808  -1356   -400   -724       C  
ATOM   8254  CD2 LEU B1109     -14.455 -13.275  96.375  1.00 85.35           C  
ANISOU 8254  CD2 LEU B1109    12025   9241  11163  -1421   -515   -518       C  
ATOM   8255  N   LYS B1110     -16.981  -8.777  98.256  1.00 79.39           N  
ANISOU 8255  N   LYS B1110    11753   8229  10181  -2000    -68  -1048       N  
ATOM   8256  CA  LYS B1110     -17.372  -7.378  98.061  1.00 79.79           C  
ANISOU 8256  CA  LYS B1110    11869   8099  10350  -2050    148  -1164       C  
ATOM   8257  C   LYS B1110     -16.309  -6.433  98.628  1.00 84.91           C  
ANISOU 8257  C   LYS B1110    12622   8822  10819  -2328    184  -1250       C  
ATOM   8258  O   LYS B1110     -15.929  -5.461  97.969  1.00 84.64           O  
ANISOU 8258  O   LYS B1110    12564   8707  10887  -2321    247  -1263       O  
ATOM   8259  CB  LYS B1110     -18.732  -7.095  98.730  1.00 82.89           C  
ANISOU 8259  CB  LYS B1110    12357   8276  10861  -2075    412  -1271       C  
ATOM   8260  CG  LYS B1110     -19.940  -7.744  98.065  1.00 91.13           C  
ANISOU 8260  CG  LYS B1110    13268   9233  12124  -1833    403  -1165       C  
ATOM   8261  CD  LYS B1110     -21.217  -7.500  98.876  1.00101.78           C  
ANISOU 8261  CD  LYS B1110    14686  10384  13600  -1865    683  -1238       C  
ATOM   8262  CE  LYS B1110     -22.466  -7.593  98.050  1.00113.78           C  
ANISOU 8262  CE  LYS B1110    16021  11792  15419  -1647    730  -1082       C  
ATOM   8263  NZ  LYS B1110     -23.636  -7.075  98.814  1.00124.56           N  
ANISOU 8263  NZ  LYS B1110    17420  12921  16986  -1660   1081  -1124       N  
ATOM   8264  N   THR B1111     -15.844  -6.742  99.857  1.00 82.75           N  
ANISOU 8264  N   THR B1111    12453   8728  10258  -2608    134  -1284       N  
ATOM   8265  CA  THR B1111     -14.846  -5.981 100.610  1.00 84.93           C  
ANISOU 8265  CA  THR B1111    12843   9160  10266  -2992    137  -1365       C  
ATOM   8266  C   THR B1111     -13.460  -6.091  99.957  1.00 89.07           C  
ANISOU 8266  C   THR B1111    13191   9914  10736  -2963   -128  -1166       C  
ATOM   8267  O   THR B1111     -12.730  -5.097  99.938  1.00 89.81           O  
ANISOU 8267  O   THR B1111    13336  10038  10752  -3181    -90  -1236       O  
ATOM   8268  CB  THR B1111     -14.822  -6.427 102.086  1.00 92.21           C  
ANISOU 8268  CB  THR B1111    13891  10300  10844  -3341    117  -1396       C  
ATOM   8269  OG1 THR B1111     -14.524  -7.821 102.171  1.00 88.14           O  
ANISOU 8269  OG1 THR B1111    13194  10015  10279  -3200   -163  -1110       O  
ATOM   8270  CG2 THR B1111     -16.142  -6.148 102.813  1.00 91.02           C  
ANISOU 8270  CG2 THR B1111    13944   9912  10727  -3421    451  -1636       C  
ATOM   8271  N   THR B1112     -13.105  -7.287  99.420  1.00 84.74           N  
ANISOU 8271  N   THR B1112    12438   9500  10258  -2701   -352   -926       N  
ATOM   8272  CA  THR B1112     -11.838  -7.559  98.722  1.00 84.56           C  
ANISOU 8272  CA  THR B1112    12211   9665  10252  -2607   -552   -708       C  
ATOM   8273  C   THR B1112     -11.825  -6.703  97.451  1.00 88.85           C  
ANISOU 8273  C   THR B1112    12729  10042  10987  -2440   -464   -786       C  
ATOM   8274  O   THR B1112     -10.843  -6.001  97.198  1.00 88.73           O  
ANISOU 8274  O   THR B1112    12663  10131  10918  -2561   -514   -741       O  
ATOM   8275  CB  THR B1112     -11.692  -9.079  98.451  1.00 86.88           C  
ANISOU 8275  CB  THR B1112    12323  10028  10661  -2338   -687   -478       C  
ATOM   8276  OG1 THR B1112     -11.863  -9.778  99.683  1.00 82.90           O  
ANISOU 8276  OG1 THR B1112    11837   9659  10003  -2502   -749   -371       O  
ATOM   8277  CG2 THR B1112     -10.339  -9.456  97.832  1.00 85.11           C  
ANISOU 8277  CG2 THR B1112    11863   9975  10499  -2228   -828   -225       C  
ATOM   8278  N   ARG B1113     -12.963  -6.711  96.713  1.00 85.79           N  
ANISOU 8278  N   ARG B1113    12364   9421  10811  -2202   -338   -876       N  
ATOM   8279  CA  ARG B1113     -13.200  -5.955  95.485  1.00 86.07           C  
ANISOU 8279  CA  ARG B1113    12345   9322  11034  -2044   -259   -888       C  
ATOM   8280  C   ARG B1113     -13.029  -4.451  95.735  1.00 93.60           C  
ANISOU 8280  C   ARG B1113    13404  10151  12010  -2255    -92   -995       C  
ATOM   8281  O   ARG B1113     -12.371  -3.775  94.943  1.00 94.42           O  
ANISOU 8281  O   ARG B1113    13427  10275  12173  -2236   -111   -928       O  
ATOM   8282  CB  ARG B1113     -14.609  -6.261  94.941  1.00 86.75           C  
ANISOU 8282  CB  ARG B1113    12419   9238  11306  -1839   -169   -909       C  
ATOM   8283  CG  ARG B1113     -14.955  -5.584  93.609  1.00101.55           C  
ANISOU 8283  CG  ARG B1113    14180  11045  13359  -1693   -125   -830       C  
ATOM   8284  CD  ARG B1113     -16.455  -5.524  93.374  1.00114.79           C  
ANISOU 8284  CD  ARG B1113    15826  12563  15227  -1585     -8   -801       C  
ATOM   8285  NE  ARG B1113     -17.120  -4.627  94.325  1.00130.31           N  
ANISOU 8285  NE  ARG B1113    17904  14283  17324  -1686    247   -892       N  
ATOM   8286  CZ  ARG B1113     -18.409  -4.692  94.647  1.00149.95           C  
ANISOU 8286  CZ  ARG B1113    20388  16609  19977  -1624    400   -886       C  
ATOM   8287  NH1 ARG B1113     -19.194  -5.612  94.098  1.00140.06           N  
ANISOU 8287  NH1 ARG B1113    19019  15444  18752  -1488    276   -779       N  
ATOM   8288  NH2 ARG B1113     -18.923  -3.840  95.526  1.00137.44           N  
ANISOU 8288  NH2 ARG B1113    18920  14767  18534  -1722    707   -996       N  
ATOM   8289  N   ASN B1114     -13.605  -3.937  96.837  1.00 91.73           N  
ANISOU 8289  N   ASN B1114    13356   9769  11729  -2474    106  -1173       N  
ATOM   8290  CA  ASN B1114     -13.531  -2.520  97.185  1.00 94.07           C  
ANISOU 8290  CA  ASN B1114    13801   9866  12077  -2715    361  -1338       C  
ATOM   8291  C   ASN B1114     -12.134  -2.102  97.640  1.00 99.90           C  
ANISOU 8291  C   ASN B1114    14582  10826  12550  -3056    243  -1359       C  
ATOM   8292  O   ASN B1114     -11.703  -0.999  97.296  1.00101.30           O  
ANISOU 8292  O   ASN B1114    14789  10881  12821  -3170    365  -1409       O  
ATOM   8293  CB  ASN B1114     -14.553  -2.172  98.271  1.00 99.58           C  
ANISOU 8293  CB  ASN B1114    14715  10326  12794  -2882    676  -1569       C  
ATOM   8294  CG  ASN B1114     -15.998  -2.263  97.832  1.00134.46           C  
ANISOU 8294  CG  ASN B1114    19066  14478  17546  -2573    861  -1521       C  
ATOM   8295  OD1 ASN B1114     -16.375  -1.879  96.711  1.00131.53           O  
ANISOU 8295  OD1 ASN B1114    18526  13976  17473  -2315    891  -1356       O  
ATOM   8296  ND2 ASN B1114     -16.847  -2.747  98.728  1.00129.85           N  
ANISOU 8296  ND2 ASN B1114    18589  13837  16909  -2623    985  -1629       N  
ATOM   8297  N   ALA B1115     -11.432  -2.966  98.401  1.00 96.91           N  
ANISOU 8297  N   ALA B1115    14177  10782  11862  -3231      4  -1277       N  
ATOM   8298  CA  ALA B1115     -10.102  -2.673  98.946  1.00 99.17           C  
ANISOU 8298  CA  ALA B1115    14454  11369  11858  -3611   -157  -1223       C  
ATOM   8299  C   ALA B1115      -8.985  -2.682  97.896  1.00102.79           C  
ANISOU 8299  C   ALA B1115    14670  11988  12396  -3450   -362   -983       C  
ATOM   8300  O   ALA B1115      -8.074  -1.854  97.986  1.00104.46           O  
ANISOU 8300  O   ALA B1115    14891  12302  12497  -3741   -384   -991       O  
ATOM   8301  CB  ALA B1115      -9.758  -3.656 100.053  1.00101.05           C  
ANISOU 8301  CB  ALA B1115    14664  11958  11773  -3830   -367  -1096       C  
ATOM   8302  N   TYR B1116      -9.032  -3.613  96.926  1.00 97.01           N  
ANISOU 8302  N   TYR B1116    13734  11283  11841  -3028   -486   -789       N  
ATOM   8303  CA  TYR B1116      -7.959  -3.729  95.941  1.00 96.41           C  
ANISOU 8303  CA  TYR B1116    13429  11367  11833  -2874   -636   -570       C  
ATOM   8304  C   TYR B1116      -8.376  -3.354  94.515  1.00 98.00           C  
ANISOU 8304  C   TYR B1116    13576  11370  12289  -2563   -531   -583       C  
ATOM   8305  O   TYR B1116      -7.761  -2.471  93.916  1.00 98.73           O  
ANISOU 8305  O   TYR B1116    13618  11463  12432  -2618   -510   -546       O  
ATOM   8306  CB  TYR B1116      -7.386  -5.161  95.940  1.00 97.47           C  
ANISOU 8306  CB  TYR B1116    13348  11736  11952  -2691   -831   -307       C  
ATOM   8307  CG  TYR B1116      -6.937  -5.660  97.298  1.00101.68           C  
ANISOU 8307  CG  TYR B1116    13854  12536  12243  -2984   -981   -167       C  
ATOM   8308  CD1 TYR B1116      -5.706  -5.287  97.828  1.00106.57           C  
ANISOU 8308  CD1 TYR B1116    14352  13477  12662  -3320  -1146     24       C  
ATOM   8309  CD2 TYR B1116      -7.728  -6.535  98.038  1.00102.09           C  
ANISOU 8309  CD2 TYR B1116    13972  12563  12256  -2949   -978   -178       C  
ATOM   8310  CE1 TYR B1116      -5.283  -5.750  99.074  1.00110.32           C  
ANISOU 8310  CE1 TYR B1116    14761  14280  12873  -3644  -1322    225       C  
ATOM   8311  CE2 TYR B1116      -7.313  -7.011  99.281  1.00105.37           C  
ANISOU 8311  CE2 TYR B1116    14333  13275  12426  -3243  -1134     13       C  
ATOM   8312  CZ  TYR B1116      -6.087  -6.616  99.795  1.00115.79           C  
ANISOU 8312  CZ  TYR B1116    15519  14953  13522  -3600  -1316    229       C  
ATOM   8313  OH  TYR B1116      -5.661  -7.081 101.016  1.00119.52           O  
ANISOU 8313  OH  TYR B1116    15898  15799  13714  -3943  -1508    486       O  
ATOM   8314  N   ILE B1117      -9.389  -4.043  93.974  1.00 91.58           N  
ANISOU 8314  N   ILE B1117    12756  10427  11612  -2275   -484   -608       N  
ATOM   8315  CA  ILE B1117      -9.859  -3.936  92.595  1.00 89.70           C  
ANISOU 8315  CA  ILE B1117    12434  10098  11548  -2015   -433   -568       C  
ATOM   8316  C   ILE B1117     -10.419  -2.529  92.256  1.00 92.69           C  
ANISOU 8316  C   ILE B1117    12872  10254  12093  -2069   -255   -615       C  
ATOM   8317  O   ILE B1117      -9.967  -1.952  91.265  1.00 92.38           O  
ANISOU 8317  O   ILE B1117    12721  10253  12127  -2011   -262   -500       O  
ATOM   8318  CB  ILE B1117     -10.879  -5.085  92.295  1.00 91.46           C  
ANISOU 8318  CB  ILE B1117    12652  10275  11824  -1794   -437   -591       C  
ATOM   8319  CG1 ILE B1117     -10.166  -6.462  92.276  1.00 91.39           C  
ANISOU 8319  CG1 ILE B1117    12543  10431  11750  -1686   -553   -505       C  
ATOM   8320  CG2 ILE B1117     -11.662  -4.868  90.986  1.00 91.73           C  
ANISOU 8320  CG2 ILE B1117    12617  10251  11984  -1626   -387   -553       C  
ATOM   8321  CD1 ILE B1117     -10.291  -7.286  93.518  1.00 96.96           C  
ANISOU 8321  CD1 ILE B1117    13298  11155  12385  -1757   -599   -500       C  
ATOM   8322  N   GLN B1118     -11.369  -1.990  93.054  1.00 89.09           N  
ANISOU 8322  N   GLN B1118    12572   9553  11724  -2171    -65   -758       N  
ATOM   8323  CA  GLN B1118     -12.039  -0.699  92.811  1.00 90.08           C  
ANISOU 8323  CA  GLN B1118    12734   9379  12114  -2182    189   -772       C  
ATOM   8324  C   GLN B1118     -11.054   0.473  92.578  1.00 95.70           C  
ANISOU 8324  C   GLN B1118    13440  10055  12865  -2357    249   -747       C  
ATOM   8325  O   GLN B1118     -11.278   1.274  91.663  1.00 95.73           O  
ANISOU 8325  O   GLN B1118    13335   9924  13114  -2240    351   -597       O  
ATOM   8326  CB  GLN B1118     -13.021  -0.362  93.954  1.00 92.73           C  
ANISOU 8326  CB  GLN B1118    13264   9433  12534  -2308    456   -971       C  
ATOM   8327  CG  GLN B1118     -13.760   0.982  93.817  1.00111.17           C  
ANISOU 8327  CG  GLN B1118    15629  11369  15244  -2300    819   -975       C  
ATOM   8328  CD  GLN B1118     -15.057   0.970  93.036  1.00132.68           C  
ANISOU 8328  CD  GLN B1118    18172  13945  18296  -1993    911   -755       C  
ATOM   8329  OE1 GLN B1118     -15.210   0.240  92.045  1.00126.49           O  
ANISOU 8329  OE1 GLN B1118    17194  13402  17464  -1789    661   -545       O  
ATOM   8330  NE2 GLN B1118     -15.984   1.844  93.435  1.00129.21           N  
ANISOU 8330  NE2 GLN B1118    17779  13108  18209  -1984   1300   -782       N  
ATOM   8331  N   LYS B1119      -9.980   0.551  93.385  1.00 93.58           N  
ANISOU 8331  N   LYS B1119    13264   9935  12356  -2655    170   -852       N  
ATOM   8332  CA  LYS B1119      -8.927   1.573  93.304  1.00 95.32           C  
ANISOU 8332  CA  LYS B1119    13490  10166  12562  -2896    199   -845       C  
ATOM   8333  C   LYS B1119      -8.325   1.676  91.881  1.00 97.98           C  
ANISOU 8333  C   LYS B1119    13589  10643  12996  -2676     66   -587       C  
ATOM   8334  O   LYS B1119      -8.033   2.777  91.414  1.00 98.54           O  
ANISOU 8334  O   LYS B1119    13635  10572  13235  -2748    190   -529       O  
ATOM   8335  CB  LYS B1119      -7.817   1.242  94.322  1.00 99.24           C  
ANISOU 8335  CB  LYS B1119    14044  10959  12703  -3251     19   -908       C  
ATOM   8336  CG  LYS B1119      -6.847   2.383  94.610  1.00115.69           C  
ANISOU 8336  CG  LYS B1119    16199  13041  14717  -3649     81   -976       C  
ATOM   8337  CD  LYS B1119      -5.525   1.866  95.162  1.00126.01           C  
ANISOU 8337  CD  LYS B1119    17403  14797  15677  -3926   -222   -854       C  
ATOM   8338  CE  LYS B1119      -4.558   2.995  95.428  1.00139.31           C  
ANISOU 8338  CE  LYS B1119    19149  16518  17263  -4377   -183   -915       C  
ATOM   8339  NZ  LYS B1119      -3.155   2.513  95.542  1.00147.54           N  
ANISOU 8339  NZ  LYS B1119    19958  18048  18054  -4552   -524   -646       N  
ATOM   8340  N   TYR B1120      -8.161   0.522  91.204  1.00 92.96           N  
ANISOU 8340  N   TYR B1120    12791  10268  12261  -2427   -149   -445       N  
ATOM   8341  CA  TYR B1120      -7.588   0.422  89.865  1.00 92.07           C  
ANISOU 8341  CA  TYR B1120    12473  10337  12172  -2243   -255   -236       C  
ATOM   8342  C   TYR B1120      -8.646   0.545  88.755  1.00 93.76           C  
ANISOU 8342  C   TYR B1120    12600  10459  12566  -2004   -185   -116       C  
ATOM   8343  O   TYR B1120      -8.302   0.998  87.661  1.00 93.90           O  
ANISOU 8343  O   TYR B1120    12473  10571  12636  -1940   -203     66       O  
ATOM   8344  CB  TYR B1120      -6.770  -0.876  89.718  1.00 92.64           C  
ANISOU 8344  CB  TYR B1120    12427  10717  12057  -2141   -450   -167       C  
ATOM   8345  CG  TYR B1120      -5.549  -0.890  90.618  1.00 96.41           C  
ANISOU 8345  CG  TYR B1120    12881  11371  12380  -2385   -560   -139       C  
ATOM   8346  CD1 TYR B1120      -4.529   0.046  90.459  1.00100.19           C  
ANISOU 8346  CD1 TYR B1120    13290  11927  12850  -2579   -577    -50       C  
ATOM   8347  CD2 TYR B1120      -5.435  -1.808  91.658  1.00 97.63           C  
ANISOU 8347  CD2 TYR B1120    13061  11639  12394  -2458   -660   -160       C  
ATOM   8348  CE1 TYR B1120      -3.426   0.070  91.311  1.00103.27           C  
ANISOU 8348  CE1 TYR B1120    13632  12534  13073  -2867   -707     16       C  
ATOM   8349  CE2 TYR B1120      -4.333  -1.797  92.515  1.00100.76           C  
ANISOU 8349  CE2 TYR B1120    13391  12269  12626  -2734   -797    -55       C  
ATOM   8350  CZ  TYR B1120      -3.329  -0.857  92.335  1.00110.54           C  
ANISOU 8350  CZ  TYR B1120    14553  13612  13836  -2951   -829     32       C  
ATOM   8351  OH  TYR B1120      -2.237  -0.827  93.169  1.00113.78           O  
ANISOU 8351  OH  TYR B1120    14865  14308  14059  -3279   -994    176       O  
ATOM   8352  N   LEU B1121      -9.918   0.194  89.035  1.00 88.39           N  
ANISOU 8352  N   LEU B1121    11986   9628  11972  -1906   -112   -180       N  
ATOM   8353  CA  LEU B1121     -11.009   0.320  88.061  1.00 87.74           C  
ANISOU 8353  CA  LEU B1121    11779   9505  12053  -1728    -71     -3       C  
ATOM   8354  C   LEU B1121     -11.247   1.792  87.723  1.00 94.34           C  
ANISOU 8354  C   LEU B1121    12544  10106  13195  -1756    118    173       C  
ATOM   8355  O   LEU B1121     -11.464   2.144  86.560  1.00 94.50           O  
ANISOU 8355  O   LEU B1121    12369  10229  13307  -1657     85    452       O  
ATOM   8356  CB  LEU B1121     -12.296  -0.313  88.623  1.00 86.74           C  
ANISOU 8356  CB  LEU B1121    11722   9255  11979  -1651    -22    -91       C  
ATOM   8357  CG  LEU B1121     -13.255  -1.056  87.662  1.00 90.16           C  
ANISOU 8357  CG  LEU B1121    12018   9849  12389  -1499   -124     55       C  
ATOM   8358  CD1 LEU B1121     -13.994  -0.116  86.725  1.00 93.96           C  
ANISOU 8358  CD1 LEU B1121    12298  10294  13110  -1438    -57    377       C  
ATOM   8359  CD2 LEU B1121     -12.575  -2.199  86.938  1.00 88.72           C  
ANISOU 8359  CD2 LEU B1121    11806   9984  11920  -1471   -309      7       C  
ATOM   8360  N   GLU B1122     -11.162   2.644  88.751  1.00 92.67           N  
ANISOU 8360  N   GLU B1122    12493   9585  13133  -1923    335     15       N  
ATOM   8361  CA  GLU B1122     -11.328   4.091  88.667  1.00 95.25           C  
ANISOU 8361  CA  GLU B1122    12800   9572  13821  -1978    612    125       C  
ATOM   8362  C   GLU B1122     -10.172   4.719  87.881  1.00100.36           C  
ANISOU 8362  C   GLU B1122    13334  10359  14439  -2051    528    284       C  
ATOM   8363  O   GLU B1122     -10.402   5.629  87.081  1.00101.87           O  
ANISOU 8363  O   GLU B1122    13362  10421  14923  -1973    647    569       O  
ATOM   8364  CB  GLU B1122     -11.421   4.695  90.077  1.00 98.52           C  
ANISOU 8364  CB  GLU B1122    13484   9620  14328  -2218    908   -194       C  
ATOM   8365  CG  GLU B1122     -12.659   4.252  90.845  1.00111.18           C  
ANISOU 8365  CG  GLU B1122    15188  11035  16019  -2143   1065   -328       C  
ATOM   8366  CD  GLU B1122     -12.647   4.466  92.347  1.00140.45           C  
ANISOU 8366  CD  GLU B1122    19209  14515  19640  -2439   1306   -721       C  
ATOM   8367  OE1 GLU B1122     -11.559   4.362  92.957  1.00146.05           O  
ANISOU 8367  OE1 GLU B1122    20064  15411  20016  -2735   1177   -920       O  
ATOM   8368  OE2 GLU B1122     -13.741   4.667  92.926  1.00133.13           O  
ANISOU 8368  OE2 GLU B1122    18367  13265  18950  -2396   1615   -813       O  
ATOM   8369  N   ARG B1123      -8.937   4.200  88.087  1.00 96.20           N  
ANISOU 8369  N   ARG B1123    12858  10114  13580  -2189    323    153       N  
ATOM   8370  CA  ARG B1123      -7.712   4.654  87.420  1.00 97.11           C  
ANISOU 8370  CA  ARG B1123    12858  10413  13627  -2273    225    291       C  
ATOM   8371  C   ARG B1123      -7.764   4.402  85.911  1.00 99.60           C  
ANISOU 8371  C   ARG B1123    12928  10996  13920  -2055     88    599       C  
ATOM   8372  O   ARG B1123      -7.332   5.261  85.139  1.00101.06           O  
ANISOU 8372  O   ARG B1123    12978  11188  14232  -2076    126    826       O  
ATOM   8373  CB  ARG B1123      -6.472   3.961  88.010  1.00 98.86           C  
ANISOU 8373  CB  ARG B1123    13130  10917  13515  -2440     28    143       C  
ATOM   8374  CG  ARG B1123      -5.959   4.550  89.318  1.00115.99           C  
ANISOU 8374  CG  ARG B1123    15501  12940  15630  -2806    124    -90       C  
ATOM   8375  CD  ARG B1123      -4.570   4.013  89.608  1.00127.43           C  
ANISOU 8375  CD  ARG B1123    16878  14760  16781  -2976   -118    -67       C  
ATOM   8376  NE  ARG B1123      -4.166   4.218  90.996  1.00137.98           N  
ANISOU 8376  NE  ARG B1123    18398  16090  17936  -3381   -108   -280       N  
ATOM   8377  CZ  ARG B1123      -3.003   3.819  91.499  1.00153.37           C  
ANISOU 8377  CZ  ARG B1123    20268  18385  19623  -3610   -327   -218       C  
ATOM   8378  NH1 ARG B1123      -2.118   3.193  90.730  1.00138.24           N  
ANISOU 8378  NH1 ARG B1123    18086  16784  17654  -3421   -527     42       N  
ATOM   8379  NH2 ARG B1123      -2.712   4.045  92.772  1.00142.66           N  
ANISOU 8379  NH2 ARG B1123    19078  17077  18049  -4052   -333   -394       N  
ATOM   8380  N   ALA B1124      -8.279   3.222  85.497  1.00 92.86           N  
ANISOU 8380  N   ALA B1124    12028  10374  12882  -1888    -59    598       N  
ATOM   8381  CA  ALA B1124      -8.396   2.824  84.093  1.00 91.74           C  
ANISOU 8381  CA  ALA B1124    11696  10542  12620  -1760   -181    826       C  
ATOM   8382  C   ALA B1124      -9.359   3.744  83.347  1.00 96.50           C  
ANISOU 8382  C   ALA B1124    12130  11040  13495  -1698    -90   1164       C  
ATOM   8383  O   ALA B1124      -9.110   4.090  82.191  1.00 97.22           O  
ANISOU 8383  O   ALA B1124    12033  11359  13546  -1692   -152   1449       O  
ATOM   8384  CB  ALA B1124      -8.864   1.380  84.000  1.00 90.70           C  
ANISOU 8384  CB  ALA B1124    11606  10606  12249  -1663   -299    682       C  
ATOM   8385  N   ARG B1125     -10.443   4.159  84.026  1.00 93.46           N  
ANISOU 8385  N   ARG B1125    11789  10314  13406  -1656     76   1170       N  
ATOM   8386  CA  ARG B1125     -11.468   5.045  83.483  1.00 95.42           C  
ANISOU 8386  CA  ARG B1125    11831  10400  14024  -1565    208   1559       C  
ATOM   8387  C   ARG B1125     -10.935   6.465  83.301  1.00101.69           C  
ANISOU 8387  C   ARG B1125    12544  10945  15148  -1622    399   1770       C  
ATOM   8388  O   ARG B1125     -11.196   7.070  82.261  1.00103.68           O  
ANISOU 8388  O   ARG B1125    12528  11298  15567  -1563    388   2220       O  
ATOM   8389  CB  ARG B1125     -12.710   5.042  84.388  1.00 95.66           C  
ANISOU 8389  CB  ARG B1125    11931  10087  14329  -1487    398   1484       C  
ATOM   8390  CG  ARG B1125     -13.608   3.835  84.145  1.00104.79           C  
ANISOU 8390  CG  ARG B1125    13039  11514  15261  -1407    207   1484       C  
ATOM   8391  CD  ARG B1125     -14.347   3.382  85.390  1.00113.77           C  
ANISOU 8391  CD  ARG B1125    14366  12381  16480  -1380    339   1196       C  
ATOM   8392  NE  ARG B1125     -15.407   4.312  85.785  1.00122.67           N  
ANISOU 8392  NE  ARG B1125    15401  13091  18117  -1289    652   1397       N  
ATOM   8393  CZ  ARG B1125     -16.543   3.950  86.373  1.00132.06           C  
ANISOU 8393  CZ  ARG B1125    16596  14126  19454  -1206    760   1369       C  
ATOM   8394  NH1 ARG B1125     -16.789   2.671  86.632  1.00108.40           N  
ANISOU 8394  NH1 ARG B1125    13705  11366  16117  -1219    554   1146       N  
ATOM   8395  NH2 ARG B1125     -17.448   4.865  86.696  1.00124.53           N  
ANISOU 8395  NH2 ARG B1125    15530  12756  19030  -1102   1110   1581       N  
ATOM   8396  N   SER B1126     -10.170   6.979  84.289  1.00 98.10           N  
ANISOU 8396  N   SER B1126    12312  10196  14765  -1776    564   1465       N  
ATOM   8397  CA  SER B1126      -9.601   8.330  84.284  1.00100.49           C  
ANISOU 8397  CA  SER B1126    12597  10195  15389  -1890    790   1580       C  
ATOM   8398  C   SER B1126      -8.543   8.535  83.192  1.00104.13           C  
ANISOU 8398  C   SER B1126    12885  11002  15678  -1932    602   1820       C  
ATOM   8399  O   SER B1126      -8.517   9.605  82.583  1.00106.19           O  
ANISOU 8399  O   SER B1126    12972  11108  16266  -1923    741   2168       O  
ATOM   8400  CB  SER B1126      -9.002   8.667  85.646  1.00104.71           C  
ANISOU 8400  CB  SER B1126    13449  10416  15920  -2143    978   1130       C  
ATOM   8401  OG  SER B1126      -7.991   7.748  86.023  1.00112.25           O  
ANISOU 8401  OG  SER B1126    14527  11729  16394  -2280    708    854       O  
ATOM   8402  N   THR B1127      -7.674   7.526  82.959  1.00 98.37           N  
ANISOU 8402  N   THR B1127    12189  10712  14476  -1970    325   1656       N  
ATOM   8403  CA  THR B1127      -6.602   7.575  81.954  1.00 98.48           C  
ANISOU 8403  CA  THR B1127    12050  11085  14284  -2011    170   1840       C  
ATOM   8404  C   THR B1127      -7.179   7.671  80.535  1.00103.08           C  
ANISOU 8404  C   THR B1127    12353  11943  14868  -1890     85   2291       C  
ATOM   8405  O   THR B1127      -6.643   8.418  79.711  1.00105.04           O  
ANISOU 8405  O   THR B1127    12427  12296  15188  -1935     91   2600       O  
ATOM   8406  CB  THR B1127      -5.657   6.370  82.080  1.00106.47           C  
ANISOU 8406  CB  THR B1127    13143  12456  14855  -2042    -35   1570       C  
ATOM   8407  OG1 THR B1127      -6.424   5.164  82.147  1.00108.38           O  
ANISOU 8407  OG1 THR B1127    13440  12837  14900  -1916   -133   1426       O  
ATOM   8408  CG2 THR B1127      -4.717   6.480  83.279  1.00103.97           C  
ANISOU 8408  CG2 THR B1127    13004  11998  14500  -2238     -7   1275       C  
ATOM   8409  N   LEU B1128      -8.281   6.944  80.263  1.00 97.85           N  
ANISOU 8409  N   LEU B1128    11638  11425  14116  -1778     -1   2354       N  
ATOM   8410  CA  LEU B1128      -8.950   6.965  78.965  1.00 98.98           C  
ANISOU 8410  CA  LEU B1128    11506  11907  14196  -1738   -117   2804       C  
ATOM   8411  C   LEU B1128      -9.806   8.226  78.789  1.00107.86           C  
ANISOU 8411  C   LEU B1128    12397  12725  15858  -1667     59   3297       C  
ATOM   8412  O   LEU B1128     -10.082   8.623  77.656  1.00109.82           O  
ANISOU 8412  O   LEU B1128    12348  13255  16122  -1676    -27   3809       O  
ATOM   8413  CB  LEU B1128      -9.796   5.711  78.784  1.00 97.03           C  
ANISOU 8413  CB  LEU B1128    11288  11943  13638  -1707   -278   2685       C  
ATOM   8414  CG  LEU B1128      -9.136   4.609  77.974  1.00 99.93           C  
ANISOU 8414  CG  LEU B1128    11697  12814  13460  -1797   -454   2511       C  
ATOM   8415  CD1 LEU B1128      -8.330   3.661  78.865  1.00 97.00           C  
ANISOU 8415  CD1 LEU B1128    11595  12354  12907  -1776   -439   1987       C  
ATOM   8416  CD2 LEU B1128     -10.163   3.862  77.179  1.00102.89           C  
ANISOU 8416  CD2 LEU B1128    11970  13557  13569  -1857   -602   2650       C  
ATOM   8417  N   SER B1129     -10.213   8.861  79.905  1.00106.54           N  
ANISOU 8417  N   SER B1129    12356  11982  16144  -1612    336   3162       N  
ATOM   8418  CA  SER B1129     -11.002  10.096  79.904  1.00110.67           C  
ANISOU 8418  CA  SER B1129    12674  12071  17305  -1514    621   3597       C  
ATOM   8419  C   SER B1129     -10.120  11.290  79.548  1.00119.82           C  
ANISOU 8419  C   SER B1129    13745  13049  18730  -1592    770   3823       C  
ATOM   8420  O   SER B1129     -10.622  12.310  79.073  1.00123.18           O  
ANISOU 8420  O   SER B1129    13893  13251  19659  -1505    955   4359       O  
ATOM   8421  CB  SER B1129     -11.664  10.312  81.260  1.00113.63           C  
ANISOU 8421  CB  SER B1129    13265  11856  18054  -1460    946   3284       C  
ATOM   8422  OG  SER B1129     -12.642   9.316  81.506  1.00119.74           O  
ANISOU 8422  OG  SER B1129    14055  12779  18663  -1368    827   3186       O  
ATOM   8423  N   LYS B1130      -8.798  11.142  79.753  1.00116.79           N  
ANISOU 8423  N   LYS B1130    13566  12778  18030  -1755    687   3462       N  
ATOM   8424  CA  LYS B1130      -7.793  12.163  79.474  1.00119.88           C  
ANISOU 8424  CA  LYS B1130    13909  13042  18599  -1877    797   3605       C  
ATOM   8425  C   LYS B1130      -7.606  12.380  77.949  1.00128.99           C  
ANISOU 8425  C   LYS B1130    14709  14665  19636  -1853    604   4184       C  
ATOM   8426  O   LYS B1130      -6.996  13.379  77.554  1.00131.15           O  
ANISOU 8426  O   LYS B1130    14859  14811  20160  -1921    720   4460       O  
ATOM   8427  CB  LYS B1130      -6.473  11.807  80.170  1.00120.16           C  
ANISOU 8427  CB  LYS B1130    14229  13139  18288  -2079    724   3080       C  
ATOM   8428  CG  LYS B1130      -6.485  12.150  81.662  1.00135.30           C  
ANISOU 8428  CG  LYS B1130    16467  14519  20421  -2219    995   2616       C  
ATOM   8429  CD  LYS B1130      -5.507  11.293  82.455  1.00144.31           C  
ANISOU 8429  CD  LYS B1130    17857  15889  21084  -2403    808   2117       C  
ATOM   8430  CE  LYS B1130      -5.639  11.492  83.946  1.00155.03           C  
ANISOU 8430  CE  LYS B1130    19539  16824  22543  -2601   1036   1660       C  
ATOM   8431  NZ  LYS B1130      -4.731  10.588  84.702  1.00160.71           N  
ANISOU 8431  NZ  LYS B1130    20435  17848  22780  -2789    805   1279       N  
ATOM   8432  N   ILE B1131      -8.157  11.470  77.100  1.00127.32           N  
ANISOU 8432  N   ILE B1131    14340  15000  19037  -1798    327   4371       N  
ATOM   8433  CA  ILE B1131      -8.156  11.578  75.635  1.00130.46           C  
ANISOU 8433  CA  ILE B1131    14405  15931  19234  -1838    131   4928       C  
ATOM   8434  C   ILE B1131      -9.173  12.676  75.274  1.00142.67           C  
ANISOU 8434  C   ILE B1131    15597  17221  21391  -1725    294   5627       C  
ATOM   8435  O   ILE B1131     -10.383  12.425  75.295  1.00142.92           O  
ANISOU 8435  O   ILE B1131    15487  17259  21558  -1620    274   5848       O  
ATOM   8436  CB  ILE B1131      -8.470  10.217  74.923  1.00131.48           C  
ANISOU 8436  CB  ILE B1131    14526  16717  18713  -1898   -180   4834       C  
ATOM   8437  CG1 ILE B1131      -7.546   9.072  75.407  1.00127.64           C  
ANISOU 8437  CG1 ILE B1131    14377  16372  17747  -1954   -261   4152       C  
ATOM   8438  CG2 ILE B1131      -8.440  10.369  73.390  1.00135.13           C  
ANISOU 8438  CG2 ILE B1131    14664  17791  18890  -2030   -370   5395       C  
ATOM   8439  CD1 ILE B1131      -8.050   7.651  75.122  1.00129.72           C  
ANISOU 8439  CD1 ILE B1131    14730  17048  17509  -1989   -449   3907       C  
ATOM   8440  N   ASN B 446      -8.686  13.908  75.025  1.00111.71           N  
ANISOU 8440  N   ASN B 446    12817  19323  10307  -1824    629   3413       N  
ATOM   8441  CA  ASN B 446      -9.550  15.051  74.704  1.00112.17           C  
ANISOU 8441  CA  ASN B 446    12888  19468  10264  -1767    720   3241       C  
ATOM   8442  C   ASN B 446      -9.912  15.081  73.205  1.00117.05           C  
ANISOU 8442  C   ASN B 446    13461  19969  11044  -1705    751   3124       C  
ATOM   8443  O   ASN B 446      -9.332  14.334  72.412  1.00116.19           O  
ANISOU 8443  O   ASN B 446    13319  19710  11117  -1710    698   3150       O  
ATOM   8444  CB  ASN B 446      -8.928  16.393  75.164  1.00114.15           C  
ANISOU 8444  CB  ASN B 446    13230  19784  10358  -1725    705   3128       C  
ATOM   8445  CG  ASN B 446      -7.470  16.646  74.832  1.00139.88           C  
ANISOU 8445  CG  ASN B 446    16526  22938  13684  -1716    609   3101       C  
ATOM   8446  OD1 ASN B 446      -6.757  15.806  74.267  1.00134.89           O  
ANISOU 8446  OD1 ASN B 446    15848  22185  13219  -1722    540   3171       O  
ATOM   8447  ND2 ASN B 446      -6.987  17.827  75.197  1.00132.47           N  
ANISOU 8447  ND2 ASN B 446    15670  22050  12611  -1707    606   2988       N  
ATOM   8448  N   GLU B 447     -10.904  15.925  72.840  1.00114.79           N  
ANISOU 8448  N   GLU B 447    13168  19768  10680  -1637    837   2996       N  
ATOM   8449  CA  GLU B 447     -11.407  16.078  71.478  1.00114.18           C  
ANISOU 8449  CA  GLU B 447    13040  19633  10710  -1567    873   2886       C  
ATOM   8450  C   GLU B 447     -10.311  16.533  70.524  1.00117.12           C  
ANISOU 8450  C   GLU B 447    13460  19858  11184  -1511    813   2809       C  
ATOM   8451  O   GLU B 447     -10.260  16.013  69.414  1.00116.06           O  
ANISOU 8451  O   GLU B 447    13266  19633  11200  -1502    800   2781       O  
ATOM   8452  CB  GLU B 447     -12.612  17.031  71.416  1.00116.03           C  
ANISOU 8452  CB  GLU B 447    13263  20012  10812  -1475    970   2776       C  
ATOM   8453  CG  GLU B 447     -13.569  16.705  70.275  1.00128.03           C  
ANISOU 8453  CG  GLU B 447    14671  21555  12420  -1440   1015   2718       C  
ATOM   8454  CD  GLU B 447     -14.973  17.281  70.347  1.00152.32           C  
ANISOU 8454  CD  GLU B 447    17684  24826  15366  -1360   1112   2647       C  
ATOM   8455  OE1 GLU B 447     -15.547  17.356  71.460  1.00146.49           O  
ANISOU 8455  OE1 GLU B 447    16937  24237  14484  -1389   1162   2683       O  
ATOM   8456  OE2 GLU B 447     -15.525  17.603  69.269  1.00146.40           O  
ANISOU 8456  OE2 GLU B 447    16876  24099  14652  -1265   1139   2558       O  
ATOM   8457  N   THR B 448      -9.441  17.482  70.948  1.00113.89           N  
ANISOU 8457  N   THR B 448    13153  19435  10686  -1490    782   2767       N  
ATOM   8458  CA  THR B 448      -8.324  18.030  70.156  1.00113.00           C  
ANISOU 8458  CA  THR B 448    13091  19202  10643  -1461    731   2696       C  
ATOM   8459  C   THR B 448      -7.373  16.918  69.669  1.00115.74           C  
ANISOU 8459  C   THR B 448    13371  19441  11165  -1509    649   2767       C  
ATOM   8460  O   THR B 448      -6.842  16.990  68.556  1.00113.92           O  
ANISOU 8460  O   THR B 448    13123  19119  11043  -1478    629   2702       O  
ATOM   8461  CB  THR B 448      -7.542  19.087  70.972  1.00123.95           C  
ANISOU 8461  CB  THR B 448    14594  20613  11890  -1477    711   2652       C  
ATOM   8462  OG1 THR B 448      -7.415  18.658  72.334  1.00124.08           O  
ANISOU 8462  OG1 THR B 448    14608  20732  11804  -1551    681   2753       O  
ATOM   8463  CG2 THR B 448      -8.170  20.494  70.905  1.00123.78           C  
ANISOU 8463  CG2 THR B 448    14673  20612  11744  -1393    793   2522       C  
ATOM   8464  N   MET B 449      -7.178  15.891  70.513  1.00113.35           N  
ANISOU 8464  N   MET B 449    13034  19152  10884  -1576    605   2906       N  
ATOM   8465  CA  MET B 449      -6.347  14.715  70.255  1.00113.45           C  
ANISOU 8465  CA  MET B 449    12989  19055  11063  -1602    529   2995       C  
ATOM   8466  C   MET B 449      -6.939  13.886  69.101  1.00115.94           C  
ANISOU 8466  C   MET B 449    13226  19275  11549  -1592    562   2962       C  
ATOM   8467  O   MET B 449      -6.233  13.589  68.136  1.00114.90           O  
ANISOU 8467  O   MET B 449    13060  19041  11556  -1564    525   2911       O  
ATOM   8468  CB  MET B 449      -6.245  13.868  71.535  1.00117.53           C  
ANISOU 8468  CB  MET B 449    13505  19615  11538  -1664    489   3173       C  
ATOM   8469  CG  MET B 449      -5.071  12.927  71.577  1.00122.22           C  
ANISOU 8469  CG  MET B 449    14069  20110  12260  -1662    391   3279       C  
ATOM   8470  SD  MET B 449      -5.030  11.945  73.105  1.00128.80           S  
ANISOU 8470  SD  MET B 449    14913  20998  13028  -1720    345   3522       S  
ATOM   8471  CE  MET B 449      -4.231  13.086  74.211  1.00125.88           C  
ANISOU 8471  CE  MET B 449    14593  20815  12421  -1731    292   3509       C  
ATOM   8472  N   LEU B 450      -8.239  13.541  69.195  1.00112.37           N  
ANISOU 8472  N   LEU B 450    12739  18881  11076  -1622    633   2977       N  
ATOM   8473  CA  LEU B 450      -8.952  12.754  68.184  1.00111.85           C  
ANISOU 8473  CA  LEU B 450    12591  18756  11149  -1639    671   2933       C  
ATOM   8474  C   LEU B 450      -9.183  13.557  66.909  1.00115.03           C  
ANISOU 8474  C   LEU B 450    12970  19178  11558  -1561    704   2771       C  
ATOM   8475  O   LEU B 450      -9.148  12.981  65.820  1.00114.74           O  
ANISOU 8475  O   LEU B 450    12870  19067  11660  -1561    700   2709       O  
ATOM   8476  CB  LEU B 450     -10.289  12.225  68.726  1.00112.70           C  
ANISOU 8476  CB  LEU B 450    12655  18957  11208  -1716    742   2992       C  
ATOM   8477  CG  LEU B 450     -10.207  11.186  69.845  1.00118.72           C  
ANISOU 8477  CG  LEU B 450    13436  19685  11986  -1814    720   3176       C  
ATOM   8478  CD1 LEU B 450     -11.569  10.909  70.409  1.00120.09           C  
ANISOU 8478  CD1 LEU B 450    13567  19992  12071  -1902    805   3223       C  
ATOM   8479  CD2 LEU B 450      -9.591   9.885  69.359  1.00121.66           C  
ANISOU 8479  CD2 LEU B 450    13794  19853  12580  -1850    671   3235       C  
ATOM   8480  N   ARG B 451      -9.392  14.886  67.046  1.00110.65           N  
ANISOU 8480  N   ARG B 451    12474  18717  10850  -1493    736   2705       N  
ATOM   8481  CA  ARG B 451      -9.588  15.823  65.935  1.00109.12           C  
ANISOU 8481  CA  ARG B 451    12285  18542  10635  -1401    767   2578       C  
ATOM   8482  C   ARG B 451      -8.320  15.880  65.086  1.00109.90           C  
ANISOU 8482  C   ARG B 451    12397  18524  10835  -1388    709   2534       C  
ATOM   8483  O   ARG B 451      -8.412  15.947  63.861  1.00109.06           O  
ANISOU 8483  O   ARG B 451    12245  18405  10788  -1347    721   2451       O  
ATOM   8484  CB  ARG B 451      -9.960  17.221  66.450  1.00110.87           C  
ANISOU 8484  CB  ARG B 451    12599  18849  10677  -1326    813   2536       C  
ATOM   8485  CG  ARG B 451     -10.722  18.065  65.440  1.00124.85           C  
ANISOU 8485  CG  ARG B 451    14361  20672  12405  -1214    869   2435       C  
ATOM   8486  CD  ARG B 451     -10.813  19.507  65.891  1.00138.25           C  
ANISOU 8486  CD  ARG B 451    16186  22392  13951  -1124    909   2390       C  
ATOM   8487  NE  ARG B 451     -11.430  20.357  64.873  1.00147.04           N  
ANISOU 8487  NE  ARG B 451    17309  23531  15029   -992    956   2314       N  
ATOM   8488  CZ  ARG B 451     -11.206  21.661  64.756  1.00159.71           C  
ANISOU 8488  CZ  ARG B 451    19049  25080  16553   -901    981   2265       C  
ATOM   8489  NH1 ARG B 451     -10.367  22.274  65.582  1.00148.13           N  
ANISOU 8489  NH1 ARG B 451    17715  23534  15032   -947    966   2263       N  
ATOM   8490  NH2 ARG B 451     -11.810  22.361  63.805  1.00143.45           N  
ANISOU 8490  NH2 ARG B 451    16998  23043  14464   -767   1022   2221       N  
ATOM   8491  N   LEU B 452      -7.141  15.807  65.742  1.00104.91           N  
ANISOU 8491  N   LEU B 452    11813  17835  10215  -1424    643   2593       N  
ATOM   8492  CA  LEU B 452      -5.837  15.786  65.085  1.00103.87           C  
ANISOU 8492  CA  LEU B 452    11674  17620  10172  -1421    585   2559       C  
ATOM   8493  C   LEU B 452      -5.726  14.557  64.170  1.00106.77           C  
ANISOU 8493  C   LEU B 452    11938  17908  10723  -1429    567   2544       C  
ATOM   8494  O   LEU B 452      -5.232  14.680  63.051  1.00106.16           O  
ANISOU 8494  O   LEU B 452    11826  17800  10709  -1401    561   2456       O  
ATOM   8495  CB  LEU B 452      -4.707  15.798  66.127  1.00104.49           C  
ANISOU 8495  CB  LEU B 452    11794  17693  10215  -1463    514   2636       C  
ATOM   8496  CG  LEU B 452      -3.295  16.036  65.596  1.00109.23           C  
ANISOU 8496  CG  LEU B 452    12383  18254  10867  -1464    457   2591       C  
ATOM   8497  CD1 LEU B 452      -3.055  17.503  65.288  1.00109.12           C  
ANISOU 8497  CD1 LEU B 452    12458  18267  10736  -1461    489   2499       C  
ATOM   8498  CD2 LEU B 452      -2.270  15.576  66.585  1.00113.10           C  
ANISOU 8498  CD2 LEU B 452    12860  18758  11355  -1499    373   2687       C  
ATOM   8499  N   GLY B 453      -6.227  13.414  64.642  1.00103.06           N  
ANISOU 8499  N   GLY B 453    11426  17404  10328  -1475    566   2623       N  
ATOM   8500  CA  GLY B 453      -6.251  12.163  63.891  1.00102.82           C  
ANISOU 8500  CA  GLY B 453    11315  17273  10478  -1495    559   2603       C  
ATOM   8501  C   GLY B 453      -7.196  12.195  62.707  1.00105.61           C  
ANISOU 8501  C   GLY B 453    11604  17672  10853  -1487    619   2480       C  
ATOM   8502  O   GLY B 453      -6.872  11.652  61.647  1.00105.20           O  
ANISOU 8502  O   GLY B 453    11489  17559  10923  -1479    611   2392       O  
ATOM   8503  N   ILE B 454      -8.371  12.845  62.882  1.00101.54           N  
ANISOU 8503  N   ILE B 454    11092  17282  10205  -1481    680   2466       N  
ATOM   8504  CA  ILE B 454      -9.395  13.016  61.841  1.00100.81           C  
ANISOU 8504  CA  ILE B 454    10925  17287  10093  -1459    734   2357       C  
ATOM   8505  C   ILE B 454      -8.769  13.810  60.687  1.00104.74           C  
ANISOU 8505  C   ILE B 454    11427  17794  10577  -1381    724   2258       C  
ATOM   8506  O   ILE B 454      -8.874  13.397  59.529  1.00104.60           O  
ANISOU 8506  O   ILE B 454    11328  17785  10632  -1381    730   2163       O  
ATOM   8507  CB  ILE B 454     -10.683  13.684  62.412  1.00103.62           C  
ANISOU 8507  CB  ILE B 454    11282  17800  10290  -1439    796   2375       C  
ATOM   8508  CG1 ILE B 454     -11.409  12.725  63.381  1.00104.92           C  
ANISOU 8508  CG1 ILE B 454    11414  17978  10473  -1545    819   2467       C  
ATOM   8509  CG2 ILE B 454     -11.632  14.157  61.292  1.00103.74           C  
ANISOU 8509  CG2 ILE B 454    11217  17951  10249  -1375    843   2265       C  
ATOM   8510  CD1 ILE B 454     -12.215  13.392  64.458  1.00111.04           C  
ANISOU 8510  CD1 ILE B 454    12220  18892  11078  -1531    865   2523       C  
ATOM   8511  N   PHE B 455      -8.059  14.905  61.026  1.00100.53           N  
ANISOU 8511  N   PHE B 455    10991  17256   9950  -1331    707   2280       N  
ATOM   8512  CA  PHE B 455      -7.349  15.758  60.080  1.00 99.43           C  
ANISOU 8512  CA  PHE B 455    10880  17115   9783  -1277    701   2211       C  
ATOM   8513  C   PHE B 455      -6.209  14.987  59.427  1.00102.49           C  
ANISOU 8513  C   PHE B 455    11210  17417  10313  -1308    653   2173       C  
ATOM   8514  O   PHE B 455      -6.000  15.142  58.230  1.00102.16           O  
ANISOU 8514  O   PHE B 455    11125  17403  10289  -1282    662   2086       O  
ATOM   8515  CB  PHE B 455      -6.834  17.021  60.784  1.00101.22           C  
ANISOU 8515  CB  PHE B 455    11239  17335   9885  -1251    699   2248       C  
ATOM   8516  CG  PHE B 455      -7.823  18.163  60.783  1.00103.16           C  
ANISOU 8516  CG  PHE B 455    11551  17659   9986  -1169    760   2231       C  
ATOM   8517  CD1 PHE B 455      -8.990  18.096  61.535  1.00107.18           C  
ANISOU 8517  CD1 PHE B 455    12047  18248  10427  -1149    799   2262       C  
ATOM   8518  CD2 PHE B 455      -7.586  19.308  60.035  1.00105.35           C  
ANISOU 8518  CD2 PHE B 455    11903  17931  10192  -1105    782   2190       C  
ATOM   8519  CE1 PHE B 455      -9.911  19.146  61.524  1.00108.61           C  
ANISOU 8519  CE1 PHE B 455    12279  18510  10476  -1045    857   2241       C  
ATOM   8520  CE2 PHE B 455      -8.498  20.368  60.042  1.00108.80           C  
ANISOU 8520  CE2 PHE B 455    12415  18421  10504  -1001    839   2184       C  
ATOM   8521  CZ  PHE B 455      -9.663  20.273  60.773  1.00107.57           C  
ANISOU 8521  CZ  PHE B 455    12233  18351  10286   -960    875   2203       C  
ATOM   8522  N   GLY B 456      -5.533  14.139  60.209  1.00 98.86           N  
ANISOU 8522  N   GLY B 456    10746  16868   9947  -1353    605   2241       N  
ATOM   8523  CA  GLY B 456      -4.442  13.279  59.765  1.00 98.87           C  
ANISOU 8523  CA  GLY B 456    10687  16781  10095  -1361    557   2213       C  
ATOM   8524  C   GLY B 456      -4.859  12.315  58.677  1.00103.83           C  
ANISOU 8524  C   GLY B 456    11217  17385  10848  -1369    579   2114       C  
ATOM   8525  O   GLY B 456      -4.184  12.214  57.649  1.00103.08           O  
ANISOU 8525  O   GLY B 456    11067  17290  10811  -1346    572   2017       O  
ATOM   8526  N   PHE B 457      -5.999  11.626  58.881  1.00102.23           N  
ANISOU 8526  N   PHE B 457    10987  17178  10676  -1412    612   2126       N  
ATOM   8527  CA  PHE B 457      -6.551  10.700  57.893  1.00103.29           C  
ANISOU 8527  CA  PHE B 457    11028  17298  10918  -1446    640   2014       C  
ATOM   8528  C   PHE B 457      -7.103  11.478  56.702  1.00107.95           C  
ANISOU 8528  C   PHE B 457    11568  18044  11406  -1411    678   1899       C  
ATOM   8529  O   PHE B 457      -6.942  11.034  55.563  1.00107.54           O  
ANISOU 8529  O   PHE B 457    11436  18004  11420  -1413    685   1773       O  
ATOM   8530  CB  PHE B 457      -7.633   9.797  58.505  1.00106.09           C  
ANISOU 8530  CB  PHE B 457    11369  17618  11322  -1532    669   2062       C  
ATOM   8531  CG  PHE B 457      -7.092   8.600  59.255  1.00108.94           C  
ANISOU 8531  CG  PHE B 457    11762  17788  11842  -1573    636   2152       C  
ATOM   8532  CD1 PHE B 457      -6.603   7.491  58.572  1.00112.96           C  
ANISOU 8532  CD1 PHE B 457    12229  18153  12537  -1584    625   2068       C  
ATOM   8533  CD2 PHE B 457      -7.093   8.569  60.647  1.00111.55           C  
ANISOU 8533  CD2 PHE B 457    12168  18083  12132  -1595    617   2321       C  
ATOM   8534  CE1 PHE B 457      -6.106   6.379  59.276  1.00115.18           C  
ANISOU 8534  CE1 PHE B 457    12555  18233  12974  -1600    595   2167       C  
ATOM   8535  CE2 PHE B 457      -6.596   7.459  61.347  1.00115.44           C  
ANISOU 8535  CE2 PHE B 457    12697  18400  12764  -1620    582   2431       C  
ATOM   8536  CZ  PHE B 457      -6.107   6.372  60.658  1.00114.50           C  
ANISOU 8536  CZ  PHE B 457    12547  18115  12841  -1615    571   2359       C  
ATOM   8537  N   LEU B 458      -7.715  12.660  56.967  1.00105.11           N  
ANISOU 8537  N   LEU B 458    11257  17803  10877  -1366    703   1942       N  
ATOM   8538  CA  LEU B 458      -8.275  13.551  55.944  1.00105.06           C  
ANISOU 8538  CA  LEU B 458    11221  17948  10749  -1305    737   1869       C  
ATOM   8539  C   LEU B 458      -7.175  14.045  55.011  1.00108.47           C  
ANISOU 8539  C   LEU B 458    11661  18376  11178  -1266    719   1814       C  
ATOM   8540  O   LEU B 458      -7.378  14.089  53.797  1.00107.93           O  
ANISOU 8540  O   LEU B 458    11519  18406  11084  -1247    736   1717       O  
ATOM   8541  CB  LEU B 458      -9.010  14.740  56.591  1.00105.13           C  
ANISOU 8541  CB  LEU B 458    11308  18045  10592  -1240    766   1945       C  
ATOM   8542  CG  LEU B 458     -10.137  15.383  55.773  1.00110.42           C  
ANISOU 8542  CG  LEU B 458    11925  18892  11138  -1165    808   1894       C  
ATOM   8543  CD1 LEU B 458     -11.369  14.476  55.705  1.00111.38           C  
ANISOU 8543  CD1 LEU B 458    11919  19116  11285  -1223    833   1849       C  
ATOM   8544  CD2 LEU B 458     -10.540  16.715  56.372  1.00113.10           C  
ANISOU 8544  CD2 LEU B 458    12372  19276  11324  -1066    834   1967       C  
ATOM   8545  N   ALA B 459      -5.999  14.371  55.581  1.00105.14           N  
ANISOU 8545  N   ALA B 459    11315  17861  10772  -1267    684   1872       N  
ATOM   8546  CA  ALA B 459      -4.817  14.803  54.842  1.00104.82           C  
ANISOU 8546  CA  ALA B 459    11276  17821  10730  -1254    669   1828       C  
ATOM   8547  C   ALA B 459      -4.211  13.617  54.094  1.00109.25           C  
ANISOU 8547  C   ALA B 459    11725  18344  11442  -1278    651   1726       C  
ATOM   8548  O   ALA B 459      -3.806  13.781  52.942  1.00108.45           O  
ANISOU 8548  O   ALA B 459    11566  18315  11323  -1266    664   1634       O  
ATOM   8549  CB  ALA B 459      -3.795  15.418  55.785  1.00105.25           C  
ANISOU 8549  CB  ALA B 459    11427  17809  10755  -1268    636   1913       C  
ATOM   8550  N   PHE B 460      -4.202  12.415  54.731  1.00106.59           N  
ANISOU 8550  N   PHE B 460    11359  17890  11249  -1310    627   1743       N  
ATOM   8551  CA  PHE B 460      -3.687  11.173  54.143  1.00106.98           C  
ANISOU 8551  CA  PHE B 460    11319  17861  11467  -1321    615   1643       C  
ATOM   8552  C   PHE B 460      -4.430  10.823  52.852  1.00110.63           C  
ANISOU 8552  C   PHE B 460    11687  18416  11931  -1337    657   1491       C  
ATOM   8553  O   PHE B 460      -3.794  10.386  51.890  1.00110.67           O  
ANISOU 8553  O   PHE B 460    11616  18433  12001  -1327    659   1366       O  
ATOM   8554  CB  PHE B 460      -3.784   9.999  55.136  1.00109.46           C  
ANISOU 8554  CB  PHE B 460    11651  18011  11929  -1350    591   1713       C  
ATOM   8555  CG  PHE B 460      -3.195   8.711  54.607  1.00111.89           C  
ANISOU 8555  CG  PHE B 460    11890  18194  12428  -1343    581   1613       C  
ATOM   8556  CD1 PHE B 460      -3.986   7.792  53.925  1.00115.45           C  
ANISOU 8556  CD1 PHE B 460    12284  18612  12970  -1394    619   1492       C  
ATOM   8557  CD2 PHE B 460      -1.844   8.430  54.767  1.00114.27           C  
ANISOU 8557  CD2 PHE B 460    12179  18423  12817  -1282    535   1627       C  
ATOM   8558  CE1 PHE B 460      -3.435   6.618  53.408  1.00117.48           C  
ANISOU 8558  CE1 PHE B 460    12493  18734  13412  -1381    617   1379       C  
ATOM   8559  CE2 PHE B 460      -1.298   7.246  54.266  1.00118.22           C  
ANISOU 8559  CE2 PHE B 460    12617  18800  13500  -1248    530   1525       C  
ATOM   8560  CZ  PHE B 460      -2.096   6.349  53.587  1.00117.03           C  
ANISOU 8560  CZ  PHE B 460    12430  18588  13447  -1296    574   1398       C  
ATOM   8561  N   GLY B 461      -5.755  10.992  52.864  1.00106.44           N  
ANISOU 8561  N   GLY B 461    11151  17970  11321  -1363    689   1497       N  
ATOM   8562  CA  GLY B 461      -6.617  10.721  51.720  1.00106.41           C  
ANISOU 8562  CA  GLY B 461    11046  18097  11288  -1387    725   1360       C  
ATOM   8563  C   GLY B 461      -6.172  11.470  50.483  1.00109.07           C  
ANISOU 8563  C   GLY B 461    11341  18582  11519  -1337    734   1279       C  
ATOM   8564  O   GLY B 461      -5.859  10.852  49.461  1.00108.77           O  
ANISOU 8564  O   GLY B 461    11210  18579  11537  -1355    743   1132       O  
ATOM   8565  N   PHE B 462      -6.066  12.808  50.605  1.00104.48           N  
ANISOU 8565  N   PHE B 462    10838  18076  10785  -1279    736   1379       N  
ATOM   8566  CA  PHE B 462      -5.636  13.714  49.539  1.00103.74           C  
ANISOU 8566  CA  PHE B 462    10735  18114  10566  -1235    750   1348       C  
ATOM   8567  C   PHE B 462      -4.217  13.406  49.047  1.00106.78           C  
ANISOU 8567  C   PHE B 462    11086  18457  11030  -1250    737   1279       C  
ATOM   8568  O   PHE B 462      -3.957  13.557  47.855  1.00106.70           O  
ANISOU 8568  O   PHE B 462    11007  18578  10959  -1244    756   1186       O  
ATOM   8569  CB  PHE B 462      -5.716  15.174  50.002  1.00104.83           C  
ANISOU 8569  CB  PHE B 462    11004  18274  10554  -1178    758   1488       C  
ATOM   8570  CG  PHE B 462      -7.103  15.754  50.174  1.00106.27           C  
ANISOU 8570  CG  PHE B 462    11208  18554  10616  -1122    781   1543       C  
ATOM   8571  CD1 PHE B 462      -8.016  15.742  49.124  1.00109.93           C  
ANISOU 8571  CD1 PHE B 462    11572  19205  10993  -1090    801   1472       C  
ATOM   8572  CD2 PHE B 462      -7.464  16.392  51.352  1.00107.92           C  
ANISOU 8572  CD2 PHE B 462    11531  18694  10781  -1091    784   1661       C  
ATOM   8573  CE1 PHE B 462      -9.287  16.305  49.275  1.00111.08           C  
ANISOU 8573  CE1 PHE B 462    11719  19468  11019  -1017    819   1524       C  
ATOM   8574  CE2 PHE B 462      -8.734  16.954  51.502  1.00110.94           C  
ANISOU 8574  CE2 PHE B 462    11922  19182  11049  -1018    810   1704       C  
ATOM   8575  CZ  PHE B 462      -9.635  16.910  50.462  1.00109.63           C  
ANISOU 8575  CZ  PHE B 462    11646  19203  10804   -975    826   1640       C  
ATOM   8576  N   VAL B 463      -3.308  12.979  49.955  1.00102.87           N  
ANISOU 8576  N   VAL B 463    10627  17804  10656  -1264    704   1325       N  
ATOM   8577  CA  VAL B 463      -1.923  12.611  49.624  1.00102.84           C  
ANISOU 8577  CA  VAL B 463    10570  17767  10735  -1264    687   1262       C  
ATOM   8578  C   VAL B 463      -1.959  11.312  48.787  1.00107.73           C  
ANISOU 8578  C   VAL B 463    11066  18380  11486  -1272    699   1086       C  
ATOM   8579  O   VAL B 463      -1.246  11.218  47.782  1.00107.79           O  
ANISOU 8579  O   VAL B 463    10990  18478  11488  -1263    715    968       O  
ATOM   8580  CB  VAL B 463      -1.020  12.499  50.894  1.00106.37           C  
ANISOU 8580  CB  VAL B 463    11078  18072  11266  -1261    640   1369       C  
ATOM   8581  CG1 VAL B 463       0.349  11.898  50.575  1.00106.67           C  
ANISOU 8581  CG1 VAL B 463    11029  18090  11411  -1241    619   1291       C  
ATOM   8582  CG2 VAL B 463      -0.847  13.860  51.563  1.00105.40           C  
ANISOU 8582  CG2 VAL B 463    11074  17974  11000  -1270    636   1503       C  
ATOM   8583  N   LEU B 464      -2.839  10.354  49.166  1.00104.71           N  
ANISOU 8583  N   LEU B 464    10675  17902  11210  -1299    700   1061       N  
ATOM   8584  CA  LEU B 464      -3.028   9.086  48.454  1.00105.71           C  
ANISOU 8584  CA  LEU B 464    10706  17990  11470  -1326    718    884       C  
ATOM   8585  C   LEU B 464      -3.560   9.333  47.033  1.00111.08           C  
ANISOU 8585  C   LEU B 464    11290  18888  12026  -1345    757    736       C  
ATOM   8586  O   LEU B 464      -3.149   8.634  46.103  1.00111.88           O  
ANISOU 8586  O   LEU B 464    11298  19020  12192  -1350    775    557       O  
ATOM   8587  CB  LEU B 464      -3.969   8.152  49.240  1.00106.05           C  
ANISOU 8587  CB  LEU B 464    10781  17883  11632  -1382    718    911       C  
ATOM   8588  CG  LEU B 464      -4.105   6.708  48.736  1.00111.98           C  
ANISOU 8588  CG  LEU B 464    11467  18519  12561  -1428    739    735       C  
ATOM   8589  CD1 LEU B 464      -2.809   5.926  48.905  1.00113.01           C  
ANISOU 8589  CD1 LEU B 464    11599  18468  12872  -1362    717    703       C  
ATOM   8590  CD2 LEU B 464      -5.220   5.990  49.453  1.00114.69           C  
ANISOU 8590  CD2 LEU B 464    11849  18747  12982  -1518    751    778       C  
ATOM   8591  N   ILE B 465      -4.438  10.350  46.869  1.00107.21           N  
ANISOU 8591  N   ILE B 465    10824  18560  11352  -1342    768    811       N  
ATOM   8592  CA  ILE B 465      -5.012  10.754  45.579  1.00107.16           C  
ANISOU 8592  CA  ILE B 465    10730  18795  11189  -1343    796    711       C  
ATOM   8593  C   ILE B 465      -3.921  11.426  44.730  1.00111.90           C  
ANISOU 8593  C   ILE B 465    11310  19507  11698  -1308    806    688       C  
ATOM   8594  O   ILE B 465      -3.780  11.073  43.557  1.00112.19           O  
ANISOU 8594  O   ILE B 465    11238  19687  11702  -1322    828    527       O  
ATOM   8595  CB  ILE B 465      -6.267  11.667  45.759  1.00109.31           C  
ANISOU 8595  CB  ILE B 465    11038  19200  11293  -1320    801    824       C  
ATOM   8596  CG1 ILE B 465      -7.396  10.985  46.590  1.00109.57           C  
ANISOU 8596  CG1 ILE B 465    11068  19159  11403  -1372    800    840       C  
ATOM   8597  CG2 ILE B 465      -6.797  12.202  44.422  1.00110.30           C  
ANISOU 8597  CG2 ILE B 465    11076  19601  11234  -1296    821    753       C  
ATOM   8598  CD1 ILE B 465      -7.947   9.587  46.099  1.00116.16           C  
ANISOU 8598  CD1 ILE B 465    11789  19989  12358  -1473    816    646       C  
ATOM   8599  N   THR B 466      -3.145  12.372  45.327  1.00108.75           N  
ANISOU 8599  N   THR B 466    11013  19054  11252  -1276    792    841       N  
ATOM   8600  CA  THR B 466      -2.044  13.103  44.670  1.00109.11           C  
ANISOU 8600  CA  THR B 466    11052  19197  11206  -1267    806    846       C  
ATOM   8601  C   THR B 466      -1.048  12.100  44.090  1.00115.26           C  
ANISOU 8601  C   THR B 466    11714  19971  12110  -1278    813    673       C  
ATOM   8602  O   THR B 466      -0.675  12.231  42.925  1.00115.68           O  
ANISOU 8602  O   THR B 466    11680  20201  12072  -1286    844    568       O  
ATOM   8603  CB  THR B 466      -1.367  14.089  45.650  1.00116.28           C  
ANISOU 8603  CB  THR B 466    12094  20005  12084  -1262    789   1024       C  
ATOM   8604  OG1 THR B 466      -2.349  14.988  46.158  1.00119.04           O  
ANISOU 8604  OG1 THR B 466    12555  20351  12323  -1237    791   1162       O  
ATOM   8605  CG2 THR B 466      -0.253  14.903  45.003  1.00112.89           C  
ANISOU 8605  CG2 THR B 466    11663  19679  11552  -1283    811   1037       C  
ATOM   8606  N   PHE B 467      -0.672  11.074  44.887  1.00112.83           N  
ANISOU 8606  N   PHE B 467    11401  19464  12004  -1270    787    642       N  
ATOM   8607  CA  PHE B 467       0.244  10.009  44.481  1.00113.95           C  
ANISOU 8607  CA  PHE B 467    11441  19560  12296  -1250    792    477       C  
ATOM   8608  C   PHE B 467      -0.278   9.291  43.241  1.00119.94           C  
ANISOU 8608  C   PHE B 467    12084  20439  13048  -1273    831    257       C  
ATOM   8609  O   PHE B 467       0.464   9.146  42.272  1.00120.23           O  
ANISOU 8609  O   PHE B 467    12019  20605  13057  -1262    859    114       O  
ATOM   8610  CB  PHE B 467       0.454   9.010  45.630  1.00115.84           C  
ANISOU 8610  CB  PHE B 467    11720  19541  12753  -1221    754    512       C  
ATOM   8611  CG  PHE B 467       1.385   7.870  45.297  1.00118.59           C  
ANISOU 8611  CG  PHE B 467    11976  19807  13276  -1169    758    350       C  
ATOM   8612  CD1 PHE B 467       2.761   8.015  45.425  1.00121.60           C  
ANISOU 8612  CD1 PHE B 467    12312  20205  13684  -1110    741    365       C  
ATOM   8613  CD2 PHE B 467       0.887   6.649  44.857  1.00121.86           C  
ANISOU 8613  CD2 PHE B 467    12344  20128  13830  -1177    781    173       C  
ATOM   8614  CE1 PHE B 467       3.622   6.961  45.108  1.00123.85           C  
ANISOU 8614  CE1 PHE B 467    12501  20424  14131  -1033    747    209       C  
ATOM   8615  CE2 PHE B 467       1.749   5.600  44.533  1.00126.02           C  
ANISOU 8615  CE2 PHE B 467    12797  20559  14527  -1108    791     12       C  
ATOM   8616  CZ  PHE B 467       3.110   5.762  44.663  1.00124.20           C  
ANISOU 8616  CZ  PHE B 467    12516  20353  14321  -1023    774     34       C  
ATOM   8617  N   SER B 468      -1.560   8.866  43.275  1.00117.65           N  
ANISOU 8617  N   SER B 468    11803  20129  12771  -1314    834    224       N  
ATOM   8618  CA  SER B 468      -2.249   8.149  42.200  1.00119.35           C  
ANISOU 8618  CA  SER B 468    11910  20463  12974  -1361    867      8       C  
ATOM   8619  C   SER B 468      -2.261   8.943  40.887  1.00125.29           C  
ANISOU 8619  C   SER B 468    12580  21527  13498  -1365    895    -54       C  
ATOM   8620  O   SER B 468      -2.156   8.340  39.816  1.00126.74           O  
ANISOU 8620  O   SER B 468    12646  21837  13671  -1388    926   -271       O  
ATOM   8621  CB  SER B 468      -3.676   7.812  42.615  1.00122.71           C  
ANISOU 8621  CB  SER B 468    12362  20848  13415  -1423    862     27       C  
ATOM   8622  OG  SER B 468      -3.695   7.070  43.823  1.00131.56           O  
ANISOU 8622  OG  SER B 468    13565  21687  14735  -1432    841     99       O  
ATOM   8623  N   CYS B 469      -2.364  10.284  40.970  1.00121.30           N  
ANISOU 8623  N   CYS B 469    12142  21138  12809  -1342    888    137       N  
ATOM   8624  CA  CYS B 469      -2.367  11.160  39.799  1.00121.63           C  
ANISOU 8624  CA  CYS B 469    12132  21462  12619  -1339    913    131       C  
ATOM   8625  C   CYS B 469      -0.965  11.253  39.193  1.00126.54           C  
ANISOU 8625  C   CYS B 469    12697  22156  13226  -1334    940     63       C  
ATOM   8626  O   CYS B 469      -0.845  11.135  37.972  1.00127.13           O  
ANISOU 8626  O   CYS B 469    12659  22455  13192  -1352    974    -86       O  
ATOM   8627  CB  CYS B 469      -2.911  12.538  40.147  1.00120.85           C  
ANISOU 8627  CB  CYS B 469    12149  21419  12350  -1306    901    367       C  
ATOM   8628  SG  CYS B 469      -4.676  12.566  40.537  1.00124.54           S  
ANISOU 8628  SG  CYS B 469    12634  21916  12769  -1296    881    424       S  
ATOM   8629  N   HIS B 470       0.090  11.450  40.027  1.00123.03           N  
ANISOU 8629  N   HIS B 470    12317  21550  12879  -1314    925    163       N  
ATOM   8630  CA  HIS B 470       1.472  11.509  39.541  1.00123.94           C  
ANISOU 8630  CA  HIS B 470    12358  21746  12986  -1313    951     97       C  
ATOM   8631  C   HIS B 470       1.915  10.139  39.024  1.00130.44           C  
ANISOU 8631  C   HIS B 470    13044  22553  13962  -1292    971   -163       C  
ATOM   8632  O   HIS B 470       2.709  10.078  38.082  1.00131.24           O  
ANISOU 8632  O   HIS B 470    13032  22833  14000  -1295   1011   -296       O  
ATOM   8633  CB  HIS B 470       2.459  12.015  40.611  1.00123.84           C  
ANISOU 8633  CB  HIS B 470    12429  21587  13037  -1304    925    258       C  
ATOM   8634  CG  HIS B 470       2.248  13.435  41.048  1.00126.05           C  
ANISOU 8634  CG  HIS B 470    12851  21878  13164  -1333    918    489       C  
ATOM   8635  ND1 HIS B 470       2.790  14.514  40.356  1.00128.01           N  
ANISOU 8635  ND1 HIS B 470    13111  22302  13227  -1379    956    558       N  
ATOM   8636  CD2 HIS B 470       1.624  13.905  42.145  1.00126.57           C  
ANISOU 8636  CD2 HIS B 470    13058  21784  13248  -1323    884    657       C  
ATOM   8637  CE1 HIS B 470       2.419  15.594  41.023  1.00126.43           C  
ANISOU 8637  CE1 HIS B 470    13070  22021  12946  -1391    944    760       C  
ATOM   8638  NE2 HIS B 470       1.722  15.276  42.107  1.00125.90           N  
ANISOU 8638  NE2 HIS B 470    13080  21762  12994  -1353    901    818       N  
ATOM   8639  N   PHE B 471       1.380   9.048  39.622  1.00127.86           N  
ANISOU 8639  N   PHE B 471    12734  22012  13834  -1276    948   -237       N  
ATOM   8640  CA  PHE B 471       1.670   7.677  39.211  1.00129.62           C  
ANISOU 8640  CA  PHE B 471    12858  22160  14230  -1251    970   -488       C  
ATOM   8641  C   PHE B 471       1.078   7.403  37.829  1.00135.19           C  
ANISOU 8641  C   PHE B 471    13450  23103  14812  -1302   1015   -707       C  
ATOM   8642  O   PHE B 471       1.732   6.740  37.024  1.00136.44           O  
ANISOU 8642  O   PHE B 471    13493  23339  15009  -1282   1055   -932       O  
ATOM   8643  CB  PHE B 471       1.146   6.658  40.236  1.00131.61           C  
ANISOU 8643  CB  PHE B 471    13187  22102  14717  -1240    939   -482       C  
ATOM   8644  CG  PHE B 471       1.684   5.265  40.021  1.00135.32           C  
ANISOU 8644  CG  PHE B 471    13592  22418  15406  -1191    960   -709       C  
ATOM   8645  CD1 PHE B 471       0.992   4.346  39.241  1.00140.40           C  
ANISOU 8645  CD1 PHE B 471    14176  23071  16097  -1243    997   -952       C  
ATOM   8646  CD2 PHE B 471       2.892   4.876  40.586  1.00138.12           C  
ANISOU 8646  CD2 PHE B 471    13940  22623  15916  -1088    943   -689       C  
ATOM   8647  CE1 PHE B 471       1.503   3.064  39.024  1.00143.45           C  
ANISOU 8647  CE1 PHE B 471    14520  23289  16696  -1191   1025  -1177       C  
ATOM   8648  CE2 PHE B 471       3.399   3.592  40.373  1.00143.11           C  
ANISOU 8648  CE2 PHE B 471    14518  23098  16757  -1014    966   -899       C  
ATOM   8649  CZ  PHE B 471       2.702   2.694  39.594  1.00142.89           C  
ANISOU 8649  CZ  PHE B 471    14454  23050  16788  -1065   1010  -1144       C  
ATOM   8650  N   TYR B 472      -0.143   7.918  37.553  1.00131.43           N  
ANISOU 8650  N   TYR B 472    12997  22761  14179  -1359   1008   -647       N  
ATOM   8651  CA  TYR B 472      -0.823   7.767  36.263  1.00132.67           C  
ANISOU 8651  CA  TYR B 472    13039  23189  14179  -1412   1040   -833       C  
ATOM   8652  C   TYR B 472      -0.052   8.507  35.163  1.00138.22           C  
ANISOU 8652  C   TYR B 472    13657  24192  14669  -1406   1078   -859       C  
ATOM   8653  O   TYR B 472       0.130   7.955  34.076  1.00139.40           O  
ANISOU 8653  O   TYR B 472    13674  24525  14767  -1428   1119  -1101       O  
ATOM   8654  CB  TYR B 472      -2.282   8.271  36.339  1.00133.08           C  
ANISOU 8654  CB  TYR B 472    13129  23338  14097  -1455   1014   -722       C  
ATOM   8655  CG  TYR B 472      -2.988   8.329  35.001  1.00135.87           C  
ANISOU 8655  CG  TYR B 472    13355  24033  14238  -1503   1036   -875       C  
ATOM   8656  CD1 TYR B 472      -3.595   7.198  34.460  1.00139.45           C  
ANISOU 8656  CD1 TYR B 472    13707  24522  14756  -1576   1053  -1146       C  
ATOM   8657  CD2 TYR B 472      -3.058   9.517  34.277  1.00136.44           C  
ANISOU 8657  CD2 TYR B 472    13411  24392  14036  -1482   1039   -745       C  
ATOM   8658  CE1 TYR B 472      -4.240   7.246  33.225  1.00141.93           C  
ANISOU 8658  CE1 TYR B 472    13889  25183  14855  -1628   1067  -1297       C  
ATOM   8659  CE2 TYR B 472      -3.691   9.575  33.040  1.00138.79           C  
ANISOU 8659  CE2 TYR B 472    13584  25032  14119  -1518   1053   -872       C  
ATOM   8660  CZ  TYR B 472      -4.285   8.438  32.520  1.00148.54           C  
ANISOU 8660  CZ  TYR B 472    14701  26329  15409  -1592   1064  -1153       C  
ATOM   8661  OH  TYR B 472      -4.910   8.519  31.305  1.00151.85           O  
ANISOU 8661  OH  TYR B 472    14985  27118  15594  -1633   1071  -1282       O  
ATOM   8662  N   ASP B 473       0.380   9.756  35.445  1.00134.45           N  
ANISOU 8662  N   ASP B 473    13259  23765  14063  -1388   1068   -614       N  
ATOM   8663  CA  ASP B 473       1.136  10.600  34.517  1.00135.05           C  
ANISOU 8663  CA  ASP B 473    13279  24109  13927  -1401   1108   -586       C  
ATOM   8664  C   ASP B 473       2.502   9.992  34.212  1.00140.44           C  
ANISOU 8664  C   ASP B 473    13853  24801  14706  -1383   1147   -758       C  
ATOM   8665  O   ASP B 473       2.965  10.085  33.078  1.00141.41           O  
ANISOU 8665  O   ASP B 473    13858  25197  14677  -1407   1198   -884       O  
ATOM   8666  CB  ASP B 473       1.293  12.025  35.072  1.00135.62           C  
ANISOU 8666  CB  ASP B 473    13492  24160  13879  -1400   1092   -278       C  
ATOM   8667  CG  ASP B 473      -0.005  12.803  35.204  1.00146.01           C  
ANISOU 8667  CG  ASP B 473    14906  25514  15058  -1392   1063   -103       C  
ATOM   8668  OD1 ASP B 473      -0.870  12.679  34.304  1.00147.31           O  
ANISOU 8668  OD1 ASP B 473    14990  25898  15084  -1401   1069   -194       O  
ATOM   8669  OD2 ASP B 473      -0.141  13.567  36.186  1.00151.50           O  
ANISOU 8669  OD2 ASP B 473    15750  26040  15773  -1371   1036    120       O  
ATOM   8670  N   PHE B 474       3.126   9.350  35.216  1.00137.05           N  
ANISOU 8670  N   PHE B 474    13456  24094  14521  -1331   1124   -764       N  
ATOM   8671  CA  PHE B 474       4.419   8.683  35.094  1.00138.33           C  
ANISOU 8671  CA  PHE B 474    13513  24238  14809  -1280   1153   -922       C  
ATOM   8672  C   PHE B 474       4.294   7.404  34.248  1.00145.81           C  
ANISOU 8672  C   PHE B 474    14333  25228  15843  -1260   1192  -1255       C  
ATOM   8673  O   PHE B 474       5.137   7.165  33.381  1.00147.19           O  
ANISOU 8673  O   PHE B 474    14369  25592  15966  -1243   1247  -1438       O  
ATOM   8674  CB  PHE B 474       4.983   8.373  36.492  1.00139.15           C  
ANISOU 8674  CB  PHE B 474    13697  24030  15143  -1213   1103   -805       C  
ATOM   8675  CG  PHE B 474       6.111   7.374  36.550  1.00141.96           C  
ANISOU 8675  CG  PHE B 474    13947  24302  15689  -1119   1118   -983       C  
ATOM   8676  CD1 PHE B 474       7.390   7.723  36.139  1.00145.84           C  
ANISOU 8676  CD1 PHE B 474    14322  24983  16107  -1101   1153  -1016       C  
ATOM   8677  CD2 PHE B 474       5.900   6.090  37.033  1.00144.72           C  
ANISOU 8677  CD2 PHE B 474    14313  24381  16293  -1045   1101  -1109       C  
ATOM   8678  CE1 PHE B 474       8.432   6.795  36.178  1.00148.36           C  
ANISOU 8678  CE1 PHE B 474    14524  25246  16598   -988   1167  -1187       C  
ATOM   8679  CE2 PHE B 474       6.944   5.165  37.084  1.00149.18           C  
ANISOU 8679  CE2 PHE B 474    14786  24854  17040   -927   1115  -1267       C  
ATOM   8680  CZ  PHE B 474       8.206   5.527  36.663  1.00148.18           C  
ANISOU 8680  CZ  PHE B 474    14528  24939  16834   -888   1145  -1307       C  
ATOM   8681  N   PHE B 475       3.245   6.598  34.496  1.00143.54           N  
ANISOU 8681  N   PHE B 475    14090  24769  15680  -1273   1171  -1341       N  
ATOM   8682  CA  PHE B 475       2.974   5.335  33.804  1.00145.98           C  
ANISOU 8682  CA  PHE B 475    14308  25065  16093  -1276   1209  -1665       C  
ATOM   8683  C   PHE B 475       2.660   5.530  32.311  1.00152.77           C  
ANISOU 8683  C   PHE B 475    15036  26307  16704  -1345   1259  -1850       C  
ATOM   8684  O   PHE B 475       3.019   4.665  31.507  1.00154.62           O  
ANISOU 8684  O   PHE B 475    15152  26618  16979  -1333   1311  -2151       O  
ATOM   8685  CB  PHE B 475       1.804   4.602  34.491  1.00147.69           C  
ANISOU 8685  CB  PHE B 475    14622  25018  16475  -1315   1174  -1672       C  
ATOM   8686  CG  PHE B 475       1.407   3.265  33.908  1.00151.66           C  
ANISOU 8686  CG  PHE B 475    15062  25451  17110  -1346   1213  -2003       C  
ATOM   8687  CD1 PHE B 475       0.356   3.168  33.001  1.00155.93           C  
ANISOU 8687  CD1 PHE B 475    15536  26213  17497  -1457   1231  -2160       C  
ATOM   8688  CD2 PHE B 475       2.057   2.097  34.293  1.00155.34           C  
ANISOU 8688  CD2 PHE B 475    15543  25622  17857  -1265   1230  -2157       C  
ATOM   8689  CE1 PHE B 475      -0.016   1.931  32.464  1.00159.15           C  
ANISOU 8689  CE1 PHE B 475    15892  26553  18026  -1510   1270  -2488       C  
ATOM   8690  CE2 PHE B 475       1.683   0.859  33.758  1.00160.63           C  
ANISOU 8690  CE2 PHE B 475    16177  26193  18662  -1302   1273  -2474       C  
ATOM   8691  CZ  PHE B 475       0.648   0.784  32.848  1.00159.66           C  
ANISOU 8691  CZ  PHE B 475    15989  26293  18382  -1437   1295  -2647       C  
ATOM   8692  N   ASN B 476       1.982   6.633  31.942  1.00149.29           N  
ANISOU 8692  N   ASN B 476    14615  26105  16004  -1408   1244  -1675       N  
ATOM   8693  CA  ASN B 476       1.567   6.862  30.557  1.00150.75           C  
ANISOU 8693  CA  ASN B 476    14678  26675  15925  -1471   1281  -1817       C  
ATOM   8694  C   ASN B 476       2.379   7.945  29.802  1.00155.61           C  
ANISOU 8694  C   ASN B 476    15236  27605  16283  -1478   1318  -1708       C  
ATOM   8695  O   ASN B 476       2.089   8.171  28.624  1.00156.55           O  
ANISOU 8695  O   ASN B 476    15252  28069  16161  -1527   1349  -1808       O  
ATOM   8696  CB  ASN B 476       0.078   7.203  30.508  1.00150.44           C  
ANISOU 8696  CB  ASN B 476    14680  26722  15757  -1532   1239  -1726       C  
ATOM   8697  CG  ASN B 476      -0.818   6.057  30.903  1.00173.75           C  
ANISOU 8697  CG  ASN B 476    17646  29462  18911  -1572   1222  -1896       C  
ATOM   8698  OD1 ASN B 476      -1.127   5.173  30.100  1.00170.30           O  
ANISOU 8698  OD1 ASN B 476    17101  29133  18474  -1628   1254  -2198       O  
ATOM   8699  ND2 ASN B 476      -1.254   6.046  32.152  1.00164.04           N  
ANISOU 8699  ND2 ASN B 476    16551  27928  17848  -1558   1175  -1712       N  
ATOM   8700  N   GLN B 477       3.401   8.572  30.439  1.00151.52           N  
ANISOU 8700  N   GLN B 477    14776  26986  15807  -1440   1317  -1517       N  
ATOM   8701  CA  GLN B 477       4.224   9.606  29.789  1.00151.82           C  
ANISOU 8701  CA  GLN B 477    14770  27302  15612  -1473   1359  -1403       C  
ATOM   8702  C   GLN B 477       5.002   9.037  28.593  1.00158.21           C  
ANISOU 8702  C   GLN B 477    15385  28391  16338  -1480   1436  -1695       C  
ATOM   8703  O   GLN B 477       5.148   9.728  27.582  1.00158.78           O  
ANISOU 8703  O   GLN B 477    15387  28807  16134  -1540   1480  -1669       O  
ATOM   8704  CB  GLN B 477       5.188  10.280  30.783  1.00151.92           C  
ANISOU 8704  CB  GLN B 477    14874  27139  15710  -1454   1344  -1172       C  
ATOM   8705  CG  GLN B 477       5.884  11.540  30.247  1.00171.40           C  
ANISOU 8705  CG  GLN B 477    17338  29860  17927  -1524   1386   -996       C  
ATOM   8706  CD  GLN B 477       4.964  12.715  30.045  1.00195.17           C  
ANISOU 8706  CD  GLN B 477    20473  32969  20713  -1572   1368   -744       C  
ATOM   8707  OE1 GLN B 477       4.508  12.988  28.931  1.00194.50           O  
ANISOU 8707  OE1 GLN B 477    20326  33181  20394  -1608   1397   -779       O  
ATOM   8708  NE2 GLN B 477       4.698  13.457  31.110  1.00185.20           N  
ANISOU 8708  NE2 GLN B 477    19389  31471  19508  -1566   1320   -482       N  
ATOM   8709  N   ALA B 478       5.473   7.778  28.711  1.00155.93           N  
ANISOU 8709  N   ALA B 478    15015  27950  16281  -1415   1456  -1968       N  
ATOM   8710  CA  ALA B 478       6.215   7.038  27.687  1.00158.19           C  
ANISOU 8710  CA  ALA B 478    15115  28453  16538  -1395   1533  -2295       C  
ATOM   8711  C   ALA B 478       5.473   7.024  26.339  1.00163.50           C  
ANISOU 8711  C   ALA B 478    15686  29487  16951  -1476   1569  -2468       C  
ATOM   8712  O   ALA B 478       6.083   7.319  25.309  1.00164.55           O  
ANISOU 8712  O   ALA B 478    15684  29973  16865  -1509   1635  -2560       O  
ATOM   8713  CB  ALA B 478       6.468   5.615  28.160  1.00159.90           C  
ANISOU 8713  CB  ALA B 478    15309  28365  17079  -1296   1535  -2550       C  
ATOM   8714  N   GLU B 479       4.155   6.731  26.356  1.00159.66           N  
ANISOU 8714  N   GLU B 479    15254  28941  16469  -1515   1524  -2499       N  
ATOM   8715  CA  GLU B 479       3.334   6.712  25.146  1.00160.94           C  
ANISOU 8715  CA  GLU B 479    15314  29459  16375  -1595   1543  -2655       C  
ATOM   8716  C   GLU B 479       2.992   8.129  24.684  1.00163.56           C  
ANISOU 8716  C   GLU B 479    15678  30094  16376  -1646   1528  -2356       C  
ATOM   8717  O   GLU B 479       2.936   8.359  23.475  1.00164.72           O  
ANISOU 8717  O   GLU B 479    15702  30642  16243  -1698   1568  -2454       O  
ATOM   8718  CB  GLU B 479       2.050   5.891  25.346  1.00162.58           C  
ANISOU 8718  CB  GLU B 479    15555  29517  16702  -1631   1500  -2799       C  
ATOM   8719  CG  GLU B 479       2.025   4.583  24.566  1.00177.31           C  
ANISOU 8719  CG  GLU B 479    17287  31444  18637  -1657   1554  -3244       C  
ATOM   8720  CD  GLU B 479       1.933   4.684  23.052  1.00201.25           C  
ANISOU 8720  CD  GLU B 479    20144  34975  21346  -1728   1605  -3454       C  
ATOM   8721  OE1 GLU B 479       2.855   4.183  22.367  1.00193.24           O  
ANISOU 8721  OE1 GLU B 479    19004  34096  20322  -1703   1682  -3718       O  
ATOM   8722  OE2 GLU B 479       0.934   5.249  22.550  1.00199.59           O  
ANISOU 8722  OE2 GLU B 479    19914  35034  20885  -1801   1568  -3360       O  
ATOM   8723  N   TRP B 480       2.780   9.079  25.630  1.00157.73           N  
ANISOU 8723  N   TRP B 480    15106  29163  15660  -1627   1473  -1994       N  
ATOM   8724  CA  TRP B 480       2.450  10.474  25.312  1.00157.02           C  
ANISOU 8724  CA  TRP B 480    15085  29292  15285  -1658   1459  -1681       C  
ATOM   8725  C   TRP B 480       3.581  11.158  24.539  1.00161.36           C  
ANISOU 8725  C   TRP B 480    15562  30120  15625  -1696   1531  -1629       C  
ATOM   8726  O   TRP B 480       3.299  11.973  23.658  1.00161.69           O  
ANISOU 8726  O   TRP B 480    15585  30489  15361  -1740   1546  -1506       O  
ATOM   8727  CB  TRP B 480       2.107  11.280  26.576  1.00153.57           C  
ANISOU 8727  CB  TRP B 480    14853  28543  14954  -1622   1396  -1336       C  
ATOM   8728  CG  TRP B 480       0.881  10.821  27.318  1.00153.70           C  
ANISOU 8728  CG  TRP B 480    14944  28335  15121  -1596   1328  -1333       C  
ATOM   8729  CD1 TRP B 480      -0.194  10.153  26.805  1.00157.70           C  
ANISOU 8729  CD1 TRP B 480    15365  28972  15582  -1622   1309  -1523       C  
ATOM   8730  CD2 TRP B 480       0.586  11.050  28.702  1.00151.49           C  
ANISOU 8730  CD2 TRP B 480    14831  27691  15039  -1554   1273  -1123       C  
ATOM   8731  NE1 TRP B 480      -1.120   9.913  27.794  1.00155.90           N  
ANISOU 8731  NE1 TRP B 480    15235  28477  15524  -1604   1249  -1447       N  
ATOM   8732  CE2 TRP B 480      -0.669  10.459  28.968  1.00155.39           C  
ANISOU 8732  CE2 TRP B 480    15327  28107  15606  -1557   1228  -1198       C  
ATOM   8733  CE3 TRP B 480       1.266  11.696  29.750  1.00151.10           C  
ANISOU 8733  CE3 TRP B 480    14921  27388  15101  -1526   1260   -886       C  
ATOM   8734  CZ2 TRP B 480      -1.253  10.484  30.240  1.00153.01           C  
ANISOU 8734  CZ2 TRP B 480    15163  27489  15485  -1526   1175  -1040       C  
ATOM   8735  CZ3 TRP B 480       0.688  11.718  31.008  1.00150.93           C  
ANISOU 8735  CZ3 TRP B 480    15039  27053  15256  -1490   1203   -738       C  
ATOM   8736  CH2 TRP B 480      -0.556  11.117  31.245  1.00151.50           C  
ANISOU 8736  CH2 TRP B 480    15111  27057  15396  -1487   1163   -811       C  
ATOM   8737  N   GLU B 481       4.851  10.811  24.853  1.00157.80           N  
ANISOU 8737  N   GLU B 481    15065  29559  15333  -1679   1575  -1721       N  
ATOM   8738  CA  GLU B 481       6.035  11.338  24.169  1.00158.77           C  
ANISOU 8738  CA  GLU B 481    15093  29952  15280  -1728   1654  -1706       C  
ATOM   8739  C   GLU B 481       6.162  10.703  22.777  1.00165.28           C  
ANISOU 8739  C   GLU B 481    15708  31169  15924  -1758   1724  -2029       C  
ATOM   8740  O   GLU B 481       6.517  11.399  21.822  1.00166.23           O  
ANISOU 8740  O   GLU B 481    15757  31654  15748  -1830   1780  -1964       O  
ATOM   8741  CB  GLU B 481       7.314  11.115  24.996  1.00159.62           C  
ANISOU 8741  CB  GLU B 481    15191  29839  15617  -1691   1674  -1716       C  
ATOM   8742  CG  GLU B 481       7.447  12.063  26.179  1.00168.38           C  
ANISOU 8742  CG  GLU B 481    16492  30673  16811  -1700   1624  -1366       C  
ATOM   8743  CD  GLU B 481       8.850  12.258  26.727  1.00184.93           C  
ANISOU 8743  CD  GLU B 481    18555  32701  19007  -1709   1655  -1318       C  
ATOM   8744  OE1 GLU B 481       9.466  11.261  27.169  1.00177.21           O  
ANISOU 8744  OE1 GLU B 481    17489  31575  18269  -1623   1654  -1521       O  
ATOM   8745  OE2 GLU B 481       9.314  13.420  26.766  1.00174.76           O  
ANISOU 8745  OE2 GLU B 481    17338  31496  17567  -1800   1676  -1067       O  
ATOM   8746  N   ARG B 482       5.837   9.392  22.660  1.00162.61           N  
ANISOU 8746  N   ARG B 482    15279  30752  15755  -1712   1723  -2376       N  
ATOM   8747  CA  ARG B 482       5.855   8.633  21.401  1.00164.89           C  
ANISOU 8747  CA  ARG B 482    15373  31380  15900  -1738   1787  -2739       C  
ATOM   8748  C   ARG B 482       4.782   9.146  20.443  1.00168.44           C  
ANISOU 8748  C   ARG B 482    15797  32184  16018  -1813   1768  -2683       C  
ATOM   8749  O   ARG B 482       5.040   9.251  19.244  1.00169.97           O  
ANISOU 8749  O   ARG B 482    15844  32803  15934  -1868   1831  -2811       O  
ATOM   8750  CB  ARG B 482       5.652   7.131  21.663  1.00166.89           C  
ANISOU 8750  CB  ARG B 482    15580  31383  16448  -1677   1784  -3106       C  
ATOM   8751  CG  ARG B 482       6.955   6.355  21.771  1.00181.16           C  
ANISOU 8751  CG  ARG B 482    17285  33095  18455  -1594   1852  -3342       C  
ATOM   8752  CD  ARG B 482       6.774   5.046  22.517  1.00195.92           C  
ANISOU 8752  CD  ARG B 482    19198  34543  20698  -1503   1828  -3571       C  
ATOM   8753  NE  ARG B 482       8.054   4.374  22.749  1.00211.27           N  
ANISOU 8753  NE  ARG B 482    21059  36365  22851  -1386   1883  -3751       N  
ATOM   8754  CZ  ARG B 482       8.834   4.581  23.807  1.00224.16           C  
ANISOU 8754  CZ  ARG B 482    23158  37001  25010  -1174   1821  -3247       C  
ATOM   8755  NH1 ARG B 482       8.473   5.445  24.749  1.00212.38           N  
ANISOU 8755  NH1 ARG B 482    21433  36058  23205  -1334   1778  -3176       N  
ATOM   8756  NH2 ARG B 482       9.982   3.928  23.930  1.00215.77           N  
ANISOU 8756  NH2 ARG B 482    21592  36604  23785  -1179   1904  -3734       N  
ATOM   8757  N   SER B 483       3.589   9.483  20.979  1.00162.98           N  
ANISOU 8757  N   SER B 483    15241  31340  15345  -1808   1681  -2484       N  
ATOM   8758  CA  SER B 483       2.457  10.022  20.223  1.00163.23           C  
ANISOU 8758  CA  SER B 483    15257  31688  15076  -1852   1644  -2387       C  
ATOM   8759  C   SER B 483       2.756  11.422  19.696  1.00166.74           C  
ANISOU 8759  C   SER B 483    15743  32411  15201  -1883   1664  -2053       C  
ATOM   8760  O   SER B 483       2.215  11.803  18.658  1.00167.79           O  
ANISOU 8760  O   SER B 483    15799  32943  15011  -1920   1666  -2033       O  
ATOM   8761  CB  SER B 483       1.202  10.050  21.085  1.00165.39           C  
ANISOU 8761  CB  SER B 483    15662  31698  15479  -1820   1548  -2243       C  
ATOM   8762  OG  SER B 483       0.882   8.751  21.553  1.00175.61           O  
ANISOU 8762  OG  SER B 483    16930  32733  17062  -1815   1535  -2540       O  
ATOM   8763  N   PHE B 484       3.589  12.192  20.419  1.00161.85           N  
ANISOU 8763  N   PHE B 484    15249  31579  14666  -1873   1678  -1786       N  
ATOM   8764  CA  PHE B 484       4.019  13.529  20.012  1.00161.97           C  
ANISOU 8764  CA  PHE B 484    15331  31797  14413  -1922   1711  -1461       C  
ATOM   8765  C   PHE B 484       5.128  13.399  18.980  1.00169.27           C  
ANISOU 8765  C   PHE B 484    16077  33079  15157  -1995   1816  -1636       C  
ATOM   8766  O   PHE B 484       5.160  14.173  18.026  1.00170.82           O  
ANISOU 8766  O   PHE B 484    16244  33643  15018  -2058   1854  -1495       O  
ATOM   8767  CB  PHE B 484       4.496  14.347  21.217  1.00161.17           C  
ANISOU 8767  CB  PHE B 484    15431  31322  14484  -1909   1692  -1143       C  
ATOM   8768  CG  PHE B 484       4.944  15.753  20.892  1.00162.56           C  
ANISOU 8768  CG  PHE B 484    15709  31645  14412  -1977   1731   -797       C  
ATOM   8769  CD1 PHE B 484       4.017  16.757  20.642  1.00165.22           C  
ANISOU 8769  CD1 PHE B 484    16177  32068  14529  -1959   1690   -498       C  
ATOM   8770  CD2 PHE B 484       6.293  16.081  20.875  1.00164.77           C  
ANISOU 8770  CD2 PHE B 484    15960  31962  14684  -2059   1810   -764       C  
ATOM   8771  CE1 PHE B 484       4.434  18.060  20.364  1.00166.57           C  
ANISOU 8771  CE1 PHE B 484    16471  32331  14485  -2024   1732   -165       C  
ATOM   8772  CE2 PHE B 484       6.708  17.385  20.596  1.00168.02           C  
ANISOU 8772  CE2 PHE B 484    16482  32486  14873  -2150   1854   -440       C  
ATOM   8773  CZ  PHE B 484       5.777  18.365  20.342  1.00166.12           C  
ANISOU 8773  CZ  PHE B 484    16394  32298  14425  -2133   1817   -139       C  
ATOM   8774  N   ARG B 485       6.030  12.412  19.168  1.00166.65           N  
ANISOU 8774  N   ARG B 485    15627  32650  15044  -1978   1865  -1941       N  
ATOM   8775  CA  ARG B 485       7.134  12.113  18.252  1.00168.92           C  
ANISOU 8775  CA  ARG B 485    15716  33269  15195  -2029   1971  -2167       C  
ATOM   8776  C   ARG B 485       6.578  11.768  16.857  1.00175.35           C  
ANISOU 8776  C   ARG B 485    16366  34551  15708  -2070   2002  -2394       C  
ATOM   8777  O   ARG B 485       7.015  12.370  15.869  1.00177.70           O  
ANISOU 8777  O   ARG B 485    16577  35260  15682  -2151   2070  -2329       O  
ATOM   8778  CB  ARG B 485       8.006  10.970  18.818  1.00169.31           C  
ANISOU 8778  CB  ARG B 485    15674  33079  15579  -1956   2002  -2477       C  
ATOM   8779  CG  ARG B 485       9.163  10.508  17.917  1.00181.19           C  
ANISOU 8779  CG  ARG B 485    16949  34920  16976  -1979   2117  -2766       C  
ATOM   8780  CD  ARG B 485      10.383  11.406  17.985  1.00189.77           C  
ANISOU 8780  CD  ARG B 485    18022  36117  17965  -2048   2182  -2549       C  
ATOM   8781  NE  ARG B 485      11.422  10.977  17.048  1.00202.04           N  
ANISOU 8781  NE  ARG B 485    19701  37325  19740  -1934   2276  -2654       N  
ATOM   8782  CZ  ARG B 485      12.262  11.798  16.425  1.00212.43           C  
ANISOU 8782  CZ  ARG B 485    21715  37444  21555  -1744   2318  -2176       C  
ATOM   8783  NH1 ARG B 485      12.197  13.109  16.635  1.00201.91           N  
ANISOU 8783  NH1 ARG B 485    19863  37444  19410  -2110   2344  -2093       N  
ATOM   8784  NH2 ARG B 485      13.171  11.320  15.588  1.00203.86           N  
ANISOU 8784  NH2 ARG B 485    20080  37340  20037  -1885   2443  -2581       N  
ATOM   8785  N   ASP B 486       5.596  10.850  16.795  1.00172.16           N  
ANISOU 8785  N   ASP B 486    15923  34094  15396  -2030   1950  -2644       N  
ATOM   8786  CA  ASP B 486       4.927  10.446  15.561  1.00174.98           C  
ANISOU 8786  CA  ASP B 486    16124  34880  15481  -2075   1964  -2885       C  
ATOM   8787  C   ASP B 486       4.075  11.577  14.952  1.00179.33           C  
ANISOU 8787  C   ASP B 486    16731  35742  15665  -2116   1919  -2557       C  
ATOM   8788  O   ASP B 486       3.922  11.611  13.727  1.00181.19           O  
ANISOU 8788  O   ASP B 486    16818  36460  15563  -2174   1955  -2670       O  
ATOM   8789  CB  ASP B 486       4.054   9.208  15.812  1.00177.32           C  
ANISOU 8789  CB  ASP B 486    16388  34984  16001  -2040   1914  -3216       C  
ATOM   8790  CG  ASP B 486       4.829   7.983  16.265  1.00186.09           C  
ANISOU 8790  CG  ASP B 486    17441  35805  17459  -1985   1963  -3571       C  
ATOM   8791  OD1 ASP B 486       5.952   7.774  15.768  1.00186.21           O  
ANISOU 8791  OD1 ASP B 486    17326  35994  17431  -1984   2057  -3744       O  
ATOM   8792  OD2 ASP B 486       4.308   7.227  17.113  1.00190.74           O  
ANISOU 8792  OD2 ASP B 486    18113  35998  18362  -1938   1909  -3672       O  
ATOM   8793  N   TYR B 487       3.548  12.498  15.787  1.00175.58           N  
ANISOU 8793  N   TYR B 487    16465  35003  15245  -2077   1844  -2156       N  
ATOM   8794  CA  TYR B 487       2.744  13.645  15.345  1.00176.94           C  
ANISOU 8794  CA  TYR B 487    16722  35405  15100  -2079   1797  -1801       C  
ATOM   8795  C   TYR B 487       3.624  14.672  14.629  1.00182.58           C  
ANISOU 8795  C   TYR B 487    17440  36414  15519  -2153   1877  -1564       C  
ATOM   8796  O   TYR B 487       3.235  15.170  13.575  1.00184.19           O  
ANISOU 8796  O   TYR B 487    17582  37047  15353  -2185   1884  -1468       O  
ATOM   8797  CB  TYR B 487       2.003  14.290  16.534  1.00176.36           C  
ANISOU 8797  CB  TYR B 487    16880  34920  15208  -1999   1704  -1465       C  
ATOM   8798  CG  TYR B 487       1.284  15.583  16.207  1.00179.63           C  
ANISOU 8798  CG  TYR B 487    17414  35507  15329  -1969   1660  -1056       C  
ATOM   8799  CD1 TYR B 487       0.103  15.580  15.467  1.00183.11           C  
ANISOU 8799  CD1 TYR B 487    17774  36279  15522  -1936   1600  -1069       C  
ATOM   8800  CD2 TYR B 487       1.763  16.806  16.666  1.00179.88           C  
ANISOU 8800  CD2 TYR B 487    17646  35361  15339  -1968   1677   -657       C  
ATOM   8801  CE1 TYR B 487      -0.570  16.765  15.173  1.00185.15           C  
ANISOU 8801  CE1 TYR B 487    18142  36693  15512  -1877   1555   -680       C  
ATOM   8802  CE2 TYR B 487       1.098  17.997  16.380  1.00181.48           C  
ANISOU 8802  CE2 TYR B 487    17982  35685  15288  -1922   1640   -274       C  
ATOM   8803  CZ  TYR B 487      -0.069  17.973  15.630  1.00190.85           C  
ANISOU 8803  CZ  TYR B 487    19082  37204  16227  -1862   1577   -279       C  
ATOM   8804  OH  TYR B 487      -0.733  19.144  15.345  1.00192.93           O  
ANISOU 8804  OH  TYR B 487    19476  37589  16241  -1786   1537    111       O  
ATOM   8805  N   VAL B 488       4.803  14.985  15.207  1.00178.01           N  
ANISOU 8805  N   VAL B 488    16927  35615  15095  -2186   1938  -1465       N  
ATOM   8806  CA  VAL B 488       5.776  15.940  14.668  1.00178.90           C  
ANISOU 8806  CA  VAL B 488    17050  35956  14967  -2286   2027  -1242       C  
ATOM   8807  C   VAL B 488       6.321  15.407  13.323  1.00187.66           C  
ANISOU 8807  C   VAL B 488    17913  37572  15819  -2360   2121  -1543       C  
ATOM   8808  O   VAL B 488       6.285  16.139  12.329  1.00188.48           O  
ANISOU 8808  O   VAL B 488    18223  37606  15786  -2339   2152  -1319       O  
ATOM   8809  CB  VAL B 488       6.898  16.248  15.706  1.00180.08           C  
ANISOU 8809  CB  VAL B 488    17304  35738  15380  -2316   2064  -1120       C  
ATOM   8810  CG1 VAL B 488       8.084  16.972  15.068  1.00180.46           C  
ANISOU 8810  CG1 VAL B 488    17302  36067  15197  -2453   2178   -994       C  
ATOM   8811  CG2 VAL B 488       6.353  17.058  16.881  1.00177.78           C  
ANISOU 8811  CG2 VAL B 488    17284  35004  15261  -2262   1981   -761       C  
ATOM   8812  N   LEU B 489       6.763  14.125  13.285  1.00185.02           N  
ANISOU 8812  N   LEU B 489    17389  37248  15663  -2341   2159  -1997       N  
ATOM   8813  CA  LEU B 489       7.283  13.462  12.079  1.00185.90           C  
ANISOU 8813  CA  LEU B 489    17441  37440  15755  -2323   2245  -2286       C  
ATOM   8814  C   LEU B 489       6.225  13.384  10.978  1.00187.42           C  
ANISOU 8814  C   LEU B 489    17839  37461  15912  -2229   2200  -2263       C  
ATOM   8815  O   LEU B 489       6.572  13.418   9.797  1.00187.20           O  
ANISOU 8815  O   LEU B 489    17882  37457  15788  -2217   2267  -2292       O  
ATOM   8816  CB  LEU B 489       7.808  12.050  12.394  1.00186.31           C  
ANISOU 8816  CB  LEU B 489    17344  37331  16115  -2264   2278  -2750       C  
ATOM   8817  CG  LEU B 489       9.148  11.968  13.132  1.00189.81           C  
ANISOU 8817  CG  LEU B 489    17881  37327  16910  -2211   2335  -2718       C  
ATOM   8818  CD1 LEU B 489       9.336  10.607  13.770  1.00190.15           C  
ANISOU 8818  CD1 LEU B 489    17777  37215  17256  -2130   2329  -3128       C  
ATOM   8819  CD2 LEU B 489      10.312  12.278  12.205  1.00192.26           C  
ANISOU 8819  CD2 LEU B 489    18387  37349  17316  -2164   2446  -2613       C  
ATOM   8820  N   CYS B 490       4.939  13.300  11.370  1.00185.10           N  
ANISOU 8820  N   CYS B 490    17406  37467  15456  -2250   2095  -2282       N  
ATOM   8821  CA  CYS B 490       3.799  13.261  10.457  1.00185.35           C  
ANISOU 8821  CA  CYS B 490    17554  37487  15384  -2186   2032  -2265       C  
ATOM   8822  C   CYS B 490       3.662  14.607   9.727  1.00187.00           C  
ANISOU 8822  C   CYS B 490    18055  37582  15413  -2144   2032  -1803       C  
ATOM   8823  O   CYS B 490       3.357  14.622   8.534  1.00186.80           O  
ANISOU 8823  O   CYS B 490    18125  37588  15261  -2108   2041  -1816       O  
ATOM   8824  CB  CYS B 490       2.523  12.906  11.215  1.00185.46           C  
ANISOU 8824  CB  CYS B 490    17516  37485  15464  -2157   1915  -2315       C  
ATOM   8825  SG  CYS B 490       1.070  12.667  10.162  1.00188.37           S  
ANISOU 8825  SG  CYS B 490    18159  37506  15907  -2027   1822  -2300       S  
ATOM   8826  N   GLN B 491       3.903  15.725  10.453  1.00184.00           N  
ANISOU 8826  N   GLN B 491    17548  37623  14742  -2253   2033  -1469       N  
ATOM   8827  CA  GLN B 491       3.823  17.103   9.956  1.00203.66           C  
ANISOU 8827  CA  GLN B 491    21432  37739  18210  -1826   2018   -817       C  
ATOM   8828  C   GLN B 491       5.061  17.456   9.130  1.00227.65           C  
ANISOU 8828  C   GLN B 491    26000  37806  22693  -1337   2120   -543       C  
ATOM   8829  O   GLN B 491       5.050  17.345   7.904  1.00203.67           O  
ANISOU 8829  O   GLN B 491    21599  37728  18060  -1846   2186   -835       O  
ATOM   8830  CB  GLN B 491       3.675  18.094  11.128  1.00204.16           C  
ANISOU 8830  CB  GLN B 491    21560  37762  18251  -1846   1977   -492       C  
ATOM   8831  CG  GLN B 491       2.395  17.950  11.958  1.00213.37           C  
ANISOU 8831  CG  GLN B 491    23238  37804  20031  -1590   1844   -406       C  
ATOM   8832  CD  GLN B 491       1.212  18.682  11.378  1.00226.11           C  
ANISOU 8832  CD  GLN B 491    25797  37860  22253  -1253   1768   -143       C  
ATOM   8833  OE1 GLN B 491       0.291  18.076  10.824  1.00223.67           O  
ANISOU 8833  OE1 GLN B 491    25325  37860  21798  -1246   1701   -289       O  
ATOM   8834  NE2 GLN B 491       1.181  19.998  11.540  1.00220.48           N  
ANISOU 8834  NE2 GLN B 491    24907  37854  21013  -1362   1780    166       N  
ATOM   8835  N   CYS B 507      -2.468  16.105  10.744  1.00184.44           N  
ANISOU 8835  N   CYS B 507    17763  37763  14551  -1852   1505  -1073       N  
ATOM   8836  CA  CYS B 507      -2.123  14.915  11.519  1.00183.80           C  
ANISOU 8836  CA  CYS B 507    17454  37697  14683  -1950   1530  -1475       C  
ATOM   8837  C   CYS B 507      -2.773  14.966  12.893  1.00182.53           C  
ANISOU 8837  C   CYS B 507    17272  37411  14669  -1916   1455  -1373       C  
ATOM   8838  O   CYS B 507      -3.225  16.030  13.319  1.00179.48           O  
ANISOU 8838  O   CYS B 507    17060  36902  14234  -1816   1403   -961       O  
ATOM   8839  CB  CYS B 507      -0.610  14.756  11.627  1.00184.59           C  
ANISOU 8839  CB  CYS B 507    17559  37663  14915  -2027   1648  -1574       C  
ATOM   8840  SG  CYS B 507       0.224  14.512  10.037  1.00188.20           S  
ANISOU 8840  SG  CYS B 507    18322  37645  15539  -1969   1743  -1677       S  
ATOM   8841  N   GLU B 508      -2.830  13.812  13.582  1.00177.31           N  
ANISOU 8841  N   GLU B 508    16570  36445  14355  -1945   1450  -1712       N  
ATOM   8842  CA  GLU B 508      -3.456  13.693  14.903  1.00174.19           C  
ANISOU 8842  CA  GLU B 508    16319  35570  14296  -1874   1381  -1622       C  
ATOM   8843  C   GLU B 508      -2.493  13.118  15.947  1.00175.23           C  
ANISOU 8843  C   GLU B 508    16546  35192  14843  -1895   1433  -1745       C  
ATOM   8844  O   GLU B 508      -1.471  12.530  15.588  1.00176.35           O  
ANISOU 8844  O   GLU B 508    16596  35373  15034  -1962   1516  -1998       O  
ATOM   8845  CB  GLU B 508      -4.722  12.815  14.831  1.00176.26           C  
ANISOU 8845  CB  GLU B 508    16444  35948  14577  -1892   1308  -1888       C  
ATOM   8846  CG  GLU B 508      -5.734  13.227  13.770  1.00188.39           C  
ANISOU 8846  CG  GLU B 508    18028  37669  15884  -1818   1241  -1771       C  
ATOM   8847  CD  GLU B 508      -7.157  12.768  14.006  1.00202.74           C  
ANISOU 8847  CD  GLU B 508    20682  37704  18648  -1541   1121  -1625       C  
ATOM   8848  OE1 GLU B 508      -7.657  12.979  15.134  1.00197.45           O  
ANISOU 8848  OE1 GLU B 508    19624  37711  17686  -1620   1086  -1597       O  
ATOM   8849  OE2 GLU B 508      -7.801  12.281  13.048  1.00195.20           O  
ANISOU 8849  OE2 GLU B 508    19295  37652  17222  -1671   1098  -1909       O  
ATOM   8850  N   ILE B 509      -2.833  13.290  17.241  1.00165.95           N  
ANISOU 8850  N   ILE B 509    15544  33557  13953  -1826   1381  -1565       N  
ATOM   8851  CA  ILE B 509      -2.073  12.794  18.396  1.00162.19           C  
ANISOU 8851  CA  ILE B 509    15174  32576  13877  -1825   1408  -1633       C  
ATOM   8852  C   ILE B 509      -2.817  11.575  18.965  1.00165.01           C  
ANISOU 8852  C   ILE B 509    15481  32716  14501  -1843   1367  -1928       C  
ATOM   8853  O   ILE B 509      -3.987  11.708  19.337  1.00165.16           O  
ANISOU 8853  O   ILE B 509    15532  32704  14516  -1807   1290  -1824       O  
ATOM   8854  CB  ILE B 509      -1.866  13.905  19.476  1.00162.33           C  
ANISOU 8854  CB  ILE B 509    15434  32234  14011  -1749   1385  -1209       C  
ATOM   8855  CG1 ILE B 509      -1.320  15.219  18.880  1.00163.31           C  
ANISOU 8855  CG1 ILE B 509    15632  32572  13846  -1747   1423   -882       C  
ATOM   8856  CG2 ILE B 509      -0.986  13.417  20.628  1.00160.93           C  
ANISOU 8856  CG2 ILE B 509    15348  31584  14215  -1752   1411  -1275       C  
ATOM   8857  CD1 ILE B 509      -2.319  16.350  18.878  1.00168.69           C  
ANISOU 8857  CD1 ILE B 509    16436  33332  14328  -1652   1357   -513       C  
ATOM   8858  N   LYS B 510      -2.147  10.398  19.022  1.00160.48           N  
ANISOU 8858  N   LYS B 510    14828  31995  14154  -1897   1421  -2290       N  
ATOM   8859  CA  LYS B 510      -2.709   9.130  19.529  1.00159.32           C  
ANISOU 8859  CA  LYS B 510    14647  31604  14284  -1933   1400  -2597       C  
ATOM   8860  C   LYS B 510      -3.301   9.291  20.926  1.00158.65           C  
ANISOU 8860  C   LYS B 510    14736  31086  14458  -1878   1333  -2371       C  
ATOM   8861  O   LYS B 510      -4.486   9.021  21.126  1.00158.22           O  
ANISOU 8861  O   LYS B 510    14662  31040  14413  -1899   1274  -2403       O  
ATOM   8862  CB  LYS B 510      -1.653   8.011  19.575  1.00162.17           C  
ANISOU 8862  CB  LYS B 510    14954  31769  14894  -1959   1477  -2944       C  
ATOM   8863  CG  LYS B 510      -1.126   7.512  18.237  1.00175.84           C  
ANISOU 8863  CG  LYS B 510    16488  33901  16420  -2021   1553  -3281       C  
ATOM   8864  CD  LYS B 510      -0.281   6.248  18.451  1.00185.88           C  
ANISOU 8864  CD  LYS B 510    17721  34904  18000  -2020   1622  -3654       C  
ATOM   8865  CE  LYS B 510       1.189   6.360  18.079  1.00192.09           C  
ANISOU 8865  CE  LYS B 510    18449  35775  18760  -1983   1712  -3709       C  
ATOM   8866  NZ  LYS B 510       2.052   5.575  19.003  1.00196.83           N  
ANISOU 8866  NZ  LYS B 510    19114  35916  19756  -1909   1743  -3830       N  
ATOM   8867  N   ASN B 511      -2.468   9.734  21.885  1.00152.35           N  
ANISOU 8867  N   ASN B 511    14096  29934  13856  -1816   1346  -2150       N  
ATOM   8868  CA  ASN B 511      -2.851   9.938  23.280  1.00149.44           C  
ANISOU 8868  CA  ASN B 511    13902  29145  13733  -1762   1292  -1926       C  
ATOM   8869  C   ASN B 511      -2.113  11.134  23.878  1.00150.75           C  
ANISOU 8869  C   ASN B 511    14231  29157  13891  -1695   1296  -1558       C  
ATOM   8870  O   ASN B 511      -0.998  11.459  23.467  1.00150.88           O  
ANISOU 8870  O   ASN B 511    14229  29263  13834  -1706   1354  -1540       O  
ATOM   8871  CB  ASN B 511      -2.617   8.673  24.121  1.00149.78           C  
ANISOU 8871  CB  ASN B 511    13968  28789  14154  -1781   1302  -2165       C  
ATOM   8872  CG  ASN B 511      -1.372   7.894  23.774  1.00171.27           C  
ANISOU 8872  CG  ASN B 511    16611  31467  16996  -1792   1378  -2436       C  
ATOM   8873  OD1 ASN B 511      -0.261   8.228  24.192  1.00167.25           O  
ANISOU 8873  OD1 ASN B 511    16165  30805  16579  -1742   1408  -2317       O  
ATOM   8874  ND2 ASN B 511      -1.539   6.819  23.019  1.00163.74           N  
ANISOU 8874  ND2 ASN B 511    15516  30651  16049  -1857   1412  -2820       N  
ATOM   8875  N   ARG B 512      -2.760  11.790  24.845  1.00144.69           N  
ANISOU 8875  N   ARG B 512    13618  28168  13190  -1636   1238  -1275       N  
ATOM   8876  CA  ARG B 512      -2.255  12.977  25.533  1.00142.46           C  
ANISOU 8876  CA  ARG B 512    13516  27704  12907  -1580   1235   -919       C  
ATOM   8877  C   ARG B 512      -2.620  12.924  27.035  1.00142.68           C  
ANISOU 8877  C   ARG B 512    13699  27303  13210  -1534   1187   -786       C  
ATOM   8878  O   ARG B 512      -3.464  12.102  27.410  1.00141.93           O  
ANISOU 8878  O   ARG B 512    13565  27111  13250  -1544   1153   -931       O  
ATOM   8879  CB  ARG B 512      -2.822  14.248  24.866  1.00143.79           C  
ANISOU 8879  CB  ARG B 512    13724  28165  12744  -1536   1217   -642       C  
ATOM   8880  CG  ARG B 512      -4.343  14.341  24.872  1.00155.84           C  
ANISOU 8880  CG  ARG B 512    15231  29808  14174  -1481   1147   -585       C  
ATOM   8881  CD  ARG B 512      -4.791  15.768  24.705  1.00167.64           C  
ANISOU 8881  CD  ARG B 512    16842  31425  15428  -1386   1122   -219       C  
ATOM   8882  NE  ARG B 512      -6.247  15.868  24.637  1.00178.33           N  
ANISOU 8882  NE  ARG B 512    18149  32943  16668  -1312   1053   -169       N  
ATOM   8883  CZ  ARG B 512      -6.909  16.999  24.424  1.00194.02           C  
ANISOU 8883  CZ  ARG B 512    20211  35075  18433  -1195   1019    127       C  
ATOM   8884  NH1 ARG B 512      -6.254  18.139  24.253  1.00182.09           N  
ANISOU 8884  NH1 ARG B 512    18849  33540  16796  -1154   1052    405       N  
ATOM   8885  NH2 ARG B 512      -8.233  16.997  24.368  1.00182.66           N  
ANISOU 8885  NH2 ARG B 512    18697  33812  16895  -1119    954    146       N  
ATOM   8886  N   PRO B 513      -2.029  13.781  27.911  1.00136.78           N  
ANISOU 8886  N   PRO B 513    13124  26307  12539  -1496   1187   -519       N  
ATOM   8887  CA  PRO B 513      -2.384  13.722  29.339  1.00134.33           C  
ANISOU 8887  CA  PRO B 513    12952  25616  12470  -1456   1143   -402       C  
ATOM   8888  C   PRO B 513      -3.848  14.068  29.601  1.00136.38           C  
ANISOU 8888  C   PRO B 513    13252  25912  12654  -1400   1086   -276       C  
ATOM   8889  O   PRO B 513      -4.413  14.931  28.922  1.00136.56           O  
ANISOU 8889  O   PRO B 513    13276  26192  12420  -1355   1076   -126       O  
ATOM   8890  CB  PRO B 513      -1.446  14.750  29.981  1.00135.08           C  
ANISOU 8890  CB  PRO B 513    13210  25529  12586  -1441   1160   -144       C  
ATOM   8891  CG  PRO B 513      -0.340  14.932  29.007  1.00140.89           C  
ANISOU 8891  CG  PRO B 513    13861  26488  13182  -1497   1224   -207       C  
ATOM   8892  CD  PRO B 513      -0.992  14.805  27.672  1.00138.36           C  
ANISOU 8892  CD  PRO B 513    13398  26560  12613  -1508   1232   -324       C  
ATOM   8893  N   SER B 514      -4.469  13.368  30.564  1.00130.95           N  
ANISOU 8893  N   SER B 514    12589  24984  12184  -1399   1052   -336       N  
ATOM   8894  CA  SER B 514      -5.867  13.594  30.918  1.00130.02           C  
ANISOU 8894  CA  SER B 514    12488  24900  12015  -1351   1002   -238       C  
ATOM   8895  C   SER B 514      -5.992  14.842  31.785  1.00130.98           C  
ANISOU 8895  C   SER B 514    12802  24851  12112  -1256    983     96       C  
ATOM   8896  O   SER B 514      -5.366  14.925  32.848  1.00129.17           O  
ANISOU 8896  O   SER B 514    12704  24304  12073  -1255    987    184       O  
ATOM   8897  CB  SER B 514      -6.455  12.377  31.628  1.00133.09           C  
ANISOU 8897  CB  SER B 514    12832  25099  12639  -1408    982   -425       C  
ATOM   8898  OG  SER B 514      -7.786  12.607  32.064  1.00139.18           O  
ANISOU 8898  OG  SER B 514    13609  25909  13364  -1371    939   -325       O  
ATOM   8899  N   LEU B 515      -6.799  15.815  31.316  1.00126.65           N  
ANISOU 8899  N   LEU B 515    12272  24524  11324  -1168    962    277       N  
ATOM   8900  CA  LEU B 515      -7.063  17.074  32.021  1.00124.79           C  
ANISOU 8900  CA  LEU B 515    12227  24147  11042  -1057    948    587       C  
ATOM   8901  C   LEU B 515      -7.906  16.821  33.277  1.00125.18           C  
ANISOU 8901  C   LEU B 515    12329  23970  11263  -1019    913    620       C  
ATOM   8902  O   LEU B 515      -7.850  17.611  34.221  1.00123.69           O  
ANISOU 8902  O   LEU B 515    12317  23550  11131   -953    911    826       O  
ATOM   8903  CB  LEU B 515      -7.761  18.088  31.098  1.00126.34           C  
ANISOU 8903  CB  LEU B 515    12416  24653  10935   -949    935    761       C  
ATOM   8904  CG  LEU B 515      -6.950  18.571  29.897  1.00132.40           C  
ANISOU 8904  CG  LEU B 515    13162  25648  11495   -980    974    796       C  
ATOM   8905  CD1 LEU B 515      -7.825  18.721  28.682  1.00134.82           C  
ANISOU 8905  CD1 LEU B 515    13324  26384  11516   -923    948    790       C  
ATOM   8906  CD2 LEU B 515      -6.228  19.873  30.191  1.00134.14           C  
ANISOU 8906  CD2 LEU B 515    13607  25690  11670   -939   1007   1083       C  
ATOM   8907  N   LEU B 516      -8.669  15.708  33.288  1.00120.08           N  
ANISOU 8907  N   LEU B 516    11533  23394  10697  -1077    892    408       N  
ATOM   8908  CA  LEU B 516      -9.488  15.282  34.421  1.00118.02           C  
ANISOU 8908  CA  LEU B 516    11295  22950  10599  -1075    867    408       C  
ATOM   8909  C   LEU B 516      -8.577  14.837  35.562  1.00119.04           C  
ANISOU 8909  C   LEU B 516    11541  22691  10997  -1133    882    402       C  
ATOM   8910  O   LEU B 516      -8.799  15.245  36.701  1.00117.47           O  
ANISOU 8910  O   LEU B 516    11473  22275  10887  -1085    871    557       O  
ATOM   8911  CB  LEU B 516     -10.440  14.147  34.001  1.00118.99           C  
ANISOU 8911  CB  LEU B 516    11218  23265  10729  -1162    849    163       C  
ATOM   8912  CG  LEU B 516     -11.510  13.737  35.008  1.00122.31           C  
ANISOU 8912  CG  LEU B 516    11628  23579  11264  -1174    827    166       C  
ATOM   8913  CD1 LEU B 516     -12.781  14.538  34.806  1.00123.02           C  
ANISOU 8913  CD1 LEU B 516    11663  23942  11136  -1053    793    303       C  
ATOM   8914  CD2 LEU B 516     -11.810  12.259  34.894  1.00124.48           C  
ANISOU 8914  CD2 LEU B 516    11761  23854  11682  -1337    833   -124       C  
ATOM   8915  N   VAL B 517      -7.529  14.035  35.243  1.00114.80           N  
ANISOU 8915  N   VAL B 517    10956  22085  10577  -1225    908    224       N  
ATOM   8916  CA  VAL B 517      -6.529  13.543  36.201  1.00113.18           C  
ANISOU 8916  CA  VAL B 517    10839  21546  10619  -1267    919    207       C  
ATOM   8917  C   VAL B 517      -5.796  14.757  36.800  1.00116.72           C  
ANISOU 8917  C   VAL B 517    11464  21848  11036  -1206    924    456       C  
ATOM   8918  O   VAL B 517      -5.601  14.805  38.018  1.00115.07           O  
ANISOU 8918  O   VAL B 517    11372  21372  10979  -1198    912    555       O  
ATOM   8919  CB  VAL B 517      -5.562  12.506  35.559  1.00117.46           C  
ANISOU 8919  CB  VAL B 517    11273  22093  11263  -1347    949    -42       C  
ATOM   8920  CG1 VAL B 517      -4.425  12.123  36.507  1.00116.25           C  
ANISOU 8920  CG1 VAL B 517    11205  21622  11342  -1358    954    -30       C  
ATOM   8921  CG2 VAL B 517      -6.322  11.259  35.119  1.00118.42           C  
ANISOU 8921  CG2 VAL B 517    11247  22301  11446  -1425    948   -303       C  
ATOM   8922  N   GLU B 518      -5.463  15.761  35.950  1.00114.55           N  
ANISOU 8922  N   GLU B 518    11214  21757  10552  -1170    944    564       N  
ATOM   8923  CA  GLU B 518      -4.810  17.009  36.366  1.00113.99           C  
ANISOU 8923  CA  GLU B 518    11320  21564  10426  -1132    958    797       C  
ATOM   8924  C   GLU B 518      -5.711  17.781  37.326  1.00117.67           C  
ANISOU 8924  C   GLU B 518    11928  21899  10883  -1040    934    994       C  
ATOM   8925  O   GLU B 518      -5.244  18.210  38.382  1.00116.24           O  
ANISOU 8925  O   GLU B 518    11894  21467  10806  -1040    935   1111       O  
ATOM   8926  CB  GLU B 518      -4.435  17.882  35.150  1.00116.55           C  
ANISOU 8926  CB  GLU B 518    11641  22131  10512  -1123    991    876       C  
ATOM   8927  CG  GLU B 518      -3.393  17.293  34.208  1.00127.64           C  
ANISOU 8927  CG  GLU B 518    12914  23683  11900  -1214   1027    697       C  
ATOM   8928  CD  GLU B 518      -2.243  16.539  34.844  1.00146.74           C  
ANISOU 8928  CD  GLU B 518    15318  25892  14546  -1285   1039    575       C  
ATOM   8929  OE1 GLU B 518      -1.359  17.185  35.454  1.00134.99           O  
ANISOU 8929  OE1 GLU B 518    13950  24239  13100  -1307   1052    710       O  
ATOM   8930  OE2 GLU B 518      -2.211  15.296  34.702  1.00143.38           O  
ANISOU 8930  OE2 GLU B 518    14756  25471  14249  -1318   1035    341       O  
ATOM   8931  N   LYS B 519      -7.012  17.902  36.986  1.00115.42           N  
ANISOU 8931  N   LYS B 519    11583  21798  10474   -962    913   1013       N  
ATOM   8932  CA  LYS B 519      -8.017  18.576  37.807  1.00115.24           C  
ANISOU 8932  CA  LYS B 519    11661  21697  10426   -853    893   1176       C  
ATOM   8933  C   LYS B 519      -8.194  17.860  39.157  1.00119.09           C  
ANISOU 8933  C   LYS B 519    12176  21938  11137   -894    878   1129       C  
ATOM   8934  O   LYS B 519      -8.294  18.532  40.185  1.00118.09           O  
ANISOU 8934  O   LYS B 519    12200  21621  11047   -839    877   1281       O  
ATOM   8935  CB  LYS B 519      -9.356  18.670  37.061  1.00118.98           C  
ANISOU 8935  CB  LYS B 519    12013  22476  10719   -762    870   1171       C  
ATOM   8936  CG  LYS B 519      -9.440  19.854  36.108  1.00131.99           C  
ANISOU 8936  CG  LYS B 519    13713  24317  12118   -652    879   1340       C  
ATOM   8937  CD  LYS B 519     -10.682  19.778  35.237  1.00141.07           C  
ANISOU 8937  CD  LYS B 519    14697  25826  13077   -567    847   1307       C  
ATOM   8938  CE  LYS B 519     -10.849  21.006  34.378  1.00148.71           C  
ANISOU 8938  CE  LYS B 519    15734  26976  13793   -427    850   1515       C  
ATOM   8939  NZ  LYS B 519     -12.098  20.941  33.575  1.00156.18           N  
ANISOU 8939  NZ  LYS B 519    16502  28301  14539   -325    808   1494       N  
ATOM   8940  N   ILE B 520      -8.187  16.504  39.152  1.00116.30           N  
ANISOU 8940  N   ILE B 520    11685  21576  10927   -997    870    920       N  
ATOM   8941  CA  ILE B 520      -8.299  15.668  40.355  1.00115.52           C  
ANISOU 8941  CA  ILE B 520    11605  21244  11044  -1053    858    874       C  
ATOM   8942  C   ILE B 520      -7.043  15.890  41.231  1.00118.75           C  
ANISOU 8942  C   ILE B 520    12156  21378  11585  -1078    863    956       C  
ATOM   8943  O   ILE B 520      -7.167  15.989  42.454  1.00116.98           O  
ANISOU 8943  O   ILE B 520    12033  20957  11457  -1067    852   1051       O  
ATOM   8944  CB  ILE B 520      -8.546  14.168  39.982  1.00119.29           C  
ANISOU 8944  CB  ILE B 520    11915  21771  11639  -1162    855    628       C  
ATOM   8945  CG1 ILE B 520      -9.993  13.964  39.478  1.00120.53           C  
ANISOU 8945  CG1 ILE B 520    11935  22185  11675  -1155    843    560       C  
ATOM   8946  CG2 ILE B 520      -8.268  13.220  41.156  1.00119.51           C  
ANISOU 8946  CG2 ILE B 520    11986  21507  11914  -1234    850    588       C  
ATOM   8947  CD1 ILE B 520     -10.221  12.726  38.601  1.00127.71           C  
ANISOU 8947  CD1 ILE B 520    12664  23241  12619  -1271    849    293       C  
ATOM   8948  N   ASN B 521      -5.858  16.022  40.601  1.00116.66           N  
ANISOU 8948  N   ASN B 521    11889  21130  11305  -1113    882    923       N  
ATOM   8949  CA  ASN B 521      -4.601  16.278  41.306  1.00116.47           C  
ANISOU 8949  CA  ASN B 521    11972  20899  11382  -1145    886    991       C  
ATOM   8950  C   ASN B 521      -4.646  17.650  41.978  1.00120.59           C  
ANISOU 8950  C   ASN B 521    12678  21325  11815  -1088    890   1212       C  
ATOM   8951  O   ASN B 521      -4.250  17.765  43.141  1.00119.25           O  
ANISOU 8951  O   ASN B 521    12612  20945  11751  -1104    877   1285       O  
ATOM   8952  CB  ASN B 521      -3.393  16.180  40.360  1.00119.52           C  
ANISOU 8952  CB  ASN B 521    12290  21382  11741  -1197    911    900       C  
ATOM   8953  CG  ASN B 521      -2.052  16.052  41.062  1.00152.22           C  
ANISOU 8953  CG  ASN B 521    16476  25340  16020  -1245    910    910       C  
ATOM   8954  OD1 ASN B 521      -1.699  16.814  41.973  1.00149.12           O  
ANISOU 8954  OD1 ASN B 521    16224  24799  15638  -1244    902   1063       O  
ATOM   8955  ND2 ASN B 521      -1.241  15.110  40.619  1.00146.24           N  
ANISOU 8955  ND2 ASN B 521    15595  24609  15362  -1285    918    739       N  
ATOM   8956  N   LEU B 522      -5.141  18.680  41.250  1.00118.34           N  
ANISOU 8956  N   LEU B 522    12440  21193  11333  -1018    907   1317       N  
ATOM   8957  CA  LEU B 522      -5.266  20.049  41.758  1.00118.19           C  
ANISOU 8957  CA  LEU B 522    12614  21073  11220   -949    920   1522       C  
ATOM   8958  C   LEU B 522      -6.290  20.104  42.887  1.00121.69           C  
ANISOU 8958  C   LEU B 522    13118  21404  11714   -877    901   1582       C  
ATOM   8959  O   LEU B 522      -6.059  20.801  43.876  1.00120.79           O  
ANISOU 8959  O   LEU B 522    13165  21100  11629   -864    907   1695       O  
ATOM   8960  CB  LEU B 522      -5.645  21.034  40.638  1.00119.50           C  
ANISOU 8960  CB  LEU B 522    12810  21428  11164   -871    944   1624       C  
ATOM   8961  CG  LEU B 522      -4.546  21.375  39.628  1.00124.93           C  
ANISOU 8961  CG  LEU B 522    13493  22213  11763   -947    977   1627       C  
ATOM   8962  CD1 LEU B 522      -5.142  21.758  38.293  1.00126.67           C  
ANISOU 8962  CD1 LEU B 522    13649  22709  11769   -877    988   1662       C  
ATOM   8963  CD2 LEU B 522      -3.653  22.488  40.134  1.00126.69           C  
ANISOU 8963  CD2 LEU B 522    13920  22242  11974   -989   1009   1781       C  
ATOM   8964  N   PHE B 523      -7.396  19.332  42.759  1.00118.54           N  
ANISOU 8964  N   PHE B 523    12583  21133  11324   -846    882   1493       N  
ATOM   8965  CA  PHE B 523      -8.447  19.228  43.775  1.00117.91           C  
ANISOU 8965  CA  PHE B 523    12521  20992  11286   -792    869   1529       C  
ATOM   8966  C   PHE B 523      -7.882  18.603  45.050  1.00120.76           C  
ANISOU 8966  C   PHE B 523    12930  21115  11837   -878    857   1509       C  
ATOM   8967  O   PHE B 523      -8.249  19.029  46.137  1.00119.50           O  
ANISOU 8967  O   PHE B 523    12876  20834  11694   -837    857   1604       O  
ATOM   8968  CB  PHE B 523      -9.647  18.413  43.254  1.00120.39           C  
ANISOU 8968  CB  PHE B 523    12648  21526  11569   -782    855   1413       C  
ATOM   8969  CG  PHE B 523     -10.648  18.000  44.310  1.00121.65           C  
ANISOU 8969  CG  PHE B 523    12785  21638  11797   -773    846   1416       C  
ATOM   8970  CD1 PHE B 523     -11.592  18.902  44.788  1.00124.90           C  
ANISOU 8970  CD1 PHE B 523    13264  22091  12103   -638    854   1542       C  
ATOM   8971  CD2 PHE B 523     -10.644  16.709  44.830  1.00123.32           C  
ANISOU 8971  CD2 PHE B 523    12914  21761  12180   -896    837   1294       C  
ATOM   8972  CE1 PHE B 523     -12.507  18.523  45.773  1.00125.70           C  
ANISOU 8972  CE1 PHE B 523    13330  22175  12255   -637    854   1540       C  
ATOM   8973  CE2 PHE B 523     -11.558  16.332  45.816  1.00125.88           C  
ANISOU 8973  CE2 PHE B 523    13221  22051  12558   -907    837   1309       C  
ATOM   8974  CZ  PHE B 523     -12.485  17.240  46.279  1.00124.29           C  
ANISOU 8974  CZ  PHE B 523    13067  21920  12236   -783    846   1428       C  
ATOM   8975  N   ALA B 524      -7.007  17.590  44.911  1.00117.84           N  
ANISOU 8975  N   ALA B 524    12480  20690  11603   -984    846   1387       N  
ATOM   8976  CA  ALA B 524      -6.365  16.911  46.034  1.00117.30           C  
ANISOU 8976  CA  ALA B 524    12447  20409  11714  -1055    828   1375       C  
ATOM   8977  C   ALA B 524      -5.336  17.823  46.706  1.00122.22           C  
ANISOU 8977  C   ALA B 524    13226  20882  12331  -1061    829   1494       C  
ATOM   8978  O   ALA B 524      -5.331  17.908  47.932  1.00121.20           O  
ANISOU 8978  O   ALA B 524    13185  20602  12262  -1066    816   1566       O  
ATOM   8979  CB  ALA B 524      -5.707  15.625  45.565  1.00118.30           C  
ANISOU 8979  CB  ALA B 524    12445  20526  11980  -1136    819   1211       C  
ATOM   8980  N   MET B 525      -4.491  18.524  45.906  1.00120.48           N  
ANISOU 8980  N   MET B 525    13036  20715  12024  -1074    849   1512       N  
ATOM   8981  CA  MET B 525      -3.458  19.449  46.388  1.00120.54           C  
ANISOU 8981  CA  MET B 525    13185  20604  12010  -1110    858   1610       C  
ATOM   8982  C   MET B 525      -4.099  20.631  47.133  1.00123.44           C  
ANISOU 8982  C   MET B 525    13730  20883  12287  -1042    872   1755       C  
ATOM   8983  O   MET B 525      -3.810  20.823  48.315  1.00122.29           O  
ANISOU 8983  O   MET B 525    13682  20585  12199  -1069    860   1805       O  
ATOM   8984  CB  MET B 525      -2.581  19.950  45.221  1.00124.02           C  
ANISOU 8984  CB  MET B 525    13609  21156  12356  -1152    887   1599       C  
ATOM   8985  CG  MET B 525      -1.332  20.703  45.673  1.00128.34           C  
ANISOU 8985  CG  MET B 525    14269  21594  12901  -1236    898   1668       C  
ATOM   8986  SD  MET B 525      -0.712  21.919  44.468  1.00134.27           S  
ANISOU 8986  SD  MET B 525    15091  22452  13471  -1279    955   1743       S  
ATOM   8987  CE  MET B 525       0.243  20.856  43.377  1.00131.45           C  
ANISOU 8987  CE  MET B 525    14510  22280  13156  -1351    958   1573       C  
ATOM   8988  N   PHE B 526      -4.989  21.391  46.451  1.00120.14           N  
ANISOU 8988  N   PHE B 526    13350  20572  11725   -943    898   1817       N  
ATOM   8989  CA  PHE B 526      -5.679  22.551  47.023  1.00119.83           C  
ANISOU 8989  CA  PHE B 526    13482  20454  11595   -843    920   1947       C  
ATOM   8990  C   PHE B 526      -6.727  22.148  48.064  1.00121.19           C  
ANISOU 8990  C   PHE B 526    13636  20593  11818   -782    904   1942       C  
ATOM   8991  O   PHE B 526      -7.018  22.947  48.954  1.00120.64           O  
ANISOU 8991  O   PHE B 526    13714  20406  11717   -727    920   2025       O  
ATOM   8992  CB  PHE B 526      -6.319  23.418  45.928  1.00123.00           C  
ANISOU 8992  CB  PHE B 526    13918  20990  11828   -728    948   2023       C  
ATOM   8993  CG  PHE B 526      -5.310  24.205  45.129  1.00125.60           C  
ANISOU 8993  CG  PHE B 526    14336  21309  12077   -787    979   2083       C  
ATOM   8994  CD1 PHE B 526      -4.656  25.298  45.686  1.00129.40           C  
ANISOU 8994  CD1 PHE B 526    15030  21597  12540   -826   1010   2185       C  
ATOM   8995  CD2 PHE B 526      -5.005  23.850  43.823  1.00128.65           C  
ANISOU 8995  CD2 PHE B 526    14594  21886  12401   -822    983   2031       C  
ATOM   8996  CE1 PHE B 526      -3.708  26.015  44.952  1.00131.39           C  
ANISOU 8996  CE1 PHE B 526    15366  21840  12717   -910   1046   2244       C  
ATOM   8997  CE2 PHE B 526      -4.062  24.572  43.087  1.00132.50           C  
ANISOU 8997  CE2 PHE B 526    15159  22382  12804   -893   1019   2094       C  
ATOM   8998  CZ  PHE B 526      -3.420  25.651  43.654  1.00130.96           C  
ANISOU 8998  CZ  PHE B 526    15176  21987  12595   -942   1052   2206       C  
ATOM   8999  N   GLY B 527      -7.259  20.927  47.953  1.00116.00           N  
ANISOU 8999  N   GLY B 527    12804  20035  11236   -804    879   1839       N  
ATOM   9000  CA  GLY B 527      -8.239  20.369  48.884  1.00114.72           C  
ANISOU 9000  CA  GLY B 527    12598  19866  11126   -780    869   1827       C  
ATOM   9001  C   GLY B 527      -7.686  20.227  50.283  1.00115.84           C  
ANISOU 9001  C   GLY B 527    12830  19816  11369   -847    856   1860       C  
ATOM   9002  O   GLY B 527      -8.385  20.535  51.249  1.00115.25           O  
ANISOU 9002  O   GLY B 527    12819  19701  11270   -797    866   1914       O  
ATOM   9003  N   THR B 528      -6.406  19.795  50.391  1.00110.76           N  
ANISOU 9003  N   THR B 528    12184  19075  10823   -954    834   1827       N  
ATOM   9004  CA  THR B 528      -5.683  19.657  51.658  1.00109.40           C  
ANISOU 9004  CA  THR B 528    12086  18746  10736  -1022    811   1862       C  
ATOM   9005  C   THR B 528      -5.545  21.037  52.296  1.00112.62           C  
ANISOU 9005  C   THR B 528    12683  19063  11042   -989    835   1958       C  
ATOM   9006  O   THR B 528      -5.882  21.187  53.460  1.00111.98           O  
ANISOU 9006  O   THR B 528    12673  18912  10961   -980    833   2000       O  
ATOM   9007  CB  THR B 528      -4.310  18.984  51.469  1.00114.90           C  
ANISOU 9007  CB  THR B 528    12721  19395  11541  -1119    780   1806       C  
ATOM   9008  OG1 THR B 528      -4.369  18.007  50.438  1.00113.66           O  
ANISOU 9008  OG1 THR B 528    12408  19333  11445  -1130    776   1697       O  
ATOM   9009  CG2 THR B 528      -3.799  18.338  52.741  1.00113.20           C  
ANISOU 9009  CG2 THR B 528    12515  19060  11437  -1175    740   1829       C  
ATOM   9010  N   GLY B 529      -5.121  22.031  51.508  1.00109.17           N  
ANISOU 9010  N   GLY B 529    12330  18633  10514   -974    863   1988       N  
ATOM   9011  CA  GLY B 529      -4.963  23.420  51.937  1.00109.05           C  
ANISOU 9011  CA  GLY B 529    12520  18510  10406   -951    896   2070       C  
ATOM   9012  C   GLY B 529      -6.222  24.054  52.501  1.00112.19           C  
ANISOU 9012  C   GLY B 529    13006  18894  10727   -816    925   2122       C  
ATOM   9013  O   GLY B 529      -6.139  24.900  53.396  1.00112.41           O  
ANISOU 9013  O   GLY B 529    13198  18796  10718   -809    946   2163       O  
ATOM   9014  N   ILE B 530      -7.399  23.640  51.987  1.00107.33           N  
ANISOU 9014  N   ILE B 530    12275  18424  10083   -709    929   2107       N  
ATOM   9015  CA  ILE B 530      -8.698  24.123  52.451  1.00107.01           C  
ANISOU 9015  CA  ILE B 530    12273  18421   9966   -562    956   2145       C  
ATOM   9016  C   ILE B 530      -9.109  23.301  53.680  1.00108.78           C  
ANISOU 9016  C   ILE B 530    12432  18639  10261   -606    939   2114       C  
ATOM   9017  O   ILE B 530      -9.530  23.885  54.675  1.00108.06           O  
ANISOU 9017  O   ILE B 530    12445  18486  10125   -551    963   2146       O  
ATOM   9018  CB  ILE B 530      -9.771  24.097  51.320  1.00110.93           C  
ANISOU 9018  CB  ILE B 530    12654  19116  10378   -429    965   2145       C  
ATOM   9019  CG1 ILE B 530      -9.375  25.037  50.161  1.00112.16           C  
ANISOU 9019  CG1 ILE B 530    12901  19276  10439   -375    986   2207       C  
ATOM   9020  CG2 ILE B 530     -11.164  24.473  51.855  1.00112.71           C  
ANISOU 9020  CG2 ILE B 530    12879  19419  10527   -267    990   2174       C  
ATOM   9021  CD1 ILE B 530      -9.977  24.671  48.806  1.00121.16           C  
ANISOU 9021  CD1 ILE B 530    13878  20647  11509   -308    974   2186       C  
ATOM   9022  N   ALA B 531      -8.970  21.959  53.618  1.00104.77           N  
ANISOU 9022  N   ALA B 531    11760  18187   9860   -708    902   2052       N  
ATOM   9023  CA  ALA B 531      -9.334  21.056  54.719  1.00104.51           C  
ANISOU 9023  CA  ALA B 531    11664  18145   9901   -767    886   2040       C  
ATOM   9024  C   ALA B 531      -8.508  21.308  55.978  1.00108.26           C  
ANISOU 9024  C   ALA B 531    12264  18468  10402   -839    873   2080       C  
ATOM   9025  O   ALA B 531      -9.066  21.269  57.065  1.00107.73           O  
ANISOU 9025  O   ALA B 531    12222  18399  10314   -829    884   2106       O  
ATOM   9026  CB  ALA B 531      -9.196  19.604  54.294  1.00105.04           C  
ANISOU 9026  CB  ALA B 531    11561  18258  10092   -866    853   1970       C  
ATOM   9027  N   MET B 532      -7.202  21.603  55.838  1.00105.16           N  
ANISOU 9027  N   MET B 532    11942  17976  10038   -915    853   2081       N  
ATOM   9028  CA  MET B 532      -6.322  21.879  56.979  1.00105.05           C  
ANISOU 9028  CA  MET B 532    12033  17846  10033   -996    833   2110       C  
ATOM   9029  C   MET B 532      -6.612  23.265  57.568  1.00110.61           C  
ANISOU 9029  C   MET B 532    12923  18485  10618   -932    879   2142       C  
ATOM   9030  O   MET B 532      -6.316  23.501  58.740  1.00110.57           O  
ANISOU 9030  O   MET B 532    13002  18419  10592   -982    872   2154       O  
ATOM   9031  CB  MET B 532      -4.835  21.738  56.600  1.00106.91           C  
ANISOU 9031  CB  MET B 532    12258  18030  10331  -1104    797   2090       C  
ATOM   9032  CG  MET B 532      -4.443  20.346  56.086  1.00110.00           C  
ANISOU 9032  CG  MET B 532    12476  18465  10855  -1153    754   2044       C  
ATOM   9033  SD  MET B 532      -4.908  18.937  57.129  1.00114.01           S  
ANISOU 9033  SD  MET B 532    12887  18963  11469  -1181    718   2062       S  
ATOM   9034  CE  MET B 532      -6.235  18.234  56.160  1.00110.75           C  
ANISOU 9034  CE  MET B 532    12344  18657  11078  -1124    748   2007       C  
ATOM   9035  N   SER B 533      -7.239  24.158  56.773  1.00108.17           N  
ANISOU 9035  N   SER B 533    12680  18194  10226   -813    926   2154       N  
ATOM   9036  CA  SER B 533      -7.611  25.505  57.198  1.00108.95           C  
ANISOU 9036  CA  SER B 533    12970  18207  10220   -721    979   2180       C  
ATOM   9037  C   SER B 533      -8.890  25.500  58.069  1.00113.52           C  
ANISOU 9037  C   SER B 533    13535  18852  10746   -608   1007   2180       C  
ATOM   9038  O   SER B 533      -9.200  26.521  58.684  1.00113.76           O  
ANISOU 9038  O   SER B 533    13722  18805  10696   -529   1053   2184       O  
ATOM   9039  CB  SER B 533      -7.791  26.420  55.988  1.00113.01           C  
ANISOU 9039  CB  SER B 533    13562  18709  10669   -617   1017   2213       C  
ATOM   9040  OG  SER B 533      -9.120  26.413  55.496  1.00122.99           O  
ANISOU 9040  OG  SER B 533    14751  20104  11878   -444   1039   2228       O  
ATOM   9041  N   THR B 534      -9.617  24.362  58.129  1.00110.26           N  
ANISOU 9041  N   THR B 534    12937  18580  10377   -608    987   2168       N  
ATOM   9042  CA  THR B 534     -10.855  24.242  58.910  1.00111.16           C  
ANISOU 9042  CA  THR B 534    13003  18796  10435   -522   1018   2167       C  
ATOM   9043  C   THR B 534     -10.572  23.858  60.384  1.00115.79           C  
ANISOU 9043  C   THR B 534    13614  19347  11033   -628   1005   2171       C  
ATOM   9044  O   THR B 534     -11.512  23.629  61.149  1.00115.56           O  
ANISOU 9044  O   THR B 534    13534  19417  10957   -588   1032   2172       O  
ATOM   9045  CB  THR B 534     -11.845  23.259  58.258  1.00121.13           C  
ANISOU 9045  CB  THR B 534    14055  20244  11724   -492   1012   2151       C  
ATOM   9046  OG1 THR B 534     -11.339  21.928  58.350  1.00121.22           O  
ANISOU 9046  OG1 THR B 534    13946  20256  11855   -651    963   2137       O  
ATOM   9047  CG2 THR B 534     -12.191  23.624  56.814  1.00119.80           C  
ANISOU 9047  CG2 THR B 534    13845  20156  11518   -382   1019   2147       C  
ATOM   9048  N   TRP B 535      -9.286  23.821  60.783  1.00112.81           N  
ANISOU 9048  N   TRP B 535    13308  18851  10702   -761    965   2175       N  
ATOM   9049  CA  TRP B 535      -8.844  23.530  62.152  1.00113.09           C  
ANISOU 9049  CA  TRP B 535    13374  18862  10731   -864    941   2189       C  
ATOM   9050  C   TRP B 535      -9.202  24.703  63.078  1.00118.98           C  
ANISOU 9050  C   TRP B 535    14284  19573  11351   -797    996   2165       C  
ATOM   9051  O   TRP B 535      -9.398  24.518  64.277  1.00118.59           O  
ANISOU 9051  O   TRP B 535    14239  19569  11251   -835    999   2169       O  
ATOM   9052  CB  TRP B 535      -7.327  23.264  62.155  1.00111.32           C  
ANISOU 9052  CB  TRP B 535    13167  18551  10580  -1008    879   2194       C  
ATOM   9053  CG  TRP B 535      -6.743  22.931  63.494  1.00112.57           C  
ANISOU 9053  CG  TRP B 535    13343  18706  10724  -1113    839   2219       C  
ATOM   9054  CD1 TRP B 535      -6.106  23.786  64.347  1.00116.02           C  
ANISOU 9054  CD1 TRP B 535    13916  19088  11077  -1169    840   2196       C  
ATOM   9055  CD2 TRP B 535      -6.740  21.649  64.134  1.00112.40           C  
ANISOU 9055  CD2 TRP B 535    13198  18743  10765  -1180    792   2274       C  
ATOM   9056  NE1 TRP B 535      -5.706  23.116  65.479  1.00115.66           N  
ANISOU 9056  NE1 TRP B 535    13828  19094  11025  -1260    790   2236       N  
ATOM   9057  CE2 TRP B 535      -6.084  21.802  65.376  1.00116.74           C  
ANISOU 9057  CE2 TRP B 535    13812  19292  11253  -1262    760   2296       C  
ATOM   9058  CE3 TRP B 535      -7.223  20.377  63.775  1.00113.33           C  
ANISOU 9058  CE3 TRP B 535    13167  18909  10986  -1186    775   2308       C  
ATOM   9059  CZ2 TRP B 535      -5.893  20.734  66.257  1.00116.24           C  
ANISOU 9059  CZ2 TRP B 535    13668  19278  11221  -1332    709   2374       C  
ATOM   9060  CZ3 TRP B 535      -7.043  19.321  64.655  1.00114.88           C  
ANISOU 9060  CZ3 TRP B 535    13299  19123  11228  -1264    732   2379       C  
ATOM   9061  CH2 TRP B 535      -6.384  19.504  65.878  1.00115.99           C  
ANISOU 9061  CH2 TRP B 535    13505  19265  11299  -1327    697   2423       C  
ATOM   9062  N   VAL B 536      -9.285  25.912  62.496  1.00117.75           N  
ANISOU 9062  N   VAL B 536    14267  19331  11142   -694   1042   2139       N  
ATOM   9063  CA  VAL B 536      -9.604  27.190  63.140  1.00119.63           C  
ANISOU 9063  CA  VAL B 536    14693  19490  11272   -604   1106   2099       C  
ATOM   9064  C   VAL B 536     -11.098  27.547  62.874  1.00125.72           C  
ANISOU 9064  C   VAL B 536    15433  20357  11977   -386   1170   2096       C  
ATOM   9065  O   VAL B 536     -11.499  28.687  63.086  1.00126.66           O  
ANISOU 9065  O   VAL B 536    15710  20399  12018   -253   1233   2064       O  
ATOM   9066  CB  VAL B 536      -8.590  28.260  62.603  1.00124.12           C  
ANISOU 9066  CB  VAL B 536    15449  19869  11840   -647   1117   2084       C  
ATOM   9067  CG1 VAL B 536      -9.096  29.701  62.595  1.00125.46           C  
ANISOU 9067  CG1 VAL B 536    15831  19911  11926   -497   1198   2054       C  
ATOM   9068  CG2 VAL B 536      -7.222  28.163  63.270  1.00123.72           C  
ANISOU 9068  CG2 VAL B 536    15446  19753  11811   -856   1067   2061       C  
ATOM   9069  N   TRP B 537     -11.924  26.578  62.438  1.00122.73           N  
ANISOU 9069  N   TRP B 537    14850  20151  11629   -348   1156   2123       N  
ATOM   9070  CA  TRP B 537     -13.353  26.831  62.203  1.00123.90           C  
ANISOU 9070  CA  TRP B 537    14929  20442  11706   -148   1210   2116       C  
ATOM   9071  C   TRP B 537     -14.135  26.362  63.443  1.00129.82           C  
ANISOU 9071  C   TRP B 537    15594  21336  12397   -160   1237   2097       C  
ATOM   9072  O   TRP B 537     -15.021  25.505  63.364  1.00129.58           O  
ANISOU 9072  O   TRP B 537    15372  21495  12370   -154   1238   2109       O  
ATOM   9073  CB  TRP B 537     -13.834  26.156  60.898  1.00122.05           C  
ANISOU 9073  CB  TRP B 537    14516  20338  11519   -108   1184   2143       C  
ATOM   9074  CG  TRP B 537     -13.327  26.773  59.622  1.00122.84           C  
ANISOU 9074  CG  TRP B 537    14696  20342  11635    -52   1174   2168       C  
ATOM   9075  CD1 TRP B 537     -12.219  27.557  59.465  1.00125.69           C  
ANISOU 9075  CD1 TRP B 537    15248  20497  12011   -107   1172   2178       C  
ATOM   9076  CD2 TRP B 537     -13.869  26.582  58.309  1.00122.69           C  
ANISOU 9076  CD2 TRP B 537    14555  20451  11612     42   1163   2189       C  
ATOM   9077  NE1 TRP B 537     -12.057  27.890  58.142  1.00125.18           N  
ANISOU 9077  NE1 TRP B 537    15196  20418  11949    -48   1167   2216       N  
ATOM   9078  CE2 TRP B 537     -13.054  27.304  57.408  1.00126.58           C  
ANISOU 9078  CE2 TRP B 537    15182  20804  12110     51   1158   2223       C  
ATOM   9079  CE3 TRP B 537     -14.978  25.881  57.805  1.00124.10           C  
ANISOU 9079  CE3 TRP B 537    14516  20867  11769    110   1159   2178       C  
ATOM   9080  CZ2 TRP B 537     -13.314  27.349  56.035  1.00126.01           C  
ANISOU 9080  CZ2 TRP B 537    15037  20825  12015    138   1147   2256       C  
ATOM   9081  CZ3 TRP B 537     -15.230  25.922  56.442  1.00125.71           C  
ANISOU 9081  CZ3 TRP B 537    14641  21171  11952    193   1143   2197       C  
ATOM   9082  CH2 TRP B 537     -14.406  26.652  55.574  1.00126.30           C  
ANISOU 9082  CH2 TRP B 537    14857  21107  12025    213   1137   2240       C  
ATOM   9083  N   THR B 538     -13.763  26.932  64.602  1.00127.92           N  
ANISOU 9083  N   THR B 538    15496  21011  12095   -196   1260   2062       N  
ATOM   9084  CA  THR B 538     -14.310  26.609  65.919  1.00128.82           C  
ANISOU 9084  CA  THR B 538    15561  21255  12132   -227   1289   2043       C  
ATOM   9085  C   THR B 538     -14.946  27.840  66.586  1.00134.48           C  
ANISOU 9085  C   THR B 538    16418  21959  12721    -54   1374   1967       C  
ATOM   9086  O   THR B 538     -14.902  28.944  66.032  1.00134.48           O  
ANISOU 9086  O   THR B 538    16572  21816  12707     89   1408   1936       O  
ATOM   9087  CB  THR B 538     -13.202  26.011  66.812  1.00139.11           C  
ANISOU 9087  CB  THR B 538    16890  22502  13465   -449   1231   2066       C  
ATOM   9088  OG1 THR B 538     -12.073  26.887  66.832  1.00139.34           O  
ANISOU 9088  OG1 THR B 538    17112  22334  13497   -498   1216   2031       O  
ATOM   9089  CG2 THR B 538     -12.766  24.625  66.358  1.00137.50           C  
ANISOU 9089  CG2 THR B 538    16526  22332  13385   -598   1156   2141       C  
ATOM   9090  N   LYS B 539     -15.551  27.629  67.774  1.00132.37           N  
ANISOU 9090  N   LYS B 539    16097  21840  12358    -64   1413   1937       N  
ATOM   9091  CA  LYS B 539     -16.211  28.662  68.571  1.00134.25           C  
ANISOU 9091  CA  LYS B 539    16444  22101  12465     96   1502   1845       C  
ATOM   9092  C   LYS B 539     -15.186  29.637  69.164  1.00139.90           C  
ANISOU 9092  C   LYS B 539    17410  22593  13151     37   1508   1772       C  
ATOM   9093  O   LYS B 539     -15.434  30.844  69.179  1.00140.92           O  
ANISOU 9093  O   LYS B 539    17712  22603  13228    204   1576   1690       O  
ATOM   9094  CB  LYS B 539     -17.046  28.020  69.693  1.00137.25           C  
ANISOU 9094  CB  LYS B 539    16674  22733  12743     60   1539   1836       C  
ATOM   9095  CG  LYS B 539     -18.185  27.117  69.203  1.00148.45           C  
ANISOU 9095  CG  LYS B 539    17838  24393  14171    104   1549   1890       C  
ATOM   9096  CD  LYS B 539     -18.529  26.023  70.213  1.00157.56           C  
ANISOU 9096  CD  LYS B 539    18835  25755  15275    -66   1551   1934       C  
ATOM   9097  CE  LYS B 539     -19.619  26.393  71.201  1.00168.50           C  
ANISOU 9097  CE  LYS B 539    20167  27360  16495     45   1648   1865       C  
ATOM   9098  NZ  LYS B 539     -20.978  26.316  70.597  1.00177.50           N  
ANISOU 9098  NZ  LYS B 539    21116  28722  17602    212   1701   1851       N  
ATOM   9099  N   ALA B 540     -14.029  29.108  69.631  1.00136.26           N  
ANISOU 9099  N   ALA B 540    16969  22077  12726   -200   1437   1801       N  
ATOM   9100  CA  ALA B 540     -12.932  29.854  70.260  1.00136.82           C  
ANISOU 9100  CA  ALA B 540    17244  21978  12765   -315   1428   1729       C  
ATOM   9101  C   ALA B 540     -12.317  30.902  69.333  1.00141.35           C  
ANISOU 9101  C   ALA B 540    18012  22294  13400   -265   1439   1699       C  
ATOM   9102  O   ALA B 540     -12.023  32.011  69.778  1.00141.70           O  
ANISOU 9102  O   ALA B 540    18269  22184  13385   -246   1489   1596       O  
ATOM   9103  CB  ALA B 540     -11.852  28.891  70.730  1.00136.49           C  
ANISOU 9103  CB  ALA B 540    17128  21973  12759   -563   1334   1794       C  
ATOM   9104  N   THR B 541     -12.137  30.550  68.050  1.00138.16           N  
ANISOU 9104  N   THR B 541    17541  21845  13108   -251   1397   1785       N  
ATOM   9105  CA  THR B 541     -11.547  31.420  67.026  1.00138.76           C  
ANISOU 9105  CA  THR B 541    17782  21698  13244   -219   1404   1788       C  
ATOM   9106  C   THR B 541     -12.497  32.562  66.647  1.00145.19           C  
ANISOU 9106  C   THR B 541    18731  22423  14010     48   1495   1751       C  
ATOM   9107  O   THR B 541     -12.034  33.598  66.162  1.00145.72           O  
ANISOU 9107  O   THR B 541    19013  22258  14095     81   1527   1734       O  
ATOM   9108  CB  THR B 541     -11.142  30.612  65.797  1.00145.53           C  
ANISOU 9108  CB  THR B 541    18500  22578  14215   -281   1335   1890       C  
ATOM   9109  OG1 THR B 541     -12.312  30.024  65.230  1.00145.84           O  
ANISOU 9109  OG1 THR B 541    18359  22792  14262   -127   1344   1939       O  
ATOM   9110  CG2 THR B 541     -10.101  29.537  66.120  1.00142.34           C  
ANISOU 9110  CG2 THR B 541    17980  22230  13872   -521   1245   1925       C  
ATOM   9111  N   LEU B 542     -13.819  32.374  66.870  1.00142.62           N  
ANISOU 9111  N   LEU B 542    18282  22284  13625    238   1540   1744       N  
ATOM   9112  CA  LEU B 542     -14.835  33.399  66.617  1.00144.28           C  
ANISOU 9112  CA  LEU B 542    18592  22449  13779    531   1627   1708       C  
ATOM   9113  C   LEU B 542     -14.709  34.497  67.673  1.00148.97           C  
ANISOU 9113  C   LEU B 542    19423  22885  14294    565   1703   1574       C  
ATOM   9114  O   LEU B 542     -14.951  35.669  67.379  1.00150.26           O  
ANISOU 9114  O   LEU B 542    19794  22852  14446    754   1771   1535       O  
ATOM   9115  CB  LEU B 542     -16.259  32.803  66.618  1.00144.83           C  
ANISOU 9115  CB  LEU B 542    18422  22811  13796    709   1650   1727       C  
ATOM   9116  CG  LEU B 542     -16.634  31.879  65.450  1.00148.73           C  
ANISOU 9116  CG  LEU B 542    18687  23468  14354    721   1591   1836       C  
ATOM   9117  CD1 LEU B 542     -17.720  30.904  65.859  1.00149.05           C  
ANISOU 9117  CD1 LEU B 542    18458  23830  14345    742   1597   1838       C  
ATOM   9118  CD2 LEU B 542     -17.084  32.671  64.228  1.00152.42           C  
ANISOU 9118  CD2 LEU B 542    19221  23861  14830    965   1614   1885       C  
ATOM   9119  N   LEU B 543     -14.289  34.108  68.894  1.00144.52           N  
ANISOU 9119  N   LEU B 543    18837  22400  13673    377   1689   1504       N  
ATOM   9120  CA  LEU B 543     -14.076  35.012  70.022  1.00145.86           C  
ANISOU 9120  CA  LEU B 543    19211  22458  13752    359   1753   1353       C  
ATOM   9121  C   LEU B 543     -12.799  35.840  69.831  1.00149.76           C  
ANISOU 9121  C   LEU B 543    19961  22646  14295    202   1744   1311       C  
ATOM   9122  O   LEU B 543     -12.772  36.996  70.253  1.00151.29           O  
ANISOU 9122  O   LEU B 543    20397  22641  14444    269   1822   1186       O  
ATOM   9123  CB  LEU B 543     -14.003  34.240  71.359  1.00145.66           C  
ANISOU 9123  CB  LEU B 543    19055  22657  13631    189   1731   1308       C  
ATOM   9124  CG  LEU B 543     -15.147  33.268  71.709  1.00149.82           C  
ANISOU 9124  CG  LEU B 543    19315  23510  14100    269   1739   1357       C  
ATOM   9125  CD1 LEU B 543     -14.703  32.264  72.754  1.00148.97           C  
ANISOU 9125  CD1 LEU B 543    19077  23590  13935     27   1683   1381       C  
ATOM   9126  CD2 LEU B 543     -16.393  34.005  72.187  1.00154.40           C  
ANISOU 9126  CD2 LEU B 543    19922  24174  14569    536   1853   1248       C  
ATOM   9127  N   ILE B 544     -11.747  35.249  69.209  1.00144.57           N  
ANISOU 9127  N   ILE B 544    19247  21955  13729    -12   1653   1405       N  
ATOM   9128  CA  ILE B 544     -10.442  35.888  68.952  1.00144.67           C  
ANISOU 9128  CA  ILE B 544    19458  21720  13788   -204   1636   1378       C  
ATOM   9129  C   ILE B 544     -10.601  37.112  68.029  1.00151.13           C  
ANISOU 9129  C   ILE B 544    20518  22256  14651    -38   1709   1383       C  
ATOM   9130  O   ILE B 544      -9.982  38.145  68.287  1.00151.98           O  
ANISOU 9130  O   ILE B 544    20884  22115  14747   -120   1757   1287       O  
ATOM   9131  CB  ILE B 544      -9.403  34.868  68.380  1.00145.33           C  
ANISOU 9131  CB  ILE B 544    19381  21879  13960   -433   1525   1488       C  
ATOM   9132  CG1 ILE B 544      -9.104  33.748  69.406  1.00144.75           C  
ANISOU 9132  CG1 ILE B 544    19113  22044  13843   -603   1452   1489       C  
ATOM   9133  CG2 ILE B 544      -8.095  35.563  67.937  1.00146.13           C  
ANISOU 9133  CG2 ILE B 544    19666  21748  14108   -624   1513   1469       C  
ATOM   9134  CD1 ILE B 544      -8.395  32.500  68.854  1.00149.22           C  
ANISOU 9134  CD1 ILE B 544    19468  22725  14502   -755   1345   1611       C  
ATOM   9135  N   TRP B 545     -11.431  36.999  66.977  1.00148.77           N  
ANISOU 9135  N   TRP B 545    20136  21995  14393    188   1717   1495       N  
ATOM   9136  CA  TRP B 545     -11.661  38.065  66.002  1.00150.76           C  
ANISOU 9136  CA  TRP B 545    20597  22004  14682    375   1778   1542       C  
ATOM   9137  C   TRP B 545     -12.521  39.194  66.559  1.00159.05           C  
ANISOU 9137  C   TRP B 545    21853  22911  15670    629   1889   1434       C  
ATOM   9138  O   TRP B 545     -12.391  40.337  66.116  1.00160.76           O  
ANISOU 9138  O   TRP B 545    22342  22827  15912    724   1954   1431       O  
ATOM   9139  CB  TRP B 545     -12.307  37.494  64.737  1.00148.44           C  
ANISOU 9139  CB  TRP B 545    20116  21854  14432    540   1741   1698       C  
ATOM   9140  CG  TRP B 545     -11.346  36.721  63.889  1.00147.44           C  
ANISOU 9140  CG  TRP B 545    19869  21770  14382    319   1653   1798       C  
ATOM   9141  CD1 TRP B 545     -11.312  35.370  63.707  1.00148.22           C  
ANISOU 9141  CD1 TRP B 545    19681  22124  14512    216   1569   1854       C  
ATOM   9142  CD2 TRP B 545     -10.238  37.254  63.154  1.00147.49           C  
ANISOU 9142  CD2 TRP B 545    20044  21554  14442    162   1646   1844       C  
ATOM   9143  NE1 TRP B 545     -10.266  35.030  62.882  1.00146.51           N  
ANISOU 9143  NE1 TRP B 545    19439  21863  14367     29   1511   1922       N  
ATOM   9144  CE2 TRP B 545      -9.590  36.168  62.527  1.00149.29           C  
ANISOU 9144  CE2 TRP B 545    20056  21940  14727    -13   1557   1920       C  
ATOM   9145  CE3 TRP B 545      -9.737  38.553  62.950  1.00150.74           C  
ANISOU 9145  CE3 TRP B 545    20772  21643  14859    149   1714   1826       C  
ATOM   9146  CZ2 TRP B 545      -8.469  36.339  61.708  1.00148.33           C  
ANISOU 9146  CZ2 TRP B 545    20005  21695  14656   -195   1533   1976       C  
ATOM   9147  CZ3 TRP B 545      -8.626  38.721  62.140  1.00151.94           C  
ANISOU 9147  CZ3 TRP B 545    21001  21665  15062    -53   1692   1893       C  
ATOM   9148  CH2 TRP B 545      -8.007  37.625  61.527  1.00150.39           C  
ANISOU 9148  CH2 TRP B 545    20566  21662  14911   -218   1602   1966       C  
ATOM   9149  N   ARG B 546     -13.400  38.874  67.510  1.00157.09           N  
ANISOU 9149  N   ARG B 546    21476  22874  15338    743   1916   1349       N  
ATOM   9150  CA  ARG B 546     -14.285  39.854  68.129  1.00160.04           C  
ANISOU 9150  CA  ARG B 546    22010  23156  15642   1003   2025   1225       C  
ATOM   9151  C   ARG B 546     -13.538  40.611  69.241  1.00166.48           C  
ANISOU 9151  C   ARG B 546    23071  23772  16413    826   2075   1039       C  
ATOM   9152  O   ARG B 546     -13.882  41.757  69.539  1.00168.56           O  
ANISOU 9152  O   ARG B 546    23586  23808  16653    999   2177    923       O  
ATOM   9153  CB  ARG B 546     -15.573  39.192  68.631  1.00160.52           C  
ANISOU 9153  CB  ARG B 546    21809  23561  15620   1197   2040   1207       C  
ATOM   9154  CG  ARG B 546     -16.474  38.711  67.483  1.00169.41           C  
ANISOU 9154  CG  ARG B 546    22729  24863  16778   1419   2011   1364       C  
ATOM   9155  CD  ARG B 546     -17.892  38.357  67.954  1.00176.47           C  
ANISOU 9155  CD  ARG B 546    23400  26073  17579   1658   2053   1325       C  
ATOM   9156  NE  ARG B 546     -18.596  37.470  67.015  1.00181.15           N  
ANISOU 9156  NE  ARG B 546    23705  26932  18190   1748   1996   1466       N  
ATOM   9157  CZ  ARG B 546     -19.724  37.770  66.370  1.00195.16           C  
ANISOU 9157  CZ  ARG B 546    25398  28819  19936   2077   2030   1513       C  
ATOM   9158  NH1 ARG B 546     -20.301  38.955  66.534  1.00186.68           N  
ANISOU 9158  NH1 ARG B 546    24515  27594  18822   2380   2123   1443       N  
ATOM   9159  NH2 ARG B 546     -20.279  36.886  65.551  1.00177.89           N  
ANISOU 9159  NH2 ARG B 546    22933  26899  17757   2108   1970   1625       N  
ATOM   9160  N   ARG B 547     -12.478  39.990  69.800  1.00162.54           N  
ANISOU 9160  N   ARG B 547    22503  23350  15903    483   2003   1010       N  
ATOM   9161  CA  ARG B 547     -11.609  40.572  70.829  1.00164.11           C  
ANISOU 9161  CA  ARG B 547    22897  23409  16048    256   2028    835       C  
ATOM   9162  C   ARG B 547     -10.639  41.574  70.185  1.00170.55           C  
ANISOU 9162  C   ARG B 547    24010  23848  16945    131   2053    828       C  
ATOM   9163  O   ARG B 547     -10.314  42.594  70.796  1.00172.49           O  
ANISOU 9163  O   ARG B 547    24525  23857  17158     72   2129    661       O  
ATOM   9164  CB  ARG B 547     -10.840  39.457  71.566  1.00162.32           C  
ANISOU 9164  CB  ARG B 547    22455  23444  15775    -49   1927    838       C  
ATOM   9165  CG  ARG B 547     -10.176  39.877  72.878  1.00175.20           C  
ANISOU 9165  CG  ARG B 547    24213  25055  17301   -262   1946    643       C  
ATOM   9166  CD  ARG B 547      -9.553  38.688  73.592  1.00184.29           C  
ANISOU 9166  CD  ARG B 547    25121  26507  18393   -514   1838    680       C  
ATOM   9167  NE  ARG B 547      -8.998  39.053  74.897  1.00193.89           N  
ANISOU 9167  NE  ARG B 547    26432  27759  19478   -706   1850    494       N  
ATOM   9168  CZ  ARG B 547      -9.666  38.988  76.046  1.00207.82           C  
ANISOU 9168  CZ  ARG B 547    28147  29717  21098   -640   1893    380       C  
ATOM   9169  NH1 ARG B 547     -10.927  38.572  76.067  1.00195.12           N  
ANISOU 9169  NH1 ARG B 547    26390  28284  19463   -391   1933    434       N  
ATOM   9170  NH2 ARG B 547      -9.079  39.342  77.181  1.00194.56           N  
ANISOU 9170  NH2 ARG B 547    26556  28079  19289   -833   1900    206       N  
ATOM   9171  N   THR B 548     -10.184  41.275  68.950  1.00166.75           N  
ANISOU 9171  N   THR B 548    23478  23317  16562     79   1996   1004       N  
ATOM   9172  CA  THR B 548      -9.275  42.119  68.165  1.00167.92           C  
ANISOU 9172  CA  THR B 548    23878  23137  16788    -51   2017   1038       C  
ATOM   9173  C   THR B 548     -10.061  43.303  67.553  1.00175.51           C  
ANISOU 9173  C   THR B 548    25104  23799  17782    262   2126   1061       C  
ATOM   9174  O   THR B 548      -9.467  44.350  67.278  1.00176.98           O  
ANISOU 9174  O   THR B 548    25597  23636  18010    180   2187   1031       O  
ATOM   9175  CB  THR B 548      -8.555  41.260  67.105  1.00172.62           C  
ANISOU 9175  CB  THR B 548    24286  23844  17459   -212   1917   1217       C  
ATOM   9176  OG1 THR B 548      -8.134  40.032  67.704  1.00169.08           O  
ANISOU 9176  OG1 THR B 548    23558  23704  16981   -407   1818   1211       O  
ATOM   9177  CG2 THR B 548      -7.346  41.961  66.497  1.00172.17           C  
ANISOU 9177  CG2 THR B 548    24445  23514  17459   -451   1927   1236       C  
ATOM   9178  N   TRP B 549     -11.391  43.128  67.355  1.00173.27           N  
ANISOU 9178  N   TRP B 549    24699  23660  17478    617   2150   1117       N  
ATOM   9179  CA  TRP B 549     -12.320  44.139  66.827  1.00175.38           C  
ANISOU 9179  CA  TRP B 549    25169  23704  17763    983   2244   1151       C  
ATOM   9180  C   TRP B 549     -12.418  45.326  67.800  1.00182.42           C  
ANISOU 9180  C   TRP B 549    26378  24312  18620   1046   2362    937       C  
ATOM   9181  O   TRP B 549     -12.362  46.483  67.372  1.00184.50           O  
ANISOU 9181  O   TRP B 549    26969  24196  18937   1156   2445    941       O  
ATOM   9182  CB  TRP B 549     -13.708  43.506  66.582  1.00173.18           C  
ANISOU 9182  CB  TRP B 549    24616  23739  17445   1321   2230   1233       C  
ATOM   9183  CG  TRP B 549     -14.811  44.478  66.261  1.00176.85           C  
ANISOU 9183  CG  TRP B 549    25243  24047  17904   1745   2325   1246       C  
ATOM   9184  CD1 TRP B 549     -15.775  44.931  67.113  1.00181.78           C  
ANISOU 9184  CD1 TRP B 549    25905  24703  18462   2008   2410   1099       C  
ATOM   9185  CD2 TRP B 549     -15.076  45.092  64.989  1.00178.14           C  
ANISOU 9185  CD2 TRP B 549    25540  24019  18125   1973   2343   1423       C  
ATOM   9186  NE1 TRP B 549     -16.619  45.797  66.456  1.00184.05           N  
ANISOU 9186  NE1 TRP B 549    26341  24820  18769   2401   2479   1170       N  
ATOM   9187  CE2 TRP B 549     -16.214  45.914  65.151  1.00185.60           C  
ANISOU 9187  CE2 TRP B 549    26603  24876  19039   2388   2437   1379       C  
ATOM   9188  CE3 TRP B 549     -14.457  45.033  63.728  1.00178.59           C  
ANISOU 9188  CE3 TRP B 549    25626  23983  18247   1872   2290   1619       C  
ATOM   9189  CZ2 TRP B 549     -16.747  46.671  64.099  1.00187.53           C  
ANISOU 9189  CZ2 TRP B 549    26999  24936  19319   2715   2472   1538       C  
ATOM   9190  CZ3 TRP B 549     -14.986  45.783  62.687  1.00182.29           C  
ANISOU 9190  CZ3 TRP B 549    26245  24278  18739   2176   2328   1777       C  
ATOM   9191  CH2 TRP B 549     -16.117  46.590  62.877  1.00186.06           C  
ANISOU 9191  CH2 TRP B 549    26843  24663  19188   2597   2414   1744       C  
ATOM   9192  N   CYS B 550     -12.544  45.022  69.108  1.00178.68           N  
ANISOU 9192  N   CYS B 550    25812  24023  18055    966   2371    751       N  
ATOM   9193  CA  CYS B 550     -12.618  45.987  70.204  1.00181.27           C  
ANISOU 9193  CA  CYS B 550    26396  24151  18326    990   2477    506       C  
ATOM   9194  C   CYS B 550     -11.287  46.746  70.324  1.00185.81           C  
ANISOU 9194  C   CYS B 550    27271  24386  18942    649   2498    410       C  
ATOM   9195  O   CYS B 550     -11.289  47.954  70.568  1.00189.12           O  
ANISOU 9195  O   CYS B 550    28036  24442  19379    717   2609    272       O  
ATOM   9196  CB  CYS B 550     -12.976  45.275  71.507  1.00181.20           C  
ANISOU 9196  CB  CYS B 550    26160  24499  18188    938   2462    356       C  
ATOM   9197  SG  CYS B 550     -13.212  46.381  72.922  1.00189.01           S  
ANISOU 9197  SG  CYS B 550    27425  25313  19078    994   2598     27       S  
ATOM   9198  N   ARG B 551     -10.163  46.025  70.127  1.00178.88           N  
ANISOU 9198  N   ARG B 551    26256  23629  18082    285   2393    483       N  
ATOM   9199  CA  ARG B 551      -8.784  46.516  70.175  1.00201.30           C  
ANISOU 9199  CA  ARG B 551    29296  26237  20950    -95   2389    412       C  
ATOM   9200  C   ARG B 551      -8.535  47.568  69.083  1.00209.62           C  
ANISOU 9200  C   ARG B 551    30671  26862  22114    -45   2459    513       C  
ATOM   9201  O   ARG B 551      -9.099  47.483  67.995  1.00160.61           O  
ANISOU 9201  O   ARG B 551    24421  20637  15967    197   2452    719       O  
ATOM   9202  CB  ARG B 551      -7.825  45.321  70.015  1.00196.38           C  
ANISOU 9202  CB  ARG B 551    28377  25913  20324   -414   2250    516       C  
ATOM   9203  CG  ARG B 551      -6.338  45.647  70.004  1.00208.58           C  
ANISOU 9203  CG  ARG B 551    30053  27307  21889   -827   2227    461       C  
ATOM   9204  CD  ARG B 551      -5.558  44.475  69.444  1.00217.47           C  
ANISOU 9204  CD  ARG B 551    30878  28709  23044  -1036   2094    622       C  
ATOM   9205  NE  ARG B 551      -4.184  44.841  69.100  1.00229.93           N  
ANISOU 9205  NE  ARG B 551    32571  30136  24656  -1392   2078    613       N  
ATOM   9206  CZ  ARG B 551      -3.372  44.099  68.353  1.00243.75           C  
ANISOU 9206  CZ  ARG B 551    34126  32036  26451  -1574   1987    757       C  
ATOM   9207  NH1 ARG B 551      -3.790  42.942  67.852  1.00228.47           N  
ANISOU 9207  NH1 ARG B 551    31886  30381  24541  -1433   1902    919       N  
ATOM   9208  NH2 ARG B 551      -2.139  44.512  68.093  1.00232.63           N  
ANISOU 9208  NH2 ARG B 551    32824  30502  25062  -1902   1984    731       N  
TER    9209      ARG B 551                                                      
HETATM 9210  C1  NAG A1201     -51.939  15.709 102.910  1.00149.67           C  
HETATM 9211  C2  NAG A1201     -52.443  15.896 101.475  1.00150.82           C  
HETATM 9212  C3  NAG A1201     -53.328  17.144 101.433  1.00152.76           C  
HETATM 9213  C4  NAG A1201     -54.443  17.061 102.474  1.00152.59           C  
HETATM 9214  C5  NAG A1201     -53.854  16.828 103.867  1.00152.77           C  
HETATM 9215  C6  NAG A1201     -54.903  16.614 104.939  1.00153.49           C  
HETATM 9216  C7  NAG A1201     -51.316  15.307  99.355  1.00148.45           C  
HETATM 9217  C8  NAG A1201     -50.180  15.639  98.433  1.00148.21           C  
HETATM 9218  N2  NAG A1201     -51.362  16.002 100.505  1.00149.30           N  
HETATM 9219  O3  NAG A1201     -53.891  17.285 100.132  1.00153.97           O  
HETATM 9220  O4  NAG A1201     -55.215  18.259 102.453  1.00151.98           O  
HETATM 9221  O5  NAG A1201     -53.021  15.651 103.850  1.00151.56           O  
HETATM 9222  O6  NAG A1201     -54.323  16.295 106.199  1.00153.97           O  
HETATM 9223  O7  NAG A1201     -52.151  14.452  99.071  1.00148.36           O  
HETATM 9224  C1  NAG A1202     -28.291  -0.690  95.413  1.00171.00           C  
HETATM 9225  C2  NAG A1202     -27.383  -1.172  94.279  1.00172.45           C  
HETATM 9226  C3  NAG A1202     -28.137  -2.160  93.391  1.00173.36           C  
HETATM 9227  C4  NAG A1202     -28.706  -3.301  94.228  1.00174.16           C  
HETATM 9228  C5  NAG A1202     -29.618  -2.738  95.319  1.00172.92           C  
HETATM 9229  C6  NAG A1202     -30.126  -3.788  96.281  1.00172.71           C  
HETATM 9230  C7  NAG A1202     -25.573   0.037  93.119  1.00173.53           C  
HETATM 9231  C8  NAG A1202     -25.256   1.136  92.150  1.00173.51           C  
HETATM 9232  N2  NAG A1202     -26.860  -0.070  93.486  1.00172.90           N  
HETATM 9233  O3  NAG A1202     -27.264  -2.669  92.387  1.00173.13           O  
HETATM 9234  O4  NAG A1202     -29.426  -4.200  93.392  1.00175.59           O  
HETATM 9235  O5  NAG A1202     -28.890  -1.786  96.115  1.00171.86           O  
HETATM 9236  O6  NAG A1202     -31.217  -4.512  95.737  1.00172.54           O  
HETATM 9237  O7  NAG A1202     -24.706  -0.724  93.543  1.00173.91           O  
HETATM 9238  C1  CLR A1203     -34.388  -3.374 103.675  1.00 77.39           C  
ANISOU 9238  C1  CLR A1203     9015  10221  10168   -535    168    755       C  
HETATM 9239  C2  CLR A1203     -34.048  -4.221 104.911  1.00 76.36           C  
ANISOU 9239  C2  CLR A1203     8848  10121  10044   -535    173    763       C  
HETATM 9240  C3  CLR A1203     -34.461  -5.697 104.804  1.00 76.82           C  
ANISOU 9240  C3  CLR A1203     8878  10188  10124   -522    176    776       C  
HETATM 9241  C4  CLR A1203     -34.010  -6.353 103.491  1.00 78.16           C  
ANISOU 9241  C4  CLR A1203     9061  10338  10299   -529    186    778       C  
HETATM 9242  C5  CLR A1203     -34.211  -5.455 102.275  1.00 80.06           C  
ANISOU 9242  C5  CLR A1203     9343  10553  10523   -532    177    766       C  
HETATM 9243  C6  CLR A1203     -34.654  -6.069 101.148  1.00 81.40           C  
ANISOU 9243  C6  CLR A1203     9524  10709  10694   -530    175    763       C  
HETATM 9244  C7  CLR A1203     -34.947  -5.361  99.831  1.00 82.45           C  
ANISOU 9244  C7  CLR A1203     9687  10829  10812   -533    168    756       C  
HETATM 9245  C8  CLR A1203     -34.339  -3.954  99.803  1.00 82.97           C  
ANISOU 9245  C8  CLR A1203     9762  10893  10870   -537    169    757       C  
HETATM 9246  C9  CLR A1203     -34.624  -3.240 101.153  1.00 82.14           C  
ANISOU 9246  C9  CLR A1203     9649  10794  10768   -535    166    756       C  
HETATM 9247  C10 CLR A1203     -33.897  -3.944 102.328  1.00 80.10           C  
ANISOU 9247  C10 CLR A1203     9367  10552  10514   -539    173    760       C  
HETATM 9248  C11 CLR A1203     -34.332  -1.716 101.126  1.00 83.08           C  
ANISOU 9248  C11 CLR A1203     9778  10903  10884   -539    168    752       C  
HETATM 9249  C12 CLR A1203     -34.575  -0.978  99.797  1.00 84.18           C  
ANISOU 9249  C12 CLR A1203     9925  11034  11025   -538    169    757       C  
HETATM 9250  C13 CLR A1203     -34.102  -1.710  98.527  1.00 84.47           C  
ANISOU 9250  C13 CLR A1203     9965  11074  11056   -537    168    761       C  
HETATM 9251  C14 CLR A1203     -34.768  -3.091  98.602  1.00 84.16           C  
ANISOU 9251  C14 CLR A1203     9926  11038  11014   -537    165    758       C  
HETATM 9252  C15 CLR A1203     -34.636  -3.667  97.191  1.00 84.88           C  
ANISOU 9252  C15 CLR A1203    10026  11129  11094   -539    166    757       C  
HETATM 9253  C16 CLR A1203     -34.737  -2.432  96.295  1.00 84.84           C  
ANISOU 9253  C16 CLR A1203    10018  11130  11087   -537    165    765       C  
HETATM 9254  C17 CLR A1203     -34.753  -1.197  97.216  1.00 85.32           C  
ANISOU 9254  C17 CLR A1203    10071  11186  11162   -535    168    769       C  
HETATM 9255  C18 CLR A1203     -32.551  -1.738  98.465  1.00 84.25           C  
ANISOU 9255  C18 CLR A1203     9938  11044  11029   -537    173    768       C  
HETATM 9256  C19 CLR A1203     -32.371  -3.752 102.224  1.00 80.07           C  
ANISOU 9256  C19 CLR A1203     9365  10551  10506   -553    183    769       C  
HETATM 9257  C20 CLR A1203     -34.244   0.109  96.545  1.00 86.90           C  
ANISOU 9257  C20 CLR A1203    10259  11387  11374   -529    172    779       C  
HETATM 9258  C21 CLR A1203     -34.208   1.362  97.431  1.00 87.51           C  
ANISOU 9258  C21 CLR A1203    10329  11453  11469   -530    179    778       C  
HETATM 9259  C22 CLR A1203     -35.142   0.468  95.363  1.00 87.04           C  
ANISOU 9259  C22 CLR A1203    10261  11420  11389   -531    176    793       C  
HETATM 9260  C23 CLR A1203     -34.365   0.700  94.072  1.00 86.36           C  
ANISOU 9260  C23 CLR A1203    10161  11349  11303   -520    176    803       C  
HETATM 9261  C24 CLR A1203     -35.349   0.869  92.919  1.00 86.36           C  
ANISOU 9261  C24 CLR A1203    10141  11376  11296   -528    179    819       C  
HETATM 9262  C25 CLR A1203     -35.454   2.328  92.493  1.00 86.77           C  
ANISOU 9262  C25 CLR A1203    10151  11441  11377   -520    194    844       C  
HETATM 9263  C26 CLR A1203     -35.379   2.485  90.982  1.00 88.46           C  
ANISOU 9263  C26 CLR A1203    10332  11693  11585   -514    195    864       C  
HETATM 9264  C27 CLR A1203     -36.664   3.042  93.079  1.00 85.41           C  
ANISOU 9264  C27 CLR A1203     9968  11264  11221   -534    211    861       C  
HETATM 9265  O1  CLR A1203     -33.904  -6.425 105.909  1.00 75.83           O  
ANISOU 9265  O1  CLR A1203     8706  10097  10010   -524    188    792       O  
HETATM 9266 NA    NA A1204     -37.899 -10.631 114.482  1.00105.52          NA1+
HETATM 9267 NA    NA A1205     -49.236   9.951  67.190  1.00 71.25          NA1+
CONECT   51  928                                                                
CONECT   89  575                                                                
CONECT  157  521                                                                
CONECT  235 9266                                                                
CONECT  258 9266                                                                
CONECT  275 9266                                                                
CONECT  449  729                                                                
CONECT  521  157                                                                
CONECT  575   89                                                                
CONECT  680  858                                                                
CONECT  729  449                                                                
CONECT  858  680                                                                
CONECT  928   51                                                                
CONECT 1012 9210                                                                
CONECT 1043 1206                                                                
CONECT 1206 1043                                                                
CONECT 1233 1852                                                                
CONECT 1852 1233                                                                
CONECT 1931 9267                                                                
CONECT 1991 2558                                                                
CONECT 2558 1991                                                                
CONECT 4133 4257                                                                
CONECT 4155 9224                                                                
CONECT 4257 4133                                                                
CONECT 4692 5569                                                                
CONECT 4730 5216                                                                
CONECT 4798 5162                                                                
CONECT 5090 5370                                                                
CONECT 5162 4798                                                                
CONECT 5216 4730                                                                
CONECT 5321 5499                                                                
CONECT 5370 5090                                                                
CONECT 5499 5321                                                                
CONECT 5569 4692                                                                
CONECT 5684 5847                                                                
CONECT 5847 5684                                                                
CONECT 5874 6493                                                                
CONECT 6493 5874                                                                
CONECT 6632 7229                                                                
CONECT 7229 6632                                                                
CONECT 8825 8840                                                                
CONECT 8840 8825                                                                
CONECT 9210 1012 9211 9221                                                      
CONECT 9211 9210 9212 9218                                                      
CONECT 9212 9211 9213 9219                                                      
CONECT 9213 9212 9214 9220                                                      
CONECT 9214 9213 9215 9221                                                      
CONECT 9215 9214 9222                                                           
CONECT 9216 9217 9218 9223                                                      
CONECT 9217 9216                                                                
CONECT 9218 9211 9216                                                           
CONECT 9219 9212                                                                
CONECT 9220 9213                                                                
CONECT 9221 9210 9214                                                           
CONECT 9222 9215                                                                
CONECT 9223 9216                                                                
CONECT 9224 4155 9225 9235                                                      
CONECT 9225 9224 9226 9232                                                      
CONECT 9226 9225 9227 9233                                                      
CONECT 9227 9226 9228 9234                                                      
CONECT 9228 9227 9229 9235                                                      
CONECT 9229 9228 9236                                                           
CONECT 9230 9231 9232 9237                                                      
CONECT 9231 9230                                                                
CONECT 9232 9225 9230                                                           
CONECT 9233 9226                                                                
CONECT 9234 9227                                                                
CONECT 9235 9224 9228                                                           
CONECT 9236 9229                                                                
CONECT 9237 9230                                                                
CONECT 9238 9239 9247                                                           
CONECT 9239 9238 9240                                                           
CONECT 9240 9239 9241 9265                                                      
CONECT 9241 9240 9242                                                           
CONECT 9242 9241 9243 9247                                                      
CONECT 9243 9242 9244                                                           
CONECT 9244 9243 9245                                                           
CONECT 9245 9244 9246 9251                                                      
CONECT 9246 9245 9247 9248                                                      
CONECT 9247 9238 9242 9246 9256                                                 
CONECT 9248 9246 9249                                                           
CONECT 9249 9248 9250                                                           
CONECT 9250 9249 9251 9254 9255                                                 
CONECT 9251 9245 9250 9252                                                      
CONECT 9252 9251 9253                                                           
CONECT 9253 9252 9254                                                           
CONECT 9254 9250 9253 9257                                                      
CONECT 9255 9250                                                                
CONECT 9256 9247                                                                
CONECT 9257 9254 9258 9259                                                      
CONECT 9258 9257                                                                
CONECT 9259 9257 9260                                                           
CONECT 9260 9259 9261                                                           
CONECT 9261 9260 9262                                                           
CONECT 9262 9261 9263 9264                                                      
CONECT 9263 9262                                                                
CONECT 9264 9262                                                                
CONECT 9265 9240                                                                
CONECT 9266  235  258  275                                                      
CONECT 9267 1931                                                                
MASTER      533    0    5   48   20    0    0    6 9265    2  100  100          
END