HEADER    MEMBRANE PROTEIN                        29-NOV-18   6IBB              
TITLE     CRYSTAL STRUCTURE OF THE RAT ISOFORM OF THE SUCCINATE RECEPTOR SUCNR1 
TITLE    2 (GPR91) IN COMPLEX WITH A NANOBODY                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINATE RECEPTOR 1;                                      
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: G-PROTEIN COUPLED RECEPTOR 91;                              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: NANOBODY6;                                                 
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: SUCNR1, GPR91;                                                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: VICUGNA PACOS;                                  
SOURCE  11 ORGANISM_COMMON: ALPACA;                                             
SOURCE  12 ORGANISM_TAXID: 30538;                                               
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    SUCNR1 GPR91 GPCR G-PROTEIN COUPLED RECEPTOR NANOBODY SUCCINATE       
KEYWDS   2 COMPLEX, MEMBRANE PROTEIN                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.HAFFKE,V.-P.JAAKOLA                                                 
REVDAT   3   06-NOV-19 6IBB    1       JRNL                                     
REVDAT   2   16-OCT-19 6IBB    1       JRNL                                     
REVDAT   1   14-AUG-19 6IBB    0                                                
JRNL        AUTH   M.HAFFKE,D.FEHLMANN,G.RUMMEL,J.BOIVINEAU,M.DUCKELY,          
JRNL        AUTH 2 N.GOMMERMANN,S.COTESTA,F.SIROCKIN,F.FREULER,                 
JRNL        AUTH 3 A.LITTLEWOOD-EVANS,K.KAUPMANN,V.P.JAAKOLA                    
JRNL        TITL   STRUCTURAL BASIS OF SPECIES-SELECTIVE ANTAGONIST BINDING TO  
JRNL        TITL 2 THE SUCCINATE RECEPTOR.                                      
JRNL        REF    NATURE                        V. 574   581 2019              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   31645725                                                     
JRNL        DOI    10.1038/S41586-019-1663-8                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.12 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
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) : 2.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 61.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 41256                          
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)  : 0.180                          
REMARK   3   R VALUE            (WORKING SET)  : 0.178                          
REMARK   3   FREE R VALUE                      : 0.216                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.730                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1950                           
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               : 50                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.12                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.27                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 6.86                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 826                      
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2316                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 787                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2309                   
REMARK   3   BIN FREE R VALUE                        : 0.2466                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.72                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : NULL                     
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            : 6643                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 374                                     
REMARK   3   SOLVENT ATOMS            : 299                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.21                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.45670                                             
REMARK   3    B22 (A**2) : -10.16440                                            
REMARK   3    B33 (A**2) : -1.29230                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.49840                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.280               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.331               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.221               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.347               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.227               
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      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7186   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9677   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2506   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 1133   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7186   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 907    ; 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   : 8266   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.08                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.89                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.60                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   76.2712   10.0708   30.8709           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0782 T22:   -0.2260                                    
REMARK   3     T33:   -0.1257 T12:    0.0126                                    
REMARK   3     T13:    0.0226 T23:   -0.0078                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2001 L22:    3.0482                                    
REMARK   3     L33:    1.4525 L12:    0.8791                                    
REMARK   3     L13:    0.1261 L23:    0.5949                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0057 S12:   -0.0655 S13:    0.0260                     
REMARK   3     S21:    0.1122 S22:    0.0035 S23:   -0.1065                     
REMARK   3     S31:    0.0885 S32:    0.0140 S33:    0.0023                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   87.2887   49.5906   34.9085           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0834 T22:   -0.3455                                    
REMARK   3     T33:   -0.1185 T12:   -0.1196                                    
REMARK   3     T13:    0.0069 T23:    0.0701                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1869 L22:    7.8471                                    
REMARK   3     L33:    3.8511 L12:   -0.6667                                    
REMARK   3     L13:    0.4028 L23:    3.5264                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1365 S12:    0.1764 S13:    0.1376                     
REMARK   3     S21:   -0.4869 S22:    0.0865 S23:   -0.2175                     
REMARK   3     S31:   -0.4940 S32:    0.1318 S33:    0.0499                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   70.3630    6.2272   -2.1961           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0134 T22:   -0.3212                                    
REMARK   3     T33:   -0.2515 T12:    0.0007                                    
REMARK   3     T13:    0.0882 T23:    0.0146                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9107 L22:    4.8875                                    
REMARK   3     L33:    3.0430 L12:    0.3683                                    
REMARK   3     L13:    0.1601 L23:   -0.0312                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0419 S12:    0.0215 S13:    0.1142                     
REMARK   3     S21:   -0.3592 S22:    0.1250 S23:    0.2289                     
REMARK   3     S31:   -0.5902 S32:   -0.1688 S33:   -0.0832                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   65.3738  -33.5554   -1.2745           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2545 T22:   -0.3994                                    
REMARK   3     T33:   -0.1901 T12:   -0.1837                                    
REMARK   3     T13:   -0.0880 T23:   -0.0750                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.3629 L22:   10.3437                                    
REMARK   3     L33:    4.7678 L12:   -0.5907                                    
REMARK   3     L13:    1.2632 L23:   -1.6151                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1299 S12:    0.2370 S13:   -0.4591                     
REMARK   3     S21:   -0.3932 S22:    0.2344 S23:    0.7649                     
REMARK   3     S31:    1.0220 S32:   -0.4381 S33:   -0.3644                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6IBB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200013156.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.00                             
REMARK 200  PH                             : 4.8-5.4                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS BUILT 20160617                 
REMARK 200  DATA SCALING SOFTWARE          : XSCALE BUILT 20160617              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 198484                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.420                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.2                               
REMARK 200  DATA REDUNDANCY                : 17.88                              
REMARK 200  R MERGE                    (I) : 0.76300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2.9200                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 20.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.59                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.11900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.320                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.8.0                                          
REMARK 200 STARTING MODEL: 4XNV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA-CITRATE 24-30% PEG400 0.05M      
REMARK 280  NASCN 2.5% 2,5-HEXANEDIOL 1% DMSO, LIPIDIC CUBIC PHASE,             
REMARK 280  TEMPERATURE 293.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       82.00000            
REMARK 290   SMTRY3   2  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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     ASP A    -6                                                      
REMARK 465     TYR A    -5                                                      
REMARK 465     LYS A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     ASP A     0                                                      
REMARK 465     LYS A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     THR A   160                                                      
REMARK 465     PRO A   161                                                      
REMARK 465     ILE A   162                                                      
REMARK 465     GLU A   163                                                      
REMARK 465     LYS A   164                                                      
REMARK 465     GLY A   165                                                      
REMARK 465     ASP A   166                                                      
REMARK 465     SER A   214                                                      
REMARK 465     GLN A   215                                                      
REMARK 465     GLN A   216                                                      
REMARK 465     GLN A   217                                                      
REMARK 465     ALA A   218                                                      
REMARK 465     THR A   219                                                      
REMARK 465     VAL A   220                                                      
REMARK 465     LEU A   221                                                      
REMARK 465     SER A   222                                                      
REMARK 465     LEU A   223                                                      
REMARK 465     GLY A   324                                                      
REMARK 465     PRO A   325                                                      
REMARK 465     HIS A   326                                                      
REMARK 465     HIS A   327                                                      
REMARK 465     HIS A   328                                                      
REMARK 465     HIS A   329                                                      
REMARK 465     HIS A   330                                                      
REMARK 465     HIS A   331                                                      
REMARK 465     HIS A   332                                                      
REMARK 465     HIS A   333                                                      
REMARK 465     HIS A   334                                                      
REMARK 465     HIS A   335                                                      
REMARK 465     ASP B     1                                                      
REMARK 465     TYR B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     ASP C    -6                                                      
REMARK 465     TYR C    -5                                                      
REMARK 465     LYS C    -4                                                      
REMARK 465     ASP C    -3                                                      
REMARK 465     ASP C    -2                                                      
REMARK 465     ASP C    -1                                                      
REMARK 465     ASP C     0                                                      
REMARK 465     LYS C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 465     ASN C     4                                                      
REMARK 465     LEU C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     PRO C   161                                                      
REMARK 465     ILE C   162                                                      
REMARK 465     GLU C   163                                                      
REMARK 465     LYS C   164                                                      
REMARK 465     GLY C   165                                                      
REMARK 465     ALA C   218                                                      
REMARK 465     THR C   219                                                      
REMARK 465     VAL C   220                                                      
REMARK 465     LEU C   221                                                      
REMARK 465     SER C   222                                                      
REMARK 465     LEU C   223                                                      
REMARK 465     PRO C   260                                                      
REMARK 465     GLN C   261                                                      
REMARK 465     LEU C   305                                                      
REMARK 465     ARG C   306                                                      
REMARK 465     GLN C   307                                                      
REMARK 465     TYR C   308                                                      
REMARK 465     PHE C   309                                                      
REMARK 465     LYS C   310                                                      
REMARK 465     SER C   311                                                      
REMARK 465     LEU C   312                                                      
REMARK 465     THR C   313                                                      
REMARK 465     SER C   314                                                      
REMARK 465     PHE C   315                                                      
REMARK 465     ARG C   316                                                      
REMARK 465     LEU C   317                                                      
REMARK 465     LEU C   318                                                      
REMARK 465     GLU C   319                                                      
REMARK 465     VAL C   320                                                      
REMARK 465     LEU C   321                                                      
REMARK 465     PHE C   322                                                      
REMARK 465     GLN C   323                                                      
REMARK 465     GLY C   324                                                      
REMARK 465     PRO C   325                                                      
REMARK 465     HIS C   326                                                      
REMARK 465     HIS C   327                                                      
REMARK 465     HIS C   328                                                      
REMARK 465     HIS C   329                                                      
REMARK 465     HIS C   330                                                      
REMARK 465     HIS C   331                                                      
REMARK 465     HIS C   332                                                      
REMARK 465     HIS C   333                                                      
REMARK 465     HIS C   334                                                      
REMARK 465     HIS C   335                                                      
REMARK 465     ASP D     1                                                      
REMARK 465     TYR D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     ASP D     5                                                      
REMARK 465     ASP D     6                                                      
REMARK 465     ASP D     7                                                      
REMARK 465     LYS D     8                                                      
REMARK 465     SER D    33                                                      
REMARK 465     GLY D    34                                                      
REMARK 465     TYR D    35                                                      
REMARK 465     THR D    36                                                      
REMARK 465     LYS D    82A                                                     
REMARK 465     SER D   136                                                      
REMARK 465     LEU D   137                                                      
REMARK 465     GLU D   138                                                      
REMARK 465     VAL D   139                                                      
REMARK 465     LEU D   140                                                      
REMARK 465     PHE D   141                                                      
REMARK 465     GLN D   142                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 159    OG                                                  
REMARK 470     LYS A 178    CG   CD   CE   NZ                                   
REMARK 470     ASN A 224    CG   OD1  ND2                                       
REMARK 470     LYS A 304    CG   CD   CE   NZ                                   
REMARK 470     LYS A 310    CG   CD   CE   NZ                                   
REMARK 470     GLN A 323    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  31    CG   CD   OE1  OE2                                  
REMARK 470     TYR B  35    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN C  15    CG   OD1  ND2                                       
REMARK 470     SER C  78    OG                                                  
REMARK 470     SER C 159    OG                                                  
REMARK 470     THR C 160    OG1  CG2                                            
REMARK 470     LYS C 178    CG   CD   CE   NZ                                   
REMARK 470     LYS C 211    CG   CD   CE   NZ                                   
REMARK 470     LYS C 212    CG   CD   CE   NZ                                   
REMARK 470     GLN C 215    CG   CD   OE1  NE2                                  
REMARK 470     GLN C 216    CG   CD   OE1  NE2                                  
REMARK 470     GLN C 217    CG   CD   OE1  NE2                                  
REMARK 470     ASN C 224    CG   OD1  ND2                                       
REMARK 470     SER C 258    OG                                                  
REMARK 470     TRP C 259    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C 259    CZ3  CH2                                            
REMARK 470     GLN C 265    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 304    CG   CD   CE   NZ                                   
REMARK 470     GLU D  31    CG   CD   OE1  OE2                                  
REMARK 470     LEU D  37    CG   CD1  CD2                                       
REMARK 470     GLU D  52    CG   CD   OE1  OE2                                  
REMARK 470     ILE D  85    CG1  CG2  CD1                                       
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    ALA B  32       73.83   -118.90                                   
REMARK 500    SER B  33      -44.84    -16.31                                   
REMARK 500    ARG B  74      -34.58   -144.47                                   
REMARK 500    LYS B  83       63.09     60.94                                   
REMARK 500    ASP B 115       75.68   -150.54                                   
REMARK 500    GLN C 216      -67.74    -94.84                                   
REMARK 500    LEU C 256     -103.18    -82.82                                   
REMARK 500    SER D  15      -20.68   -147.32                                   
REMARK 500    ALA D  38      -63.13    -29.88                                   
REMARK 500    ARG D  74      -10.36   -140.61                                   
REMARK 500    ASN D  81      -26.76     90.37                                   
REMARK 500    ALA D  82       46.05    -86.16                                   
REMARK 500    LYS D  83       -9.52     96.66                                   
REMARK 500    ARG D 111      -69.90    -95.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 624        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH C 582        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH C 583        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH D 235        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH D 236        DISTANCE =  5.89 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLC A  401                                                       
REMARK 610     OLC A  402                                                       
REMARK 610     OLC A  404                                                       
REMARK 610     OLC A  408                                                       
REMARK 610     OLC C  401                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H95 A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC C 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC C 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC C 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC C 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC C 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 409                 
DBREF  6IBB A    2   317  UNP    Q6IYF9   SUCR1_RAT        2    317             
DBREF  6IBB B    1   142  PDB    6IBB     6IBB             1    142             
DBREF  6IBB C    2   317  UNP    Q6IYF9   SUCR1_RAT        2    317             
DBREF  6IBB D    1   142  PDB    6IBB     6IBB             1    142             
SEQADV 6IBB ASP A   -6  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB TYR A   -5  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB LYS A   -4  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB ASP A   -3  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB ASP A   -2  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB ASP A   -1  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB ASP A    0  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB LYS A    1  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB LEU A  318  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB GLU A  319  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB VAL A  320  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB LEU A  321  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB PHE A  322  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB GLN A  323  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB GLY A  324  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB PRO A  325  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS A  326  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS A  327  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS A  328  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS A  329  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS A  330  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS A  331  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS A  332  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS A  333  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS A  334  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS A  335  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB ASP C   -6  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB TYR C   -5  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB LYS C   -4  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB ASP C   -3  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB ASP C   -2  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB ASP C   -1  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB ASP C    0  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB LYS C    1  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB LEU C  318  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB GLU C  319  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB VAL C  320  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB LEU C  321  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB PHE C  322  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB GLN C  323  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB GLY C  324  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB PRO C  325  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS C  326  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS C  327  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS C  328  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS C  329  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS C  330  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS C  331  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS C  332  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS C  333  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS C  334  UNP  Q6IYF9              EXPRESSION TAG                 
SEQADV 6IBB HIS C  335  UNP  Q6IYF9              EXPRESSION TAG                 
SEQRES   1 A  342  ASP TYR LYS ASP ASP ASP ASP LYS ALA GLN ASN LEU SER          
SEQRES   2 A  342  CYS GLU ASN TRP LEU ALA LEU GLU ASN ILE LEU LYS LYS          
SEQRES   3 A  342  TYR TYR LEU SER ALA PHE TYR GLY ILE GLU PHE ILE VAL          
SEQRES   4 A  342  GLY MET LEU GLY ASN PHE THR VAL VAL PHE GLY TYR LEU          
SEQRES   5 A  342  PHE CYS MET LYS ASN TRP ASN SER SER ASN VAL TYR LEU          
SEQRES   6 A  342  PHE ASN LEU SER ILE SER ASP LEU ALA PHE LEU CYS THR          
SEQRES   7 A  342  LEU PRO MET LEU ILE ARG SER TYR ALA THR GLY ASN TRP          
SEQRES   8 A  342  THR TYR GLY ASP VAL LEU CYS ILE SER ASN ARG TYR VAL          
SEQRES   9 A  342  LEU HIS ALA ASN LEU TYR THR SER ILE LEU PHE LEU THR          
SEQRES  10 A  342  PHE ILE SER ILE ASP ARG TYR LEU LEU MET LYS PHE PRO          
SEQRES  11 A  342  PHE ARG GLU HIS ILE LEU GLN LYS LYS GLU PHE ALA ILE          
SEQRES  12 A  342  LEU ILE SER LEU ALA VAL TRP VAL LEU VAL THR LEU GLU          
SEQRES  13 A  342  VAL LEU PRO MET LEU THR PHE ILE THR SER THR PRO ILE          
SEQRES  14 A  342  GLU LYS GLY ASP SER CYS VAL ASP TYR ALA SER SER GLY          
SEQRES  15 A  342  ASN PRO LYS TYR SER LEU ILE TYR SER LEU CYS LEU THR          
SEQRES  16 A  342  LEU LEU GLY PHE LEU ILE PRO LEU SER VAL MET CYS PHE          
SEQRES  17 A  342  PHE TYR TYR LYS MET VAL VAL PHE LEU LYS LYS ARG SER          
SEQRES  18 A  342  GLN GLN GLN ALA THR VAL LEU SER LEU ASN LYS PRO LEU          
SEQRES  19 A  342  ARG LEU VAL VAL LEU ALA VAL VAL ILE PHE SER VAL LEU          
SEQRES  20 A  342  PHE THR PRO TYR HIS ILE MET ARG ASN VAL ARG ILE ALA          
SEQRES  21 A  342  SER ARG LEU ASP SER TRP PRO GLN GLY CYS SER GLN LYS          
SEQRES  22 A  342  ALA ILE LYS CYS LEU TYR ILE LEU THR ARG PRO LEU ALA          
SEQRES  23 A  342  PHE LEU ASN SER ALA VAL ASN PRO ILE PHE TYR PHE LEU          
SEQRES  24 A  342  VAL GLY ASP HIS PHE ARG ASP MET LEU PHE SER LYS LEU          
SEQRES  25 A  342  ARG GLN TYR PHE LYS SER LEU THR SER PHE ARG LEU LEU          
SEQRES  26 A  342  GLU VAL LEU PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS          
SEQRES  27 A  342  HIS HIS HIS HIS                                              
SEQRES   1 B  142  ASP TYR LYS ASP ASP ASP ASP LYS GLU VAL GLN LEU VAL          
SEQRES   2 B  142  GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU          
SEQRES   3 B  142  ARG LEU SER CYS GLU ALA SER GLY TYR THR LEU ALA ASN          
SEQRES   4 B  142  TYR ALA ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU          
SEQRES   5 B  142  ARG GLU GLY VAL SER CYS ILE SER SER GLY GLY SER THR          
SEQRES   6 B  142  VAL TYR SER GLU SER VAL LYS ASP ARG PHE THR ILE SER          
SEQRES   7 B  142  ARG ASP ASN ALA LYS LYS ILE VAL TYR LEU GLN MET ASN          
SEQRES   8 B  142  SER LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA          
SEQRES   9 B  142  ALA ASP PRO PHE GLY GLU ARG LEU CYS ILE ASP PRO ASN          
SEQRES  10 B  142  THR PHE ALA GLY TYR LEU GLU THR TRP GLY GLN GLY THR          
SEQRES  11 B  142  GLN VAL THR VAL SER SER LEU GLU VAL LEU PHE GLN              
SEQRES   1 C  342  ASP TYR LYS ASP ASP ASP ASP LYS ALA GLN ASN LEU SER          
SEQRES   2 C  342  CYS GLU ASN TRP LEU ALA LEU GLU ASN ILE LEU LYS LYS          
SEQRES   3 C  342  TYR TYR LEU SER ALA PHE TYR GLY ILE GLU PHE ILE VAL          
SEQRES   4 C  342  GLY MET LEU GLY ASN PHE THR VAL VAL PHE GLY TYR LEU          
SEQRES   5 C  342  PHE CYS MET LYS ASN TRP ASN SER SER ASN VAL TYR LEU          
SEQRES   6 C  342  PHE ASN LEU SER ILE SER ASP LEU ALA PHE LEU CYS THR          
SEQRES   7 C  342  LEU PRO MET LEU ILE ARG SER TYR ALA THR GLY ASN TRP          
SEQRES   8 C  342  THR TYR GLY ASP VAL LEU CYS ILE SER ASN ARG TYR VAL          
SEQRES   9 C  342  LEU HIS ALA ASN LEU TYR THR SER ILE LEU PHE LEU THR          
SEQRES  10 C  342  PHE ILE SER ILE ASP ARG TYR LEU LEU MET LYS PHE PRO          
SEQRES  11 C  342  PHE ARG GLU HIS ILE LEU GLN LYS LYS GLU PHE ALA ILE          
SEQRES  12 C  342  LEU ILE SER LEU ALA VAL TRP VAL LEU VAL THR LEU GLU          
SEQRES  13 C  342  VAL LEU PRO MET LEU THR PHE ILE THR SER THR PRO ILE          
SEQRES  14 C  342  GLU LYS GLY ASP SER CYS VAL ASP TYR ALA SER SER GLY          
SEQRES  15 C  342  ASN PRO LYS TYR SER LEU ILE TYR SER LEU CYS LEU THR          
SEQRES  16 C  342  LEU LEU GLY PHE LEU ILE PRO LEU SER VAL MET CYS PHE          
SEQRES  17 C  342  PHE TYR TYR LYS MET VAL VAL PHE LEU LYS LYS ARG SER          
SEQRES  18 C  342  GLN GLN GLN ALA THR VAL LEU SER LEU ASN LYS PRO LEU          
SEQRES  19 C  342  ARG LEU VAL VAL LEU ALA VAL VAL ILE PHE SER VAL LEU          
SEQRES  20 C  342  PHE THR PRO TYR HIS ILE MET ARG ASN VAL ARG ILE ALA          
SEQRES  21 C  342  SER ARG LEU ASP SER TRP PRO GLN GLY CYS SER GLN LYS          
SEQRES  22 C  342  ALA ILE LYS CYS LEU TYR ILE LEU THR ARG PRO LEU ALA          
SEQRES  23 C  342  PHE LEU ASN SER ALA VAL ASN PRO ILE PHE TYR PHE LEU          
SEQRES  24 C  342  VAL GLY ASP HIS PHE ARG ASP MET LEU PHE SER LYS LEU          
SEQRES  25 C  342  ARG GLN TYR PHE LYS SER LEU THR SER PHE ARG LEU LEU          
SEQRES  26 C  342  GLU VAL LEU PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS          
SEQRES  27 C  342  HIS HIS HIS HIS                                              
SEQRES   1 D  142  ASP TYR LYS ASP ASP ASP ASP LYS GLU VAL GLN LEU VAL          
SEQRES   2 D  142  GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU          
SEQRES   3 D  142  ARG LEU SER CYS GLU ALA SER GLY TYR THR LEU ALA ASN          
SEQRES   4 D  142  TYR ALA ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU          
SEQRES   5 D  142  ARG GLU GLY VAL SER CYS ILE SER SER GLY GLY SER THR          
SEQRES   6 D  142  VAL TYR SER GLU SER VAL LYS ASP ARG PHE THR ILE SER          
SEQRES   7 D  142  ARG ASP ASN ALA LYS LYS ILE VAL TYR LEU GLN MET ASN          
SEQRES   8 D  142  SER LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA          
SEQRES   9 D  142  ALA ASP PRO PHE GLY GLU ARG LEU CYS ILE ASP PRO ASN          
SEQRES  10 D  142  THR PHE ALA GLY TYR LEU GLU THR TRP GLY GLN GLY THR          
SEQRES  11 D  142  GLN VAL THR VAL SER SER LEU GLU VAL LEU PHE GLN              
HET    OLC  A 401      12                                                       
HET    OLC  A 402      11                                                       
HET    OLC  A 403      25                                                       
HET    OLC  A 404      19                                                       
HET    OLC  A 405      25                                                       
HET    OLC  A 406      25                                                       
HET    OLC  A 407      25                                                       
HET    OLC  A 408      21                                                       
HET    GOL  A 409       6                                                       
HET    H95  A 410      22                                                       
HET    OLC  C 401      13                                                       
HET    OLC  C 402      25                                                       
HET    CLR  C 403      28                                                       
HET    OLC  C 404      25                                                       
HET    OLC  C 405      25                                                       
HET    OLC  C 406      25                                                       
HET    OLC  C 407      25                                                       
HET    OLC  C 408      25                                                       
HET    GOL  C 409       6                                                       
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     H95 (2~{S},5~{R})-HEXANE-2,5-DIOL                                    
HETNAM     CLR CHOLESTEROL                                                      
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  OLC    15(C21 H40 O4)                                               
FORMUL  13  GOL    2(C3 H8 O3)                                                  
FORMUL  14  H95    C6 H14 O2                                                    
FORMUL  17  CLR    C27 H46 O                                                    
FORMUL  24  HOH   *299(H2 O)                                                    
HELIX    1 AA1 CYS A    7  TYR A   20  1                                  14    
HELIX    2 AA2 TYR A   20  MET A   48  1                                  29    
HELIX    3 AA3 ASN A   52  CYS A   70  1                                  19    
HELIX    4 AA4 THR A   71  GLY A   82  1                                  12    
HELIX    5 AA5 TYR A   86  PHE A  122  1                                  37    
HELIX    6 AA6 HIS A  127  GLN A  130  5                                   4    
HELIX    7 AA7 LYS A  131  LEU A  151  1                                  21    
HELIX    8 AA8 PRO A  152  PHE A  156  5                                   5    
HELIX    9 AA9 ASP A  170  SER A  174  5                                   5    
HELIX   10 AB1 ASN A  176  PHE A  192  1                                  17    
HELIX   11 AB2 PHE A  192  LYS A  212  1                                  21    
HELIX   12 AB3 PRO A  226  SER A  254  1                                  29    
HELIX   13 AB4 CYS A  263  LEU A  281  1                                  19    
HELIX   14 AB5 LEU A  281  ASN A  286  1                                   6    
HELIX   15 AB6 PRO A  287  LEU A  292  5                                   6    
HELIX   16 AB7 HIS A  296  SER A  314  1                                  19    
HELIX   17 AB8 PHE A  315  GLN A  323  1                                   9    
HELIX   18 AB9 GLN B   94  THR B   98  5                                   5    
HELIX   19 AC1 ARG B  111  ILE B  114  5                                   4    
HELIX   20 AC2 ASP B  115  ALA B  120  1                                   6    
HELIX   21 AC3 GLY B  121  LEU B  123  5                                   3    
HELIX   22 AC4 SER B  136  GLN B  142  1                                   7    
HELIX   23 AC5 GLU C    8  TYR C   20  1                                  13    
HELIX   24 AC6 TYR C   20  CYS C   47  1                                  28    
HELIX   25 AC7 ASN C   52  CYS C   70  1                                  19    
HELIX   26 AC8 THR C   71  GLY C   82  1                                  12    
HELIX   27 AC9 TYR C   86  PHE C  122  1                                  37    
HELIX   28 AD1 HIS C  127  GLN C  130  5                                   4    
HELIX   29 AD2 LYS C  131  LEU C  151  1                                  21    
HELIX   30 AD3 LEU C  151  PHE C  156  1                                   6    
HELIX   31 AD4 ASP C  170  SER C  174  5                                   5    
HELIX   32 AD5 ASN C  176  PHE C  192  1                                  17    
HELIX   33 AD6 PHE C  192  GLN C  217  1                                  26    
HELIX   34 AD7 PRO C  226  ARG C  255  1                                  30    
HELIX   35 AD8 CYS C  263  PHE C  280  1                                  18    
HELIX   36 AD9 LEU C  281  ASN C  286  1                                   6    
HELIX   37 AE1 PRO C  287  LEU C  292  5                                   6    
HELIX   38 AE2 HIS C  296  LYS C  304  1                                   9    
HELIX   39 AE3 GLU D   69  LYS D   72  5                                   4    
HELIX   40 AE4 GLN D   94  THR D   98  5                                   5    
HELIX   41 AE5 ASP D  115  ALA D  120  1                                   6    
SHEET    1 AA1 4 VAL B  13  SER B  15  0                                        
SHEET    2 AA1 4 LEU B  26  GLU B  31 -1  O  SER B  29   N  SER B  15           
SHEET    3 AA1 4 ILE B  85  MET B  90 -1  O  MET B  90   N  LEU B  26           
SHEET    4 AA1 4 PHE B  75  ARG B  79 -1  N  THR B  76   O  GLN B  89           
SHEET    1 AA2 6 LEU B  19  VAL B  20  0                                        
SHEET    2 AA2 6 THR B 130  VAL B 134  1  O  THR B 133   N  VAL B  20           
SHEET    3 AA2 6 ALA B  99  ASP B 106 -1  N  TYR B 101   O  THR B 130           
SHEET    4 AA2 6 ALA B  41  GLN B  47 -1  N  PHE B  45   O  TYR B 102           
SHEET    5 AA2 6 GLU B  54  ILE B  59 -1  O  SER B  57   N  TRP B  44           
SHEET    6 AA2 6 THR B  65  TYR B  67 -1  O  VAL B  66   N  CYS B  58           
SHEET    1 AA3 4 VAL D  13  GLU D  14  0                                        
SHEET    2 AA3 4 LEU D  26  GLU D  31 -1  O  GLU D  31   N  VAL D  13           
SHEET    3 AA3 4 ILE D  85  MET D  90 -1  O  MET D  90   N  LEU D  26           
SHEET    4 AA3 4 PHE D  75  ARG D  79 -1  N  THR D  76   O  GLN D  89           
SHEET    1 AA4 6 LEU D  19  VAL D  20  0                                        
SHEET    2 AA4 6 THR D 130  VAL D 134  1  O  THR D 133   N  VAL D  20           
SHEET    3 AA4 6 ALA D  99  ASP D 106 -1  N  TYR D 101   O  THR D 130           
SHEET    4 AA4 6 ALA D  41  GLN D  47 -1  N  PHE D  45   O  TYR D 102           
SHEET    5 AA4 6 GLU D  54  ILE D  59 -1  O  SER D  57   N  TRP D  44           
SHEET    6 AA4 6 THR D  65  TYR D  67 -1  O  VAL D  66   N  CYS D  58           
SHEET    1 AA5 4 LEU D  19  VAL D  20  0                                        
SHEET    2 AA5 4 THR D 130  VAL D 134  1  O  THR D 133   N  VAL D  20           
SHEET    3 AA5 4 ALA D  99  ASP D 106 -1  N  TYR D 101   O  THR D 130           
SHEET    4 AA5 4 THR D 125  TRP D 126 -1  O  THR D 125   N  ALA D 105           
SSBOND   1 CYS A    7    CYS A  263                          1555   1555  2.04  
SSBOND   2 CYS A   91    CYS A  168                          1555   1555  2.05  
SSBOND   3 CYS B   30    CYS B  103                          1555   1555  2.04  
SSBOND   4 CYS B   58    CYS B  113                          1555   1555  2.06  
SSBOND   5 CYS C    7    CYS C  263                          1555   1555  2.03  
SSBOND   6 CYS C   91    CYS C  168                          1555   1555  2.04  
SSBOND   7 CYS D   30    CYS D  103                          1555   1555  2.05  
SSBOND   8 CYS D   58    CYS D  113                          1555   1555  2.06  
SITE     1 AC1  2 TYR A  20  HOH A 549                                          
SITE     1 AC2  5 LEU A 185  THR A 188  ILE A 246  ASN A 249                    
SITE     2 AC2  5 HOH A 550                                                     
SITE     1 AC3  7 VAL A  32  GLY A  36  THR A  39  ALA A 284                    
SITE     2 AC3  7 ILE A 288  PHE A 291  ARG A 298                               
SITE     1 AC4  9 ILE A  92  ARG A  95  TYR A  96  TRP A 143                    
SITE     2 AC4  9 LEU A 151  MET A 153  LEU A 154  OLC A 407                    
SITE     3 AC4  9 OLC C 406                                                     
SITE     1 AC5  4 MET A  34  PHE A  38  CYS A  70  TYR A  86                    
SITE     1 AC6  8 TRP A  10  PRO A 243  MET A 247  CYS A 263                    
SITE     2 AC6  8 SER A 264  HOH A 520  OLC C 402  OLC C 407                    
SITE     1 AC7  8 LYS A  49  ASN A  50  TRP A  51  ASN A  60                    
SITE     2 AC7  8 LYS A 132  TRP A 143  OLC A 404  HOH A 523                    
SITE     1 AC8  9 THR A 155  PHE A 156  THR A 158  GLY A 175                    
SITE     2 AC8  9 ASN A 176  TYR A 179  ILE A 182  LEU A 190                    
SITE     3 AC8  9 LEU C 232                                                     
SITE     1 AC9  6 GLU A  14  SER A 173  LYS A 269  ILE A 273                    
SITE     2 AC9  6 ARG A 276  HOH A 533                                          
SITE     1 AD1  6 LYS A 225  ARG A 228  PHE A 291  HIS A 296                    
SITE     2 AD1  6 PHE A 297  ARG A 298                                          
SITE     1 AD2  9 ILE A  16  LEU A  17  TYR A  20  TYR A  21                    
SITE     2 AD2  9 LEU C 129  PHE C 134  ALA C 141  OLC C 402                    
SITE     3 AD2  9 OLC C 408                                                     
SITE     1 AD3  9 SER A 238  VAL A 239  PRO A 243  THR A 275                    
SITE     2 AD3  9 OLC A 406  LEU C 140  VAL C 144  OLC C 401                    
SITE     3 AD3  9 OLC C 407                                                     
SITE     1 AD4  5 PHE C 111  LEU C 145  VAL C 198  OLC C 408                    
SITE     2 AD4  5 HOH C 529                                                     
SITE     1 AD5  9 TYR C  44  LEU C  45  MET C  48  LYS C  49                    
SITE     2 AD5  9 TRP C  51  ASN C  60  LYS C 132  TRP C 143                    
SITE     3 AD5  9 OLC C 407                                                     
SITE     1 AD6  5 SER C 197  PHE C 201  TYR C 204  LYS C 205                    
SITE     2 AD6  5 OLC C 406                                                     
SITE     1 AD7 10 LEU A 154  OLC A 404  LEU C 193  CYS C 200                    
SITE     2 AD7 10 TYR C 203  TYR C 204  SER C 238  THR C 242                    
SITE     3 AD7 10 OLC C 405  HOH C 547                                          
SITE     1 AD8  6 OLC A 406  TYR C  96  LEU C 140  TRP C 143                    
SITE     2 AD8  6 OLC C 402  OLC C 404                                          
SITE     1 AD9 11 SER C  53  TYR C  57  PHE C 111  ILE C 114                    
SITE     2 AD9 11 ASP C 115  LEU C 118  LEU C 129  PHE C 134                    
SITE     3 AD9 11 OLC C 401  CLR C 403  HOH C 502                               
SITE     1 AE1  9 LYS C  18  VAL C 169  ASP C 170  SER C 173                    
SITE     2 AE1  9 LYS C 269  ILE C 273  ARG C 276  HOH C 514                    
SITE     3 AE1  9 HOH C 518                                                     
CRYST1   60.220  164.000   63.420  90.00 102.63  90.00 P 1 21 1      4          
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      0.016606  0.000000  0.003721        0.00000                         
SCALE2      0.000000  0.006098  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016159        0.00000                         
ATOM      1  N   SER A   6      61.522 -22.235  15.757  1.00 69.30           N  
ANISOU    1  N   SER A   6    11788   6152   8393  -2178    541  -1029       N  
ATOM      2  CA  SER A   6      60.558 -21.162  15.506  1.00 68.87           C  
ANISOU    2  CA  SER A   6    11556   6294   8319  -2246    421  -1011       C  
ATOM      3  C   SER A   6      61.160 -19.774  15.775  1.00 69.94           C  
ANISOU    3  C   SER A   6    11553   6569   8453  -2075    409   -940       C  
ATOM      4  O   SER A   6      61.076 -18.900  14.902  1.00 70.61           O  
ANISOU    4  O   SER A   6    11596   6765   8469  -2073    325   -962       O  
ATOM      5  CB  SER A   6      59.275 -21.384  16.307  1.00 74.41           C  
ANISOU    5  CB  SER A   6    12133   7036   9102  -2391    387   -975       C  
ATOM      6  OG  SER A   6      59.534 -21.638  17.680  1.00 87.07           O  
ANISOU    6  OG  SER A   6    13708   8596  10778  -2325    481   -886       O  
ATOM      7  N   CYS A   7      61.795 -19.583  16.960  1.00 61.96           N  
ANISOU    7  N   CYS A   7    10491   5542   7508  -1939    485   -855       N  
ATOM      8  CA  CYS A   7      62.470 -18.325  17.336  1.00 59.71           C  
ANISOU    8  CA  CYS A   7    10083   5374   7231  -1775    483   -788       C  
ATOM      9  C   CYS A   7      63.978 -18.544  17.607  1.00 58.53           C  
ANISOU    9  C   CYS A   7    10021   5120   7096  -1600    579   -777       C  
ATOM     10  O   CYS A   7      64.626 -17.697  18.227  1.00 56.53           O  
ANISOU   10  O   CYS A   7     9673   4933   6873  -1461    591   -711       O  
ATOM     11  CB  CYS A   7      61.773 -17.652  18.519  1.00 59.71           C  
ANISOU   11  CB  CYS A   7     9907   5479   7301  -1778    465   -700       C  
ATOM     12  SG  CYS A   7      59.991 -17.408  18.295  1.00 63.58           S  
ANISOU   12  SG  CYS A   7    10248   6080   7828  -1976    364   -726       S  
ATOM     13  N   GLU A   8      64.532 -19.677  17.115  1.00 52.97           N  
ANISOU   13  N   GLU A   8     9491   4248   6385  -1605    643   -851       N  
ATOM     14  CA  GLU A   8      65.937 -20.039  17.312  1.00 51.69           C  
ANISOU   14  CA  GLU A   8     9404   3963   6274  -1438    731   -860       C  
ATOM     15  C   GLU A   8      66.897 -19.017  16.684  1.00 51.79           C  
ANISOU   15  C   GLU A   8     9356   4067   6257  -1315    754   -886       C  
ATOM     16  O   GLU A   8      67.949 -18.755  17.274  1.00 52.19           O  
ANISOU   16  O   GLU A   8     9361   4091   6379  -1153    798   -849       O  
ATOM     17  CB  GLU A   8      66.247 -21.494  16.883  1.00 53.01           C  
ANISOU   17  CB  GLU A   8     9764   3917   6460  -1472    797   -949       C  
ATOM     18  CG  GLU A   8      66.136 -21.805  15.397  1.00 68.92           C  
ANISOU   18  CG  GLU A   8    11894   5911   8382  -1578    814  -1084       C  
ATOM     19  CD  GLU A   8      66.618 -23.181  14.955  1.00103.33           C  
ANISOU   19  CD  GLU A   8    16445  10046  12769  -1589    902  -1189       C  
ATOM     20  OE1 GLU A   8      66.280 -24.184  15.627  1.00107.03           O  
ANISOU   20  OE1 GLU A   8    16991  10371  13306  -1625    905  -1159       O  
ATOM     21  OE2 GLU A   8      67.320 -23.257  13.920  1.00 97.80           O  
ANISOU   21  OE2 GLU A   8    15832   9307  12020  -1569    974  -1306       O  
ATOM     22  N   ASN A   9      66.513 -18.399  15.540  1.00 44.52           N  
ANISOU   22  N   ASN A   9     8432   3255   5230  -1398    714   -941       N  
ATOM     23  CA  ASN A   9      67.317 -17.360  14.876  1.00 42.70           C  
ANISOU   23  CA  ASN A   9     8160   3116   4947  -1314    739   -961       C  
ATOM     24  C   ASN A   9      67.486 -16.136  15.769  1.00 41.78           C  
ANISOU   24  C   ASN A   9     7865   3131   4879  -1206    697   -851       C  
ATOM     25  O   ASN A   9      68.620 -15.746  16.018  1.00 41.01           O  
ANISOU   25  O   ASN A   9     7726   3026   4831  -1064    762   -841       O  
ATOM     26  CB  ASN A   9      66.740 -16.990  13.515  1.00 43.36           C  
ANISOU   26  CB  ASN A   9     8314   3275   4887  -1450    682  -1028       C  
ATOM     27  CG  ASN A   9      66.895 -18.077  12.486  1.00 52.08           C  
ANISOU   27  CG  ASN A   9     9619   4245   5922  -1540    751  -1159       C  
ATOM     28  OD1 ASN A   9      67.609 -19.055  12.692  1.00 45.00           O  
ANISOU   28  OD1 ASN A   9     8804   3193   5101  -1477    862  -1213       O  
ATOM     29  ND2 ASN A   9      66.249 -17.918  11.338  1.00 41.03           N  
ANISOU   29  ND2 ASN A   9     8313   2897   4381  -1689    679  -1216       N  
ATOM     30  N   TRP A  10      66.377 -15.593  16.327  1.00 35.84           N  
ANISOU   30  N   TRP A  10     7000   2487   4131  -1273    596   -776       N  
ATOM     31  CA  TRP A  10      66.397 -14.476  17.282  1.00 34.24           C  
ANISOU   31  CA  TRP A  10     6632   2400   3978  -1184    561   -677       C  
ATOM     32  C   TRP A  10      67.216 -14.826  18.536  1.00 38.80           C  
ANISOU   32  C   TRP A  10     7196   2896   4649  -1058    623   -621       C  
ATOM     33  O   TRP A  10      67.865 -13.956  19.108  1.00 37.08           O  
ANISOU   33  O   TRP A  10     6883   2741   4465   -941    625   -567       O  
ATOM     34  CB  TRP A  10      64.971 -14.071  17.696  1.00 31.99           C  
ANISOU   34  CB  TRP A  10     6233   2215   3705  -1291    465   -631       C  
ATOM     35  CG  TRP A  10      64.201 -13.329  16.640  1.00 32.40           C  
ANISOU   35  CG  TRP A  10     6247   2376   3689  -1378    357   -656       C  
ATOM     36  CD1 TRP A  10      63.066 -13.749  16.009  1.00 35.32           C  
ANISOU   36  CD1 TRP A  10     6638   2753   4030  -1534    271   -699       C  
ATOM     37  CD2 TRP A  10      64.530 -12.045  16.069  1.00 31.64           C  
ANISOU   37  CD2 TRP A  10     6095   2383   3544  -1318    308   -636       C  
ATOM     38  NE1 TRP A  10      62.641 -12.795  15.109  1.00 34.55           N  
ANISOU   38  NE1 TRP A  10     6498   2758   3872  -1568    151   -701       N  
ATOM     39  CE2 TRP A  10      63.531 -11.745  15.114  1.00 35.66           C  
ANISOU   39  CE2 TRP A  10     6603   2954   3993  -1439    177   -660       C  
ATOM     40  CE3 TRP A  10      65.576 -11.124  16.269  1.00 31.95           C  
ANISOU   40  CE3 TRP A  10     6091   2462   3587  -1181    355   -600       C  
ATOM     41  CZ2 TRP A  10      63.556 -10.569  14.349  1.00 34.12           C  
ANISOU   41  CZ2 TRP A  10     6386   2847   3730  -1423     87   -639       C  
ATOM     42  CZ3 TRP A  10      65.596  -9.962  15.517  1.00 33.24           C  
ANISOU   42  CZ3 TRP A  10     6226   2717   3686  -1173    287   -586       C  
ATOM     43  CH2 TRP A  10      64.602  -9.698  14.563  1.00 33.87           C  
ANISOU   43  CH2 TRP A  10     6327   2846   3695  -1292    153   -602       C  
ATOM     44  N   LEU A  11      67.212 -16.104  18.935  1.00 38.00           N  
ANISOU   44  N   LEU A  11     7204   2647   4588  -1084    661   -633       N  
ATOM     45  CA  LEU A  11      67.960 -16.566  20.101  1.00 39.32           C  
ANISOU   45  CA  LEU A  11     7392   2710   4837   -972    692   -572       C  
ATOM     46  C   LEU A  11      69.467 -16.606  19.835  1.00 41.18           C  
ANISOU   46  C   LEU A  11     7648   2870   5131   -812    748   -612       C  
ATOM     47  O   LEU A  11      70.247 -16.187  20.689  1.00 42.25           O  
ANISOU   47  O   LEU A  11     7715   3008   5329   -683    739   -550       O  
ATOM     48  CB  LEU A  11      67.444 -17.939  20.576  1.00 40.55           C  
ANISOU   48  CB  LEU A  11     7679   2712   5015  -1061    704   -566       C  
ATOM     49  CG  LEU A  11      67.864 -18.324  21.989  1.00 47.24           C  
ANISOU   49  CG  LEU A  11     8560   3467   5924   -985    700   -470       C  
ATOM     50  CD1 LEU A  11      67.180 -17.453  23.027  1.00 47.64           C  
ANISOU   50  CD1 LEU A  11     8503   3650   5949  -1026    667   -378       C  
ATOM     51  CD2 LEU A  11      67.620 -19.794  22.253  1.00 50.70           C  
ANISOU   51  CD2 LEU A  11     9171   3707   6386  -1054    720   -474       C  
ATOM     52  N   ALA A  12      69.865 -17.113  18.665  1.00 35.31           N  
ANISOU   52  N   ALA A  12     6992   2056   4367   -828    811   -723       N  
ATOM     53  CA  ALA A  12      71.255 -17.202  18.230  1.00 34.61           C  
ANISOU   53  CA  ALA A  12     6912   1892   4347   -692    894   -793       C  
ATOM     54  C   ALA A  12      71.845 -15.793  18.070  1.00 40.11           C  
ANISOU   54  C   ALA A  12     7471   2740   5029   -616    898   -774       C  
ATOM     55  O   ALA A  12      72.967 -15.542  18.508  1.00 38.49           O  
ANISOU   55  O   ALA A  12     7190   2509   4925   -471    924   -762       O  
ATOM     56  CB  ALA A  12      71.329 -17.971  16.916  1.00 34.54           C  
ANISOU   56  CB  ALA A  12     7039   1793   4292   -765    979   -932       C  
ATOM     57  N   LEU A  13      71.034 -14.869  17.506  1.00 39.11           N  
ANISOU   57  N   LEU A  13     7307   2766   4787   -718    853   -764       N  
ATOM     58  CA  LEU A  13      71.321 -13.451  17.268  1.00 39.38           C  
ANISOU   58  CA  LEU A  13     7231   2949   4783   -681    839   -736       C  
ATOM     59  C   LEU A  13      71.534 -12.735  18.605  1.00 39.75           C  
ANISOU   59  C   LEU A  13     7143   3056   4906   -579    784   -627       C  
ATOM     60  O   LEU A  13      72.526 -12.033  18.772  1.00 38.89           O  
ANISOU   60  O   LEU A  13     6950   2980   4847   -471    812   -619       O  
ATOM     61  CB  LEU A  13      70.121 -12.812  16.528  1.00 40.54           C  
ANISOU   61  CB  LEU A  13     7386   3217   4802   -823    759   -729       C  
ATOM     62  CG  LEU A  13      70.340 -12.018  15.238  1.00 47.44           C  
ANISOU   62  CG  LEU A  13     8297   4163   5563   -868    779   -782       C  
ATOM     63  CD1 LEU A  13      71.658 -11.241  15.230  1.00 48.51           C  
ANISOU   63  CD1 LEU A  13     8362   4329   5742   -747    860   -784       C  
ATOM     64  CD2 LEU A  13      70.255 -12.908  14.044  1.00 50.51           C  
ANISOU   64  CD2 LEU A  13     8859   4465   5866   -969    840   -896       C  
ATOM     65  N   GLU A  14      70.632 -12.956  19.570  1.00 34.87           N  
ANISOU   65  N   GLU A  14     6510   2446   4295   -625    715   -551       N  
ATOM     66  CA  GLU A  14      70.694 -12.386  20.927  1.00 33.45           C  
ANISOU   66  CA  GLU A  14     6234   2313   4164   -554    667   -451       C  
ATOM     67  C   GLU A  14      71.999 -12.770  21.626  1.00 36.36           C  
ANISOU   67  C   GLU A  14     6603   2576   4635   -407    688   -436       C  
ATOM     68  O   GLU A  14      72.572 -11.945  22.313  1.00 36.91           O  
ANISOU   68  O   GLU A  14     6577   2705   4741   -318    660   -385       O  
ATOM     69  CB  GLU A  14      69.517 -12.914  21.738  1.00 34.48           C  
ANISOU   69  CB  GLU A  14     6394   2430   4278   -655    628   -397       C  
ATOM     70  CG  GLU A  14      69.135 -12.095  22.938  1.00 46.87           C  
ANISOU   70  CG  GLU A  14     7868   4087   5853   -638    587   -309       C  
ATOM     71  CD  GLU A  14      68.566 -12.922  24.072  1.00 68.72           C  
ANISOU   71  CD  GLU A  14    10708   6778   8625   -699    585   -253       C  
ATOM     72  OE1 GLU A  14      69.004 -12.715  25.230  1.00 51.91           O  
ANISOU   72  OE1 GLU A  14     8574   4636   6512   -633    569   -182       O  
ATOM     73  OE2 GLU A  14      67.688 -13.779  23.803  1.00 60.51           O  
ANISOU   73  OE2 GLU A  14     9740   5685   7565   -822    599   -280       O  
ATOM     74  N   ASN A  15      72.480 -14.011  21.427  1.00 32.22           N  
ANISOU   74  N   ASN A  15     6183   1890   4169   -379    728   -485       N  
ATOM     75  CA  ASN A  15      73.730 -14.496  22.020  1.00 31.89           C  
ANISOU   75  CA  ASN A  15     6138   1722   4256   -229    729   -479       C  
ATOM     76  C   ASN A  15      74.954 -13.858  21.391  1.00 35.47           C  
ANISOU   76  C   ASN A  15     6494   2206   4778   -122    790   -548       C  
ATOM     77  O   ASN A  15      75.902 -13.529  22.093  1.00 35.30           O  
ANISOU   77  O   ASN A  15     6385   2169   4859      5    757   -515       O  
ATOM     78  CB  ASN A  15      73.806 -16.040  21.990  1.00 29.47           C  
ANISOU   78  CB  ASN A  15     5975   1214   4007   -230    749   -516       C  
ATOM     79  CG  ASN A  15      72.774 -16.697  22.871  1.00 52.05           C  
ANISOU   79  CG  ASN A  15     8937   4022   6819   -326    689   -430       C  
ATOM     80  OD1 ASN A  15      72.323 -16.124  23.871  1.00 41.08           O  
ANISOU   80  OD1 ASN A  15     7509   2712   5389   -346    628   -331       O  
ATOM     81  ND2 ASN A  15      72.373 -17.916  22.511  1.00 49.59           N  
ANISOU   81  ND2 ASN A  15     8765   3570   6508   -399    718   -474       N  
ATOM     82  N   ILE A  16      74.918 -13.696  20.074  1.00 33.53           N  
ANISOU   82  N   ILE A  16     6269   1999   4473   -184    879   -647       N  
ATOM     83  CA  ILE A  16      75.932 -13.074  19.218  1.00 34.25           C  
ANISOU   83  CA  ILE A  16     6291   2127   4595   -130    976   -733       C  
ATOM     84  C   ILE A  16      76.059 -11.557  19.538  1.00 37.41           C  
ANISOU   84  C   ILE A  16     6559   2691   4965   -109    933   -667       C  
ATOM     85  O   ILE A  16      77.180 -11.043  19.667  1.00 36.82           O  
ANISOU   85  O   ILE A  16     6377   2624   4989     -6    967   -687       O  
ATOM     86  CB  ILE A  16      75.574 -13.445  17.748  1.00 37.67           C  
ANISOU   86  CB  ILE A  16     6843   2547   4923   -249   1075   -848       C  
ATOM     87  CG1 ILE A  16      76.150 -14.829  17.449  1.00 39.30           C  
ANISOU   87  CG1 ILE A  16     7140   2564   5230   -204   1160   -949       C  
ATOM     88  CG2 ILE A  16      76.022 -12.435  16.710  1.00 38.47           C  
ANISOU   88  CG2 ILE A  16     6913   2752   4954   -280   1162   -910       C  
ATOM     89  CD1 ILE A  16      75.324 -15.682  16.457  1.00 55.15           C  
ANISOU   89  CD1 ILE A  16     9320   4513   7121   -350   1203  -1030       C  
ATOM     90  N   LEU A  17      74.904 -10.883  19.738  1.00 32.22           N  
ANISOU   90  N   LEU A  17     5899   2151   4191   -204    855   -592       N  
ATOM     91  CA  LEU A  17      74.797  -9.485  20.121  1.00 30.75           C  
ANISOU   91  CA  LEU A  17     5605   2107   3973   -195    803   -524       C  
ATOM     92  C   LEU A  17      75.445  -9.251  21.473  1.00 34.69           C  
ANISOU   92  C   LEU A  17     6012   2593   4573    -78    743   -452       C  
ATOM     93  O   LEU A  17      76.179  -8.281  21.632  1.00 36.00           O  
ANISOU   93  O   LEU A  17     6075   2825   4778    -15    745   -443       O  
ATOM     94  CB  LEU A  17      73.322  -9.054  20.167  1.00 30.89           C  
ANISOU   94  CB  LEU A  17     5637   2220   3881   -311    725   -468       C  
ATOM     95  CG  LEU A  17      72.607  -8.811  18.828  1.00 35.90           C  
ANISOU   95  CG  LEU A  17     6334   2909   4397   -431    734   -517       C  
ATOM     96  CD1 LEU A  17      71.210  -8.335  19.067  1.00 35.84           C  
ANISOU   96  CD1 LEU A  17     6297   2989   4332   -521    635   -457       C  
ATOM     97  CD2 LEU A  17      73.327  -7.772  17.991  1.00 37.23           C  
ANISOU   97  CD2 LEU A  17     6471   3144   4529   -415    781   -546       C  
ATOM     98  N   LYS A  18      75.207 -10.139  22.442  1.00 30.49           N  
ANISOU   98  N   LYS A  18     5533   1972   4079    -58    687   -401       N  
ATOM     99  CA  LYS A  18      75.829 -10.009  23.750  1.00 30.62           C  
ANISOU   99  CA  LYS A  18     5498   1961   4175     42    610   -328       C  
ATOM    100  C   LYS A  18      77.306 -10.323  23.701  1.00 35.36           C  
ANISOU  100  C   LYS A  18     6043   2467   4927    179    630   -377       C  
ATOM    101  O   LYS A  18      78.105  -9.527  24.179  1.00 37.07           O  
ANISOU  101  O   LYS A  18     6148   2729   5208    259    594   -356       O  
ATOM    102  CB  LYS A  18      75.125 -10.851  24.822  1.00 32.88           C  
ANISOU  102  CB  LYS A  18     5887   2172   4435      6    541   -249       C  
ATOM    103  CG  LYS A  18      73.697 -10.404  25.126  1.00 37.90           C  
ANISOU  103  CG  LYS A  18     6535   2913   4950   -121    523   -199       C  
ATOM    104  CD  LYS A  18      73.197 -10.998  26.419  1.00 46.38           C  
ANISOU  104  CD  LYS A  18     7703   3922   5999   -157    470   -116       C  
ATOM    105  CE  LYS A  18      72.838 -12.462  26.344  1.00 38.71           C  
ANISOU  105  CE  LYS A  18     6873   2807   5028   -216    488   -129       C  
ATOM    106  NZ  LYS A  18      72.798 -13.048  27.716  1.00 53.16           N  
ANISOU  106  NZ  LYS A  18     8814   4548   6837   -235    431    -35       N  
ATOM    107  N   LYS A  19      77.668 -11.451  23.103  1.00 32.14           N  
ANISOU  107  N   LYS A  19     5699   1923   4588    203    689   -453       N  
ATOM    108  CA  LYS A  19      79.050 -11.920  23.006  1.00 32.10           C  
ANISOU  108  CA  LYS A  19     5629   1802   4765    341    718   -520       C  
ATOM    109  C   LYS A  19      79.983 -10.978  22.222  1.00 38.47           C  
ANISOU  109  C   LYS A  19     6297   2691   5627    378    817   -605       C  
ATOM    110  O   LYS A  19      81.070 -10.692  22.711  1.00 38.87           O  
ANISOU  110  O   LYS A  19     6222   2722   5825    494    783   -608       O  
ATOM    111  CB  LYS A  19      79.104 -13.349  22.415  1.00 32.53           C  
ANISOU  111  CB  LYS A  19     5794   1685   4880    348    782   -600       C  
ATOM    112  CG  LYS A  19      80.328 -14.143  22.838  1.00 32.70           C  
ANISOU  112  CG  LYS A  19     5767   1537   5122    512    750   -631       C  
ATOM    113  CD  LYS A  19      80.287 -15.577  22.338  1.00 37.56           C  
ANISOU  113  CD  LYS A  19     6508   1964   5800    520    803   -704       C  
ATOM    114  CE  LYS A  19      81.206 -16.483  23.127  1.00 47.20           C  
ANISOU  114  CE  LYS A  19     7709   2989   7236    685    704   -686       C  
ATOM    115  NZ  LYS A  19      80.613 -16.897  24.446  1.00 55.02           N  
ANISOU  115  NZ  LYS A  19     8819   3916   8171    676    526   -527       N  
ATOM    116  N   TYR A  20      79.566 -10.507  21.028  1.00 34.75           N  
ANISOU  116  N   TYR A  20     5856   2308   5039    271    931   -672       N  
ATOM    117  CA  TYR A  20      80.421  -9.726  20.134  1.00 34.46           C  
ANISOU  117  CA  TYR A  20     5727   2331   5036    278   1055   -763       C  
ATOM    118  C   TYR A  20      80.084  -8.241  19.982  1.00 38.92           C  
ANISOU  118  C   TYR A  20     6245   3065   5478    204   1043   -713       C  
ATOM    119  O   TYR A  20      81.007  -7.426  19.916  1.00 39.20           O  
ANISOU  119  O   TYR A  20     6161   3147   5585    247   1090   -742       O  
ATOM    120  CB  TYR A  20      80.459 -10.406  18.755  1.00 35.04           C  
ANISOU  120  CB  TYR A  20     5896   2340   5078    215   1218   -899       C  
ATOM    121  CG  TYR A  20      81.069 -11.782  18.868  1.00 35.93           C  
ANISOU  121  CG  TYR A  20     6027   2268   5358    313   1249   -971       C  
ATOM    122  CD1 TYR A  20      82.417 -11.942  19.183  1.00 37.33           C  
ANISOU  122  CD1 TYR A  20     6057   2362   5765    462   1278  -1029       C  
ATOM    123  CD2 TYR A  20      80.281 -12.926  18.774  1.00 36.29           C  
ANISOU  123  CD2 TYR A  20     6227   2210   5351    264   1229   -973       C  
ATOM    124  CE1 TYR A  20      82.976 -13.204  19.349  1.00 34.86           C  
ANISOU  124  CE1 TYR A  20     5751   1862   5633    571   1285  -1091       C  
ATOM    125  CE2 TYR A  20      80.833 -14.195  18.940  1.00 36.85           C  
ANISOU  125  CE2 TYR A  20     6325   2092   5587    363   1244  -1031       C  
ATOM    126  CZ  TYR A  20      82.180 -14.323  19.247  1.00 41.66           C  
ANISOU  126  CZ  TYR A  20     6784   2613   6430    523   1266  -1087       C  
ATOM    127  OH  TYR A  20      82.774 -15.544  19.418  1.00 42.64           O  
ANISOU  127  OH  TYR A  20     6920   2535   6746    639   1268  -1147       O  
ATOM    128  N   TYR A  21      78.798  -7.884  19.894  1.00 34.13           N  
ANISOU  128  N   TYR A  21     5723   2541   4704     95    983   -646       N  
ATOM    129  CA  TYR A  21      78.417  -6.489  19.713  1.00 33.05           C  
ANISOU  129  CA  TYR A  21     5548   2545   4464     34    961   -599       C  
ATOM    130  C   TYR A  21      78.568  -5.694  21.030  1.00 36.58           C  
ANISOU  130  C   TYR A  21     5884   3050   4965    104    849   -504       C  
ATOM    131  O   TYR A  21      79.249  -4.656  21.036  1.00 36.50           O  
ANISOU  131  O   TYR A  21     5778   3103   4988    130    868   -506       O  
ATOM    132  CB  TYR A  21      77.017  -6.401  19.065  1.00 33.28           C  
ANISOU  132  CB  TYR A  21     5691   2630   4322   -101    928   -575       C  
ATOM    133  CG  TYR A  21      76.365  -5.042  19.098  1.00 33.04           C  
ANISOU  133  CG  TYR A  21     5624   2727   4201   -152    859   -505       C  
ATOM    134  CD1 TYR A  21      76.608  -4.106  18.098  1.00 34.26           C  
ANISOU  134  CD1 TYR A  21     5795   2942   4280   -208    914   -532       C  
ATOM    135  CD2 TYR A  21      75.480  -4.696  20.116  1.00 33.34           C  
ANISOU  135  CD2 TYR A  21     5623   2816   4227   -152    744   -414       C  
ATOM    136  CE1 TYR A  21      75.988  -2.854  18.112  1.00 33.33           C  
ANISOU  136  CE1 TYR A  21     5653   2923   4090   -249    835   -463       C  
ATOM    137  CE2 TYR A  21      74.891  -3.435  20.166  1.00 33.11           C  
ANISOU  137  CE2 TYR A  21     5549   2890   4140   -187    683   -359       C  
ATOM    138  CZ  TYR A  21      75.126  -2.524  19.147  1.00 36.22           C  
ANISOU  138  CZ  TYR A  21     5959   3333   4469   -231    718   -380       C  
ATOM    139  OH  TYR A  21      74.530  -1.282  19.189  1.00 29.00           O  
ANISOU  139  OH  TYR A  21     5009   2501   3508   -258    644   -322       O  
ATOM    140  N   LEU A  22      77.969  -6.177  22.142  1.00 32.63           N  
ANISOU  140  N   LEU A  22     5408   2521   4468    124    743   -427       N  
ATOM    141  CA  LEU A  22      78.080  -5.477  23.443  1.00 31.74           C  
ANISOU  141  CA  LEU A  22     5219   2455   4384    177    640   -342       C  
ATOM    142  C   LEU A  22      79.521  -5.343  23.898  1.00 34.91           C  
ANISOU  142  C   LEU A  22     5511   2816   4937    295    630   -363       C  
ATOM    143  O   LEU A  22      79.924  -4.264  24.269  1.00 33.35           O  
ANISOU  143  O   LEU A  22     5222   2693   4755    315    601   -340       O  
ATOM    144  CB  LEU A  22      77.238  -6.130  24.565  1.00 31.16           C  
ANISOU  144  CB  LEU A  22     5220   2344   4274    162    547   -262       C  
ATOM    145  CG  LEU A  22      75.716  -5.942  24.518  1.00 35.11           C  
ANISOU  145  CG  LEU A  22     5781   2914   4646     45    534   -226       C  
ATOM    146  CD1 LEU A  22      75.053  -6.594  25.719  1.00 34.35           C  
ANISOU  146  CD1 LEU A  22     5753   2772   4525     24    470   -156       C  
ATOM    147  CD2 LEU A  22      75.312  -4.450  24.446  1.00 35.18           C  
ANISOU  147  CD2 LEU A  22     5712   3057   4598     10    522   -204       C  
ATOM    148  N   SER A  23      80.308  -6.422  23.817  1.00 33.78           N  
ANISOU  148  N   SER A  23     5369   2548   4919    372    653   -416       N  
ATOM    149  CA  SER A  23      81.699  -6.413  24.267  1.00 33.75           C  
ANISOU  149  CA  SER A  23     5238   2487   5099    496    625   -445       C  
ATOM    150  C   SER A  23      82.600  -5.499  23.419  1.00 35.83           C  
ANISOU  150  C   SER A  23     5375   2816   5424    497    740   -529       C  
ATOM    151  O   SER A  23      83.425  -4.811  24.014  1.00 35.90           O  
ANISOU  151  O   SER A  23     5256   2853   5530    558    685   -517       O  
ATOM    152  CB  SER A  23      82.249  -7.835  24.393  1.00 36.42           C  
ANISOU  152  CB  SER A  23     5605   2658   5577    585    615   -484       C  
ATOM    153  OG  SER A  23      82.329  -8.447  23.123  1.00 46.78           O  
ANISOU  153  OG  SER A  23     6948   3921   6904    556    773   -600       O  
ATOM    154  N   ALA A  24      82.412  -5.439  22.064  1.00 30.95           N  
ANISOU  154  N   ALA A  24     4804   2223   4734    413    895   -612       N  
ATOM    155  CA  ALA A  24      83.178  -4.548  21.170  1.00 29.48           C  
ANISOU  155  CA  ALA A  24     4534   2097   4571    381   1028   -692       C  
ATOM    156  C   ALA A  24      82.775  -3.073  21.351  1.00 33.74           C  
ANISOU  156  C   ALA A  24     5053   2769   4997    315    983   -619       C  
ATOM    157  O   ALA A  24      83.661  -2.227  21.477  1.00 33.88           O  
ANISOU  157  O   ALA A  24     4947   2826   5099    339   1006   -639       O  
ATOM    158  CB  ALA A  24      83.021  -4.959  19.719  1.00 29.75           C  
ANISOU  158  CB  ALA A  24     4669   2109   4527    293   1200   -794       C  
ATOM    159  N   PHE A  25      81.455  -2.768  21.384  1.00 29.16           N  
ANISOU  159  N   PHE A  25     4583   2251   4245    234    917   -540       N  
ATOM    160  CA  PHE A  25      80.942  -1.409  21.585  1.00 28.86           C  
ANISOU  160  CA  PHE A  25     4533   2323   4111    180    863   -471       C  
ATOM    161  C   PHE A  25      81.304  -0.902  23.011  1.00 33.15           C  
ANISOU  161  C   PHE A  25     4976   2886   4735    258    741   -406       C  
ATOM    162  O   PHE A  25      81.811   0.213  23.141  1.00 31.71           O  
ANISOU  162  O   PHE A  25     4712   2761   4577    257    741   -402       O  
ATOM    163  CB  PHE A  25      79.416  -1.353  21.321  1.00 30.84           C  
ANISOU  163  CB  PHE A  25     4904   2616   4197     90    812   -415       C  
ATOM    164  CG  PHE A  25      78.809  -0.102  20.700  1.00 32.76           C  
ANISOU  164  CG  PHE A  25     5177   2947   4324      5    809   -385       C  
ATOM    165  CD1 PHE A  25      79.231   1.170  21.089  1.00 34.47           C  
ANISOU  165  CD1 PHE A  25     5310   3220   4565     20    786   -355       C  
ATOM    166  CD2 PHE A  25      77.722  -0.194  19.832  1.00 34.89           C  
ANISOU  166  CD2 PHE A  25     5560   3234   4462    -89    801   -377       C  
ATOM    167  CE1 PHE A  25      78.623   2.320  20.566  1.00 34.73           C  
ANISOU  167  CE1 PHE A  25     5382   3314   4499    -51    767   -318       C  
ATOM    168  CE2 PHE A  25      77.101   0.956  19.328  1.00 36.95           C  
ANISOU  168  CE2 PHE A  25     5852   3561   4627   -156    762   -336       C  
ATOM    169  CZ  PHE A  25      77.561   2.206  19.696  1.00 34.60           C  
ANISOU  169  CZ  PHE A  25     5478   3308   4359   -133    748   -305       C  
ATOM    170  N   TYR A  26      81.121  -1.721  24.067  1.00 30.96           N  
ANISOU  170  N   TYR A  26     4715   2552   4494    319    638   -359       N  
ATOM    171  CA  TYR A  26      81.544  -1.260  25.402  1.00 32.30           C  
ANISOU  171  CA  TYR A  26     4815   2735   4723    382    516   -302       C  
ATOM    172  C   TYR A  26      83.067  -1.047  25.475  1.00 36.77           C  
ANISOU  172  C   TYR A  26     5234   3273   5464    462    525   -358       C  
ATOM    173  O   TYR A  26      83.499  -0.099  26.114  1.00 36.05           O  
ANISOU  173  O   TYR A  26     5064   3233   5401    475    464   -334       O  
ATOM    174  CB  TYR A  26      81.063  -2.169  26.547  1.00 34.31           C  
ANISOU  174  CB  TYR A  26     5149   2926   4963    416    400   -233       C  
ATOM    175  CG  TYR A  26      79.565  -2.240  26.757  1.00 37.03           C  
ANISOU  175  CG  TYR A  26     5609   3308   5154    330    384   -176       C  
ATOM    176  CD1 TYR A  26      78.765  -1.108  26.616  1.00 40.45           C  
ANISOU  176  CD1 TYR A  26     6035   3845   5489    260    398   -155       C  
ATOM    177  CD2 TYR A  26      78.964  -3.406  27.221  1.00 37.40           C  
ANISOU  177  CD2 TYR A  26     5763   3278   5169    322    347   -142       C  
ATOM    178  CE1 TYR A  26      77.390  -1.165  26.831  1.00 42.81           C  
ANISOU  178  CE1 TYR A  26     6408   4176   5680    187    386   -116       C  
ATOM    179  CE2 TYR A  26      77.593  -3.476  27.437  1.00 37.97           C  
ANISOU  179  CE2 TYR A  26     5921   3387   5119    232    346   -100       C  
ATOM    180  CZ  TYR A  26      76.807  -2.356  27.238  1.00 46.17           C  
ANISOU  180  CZ  TYR A  26     6928   4535   6080    168    367    -92       C  
ATOM    181  OH  TYR A  26      75.457  -2.427  27.471  1.00 47.20           O  
ANISOU  181  OH  TYR A  26     7114   4699   6121     85    368    -64       O  
ATOM    182  N   GLY A  27      83.843  -1.918  24.808  1.00 33.21           N  
ANISOU  182  N   GLY A  27     4742   2739   5136    510    608   -442       N  
ATOM    183  CA  GLY A  27      85.297  -1.820  24.700  1.00 33.02           C  
ANISOU  183  CA  GLY A  27     4552   2681   5313    584    645   -522       C  
ATOM    184  C   GLY A  27      85.792  -0.521  24.068  1.00 37.55           C  
ANISOU  184  C   GLY A  27     5038   3345   5885    520    749   -568       C  
ATOM    185  O   GLY A  27      86.784   0.036  24.535  1.00 37.99           O  
ANISOU  185  O   GLY A  27     4946   3412   6076    565    709   -586       O  
ATOM    186  N   ILE A  28      85.113  -0.021  23.007  1.00 33.43           N  
ANISOU  186  N   ILE A  28     4611   2881   5209    408    871   -582       N  
ATOM    187  CA  ILE A  28      85.449   1.260  22.355  1.00 33.70           C  
ANISOU  187  CA  ILE A  28     4605   2992   5207    326    968   -608       C  
ATOM    188  C   ILE A  28      85.106   2.412  23.319  1.00 34.21           C  
ANISOU  188  C   ILE A  28     4652   3129   5216    317    833   -516       C  
ATOM    189  O   ILE A  28      85.935   3.298  23.541  1.00 35.33           O  
ANISOU  189  O   ILE A  28     4681   3301   5442    316    837   -535       O  
ATOM    190  CB  ILE A  28      84.786   1.443  20.947  1.00 37.23           C  
ANISOU  190  CB  ILE A  28     5194   3466   5486    203   1109   -636       C  
ATOM    191  CG1 ILE A  28      85.184   0.304  19.990  1.00 38.23           C  
ANISOU  191  CG1 ILE A  28     5352   3516   5659    202   1259   -745       C  
ATOM    192  CG2 ILE A  28      85.152   2.799  20.335  1.00 37.03           C  
ANISOU  192  CG2 ILE A  28     5151   3504   5415    112   1196   -648       C  
ATOM    193  CD1 ILE A  28      84.132   0.014  18.834  1.00 49.59           C  
ANISOU  193  CD1 ILE A  28     6993   4960   6890     89   1329   -747       C  
ATOM    194  N   GLU A  29      83.909   2.369  23.921  1.00 26.55           N  
ANISOU  194  N   GLU A  29     3789   2182   4119    307    723   -426       N  
ATOM    195  CA  GLU A  29      83.470   3.348  24.923  1.00 25.19           C  
ANISOU  195  CA  GLU A  29     3614   2067   3891    301    604   -349       C  
ATOM    196  C   GLU A  29      84.434   3.455  26.089  1.00 32.62           C  
ANISOU  196  C   GLU A  29     4439   2990   4965    380    495   -343       C  
ATOM    197  O   GLU A  29      84.769   4.566  26.510  1.00 32.82           O  
ANISOU  197  O   GLU A  29     4405   3063   5003    362    460   -332       O  
ATOM    198  CB  GLU A  29      82.055   3.045  25.404  1.00 25.16           C  
ANISOU  198  CB  GLU A  29     3730   2076   3753    280    528   -275       C  
ATOM    199  CG  GLU A  29      81.099   3.357  24.279  1.00 29.59           C  
ANISOU  199  CG  GLU A  29     4382   2672   4187    192    601   -274       C  
ATOM    200  CD  GLU A  29      79.659   2.956  24.457  1.00 40.53           C  
ANISOU  200  CD  GLU A  29     5869   4069   5463    158    550   -223       C  
ATOM    201  OE1 GLU A  29      79.303   2.414  25.524  1.00 26.28           O  
ANISOU  201  OE1 GLU A  29     4078   2246   3662    193    474   -186       O  
ATOM    202  OE2 GLU A  29      78.876   3.216  23.520  1.00 38.85           O  
ANISOU  202  OE2 GLU A  29     5722   3881   5159     88    584   -221       O  
ATOM    203  N   PHE A  30      84.934   2.313  26.563  1.00 31.59           N  
ANISOU  203  N   PHE A  30     4279   2783   4941    465    436   -354       N  
ATOM    204  CA  PHE A  30      85.925   2.272  27.633  1.00 32.83           C  
ANISOU  204  CA  PHE A  30     4327   2907   5239    547    304   -349       C  
ATOM    205  C   PHE A  30      87.215   3.051  27.277  1.00 36.95           C  
ANISOU  205  C   PHE A  30     4672   3449   5919    551    360   -426       C  
ATOM    206  O   PHE A  30      87.622   3.883  28.067  1.00 36.46           O  
ANISOU  206  O   PHE A  30     4547   3421   5886    551    261   -404       O  
ATOM    207  CB  PHE A  30      86.219   0.833  28.085  1.00 34.54           C  
ANISOU  207  CB  PHE A  30     4555   3015   5555    644    222   -344       C  
ATOM    208  CG  PHE A  30      87.264   0.771  29.166  1.00 36.77           C  
ANISOU  208  CG  PHE A  30     4730   3252   5989    732     51   -331       C  
ATOM    209  CD1 PHE A  30      88.563   0.366  28.877  1.00 40.31           C  
ANISOU  209  CD1 PHE A  30     5003   3636   6676    817     60   -415       C  
ATOM    210  CD2 PHE A  30      86.964   1.157  30.470  1.00 39.42           C  
ANISOU  210  CD2 PHE A  30     5135   3608   6235    727   -119   -243       C  
ATOM    211  CE1 PHE A  30      89.544   0.342  29.880  1.00 41.25           C  
ANISOU  211  CE1 PHE A  30     5009   3712   6954    901   -127   -403       C  
ATOM    212  CE2 PHE A  30      87.940   1.114  31.475  1.00 41.86           C  
ANISOU  212  CE2 PHE A  30     5362   3872   6671    800   -303   -227       C  
ATOM    213  CZ  PHE A  30      89.223   0.710  31.172  1.00 39.96           C  
ANISOU  213  CZ  PHE A  30     4937   3568   6679    890   -319   -303       C  
ATOM    214  N   ILE A  31      87.812   2.813  26.093  1.00 33.66           N  
ANISOU  214  N   ILE A  31     4184   3011   5593    538    529   -522       N  
ATOM    215  CA  ILE A  31      89.039   3.482  25.641  1.00 33.99           C  
ANISOU  215  CA  ILE A  31     4052   3069   5795    523    622   -613       C  
ATOM    216  C   ILE A  31      88.815   4.989  25.464  1.00 38.68           C  
ANISOU  216  C   ILE A  31     4667   3751   6278    416    662   -588       C  
ATOM    217  O   ILE A  31      89.483   5.784  26.120  1.00 38.45           O  
ANISOU  217  O   ILE A  31     4530   3747   6333    418    585   -589       O  
ATOM    218  CB  ILE A  31      89.646   2.800  24.361  1.00 37.30           C  
ANISOU  218  CB  ILE A  31     4414   3440   6317    517    831   -734       C  
ATOM    219  CG1 ILE A  31      90.099   1.359  24.643  1.00 37.79           C  
ANISOU  219  CG1 ILE A  31     4424   3394   6542    643    781   -772       C  
ATOM    220  CG2 ILE A  31      90.807   3.612  23.775  1.00 37.73           C  
ANISOU  220  CG2 ILE A  31     4295   3520   6521    470    969   -837       C  
ATOM    221  CD1 ILE A  31      89.971   0.409  23.422  1.00 41.98           C  
ANISOU  221  CD1 ILE A  31     5014   3870   7068    623    981   -864       C  
ATOM    222  N   VAL A  32      87.857   5.371  24.592  1.00 34.75           N  
ANISOU  222  N   VAL A  32     4317   3292   5596    322    769   -565       N  
ATOM    223  CA  VAL A  32      87.506   6.763  24.286  1.00 32.80           C  
ANISOU  223  CA  VAL A  32     4122   3108   5233    220    807   -534       C  
ATOM    224  C   VAL A  32      87.145   7.524  25.561  1.00 36.29           C  
ANISOU  224  C   VAL A  32     4570   3583   5636    239    635   -456       C  
ATOM    225  O   VAL A  32      87.697   8.598  25.798  1.00 37.24           O  
ANISOU  225  O   VAL A  32     4620   3730   5800    202    624   -466       O  
ATOM    226  CB  VAL A  32      86.413   6.861  23.172  1.00 35.82           C  
ANISOU  226  CB  VAL A  32     4682   3506   5422    132    904   -508       C  
ATOM    227  CG1 VAL A  32      86.002   8.312  22.916  1.00 35.56           C  
ANISOU  227  CG1 VAL A  32     4717   3520   5275     41    907   -459       C  
ATOM    228  CG2 VAL A  32      86.877   6.198  21.864  1.00 35.00           C  
ANISOU  228  CG2 VAL A  32     4590   3369   5339     89   1094   -600       C  
ATOM    229  N   GLY A  33      86.261   6.942  26.370  1.00 32.69           N  
ANISOU  229  N   GLY A  33     4202   3119   5099    289    513   -389       N  
ATOM    230  CA  GLY A  33      85.779   7.491  27.637  1.00 32.30           C  
ANISOU  230  CA  GLY A  33     4189   3096   4990    302    364   -322       C  
ATOM    231  C   GLY A  33      86.852   7.684  28.694  1.00 36.28           C  
ANISOU  231  C   GLY A  33     4572   3588   5626    351    243   -336       C  
ATOM    232  O   GLY A  33      86.909   8.738  29.322  1.00 34.42           O  
ANISOU  232  O   GLY A  33     4327   3386   5366    317    183   -321       O  
ATOM    233  N   MET A  34      87.723   6.676  28.882  1.00 34.87           N  
ANISOU  233  N   MET A  34     4299   3354   5597    431    197   -371       N  
ATOM    234  CA  MET A  34      88.819   6.723  29.846  1.00 35.88           C  
ANISOU  234  CA  MET A  34     4297   3458   5877    487     52   -386       C  
ATOM    235  C   MET A  34      89.836   7.804  29.471  1.00 40.14           C  
ANISOU  235  C   MET A  34     4681   4030   6540    436    117   -457       C  
ATOM    236  O   MET A  34      90.179   8.616  30.325  1.00 40.67           O  
ANISOU  236  O   MET A  34     4710   4120   6624    419      0   -444       O  
ATOM    237  CB  MET A  34      89.485   5.346  29.956  1.00 38.95           C  
ANISOU  237  CB  MET A  34     4613   3763   6423    594     -8   -411       C  
ATOM    238  CG  MET A  34      89.585   4.807  31.367  1.00 44.07           C  
ANISOU  238  CG  MET A  34     5299   4364   7082    666   -244   -344       C  
ATOM    239  SD  MET A  34      88.052   4.758  32.339  1.00 49.23           S  
ANISOU  239  SD  MET A  34     6209   5037   7460    624   -332   -227       S  
ATOM    240  CE  MET A  34      88.711   4.275  33.847  1.00 45.80           C  
ANISOU  240  CE  MET A  34     5785   4536   7080    694   -599   -174       C  
ATOM    241  N   LEU A  35      90.266   7.855  28.187  1.00 36.28           N  
ANISOU  241  N   LEU A  35     4121   3543   6119    395    312   -533       N  
ATOM    242  CA  LEU A  35      91.210   8.848  27.687  1.00 37.07           C  
ANISOU  242  CA  LEU A  35     4085   3669   6331    323    414   -606       C  
ATOM    243  C   LEU A  35      90.665  10.280  27.742  1.00 42.94           C  
ANISOU  243  C   LEU A  35     4921   4466   6928    221    426   -562       C  
ATOM    244  O   LEU A  35      91.350  11.175  28.251  1.00 43.96           O  
ANISOU  244  O   LEU A  35     4956   4611   7137    186    370   -584       O  
ATOM    245  CB  LEU A  35      91.704   8.516  26.271  1.00 37.84           C  
ANISOU  245  CB  LEU A  35     4123   3750   6504    284    647   -699       C  
ATOM    246  CG  LEU A  35      92.568   7.255  26.110  1.00 44.77           C  
ANISOU  246  CG  LEU A  35     4851   4563   7598    383    672   -784       C  
ATOM    247  CD1 LEU A  35      92.576   6.774  24.652  1.00 44.97           C  
ANISOU  247  CD1 LEU A  35     4905   4570   7613    334    924   -865       C  
ATOM    248  CD2 LEU A  35      93.994   7.463  26.642  1.00 49.39           C  
ANISOU  248  CD2 LEU A  35     5179   5132   8454    423    602   -860       C  
ATOM    249  N   GLY A  36      89.458  10.489  27.212  1.00 38.24           N  
ANISOU  249  N   GLY A  36     4505   3889   6136    174    489   -505       N  
ATOM    250  CA  GLY A  36      88.820  11.801  27.184  1.00 36.83           C  
ANISOU  250  CA  GLY A  36     4427   3743   5825     91    497   -461       C  
ATOM    251  C   GLY A  36      88.553  12.362  28.566  1.00 40.61           C  
ANISOU  251  C   GLY A  36     4928   4235   6268    114    323   -415       C  
ATOM    252  O   GLY A  36      88.800  13.549  28.815  1.00 39.91           O  
ANISOU  252  O   GLY A  36     4822   4158   6183     54    309   -422       O  
ATOM    253  N   ASN A  37      88.066  11.509  29.484  1.00 37.21           N  
ANISOU  253  N   ASN A  37     4548   3795   5797    192    195   -372       N  
ATOM    254  CA  ASN A  37      87.753  11.934  30.846  1.00 37.30           C  
ANISOU  254  CA  ASN A  37     4612   3816   5746    203     39   -333       C  
ATOM    255  C   ASN A  37      88.990  12.140  31.701  1.00 42.92           C  
ANISOU  255  C   ASN A  37     5193   4518   6598    220    -89   -369       C  
ATOM    256  O   ASN A  37      88.951  13.025  32.541  1.00 42.50           O  
ANISOU  256  O   ASN A  37     5173   4479   6498    184   -176   -360       O  
ATOM    257  CB  ASN A  37      86.738  11.021  31.526  1.00 36.93           C  
ANISOU  257  CB  ASN A  37     4692   3760   5580    254    -38   -272       C  
ATOM    258  CG  ASN A  37      85.334  11.329  31.080  1.00 41.27           C  
ANISOU  258  CG  ASN A  37     5373   4330   5977    216     45   -235       C  
ATOM    259  OD1 ASN A  37      84.774  12.372  31.410  1.00 30.46           O  
ANISOU  259  OD1 ASN A  37     4059   2980   4533    174     40   -224       O  
ATOM    260  ND2 ASN A  37      84.742  10.443  30.299  1.00 31.90           N  
ANISOU  260  ND2 ASN A  37     4232   3134   4755    232    119   -222       N  
ATOM    261  N   PHE A  38      90.095  11.390  31.488  1.00 41.02           N  
ANISOU  261  N   PHE A  38     4797   4250   6539    271   -103   -418       N  
ATOM    262  CA  PHE A  38      91.310  11.680  32.265  1.00 41.16           C  
ANISOU  262  CA  PHE A  38     4665   4258   6717    283   -243   -458       C  
ATOM    263  C   PHE A  38      91.978  12.967  31.772  1.00 42.19           C  
ANISOU  263  C   PHE A  38     4692   4414   6925    186   -148   -520       C  
ATOM    264  O   PHE A  38      92.437  13.748  32.596  1.00 41.47           O  
ANISOU  264  O   PHE A  38     4559   4331   6866    152   -268   -532       O  
ATOM    265  CB  PHE A  38      92.280  10.492  32.356  1.00 44.05           C  
ANISOU  265  CB  PHE A  38     4881   4574   7283    382   -325   -493       C  
ATOM    266  CG  PHE A  38      91.843   9.430  33.349  1.00 47.61           C  
ANISOU  266  CG  PHE A  38     5444   4982   7664    468   -509   -418       C  
ATOM    267  CD1 PHE A  38      91.560   9.762  34.676  1.00 51.99           C  
ANISOU  267  CD1 PHE A  38     6112   5541   8099    454   -699   -360       C  
ATOM    268  CD2 PHE A  38      91.753   8.094  32.971  1.00 50.17           C  
ANISOU  268  CD2 PHE A  38     5773   5252   8037    554   -489   -410       C  
ATOM    269  CE1 PHE A  38      91.134   8.785  35.585  1.00 52.90           C  
ANISOU  269  CE1 PHE A  38     6363   5610   8125    514   -857   -285       C  
ATOM    270  CE2 PHE A  38      91.339   7.118  33.887  1.00 53.38           C  
ANISOU  270  CE2 PHE A  38     6305   5606   8370    621   -658   -333       C  
ATOM    271  CZ  PHE A  38      91.047   7.468  35.189  1.00 51.59           C  
ANISOU  271  CZ  PHE A  38     6203   5386   8012    597   -841   -268       C  
ATOM    272  N   THR A  39      91.926  13.244  30.450  1.00 37.36           N  
ANISOU  272  N   THR A  39     4071   3812   6313    126     66   -553       N  
ATOM    273  CA  THR A  39      92.455  14.470  29.833  1.00 36.22           C  
ANISOU  273  CA  THR A  39     3865   3682   6216     13    187   -602       C  
ATOM    274  C   THR A  39      91.850  15.747  30.469  1.00 39.03           C  
ANISOU  274  C   THR A  39     4343   4051   6436    -52    120   -558       C  
ATOM    275  O   THR A  39      92.593  16.620  30.948  1.00 39.65           O  
ANISOU  275  O   THR A  39     4336   4130   6598   -108     62   -597       O  
ATOM    276  CB  THR A  39      92.251  14.428  28.294  1.00 40.10           C  
ANISOU  276  CB  THR A  39     4396   4171   6669    -47    425   -624       C  
ATOM    277  OG1 THR A  39      92.955  13.309  27.777  1.00 39.12           O  
ANISOU  277  OG1 THR A  39     4139   4028   6697      8    498   -689       O  
ATOM    278  CG2 THR A  39      92.718  15.723  27.573  1.00 36.69           C  
ANISOU  278  CG2 THR A  39     3945   3742   6253   -185    566   -661       C  
ATOM    279  N   VAL A  40      90.510  15.859  30.427  1.00 32.38           N  
ANISOU  279  N   VAL A  40     3691   3212   5399    -46    135   -488       N  
ATOM    280  CA  VAL A  40      89.745  16.996  30.950  1.00 30.22           C  
ANISOU  280  CA  VAL A  40     3546   2939   4996    -93     92   -452       C  
ATOM    281  C   VAL A  40      89.828  17.075  32.505  1.00 36.81           C  
ANISOU  281  C   VAL A  40     4394   3777   5815    -62   -102   -447       C  
ATOM    282  O   VAL A  40      89.927  18.183  33.023  1.00 36.22           O  
ANISOU  282  O   VAL A  40     4344   3696   5723   -122   -144   -463       O  
ATOM    283  CB  VAL A  40      88.284  17.025  30.403  1.00 31.63           C  
ANISOU  283  CB  VAL A  40     3896   3116   5006    -88    165   -390       C  
ATOM    284  CG1 VAL A  40      88.269  17.052  28.868  1.00 30.19           C  
ANISOU  284  CG1 VAL A  40     3728   2924   4819   -140    337   -393       C  
ATOM    285  CG2 VAL A  40      87.439  15.851  30.937  1.00 30.88           C  
ANISOU  285  CG2 VAL A  40     3872   3031   4830      1     97   -347       C  
ATOM    286  N   VAL A  41      89.806  15.908  33.239  1.00 35.75           N  
ANISOU  286  N   VAL A  41     4261   3644   5678     23   -222   -424       N  
ATOM    287  CA  VAL A  41      89.906  15.850  34.717  1.00 36.51           C  
ANISOU  287  CA  VAL A  41     4402   3737   5734     44   -418   -411       C  
ATOM    288  C   VAL A  41      91.274  16.387  35.179  1.00 43.28           C  
ANISOU  288  C   VAL A  41     5105   4590   6750      8   -528   -470       C  
ATOM    289  O   VAL A  41      91.309  17.306  36.010  1.00 42.02           O  
ANISOU  289  O   VAL A  41     4997   4429   6538    -49   -615   -484       O  
ATOM    290  CB  VAL A  41      89.538  14.470  35.345  1.00 39.54           C  
ANISOU  290  CB  VAL A  41     4854   4108   6060    130   -522   -360       C  
ATOM    291  CG1 VAL A  41      90.094  14.309  36.761  1.00 39.00           C  
ANISOU  291  CG1 VAL A  41     4803   4024   5990    143   -749   -353       C  
ATOM    292  CG2 VAL A  41      88.033  14.275  35.357  1.00 39.23           C  
ANISOU  292  CG2 VAL A  41     4996   4078   5832    133   -449   -308       C  
ATOM    293  N   PHE A  42      92.378  15.857  34.598  1.00 42.18           N  
ANISOU  293  N   PHE A  42     4771   4443   6813     35   -511   -516       N  
ATOM    294  CA  PHE A  42      93.733  16.324  34.880  1.00 43.62           C  
ANISOU  294  CA  PHE A  42     4764   4621   7188     -2   -601   -585       C  
ATOM    295  C   PHE A  42      93.927  17.761  34.386  1.00 48.60           C  
ANISOU  295  C   PHE A  42     5374   5261   7830   -124   -478   -630       C  
ATOM    296  O   PHE A  42      94.557  18.563  35.087  1.00 49.74           O  
ANISOU  296  O   PHE A  42     5467   5403   8027   -185   -591   -668       O  
ATOM    297  CB  PHE A  42      94.810  15.350  34.380  1.00 46.17           C  
ANISOU  297  CB  PHE A  42     4865   4928   7750     65   -600   -636       C  
ATOM    298  CG  PHE A  42      95.019  14.218  35.366  1.00 49.09           C  
ANISOU  298  CG  PHE A  42     5230   5266   8155    175   -832   -598       C  
ATOM    299  CD1 PHE A  42      94.303  13.028  35.249  1.00 52.82           C  
ANISOU  299  CD1 PHE A  42     5813   5717   8542    265   -823   -538       C  
ATOM    300  CD2 PHE A  42      95.885  14.363  36.449  1.00 52.19           C  
ANISOU  300  CD2 PHE A  42     5532   5644   8653    180  -1076   -616       C  
ATOM    301  CE1 PHE A  42      94.474  11.993  36.176  1.00 53.95           C  
ANISOU  301  CE1 PHE A  42     5981   5814   8704    360  -1045   -491       C  
ATOM    302  CE2 PHE A  42      96.056  13.327  37.377  1.00 55.28           C  
ANISOU  302  CE2 PHE A  42     5951   5993   9061    278  -1316   -567       C  
ATOM    303  CZ  PHE A  42      95.348  12.150  37.235  1.00 53.32           C  
ANISOU  303  CZ  PHE A  42     5822   5714   8724    367  -1295   -501       C  
ATOM    304  N   GLY A  43      93.271  18.099  33.270  1.00 43.21           N  
ANISOU  304  N   GLY A  43     4766   4581   7072   -164   -269   -617       N  
ATOM    305  CA  GLY A  43      93.243  19.455  32.726  1.00 42.18           C  
ANISOU  305  CA  GLY A  43     4669   4441   6918   -281   -146   -638       C  
ATOM    306  C   GLY A  43      92.658  20.451  33.711  1.00 45.13           C  
ANISOU  306  C   GLY A  43     5186   4803   7160   -320   -249   -618       C  
ATOM    307  O   GLY A  43      93.210  21.532  33.871  1.00 46.12           O  
ANISOU  307  O   GLY A  43     5273   4911   7341   -413   -258   -662       O  
ATOM    308  N   TYR A  44      91.583  20.077  34.442  1.00 40.28           N  
ANISOU  308  N   TYR A  44     4733   4192   6380   -256   -326   -562       N  
ATOM    309  CA  TYR A  44      90.978  20.933  35.471  1.00 39.13           C  
ANISOU  309  CA  TYR A  44     4730   4031   6105   -288   -411   -558       C  
ATOM    310  C   TYR A  44      91.830  21.015  36.732  1.00 46.83           C  
ANISOU  310  C   TYR A  44     5657   5009   7129   -307   -614   -597       C  
ATOM    311  O   TYR A  44      91.955  22.097  37.315  1.00 45.99           O  
ANISOU  311  O   TYR A  44     5592   4882   6999   -385   -659   -635       O  
ATOM    312  CB  TYR A  44      89.556  20.475  35.820  1.00 37.52           C  
ANISOU  312  CB  TYR A  44     4703   3832   5720   -225   -403   -501       C  
ATOM    313  CG  TYR A  44      88.466  21.200  35.054  1.00 35.62           C  
ANISOU  313  CG  TYR A  44     4570   3568   5395   -244   -256   -477       C  
ATOM    314  CD1 TYR A  44      88.701  21.708  33.777  1.00 36.96           C  
ANISOU  314  CD1 TYR A  44     4693   3719   5630   -290   -121   -477       C  
ATOM    315  CD2 TYR A  44      87.178  21.301  35.568  1.00 34.70           C  
ANISOU  315  CD2 TYR A  44     4603   3445   5137   -214   -251   -454       C  
ATOM    316  CE1 TYR A  44      87.703  22.369  33.067  1.00 35.56           C  
ANISOU  316  CE1 TYR A  44     4627   3508   5378   -303    -19   -444       C  
ATOM    317  CE2 TYR A  44      86.162  21.925  34.851  1.00 34.42           C  
ANISOU  317  CE2 TYR A  44     4645   3379   5052   -216   -139   -433       C  
ATOM    318  CZ  TYR A  44      86.432  22.469  33.606  1.00 36.80           C  
ANISOU  318  CZ  TYR A  44     4909   3654   5418   -257    -39   -422       C  
ATOM    319  OH  TYR A  44      85.432  23.086  32.900  1.00 29.63           O  
ANISOU  319  OH  TYR A  44     4090   2705   4462   -255     40   -390       O  
ATOM    320  N   LEU A  45      92.422  19.882  37.153  1.00 45.97           N  
ANISOU  320  N   LEU A  45     5463   4915   7089   -238   -747   -587       N  
ATOM    321  CA  LEU A  45      93.261  19.840  38.356  1.00 46.99           C  
ANISOU  321  CA  LEU A  45     5549   5040   7264   -249   -980   -613       C  
ATOM    322  C   LEU A  45      94.622  20.546  38.148  1.00 56.55           C  
ANISOU  322  C   LEU A  45     6552   6248   8688   -326  -1013   -691       C  
ATOM    323  O   LEU A  45      95.205  21.011  39.122  1.00 56.04           O  
ANISOU  323  O   LEU A  45     6476   6175   8641   -375  -1196   -725       O  
ATOM    324  CB  LEU A  45      93.428  18.402  38.909  1.00 46.46           C  
ANISOU  324  CB  LEU A  45     5471   4972   7210   -146  -1138   -567       C  
ATOM    325  CG  LEU A  45      92.150  17.569  39.171  1.00 49.94           C  
ANISOU  325  CG  LEU A  45     6116   5413   7446    -84  -1115   -490       C  
ATOM    326  CD1 LEU A  45      92.464  16.087  39.220  1.00 49.70           C  
ANISOU  326  CD1 LEU A  45     6032   5366   7485     20  -1209   -447       C  
ATOM    327  CD2 LEU A  45      91.403  18.016  40.425  1.00 49.93           C  
ANISOU  327  CD2 LEU A  45     6334   5405   7230   -131  -1217   -475       C  
ATOM    328  N   PHE A  46      95.097  20.673  36.887  1.00 57.92           N  
ANISOU  328  N   PHE A  46     6572   6424   9011   -351   -831   -725       N  
ATOM    329  CA  PHE A  46      96.356  21.368  36.577  1.00 59.97           C  
ANISOU  329  CA  PHE A  46     6625   6680   9482   -442   -818   -809       C  
ATOM    330  C   PHE A  46      96.207  22.825  36.094  1.00 63.97           C  
ANISOU  330  C   PHE A  46     7193   7164   9948   -574   -669   -838       C  
ATOM    331  O   PHE A  46      97.026  23.649  36.481  1.00 63.50           O  
ANISOU  331  O   PHE A  46     7046   7092   9988   -670   -741   -901       O  
ATOM    332  CB  PHE A  46      97.205  20.579  35.563  1.00 63.01           C  
ANISOU  332  CB  PHE A  46     6776   7076  10091   -406   -711   -850       C  
ATOM    333  CG  PHE A  46      97.658  19.202  35.993  1.00 66.28           C  
ANISOU  333  CG  PHE A  46     7074   7490  10618   -278   -873   -841       C  
ATOM    334  CD1 PHE A  46      97.748  18.162  35.072  1.00 70.35           C  
ANISOU  334  CD1 PHE A  46     7497   8005  11228   -196   -745   -844       C  
ATOM    335  CD2 PHE A  46      98.012  18.946  37.317  1.00 69.67           C  
ANISOU  335  CD2 PHE A  46     7501   7911  11061   -243  -1163   -832       C  
ATOM    336  CE1 PHE A  46      98.169  16.891  35.467  1.00 71.65           C  
ANISOU  336  CE1 PHE A  46     7558   8151  11513    -69   -901   -836       C  
ATOM    337  CE2 PHE A  46      98.426  17.672  37.712  1.00 72.81           C  
ANISOU  337  CE2 PHE A  46     7807   8291  11566   -120  -1335   -812       C  
ATOM    338  CZ  PHE A  46      98.512  16.657  36.782  1.00 71.11           C  
ANISOU  338  CZ  PHE A  46     7488   8067  11463    -29  -1202   -816       C  
ATOM    339  N   CYS A  47      95.197  23.133  35.241  1.00 60.95           N  
ANISOU  339  N   CYS A  47     6958   6768   9432   -580   -476   -792       N  
ATOM    340  CA  CYS A  47      94.982  24.463  34.643  1.00 61.11           C  
ANISOU  340  CA  CYS A  47     7060   6747   9414   -695   -333   -803       C  
ATOM    341  C   CYS A  47      94.039  25.385  35.422  1.00 63.95           C  
ANISOU  341  C   CYS A  47     7633   7069   9597   -715   -391   -782       C  
ATOM    342  O   CYS A  47      94.343  26.575  35.553  1.00 63.11           O  
ANISOU  342  O   CYS A  47     7548   6918   9512   -821   -385   -824       O  
ATOM    343  CB  CYS A  47      94.522  24.348  33.191  1.00 61.93           C  
ANISOU  343  CB  CYS A  47     7202   6841   9488   -702   -105   -766       C  
ATOM    344  SG  CYS A  47      95.555  23.285  32.156  1.00 66.23           S  
ANISOU  344  SG  CYS A  47     7517   7421  10227   -688     16   -809       S  
ATOM    345  N   MET A  48      92.853  24.873  35.827  1.00 59.77           N  
ANISOU  345  N   MET A  48     7260   6548   8900   -619   -419   -724       N  
ATOM    346  CA  MET A  48      91.800  25.662  36.484  1.00 59.03           C  
ANISOU  346  CA  MET A  48     7366   6416   8645   -625   -437   -714       C  
ATOM    347  C   MET A  48      92.035  25.894  37.972  1.00 64.21           C  
ANISOU  347  C   MET A  48     8072   7073   9251   -648   -624   -759       C  
ATOM    348  O   MET A  48      91.976  24.956  38.768  1.00 64.31           O  
ANISOU  348  O   MET A  48     8101   7123   9210   -585   -753   -741       O  
ATOM    349  CB  MET A  48      90.413  25.061  36.233  1.00 60.82           C  
ANISOU  349  CB  MET A  48     7724   6652   8731   -528   -366   -647       C  
ATOM    350  CG  MET A  48      90.167  24.735  34.783  1.00 64.12           C  
ANISOU  350  CG  MET A  48     8112   7070   9180   -509   -206   -601       C  
ATOM    351  SD  MET A  48      89.460  26.110  33.884  1.00 67.51           S  
ANISOU  351  SD  MET A  48     8660   7417   9574   -576    -69   -583       S  
ATOM    352  CE  MET A  48      89.812  25.661  32.283  1.00 63.55           C  
ANISOU  352  CE  MET A  48     8092   6926   9128   -594     80   -545       C  
ATOM    353  N   LYS A  49      92.292  27.164  38.346  1.00 61.20           N  
ANISOU  353  N   LYS A  49     7734   6640   8877   -749   -641   -816       N  
ATOM    354  CA  LYS A  49      92.537  27.545  39.738  1.00 60.52           C  
ANISOU  354  CA  LYS A  49     7720   6545   8729   -797   -813   -871       C  
ATOM    355  C   LYS A  49      91.337  28.241  40.378  1.00 62.25           C  
ANISOU  355  C   LYS A  49     8164   6717   8773   -796   -773   -885       C  
ATOM    356  O   LYS A  49      91.223  28.218  41.601  1.00 63.49           O  
ANISOU  356  O   LYS A  49     8431   6879   8814   -807   -898   -916       O  
ATOM    357  CB  LYS A  49      93.836  28.367  39.894  1.00 63.05           C  
ANISOU  357  CB  LYS A  49     7917   6843   9196   -922   -889   -946       C  
ATOM    358  CG  LYS A  49      95.122  27.639  39.457  1.00 75.42           C  
ANISOU  358  CG  LYS A  49     9228   8457  10969   -925   -941   -956       C  
ATOM    359  CD  LYS A  49      95.572  26.531  40.420  1.00 87.51           C  
ANISOU  359  CD  LYS A  49    10698  10038  12515   -865  -1173   -953       C  
ATOM    360  CE  LYS A  49      95.399  25.141  39.838  1.00100.05           C  
ANISOU  360  CE  LYS A  49    12210  11671  14134   -736  -1145   -887       C  
ATOM    361  NZ  LYS A  49      95.884  24.086  40.768  1.00105.58           N  
ANISOU  361  NZ  LYS A  49    12849  12397  14868   -677  -1390   -877       N  
ATOM    362  N   ASN A  50      90.438  28.836  39.571  1.00 55.37           N  
ANISOU  362  N   ASN A  50     7363   5794   7882   -781   -604   -864       N  
ATOM    363  CA  ASN A  50      89.221  29.492  40.066  1.00 53.72           C  
ANISOU  363  CA  ASN A  50     7340   5529   7544   -761   -544   -885       C  
ATOM    364  C   ASN A  50      88.019  28.946  39.292  1.00 53.38           C  
ANISOU  364  C   ASN A  50     7331   5495   7457   -656   -416   -815       C  
ATOM    365  O   ASN A  50      87.898  29.158  38.076  1.00 54.54           O  
ANISOU  365  O   ASN A  50     7431   5616   7677   -646   -311   -768       O  
ATOM    366  CB  ASN A  50      89.336  31.042  40.039  1.00 56.60           C  
ANISOU  366  CB  ASN A  50     7765   5790   7949   -855   -500   -948       C  
ATOM    367  CG  ASN A  50      89.318  31.712  38.668  1.00 79.44           C  
ANISOU  367  CG  ASN A  50    10618   8621  10946   -876   -367   -907       C  
ATOM    368  OD1 ASN A  50      90.002  31.305  37.709  1.00 68.18           O  
ANISOU  368  OD1 ASN A  50     9062   7230   9615   -891   -329   -863       O  
ATOM    369  ND2 ASN A  50      88.528  32.769  38.555  1.00 71.51           N  
ANISOU  369  ND2 ASN A  50     9736   7510   9923   -883   -292   -926       N  
ATOM    370  N   TRP A  51      87.196  28.139  39.971  1.00 44.82           N  
ANISOU  370  N   TRP A  51     6327   4450   6251   -586   -433   -803       N  
ATOM    371  CA  TRP A  51      86.067  27.457  39.331  1.00 42.08           C  
ANISOU  371  CA  TRP A  51     5998   4122   5867   -490   -331   -741       C  
ATOM    372  C   TRP A  51      84.762  28.209  39.446  1.00 41.16           C  
ANISOU  372  C   TRP A  51     5998   3940   5702   -460   -232   -770       C  
ATOM    373  O   TRP A  51      84.437  28.710  40.514  1.00 41.22           O  
ANISOU  373  O   TRP A  51     6111   3917   5633   -490   -248   -845       O  
ATOM    374  CB  TRP A  51      85.888  26.026  39.898  1.00 40.42           C  
ANISOU  374  CB  TRP A  51     5797   3991   5570   -434   -393   -706       C  
ATOM    375  CG  TRP A  51      86.979  25.038  39.573  1.00 41.11           C  
ANISOU  375  CG  TRP A  51     5751   4136   5733   -423   -478   -663       C  
ATOM    376  CD1 TRP A  51      88.270  25.316  39.227  1.00 44.21           C  
ANISOU  376  CD1 TRP A  51     6013   4529   6258   -477   -532   -679       C  
ATOM    377  CD2 TRP A  51      86.897  23.607  39.686  1.00 40.53           C  
ANISOU  377  CD2 TRP A  51     5660   4119   5620   -357   -525   -609       C  
ATOM    378  NE1 TRP A  51      88.983  24.148  39.077  1.00 43.71           N  
ANISOU  378  NE1 TRP A  51     5835   4518   6255   -436   -605   -644       N  
ATOM    379  CE2 TRP A  51      88.168  23.085  39.358  1.00 44.23           C  
ANISOU  379  CE2 TRP A  51     5978   4614   6215   -360   -609   -597       C  
ATOM    380  CE3 TRP A  51      85.869  22.714  40.029  1.00 41.57           C  
ANISOU  380  CE3 TRP A  51     5886   4274   5632   -300   -498   -574       C  
ATOM    381  CZ2 TRP A  51      88.436  21.711  39.345  1.00 43.10           C  
ANISOU  381  CZ2 TRP A  51     5780   4510   6087   -294   -674   -549       C  
ATOM    382  CZ3 TRP A  51      86.141  21.355  40.025  1.00 42.66           C  
ANISOU  382  CZ3 TRP A  51     5987   4454   5770   -249   -564   -520       C  
ATOM    383  CH2 TRP A  51      87.414  20.869  39.694  1.00 43.05           C  
ANISOU  383  CH2 TRP A  51     5891   4518   5949   -240   -656   -507       C  
ATOM    384  N   ASN A  52      84.001  28.263  38.358  1.00 34.22           N  
ANISOU  384  N   ASN A  52     5101   3035   4867   -402   -135   -718       N  
ATOM    385  CA  ASN A  52      82.658  28.836  38.355  1.00 32.53           C  
ANISOU  385  CA  ASN A  52     4965   2756   4639   -349    -50   -740       C  
ATOM    386  C   ASN A  52      81.645  27.654  38.433  1.00 35.48           C  
ANISOU  386  C   ASN A  52     5340   3196   4946   -268    -13   -707       C  
ATOM    387  O   ASN A  52      82.075  26.499  38.545  1.00 33.22           O  
ANISOU  387  O   ASN A  52     5013   2992   4615   -262    -60   -667       O  
ATOM    388  CB  ASN A  52      82.432  29.708  37.104  1.00 28.05           C  
ANISOU  388  CB  ASN A  52     4386   2100   4171   -340      4   -698       C  
ATOM    389  CG  ASN A  52      82.485  29.003  35.779  1.00 41.67           C  
ANISOU  389  CG  ASN A  52     6042   3862   5929   -311     28   -600       C  
ATOM    390  OD1 ASN A  52      82.250  27.800  35.650  1.00 39.36           O  
ANISOU  390  OD1 ASN A  52     5707   3653   5594   -263     28   -560       O  
ATOM    391  ND2 ASN A  52      82.790  29.748  34.749  1.00 37.22           N  
ANISOU  391  ND2 ASN A  52     5483   3228   5432   -348     52   -560       N  
ATOM    392  N   SER A  53      80.329  27.937  38.313  1.00 31.83           N  
ANISOU  392  N   SER A  53     4911   2689   4495   -206     68   -725       N  
ATOM    393  CA  SER A  53      79.268  26.926  38.330  1.00 30.91           C  
ANISOU  393  CA  SER A  53     4784   2626   4334   -141    117   -702       C  
ATOM    394  C   SER A  53      79.420  25.845  37.265  1.00 35.44           C  
ANISOU  394  C   SER A  53     5281   3263   4923   -108    101   -602       C  
ATOM    395  O   SER A  53      79.321  24.666  37.614  1.00 34.85           O  
ANISOU  395  O   SER A  53     5201   3262   4776    -97     90   -581       O  
ATOM    396  CB  SER A  53      77.896  27.568  38.222  1.00 33.89           C  
ANISOU  396  CB  SER A  53     5172   2932   4771    -79    201   -744       C  
ATOM    397  OG  SER A  53      77.728  28.568  39.209  1.00 44.73           O  
ANISOU  397  OG  SER A  53     6620   4239   6136   -106    236   -853       O  
ATOM    398  N   SER A  54      79.678  26.231  35.979  1.00 31.16           N  
ANISOU  398  N   SER A  54     4695   2683   4461   -102    101   -542       N  
ATOM    399  CA  SER A  54      79.874  25.288  34.867  1.00 29.76           C  
ANISOU  399  CA  SER A  54     4461   2557   4292    -85     99   -457       C  
ATOM    400  C   SER A  54      81.052  24.343  35.128  1.00 34.22           C  
ANISOU  400  C   SER A  54     4979   3197   4827   -118     52   -444       C  
ATOM    401  O   SER A  54      80.931  23.143  34.879  1.00 34.73           O  
ANISOU  401  O   SER A  54     5013   3320   4862    -86     54   -404       O  
ATOM    402  CB  SER A  54      80.088  26.032  33.555  1.00 32.06           C  
ANISOU  402  CB  SER A  54     4749   2782   4650   -104    111   -406       C  
ATOM    403  OG  SER A  54      78.917  26.720  33.160  1.00 37.36           O  
ANISOU  403  OG  SER A  54     5456   3377   5361    -53    127   -397       O  
ATOM    404  N   ASN A  55      82.171  24.872  35.680  1.00 30.73           N  
ANISOU  404  N   ASN A  55     4526   2746   4403   -181      1   -484       N  
ATOM    405  CA  ASN A  55      83.370  24.090  36.001  1.00 30.30           C  
ANISOU  405  CA  ASN A  55     4407   2750   4355   -208    -69   -481       C  
ATOM    406  C   ASN A  55      83.077  22.967  37.002  1.00 35.91           C  
ANISOU  406  C   ASN A  55     5153   3518   4975   -174   -120   -482       C  
ATOM    407  O   ASN A  55      83.574  21.855  36.832  1.00 35.97           O  
ANISOU  407  O   ASN A  55     5105   3571   4990   -151   -158   -445       O  
ATOM    408  CB  ASN A  55      84.468  24.984  36.547  1.00 26.99           C  
ANISOU  408  CB  ASN A  55     3970   2303   3980   -285   -130   -535       C  
ATOM    409  CG  ASN A  55      84.999  26.027  35.597  1.00 39.69           C  
ANISOU  409  CG  ASN A  55     5546   3854   5680   -342    -81   -532       C  
ATOM    410  OD1 ASN A  55      85.324  27.137  36.014  1.00 38.14           O  
ANISOU  410  OD1 ASN A  55     5384   3599   5507   -403    -97   -582       O  
ATOM    411  ND2 ASN A  55      85.123  25.706  34.318  1.00 27.17           N  
ANISOU  411  ND2 ASN A  55     3909   2275   4139   -338    -16   -477       N  
ATOM    412  N   VAL A  56      82.274  23.273  38.047  1.00 31.81           N  
ANISOU  412  N   VAL A  56     4733   2983   4369   -176   -113   -528       N  
ATOM    413  CA  VAL A  56      81.861  22.336  39.085  1.00 30.16           C  
ANISOU  413  CA  VAL A  56     4599   2815   4046   -167   -143   -532       C  
ATOM    414  C   VAL A  56      80.995  21.221  38.472  1.00 32.97           C  
ANISOU  414  C   VAL A  56     4937   3205   4385   -106    -82   -475       C  
ATOM    415  O   VAL A  56      81.280  20.042  38.706  1.00 31.35           O  
ANISOU  415  O   VAL A  56     4735   3040   4139    -93   -135   -435       O  
ATOM    416  CB  VAL A  56      81.160  23.068  40.266  1.00 32.74           C  
ANISOU  416  CB  VAL A  56     5049   3111   4281   -203   -112   -613       C  
ATOM    417  CG1 VAL A  56      80.359  22.087  41.132  1.00 32.41           C  
ANISOU  417  CG1 VAL A  56     5102   3104   4107   -200    -86   -613       C  
ATOM    418  CG2 VAL A  56      82.177  23.816  41.116  1.00 31.83           C  
ANISOU  418  CG2 VAL A  56     4973   2974   4145   -277   -212   -667       C  
ATOM    419  N   TYR A  57      79.966  21.587  37.663  1.00 28.85           N  
ANISOU  419  N   TYR A  57     4397   2660   3905    -70     14   -468       N  
ATOM    420  CA  TYR A  57      79.086  20.575  37.053  1.00 27.84           C  
ANISOU  420  CA  TYR A  57     4249   2562   3767    -23     65   -420       C  
ATOM    421  C   TYR A  57      79.806  19.661  36.083  1.00 31.96           C  
ANISOU  421  C   TYR A  57     4700   3113   4329     -5     35   -354       C  
ATOM    422  O   TYR A  57      79.510  18.469  36.050  1.00 34.18           O  
ANISOU  422  O   TYR A  57     4987   3429   4572     19     38   -320       O  
ATOM    423  CB  TYR A  57      77.900  21.213  36.328  1.00 27.58           C  
ANISOU  423  CB  TYR A  57     4198   2491   3791     12    143   -426       C  
ATOM    424  CG  TYR A  57      77.039  22.124  37.157  1.00 27.74           C  
ANISOU  424  CG  TYR A  57     4266   2469   3807      9    196   -506       C  
ATOM    425  CD1 TYR A  57      76.602  21.742  38.426  1.00 28.30           C  
ANISOU  425  CD1 TYR A  57     4408   2562   3781    -17    230   -560       C  
ATOM    426  CD2 TYR A  57      76.616  23.360  36.659  1.00 28.29           C  
ANISOU  426  CD2 TYR A  57     4317   2464   3967     31    221   -531       C  
ATOM    427  CE1 TYR A  57      75.786  22.573  39.186  1.00 27.45           C  
ANISOU  427  CE1 TYR A  57     4344   2413   3672    -25    307   -652       C  
ATOM    428  CE2 TYR A  57      75.793  24.195  37.411  1.00 27.94           C  
ANISOU  428  CE2 TYR A  57     4306   2369   3943     39    281   -618       C  
ATOM    429  CZ  TYR A  57      75.367  23.787  38.663  1.00 33.72           C  
ANISOU  429  CZ  TYR A  57     5098   3133   4583     11    336   -686       C  
ATOM    430  OH  TYR A  57      74.546  24.592  39.396  1.00 37.85           O  
ANISOU  430  OH  TYR A  57     5651   3603   5128     13    421   -790       O  
ATOM    431  N   LEU A  58      80.693  20.232  35.253  1.00 27.14           N  
ANISOU  431  N   LEU A  58     4030   2485   3799    -22     24   -344       N  
ATOM    432  CA  LEU A  58      81.480  19.515  34.249  1.00 25.97           C  
ANISOU  432  CA  LEU A  58     3809   2357   3702    -16     24   -302       C  
ATOM    433  C   LEU A  58      82.375  18.524  34.964  1.00 29.50           C  
ANISOU  433  C   LEU A  58     4228   2836   4143     -9    -56   -301       C  
ATOM    434  O   LEU A  58      82.422  17.357  34.570  1.00 29.00           O  
ANISOU  434  O   LEU A  58     4140   2794   4084     26    -52   -268       O  
ATOM    435  CB  LEU A  58      82.325  20.489  33.374  1.00 25.17           C  
ANISOU  435  CB  LEU A  58     3659   2221   3682    -60     48   -306       C  
ATOM    436  CG  LEU A  58      81.585  21.193  32.241  1.00 28.74           C  
ANISOU  436  CG  LEU A  58     4144   2630   4145    -64    113   -276       C  
ATOM    437  CD1 LEU A  58      82.296  22.461  31.818  1.00 27.98           C  
ANISOU  437  CD1 LEU A  58     4047   2479   4105   -127    128   -289       C  
ATOM    438  CD2 LEU A  58      81.416  20.279  31.035  1.00 32.02           C  
ANISOU  438  CD2 LEU A  58     4545   3068   4554    -50    159   -228       C  
ATOM    439  N   PHE A  59      83.044  18.969  36.047  1.00 25.69           N  
ANISOU  439  N   PHE A  59     3762   2349   3652    -40   -139   -339       N  
ATOM    440  CA  PHE A  59      83.926  18.094  36.821  1.00 26.32           C  
ANISOU  440  CA  PHE A  59     3823   2447   3730    -32   -255   -333       C  
ATOM    441  C   PHE A  59      83.160  16.892  37.413  1.00 31.84           C  
ANISOU  441  C   PHE A  59     4612   3161   4326      2   -273   -297       C  
ATOM    442  O   PHE A  59      83.661  15.761  37.387  1.00 30.61           O  
ANISOU  442  O   PHE A  59     4426   3010   4193     38   -333   -263       O  
ATOM    443  CB  PHE A  59      84.665  18.865  37.916  1.00 27.66           C  
ANISOU  443  CB  PHE A  59     4015   2604   3890    -83   -361   -379       C  
ATOM    444  CG  PHE A  59      85.821  18.072  38.468  1.00 29.48           C  
ANISOU  444  CG  PHE A  59     4194   2844   4165    -72   -512   -369       C  
ATOM    445  CD1 PHE A  59      87.003  17.936  37.742  1.00 33.29           C  
ANISOU  445  CD1 PHE A  59     4514   3327   4806    -61   -536   -377       C  
ATOM    446  CD2 PHE A  59      85.717  17.422  39.692  1.00 31.45           C  
ANISOU  446  CD2 PHE A  59     4556   3093   4301    -73   -628   -353       C  
ATOM    447  CE1 PHE A  59      88.074  17.200  38.251  1.00 34.72           C  
ANISOU  447  CE1 PHE A  59     4622   3506   5062    -36   -690   -373       C  
ATOM    448  CE2 PHE A  59      86.778  16.673  40.194  1.00 34.78           C  
ANISOU  448  CE2 PHE A  59     4934   3507   4773    -52   -798   -333       C  
ATOM    449  CZ  PHE A  59      87.952  16.570  39.474  1.00 33.85           C  
ANISOU  449  CZ  PHE A  59     4630   3388   4842    -26   -836   -345       C  
ATOM    450  N   ASN A  60      81.946  17.168  37.929  1.00 28.86           N  
ANISOU  450  N   ASN A  60     4339   2782   3844    -13   -211   -311       N  
ATOM    451  CA  ASN A  60      80.996  16.215  38.489  1.00 28.47           C  
ANISOU  451  CA  ASN A  60     4387   2744   3687     -5   -188   -288       C  
ATOM    452  C   ASN A  60      80.521  15.249  37.421  1.00 30.64           C  
ANISOU  452  C   ASN A  60     4612   3030   4000     41   -125   -241       C  
ATOM    453  O   ASN A  60      80.410  14.061  37.691  1.00 31.73           O  
ANISOU  453  O   ASN A  60     4794   3170   4093     55   -155   -203       O  
ATOM    454  CB  ASN A  60      79.812  16.972  39.067  1.00 28.82           C  
ANISOU  454  CB  ASN A  60     4514   2781   3654    -37    -98   -337       C  
ATOM    455  CG  ASN A  60      79.936  17.152  40.531  1.00 46.80           C  
ANISOU  455  CG  ASN A  60     6919   5052   5812    -94   -154   -373       C  
ATOM    456  OD1 ASN A  60      79.570  16.265  41.295  1.00 46.99           O  
ANISOU  456  OD1 ASN A  60     7050   5083   5722   -117   -167   -353       O  
ATOM    457  ND2 ASN A  60      80.466  18.292  40.951  1.00 35.51           N  
ANISOU  457  ND2 ASN A  60     5496   3603   4395   -130   -190   -427       N  
ATOM    458  N   LEU A  61      80.261  15.757  36.203  1.00 25.74           N  
ANISOU  458  N   LEU A  61     3917   2408   3455     56    -47   -242       N  
ATOM    459  CA  LEU A  61      79.847  14.964  35.040  1.00 24.90           C  
ANISOU  459  CA  LEU A  61     3772   2310   3381     87     10   -204       C  
ATOM    460  C   LEU A  61      80.927  13.909  34.714  1.00 29.77           C  
ANISOU  460  C   LEU A  61     4338   2925   4048    114    -42   -178       C  
ATOM    461  O   LEU A  61      80.603  12.742  34.465  1.00 29.27           O  
ANISOU  461  O   LEU A  61     4294   2862   3966    138    -31   -148       O  
ATOM    462  CB  LEU A  61      79.581  15.912  33.845  1.00 24.34           C  
ANISOU  462  CB  LEU A  61     3652   2226   3370     83     74   -208       C  
ATOM    463  CG  LEU A  61      79.209  15.327  32.488  1.00 28.27           C  
ANISOU  463  CG  LEU A  61     4127   2727   3889     98    127   -174       C  
ATOM    464  CD1 LEU A  61      77.806  14.748  32.493  1.00 28.12           C  
ANISOU  464  CD1 LEU A  61     4147   2718   3821    109    161   -162       C  
ATOM    465  CD2 LEU A  61      79.369  16.384  31.390  1.00 27.89           C  
ANISOU  465  CD2 LEU A  61     4054   2653   3889     76    160   -170       C  
ATOM    466  N   SER A  62      82.206  14.310  34.817  1.00 27.51           N  
ANISOU  466  N   SER A  62     3983   2632   3837    109   -103   -198       N  
ATOM    467  CA  SER A  62      83.382  13.462  34.612  1.00 27.44           C  
ANISOU  467  CA  SER A  62     3894   2614   3919    142   -161   -192       C  
ATOM    468  C   SER A  62      83.558  12.406  35.690  1.00 31.76           C  
ANISOU  468  C   SER A  62     4499   3145   4423    171   -277   -165       C  
ATOM    469  O   SER A  62      84.075  11.342  35.363  1.00 32.27           O  
ANISOU  469  O   SER A  62     4518   3187   4554    218   -305   -148       O  
ATOM    470  CB  SER A  62      84.640  14.308  34.527  1.00 29.34           C  
ANISOU  470  CB  SER A  62     4028   2850   4269    119   -196   -232       C  
ATOM    471  OG  SER A  62      84.792  14.824  33.221  1.00 37.81           O  
ANISOU  471  OG  SER A  62     5037   3924   5404     96    -82   -248       O  
ATOM    472  N   ILE A  63      83.192  12.702  36.976  1.00 28.22           N  
ANISOU  472  N   ILE A  63     4161   2696   3864    139   -345   -162       N  
ATOM    473  CA  ILE A  63      83.271  11.731  38.078  1.00 28.88           C  
ANISOU  473  CA  ILE A  63     4348   2755   3870    147   -464   -124       C  
ATOM    474  C   ILE A  63      82.206  10.643  37.829  1.00 32.82           C  
ANISOU  474  C   ILE A  63     4926   3246   4297    159   -389    -84       C  
ATOM    475  O   ILE A  63      82.505   9.462  37.911  1.00 32.99           O  
ANISOU  475  O   ILE A  63     4970   3231   4333    197   -455    -43       O  
ATOM    476  CB  ILE A  63      83.160  12.366  39.506  1.00 32.71           C  
ANISOU  476  CB  ILE A  63     4960   3240   4227     86   -545   -138       C  
ATOM    477  CG1 ILE A  63      84.287  13.406  39.817  1.00 33.52           C  
ANISOU  477  CG1 ILE A  63     4988   3344   4403     64   -642   -182       C  
ATOM    478  CG2 ILE A  63      83.088  11.280  40.603  1.00 33.46           C  
ANISOU  478  CG2 ILE A  63     5208   3300   4204     78   -659    -84       C  
ATOM    479  CD1 ILE A  63      85.828  13.032  39.356  1.00 38.92           C  
ANISOU  479  CD1 ILE A  63     5503   4010   5275    117   -763   -181       C  
ATOM    480  N   SER A  64      80.982  11.062  37.483  1.00 28.30           N  
ANISOU  480  N   SER A  64     4386   2701   3666    128   -256    -99       N  
ATOM    481  CA  SER A  64      79.863  10.198  37.123  1.00 27.17           C  
ANISOU  481  CA  SER A  64     4295   2558   3470    126   -169    -74       C  
ATOM    482  C   SER A  64      80.266   9.238  35.957  1.00 32.31           C  
ANISOU  482  C   SER A  64     4867   3190   4218    179   -153    -52       C  
ATOM    483  O   SER A  64      79.991   8.041  36.042  1.00 33.51           O  
ANISOU  483  O   SER A  64     5080   3313   4340    190   -163    -17       O  
ATOM    484  CB  SER A  64      78.679  11.078  36.728  1.00 29.81           C  
ANISOU  484  CB  SER A  64     4619   2925   3784     95    -45   -109       C  
ATOM    485  OG  SER A  64      77.557  10.351  36.266  1.00 36.24           O  
ANISOU  485  OG  SER A  64     5451   3744   4573     88     39    -95       O  
ATOM    486  N   ASP A  65      80.941   9.757  34.899  1.00 28.08           N  
ANISOU  486  N   ASP A  65     4210   2666   3795    202   -122    -79       N  
ATOM    487  CA  ASP A  65      81.400   8.985  33.747  1.00 27.57           C  
ANISOU  487  CA  ASP A  65     4074   2583   3819    240    -83    -78       C  
ATOM    488  C   ASP A  65      82.445   7.973  34.149  1.00 32.70           C  
ANISOU  488  C   ASP A  65     4702   3184   4539    294   -186    -65       C  
ATOM    489  O   ASP A  65      82.299   6.802  33.804  1.00 32.48           O  
ANISOU  489  O   ASP A  65     4700   3119   4522    324   -173    -46       O  
ATOM    490  CB  ASP A  65      81.981   9.883  32.656  1.00 29.17           C  
ANISOU  490  CB  ASP A  65     4171   2804   4110    232    -17   -116       C  
ATOM    491  CG  ASP A  65      81.055  10.878  31.979  1.00 34.61           C  
ANISOU  491  CG  ASP A  65     4876   3520   4753    189     70   -122       C  
ATOM    492  OD1 ASP A  65      79.806  10.702  32.061  1.00 34.23           O  
ANISOU  492  OD1 ASP A  65     4897   3483   4628    175    100   -105       O  
ATOM    493  OD2 ASP A  65      81.572  11.811  31.346  1.00 33.37           O  
ANISOU  493  OD2 ASP A  65     4662   3368   4648    168    104   -145       O  
ATOM    494  N   LEU A  66      83.491   8.407  34.883  1.00 30.46           N  
ANISOU  494  N   LEU A  66     4370   2892   4313    308   -299    -76       N  
ATOM    495  CA  LEU A  66      84.555   7.518  35.365  1.00 30.95           C  
ANISOU  495  CA  LEU A  66     4396   2897   4467    370   -434    -62       C  
ATOM    496  C   LEU A  66      84.034   6.385  36.252  1.00 36.17           C  
ANISOU  496  C   LEU A  66     5210   3507   5025    381   -520      3       C  
ATOM    497  O   LEU A  66      84.528   5.269  36.137  1.00 35.87           O  
ANISOU  497  O   LEU A  66     5158   3403   5068    444   -581     22       O  
ATOM    498  CB  LEU A  66      85.682   8.288  36.066  1.00 31.11           C  
ANISOU  498  CB  LEU A  66     4335   2920   4565    372   -563    -86       C  
ATOM    499  CG  LEU A  66      86.603   9.093  35.145  1.00 36.25           C  
ANISOU  499  CG  LEU A  66     4806   3596   5372    370   -492   -152       C  
ATOM    500  CD1 LEU A  66      87.407  10.086  35.925  1.00 35.32           C  
ANISOU  500  CD1 LEU A  66     4633   3493   5295    340   -605   -178       C  
ATOM    501  CD2 LEU A  66      87.529   8.176  34.329  1.00 39.62           C  
ANISOU  501  CD2 LEU A  66     5093   3980   5981    441   -473   -184       C  
ATOM    502  N   ALA A  67      83.013   6.658  37.097  1.00 32.90           N  
ANISOU  502  N   ALA A  67     4946   3116   4439    314   -509     30       N  
ATOM    503  CA  ALA A  67      82.374   5.677  37.975  1.00 31.89           C  
ANISOU  503  CA  ALA A  67     4993   2942   4181    291   -560     91       C  
ATOM    504  C   ALA A  67      81.763   4.548  37.130  1.00 36.96           C  
ANISOU  504  C   ALA A  67     5649   3552   4841    312   -468    108       C  
ATOM    505  O   ALA A  67      81.958   3.369  37.441  1.00 38.66           O  
ANISOU  505  O   ALA A  67     5940   3689   5059    344   -548    155       O  
ATOM    506  CB  ALA A  67      81.303   6.355  38.815  1.00 32.38           C  
ANISOU  506  CB  ALA A  67     5185   3047   4069    199   -501     89       C  
ATOM    507  N   PHE A  68      81.083   4.910  36.029  1.00 32.43           N  
ANISOU  507  N   PHE A  68     5008   3029   4286    294   -313     69       N  
ATOM    508  CA  PHE A  68      80.493   3.955  35.089  1.00 31.11           C  
ANISOU  508  CA  PHE A  68     4848   2839   4135    301   -222     72       C  
ATOM    509  C   PHE A  68      81.564   3.260  34.230  1.00 36.67           C  
ANISOU  509  C   PHE A  68     5449   3489   4994    382   -241     51       C  
ATOM    510  O   PHE A  68      81.501   2.049  34.070  1.00 36.46           O  
ANISOU  510  O   PHE A  68     5474   3392   4986    410   -251     72       O  
ATOM    511  CB  PHE A  68      79.428   4.638  34.192  1.00 31.28           C  
ANISOU  511  CB  PHE A  68     4834   2928   4124    252    -78     38       C  
ATOM    512  CG  PHE A  68      78.981   3.799  33.012  1.00 31.38           C  
ANISOU  512  CG  PHE A  68     4836   2922   4165    255      6     28       C  
ATOM    513  CD1 PHE A  68      78.375   2.557  33.206  1.00 34.33           C  
ANISOU  513  CD1 PHE A  68     5311   3245   4490    238      9     60       C  
ATOM    514  CD2 PHE A  68      79.209   4.226  31.712  1.00 31.75           C  
ANISOU  514  CD2 PHE A  68     4789   2994   4278    263     81    -13       C  
ATOM    515  CE1 PHE A  68      77.992   1.766  32.113  1.00 34.82           C  
ANISOU  515  CE1 PHE A  68     5371   3284   4577    233     81     44       C  
ATOM    516  CE2 PHE A  68      78.812   3.447  30.619  1.00 34.07           C  
ANISOU  516  CE2 PHE A  68     5095   3268   4580    254    153    -27       C  
ATOM    517  CZ  PHE A  68      78.214   2.217  30.827  1.00 32.68           C  
ANISOU  517  CZ  PHE A  68     5011   3044   4364    242    150     -2       C  
ATOM    518  N   LEU A  69      82.498   4.028  33.631  1.00 34.22           N  
ANISOU  518  N   LEU A  69     4995   3207   4801    412   -226      0       N  
ATOM    519  CA  LEU A  69      83.543   3.492  32.748  1.00 33.90           C  
ANISOU  519  CA  LEU A  69     4833   3122   4926    480   -207    -45       C  
ATOM    520  C   LEU A  69      84.465   2.493  33.445  1.00 41.66           C  
ANISOU  520  C   LEU A  69     5808   4010   6010    563   -355    -22       C  
ATOM    521  O   LEU A  69      84.980   1.579  32.789  1.00 39.59           O  
ANISOU  521  O   LEU A  69     5492   3681   5869    625   -329    -51       O  
ATOM    522  CB  LEU A  69      84.352   4.612  32.064  1.00 32.60           C  
ANISOU  522  CB  LEU A  69     4518   3008   4860    473   -148   -107       C  
ATOM    523  CG  LEU A  69      83.594   5.477  31.070  1.00 34.95           C  
ANISOU  523  CG  LEU A  69     4822   3372   5084    402     -2   -130       C  
ATOM    524  CD1 LEU A  69      84.223   6.829  30.958  1.00 34.07           C  
ANISOU  524  CD1 LEU A  69     4618   3307   5019    372     14   -164       C  
ATOM    525  CD2 LEU A  69      83.475   4.805  29.704  1.00 35.30           C  
ANISOU  525  CD2 LEU A  69     4857   3398   5159    400    127   -167       C  
ATOM    526  N   CYS A  70      84.646   2.646  34.772  1.00 42.91           N  
ANISOU  526  N   CYS A  70     6033   4153   6116    563   -517     30       N  
ATOM    527  CA  CYS A  70      85.476   1.732  35.562  1.00 45.33           C  
ANISOU  527  CA  CYS A  70     6359   4358   6508    641   -703     70       C  
ATOM    528  C   CYS A  70      84.861   0.326  35.737  1.00 43.38           C  
ANISOU  528  C   CYS A  70     6267   4017   6199    655   -723    130       C  
ATOM    529  O   CYS A  70      85.600  -0.585  36.070  1.00 43.08           O  
ANISOU  529  O   CYS A  70     6230   3871   6268    738   -863    157       O  
ATOM    530  CB  CYS A  70      85.854   2.352  36.902  1.00 48.42           C  
ANISOU  530  CB  CYS A  70     6803   4757   6838    621   -884    112       C  
ATOM    531  SG  CYS A  70      87.193   3.562  36.787  1.00 54.48           S  
ANISOU  531  SG  CYS A  70     7348   5578   7775    643   -937     38       S  
ATOM    532  N   THR A  71      83.541   0.156  35.486  1.00 36.83           N  
ANISOU  532  N   THR A  71     5558   3222   5215    575   -590    146       N  
ATOM    533  CA  THR A  71      82.792  -1.111  35.581  1.00 35.98           C  
ANISOU  533  CA  THR A  71     5606   3032   5033    560   -580    197       C  
ATOM    534  C   THR A  71      82.792  -1.887  34.249  1.00 39.90           C  
ANISOU  534  C   THR A  71     6033   3489   5639    600   -458    142       C  
ATOM    535  O   THR A  71      82.545  -3.102  34.234  1.00 39.33           O  
ANISOU  535  O   THR A  71     6060   3314   5569    618   -475    172       O  
ATOM    536  CB  THR A  71      81.318  -0.858  35.946  1.00 35.78           C  
ANISOU  536  CB  THR A  71     5724   3069   4800    439   -483    227       C  
ATOM    537  OG1 THR A  71      80.599  -0.374  34.793  1.00 27.34           O  
ANISOU  537  OG1 THR A  71     4576   2084   3730    398   -308    167       O  
ATOM    538  CG2 THR A  71      81.143   0.031  37.171  1.00 27.34           C  
ANISOU  538  CG2 THR A  71     4736   2053   3601    377   -552    258       C  
ATOM    539  N   LEU A  72      82.983  -1.156  33.130  1.00 34.85           N  
ANISOU  539  N   LEU A  72     5248   2926   5069    598   -325     62       N  
ATOM    540  CA  LEU A  72      82.973  -1.702  31.776  1.00 32.81           C  
ANISOU  540  CA  LEU A  72     4933   2645   4887    614   -187     -5       C  
ATOM    541  C   LEU A  72      83.905  -2.904  31.595  1.00 38.46           C  
ANISOU  541  C   LEU A  72     5610   3227   5774    720   -239    -29       C  
ATOM    542  O   LEU A  72      83.407  -3.907  31.068  1.00 38.79           O  
ANISOU  542  O   LEU A  72     5732   3202   5803    714   -174    -38       O  
ATOM    543  CB  LEU A  72      83.222  -0.613  30.718  1.00 31.46           C  
ANISOU  543  CB  LEU A  72     4628   2570   4755    587    -56    -82       C  
ATOM    544  CG  LEU A  72      82.051   0.343  30.475  1.00 34.08           C  
ANISOU  544  CG  LEU A  72     5009   3010   4930    485     27    -69       C  
ATOM    545  CD1 LEU A  72      82.292   1.210  29.250  1.00 33.33           C  
ANISOU  545  CD1 LEU A  72     4816   2979   4869    456    152   -136       C  
ATOM    546  CD2 LEU A  72      80.729  -0.399  30.348  1.00 34.30           C  
ANISOU  546  CD2 LEU A  72     5172   3026   4834    423     73    -37       C  
ATOM    547  N   PRO A  73      85.194  -2.923  32.069  1.00 35.31           N  
ANISOU  547  N   PRO A  73     5096   2773   5547    820   -368    -40       N  
ATOM    548  CA  PRO A  73      86.002  -4.150  31.898  1.00 34.71           C  
ANISOU  548  CA  PRO A  73     4979   2549   5659    935   -424    -67       C  
ATOM    549  C   PRO A  73      85.328  -5.420  32.424  1.00 40.48           C  
ANISOU  549  C   PRO A  73     5910   3161   6310    937   -501     13       C  
ATOM    550  O   PRO A  73      85.506  -6.469  31.809  1.00 39.97           O  
ANISOU  550  O   PRO A  73     5848   2986   6355    995   -455    -28       O  
ATOM    551  CB  PRO A  73      87.308  -3.822  32.630  1.00 35.90           C  
ANISOU  551  CB  PRO A  73     4988   2670   5983   1029   -601    -67       C  
ATOM    552  CG  PRO A  73      87.410  -2.348  32.556  1.00 39.44           C  
ANISOU  552  CG  PRO A  73     5338   3264   6383    960   -546    -97       C  
ATOM    553  CD  PRO A  73      85.998  -1.861  32.725  1.00 35.39           C  
ANISOU  553  CD  PRO A  73     4996   2841   5608    836   -473    -39       C  
ATOM    554  N   MET A  74      84.508  -5.321  33.509  1.00 40.07           N  
ANISOU  554  N   MET A  74     6035   3127   6062    861   -594    119       N  
ATOM    555  CA  MET A  74      83.762  -6.457  34.084  1.00 41.34           C  
ANISOU  555  CA  MET A  74     6413   3179   6114    830   -651    204       C  
ATOM    556  C   MET A  74      82.642  -6.907  33.163  1.00 44.58           C  
ANISOU  556  C   MET A  74     6896   3610   6431    744   -462    171       C  
ATOM    557  O   MET A  74      82.464  -8.101  32.966  1.00 44.74           O  
ANISOU  557  O   MET A  74     7014   3506   6479    761   -460    181       O  
ATOM    558  CB  MET A  74      83.178  -6.126  35.461  1.00 44.75           C  
ANISOU  558  CB  MET A  74     7019   3636   6348    747   -769    312       C  
ATOM    559  CG  MET A  74      84.103  -6.429  36.610  1.00 50.45           C  
ANISOU  559  CG  MET A  74     7788   4252   7130    827  -1021    388       C  
ATOM    560  SD  MET A  74      83.672  -5.500  38.107  1.00 57.57           S  
ANISOU  560  SD  MET A  74     8847   5233   7795    717  -1137    477       S  
ATOM    561  CE  MET A  74      82.208  -6.231  38.544  1.00 54.27           C  
ANISOU  561  CE  MET A  74     8698   4783   7141    579  -1050    550       C  
ATOM    562  N   LEU A  75      81.878  -5.958  32.626  1.00 41.95           N  
ANISOU  562  N   LEU A  75     6522   3426   5992    650   -320    133       N  
ATOM    563  CA  LEU A  75      80.788  -6.186  31.675  1.00 42.53           C  
ANISOU  563  CA  LEU A  75     6641   3540   5979    561   -156     95       C  
ATOM    564  C   LEU A  75      81.341  -6.837  30.400  1.00 45.26           C  
ANISOU  564  C   LEU A  75     6908   3821   6468    621    -61      1       C  
ATOM    565  O   LEU A  75      80.809  -7.849  29.957  1.00 45.01           O  
ANISOU  565  O   LEU A  75     6973   3708   6418    595     -9    -10       O  
ATOM    566  CB  LEU A  75      80.123  -4.844  31.313  1.00 42.84           C  
ANISOU  566  CB  LEU A  75     6614   3746   5919    476    -57     68       C  
ATOM    567  CG  LEU A  75      78.908  -4.412  32.109  1.00 48.57           C  
ANISOU  567  CG  LEU A  75     7442   4542   6470    368    -56    127       C  
ATOM    568  CD1 LEU A  75      79.264  -4.139  33.606  1.00 50.11           C  
ANISOU  568  CD1 LEU A  75     7698   4724   6619    382   -197    200       C  
ATOM    569  CD2 LEU A  75      78.300  -3.145  31.502  1.00 48.22           C  
ANISOU  569  CD2 LEU A  75     7310   4638   6372    306     47     84       C  
ATOM    570  N   ILE A  76      82.411  -6.257  29.823  1.00 41.12           N  
ANISOU  570  N   ILE A  76     6211   3326   6086    694    -29    -75       N  
ATOM    571  CA  ILE A  76      83.065  -6.782  28.617  1.00 40.17           C  
ANISOU  571  CA  ILE A  76     6004   3146   6111    748     86   -185       C  
ATOM    572  C   ILE A  76      83.477  -8.255  28.820  1.00 42.77           C  
ANISOU  572  C   ILE A  76     6395   3290   6566    840     18   -183       C  
ATOM    573  O   ILE A  76      83.155  -9.075  27.969  1.00 40.74           O  
ANISOU  573  O   ILE A  76     6196   2967   6314    821    125   -240       O  
ATOM    574  CB  ILE A  76      84.233  -5.871  28.109  1.00 42.46           C  
ANISOU  574  CB  ILE A  76     6091   3496   6545    801    139   -269       C  
ATOM    575  CG1 ILE A  76      83.755  -4.401  27.895  1.00 42.08           C  
ANISOU  575  CG1 ILE A  76     6009   3616   6364    704    199   -260       C  
ATOM    576  CG2 ILE A  76      84.872  -6.431  26.821  1.00 42.19           C  
ANISOU  576  CG2 ILE A  76     5979   3402   6649    838    299   -400       C  
ATOM    577  CD1 ILE A  76      84.820  -3.371  28.094  1.00 42.39           C  
ANISOU  577  CD1 ILE A  76     5880   3711   6515    746    170   -290       C  
ATOM    578  N   ARG A  77      84.133  -8.594  29.953  1.00 41.15           N  
ANISOU  578  N   ARG A  77     6194   2992   6449    932   -172   -112       N  
ATOM    579  CA  ARG A  77      84.540  -9.976  30.228  1.00 42.09           C  
ANISOU  579  CA  ARG A  77     6382   2914   6698   1029   -266    -97       C  
ATOM    580  C   ARG A  77      83.360 -10.907  30.417  1.00 46.18           C  
ANISOU  580  C   ARG A  77     7128   3361   7058    942   -258    -30       C  
ATOM    581  O   ARG A  77      83.342 -11.980  29.809  1.00 46.14           O  
ANISOU  581  O   ARG A  77     7174   3228   7129    971   -198    -81       O  
ATOM    582  CB  ARG A  77      85.533 -10.093  31.394  1.00 46.30           C  
ANISOU  582  CB  ARG A  77     6873   3353   7366   1150   -504    -29       C  
ATOM    583  CG  ARG A  77      86.904  -9.459  31.120  1.00 70.41           C  
ANISOU  583  CG  ARG A  77     9665   6429  10659   1263   -515   -123       C  
ATOM    584  CD  ARG A  77      87.827 -10.276  30.204  1.00 90.50           C  
ANISOU  584  CD  ARG A  77    12073   8843  13470   1384   -428   -252       C  
ATOM    585  NE  ARG A  77      87.511 -10.129  28.776  1.00 99.94           N  
ANISOU  585  NE  ARG A  77    13232  10111  14628   1309   -155   -377       N  
ATOM    586  CZ  ARG A  77      87.888  -9.108  28.007  1.00110.38           C  
ANISOU  586  CZ  ARG A  77    14396  11567  15978   1271      0   -473       C  
ATOM    587  NH1 ARG A  77      87.547  -9.072  26.726  1.00 91.82           N  
ANISOU  587  NH1 ARG A  77    12059   9265  13564   1190    233   -574       N  
ATOM    588  NH2 ARG A  77      88.599  -8.108  28.519  1.00 98.84           N  
ANISOU  588  NH2 ARG A  77    12775  10185  14595   1300    -81   -468       N  
ATOM    589  N   SER A  78      82.358 -10.492  31.225  1.00 41.69           N  
ANISOU  589  N   SER A  78     6694   2872   6274    826   -300     71       N  
ATOM    590  CA  SER A  78      81.165 -11.305  31.446  1.00 41.20           C  
ANISOU  590  CA  SER A  78     6841   2753   6059    719   -275    130       C  
ATOM    591  C   SER A  78      80.405 -11.588  30.133  1.00 45.12           C  
ANISOU  591  C   SER A  78     7342   3285   6517    638    -82     39       C  
ATOM    592  O   SER A  78      79.908 -12.689  29.951  1.00 45.32           O  
ANISOU  592  O   SER A  78     7500   3193   6524    603    -58     43       O  
ATOM    593  CB  SER A  78      80.252 -10.658  32.472  1.00 44.58           C  
ANISOU  593  CB  SER A  78     7383   3278   6279    600   -319    230       C  
ATOM    594  OG  SER A  78      79.682  -9.461  31.966  1.00 58.36           O  
ANISOU  594  OG  SER A  78     9028   5212   7932    519   -199    185       O  
ATOM    595  N   TYR A  79      80.336 -10.613  29.218  1.00 40.98           N  
ANISOU  595  N   TYR A  79     6686   2910   5976    603     44    -41       N  
ATOM    596  CA  TYR A  79      79.653 -10.790  27.935  1.00 40.02           C  
ANISOU  596  CA  TYR A  79     6578   2825   5802    520    205   -126       C  
ATOM    597  C   TYR A  79      80.431 -11.681  26.963  1.00 43.38           C  
ANISOU  597  C   TYR A  79     6973   3124   6385    600    281   -233       C  
ATOM    598  O   TYR A  79      79.830 -12.551  26.318  1.00 42.61           O  
ANISOU  598  O   TYR A  79     6983   2955   6251    541    355   -273       O  
ATOM    599  CB  TYR A  79      79.331  -9.439  27.285  1.00 39.86           C  
ANISOU  599  CB  TYR A  79     6453   2992   5700    452    295   -165       C  
ATOM    600  CG  TYR A  79      78.141  -8.744  27.890  1.00 40.42           C  
ANISOU  600  CG  TYR A  79     6575   3179   5603    339    273    -90       C  
ATOM    601  CD1 TYR A  79      76.917  -9.398  28.022  1.00 42.19           C  
ANISOU  601  CD1 TYR A  79     6932   3381   5718    231    290    -56       C  
ATOM    602  CD2 TYR A  79      78.211  -7.410  28.270  1.00 41.30           C  
ANISOU  602  CD2 TYR A  79     6594   3422   5676    334    251    -67       C  
ATOM    603  CE1 TYR A  79      75.805  -8.749  28.560  1.00 43.33           C  
ANISOU  603  CE1 TYR A  79     7098   3633   5733    126    290     -5       C  
ATOM    604  CE2 TYR A  79      77.106  -6.748  28.797  1.00 42.77           C  
ANISOU  604  CE2 TYR A  79     6815   3708   5729    237    247    -15       C  
ATOM    605  CZ  TYR A  79      75.910  -7.426  28.961  1.00 53.52           C  
ANISOU  605  CZ  TYR A  79     8291   5046   6996    136    270     13       C  
ATOM    606  OH  TYR A  79      74.831  -6.758  29.488  1.00 61.59           O  
ANISOU  606  OH  TYR A  79     9323   6166   7912     43    282     47       O  
ATOM    607  N   ALA A  80      81.763 -11.461  26.869  1.00 39.80           N  
ANISOU  607  N   ALA A  80     6368   2641   6115    730    267   -290       N  
ATOM    608  CA  ALA A  80      82.663 -12.194  25.981  1.00 40.12           C  
ANISOU  608  CA  ALA A  80     6343   2562   6340    821    359   -415       C  
ATOM    609  C   ALA A  80      82.729 -13.678  26.329  1.00 47.73           C  
ANISOU  609  C   ALA A  80     7427   3310   7397    888    287   -397       C  
ATOM    610  O   ALA A  80      82.835 -14.504  25.425  1.00 48.84           O  
ANISOU  610  O   ALA A  80     7597   3349   7610    900    402   -501       O  
ATOM    611  CB  ALA A  80      84.052 -11.573  26.000  1.00 40.37           C  
ANISOU  611  CB  ALA A  80     6163   2609   6568    943    347   -474       C  
ATOM    612  N   THR A  81      82.630 -14.014  27.637  1.00 45.30           N  
ANISOU  612  N   THR A  81     7211   2928   7074    920     98   -264       N  
ATOM    613  CA  THR A  81      82.679 -15.378  28.164  1.00 44.77           C  
ANISOU  613  CA  THR A  81     7287   2641   7083    980     -9   -215       C  
ATOM    614  C   THR A  81      81.275 -15.940  28.487  1.00 51.15           C  
ANISOU  614  C   THR A  81     8326   3431   7678    827     -7   -129       C  
ATOM    615  O   THR A  81      81.132 -17.136  28.724  1.00 51.94           O  
ANISOU  615  O   THR A  81     8577   3345   7814    842    -56    -99       O  
ATOM    616  CB  THR A  81      83.623 -15.448  29.399  1.00 48.52           C  
ANISOU  616  CB  THR A  81     7729   3018   7690   1118   -240   -120       C  
ATOM    617  OG1 THR A  81      82.998 -14.873  30.556  1.00 42.39           O  
ANISOU  617  OG1 THR A  81     7061   2329   6718   1030   -363     24       O  
ATOM    618  CG2 THR A  81      85.016 -14.833  29.143  1.00 43.22           C  
ANISOU  618  CG2 THR A  81     6798   2374   7249   1262   -253   -209       C  
ATOM    619  N   GLY A  82      80.269 -15.076  28.529  1.00 49.51           N  
ANISOU  619  N   GLY A  82     8138   3406   7266    683     47    -90       N  
ATOM    620  CA  GLY A  82      78.894 -15.455  28.836  1.00 50.49           C  
ANISOU  620  CA  GLY A  82     8444   3539   7201    523     65    -22       C  
ATOM    621  C   GLY A  82      78.643 -15.836  30.287  1.00 57.91           C  
ANISOU  621  C   GLY A  82     9541   4396   8065    502    -90    126       C  
ATOM    622  O   GLY A  82      77.614 -16.446  30.589  1.00 59.46           O  
ANISOU  622  O   GLY A  82     9910   4544   8136    376    -71    180       O  
ATOM    623  N   ASN A  83      79.558 -15.460  31.205  1.00 54.30           N  
ANISOU  623  N   ASN A  83     9036   3922   7672    610   -243    192       N  
ATOM    624  CA  ASN A  83      79.444 -15.794  32.624  1.00 53.87           C  
ANISOU  624  CA  ASN A  83     9160   3781   7528    587   -408    338       C  
ATOM    625  C   ASN A  83      79.905 -14.639  33.559  1.00 54.54           C  
ANISOU  625  C   ASN A  83     9174   3982   7569    617   -525    401       C  
ATOM    626  O   ASN A  83      80.974 -14.071  33.349  1.00 54.30           O  
ANISOU  626  O   ASN A  83     8961   3980   7692    747   -579    353       O  
ATOM    627  CB  ASN A  83      80.215 -17.116  32.876  1.00 57.01           C  
ANISOU  627  CB  ASN A  83     9668   3915   8078    706   -544    375       C  
ATOM    628  CG  ASN A  83      80.311 -17.611  34.304  1.00 88.05           C  
ANISOU  628  CG  ASN A  83    13818   7711  11924    693   -745    536       C  
ATOM    629  OD1 ASN A  83      79.441 -17.387  35.162  1.00 82.67           O  
ANISOU  629  OD1 ASN A  83    13294   7096  11021    538   -740    627       O  
ATOM    630  ND2 ASN A  83      81.385 -18.331  34.573  1.00 80.82           N  
ANISOU  630  ND2 ASN A  83    12924   6594  11191    854   -926    571       N  
ATOM    631  N   TRP A  84      79.080 -14.299  34.580  1.00 47.94           N  
ANISOU  631  N   TRP A  84     8483   3208   6524    484   -553    500       N  
ATOM    632  CA  TRP A  84      79.374 -13.274  35.583  1.00 46.19           C  
ANISOU  632  CA  TRP A  84     8245   3083   6220    483   -661    563       C  
ATOM    633  C   TRP A  84      80.093 -13.927  36.762  1.00 50.08           C  
ANISOU  633  C   TRP A  84     8904   3397   6725    550   -899    685       C  
ATOM    634  O   TRP A  84      79.465 -14.686  37.504  1.00 51.42           O  
ANISOU  634  O   TRP A  84     9322   3459   6757    452   -938    782       O  
ATOM    635  CB  TRP A  84      78.084 -12.612  36.074  1.00 44.77           C  
ANISOU  635  CB  TRP A  84     8152   3051   5809    298   -550    592       C  
ATOM    636  CG  TRP A  84      78.348 -11.473  37.014  1.00 46.07           C  
ANISOU  636  CG  TRP A  84     8295   3326   5886    289   -632    634       C  
ATOM    637  CD1 TRP A  84      78.333 -11.513  38.377  1.00 48.93           C  
ANISOU  637  CD1 TRP A  84     8853   3638   6102    232   -760    744       C  
ATOM    638  CD2 TRP A  84      78.776 -10.156  36.657  1.00 45.90           C  
ANISOU  638  CD2 TRP A  84     8057   3466   5919    340   -603    563       C  
ATOM    639  NE1 TRP A  84      78.664 -10.280  38.890  1.00 47.91           N  
ANISOU  639  NE1 TRP A  84     8640   3637   5926    239   -804    738       N  
ATOM    640  CE2 TRP A  84      78.943  -9.429  37.857  1.00 49.49           C  
ANISOU  640  CE2 TRP A  84     8582   3966   6255    307   -710    629       C  
ATOM    641  CE3 TRP A  84      78.984  -9.498  35.432  1.00 47.30           C  
ANISOU  641  CE3 TRP A  84     8006   3750   6214    393   -487    451       C  
ATOM    642  CZ2 TRP A  84      79.338  -8.086  37.869  1.00 49.05           C  
ANISOU  642  CZ2 TRP A  84     8366   4055   6217    334   -710    583       C  
ATOM    643  CZ3 TRP A  84      79.385  -8.170  35.443  1.00 48.66           C  
ANISOU  643  CZ3 TRP A  84     8025   4063   6402    418   -487    414       C  
ATOM    644  CH2 TRP A  84      79.548  -7.473  36.648  1.00 49.36           C  
ANISOU  644  CH2 TRP A  84     8176   4191   6387    391   -597    477       C  
ATOM    645  N   THR A  85      81.392 -13.641  36.952  1.00 44.92           N  
ANISOU  645  N   THR A  85     8121   2708   6238    709  -1065    682       N  
ATOM    646  CA  THR A  85      82.176 -14.284  38.021  1.00 44.17           C  
ANISOU  646  CA  THR A  85     8170   2427   6185    794  -1335    799       C  
ATOM    647  C   THR A  85      82.521 -13.360  39.177  1.00 48.65           C  
ANISOU  647  C   THR A  85     8772   3072   6639    774  -1498    876       C  
ATOM    648  O   THR A  85      83.303 -13.743  40.050  1.00 49.25           O  
ANISOU  648  O   THR A  85     8947   3007   6759    854  -1755    971       O  
ATOM    649  CB  THR A  85      83.459 -14.894  37.439  1.00 49.19           C  
ANISOU  649  CB  THR A  85     8642   2912   7134   1006  -1442    741       C  
ATOM    650  OG1 THR A  85      84.335 -13.836  37.039  1.00 52.83           O  
ANISOU  650  OG1 THR A  85     8819   3507   7748   1101  -1436    646       O  
ATOM    651  CG2 THR A  85      83.189 -15.860  36.280  1.00 43.29           C  
ANISOU  651  CG2 THR A  85     7878   2069   6501   1028  -1278    653       C  
ATOM    652  N   TYR A  86      81.958 -12.145  39.180  1.00 44.55           N  
ANISOU  652  N   TYR A  86     8176   2768   5982    669  -1362    832       N  
ATOM    653  CA  TYR A  86      82.258 -11.099  40.158  1.00 43.61           C  
ANISOU  653  CA  TYR A  86     8070   2746   5755    639  -1482    876       C  
ATOM    654  C   TYR A  86      81.336 -11.054  41.371  1.00 48.57           C  
ANISOU  654  C   TYR A  86     8991   3382   6083    461  -1494    982       C  
ATOM    655  O   TYR A  86      81.557 -10.240  42.267  1.00 47.74           O  
ANISOU  655  O   TYR A  86     8935   3343   5861    421  -1595   1019       O  
ATOM    656  CB  TYR A  86      82.281  -9.745  39.448  1.00 43.74           C  
ANISOU  656  CB  TYR A  86     7829   2976   5815    639  -1329    759       C  
ATOM    657  CG  TYR A  86      83.219  -9.744  38.269  1.00 43.55           C  
ANISOU  657  CG  TYR A  86     7530   2947   6070    792  -1293    649       C  
ATOM    658  CD1 TYR A  86      84.600  -9.786  38.453  1.00 45.28           C  
ANISOU  658  CD1 TYR A  86     7616   3083   6504    950  -1493    644       C  
ATOM    659  CD2 TYR A  86      82.730  -9.768  36.965  1.00 43.50           C  
ANISOU  659  CD2 TYR A  86     7405   3006   6116    774  -1061    545       C  
ATOM    660  CE1 TYR A  86      85.471  -9.831  37.369  1.00 46.87           C  
ANISOU  660  CE1 TYR A  86     7561   3274   6974   1082  -1432    528       C  
ATOM    661  CE2 TYR A  86      83.592  -9.830  35.872  1.00 44.00           C  
ANISOU  661  CE2 TYR A  86     7244   3054   6419    899  -1006    436       C  
ATOM    662  CZ  TYR A  86      84.961  -9.857  36.080  1.00 51.73           C  
ANISOU  662  CZ  TYR A  86     8082   3955   7616   1051  -1177    423       C  
ATOM    663  OH  TYR A  86      85.817  -9.871  35.014  1.00 53.92           O  
ANISOU  663  OH  TYR A  86     8126   4224   8137   1162  -1095    300       O  
ATOM    664  N   GLY A  87      80.328 -11.922  41.397  1.00 46.88           N  
ANISOU  664  N   GLY A  87     8972   3097   5744    345  -1383   1022       N  
ATOM    665  CA  GLY A  87      79.394 -11.985  42.512  1.00 47.96           C  
ANISOU  665  CA  GLY A  87     9398   3230   5595    155  -1357   1113       C  
ATOM    666  C   GLY A  87      78.289 -10.944  42.505  1.00 54.63           C  
ANISOU  666  C   GLY A  87    10196   4283   6279      0  -1118   1042       C  
ATOM    667  O   GLY A  87      78.305  -9.984  41.724  1.00 52.50           O  
ANISOU  667  O   GLY A  87     9669   4171   6106     43  -1000    933       O  
ATOM    668  N   ASP A  88      77.327 -11.153  43.421  1.00 53.51           N  
ANISOU  668  N   ASP A  88    10315   4127   5890   -187  -1050   1107       N  
ATOM    669  CA  ASP A  88      76.102 -10.388  43.641  1.00 53.41           C  
ANISOU  669  CA  ASP A  88    10314   4274   5706   -364   -816   1050       C  
ATOM    670  C   ASP A  88      76.280  -8.909  43.920  1.00 54.88           C  
ANISOU  670  C   ASP A  88    10360   4632   5860   -356   -795    986       C  
ATOM    671  O   ASP A  88      75.603  -8.119  43.281  1.00 55.47           O  
ANISOU  671  O   ASP A  88    10245   4859   5971   -386   -601    881       O  
ATOM    672  CB  ASP A  88      75.278 -11.031  44.779  1.00 55.68           C  
ANISOU  672  CB  ASP A  88    10951   4472   5733   -564   -782   1146       C  
ATOM    673  CG  ASP A  88      74.400 -12.184  44.351  1.00 66.93           C  
ANISOU  673  CG  ASP A  88    12485   5797   7148   -660   -654   1163       C  
ATOM    674  OD1 ASP A  88      73.759 -12.794  45.229  1.00 69.49           O  
ANISOU  674  OD1 ASP A  88    13120   5997   7289   -801   -673   1263       O  
ATOM    675  OD2 ASP A  88      74.342 -12.469  43.134  1.00 71.37           O  
ANISOU  675  OD2 ASP A  88    12835   6404   7877   -607   -535   1075       O  
ATOM    676  N   VAL A  89      77.141  -8.536  44.891  1.00 49.61           N  
ANISOU  676  N   VAL A  89     9800   3932   5120   -325  -1001   1050       N  
ATOM    677  CA  VAL A  89      77.381  -7.146  45.345  1.00 48.24           C  
ANISOU  677  CA  VAL A  89     9540   3899   4891   -333  -1008    998       C  
ATOM    678  C   VAL A  89      77.879  -6.239  44.220  1.00 49.03           C  
ANISOU  678  C   VAL A  89     9289   4123   5218   -192   -965    886       C  
ATOM    679  O   VAL A  89      77.313  -5.168  44.015  1.00 47.50           O  
ANISOU  679  O   VAL A  89     8969   4079   4998   -242   -802    798       O  
ATOM    680  CB  VAL A  89      78.300  -7.095  46.598  1.00 51.72           C  
ANISOU  680  CB  VAL A  89    10186   4253   5212   -327  -1281   1098       C  
ATOM    681  CG1 VAL A  89      78.702  -5.663  46.945  1.00 51.59           C  
ANISOU  681  CG1 VAL A  89    10052   4373   5177   -315  -1309   1032       C  
ATOM    682  CG2 VAL A  89      77.624  -7.771  47.789  1.00 51.29           C  
ANISOU  682  CG2 VAL A  89    10517   4101   4869   -515  -1279   1200       C  
ATOM    683  N   LEU A  90      78.913  -6.680  43.486  1.00 45.53           N  
ANISOU  683  N   LEU A  90     8694   3608   4999    -22  -1100    888       N  
ATOM    684  CA  LEU A  90      79.460  -5.944  42.348  1.00 44.71           C  
ANISOU  684  CA  LEU A  90     8273   3604   5111    102  -1049    784       C  
ATOM    685  C   LEU A  90      78.451  -5.861  41.223  1.00 45.69           C  
ANISOU  685  C   LEU A  90     8267   3819   5275     60   -797    698       C  
ATOM    686  O   LEU A  90      78.446  -4.878  40.512  1.00 43.92           O  
ANISOU  686  O   LEU A  90     7835   3720   5131     91   -699    610       O  
ATOM    687  CB  LEU A  90      80.772  -6.563  41.862  1.00 44.98           C  
ANISOU  687  CB  LEU A  90     8185   3525   5379    282  -1232    795       C  
ATOM    688  CG  LEU A  90      82.042  -6.042  42.535  1.00 49.27           C  
ANISOU  688  CG  LEU A  90     8686   4047   5988    370  -1477    823       C  
ATOM    689  CD1 LEU A  90      83.185  -6.998  42.322  1.00 49.49           C  
ANISOU  689  CD1 LEU A  90     8657   3914   6234    532  -1682    858       C  
ATOM    690  CD2 LEU A  90      82.423  -4.688  42.003  1.00 50.74           C  
ANISOU  690  CD2 LEU A  90     8619   4389   6271    407  -1407    720       C  
ATOM    691  N   CYS A  91      77.558  -6.861  41.094  1.00 43.10           N  
ANISOU  691  N   CYS A  91     8071   3424   4879    -24   -698    725       N  
ATOM    692  CA  CYS A  91      76.486  -6.849  40.097  1.00 42.41           C  
ANISOU  692  CA  CYS A  91     7879   3418   4817    -84   -476    647       C  
ATOM    693  C   CYS A  91      75.504  -5.713  40.420  1.00 42.53           C  
ANISOU  693  C   CYS A  91     7861   3586   4711   -202   -321    593       C  
ATOM    694  O   CYS A  91      75.184  -4.932  39.534  1.00 41.05           O  
ANISOU  694  O   CYS A  91     7476   3515   4606   -181   -208    507       O  
ATOM    695  CB  CYS A  91      75.790  -8.204  40.041  1.00 43.40           C  
ANISOU  695  CB  CYS A  91     8170   3423   4895   -161   -426    692       C  
ATOM    696  SG  CYS A  91      74.375  -8.271  38.916  1.00 48.15           S  
ANISOU  696  SG  CYS A  91     8660   4116   5519   -258   -178    600       S  
ATOM    697  N   ILE A  92      75.070  -5.604  41.698  1.00 39.05           N  
ANISOU  697  N   ILE A  92     7623   3136   4076   -322   -323    641       N  
ATOM    698  CA  ILE A  92      74.169  -4.560  42.198  1.00 39.14           C  
ANISOU  698  CA  ILE A  92     7629   3273   3968   -439   -173    584       C  
ATOM    699  C   ILE A  92      74.836  -3.171  42.055  1.00 41.67           C  
ANISOU  699  C   ILE A  92     7772   3702   4360   -351   -215    524       C  
ATOM    700  O   ILE A  92      74.235  -2.269  41.475  1.00 41.67           O  
ANISOU  700  O   ILE A  92     7606   3817   4410   -363    -75    437       O  
ATOM    701  CB  ILE A  92      73.737  -4.833  43.680  1.00 43.13           C  
ANISOU  701  CB  ILE A  92     8431   3722   4235   -593   -173    650       C  
ATOM    702  CG1 ILE A  92      73.062  -6.223  43.885  1.00 44.35           C  
ANISOU  702  CG1 ILE A  92     8785   3759   4306   -703   -118    714       C  
ATOM    703  CG2 ILE A  92      72.861  -3.696  44.273  1.00 44.63           C  
ANISOU  703  CG2 ILE A  92     8620   4035   4302   -713     -5    573       C  
ATOM    704  CD1 ILE A  92      71.771  -6.546  43.059  1.00 56.06           C  
ANISOU  704  CD1 ILE A  92    10154   5296   5851   -784    107    640       C  
ATOM    705  N   SER A  93      76.072  -3.010  42.565  1.00 37.21           N  
ANISOU  705  N   SER A  93     7236   3089   3811   -265   -418    571       N  
ATOM    706  CA  SER A  93      76.755  -1.723  42.543  1.00 37.65           C  
ANISOU  706  CA  SER A  93     7140   3236   3927   -200   -464    517       C  
ATOM    707  C   SER A  93      77.064  -1.226  41.125  1.00 40.85           C  
ANISOU  707  C   SER A  93     7272   3709   4541    -89   -412    443       C  
ATOM    708  O   SER A  93      77.011  -0.014  40.888  1.00 41.21           O  
ANISOU  708  O   SER A  93     7183   3857   4618    -81   -350    375       O  
ATOM    709  CB  SER A  93      77.987  -1.715  43.451  1.00 42.46           C  
ANISOU  709  CB  SER A  93     7847   3779   4507   -151   -705    581       C  
ATOM    710  OG  SER A  93      79.014  -2.610  43.071  1.00 53.47           O  
ANISOU  710  OG  SER A  93     9243   5052   6023    -39   -884    646       O  
ATOM    711  N   ASN A  94      77.278  -2.145  40.173  1.00 35.82           N  
ANISOU  711  N   ASN A  94     6569   3010   4030    -17   -418    452       N  
ATOM    712  CA  ASN A  94      77.516  -1.789  38.770  1.00 34.02           C  
ANISOU  712  CA  ASN A  94     6115   2838   3974     67   -349    380       C  
ATOM    713  C   ASN A  94      76.238  -1.352  38.093  1.00 37.23           C  
ANISOU  713  C   ASN A  94     6454   3336   4354     -9   -158    320       C  
ATOM    714  O   ASN A  94      76.282  -0.415  37.303  1.00 37.35           O  
ANISOU  714  O   ASN A  94     6306   3437   4449     25   -100    259       O  
ATOM    715  CB  ASN A  94      78.170  -2.928  38.001  1.00 30.38           C  
ANISOU  715  CB  ASN A  94     5621   2274   3649    160   -405    395       C  
ATOM    716  CG  ASN A  94      79.634  -3.102  38.285  1.00 58.23           C  
ANISOU  716  CG  ASN A  94     9112   5723   7290    278   -595    424       C  
ATOM    717  OD1 ASN A  94      80.175  -2.630  39.303  1.00 57.34           O  
ANISOU  717  OD1 ASN A  94     9059   5607   7122    277   -730    461       O  
ATOM    718  ND2 ASN A  94      80.308  -3.800  37.389  1.00 54.21           N  
ANISOU  718  ND2 ASN A  94     8503   5144   6950    379   -613    399       N  
ATOM    719  N   ARG A  95      75.095  -2.018  38.397  1.00 32.99           N  
ANISOU  719  N   ARG A  95     6042   2780   3713   -117    -65    338       N  
ATOM    720  CA  ARG A  95      73.772  -1.655  37.859  1.00 32.22           C  
ANISOU  720  CA  ARG A  95     5872   2766   3606   -197    105    278       C  
ATOM    721  C   ARG A  95      73.402  -0.241  38.345  1.00 37.27           C  
ANISOU  721  C   ARG A  95     6450   3507   4203   -230    163    227       C  
ATOM    722  O   ARG A  95      72.741   0.497  37.630  1.00 36.15           O  
ANISOU  722  O   ARG A  95     6166   3445   4125   -231    254    164       O  
ATOM    723  CB  ARG A  95      72.711  -2.665  38.342  1.00 29.32           C  
ANISOU  723  CB  ARG A  95     5659   2348   3135   -322    188    305       C  
ATOM    724  CG  ARG A  95      71.412  -2.671  37.522  1.00 32.22           C  
ANISOU  724  CG  ARG A  95     5925   2774   3543   -391    338    243       C  
ATOM    725  CD  ARG A  95      70.473  -3.843  37.833  1.00 38.92           C  
ANISOU  725  CD  ARG A  95     6911   3558   4319   -516    416    267       C  
ATOM    726  NE  ARG A  95      71.190  -5.099  38.119  1.00 52.72           N  
ANISOU  726  NE  ARG A  95     8832   5166   6033   -497    311    351       N  
ATOM    727  CZ  ARG A  95      70.640  -6.308  38.135  1.00 73.47           C  
ANISOU  727  CZ  ARG A  95    11583   7705   8627   -580    349    382       C  
ATOM    728  NH1 ARG A  95      69.365  -6.471  37.809  1.00 71.35           N  
ANISOU  728  NH1 ARG A  95    11266   7481   8364   -692    493    330       N  
ATOM    729  NH2 ARG A  95      71.376  -7.372  38.425  1.00 63.42           N  
ANISOU  729  NH2 ARG A  95    10473   6289   7334   -547    234    462       N  
ATOM    730  N   TYR A  96      73.823   0.117  39.576  1.00 35.96           N  
ANISOU  730  N   TYR A  96     6404   3329   3929   -258    100    254       N  
ATOM    731  CA  TYR A  96      73.550   1.413  40.180  1.00 35.83           C  
ANISOU  731  CA  TYR A  96     6360   3391   3862   -294    154    201       C  
ATOM    732  C   TYR A  96      74.333   2.531  39.517  1.00 38.60           C  
ANISOU  732  C   TYR A  96     6538   3797   4332   -193    100    162       C  
ATOM    733  O   TYR A  96      73.735   3.563  39.225  1.00 38.65           O  
ANISOU  733  O   TYR A  96     6435   3875   4373   -203    194     96       O  
ATOM    734  CB  TYR A  96      73.750   1.407  41.730  1.00 37.46           C  
ANISOU  734  CB  TYR A  96     6782   3560   3890   -375    103    239       C  
ATOM    735  CG  TYR A  96      73.925   2.805  42.299  1.00 39.30           C  
ANISOU  735  CG  TYR A  96     6984   3858   4089   -381    108    182       C  
ATOM    736  CD1 TYR A  96      72.850   3.691  42.370  1.00 40.93           C  
ANISOU  736  CD1 TYR A  96     7127   4138   4284   -444    281     93       C  
ATOM    737  CD2 TYR A  96      75.186   3.278  42.657  1.00 39.85           C  
ANISOU  737  CD2 TYR A  96     7062   3913   4169   -314    -63    207       C  
ATOM    738  CE1 TYR A  96      73.021   5.000  42.814  1.00 41.44           C  
ANISOU  738  CE1 TYR A  96     7161   4251   4335   -441    290     32       C  
ATOM    739  CE2 TYR A  96      75.368   4.585  43.099  1.00 41.08           C  
ANISOU  739  CE2 TYR A  96     7184   4123   4302   -322    -59    148       C  
ATOM    740  CZ  TYR A  96      74.284   5.443  43.179  1.00 48.82           C  
ANISOU  740  CZ  TYR A  96     8122   5168   5259   -386    121     61       C  
ATOM    741  OH  TYR A  96      74.473   6.734  43.606  1.00 48.36           O  
ANISOU  741  OH  TYR A  96     8038   5150   5188   -390    126     -3       O  
ATOM    742  N   VAL A  97      75.661   2.364  39.327  1.00 34.69           N  
ANISOU  742  N   VAL A  97     6014   3259   3906    -99    -49    198       N  
ATOM    743  CA  VAL A  97      76.537   3.405  38.722  1.00 33.69           C  
ANISOU  743  CA  VAL A  97     5725   3178   3897    -16    -95    159       C  
ATOM    744  C   VAL A  97      76.198   3.632  37.235  1.00 35.01           C  
ANISOU  744  C   VAL A  97     5731   3388   4184     23     -3    116       C  
ATOM    745  O   VAL A  97      76.350   4.743  36.745  1.00 34.62           O  
ANISOU  745  O   VAL A  97     5566   3392   4196     48     22     72       O  
ATOM    746  CB  VAL A  97      78.065   3.178  38.962  1.00 37.41           C  
ANISOU  746  CB  VAL A  97     6186   3594   4433     67   -274    196       C  
ATOM    747  CG1 VAL A  97      78.378   3.026  40.457  1.00 37.10           C  
ANISOU  747  CG1 VAL A  97     6329   3510   4258     20   -397    245       C  
ATOM    748  CG2 VAL A  97      78.584   1.972  38.191  1.00 36.92           C  
ANISOU  748  CG2 VAL A  97     6090   3459   4477    140   -320    226       C  
ATOM    749  N   LEU A  98      75.729   2.582  36.531  1.00 29.66           N  
ANISOU  749  N   LEU A  98     5064   2678   3529     18     43    130       N  
ATOM    750  CA  LEU A  98      75.290   2.658  35.143  1.00 29.19           C  
ANISOU  750  CA  LEU A  98     4888   2651   3552     34    122     94       C  
ATOM    751  C   LEU A  98      74.106   3.620  35.066  1.00 31.51           C  
ANISOU  751  C   LEU A  98     5129   3018   3824    -22    221     49       C  
ATOM    752  O   LEU A  98      74.127   4.536  34.248  1.00 30.97           O  
ANISOU  752  O   LEU A  98     4951   2994   3823      8    240     16       O  
ATOM    753  CB  LEU A  98      74.861   1.259  34.674  1.00 29.87           C  
ANISOU  753  CB  LEU A  98     5032   2679   3639     15    148    115       C  
ATOM    754  CG  LEU A  98      74.399   1.040  33.228  1.00 35.19           C  
ANISOU  754  CG  LEU A  98     5622   3371   4377     18    214     81       C  
ATOM    755  CD1 LEU A  98      74.490  -0.429  32.896  1.00 36.12           C  
ANISOU  755  CD1 LEU A  98     5810   3403   4512     25    203    101       C  
ATOM    756  CD2 LEU A  98      72.940   1.456  33.014  1.00 35.67           C  
ANISOU  756  CD2 LEU A  98     5656   3490   4408    -61    304     52       C  
ATOM    757  N   HIS A  99      73.070   3.399  35.897  1.00 27.68           N  
ANISOU  757  N   HIS A  99     4724   2539   3255   -105    287     45       N  
ATOM    758  CA  HIS A  99      71.868   4.231  35.908  1.00 27.31           C  
ANISOU  758  CA  HIS A  99     4610   2552   3215   -153    388    -11       C  
ATOM    759  C   HIS A  99      72.118   5.596  36.536  1.00 32.44           C  
ANISOU  759  C   HIS A  99     5231   3237   3858   -139    386    -47       C  
ATOM    760  O   HIS A  99      71.590   6.584  36.014  1.00 31.82           O  
ANISOU  760  O   HIS A  99     5042   3199   3851   -123    427    -93       O  
ATOM    761  CB  HIS A  99      70.677   3.495  36.529  1.00 27.56           C  
ANISOU  761  CB  HIS A  99     4717   2575   3180   -256    485    -19       C  
ATOM    762  CG  HIS A  99      70.217   2.353  35.676  1.00 30.83           C  
ANISOU  762  CG  HIS A  99     5128   2959   3625   -277    498     -1       C  
ATOM    763  ND1 HIS A  99      70.607   1.048  35.941  1.00 32.46           N  
ANISOU  763  ND1 HIS A  99     5467   3090   3775   -296    460     56       N  
ATOM    764  CD2 HIS A  99      69.506   2.369  34.523  1.00 32.58           C  
ANISOU  764  CD2 HIS A  99     5239   3208   3932   -277    527    -30       C  
ATOM    765  CE1 HIS A  99      70.064   0.310  34.991  1.00 31.87           C  
ANISOU  765  CE1 HIS A  99     5359   3001   3750   -315    486     50       C  
ATOM    766  NE2 HIS A  99      69.397   1.067  34.110  1.00 32.65           N  
ANISOU  766  NE2 HIS A  99     5312   3164   3928   -308    522     -1       N  
ATOM    767  N   ALA A 100      72.973   5.674  37.599  1.00 28.65           N  
ANISOU  767  N   ALA A 100     4853   2732   3299   -141    318    -23       N  
ATOM    768  CA  ALA A 100      73.357   6.956  38.236  1.00 26.99           C  
ANISOU  768  CA  ALA A 100     4632   2548   3074   -133    302    -61       C  
ATOM    769  C   ALA A 100      74.089   7.824  37.216  1.00 31.17           C  
ANISOU  769  C   ALA A 100     5026   3097   3722    -52    252    -73       C  
ATOM    770  O   ALA A 100      73.766   9.004  37.109  1.00 32.41           O  
ANISOU  770  O   ALA A 100     5113   3282   3919    -47    293   -122       O  
ATOM    771  CB  ALA A 100      74.215   6.730  39.468  1.00 27.16           C  
ANISOU  771  CB  ALA A 100     4800   2534   2985   -155    208    -26       C  
ATOM    772  N   ASN A 101      74.948   7.222  36.360  1.00 27.03           N  
ANISOU  772  N   ASN A 101     4459   2549   3260      5    183    -34       N  
ATOM    773  CA  ASN A 101      75.595   7.947  35.258  1.00 26.77           C  
ANISOU  773  CA  ASN A 101     4308   2531   3331     61    164    -48       C  
ATOM    774  C   ASN A 101      74.583   8.493  34.239  1.00 30.33           C  
ANISOU  774  C   ASN A 101     4679   3012   3832     55    240    -75       C  
ATOM    775  O   ASN A 101      74.677   9.666  33.907  1.00 31.08           O  
ANISOU  775  O   ASN A 101     4713   3123   3973     70    243   -100       O  
ATOM    776  CB  ASN A 101      76.689   7.127  34.533  1.00 24.21           C  
ANISOU  776  CB  ASN A 101     3955   2174   3070    113    105    -18       C  
ATOM    777  CG  ASN A 101      77.480   7.907  33.483  1.00 40.19           C  
ANISOU  777  CG  ASN A 101     5869   4211   5189    151    105    -39       C  
ATOM    778  OD1 ASN A 101      77.757   7.402  32.402  1.00 38.90           O  
ANISOU  778  OD1 ASN A 101     5666   4035   5077    171    130    -39       O  
ATOM    779  ND2 ASN A 101      77.866   9.160  33.757  1.00 27.44           N  
ANISOU  779  ND2 ASN A 101     4216   2617   3593    149     89    -64       N  
ATOM    780  N   LEU A 102      73.635   7.673  33.743  1.00 25.04           N  
ANISOU  780  N   LEU A 102     4014   2342   3158     30    288    -68       N  
ATOM    781  CA  LEU A 102      72.650   8.148  32.758  1.00 24.94           C  
ANISOU  781  CA  LEU A 102     3924   2352   3199     24    329    -90       C  
ATOM    782  C   LEU A 102      71.897   9.410  33.216  1.00 28.23           C  
ANISOU  782  C   LEU A 102     4294   2789   3642     17    365   -135       C  
ATOM    783  O   LEU A 102      71.809  10.404  32.482  1.00 26.27           O  
ANISOU  783  O   LEU A 102     3978   2543   3459     45    349   -146       O  
ATOM    784  CB  LEU A 102      71.610   7.048  32.514  1.00 25.33           C  
ANISOU  784  CB  LEU A 102     3992   2398   3233    -21    370    -86       C  
ATOM    785  CG  LEU A 102      71.404   6.419  31.121  1.00 31.92           C  
ANISOU  785  CG  LEU A 102     4803   3227   4100    -22    358    -73       C  
ATOM    786  CD1 LEU A 102      72.730   6.251  30.320  1.00 32.41           C  
ANISOU  786  CD1 LEU A 102     4875   3265   4173     22    318    -51       C  
ATOM    787  CD2 LEU A 102      70.743   5.038  31.277  1.00 33.50           C  
ANISOU  787  CD2 LEU A 102     5056   3407   4265    -77    392    -65       C  
ATOM    788  N   TYR A 103      71.353   9.335  34.443  1.00 25.43           N  
ANISOU  788  N   TYR A 103     3988   2440   3235    -26    419   -164       N  
ATOM    789  CA  TYR A 103      70.464  10.311  35.045  1.00 24.14           C  
ANISOU  789  CA  TYR A 103     3784   2289   3100    -42    486   -228       C  
ATOM    790  C   TYR A 103      71.172  11.492  35.669  1.00 27.16           C  
ANISOU  790  C   TYR A 103     4181   2663   3474    -20    465   -255       C  
ATOM    791  O   TYR A 103      70.649  12.582  35.497  1.00 26.32           O  
ANISOU  791  O   TYR A 103     4003   2552   3444      3    490   -301       O  
ATOM    792  CB  TYR A 103      69.499   9.610  35.997  1.00 23.74           C  
ANISOU  792  CB  TYR A 103     3782   2246   2993   -117    585   -261       C  
ATOM    793  CG  TYR A 103      68.622   8.645  35.219  1.00 24.86           C  
ANISOU  793  CG  TYR A 103     3876   2392   3175   -143    608   -248       C  
ATOM    794  CD1 TYR A 103      68.621   7.278  35.508  1.00 26.15           C  
ANISOU  794  CD1 TYR A 103     4136   2542   3259   -199    624   -211       C  
ATOM    795  CD2 TYR A 103      67.897   9.075  34.109  1.00 25.49           C  
ANISOU  795  CD2 TYR A 103     3830   2483   3373   -111    588   -264       C  
ATOM    796  CE1 TYR A 103      67.851   6.381  34.761  1.00 27.05           C  
ANISOU  796  CE1 TYR A 103     4211   2655   3410   -232    640   -204       C  
ATOM    797  CE2 TYR A 103      67.125   8.196  33.361  1.00 26.26           C  
ANISOU  797  CE2 TYR A 103     3887   2585   3506   -142    590   -255       C  
ATOM    798  CZ  TYR A 103      67.102   6.851  33.689  1.00 35.24           C  
ANISOU  798  CZ  TYR A 103     5114   3713   4565   -206    623   -229       C  
ATOM    799  OH  TYR A 103      66.329   6.026  32.920  1.00 32.32           O  
ANISOU  799  OH  TYR A 103     4703   3343   4235   -244    621   -226       O  
ATOM    800  N   THR A 104      72.379  11.335  36.283  1.00 24.18           N  
ANISOU  800  N   THR A 104     3887   2276   3023    -21    403   -227       N  
ATOM    801  CA  THR A 104      73.114  12.513  36.780  1.00 23.98           C  
ANISOU  801  CA  THR A 104     3870   2242   2999     -7    369   -255       C  
ATOM    802  C   THR A 104      73.650  13.304  35.593  1.00 30.71           C  
ANISOU  802  C   THR A 104     4632   3086   3951     46    321   -240       C  
ATOM    803  O   THR A 104      73.664  14.515  35.649  1.00 32.44           O  
ANISOU  803  O   THR A 104     4822   3290   4214     58    326   -278       O  
ATOM    804  CB  THR A 104      74.269  12.169  37.723  1.00 29.47           C  
ANISOU  804  CB  THR A 104     4667   2927   3603    -26    290   -230       C  
ATOM    805  OG1 THR A 104      75.172  11.279  37.079  1.00 25.94           O  
ANISOU  805  OG1 THR A 104     4206   2472   3180      9    210   -167       O  
ATOM    806  CG2 THR A 104      73.809  11.624  39.087  1.00 27.14           C  
ANISOU  806  CG2 THR A 104     4509   2629   3174    -99    331   -245       C  
ATOM    807  N   SER A 105      74.020  12.626  34.495  1.00 27.74           N  
ANISOU  807  N   SER A 105     4222   2711   3606     69    286   -190       N  
ATOM    808  CA  SER A 105      74.544  13.242  33.278  1.00 26.91           C  
ANISOU  808  CA  SER A 105     4057   2596   3572     99    256   -171       C  
ATOM    809  C   SER A 105      73.628  14.267  32.673  1.00 32.48           C  
ANISOU  809  C   SER A 105     4712   3287   4343    112    276   -191       C  
ATOM    810  O   SER A 105      74.073  15.392  32.410  1.00 33.70           O  
ANISOU  810  O   SER A 105     4850   3416   4538    124    254   -197       O  
ATOM    811  CB  SER A 105      74.883  12.181  32.238  1.00 28.24           C  
ANISOU  811  CB  SER A 105     4219   2767   3745    107    243   -128       C  
ATOM    812  OG  SER A 105      76.088  11.532  32.597  1.00 35.50           O  
ANISOU  812  OG  SER A 105     5159   3680   4649    116    203   -113       O  
ATOM    813  N   ILE A 106      72.365  13.876  32.401  1.00 28.47           N  
ANISOU  813  N   ILE A 106     4175   2786   3855    109    307   -198       N  
ATOM    814  CA  ILE A 106      71.368  14.776  31.812  1.00 27.89           C  
ANISOU  814  CA  ILE A 106     4039   2690   3870    133    302   -216       C  
ATOM    815  C   ILE A 106      71.037  15.922  32.811  1.00 32.82           C  
ANISOU  815  C   ILE A 106     4647   3290   4533    145    339   -282       C  
ATOM    816  O   ILE A 106      70.833  17.047  32.377  1.00 32.69           O  
ANISOU  816  O   ILE A 106     4596   3229   4595    178    310   -291       O  
ATOM    817  CB  ILE A 106      70.125  13.993  31.266  1.00 30.19           C  
ANISOU  817  CB  ILE A 106     4283   2995   4193    124    310   -213       C  
ATOM    818  CG1 ILE A 106      69.239  14.894  30.355  1.00 31.21           C  
ANISOU  818  CG1 ILE A 106     4342   3088   4428    160    255   -212       C  
ATOM    819  CG2 ILE A 106      69.329  13.323  32.376  1.00 27.35           C  
ANISOU  819  CG2 ILE A 106     3917   2661   3814     90    394   -263       C  
ATOM    820  CD1 ILE A 106      68.253  14.183  29.412  1.00 37.69           C  
ANISOU  820  CD1 ILE A 106     5116   3917   5285    149    213   -193       C  
ATOM    821  N   LEU A 107      71.065  15.652  34.143  1.00 29.74           N  
ANISOU  821  N   LEU A 107     4302   2919   4079    113    401   -328       N  
ATOM    822  CA  LEU A 107      70.832  16.700  35.143  1.00 29.09           C  
ANISOU  822  CA  LEU A 107     4227   2812   4015    112    452   -405       C  
ATOM    823  C   LEU A 107      72.002  17.685  35.226  1.00 31.21           C  
ANISOU  823  C   LEU A 107     4533   3050   4276    120    397   -400       C  
ATOM    824  O   LEU A 107      71.769  18.899  35.299  1.00 31.19           O  
ANISOU  824  O   LEU A 107     4508   3000   4345    144    406   -445       O  
ATOM    825  CB  LEU A 107      70.479  16.138  36.524  1.00 28.74           C  
ANISOU  825  CB  LEU A 107     4249   2793   3879     54    543   -459       C  
ATOM    826  CG  LEU A 107      68.999  16.072  36.877  1.00 32.77           C  
ANISOU  826  CG  LEU A 107     4697   3307   4448     39    657   -532       C  
ATOM    827  CD1 LEU A 107      68.810  15.379  38.213  1.00 33.91           C  
ANISOU  827  CD1 LEU A 107     4946   3476   4463    -45    757   -574       C  
ATOM    828  CD2 LEU A 107      68.386  17.438  36.973  1.00 33.60           C  
ANISOU  828  CD2 LEU A 107     4724   3364   4677     83    698   -615       C  
ATOM    829  N   PHE A 108      73.250  17.183  35.151  1.00 26.61           N  
ANISOU  829  N   PHE A 108     3996   2487   3626    103    338   -348       N  
ATOM    830  CA  PHE A 108      74.419  18.059  35.150  1.00 27.23           C  
ANISOU  830  CA  PHE A 108     4090   2540   3714    100    285   -346       C  
ATOM    831  C   PHE A 108      74.360  19.019  33.952  1.00 31.24           C  
ANISOU  831  C   PHE A 108     4550   3002   4317    130    260   -323       C  
ATOM    832  O   PHE A 108      74.565  20.206  34.134  1.00 31.34           O  
ANISOU  832  O   PHE A 108     4571   2967   4371    130    253   -355       O  
ATOM    833  CB  PHE A 108      75.760  17.290  35.272  1.00 28.77           C  
ANISOU  833  CB  PHE A 108     4314   2763   3854     80    223   -304       C  
ATOM    834  CG  PHE A 108      76.014  16.763  36.673  1.00 30.94           C  
ANISOU  834  CG  PHE A 108     4670   3057   4029     44    211   -328       C  
ATOM    835  CD1 PHE A 108      75.870  17.590  37.790  1.00 34.69           C  
ANISOU  835  CD1 PHE A 108     5204   3514   4462     12    232   -395       C  
ATOM    836  CD2 PHE A 108      76.414  15.442  36.879  1.00 32.85           C  
ANISOU  836  CD2 PHE A 108     4947   3322   4210     38    174   -283       C  
ATOM    837  CE1 PHE A 108      76.091  17.091  39.086  1.00 35.35           C  
ANISOU  837  CE1 PHE A 108     5395   3611   4424    -37    214   -412       C  
ATOM    838  CE2 PHE A 108      76.616  14.943  38.181  1.00 34.59           C  
ANISOU  838  CE2 PHE A 108     5273   3548   4323     -2    145   -291       C  
ATOM    839  CZ  PHE A 108      76.438  15.762  39.269  1.00 32.62           C  
ANISOU  839  CZ  PHE A 108     5095   3288   4012    -45    165   -353       C  
ATOM    840  N   LEU A 109      73.932  18.524  32.777  1.00 28.31           N  
ANISOU  840  N   LEU A 109     4147   2637   3974    148    245   -271       N  
ATOM    841  CA  LEU A 109      73.767  19.318  31.565  1.00 27.75           C  
ANISOU  841  CA  LEU A 109     4059   2514   3969    166    207   -234       C  
ATOM    842  C   LEU A 109      72.614  20.307  31.652  1.00 32.84           C  
ANISOU  842  C   LEU A 109     4670   3101   4705    207    208   -273       C  
ATOM    843  O   LEU A 109      72.703  21.405  31.093  1.00 34.15           O  
ANISOU  843  O   LEU A 109     4849   3197   4930    222    167   -257       O  
ATOM    844  CB  LEU A 109      73.665  18.428  30.322  1.00 27.18           C  
ANISOU  844  CB  LEU A 109     3986   2464   3876    161    183   -170       C  
ATOM    845  CG  LEU A 109      74.974  18.277  29.497  1.00 31.53           C  
ANISOU  845  CG  LEU A 109     4571   3018   4392    124    172   -125       C  
ATOM    846  CD1 LEU A 109      75.526  19.635  29.042  1.00 30.98           C  
ANISOU  846  CD1 LEU A 109     4528   2884   4358    107    152   -115       C  
ATOM    847  CD2 LEU A 109      76.050  17.517  30.252  1.00 31.36           C  
ANISOU  847  CD2 LEU A 109     4544   3040   4330    108    193   -142       C  
ATOM    848  N   THR A 110      71.564  19.945  32.389  1.00 28.98           N  
ANISOU  848  N   THR A 110     4139   2632   4238    224    260   -328       N  
ATOM    849  CA  THR A 110      70.410  20.801  32.628  1.00 29.25           C  
ANISOU  849  CA  THR A 110     4113   2610   4388    271    279   -389       C  
ATOM    850  C   THR A 110      70.896  22.009  33.418  1.00 34.54           C  
ANISOU  850  C   THR A 110     4821   3225   5076    271    303   -448       C  
ATOM    851  O   THR A 110      70.610  23.144  33.041  1.00 34.96           O  
ANISOU  851  O   THR A 110     4858   3193   5233    314    268   -459       O  
ATOM    852  CB  THR A 110      69.299  19.987  33.330  1.00 34.87           C  
ANISOU  852  CB  THR A 110     4766   3368   5113    267    362   -450       C  
ATOM    853  OG1 THR A 110      68.898  18.967  32.426  1.00 33.76           O  
ANISOU  853  OG1 THR A 110     4596   3268   4963    260    323   -389       O  
ATOM    854  CG2 THR A 110      68.076  20.820  33.684  1.00 33.31           C  
ANISOU  854  CG2 THR A 110     4477   3114   5066    318    405   -536       C  
ATOM    855  N   PHE A 111      71.703  21.759  34.466  1.00 31.30           N  
ANISOU  855  N   PHE A 111     4473   2856   4563    221    347   -481       N  
ATOM    856  CA  PHE A 111      72.235  22.806  35.324  1.00 30.56           C  
ANISOU  856  CA  PHE A 111     4430   2716   4463    203    367   -547       C  
ATOM    857  C   PHE A 111      73.291  23.643  34.619  1.00 35.22           C  
ANISOU  857  C   PHE A 111     5052   3256   5073    193    291   -496       C  
ATOM    858  O   PHE A 111      73.252  24.862  34.790  1.00 37.46           O  
ANISOU  858  O   PHE A 111     5352   3458   5424    206    292   -542       O  
ATOM    859  CB  PHE A 111      72.684  22.260  36.683  1.00 31.70           C  
ANISOU  859  CB  PHE A 111     4646   2916   4481    143    418   -596       C  
ATOM    860  CG  PHE A 111      71.466  22.031  37.550  1.00 32.84           C  
ANISOU  860  CG  PHE A 111     4777   3070   4629    141    532   -685       C  
ATOM    861  CD1 PHE A 111      70.757  23.108  38.088  1.00 35.80           C  
ANISOU  861  CD1 PHE A 111     5136   3378   5090    163    606   -791       C  
ATOM    862  CD2 PHE A 111      70.994  20.742  37.792  1.00 33.72           C  
ANISOU  862  CD2 PHE A 111     4891   3250   4672    113    577   -670       C  
ATOM    863  CE1 PHE A 111      69.613  22.896  38.874  1.00 36.62           C  
ANISOU  863  CE1 PHE A 111     5214   3490   5212    154    740   -890       C  
ATOM    864  CE2 PHE A 111      69.845  20.529  38.565  1.00 36.48           C  
ANISOU  864  CE2 PHE A 111     5223   3607   5029     93    706   -759       C  
ATOM    865  CZ  PHE A 111      69.165  21.604  39.108  1.00 35.35           C  
ANISOU  865  CZ  PHE A 111     5054   3405   4974    113    794   -873       C  
ATOM    866  N   ILE A 112      74.143  23.050  33.753  1.00 30.35           N  
ANISOU  866  N   ILE A 112     4443   2677   4414    169    238   -410       N  
ATOM    867  CA  ILE A 112      75.091  23.838  32.929  1.00 29.87           C  
ANISOU  867  CA  ILE A 112     4409   2565   4377    144    187   -363       C  
ATOM    868  C   ILE A 112      74.280  24.800  32.012  1.00 33.03           C  
ANISOU  868  C   ILE A 112     4806   2868   4876    189    152   -337       C  
ATOM    869  O   ILE A 112      74.576  25.984  32.003  1.00 33.72           O  
ANISOU  869  O   ILE A 112     4931   2870   5013    181    135   -349       O  
ATOM    870  CB  ILE A 112      76.118  22.979  32.122  1.00 32.55           C  
ANISOU  870  CB  ILE A 112     4748   2960   4661    104    165   -292       C  
ATOM    871  CG1 ILE A 112      76.940  22.068  33.058  1.00 32.49           C  
ANISOU  871  CG1 ILE A 112     4735   3028   4580     75    171   -315       C  
ATOM    872  CG2 ILE A 112      77.063  23.885  31.316  1.00 32.02           C  
ANISOU  872  CG2 ILE A 112     4710   2835   4620     58    142   -257       C  
ATOM    873  CD1 ILE A 112      77.321  20.705  32.546  1.00 34.87           C  
ANISOU  873  CD1 ILE A 112     5014   3394   4839     72    167   -265       C  
ATOM    874  N   SER A 113      73.215  24.305  31.327  1.00 28.56           N  
ANISOU  874  N   SER A 113     4198   2306   4347    237    131   -304       N  
ATOM    875  CA  SER A 113      72.324  25.115  30.458  1.00 27.30           C  
ANISOU  875  CA  SER A 113     4032   2049   4292    290     64   -271       C  
ATOM    876  C   SER A 113      71.688  26.312  31.190  1.00 31.83           C  
ANISOU  876  C   SER A 113     4584   2524   4984    344     78   -353       C  
ATOM    877  O   SER A 113      71.485  27.353  30.576  1.00 31.84           O  
ANISOU  877  O   SER A 113     4616   2411   5070    375      9   -323       O  
ATOM    878  CB  SER A 113      71.206  24.252  29.877  1.00 27.49           C  
ANISOU  878  CB  SER A 113     3993   2108   4344    330     32   -244       C  
ATOM    879  OG  SER A 113      71.755  23.147  29.183  1.00 32.21           O  
ANISOU  879  OG  SER A 113     4620   2784   4834    281     25   -178       O  
ATOM    880  N   ILE A 114      71.316  26.136  32.475  1.00 27.94           N  
ANISOU  880  N   ILE A 114     4051   2069   4497    354    169   -458       N  
ATOM    881  CA  ILE A 114      70.731  27.195  33.294  1.00 27.77           C  
ANISOU  881  CA  ILE A 114     4010   1958   4582    398    215   -563       C  
ATOM    882  C   ILE A 114      71.858  28.186  33.648  1.00 32.97           C  
ANISOU  882  C   ILE A 114     4762   2557   5207    348    212   -579       C  
ATOM    883  O   ILE A 114      71.631  29.390  33.662  1.00 33.06           O  
ANISOU  883  O   ILE A 114     4792   2445   5324    385    194   -614       O  
ATOM    884  CB  ILE A 114      70.024  26.609  34.545  1.00 29.96           C  
ANISOU  884  CB  ILE A 114     4236   2301   4847    398    339   -676       C  
ATOM    885  CG1 ILE A 114      68.852  25.673  34.123  1.00 28.92           C  
ANISOU  885  CG1 ILE A 114     3996   2218   4774    439    344   -664       C  
ATOM    886  CG2 ILE A 114      69.566  27.731  35.512  1.00 27.91           C  
ANISOU  886  CG2 ILE A 114     3975   1951   4681    427    420   -809       C  
ATOM    887  CD1 ILE A 114      68.315  24.749  35.247  1.00 34.04           C  
ANISOU  887  CD1 ILE A 114     4613   2956   5364    402    480   -752       C  
ATOM    888  N   ASP A 115      73.082  27.670  33.866  1.00 29.73           N  
ANISOU  888  N   ASP A 115     4405   2227   4663    266    217   -551       N  
ATOM    889  CA  ASP A 115      74.223  28.515  34.138  1.00 29.35           C  
ANISOU  889  CA  ASP A 115     4431   2134   4588    204    204   -564       C  
ATOM    890  C   ASP A 115      74.532  29.402  32.917  1.00 33.72           C  
ANISOU  890  C   ASP A 115     5026   2585   5203    201    129   -481       C  
ATOM    891  O   ASP A 115      74.743  30.605  33.102  1.00 32.57           O  
ANISOU  891  O   ASP A 115     4931   2329   5116    191    121   -515       O  
ATOM    892  CB  ASP A 115      75.468  27.704  34.568  1.00 30.42           C  
ANISOU  892  CB  ASP A 115     4587   2377   4595    122    205   -550       C  
ATOM    893  CG  ASP A 115      76.555  28.607  35.148  1.00 39.77           C  
ANISOU  893  CG  ASP A 115     5829   3518   5764     52    193   -594       C  
ATOM    894  OD1 ASP A 115      76.269  29.332  36.141  1.00 38.81           O  
ANISOU  894  OD1 ASP A 115     5744   3344   5658     52    230   -693       O  
ATOM    895  OD2 ASP A 115      77.675  28.616  34.598  1.00 42.89           O  
ANISOU  895  OD2 ASP A 115     6230   3928   6138     -8    155   -539       O  
ATOM    896  N   ARG A 116      74.537  28.808  31.687  1.00 29.74           N  
ANISOU  896  N   ARG A 116     4516   2107   4675    200     79   -374       N  
ATOM    897  CA  ARG A 116      74.833  29.522  30.435  1.00 28.75           C  
ANISOU  897  CA  ARG A 116     4461   1888   4574    177     10   -280       C  
ATOM    898  C   ARG A 116      73.794  30.583  30.135  1.00 35.78           C  
ANISOU  898  C   ARG A 116     5368   2630   5596    257    -51   -280       C  
ATOM    899  O   ARG A 116      74.144  31.673  29.664  1.00 37.56           O  
ANISOU  899  O   ARG A 116     5680   2731   5859    232    -96   -244       O  
ATOM    900  CB  ARG A 116      75.026  28.570  29.228  1.00 24.66           C  
ANISOU  900  CB  ARG A 116     3954   1436   3978    147    -19   -177       C  
ATOM    901  CG  ARG A 116      76.031  27.391  29.394  1.00 27.66           C  
ANISOU  901  CG  ARG A 116     4305   1953   4252     82     38   -176       C  
ATOM    902  CD  ARG A 116      77.289  27.683  30.210  1.00 29.63           C  
ANISOU  902  CD  ARG A 116     4555   2226   4477     12     81   -230       C  
ATOM    903  NE  ARG A 116      78.190  28.614  29.527  1.00 32.43           N  
ANISOU  903  NE  ARG A 116     4979   2503   4842    -67     76   -193       N  
ATOM    904  CZ  ARG A 116      79.282  29.134  30.072  1.00 39.04           C  
ANISOU  904  CZ  ARG A 116     5817   3334   5683   -140    101   -238       C  
ATOM    905  NH1 ARG A 116      79.613  28.839  31.322  1.00 29.33           N  
ANISOU  905  NH1 ARG A 116     4534   2169   4442   -138    113   -317       N  
ATOM    906  NH2 ARG A 116      80.039  29.976  29.380  1.00 24.63           N  
ANISOU  906  NH2 ARG A 116     4054   1431   3872   -225    108   -203       N  
ATOM    907  N   TYR A 117      72.523  30.296  30.446  1.00 33.19           N  
ANISOU  907  N   TYR A 117     4951   2306   5352    353    -53   -326       N  
ATOM    908  CA  TYR A 117      71.430  31.246  30.266  1.00 33.41           C  
ANISOU  908  CA  TYR A 117     4958   2189   5547    452   -117   -344       C  
ATOM    909  C   TYR A 117      71.603  32.406  31.262  1.00 37.05           C  
ANISOU  909  C   TYR A 117     5445   2549   6083    461    -62   -451       C  
ATOM    910  O   TYR A 117      71.501  33.571  30.873  1.00 37.08           O  
ANISOU  910  O   TYR A 117     5510   2392   6188    492   -129   -430       O  
ATOM    911  CB  TYR A 117      70.063  30.544  30.444  1.00 35.46           C  
ANISOU  911  CB  TYR A 117     5083   2495   5897    543   -112   -390       C  
ATOM    912  CG  TYR A 117      68.911  31.512  30.619  1.00 38.36           C  
ANISOU  912  CG  TYR A 117     5382   2716   6476    659   -150   -454       C  
ATOM    913  CD1 TYR A 117      68.409  32.231  29.539  1.00 40.21           C  
ANISOU  913  CD1 TYR A 117     5646   2811   6822    722   -308   -365       C  
ATOM    914  CD2 TYR A 117      68.358  31.749  31.878  1.00 39.81           C  
ANISOU  914  CD2 TYR A 117     5482   2892   6752    704    -29   -609       C  
ATOM    915  CE1 TYR A 117      67.387  33.165  29.703  1.00 42.14           C  
ANISOU  915  CE1 TYR A 117     5817   2903   7291    843   -360   -427       C  
ATOM    916  CE2 TYR A 117      67.339  32.687  32.055  1.00 41.08           C  
ANISOU  916  CE2 TYR A 117     5567   2907   7135    818    -49   -687       C  
ATOM    917  CZ  TYR A 117      66.836  33.372  30.958  1.00 49.78           C  
ANISOU  917  CZ  TYR A 117     6676   3865   8373    896   -222   -595       C  
ATOM    918  OH  TYR A 117      65.827  34.296  31.110  1.00 52.87           O  
ANISOU  918  OH  TYR A 117     6977   4097   9013   1024   -261   -671       O  
ATOM    919  N   LEU A 118      71.864  32.090  32.542  1.00 33.62           N  
ANISOU  919  N   LEU A 118     4982   2198   5594    430     55   -563       N  
ATOM    920  CA  LEU A 118      72.026  33.117  33.567  1.00 33.09           C  
ANISOU  920  CA  LEU A 118     4952   2043   5577    426    118   -681       C  
ATOM    921  C   LEU A 118      73.223  34.006  33.282  1.00 37.48           C  
ANISOU  921  C   LEU A 118     5626   2521   6093    340     77   -637       C  
ATOM    922  O   LEU A 118      73.127  35.214  33.462  1.00 35.97           O  
ANISOU  922  O   LEU A 118     5487   2178   6002    362     68   -685       O  
ATOM    923  CB  LEU A 118      72.074  32.532  34.994  1.00 32.60           C  
ANISOU  923  CB  LEU A 118     4866   2092   5430    389    244   -805       C  
ATOM    924  CG  LEU A 118      70.737  32.035  35.569  1.00 37.15           C  
ANISOU  924  CG  LEU A 118     5334   2701   6080    465    329   -899       C  
ATOM    925  CD1 LEU A 118      70.950  31.234  36.858  1.00 37.77           C  
ANISOU  925  CD1 LEU A 118     5431   2904   6014    393    449   -991       C  
ATOM    926  CD2 LEU A 118      69.774  33.178  35.815  1.00 38.35           C  
ANISOU  926  CD2 LEU A 118     5447   2694   6431    560    357  -1002       C  
ATOM    927  N   LEU A 119      74.310  33.414  32.753  1.00 35.11           N  
ANISOU  927  N   LEU A 119     5363   2314   5663    245     56   -548       N  
ATOM    928  CA  LEU A 119      75.543  34.112  32.416  1.00 34.91           C  
ANISOU  928  CA  LEU A 119     5432   2236   5597    142     34   -507       C  
ATOM    929  C   LEU A 119      75.363  35.060  31.236  1.00 42.99           C  
ANISOU  929  C   LEU A 119     6539   3097   6697    154    -51   -411       C  
ATOM    930  O   LEU A 119      76.019  36.098  31.160  1.00 43.48           O  
ANISOU  930  O   LEU A 119     6694   3045   6781     91    -61   -409       O  
ATOM    931  CB  LEU A 119      76.650  33.081  32.151  1.00 34.02           C  
ANISOU  931  CB  LEU A 119     5303   2272   5351     47     49   -451       C  
ATOM    932  CG  LEU A 119      78.067  33.625  32.026  1.00 37.41           C  
ANISOU  932  CG  LEU A 119     5792   2680   5743    -79     53   -435       C  
ATOM    933  CD1 LEU A 119      78.567  34.244  33.347  1.00 36.02           C  
ANISOU  933  CD1 LEU A 119     5631   2482   5573   -124     84   -556       C  
ATOM    934  CD2 LEU A 119      78.985  32.572  31.479  1.00 37.93           C  
ANISOU  934  CD2 LEU A 119     5817   2877   5717   -149     67   -373       C  
ATOM    935  N   MET A 120      74.458  34.712  30.329  1.00 42.74           N  
ANISOU  935  N   MET A 120     6487   3048   6703    230   -122   -329       N  
ATOM    936  CA  MET A 120      74.101  35.511  29.167  1.00 43.60           C  
ANISOU  936  CA  MET A 120     6692   2998   6877    253   -234   -222       C  
ATOM    937  C   MET A 120      73.470  36.822  29.639  1.00 45.59           C  
ANISOU  937  C   MET A 120     6967   3059   7295    335   -264   -291       C  
ATOM    938  O   MET A 120      73.800  37.872  29.091  1.00 47.34           O  
ANISOU  938  O   MET A 120     7317   3121   7551    299   -325   -233       O  
ATOM    939  CB  MET A 120      73.118  34.697  28.316  1.00 47.20           C  
ANISOU  939  CB  MET A 120     7097   3495   7342    329   -316   -143       C  
ATOM    940  CG  MET A 120      72.759  35.308  26.983  1.00 51.91           C  
ANISOU  940  CG  MET A 120     7808   3939   7976    346   -465    -12       C  
ATOM    941  SD  MET A 120      71.445  34.306  26.247  1.00 56.68           S  
ANISOU  941  SD  MET A 120     8324   4604   8607    443   -574     50       S  
ATOM    942  CE  MET A 120      72.365  33.367  25.144  1.00 53.66           C  
ANISOU  942  CE  MET A 120     8043   4340   8004    302   -559    165       C  
ATOM    943  N   LYS A 121      72.600  36.771  30.669  1.00 39.80           N  
ANISOU  943  N   LYS A 121     6121   2337   6667    436   -209   -421       N  
ATOM    944  CA  LYS A 121      71.921  37.949  31.220  1.00 40.10           C  
ANISOU  944  CA  LYS A 121     6158   2194   6884    528   -214   -517       C  
ATOM    945  C   LYS A 121      72.761  38.646  32.273  1.00 44.65           C  
ANISOU  945  C   LYS A 121     6797   2739   7429    448   -115   -629       C  
ATOM    946  O   LYS A 121      72.717  39.863  32.364  1.00 46.57           O  
ANISOU  946  O   LYS A 121     7117   2795   7782    469   -141   -662       O  
ATOM    947  CB  LYS A 121      70.563  37.585  31.840  1.00 42.76           C  
ANISOU  947  CB  LYS A 121     6334   2552   7358    664   -171   -628       C  
ATOM    948  CG  LYS A 121      69.553  36.947  30.896  1.00 46.99           C  
ANISOU  948  CG  LYS A 121     6779   3115   7959    753   -277   -540       C  
ATOM    949  CD  LYS A 121      68.487  36.215  31.675  1.00 58.12           C  
ANISOU  949  CD  LYS A 121     8011   4609   9464    840   -184   -669       C  
ATOM    950  CE  LYS A 121      67.437  37.083  32.331  1.00 77.03           C  
ANISOU  950  CE  LYS A 121    10312   6836  12120    983   -186   -783       C  
ATOM    951  NZ  LYS A 121      66.659  36.317  33.345  1.00 89.54           N  
ANISOU  951  NZ  LYS A 121    11724   8520  13778   1034    -39   -937       N  
ATOM    952  N   PHE A 122      73.476  37.885  33.106  1.00 39.99           N  
ANISOU  952  N   PHE A 122     6178   2321   6696    361    -14   -692       N  
ATOM    953  CA  PHE A 122      74.295  38.437  34.175  1.00 39.37           C  
ANISOU  953  CA  PHE A 122     6158   2231   6570    274     63   -804       C  
ATOM    954  C   PHE A 122      75.710  37.900  34.073  1.00 39.49           C  
ANISOU  954  C   PHE A 122     6210   2375   6420    126     67   -746       C  
ATOM    955  O   PHE A 122      76.073  37.006  34.838  1.00 37.12           O  
ANISOU  955  O   PHE A 122     5858   2235   6010     84    122   -796       O  
ATOM    956  CB  PHE A 122      73.666  38.184  35.558  1.00 42.28           C  
ANISOU  956  CB  PHE A 122     6459   2657   6948    318    179   -973       C  
ATOM    957  CG  PHE A 122      72.184  38.462  35.619  1.00 45.17           C  
ANISOU  957  CG  PHE A 122     6739   2926   7497    470    198  -1040       C  
ATOM    958  CD1 PHE A 122      71.704  39.769  35.640  1.00 48.78           C  
ANISOU  958  CD1 PHE A 122     7234   3168   8134    544    183  -1105       C  
ATOM    959  CD2 PHE A 122      71.263  37.418  35.612  1.00 48.13           C  
ANISOU  959  CD2 PHE A 122     6987   3416   7885    542    225  -1041       C  
ATOM    960  CE1 PHE A 122      70.329  40.027  35.661  1.00 49.71           C  
ANISOU  960  CE1 PHE A 122     7245   3187   8457    698    193  -1173       C  
ATOM    961  CE2 PHE A 122      69.888  37.680  35.636  1.00 50.92           C  
ANISOU  961  CE2 PHE A 122     7231   3679   8438    682    240  -1110       C  
ATOM    962  CZ  PHE A 122      69.433  38.980  35.666  1.00 48.50           C  
ANISOU  962  CZ  PHE A 122     6945   3159   8323    764    224  -1180       C  
ATOM    963  N   PRO A 123      76.534  38.461  33.137  1.00 35.80           N  
ANISOU  963  N   PRO A 123     5832   1830   5939     43      9   -643       N  
ATOM    964  CA  PRO A 123      77.922  37.955  32.958  1.00 34.92           C  
ANISOU  964  CA  PRO A 123     5730   1838   5700   -101     23   -596       C  
ATOM    965  C   PRO A 123      78.867  38.065  34.155  1.00 35.62           C  
ANISOU  965  C   PRO A 123     5815   1988   5731   -197     72   -710       C  
ATOM    966  O   PRO A 123      79.905  37.414  34.158  1.00 33.57           O  
ANISOU  966  O   PRO A 123     5517   1855   5383   -291     78   -688       O  
ATOM    967  CB  PRO A 123      78.474  38.768  31.776  1.00 36.55           C  
ANISOU  967  CB  PRO A 123     6050   1910   5928   -178    -26   -486       C  
ATOM    968  CG  PRO A 123      77.376  39.600  31.285  1.00 40.52           C  
ANISOU  968  CG  PRO A 123     6608   2239   6548    -63    -96   -442       C  
ATOM    969  CD  PRO A 123      76.222  39.562  32.199  1.00 36.08           C  
ANISOU  969  CD  PRO A 123     5970   1658   6083     70    -70   -566       C  
ATOM    970  N   PHE A 124      78.518  38.875  35.150  1.00 32.09           N  
ANISOU  970  N   PHE A 124     5407   1446   5339   -174    101   -835       N  
ATOM    971  CA  PHE A 124      79.375  39.128  36.307  1.00 32.35           C  
ANISOU  971  CA  PHE A 124     5468   1513   5312   -276    128   -950       C  
ATOM    972  C   PHE A 124      79.032  38.252  37.487  1.00 38.87           C  
ANISOU  972  C   PHE A 124     6242   2475   6050   -247    174  -1046       C  
ATOM    973  O   PHE A 124      79.583  38.452  38.578  1.00 39.57           O  
ANISOU  973  O   PHE A 124     6373   2588   6075   -325    187  -1151       O  
ATOM    974  CB  PHE A 124      79.394  40.631  36.679  1.00 32.73           C  
ANISOU  974  CB  PHE A 124     5624   1360   5452   -302    135  -1036       C  
ATOM    975  CG  PHE A 124      80.080  41.495  35.650  1.00 33.25           C  
ANISOU  975  CG  PHE A 124     5767   1297   5570   -384     89   -940       C  
ATOM    976  CD1 PHE A 124      79.388  41.973  34.542  1.00 35.95           C  
ANISOU  976  CD1 PHE A 124     6156   1502   6003   -308     48   -835       C  
ATOM    977  CD2 PHE A 124      81.423  41.829  35.782  1.00 34.66           C  
ANISOU  977  CD2 PHE A 124     5977   1487   5706   -546     81   -952       C  
ATOM    978  CE1 PHE A 124      80.032  42.770  33.583  1.00 36.09           C  
ANISOU  978  CE1 PHE A 124     6276   1390   6045   -403     10   -738       C  
ATOM    979  CE2 PHE A 124      82.065  42.627  34.823  1.00 36.21           C  
ANISOU  979  CE2 PHE A 124     6252   1561   5947   -643     60   -867       C  
ATOM    980  CZ  PHE A 124      81.366  43.088  33.732  1.00 34.12           C  
ANISOU  980  CZ  PHE A 124     6058   1156   5749   -575     30   -757       C  
ATOM    981  N   ARG A 125      78.118  37.282  37.267  1.00 35.57           N  
ANISOU  981  N   ARG A 125     5748   2145   5624   -145    195  -1008       N  
ATOM    982  CA  ARG A 125      77.672  36.270  38.240  1.00 36.03           C  
ANISOU  982  CA  ARG A 125     5762   2338   5589   -119    248  -1077       C  
ATOM    983  C   ARG A 125      77.266  36.867  39.582  1.00 44.39           C  
ANISOU  983  C   ARG A 125     6888   3341   6638   -126    323  -1243       C  
ATOM    984  O   ARG A 125      77.726  36.428  40.637  1.00 45.09           O  
ANISOU  984  O   ARG A 125     7015   3521   6595   -201    337  -1313       O  
ATOM    985  CB  ARG A 125      78.744  35.168  38.408  1.00 32.17           C  
ANISOU  985  CB  ARG A 125     5239   2018   4964   -205    205  -1026       C  
ATOM    986  CG  ARG A 125      79.067  34.418  37.135  1.00 21.14           C  
ANISOU  986  CG  ARG A 125     3772    688   3571   -195    162   -882       C  
ATOM    987  CD  ARG A 125      80.120  33.355  37.377  1.00 20.57           C  
ANISOU  987  CD  ARG A 125     3653    766   3395   -267    124   -852       C  
ATOM    988  NE  ARG A 125      80.233  32.469  36.221  1.00 25.03           N  
ANISOU  988  NE  ARG A 125     4148   1402   3960   -244    109   -733       N  
ATOM    989  CZ  ARG A 125      79.473  31.398  36.017  1.00 34.74           C  
ANISOU  989  CZ  ARG A 125     5329   2712   5157   -170    127   -694       C  
ATOM    990  NH1 ARG A 125      79.636  30.661  34.929  1.00 24.46           N  
ANISOU  990  NH1 ARG A 125     3979   1463   3852   -160    115   -594       N  
ATOM    991  NH2 ARG A 125      78.557  31.047  36.909  1.00 22.30           N  
ANISOU  991  NH2 ARG A 125     3761   1162   3549   -116    168   -761       N  
ATOM    992  N   GLU A 126      76.419  37.888  39.539  1.00 44.32           N  
ANISOU  992  N   GLU A 126     6901   3171   6766    -49    366  -1309       N  
ATOM    993  CA  GLU A 126      76.015  38.594  40.747  1.00 45.78           C  
ANISOU  993  CA  GLU A 126     7159   3276   6960    -56    459  -1486       C  
ATOM    994  C   GLU A 126      74.942  37.828  41.546  1.00 53.96           C  
ANISOU  994  C   GLU A 126     8151   4394   7957      1    577  -1581       C  
ATOM    995  O   GLU A 126      74.880  37.987  42.765  1.00 54.90           O  
ANISOU  995  O   GLU A 126     8351   4516   7990    -55    665  -1725       O  
ATOM    996  CB  GLU A 126      75.612  40.052  40.425  1.00 46.72           C  
ANISOU  996  CB  GLU A 126     7323   3169   7261      1    462  -1533       C  
ATOM    997  CG  GLU A 126      76.815  40.925  40.092  1.00 51.42           C  
ANISOU  997  CG  GLU A 126     8008   3678   7852   -109    378  -1488       C  
ATOM    998  CD  GLU A 126      76.581  42.122  39.191  1.00 65.79           C  
ANISOU  998  CD  GLU A 126     9872   5279   9846    -56    334  -1446       C  
ATOM    999  OE1 GLU A 126      76.524  43.260  39.708  1.00 74.83           O  
ANISOU  999  OE1 GLU A 126    11108   6262  11062    -72    367  -1562       O  
ATOM   1000  OE2 GLU A 126      76.477  41.928  37.962  1.00 63.21           O  
ANISOU 1000  OE2 GLU A 126     9506   4934   9578     -7    259  -1296       O  
ATOM   1001  N   HIS A 127      74.168  36.953  40.881  1.00 52.06           N  
ANISOU 1001  N   HIS A 127     7795   4224   7759     91    580  -1500       N  
ATOM   1002  CA  HIS A 127      73.084  36.183  41.491  1.00 53.17           C  
ANISOU 1002  CA  HIS A 127     7877   4441   7884    141    700  -1581       C  
ATOM   1003  C   HIS A 127      73.547  34.906  42.200  1.00 57.78           C  
ANISOU 1003  C   HIS A 127     8494   5209   8250     48    716  -1565       C  
ATOM   1004  O   HIS A 127      74.529  34.293  41.785  1.00 56.42           O  
ANISOU 1004  O   HIS A 127     8324   5128   7982     -7    607  -1443       O  
ATOM   1005  CB  HIS A 127      71.984  35.912  40.462  1.00 54.68           C  
ANISOU 1005  CB  HIS A 127     7925   4607   8242    276    687  -1511       C  
ATOM   1006  CG  HIS A 127      71.242  37.178  40.147  1.00 58.86           C  
ANISOU 1006  CG  HIS A 127     8429   4936   8999    381    693  -1573       C  
ATOM   1007  ND1 HIS A 127      71.654  38.019  39.126  1.00 61.05           N  
ANISOU 1007  ND1 HIS A 127     8734   5087   9375    408    561  -1466       N  
ATOM   1008  CD2 HIS A 127      70.229  37.774  40.819  1.00 60.71           C  
ANISOU 1008  CD2 HIS A 127     8631   5065   9370    451    819  -1740       C  
ATOM   1009  CE1 HIS A 127      70.845  39.064  39.177  1.00 60.46           C  
ANISOU 1009  CE1 HIS A 127     8642   4830   9501    506    591  -1558       C  
ATOM   1010  NE2 HIS A 127      69.969  38.958  40.174  1.00 60.68           N  
ANISOU 1010  NE2 HIS A 127     8621   4865   9572    542    748  -1730       N  
ATOM   1011  N   ILE A 128      72.856  34.544  43.316  1.00 56.13           N  
ANISOU 1011  N   ILE A 128     8319   5042   7965     26    857  -1696       N  
ATOM   1012  CA  ILE A 128      73.184  33.394  44.183  1.00 57.02           C  
ANISOU 1012  CA  ILE A 128     8503   5307   7855    -71    880  -1695       C  
ATOM   1013  C   ILE A 128      73.289  32.092  43.383  1.00 57.72           C  
ANISOU 1013  C   ILE A 128     8500   5522   7908    -46    799  -1534       C  
ATOM   1014  O   ILE A 128      74.247  31.352  43.584  1.00 57.87           O  
ANISOU 1014  O   ILE A 128     8574   5640   7775   -123    709  -1460       O  
ATOM   1015  CB  ILE A 128      72.264  33.260  45.455  1.00 61.36           C  
ANISOU 1015  CB  ILE A 128     9121   5866   8329   -107   1073  -1866       C  
ATOM   1016  CG1 ILE A 128      72.838  32.249  46.484  1.00 62.35           C  
ANISOU 1016  CG1 ILE A 128     9386   6122   8183   -238   1067  -1859       C  
ATOM   1017  CG2 ILE A 128      70.787  32.964  45.137  1.00 62.38           C  
ANISOU 1017  CG2 ILE A 128     9104   5984   8615     -1   1208  -1910       C  
ATOM   1018  CD1 ILE A 128      73.835  32.877  47.517  1.00 70.66           C  
ANISOU 1018  CD1 ILE A 128    10630   7146   9073   -367   1025  -1941       C  
ATOM   1019  N   LEU A 129      72.378  31.873  42.424  1.00 52.00           N  
ANISOU 1019  N   LEU A 129     7637   4784   7337     63    812  -1480       N  
ATOM   1020  CA  LEU A 129      72.378  30.701  41.557  1.00 51.60           C  
ANISOU 1020  CA  LEU A 129     7500   4837   7267     91    742  -1337       C  
ATOM   1021  C   LEU A 129      73.621  30.610  40.645  1.00 49.60           C  
ANISOU 1021  C   LEU A 129     7250   4608   6987     65    584  -1193       C  
ATOM   1022  O   LEU A 129      73.906  29.535  40.117  1.00 48.04           O  
ANISOU 1022  O   LEU A 129     7012   4509   6732     61    529  -1086       O  
ATOM   1023  CB  LEU A 129      71.098  30.686  40.717  1.00 52.77           C  
ANISOU 1023  CB  LEU A 129     7505   4943   7603    209    774  -1325       C  
ATOM   1024  CG  LEU A 129      69.921  29.940  41.337  1.00 58.57           C  
ANISOU 1024  CG  LEU A 129     8181   5735   8336    220    918  -1408       C  
ATOM   1025  CD1 LEU A 129      68.744  30.873  41.572  1.00 59.29           C  
ANISOU 1025  CD1 LEU A 129     8199   5710   8619    297   1041  -1556       C  
ATOM   1026  CD2 LEU A 129      69.494  28.807  40.453  1.00 62.33           C  
ANISOU 1026  CD2 LEU A 129     8548   6293   8840    262    867  -1292       C  
ATOM   1027  N   GLN A 130      74.362  31.734  40.478  1.00 41.84           N  
ANISOU 1027  N   GLN A 130     6317   3530   6049     40    526  -1202       N  
ATOM   1028  CA  GLN A 130      75.568  31.820  39.642  1.00 38.09           C  
ANISOU 1028  CA  GLN A 130     5843   3063   5565     -2    405  -1087       C  
ATOM   1029  C   GLN A 130      76.890  31.589  40.397  1.00 38.20           C  
ANISOU 1029  C   GLN A 130     5930   3144   5439   -116    346  -1097       C  
ATOM   1030  O   GLN A 130      77.946  31.621  39.768  1.00 37.26           O  
ANISOU 1030  O   GLN A 130     5793   3038   5328   -159    259  -1018       O  
ATOM   1031  CB  GLN A 130      75.612  33.153  38.917  1.00 37.47           C  
ANISOU 1031  CB  GLN A 130     5774   2833   5629     27    371  -1077       C  
ATOM   1032  CG  GLN A 130      74.419  33.414  38.025  1.00 38.82           C  
ANISOU 1032  CG  GLN A 130     5872   2924   5955    145    378  -1043       C  
ATOM   1033  CD  GLN A 130      74.578  34.740  37.333  1.00 46.35           C  
ANISOU 1033  CD  GLN A 130     6866   3711   7034    164    323  -1020       C  
ATOM   1034  OE1 GLN A 130      74.344  35.792  37.919  1.00 45.88           O  
ANISOU 1034  OE1 GLN A 130     6854   3528   7050    178    364  -1127       O  
ATOM   1035  NE2 GLN A 130      75.033  34.722  36.089  1.00 29.21           N  
ANISOU 1035  NE2 GLN A 130     4695   1524   4877    153    233   -884       N  
ATOM   1036  N   LYS A 131      76.831  31.326  41.722  1.00 31.94           N  
ANISOU 1036  N   LYS A 131     5219   2395   4522   -170    392  -1193       N  
ATOM   1037  CA  LYS A 131      78.005  31.130  42.575  1.00 31.08           C  
ANISOU 1037  CA  LYS A 131     5193   2341   4276   -278    311  -1210       C  
ATOM   1038  C   LYS A 131      78.443  29.670  42.637  1.00 36.27           C  
ANISOU 1038  C   LYS A 131     5826   3131   4825   -294    246  -1122       C  
ATOM   1039  O   LYS A 131      77.600  28.767  42.538  1.00 34.16           O  
ANISOU 1039  O   LYS A 131     5529   2918   4534   -244    307  -1094       O  
ATOM   1040  CB  LYS A 131      77.743  31.695  43.982  1.00 32.78           C  
ANISOU 1040  CB  LYS A 131     5545   2516   4393   -342    380  -1361       C  
ATOM   1041  CG  LYS A 131      78.229  33.131  44.196  1.00 45.62           C  
ANISOU 1041  CG  LYS A 131     7235   4020   6079   -389    368  -1447       C  
ATOM   1042  CD  LYS A 131      77.390  34.207  43.511  1.00 51.15           C  
ANISOU 1042  CD  LYS A 131     7892   4582   6962   -298    454  -1487       C  
ATOM   1043  CE  LYS A 131      77.709  35.616  43.984  1.00 60.22           C  
ANISOU 1043  CE  LYS A 131     9133   5592   8155   -350    464  -1598       C  
ATOM   1044  NZ  LYS A 131      79.076  36.069  43.596  1.00 64.15           N  
ANISOU 1044  NZ  LYS A 131     9631   6068   8676   -426    335  -1532       N  
ATOM   1045  N   LYS A 132      79.769  29.435  42.804  1.00 34.84           N  
ANISOU 1045  N   LYS A 132     5652   2994   4591   -366    117  -1083       N  
ATOM   1046  CA  LYS A 132      80.319  28.083  42.810  1.00 35.53           C  
ANISOU 1046  CA  LYS A 132     5708   3188   4604   -371     33   -997       C  
ATOM   1047  C   LYS A 132      79.921  27.285  44.054  1.00 43.18           C  
ANISOU 1047  C   LYS A 132     6797   4210   5400   -407     46  -1035       C  
ATOM   1048  O   LYS A 132      79.810  26.072  43.952  1.00 43.76           O  
ANISOU 1048  O   LYS A 132     6850   4354   5424   -380     28   -962       O  
ATOM   1049  CB  LYS A 132      81.837  28.054  42.547  1.00 36.70           C  
ANISOU 1049  CB  LYS A 132     5797   3360   4788   -424   -110   -949       C  
ATOM   1050  CG  LYS A 132      82.771  28.285  43.717  1.00 43.45           C  
ANISOU 1050  CG  LYS A 132     6740   4220   5550   -523   -228  -1009       C  
ATOM   1051  CD  LYS A 132      83.950  27.301  43.585  1.00 53.77           C  
ANISOU 1051  CD  LYS A 132     7963   5602   6865   -536   -380   -931       C  
ATOM   1052  CE  LYS A 132      84.991  27.424  44.675  1.00 68.28           C  
ANISOU 1052  CE  LYS A 132     9868   7447   8627   -631   -545   -976       C  
ATOM   1053  NZ  LYS A 132      85.967  28.513  44.402  1.00 78.20           N  
ANISOU 1053  NZ  LYS A 132    11060   8654  10000   -699   -598  -1019       N  
ATOM   1054  N   GLU A 133      79.648  27.958  45.191  1.00 40.63           N  
ANISOU 1054  N   GLU A 133     6614   3845   4981   -473     91  -1151       N  
ATOM   1055  CA  GLU A 133      79.231  27.308  46.441  1.00 40.31           C  
ANISOU 1055  CA  GLU A 133     6728   3841   4745   -534    123  -1199       C  
ATOM   1056  C   GLU A 133      77.839  26.743  46.249  1.00 44.58           C  
ANISOU 1056  C   GLU A 133     7244   4399   5295   -472    289  -1205       C  
ATOM   1057  O   GLU A 133      77.537  25.662  46.763  1.00 44.93           O  
ANISOU 1057  O   GLU A 133     7359   4504   5209   -499    303  -1175       O  
ATOM   1058  CB  GLU A 133      79.246  28.297  47.622  1.00 41.55           C  
ANISOU 1058  CB  GLU A 133     7053   3938   4798   -630    155  -1339       C  
ATOM   1059  CG  GLU A 133      80.637  28.765  48.042  1.00 54.48           C  
ANISOU 1059  CG  GLU A 133     8735   5562   6402   -715    -27  -1346       C  
ATOM   1060  CD  GLU A 133      81.389  29.712  47.118  1.00 77.34           C  
ANISOU 1060  CD  GLU A 133    11498   8402   9487   -692    -79  -1332       C  
ATOM   1061  OE1 GLU A 133      82.640  29.700  47.157  1.00 68.45           O  
ANISOU 1061  OE1 GLU A 133    10335   7296   8376   -743   -247  -1292       O  
ATOM   1062  OE2 GLU A 133      80.734  30.456  46.350  1.00 75.25           O  
ANISOU 1062  OE2 GLU A 133    11165   8068   9360   -626     44  -1359       O  
ATOM   1063  N   PHE A 134      76.996  27.463  45.486  1.00 40.31           N  
ANISOU 1063  N   PHE A 134     6599   3798   4917   -393    405  -1240       N  
ATOM   1064  CA  PHE A 134      75.651  27.018  45.151  1.00 40.65           C  
ANISOU 1064  CA  PHE A 134     6575   3851   5019   -325    550  -1250       C  
ATOM   1065  C   PHE A 134      75.737  25.796  44.202  1.00 42.79           C  
ANISOU 1065  C   PHE A 134     6740   4199   5318   -271    485  -1108       C  
ATOM   1066  O   PHE A 134      74.998  24.830  44.382  1.00 42.88           O  
ANISOU 1066  O   PHE A 134     6761   4261   5270   -270    556  -1094       O  
ATOM   1067  CB  PHE A 134      74.875  28.160  44.505  1.00 43.52           C  
ANISOU 1067  CB  PHE A 134     6842   4116   5576   -244    640  -1312       C  
ATOM   1068  CG  PHE A 134      73.409  27.888  44.334  1.00 47.38           C  
ANISOU 1068  CG  PHE A 134     7251   4601   6152   -176    791  -1355       C  
ATOM   1069  CD1 PHE A 134      72.503  28.203  45.346  1.00 52.04           C  
ANISOU 1069  CD1 PHE A 134     7906   5159   6708   -208    964  -1506       C  
ATOM   1070  CD2 PHE A 134      72.918  27.342  43.149  1.00 51.89           C  
ANISOU 1070  CD2 PHE A 134     7675   5197   6845    -88    766  -1256       C  
ATOM   1071  CE1 PHE A 134      71.131  27.957  45.186  1.00 53.85           C  
ANISOU 1071  CE1 PHE A 134     8030   5384   7047   -148   1112  -1559       C  
ATOM   1072  CE2 PHE A 134      71.546  27.104  42.985  1.00 55.74           C  
ANISOU 1072  CE2 PHE A 134     8068   5679   7432    -28    891  -1301       C  
ATOM   1073  CZ  PHE A 134      70.662  27.391  44.015  1.00 53.63           C  
ANISOU 1073  CZ  PHE A 134     7843   5384   7151    -57   1065  -1453       C  
ATOM   1074  N   ALA A 135      76.678  25.827  43.229  1.00 37.67           N  
ANISOU 1074  N   ALA A 135     6002   3556   4754   -239    359  -1011       N  
ATOM   1075  CA  ALA A 135      76.901  24.753  42.266  1.00 36.60           C  
ANISOU 1075  CA  ALA A 135     5772   3483   4650   -193    299   -888       C  
ATOM   1076  C   ALA A 135      77.250  23.427  42.981  1.00 39.39           C  
ANISOU 1076  C   ALA A 135     6204   3911   4850   -239    243   -843       C  
ATOM   1077  O   ALA A 135      76.719  22.384  42.603  1.00 38.16           O  
ANISOU 1077  O   ALA A 135     6013   3799   4686   -207    274   -785       O  
ATOM   1078  CB  ALA A 135      77.989  25.141  41.286  1.00 36.96           C  
ANISOU 1078  CB  ALA A 135     5735   3515   4795   -179    193   -819       C  
ATOM   1079  N   ILE A 136      78.096  23.496  44.035  1.00 35.98           N  
ANISOU 1079  N   ILE A 136     5890   3485   4297   -318    153   -870       N  
ATOM   1080  CA  ILE A 136      78.512  22.373  44.883  1.00 36.42           C  
ANISOU 1080  CA  ILE A 136     6056   3590   4194   -371     67   -826       C  
ATOM   1081  C   ILE A 136      77.300  21.746  45.603  1.00 40.10           C  
ANISOU 1081  C   ILE A 136     6631   4071   4534   -404    205   -863       C  
ATOM   1082  O   ILE A 136      77.139  20.536  45.533  1.00 40.59           O  
ANISOU 1082  O   ILE A 136     6707   4173   4543   -396    189   -788       O  
ATOM   1083  CB  ILE A 136      79.643  22.806  45.865  1.00 39.38           C  
ANISOU 1083  CB  ILE A 136     6540   3951   4472   -455    -80   -857       C  
ATOM   1084  CG1 ILE A 136      80.899  23.267  45.068  1.00 39.24           C  
ANISOU 1084  CG1 ILE A 136     6382   3925   4603   -429   -211   -817       C  
ATOM   1085  CG2 ILE A 136      79.981  21.672  46.874  1.00 38.54           C  
ANISOU 1085  CG2 ILE A 136     6584   3878   4182   -514   -191   -809       C  
ATOM   1086  CD1 ILE A 136      82.015  23.973  45.890  1.00 40.05           C  
ANISOU 1086  CD1 ILE A 136     6552   4002   4661   -514   -352   -868       C  
ATOM   1087  N   LEU A 137      76.435  22.562  46.244  1.00 36.12           N  
ANISOU 1087  N   LEU A 137     6196   3530   3999   -440    354   -984       N  
ATOM   1088  CA  LEU A 137      75.221  22.081  46.918  1.00 36.50           C  
ANISOU 1088  CA  LEU A 137     6333   3589   3947   -484    526  -1044       C  
ATOM   1089  C   LEU A 137      74.230  21.399  45.961  1.00 38.98           C  
ANISOU 1089  C   LEU A 137     6499   3929   4382   -406    623   -999       C  
ATOM   1090  O   LEU A 137      73.646  20.370  46.315  1.00 38.15           O  
ANISOU 1090  O   LEU A 137     6455   3858   4182   -446    690   -978       O  
ATOM   1091  CB  LEU A 137      74.520  23.208  47.690  1.00 37.34           C  
ANISOU 1091  CB  LEU A 137     6511   3639   4035   -529    686  -1204       C  
ATOM   1092  CG  LEU A 137      75.330  23.912  48.781  1.00 43.53           C  
ANISOU 1092  CG  LEU A 137     7474   4392   4673   -629    616  -1275       C  
ATOM   1093  CD1 LEU A 137      74.547  25.049  49.356  1.00 43.13           C  
ANISOU 1093  CD1 LEU A 137     7468   4274   4645   -656    799  -1445       C  
ATOM   1094  CD2 LEU A 137      75.780  22.921  49.887  1.00 47.76           C  
ANISOU 1094  CD2 LEU A 137     8233   4966   4947   -746    537  -1236       C  
ATOM   1095  N   ILE A 138      74.026  22.003  44.767  1.00 36.14           N  
ANISOU 1095  N   ILE A 138     5960   3544   4226   -306    626   -986       N  
ATOM   1096  CA  ILE A 138      73.174  21.506  43.678  1.00 35.49           C  
ANISOU 1096  CA  ILE A 138     5726   3480   4280   -227    679   -939       C  
ATOM   1097  C   ILE A 138      73.725  20.172  43.213  1.00 37.21           C  
ANISOU 1097  C   ILE A 138     5936   3754   4448   -221    573   -811       C  
ATOM   1098  O   ILE A 138      72.940  19.247  43.005  1.00 37.42           O  
ANISOU 1098  O   ILE A 138     5936   3811   4470   -217    639   -785       O  
ATOM   1099  CB  ILE A 138      73.084  22.529  42.498  1.00 38.97           C  
ANISOU 1099  CB  ILE A 138     6015   3867   4924   -133    656   -936       C  
ATOM   1100  CG1 ILE A 138      72.213  23.769  42.860  1.00 40.23           C  
ANISOU 1100  CG1 ILE A 138     6157   3952   5177   -115    783  -1071       C  
ATOM   1101  CG2 ILE A 138      72.637  21.886  41.155  1.00 38.79           C  
ANISOU 1101  CG2 ILE A 138     5852   3868   5019    -56    631   -845       C  
ATOM   1102  CD1 ILE A 138      70.671  23.539  43.103  1.00 52.45           C  
ANISOU 1102  CD1 ILE A 138     7637   5497   6794    -97    959  -1157       C  
ATOM   1103  N   SER A 139      75.069  20.086  43.021  1.00 30.74           N  
ANISOU 1103  N   SER A 139     5129   2942   3608   -219    411   -738       N  
ATOM   1104  CA  SER A 139      75.754  18.881  42.562  1.00 29.63           C  
ANISOU 1104  CA  SER A 139     4973   2841   3446   -202    300   -626       C  
ATOM   1105  C   SER A 139      75.487  17.711  43.510  1.00 35.78           C  
ANISOU 1105  C   SER A 139     5891   3643   4060   -266    313   -606       C  
ATOM   1106  O   SER A 139      75.098  16.649  43.059  1.00 35.95           O  
ANISOU 1106  O   SER A 139     5886   3687   4087   -247    328   -544       O  
ATOM   1107  CB  SER A 139      77.242  19.142  42.416  1.00 29.79           C  
ANISOU 1107  CB  SER A 139     4974   2855   3488   -198    140   -585       C  
ATOM   1108  OG  SER A 139      77.470  19.831  41.204  1.00 34.64           O  
ANISOU 1108  OG  SER A 139     5450   3452   4259   -139    135   -569       O  
ATOM   1109  N   LEU A 140      75.592  17.959  44.817  1.00 34.44           N  
ANISOU 1109  N   LEU A 140     5886   3461   3737   -353    320   -663       N  
ATOM   1110  CA  LEU A 140      75.297  17.033  45.900  1.00 35.37           C  
ANISOU 1110  CA  LEU A 140     6189   3588   3663   -443    344   -654       C  
ATOM   1111  C   LEU A 140      73.805  16.613  45.867  1.00 36.32           C  
ANISOU 1111  C   LEU A 140     6296   3720   3784   -464    549   -697       C  
ATOM   1112  O   LEU A 140      73.512  15.428  46.056  1.00 36.67           O  
ANISOU 1112  O   LEU A 140     6415   3778   3741   -502    561   -638       O  
ATOM   1113  CB  LEU A 140      75.668  17.705  47.248  1.00 36.75           C  
ANISOU 1113  CB  LEU A 140     6553   3738   3670   -543    321   -727       C  
ATOM   1114  CG  LEU A 140      75.565  16.835  48.511  1.00 44.29           C  
ANISOU 1114  CG  LEU A 140     7756   4690   4381   -657    292   -699       C  
ATOM   1115  CD1 LEU A 140      76.545  15.661  48.471  1.00 45.77           C  
ANISOU 1115  CD1 LEU A 140     7971   4879   4542   -629     69   -558       C  
ATOM   1116  CD2 LEU A 140      75.753  17.676  49.776  1.00 46.84           C  
ANISOU 1116  CD2 LEU A 140     8278   4987   4531   -768    290   -790       C  
ATOM   1117  N   ALA A 141      72.881  17.575  45.592  1.00 29.40           N  
ANISOU 1117  N   ALA A 141     5313   2831   3025   -437    703   -800       N  
ATOM   1118  CA  ALA A 141      71.438  17.333  45.473  1.00 28.18           C  
ANISOU 1118  CA  ALA A 141     5095   2687   2926   -447    897   -860       C  
ATOM   1119  C   ALA A 141      71.090  16.469  44.261  1.00 33.02           C  
ANISOU 1119  C   ALA A 141     5558   3325   3661   -376    869   -772       C  
ATOM   1120  O   ALA A 141      70.146  15.682  44.347  1.00 35.46           O  
ANISOU 1120  O   ALA A 141     5866   3653   3955   -416    983   -781       O  
ATOM   1121  CB  ALA A 141      70.678  18.640  45.420  1.00 28.66           C  
ANISOU 1121  CB  ALA A 141     5054   2713   3122   -413   1031   -991       C  
ATOM   1122  N   VAL A 142      71.860  16.585  43.149  1.00 27.17           N  
ANISOU 1122  N   VAL A 142     4704   2586   3034   -283    725   -692       N  
ATOM   1123  CA  VAL A 142      71.727  15.777  41.907  1.00 26.05           C  
ANISOU 1123  CA  VAL A 142     4441   2464   2993   -220    677   -604       C  
ATOM   1124  C   VAL A 142      72.096  14.329  42.277  1.00 32.92           C  
ANISOU 1124  C   VAL A 142     5427   3350   3730   -269    623   -521       C  
ATOM   1125  O   VAL A 142      71.338  13.414  41.967  1.00 32.88           O  
ANISOU 1125  O   VAL A 142     5397   3359   3735   -282    684   -497       O  
ATOM   1126  CB  VAL A 142      72.589  16.343  40.721  1.00 27.33           C  
ANISOU 1126  CB  VAL A 142     4487   2615   3282   -130    553   -551       C  
ATOM   1127  CG1 VAL A 142      72.687  15.359  39.556  1.00 26.28           C  
ANISOU 1127  CG1 VAL A 142     4276   2502   3205    -86    496   -460       C  
ATOM   1128  CG2 VAL A 142      72.057  17.692  40.240  1.00 26.28           C  
ANISOU 1128  CG2 VAL A 142     4247   2448   3290    -80    603   -619       C  
ATOM   1129  N   TRP A 143      73.213  14.139  43.010  1.00 31.90           N  
ANISOU 1129  N   TRP A 143     5433   3211   3478   -301    503   -480       N  
ATOM   1130  CA  TRP A 143      73.627  12.821  43.492  1.00 33.23           C  
ANISOU 1130  CA  TRP A 143     5734   3373   3519   -344    427   -397       C  
ATOM   1131  C   TRP A 143      72.610  12.205  44.450  1.00 38.52           C  
ANISOU 1131  C   TRP A 143     6548   4041   4046   -453    567   -429       C  
ATOM   1132  O   TRP A 143      72.371  11.009  44.373  1.00 39.60           O  
ANISOU 1132  O   TRP A 143     6734   4172   4139   -478    569   -366       O  
ATOM   1133  CB  TRP A 143      75.013  12.879  44.146  1.00 32.57           C  
ANISOU 1133  CB  TRP A 143     5758   3269   3349   -353    246   -354       C  
ATOM   1134  CG  TRP A 143      76.114  12.925  43.132  1.00 34.13           C  
ANISOU 1134  CG  TRP A 143     5813   3466   3689   -256    105   -299       C  
ATOM   1135  CD1 TRP A 143      76.866  14.005  42.781  1.00 36.79           C  
ANISOU 1135  CD1 TRP A 143     6056   3804   4119   -217     47   -330       C  
ATOM   1136  CD2 TRP A 143      76.522  11.849  42.268  1.00 34.38           C  
ANISOU 1136  CD2 TRP A 143     5775   3493   3797   -193     34   -216       C  
ATOM   1137  NE1 TRP A 143      77.767  13.655  41.801  1.00 36.63           N  
ANISOU 1137  NE1 TRP A 143     5914   3784   4221   -143    -51   -272       N  
ATOM   1138  CE2 TRP A 143      77.555  12.346  41.442  1.00 38.22           C  
ANISOU 1138  CE2 TRP A 143     6122   3981   4417   -122    -56   -207       C  
ATOM   1139  CE3 TRP A 143      76.135  10.497  42.137  1.00 35.79           C  
ANISOU 1139  CE3 TRP A 143     6001   3657   3939   -199     43   -155       C  
ATOM   1140  CZ2 TRP A 143      78.205  11.543  40.492  1.00 37.49           C  
ANISOU 1140  CZ2 TRP A 143     5936   3882   4428    -54   -122   -148       C  
ATOM   1141  CZ3 TRP A 143      76.781   9.703  41.198  1.00 37.25           C  
ANISOU 1141  CZ3 TRP A 143     6096   3827   4228   -124    -37    -93       C  
ATOM   1142  CH2 TRP A 143      77.801  10.226  40.389  1.00 37.85           C  
ANISOU 1142  CH2 TRP A 143     6032   3910   4439    -51   -112    -95       C  
ATOM   1143  N   VAL A 144      71.986  13.005  45.320  1.00 34.19           N  
ANISOU 1143  N   VAL A 144     6068   3492   3429   -525    700   -535       N  
ATOM   1144  CA  VAL A 144      71.010  12.466  46.269  1.00 33.66           C  
ANISOU 1144  CA  VAL A 144     6145   3423   3221   -649    867   -581       C  
ATOM   1145  C   VAL A 144      69.698  12.096  45.550  1.00 37.30           C  
ANISOU 1145  C   VAL A 144     6450   3907   3817   -639   1031   -618       C  
ATOM   1146  O   VAL A 144      69.156  11.017  45.803  1.00 36.82           O  
ANISOU 1146  O   VAL A 144     6469   3844   3677   -716   1100   -586       O  
ATOM   1147  CB  VAL A 144      70.804  13.399  47.509  1.00 36.69           C  
ANISOU 1147  CB  VAL A 144     6672   3795   3472   -745    977   -697       C  
ATOM   1148  CG1 VAL A 144      69.600  12.976  48.345  1.00 35.87           C  
ANISOU 1148  CG1 VAL A 144     6683   3692   3253   -880   1210   -775       C  
ATOM   1149  CG2 VAL A 144      72.060  13.464  48.368  1.00 36.29           C  
ANISOU 1149  CG2 VAL A 144     6824   3720   3246   -788    793   -646       C  
ATOM   1150  N   LEU A 145      69.186  13.000  44.689  1.00 33.76           N  
ANISOU 1150  N   LEU A 145     5787   3471   3571   -551   1083   -684       N  
ATOM   1151  CA  LEU A 145      67.934  12.795  43.965  1.00 34.16           C  
ANISOU 1151  CA  LEU A 145     5665   3540   3776   -533   1210   -726       C  
ATOM   1152  C   LEU A 145      68.003  11.589  43.046  1.00 35.09           C  
ANISOU 1152  C   LEU A 145     5738   3669   3928   -505   1123   -616       C  
ATOM   1153  O   LEU A 145      67.092  10.765  43.086  1.00 34.42           O  
ANISOU 1153  O   LEU A 145     5651   3592   3835   -573   1232   -626       O  
ATOM   1154  CB  LEU A 145      67.482  14.064  43.193  1.00 35.11           C  
ANISOU 1154  CB  LEU A 145     5573   3654   4113   -429   1234   -802       C  
ATOM   1155  CG  LEU A 145      66.417  13.886  42.065  1.00 41.05           C  
ANISOU 1155  CG  LEU A 145     6109   4419   5068   -371   1271   -812       C  
ATOM   1156  CD1 LEU A 145      65.016  13.594  42.643  1.00 41.54           C  
ANISOU 1156  CD1 LEU A 145     6128   4492   5162   -458   1488   -920       C  
ATOM   1157  CD2 LEU A 145      66.360  15.113  41.151  1.00 44.64           C  
ANISOU 1157  CD2 LEU A 145     6394   4850   5717   -250   1207   -840       C  
ATOM   1158  N   VAL A 146      69.070  11.481  42.227  1.00 29.61           N  
ANISOU 1158  N   VAL A 146     5007   2969   3273   -414    940   -521       N  
ATOM   1159  CA  VAL A 146      69.234  10.373  41.277  1.00 28.16           C  
ANISOU 1159  CA  VAL A 146     4783   2787   3129   -380    856   -426       C  
ATOM   1160  C   VAL A 146      69.348   9.006  42.021  1.00 33.41           C  
ANISOU 1160  C   VAL A 146     5634   3431   3631   -471    855   -363       C  
ATOM   1161  O   VAL A 146      68.702   8.043  41.609  1.00 32.49           O  
ANISOU 1161  O   VAL A 146     5496   3313   3536   -501    900   -338       O  
ATOM   1162  CB  VAL A 146      70.364  10.632  40.253  1.00 30.39           C  
ANISOU 1162  CB  VAL A 146     4988   3065   3492   -272    690   -359       C  
ATOM   1163  CG1 VAL A 146      70.610   9.414  39.378  1.00 29.60           C  
ANISOU 1163  CG1 VAL A 146     4873   2958   3414   -246    619   -274       C  
ATOM   1164  CG2 VAL A 146      70.030  11.845  39.375  1.00 30.12           C  
ANISOU 1164  CG2 VAL A 146     4786   3041   3619   -197    701   -408       C  
ATOM   1165  N   THR A 147      70.104   8.954  43.138  1.00 31.01           N  
ANISOU 1165  N   THR A 147     5520   3102   3160   -524    801   -340       N  
ATOM   1166  CA  THR A 147      70.235   7.774  43.994  1.00 30.41           C  
ANISOU 1166  CA  THR A 147     5660   2988   2907   -619    783   -274       C  
ATOM   1167  C   THR A 147      68.852   7.292  44.448  1.00 34.86           C  
ANISOU 1167  C   THR A 147     6267   3558   3420   -743    993   -331       C  
ATOM   1168  O   THR A 147      68.590   6.099  44.374  1.00 35.60           O  
ANISOU 1168  O   THR A 147     6434   3625   3469   -794   1001   -270       O  
ATOM   1169  CB  THR A 147      71.184   8.064  45.162  1.00 32.59           C  
ANISOU 1169  CB  THR A 147     6133   3236   3014   -659    678   -252       C  
ATOM   1170  OG1 THR A 147      72.454   8.373  44.603  1.00 31.09           O  
ANISOU 1170  OG1 THR A 147     5865   3039   2908   -543    482   -198       O  
ATOM   1171  CG2 THR A 147      71.334   6.880  46.120  1.00 29.37           C  
ANISOU 1171  CG2 THR A 147     5987   2772   2401   -767    640   -173       C  
ATOM   1172  N   LEU A 148      67.961   8.219  44.843  1.00 31.74           N  
ANISOU 1172  N   LEU A 148     5811   3194   3056   -787   1168   -455       N  
ATOM   1173  CA  LEU A 148      66.606   7.890  45.285  1.00 31.89           C  
ANISOU 1173  CA  LEU A 148     5836   3224   3058   -909   1397   -537       C  
ATOM   1174  C   LEU A 148      65.708   7.500  44.120  1.00 34.38           C  
ANISOU 1174  C   LEU A 148     5928   3563   3571   -867   1446   -549       C  
ATOM   1175  O   LEU A 148      64.818   6.682  44.296  1.00 33.88           O  
ANISOU 1175  O   LEU A 148     5887   3497   3487   -973   1579   -567       O  
ATOM   1176  CB  LEU A 148      65.981   9.004  46.158  1.00 32.36           C  
ANISOU 1176  CB  LEU A 148     5899   3300   3098   -970   1581   -683       C  
ATOM   1177  CG  LEU A 148      66.742   9.387  47.446  1.00 37.60           C  
ANISOU 1177  CG  LEU A 148     6820   3936   3528  -1050   1556   -688       C  
ATOM   1178  CD1 LEU A 148      66.101  10.557  48.121  1.00 37.56           C  
ANISOU 1178  CD1 LEU A 148     6795   3944   3533  -1098   1750   -850       C  
ATOM   1179  CD2 LEU A 148      66.861   8.225  48.425  1.00 40.81           C  
ANISOU 1179  CD2 LEU A 148     7519   4304   3683  -1203   1569   -614       C  
ATOM   1180  N   GLU A 149      65.964   8.044  42.927  1.00 30.84           N  
ANISOU 1180  N   GLU A 149     5282   3133   3301   -726   1331   -535       N  
ATOM   1181  CA  GLU A 149      65.220   7.678  41.711  1.00 30.52           C  
ANISOU 1181  CA  GLU A 149     5045   3113   3440   -681   1333   -535       C  
ATOM   1182  C   GLU A 149      65.547   6.233  41.266  1.00 33.38           C  
ANISOU 1182  C   GLU A 149     5490   3448   3745   -702   1245   -424       C  
ATOM   1183  O   GLU A 149      64.667   5.536  40.751  1.00 31.54           O  
ANISOU 1183  O   GLU A 149     5173   3221   3588   -744   1307   -436       O  
ATOM   1184  CB  GLU A 149      65.576   8.619  40.557  1.00 31.23           C  
ANISOU 1184  CB  GLU A 149     4951   3216   3697   -534   1211   -532       C  
ATOM   1185  CG  GLU A 149      65.020  10.021  40.687  1.00 38.48           C  
ANISOU 1185  CG  GLU A 149     5742   4145   4733   -495   1292   -645       C  
ATOM   1186  CD  GLU A 149      65.295  10.897  39.483  1.00 52.52           C  
ANISOU 1186  CD  GLU A 149     7361   5921   6671   -360   1163   -628       C  
ATOM   1187  OE1 GLU A 149      65.914  10.413  38.508  1.00 50.63           O  
ANISOU 1187  OE1 GLU A 149     7121   5681   6436   -305   1019   -532       O  
ATOM   1188  OE2 GLU A 149      64.874  12.073  39.510  1.00 47.12           O  
ANISOU 1188  OE2 GLU A 149     6563   5231   6111   -315   1212   -714       O  
ATOM   1189  N   VAL A 150      66.838   5.832  41.419  1.00 30.42           N  
ANISOU 1189  N   VAL A 150     5262   3037   3257   -665   1090   -324       N  
ATOM   1190  CA  VAL A 150      67.404   4.532  41.032  1.00 31.12           C  
ANISOU 1190  CA  VAL A 150     5443   3081   3301   -659    980   -218       C  
ATOM   1191  C   VAL A 150      67.155   3.435  42.129  1.00 37.25           C  
ANISOU 1191  C   VAL A 150     6452   3806   3896   -801   1046   -178       C  
ATOM   1192  O   VAL A 150      66.950   2.276  41.797  1.00 37.47           O  
ANISOU 1192  O   VAL A 150     6531   3793   3914   -836   1033   -122       O  
ATOM   1193  CB  VAL A 150      68.899   4.732  40.639  1.00 34.01           C  
ANISOU 1193  CB  VAL A 150     5819   3427   3676   -538    785   -145       C  
ATOM   1194  CG1 VAL A 150      69.649   3.408  40.487  1.00 33.71           C  
ANISOU 1194  CG1 VAL A 150     5901   3323   3585   -525    666    -43       C  
ATOM   1195  CG2 VAL A 150      69.006   5.543  39.358  1.00 33.52           C  
ANISOU 1195  CG2 VAL A 150     5547   3404   3784   -426    738   -171       C  
ATOM   1196  N   LEU A 151      67.099   3.826  43.410  1.00 35.97           N  
ANISOU 1196  N   LEU A 151     6442   3640   3586   -892   1125   -213       N  
ATOM   1197  CA  LEU A 151      66.869   2.928  44.547  1.00 36.68           C  
ANISOU 1197  CA  LEU A 151     6789   3676   3473  -1046   1196   -176       C  
ATOM   1198  C   LEU A 151      65.657   1.957  44.364  1.00 41.59           C  
ANISOU 1198  C   LEU A 151     7397   4288   4117  -1165   1357   -196       C  
ATOM   1199  O   LEU A 151      65.894   0.760  44.555  1.00 40.63           O  
ANISOU 1199  O   LEU A 151     7454   4093   3890  -1226   1305   -102       O  
ATOM   1200  CB  LEU A 151      66.775   3.717  45.859  1.00 36.67           C  
ANISOU 1200  CB  LEU A 151     6932   3686   3315  -1141   1297   -242       C  
ATOM   1201  CG  LEU A 151      66.976   2.988  47.186  1.00 43.24           C  
ANISOU 1201  CG  LEU A 151     8099   4452   3880  -1297   1314   -185       C  
ATOM   1202  CD1 LEU A 151      68.128   2.004  47.139  1.00 45.15           C  
ANISOU 1202  CD1 LEU A 151     8506   4610   4039  -1247   1069    -29       C  
ATOM   1203  CD2 LEU A 151      67.270   3.968  48.263  1.00 46.42           C  
ANISOU 1203  CD2 LEU A 151     8632   4868   4138  -1351   1350   -246       C  
ATOM   1204  N   PRO A 152      64.423   2.380  43.912  1.00 37.40           N  
ANISOU 1204  N   PRO A 152     6651   3819   3742  -1193   1530   -311       N  
ATOM   1205  CA  PRO A 152      63.318   1.406  43.744  1.00 36.30           C  
ANISOU 1205  CA  PRO A 152     6491   3668   3634  -1316   1672   -332       C  
ATOM   1206  C   PRO A 152      63.607   0.190  42.862  1.00 41.76           C  
ANISOU 1206  C   PRO A 152     7198   4308   4362  -1285   1543   -231       C  
ATOM   1207  O   PRO A 152      62.915  -0.816  43.011  1.00 40.20           O  
ANISOU 1207  O   PRO A 152     7071   4074   4129  -1416   1645   -224       O  
ATOM   1208  CB  PRO A 152      62.178   2.250  43.184  1.00 37.59           C  
ANISOU 1208  CB  PRO A 152     6363   3908   4013  -1297   1810   -470       C  
ATOM   1209  CG  PRO A 152      62.452   3.610  43.687  1.00 41.81           C  
ANISOU 1209  CG  PRO A 152     6864   4477   4547  -1237   1831   -540       C  
ATOM   1210  CD  PRO A 152      63.939   3.756  43.652  1.00 37.66           C  
ANISOU 1210  CD  PRO A 152     6459   3922   3928  -1124   1605   -430       C  
ATOM   1211  N   MET A 153      64.660   0.251  41.997  1.00 40.21           N  
ANISOU 1211  N   MET A 153     6951   4099   4229  -1123   1333   -157       N  
ATOM   1212  CA  MET A 153      65.127  -0.863  41.143  1.00 39.56           C  
ANISOU 1212  CA  MET A 153     6897   3955   4177  -1078   1204    -68       C  
ATOM   1213  C   MET A 153      65.509  -2.080  41.999  1.00 48.06           C  
ANISOU 1213  C   MET A 153     8262   4927   5074  -1176   1177     29       C  
ATOM   1214  O   MET A 153      65.440  -3.215  41.524  1.00 48.42           O  
ANISOU 1214  O   MET A 153     8358   4906   5135  -1202   1146     81       O  
ATOM   1215  CB  MET A 153      66.375  -0.432  40.378  1.00 40.71           C  
ANISOU 1215  CB  MET A 153     6977   4100   4391   -900   1007    -18       C  
ATOM   1216  CG  MET A 153      66.257  -0.565  38.920  1.00 42.92           C  
ANISOU 1216  CG  MET A 153     7049   4415   4842   -813    965    -44       C  
ATOM   1217  SD  MET A 153      67.708   0.057  38.059  1.00 44.67           S  
ANISOU 1217  SD  MET A 153     7205   4635   5132   -629    772      3       S  
ATOM   1218  CE  MET A 153      66.958   1.215  36.997  1.00 40.32           C  
ANISOU 1218  CE  MET A 153     6401   4175   4745   -571    804    -80       C  
ATOM   1219  N   LEU A 154      65.935  -1.832  43.254  1.00 47.04           N  
ANISOU 1219  N   LEU A 154     8335   4771   4767  -1231   1175     57       N  
ATOM   1220  CA  LEU A 154      66.348  -2.842  44.224  1.00 48.14           C  
ANISOU 1220  CA  LEU A 154     8785   4799   4705  -1329   1127    160       C  
ATOM   1221  C   LEU A 154      65.251  -3.870  44.492  1.00 50.80           C  
ANISOU 1221  C   LEU A 154     9223   5092   4985  -1513   1299    154       C  
ATOM   1222  O   LEU A 154      65.566  -5.032  44.733  1.00 50.84           O  
ANISOU 1222  O   LEU A 154     9432   4983   4901  -1561   1224    256       O  
ATOM   1223  CB  LEU A 154      66.754  -2.135  45.532  1.00 49.41           C  
ANISOU 1223  CB  LEU A 154     9127   4966   4682  -1386   1131    159       C  
ATOM   1224  CG  LEU A 154      67.777  -2.815  46.446  1.00 56.23           C  
ANISOU 1224  CG  LEU A 154    10299   5715   5352  -1402    947    292       C  
ATOM   1225  CD1 LEU A 154      68.968  -3.371  45.651  1.00 57.62           C  
ANISOU 1225  CD1 LEU A 154    10402   5847   5643  -1202    680    374       C  
ATOM   1226  CD2 LEU A 154      68.275  -1.842  47.489  1.00 58.63           C  
ANISOU 1226  CD2 LEU A 154    10767   6040   5470  -1475    966    268       C  
ATOM   1227  N   THR A 155      63.968  -3.442  44.439  1.00 46.65           N  
ANISOU 1227  N   THR A 155     8542   4650   4532  -1614   1526     30       N  
ATOM   1228  CA  THR A 155      62.786  -4.292  44.650  1.00 46.16           C  
ANISOU 1228  CA  THR A 155     8525   4564   4450  -1805   1724     -5       C  
ATOM   1229  C   THR A 155      62.547  -5.210  43.449  1.00 49.79           C  
ANISOU 1229  C   THR A 155     8865   4992   5060  -1768   1663     20       C  
ATOM   1230  O   THR A 155      61.807  -6.183  43.557  1.00 49.05           O  
ANISOU 1230  O   THR A 155     8856   4845   4937  -1922   1775     25       O  
ATOM   1231  CB  THR A 155      61.510  -3.448  44.886  1.00 49.84           C  
ANISOU 1231  CB  THR A 155     8804   5134   4999  -1903   1980   -166       C  
ATOM   1232  OG1 THR A 155      61.180  -2.747  43.689  1.00 47.03           O  
ANISOU 1232  OG1 THR A 155     8109   4865   4896  -1766   1947   -244       O  
ATOM   1233  CG2 THR A 155      61.622  -2.499  46.053  1.00 46.19           C  
ANISOU 1233  CG2 THR A 155     8450   4704   4395  -1951   2075   -218       C  
ATOM   1234  N   PHE A 156      63.106  -4.852  42.295  1.00 47.50           N  
ANISOU 1234  N   PHE A 156     8381   4737   4930  -1580   1504     24       N  
ATOM   1235  CA  PHE A 156      62.938  -5.608  41.063  1.00 47.76           C  
ANISOU 1235  CA  PHE A 156     8300   4744   5101  -1536   1437     36       C  
ATOM   1236  C   PHE A 156      63.968  -6.711  40.922  1.00 59.94           C  
ANISOU 1236  C   PHE A 156    10038   6158   6577  -1477   1263    162       C  
ATOM   1237  O   PHE A 156      63.739  -7.648  40.172  1.00 59.41           O  
ANISOU 1237  O   PHE A 156     9959   6036   6580  -1490   1239    176       O  
ATOM   1238  CB  PHE A 156      62.889  -4.671  39.840  1.00 47.32           C  
ANISOU 1238  CB  PHE A 156     7944   4790   5244  -1387   1376    -34       C  
ATOM   1239  CG  PHE A 156      61.672  -3.792  39.929  1.00 46.59           C  
ANISOU 1239  CG  PHE A 156     7650   4801   5252  -1453   1547   -161       C  
ATOM   1240  CD1 PHE A 156      60.395  -4.340  39.872  1.00 47.97           C  
ANISOU 1240  CD1 PHE A 156     7751   4985   5491  -1607   1705   -229       C  
ATOM   1241  CD2 PHE A 156      61.796  -2.431  40.176  1.00 47.46           C  
ANISOU 1241  CD2 PHE A 156     7647   4988   5398  -1371   1558   -219       C  
ATOM   1242  CE1 PHE A 156      59.270  -3.544  40.063  1.00 48.76           C  
ANISOU 1242  CE1 PHE A 156     7652   5172   5704  -1668   1871   -357       C  
ATOM   1243  CE2 PHE A 156      60.668  -1.629  40.342  1.00 49.79           C  
ANISOU 1243  CE2 PHE A 156     7755   5362   5802  -1425   1721   -344       C  
ATOM   1244  CZ  PHE A 156      59.410  -2.190  40.282  1.00 47.85           C  
ANISOU 1244  CZ  PHE A 156     7420   5125   5634  -1569   1877   -416       C  
ATOM   1245  N   ILE A 157      65.051  -6.645  41.709  1.00 63.51           N  
ANISOU 1245  N   ILE A 157    10681   6551   6898  -1422   1143    247       N  
ATOM   1246  CA  ILE A 157      66.133  -7.634  41.731  1.00 66.64           C  
ANISOU 1246  CA  ILE A 157    11267   6810   7244  -1349    956    368       C  
ATOM   1247  C   ILE A 157      65.615  -9.016  42.149  1.00 77.08           C  
ANISOU 1247  C   ILE A 157    12812   8002   8472  -1506   1012    429       C  
ATOM   1248  O   ILE A 157      66.189 -10.017  41.715  1.00 78.76           O  
ANISOU 1248  O   ILE A 157    13102   8099   8726  -1443    888    497       O  
ATOM   1249  CB  ILE A 157      67.348  -7.148  42.587  1.00 70.23           C  
ANISOU 1249  CB  ILE A 157    11862   7235   7587  -1265    802    439       C  
ATOM   1250  CG1 ILE A 157      67.807  -5.696  42.228  1.00 71.16           C  
ANISOU 1250  CG1 ILE A 157    11756   7479   7803  -1123    757    372       C  
ATOM   1251  CG2 ILE A 157      68.519  -8.125  42.542  1.00 71.18           C  
ANISOU 1251  CG2 ILE A 157    12151   7202   7691  -1172    587    560       C  
ATOM   1252  CD1 ILE A 157      67.988  -5.295  40.648  1.00 80.06           C  
ANISOU 1252  CD1 ILE A 157    12591   8675   9152   -970    714    313       C  
ATOM   1253  N   THR A 158      64.503  -9.077  42.930  1.00 76.37           N  
ANISOU 1253  N   THR A 158    12817   7928   8272  -1714   1214    393       N  
ATOM   1254  CA  THR A 158      63.886 -10.335  43.374  1.00 77.81           C  
ANISOU 1254  CA  THR A 158    13220   7989   8353  -1900   1303    444       C  
ATOM   1255  C   THR A 158      63.538 -11.208  42.140  1.00 84.10           C  
ANISOU 1255  C   THR A 158    13890   8750   9316  -1881   1292    422       C  
ATOM   1256  O   THR A 158      62.806 -10.765  41.250  1.00 83.76           O  
ANISOU 1256  O   THR A 158    13575   8821   9431  -1869   1375    313       O  
ATOM   1257  CB  THR A 158      62.722 -10.079  44.378  1.00 89.98           C  
ANISOU 1257  CB  THR A 158    14841   9579   9767  -2136   1561    380       C  
ATOM   1258  OG1 THR A 158      62.434 -11.268  45.125  1.00 87.15           O  
ANISOU 1258  OG1 THR A 158    14787   9077   9250  -2326   1621    461       O  
ATOM   1259  CG2 THR A 158      61.449  -9.509  43.727  1.00 89.81           C  
ANISOU 1259  CG2 THR A 158    14503   9702   9919  -2193   1763    221       C  
ATOM   1260  N   SER A 159      64.167 -12.413  42.070  1.00 82.05           N  
ANISOU 1260  N   SER A 159    13833   8320   9022  -1863   1163    527       N  
ATOM   1261  CA  SER A 159      64.068 -13.416  40.997  1.00121.42           C  
ANISOU 1261  CA  SER A 159    18770  13228  14136  -1842   1126    522       C  
ATOM   1262  C   SER A 159      64.569 -12.880  39.661  1.00155.94           C  
ANISOU 1262  C   SER A 159    22874  17680  18695  -1636   1017    463       C  
ATOM   1263  O   SER A 159      65.662 -12.321  39.601  1.00120.12           O  
ANISOU 1263  O   SER A 159    18316  13145  14177  -1460    865    499       O  
ATOM   1264  CB  SER A 159      62.652 -13.978  40.871  1.00125.11           C  
ANISOU 1264  CB  SER A 159    19198  13713  14625  -2059   1333    450       C  
ATOM   1265  N   SER A 167      72.858 -14.657  35.808  1.00 57.49           N  
ANISOU 1265  N   SER A 167    10224   4658   6960   -374    -16    594       N  
ATOM   1266  CA  SER A 167      74.134 -14.221  36.369  1.00 57.36           C  
ANISOU 1266  CA  SER A 167    10182   4618   6993   -222   -179    641       C  
ATOM   1267  C   SER A 167      74.058 -12.727  36.763  1.00 57.65           C  
ANISOU 1267  C   SER A 167    10091   4852   6962   -237   -150    620       C  
ATOM   1268  O   SER A 167      73.704 -12.468  37.912  1.00 59.32           O  
ANISOU 1268  O   SER A 167    10439   5083   7018   -339   -156    685       O  
ATOM   1269  CB  SER A 167      75.284 -14.554  35.421  1.00 62.16           C  
ANISOU 1269  CB  SER A 167    10662   5148   7809    -35   -249    585       C  
ATOM   1270  OG  SER A 167      75.881 -15.800  35.752  1.00 66.54           O  
ANISOU 1270  OG  SER A 167    11381   5475   8428     35   -382    654       O  
ATOM   1271  N   CYS A 168      74.327 -11.758  35.848  1.00 48.94           N  
ANISOU 1271  N   CYS A 168     8750   3887   5958   -152   -108    530       N  
ATOM   1272  CA  CYS A 168      74.101 -10.328  36.139  1.00 46.02           C  
ANISOU 1272  CA  CYS A 168     8263   3696   5526   -179    -64    503       C  
ATOM   1273  C   CYS A 168      73.187  -9.723  35.067  1.00 47.99           C  
ANISOU 1273  C   CYS A 168     8347   4089   5799   -237     92    405       C  
ATOM   1274  O   CYS A 168      73.647  -9.112  34.104  1.00 47.23           O  
ANISOU 1274  O   CYS A 168     8078   4063   5803   -150    104    338       O  
ATOM   1275  CB  CYS A 168      75.382  -9.518  36.331  1.00 45.33           C  
ANISOU 1275  CB  CYS A 168     8067   3640   5515    -37   -190    506       C  
ATOM   1276  SG  CYS A 168      75.099  -7.866  37.041  1.00 48.81           S  
ANISOU 1276  SG  CYS A 168     8431   4264   5852    -89   -155    490       S  
ATOM   1277  N   VAL A 169      71.878  -9.932  35.237  1.00 43.56           N  
ANISOU 1277  N   VAL A 169     7846   3560   5146   -392    207    399       N  
ATOM   1278  CA  VAL A 169      70.847  -9.525  34.281  1.00 42.15           C  
ANISOU 1278  CA  VAL A 169     7527   3497   4993   -462    332    314       C  
ATOM   1279  C   VAL A 169      70.644  -8.003  34.256  1.00 46.47           C  
ANISOU 1279  C   VAL A 169     7908   4210   5539   -448    369    269       C  
ATOM   1280  O   VAL A 169      71.008  -7.308  35.210  1.00 46.61           O  
ANISOU 1280  O   VAL A 169     7950   4260   5499   -432    332    302       O  
ATOM   1281  CB  VAL A 169      69.503 -10.308  34.475  1.00 44.88           C  
ANISOU 1281  CB  VAL A 169     7969   3812   5270   -637    438    313       C  
ATOM   1282  CG1 VAL A 169      69.719 -11.822  34.430  1.00 43.82           C  
ANISOU 1282  CG1 VAL A 169     8008   3499   5144   -653    401    355       C  
ATOM   1283  CG2 VAL A 169      68.782  -9.909  35.754  1.00 44.57           C  
ANISOU 1283  CG2 VAL A 169     8012   3816   5105   -760    503    345       C  
ATOM   1284  N   ASP A 170      70.103  -7.488  33.122  1.00 40.98           N  
ANISOU 1284  N   ASP A 170     7055   3609   4907   -453    428    194       N  
ATOM   1285  CA  ASP A 170      69.758  -6.088  32.941  1.00 38.49           C  
ANISOU 1285  CA  ASP A 170     6584   3436   4607   -445    462    149       C  
ATOM   1286  C   ASP A 170      68.477  -5.889  33.746  1.00 39.82           C  
ANISOU 1286  C   ASP A 170     6768   3655   4709   -580    559    139       C  
ATOM   1287  O   ASP A 170      67.691  -6.845  33.867  1.00 38.07           O  
ANISOU 1287  O   ASP A 170     6629   3378   4457   -691    616    144       O  
ATOM   1288  CB  ASP A 170      69.534  -5.737  31.456  1.00 39.43           C  
ANISOU 1288  CB  ASP A 170     6562   3614   4803   -420    477     84       C  
ATOM   1289  CG  ASP A 170      69.133  -4.286  31.273  1.00 46.03           C  
ANISOU 1289  CG  ASP A 170     7249   4578   5661   -409    495     47       C  
ATOM   1290  OD1 ASP A 170      67.917  -3.997  31.324  1.00 44.97           O  
ANISOU 1290  OD1 ASP A 170     7054   4503   5529   -497    555     14       O  
ATOM   1291  OD2 ASP A 170      70.041  -3.424  31.159  1.00 52.63           O  
ANISOU 1291  OD2 ASP A 170     8027   5448   6523   -313    449     48       O  
ATOM   1292  N   TYR A 171      68.269  -4.660  34.310  1.00 33.96           N  
ANISOU 1292  N   TYR A 171     5945   3008   3950   -578    588    118       N  
ATOM   1293  CA  TYR A 171      67.093  -4.375  35.129  1.00 33.31           C  
ANISOU 1293  CA  TYR A 171     5863   2975   3820   -703    703     89       C  
ATOM   1294  C   TYR A 171      65.770  -4.788  34.437  1.00 36.14           C  
ANISOU 1294  C   TYR A 171     6134   3360   4239   -807    789     32       C  
ATOM   1295  O   TYR A 171      64.898  -5.339  35.098  1.00 37.17           O  
ANISOU 1295  O   TYR A 171     6330   3470   4324   -941    890     24       O  
ATOM   1296  CB  TYR A 171      67.077  -2.910  35.623  1.00 34.52           C  
ANISOU 1296  CB  TYR A 171     5917   3223   3975   -668    726     53       C  
ATOM   1297  CG  TYR A 171      65.701  -2.272  35.655  1.00 35.56           C  
ANISOU 1297  CG  TYR A 171     5915   3438   4157   -752    849    -27       C  
ATOM   1298  CD1 TYR A 171      64.782  -2.590  36.660  1.00 36.59           C  
ANISOU 1298  CD1 TYR A 171     6116   3564   4223   -892    982    -49       C  
ATOM   1299  CD2 TYR A 171      65.290  -1.409  34.642  1.00 36.17           C  
ANISOU 1299  CD2 TYR A 171     5797   3590   4357   -697    832    -83       C  
ATOM   1300  CE1 TYR A 171      63.497  -2.051  36.657  1.00 36.30           C  
ANISOU 1300  CE1 TYR A 171     5925   3599   4268   -967   1106   -140       C  
ATOM   1301  CE2 TYR A 171      64.013  -0.853  34.641  1.00 36.97           C  
ANISOU 1301  CE2 TYR A 171     5753   3755   4539   -760    925   -160       C  
ATOM   1302  CZ  TYR A 171      63.123  -1.174  35.650  1.00 42.15           C  
ANISOU 1302  CZ  TYR A 171     6450   4409   5155   -891   1067   -195       C  
ATOM   1303  OH  TYR A 171      61.866  -0.633  35.625  1.00 43.57           O  
ANISOU 1303  OH  TYR A 171     6457   4650   5448   -948   1167   -287       O  
ATOM   1304  N   ALA A 172      65.655  -4.562  33.124  1.00 31.05           N  
ANISOU 1304  N   ALA A 172     5353   2754   3691   -756    745     -6       N  
ATOM   1305  CA  ALA A 172      64.480  -4.856  32.302  1.00 29.90           C  
ANISOU 1305  CA  ALA A 172     5106   2637   3618   -841    784    -63       C  
ATOM   1306  C   ALA A 172      64.117  -6.357  32.218  1.00 34.49           C  
ANISOU 1306  C   ALA A 172     5811   3124   4170   -946    813    -47       C  
ATOM   1307  O   ALA A 172      63.045  -6.699  31.725  1.00 34.06           O  
ANISOU 1307  O   ALA A 172     5681   3088   4171  -1046    853    -97       O  
ATOM   1308  CB  ALA A 172      64.657  -4.255  30.906  1.00 29.68           C  
ANISOU 1308  CB  ALA A 172     4949   2658   3669   -757    699    -92       C  
ATOM   1309  N   SER A 173      64.991  -7.239  32.714  1.00 32.74           N  
ANISOU 1309  N   SER A 173     5774   2793   3872   -926    783     19       N  
ATOM   1310  CA  SER A 173      64.766  -8.697  32.730  1.00 32.81           C  
ANISOU 1310  CA  SER A 173     5931   2685   3849  -1021    804     43       C  
ATOM   1311  C   SER A 173      64.250  -9.243  34.070  1.00 39.38           C  
ANISOU 1311  C   SER A 173     6913   3464   4587  -1156    898     81       C  
ATOM   1312  O   SER A 173      63.629 -10.296  34.066  1.00 40.16           O  
ANISOU 1312  O   SER A 173     7098   3489   4671  -1281    952     81       O  
ATOM   1313  CB  SER A 173      66.042  -9.435  32.346  1.00 33.48           C  
ANISOU 1313  CB  SER A 173     6135   2655   3930   -910    705     91       C  
ATOM   1314  OG  SER A 173      66.419  -9.115  31.018  1.00 38.09           O  
ANISOU 1314  OG  SER A 173     6603   3279   4588   -818    649     45       O  
ATOM   1315  N   SER A 174      64.491  -8.555  35.208  1.00 37.25           N  
ANISOU 1315  N   SER A 174     6688   3225   4239  -1148    924    109       N  
ATOM   1316  CA  SER A 174      64.094  -9.076  36.531  1.00 38.15           C  
ANISOU 1316  CA  SER A 174     6988   3279   4229  -1290   1017    150       C  
ATOM   1317  C   SER A 174      62.865  -8.416  37.161  1.00 44.60           C  
ANISOU 1317  C   SER A 174     7710   4196   5041  -1425   1185     77       C  
ATOM   1318  O   SER A 174      62.618  -7.228  36.945  1.00 45.09           O  
ANISOU 1318  O   SER A 174     7580   4376   5178  -1365   1204     11       O  
ATOM   1319  CB  SER A 174      65.266  -8.991  37.504  1.00 41.23           C  
ANISOU 1319  CB  SER A 174     7559   3603   4505  -1214    924    241       C  
ATOM   1320  OG  SER A 174      65.666  -7.630  37.615  1.00 55.86           O  
ANISOU 1320  OG  SER A 174     9282   5564   6377  -1111    895    211       O  
ATOM   1321  N   GLY A 175      62.173  -9.180  38.009  1.00 41.70           N  
ANISOU 1321  N   GLY A 175     7492   3769   4583  -1605   1311     89       N  
ATOM   1322  CA  GLY A 175      61.023  -8.717  38.776  1.00 41.80           C  
ANISOU 1322  CA  GLY A 175     7445   3855   4580  -1760   1508     13       C  
ATOM   1323  C   GLY A 175      59.699  -8.781  38.062  1.00 46.66           C  
ANISOU 1323  C   GLY A 175     7844   4535   5348  -1862   1616    -93       C  
ATOM   1324  O   GLY A 175      59.638  -9.197  36.903  1.00 47.55           O  
ANISOU 1324  O   GLY A 175     7865   4637   5566  -1820   1526   -103       O  
ATOM   1325  N   ASN A 176      58.628  -8.372  38.762  1.00 43.22           N  
ANISOU 1325  N   ASN A 176     7326   4165   4930  -2002   1811   -179       N  
ATOM   1326  CA  ASN A 176      57.266  -8.349  38.229  1.00 43.68           C  
ANISOU 1326  CA  ASN A 176     7144   4291   5161  -2110   1926   -296       C  
ATOM   1327  C   ASN A 176      57.137  -7.269  37.131  1.00 47.86           C  
ANISOU 1327  C   ASN A 176     7373   4930   5882  -1949   1815   -364       C  
ATOM   1328  O   ASN A 176      57.335  -6.093  37.433  1.00 47.54           O  
ANISOU 1328  O   ASN A 176     7237   4962   5864  -1853   1823   -397       O  
ATOM   1329  CB  ASN A 176      56.253  -8.119  39.355  1.00 46.53           C  
ANISOU 1329  CB  ASN A 176     7492   4688   5498  -2295   2181   -381       C  
ATOM   1330  CG  ASN A 176      54.817  -8.336  38.969  1.00 72.32           C  
ANISOU 1330  CG  ASN A 176    10530   8001   8945  -2444   2322   -501       C  
ATOM   1331  OD1 ASN A 176      54.310  -7.780  37.988  1.00 65.80           O  
ANISOU 1331  OD1 ASN A 176     9415   7257   8328  -2365   2253   -580       O  
ATOM   1332  ND2 ASN A 176      54.126  -9.143  39.753  1.00 67.01           N  
ANISOU 1332  ND2 ASN A 176     9990   7275   8197  -2672   2518   -518       N  
ATOM   1333  N   PRO A 177      56.797  -7.649  35.866  1.00 44.76           N  
ANISOU 1333  N   PRO A 177     6847   4543   5619  -1926   1708   -384       N  
ATOM   1334  CA  PRO A 177      56.704  -6.637  34.794  1.00 44.05           C  
ANISOU 1334  CA  PRO A 177     6507   4543   5688  -1781   1580   -434       C  
ATOM   1335  C   PRO A 177      55.612  -5.584  34.984  1.00 49.45           C  
ANISOU 1335  C   PRO A 177     6921   5328   6538  -1803   1683   -553       C  
ATOM   1336  O   PRO A 177      55.796  -4.453  34.538  1.00 48.60           O  
ANISOU 1336  O   PRO A 177     6666   5284   6517  -1657   1591   -574       O  
ATOM   1337  CB  PRO A 177      56.504  -7.462  33.522  1.00 45.48           C  
ANISOU 1337  CB  PRO A 177     6652   4690   5937  -1800   1461   -431       C  
ATOM   1338  CG  PRO A 177      55.961  -8.780  33.990  1.00 49.79           C  
ANISOU 1338  CG  PRO A 177     7336   5155   6429  -1997   1582   -427       C  
ATOM   1339  CD  PRO A 177      56.545  -9.018  35.347  1.00 45.58           C  
ANISOU 1339  CD  PRO A 177     7048   4557   5712  -2034   1685   -358       C  
ATOM   1340  N   LYS A 178      54.508  -5.929  35.685  1.00 47.43           N  
ANISOU 1340  N   LYS A 178     6608   5081   6334  -1985   1882   -635       N  
ATOM   1341  CA  LYS A 178      53.403  -5.001  35.947  1.00 47.58           C  
ANISOU 1341  CA  LYS A 178     6352   5186   6539  -2015   2008   -769       C  
ATOM   1342  C   LYS A 178      53.894  -3.779  36.741  1.00 52.32           C  
ANISOU 1342  C   LYS A 178     6961   5825   7092  -1910   2063   -783       C  
ATOM   1343  O   LYS A 178      53.673  -2.644  36.306  1.00 53.28           O  
ANISOU 1343  O   LYS A 178     6862   6008   7372  -1783   1998   -842       O  
ATOM   1344  CB  LYS A 178      52.227  -5.716  36.646  1.00 49.93           C  
ANISOU 1344  CB  LYS A 178     6610   5474   6885  -2252   2245   -858       C  
ATOM   1345  N   TYR A 179      54.639  -4.012  37.842  1.00 48.08           N  
ANISOU 1345  N   TYR A 179     6696   5240   6331  -1954   2155   -720       N  
ATOM   1346  CA  TYR A 179      55.175  -2.935  38.678  1.00 47.97           C  
ANISOU 1346  CA  TYR A 179     6731   5254   6241  -1874   2204   -732       C  
ATOM   1347  C   TYR A 179      56.407  -2.281  38.074  1.00 47.01           C  
ANISOU 1347  C   TYR A 179     6643   5135   6083  -1660   1976   -645       C  
ATOM   1348  O   TYR A 179      56.567  -1.064  38.168  1.00 45.05           O  
ANISOU 1348  O   TYR A 179     6280   4935   5900  -1546   1959   -689       O  
ATOM   1349  CB  TYR A 179      55.431  -3.408  40.120  1.00 50.85           C  
ANISOU 1349  CB  TYR A 179     7388   5565   6369  -2019   2376   -699       C  
ATOM   1350  CG  TYR A 179      54.191  -3.947  40.800  1.00 56.34           C  
ANISOU 1350  CG  TYR A 179     8063   6257   7088  -2254   2641   -795       C  
ATOM   1351  CD1 TYR A 179      53.048  -3.162  40.937  1.00 59.71           C  
ANISOU 1351  CD1 TYR A 179     8204   6758   7723  -2300   2816   -960       C  
ATOM   1352  CD2 TYR A 179      54.170  -5.226  41.344  1.00 57.93           C  
ANISOU 1352  CD2 TYR A 179     8532   6371   7107  -2433   2725   -725       C  
ATOM   1353  CE1 TYR A 179      51.900  -3.655  41.553  1.00 61.91           C  
ANISOU 1353  CE1 TYR A 179     8444   7037   8043  -2527   3081  -1064       C  
ATOM   1354  CE2 TYR A 179      53.026  -5.732  41.956  1.00 59.48           C  
ANISOU 1354  CE2 TYR A 179     8716   6562   7321  -2669   2985   -816       C  
ATOM   1355  CZ  TYR A 179      51.894  -4.941  42.060  1.00 71.49           C  
ANISOU 1355  CZ  TYR A 179     9933   8169   9061  -2719   3173   -990       C  
ATOM   1356  OH  TYR A 179      50.760  -5.426  42.666  1.00 80.35           O  
ANISOU 1356  OH  TYR A 179    11024   9288  10218  -2962   3453  -1095       O  
ATOM   1357  N   SER A 180      57.271  -3.096  37.452  1.00 41.59           N  
ANISOU 1357  N   SER A 180     6112   4390   5302  -1610   1812   -529       N  
ATOM   1358  CA  SER A 180      58.502  -2.649  36.798  1.00 39.56           C  
ANISOU 1358  CA  SER A 180     5894   4126   5010  -1424   1607   -448       C  
ATOM   1359  C   SER A 180      58.231  -1.694  35.647  1.00 39.67           C  
ANISOU 1359  C   SER A 180     5656   4206   5211  -1296   1490   -495       C  
ATOM   1360  O   SER A 180      59.007  -0.762  35.468  1.00 39.18           O  
ANISOU 1360  O   SER A 180     5579   4164   5143  -1156   1394   -470       O  
ATOM   1361  CB  SER A 180      59.314  -3.846  36.321  1.00 41.53           C  
ANISOU 1361  CB  SER A 180     6332   4292   5157  -1414   1485   -340       C  
ATOM   1362  OG  SER A 180      60.564  -3.387  35.847  1.00 49.72           O  
ANISOU 1362  OG  SER A 180     7409   5323   6159  -1245   1321   -274       O  
ATOM   1363  N   LEU A 181      57.141  -1.918  34.870  1.00 34.38           N  
ANISOU 1363  N   LEU A 181     4795   3562   4704  -1350   1487   -559       N  
ATOM   1364  CA  LEU A 181      56.771  -1.048  33.757  1.00 33.83           C  
ANISOU 1364  CA  LEU A 181     4497   3544   4814  -1240   1353   -599       C  
ATOM   1365  C   LEU A 181      56.379   0.334  34.247  1.00 39.45           C  
ANISOU 1365  C   LEU A 181     5043   4308   5640  -1175   1418   -680       C  
ATOM   1366  O   LEU A 181      56.884   1.323  33.719  1.00 40.08           O  
ANISOU 1366  O   LEU A 181     5066   4403   5760  -1030   1290   -659       O  
ATOM   1367  CB  LEU A 181      55.701  -1.682  32.840  1.00 33.51           C  
ANISOU 1367  CB  LEU A 181     4303   3512   4919  -1322   1308   -645       C  
ATOM   1368  CG  LEU A 181      55.169  -0.810  31.677  1.00 37.26           C  
ANISOU 1368  CG  LEU A 181     4540   4031   5586  -1224   1146   -685       C  
ATOM   1369  CD1 LEU A 181      56.295  -0.365  30.708  1.00 35.47           C  
ANISOU 1369  CD1 LEU A 181     4403   3793   5282  -1073    946   -594       C  
ATOM   1370  CD2 LEU A 181      54.043  -1.512  30.958  1.00 39.14           C  
ANISOU 1370  CD2 LEU A 181     4631   4276   5965  -1331   1108   -740       C  
ATOM   1371  N   ILE A 182      55.547   0.404  35.304  1.00 37.22           N  
ANISOU 1371  N   ILE A 182     4702   4041   5399  -1286   1629   -774       N  
ATOM   1372  CA  ILE A 182      55.157   1.666  35.925  1.00 37.11           C  
ANISOU 1372  CA  ILE A 182     4544   4063   5492  -1235   1729   -871       C  
ATOM   1373  C   ILE A 182      56.429   2.407  36.376  1.00 40.17           C  
ANISOU 1373  C   ILE A 182     5099   4439   5724  -1121   1677   -805       C  
ATOM   1374  O   ILE A 182      56.641   3.555  35.965  1.00 40.22           O  
ANISOU 1374  O   ILE A 182     4994   4462   5827   -983   1581   -819       O  
ATOM   1375  CB  ILE A 182      54.132   1.468  37.085  1.00 40.40           C  
ANISOU 1375  CB  ILE A 182     4911   4492   5946  -1401   2007   -991       C  
ATOM   1376  CG1 ILE A 182      52.832   0.789  36.578  1.00 41.05           C  
ANISOU 1376  CG1 ILE A 182     4792   4589   6214  -1520   2057  -1068       C  
ATOM   1377  CG2 ILE A 182      53.827   2.811  37.785  1.00 40.12           C  
ANISOU 1377  CG2 ILE A 182     4741   4485   6019  -1340   2127  -1105       C  
ATOM   1378  CD1 ILE A 182      51.868   0.280  37.725  1.00 46.66           C  
ANISOU 1378  CD1 ILE A 182     5486   5305   6939  -1728   2365  -1184       C  
ATOM   1379  N   TYR A 183      57.298   1.730  37.160  1.00 34.45           N  
ANISOU 1379  N   TYR A 183     4645   3676   4767  -1179   1719   -726       N  
ATOM   1380  CA  TYR A 183      58.539   2.338  37.641  1.00 33.82           C  
ANISOU 1380  CA  TYR A 183     4727   3582   4539  -1086   1657   -663       C  
ATOM   1381  C   TYR A 183      59.431   2.832  36.506  1.00 35.96           C  
ANISOU 1381  C   TYR A 183     4963   3855   4847   -919   1433   -589       C  
ATOM   1382  O   TYR A 183      59.951   3.941  36.588  1.00 35.10           O  
ANISOU 1382  O   TYR A 183     4829   3758   4750   -815   1387   -596       O  
ATOM   1383  CB  TYR A 183      59.303   1.411  38.604  1.00 34.47           C  
ANISOU 1383  CB  TYR A 183     5106   3611   4378  -1176   1701   -581       C  
ATOM   1384  CG  TYR A 183      60.722   1.861  38.883  1.00 35.93           C  
ANISOU 1384  CG  TYR A 183     5449   3776   4426  -1069   1577   -498       C  
ATOM   1385  CD1 TYR A 183      60.978   3.020  39.615  1.00 36.92           C  
ANISOU 1385  CD1 TYR A 183     5577   3923   4526  -1028   1625   -548       C  
ATOM   1386  CD2 TYR A 183      61.809   1.174  38.350  1.00 36.95           C  
ANISOU 1386  CD2 TYR A 183     5703   3860   4475  -1002   1408   -382       C  
ATOM   1387  CE1 TYR A 183      62.283   3.467  39.825  1.00 36.29           C  
ANISOU 1387  CE1 TYR A 183     5623   3826   4338   -934   1498   -478       C  
ATOM   1388  CE2 TYR A 183      63.116   1.609  38.562  1.00 37.17           C  
ANISOU 1388  CE2 TYR A 183     5841   3871   4411   -901   1289   -317       C  
ATOM   1389  CZ  TYR A 183      63.348   2.732  39.330  1.00 40.59           C  
ANISOU 1389  CZ  TYR A 183     6281   4331   4812   -875   1331   -361       C  
ATOM   1390  OH  TYR A 183      64.640   3.119  39.558  1.00 41.16           O  
ANISOU 1390  OH  TYR A 183     6457   4385   4799   -789   1206   -299       O  
ATOM   1391  N   SER A 184      59.599   2.010  35.458  1.00 31.17           N  
ANISOU 1391  N   SER A 184     4365   3230   4250   -907   1307   -525       N  
ATOM   1392  CA  SER A 184      60.394   2.330  34.275  1.00 29.51           C  
ANISOU 1392  CA  SER A 184     4136   3016   4061   -777   1114   -459       C  
ATOM   1393  C   SER A 184      59.852   3.563  33.593  1.00 34.12           C  
ANISOU 1393  C   SER A 184     4508   3637   4820   -687   1050   -515       C  
ATOM   1394  O   SER A 184      60.626   4.450  33.258  1.00 33.82           O  
ANISOU 1394  O   SER A 184     4476   3599   4776   -575    955   -483       O  
ATOM   1395  CB  SER A 184      60.401   1.161  33.300  1.00 29.93           C  
ANISOU 1395  CB  SER A 184     4232   3041   4101   -812   1029   -409       C  
ATOM   1396  OG  SER A 184      61.130   1.506  32.134  1.00 31.11           O  
ANISOU 1396  OG  SER A 184     4368   3188   4263   -700    865   -360       O  
ATOM   1397  N   LEU A 185      58.518   3.626  33.414  1.00 32.64           N  
ANISOU 1397  N   LEU A 185     4130   3473   4798   -740   1100   -599       N  
ATOM   1398  CA  LEU A 185      57.806   4.765  32.824  1.00 32.57           C  
ANISOU 1398  CA  LEU A 185     3897   3485   4993   -657   1031   -661       C  
ATOM   1399  C   LEU A 185      57.987   6.045  33.668  1.00 37.21           C  
ANISOU 1399  C   LEU A 185     4449   4076   5612   -586   1109   -715       C  
ATOM   1400  O   LEU A 185      58.273   7.088  33.098  1.00 36.65           O  
ANISOU 1400  O   LEU A 185     4307   3997   5622   -469    991   -705       O  
ATOM   1401  CB  LEU A 185      56.317   4.420  32.616  1.00 32.35           C  
ANISOU 1401  CB  LEU A 185     3662   3476   5152   -741   1080   -752       C  
ATOM   1402  CG  LEU A 185      55.995   3.515  31.430  1.00 36.12           C  
ANISOU 1402  CG  LEU A 185     4118   3949   5658   -783    940   -711       C  
ATOM   1403  CD1 LEU A 185      54.583   3.015  31.515  1.00 35.99           C  
ANISOU 1403  CD1 LEU A 185     3910   3951   5813   -896   1021   -810       C  
ATOM   1404  CD2 LEU A 185      56.227   4.218  30.102  1.00 39.50           C  
ANISOU 1404  CD2 LEU A 185     4492   4371   6147   -663    708   -660       C  
ATOM   1405  N   CYS A 186      57.887   5.954  35.017  1.00 35.75           N  
ANISOU 1405  N   CYS A 186     4341   3895   5348   -667   1305   -769       N  
ATOM   1406  CA  CYS A 186      58.141   7.095  35.907  1.00 36.97           C  
ANISOU 1406  CA  CYS A 186     4500   4047   5500   -618   1393   -827       C  
ATOM   1407  C   CYS A 186      59.621   7.511  35.823  1.00 37.72           C  
ANISOU 1407  C   CYS A 186     4766   4123   5441   -526   1270   -728       C  
ATOM   1408  O   CYS A 186      59.902   8.707  35.769  1.00 36.16           O  
ANISOU 1408  O   CYS A 186     4518   3916   5305   -428   1226   -749       O  
ATOM   1409  CB  CYS A 186      57.731   6.791  37.346  1.00 38.71           C  
ANISOU 1409  CB  CYS A 186     4798   4272   5637   -751   1637   -908       C  
ATOM   1410  SG  CYS A 186      55.964   6.437  37.555  1.00 43.74           S  
ANISOU 1410  SG  CYS A 186     5200   4933   6487   -869   1830  -1058       S  
ATOM   1411  N   LEU A 187      60.560   6.524  35.772  1.00 31.53           N  
ANISOU 1411  N   LEU A 187     4174   3326   4478   -558   1212   -625       N  
ATOM   1412  CA  LEU A 187      61.997   6.800  35.684  1.00 30.06           C  
ANISOU 1412  CA  LEU A 187     4131   3122   4166   -478   1097   -537       C  
ATOM   1413  C   LEU A 187      62.372   7.466  34.329  1.00 36.42           C  
ANISOU 1413  C   LEU A 187     4847   3925   5065   -360    923   -493       C  
ATOM   1414  O   LEU A 187      63.226   8.363  34.307  1.00 35.79           O  
ANISOU 1414  O   LEU A 187     4800   3836   4964   -280    860   -470       O  
ATOM   1415  CB  LEU A 187      62.812   5.531  35.989  1.00 28.56           C  
ANISOU 1415  CB  LEU A 187     4145   2908   3798   -537   1080   -450       C  
ATOM   1416  CG  LEU A 187      64.352   5.607  36.051  1.00 30.57           C  
ANISOU 1416  CG  LEU A 187     4546   3139   3931   -467    969   -366       C  
ATOM   1417  CD1 LEU A 187      64.839   6.472  37.202  1.00 29.71           C  
ANISOU 1417  CD1 LEU A 187     4509   3030   3748   -460   1017   -395       C  
ATOM   1418  CD2 LEU A 187      64.952   4.199  36.167  1.00 28.95           C  
ANISOU 1418  CD2 LEU A 187     4507   2894   3600   -516    938   -286       C  
ATOM   1419  N   THR A 188      61.675   7.083  33.224  1.00 32.71           N  
ANISOU 1419  N   THR A 188     4270   3461   4699   -362    848   -487       N  
ATOM   1420  CA  THR A 188      61.852   7.693  31.896  1.00 32.04           C  
ANISOU 1420  CA  THR A 188     4115   3367   4690   -272    684   -446       C  
ATOM   1421  C   THR A 188      61.430   9.178  32.002  1.00 36.66           C  
ANISOU 1421  C   THR A 188     4568   3943   5417   -193    674   -505       C  
ATOM   1422  O   THR A 188      62.208  10.057  31.636  1.00 37.11           O  
ANISOU 1422  O   THR A 188     4662   3980   5460   -113    590   -466       O  
ATOM   1423  CB  THR A 188      61.056   6.899  30.825  1.00 33.04           C  
ANISOU 1423  CB  THR A 188     4169   3498   4885   -314    607   -438       C  
ATOM   1424  OG1 THR A 188      61.498   5.547  30.825  1.00 30.46           O  
ANISOU 1424  OG1 THR A 188     3979   3165   4429   -387    632   -392       O  
ATOM   1425  CG2 THR A 188      61.196   7.474  29.404  1.00 28.85           C  
ANISOU 1425  CG2 THR A 188     3603   2952   4405   -241    426   -389       C  
ATOM   1426  N   LEU A 189      60.229   9.441  32.560  1.00 33.24           N  
ANISOU 1426  N   LEU A 189     3984   3518   5126   -221    776   -606       N  
ATOM   1427  CA  LEU A 189      59.683  10.782  32.783  1.00 33.66           C  
ANISOU 1427  CA  LEU A 189     3895   3550   5344   -144    790   -684       C  
ATOM   1428  C   LEU A 189      60.558  11.669  33.702  1.00 39.74           C  
ANISOU 1428  C   LEU A 189     4768   4303   6028   -106    857   -698       C  
ATOM   1429  O   LEU A 189      61.046  12.711  33.255  1.00 40.38           O  
ANISOU 1429  O   LEU A 189     4845   4349   6148    -13    754   -671       O  
ATOM   1430  CB  LEU A 189      58.240  10.688  33.314  1.00 33.67           C  
ANISOU 1430  CB  LEU A 189     3708   3564   5521   -196    923   -809       C  
ATOM   1431  CG  LEU A 189      57.476  12.002  33.444  1.00 38.13           C  
ANISOU 1431  CG  LEU A 189     4084   4094   6312   -108    939   -909       C  
ATOM   1432  CD1 LEU A 189      57.010  12.504  32.074  1.00 38.05           C  
ANISOU 1432  CD1 LEU A 189     3930   4048   6478    -12    714   -871       C  
ATOM   1433  CD2 LEU A 189      56.315  11.847  34.398  1.00 38.41           C  
ANISOU 1433  CD2 LEU A 189     3972   4146   6476   -183   1154  -1057       C  
ATOM   1434  N   LEU A 190      60.752  11.267  34.969  1.00 36.64           N  
ANISOU 1434  N   LEU A 190     4481   3928   5513   -187   1020   -738       N  
ATOM   1435  CA  LEU A 190      61.566  12.028  35.930  1.00 36.17           C  
ANISOU 1435  CA  LEU A 190     4536   3854   5354   -170   1080   -758       C  
ATOM   1436  C   LEU A 190      63.053  12.143  35.537  1.00 35.46           C  
ANISOU 1436  C   LEU A 190     4593   3753   5128   -120    941   -648       C  
ATOM   1437  O   LEU A 190      63.616  13.215  35.639  1.00 35.01           O  
ANISOU 1437  O   LEU A 190     4551   3669   5084    -58    906   -656       O  
ATOM   1438  CB  LEU A 190      61.437  11.443  37.357  1.00 36.82           C  
ANISOU 1438  CB  LEU A 190     4733   3954   5301   -290   1272   -816       C  
ATOM   1439  CG  LEU A 190      60.228  11.896  38.167  1.00 43.42           C  
ANISOU 1439  CG  LEU A 190     5450   4790   6259   -334   1469   -968       C  
ATOM   1440  CD1 LEU A 190      59.869  10.883  39.212  1.00 44.32           C  
ANISOU 1440  CD1 LEU A 190     5669   4927   6243   -488   1654  -1006       C  
ATOM   1441  CD2 LEU A 190      60.498  13.219  38.859  1.00 48.68           C  
ANISOU 1441  CD2 LEU A 190     6140   5424   6934   -284   1522  -1042       C  
ATOM   1442  N   GLY A 191      63.667  11.043  35.110  1.00 28.75           N  
ANISOU 1442  N   GLY A 191     3842   2918   4162   -152    875   -556       N  
ATOM   1443  CA  GLY A 191      65.082  11.014  34.774  1.00 26.86           C  
ANISOU 1443  CA  GLY A 191     3724   2669   3811   -113    765   -465       C  
ATOM   1444  C   GLY A 191      65.486  11.503  33.400  1.00 29.90           C  
ANISOU 1444  C   GLY A 191     4062   3038   4260    -36    620   -406       C  
ATOM   1445  O   GLY A 191      66.594  12.021  33.258  1.00 29.42           O  
ANISOU 1445  O   GLY A 191     4066   2962   4150      5    558   -364       O  
ATOM   1446  N   PHE A 192      64.633  11.315  32.362  1.00 25.31           N  
ANISOU 1446  N   PHE A 192     3379   2457   3781    -27    562   -400       N  
ATOM   1447  CA  PHE A 192      64.994  11.713  31.006  1.00 23.32           C  
ANISOU 1447  CA  PHE A 192     3116   2183   3560     27    420   -336       C  
ATOM   1448  C   PHE A 192      64.161  12.861  30.461  1.00 27.79           C  
ANISOU 1448  C   PHE A 192     3555   2716   4288     89    352   -366       C  
ATOM   1449  O   PHE A 192      64.740  13.890  30.132  1.00 27.02           O  
ANISOU 1449  O   PHE A 192     3482   2581   4203    145    288   -340       O  
ATOM   1450  CB  PHE A 192      64.975  10.490  30.043  1.00 24.43           C  
ANISOU 1450  CB  PHE A 192     3293   2338   3651    -16    364   -283       C  
ATOM   1451  CG  PHE A 192      65.027  10.717  28.530  1.00 24.43           C  
ANISOU 1451  CG  PHE A 192     3292   2318   3672     11    226   -228       C  
ATOM   1452  CD1 PHE A 192      65.903  11.645  27.972  1.00 25.90           C  
ANISOU 1452  CD1 PHE A 192     3531   2476   3834     59    158   -184       C  
ATOM   1453  CD2 PHE A 192      64.284   9.915  27.664  1.00 25.90           C  
ANISOU 1453  CD2 PHE A 192     3449   2511   3881    -30    166   -218       C  
ATOM   1454  CE1 PHE A 192      65.940  11.849  26.583  1.00 26.95           C  
ANISOU 1454  CE1 PHE A 192     3695   2584   3961     64     38   -130       C  
ATOM   1455  CE2 PHE A 192      64.355  10.091  26.270  1.00 27.37           C  
ANISOU 1455  CE2 PHE A 192     3668   2674   4055    -22     33   -165       C  
ATOM   1456  CZ  PHE A 192      65.177  11.056  25.742  1.00 25.03           C  
ANISOU 1456  CZ  PHE A 192     3436   2347   3726     22    -26   -119       C  
ATOM   1457  N   LEU A 193      62.840  12.673  30.299  1.00 25.13           N  
ANISOU 1457  N   LEU A 193     3083   2384   4084     78    353   -416       N  
ATOM   1458  CA  LEU A 193      61.951  13.622  29.639  1.00 25.43           C  
ANISOU 1458  CA  LEU A 193     2981   2377   4302    145    251   -438       C  
ATOM   1459  C   LEU A 193      61.837  15.000  30.315  1.00 33.78           C  
ANISOU 1459  C   LEU A 193     3979   3387   5468    218    290   -501       C  
ATOM   1460  O   LEU A 193      61.885  16.012  29.607  1.00 34.42           O  
ANISOU 1460  O   LEU A 193     4047   3406   5623    290    164   -466       O  
ATOM   1461  CB  LEU A 193      60.562  13.016  29.414  1.00 25.46           C  
ANISOU 1461  CB  LEU A 193     2829   2399   4446    113    246   -491       C  
ATOM   1462  CG  LEU A 193      60.496  11.722  28.573  1.00 31.01           C  
ANISOU 1462  CG  LEU A 193     3580   3134   5068     40    180   -435       C  
ATOM   1463  CD1 LEU A 193      59.093  11.177  28.572  1.00 31.28           C  
ANISOU 1463  CD1 LEU A 193     3443   3187   5256     -4    194   -505       C  
ATOM   1464  CD2 LEU A 193      60.972  11.951  27.115  1.00 32.26           C  
ANISOU 1464  CD2 LEU A 193     3823   3261   5172     70    -13   -335       C  
ATOM   1465  N   ILE A 194      61.678  15.056  31.651  1.00 32.02           N  
ANISOU 1465  N   ILE A 194     3739   3182   5247    191    463   -593       N  
ATOM   1466  CA  ILE A 194      61.574  16.340  32.357  1.00 32.60           C  
ANISOU 1466  CA  ILE A 194     3766   3204   5417    252    522   -672       C  
ATOM   1467  C   ILE A 194      62.907  17.109  32.249  1.00 36.79           C  
ANISOU 1467  C   ILE A 194     4442   3701   5834    285    459   -605       C  
ATOM   1468  O   ILE A 194      62.832  18.243  31.796  1.00 38.18           O  
ANISOU 1468  O   ILE A 194     4580   3806   6122    363    371   -601       O  
ATOM   1469  CB  ILE A 194      61.016  16.228  33.807  1.00 35.84           C  
ANISOU 1469  CB  ILE A 194     4136   3638   5844    198    739   -801       C  
ATOM   1470  CG1 ILE A 194      59.517  15.789  33.767  1.00 35.83           C  
ANISOU 1470  CG1 ILE A 194     3936   3652   6027    178    798   -887       C  
ATOM   1471  CG2 ILE A 194      61.217  17.549  34.595  1.00 34.57           C  
ANISOU 1471  CG2 ILE A 194     3981   3420   5735    251    811   -883       C  
ATOM   1472  CD1 ILE A 194      58.914  15.386  35.077  1.00 33.95           C  
ANISOU 1472  CD1 ILE A 194     3669   3447   5782     88   1037  -1011       C  
ATOM   1473  N   PRO A 195      64.121  16.543  32.533  1.00 31.81           N  
ANISOU 1473  N   PRO A 195     3971   3111   5006    233    481   -547       N  
ATOM   1474  CA  PRO A 195      65.352  17.346  32.357  1.00 30.86           C  
ANISOU 1474  CA  PRO A 195     3956   2955   4813    262    416   -494       C  
ATOM   1475  C   PRO A 195      65.572  17.784  30.906  1.00 33.81           C  
ANISOU 1475  C   PRO A 195     4335   3286   5226    306    255   -404       C  
ATOM   1476  O   PRO A 195      66.082  18.879  30.654  1.00 33.53           O  
ANISOU 1476  O   PRO A 195     4335   3189   5216    346    199   -385       O  
ATOM   1477  CB  PRO A 195      66.472  16.414  32.859  1.00 32.08           C  
ANISOU 1477  CB  PRO A 195     4245   3166   4780    196    457   -452       C  
ATOM   1478  CG  PRO A 195      65.786  15.439  33.750  1.00 35.87           C  
ANISOU 1478  CG  PRO A 195     4712   3691   5224    133    578   -507       C  
ATOM   1479  CD  PRO A 195      64.437  15.224  33.129  1.00 31.95           C  
ANISOU 1479  CD  PRO A 195     4073   3193   4872    146    567   -535       C  
ATOM   1480  N   LEU A 196      65.131  16.956  29.956  1.00 29.29           N  
ANISOU 1480  N   LEU A 196     3739   2736   4653    289    181   -353       N  
ATOM   1481  CA  LEU A 196      65.261  17.249  28.541  1.00 28.79           C  
ANISOU 1481  CA  LEU A 196     3709   2632   4598    310     27   -266       C  
ATOM   1482  C   LEU A 196      64.402  18.456  28.172  1.00 34.07           C  
ANISOU 1482  C   LEU A 196     4285   3215   5446    388    -70   -283       C  
ATOM   1483  O   LEU A 196      64.920  19.372  27.544  1.00 34.58           O  
ANISOU 1483  O   LEU A 196     4420   3211   5507    417   -162   -227       O  
ATOM   1484  CB  LEU A 196      64.943  16.008  27.665  1.00 28.64           C  
ANISOU 1484  CB  LEU A 196     3701   2657   4524    260    -26   -219       C  
ATOM   1485  CG  LEU A 196      65.059  16.203  26.145  1.00 32.12           C  
ANISOU 1485  CG  LEU A 196     4211   3058   4935    259   -185   -128       C  
ATOM   1486  CD1 LEU A 196      66.519  16.249  25.710  1.00 31.19           C  
ANISOU 1486  CD1 LEU A 196     4247   2939   4666    226   -173    -66       C  
ATOM   1487  CD2 LEU A 196      64.305  15.121  25.410  1.00 34.49           C  
ANISOU 1487  CD2 LEU A 196     4487   3391   5226    214   -246   -112       C  
ATOM   1488  N   SER A 197      63.121  18.484  28.592  1.00 31.97           N  
ANISOU 1488  N   SER A 197     3859   2943   5344    421    -44   -366       N  
ATOM   1489  CA  SER A 197      62.226  19.623  28.318  1.00 33.00           C  
ANISOU 1489  CA  SER A 197     3872   2979   5686    513   -141   -396       C  
ATOM   1490  C   SER A 197      62.680  20.895  29.041  1.00 35.68           C  
ANISOU 1490  C   SER A 197     4237   3246   6072    566    -85   -442       C  
ATOM   1491  O   SER A 197      62.474  21.985  28.510  1.00 36.66           O  
ANISOU 1491  O   SER A 197     4348   3265   6314    640   -208   -418       O  
ATOM   1492  CB  SER A 197      60.785  19.295  28.683  1.00 37.71           C  
ANISOU 1492  CB  SER A 197     4264   3590   6474    532   -103   -495       C  
ATOM   1493  OG  SER A 197      60.721  18.960  30.057  1.00 50.00           O  
ANISOU 1493  OG  SER A 197     5786   5200   8012    492    115   -603       O  
ATOM   1494  N   VAL A 198      63.288  20.759  30.247  1.00 30.68           N  
ANISOU 1494  N   VAL A 198     3654   2661   5342    523     87   -507       N  
ATOM   1495  CA  VAL A 198      63.829  21.889  31.013  1.00 29.57           C  
ANISOU 1495  CA  VAL A 198     3560   2459   5215    553    150   -559       C  
ATOM   1496  C   VAL A 198      64.951  22.550  30.188  1.00 35.48           C  
ANISOU 1496  C   VAL A 198     4451   3153   5875    555     31   -449       C  
ATOM   1497  O   VAL A 198      64.954  23.762  30.092  1.00 37.36           O  
ANISOU 1497  O   VAL A 198     4696   3287   6214    614    -24   -456       O  
ATOM   1498  CB  VAL A 198      64.252  21.545  32.476  1.00 31.64           C  
ANISOU 1498  CB  VAL A 198     3870   2785   5365    490    342   -646       C  
ATOM   1499  CG1 VAL A 198      64.990  22.720  33.135  1.00 31.58           C  
ANISOU 1499  CG1 VAL A 198     3943   2713   5343    506    379   -687       C  
ATOM   1500  CG2 VAL A 198      63.049  21.156  33.315  1.00 30.34           C  
ANISOU 1500  CG2 VAL A 198     3572   2650   5306    482    483   -770       C  
ATOM   1501  N   MET A 199      65.833  21.760  29.534  1.00 32.91           N  
ANISOU 1501  N   MET A 199     4236   2890   5380    488     -6   -353       N  
ATOM   1502  CA  MET A 199      66.897  22.267  28.652  1.00 32.67           C  
ANISOU 1502  CA  MET A 199     4338   2816   5260    468    -96   -254       C  
ATOM   1503  C   MET A 199      66.309  22.968  27.446  1.00 36.30           C  
ANISOU 1503  C   MET A 199     4799   3178   5817    517   -265   -184       C  
ATOM   1504  O   MET A 199      66.810  24.024  27.079  1.00 34.71           O  
ANISOU 1504  O   MET A 199     4681   2884   5624    530   -327   -142       O  
ATOM   1505  CB  MET A 199      67.836  21.150  28.182  1.00 34.81           C  
ANISOU 1505  CB  MET A 199     4700   3173   5352    388    -81   -186       C  
ATOM   1506  CG  MET A 199      68.890  20.818  29.201  1.00 38.47           C  
ANISOU 1506  CG  MET A 199     5210   3697   5708    342     36   -223       C  
ATOM   1507  SD  MET A 199      70.191  19.728  28.589  1.00 42.49           S  
ANISOU 1507  SD  MET A 199     5819   4276   6051    267     43   -148       S  
ATOM   1508  CE  MET A 199      69.320  18.185  28.484  1.00 38.53           C  
ANISOU 1508  CE  MET A 199     5267   3849   5525    251     59   -150       C  
ATOM   1509  N   CYS A 200      65.257  22.374  26.833  1.00 34.24           N  
ANISOU 1509  N   CYS A 200     4455   2930   5624    536   -350   -169       N  
ATOM   1510  CA  CYS A 200      64.498  22.915  25.698  1.00 34.94           C  
ANISOU 1510  CA  CYS A 200     4535   2925   5817    586   -546   -101       C  
ATOM   1511  C   CYS A 200      63.868  24.265  26.061  1.00 40.12           C  
ANISOU 1511  C   CYS A 200     5110   3453   6681    690   -595   -152       C  
ATOM   1512  O   CYS A 200      63.889  25.184  25.241  1.00 40.00           O  
ANISOU 1512  O   CYS A 200     5173   3318   6705    724   -749    -74       O  
ATOM   1513  CB  CYS A 200      63.431  21.928  25.244  1.00 35.46           C  
ANISOU 1513  CB  CYS A 200     4495   3042   5937    583   -616   -104       C  
ATOM   1514  SG  CYS A 200      64.073  20.493  24.357  1.00 39.67           S  
ANISOU 1514  SG  CYS A 200     5157   3678   6238    468   -622    -21       S  
ATOM   1515  N   PHE A 201      63.311  24.372  27.294  1.00 36.87           N  
ANISOU 1515  N   PHE A 201     4554   3057   6399    735   -457   -286       N  
ATOM   1516  CA  PHE A 201      62.711  25.576  27.847  1.00 37.40           C  
ANISOU 1516  CA  PHE A 201     4525   3006   6680    836   -456   -371       C  
ATOM   1517  C   PHE A 201      63.763  26.681  27.932  1.00 43.48           C  
ANISOU 1517  C   PHE A 201     5447   3687   7385    832   -454   -338       C  
ATOM   1518  O   PHE A 201      63.492  27.833  27.548  1.00 42.98           O  
ANISOU 1518  O   PHE A 201     5395   3475   7460    909   -575   -315       O  
ATOM   1519  CB  PHE A 201      62.128  25.288  29.244  1.00 39.69           C  
ANISOU 1519  CB  PHE A 201     4666   3354   7060    846   -250   -534       C  
ATOM   1520  CG  PHE A 201      61.774  26.517  30.056  1.00 42.41           C  
ANISOU 1520  CG  PHE A 201     4941   3585   7587    931   -183   -650       C  
ATOM   1521  CD1 PHE A 201      60.594  27.215  29.814  1.00 46.20           C  
ANISOU 1521  CD1 PHE A 201     5260   3946   8347   1052   -283   -699       C  
ATOM   1522  CD2 PHE A 201      62.627  26.985  31.052  1.00 45.63           C  
ANISOU 1522  CD2 PHE A 201     5443   3996   7896    892    -28   -716       C  
ATOM   1523  CE1 PHE A 201      60.280  28.362  30.550  1.00 47.57           C  
ANISOU 1523  CE1 PHE A 201     5369   4000   8704   1137   -212   -818       C  
ATOM   1524  CE2 PHE A 201      62.315  28.136  31.787  1.00 49.08           C  
ANISOU 1524  CE2 PHE A 201     5832   4320   8495    965     41   -834       C  
ATOM   1525  CZ  PHE A 201      61.138  28.810  31.538  1.00 47.25           C  
ANISOU 1525  CZ  PHE A 201     5439   3966   8547   1089    -41   -888       C  
ATOM   1526  N   PHE A 202      64.954  26.332  28.482  1.00 39.77           N  
ANISOU 1526  N   PHE A 202     5090   3300   6719    741   -323   -339       N  
ATOM   1527  CA  PHE A 202      66.058  27.272  28.621  1.00 38.60           C  
ANISOU 1527  CA  PHE A 202     5081   3087   6499    714   -307   -315       C  
ATOM   1528  C   PHE A 202      66.663  27.620  27.275  1.00 45.49           C  
ANISOU 1528  C   PHE A 202     6101   3894   7287    679   -459   -169       C  
ATOM   1529  O   PHE A 202      67.102  28.758  27.105  1.00 45.38           O  
ANISOU 1529  O   PHE A 202     6180   3761   7302    688   -506   -140       O  
ATOM   1530  CB  PHE A 202      67.086  26.794  29.649  1.00 38.80           C  
ANISOU 1530  CB  PHE A 202     5160   3218   6364    629   -141   -368       C  
ATOM   1531  CG  PHE A 202      66.634  27.146  31.050  1.00 38.42           C  
ANISOU 1531  CG  PHE A 202     5031   3163   6404    662      0   -518       C  
ATOM   1532  CD1 PHE A 202      66.799  28.435  31.550  1.00 39.24           C  
ANISOU 1532  CD1 PHE A 202     5168   3150   6592    697     20   -580       C  
ATOM   1533  CD2 PHE A 202      65.982  26.211  31.844  1.00 38.52           C  
ANISOU 1533  CD2 PHE A 202     4945   3274   6418    650    119   -604       C  
ATOM   1534  CE1 PHE A 202      66.349  28.767  32.830  1.00 39.09           C  
ANISOU 1534  CE1 PHE A 202     5087   3119   6647    719    164   -733       C  
ATOM   1535  CE2 PHE A 202      65.523  26.550  33.121  1.00 40.29           C  
ANISOU 1535  CE2 PHE A 202     5112   3487   6711    665    268   -752       C  
ATOM   1536  CZ  PHE A 202      65.718  27.821  33.608  1.00 37.92           C  
ANISOU 1536  CZ  PHE A 202     4849   3075   6485    699    293   -819       C  
ATOM   1537  N   TYR A 203      66.576  26.694  26.285  1.00 44.61           N  
ANISOU 1537  N   TYR A 203     6019   3848   7082    637   -538    -80       N  
ATOM   1538  CA  TYR A 203      67.031  26.932  24.914  1.00 46.42           C  
ANISOU 1538  CA  TYR A 203     6407   4017   7214    588   -678     58       C  
ATOM   1539  C   TYR A 203      66.182  28.056  24.302  1.00 51.69           C  
ANISOU 1539  C   TYR A 203     7078   4513   8048    679   -866    103       C  
ATOM   1540  O   TYR A 203      66.733  28.999  23.738  1.00 49.82           O  
ANISOU 1540  O   TYR A 203     6993   4161   7777    656   -943    182       O  
ATOM   1541  CB  TYR A 203      66.981  25.657  24.021  1.00 48.81           C  
ANISOU 1541  CB  TYR A 203     6741   4422   7383    523   -718    124       C  
ATOM   1542  CG  TYR A 203      67.099  26.003  22.548  1.00 52.40           C  
ANISOU 1542  CG  TYR A 203     7360   4791   7758    482   -888    259       C  
ATOM   1543  CD1 TYR A 203      68.286  26.516  22.026  1.00 55.17           C  
ANISOU 1543  CD1 TYR A 203     7896   5101   7965    392   -864    330       C  
ATOM   1544  CD2 TYR A 203      65.991  25.945  21.708  1.00 53.13           C  
ANISOU 1544  CD2 TYR A 203     7429   4827   7932    529  -1082    312       C  
ATOM   1545  CE1 TYR A 203      68.368  26.948  20.706  1.00 56.74           C  
ANISOU 1545  CE1 TYR A 203     8275   5204   8078    340  -1012    454       C  
ATOM   1546  CE2 TYR A 203      66.069  26.357  20.379  1.00 54.16           C  
ANISOU 1546  CE2 TYR A 203     7742   4861   7976    485  -1259    442       C  
ATOM   1547  CZ  TYR A 203      67.267  26.834  19.876  1.00 65.16           C  
ANISOU 1547  CZ  TYR A 203     9343   6216   9199    384  -1214    515       C  
ATOM   1548  OH  TYR A 203      67.368  27.245  18.568  1.00 71.77           O  
ANISOU 1548  OH  TYR A 203    10392   6954   9924    319  -1372    645       O  
ATOM   1549  N   TYR A 204      64.848  27.945  24.440  1.00 50.98           N  
ANISOU 1549  N   TYR A 204     6817   4404   8149    778   -938     50       N  
ATOM   1550  CA  TYR A 204      63.881  28.924  23.958  1.00 51.88           C  
ANISOU 1550  CA  TYR A 204     6889   4351   8472    889  -1133     76       C  
ATOM   1551  C   TYR A 204      64.124  30.326  24.561  1.00 53.43           C  
ANISOU 1551  C   TYR A 204     7111   4402   8789    952  -1103     30       C  
ATOM   1552  O   TYR A 204      64.105  31.300  23.816  1.00 53.27           O  
ANISOU 1552  O   TYR A 204     7204   4218   8820    985  -1273    121       O  
ATOM   1553  CB  TYR A 204      62.433  28.429  24.189  1.00 54.85           C  
ANISOU 1553  CB  TYR A 204     7025   4754   9060    982  -1179     -6       C  
ATOM   1554  CG  TYR A 204      61.385  29.503  23.983  1.00 59.88           C  
ANISOU 1554  CG  TYR A 204     7557   5213   9984   1127  -1350    -24       C  
ATOM   1555  CD1 TYR A 204      60.970  29.863  22.706  1.00 63.13           C  
ANISOU 1555  CD1 TYR A 204     8050   5499  10438   1161  -1631    109       C  
ATOM   1556  CD2 TYR A 204      60.840  30.192  25.066  1.00 61.22           C  
ANISOU 1556  CD2 TYR A 204     7555   5324  10379   1228  -1233   -176       C  
ATOM   1557  CE1 TYR A 204      60.035  30.881  22.508  1.00 66.58           C  
ANISOU 1557  CE1 TYR A 204     8390   5751  11157   1307  -1814     99       C  
ATOM   1558  CE2 TYR A 204      59.913  31.217  24.881  1.00 62.40           C  
ANISOU 1558  CE2 TYR A 204     7599   5292  10819   1374  -1387   -202       C  
ATOM   1559  CZ  TYR A 204      59.498  31.544  23.600  1.00 75.25           C  
ANISOU 1559  CZ  TYR A 204     9295   6792  12506   1421  -1688    -61       C  
ATOM   1560  OH  TYR A 204      58.582  32.551  23.398  1.00 83.52           O  
ANISOU 1560  OH  TYR A 204    10232   7644  13859   1577  -1867    -81       O  
ATOM   1561  N   LYS A 205      64.344  30.421  25.891  1.00 48.38           N  
ANISOU 1561  N   LYS A 205     6386   3811   8184    960   -896   -108       N  
ATOM   1562  CA  LYS A 205      64.588  31.687  26.608  1.00 47.29           C  
ANISOU 1562  CA  LYS A 205     6271   3542   8153   1009   -841   -178       C  
ATOM   1563  C   LYS A 205      65.848  32.416  26.129  1.00 53.31           C  
ANISOU 1563  C   LYS A 205     7263   4231   8762    922   -868    -78       C  
ATOM   1564  O   LYS A 205      65.821  33.638  25.971  1.00 54.69           O  
ANISOU 1564  O   LYS A 205     7506   4227   9047    973   -949    -61       O  
ATOM   1565  CB  LYS A 205      64.614  31.486  28.126  1.00 48.01           C  
ANISOU 1565  CB  LYS A 205     6250   3720   8271   1008   -606   -351       C  
ATOM   1566  CG  LYS A 205      63.258  31.135  28.707  1.00 58.50           C  
ANISOU 1566  CG  LYS A 205     7347   5071   9808   1103   -558   -477       C  
ATOM   1567  CD  LYS A 205      63.172  31.443  30.192  1.00 69.90           C  
ANISOU 1567  CD  LYS A 205     8715   6525  11321   1118   -338   -659       C  
ATOM   1568  CE  LYS A 205      62.435  32.729  30.501  1.00 79.86           C  
ANISOU 1568  CE  LYS A 205     9894   7595  12853   1248   -364   -754       C  
ATOM   1569  NZ  LYS A 205      60.989  32.650  30.156  1.00 90.03           N  
ANISOU 1569  NZ  LYS A 205    10967   8826  14414   1373   -464   -794       N  
ATOM   1570  N   MET A 206      66.931  31.666  25.863  1.00 50.31           N  
ANISOU 1570  N   MET A 206     6997   3978   8142    789   -799    -14       N  
ATOM   1571  CA  MET A 206      68.193  32.185  25.332  1.00 49.97           C  
ANISOU 1571  CA  MET A 206     7156   3889   7942    681   -800     78       C  
ATOM   1572  C   MET A 206      67.966  32.847  23.962  1.00 55.99           C  
ANISOU 1572  C   MET A 206     8070   4496   8709    684  -1012    227       C  
ATOM   1573  O   MET A 206      68.485  33.941  23.726  1.00 54.49           O  
ANISOU 1573  O   MET A 206     8022   4160   8522    657  -1052    274       O  
ATOM   1574  CB  MET A 206      69.229  31.064  25.191  1.00 51.69           C  
ANISOU 1574  CB  MET A 206     7427   4281   7934    551   -689    107       C  
ATOM   1575  CG  MET A 206      69.809  30.594  26.500  1.00 55.15           C  
ANISOU 1575  CG  MET A 206     7782   4844   8329    521   -501    -13       C  
ATOM   1576  SD  MET A 206      71.009  29.268  26.230  1.00 59.01           S  
ANISOU 1576  SD  MET A 206     8319   5514   8590    390   -402     27       S  
ATOM   1577  CE  MET A 206      72.504  30.098  26.736  1.00 55.60           C  
ANISOU 1577  CE  MET A 206     7981   5051   8095    295   -309      4       C  
ATOM   1578  N   VAL A 207      67.184  32.176  23.076  1.00 54.46           N  
ANISOU 1578  N   VAL A 207     7859   4327   8508    705  -1155    302       N  
ATOM   1579  CA  VAL A 207      66.830  32.634  21.726  1.00 54.65           C  
ANISOU 1579  CA  VAL A 207     8038   4213   8515    703  -1387    453       C  
ATOM   1580  C   VAL A 207      66.072  33.959  21.800  1.00 61.53           C  
ANISOU 1580  C   VAL A 207     8895   4862   9621    834  -1542    455       C  
ATOM   1581  O   VAL A 207      66.447  34.902  21.106  1.00 61.95           O  
ANISOU 1581  O   VAL A 207     9149   4753   9634    798  -1657    565       O  
ATOM   1582  CB  VAL A 207      66.091  31.542  20.897  1.00 57.47           C  
ANISOU 1582  CB  VAL A 207     8361   4656   8818    697  -1510    512       C  
ATOM   1583  CG1 VAL A 207      65.459  32.125  19.637  1.00 57.16           C  
ANISOU 1583  CG1 VAL A 207     8465   4451   8800    720  -1794    657       C  
ATOM   1584  CG2 VAL A 207      67.034  30.400  20.531  1.00 56.81           C  
ANISOU 1584  CG2 VAL A 207     8364   4746   8476    549  -1375    538       C  
ATOM   1585  N   VAL A 208      65.066  34.049  22.691  1.00 59.33           N  
ANISOU 1585  N   VAL A 208     8382   4571   9589    978  -1525    325       N  
ATOM   1586  CA  VAL A 208      64.269  35.263  22.916  1.00 59.65           C  
ANISOU 1586  CA  VAL A 208     8363   4399   9903   1128  -1649    291       C  
ATOM   1587  C   VAL A 208      65.174  36.432  23.349  1.00 64.67           C  
ANISOU 1587  C   VAL A 208     9140   4907  10523   1094  -1564    276       C  
ATOM   1588  O   VAL A 208      64.982  37.547  22.865  1.00 66.30           O  
ANISOU 1588  O   VAL A 208     9461   4894  10834   1147  -1731    351       O  
ATOM   1589  CB  VAL A 208      63.102  34.998  23.914  1.00 63.61           C  
ANISOU 1589  CB  VAL A 208     8562   4940  10668   1271  -1582    119       C  
ATOM   1590  CG1 VAL A 208      62.382  36.287  24.303  1.00 63.35           C  
ANISOU 1590  CG1 VAL A 208     8449   4683  10941   1431  -1667     52       C  
ATOM   1591  CG2 VAL A 208      62.109  33.991  23.342  1.00 63.18           C  
ANISOU 1591  CG2 VAL A 208     8369   4977  10659   1303  -1705    145       C  
ATOM   1592  N   PHE A 209      66.167  36.168  24.236  1.00 60.34           N  
ANISOU 1592  N   PHE A 209     8594   4489   9845   1000  -1321    186       N  
ATOM   1593  CA  PHE A 209      67.124  37.161  24.746  1.00 59.39           C  
ANISOU 1593  CA  PHE A 209     8595   4276   9695    944  -1219    154       C  
ATOM   1594  C   PHE A 209      68.024  37.652  23.625  1.00 65.33           C  
ANISOU 1594  C   PHE A 209     9615   4936  10272    817  -1313    323       C  
ATOM   1595  O   PHE A 209      68.279  38.855  23.525  1.00 64.48           O  
ANISOU 1595  O   PHE A 209     9640   4634  10226    819  -1370    356       O  
ATOM   1596  CB  PHE A 209      67.971  36.578  25.895  1.00 60.21           C  
ANISOU 1596  CB  PHE A 209     8633   4563   9681    859   -966     28       C  
ATOM   1597  CG  PHE A 209      68.935  37.546  26.549  1.00 60.86           C  
ANISOU 1597  CG  PHE A 209     8815   4565   9745    798   -859    -29       C  
ATOM   1598  CD1 PHE A 209      68.541  38.320  27.636  1.00 63.02           C  
ANISOU 1598  CD1 PHE A 209     9000   4748  10197    888   -782   -180       C  
ATOM   1599  CD2 PHE A 209      70.242  37.673  26.088  1.00 61.82           C  
ANISOU 1599  CD2 PHE A 209     9115   4701   9674    641   -823     56       C  
ATOM   1600  CE1 PHE A 209      69.436  39.208  28.246  1.00 62.70           C  
ANISOU 1600  CE1 PHE A 209     9061   4630  10133    821   -690   -239       C  
ATOM   1601  CE2 PHE A 209      71.139  38.547  26.711  1.00 63.44           C  
ANISOU 1601  CE2 PHE A 209     9399   4833   9870    573   -729     -4       C  
ATOM   1602  CZ  PHE A 209      70.730  39.302  27.788  1.00 61.25           C  
ANISOU 1602  CZ  PHE A 209     9045   4467   9761    663   -670   -148       C  
ATOM   1603  N   LEU A 210      68.506  36.721  22.785  1.00 64.09           N  
ANISOU 1603  N   LEU A 210     9544   4911   9895    698  -1316    423       N  
ATOM   1604  CA  LEU A 210      69.368  37.060  21.662  1.00 65.48           C  
ANISOU 1604  CA  LEU A 210     9983   5019   9880    553  -1375    577       C  
ATOM   1605  C   LEU A 210      68.625  37.825  20.555  1.00 72.21           C  
ANISOU 1605  C   LEU A 210    10988   5652  10797    607  -1647    724       C  
ATOM   1606  O   LEU A 210      69.120  38.864  20.115  1.00 71.90           O  
ANISOU 1606  O   LEU A 210    11159   5437  10722    543  -1705    811       O  
ATOM   1607  CB  LEU A 210      70.098  35.828  21.128  1.00 65.62           C  
ANISOU 1607  CB  LEU A 210    10042   5237   9654    413  -1279    621       C  
ATOM   1608  CG  LEU A 210      71.250  35.316  21.999  1.00 70.49           C  
ANISOU 1608  CG  LEU A 210    10590   6023  10169    318  -1032    517       C  
ATOM   1609  CD1 LEU A 210      71.721  33.984  21.513  1.00 71.05           C  
ANISOU 1609  CD1 LEU A 210    10638   6291  10066    235   -954    533       C  
ATOM   1610  CD2 LEU A 210      72.428  36.289  22.008  1.00 73.20           C  
ANISOU 1610  CD2 LEU A 210    11101   6280  10432    185   -952    545       C  
ATOM   1611  N   LYS A 211      67.414  37.358  20.168  1.00 70.16           N  
ANISOU 1611  N   LYS A 211    10617   5390  10651    726  -1823    746       N  
ATOM   1612  CA  LYS A 211      66.559  38.002  19.162  1.00 70.53           C  
ANISOU 1612  CA  LYS A 211    10780   5230  10790    801  -2124    881       C  
ATOM   1613  C   LYS A 211      66.183  39.450  19.551  1.00 76.87           C  
ANISOU 1613  C   LYS A 211    11598   5776  11832    923  -2221    863       C  
ATOM   1614  O   LYS A 211      65.983  40.287  18.666  1.00 76.26           O  
ANISOU 1614  O   LYS A 211    11729   5483  11765    928  -2446   1008       O  
ATOM   1615  CB  LYS A 211      65.293  37.167  18.884  1.00 72.25           C  
ANISOU 1615  CB  LYS A 211    10810   5513  11129    919  -2282    871       C  
ATOM   1616  CG  LYS A 211      65.536  35.913  18.053  1.00 85.82           C  
ANISOU 1616  CG  LYS A 211    12609   7401  12599    793  -2296    953       C  
ATOM   1617  CD  LYS A 211      65.176  36.088  16.582  1.00 96.13           C  
ANISOU 1617  CD  LYS A 211    14160   8565  13801    749  -2590   1146       C  
ATOM   1618  CE  LYS A 211      64.749  34.785  15.934  1.00107.11           C  
ANISOU 1618  CE  LYS A 211    15543  10110  15043    688  -2658   1188       C  
ATOM   1619  NZ  LYS A 211      65.872  33.820  15.766  1.00113.13           N  
ANISOU 1619  NZ  LYS A 211    16416  11063  15506    499  -2419   1184       N  
ATOM   1620  N   LYS A 212      66.110  39.739  20.874  1.00 74.63           N  
ANISOU 1620  N   LYS A 212    11116   5510  11730   1014  -2050    684       N  
ATOM   1621  CA  LYS A 212      65.805  41.067  21.426  1.00 74.76           C  
ANISOU 1621  CA  LYS A 212    11127   5294  11985   1131  -2092    626       C  
ATOM   1622  C   LYS A 212      67.014  42.034  21.370  1.00 79.93           C  
ANISOU 1622  C   LYS A 212    12042   5825  12503    991  -2022    687       C  
ATOM   1623  O   LYS A 212      66.851  43.239  21.605  1.00 79.85           O  
ANISOU 1623  O   LYS A 212    12104   5576  12661   1065  -2104    685       O  
ATOM   1624  CB  LYS A 212      65.330  40.929  22.881  1.00 77.00           C  
ANISOU 1624  CB  LYS A 212    11126   5659  12470   1246  -1896    398       C  
ATOM   1625  CG  LYS A 212      63.824  40.773  23.034  1.00 92.62           C  
ANISOU 1625  CG  LYS A 212    12845   7609  14738   1445  -2012    318       C  
ATOM   1626  CD  LYS A 212      63.420  40.508  24.484  1.00105.06           C  
ANISOU 1626  CD  LYS A 212    14159   9290  16469   1522  -1768     82       C  
ATOM   1627  CE  LYS A 212      63.477  41.730  25.375  1.00119.45           C  
ANISOU 1627  CE  LYS A 212    15970  10914  18501   1613  -1703    -40       C  
ATOM   1628  NZ  LYS A 212      63.656  41.355  26.803  1.00130.05           N  
ANISOU 1628  NZ  LYS A 212    17139  12394  19881   1615  -1413   -263       N  
ATOM   1629  N   ARG A 213      68.222  41.499  21.095  1.00 76.91           N  
ANISOU 1629  N   ARG A 213    11785   5603  11836    790  -1862    728       N  
ATOM   1630  CA  ARG A 213      69.480  42.253  21.056  1.00108.76           C  
ANISOU 1630  CA  ARG A 213    16037   9561  15724    625  -1757    769       C  
ATOM   1631  C   ARG A 213      70.265  42.013  19.762  1.00152.13           C  
ANISOU 1631  C   ARG A 213    21790  15077  20937    433  -1799    947       C  
ATOM   1632  O   ARG A 213      69.687  41.699  18.722  1.00120.85           O  
ANISOU 1632  O   ARG A 213    17938  11049  16931    450  -2009   1086       O  
ATOM   1633  CB  ARG A 213      70.346  41.891  22.279  1.00108.29           C  
ANISOU 1633  CB  ARG A 213    15845   9683  15616    555  -1474    603       C  
ATOM   1634  CG  ARG A 213      69.722  42.288  23.619  1.00114.75           C  
ANISOU 1634  CG  ARG A 213    16457  10465  16677    710  -1399    416       C  
ATOM   1635  CD  ARG A 213      70.200  41.420  24.762  1.00118.94           C  
ANISOU 1635  CD  ARG A 213    16815  11236  17140    665  -1158    257       C  
ATOM   1636  NE  ARG A 213      71.458  41.901  25.340  1.00126.22           N  
ANISOU 1636  NE  ARG A 213    17838  12167  17954    516  -1005    214       N  
ATOM   1637  CZ  ARG A 213      72.656  41.382  25.087  1.00142.02           C  
ANISOU 1637  CZ  ARG A 213    19907  14318  19736    341   -898    258       C  
ATOM   1638  NH1 ARG A 213      73.739  41.887  25.662  1.00129.33           N  
ANISOU 1638  NH1 ARG A 213    18366  12706  18069    213   -774    207       N  
ATOM   1639  NH2 ARG A 213      72.781  40.348  24.261  1.00129.20           N  
ANISOU 1639  NH2 ARG A 213    18277  12845  17966    292   -914    343       N  
ATOM   1640  N   ASN A 224      75.071  33.471  19.083  1.00 68.35           N  
ANISOU 1640  N   ASN A 224    10795   6033   9143   -284   -705    740       N  
ATOM   1641  CA  ASN A 224      74.955  32.068  18.695  1.00 67.54           C  
ANISOU 1641  CA  ASN A 224    10646   6092   8924   -312   -658    736       C  
ATOM   1642  C   ASN A 224      75.875  31.142  19.510  1.00 69.62           C  
ANISOU 1642  C   ASN A 224    10741   6537   9173   -344   -453    618       C  
ATOM   1643  O   ASN A 224      75.506  29.990  19.757  1.00 68.89           O  
ANISOU 1643  O   ASN A 224    10518   6579   9078   -286   -430    570       O  
ATOM   1644  CB  ASN A 224      75.193  31.899  17.198  1.00 68.54           C  
ANISOU 1644  CB  ASN A 224    11018   6175   8850   -460   -684    856       C  
ATOM   1645  N   LYS A 225      77.057  31.645  19.934  1.00 64.55           N  
ANISOU 1645  N   LYS A 225    10104   5890   8531   -437   -318    573       N  
ATOM   1646  CA  LYS A 225      78.028  30.902  20.743  1.00 64.01           C  
ANISOU 1646  CA  LYS A 225     9877   5974   8469   -468   -150    465       C  
ATOM   1647  C   LYS A 225      77.437  30.311  22.065  1.00 67.28           C  
ANISOU 1647  C   LYS A 225    10078   6486   8998   -323   -157    363       C  
ATOM   1648  O   LYS A 225      77.718  29.142  22.331  1.00 67.25           O  
ANISOU 1648  O   LYS A 225     9965   6627   8960   -319    -79    313       O  
ATOM   1649  CB  LYS A 225      79.288  31.739  21.020  1.00 66.56           C  
ANISOU 1649  CB  LYS A 225    10231   6253   8805   -587    -38    432       C  
ATOM   1650  CG  LYS A 225      80.463  30.929  21.560  1.00 74.38           C  
ANISOU 1650  CG  LYS A 225    11082   7394   9785   -652    125    340       C  
ATOM   1651  CD  LYS A 225      81.651  31.807  21.926  1.00 81.73           C  
ANISOU 1651  CD  LYS A 225    11994   8285  10774   -749    212    287       C  
ATOM   1652  CE  LYS A 225      82.919  31.008  22.109  1.00 83.24           C  
ANISOU 1652  CE  LYS A 225    12056   8608  10962   -832    362    208       C  
ATOM   1653  NZ  LYS A 225      83.460  30.504  20.816  1.00 86.45           N  
ANISOU 1653  NZ  LYS A 225    12565   9026  11257   -971    475    252       N  
ATOM   1654  N   PRO A 226      76.616  31.017  22.893  1.00 62.51           N  
ANISOU 1654  N   PRO A 226     9418   5809   8526   -209   -239    328       N  
ATOM   1655  CA  PRO A 226      76.093  30.362  24.111  1.00 61.52           C  
ANISOU 1655  CA  PRO A 226     9111   5785   8480    -99   -216    226       C  
ATOM   1656  C   PRO A 226      75.009  29.318  23.844  1.00 63.16           C  
ANISOU 1656  C   PRO A 226     9252   6067   8680    -17   -274    241       C  
ATOM   1657  O   PRO A 226      74.722  28.515  24.732  1.00 64.41           O  
ANISOU 1657  O   PRO A 226     9275   6333   8866     40   -225    164       O  
ATOM   1658  CB  PRO A 226      75.553  31.528  24.950  1.00 63.46           C  
ANISOU 1658  CB  PRO A 226     9338   5909   8865    -17   -266    177       C  
ATOM   1659  CG  PRO A 226      75.971  32.785  24.242  1.00 68.00           C  
ANISOU 1659  CG  PRO A 226    10079   6320   9438    -90   -313    251       C  
ATOM   1660  CD  PRO A 226      76.142  32.415  22.811  1.00 63.99           C  
ANISOU 1660  CD  PRO A 226     9705   5810   8799   -176   -344    368       C  
ATOM   1661  N   LEU A 227      74.406  29.326  22.632  1.00 56.35           N  
ANISOU 1661  N   LEU A 227     8495   5142   7774    -22   -384    341       N  
ATOM   1662  CA  LEU A 227      73.363  28.372  22.237  1.00 54.30           C  
ANISOU 1662  CA  LEU A 227     8182   4941   7508     40   -460    361       C  
ATOM   1663  C   LEU A 227      73.933  27.004  21.884  1.00 54.95           C  
ANISOU 1663  C   LEU A 227     8254   5167   7459    -30   -367    357       C  
ATOM   1664  O   LEU A 227      73.180  26.034  21.915  1.00 54.81           O  
ANISOU 1664  O   LEU A 227     8155   5224   7445     21   -395    342       O  
ATOM   1665  CB  LEU A 227      72.553  28.877  21.037  1.00 54.24           C  
ANISOU 1665  CB  LEU A 227     8307   4807   7494     51   -638    473       C  
ATOM   1666  CG  LEU A 227      71.704  30.124  21.209  1.00 59.69           C  
ANISOU 1666  CG  LEU A 227     8987   5340   8352    159   -779    484       C  
ATOM   1667  CD1 LEU A 227      71.276  30.667  19.846  1.00 59.02           C  
ANISOU 1667  CD1 LEU A 227     9086   5113   8225    137   -971    621       C  
ATOM   1668  CD2 LEU A 227      70.489  29.844  22.082  1.00 64.10           C  
ANISOU 1668  CD2 LEU A 227     9339   5942   9074    300   -809    395       C  
ATOM   1669  N   ARG A 228      75.237  26.926  21.507  1.00 48.57           N  
ANISOU 1669  N   ARG A 228     7521   4388   6546   -149   -254    366       N  
ATOM   1670  CA  ARG A 228      75.893  25.689  21.080  1.00 47.38           C  
ANISOU 1670  CA  ARG A 228     7365   4354   6284   -217   -153    354       C  
ATOM   1671  C   ARG A 228      75.695  24.542  22.089  1.00 48.37           C  
ANISOU 1671  C   ARG A 228     7318   4605   6454   -142   -102    271       C  
ATOM   1672  O   ARG A 228      75.163  23.492  21.721  1.00 47.92           O  
ANISOU 1672  O   ARG A 228     7245   4610   6354   -126   -121    279       O  
ATOM   1673  CB  ARG A 228      77.399  25.887  20.806  1.00 47.12           C  
ANISOU 1673  CB  ARG A 228     7388   4330   6185   -345    -14    343       C  
ATOM   1674  CG  ARG A 228      77.792  26.848  19.697  1.00 54.60           C  
ANISOU 1674  CG  ARG A 228     8535   5161   7051   -460    -26    427       C  
ATOM   1675  CD  ARG A 228      79.318  27.017  19.637  1.00 60.99           C  
ANISOU 1675  CD  ARG A 228     9354   5991   7827   -591    143    388       C  
ATOM   1676  NE  ARG A 228      79.886  27.444  20.924  1.00 63.24           N  
ANISOU 1676  NE  ARG A 228     9497   6296   8235   -557    187    307       N  
ATOM   1677  CZ  ARG A 228      81.176  27.398  21.250  1.00 73.81           C  
ANISOU 1677  CZ  ARG A 228    10764   7683   9599   -637    320    242       C  
ATOM   1678  NH1 ARG A 228      82.076  26.960  20.376  1.00 57.69           N  
ANISOU 1678  NH1 ARG A 228     8767   5673   7478   -756    447    241       N  
ATOM   1679  NH2 ARG A 228      81.576  27.791  22.451  1.00 63.02           N  
ANISOU 1679  NH2 ARG A 228     9277   6330   8338   -604    326    171       N  
ATOM   1680  N   LEU A 229      76.103  24.772  23.355  1.00 41.62           N  
ANISOU 1680  N   LEU A 229     6356   3780   5679   -106    -46    194       N  
ATOM   1681  CA  LEU A 229      76.031  23.824  24.457  1.00 39.83           C  
ANISOU 1681  CA  LEU A 229     5994   3656   5483    -48      1    119       C  
ATOM   1682  C   LEU A 229      74.640  23.204  24.622  1.00 42.51           C  
ANISOU 1682  C   LEU A 229     6275   4021   5857     36    -64    115       C  
ATOM   1683  O   LEU A 229      74.534  21.979  24.738  1.00 42.17           O  
ANISOU 1683  O   LEU A 229     6181   4065   5776     43    -30     96       O  
ATOM   1684  CB  LEU A 229      76.494  24.489  25.774  1.00 39.45           C  
ANISOU 1684  CB  LEU A 229     5881   3602   5506    -29     36     47       C  
ATOM   1685  CG  LEU A 229      76.881  23.517  26.909  1.00 44.44           C  
ANISOU 1685  CG  LEU A 229     6411   4339   6133     -7     94    -23       C  
ATOM   1686  CD1 LEU A 229      78.113  23.993  27.632  1.00 45.32           C  
ANISOU 1686  CD1 LEU A 229     6501   4458   6262    -56    138    -70       C  
ATOM   1687  CD2 LEU A 229      75.720  23.261  27.866  1.00 43.94           C  
ANISOU 1687  CD2 LEU A 229     6285   4294   6116     76     72    -70       C  
ATOM   1688  N   VAL A 230      73.589  24.045  24.667  1.00 37.87           N  
ANISOU 1688  N   VAL A 230     5683   3349   5356    100   -156    125       N  
ATOM   1689  CA  VAL A 230      72.203  23.618  24.883  1.00 37.14           C  
ANISOU 1689  CA  VAL A 230     5505   3269   5336    181   -216    106       C  
ATOM   1690  C   VAL A 230      71.660  22.856  23.687  1.00 39.44           C  
ANISOU 1690  C   VAL A 230     5844   3578   5566    159   -291    173       C  
ATOM   1691  O   VAL A 230      71.034  21.803  23.868  1.00 38.25           O  
ANISOU 1691  O   VAL A 230     5617   3501   5415    180   -282    146       O  
ATOM   1692  CB  VAL A 230      71.264  24.753  25.322  1.00 40.77           C  
ANISOU 1692  CB  VAL A 230     5920   3628   5944    266   -286     79       C  
ATOM   1693  CG1 VAL A 230      70.084  24.188  26.109  1.00 40.35           C  
ANISOU 1693  CG1 VAL A 230     5723   3621   5986    342   -273      5       C  
ATOM   1694  CG2 VAL A 230      72.019  25.773  26.163  1.00 41.24           C  
ANISOU 1694  CG2 VAL A 230     5996   3638   6037    258   -226     31       C  
ATOM   1695  N   VAL A 231      71.924  23.362  22.470  1.00 34.56           N  
ANISOU 1695  N   VAL A 231     5366   2887   4880    103   -362    259       N  
ATOM   1696  CA  VAL A 231      71.486  22.682  21.254  1.00 34.39           C  
ANISOU 1696  CA  VAL A 231     5425   2872   4769     62   -442    324       C  
ATOM   1697  C   VAL A 231      72.123  21.291  21.190  1.00 37.87           C  
ANISOU 1697  C   VAL A 231     5855   3429   5104      5   -325    294       C  
ATOM   1698  O   VAL A 231      71.391  20.323  21.010  1.00 37.94           O  
ANISOU 1698  O   VAL A 231     5822   3489   5104     20   -358    286       O  
ATOM   1699  CB  VAL A 231      71.721  23.521  19.980  1.00 37.50           C  
ANISOU 1699  CB  VAL A 231     6011   3158   5078     -9   -532    426       C  
ATOM   1700  CG1 VAL A 231      71.470  22.706  18.715  1.00 36.80           C  
ANISOU 1700  CG1 VAL A 231     6041   3090   4851    -82   -590    486       C  
ATOM   1701  CG2 VAL A 231      70.819  24.743  19.995  1.00 37.53           C  
ANISOU 1701  CG2 VAL A 231     6019   3031   5210     70   -691    464       C  
ATOM   1702  N   LEU A 232      73.454  21.198  21.448  1.00 33.12           N  
ANISOU 1702  N   LEU A 232     5272   2865   4448    -51   -191    266       N  
ATOM   1703  CA  LEU A 232      74.204  19.961  21.417  1.00 32.73           C  
ANISOU 1703  CA  LEU A 232     5206   2906   4324    -95    -79    231       C  
ATOM   1704  C   LEU A 232      73.727  18.979  22.488  1.00 34.10           C  
ANISOU 1704  C   LEU A 232     5244   3160   4555    -27    -51    169       C  
ATOM   1705  O   LEU A 232      73.503  17.826  22.156  1.00 32.28           O  
ANISOU 1705  O   LEU A 232     5012   2979   4275    -41    -35    163       O  
ATOM   1706  CB  LEU A 232      75.729  20.199  21.461  1.00 33.31           C  
ANISOU 1706  CB  LEU A 232     5304   2988   4365   -163     45    209       C  
ATOM   1707  CG  LEU A 232      76.638  18.949  21.196  1.00 38.11           C  
ANISOU 1707  CG  LEU A 232     5899   3670   4912   -210    164    170       C  
ATOM   1708  CD1 LEU A 232      76.383  18.305  19.821  1.00 36.90           C  
ANISOU 1708  CD1 LEU A 232     5871   3510   4638   -280    161    208       C  
ATOM   1709  CD2 LEU A 232      78.111  19.280  21.361  1.00 40.64           C  
ANISOU 1709  CD2 LEU A 232     6197   3997   5250   -265    279    133       C  
ATOM   1710  N   ALA A 233      73.494  19.447  23.726  1.00 29.18           N  
ANISOU 1710  N   ALA A 233     4523   2537   4025     37    -45    122       N  
ATOM   1711  CA  ALA A 233      72.978  18.630  24.821  1.00 27.69           C  
ANISOU 1711  CA  ALA A 233     4230   2413   3878     87    -12     65       C  
ATOM   1712  C   ALA A 233      71.579  18.117  24.481  1.00 33.29           C  
ANISOU 1712  C   ALA A 233     4904   3127   4617    115    -84     74       C  
ATOM   1713  O   ALA A 233      71.336  16.922  24.652  1.00 35.24           O  
ANISOU 1713  O   ALA A 233     5121   3435   4835    108    -50     54       O  
ATOM   1714  CB  ALA A 233      72.961  19.423  26.121  1.00 28.14           C  
ANISOU 1714  CB  ALA A 233     4222   2455   4013    132     11     11       C  
ATOM   1715  N   VAL A 234      70.668  18.978  23.963  1.00 29.31           N  
ANISOU 1715  N   VAL A 234     4404   2553   4178    146   -193    105       N  
ATOM   1716  CA  VAL A 234      69.330  18.513  23.540  1.00 29.00           C  
ANISOU 1716  CA  VAL A 234     4315   2515   4189    170   -285    113       C  
ATOM   1717  C   VAL A 234      69.447  17.418  22.434  1.00 32.69           C  
ANISOU 1717  C   VAL A 234     4868   3017   4535    100   -306    155       C  
ATOM   1718  O   VAL A 234      68.794  16.389  22.525  1.00 31.80           O  
ANISOU 1718  O   VAL A 234     4701   2954   4426     96   -303    131       O  
ATOM   1719  CB  VAL A 234      68.354  19.657  23.153  1.00 31.54           C  
ANISOU 1719  CB  VAL A 234     4617   2741   4627    226   -427    141       C  
ATOM   1720  CG1 VAL A 234      67.094  19.118  22.480  1.00 31.00           C  
ANISOU 1720  CG1 VAL A 234     4503   2670   4605    237   -553    160       C  
ATOM   1721  CG2 VAL A 234      67.968  20.469  24.372  1.00 31.03           C  
ANISOU 1721  CG2 VAL A 234     4437   2647   4705    302   -385     68       C  
ATOM   1722  N   VAL A 235      70.320  17.629  21.440  1.00 29.63           N  
ANISOU 1722  N   VAL A 235     4621   2601   4036     35   -307    210       N  
ATOM   1723  CA  VAL A 235      70.557  16.699  20.326  1.00 28.70           C  
ANISOU 1723  CA  VAL A 235     4612   2505   3787    -44   -306    239       C  
ATOM   1724  C   VAL A 235      71.162  15.378  20.811  1.00 31.65           C  
ANISOU 1724  C   VAL A 235     4947   2959   4120    -61   -174    184       C  
ATOM   1725  O   VAL A 235      70.558  14.336  20.583  1.00 32.39           O  
ANISOU 1725  O   VAL A 235     5031   3085   4191    -76   -191    171       O  
ATOM   1726  CB  VAL A 235      71.386  17.376  19.194  1.00 31.37           C  
ANISOU 1726  CB  VAL A 235     5122   2785   4011   -123   -312    300       C  
ATOM   1727  CG1 VAL A 235      71.842  16.359  18.142  1.00 30.34           C  
ANISOU 1727  CG1 VAL A 235     5114   2682   3730   -218   -259    306       C  
ATOM   1728  CG2 VAL A 235      70.598  18.532  18.551  1.00 30.31           C  
ANISOU 1728  CG2 VAL A 235     5058   2553   3904   -111   -486    374       C  
ATOM   1729  N   ILE A 236      72.327  15.421  21.496  1.00 27.51           N  
ANISOU 1729  N   ILE A 236     4398   2457   3596    -57    -56    150       N  
ATOM   1730  CA  ILE A 236      73.007  14.240  22.034  1.00 27.16           C  
ANISOU 1730  CA  ILE A 236     4317   2471   3533    -60     51    103       C  
ATOM   1731  C   ILE A 236      72.042  13.394  22.896  1.00 31.22           C  
ANISOU 1731  C   ILE A 236     4739   3024   4099    -18     38     71       C  
ATOM   1732  O   ILE A 236      71.898  12.213  22.615  1.00 30.38           O  
ANISOU 1732  O   ILE A 236     4651   2941   3949    -43     60     59       O  
ATOM   1733  CB  ILE A 236      74.354  14.574  22.765  1.00 29.42           C  
ANISOU 1733  CB  ILE A 236     4569   2766   3843    -51    143     73       C  
ATOM   1734  CG1 ILE A 236      75.422  15.019  21.744  1.00 29.29           C  
ANISOU 1734  CG1 ILE A 236     4644   2721   3766   -122    196     90       C  
ATOM   1735  CG2 ILE A 236      74.863  13.356  23.600  1.00 29.64           C  
ANISOU 1735  CG2 ILE A 236     4537   2842   3883    -27    213     27       C  
ATOM   1736  CD1 ILE A 236      76.821  15.353  22.313  1.00 36.53           C  
ANISOU 1736  CD1 ILE A 236     5511   3644   4723   -128    285     53       C  
ATOM   1737  N   PHE A 237      71.351  14.005  23.895  1.00 27.65           N  
ANISOU 1737  N   PHE A 237     4199   2571   3737     36     13     51       N  
ATOM   1738  CA  PHE A 237      70.437  13.254  24.763  1.00 27.11           C  
ANISOU 1738  CA  PHE A 237     4048   2537   3714     58     28     13       C  
ATOM   1739  C   PHE A 237      69.200  12.754  24.021  1.00 30.79           C  
ANISOU 1739  C   PHE A 237     4500   3003   4196     38    -49     23       C  
ATOM   1740  O   PHE A 237      68.842  11.589  24.208  1.00 29.26           O  
ANISOU 1740  O   PHE A 237     4289   2841   3985     14    -16      1       O  
ATOM   1741  CB  PHE A 237      70.084  14.013  26.057  1.00 28.35           C  
ANISOU 1741  CB  PHE A 237     4123   2693   3955    106     52    -29       C  
ATOM   1742  CG  PHE A 237      71.266  14.040  27.000  1.00 29.04           C  
ANISOU 1742  CG  PHE A 237     4228   2798   4010    110    126    -49       C  
ATOM   1743  CD1 PHE A 237      71.684  12.885  27.652  1.00 31.74           C  
ANISOU 1743  CD1 PHE A 237     4581   3176   4304     95    183    -65       C  
ATOM   1744  CD2 PHE A 237      72.009  15.197  27.175  1.00 30.58           C  
ANISOU 1744  CD2 PHE A 237     4436   2962   4222    123    124    -49       C  
ATOM   1745  CE1 PHE A 237      72.805  12.898  28.492  1.00 32.02           C  
ANISOU 1745  CE1 PHE A 237     4632   3218   4315    102    218    -77       C  
ATOM   1746  CE2 PHE A 237      73.147  15.200  27.989  1.00 33.56           C  
ANISOU 1746  CE2 PHE A 237     4823   3354   4575    120    171    -68       C  
ATOM   1747  CZ  PHE A 237      73.549  14.044  28.626  1.00 31.19           C  
ANISOU 1747  CZ  PHE A 237     4527   3092   4232    112    209    -81       C  
ATOM   1748  N   SER A 238      68.601  13.585  23.132  1.00 28.19           N  
ANISOU 1748  N   SER A 238     4187   2629   3895     42   -164     61       N  
ATOM   1749  CA  SER A 238      67.442  13.167  22.326  1.00 27.95           C  
ANISOU 1749  CA  SER A 238     4143   2593   3885     19   -272     75       C  
ATOM   1750  C   SER A 238      67.778  11.934  21.495  1.00 32.41           C  
ANISOU 1750  C   SER A 238     4807   3180   4327    -53   -253     86       C  
ATOM   1751  O   SER A 238      67.042  10.961  21.520  1.00 31.88           O  
ANISOU 1751  O   SER A 238     4701   3140   4272    -79   -260     61       O  
ATOM   1752  CB  SER A 238      66.989  14.278  21.385  1.00 30.47           C  
ANISOU 1752  CB  SER A 238     4499   2844   4233     33   -426    130       C  
ATOM   1753  OG  SER A 238      66.278  15.310  22.048  1.00 36.34           O  
ANISOU 1753  OG  SER A 238     5127   3551   5129    109   -470    109       O  
ATOM   1754  N   VAL A 239      68.916  11.956  20.814  1.00 29.28           N  
ANISOU 1754  N   VAL A 239     4536   2770   3819    -92   -211    113       N  
ATOM   1755  CA  VAL A 239      69.348  10.883  19.925  1.00 29.18           C  
ANISOU 1755  CA  VAL A 239     4632   2766   3687   -163   -174    111       C  
ATOM   1756  C   VAL A 239      69.863   9.645  20.669  1.00 32.91           C  
ANISOU 1756  C   VAL A 239     5072   3276   4156   -159    -49     61       C  
ATOM   1757  O   VAL A 239      69.544   8.527  20.259  1.00 31.42           O  
ANISOU 1757  O   VAL A 239     4920   3094   3925   -203    -44     43       O  
ATOM   1758  CB  VAL A 239      70.362  11.461  18.907  1.00 33.42           C  
ANISOU 1758  CB  VAL A 239     5315   3269   4115   -215   -153    145       C  
ATOM   1759  CG1 VAL A 239      71.152  10.388  18.208  1.00 33.87           C  
ANISOU 1759  CG1 VAL A 239     5481   3332   4055   -287    -68    120       C  
ATOM   1760  CG2 VAL A 239      69.636  12.316  17.892  1.00 33.35           C  
ANISOU 1760  CG2 VAL A 239     5383   3207   4081   -240   -310    209       C  
ATOM   1761  N   LEU A 240      70.650   9.827  21.743  1.00 30.49           N  
ANISOU 1761  N   LEU A 240     4708   2983   3893   -110     37     40       N  
ATOM   1762  CA  LEU A 240      71.217   8.689  22.474  1.00 30.17           C  
ANISOU 1762  CA  LEU A 240     4653   2962   3850   -100    131      5       C  
ATOM   1763  C   LEU A 240      70.252   7.987  23.461  1.00 34.48           C  
ANISOU 1763  C   LEU A 240     5125   3528   4446    -90    132    -17       C  
ATOM   1764  O   LEU A 240      70.331   6.770  23.616  1.00 34.79           O  
ANISOU 1764  O   LEU A 240     5192   3567   4461   -110    176    -34       O  
ATOM   1765  CB  LEU A 240      72.519   9.101  23.203  1.00 29.76           C  
ANISOU 1765  CB  LEU A 240     4579   2910   3818    -60    201     -5       C  
ATOM   1766  CG  LEU A 240      73.712   9.569  22.344  1.00 33.81           C  
ANISOU 1766  CG  LEU A 240     5153   3403   4291    -85    246     -1       C  
ATOM   1767  CD1 LEU A 240      74.977   9.559  23.147  1.00 34.84           C  
ANISOU 1767  CD1 LEU A 240     5234   3538   4466    -48    314    -27       C  
ATOM   1768  CD2 LEU A 240      73.913   8.717  21.110  1.00 33.53           C  
ANISOU 1768  CD2 LEU A 240     5212   3351   4175   -145    282    -13       C  
ATOM   1769  N   PHE A 241      69.378   8.742  24.139  1.00 30.61           N  
ANISOU 1769  N   PHE A 241     4549   3051   4032    -62     96    -22       N  
ATOM   1770  CA  PHE A 241      68.490   8.208  25.177  1.00 29.33           C  
ANISOU 1770  CA  PHE A 241     4315   2909   3919    -65    128    -53       C  
ATOM   1771  C   PHE A 241      67.121   7.729  24.689  1.00 31.64           C  
ANISOU 1771  C   PHE A 241     4562   3208   4252   -108     73    -66       C  
ATOM   1772  O   PHE A 241      66.556   6.851  25.328  1.00 30.42           O  
ANISOU 1772  O   PHE A 241     4380   3067   4112   -141    124    -94       O  
ATOM   1773  CB  PHE A 241      68.313   9.248  26.307  1.00 30.62           C  
ANISOU 1773  CB  PHE A 241     4403   3081   4151    -20    152    -75       C  
ATOM   1774  CG  PHE A 241      69.432   9.395  27.318  1.00 31.37           C  
ANISOU 1774  CG  PHE A 241     4529   3178   4212      7    216    -79       C  
ATOM   1775  CD1 PHE A 241      70.726   8.944  27.031  1.00 33.96           C  
ANISOU 1775  CD1 PHE A 241     4927   3496   4480     10    232    -58       C  
ATOM   1776  CD2 PHE A 241      69.189   9.956  28.569  1.00 31.97           C  
ANISOU 1776  CD2 PHE A 241     4563   3264   4322     25    258   -112       C  
ATOM   1777  CE1 PHE A 241      71.765   9.099  27.959  1.00 34.36           C  
ANISOU 1777  CE1 PHE A 241     4991   3546   4519     37    263    -63       C  
ATOM   1778  CE2 PHE A 241      70.220  10.081  29.510  1.00 34.56           C  
ANISOU 1778  CE2 PHE A 241     4932   3592   4608     41    292   -114       C  
ATOM   1779  CZ  PHE A 241      71.501   9.653  29.198  1.00 32.96           C  
ANISOU 1779  CZ  PHE A 241     4787   3379   4359     49    282    -86       C  
ATOM   1780  N   THR A 242      66.578   8.309  23.585  1.00 28.33           N  
ANISOU 1780  N   THR A 242     4138   2773   3851   -116    -39    -44       N  
ATOM   1781  CA  THR A 242      65.254   7.959  23.051  1.00 27.44           C  
ANISOU 1781  CA  THR A 242     3966   2664   3796   -155   -126    -57       C  
ATOM   1782  C   THR A 242      65.161   6.466  22.648  1.00 30.22           C  
ANISOU 1782  C   THR A 242     4384   3020   4077   -231   -100    -69       C  
ATOM   1783  O   THR A 242      64.251   5.807  23.155  1.00 29.67           O  
ANISOU 1783  O   THR A 242     4238   2968   4069   -267    -77   -106       O  
ATOM   1784  CB  THR A 242      64.826   8.935  21.931  1.00 31.13           C  
ANISOU 1784  CB  THR A 242     4441   3101   4287   -144   -282    -17       C  
ATOM   1785  OG1 THR A 242      64.694  10.231  22.503  1.00 31.81           O  
ANISOU 1785  OG1 THR A 242     4443   3169   4472    -70   -299    -18       O  
ATOM   1786  CG2 THR A 242      63.507   8.556  21.258  1.00 24.97           C  
ANISOU 1786  CG2 THR A 242     3600   2319   3569   -188   -409    -27       C  
ATOM   1787  N   PRO A 243      66.038   5.883  21.785  1.00 26.88           N  
ANISOU 1787  N   PRO A 243     4099   2579   3535   -263    -89    -50       N  
ATOM   1788  CA  PRO A 243      65.861   4.444  21.436  1.00 26.00           C  
ANISOU 1788  CA  PRO A 243     4051   2458   3369   -335    -62    -73       C  
ATOM   1789  C   PRO A 243      65.979   3.526  22.648  1.00 27.15           C  
ANISOU 1789  C   PRO A 243     4174   2606   3534   -335     53   -100       C  
ATOM   1790  O   PRO A 243      65.135   2.652  22.835  1.00 25.65           O  
ANISOU 1790  O   PRO A 243     3959   2416   3369   -395     61   -125       O  
ATOM   1791  CB  PRO A 243      66.940   4.191  20.365  1.00 27.63           C  
ANISOU 1791  CB  PRO A 243     4409   2636   3453   -356    -46    -61       C  
ATOM   1792  CG  PRO A 243      67.325   5.565  19.867  1.00 31.43           C  
ANISOU 1792  CG  PRO A 243     4907   3114   3920   -322   -102    -22       C  
ATOM   1793  CD  PRO A 243      67.196   6.457  21.065  1.00 27.47           C  
ANISOU 1793  CD  PRO A 243     4280   2633   3525   -248    -85    -18       C  
ATOM   1794  N   TYR A 244      66.958   3.794  23.526  1.00 24.04           N  
ANISOU 1794  N   TYR A 244     3789   2212   3133   -276    133    -91       N  
ATOM   1795  CA  TYR A 244      67.124   3.033  24.755  1.00 24.39           C  
ANISOU 1795  CA  TYR A 244     3836   2249   3182   -276    222   -102       C  
ATOM   1796  C   TYR A 244      65.852   3.080  25.646  1.00 29.04           C  
ANISOU 1796  C   TYR A 244     4323   2864   3845   -310    243   -129       C  
ATOM   1797  O   TYR A 244      65.362   2.022  26.022  1.00 29.43           O  
ANISOU 1797  O   TYR A 244     4393   2900   3888   -372    289   -145       O  
ATOM   1798  CB  TYR A 244      68.408   3.444  25.504  1.00 24.89           C  
ANISOU 1798  CB  TYR A 244     3927   2305   3226   -206    271    -85       C  
ATOM   1799  CG  TYR A 244      68.417   3.044  26.960  1.00 26.42           C  
ANISOU 1799  CG  TYR A 244     4120   2495   3422   -204    332    -87       C  
ATOM   1800  CD1 TYR A 244      68.755   1.750  27.348  1.00 29.02           C  
ANISOU 1800  CD1 TYR A 244     4535   2780   3713   -228    370    -80       C  
ATOM   1801  CD2 TYR A 244      68.033   3.944  27.952  1.00 27.21           C  
ANISOU 1801  CD2 TYR A 244     4154   2626   3558   -187    352    -97       C  
ATOM   1802  CE1 TYR A 244      68.700   1.357  28.693  1.00 30.99           C  
ANISOU 1802  CE1 TYR A 244     4817   3015   3942   -243    416    -71       C  
ATOM   1803  CE2 TYR A 244      67.955   3.560  29.292  1.00 28.36           C  
ANISOU 1803  CE2 TYR A 244     4329   2767   3681   -208    415   -102       C  
ATOM   1804  CZ  TYR A 244      68.299   2.268  29.660  1.00 37.80           C  
ANISOU 1804  CZ  TYR A 244     5625   3918   4820   -239    441    -82       C  
ATOM   1805  OH  TYR A 244      68.263   1.924  30.990  1.00 41.25           O  
ANISOU 1805  OH  TYR A 244     6122   4340   5211   -270    492    -74       O  
ATOM   1806  N   HIS A 245      65.296   4.286  25.911  1.00 25.58           N  
ANISOU 1806  N   HIS A 245     3778   2456   3485   -275    215   -140       N  
ATOM   1807  CA  HIS A 245      64.100   4.479  26.745  1.00 24.54           C  
ANISOU 1807  CA  HIS A 245     3526   2349   3448   -302    256   -185       C  
ATOM   1808  C   HIS A 245      62.816   3.914  26.138  1.00 31.09           C  
ANISOU 1808  C   HIS A 245     4279   3186   4349   -374    208   -216       C  
ATOM   1809  O   HIS A 245      61.996   3.391  26.890  1.00 31.74           O  
ANISOU 1809  O   HIS A 245     4299   3279   4480   -436    288   -258       O  
ATOM   1810  CB  HIS A 245      63.926   5.939  27.169  1.00 23.72           C  
ANISOU 1810  CB  HIS A 245     3326   2261   3427   -234    244   -201       C  
ATOM   1811  CG  HIS A 245      64.840   6.299  28.302  1.00 26.04           C  
ANISOU 1811  CG  HIS A 245     3673   2555   3668   -197    328   -197       C  
ATOM   1812  ND1 HIS A 245      66.091   6.836  28.078  1.00 27.07           N  
ANISOU 1812  ND1 HIS A 245     3876   2672   3739   -140    297   -158       N  
ATOM   1813  CD2 HIS A 245      64.668   6.139  29.636  1.00 27.30           C  
ANISOU 1813  CD2 HIS A 245     3833   2722   3816   -223    438   -231       C  
ATOM   1814  CE1 HIS A 245      66.636   6.990  29.272  1.00 26.20           C  
ANISOU 1814  CE1 HIS A 245     3798   2564   3594   -126    369   -167       C  
ATOM   1815  NE2 HIS A 245      65.821   6.578  30.241  1.00 26.47           N  
ANISOU 1815  NE2 HIS A 245     3805   2609   3641   -177    453   -207       N  
ATOM   1816  N   ILE A 246      62.645   3.958  24.808  1.00 28.37           N  
ANISOU 1816  N   ILE A 246     3948   2832   4000   -382     83   -196       N  
ATOM   1817  CA  ILE A 246      61.486   3.333  24.161  1.00 27.96           C  
ANISOU 1817  CA  ILE A 246     3833   2784   4008   -461     13   -225       C  
ATOM   1818  C   ILE A 246      61.609   1.791  24.341  1.00 34.80           C  
ANISOU 1818  C   ILE A 246     4798   3629   4795   -548     95   -235       C  
ATOM   1819  O   ILE A 246      60.670   1.131  24.789  1.00 36.69           O  
ANISOU 1819  O   ILE A 246     4967   3876   5099   -627    141   -277       O  
ATOM   1820  CB  ILE A 246      61.409   3.706  22.641  1.00 30.34           C  
ANISOU 1820  CB  ILE A 246     4172   3071   4286   -459   -161   -192       C  
ATOM   1821  CG1 ILE A 246      61.039   5.205  22.414  1.00 29.81           C  
ANISOU 1821  CG1 ILE A 246     4000   3005   4321   -381   -272   -178       C  
ATOM   1822  CG2 ILE A 246      60.449   2.754  21.870  1.00 29.30           C  
ANISOU 1822  CG2 ILE A 246     4026   2935   4172   -561   -243   -219       C  
ATOM   1823  CD1 ILE A 246      61.207   5.681  20.930  1.00 25.32           C  
ANISOU 1823  CD1 ILE A 246     3525   2408   3687   -381   -450   -124       C  
ATOM   1824  N   MET A 247      62.778   1.236  24.015  1.00 30.28           N  
ANISOU 1824  N   MET A 247     4384   3023   4097   -534    120   -201       N  
ATOM   1825  CA  MET A 247      63.009  -0.203  24.037  1.00 29.30           C  
ANISOU 1825  CA  MET A 247     4372   2856   3904   -601    180   -207       C  
ATOM   1826  C   MET A 247      62.988  -0.795  25.409  1.00 32.83           C  
ANISOU 1826  C   MET A 247     4832   3290   4353   -626    305   -213       C  
ATOM   1827  O   MET A 247      62.575  -1.961  25.553  1.00 32.80           O  
ANISOU 1827  O   MET A 247     4879   3251   4334   -712    348   -228       O  
ATOM   1828  CB  MET A 247      64.292  -0.575  23.278  1.00 31.58           C  
ANISOU 1828  CB  MET A 247     4813   3103   4084   -568    176   -182       C  
ATOM   1829  CG  MET A 247      64.177  -0.322  21.784  1.00 35.57           C  
ANISOU 1829  CG  MET A 247     5356   3609   4551   -592     64   -183       C  
ATOM   1830  SD  MET A 247      62.854  -1.350  21.101  1.00 42.10           S  
ANISOU 1830  SD  MET A 247     6178   4423   5395   -723     -5   -224       S  
ATOM   1831  CE  MET A 247      61.766  -0.202  20.640  1.00 38.82           C  
ANISOU 1831  CE  MET A 247     5611   4059   5079   -722   -149   -223       C  
ATOM   1832  N   ARG A 248      63.400  -0.012  26.425  1.00 28.03           N  
ANISOU 1832  N   ARG A 248     4192   2703   3754   -562    360   -201       N  
ATOM   1833  CA  ARG A 248      63.395  -0.503  27.788  1.00 27.85           C  
ANISOU 1833  CA  ARG A 248     4209   2664   3707   -596    473   -202       C  
ATOM   1834  C   ARG A 248      61.966  -0.716  28.277  1.00 31.45           C  
ANISOU 1834  C   ARG A 248     4559   3145   4246   -697    534   -255       C  
ATOM   1835  O   ARG A 248      61.689  -1.742  28.870  1.00 32.17           O  
ANISOU 1835  O   ARG A 248     4718   3201   4302   -786    615   -259       O  
ATOM   1836  CB  ARG A 248      64.181   0.409  28.718  1.00 28.38           C  
ANISOU 1836  CB  ARG A 248     4285   2748   3751   -516    507   -182       C  
ATOM   1837  CG  ARG A 248      64.521  -0.310  30.023  1.00 33.05           C  
ANISOU 1837  CG  ARG A 248     4990   3301   4267   -554    598   -162       C  
ATOM   1838  CD  ARG A 248      63.986   0.465  31.187  1.00 41.18           C  
ANISOU 1838  CD  ARG A 248     5961   4370   5316   -571    681   -194       C  
ATOM   1839  NE  ARG A 248      64.954   1.449  31.638  1.00 36.02           N  
ANISOU 1839  NE  ARG A 248     5327   3728   4632   -478    656   -173       N  
ATOM   1840  CZ  ARG A 248      64.663   2.660  32.093  1.00 41.20           C  
ANISOU 1840  CZ  ARG A 248     5891   4426   5335   -447    682   -211       C  
ATOM   1841  NH1 ARG A 248      65.627   3.467  32.495  1.00 14.01           N  
ANISOU 1841  NH1 ARG A 248     2483    985   1856   -372    654   -191       N  
ATOM   1842  NH2 ARG A 248      63.404   3.068  32.160  1.00 34.98           N  
ANISOU 1842  NH2 ARG A 248     4970   3672   4647   -490    738   -277       N  
ATOM   1843  N   ASN A 249      61.058   0.197  27.930  1.00 26.92           N  
ANISOU 1843  N   ASN A 249     3816   2622   3791   -686    489   -297       N  
ATOM   1844  CA  ASN A 249      59.643   0.166  28.274  1.00 26.10           C  
ANISOU 1844  CA  ASN A 249     3559   2547   3812   -770    542   -366       C  
ATOM   1845  C   ASN A 249      58.894  -0.878  27.460  1.00 30.74           C  
ANISOU 1845  C   ASN A 249     4134   3118   4428   -873    493   -386       C  
ATOM   1846  O   ASN A 249      58.054  -1.587  28.021  1.00 31.33           O  
ANISOU 1846  O   ASN A 249     4170   3189   4546   -987    591   -430       O  
ATOM   1847  CB  ASN A 249      59.045   1.588  28.167  1.00 28.17           C  
ANISOU 1847  CB  ASN A 249     3633   2853   4217   -698    492   -406       C  
ATOM   1848  CG  ASN A 249      59.538   2.494  29.286  1.00 45.43           C  
ANISOU 1848  CG  ASN A 249     5825   5051   6384   -632    588   -413       C  
ATOM   1849  OD1 ASN A 249      59.273   2.266  30.467  1.00 36.14           O  
ANISOU 1849  OD1 ASN A 249     4659   3879   5194   -693    740   -450       O  
ATOM   1850  ND2 ASN A 249      60.274   3.534  28.960  1.00 35.32           N  
ANISOU 1850  ND2 ASN A 249     4557   3772   5091   -521    507   -378       N  
ATOM   1851  N   VAL A 250      59.252  -1.047  26.166  1.00 27.98           N  
ANISOU 1851  N   VAL A 250     3841   2751   4039   -849    353   -355       N  
ATOM   1852  CA  VAL A 250      58.688  -2.101  25.284  1.00 27.56           C  
ANISOU 1852  CA  VAL A 250     3814   2673   3985   -951    291   -373       C  
ATOM   1853  C   VAL A 250      59.157  -3.492  25.787  1.00 33.20           C  
ANISOU 1853  C   VAL A 250     4700   3322   4591  -1026    401   -357       C  
ATOM   1854  O   VAL A 250      58.353  -4.435  25.845  1.00 33.68           O  
ANISOU 1854  O   VAL A 250     4750   3362   4684  -1150    440   -393       O  
ATOM   1855  CB  VAL A 250      59.032  -1.888  23.774  1.00 29.77           C  
ANISOU 1855  CB  VAL A 250     4149   2945   4218   -916    121   -347       C  
ATOM   1856  CG1 VAL A 250      58.567  -3.066  22.938  1.00 28.77           C  
ANISOU 1856  CG1 VAL A 250     4085   2782   4062  -1032     67   -372       C  
ATOM   1857  CG2 VAL A 250      58.441  -0.584  23.240  1.00 28.85           C  
ANISOU 1857  CG2 VAL A 250     3877   2873   4211   -854    -14   -353       C  
ATOM   1858  N   ARG A 251      60.451  -3.602  26.178  1.00 28.67           N  
ANISOU 1858  N   ARG A 251     4279   2710   3904   -950    444   -303       N  
ATOM   1859  CA  ARG A 251      61.008  -4.845  26.707  1.00 28.07           C  
ANISOU 1859  CA  ARG A 251     4374   2554   3736   -995    525   -277       C  
ATOM   1860  C   ARG A 251      60.270  -5.325  27.940  1.00 35.64           C  
ANISOU 1860  C   ARG A 251     5325   3504   4714  -1099    655   -294       C  
ATOM   1861  O   ARG A 251      59.924  -6.510  28.009  1.00 36.85           O  
ANISOU 1861  O   ARG A 251     5563   3594   4843  -1209    700   -300       O  
ATOM   1862  CB  ARG A 251      62.518  -4.719  26.970  1.00 25.35           C  
ANISOU 1862  CB  ARG A 251     4159   2171   3300   -878    528   -220       C  
ATOM   1863  CG  ARG A 251      63.153  -5.858  27.762  1.00 24.13           C  
ANISOU 1863  CG  ARG A 251     4175   1924   3071   -900    597   -183       C  
ATOM   1864  CD  ARG A 251      63.226  -7.195  27.062  1.00 28.79           C  
ANISOU 1864  CD  ARG A 251     4885   2424   3632   -959    584   -190       C  
ATOM   1865  NE  ARG A 251      64.009  -8.125  27.865  1.00 31.00           N  
ANISOU 1865  NE  ARG A 251     5330   2598   3850   -948    628   -142       N  
ATOM   1866  CZ  ARG A 251      63.618  -9.346  28.228  1.00 50.01           C  
ANISOU 1866  CZ  ARG A 251     7851   4916   6236  -1053    677   -136       C  
ATOM   1867  NH1 ARG A 251      62.456  -9.832  27.809  1.00 37.99           N  
ANISOU 1867  NH1 ARG A 251     6283   3402   4750  -1186    697   -184       N  
ATOM   1868  NH2 ARG A 251      64.398 -10.098  28.988  1.00 35.43           N  
ANISOU 1868  NH2 ARG A 251     6165   2961   4335  -1027    693    -80       N  
ATOM   1869  N   ILE A 252      60.044  -4.418  28.919  1.00 32.32           N  
ANISOU 1869  N   ILE A 252     4815   3137   4329  -1075    727   -306       N  
ATOM   1870  CA  ILE A 252      59.359  -4.750  30.166  1.00 31.05           C  
ANISOU 1870  CA  ILE A 252     4657   2971   4169  -1186    878   -331       C  
ATOM   1871  C   ILE A 252      57.890  -5.125  29.887  1.00 35.98           C  
ANISOU 1871  C   ILE A 252     5134   3621   4917  -1323    914   -408       C  
ATOM   1872  O   ILE A 252      57.424  -6.138  30.409  1.00 36.33           O  
ANISOU 1872  O   ILE A 252     5252   3618   4934  -1461   1018   -418       O  
ATOM   1873  CB  ILE A 252      59.552  -3.651  31.247  1.00 32.63           C  
ANISOU 1873  CB  ILE A 252     4818   3218   4362  -1129    954   -337       C  
ATOM   1874  CG1 ILE A 252      61.057  -3.444  31.541  1.00 30.33           C  
ANISOU 1874  CG1 ILE A 252     4681   2892   3949  -1009    903   -259       C  
ATOM   1875  CG2 ILE A 252      58.767  -4.003  32.543  1.00 33.16           C  
ANISOU 1875  CG2 ILE A 252     4905   3280   4414  -1269   1137   -375       C  
ATOM   1876  CD1 ILE A 252      61.369  -2.118  32.265  1.00 28.15           C  
ANISOU 1876  CD1 ILE A 252     4348   2671   3679   -926    928   -269       C  
ATOM   1877  N   ALA A 253      57.206  -4.359  29.014  1.00 33.47           N  
ANISOU 1877  N   ALA A 253     4615   3367   4736  -1289    815   -457       N  
ATOM   1878  CA  ALA A 253      55.822  -4.600  28.583  1.00 33.71           C  
ANISOU 1878  CA  ALA A 253     4465   3426   4918  -1403    805   -536       C  
ATOM   1879  C   ALA A 253      55.684  -5.965  27.895  1.00 39.04           C  
ANISOU 1879  C   ALA A 253     5249   4038   5546  -1514    765   -529       C  
ATOM   1880  O   ALA A 253      54.697  -6.657  28.141  1.00 40.07           O  
ANISOU 1880  O   ALA A 253     5317   4160   5748  -1665    845   -584       O  
ATOM   1881  CB  ALA A 253      55.360  -3.496  27.638  1.00 34.34           C  
ANISOU 1881  CB  ALA A 253     4344   3566   5138  -1314    646   -567       C  
ATOM   1882  N   SER A 254      56.686  -6.369  27.071  1.00 34.14           N  
ANISOU 1882  N   SER A 254     4797   3367   4808  -1448    658   -470       N  
ATOM   1883  CA  SER A 254      56.701  -7.668  26.378  1.00 33.26           C  
ANISOU 1883  CA  SER A 254     4818   3179   4639  -1541    622   -467       C  
ATOM   1884  C   SER A 254      56.816  -8.889  27.334  1.00 38.72           C  
ANISOU 1884  C   SER A 254     5679   3782   5251  -1649    769   -446       C  
ATOM   1885  O   SER A 254      56.509 -10.012  26.926  1.00 39.15           O  
ANISOU 1885  O   SER A 254     5815   3769   5292  -1763    767   -463       O  
ATOM   1886  CB  SER A 254      57.769  -7.708  25.289  1.00 33.55           C  
ANISOU 1886  CB  SER A 254     4988   3182   4577  -1439    498   -426       C  
ATOM   1887  OG  SER A 254      59.065  -7.857  25.838  1.00 36.90           O  
ANISOU 1887  OG  SER A 254     5582   3552   4888  -1346    555   -363       O  
ATOM   1888  N   ARG A 255      57.204  -8.658  28.606  1.00 35.72           N  
ANISOU 1888  N   ARG A 255     5362   3396   4815  -1624    891   -410       N  
ATOM   1889  CA  ARG A 255      57.332  -9.694  29.630  1.00 36.03           C  
ANISOU 1889  CA  ARG A 255     5585   3343   4762  -1727   1022   -375       C  
ATOM   1890  C   ARG A 255      56.013  -9.938  30.365  1.00 43.96           C  
ANISOU 1890  C   ARG A 255     6489   4371   5843  -1909   1171   -439       C  
ATOM   1891  O   ARG A 255      55.926 -10.878  31.147  1.00 44.81           O  
ANISOU 1891  O   ARG A 255     6756   4397   5874  -2032   1288   -415       O  
ATOM   1892  CB  ARG A 255      58.437  -9.344  30.627  1.00 33.93           C  
ANISOU 1892  CB  ARG A 255     5460   3051   4380  -1623   1061   -300       C  
ATOM   1893  CG  ARG A 255      59.834  -9.398  30.053  1.00 40.74           C  
ANISOU 1893  CG  ARG A 255     6452   3860   5167  -1470    943   -236       C  
ATOM   1894  CD  ARG A 255      60.856  -9.705  31.123  1.00 46.66           C  
ANISOU 1894  CD  ARG A 255     7397   4532   5799  -1422    977   -155       C  
ATOM   1895  NE  ARG A 255      61.015  -8.596  32.058  1.00 51.96           N  
ANISOU 1895  NE  ARG A 255     8010   5280   6454  -1367   1020   -148       N  
ATOM   1896  CZ  ARG A 255      60.701  -8.647  33.349  1.00 66.32           C  
ANISOU 1896  CZ  ARG A 255     9902   7089   8207  -1457   1140   -135       C  
ATOM   1897  NH1 ARG A 255      60.234  -9.768  33.882  1.00 45.82           N  
ANISOU 1897  NH1 ARG A 255     7448   4406   5553  -1610   1228   -118       N  
ATOM   1898  NH2 ARG A 255      60.861  -7.577  34.119  1.00 59.25           N  
ANISOU 1898  NH2 ARG A 255     8955   6265   7294  -1406   1177   -142       N  
ATOM   1899  N   LEU A 256      54.988  -9.111  30.105  1.00 43.10           N  
ANISOU 1899  N   LEU A 256     6117   4365   5895  -1929   1168   -524       N  
ATOM   1900  CA  LEU A 256      53.660  -9.233  30.709  1.00 44.32           C  
ANISOU 1900  CA  LEU A 256     6119   4553   6166  -2099   1319   -611       C  
ATOM   1901  C   LEU A 256      52.904 -10.425  30.161  1.00 55.09           C  
ANISOU 1901  C   LEU A 256     7490   5865   7579  -2269   1314   -649       C  
ATOM   1902  O   LEU A 256      53.057 -10.739  28.981  1.00 56.05           O  
ANISOU 1902  O   LEU A 256     7620   5967   7709  -2235   1149   -642       O  
ATOM   1903  CB  LEU A 256      52.840  -7.959  30.451  1.00 43.88           C  
ANISOU 1903  CB  LEU A 256     5751   4614   6306  -2041   1287   -698       C  
ATOM   1904  CG  LEU A 256      53.259  -6.728  31.247  1.00 47.59           C  
ANISOU 1904  CG  LEU A 256     6180   5138   6765  -1918   1349   -694       C  
ATOM   1905  CD1 LEU A 256      52.694  -5.487  30.639  1.00 47.62           C  
ANISOU 1905  CD1 LEU A 256     5904   5228   6960  -1813   1245   -759       C  
ATOM   1906  CD2 LEU A 256      52.839  -6.845  32.682  1.00 49.19           C  
ANISOU 1906  CD2 LEU A 256     6417   5337   6936  -2045   1596   -733       C  
ATOM   1907  N   ASP A 257      52.061 -11.075  30.991  1.00 56.08           N  
ANISOU 1907  N   ASP A 257     7611   5966   7732  -2465   1500   -695       N  
ATOM   1908  CA  ASP A 257      51.254 -12.229  30.546  1.00 57.76           C  
ANISOU 1908  CA  ASP A 257     7820   6123   8001  -2655   1513   -740       C  
ATOM   1909  C   ASP A 257      50.323 -11.860  29.383  1.00 64.75           C  
ANISOU 1909  C   ASP A 257     8418   7088   9094  -2665   1367   -833       C  
ATOM   1910  O   ASP A 257      50.169 -12.651  28.451  1.00 66.41           O  
ANISOU 1910  O   ASP A 257     8666   7253   9315  -2735   1254   -844       O  
ATOM   1911  CB  ASP A 257      50.453 -12.848  31.707  1.00 60.41           C  
ANISOU 1911  CB  ASP A 257     8196   6424   8334  -2878   1763   -778       C  
ATOM   1912  CG  ASP A 257      51.288 -13.348  32.880  1.00 79.15           C  
ANISOU 1912  CG  ASP A 257    10896   8697  10482  -2897   1886   -675       C  
ATOM   1913  OD1 ASP A 257      52.375 -13.934  32.638  1.00 80.89           O  
ANISOU 1913  OD1 ASP A 257    11367   8808  10560  -2834   1782   -577       O  
ATOM   1914  OD2 ASP A 257      50.848 -13.171  34.041  1.00 88.33           O  
ANISOU 1914  OD2 ASP A 257    12067   9881  11612  -2977   2082   -695       O  
ATOM   1915  N   SER A 258      49.774 -10.634  29.406  1.00 61.84           N  
ANISOU 1915  N   SER A 258     7777   6831   8887  -2584   1350   -897       N  
ATOM   1916  CA  SER A 258      48.874 -10.083  28.394  1.00 62.37           C  
ANISOU 1916  CA  SER A 258     7550   6975   9174  -2569   1185   -980       C  
ATOM   1917  C   SER A 258      49.547  -9.857  27.024  1.00 67.78           C  
ANISOU 1917  C   SER A 258     8296   7656   9800  -2424    912   -923       C  
ATOM   1918  O   SER A 258      48.845  -9.563  26.047  1.00 67.99           O  
ANISOU 1918  O   SER A 258     8130   7727   9976  -2426    733   -975       O  
ATOM   1919  CB  SER A 258      48.272  -8.771  28.893  1.00 66.35           C  
ANISOU 1919  CB  SER A 258     7772   7576   9861  -2494   1245  -1054       C  
ATOM   1920  OG  SER A 258      49.180  -7.691  28.734  1.00 75.35           O  
ANISOU 1920  OG  SER A 258     8949   8746  10935  -2275   1137   -989       O  
ATOM   1921  N   TRP A 259      50.894  -9.951  26.957  1.00 64.14           N  
ANISOU 1921  N   TRP A 259     8097   7143   9130  -2301    878   -819       N  
ATOM   1922  CA  TRP A 259      51.636  -9.729  25.715  1.00 63.71           C  
ANISOU 1922  CA  TRP A 259     8126   7081   8999  -2172    658   -770       C  
ATOM   1923  C   TRP A 259      51.504 -10.914  24.736  1.00 69.43           C  
ANISOU 1923  C   TRP A 259     8972   7735   9675  -2287    559   -781       C  
ATOM   1924  O   TRP A 259      51.618 -12.066  25.171  1.00 69.11           O  
ANISOU 1924  O   TRP A 259     9104   7605   9551  -2403    677   -770       O  
ATOM   1925  CB  TRP A 259      53.108  -9.395  25.995  1.00 61.73           C  
ANISOU 1925  CB  TRP A 259     8083   6801   8570  -2007    673   -673       C  
ATOM   1926  CG  TRP A 259      53.829  -8.853  24.801  1.00 62.28           C  
ANISOU 1926  CG  TRP A 259     8195   6885   8584  -1867    478   -635       C  
ATOM   1927  CD1 TRP A 259      54.481  -9.567  23.837  1.00 65.04           C  
ANISOU 1927  CD1 TRP A 259     8731   7169   8814  -1864    382   -608       C  
ATOM   1928  CD2 TRP A 259      53.911  -7.478  24.407  1.00 62.01           C  
ANISOU 1928  CD2 TRP A 259     8022   6927   8612  -1725    363   -627       C  
ATOM   1929  NE1 TRP A 259      54.985  -8.720  22.879  1.00 64.32           N  
ANISOU 1929  NE1 TRP A 259     8633   7115   8691  -1739    226   -583       N  
ATOM   1930  CE2 TRP A 259      54.669  -7.428  23.215  1.00 65.69           C  
ANISOU 1930  CE2 TRP A 259     8617   7372   8972  -1650    205   -586       C  
ATOM   1931  CE3 TRP A 259      53.481  -6.273  24.986  1.00 63.09           C  
ANISOU 1931  CE3 TRP A 259     7956   7138   8878  -1654    391   -652       C  
ATOM   1932  CZ2 TRP A 259      54.976  -6.226  22.576  1.00 64.97           C  
ANISOU 1932  CZ2 TRP A 259     8465   7330   8892  -1519     68   -560       C  
ATOM   1933  CZ3 TRP A 259      53.790  -5.082  24.352  1.00 64.59           C  
ANISOU 1933  CZ3 TRP A 259     8078   7370   9093  -1509    244   -626       C  
ATOM   1934  CH2 TRP A 259      54.536  -5.064  23.166  1.00 65.18           C  
ANISOU 1934  CH2 TRP A 259     8294   7422   9051  -1447     83   -574       C  
ATOM   1935  N   PRO A 260      51.291 -10.650  23.416  1.00 67.24           N  
ANISOU 1935  N   PRO A 260     8629   7485   9436  -2261    339   -801       N  
ATOM   1936  CA  PRO A 260      51.142 -11.760  22.454  1.00 67.62           C  
ANISOU 1936  CA  PRO A 260     8804   7464   9426  -2382    241   -824       C  
ATOM   1937  C   PRO A 260      52.317 -12.738  22.369  1.00 73.52           C  
ANISOU 1937  C   PRO A 260     9871   8095   9967  -2363    301   -766       C  
ATOM   1938  O   PRO A 260      53.466 -12.375  22.619  1.00 73.43           O  
ANISOU 1938  O   PRO A 260     9989   8069   9841  -2212    333   -698       O  
ATOM   1939  CB  PRO A 260      50.901 -11.049  21.114  1.00 69.14           C  
ANISOU 1939  CB  PRO A 260     8902   7711   9658  -2324    -16   -838       C  
ATOM   1940  CG  PRO A 260      51.385  -9.655  21.314  1.00 73.39           C  
ANISOU 1940  CG  PRO A 260     9351   8319  10215  -2136    -48   -791       C  
ATOM   1941  CD  PRO A 260      51.100  -9.345  22.748  1.00 68.79           C  
ANISOU 1941  CD  PRO A 260     8643   7767   9728  -2136    161   -805       C  
ATOM   1942  N   GLN A 261      52.004 -13.987  22.014  1.00 71.56           N  
ANISOU 1942  N   GLN A 261     9741   7760   9690  -2520    313   -802       N  
ATOM   1943  CA  GLN A 261      52.955 -15.088  21.856  1.00 71.86           C  
ANISOU 1943  CA  GLN A 261    10074   7664   9566  -2522    367   -766       C  
ATOM   1944  C   GLN A 261      53.654 -15.050  20.493  1.00 74.51           C  
ANISOU 1944  C   GLN A 261    10544   7974   9793  -2452    210   -770       C  
ATOM   1945  O   GLN A 261      53.090 -14.551  19.509  1.00 74.11           O  
ANISOU 1945  O   GLN A 261    10387   7988   9784  -2479     39   -812       O  
ATOM   1946  CB  GLN A 261      52.267 -16.448  22.092  1.00 73.79           C  
ANISOU 1946  CB  GLN A 261    10398   7807   9832  -2731    465   -807       C  
ATOM   1947  CG  GLN A 261      51.059 -16.732  21.194  1.00 96.34           C  
ANISOU 1947  CG  GLN A 261    13122  10687  12797  -2907    346   -901       C  
ATOM   1948  CD  GLN A 261      50.215 -17.839  21.763  1.00122.52           C  
ANISOU 1948  CD  GLN A 261    16472  13918  16162  -3124    480   -941       C  
ATOM   1949  OE1 GLN A 261      50.445 -19.026  21.504  1.00119.70           O  
ANISOU 1949  OE1 GLN A 261    16342  13426  15713  -3207    505   -944       O  
ATOM   1950  NE2 GLN A 261      49.221 -17.474  22.562  1.00115.45           N  
ANISOU 1950  NE2 GLN A 261    15357  13093  15418  -3225    582   -978       N  
ATOM   1951  N   GLY A 262      54.879 -15.574  20.463  1.00 69.50           N  
ANISOU 1951  N   GLY A 262    10146   7240   9023  -2365    271   -728       N  
ATOM   1952  CA  GLY A 262      55.704 -15.622  19.260  1.00 67.89           C  
ANISOU 1952  CA  GLY A 262    10100   6994   8700  -2298    177   -739       C  
ATOM   1953  C   GLY A 262      57.105 -15.069  19.432  1.00 67.50           C  
ANISOU 1953  C   GLY A 262    10143   6939   8565  -2100    221   -677       C  
ATOM   1954  O   GLY A 262      57.584 -14.865  20.556  1.00 66.46           O  
ANISOU 1954  O   GLY A 262    10002   6802   8446  -2013    329   -618       O  
ATOM   1955  N   CYS A 263      57.758 -14.795  18.291  1.00 60.75           N  
ANISOU 1955  N   CYS A 263     9379   6086   7618  -2038    134   -696       N  
ATOM   1956  CA  CYS A 263      59.131 -14.304  18.227  1.00 58.48           C  
ANISOU 1956  CA  CYS A 263     9179   5789   7252  -1865    175   -656       C  
ATOM   1957  C   CYS A 263      59.271 -12.814  18.538  1.00 55.82           C  
ANISOU 1957  C   CYS A 263     8680   5580   6950  -1743    134   -602       C  
ATOM   1958  O   CYS A 263      60.395 -12.334  18.661  1.00 53.48           O  
ANISOU 1958  O   CYS A 263     8430   5281   6607  -1602    179   -564       O  
ATOM   1959  CB  CYS A 263      59.758 -14.664  16.885  1.00 59.27           C  
ANISOU 1959  CB  CYS A 263     9453   5832   7235  -1872    132   -712       C  
ATOM   1960  SG  CYS A 263      59.757 -16.439  16.513  1.00 63.42           S  
ANISOU 1960  SG  CYS A 263    10193   6183   7721  -2002    195   -789       S  
ATOM   1961  N   SER A 264      58.134 -12.101  18.692  1.00 50.06           N  
ANISOU 1961  N   SER A 264     7752   4952   6318  -1795     51   -604       N  
ATOM   1962  CA  SER A 264      58.049 -10.675  19.020  1.00 49.17           C  
ANISOU 1962  CA  SER A 264     7466   4951   6266  -1692      4   -562       C  
ATOM   1963  C   SER A 264      58.909 -10.347  20.249  1.00 51.76           C  
ANISOU 1963  C   SER A 264     7796   5274   6595  -1566    142   -503       C  
ATOM   1964  O   SER A 264      59.760  -9.468  20.165  1.00 51.51           O  
ANISOU 1964  O   SER A 264     7769   5277   6525  -1436    130   -465       O  
ATOM   1965  CB  SER A 264      56.597 -10.284  19.268  1.00 53.26           C  
ANISOU 1965  CB  SER A 264     7758   5546   6933  -1781    -64   -590       C  
ATOM   1966  OG  SER A 264      56.441  -8.879  19.184  1.00 68.06           O  
ANISOU 1966  OG  SER A 264     9473   7515   8871  -1681   -149   -563       O  
ATOM   1967  N   GLN A 265      58.745 -11.127  21.348  1.00 46.75           N  
ANISOU 1967  N   GLN A 265     7186   4585   5991  -1618    267   -495       N  
ATOM   1968  CA  GLN A 265      59.478 -11.020  22.613  1.00 45.12           C  
ANISOU 1968  CA  GLN A 265     7014   4357   5773  -1528    386   -437       C  
ATOM   1969  C   GLN A 265      60.992 -11.171  22.428  1.00 45.26           C  
ANISOU 1969  C   GLN A 265     7191   4306   5700  -1398    408   -403       C  
ATOM   1970  O   GLN A 265      61.771 -10.441  23.040  1.00 43.69           O  
ANISOU 1970  O   GLN A 265     6971   4136   5493  -1275    436   -356       O  
ATOM   1971  CB  GLN A 265      58.951 -12.065  23.597  1.00 46.55           C  
ANISOU 1971  CB  GLN A 265     7245   4467   5975  -1647    499   -436       C  
ATOM   1972  CG  GLN A 265      57.579 -11.703  24.164  1.00 70.86           C  
ANISOU 1972  CG  GLN A 265    10129   7628   9166  -1758    529   -470       C  
ATOM   1973  CD  GLN A 265      56.771 -12.895  24.622  1.00 93.29           C  
ANISOU 1973  CD  GLN A 265    13021  10395  12029  -1934    627   -494       C  
ATOM   1974  OE1 GLN A 265      56.750 -13.957  23.983  1.00 86.88           O  
ANISOU 1974  OE1 GLN A 265    12333   9491  11185  -2024    606   -519       O  
ATOM   1975  NE2 GLN A 265      56.057 -12.728  25.730  1.00 89.24           N  
ANISOU 1975  NE2 GLN A 265    12417   9917  11571  -2001    745   -495       N  
ATOM   1976  N   LYS A 266      61.401 -12.112  21.571  1.00 40.52           N  
ANISOU 1976  N   LYS A 266     6741   3612   5043  -1427    397   -438       N  
ATOM   1977  CA  LYS A 266      62.804 -12.387  21.260  1.00 38.69           C  
ANISOU 1977  CA  LYS A 266     6648   3301   4752  -1312    429   -430       C  
ATOM   1978  C   LYS A 266      63.395 -11.311  20.343  1.00 38.63           C  
ANISOU 1978  C   LYS A 266     6603   3370   4705  -1221    371   -438       C  
ATOM   1979  O   LYS A 266      64.557 -10.930  20.500  1.00 37.68           O  
ANISOU 1979  O   LYS A 266     6509   3236   4570  -1094    409   -414       O  
ATOM   1980  CB  LYS A 266      62.951 -13.796  20.679  1.00 40.44           C  
ANISOU 1980  CB  LYS A 266     7042   3384   4940  -1383    457   -481       C  
ATOM   1981  CG  LYS A 266      62.939 -14.866  21.742  1.00 49.72           C  
ANISOU 1981  CG  LYS A 266     8307   4442   6141  -1423    534   -450       C  
ATOM   1982  CD  LYS A 266      63.807 -16.029  21.307  1.00 63.42           C  
ANISOU 1982  CD  LYS A 266    10230   6013   7855  -1391    574   -482       C  
ATOM   1983  CE  LYS A 266      63.617 -17.252  22.158  1.00 71.95           C  
ANISOU 1983  CE  LYS A 266    11432   6949   8956  -1466    627   -457       C  
ATOM   1984  NZ  LYS A 266      64.216 -18.437  21.500  1.00 88.37           N  
ANISOU 1984  NZ  LYS A 266    13688   8859  11029  -1459    652   -513       N  
ATOM   1985  N   ALA A 267      62.583 -10.795  19.414  1.00 33.52           N  
ANISOU 1985  N   ALA A 267     5890   2799   4045  -1293    270   -468       N  
ATOM   1986  CA  ALA A 267      62.981  -9.717  18.514  1.00 32.37           C  
ANISOU 1986  CA  ALA A 267     5726   2723   3849  -1232    199   -466       C  
ATOM   1987  C   ALA A 267      63.250  -8.462  19.354  1.00 37.18           C  
ANISOU 1987  C   ALA A 267     6201   3415   4510  -1117    205   -404       C  
ATOM   1988  O   ALA A 267      64.338  -7.901  19.251  1.00 38.16           O  
ANISOU 1988  O   ALA A 267     6356   3543   4600  -1012    237   -385       O  
ATOM   1989  CB  ALA A 267      61.898  -9.464  17.485  1.00 32.67           C  
ANISOU 1989  CB  ALA A 267     5730   2813   3869  -1343     59   -498       C  
ATOM   1990  N   ILE A 268      62.308  -8.100  20.263  1.00 33.03           N  
ANISOU 1990  N   ILE A 268     5529   2947   4074  -1143    195   -383       N  
ATOM   1991  CA  ILE A 268      62.360  -6.961  21.203  1.00 31.51           C  
ANISOU 1991  CA  ILE A 268     5203   2828   3941  -1053    211   -338       C  
ATOM   1992  C   ILE A 268      63.598  -7.051  22.121  1.00 36.57           C  
ANISOU 1992  C   ILE A 268     5912   3426   4558   -947    312   -298       C  
ATOM   1993  O   ILE A 268      64.203  -6.039  22.430  1.00 38.75           O  
ANISOU 1993  O   ILE A 268     6138   3748   4839   -847    311   -267       O  
ATOM   1994  CB  ILE A 268      61.036  -6.882  22.028  1.00 33.37           C  
ANISOU 1994  CB  ILE A 268     5288   3109   4281  -1132    221   -349       C  
ATOM   1995  CG1 ILE A 268      59.867  -6.371  21.149  1.00 32.51           C  
ANISOU 1995  CG1 ILE A 268     5051   3062   4237  -1198     84   -383       C  
ATOM   1996  CG2 ILE A 268      61.202  -6.024  23.303  1.00 32.74           C  
ANISOU 1996  CG2 ILE A 268     5115   3076   4249  -1052    292   -314       C  
ATOM   1997  CD1 ILE A 268      58.495  -6.721  21.666  1.00 33.25           C  
ANISOU 1997  CD1 ILE A 268     5005   3179   4450  -1314     97   -425       C  
ATOM   1998  N   LYS A 269      63.970  -8.250  22.542  1.00 31.86           N  
ANISOU 1998  N   LYS A 269     5431   2733   3942   -970    383   -299       N  
ATOM   1999  CA  LYS A 269      65.153  -8.506  23.363  1.00 30.71           C  
ANISOU 1999  CA  LYS A 269     5363   2523   3784   -871    449   -260       C  
ATOM   2000  C   LYS A 269      66.399  -8.048  22.572  1.00 34.25           C  
ANISOU 2000  C   LYS A 269     5844   2966   4202   -764    438   -269       C  
ATOM   2001  O   LYS A 269      67.217  -7.301  23.103  1.00 33.59           O  
ANISOU 2001  O   LYS A 269     5720   2909   4132   -661    449   -235       O  
ATOM   2002  CB  LYS A 269      65.210 -10.006  23.660  1.00 31.70           C  
ANISOU 2002  CB  LYS A 269     5626   2520   3898   -928    499   -266       C  
ATOM   2003  CG  LYS A 269      65.861 -10.389  24.951  1.00 39.32           C  
ANISOU 2003  CG  LYS A 269     6657   3416   4867   -873    545   -207       C  
ATOM   2004  CD  LYS A 269      65.291 -11.723  25.424  1.00 40.86           C  
ANISOU 2004  CD  LYS A 269     6968   3502   5055   -985    586   -203       C  
ATOM   2005  CE  LYS A 269      65.997 -12.230  26.647  1.00 56.00           C  
ANISOU 2005  CE  LYS A 269     8997   5322   6960   -935    611   -134       C  
ATOM   2006  NZ  LYS A 269      65.429 -13.524  27.100  1.00 73.13           N  
ANISOU 2006  NZ  LYS A 269    11292   7382   9110  -1063    653   -119       N  
ATOM   2007  N   CYS A 270      66.483  -8.431  21.273  1.00 31.44           N  
ANISOU 2007  N   CYS A 270     5561   2582   3802   -805    421   -323       N  
ATOM   2008  CA  CYS A 270      67.566  -8.062  20.355  1.00 30.17           C  
ANISOU 2008  CA  CYS A 270     5446   2415   3602   -737    437   -350       C  
ATOM   2009  C   CYS A 270      67.638  -6.570  20.099  1.00 29.65           C  
ANISOU 2009  C   CYS A 270     5284   2455   3525   -693    388   -323       C  
ATOM   2010  O   CYS A 270      68.727  -6.012  20.248  1.00 27.18           O  
ANISOU 2010  O   CYS A 270     4956   2147   3224   -597    427   -311       O  
ATOM   2011  CB  CYS A 270      67.501  -8.860  19.057  1.00 30.40           C  
ANISOU 2011  CB  CYS A 270     5599   2385   3566   -817    443   -422       C  
ATOM   2012  SG  CYS A 270      67.767 -10.634  19.281  1.00 34.95           S  
ANISOU 2012  SG  CYS A 270     6311   2801   4166   -842    518   -464       S  
ATOM   2013  N   LEU A 271      66.492  -5.920  19.752  1.00 28.06           N  
ANISOU 2013  N   LEU A 271     5011   2330   3319   -762    297   -315       N  
ATOM   2014  CA  LEU A 271      66.393  -4.453  19.524  1.00 29.14           C  
ANISOU 2014  CA  LEU A 271     5059   2555   3458   -723    229   -282       C  
ATOM   2015  C   LEU A 271      66.819  -3.665  20.777  1.00 32.69           C  
ANISOU 2015  C   LEU A 271     5407   3040   3972   -624    265   -236       C  
ATOM   2016  O   LEU A 271      67.534  -2.681  20.654  1.00 33.56           O  
ANISOU 2016  O   LEU A 271     5495   3181   4075   -555    263   -217       O  
ATOM   2017  CB  LEU A 271      64.963  -4.035  19.129  1.00 29.86           C  
ANISOU 2017  CB  LEU A 271     5071   2702   3572   -804    108   -281       C  
ATOM   2018  CG  LEU A 271      64.582  -4.044  17.651  1.00 36.76           C  
ANISOU 2018  CG  LEU A 271     6032   3573   4361   -888      6   -307       C  
ATOM   2019  CD1 LEU A 271      64.645  -5.449  17.071  1.00 38.36           C  
ANISOU 2019  CD1 LEU A 271     6376   3700   4500   -974     48   -364       C  
ATOM   2020  CD2 LEU A 271      63.156  -3.556  17.469  1.00 39.48           C  
ANISOU 2020  CD2 LEU A 271     6260   3971   4769   -948   -141   -298       C  
ATOM   2021  N   TYR A 272      66.375  -4.099  21.974  1.00 27.85           N  
ANISOU 2021  N   TYR A 272     4750   2418   3414   -631    302   -222       N  
ATOM   2022  CA  TYR A 272      66.732  -3.473  23.241  1.00 27.37           C  
ANISOU 2022  CA  TYR A 272     4622   2384   3394   -556    338   -184       C  
ATOM   2023  C   TYR A 272      68.264  -3.514  23.501  1.00 32.46           C  
ANISOU 2023  C   TYR A 272     5324   2985   4025   -457    385   -170       C  
ATOM   2024  O   TYR A 272      68.834  -2.508  23.902  1.00 34.11           O  
ANISOU 2024  O   TYR A 272     5475   3234   4250   -386    381   -147       O  
ATOM   2025  CB  TYR A 272      65.929  -4.103  24.397  1.00 27.58           C  
ANISOU 2025  CB  TYR A 272     4630   2396   3452   -613    381   -178       C  
ATOM   2026  CG  TYR A 272      66.285  -3.563  25.763  1.00 28.32           C  
ANISOU 2026  CG  TYR A 272     4690   2509   3561   -556    424   -143       C  
ATOM   2027  CD1 TYR A 272      66.451  -2.192  25.973  1.00 29.65           C  
ANISOU 2027  CD1 TYR A 272     4764   2746   3755   -491    401   -133       C  
ATOM   2028  CD2 TYR A 272      66.494  -4.419  26.841  1.00 28.36           C  
ANISOU 2028  CD2 TYR A 272     4777   2452   3544   -572    479   -118       C  
ATOM   2029  CE1 TYR A 272      66.816  -1.688  27.220  1.00 29.41           C  
ANISOU 2029  CE1 TYR A 272     4719   2729   3726   -447    438   -109       C  
ATOM   2030  CE2 TYR A 272      66.845  -3.925  28.097  1.00 29.27           C  
ANISOU 2030  CE2 TYR A 272     4889   2581   3649   -532    506    -85       C  
ATOM   2031  CZ  TYR A 272      67.009  -2.555  28.280  1.00 34.80           C  
ANISOU 2031  CZ  TYR A 272     5492   3357   4373   -470    489    -86       C  
ATOM   2032  OH  TYR A 272      67.318  -2.036  29.516  1.00 31.38           O  
ANISOU 2032  OH  TYR A 272     5065   2938   3920   -442    515    -63       O  
ATOM   2033  N   ILE A 273      68.906  -4.671  23.269  1.00 28.02           N  
ANISOU 2033  N   ILE A 273     4865   2334   3448   -454    426   -190       N  
ATOM   2034  CA  ILE A 273      70.355  -4.877  23.388  1.00 25.90           C  
ANISOU 2034  CA  ILE A 273     4634   2009   3199   -358    465   -192       C  
ATOM   2035  C   ILE A 273      71.108  -3.907  22.479  1.00 28.29           C  
ANISOU 2035  C   ILE A 273     4905   2355   3490   -317    470   -213       C  
ATOM   2036  O   ILE A 273      72.085  -3.344  22.944  1.00 27.93           O  
ANISOU 2036  O   ILE A 273     4814   2317   3482   -234    484   -198       O  
ATOM   2037  CB  ILE A 273      70.744  -6.378  23.138  1.00 27.25           C  
ANISOU 2037  CB  ILE A 273     4917   2059   3377   -366    505   -224       C  
ATOM   2038  CG1 ILE A 273      70.305  -7.265  24.326  1.00 26.87           C  
ANISOU 2038  CG1 ILE A 273     4917   1949   3343   -390    501   -183       C  
ATOM   2039  CG2 ILE A 273      72.244  -6.566  22.802  1.00 24.97           C  
ANISOU 2039  CG2 ILE A 273     4646   1708   3135   -267    551   -257       C  
ATOM   2040  CD1 ILE A 273      70.191  -8.837  23.986  1.00 26.93           C  
ANISOU 2040  CD1 ILE A 273     5052   1829   3350   -443    529   -214       C  
ATOM   2041  N   LEU A 274      70.686  -3.729  21.198  1.00 25.82           N  
ANISOU 2041  N   LEU A 274     4627   2065   3117   -384    456   -245       N  
ATOM   2042  CA  LEU A 274      71.342  -2.758  20.280  1.00 27.91           C  
ANISOU 2042  CA  LEU A 274     4892   2367   3347   -369    467   -258       C  
ATOM   2043  C   LEU A 274      71.403  -1.319  20.813  1.00 30.47           C  
ANISOU 2043  C   LEU A 274     5114   2765   3696   -322    426   -210       C  
ATOM   2044  O   LEU A 274      72.394  -0.624  20.568  1.00 29.55           O  
ANISOU 2044  O   LEU A 274     4985   2659   3586   -278    462   -214       O  
ATOM   2045  CB  LEU A 274      70.697  -2.702  18.861  1.00 28.43           C  
ANISOU 2045  CB  LEU A 274     5041   2446   3317   -469    431   -286       C  
ATOM   2046  CG  LEU A 274      70.795  -3.958  18.000  1.00 33.52           C  
ANISOU 2046  CG  LEU A 274     5812   3014   3909   -532    483   -353       C  
ATOM   2047  CD1 LEU A 274      70.060  -3.749  16.684  1.00 34.34           C  
ANISOU 2047  CD1 LEU A 274     6007   3141   3899   -644    416   -371       C  
ATOM   2048  CD2 LEU A 274      72.261  -4.361  17.757  1.00 33.75           C  
ANISOU 2048  CD2 LEU A 274     5882   2980   3962   -471    610   -410       C  
ATOM   2049  N   THR A 275      70.333  -0.879  21.510  1.00 25.25           N  
ANISOU 2049  N   THR A 275     4383   2152   3060   -337    360   -174       N  
ATOM   2050  CA  THR A 275      70.181   0.491  22.013  1.00 24.63           C  
ANISOU 2050  CA  THR A 275     4211   2135   3014   -298    318   -137       C  
ATOM   2051  C   THR A 275      70.985   0.789  23.275  1.00 28.86           C  
ANISOU 2051  C   THR A 275     4695   2671   3599   -218    354   -118       C  
ATOM   2052  O   THR A 275      71.281   1.941  23.528  1.00 27.02           O  
ANISOU 2052  O   THR A 275     4406   2475   3386   -178    338   -100       O  
ATOM   2053  CB  THR A 275      68.690   0.825  22.258  1.00 26.11           C  
ANISOU 2053  CB  THR A 275     4326   2363   3230   -343    247   -125       C  
ATOM   2054  OG1 THR A 275      68.209   0.120  23.416  1.00 25.90           O  
ANISOU 2054  OG1 THR A 275     4272   2328   3242   -354    284   -126       O  
ATOM   2055  CG2 THR A 275      67.804   0.566  21.041  1.00 16.36           C  
ANISOU 2055  CG2 THR A 275     3131   1129   1955   -427    174   -140       C  
ATOM   2056  N   ARG A 276      71.266  -0.218  24.107  1.00 27.43           N  
ANISOU 2056  N   ARG A 276     4542   2443   3436   -201    388   -118       N  
ATOM   2057  CA  ARG A 276      71.983   0.003  25.363  1.00 27.28           C  
ANISOU 2057  CA  ARG A 276     4494   2419   3453   -134    394    -93       C  
ATOM   2058  C   ARG A 276      73.346   0.688  25.163  1.00 31.91           C  
ANISOU 2058  C   ARG A 276     5049   3006   4069    -64    406   -100       C  
ATOM   2059  O   ARG A 276      73.480   1.787  25.684  1.00 31.24           O  
ANISOU 2059  O   ARG A 276     4904   2965   3998    -38    384    -83       O  
ATOM   2060  CB  ARG A 276      72.095  -1.279  26.197  1.00 26.69           C  
ANISOU 2060  CB  ARG A 276     4485   2273   3381   -132    408    -82       C  
ATOM   2061  CG  ARG A 276      70.739  -1.815  26.639  1.00 31.29           C  
ANISOU 2061  CG  ARG A 276     5089   2860   3938   -215    411    -73       C  
ATOM   2062  CD  ARG A 276      70.767  -2.460  28.012  1.00 33.41           C  
ANISOU 2062  CD  ARG A 276     5418   3082   4194   -217    418    -38       C  
ATOM   2063  NE  ARG A 276      71.542  -3.700  28.034  1.00 34.40           N  
ANISOU 2063  NE  ARG A 276     5639   3103   4329   -187    415    -29       N  
ATOM   2064  CZ  ARG A 276      71.068  -4.891  27.679  1.00 43.29           C  
ANISOU 2064  CZ  ARG A 276     6845   4161   5443   -245    436    -40       C  
ATOM   2065  NH1 ARG A 276      69.820  -5.015  27.238  1.00 23.47           N  
ANISOU 2065  NH1 ARG A 276     4323   1685   2910   -345    459    -62       N  
ATOM   2066  NH2 ARG A 276      71.843  -5.967  27.745  1.00 25.60           N  
ANISOU 2066  NH2 ARG A 276     4690   1808   3227   -202    428    -34       N  
ATOM   2067  N   PRO A 277      74.345   0.152  24.391  1.00 28.96           N  
ANISOU 2067  N   PRO A 277     4705   2585   3714    -41    451   -136       N  
ATOM   2068  CA  PRO A 277      75.612   0.889  24.228  1.00 27.89           C  
ANISOU 2068  CA  PRO A 277     4515   2456   3625     13    476   -152       C  
ATOM   2069  C   PRO A 277      75.477   2.248  23.541  1.00 29.20           C  
ANISOU 2069  C   PRO A 277     4655   2683   3758    -18    475   -148       C  
ATOM   2070  O   PRO A 277      76.357   3.083  23.704  1.00 28.71           O  
ANISOU 2070  O   PRO A 277     4537   2637   3736     16    486   -150       O  
ATOM   2071  CB  PRO A 277      76.492  -0.092  23.451  1.00 29.51           C  
ANISOU 2071  CB  PRO A 277     4754   2592   3865     30    546   -209       C  
ATOM   2072  CG  PRO A 277      75.545  -0.903  22.697  1.00 33.74           C  
ANISOU 2072  CG  PRO A 277     5380   3107   4332    -41    560   -225       C  
ATOM   2073  CD  PRO A 277      74.391  -1.113  23.633  1.00 29.57           C  
ANISOU 2073  CD  PRO A 277     4860   2595   3781    -66    493   -175       C  
ATOM   2074  N   LEU A 278      74.375   2.483  22.811  1.00 25.07           N  
ANISOU 2074  N   LEU A 278     4171   2187   3168    -84    449   -138       N  
ATOM   2075  CA  LEU A 278      74.083   3.764  22.163  1.00 25.51           C  
ANISOU 2075  CA  LEU A 278     4222   2283   3189   -115    419   -119       C  
ATOM   2076  C   LEU A 278      73.757   4.816  23.268  1.00 31.21           C  
ANISOU 2076  C   LEU A 278     4861   3042   3954    -76    366    -84       C  
ATOM   2077  O   LEU A 278      74.270   5.944  23.253  1.00 31.75           O  
ANISOU 2077  O   LEU A 278     4900   3126   4037    -60    363    -74       O  
ATOM   2078  CB  LEU A 278      72.931   3.575  21.149  1.00 26.09           C  
ANISOU 2078  CB  LEU A 278     4364   2361   3190   -192    372   -114       C  
ATOM   2079  CG  LEU A 278      72.508   4.753  20.257  1.00 32.87           C  
ANISOU 2079  CG  LEU A 278     5251   3240   3999   -232    310    -85       C  
ATOM   2080  CD1 LEU A 278      73.633   5.211  19.329  1.00 34.50           C  
ANISOU 2080  CD1 LEU A 278     5522   3430   4157   -256    382   -100       C  
ATOM   2081  CD2 LEU A 278      71.296   4.390  19.419  1.00 35.47           C  
ANISOU 2081  CD2 LEU A 278     5642   3567   4268   -305    229    -79       C  
ATOM   2082  N   ALA A 279      72.971   4.420  24.268  1.00 28.11           N  
ANISOU 2082  N   ALA A 279     4440   2659   3582    -67    340    -73       N  
ATOM   2083  CA  ALA A 279      72.694   5.292  25.397  1.00 28.37           C  
ANISOU 2083  CA  ALA A 279     4408   2721   3650    -37    314    -57       C  
ATOM   2084  C   ALA A 279      73.980   5.537  26.201  1.00 35.22           C  
ANISOU 2084  C   ALA A 279     5254   3580   4547     17    332    -59       C  
ATOM   2085  O   ALA A 279      74.250   6.665  26.592  1.00 34.09           O  
ANISOU 2085  O   ALA A 279     5070   3457   4427     38    316    -54       O  
ATOM   2086  CB  ALA A 279      71.639   4.678  26.291  1.00 28.64           C  
ANISOU 2086  CB  ALA A 279     4432   2762   3687    -58    312    -57       C  
ATOM   2087  N   PHE A 280      74.805   4.496  26.390  1.00 34.22           N  
ANISOU 2087  N   PHE A 280     5155   3415   4434     41    354    -68       N  
ATOM   2088  CA  PHE A 280      76.016   4.614  27.207  1.00 34.14           C  
ANISOU 2088  CA  PHE A 280     5112   3388   4471     97    342    -69       C  
ATOM   2089  C   PHE A 280      77.183   5.327  26.482  1.00 34.75           C  
ANISOU 2089  C   PHE A 280     5143   3468   4594    113    372    -94       C  
ATOM   2090  O   PHE A 280      78.191   5.623  27.109  1.00 34.83           O  
ANISOU 2090  O   PHE A 280     5101   3471   4660    153    353   -101       O  
ATOM   2091  CB  PHE A 280      76.418   3.242  27.781  1.00 36.03           C  
ANISOU 2091  CB  PHE A 280     5392   3570   4727    126    331    -65       C  
ATOM   2092  CG  PHE A 280      75.273   2.427  28.355  1.00 38.26           C  
ANISOU 2092  CG  PHE A 280     5741   3840   4956     87    322    -41       C  
ATOM   2093  CD1 PHE A 280      74.172   3.047  28.933  1.00 42.79           C  
ANISOU 2093  CD1 PHE A 280     6308   4460   5489     46    319    -29       C  
ATOM   2094  CD2 PHE A 280      75.311   1.044  28.344  1.00 41.95           C  
ANISOU 2094  CD2 PHE A 280     6274   4241   5424     87    327    -38       C  
ATOM   2095  CE1 PHE A 280      73.096   2.295  29.416  1.00 44.58           C  
ANISOU 2095  CE1 PHE A 280     6586   4677   5675     -8    334    -19       C  
ATOM   2096  CE2 PHE A 280      74.248   0.291  28.856  1.00 45.39           C  
ANISOU 2096  CE2 PHE A 280     6778   4660   5808     32    330    -17       C  
ATOM   2097  CZ  PHE A 280      73.146   0.922  29.383  1.00 43.24           C  
ANISOU 2097  CZ  PHE A 280     6492   4445   5494    -20    339     -9       C  
ATOM   2098  N   LEU A 281      77.020   5.672  25.205  1.00 29.21           N  
ANISOU 2098  N   LEU A 281     4463   2774   3861     70    415   -107       N  
ATOM   2099  CA  LEU A 281      78.021   6.417  24.441  1.00 28.78           C  
ANISOU 2099  CA  LEU A 281     4383   2721   3832     58    466   -131       C  
ATOM   2100  C   LEU A 281      78.231   7.781  25.109  1.00 35.65           C  
ANISOU 2100  C   LEU A 281     5201   3619   4727     68    427   -113       C  
ATOM   2101  O   LEU A 281      79.336   8.310  25.052  1.00 37.84           O  
ANISOU 2101  O   LEU A 281     5427   3892   5057     72    458   -135       O  
ATOM   2102  CB  LEU A 281      77.551   6.574  22.998  1.00 28.01           C  
ANISOU 2102  CB  LEU A 281     4363   2623   3657    -12    506   -134       C  
ATOM   2103  CG  LEU A 281      78.521   7.103  21.952  1.00 33.49           C  
ANISOU 2103  CG  LEU A 281     5074   3307   4345    -56    592   -166       C  
ATOM   2104  CD1 LEU A 281      79.942   6.565  22.143  1.00 34.40           C  
ANISOU 2104  CD1 LEU A 281     5113   3397   4561    -17    672   -226       C  
ATOM   2105  CD2 LEU A 281      78.023   6.756  20.548  1.00 35.15           C  
ANISOU 2105  CD2 LEU A 281     5404   3503   4449   -135    630   -173       C  
ATOM   2106  N   ASN A 282      77.163   8.312  25.779  1.00 30.39           N  
ANISOU 2106  N   ASN A 282     4540   2975   4032     69    367    -81       N  
ATOM   2107  CA  ASN A 282      77.097   9.516  26.603  1.00 29.63           C  
ANISOU 2107  CA  ASN A 282     4407   2896   3955     81    327    -72       C  
ATOM   2108  C   ASN A 282      78.405   9.681  27.400  1.00 31.93           C  
ANISOU 2108  C   ASN A 282     4644   3183   4307    113    319    -91       C  
ATOM   2109  O   ASN A 282      79.072  10.698  27.247  1.00 29.94           O  
ANISOU 2109  O   ASN A 282     4358   2930   4086     99    329   -101       O  
ATOM   2110  CB  ASN A 282      75.878   9.402  27.576  1.00 30.95           C  
ANISOU 2110  CB  ASN A 282     4581   3079   4101     89    289    -60       C  
ATOM   2111  CG  ASN A 282      75.891  10.293  28.820  1.00 49.74           C  
ANISOU 2111  CG  ASN A 282     6934   5470   6496    106    262    -68       C  
ATOM   2112  OD1 ASN A 282      75.862  11.529  28.756  1.00 44.67           O  
ANISOU 2112  OD1 ASN A 282     6273   4826   5874    103    253    -72       O  
ATOM   2113  ND2 ASN A 282      75.916   9.684  29.985  1.00 36.60           N  
ANISOU 2113  ND2 ASN A 282     5286   3806   4813    118    247    -70       N  
ATOM   2114  N   SER A 283      78.804   8.652  28.178  1.00 28.58           N  
ANISOU 2114  N   SER A 283     4212   2744   3903    150    294    -95       N  
ATOM   2115  CA  SER A 283      79.990   8.704  29.033  1.00 29.65           C  
ANISOU 2115  CA  SER A 283     4293   2868   4104    186    249   -109       C  
ATOM   2116  C   SER A 283      81.318   8.919  28.279  1.00 35.59           C  
ANISOU 2116  C   SER A 283     4966   3609   4948    188    295   -148       C  
ATOM   2117  O   SER A 283      82.293   9.376  28.882  1.00 35.79           O  
ANISOU 2117  O   SER A 283     4920   3633   5045    204    253   -166       O  
ATOM   2118  CB  SER A 283      80.064   7.482  29.947  1.00 33.53           C  
ANISOU 2118  CB  SER A 283     4816   3331   4594    225    191    -93       C  
ATOM   2119  OG  SER A 283      79.934   6.262  29.242  1.00 44.96           O  
ANISOU 2119  OG  SER A 283     6289   4746   6050    236    231    -97       O  
ATOM   2120  N   ALA A 284      81.343   8.646  26.968  1.00 32.89           N  
ANISOU 2120  N   ALA A 284     4638   3258   4600    159    385   -167       N  
ATOM   2121  CA  ALA A 284      82.538   8.821  26.134  1.00 32.15           C  
ANISOU 2121  CA  ALA A 284     4477   3152   4587    142    468   -218       C  
ATOM   2122  C   ALA A 284      82.471  10.100  25.319  1.00 36.23           C  
ANISOU 2122  C   ALA A 284     5019   3685   5062     67    526   -215       C  
ATOM   2123  O   ALA A 284      83.512  10.696  25.044  1.00 36.79           O  
ANISOU 2123  O   ALA A 284     5023   3752   5204     39    581   -253       O  
ATOM   2124  CB  ALA A 284      82.725   7.614  25.220  1.00 32.25           C  
ANISOU 2124  CB  ALA A 284     4507   3132   4613    147    551   -255       C  
ATOM   2125  N   VAL A 285      81.259  10.538  24.930  1.00 32.03           N  
ANISOU 2125  N   VAL A 285     4583   3163   4425     33    509   -170       N  
ATOM   2126  CA  VAL A 285      81.138  11.747  24.116  1.00 31.75           C  
ANISOU 2126  CA  VAL A 285     4596   3124   4343    -36    542   -154       C  
ATOM   2127  C   VAL A 285      80.880  13.033  24.944  1.00 36.31           C  
ANISOU 2127  C   VAL A 285     5157   3705   4932    -30    469   -128       C  
ATOM   2128  O   VAL A 285      81.279  14.097  24.479  1.00 36.20           O  
ANISOU 2128  O   VAL A 285     5157   3674   4922    -83    500   -126       O  
ATOM   2129  CB  VAL A 285      80.114  11.609  22.957  1.00 35.51           C  
ANISOU 2129  CB  VAL A 285     5191   3591   4709    -84    555   -122       C  
ATOM   2130  CG1 VAL A 285      80.430  10.385  22.091  1.00 35.66           C  
ANISOU 2130  CG1 VAL A 285     5243   3599   4708   -104    641   -161       C  
ATOM   2131  CG2 VAL A 285      78.669  11.568  23.469  1.00 34.92           C  
ANISOU 2131  CG2 VAL A 285     5146   3528   4594    -51    455    -78       C  
ATOM   2132  N   ASN A 286      80.258  12.954  26.157  1.00 30.68           N  
ANISOU 2132  N   ASN A 286     4427   3008   4223     23    387   -115       N  
ATOM   2133  CA  ASN A 286      79.921  14.159  26.918  1.00 29.26           C  
ANISOU 2133  CA  ASN A 286     4244   2824   4050     26    333   -105       C  
ATOM   2134  C   ASN A 286      81.169  14.980  27.442  1.00 34.55           C  
ANISOU 2134  C   ASN A 286     4849   3488   4791      9    331   -137       C  
ATOM   2135  O   ASN A 286      80.966  16.181  27.684  1.00 34.89           O  
ANISOU 2135  O   ASN A 286     4910   3512   4836    -10    308   -132       O  
ATOM   2136  CB  ASN A 286      78.891  13.887  28.008  1.00 25.35           C  
ANISOU 2136  CB  ASN A 286     3759   2344   3528     68    275    -98       C  
ATOM   2137  CG  ASN A 286      79.369  13.161  29.223  1.00 39.55           C  
ANISOU 2137  CG  ASN A 286     5527   4157   5342    103    239   -115       C  
ATOM   2138  OD1 ASN A 286      80.556  13.137  29.539  1.00 37.71           O  
ANISOU 2138  OD1 ASN A 286     5243   3921   5163    108    224   -136       O  
ATOM   2139  ND2 ASN A 286      78.442  12.556  29.941  1.00 27.90           N  
ANISOU 2139  ND2 ASN A 286     4087   2693   3821    121    217   -106       N  
ATOM   2140  N   PRO A 287      82.455  14.488  27.485  1.00 31.04           N  
ANISOU 2140  N   PRO A 287     4324   3048   4421     10    357   -174       N  
ATOM   2141  CA  PRO A 287      83.575  15.397  27.803  1.00 30.35           C  
ANISOU 2141  CA  PRO A 287     4166   2954   4413    -23    356   -208       C  
ATOM   2142  C   PRO A 287      83.739  16.561  26.805  1.00 34.43           C  
ANISOU 2142  C   PRO A 287     4721   3441   4918   -105    429   -202       C  
ATOM   2143  O   PRO A 287      84.506  17.484  27.083  1.00 35.51           O  
ANISOU 2143  O   PRO A 287     4813   3564   5114   -147    429   -227       O  
ATOM   2144  CB  PRO A 287      84.795  14.469  27.753  1.00 31.90           C  
ANISOU 2144  CB  PRO A 287     4253   3156   4712     -3    380   -254       C  
ATOM   2145  CG  PRO A 287      84.237  13.129  28.106  1.00 36.41           C  
ANISOU 2145  CG  PRO A 287     4850   3733   5251     66    339   -235       C  
ATOM   2146  CD  PRO A 287      82.972  13.115  27.302  1.00 32.48           C  
ANISOU 2146  CD  PRO A 287     4464   3236   4642     45    383   -195       C  
ATOM   2147  N   ILE A 288      82.990  16.539  25.669  1.00 29.38           N  
ANISOU 2147  N   ILE A 288     4180   2786   4196   -135    478   -165       N  
ATOM   2148  CA  ILE A 288      82.938  17.585  24.647  1.00 28.72           C  
ANISOU 2148  CA  ILE A 288     4181   2660   4069   -218    529   -138       C  
ATOM   2149  C   ILE A 288      82.346  18.907  25.215  1.00 31.98           C  
ANISOU 2149  C   ILE A 288     4637   3037   4479   -216    452   -110       C  
ATOM   2150  O   ILE A 288      82.643  19.989  24.704  1.00 31.01           O  
ANISOU 2150  O   ILE A 288     4565   2864   4352   -286    480    -95       O  
ATOM   2151  CB  ILE A 288      82.183  17.108  23.359  1.00 31.77           C  
ANISOU 2151  CB  ILE A 288     4684   3035   4351   -248    566    -98       C  
ATOM   2152  CG1 ILE A 288      82.462  18.039  22.149  1.00 32.82           C  
ANISOU 2152  CG1 ILE A 288     4927   3118   4427   -359    635    -71       C  
ATOM   2153  CG2 ILE A 288      80.668  16.962  23.581  1.00 31.34           C  
ANISOU 2153  CG2 ILE A 288     4687   2980   4240   -189    465    -49       C  
ATOM   2154  CD1 ILE A 288      83.726  17.722  21.364  1.00 44.26           C  
ANISOU 2154  CD1 ILE A 288     6351   4570   5894   -443    789   -126       C  
ATOM   2155  N   PHE A 289      81.518  18.818  26.261  1.00 27.34           N  
ANISOU 2155  N   PHE A 289     4034   2463   3891   -141    367   -108       N  
ATOM   2156  CA  PHE A 289      80.906  20.013  26.826  1.00 26.93           C  
ANISOU 2156  CA  PHE A 289     4016   2368   3848   -131    308    -98       C  
ATOM   2157  C   PHE A 289      81.924  20.969  27.500  1.00 31.82           C  
ANISOU 2157  C   PHE A 289     4592   2967   4531   -171    307   -139       C  
ATOM   2158  O   PHE A 289      81.634  22.163  27.585  1.00 31.16           O  
ANISOU 2158  O   PHE A 289     4559   2823   4458   -189    283   -131       O  
ATOM   2159  CB  PHE A 289      79.735  19.632  27.749  1.00 28.21           C  
ANISOU 2159  CB  PHE A 289     4173   2552   3996    -53    248   -102       C  
ATOM   2160  CG  PHE A 289      78.597  19.057  26.928  1.00 29.79           C  
ANISOU 2160  CG  PHE A 289     4420   2752   4148    -31    238    -59       C  
ATOM   2161  CD1 PHE A 289      77.852  19.872  26.067  1.00 32.47           C  
ANISOU 2161  CD1 PHE A 289     4831   3031   4475    -45    206    -15       C  
ATOM   2162  CD2 PHE A 289      78.313  17.693  26.958  1.00 30.55           C  
ANISOU 2162  CD2 PHE A 289     4496   2899   4214     -4    248    -61       C  
ATOM   2163  CE1 PHE A 289      76.837  19.330  25.271  1.00 32.76           C  
ANISOU 2163  CE1 PHE A 289     4909   3068   4472    -32    173     25       C  
ATOM   2164  CE2 PHE A 289      77.289  17.157  26.172  1.00 32.79           C  
ANISOU 2164  CE2 PHE A 289     4821   3182   4456      3    232    -27       C  
ATOM   2165  CZ  PHE A 289      76.557  17.978  25.338  1.00 31.20           C  
ANISOU 2165  CZ  PHE A 289     4681   2929   4244    -11    189     15       C  
ATOM   2166  N   TYR A 290      83.133  20.463  27.895  1.00 28.32           N  
ANISOU 2166  N   TYR A 290     4054   2563   4143   -186    326   -184       N  
ATOM   2167  CA  TYR A 290      84.251  21.233  28.485  1.00 27.22           C  
ANISOU 2167  CA  TYR A 290     3850   2411   4080   -236    317   -231       C  
ATOM   2168  C   TYR A 290      84.808  22.300  27.516  1.00 31.17           C  
ANISOU 2168  C   TYR A 290     4388   2855   4600   -337    391   -223       C  
ATOM   2169  O   TYR A 290      85.499  23.226  27.946  1.00 29.49           O  
ANISOU 2169  O   TYR A 290     4147   2613   4444   -392    382   -256       O  
ATOM   2170  CB  TYR A 290      85.419  20.276  28.808  1.00 27.00           C  
ANISOU 2170  CB  TYR A 290     3695   2435   4130   -227    318   -276       C  
ATOM   2171  CG  TYR A 290      85.315  19.559  30.133  1.00 27.68           C  
ANISOU 2171  CG  TYR A 290     3746   2558   4215   -154    212   -292       C  
ATOM   2172  CD1 TYR A 290      84.513  18.424  30.275  1.00 29.56           C  
ANISOU 2172  CD1 TYR A 290     4017   2822   4391    -84    193   -264       C  
ATOM   2173  CD2 TYR A 290      86.108  19.936  31.215  1.00 27.11           C  
ANISOU 2173  CD2 TYR A 290     3612   2490   4201   -168    128   -336       C  
ATOM   2174  CE1 TYR A 290      84.432  17.742  31.492  1.00 29.02           C  
ANISOU 2174  CE1 TYR A 290     3943   2777   4304    -33     99   -271       C  
ATOM   2175  CE2 TYR A 290      86.060  19.244  32.426  1.00 26.90           C  
ANISOU 2175  CE2 TYR A 290     3581   2489   4151   -113     19   -343       C  
ATOM   2176  CZ  TYR A 290      85.207  18.161  32.564  1.00 33.87           C  
ANISOU 2176  CZ  TYR A 290     4518   3392   4960    -48      9   -306       C  
ATOM   2177  OH  TYR A 290      85.161  17.485  33.755  1.00 31.71           O  
ANISOU 2177  OH  TYR A 290     4268   3133   4646    -10    -96   -305       O  
ATOM   2178  N   PHE A 291      84.574  22.098  26.197  1.00 29.08           N  
ANISOU 2178  N   PHE A 291     4195   2575   4281   -375    468   -181       N  
ATOM   2179  CA  PHE A 291      85.065  22.911  25.083  1.00 28.21           C  
ANISOU 2179  CA  PHE A 291     4155   2407   4155   -489    558   -162       C  
ATOM   2180  C   PHE A 291      83.981  23.764  24.502  1.00 33.47           C  
ANISOU 2180  C   PHE A 291     4981   2995   4740   -497    516    -87       C  
ATOM   2181  O   PHE A 291      84.128  24.277  23.388  1.00 34.22           O  
ANISOU 2181  O   PHE A 291     5187   3035   4782   -591    578    -46       O  
ATOM   2182  CB  PHE A 291      85.685  22.004  24.001  1.00 29.67           C  
ANISOU 2182  CB  PHE A 291     4324   2624   4324   -541    683   -176       C  
ATOM   2183  CG  PHE A 291      86.724  21.069  24.568  1.00 31.45           C  
ANISOU 2183  CG  PHE A 291     4373   2915   4660   -510    711   -254       C  
ATOM   2184  CD1 PHE A 291      88.037  21.492  24.750  1.00 34.60           C  
ANISOU 2184  CD1 PHE A 291     4652   3315   5179   -581    767   -320       C  
ATOM   2185  CD2 PHE A 291      86.377  19.782  24.973  1.00 33.75           C  
ANISOU 2185  CD2 PHE A 291     4614   3259   4952   -408    666   -262       C  
ATOM   2186  CE1 PHE A 291      88.985  20.643  25.317  1.00 35.89           C  
ANISOU 2186  CE1 PHE A 291     4636   3529   5472   -538    762   -392       C  
ATOM   2187  CE2 PHE A 291      87.327  18.926  25.528  1.00 36.98           C  
ANISOU 2187  CE2 PHE A 291     4866   3709   5477   -367    665   -326       C  
ATOM   2188  CZ  PHE A 291      88.628  19.359  25.684  1.00 35.64           C  
ANISOU 2188  CZ  PHE A 291     4566   3538   5437   -426    707   -391       C  
ATOM   2189  N   LEU A 292      82.893  23.948  25.262  1.00 29.71           N  
ANISOU 2189  N   LEU A 292     4521   2508   4260   -403    410    -71       N  
ATOM   2190  CA  LEU A 292      81.758  24.765  24.832  1.00 28.87           C  
ANISOU 2190  CA  LEU A 292     4539   2317   4113   -384    344     -7       C  
ATOM   2191  C   LEU A 292      81.369  25.787  25.902  1.00 34.80           C  
ANISOU 2191  C   LEU A 292     5281   3014   4928   -339    273    -34       C  
ATOM   2192  O   LEU A 292      80.237  26.282  25.877  1.00 36.17           O  
ANISOU 2192  O   LEU A 292     5514   3125   5104   -280    201     -2       O  
ATOM   2193  CB  LEU A 292      80.560  23.847  24.470  1.00 28.16           C  
ANISOU 2193  CB  LEU A 292     4473   2259   3967   -307    295     31       C  
ATOM   2194  CG  LEU A 292      80.765  22.855  23.310  1.00 31.45           C  
ANISOU 2194  CG  LEU A 292     4930   2716   4304   -353    358     57       C  
ATOM   2195  CD1 LEU A 292      79.603  21.932  23.198  1.00 30.78           C  
ANISOU 2195  CD1 LEU A 292     4851   2665   4180   -277    296     81       C  
ATOM   2196  CD2 LEU A 292      81.007  23.580  21.967  1.00 33.77           C  
ANISOU 2196  CD2 LEU A 292     5376   2932   4522   -466    397    116       C  
ATOM   2197  N   VAL A 293      82.292  26.113  26.844  1.00 30.72           N  
ANISOU 2197  N   VAL A 293     4688   2514   4471   -368    289   -101       N  
ATOM   2198  CA  VAL A 293      81.955  27.060  27.924  1.00 30.72           C  
ANISOU 2198  CA  VAL A 293     4691   2460   4520   -334    231   -142       C  
ATOM   2199  C   VAL A 293      82.692  28.420  27.799  1.00 35.86           C  
ANISOU 2199  C   VAL A 293     5397   3014   5213   -430    248   -150       C  
ATOM   2200  O   VAL A 293      82.666  29.218  28.729  1.00 39.50           O  
ANISOU 2200  O   VAL A 293     5860   3430   5720   -421    212   -200       O  
ATOM   2201  CB  VAL A 293      82.060  26.461  29.354  1.00 33.41           C  
ANISOU 2201  CB  VAL A 293     4937   2881   4877   -281    202   -216       C  
ATOM   2202  CG1 VAL A 293      80.974  25.423  29.585  1.00 32.77           C  
ANISOU 2202  CG1 VAL A 293     4840   2857   4755   -185    180   -205       C  
ATOM   2203  CG2 VAL A 293      83.445  25.898  29.654  1.00 33.03           C  
ANISOU 2203  CG2 VAL A 293     4790   2903   4856   -336    226   -257       C  
ATOM   2204  N   GLY A 294      83.274  28.675  26.637  1.00 30.64           N  
ANISOU 2204  N   GLY A 294     4797   2316   4529   -528    309   -102       N  
ATOM   2205  CA  GLY A 294      83.926  29.924  26.261  1.00 29.88           C  
ANISOU 2205  CA  GLY A 294     4779   2115   4458   -642    341    -92       C  
ATOM   2206  C   GLY A 294      85.263  30.284  26.866  1.00 34.91           C  
ANISOU 2206  C   GLY A 294     5325   2772   5168   -735    386   -169       C  
ATOM   2207  O   GLY A 294      85.750  31.386  26.612  1.00 38.15           O  
ANISOU 2207  O   GLY A 294     5804   3086   5604   -838    413   -165       O  
ATOM   2208  N   ASP A 295      85.869  29.393  27.648  1.00 29.98           N  
ANISOU 2208  N   ASP A 295     4548   2260   4580   -707    384   -236       N  
ATOM   2209  CA  ASP A 295      87.127  29.634  28.365  1.00 29.57           C  
ANISOU 2209  CA  ASP A 295     4381   2237   4616   -782    391   -318       C  
ATOM   2210  C   ASP A 295      88.438  29.374  27.579  1.00 37.99           C  
ANISOU 2210  C   ASP A 295     5360   3338   5738   -903    505   -339       C  
ATOM   2211  O   ASP A 295      89.506  29.687  28.106  1.00 39.29           O  
ANISOU 2211  O   ASP A 295     5416   3515   5998   -977    506   -410       O  
ATOM   2212  CB  ASP A 295      87.140  28.826  29.672  1.00 30.26           C  
ANISOU 2212  CB  ASP A 295     4359   2418   4722   -691    303   -377       C  
ATOM   2213  CG  ASP A 295      86.958  27.318  29.523  1.00 35.78           C  
ANISOU 2213  CG  ASP A 295     4985   3220   5392   -608    308   -361       C  
ATOM   2214  OD1 ASP A 295      86.813  26.846  28.380  1.00 35.53           O  
ANISOU 2214  OD1 ASP A 295     4980   3194   5326   -620    387   -312       O  
ATOM   2215  OD2 ASP A 295      86.987  26.609  30.555  1.00 38.43           O  
ANISOU 2215  OD2 ASP A 295     5249   3620   5731   -541    232   -397       O  
ATOM   2216  N   HIS A 296      88.372  28.818  26.341  1.00 34.99           N  
ANISOU 2216  N   HIS A 296     5024   2969   5302   -932    604   -289       N  
ATOM   2217  CA  HIS A 296      89.543  28.433  25.535  1.00 34.43           C  
ANISOU 2217  CA  HIS A 296     4867   2934   5280  -1044    746   -323       C  
ATOM   2218  C   HIS A 296      90.369  27.325  26.240  1.00 38.37           C  
ANISOU 2218  C   HIS A 296     5144   3546   5890   -989    729   -407       C  
ATOM   2219  O   HIS A 296      91.604  27.347  26.225  1.00 39.25           O  
ANISOU 2219  O   HIS A 296     5112   3680   6123  -1077    800   -479       O  
ATOM   2220  CB  HIS A 296      90.399  29.645  25.097  1.00 35.32           C  
ANISOU 2220  CB  HIS A 296     5020   2962   5437  -1218    837   -339       C  
ATOM   2221  CG  HIS A 296      89.773  30.443  23.995  1.00 39.00           C  
ANISOU 2221  CG  HIS A 296     5718   3315   5783  -1293    887   -243       C  
ATOM   2222  ND1 HIS A 296      90.151  30.267  22.675  1.00 40.66           N  
ANISOU 2222  ND1 HIS A 296     6008   3514   5927  -1411   1042   -215       N  
ATOM   2223  CD2 HIS A 296      88.789  31.373  24.049  1.00 40.89           C  
ANISOU 2223  CD2 HIS A 296     6132   3445   5959  -1262    792   -172       C  
ATOM   2224  CE1 HIS A 296      89.405  31.105  21.972  1.00 40.45           C  
ANISOU 2224  CE1 HIS A 296     6215   3369   5785  -1455   1020   -115       C  
ATOM   2225  NE2 HIS A 296      88.571  31.795  22.755  1.00 41.02           N  
ANISOU 2225  NE2 HIS A 296     6341   3375   5869  -1359    865    -86       N  
ATOM   2226  N   PHE A 297      89.663  26.352  26.848  1.00 33.98           N  
ANISOU 2226  N   PHE A 297     4561   3051   5300   -845    632   -395       N  
ATOM   2227  CA  PHE A 297      90.229  25.221  27.588  1.00 33.33           C  
ANISOU 2227  CA  PHE A 297     4304   3057   5303   -767    579   -452       C  
ATOM   2228  C   PHE A 297      91.235  24.396  26.759  1.00 39.24           C  
ANISOU 2228  C   PHE A 297     4922   3848   6140   -813    712   -499       C  
ATOM   2229  O   PHE A 297      92.267  23.978  27.292  1.00 38.08           O  
ANISOU 2229  O   PHE A 297     4587   3742   6139   -809    687   -574       O  
ATOM   2230  CB  PHE A 297      89.090  24.340  28.158  1.00 34.31           C  
ANISOU 2230  CB  PHE A 297     4479   3220   5338   -622    478   -410       C  
ATOM   2231  CG  PHE A 297      89.473  23.103  28.950  1.00 34.30           C  
ANISOU 2231  CG  PHE A 297     4344   3292   5397   -532    399   -447       C  
ATOM   2232  CD1 PHE A 297      90.389  23.176  29.991  1.00 35.45           C  
ANISOU 2232  CD1 PHE A 297     4363   3457   5648   -538    300   -508       C  
ATOM   2233  CD2 PHE A 297      88.889  21.872  28.671  1.00 36.25           C  
ANISOU 2233  CD2 PHE A 297     4603   3577   5592   -444    406   -417       C  
ATOM   2234  CE1 PHE A 297      90.709  22.042  30.746  1.00 36.76           C  
ANISOU 2234  CE1 PHE A 297     4427   3675   5865   -450    197   -528       C  
ATOM   2235  CE2 PHE A 297      89.226  20.731  29.413  1.00 38.40           C  
ANISOU 2235  CE2 PHE A 297     4772   3898   5920   -359    322   -441       C  
ATOM   2236  CZ  PHE A 297      90.140  20.823  30.440  1.00 36.16           C  
ANISOU 2236  CZ  PHE A 297     4372   3628   5741   -361    213   -493       C  
ATOM   2237  N   ARG A 298      90.935  24.189  25.454  1.00 38.15           N  
ANISOU 2237  N   ARG A 298     4886   3692   5917   -857    849   -461       N  
ATOM   2238  CA  ARG A 298      91.755  23.453  24.477  1.00 38.20           C  
ANISOU 2238  CA  ARG A 298     4808   3727   5981   -915   1018   -511       C  
ATOM   2239  C   ARG A 298      93.095  24.128  24.335  1.00 43.29           C  
ANISOU 2239  C   ARG A 298     5322   4356   6769  -1053   1125   -592       C  
ATOM   2240  O   ARG A 298      94.121  23.443  24.371  1.00 42.92           O  
ANISOU 2240  O   ARG A 298     5072   4355   6882  -1053   1186   -683       O  
ATOM   2241  CB  ARG A 298      91.049  23.390  23.115  1.00 36.95           C  
ANISOU 2241  CB  ARG A 298     4846   3534   5659   -969   1136   -446       C  
ATOM   2242  CG  ARG A 298      91.812  22.635  22.030  1.00 49.27           C  
ANISOU 2242  CG  ARG A 298     6354   5118   7249  -1038   1334   -507       C  
ATOM   2243  CD  ARG A 298      91.595  23.251  20.651  1.00 61.80           C  
ANISOU 2243  CD  ARG A 298     8154   6643   8683  -1188   1486   -459       C  
ATOM   2244  NE  ARG A 298      90.172  23.385  20.334  1.00 64.60           N  
ANISOU 2244  NE  ARG A 298     8737   6959   8848  -1141   1378   -342       N  
ATOM   2245  CZ  ARG A 298      89.615  24.474  19.819  1.00 76.31           C  
ANISOU 2245  CZ  ARG A 298    10425   8359  10211  -1226   1361   -257       C  
ATOM   2246  NH1 ARG A 298      90.361  25.533  19.517  1.00 61.34           N  
ANISOU 2246  NH1 ARG A 298     8560   6405   8343  -1379   1461   -272       N  
ATOM   2247  NH2 ARG A 298      88.310  24.512  19.589  1.00 64.64           N  
ANISOU 2247  NH2 ARG A 298     9120   6844   8594  -1162   1238   -157       N  
ATOM   2248  N   ASP A 299      93.077  25.476  24.194  1.00 41.06           N  
ANISOU 2248  N   ASP A 299     5153   4004   6446  -1170   1143   -564       N  
ATOM   2249  CA  ASP A 299      94.251  26.331  24.086  1.00 42.15           C  
ANISOU 2249  CA  ASP A 299     5194   4113   6708  -1327   1243   -633       C  
ATOM   2250  C   ASP A 299      95.060  26.286  25.368  1.00 48.41           C  
ANISOU 2250  C   ASP A 299     5760   4949   7686  -1283   1109   -715       C  
ATOM   2251  O   ASP A 299      96.285  26.243  25.300  1.00 47.63           O  
ANISOU 2251  O   ASP A 299     5461   4871   7764  -1366   1194   -812       O  
ATOM   2252  CB  ASP A 299      93.862  27.769  23.697  1.00 44.48           C  
ANISOU 2252  CB  ASP A 299     5700   4304   6896  -1451   1268   -567       C  
ATOM   2253  CG  ASP A 299      93.266  27.890  22.302  1.00 54.93           C  
ANISOU 2253  CG  ASP A 299     7258   5571   8042  -1528   1398   -484       C  
ATOM   2254  OD1 ASP A 299      93.693  27.138  21.403  1.00 55.97           O  
ANISOU 2254  OD1 ASP A 299     7362   5738   8166  -1579   1563   -519       O  
ATOM   2255  OD2 ASP A 299      92.380  28.737  22.111  1.00 61.01           O  
ANISOU 2255  OD2 ASP A 299     8244   6255   8682  -1539   1329   -389       O  
ATOM   2256  N   MET A 300      94.376  26.223  26.529  1.00 48.21           N  
ANISOU 2256  N   MET A 300     5760   4936   7620  -1155    901   -682       N  
ATOM   2257  CA  MET A 300      95.005  26.080  27.847  1.00 49.25           C  
ANISOU 2257  CA  MET A 300     5716   5108   7890  -1102    734   -746       C  
ATOM   2258  C   MET A 300      95.683  24.711  27.975  1.00 54.24           C  
ANISOU 2258  C   MET A 300     6135   5812   8660  -1013    720   -805       C  
ATOM   2259  O   MET A 300      96.749  24.625  28.580  1.00 53.66           O  
ANISOU 2259  O   MET A 300     5852   5764   8773  -1028    651   -887       O  
ATOM   2260  CB  MET A 300      93.975  26.219  28.968  1.00 51.91           C  
ANISOU 2260  CB  MET A 300     6174   5439   8110   -992    540   -693       C  
ATOM   2261  CG  MET A 300      93.451  27.606  29.166  1.00 55.60           C  
ANISOU 2261  CG  MET A 300     6808   5825   8493  -1061    516   -662       C  
ATOM   2262  SD  MET A 300      92.313  27.561  30.570  1.00 59.69           S  
ANISOU 2262  SD  MET A 300     7436   6348   8897   -923    315   -631       S  
ATOM   2263  CE  MET A 300      91.631  29.042  30.419  1.00 55.47           C  
ANISOU 2263  CE  MET A 300     7087   5704   8285   -993    338   -601       C  
ATOM   2264  N   LEU A 301      95.065  23.648  27.412  1.00 53.38           N  
ANISOU 2264  N   LEU A 301     6080   5730   8473   -920    772   -766       N  
ATOM   2265  CA  LEU A 301      95.606  22.280  27.437  1.00 54.43           C  
ANISOU 2265  CA  LEU A 301     6036   5913   8734   -824    768   -817       C  
ATOM   2266  C   LEU A 301      96.917  22.169  26.675  1.00 62.95           C  
ANISOU 2266  C   LEU A 301     6909   6998  10012   -921    947   -924       C  
ATOM   2267  O   LEU A 301      97.874  21.621  27.218  1.00 63.14           O  
ANISOU 2267  O   LEU A 301     6695   7048  10248   -875    875  -1005       O  
ATOM   2268  CB  LEU A 301      94.597  21.230  26.930  1.00 54.00           C  
ANISOU 2268  CB  LEU A 301     6106   5872   8538   -719    799   -754       C  
ATOM   2269  CG  LEU A 301      93.488  20.826  27.901  1.00 57.97           C  
ANISOU 2269  CG  LEU A 301     6732   6387   8909   -588    610   -675       C  
ATOM   2270  CD1 LEU A 301      92.462  19.932  27.224  1.00 57.47           C  
ANISOU 2270  CD1 LEU A 301     6799   6331   8707   -519    669   -617       C  
ATOM   2271  CD2 LEU A 301      94.047  20.141  29.128  1.00 59.87           C  
ANISOU 2271  CD2 LEU A 301     6825   6656   9268   -490    420   -708       C  
ATOM   2272  N   PHE A 302      96.975  22.710  25.441  1.00 62.65           N  
ANISOU 2272  N   PHE A 302     6964   6929   9911  -1061   1176   -928       N  
ATOM   2273  CA  PHE A 302      98.189  22.682  24.622  1.00 63.87           C  
ANISOU 2273  CA  PHE A 302     6942   7084  10239  -1183   1396  -1041       C  
ATOM   2274  C   PHE A 302      99.307  23.520  25.229  1.00 68.41           C  
ANISOU 2274  C   PHE A 302     7320   7655  11017  -1282   1358  -1124       C  
ATOM   2275  O   PHE A 302     100.451  23.065  25.260  1.00 66.65           O  
ANISOU 2275  O   PHE A 302     6822   7458  11044  -1289   1407  -1241       O  
ATOM   2276  CB  PHE A 302      97.908  23.109  23.169  1.00 66.28           C  
ANISOU 2276  CB  PHE A 302     7448   7351  10386  -1332   1651  -1014       C  
ATOM   2277  CG  PHE A 302      96.989  22.199  22.386  1.00 68.67           C  
ANISOU 2277  CG  PHE A 302     7925   7658  10509  -1261   1713   -954       C  
ATOM   2278  CD1 PHE A 302      97.178  20.822  22.386  1.00 72.53           C  
ANISOU 2278  CD1 PHE A 302     8282   8186  11089  -1135   1721  -1008       C  
ATOM   2279  CD2 PHE A 302      95.963  22.722  21.611  1.00 71.66           C  
ANISOU 2279  CD2 PHE A 302     8601   7992  10636  -1325   1759   -847       C  
ATOM   2280  CE1 PHE A 302      96.323  19.982  21.666  1.00 73.93           C  
ANISOU 2280  CE1 PHE A 302     8628   8364  11098  -1080   1776   -958       C  
ATOM   2281  CE2 PHE A 302      95.123  21.880  20.871  1.00 74.58           C  
ANISOU 2281  CE2 PHE A 302     9129   8366  10842  -1270   1803   -796       C  
ATOM   2282  CZ  PHE A 302      95.307  20.518  20.906  1.00 72.77           C  
ANISOU 2282  CZ  PHE A 302     8771   8182  10697  -1153   1816   -855       C  
ATOM   2283  N   SER A 303      98.969  24.724  25.736  1.00 67.75           N  
ANISOU 2283  N   SER A 303     7368   7533  10841  -1355   1264  -1070       N  
ATOM   2284  CA  SER A 303      99.915  25.658  26.361  1.00 68.99           C  
ANISOU 2284  CA  SER A 303     7373   7676  11164  -1466   1211  -1142       C  
ATOM   2285  C   SER A 303     100.600  25.029  27.571  1.00 76.78           C  
ANISOU 2285  C   SER A 303     8108   8712  12355  -1349    983  -1206       C  
ATOM   2286  O   SER A 303     101.829  25.062  27.643  1.00 76.18           O  
ANISOU 2286  O   SER A 303     7767   8649  12529  -1418   1009  -1320       O  
ATOM   2287  CB  SER A 303      99.225  26.964  26.751  1.00 71.70           C  
ANISOU 2287  CB  SER A 303     7943   7957  11345  -1537   1130  -1064       C  
ATOM   2288  OG  SER A 303      98.711  27.645  25.619  1.00 78.44           O  
ANISOU 2288  OG  SER A 303     9023   8747  12034  -1661   1324  -1003       O  
ATOM   2289  N   LYS A 304      99.806  24.418  28.491  1.00 76.44           N  
ANISOU 2289  N   LYS A 304     8148   8690  12207  -1177    760  -1134       N  
ATOM   2290  CA  LYS A 304     100.297  23.738  29.697  1.00 77.50           C  
ANISOU 2290  CA  LYS A 304     8101   8859  12487  -1055    509  -1169       C  
ATOM   2291  C   LYS A 304     101.174  22.543  29.308  1.00 84.56           C  
ANISOU 2291  C   LYS A 304     8731   9782  13614   -984    568  -1255       C  
ATOM   2292  O   LYS A 304     102.240  22.363  29.896  1.00 83.97           O  
ANISOU 2292  O   LYS A 304     8396   9721  13788   -971    445  -1341       O  
ATOM   2293  CB  LYS A 304      99.131  23.306  30.603  1.00 79.82           C  
ANISOU 2293  CB  LYS A 304     8590   9159  12577   -908    302  -1065       C  
ATOM   2294  N   LEU A 305     100.751  21.774  28.272  1.00 83.71           N  
ANISOU 2294  N   LEU A 305     8689   9678  13440   -944    760  -1240       N  
ATOM   2295  CA  LEU A 305     101.492  20.634  27.731  1.00 85.00           C  
ANISOU 2295  CA  LEU A 305     8627   9855  13815   -879    866  -1331       C  
ATOM   2296  C   LEU A 305     102.834  21.108  27.181  1.00 92.52           C  
ANISOU 2296  C   LEU A 305     9317  10806  15031  -1024   1044  -1473       C  
ATOM   2297  O   LEU A 305     103.841  20.440  27.409  1.00 92.66           O  
ANISOU 2297  O   LEU A 305     9035  10833  15339   -962   1003  -1579       O  
ATOM   2298  CB  LEU A 305     100.687  19.919  26.629  1.00 85.32           C  
ANISOU 2298  CB  LEU A 305     8840   9891  13688   -847   1067  -1290       C  
ATOM   2299  CG  LEU A 305     101.248  18.568  26.160  1.00 90.48           C  
ANISOU 2299  CG  LEU A 305     9303  10547  14528   -747   1162  -1378       C  
ATOM   2300  CD1 LEU A 305     100.513  17.411  26.818  1.00 90.68           C  
ANISOU 2300  CD1 LEU A 305     9393  10572  14489   -547    951  -1303       C  
ATOM   2301  CD2 LEU A 305     101.203  18.449  24.646  1.00 92.88           C  
ANISOU 2301  CD2 LEU A 305     9698  10840  14751   -848   1497  -1417       C  
ATOM   2302  N   ARG A 306     102.848  22.267  26.478  1.00 91.75           N  
ANISOU 2302  N   ARG A 306     9329  10688  14845  -1219   1237  -1476       N  
ATOM   2303  CA  ARG A 306     104.061  22.878  25.923  1.00 92.89           C  
ANISOU 2303  CA  ARG A 306     9254  10825  15213  -1398   1437  -1609       C  
ATOM   2304  C   ARG A 306     105.009  23.331  27.036  1.00100.68           C  
ANISOU 2304  C   ARG A 306     9989  11823  16443  -1414   1217  -1678       C  
ATOM   2305  O   ARG A 306     106.220  23.190  26.882  1.00100.12           O  
ANISOU 2305  O   ARG A 306     9599  11762  16681  -1470   1301  -1820       O  
ATOM   2306  CB  ARG A 306     103.730  24.046  24.979  1.00 92.20           C  
ANISOU 2306  CB  ARG A 306     9403  10700  14931  -1610   1679  -1571       C  
ATOM   2307  CG  ARG A 306     103.295  23.615  23.579  1.00100.33           C  
ANISOU 2307  CG  ARG A 306    10593  11718  15812  -1656   1971  -1562       C  
ATOM   2308  CD  ARG A 306     103.158  24.782  22.613  1.00110.06           C  
ANISOU 2308  CD  ARG A 306    12038  12900  16881  -1891   2215  -1536       C  
ATOM   2309  NE  ARG A 306     102.011  25.644  22.919  1.00121.88           N  
ANISOU 2309  NE  ARG A 306    13860  14352  18095  -1897   2075  -1380       N  
ATOM   2310  CZ  ARG A 306     102.101  26.863  23.447  1.00140.34           C  
ANISOU 2310  CZ  ARG A 306    16258  16647  20418  -2006   1994  -1352       C  
ATOM   2311  NH1 ARG A 306     101.005  27.569  23.692  1.00129.21           N  
ANISOU 2311  NH1 ARG A 306    15140  15187  18768  -1990   1872  -1218       N  
ATOM   2312  NH2 ARG A 306     103.288  27.386  23.733  1.00128.24           N  
ANISOU 2312  NH2 ARG A 306    14485  15115  19125  -2132   2036  -1467       N  
ATOM   2313  N   GLN A 307     104.455  23.842  28.162  1.00100.73           N  
ANISOU 2313  N   GLN A 307    10132  11824  16317  -1364    934  -1587       N  
ATOM   2314  CA  GLN A 307     105.219  24.291  29.334  1.00102.27           C  
ANISOU 2314  CA  GLN A 307    10140  12025  16693  -1379    679  -1639       C  
ATOM   2315  C   GLN A 307     105.962  23.122  29.996  1.00110.37           C  
ANISOU 2315  C   GLN A 307    10864  13077  17994  -1219    480  -1708       C  
ATOM   2316  O   GLN A 307     107.069  23.322  30.495  1.00109.88           O  
ANISOU 2316  O   GLN A 307    10517  13021  18211  -1266    371  -1811       O  
ATOM   2317  CB  GLN A 307     104.319  25.020  30.352  1.00103.71           C  
ANISOU 2317  CB  GLN A 307    10585  12190  16630  -1361    442  -1527       C  
ATOM   2318  CG  GLN A 307     103.802  26.388  29.893  1.00122.44           C  
ANISOU 2318  CG  GLN A 307    13195  14515  18813  -1535    585  -1483       C  
ATOM   2319  CD  GLN A 307     104.869  27.457  29.877  1.00145.44           C  
ANISOU 2319  CD  GLN A 307    15934  17407  21922  -1736    650  -1589       C  
ATOM   2320  OE1 GLN A 307     105.568  27.658  28.877  1.00141.39           O  
ANISOU 2320  OE1 GLN A 307    15318  16883  21522  -1880    924  -1662       O  
ATOM   2321  NE2 GLN A 307     105.010  28.173  30.984  1.00137.87           N  
ANISOU 2321  NE2 GLN A 307    14946  16438  20999  -1765    407  -1604       N  
ATOM   2322  N   TYR A 308     105.366  21.905  29.976  1.00110.48           N  
ANISOU 2322  N   TYR A 308    10937  13098  17940  -1032    426  -1651       N  
ATOM   2323  CA  TYR A 308     105.979  20.680  30.506  1.00112.00           C  
ANISOU 2323  CA  TYR A 308    10873  13296  18386   -861    240  -1703       C  
ATOM   2324  C   TYR A 308     107.069  20.165  29.548  1.00119.55           C  
ANISOU 2324  C   TYR A 308    11504  14250  19668   -891    489  -1860       C  
ATOM   2325  O   TYR A 308     108.015  19.515  29.997  1.00119.26           O  
ANISOU 2325  O   TYR A 308    11148  14208  19958   -801    343  -1953       O  
ATOM   2326  CB  TYR A 308     104.933  19.572  30.756  1.00113.38           C  
ANISOU 2326  CB  TYR A 308    11244  13464  18371   -667    123  -1589       C  
ATOM   2327  CG  TYR A 308     103.953  19.818  31.890  1.00115.48           C  
ANISOU 2327  CG  TYR A 308    11782  13730  18364   -609   -151  -1453       C  
ATOM   2328  CD1 TYR A 308     102.586  19.620  31.710  1.00117.51           C  
ANISOU 2328  CD1 TYR A 308    12367  13988  18294   -572    -89  -1333       C  
ATOM   2329  CD2 TYR A 308     104.398  20.170  33.164  1.00116.20           C  
ANISOU 2329  CD2 TYR A 308    11799  13819  18532   -589   -476  -1452       C  
ATOM   2330  CE1 TYR A 308     101.681  19.812  32.755  1.00118.14           C  
ANISOU 2330  CE1 TYR A 308    12684  14066  18137   -523   -312  -1225       C  
ATOM   2331  CE2 TYR A 308     103.501  20.369  34.215  1.00117.01           C  
ANISOU 2331  CE2 TYR A 308    12167  13920  18372   -548   -704  -1339       C  
ATOM   2332  CZ  TYR A 308     102.143  20.186  34.006  1.00123.90           C  
ANISOU 2332  CZ  TYR A 308    13353  14793  18929   -515   -608  -1230       C  
ATOM   2333  OH  TYR A 308     101.248  20.374  35.031  1.00124.16           O  
ANISOU 2333  OH  TYR A 308    13638  14824  18713   -481   -802  -1135       O  
ATOM   2334  N   PHE A 309     106.926  20.443  28.234  1.00118.83           N  
ANISOU 2334  N   PHE A 309    11501  14158  19490  -1018    861  -1893       N  
ATOM   2335  CA  PHE A 309     107.897  20.050  27.211  1.00120.15           C  
ANISOU 2335  CA  PHE A 309    11399  14323  19930  -1081   1164  -2054       C  
ATOM   2336  C   PHE A 309     109.097  21.014  27.206  1.00127.28           C  
ANISOU 2336  C   PHE A 309    12032  15232  21096  -1268   1242  -2186       C  
ATOM   2337  O   PHE A 309     110.234  20.570  27.034  1.00126.76           O  
ANISOU 2337  O   PHE A 309    11594  15166  21402  -1264   1321  -2346       O  
ATOM   2338  CB  PHE A 309     107.237  19.979  25.819  1.00122.18           C  
ANISOU 2338  CB  PHE A 309    11898  14573  19951  -1167   1528  -2032       C  
ATOM   2339  CG  PHE A 309     108.127  19.427  24.728  1.00124.11           C  
ANISOU 2339  CG  PHE A 309    11905  14811  20439  -1216   1862  -2202       C  
ATOM   2340  CD1 PHE A 309     108.236  18.056  24.521  1.00127.42           C  
ANISOU 2340  CD1 PHE A 309    12211  15216  20986  -1036   1879  -2251       C  
ATOM   2341  CD2 PHE A 309     108.856  20.280  23.903  1.00126.51           C  
ANISOU 2341  CD2 PHE A 309    12108  15115  20845  -1449   2174  -2318       C  
ATOM   2342  CE1 PHE A 309     109.070  17.546  23.519  1.00128.34           C  
ANISOU 2342  CE1 PHE A 309    12104  15320  21340  -1081   2206  -2427       C  
ATOM   2343  CE2 PHE A 309     109.693  19.769  22.904  1.00129.40           C  
ANISOU 2343  CE2 PHE A 309    12252  15474  21439  -1506   2511  -2492       C  
ATOM   2344  CZ  PHE A 309     109.790  18.406  22.715  1.00127.45           C  
ANISOU 2344  CZ  PHE A 309    11886  15214  21324  -1318   2529  -2550       C  
ATOM   2345  N   LYS A 310     108.834  22.327  27.388  1.00126.50           N  
ANISOU 2345  N   LYS A 310    12116  15132  20818  -1434   1226  -2126       N  
ATOM   2346  CA  LYS A 310     109.844  23.388  27.422  1.00127.58           C  
ANISOU 2346  CA  LYS A 310    12048  15267  21160  -1639   1292  -2235       C  
ATOM   2347  C   LYS A 310     110.649  23.400  28.727  1.00135.04           C  
ANISOU 2347  C   LYS A 310    12691  16223  22395  -1568    936  -2295       C  
ATOM   2348  O   LYS A 310     111.736  23.979  28.757  1.00134.77           O  
ANISOU 2348  O   LYS A 310    12358  16193  22656  -1706    990  -2433       O  
ATOM   2349  CB  LYS A 310     109.206  24.761  27.167  1.00130.00           C  
ANISOU 2349  CB  LYS A 310    12682  15548  21163  -1826   1370  -2140       C  
ATOM   2350  N   SER A 311     110.127  22.757  29.796  1.00134.42           N  
ANISOU 2350  N   SER A 311    12695  16147  22231  -1366    571  -2193       N  
ATOM   2351  CA  SER A 311     110.797  22.663  31.099  1.00135.76           C  
ANISOU 2351  CA  SER A 311    12631  16319  22631  -1284    180  -2225       C  
ATOM   2352  C   SER A 311     112.005  21.706  31.067  1.00143.34           C  
ANISOU 2352  C   SER A 311    13141  17277  24045  -1177    146  -2374       C  
ATOM   2353  O   SER A 311     112.894  21.817  31.915  1.00142.86           O  
ANISOU 2353  O   SER A 311    12799  17216  24267  -1164   -124  -2445       O  
ATOM   2354  CB  SER A 311     109.811  22.253  32.188  1.00139.33           C  
ANISOU 2354  CB  SER A 311    13355  16767  22816  -1117   -172  -2064       C  
ATOM   2355  OG  SER A 311     109.252  20.976  31.932  1.00148.16           O  
ANISOU 2355  OG  SER A 311    14558  17878  23859   -923   -161  -2003       O  
ATOM   2356  N   LEU A 312     112.032  20.781  30.081  1.00142.78           N  
ANISOU 2356  N   LEU A 312    13002  17198  24048  -1100    415  -2426       N  
ATOM   2357  CA  LEU A 312     113.101  19.806  29.848  1.00143.91           C  
ANISOU 2357  CA  LEU A 312    12725  17326  24629   -988    446  -2581       C  
ATOM   2358  C   LEU A 312     114.387  20.530  29.398  1.00150.32           C  
ANISOU 2358  C   LEU A 312    13156  18149  25809  -1182    663  -2781       C  
ATOM   2359  O   LEU A 312     115.443  20.333  30.004  1.00149.94           O  
ANISOU 2359  O   LEU A 312    12703  18092  26175  -1122    472  -2901       O  
ATOM   2360  CB  LEU A 312     112.642  18.783  28.777  1.00144.10           C  
ANISOU 2360  CB  LEU A 312    12844  17333  24577   -883    727  -2585       C  
ATOM   2361  CG  LEU A 312     113.494  17.519  28.577  1.00149.06           C  
ANISOU 2361  CG  LEU A 312    13084  17924  25628   -720    756  -2735       C  
ATOM   2362  CD1 LEU A 312     112.617  16.314  28.300  1.00149.33           C  
ANISOU 2362  CD1 LEU A 312    13306  17921  25512   -493    677  -2636       C  
ATOM   2363  CD2 LEU A 312     114.489  17.687  27.434  1.00151.56           C  
ANISOU 2363  CD2 LEU A 312    13172  18246  26168   -873   1235  -2931       C  
ATOM   2364  N   THR A 313     114.286  21.357  28.337  1.00148.83           N  
ANISOU 2364  N   THR A 313    13101  17976  25473  -1417   1056  -2815       N  
ATOM   2365  CA  THR A 313     115.404  22.106  27.752  1.00149.62           C  
ANISOU 2365  CA  THR A 313    12890  18085  25873  -1643   1331  -3001       C  
ATOM   2366  C   THR A 313     115.856  23.278  28.620  1.00155.19           C  
ANISOU 2366  C   THR A 313    13516  18800  26648  -1794   1106  -3007       C  
ATOM   2367  O   THR A 313     117.057  23.429  28.857  1.00155.00           O  
ANISOU 2367  O   THR A 313    13066  18781  27045  -1847   1050  -3168       O  
ATOM   2368  CB  THR A 313     115.087  22.552  26.311  1.00159.35           C  
ANISOU 2368  CB  THR A 313    14330  19316  26900  -1847   1845  -3027       C  
ATOM   2369  OG1 THR A 313     113.833  23.237  26.286  1.00159.07           O  
ANISOU 2369  OG1 THR A 313    14789  19276  26376  -1916   1831  -2835       O  
ATOM   2370  CG2 THR A 313     115.080  21.392  25.319  1.00158.79           C  
ANISOU 2370  CG2 THR A 313    14214  19234  26886  -1738   2125  -3099       C  
ATOM   2371  N   SER A 314     114.903  24.113  29.075  1.00152.78           N  
ANISOU 2371  N   SER A 314    13611  18492  25946  -1865    982  -2843       N  
ATOM   2372  CA  SER A 314     115.186  25.292  29.893  1.00153.14           C  
ANISOU 2372  CA  SER A 314    13654  18537  25996  -2018    776  -2837       C  
ATOM   2373  C   SER A 314     115.502  24.939  31.342  1.00158.08           C  
ANISOU 2373  C   SER A 314    14131  19166  26764  -1854    260  -2811       C  
ATOM   2374  O   SER A 314     114.777  24.156  31.961  1.00158.09           O  
ANISOU 2374  O   SER A 314    14305  19164  26600  -1635     10  -2688       O  
ATOM   2375  CB  SER A 314     114.029  26.284  29.826  1.00156.80           C  
ANISOU 2375  CB  SER A 314    14606  18980  25990  -2137    838  -2678       C  
ATOM   2376  OG  SER A 314     113.833  26.755  28.503  1.00165.88           O  
ANISOU 2376  OG  SER A 314    15904  20115  27010  -2318   1289  -2698       O  
ATOM   2377  N   PHE A 315     116.592  25.519  31.876  1.00154.69           N  
ANISOU 2377  N   PHE A 315    13393  18742  26640  -1972     99  -2927       N  
ATOM   2378  CA  PHE A 315     117.031  25.332  33.258  1.00154.54           C  
ANISOU 2378  CA  PHE A 315    13224  18722  26772  -1856   -409  -2915       C  
ATOM   2379  C   PHE A 315     116.778  26.621  34.037  1.00160.41           C  
ANISOU 2379  C   PHE A 315    14191  19458  27298  -2024   -600  -2855       C  
ATOM   2380  O   PHE A 315     117.622  27.522  34.034  1.00160.05           O  
ANISOU 2380  O   PHE A 315    13927  19413  27471  -2230   -566  -2975       O  
ATOM   2381  CB  PHE A 315     118.521  24.939  33.322  1.00155.85           C  
ANISOU 2381  CB  PHE A 315    12810  18893  27513  -1835   -497  -3112       C  
ATOM   2382  CG  PHE A 315     118.846  23.545  32.848  1.00156.78           C  
ANISOU 2382  CG  PHE A 315    12684  19000  27884  -1621   -405  -3175       C  
ATOM   2383  CD1 PHE A 315     119.351  23.327  31.573  1.00159.39           C  
ANISOU 2383  CD1 PHE A 315    12812  19336  28412  -1701     71  -3320       C  
ATOM   2384  CD2 PHE A 315     118.676  22.450  33.689  1.00158.76           C  
ANISOU 2384  CD2 PHE A 315    12918  19227  28176  -1346   -791  -3095       C  
ATOM   2385  CE1 PHE A 315     119.660  22.037  31.138  1.00160.40           C  
ANISOU 2385  CE1 PHE A 315    12718  19445  28781  -1502    167  -3394       C  
ATOM   2386  CE2 PHE A 315     118.979  21.160  33.251  1.00161.66           C  
ANISOU 2386  CE2 PHE A 315    13067  19568  28788  -1144   -708  -3157       C  
ATOM   2387  CZ  PHE A 315     119.466  20.963  31.980  1.00159.70           C  
ANISOU 2387  CZ  PHE A 315    12612  19326  28742  -1219   -227  -3311       C  
ATOM   2388  N   ARG A 316     115.602  26.723  34.679  1.00158.54           N  
ANISOU 2388  N   ARG A 316    14392  19210  26635  -1944   -783  -2676       N  
ATOM   2389  CA  ARG A 316     115.234  27.910  35.455  1.00159.10           C  
ANISOU 2389  CA  ARG A 316    14726  19265  26462  -2083   -960  -2614       C  
ATOM   2390  C   ARG A 316     116.004  28.020  36.768  1.00164.23           C  
ANISOU 2390  C   ARG A 316    15174  19914  27310  -2072  -1426  -2662       C  
ATOM   2391  O   ARG A 316     116.198  29.131  37.260  1.00163.50           O  
ANISOU 2391  O   ARG A 316    15152  19807  27164  -2251  -1529  -2686       O  
ATOM   2392  CB  ARG A 316     113.713  28.004  35.672  1.00159.66           C  
ANISOU 2392  CB  ARG A 316    15313  19319  26031  -2002   -977  -2427       C  
ATOM   2393  CG  ARG A 316     112.953  28.560  34.464  1.00169.86           C  
ANISOU 2393  CG  ARG A 316    16868  20593  27077  -2108   -542  -2379       C  
ATOM   2394  CD  ARG A 316     113.134  30.062  34.283  1.00183.14           C  
ANISOU 2394  CD  ARG A 316    18664  22236  28683  -2371   -401  -2411       C  
ATOM   2395  NE  ARG A 316     112.695  30.510  32.960  1.00194.65           N  
ANISOU 2395  NE  ARG A 316    20297  23668  29992  -2492     31  -2388       N  
ATOM   2396  CZ  ARG A 316     112.811  31.756  32.510  1.00210.27           C  
ANISOU 2396  CZ  ARG A 316    22391  25597  31906  -2730    233  -2409       C  
ATOM   2397  NH1 ARG A 316     113.357  32.697  33.271  1.00195.45           N  
ANISOU 2397  NH1 ARG A 316    20461  23693  30109  -2877     56  -2465       N  
ATOM   2398  NH2 ARG A 316     112.382  32.070  31.295  1.00195.53           N  
ANISOU 2398  NH2 ARG A 316    20706  23697  29887  -2830    604  -2374       N  
ATOM   2399  N   LEU A 317     116.477  26.877  37.309  1.00161.65           N  
ANISOU 2399  N   LEU A 317    14600  19597  27223  -1868  -1712  -2678       N  
ATOM   2400  CA  LEU A 317     117.278  26.808  38.537  1.00161.52           C  
ANISOU 2400  CA  LEU A 317    14370  19576  27426  -1835  -2195  -2720       C  
ATOM   2401  C   LEU A 317     118.662  27.439  38.335  1.00164.76           C  
ANISOU 2401  C   LEU A 317    14325  19994  28283  -2024  -2163  -2915       C  
ATOM   2402  O   LEU A 317     119.255  27.927  39.296  1.00164.08           O  
ANISOU 2402  O   LEU A 317    14130  19901  28311  -2097  -2521  -2956       O  
ATOM   2403  CB  LEU A 317     117.394  25.361  39.065  1.00161.85           C  
ANISOU 2403  CB  LEU A 317    14281  19607  27609  -1556  -2503  -2674       C  
ATOM   2404  CG  LEU A 317     117.982  24.299  38.123  1.00167.33           C  
ANISOU 2404  CG  LEU A 317    14593  20300  28684  -1427  -2289  -2777       C  
ATOM   2405  CD1 LEU A 317     118.983  23.424  38.848  1.00167.47           C  
ANISOU 2405  CD1 LEU A 317    14225  20292  29114  -1264  -2706  -2839       C  
ATOM   2406  CD2 LEU A 317     116.886  23.452  37.490  1.00170.97           C  
ANISOU 2406  CD2 LEU A 317    15330  20757  28876  -1267  -2049  -2662       C  
ATOM   2407  N   LEU A 318     119.157  27.438  37.079  1.00161.23           N  
ANISOU 2407  N   LEU A 318    13623  19559  28076  -2116  -1726  -3038       N  
ATOM   2408  CA  LEU A 318     120.439  28.021  36.679  1.00161.08           C  
ANISOU 2408  CA  LEU A 318    13160  19551  28494  -2317  -1596  -3240       C  
ATOM   2409  C   LEU A 318     120.259  29.430  36.105  1.00166.38           C  
ANISOU 2409  C   LEU A 318    14024  20212  28982  -2616  -1258  -3263       C  
ATOM   2410  O   LEU A 318     121.177  30.247  36.210  1.00165.30           O  
ANISOU 2410  O   LEU A 318    13630  20073  29102  -2827  -1267  -3397       O  
ATOM   2411  CB  LEU A 318     121.159  27.120  35.660  1.00160.89           C  
ANISOU 2411  CB  LEU A 318    12711  19539  28883  -2238  -1312  -3383       C  
ATOM   2412  CG  LEU A 318     121.845  25.873  36.215  1.00165.26           C  
ANISOU 2412  CG  LEU A 318    12907  20082  29801  -1979  -1667  -3425       C  
ATOM   2413  CD1 LEU A 318     121.868  24.770  35.186  1.00165.05           C  
ANISOU 2413  CD1 LEU A 318    12799  20094  29818  -1816  -1348  -3419       C  
ATOM   2414  CD2 LEU A 318     123.261  26.179  36.689  1.00166.89           C  
ANISOU 2414  CD2 LEU A 318    12997  20607  29807  -2089  -1819  -3260       C  
ATOM   2415  N   GLU A 319     119.083  29.710  35.496  1.00164.43           N  
ANISOU 2415  N   GLU A 319    14226  19951  28301  -2636   -971  -3132       N  
ATOM   2416  CA  GLU A 319     118.751  31.009  34.901  1.00164.52           C  
ANISOU 2416  CA  GLU A 319    14488  19931  28090  -2898   -651  -3123       C  
ATOM   2417  C   GLU A 319     118.671  32.127  35.939  1.00168.92           C  
ANISOU 2417  C   GLU A 319    15225  20457  28499  -3043   -932  -3096       C  
ATOM   2418  O   GLU A 319     119.174  33.220  35.684  1.00168.51           O  
ANISOU 2418  O   GLU A 319    15116  20377  28531  -3304   -769  -3184       O  
ATOM   2419  CB  GLU A 319     117.459  30.930  34.074  1.00165.83           C  
ANISOU 2419  CB  GLU A 319    15098  20081  27831  -2844   -350  -2974       C  
ATOM   2420  CG  GLU A 319     117.686  30.536  32.623  1.00175.11           C  
ANISOU 2420  CG  GLU A 319    16143  21266  29125  -2887    125  -3045       C  
ATOM   2421  CD  GLU A 319     117.968  31.672  31.657  1.00195.88           C  
ANISOU 2421  CD  GLU A 319    19718  24439  30267  -3079    235  -2189       C  
ATOM   2422  OE1 GLU A 319     117.184  31.831  30.694  1.00190.83           O  
ANISOU 2422  OE1 GLU A 319    19016  23506  29985  -3160    632  -2495       O  
ATOM   2423  OE2 GLU A 319     118.971  32.396  31.851  1.00186.47           O  
ANISOU 2423  OE2 GLU A 319    18020  23108  29721  -3303    312  -2542       O  
ATOM   2424  N   VAL A 320     118.061  31.847  37.108  1.00166.29           N  
ANISOU 2424  N   VAL A 320    15117  20122  27943  -2885  -1345  -2981       N  
ATOM   2425  CA  VAL A 320     117.920  32.800  38.217  1.00166.52           C  
ANISOU 2425  CA  VAL A 320    15350  20119  27801  -3001  -1645  -2956       C  
ATOM   2426  C   VAL A 320     119.288  33.014  38.901  1.00170.74           C  
ANISOU 2426  C   VAL A 320    15452  20666  28755  -3107  -1936  -3114       C  
ATOM   2427  O   VAL A 320     119.630  34.149  39.246  1.00169.99           O  
ANISOU 2427  O   VAL A 320    15384  20540  28666  -3332  -1991  -3176       O  
ATOM   2428  CB  VAL A 320     116.804  32.368  39.216  1.00170.66           C  
ANISOU 2428  CB  VAL A 320    16272  20637  27934  -2806  -1961  -2789       C  
ATOM   2429  CG1 VAL A 320     116.658  33.361  40.369  1.00170.54           C  
ANISOU 2429  CG1 VAL A 320    16498  20582  27718  -2939  -2236  -2776       C  
ATOM   2430  CG2 VAL A 320     115.464  32.190  38.505  1.00170.52           C  
ANISOU 2430  CG2 VAL A 320    16637  20608  27543  -2700  -1671  -2645       C  
ATOM   2431  N   LEU A 321     120.069  31.927  39.059  1.00167.60           N  
ANISOU 2431  N   LEU A 321    14650  20308  28721  -2947  -2119  -3183       N  
ATOM   2432  CA  LEU A 321     121.389  31.928  39.693  1.00167.77           C  
ANISOU 2432  CA  LEU A 321    14410  20500  28836  -3019  -2379  -3162       C  
ATOM   2433  C   LEU A 321     122.451  32.725  38.922  1.00172.30           C  
ANISOU 2433  C   LEU A 321    15049  21382  29037  -3312  -2021  -2976       C  
ATOM   2434  O   LEU A 321     123.312  33.344  39.553  1.00172.87           O  
ANISOU 2434  O   LEU A 321    15038  21551  29093  -3485  -2218  -2969       O  
ATOM   2435  CB  LEU A 321     121.865  30.486  39.917  1.00167.90           C  
ANISOU 2435  CB  LEU A 321    14275  20691  28830  -2771  -2534  -3033       C  
ATOM   2436  CG  LEU A 321     122.861  30.282  41.053  1.00172.67           C  
ANISOU 2436  CG  LEU A 321    15049  21734  28822  -2798  -2829  -2701       C  
ATOM   2437  CD1 LEU A 321     122.325  29.306  42.068  1.00172.89           C  
ANISOU 2437  CD1 LEU A 321    15257  21726  28706  -2572  -3229  -2627       C  
ATOM   2438  CD2 LEU A 321     124.204  29.818  40.526  1.00175.07           C  
ANISOU 2438  CD2 LEU A 321    15238  22453  28828  -2788  -2624  -2462       C  
ATOM   2439  N   PHE A 322     122.402  32.704  37.574  1.00167.90           N  
ANISOU 2439  N   PHE A 322    14258  20690  28847  -3354  -1577  -3158       N  
ATOM   2440  CA  PHE A 322     123.381  33.403  36.737  1.00167.17           C  
ANISOU 2440  CA  PHE A 322    14053  20732  28732  -3614  -1262  -3127       C  
ATOM   2441  C   PHE A 322     122.893  34.755  36.191  1.00171.43           C  
ANISOU 2441  C   PHE A 322    15074  21285  28778  -3868   -989  -2953       C  
ATOM   2442  O   PHE A 322     123.710  35.666  36.033  1.00171.04           O  
ANISOU 2442  O   PHE A 322    14976  21308  28703  -4123   -909  -2923       O  
ATOM   2443  CB  PHE A 322     123.888  32.494  35.604  1.00168.39           C  
ANISOU 2443  CB  PHE A 322    14124  21093  28764  -3524   -944  -2976       C  
ATOM   2444  CG  PHE A 322     124.887  31.456  36.063  1.00169.18           C  
ANISOU 2444  CG  PHE A 322    14045  21480  28754  -3354  -1181  -2799       C  
ATOM   2445  CD1 PHE A 322     126.249  31.727  36.057  1.00171.97           C  
ANISOU 2445  CD1 PHE A 322    14359  22196  28787  -3500  -1206  -2544       C  
ATOM   2446  CD2 PHE A 322     124.465  30.210  36.508  1.00170.49           C  
ANISOU 2446  CD2 PHE A 322    14302  21705  28771  -3053  -1367  -2690       C  
ATOM   2447  CE1 PHE A 322     127.171  30.769  36.488  1.00172.56           C  
ANISOU 2447  CE1 PHE A 322    14244  22536  28785  -3343  -1397  -2408       C  
ATOM   2448  CE2 PHE A 322     125.388  29.254  36.941  1.00172.94           C  
ANISOU 2448  CE2 PHE A 322    14554  22350  28804  -2901  -1549  -2450       C  
ATOM   2449  CZ  PHE A 322     126.734  29.540  36.928  1.00170.99           C  
ANISOU 2449  CZ  PHE A 322    13986  22277  28704  -3040  -1571  -2453       C  
ATOM   2450  N   GLN A 323     121.581  34.892  35.913  1.00168.19           N  
ANISOU 2450  N   GLN A 323    14716  20530  28660  -3808   -830  -3221       N  
ATOM   2451  CA  GLN A 323     120.998  36.135  35.397  1.00208.46           C  
ANISOU 2451  CA  GLN A 323    22285  26877  30042  -3887   -931  -1066       C  
ATOM   2452  C   GLN A 323     119.978  36.738  36.363  1.00248.42           C  
ANISOU 2452  C   GLN A 323    29850  31753  32785  -1850   -541   -330       C  
ATOM   2453  O   GLN A 323     119.128  36.028  36.898  1.00206.19           O  
ANISOU 2453  O   GLN A 323    21364  25738  31241  -3727  -1070  -2163       O  
ATOM   2454  CB  GLN A 323     120.376  35.918  34.010  1.00209.78           C  
ANISOU 2454  CB  GLN A 323    22573  26966  30169  -3795   -660   -982       C  
TER    2455      GLN A 323                                                      
ATOM   2456  N   VAL B  10     102.138  42.810  26.237  1.00 72.97           N  
ANISOU 2456  N   VAL B  10     8653   7694  11379  -2604   3644  -2052       N  
ATOM   2457  CA  VAL B  10     101.495  44.109  26.462  1.00 72.29           C  
ANISOU 2457  CA  VAL B  10     8942   7491  11032  -2783   3651  -1722       C  
ATOM   2458  C   VAL B  10     101.602  44.526  27.942  1.00 73.75           C  
ANISOU 2458  C   VAL B  10     8849   7652  11520  -2651   3187  -1721       C  
ATOM   2459  O   VAL B  10     101.407  43.687  28.828  1.00 74.23           O  
ANISOU 2459  O   VAL B  10     8752   7765  11688  -2325   2693  -1736       O  
ATOM   2460  CB  VAL B  10     100.034  44.100  25.921  1.00 76.29           C  
ANISOU 2460  CB  VAL B  10    10117   7956  10915  -2707   3530  -1298       C  
ATOM   2461  CG1 VAL B  10      99.218  45.284  26.431  1.00 75.94           C  
ANISOU 2461  CG1 VAL B  10    10416   7790  10646  -2766   3347   -967       C  
ATOM   2462  CG2 VAL B  10     100.019  44.064  24.398  1.00 76.31           C  
ANISOU 2462  CG2 VAL B  10    10500   7931  10564  -2899   4042  -1299       C  
ATOM   2463  N   GLN B  11     101.927  45.817  28.190  1.00 67.14           N  
ANISOU 2463  N   GLN B  11     7996   6710  10804  -2911   3359  -1713       N  
ATOM   2464  CA  GLN B  11     102.029  46.433  29.518  1.00 65.87           C  
ANISOU 2464  CA  GLN B  11     7633   6502  10893  -2825   2959  -1718       C  
ATOM   2465  C   GLN B  11     100.894  47.475  29.675  1.00 66.22           C  
ANISOU 2465  C   GLN B  11     8217   6431  10511  -2878   2846  -1288       C  
ATOM   2466  O   GLN B  11     100.802  48.398  28.863  1.00 66.67           O  
ANISOU 2466  O   GLN B  11     8608   6368  10355  -3172   3242  -1153       O  
ATOM   2467  CB  GLN B  11     103.436  47.060  29.717  1.00 67.45           C  
ANISOU 2467  CB  GLN B  11     7303   6658  11666  -3075   3219  -2132       C  
ATOM   2468  CG  GLN B  11     103.577  48.070  30.873  1.00 92.17           C  
ANISOU 2468  CG  GLN B  11    10302   9695  15022  -3079   2897  -2140       C  
ATOM   2469  CD  GLN B  11     103.495  47.454  32.256  1.00121.72           C  
ANISOU 2469  CD  GLN B  11    13812  13497  18940  -2661   2209  -2225       C  
ATOM   2470  OE1 GLN B  11     104.274  46.561  32.619  1.00119.59           O  
ANISOU 2470  OE1 GLN B  11    13108  13305  19026  -2450   2008  -2571       O  
ATOM   2471  NE2 GLN B  11     102.559  47.936  33.069  1.00114.21           N  
ANISOU 2471  NE2 GLN B  11    13177  12488  17731  -2525   1832  -1926       N  
ATOM   2472  N   LEU B  12     100.028  47.318  30.698  1.00 58.14           N  
ANISOU 2472  N   LEU B  12     7308   5425   9358  -2591   2322  -1086       N  
ATOM   2473  CA  LEU B  12      98.906  48.235  30.928  1.00 55.74           C  
ANISOU 2473  CA  LEU B  12     7453   5022   8703  -2592   2171   -731       C  
ATOM   2474  C   LEU B  12      99.186  49.254  32.018  1.00 57.81           C  
ANISOU 2474  C   LEU B  12     7575   5196   9195  -2631   1978   -776       C  
ATOM   2475  O   LEU B  12      99.942  48.973  32.951  1.00 57.87           O  
ANISOU 2475  O   LEU B  12     7165   5244   9578  -2518   1747  -1038       O  
ATOM   2476  CB  LEU B  12      97.594  47.488  31.239  1.00 55.17           C  
ANISOU 2476  CB  LEU B  12     7635   5011   8317  -2291   1797   -485       C  
ATOM   2477  CG  LEU B  12      97.012  46.553  30.173  1.00 58.62           C  
ANISOU 2477  CG  LEU B  12     8296   5510   8467  -2228   1908   -397       C  
ATOM   2478  CD1 LEU B  12      95.830  45.800  30.728  1.00 57.96           C  
ANISOU 2478  CD1 LEU B  12     8355   5467   8200  -1955   1526   -221       C  
ATOM   2479  CD2 LEU B  12      96.593  47.311  28.913  1.00 60.61           C  
ANISOU 2479  CD2 LEU B  12     8997   5664   8366  -2438   2234   -227       C  
ATOM   2480  N   VAL B  13      98.558  50.438  31.899  1.00 52.46           N  
ANISOU 2480  N   VAL B  13     7273   4378   8282  -2765   2031   -536       N  
ATOM   2481  CA  VAL B  13      98.690  51.553  32.840  1.00 51.92           C  
ANISOU 2481  CA  VAL B  13     7153   4194   8380  -2818   1863   -551       C  
ATOM   2482  C   VAL B  13      97.386  52.373  32.863  1.00 55.01           C  
ANISOU 2482  C   VAL B  13     8047   4474   8378  -2761   1714   -205       C  
ATOM   2483  O   VAL B  13      96.890  52.758  31.801  1.00 54.52           O  
ANISOU 2483  O   VAL B  13     8396   4316   8003  -2885   1947    -10       O  
ATOM   2484  CB  VAL B  13      99.988  52.399  32.611  1.00 55.49           C  
ANISOU 2484  CB  VAL B  13     7338   4529   9218  -3176   2232   -818       C  
ATOM   2485  CG1 VAL B  13     100.073  52.966  31.199  1.00 55.73           C  
ANISOU 2485  CG1 VAL B  13     7727   4421   9028  -3523   2798   -702       C  
ATOM   2486  CG2 VAL B  13     100.157  53.487  33.661  1.00 54.74           C  
ANISOU 2486  CG2 VAL B  13     7155   4308   9337  -3211   2004   -876       C  
ATOM   2487  N   GLU B  14      96.808  52.573  34.067  1.00 51.29           N  
ANISOU 2487  N   GLU B  14     7565   4013   7911  -2541   1306   -150       N  
ATOM   2488  CA  GLU B  14      95.544  53.292  34.254  1.00 51.51           C  
ANISOU 2488  CA  GLU B  14     7985   3951   7634  -2439   1122    113       C  
ATOM   2489  C   GLU B  14      95.762  54.771  34.581  1.00 58.52           C  
ANISOU 2489  C   GLU B  14     8975   4641   8618  -2604   1137    115       C  
ATOM   2490  O   GLU B  14      96.722  55.116  35.267  1.00 60.42           O  
ANISOU 2490  O   GLU B  14     8904   4855   9198  -2686   1102   -109       O  
ATOM   2491  CB  GLU B  14      94.644  52.636  35.332  1.00 52.62           C  
ANISOU 2491  CB  GLU B  14     8100   4207   7685  -2112    733    172       C  
ATOM   2492  CG  GLU B  14      94.300  51.161  35.141  1.00 55.26           C  
ANISOU 2492  CG  GLU B  14     8364   4699   7932  -1941    684    180       C  
ATOM   2493  CD  GLU B  14      95.294  50.166  35.715  1.00 67.04           C  
ANISOU 2493  CD  GLU B  14     9494   6288   9688  -1852    594    -49       C  
ATOM   2494  OE1 GLU B  14      94.998  48.949  35.702  1.00 49.21           O  
ANISOU 2494  OE1 GLU B  14     7209   4126   7362  -1692    517    -40       O  
ATOM   2495  OE2 GLU B  14      96.378  50.597  36.166  1.00 60.56           O  
ANISOU 2495  OE2 GLU B  14     8414   5430   9165  -1934    580   -262       O  
ATOM   2496  N   SER B  15      94.860  55.637  34.092  1.00 54.70           N  
ANISOU 2496  N   SER B  15     8935   3999   7849  -2631   1153    344       N  
ATOM   2497  CA  SER B  15      94.868  57.085  34.299  1.00 54.17           C  
ANISOU 2497  CA  SER B  15     9074   3696   7813  -2768   1151    389       C  
ATOM   2498  C   SER B  15      93.493  57.560  34.737  1.00 56.32           C  
ANISOU 2498  C   SER B  15     9639   3919   7841  -2514    823    569       C  
ATOM   2499  O   SER B  15      92.532  56.800  34.653  1.00 55.70           O  
ANISOU 2499  O   SER B  15     9624   3975   7566  -2286    670    662       O  
ATOM   2500  CB  SER B  15      95.304  57.809  33.031  1.00 58.59           C  
ANISOU 2500  CB  SER B  15     9964   4027   8270  -3099   1567    469       C  
ATOM   2501  OG  SER B  15      96.716  57.788  32.935  1.00 71.67           O  
ANISOU 2501  OG  SER B  15    11272   5683  10275  -3393   1908    225       O  
ATOM   2502  N   GLY B  16      93.415  58.805  35.204  1.00 52.57           N  
ANISOU 2502  N   GLY B  16     9314   3244   7416  -2562    728    583       N  
ATOM   2503  CA  GLY B  16      92.189  59.401  35.714  1.00 52.13           C  
ANISOU 2503  CA  GLY B  16     9491   3123   7192  -2319    420    694       C  
ATOM   2504  C   GLY B  16      91.997  58.959  37.144  1.00 58.24           C  
ANISOU 2504  C   GLY B  16     9955   4076   8098  -2095    148    562       C  
ATOM   2505  O   GLY B  16      92.828  58.221  37.693  1.00 57.05           O  
ANISOU 2505  O   GLY B  16     9464   4071   8141  -2110    154    404       O  
ATOM   2506  N   GLY B  17      90.909  59.390  37.763  1.00 57.30           N  
ANISOU 2506  N   GLY B  17     9974   3932   7868  -1873    -94    608       N  
ATOM   2507  CA  GLY B  17      90.651  58.963  39.138  1.00 57.31           C  
ANISOU 2507  CA  GLY B  17     9766   4082   7927  -1665   -303    492       C  
ATOM   2508  C   GLY B  17      91.334  59.847  40.160  1.00 58.80           C  
ANISOU 2508  C   GLY B  17     9878   4161   8301  -1709   -423    339       C  
ATOM   2509  O   GLY B  17      92.482  60.271  39.982  1.00 58.53           O  
ANISOU 2509  O   GLY B  17     9737   4022   8477  -1937   -317    241       O  
ATOM   2510  N   GLY B  18      90.598  60.122  41.218  1.00 51.73           N  
ANISOU 2510  N   GLY B  18     9032   3282   7340  -1495   -630    293       N  
ATOM   2511  CA  GLY B  18      91.015  60.966  42.319  1.00 50.37           C  
ANISOU 2511  CA  GLY B  18     8839   3008   7290  -1471   -803    135       C  
ATOM   2512  C   GLY B  18      89.798  61.187  43.172  1.00 53.30           C  
ANISOU 2512  C   GLY B  18     9353   3404   7496  -1215   -953    131       C  
ATOM   2513  O   GLY B  18      88.977  60.273  43.318  1.00 54.19           O  
ANISOU 2513  O   GLY B  18     9451   3680   7459  -1061   -924    181       O  
ATOM   2514  N   LEU B  19      89.660  62.395  43.717  1.00 47.98           N  
ANISOU 2514  N   LEU B  19     8809   2554   6866  -1185  -1085     52       N  
ATOM   2515  CA  LEU B  19      88.516  62.751  44.545  1.00 46.91           C  
ANISOU 2515  CA  LEU B  19     8800   2421   6601   -945  -1201      1       C  
ATOM   2516  C   LEU B  19      87.406  63.294  43.653  1.00 49.36           C  
ANISOU 2516  C   LEU B  19     9276   2630   6848   -884  -1180    114       C  
ATOM   2517  O   LEU B  19      87.662  64.084  42.754  1.00 50.36           O  
ANISOU 2517  O   LEU B  19     9556   2553   7027  -1022  -1168    200       O  
ATOM   2518  CB  LEU B  19      88.911  63.768  45.656  1.00 46.30           C  
ANISOU 2518  CB  LEU B  19     8788   2199   6604   -906  -1388   -180       C  
ATOM   2519  CG  LEU B  19      87.849  64.143  46.718  1.00 50.03           C  
ANISOU 2519  CG  LEU B  19     9389   2686   6936   -651  -1486   -291       C  
ATOM   2520  CD1 LEU B  19      87.514  62.968  47.644  1.00 49.50           C  
ANISOU 2520  CD1 LEU B  19     9287   2843   6679   -497  -1433   -331       C  
ATOM   2521  CD2 LEU B  19      88.305  65.336  47.559  1.00 53.78           C  
ANISOU 2521  CD2 LEU B  19     9964   2970   7502   -634  -1684   -471       C  
ATOM   2522  N   VAL B  20      86.190  62.850  43.904  1.00 43.91           N  
ANISOU 2522  N   VAL B  20     8569   2062   6051   -677  -1176     94       N  
ATOM   2523  CA  VAL B  20      84.983  63.256  43.205  1.00 44.26           C  
ANISOU 2523  CA  VAL B  20     8714   2029   6072   -543  -1228    124       C  
ATOM   2524  C   VAL B  20      83.847  63.310  44.248  1.00 48.66           C  
ANISOU 2524  C   VAL B  20     9209   2666   6615   -305  -1255    -54       C  
ATOM   2525  O   VAL B  20      83.836  62.498  45.177  1.00 47.45           O  
ANISOU 2525  O   VAL B  20     8948   2688   6393   -273  -1140   -122       O  
ATOM   2526  CB  VAL B  20      84.686  62.346  41.970  1.00 49.10           C  
ANISOU 2526  CB  VAL B  20     9288   2737   6630   -584  -1136    264       C  
ATOM   2527  CG1 VAL B  20      84.638  60.872  42.337  1.00 49.25           C  
ANISOU 2527  CG1 VAL B  20     9086   3022   6607   -578   -984    254       C  
ATOM   2528  CG2 VAL B  20      83.418  62.760  41.239  1.00 49.14           C  
ANISOU 2528  CG2 VAL B  20     9402   2642   6626   -401  -1275    252       C  
ATOM   2529  N   GLN B  21      82.932  64.293  44.123  1.00 45.52           N  
ANISOU 2529  N   GLN B  21     8909   2112   6275   -138  -1400   -144       N  
ATOM   2530  CA  GLN B  21      81.795  64.455  45.030  1.00 45.88           C  
ANISOU 2530  CA  GLN B  21     8863   2216   6352     87  -1393   -365       C  
ATOM   2531  C   GLN B  21      80.630  63.522  44.640  1.00 50.62           C  
ANISOU 2531  C   GLN B  21     9250   2987   6996    191  -1283   -426       C  
ATOM   2532  O   GLN B  21      80.458  63.269  43.446  1.00 48.49           O  
ANISOU 2532  O   GLN B  21     8982   2692   6750    175  -1359   -318       O  
ATOM   2533  CB  GLN B  21      81.337  65.934  45.115  1.00 47.94           C  
ANISOU 2533  CB  GLN B  21     9284   2223   6706    247  -1619   -493       C  
ATOM   2534  CG  GLN B  21      80.732  66.556  43.840  1.00 72.42           C  
ANISOU 2534  CG  GLN B  21    12516   5122   9879    361  -1839   -446       C  
ATOM   2535  CD  GLN B  21      79.812  67.709  44.191  1.00105.98           C  
ANISOU 2535  CD  GLN B  21    16856   9166  14246    615  -2061   -659       C  
ATOM   2536  OE1 GLN B  21      78.755  67.524  44.808  1.00106.97           O  
ANISOU 2536  OE1 GLN B  21    16767   9405  14470    817  -2014   -916       O  
ATOM   2537  NE2 GLN B  21      80.190  68.930  43.820  1.00 96.88           N  
ANISOU 2537  NE2 GLN B  21    16029   7684  13097    605  -2283   -576       N  
ATOM   2538  N   PRO B  22      79.847  62.971  45.615  1.00 49.04           N  
ANISOU 2538  N   PRO B  22     8882   2949   6804    278  -1082   -609       N  
ATOM   2539  CA  PRO B  22      78.690  62.135  45.243  1.00 48.63           C  
ANISOU 2539  CA  PRO B  22     8577   3033   6867    348   -953   -718       C  
ATOM   2540  C   PRO B  22      77.827  62.860  44.204  1.00 53.31           C  
ANISOU 2540  C   PRO B  22     9126   3486   7645    533  -1231   -815       C  
ATOM   2541  O   PRO B  22      77.427  63.996  44.424  1.00 53.80           O  
ANISOU 2541  O   PRO B  22     9256   3387   7798    707  -1415   -966       O  
ATOM   2542  CB  PRO B  22      77.950  61.951  46.576  1.00 49.94           C  
ANISOU 2542  CB  PRO B  22     8636   3300   7040    418   -685   -960       C  
ATOM   2543  CG  PRO B  22      79.014  62.079  47.606  1.00 53.97           C  
ANISOU 2543  CG  PRO B  22     9385   3796   7323    332   -635   -874       C  
ATOM   2544  CD  PRO B  22      79.917  63.152  47.084  1.00 50.14           C  
ANISOU 2544  CD  PRO B  22     9080   3123   6848    316   -951   -753       C  
ATOM   2545  N   GLY B  23      77.639  62.232  43.054  1.00 49.67           N  
ANISOU 2545  N   GLY B  23     8600   3057   7214    511  -1305   -723       N  
ATOM   2546  CA  GLY B  23      76.897  62.807  41.943  1.00 49.13           C  
ANISOU 2546  CA  GLY B  23     8563   2835   7270    711  -1637   -798       C  
ATOM   2547  C   GLY B  23      77.796  63.161  40.778  1.00 52.13           C  
ANISOU 2547  C   GLY B  23     9306   3033   7468    622  -1841   -509       C  
ATOM   2548  O   GLY B  23      77.321  63.284  39.640  1.00 51.96           O  
ANISOU 2548  O   GLY B  23     9403   2885   7455    759  -2110   -503       O  
ATOM   2549  N   GLY B  24      79.093  63.291  41.077  1.00 47.05           N  
ANISOU 2549  N   GLY B  24     8845   2368   6662    392  -1703   -296       N  
ATOM   2550  CA  GLY B  24      80.152  63.634  40.133  1.00 46.84           C  
ANISOU 2550  CA  GLY B  24     9151   2169   6475    223  -1767    -34       C  
ATOM   2551  C   GLY B  24      80.528  62.575  39.110  1.00 51.36           C  
ANISOU 2551  C   GLY B  24     9734   2848   6935     81  -1670    136       C  
ATOM   2552  O   GLY B  24      79.971  61.475  39.100  1.00 51.36           O  
ANISOU 2552  O   GLY B  24     9469   3058   6989    117  -1579     60       O  
ATOM   2553  N   SER B  25      81.494  62.919  38.240  1.00 48.43           N  
ANISOU 2553  N   SER B  25     9679   2311   6412    -99  -1657    354       N  
ATOM   2554  CA  SER B  25      81.982  62.094  37.136  1.00 48.91           C  
ANISOU 2554  CA  SER B  25     9841   2418   6327   -245  -1553    522       C  
ATOM   2555  C   SER B  25      83.498  61.984  37.110  1.00 50.53           C  
ANISOU 2555  C   SER B  25    10103   2625   6471   -565  -1289    677       C  
ATOM   2556  O   SER B  25      84.196  62.912  37.509  1.00 49.97           O  
ANISOU 2556  O   SER B  25    10163   2388   6436   -686  -1262    702       O  
ATOM   2557  CB  SER B  25      81.553  62.684  35.792  1.00 55.62           C  
ANISOU 2557  CB  SER B  25    11118   2996   7017   -127  -1802    608       C  
ATOM   2558  OG  SER B  25      80.233  63.199  35.775  1.00 73.52           O  
ANISOU 2558  OG  SER B  25    13322   5232   9382    210  -2123    416       O  
ATOM   2559  N   LEU B  26      83.994  60.872  36.563  1.00 45.04           N  
ANISOU 2559  N   LEU B  26     9306   2095   5711   -700  -1106    754       N  
ATOM   2560  CA  LEU B  26      85.405  60.590  36.314  1.00 44.20           C  
ANISOU 2560  CA  LEU B  26     9201   2009   5584   -993   -843    856       C  
ATOM   2561  C   LEU B  26      85.505  59.737  35.050  1.00 46.59           C  
ANISOU 2561  C   LEU B  26     9605   2366   5730  -1055   -738    954       C  
ATOM   2562  O   LEU B  26      84.653  58.874  34.802  1.00 45.03           O  
ANISOU 2562  O   LEU B  26     9282   2318   5510   -894   -829    904       O  
ATOM   2563  CB  LEU B  26      86.085  59.833  37.468  1.00 44.40           C  
ANISOU 2563  CB  LEU B  26     8848   2261   5761  -1068   -707    762       C  
ATOM   2564  CG  LEU B  26      86.453  60.563  38.749  1.00 49.65           C  
ANISOU 2564  CG  LEU B  26     9429   2879   6557  -1069   -762    657       C  
ATOM   2565  CD1 LEU B  26      87.018  59.583  39.740  1.00 49.66           C  
ANISOU 2565  CD1 LEU B  26     9134   3100   6637  -1085   -685    569       C  
ATOM   2566  CD2 LEU B  26      87.486  61.653  38.503  1.00 52.53           C  
ANISOU 2566  CD2 LEU B  26     9976   3005   6978  -1290   -703    696       C  
ATOM   2567  N   ARG B  27      86.541  59.990  34.255  1.00 42.69           N  
ANISOU 2567  N   ARG B  27     9340   1740   5140  -1303   -526   1069       N  
ATOM   2568  CA  ARG B  27      86.824  59.231  33.058  1.00 42.26           C  
ANISOU 2568  CA  ARG B  27     9422   1724   4910  -1396   -366   1153       C  
ATOM   2569  C   ARG B  27      88.171  58.562  33.270  1.00 46.59           C  
ANISOU 2569  C   ARG B  27     9684   2419   5600  -1659    -39   1113       C  
ATOM   2570  O   ARG B  27      89.195  59.246  33.384  1.00 46.76           O  
ANISOU 2570  O   ARG B  27     9739   2306   5720  -1896    150   1110       O  
ATOM   2571  CB  ARG B  27      86.805  60.096  31.773  1.00 42.04           C  
ANISOU 2571  CB  ARG B  27    10005   1376   4594  -1452   -365   1309       C  
ATOM   2572  CG  ARG B  27      86.837  59.190  30.520  1.00 52.08           C  
ANISOU 2572  CG  ARG B  27    11458   2707   5624  -1477   -249   1371       C  
ATOM   2573  CD  ARG B  27      86.652  59.918  29.216  1.00 59.51           C  
ANISOU 2573  CD  ARG B  27    13101   3319   6191  -1484   -279   1530       C  
ATOM   2574  NE  ARG B  27      87.870  60.626  28.833  1.00 67.37           N  
ANISOU 2574  NE  ARG B  27    14390   4092   7117  -1851    126   1638       N  
ATOM   2575  CZ  ARG B  27      88.109  61.099  27.617  1.00 84.96           C  
ANISOU 2575  CZ  ARG B  27    17281   6021   8977  -1981    290   1798       C  
ATOM   2576  NH1 ARG B  27      87.224  60.925  26.643  1.00 78.95           N  
ANISOU 2576  NH1 ARG B  27    16988   5153   7856  -1732     17   1870       N  
ATOM   2577  NH2 ARG B  27      89.242  61.742  27.359  1.00 71.68           N  
ANISOU 2577  NH2 ARG B  27    15821   4129   7286  -2368    735   1869       N  
ATOM   2578  N   LEU B  28      88.167  57.230  33.371  1.00 43.16           N  
ANISOU 2578  N   LEU B  28     8940   2242   5215  -1609     10   1049       N  
ATOM   2579  CA  LEU B  28      89.409  56.489  33.543  1.00 43.65           C  
ANISOU 2579  CA  LEU B  28     8709   2440   5435  -1803    266    972       C  
ATOM   2580  C   LEU B  28      89.950  56.067  32.180  1.00 49.73           C  
ANISOU 2580  C   LEU B  28     9667   3185   6044  -1967    531   1028       C  
ATOM   2581  O   LEU B  28      89.186  55.886  31.228  1.00 48.97           O  
ANISOU 2581  O   LEU B  28     9869   3044   5694  -1860    455   1116       O  
ATOM   2582  CB  LEU B  28      89.242  55.274  34.478  1.00 43.91           C  
ANISOU 2582  CB  LEU B  28     8344   2728   5613  -1660    176    864       C  
ATOM   2583  CG  LEU B  28      88.588  55.522  35.850  1.00 47.72           C  
ANISOU 2583  CG  LEU B  28     8696   3249   6185  -1478    -49    806       C  
ATOM   2584  CD1 LEU B  28      88.486  54.252  36.625  1.00 46.99           C  
ANISOU 2584  CD1 LEU B  28     8336   3358   6161  -1367    -77    732       C  
ATOM   2585  CD2 LEU B  28      89.335  56.550  36.658  1.00 47.02           C  
ANISOU 2585  CD2 LEU B  28     8575   3050   6241  -1567    -71    745       C  
ATOM   2586  N   SER B  29      91.265  55.949  32.079  1.00 48.00           N  
ANISOU 2586  N   SER B  29     9280   2979   5979  -2219    837    945       N  
ATOM   2587  CA  SER B  29      91.900  55.553  30.842  1.00 48.87           C  
ANISOU 2587  CA  SER B  29     9543   3070   5954  -2403   1168    960       C  
ATOM   2588  C   SER B  29      92.774  54.341  31.090  1.00 52.54           C  
ANISOU 2588  C   SER B  29     9537   3765   6661  -2448   1316    777       C  
ATOM   2589  O   SER B  29      93.358  54.225  32.161  1.00 51.02           O  
ANISOU 2589  O   SER B  29     8954   3655   6777  -2449   1247    629       O  
ATOM   2590  CB  SER B  29      92.687  56.724  30.253  1.00 54.28           C  
ANISOU 2590  CB  SER B  29    10556   3481   6586  -2717   1492   1012       C  
ATOM   2591  OG  SER B  29      94.075  56.461  30.105  1.00 69.30           O  
ANISOU 2591  OG  SER B  29    12123   5423   8784  -3004   1861    830       O  
ATOM   2592  N   CYS B  30      92.798  53.402  30.129  1.00 51.20           N  
ANISOU 2592  N   CYS B  30     9426   3687   6340  -2444   1463    773       N  
ATOM   2593  CA  CYS B  30      93.613  52.178  30.161  1.00 50.37           C  
ANISOU 2593  CA  CYS B  30     8920   3777   6440  -2467   1611    587       C  
ATOM   2594  C   CYS B  30      94.406  52.196  28.869  1.00 56.94           C  
ANISOU 2594  C   CYS B  30     9948   4533   7155  -2727   2066    553       C  
ATOM   2595  O   CYS B  30      93.830  52.045  27.790  1.00 55.69           O  
ANISOU 2595  O   CYS B  30    10211   4316   6634  -2698   2124    681       O  
ATOM   2596  CB  CYS B  30      92.748  50.926  30.284  1.00 49.70           C  
ANISOU 2596  CB  CYS B  30     8740   3867   6278  -2197   1358    598       C  
ATOM   2597  SG  CYS B  30      93.675  49.361  30.257  1.00 52.93           S  
ANISOU 2597  SG  CYS B  30     8724   4473   6914  -2181   1492    374       S  
ATOM   2598  N   GLU B  31      95.708  52.490  28.975  1.00 56.95           N  
ANISOU 2598  N   GLU B  31     9671   4507   7459  -2989   2394    365       N  
ATOM   2599  CA  GLU B  31      96.600  52.582  27.823  1.00 58.84           C  
ANISOU 2599  CA  GLU B  31    10052   4661   7643  -3299   2937    284       C  
ATOM   2600  C   GLU B  31      97.608  51.459  27.810  1.00 67.35           C  
ANISOU 2600  C   GLU B  31    10599   5937   9055  -3329   3130    -22       C  
ATOM   2601  O   GLU B  31      98.015  50.981  28.871  1.00 67.46           O  
ANISOU 2601  O   GLU B  31    10096   6088   9448  -3189   2876   -208       O  
ATOM   2602  CB  GLU B  31      97.352  53.928  27.831  1.00 60.16           C  
ANISOU 2602  CB  GLU B  31    10332   4586   7941  -3648   3260    265       C  
ATOM   2603  N   ALA B  32      98.030  51.056  26.610  1.00 67.61           N  
ANISOU 2603  N   ALA B  32    10790   5964   8933  -3497   3570    -89       N  
ATOM   2604  CA  ALA B  32      99.073  50.055  26.443  1.00 69.93           C  
ANISOU 2604  CA  ALA B  32    10589   6423   9558  -3548   3825   -423       C  
ATOM   2605  C   ALA B  32     100.214  50.741  25.691  1.00 80.79           C  
ANISOU 2605  C   ALA B  32    11986   7655  11054  -3991   4507   -595       C  
ATOM   2606  O   ALA B  32     100.405  50.547  24.497  1.00 80.56           O  
ANISOU 2606  O   ALA B  32    12367   7554  10689  -4160   4947   -549       O  
ATOM   2607  CB  ALA B  32      98.545  48.852  25.691  1.00 70.60           C  
ANISOU 2607  CB  ALA B  32    10825   6640   9358  -3342   3767   -391       C  
ATOM   2608  N   SER B  33     100.925  51.604  26.428  1.00 83.11           N  
ANISOU 2608  N   SER B  33    11870   7886  11824  -4189   4599   -800       N  
ATOM   2609  CA  SER B  33     102.041  52.499  26.085  1.00 85.93           C  
ANISOU 2609  CA  SER B  33    12131   8073  12444  -4663   5242  -1015       C  
ATOM   2610  C   SER B  33     102.786  52.222  24.749  1.00 94.93           C  
ANISOU 2610  C   SER B  33    13292   9229  13547  -4929   5939  -1227       C  
ATOM   2611  O   SER B  33     103.063  53.173  24.012  1.00 95.53           O  
ANISOU 2611  O   SER B  33    13681   9084  13533  -5359   6578  -1233       O  
ATOM   2612  CB  SER B  33     103.047  52.539  27.235  1.00 91.12           C  
ANISOU 2612  CB  SER B  33    12033   8777  13811  -4715   5107  -1384       C  
ATOM   2613  OG  SER B  33     102.465  52.122  28.465  1.00101.84           O  
ANISOU 2613  OG  SER B  33    13292  10191  15209  -4373   4405  -1254       O  
ATOM   2614  N   GLY B  34     103.106  50.956  24.461  1.00 93.31           N  
ANISOU 2614  N   GLY B  34    12794   9260  13398  -4684   5834  -1400       N  
ATOM   2615  CA  GLY B  34     103.833  50.576  23.254  1.00 93.52           C  
ANISOU 2615  CA  GLY B  34    12794   9332  13407  -4884   6458  -1644       C  
ATOM   2616  C   GLY B  34     103.038  50.004  22.091  1.00 98.73           C  
ANISOU 2616  C   GLY B  34    14285   9910  13318  -4879   6670  -1330       C  
ATOM   2617  O   GLY B  34     103.555  50.001  20.968  1.00 99.35           O  
ANISOU 2617  O   GLY B  34    14789   9811  13147  -5253   7360  -1333       O  
ATOM   2618  N   TYR B  35     101.799  49.489  22.323  1.00 94.92           N  
ANISOU 2618  N   TYR B  35    14051   9541  12473  -4461   6091  -1083       N  
ATOM   2619  CA  TYR B  35     101.009  48.878  21.238  1.00 94.43           C  
ANISOU 2619  CA  TYR B  35    14743   9416  11720  -4385   6171   -833       C  
ATOM   2620  C   TYR B  35      99.462  49.000  21.368  1.00 96.12           C  
ANISOU 2620  C   TYR B  35    15469   9576  11478  -4055   5511   -421       C  
ATOM   2621  O   TYR B  35      98.938  49.399  22.405  1.00 94.76           O  
ANISOU 2621  O   TYR B  35    15087   9415  11504  -3900   5030   -308       O  
ATOM   2622  CB  TYR B  35     101.409  47.397  21.056  1.00 95.71           C  
ANISOU 2622  CB  TYR B  35    14645   9789  11932  -4234   6280  -1101       C  
ATOM   2623  N   THR B  36      98.750  48.634  20.278  1.00 91.32           N  
ANISOU 2623  N   THR B  36    15536   8899  10262  -3947   5504   -234       N  
ATOM   2624  CA  THR B  36      97.287  48.650  20.138  1.00 89.71           C  
ANISOU 2624  CA  THR B  36    15842   8632   9612  -3627   4912     85       C  
ATOM   2625  C   THR B  36      96.578  47.551  20.956  1.00 89.12           C  
ANISOU 2625  C   THR B  36    15289   8798   9775  -3233   4286     40       C  
ATOM   2626  O   THR B  36      97.069  46.417  21.050  1.00 88.70           O  
ANISOU 2626  O   THR B  36    14767   8941   9992  -3153   4331   -207       O  
ATOM   2627  CB  THR B  36      96.883  48.602  18.634  1.00 96.44           C  
ANISOU 2627  CB  THR B  36    17565   9320   9760  -3633   5105    227       C  
ATOM   2628  OG1 THR B  36      95.459  48.579  18.512  1.00 95.85           O  
ANISOU 2628  OG1 THR B  36    17917   9182   9321  -3289   4465    472       O  
ATOM   2629  CG2 THR B  36      97.482  47.405  17.879  1.00 94.04           C  
ANISOU 2629  CG2 THR B  36    17155   9176   9400  -3619   5411    -26       C  
ATOM   2630  N   LEU B  37      95.391  47.888  21.497  1.00 81.75           N  
ANISOU 2630  N   LEU B  37    14514   7822   8725  -2992   3723    268       N  
ATOM   2631  CA  LEU B  37      94.553  46.948  22.245  1.00 80.06           C  
ANISOU 2631  CA  LEU B  37    13948   7787   8686  -2653   3170    254       C  
ATOM   2632  C   LEU B  37      93.495  46.303  21.311  1.00 82.05           C  
ANISOU 2632  C   LEU B  37    14641   8027   8508  -2424   2916    325       C  
ATOM   2633  O   LEU B  37      92.428  45.880  21.767  1.00 80.82           O  
ANISOU 2633  O   LEU B  37    14392   7930   8385  -2159   2421    378       O  
ATOM   2634  CB  LEU B  37      93.900  47.647  23.457  1.00 79.58           C  
ANISOU 2634  CB  LEU B  37    13720   7699   8817  -2539   2753    396       C  
ATOM   2635  CG  LEU B  37      94.835  48.124  24.571  1.00 83.12           C  
ANISOU 2635  CG  LEU B  37    13667   8181   9733  -2690   2866    286       C  
ATOM   2636  CD1 LEU B  37      94.078  48.935  25.603  1.00 82.70           C  
ANISOU 2636  CD1 LEU B  37    13597   8067   9757  -2574   2473    444       C  
ATOM   2637  CD2 LEU B  37      95.537  46.962  25.241  1.00 85.29           C  
ANISOU 2637  CD2 LEU B  37    13315   8663  10428  -2607   2842     32       C  
ATOM   2638  N   ALA B  38      93.838  46.198  20.004  1.00 77.30           N  
ANISOU 2638  N   ALA B  38    14506   7344   7521  -2542   3284    289       N  
ATOM   2639  CA  ALA B  38      93.000  45.692  18.919  1.00 76.25           C  
ANISOU 2639  CA  ALA B  38    14899   7162   6912  -2352   3096    323       C  
ATOM   2640  C   ALA B  38      92.542  44.258  19.084  1.00 77.23           C  
ANISOU 2640  C   ALA B  38    14645   7482   7219  -2097   2771    164       C  
ATOM   2641  O   ALA B  38      91.339  44.000  19.077  1.00 76.57           O  
ANISOU 2641  O   ALA B  38    14677   7385   7031  -1842   2265    227       O  
ATOM   2642  CB  ALA B  38      93.704  45.872  17.579  1.00 76.96           C  
ANISOU 2642  CB  ALA B  38    15549   7123   6567  -2573   3663    285       C  
ATOM   2643  N   ASN B  39      93.499  43.328  19.218  1.00 71.93           N  
ANISOU 2643  N   ASN B  39    13512   6971   6847  -2168   3061    -70       N  
ATOM   2644  CA  ASN B  39      93.256  41.889  19.350  1.00 70.03           C  
ANISOU 2644  CA  ASN B  39    12923   6885   6800  -1958   2824   -245       C  
ATOM   2645  C   ASN B  39      92.913  41.457  20.784  1.00 67.76           C  
ANISOU 2645  C   ASN B  39    12055   6702   6989  -1812   2437   -243       C  
ATOM   2646  O   ASN B  39      92.756  40.261  21.027  1.00 67.19           O  
ANISOU 2646  O   ASN B  39    11692   6723   7113  -1659   2260   -379       O  
ATOM   2647  CB  ASN B  39      94.472  41.103  18.821  1.00 73.76           C  
ANISOU 2647  CB  ASN B  39    13189   7453   7385  -2077   3302   -520       C  
ATOM   2648  CG  ASN B  39      94.645  41.123  17.321  1.00104.11           C  
ANISOU 2648  CG  ASN B  39    17640  11207  10711  -2176   3680   -565       C  
ATOM   2649  OD1 ASN B  39      94.612  40.078  16.664  1.00101.06           O  
ANISOU 2649  OD1 ASN B  39    17344  10872  10181  -2047   3662   -725       O  
ATOM   2650  ND2 ASN B  39      94.859  42.301  16.742  1.00 98.92           N  
ANISOU 2650  ND2 ASN B  39    17455  10389   9740  -2414   4050   -432       N  
ATOM   2651  N   TYR B  40      92.758  42.419  21.713  1.00 60.85           N  
ANISOU 2651  N   TYR B  40    11072   5785   6265  -1858   2309    -88       N  
ATOM   2652  CA  TYR B  40      92.455  42.166  23.125  1.00 59.52           C  
ANISOU 2652  CA  TYR B  40    10443   5688   6486  -1740   1989    -69       C  
ATOM   2653  C   TYR B  40      91.044  42.565  23.556  1.00 59.99           C  
ANISOU 2653  C   TYR B  40    10646   5688   6459  -1585   1555    105       C  
ATOM   2654  O   TYR B  40      90.444  43.464  22.977  1.00 59.83           O  
ANISOU 2654  O   TYR B  40    11052   5550   6133  -1585   1479    238       O  
ATOM   2655  CB  TYR B  40      93.454  42.906  24.030  1.00 60.89           C  
ANISOU 2655  CB  TYR B  40    10299   5870   6967  -1900   2176    -88       C  
ATOM   2656  CG  TYR B  40      94.860  42.358  24.020  1.00 63.68           C  
ANISOU 2656  CG  TYR B  40    10287   6305   7603  -2013   2523   -345       C  
ATOM   2657  CD1 TYR B  40      95.769  42.735  23.037  1.00 66.48           C  
ANISOU 2657  CD1 TYR B  40    10802   6622   7834  -2248   3025   -450       C  
ATOM   2658  CD2 TYR B  40      95.317  41.546  25.051  1.00 64.69           C  
ANISOU 2658  CD2 TYR B  40     9915   6522   8141  -1891   2359   -501       C  
ATOM   2659  CE1 TYR B  40      97.078  42.255  23.038  1.00 69.14           C  
ANISOU 2659  CE1 TYR B  40    10726   7039   8505  -2357   3369   -751       C  
ATOM   2660  CE2 TYR B  40      96.625  41.064  25.069  1.00 66.18           C  
ANISOU 2660  CE2 TYR B  40     9720   6776   8648  -1954   2620   -792       C  
ATOM   2661  CZ  TYR B  40      97.504  41.421  24.058  1.00 77.12           C  
ANISOU 2661  CZ  TYR B  40    11185   8152   9967  -2191   3133   -938       C  
ATOM   2662  OH  TYR B  40      98.798  40.951  24.068  1.00 79.67           O  
ANISOU 2662  OH  TYR B  40    11059   8543  10667  -2257   3415  -1287       O  
ATOM   2663  N   ALA B  41      90.536  41.895  24.594  1.00 54.06           N  
ANISOU 2663  N   ALA B  41     9550   4999   5990  -1452   1283     86       N  
ATOM   2664  CA  ALA B  41      89.286  42.212  25.280  1.00 52.04           C  
ANISOU 2664  CA  ALA B  41     9290   4706   5775  -1330    932    197       C  
ATOM   2665  C   ALA B  41      89.758  42.953  26.513  1.00 51.32           C  
ANISOU 2665  C   ALA B  41     8973   4619   5907  -1402    967    267       C  
ATOM   2666  O   ALA B  41      90.745  42.534  27.131  1.00 50.96           O  
ANISOU 2666  O   ALA B  41     8636   4634   6094  -1450   1103    178       O  
ATOM   2667  CB  ALA B  41      88.553  40.944  25.700  1.00 52.53           C  
ANISOU 2667  CB  ALA B  41     9126   4812   6020  -1191    715    110       C  
ATOM   2668  N   ILE B  42      89.101  44.064  26.863  1.00 43.86           N  
ANISOU 2668  N   ILE B  42     8164   3601   4901  -1389    819    397       N  
ATOM   2669  CA  ILE B  42      89.535  44.840  28.024  1.00 41.49           C  
ANISOU 2669  CA  ILE B  42     7682   3291   4792  -1451    836    451       C  
ATOM   2670  C   ILE B  42      88.489  44.824  29.115  1.00 41.79           C  
ANISOU 2670  C   ILE B  42     7587   3333   4959  -1320    566    493       C  
ATOM   2671  O   ILE B  42      87.317  45.084  28.861  1.00 40.96           O  
ANISOU 2671  O   ILE B  42     7628   3180   4754  -1223    370    527       O  
ATOM   2672  CB  ILE B  42      89.988  46.281  27.629  1.00 44.36           C  
ANISOU 2672  CB  ILE B  42     8309   3540   5007  -1604    994    545       C  
ATOM   2673  CG1 ILE B  42      90.989  46.276  26.418  1.00 44.74           C  
ANISOU 2673  CG1 ILE B  42     8538   3562   4899  -1783   1367    488       C  
ATOM   2674  CG2 ILE B  42      90.530  47.096  28.831  1.00 44.22           C  
ANISOU 2674  CG2 ILE B  42     8086   3502   5214  -1674    997    568       C  
ATOM   2675  CD1 ILE B  42      92.387  45.650  26.635  1.00 47.75           C  
ANISOU 2675  CD1 ILE B  42     8541   4042   5561  -1906   1651    306       C  
ATOM   2676  N   GLY B  43      88.930  44.528  30.326  1.00 36.12           N  
ANISOU 2676  N   GLY B  43     6605   2657   4463  -1310    558    466       N  
ATOM   2677  CA  GLY B  43      88.052  44.524  31.475  1.00 35.46           C  
ANISOU 2677  CA  GLY B  43     6431   2563   4479  -1215    382    501       C  
ATOM   2678  C   GLY B  43      88.461  45.514  32.540  1.00 39.59           C  
ANISOU 2678  C   GLY B  43     6905   3056   5083  -1245    366    546       C  
ATOM   2679  O   GLY B  43      89.647  45.676  32.837  1.00 38.98           O  
ANISOU 2679  O   GLY B  43     6721   2987   5103  -1316    459    500       O  
ATOM   2680  N   TRP B  44      87.467  46.172  33.125  1.00 36.87           N  
ANISOU 2680  N   TRP B  44     6613   2671   4727  -1184    237    596       N  
ATOM   2681  CA  TRP B  44      87.621  47.093  34.242  1.00 37.01           C  
ANISOU 2681  CA  TRP B  44     6607   2650   4806  -1183    190    625       C  
ATOM   2682  C   TRP B  44      87.130  46.368  35.494  1.00 39.62           C  
ANISOU 2682  C   TRP B  44     6842   2998   5215  -1094    137    602       C  
ATOM   2683  O   TRP B  44      86.026  45.799  35.511  1.00 38.53           O  
ANISOU 2683  O   TRP B  44     6695   2864   5082  -1042    119    584       O  
ATOM   2684  CB  TRP B  44      86.874  48.411  33.997  1.00 36.21           C  
ANISOU 2684  CB  TRP B  44     6673   2466   4620  -1168    100    680       C  
ATOM   2685  CG  TRP B  44      87.653  49.376  33.153  1.00 37.69           C  
ANISOU 2685  CG  TRP B  44     7037   2571   4713  -1290    188    731       C  
ATOM   2686  CD1 TRP B  44      87.474  49.639  31.824  1.00 40.81           C  
ANISOU 2686  CD1 TRP B  44     7684   2900   4922  -1318    213    776       C  
ATOM   2687  CD2 TRP B  44      88.759  50.185  33.579  1.00 37.68           C  
ANISOU 2687  CD2 TRP B  44     7009   2517   4792  -1418    285    729       C  
ATOM   2688  NE1 TRP B  44      88.384  50.586  31.401  1.00 40.86           N  
ANISOU 2688  NE1 TRP B  44     7865   2798   4863  -1480    369    829       N  
ATOM   2689  CE2 TRP B  44      89.183  50.941  32.459  1.00 42.12           C  
ANISOU 2689  CE2 TRP B  44     7817   2968   5220  -1557    422    787       C  
ATOM   2690  CE3 TRP B  44      89.450  50.330  34.793  1.00 38.68           C  
ANISOU 2690  CE3 TRP B  44     6946   2660   5090  -1429    260    666       C  
ATOM   2691  CZ2 TRP B  44      90.275  51.810  32.516  1.00 41.24           C  
ANISOU 2691  CZ2 TRP B  44     7718   2763   5188  -1747    590    773       C  
ATOM   2692  CZ3 TRP B  44      90.527  51.199  34.852  1.00 40.14           C  
ANISOU 2692  CZ3 TRP B  44     7108   2768   5374  -1583    358    627       C  
ATOM   2693  CH2 TRP B  44      90.931  51.925  33.724  1.00 41.11           C  
ANISOU 2693  CH2 TRP B  44     7429   2783   5409  -1761    548    676       C  
ATOM   2694  N   PHE B  45      88.009  46.315  36.503  1.00 35.08           N  
ANISOU 2694  N   PHE B  45     6210   2415   4702  -1082    121    581       N  
ATOM   2695  CA  PHE B  45      87.788  45.650  37.784  1.00 34.71           C  
ANISOU 2695  CA  PHE B  45     6184   2341   4661   -995     79    575       C  
ATOM   2696  C   PHE B  45      88.064  46.641  38.916  1.00 39.70           C  
ANISOU 2696  C   PHE B  45     6872   2929   5284   -960     -7    572       C  
ATOM   2697  O   PHE B  45      88.827  47.590  38.736  1.00 39.55           O  
ANISOU 2697  O   PHE B  45     6810   2901   5318  -1014    -44    547       O  
ATOM   2698  CB  PHE B  45      88.715  44.412  37.908  1.00 36.23           C  
ANISOU 2698  CB  PHE B  45     6328   2532   4905   -950     61    524       C  
ATOM   2699  CG  PHE B  45      88.469  43.346  36.858  1.00 37.34           C  
ANISOU 2699  CG  PHE B  45     6425   2705   5057   -974    141    507       C  
ATOM   2700  CD1 PHE B  45      89.084  43.416  35.609  1.00 39.62           C  
ANISOU 2700  CD1 PHE B  45     6630   3052   5371  -1042    208    460       C  
ATOM   2701  CD2 PHE B  45      87.597  42.294  37.104  1.00 38.80           C  
ANISOU 2701  CD2 PHE B  45     6674   2845   5224   -946    176    523       C  
ATOM   2702  CE1 PHE B  45      88.813  42.465  34.625  1.00 39.78           C  
ANISOU 2702  CE1 PHE B  45     6643   3098   5375  -1050    269    428       C  
ATOM   2703  CE2 PHE B  45      87.331  41.341  36.114  1.00 41.42           C  
ANISOU 2703  CE2 PHE B  45     6961   3192   5583   -968    227    483       C  
ATOM   2704  CZ  PHE B  45      87.940  41.435  34.883  1.00 38.70           C  
ANISOU 2704  CZ  PHE B  45     6544   2920   5241  -1004    252    434       C  
ATOM   2705  N   ARG B  46      87.437  46.442  40.069  1.00 35.53           N  
ANISOU 2705  N   ARG B  46     6460   2354   4684   -888    -14    585       N  
ATOM   2706  CA  ARG B  46      87.661  47.323  41.209  1.00 34.55           C  
ANISOU 2706  CA  ARG B  46     6433   2180   4514   -833   -107    566       C  
ATOM   2707  C   ARG B  46      87.781  46.545  42.496  1.00 40.12           C  
ANISOU 2707  C   ARG B  46     7333   2811   5101   -727   -148    564       C  
ATOM   2708  O   ARG B  46      87.238  45.433  42.626  1.00 39.17           O  
ANISOU 2708  O   ARG B  46     7309   2656   4920   -721    -39    603       O  
ATOM   2709  CB  ARG B  46      86.596  48.432  41.306  1.00 31.85           C  
ANISOU 2709  CB  ARG B  46     6121   1829   4151   -844    -67    570       C  
ATOM   2710  CG  ARG B  46      85.182  47.946  41.605  1.00 34.68           C  
ANISOU 2710  CG  ARG B  46     6515   2185   4478   -830     83    562       C  
ATOM   2711  CD  ARG B  46      84.237  49.119  41.680  1.00 41.07           C  
ANISOU 2711  CD  ARG B  46     7298   2984   5322   -808     83    508       C  
ATOM   2712  NE  ARG B  46      82.864  48.703  41.963  1.00 43.59           N  
ANISOU 2712  NE  ARG B  46     7572   3304   5686   -808    253    432       N  
ATOM   2713  CZ  ARG B  46      81.814  49.506  41.862  1.00 53.04           C  
ANISOU 2713  CZ  ARG B  46     8671   4499   6982   -768    258    326       C  
ATOM   2714  NH1 ARG B  46      81.966  50.758  41.459  1.00 44.94           N  
ANISOU 2714  NH1 ARG B  46     7647   3449   5977   -714     79    321       N  
ATOM   2715  NH2 ARG B  46      80.599  49.053  42.124  1.00 38.60           N  
ANISOU 2715  NH2 ARG B  46     6734   2674   5260   -786    443    201       N  
ATOM   2716  N   GLN B  47      88.514  47.117  43.447  1.00 38.27           N  
ANISOU 2716  N   GLN B  47     7194   2523   4822   -643   -316    512       N  
ATOM   2717  CA  GLN B  47      88.670  46.498  44.749  1.00 39.21           C  
ANISOU 2717  CA  GLN B  47     7605   2533   4759   -506   -405    511       C  
ATOM   2718  C   GLN B  47      88.676  47.541  45.862  1.00 46.92           C  
ANISOU 2718  C   GLN B  47     8757   3454   5616   -430   -510    462       C  
ATOM   2719  O   GLN B  47      89.548  48.419  45.892  1.00 47.17           O  
ANISOU 2719  O   GLN B  47     8668   3492   5763   -408   -712    366       O  
ATOM   2720  CB  GLN B  47      89.892  45.571  44.805  1.00 40.06           C  
ANISOU 2720  CB  GLN B  47     7709   2594   4917   -394   -623    449       C  
ATOM   2721  CG  GLN B  47      89.867  44.652  46.011  1.00 46.90           C  
ANISOU 2721  CG  GLN B  47     8986   3298   5535   -235   -711    485       C  
ATOM   2722  CD  GLN B  47      91.221  44.551  46.645  1.00 62.95           C  
ANISOU 2722  CD  GLN B  47    11083   5246   7588    -29  -1104    349       C  
ATOM   2723  OE1 GLN B  47      92.154  43.968  46.066  1.00 64.33           O  
ANISOU 2723  OE1 GLN B  47    11043   5437   7961     28  -1260    249       O  
ATOM   2724  NE2 GLN B  47      91.351  45.117  47.857  1.00 39.22           N  
ANISOU 2724  NE2 GLN B  47     8366   2144   4393    105  -1289    305       N  
ATOM   2725  N   ALA B  48      87.665  47.455  46.746  1.00 44.42           N  
ANISOU 2725  N   ALA B  48     8717   3074   5086   -410   -339    507       N  
ATOM   2726  CA  ALA B  48      87.516  48.309  47.915  1.00 44.62           C  
ANISOU 2726  CA  ALA B  48     8982   3033   4937   -324   -396    454       C  
ATOM   2727  C   ALA B  48      88.309  47.637  49.084  1.00 50.50           C  
ANISOU 2727  C   ALA B  48    10125   3628   5432   -137   -625    437       C  
ATOM   2728  O   ALA B  48      88.508  46.410  49.043  1.00 48.64           O  
ANISOU 2728  O   ALA B  48    10033   3323   5126    -99   -627    502       O  
ATOM   2729  CB  ALA B  48      86.038  48.442  48.268  1.00 45.18           C  
ANISOU 2729  CB  ALA B  48     9163   3099   4902   -397    -53    474       C  
ATOM   2730  N   PRO B  49      88.804  48.395  50.106  1.00 48.53           N  
ANISOU 2730  N   PRO B  49    10087   3305   5046      4   -867    338       N  
ATOM   2731  CA  PRO B  49      89.573  47.744  51.190  1.00 48.87           C  
ANISOU 2731  CA  PRO B  49    10563   3180   4826    230  -1165    303       C  
ATOM   2732  C   PRO B  49      88.839  46.583  51.849  1.00 54.35           C  
ANISOU 2732  C   PRO B  49    11766   3723   5162    254   -927    446       C  
ATOM   2733  O   PRO B  49      87.643  46.672  52.114  1.00 53.89           O  
ANISOU 2733  O   PRO B  49    11854   3661   4960    124   -519    516       O  
ATOM   2734  CB  PRO B  49      89.856  48.875  52.172  1.00 50.59           C  
ANISOU 2734  CB  PRO B  49    10958   3345   4917    353  -1387    169       C  
ATOM   2735  CG  PRO B  49      89.762  50.128  51.347  1.00 54.85           C  
ANISOU 2735  CG  PRO B  49    11014   4032   5794    195  -1328    104       C  
ATOM   2736  CD  PRO B  49      88.691  49.853  50.329  1.00 49.89           C  
ANISOU 2736  CD  PRO B  49    10153   3517   5286    -11   -918    240       C  
ATOM   2737  N   GLY B  50      89.553  45.476  52.008  1.00 52.87           N  
ANISOU 2737  N   GLY B  50    11804   3403   4882    402  -1160    471       N  
ATOM   2738  CA  GLY B  50      89.046  44.239  52.597  1.00 53.57           C  
ANISOU 2738  CA  GLY B  50    12447   3284   4624    430   -974    620       C  
ATOM   2739  C   GLY B  50      88.001  43.463  51.815  1.00 57.34           C  
ANISOU 2739  C   GLY B  50    12780   3801   5205    179   -492    754       C  
ATOM   2740  O   GLY B  50      87.593  42.385  52.247  1.00 58.89           O  
ANISOU 2740  O   GLY B  50    13432   3797   5148    162   -298    877       O  
ATOM   2741  N   LYS B  51      87.539  44.003  50.692  1.00 53.43           N  
ANISOU 2741  N   LYS B  51    11696   3534   5070    -15   -304    724       N  
ATOM   2742  CA  LYS B  51      86.527  43.382  49.836  1.00 53.08           C  
ANISOU 2742  CA  LYS B  51    11432   3548   5187   -242     96    795       C  
ATOM   2743  C   LYS B  51      87.143  42.627  48.659  1.00 54.75           C  
ANISOU 2743  C   LYS B  51    11306   3827   5669   -252    -52    799       C  
ATOM   2744  O   LYS B  51      88.285  42.870  48.279  1.00 54.23           O  
ANISOU 2744  O   LYS B  51    11009   3832   5762   -134   -402    716       O  
ATOM   2745  CB  LYS B  51      85.485  44.416  49.355  1.00 55.77           C  
ANISOU 2745  CB  LYS B  51    11397   4067   5725   -413    370    733       C  
ATOM   2746  CG  LYS B  51      84.613  44.954  50.488  1.00 77.24           C  
ANISOU 2746  CG  LYS B  51    14439   6710   8197   -439    646    706       C  
ATOM   2747  CD  LYS B  51      83.226  45.358  50.010  1.00 90.42           C  
ANISOU 2747  CD  LYS B  51    15774   8493  10088   -635   1041    629       C  
ATOM   2748  CE  LYS B  51      82.357  45.793  51.167  1.00101.07           C  
ANISOU 2748  CE  LYS B  51    17434   9757  11211   -674   1388    564       C  
ATOM   2749  NZ  LYS B  51      80.994  46.181  50.719  1.00110.25           N  
ANISOU 2749  NZ  LYS B  51    18203  11025  12661   -846   1758    424       N  
ATOM   2750  N   GLU B  52      86.378  41.707  48.092  1.00 49.83           N  
ANISOU 2750  N   GLU B  52    10643   3175   5116   -405    236    864       N  
ATOM   2751  CA  GLU B  52      86.792  40.892  46.960  1.00 48.86           C  
ANISOU 2751  CA  GLU B  52    10237   3102   5224   -426    149    859       C  
ATOM   2752  C   GLU B  52      86.783  41.737  45.678  1.00 49.79           C  
ANISOU 2752  C   GLU B  52     9788   3472   5657   -521    133    780       C  
ATOM   2753  O   GLU B  52      85.916  42.595  45.531  1.00 49.57           O  
ANISOU 2753  O   GLU B  52     9598   3544   5693   -632    314    756       O  
ATOM   2754  CB  GLU B  52      85.821  39.702  46.838  1.00 50.35           C  
ANISOU 2754  CB  GLU B  52    10591   3155   5385   -582    490    936       C  
ATOM   2755  CG  GLU B  52      86.234  38.604  45.869  1.00 66.34           C  
ANISOU 2755  CG  GLU B  52    12450   5168   7589   -580    400    932       C  
ATOM   2756  CD  GLU B  52      85.300  37.405  45.779  1.00 96.29           C  
ANISOU 2756  CD  GLU B  52    16419   8789  11377   -746    724    991       C  
ATOM   2757  OE1 GLU B  52      85.582  36.504  44.956  1.00 94.99           O  
ANISOU 2757  OE1 GLU B  52    16176   8580  11337   -727    632    982       O  
ATOM   2758  OE2 GLU B  52      84.291  37.361  46.523  1.00 90.75           O  
ANISOU 2758  OE2 GLU B  52    15922   7989  10572   -909   1090   1022       O  
ATOM   2759  N   ARG B  53      87.750  41.486  44.758  1.00 44.09           N  
ANISOU 2759  N   ARG B  53     8799   2830   5122   -470    -78    726       N  
ATOM   2760  CA  ARG B  53      87.848  42.104  43.435  1.00 42.83           C  
ANISOU 2760  CA  ARG B  53     8203   2865   5205   -568    -66    668       C  
ATOM   2761  C   ARG B  53      86.518  41.853  42.721  1.00 46.46           C  
ANISOU 2761  C   ARG B  53     8547   3370   5735   -730    213    696       C  
ATOM   2762  O   ARG B  53      85.994  40.740  42.724  1.00 46.08           O  
ANISOU 2762  O   ARG B  53     8621   3222   5664   -779    359    728       O  
ATOM   2763  CB  ARG B  53      89.023  41.515  42.621  1.00 42.81           C  
ANISOU 2763  CB  ARG B  53     8004   2900   5361   -506   -240    593       C  
ATOM   2764  CG  ARG B  53      89.274  42.244  41.291  1.00 52.20           C  
ANISOU 2764  CG  ARG B  53     8828   4264   6743   -617   -197    535       C  
ATOM   2765  CD  ARG B  53      90.305  41.621  40.328  1.00 57.54           C  
ANISOU 2765  CD  ARG B  53     9286   4992   7584   -599   -261    432       C  
ATOM   2766  NE  ARG B  53      90.385  40.146  40.216  1.00 56.34           N  
ANISOU 2766  NE  ARG B  53     9222   4752   7434   -522   -281    421       N  
ATOM   2767  CZ  ARG B  53      89.410  39.323  39.807  1.00 72.68           C  
ANISOU 2767  CZ  ARG B  53    11368   6784   9463   -594   -119    488       C  
ATOM   2768  NH1 ARG B  53      89.637  38.017  39.700  1.00 53.70           N  
ANISOU 2768  NH1 ARG B  53     9051   4274   7080   -521   -160    462       N  
ATOM   2769  NH2 ARG B  53      88.189  39.793  39.553  1.00 56.23           N  
ANISOU 2769  NH2 ARG B  53     9271   4750   7344   -728     62    553       N  
ATOM   2770  N   GLU B  54      85.966  42.912  42.151  1.00 43.88           N  
ANISOU 2770  N   GLU B  54     8001   3167   5505   -805    263    663       N  
ATOM   2771  CA  GLU B  54      84.660  42.942  41.518  1.00 43.08           C  
ANISOU 2771  CA  GLU B  54     7751   3112   5507   -915    447    630       C  
ATOM   2772  C   GLU B  54      84.785  43.514  40.123  1.00 45.61           C  
ANISOU 2772  C   GLU B  54     7824   3555   5951   -940    350    594       C  
ATOM   2773  O   GLU B  54      85.293  44.618  39.952  1.00 45.04           O  
ANISOU 2773  O   GLU B  54     7705   3533   5875   -917    237    597       O  
ATOM   2774  CB  GLU B  54      83.727  43.808  42.396  1.00 44.58           C  
ANISOU 2774  CB  GLU B  54     8004   3281   5651   -932    577    599       C  
ATOM   2775  CG  GLU B  54      82.450  44.294  41.741  1.00 55.46           C  
ANISOU 2775  CG  GLU B  54     9142   4729   7203   -996    672    495       C  
ATOM   2776  CD  GLU B  54      81.699  45.351  42.524  1.00 69.67           C  
ANISOU 2776  CD  GLU B  54    10949   6526   8998   -977    754    421       C  
ATOM   2777  OE1 GLU B  54      80.449  45.314  42.517  1.00 60.81           O  
ANISOU 2777  OE1 GLU B  54     9681   5400   8023  -1036    938    290       O  
ATOM   2778  OE2 GLU B  54      82.355  46.225  43.134  1.00 66.45           O  
ANISOU 2778  OE2 GLU B  54    10664   6114   8470   -900    632    459       O  
ATOM   2779  N   GLY B  55      84.323  42.741  39.143  1.00 41.82           N  
ANISOU 2779  N   GLY B  55     7231   3097   5563   -991    400    556       N  
ATOM   2780  CA  GLY B  55      84.279  43.139  37.745  1.00 39.83           C  
ANISOU 2780  CA  GLY B  55     6832   2932   5370  -1004    316    518       C  
ATOM   2781  C   GLY B  55      83.241  44.224  37.605  1.00 40.45           C  
ANISOU 2781  C   GLY B  55     6844   3032   5494   -993    287    465       C  
ATOM   2782  O   GLY B  55      82.194  44.179  38.254  1.00 40.42           O  
ANISOU 2782  O   GLY B  55     6801   2994   5565  -1008    391    396       O  
ATOM   2783  N   VAL B  56      83.535  45.220  36.805  1.00 35.40           N  
ANISOU 2783  N   VAL B  56     6208   2426   4816   -969    160    482       N  
ATOM   2784  CA  VAL B  56      82.616  46.336  36.649  1.00 35.37           C  
ANISOU 2784  CA  VAL B  56     6183   2408   4848   -916     68    426       C  
ATOM   2785  C   VAL B  56      82.154  46.487  35.203  1.00 39.92           C  
ANISOU 2785  C   VAL B  56     6763   2985   5418   -873    -81    375       C  
ATOM   2786  O   VAL B  56      80.962  46.713  34.957  1.00 39.27           O  
ANISOU 2786  O   VAL B  56     6590   2883   5446   -798   -185    244       O  
ATOM   2787  CB  VAL B  56      83.265  47.620  37.259  1.00 38.23           C  
ANISOU 2787  CB  VAL B  56     6648   2742   5137   -901     18    495       C  
ATOM   2788  CG1 VAL B  56      83.117  48.831  36.383  1.00 37.88           C  
ANISOU 2788  CG1 VAL B  56     6689   2651   5052   -860   -136    504       C  
ATOM   2789  CG2 VAL B  56      82.723  47.885  38.645  1.00 37.85           C  
ANISOU 2789  CG2 VAL B  56     6593   2668   5119   -872     96    451       C  
ATOM   2790  N   SER B  57      83.084  46.333  34.249  1.00 37.33           N  
ANISOU 2790  N   SER B  57     6549   2671   4964   -910    -95    450       N  
ATOM   2791  CA  SER B  57      82.774  46.532  32.837  1.00 38.06           C  
ANISOU 2791  CA  SER B  57     6764   2738   4959   -861   -238    422       C  
ATOM   2792  C   SER B  57      83.802  45.864  31.945  1.00 41.52           C  
ANISOU 2792  C   SER B  57     7296   3208   5273   -934   -142    470       C  
ATOM   2793  O   SER B  57      84.965  45.782  32.312  1.00 41.39           O  
ANISOU 2793  O   SER B  57     7264   3219   5245  -1022      6    536       O  
ATOM   2794  CB  SER B  57      82.700  48.026  32.522  1.00 42.36           C  
ANISOU 2794  CB  SER B  57     7510   3193   5394   -807   -376    475       C  
ATOM   2795  OG  SER B  57      82.112  48.205  31.247  1.00 57.65           O  
ANISOU 2795  OG  SER B  57     9632   5064   7209   -709   -574    431       O  
ATOM   2796  N   CYS B  58      83.385  45.434  30.753  1.00 37.47           N  
ANISOU 2796  N   CYS B  58     6878   2684   4673   -885   -241    406       N  
ATOM   2797  CA  CYS B  58      84.259  44.728  29.831  1.00 37.70           C  
ANISOU 2797  CA  CYS B  58     7006   2744   4573   -945   -127    417       C  
ATOM   2798  C   CYS B  58      83.876  45.056  28.401  1.00 41.41           C  
ANISOU 2798  C   CYS B  58     7772   3149   4813   -871   -277    391       C  
ATOM   2799  O   CYS B  58      82.697  45.235  28.094  1.00 40.28           O  
ANISOU 2799  O   CYS B  58     7654   2956   4694   -732   -538    295       O  
ATOM   2800  CB  CYS B  58      84.188  43.218  30.113  1.00 38.68           C  
ANISOU 2800  CB  CYS B  58     6918   2926   4853   -957    -59    328       C  
ATOM   2801  SG  CYS B  58      85.381  42.212  29.199  1.00 42.81           S  
ANISOU 2801  SG  CYS B  58     7496   3494   5275  -1015    103    300       S  
ATOM   2802  N   ILE B  59      84.884  45.128  27.523  1.00 39.74           N  
ANISOU 2802  N   ILE B  59     7797   2924   4380   -957   -112    452       N  
ATOM   2803  CA  ILE B  59      84.742  45.399  26.089  1.00 39.56           C  
ANISOU 2803  CA  ILE B  59     8183   2812   4038   -903   -197    451       C  
ATOM   2804  C   ILE B  59      85.483  44.312  25.254  1.00 43.47           C  
ANISOU 2804  C   ILE B  59     8720   3370   4425   -966      0    383       C  
ATOM   2805  O   ILE B  59      86.668  44.051  25.490  1.00 41.00           O  
ANISOU 2805  O   ILE B  59     8281   3122   4176  -1114    305    401       O  
ATOM   2806  CB  ILE B  59      85.123  46.867  25.699  1.00 42.49           C  
ANISOU 2806  CB  ILE B  59     8956   3033   4154   -956   -152    601       C  
ATOM   2807  CG1 ILE B  59      84.634  47.215  24.276  1.00 42.29           C  
ANISOU 2807  CG1 ILE B  59     9469   2856   3742   -835   -344    606       C  
ATOM   2808  CG2 ILE B  59      86.630  47.195  25.896  1.00 43.26           C  
ANISOU 2808  CG2 ILE B  59     9046   3145   4246  -1197    256    690       C  
ATOM   2809  CD1 ILE B  59      84.323  48.725  24.056  1.00 46.72           C  
ANISOU 2809  CD1 ILE B  59    10475   3197   4078   -783   -492    739       C  
ATOM   2810  N   SER B  60      84.767  43.658  24.322  1.00 41.39           N  
ANISOU 2810  N   SER B  60     8600   3088   4040   -837   -201    265       N  
ATOM   2811  CA  SER B  60      85.374  42.633  23.482  1.00 42.21           C  
ANISOU 2811  CA  SER B  60     8772   3241   4024   -873    -36    175       C  
ATOM   2812  C   SER B  60      86.087  43.262  22.299  1.00 50.01           C  
ANISOU 2812  C   SER B  60    10268   4141   4591   -943    160    247       C  
ATOM   2813  O   SER B  60      85.838  44.422  21.974  1.00 50.59           O  
ANISOU 2813  O   SER B  60    10717   4077   4427   -919     68    363       O  
ATOM   2814  CB  SER B  60      84.336  41.618  23.008  1.00 44.22           C  
ANISOU 2814  CB  SER B  60     8969   3499   4335   -715   -331     -9       C  
ATOM   2815  OG  SER B  60      83.592  42.079  21.895  1.00 51.84           O  
ANISOU 2815  OG  SER B  60    10364   4348   4985   -557   -622    -57       O  
ATOM   2816  N   SER B  61      86.962  42.484  21.643  1.00 48.31           N  
ANISOU 2816  N   SER B  61    10098   3983   4275  -1029    445    167       N  
ATOM   2817  CA  SER B  61      87.681  42.846  20.421  1.00 48.49           C  
ANISOU 2817  CA  SER B  61    10624   3923   3877  -1125    728    195       C  
ATOM   2818  C   SER B  61      86.688  43.251  19.317  1.00 52.84           C  
ANISOU 2818  C   SER B  61    11772   4312   3994   -940    394    209       C  
ATOM   2819  O   SER B  61      87.050  43.987  18.404  1.00 52.08           O  
ANISOU 2819  O   SER B  61    12261   4067   3460  -1005    569    306       O  
ATOM   2820  CB  SER B  61      88.484  41.642  19.938  1.00 53.24           C  
ANISOU 2820  CB  SER B  61    11092   4632   4503  -1182   1011     26       C  
ATOM   2821  OG  SER B  61      89.815  41.685  20.420  1.00 66.77           O  
ANISOU 2821  OG  SER B  61    12535   6419   6416  -1395   1454     13       O  
ATOM   2822  N   GLY B  62      85.469  42.713  19.397  1.00 50.52           N  
ANISOU 2822  N   GLY B  62    11338   4028   3828   -713    -79     88       N  
ATOM   2823  CA  GLY B  62      84.379  42.973  18.466  1.00 50.81           C  
ANISOU 2823  CA  GLY B  62    11840   3915   3551   -467   -538     25       C  
ATOM   2824  C   GLY B  62      83.529  44.167  18.857  1.00 57.02           C  
ANISOU 2824  C   GLY B  62    12743   4569   4354   -336   -893    117       C  
ATOM   2825  O   GLY B  62      82.529  44.452  18.195  1.00 58.70           O  
ANISOU 2825  O   GLY B  62    13292   4640   4370    -81  -1370     31       O  
ATOM   2826  N   GLY B  63      83.917  44.857  19.930  1.00 52.50           N  
ANISOU 2826  N   GLY B  63    11889   4032   4028   -484   -697    262       N  
ATOM   2827  CA  GLY B  63      83.236  46.056  20.412  1.00 51.76           C  
ANISOU 2827  CA  GLY B  63    11878   3811   3978   -377   -978    348       C  
ATOM   2828  C   GLY B  63      82.037  45.847  21.315  1.00 54.96           C  
ANISOU 2828  C   GLY B  63    11762   4288   4832   -213  -1353    191       C  
ATOM   2829  O   GLY B  63      81.398  46.830  21.686  1.00 55.31           O  
ANISOU 2829  O   GLY B  63    11854   4227   4936    -95  -1607    219       O  
ATOM   2830  N   SER B  64      81.714  44.579  21.684  1.00 50.64           N  
ANISOU 2830  N   SER B  64    10724   3900   4618   -215  -1365     11       N  
ATOM   2831  CA  SER B  64      80.603  44.234  22.595  1.00 49.57           C  
ANISOU 2831  CA  SER B  64    10056   3830   4951   -123  -1607   -166       C  
ATOM   2832  C   SER B  64      80.927  44.727  23.988  1.00 50.38           C  
ANISOU 2832  C   SER B  64     9821   4000   5320   -271  -1360    -35       C  
ATOM   2833  O   SER B  64      82.071  44.622  24.417  1.00 49.03           O  
ANISOU 2833  O   SER B  64     9600   3901   5127   -470   -977    117       O  
ATOM   2834  CB  SER B  64      80.369  42.722  22.643  1.00 53.14           C  
ANISOU 2834  CB  SER B  64    10137   4394   5661   -156  -1575   -359       C  
ATOM   2835  OG  SER B  64      79.893  42.220  21.406  1.00 64.65           O  
ANISOU 2835  OG  SER B  64    11862   5785   6919     10  -1872   -537       O  
ATOM   2836  N   THR B  65      79.926  45.271  24.691  1.00 46.94           N  
ANISOU 2836  N   THR B  65     9151   3537   5148   -160  -1593   -127       N  
ATOM   2837  CA  THR B  65      80.092  45.833  26.041  1.00 45.98           C  
ANISOU 2837  CA  THR B  65     8756   3463   5253   -268  -1399    -27       C  
ATOM   2838  C   THR B  65      79.161  45.178  27.064  1.00 46.92           C  
ANISOU 2838  C   THR B  65     8348   3664   5816   -268  -1411   -216       C  
ATOM   2839  O   THR B  65      77.974  44.950  26.778  1.00 46.41           O  
ANISOU 2839  O   THR B  65     8122   3566   5948   -116  -1710   -466       O  
ATOM   2840  CB  THR B  65      79.873  47.353  26.026  1.00 52.62           C  
ANISOU 2840  CB  THR B  65     9885   4159   5949   -158  -1585     64       C  
ATOM   2841  OG1 THR B  65      78.517  47.600  25.666  1.00 56.80           O  
ANISOU 2841  OG1 THR B  65    10392   4599   6591    105  -2046   -163       O  
ATOM   2842  CG2 THR B  65      80.813  48.087  25.066  1.00 47.94           C  
ANISOU 2842  CG2 THR B  65     9879   3436   4899   -210  -1494    274       C  
ATOM   2843  N   VAL B  66      79.715  44.876  28.256  1.00 40.44           N  
ANISOU 2843  N   VAL B  66     7281   2931   5154   -443  -1079   -117       N  
ATOM   2844  CA  VAL B  66      78.997  44.291  29.398  1.00 38.65           C  
ANISOU 2844  CA  VAL B  66     6641   2753   5290   -500   -969   -247       C  
ATOM   2845  C   VAL B  66      79.238  45.122  30.645  1.00 41.46           C  
ANISOU 2845  C   VAL B  66     6933   3118   5701   -557   -806   -131       C  
ATOM   2846  O   VAL B  66      80.293  45.735  30.782  1.00 41.39           O  
ANISOU 2846  O   VAL B  66     7128   3108   5490   -614   -698     69       O  
ATOM   2847  CB  VAL B  66      79.230  42.767  29.630  1.00 40.96           C  
ANISOU 2847  CB  VAL B  66     6752   3098   5714   -636   -751   -286       C  
ATOM   2848  CG1 VAL B  66      78.685  41.958  28.467  1.00 39.98           C  
ANISOU 2848  CG1 VAL B  66     6633   2950   5607   -560   -959   -475       C  
ATOM   2849  CG2 VAL B  66      80.696  42.439  29.895  1.00 40.31           C  
ANISOU 2849  CG2 VAL B  66     6798   3062   5457   -761   -486    -70       C  
ATOM   2850  N   TYR B  67      78.238  45.200  31.518  1.00 37.65           N  
ANISOU 2850  N   TYR B  67     6168   2635   5500   -543   -786   -287       N  
ATOM   2851  CA  TYR B  67      78.309  46.008  32.740  1.00 36.79           C  
ANISOU 2851  CA  TYR B  67     6012   2529   5438   -575   -642   -217       C  
ATOM   2852  C   TYR B  67      77.688  45.234  33.890  1.00 40.03           C  
ANISOU 2852  C   TYR B  67     6139   2962   6109   -687   -380   -335       C  
ATOM   2853  O   TYR B  67      76.707  44.513  33.691  1.00 38.74           O  
ANISOU 2853  O   TYR B  67     5733   2789   6199   -696   -391   -563       O  
ATOM   2854  CB  TYR B  67      77.562  47.360  32.568  1.00 37.24           C  
ANISOU 2854  CB  TYR B  67     6105   2514   5532   -392   -918   -317       C  
ATOM   2855  CG  TYR B  67      78.050  48.195  31.407  1.00 37.45           C  
ANISOU 2855  CG  TYR B  67     6511   2454   5265   -279  -1179   -196       C  
ATOM   2856  CD1 TYR B  67      77.482  48.066  30.144  1.00 38.72           C  
ANISOU 2856  CD1 TYR B  67     6790   2551   5372   -121  -1504   -326       C  
ATOM   2857  CD2 TYR B  67      79.086  49.110  31.568  1.00 37.56           C  
ANISOU 2857  CD2 TYR B  67     6803   2422   5046   -338  -1097     36       C  
ATOM   2858  CE1 TYR B  67      77.960  48.797  29.059  1.00 39.06           C  
ANISOU 2858  CE1 TYR B  67     7297   2476   5070    -27  -1709   -191       C  
ATOM   2859  CE2 TYR B  67      79.563  49.859  30.495  1.00 38.28           C  
ANISOU 2859  CE2 TYR B  67     7305   2394   4846   -280  -1261    160       C  
ATOM   2860  CZ  TYR B  67      78.998  49.700  29.241  1.00 45.99           C  
ANISOU 2860  CZ  TYR B  67     8470   3294   5708   -125  -1554     62       C  
ATOM   2861  OH  TYR B  67      79.463  50.440  28.176  1.00 46.18           O  
ANISOU 2861  OH  TYR B  67     9007   3163   5378    -74  -1688    203       O  
ATOM   2862  N   SER B  68      78.253  45.400  35.093  1.00 37.44           N  
ANISOU 2862  N   SER B  68     5867   2645   5715   -778   -140   -196       N  
ATOM   2863  CA  SER B  68      77.742  44.774  36.302  1.00 37.66           C  
ANISOU 2863  CA  SER B  68     5751   2657   5901   -895    161   -270       C  
ATOM   2864  C   SER B  68      76.414  45.442  36.685  1.00 44.40           C  
ANISOU 2864  C   SER B  68     6355   3495   7020   -834    154   -528       C  
ATOM   2865  O   SER B  68      76.133  46.555  36.241  1.00 44.24           O  
ANISOU 2865  O   SER B  68     6330   3469   7009   -671   -114   -593       O  
ATOM   2866  CB  SER B  68      78.764  44.861  37.428  1.00 40.71           C  
ANISOU 2866  CB  SER B  68     6350   3036   6081   -958    347    -60       C  
ATOM   2867  OG  SER B  68      78.947  46.191  37.881  1.00 53.15           O  
ANISOU 2867  OG  SER B  68     8000   4614   7581   -875    264    -24       O  
ATOM   2868  N   GLU B  69      75.574  44.745  37.454  1.00 42.93           N  
ANISOU 2868  N   GLU B  69     5965   3280   7065   -964    455   -697       N  
ATOM   2869  CA  GLU B  69      74.276  45.276  37.860  1.00 43.04           C  
ANISOU 2869  CA  GLU B  69     5668   3284   7401   -930    518  -1008       C  
ATOM   2870  C   GLU B  69      74.423  46.538  38.720  1.00 47.89           C  
ANISOU 2870  C   GLU B  69     6393   3905   7899   -840    537   -956       C  
ATOM   2871  O   GLU B  69      73.530  47.381  38.722  1.00 48.56           O  
ANISOU 2871  O   GLU B  69     6253   3988   8211   -712    419  -1206       O  
ATOM   2872  CB  GLU B  69      73.456  44.193  38.594  1.00 44.16           C  
ANISOU 2872  CB  GLU B  69     5601   3372   7807  -1157    957  -1193       C  
ATOM   2873  CG  GLU B  69      72.976  43.053  37.711  1.00 54.37           C  
ANISOU 2873  CG  GLU B  69     6682   4635   9342  -1239    910  -1357       C  
ATOM   2874  CD  GLU B  69      72.088  43.456  36.549  1.00 78.15           C  
ANISOU 2874  CD  GLU B  69     9357   7674  12662  -1052    492  -1682       C  
ATOM   2875  OE1 GLU B  69      72.516  43.266  35.386  1.00 59.44           O  
ANISOU 2875  OE1 GLU B  69     7100   5319  10164   -935    134  -1611       O  
ATOM   2876  OE2 GLU B  69      70.974  43.975  36.799  1.00 76.04           O  
ANISOU 2876  OE2 GLU B  69     8729   7403  12758  -1004    510  -2028       O  
ATOM   2877  N   SER B  70      75.564  46.675  39.411  1.00 44.50           N  
ANISOU 2877  N   SER B  70     6300   3474   7134   -885    639   -662       N  
ATOM   2878  CA  SER B  70      75.892  47.785  40.303  1.00 44.93           C  
ANISOU 2878  CA  SER B  70     6513   3522   7037   -814    655   -591       C  
ATOM   2879  C   SER B  70      76.343  49.083  39.599  1.00 51.75           C  
ANISOU 2879  C   SER B  70     7481   4382   7798   -631    263   -516       C  
ATOM   2880  O   SER B  70      76.417  50.130  40.252  1.00 52.89           O  
ANISOU 2880  O   SER B  70     7713   4501   7881   -556    238   -514       O  
ATOM   2881  CB  SER B  70      76.948  47.340  41.314  1.00 48.05           C  
ANISOU 2881  CB  SER B  70     7234   3893   7132   -919    870   -344       C  
ATOM   2882  OG  SER B  70      78.047  46.692  40.692  1.00 57.00           O  
ANISOU 2882  OG  SER B  70     8523   5036   8099   -949    748   -134       O  
ATOM   2883  N   VAL B  71      76.698  49.018  38.298  1.00 47.73           N  
ANISOU 2883  N   VAL B  71     7023   3875   7239   -571    -20   -444       N  
ATOM   2884  CA  VAL B  71      77.218  50.178  37.579  1.00 47.08           C  
ANISOU 2884  CA  VAL B  71     7143   3742   7004   -438   -336   -335       C  
ATOM   2885  C   VAL B  71      76.490  50.419  36.248  1.00 54.48           C  
ANISOU 2885  C   VAL B  71     8027   4631   8043   -273   -687   -481       C  
ATOM   2886  O   VAL B  71      76.767  51.424  35.579  1.00 53.16           O  
ANISOU 2886  O   VAL B  71     8096   4372   7730   -148   -962   -400       O  
ATOM   2887  CB  VAL B  71      78.770  50.141  37.401  1.00 49.78           C  
ANISOU 2887  CB  VAL B  71     7770   4087   7056   -534   -318    -40       C  
ATOM   2888  CG1 VAL B  71      79.501  49.858  38.716  1.00 48.92           C  
ANISOU 2888  CG1 VAL B  71     7730   4005   6852   -644    -66     66       C  
ATOM   2889  CG2 VAL B  71      79.207  49.174  36.300  1.00 49.27           C  
ANISOU 2889  CG2 VAL B  71     7746   4054   6918   -591   -354     34       C  
ATOM   2890  N   LYS B  72      75.561  49.508  35.862  1.00 54.55           N  
ANISOU 2890  N   LYS B  72     7758   4671   8295   -270   -692   -708       N  
ATOM   2891  CA  LYS B  72      74.779  49.641  34.620  1.00 55.58           C  
ANISOU 2891  CA  LYS B  72     7828   4747   8544    -76  -1089   -905       C  
ATOM   2892  C   LYS B  72      73.973  50.938  34.644  1.00 61.13           C  
ANISOU 2892  C   LYS B  72     8480   5358   9391    167  -1385  -1105       C  
ATOM   2893  O   LYS B  72      73.585  51.402  35.726  1.00 61.97           O  
ANISOU 2893  O   LYS B  72     8403   5480   9664    157  -1199  -1222       O  
ATOM   2894  CB  LYS B  72      73.890  48.405  34.348  1.00 58.58           C  
ANISOU 2894  CB  LYS B  72     7857   5171   9228   -131  -1037  -1170       C  
ATOM   2895  CG  LYS B  72      72.688  48.247  35.280  1.00 81.07           C  
ANISOU 2895  CG  LYS B  72    10253   8043  12508   -175   -813  -1510       C  
ATOM   2896  CD  LYS B  72      71.618  47.373  34.658  1.00 94.69           C  
ANISOU 2896  CD  LYS B  72    11596   9765  14617   -162   -919  -1871       C  
ATOM   2897  CE  LYS B  72      70.265  47.647  35.262  1.00106.73           C  
ANISOU 2897  CE  LYS B  72    12620  11288  16643   -163   -765  -2301       C  
ATOM   2898  NZ  LYS B  72      69.207  46.833  34.614  1.00116.23           N  
ANISOU 2898  NZ  LYS B  72    13390  12479  18293   -180   -856  -2703       N  
ATOM   2899  N   ASP B  73      73.784  51.560  33.469  1.00 57.98           N  
ANISOU 2899  N   ASP B  73     8303   4839   8888    397  -1848  -1133       N  
ATOM   2900  CA  ASP B  73      73.079  52.855  33.322  1.00 57.40           C  
ANISOU 2900  CA  ASP B  73     8275   4623   8911    686  -2234  -1310       C  
ATOM   2901  C   ASP B  73      73.769  54.015  34.084  1.00 58.67           C  
ANISOU 2901  C   ASP B  73     8694   4717   8881    660  -2126  -1091       C  
ATOM   2902  O   ASP B  73      73.108  55.005  34.422  1.00 60.96           O  
ANISOU 2902  O   ASP B  73     8917   4911   9334    861  -2322  -1278       O  
ATOM   2903  CB  ASP B  73      71.578  52.736  33.689  1.00 59.66           C  
ANISOU 2903  CB  ASP B  73     8006   4936   9725    832  -2325  -1802       C  
ATOM   2904  CG  ASP B  73      70.817  51.707  32.866  1.00 78.43           C  
ANISOU 2904  CG  ASP B  73    10092   7350  12357    871  -2491  -2081       C  
ATOM   2905  OD1 ASP B  73      69.822  51.151  33.383  1.00 81.56           O  
ANISOU 2905  OD1 ASP B  73     9961   7838  13191    770  -2249  -2407       O  
ATOM   2906  OD2 ASP B  73      71.223  51.448  31.706  1.00 85.20           O  
ANISOU 2906  OD2 ASP B  73    11267   8133  12972    986  -2840  -1986       O  
ATOM   2907  N   ARG B  74      75.095  53.896  34.341  1.00 50.34           N  
ANISOU 2907  N   ARG B  74     7910   3702   7516    425  -1836   -734       N  
ATOM   2908  CA  ARG B  74      75.925  54.892  35.037  1.00 48.26           C  
ANISOU 2908  CA  ARG B  74     7887   3374   7077    360  -1723   -528       C  
ATOM   2909  C   ARG B  74      77.337  54.943  34.453  1.00 49.60           C  
ANISOU 2909  C   ARG B  74     8459   3497   6888    192  -1643   -181       C  
ATOM   2910  O   ARG B  74      77.958  56.013  34.453  1.00 48.69           O  
ANISOU 2910  O   ARG B  74     8654   3239   6609    187  -1703    -27       O  
ATOM   2911  CB  ARG B  74      76.025  54.590  36.535  1.00 47.49           C  
ANISOU 2911  CB  ARG B  74     7535   3408   7101    204  -1327   -560       C  
ATOM   2912  CG  ARG B  74      74.781  54.902  37.365  1.00 51.28           C  
ANISOU 2912  CG  ARG B  74     7657   3909   7917    330  -1293   -903       C  
ATOM   2913  CD  ARG B  74      74.944  54.399  38.788  1.00 49.64           C  
ANISOU 2913  CD  ARG B  74     7304   3821   7738    138   -834   -900       C  
ATOM   2914  NE  ARG B  74      76.124  55.013  39.370  1.00 57.15           N  
ANISOU 2914  NE  ARG B  74     8562   4733   8418     59   -764   -645       N  
ATOM   2915  CZ  ARG B  74      77.099  54.374  40.000  1.00 63.70           C  
ANISOU 2915  CZ  ARG B  74     9507   5633   9061   -133   -501   -444       C  
ATOM   2916  NH1 ARG B  74      77.011  53.069  40.231  1.00 35.38           N  
ANISOU 2916  NH1 ARG B  74     5795   2148   5499   -273   -244   -442       N  
ATOM   2917  NH2 ARG B  74      78.156  55.040  40.438  1.00 52.84           N  
ANISOU 2917  NH2 ARG B  74     8378   4207   7494   -175   -515   -269       N  
ATOM   2918  N   PHE B  75      77.863  53.773  34.011  1.00 44.16           N  
ANISOU 2918  N   PHE B  75     7744   2923   6111     37  -1474    -84       N  
ATOM   2919  CA  PHE B  75      79.191  53.621  33.401  1.00 43.19           C  
ANISOU 2919  CA  PHE B  75     7925   2785   5702   -138  -1341    185       C  
ATOM   2920  C   PHE B  75      79.106  53.303  31.895  1.00 49.95           C  
ANISOU 2920  C   PHE B  75     9033   3572   6373    -69  -1539    209       C  
ATOM   2921  O   PHE B  75      78.118  52.735  31.424  1.00 49.58           O  
ANISOU 2921  O   PHE B  75     8830   3554   6455     76  -1737     11       O  
ATOM   2922  CB  PHE B  75      80.014  52.535  34.110  1.00 43.96           C  
ANISOU 2922  CB  PHE B  75     7825   3053   5824   -356   -988    266       C  
ATOM   2923  CG  PHE B  75      80.521  52.800  35.516  1.00 44.90           C  
ANISOU 2923  CG  PHE B  75     7842   3217   6003   -449   -783    305       C  
ATOM   2924  CD1 PHE B  75      79.866  53.699  36.360  1.00 46.53           C  
ANISOU 2924  CD1 PHE B  75     7983   3371   6325   -341   -851    192       C  
ATOM   2925  CD2 PHE B  75      81.602  52.088  36.026  1.00 46.30           C  
ANISOU 2925  CD2 PHE B  75     7982   3483   6126   -615   -550    417       C  
ATOM   2926  CE1 PHE B  75      80.310  53.911  37.661  1.00 47.06           C  
ANISOU 2926  CE1 PHE B  75     8002   3472   6407   -409   -678    212       C  
ATOM   2927  CE2 PHE B  75      82.035  52.289  37.336  1.00 49.12           C  
ANISOU 2927  CE2 PHE B  75     8287   3863   6512   -661   -426    428       C  
ATOM   2928  CZ  PHE B  75      81.393  53.210  38.141  1.00 46.82           C  
ANISOU 2928  CZ  PHE B  75     7980   3519   6292   -564   -484    334       C  
ATOM   2929  N   THR B  76      80.144  53.684  31.145  1.00 48.44           N  
ANISOU 2929  N   THR B  76     9244   3277   5885   -180  -1473    427       N  
ATOM   2930  CA  THR B  76      80.258  53.445  29.703  1.00 48.26           C  
ANISOU 2930  CA  THR B  76     9584   3164   5590   -140  -1599    484       C  
ATOM   2931  C   THR B  76      81.715  53.141  29.426  1.00 51.18           C  
ANISOU 2931  C   THR B  76    10116   3568   5761   -412  -1232    687       C  
ATOM   2932  O   THR B  76      82.600  53.938  29.763  1.00 51.71           O  
ANISOU 2932  O   THR B  76    10331   3551   5765   -566  -1051    828       O  
ATOM   2933  CB  THR B  76      79.769  54.665  28.868  1.00 58.26           C  
ANISOU 2933  CB  THR B  76    11343   4151   6644     75  -1972    505       C  
ATOM   2934  OG1 THR B  76      78.442  55.018  29.255  1.00 60.71           O  
ANISOU 2934  OG1 THR B  76    11417   4432   7217    351  -2329    258       O  
ATOM   2935  CG2 THR B  76      79.820  54.412  27.346  1.00 53.66           C  
ANISOU 2935  CG2 THR B  76    11242   3442   5704    145  -2129    561       C  
ATOM   2936  N   ILE B  77      81.955  51.990  28.830  1.00 46.20           N  
ANISOU 2936  N   ILE B  77     9423   3055   5074   -471  -1122    664       N  
ATOM   2937  CA  ILE B  77      83.280  51.559  28.427  1.00 46.05           C  
ANISOU 2937  CA  ILE B  77     9516   3081   4900   -705   -777    792       C  
ATOM   2938  C   ILE B  77      83.374  51.833  26.920  1.00 52.28           C  
ANISOU 2938  C   ILE B  77    10862   3699   5304   -673   -847    867       C  
ATOM   2939  O   ILE B  77      82.363  51.738  26.223  1.00 53.15           O  
ANISOU 2939  O   ILE B  77    11144   3738   5314   -443  -1196    771       O  
ATOM   2940  CB  ILE B  77      83.542  50.071  28.844  1.00 48.89           C  
ANISOU 2940  CB  ILE B  77     9459   3667   5451   -783   -592    706       C  
ATOM   2941  CG1 ILE B  77      85.043  49.729  28.793  1.00 48.31           C  
ANISOU 2941  CG1 ILE B  77     9373   3654   5331  -1017   -225    790       C  
ATOM   2942  CG2 ILE B  77      82.680  49.062  28.062  1.00 49.40           C  
ANISOU 2942  CG2 ILE B  77     9487   3779   5502   -643   -781    565       C  
ATOM   2943  CD1 ILE B  77      85.415  48.355  29.215  1.00 40.65           C  
ANISOU 2943  CD1 ILE B  77     8050   2859   4535  -1065    -80    709       C  
ATOM   2944  N   SER B  78      84.540  52.256  26.427  1.00 49.54           N  
ANISOU 2944  N   SER B  78    10828   3258   4739   -895   -528   1017       N  
ATOM   2945  CA  SER B  78      84.710  52.513  24.999  1.00 50.48           C  
ANISOU 2945  CA  SER B  78    11569   3186   4424   -900   -511   1106       C  
ATOM   2946  C   SER B  78      86.161  52.396  24.595  1.00 59.21           C  
ANISOU 2946  C   SER B  78    12797   4294   5405  -1223     13   1194       C  
ATOM   2947  O   SER B  78      87.038  52.339  25.451  1.00 57.22           O  
ANISOU 2947  O   SER B  78    12152   4160   5430  -1424    299   1181       O  
ATOM   2948  CB  SER B  78      84.153  53.886  24.612  1.00 54.79           C  
ANISOU 2948  CB  SER B  78    12668   3421   4727   -758   -797   1206       C  
ATOM   2949  OG  SER B  78      84.872  54.983  25.156  1.00 64.27           O  
ANISOU 2949  OG  SER B  78    13962   4481   5975   -949   -584   1338       O  
ATOM   2950  N   ARG B  79      86.405  52.339  23.291  1.00 62.87           N  
ANISOU 2950  N   ARG B  79    13810   4622   5458  -1263    131   1253       N  
ATOM   2951  CA  ARG B  79      87.734  52.342  22.688  1.00 66.66           C  
ANISOU 2951  CA  ARG B  79    14514   5052   5762  -1584    683   1314       C  
ATOM   2952  C   ARG B  79      87.800  53.645  21.901  1.00 80.24           C  
ANISOU 2952  C   ARG B  79    17025   6402   7060  -1655    739   1504       C  
ATOM   2953  O   ARG B  79      86.776  54.057  21.344  1.00 81.00           O  
ANISOU 2953  O   ARG B  79    17601   6307   6867  -1379    295   1556       O  
ATOM   2954  CB  ARG B  79      87.898  51.165  21.720  1.00 67.14           C  
ANISOU 2954  CB  ARG B  79    14675   5222   5614  -1565    806   1220       C  
ATOM   2955  CG  ARG B  79      87.884  49.797  22.362  1.00 67.14           C  
ANISOU 2955  CG  ARG B  79    13981   5538   5992  -1509    781   1038       C  
ATOM   2956  CD  ARG B  79      87.917  48.745  21.277  1.00 67.81           C  
ANISOU 2956  CD  ARG B  79    14256   5681   5826  -1469    868    941       C  
ATOM   2957  NE  ARG B  79      87.748  47.394  21.807  1.00 62.29           N  
ANISOU 2957  NE  ARG B  79    12974   5235   5460  -1373    765    767       N  
ATOM   2958  CZ  ARG B  79      88.747  46.621  22.216  1.00 72.84           C  
ANISOU 2958  CZ  ARG B  79    13857   6743   7073  -1529   1092    668       C  
ATOM   2959  NH1 ARG B  79      89.996  47.061  22.178  1.00 52.35           N  
ANISOU 2959  NH1 ARG B  79    11241   4127   4522  -1795   1548    684       N  
ATOM   2960  NH2 ARG B  79      88.502  45.406  22.684  1.00 66.67           N  
ANISOU 2960  NH2 ARG B  79    12637   6136   6556  -1417    956    528       N  
ATOM   2961  N   ASP B  80      88.973  54.310  21.853  1.00 83.09           N  
ANISOU 2961  N   ASP B  80    17540   6632   7397  -2018   1264   1588       N  
ATOM   2962  CA  ASP B  80      89.114  55.569  21.098  1.00 85.35           C  
ANISOU 2962  CA  ASP B  80    18654   6512   7265  -2141   1396   1789       C  
ATOM   2963  C   ASP B  80      89.007  55.329  19.579  1.00 94.82           C  
ANISOU 2963  C   ASP B  80    20667   7519   7841  -2096   1470   1865       C  
ATOM   2964  O   ASP B  80      88.827  54.184  19.152  1.00 95.88           O  
ANISOU 2964  O   ASP B  80    20665   7859   7906  -1954   1385   1740       O  
ATOM   2965  CB  ASP B  80      90.412  56.319  21.472  1.00 87.57           C  
ANISOU 2965  CB  ASP B  80    18842   6686   7743  -2588   1989   1823       C  
ATOM   2966  CG  ASP B  80      91.693  55.603  21.101  1.00101.09           C  
ANISOU 2966  CG  ASP B  80    20308   8553   9549  -2928   2634   1693       C  
ATOM   2967  OD1 ASP B  80      91.892  54.469  21.574  1.00102.30           O  
ANISOU 2967  OD1 ASP B  80    19763   9054  10053  -2866   2617   1502       O  
ATOM   2968  OD2 ASP B  80      92.504  56.186  20.343  1.00108.53           O  
ANISOU 2968  OD2 ASP B  80    21772   9245  10222  -3260   3174   1768       O  
ATOM   2969  N   ASN B  81      89.092  56.401  18.774  1.00 94.19           N  
ANISOU 2969  N   ASN B  81    21480   7022   7287  -2207   1611   2069       N  
ATOM   2970  CA  ASN B  81      89.002  56.335  17.315  1.00 95.43           C  
ANISOU 2970  CA  ASN B  81    22583   6923   6753  -2166   1692   2170       C  
ATOM   2971  C   ASN B  81      89.949  55.257  16.769  1.00101.91           C  
ANISOU 2971  C   ASN B  81    23217   7968   7535  -2420   2283   2037       C  
ATOM   2972  O   ASN B  81      89.464  54.224  16.298  1.00102.22           O  
ANISOU 2972  O   ASN B  81    23251   8172   7415  -2176   2037   1921       O  
ATOM   2973  CB  ASN B  81      89.258  57.723  16.666  1.00 95.82           C  
ANISOU 2973  CB  ASN B  81    23638   6446   6322  -2358   1924   2431       C  
ATOM   2974  CG  ASN B  81      88.420  58.871  17.223  1.00118.66           C  
ANISOU 2974  CG  ASN B  81    26734   9079   9274  -2115   1362   2550       C  
ATOM   2975  OD1 ASN B  81      87.843  58.805  18.322  1.00115.87           O  
ANISOU 2975  OD1 ASN B  81    25614   8956   9456  -1940    985   2434       O  
ATOM   2976  ND2 ASN B  81      88.349  59.971  16.480  1.00104.48           N  
ANISOU 2976  ND2 ASN B  81    26020   6768   6910  -2098   1310   2780       N  
ATOM   2977  N   ALA B  82      91.283  55.438  16.950  1.00 99.00           N  
ANISOU 2977  N   ALA B  82    22569   7633   7412  -2894   3027   1999       N  
ATOM   2978  CA  ALA B  82      92.317  54.494  16.492  1.00 98.33           C  
ANISOU 2978  CA  ALA B  82    22227   7754   7378  -3168   3659   1822       C  
ATOM   2979  C   ALA B  82      92.350  53.168  17.265  1.00 98.77           C  
ANISOU 2979  C   ALA B  82    21274   8284   7969  -3010   3472   1565       C  
ATOM   2980  O   ALA B  82      93.020  52.229  16.827  1.00 99.38           O  
ANISOU 2980  O   ALA B  82    21171   8539   8048  -3117   3843   1393       O  
ATOM   2981  CB  ALA B  82      93.687  55.154  16.511  1.00 99.21           C  
ANISOU 2981  CB  ALA B  82    22276   7738   7680  -3714   4476   1802       C  
ATOM   2982  N   LYS B  83      91.620  53.090  18.397  1.00 91.65           N  
ANISOU 2982  N   LYS B  83    19762   7561   7501  -2756   2916   1534       N  
ATOM   2983  CA  LYS B  83      91.518  51.915  19.268  1.00 89.70           C  
ANISOU 2983  CA  LYS B  83    18624   7706   7751  -2589   2683   1327       C  
ATOM   2984  C   LYS B  83      92.898  51.516  19.846  1.00 89.40           C  
ANISOU 2984  C   LYS B  83    17893   7874   8202  -2907   3223   1134       C  
ATOM   2985  O   LYS B  83      93.415  50.429  19.569  1.00 89.44           O  
ANISOU 2985  O   LYS B  83    17590   8086   8306  -2927   3434    945       O  
ATOM   2986  CB  LYS B  83      90.785  50.741  18.568  1.00 91.98           C  
ANISOU 2986  CB  LYS B  83    19028   8124   7796  -2291   2370   1236       C  
ATOM   2987  CG  LYS B  83      89.425  51.104  17.953  1.00104.14           C  
ANISOU 2987  CG  LYS B  83    21208   9457   8903  -1939   1767   1357       C  
ATOM   2988  CD  LYS B  83      88.532  49.890  17.717  1.00116.40           C  
ANISOU 2988  CD  LYS B  83    22591  11194  10443  -1607   1317   1195       C  
ATOM   2989  CE  LYS B  83      88.712  49.237  16.364  1.00129.60           C  
ANISOU 2989  CE  LYS B  83    24854  12794  11594  -1594   1492   1146       C  
ATOM   2990  NZ  LYS B  83      87.882  48.007  16.236  1.00138.21           N  
ANISOU 2990  NZ  LYS B  83    25685  14071  12758  -1288   1047    950       N  
ATOM   2991  N   LYS B  84      93.481  52.433  20.647  1.00 81.47           N  
ANISOU 2991  N   LYS B  84    16641   6792   7521  -3134   3403   1153       N  
ATOM   2992  CA  LYS B  84      94.785  52.335  21.330  1.00 79.15           C  
ANISOU 2992  CA  LYS B  84    15674   6640   7760  -3426   3836    940       C  
ATOM   2993  C   LYS B  84      94.579  52.326  22.861  1.00 79.02           C  
ANISOU 2993  C   LYS B  84    14975   6790   8260  -3272   3419    880       C  
ATOM   2994  O   LYS B  84      95.355  51.719  23.608  1.00 78.66           O  
ANISOU 2994  O   LYS B  84    14247   6948   8691  -3336   3524    655       O  
ATOM   2995  CB  LYS B  84      95.660  53.556  20.960  1.00 81.34           C  
ANISOU 2995  CB  LYS B  84    16306   6625   7975  -3861   4422    988       C  
ATOM   2996  CG  LYS B  84      95.702  53.868  19.455  1.00 93.23           C  
ANISOU 2996  CG  LYS B  84    18698   7869   8855  -4039   4866   1110       C  
ATOM   2997  CD  LYS B  84      96.539  55.066  19.118  1.00 98.79           C  
ANISOU 2997  CD  LYS B  84    19812   8234   9489  -4500   5478   1178       C  
ATOM   2998  CE  LYS B  84      97.983  54.734  18.812  1.00111.13           C  
ANISOU 2998  CE  LYS B  84    20970   9877  11379  -4933   6279    883       C  
ATOM   2999  NZ  LYS B  84      98.791  55.970  18.584  1.00117.80           N  
ANISOU 2999  NZ  LYS B  84    22162  10364  12233  -5434   6912    925       N  
ATOM   3000  N   ILE B  85      93.539  53.051  23.310  1.00 71.30           N  
ANISOU 3000  N   ILE B  85    14228   5697   7167  -3063   2946   1068       N  
ATOM   3001  CA  ILE B  85      93.152  53.288  24.697  1.00 68.66           C  
ANISOU 3001  CA  ILE B  85    13430   5456   7203  -2910   2552   1052       C  
ATOM   3002  C   ILE B  85      91.729  52.758  24.925  1.00 63.50           C  
ANISOU 3002  C   ILE B  85    12785   4905   6437  -2513   1978   1116       C  
ATOM   3003  O   ILE B  85      90.922  52.715  23.992  1.00 62.45           O  
ANISOU 3003  O   ILE B  85    13154   4666   5907  -2359   1807   1217       O  
ATOM   3004  CB  ILE B  85      93.206  54.840  24.970  1.00 72.70           C  
ANISOU 3004  CB  ILE B  85    14253   5676   7696  -3071   2588   1190       C  
ATOM   3005  CG1 ILE B  85      94.455  55.521  24.350  1.00 74.56           C  
ANISOU 3005  CG1 ILE B  85    14725   5697   7906  -3518   3234   1165       C  
ATOM   3006  CG2 ILE B  85      93.054  55.227  26.450  1.00 74.11           C  
ANISOU 3006  CG2 ILE B  85    13936   5935   8286  -2978   2283   1131       C  
ATOM   3007  CD1 ILE B  85      95.883  55.048  24.818  1.00 88.92           C  
ANISOU 3007  CD1 ILE B  85    15856   7691  10239  -3801   3670    868       C  
ATOM   3008  N   VAL B  86      91.430  52.369  26.173  1.00 53.71           N  
ANISOU 3008  N   VAL B  86    11006   3851   5552  -2353   1686   1035       N  
ATOM   3009  CA  VAL B  86      90.093  51.973  26.602  1.00 50.97           C  
ANISOU 3009  CA  VAL B  86    10585   3588   5193  -2027   1203   1059       C  
ATOM   3010  C   VAL B  86      89.668  52.964  27.703  1.00 53.32           C  
ANISOU 3010  C   VAL B  86    10792   3807   5658  -1960    963   1109       C  
ATOM   3011  O   VAL B  86      90.432  53.211  28.634  1.00 53.01           O  
ANISOU 3011  O   VAL B  86    10423   3811   5908  -2087   1076   1045       O  
ATOM   3012  CB  VAL B  86      89.948  50.474  27.005  1.00 52.68           C  
ANISOU 3012  CB  VAL B  86    10336   4068   5612  -1887   1103    917       C  
ATOM   3013  CG1 VAL B  86      88.575  50.181  27.596  1.00 51.34           C  
ANISOU 3013  CG1 VAL B  86    10050   3959   5498  -1611    675    918       C  
ATOM   3014  CG2 VAL B  86      90.189  49.574  25.807  1.00 52.35           C  
ANISOU 3014  CG2 VAL B  86    10457   4073   5361  -1913   1287    862       C  
ATOM   3015  N   TYR B  87      88.480  53.562  27.554  1.00 48.59           N  
ANISOU 3015  N   TYR B  87    10500   3080   4883  -1749    616   1195       N  
ATOM   3016  CA  TYR B  87      87.925  54.514  28.508  1.00 48.31           C  
ANISOU 3016  CA  TYR B  87    10414   2956   4984  -1647    368   1220       C  
ATOM   3017  C   TYR B  87      86.821  53.901  29.344  1.00 50.58           C  
ANISOU 3017  C   TYR B  87    10346   3416   5455  -1384     39   1120       C  
ATOM   3018  O   TYR B  87      86.086  53.037  28.865  1.00 49.63           O  
ANISOU 3018  O   TYR B  87    10198   3388   5271  -1229   -109   1063       O  
ATOM   3019  CB  TYR B  87      87.336  55.721  27.778  1.00 50.46           C  
ANISOU 3019  CB  TYR B  87    11297   2919   4956  -1574    196   1354       C  
ATOM   3020  CG  TYR B  87      88.348  56.493  26.968  1.00 54.52           C  
ANISOU 3020  CG  TYR B  87    12277   3190   5250  -1869    568   1478       C  
ATOM   3021  CD1 TYR B  87      88.473  56.290  25.597  1.00 57.24           C  
ANISOU 3021  CD1 TYR B  87    13133   3412   5204  -1924    723   1556       C  
ATOM   3022  CD2 TYR B  87      89.182  57.434  27.570  1.00 55.09           C  
ANISOU 3022  CD2 TYR B  87    12298   3132   5500  -2111    789   1499       C  
ATOM   3023  CE1 TYR B  87      89.404  57.001  24.847  1.00 57.78           C  
ANISOU 3023  CE1 TYR B  87    13678   3227   5047  -2236   1150   1669       C  
ATOM   3024  CE2 TYR B  87      90.125  58.138  26.830  1.00 55.83           C  
ANISOU 3024  CE2 TYR B  87    12806   2977   5431  -2435   1202   1591       C  
ATOM   3025  CZ  TYR B  87      90.241  57.907  25.472  1.00 65.78           C  
ANISOU 3025  CZ  TYR B  87    14591   4114   6288  -2511   1414   1681       C  
ATOM   3026  OH  TYR B  87      91.156  58.614  24.731  1.00 74.43           O  
ANISOU 3026  OH  TYR B  87    16150   4934   7195  -2867   1897   1773       O  
ATOM   3027  N   LEU B  88      86.696  54.377  30.598  1.00 45.42           N  
ANISOU 3027  N   LEU B  88     9436   2788   5033  -1348    -54   1081       N  
ATOM   3028  CA  LEU B  88      85.604  54.044  31.504  1.00 42.79           C  
ANISOU 3028  CA  LEU B  88     8818   2571   4868  -1129   -304    981       C  
ATOM   3029  C   LEU B  88      85.003  55.353  32.054  1.00 46.22           C  
ANISOU 3029  C   LEU B  88     9379   2842   5339  -1020   -511    986       C  
ATOM   3030  O   LEU B  88      85.543  55.957  32.994  1.00 46.14           O  
ANISOU 3030  O   LEU B  88     9260   2809   5461  -1108   -438    983       O  
ATOM   3031  CB  LEU B  88      85.953  53.030  32.617  1.00 41.61           C  
ANISOU 3031  CB  LEU B  88     8222   2640   4948  -1160   -192    892       C  
ATOM   3032  CG  LEU B  88      84.741  52.525  33.437  1.00 43.82           C  
ANISOU 3032  CG  LEU B  88     8263   3022   5366   -972   -361    785       C  
ATOM   3033  CD1 LEU B  88      83.850  51.619  32.620  1.00 43.26           C  
ANISOU 3033  CD1 LEU B  88     8174   3007   5255   -864   -460    721       C  
ATOM   3034  CD2 LEU B  88      85.166  51.848  34.714  1.00 44.62           C  
ANISOU 3034  CD2 LEU B  88     8073   3253   5627  -1010   -248    737       C  
ATOM   3035  N   GLN B  89      83.923  55.826  31.402  1.00 40.75           N  
ANISOU 3035  N   GLN B  89     8943   2013   4527   -812   -800    972       N  
ATOM   3036  CA  GLN B  89      83.197  57.004  31.864  1.00 39.44           C  
ANISOU 3036  CA  GLN B  89     8887   1683   4417   -649  -1051    935       C  
ATOM   3037  C   GLN B  89      82.351  56.526  33.057  1.00 44.02           C  
ANISOU 3037  C   GLN B  89     8997   2454   5274   -510  -1125    752       C  
ATOM   3038  O   GLN B  89      81.661  55.501  32.954  1.00 44.49           O  
ANISOU 3038  O   GLN B  89     8820   2669   5417   -423  -1163    640       O  
ATOM   3039  CB  GLN B  89      82.304  57.591  30.759  1.00 39.65           C  
ANISOU 3039  CB  GLN B  89     9343   1484   4239   -424  -1395    939       C  
ATOM   3040  CG  GLN B  89      81.690  58.952  31.105  1.00 45.03           C  
ANISOU 3040  CG  GLN B  89    10223   1928   4958   -244  -1677    907       C  
ATOM   3041  CD  GLN B  89      82.740  60.021  31.250  1.00 59.66           C  
ANISOU 3041  CD  GLN B  89    12367   3575   6725   -468  -1481   1074       C  
ATOM   3042  OE1 GLN B  89      83.381  60.440  30.277  1.00 60.77           O  
ANISOU 3042  OE1 GLN B  89    12997   3499   6594   -621  -1361   1249       O  
ATOM   3043  NE2 GLN B  89      82.941  60.478  32.467  1.00 48.58           N  
ANISOU 3043  NE2 GLN B  89    10686   2220   5551   -509  -1422   1007       N  
ATOM   3044  N   MET B  90      82.484  57.211  34.204  1.00 39.14           N  
ANISOU 3044  N   MET B  90     8259   1819   4794   -521  -1097    717       N  
ATOM   3045  CA  MET B  90      81.768  56.870  35.431  1.00 38.31           C  
ANISOU 3045  CA  MET B  90     7784   1867   4906   -419  -1093    550       C  
ATOM   3046  C   MET B  90      80.932  58.072  35.844  1.00 46.18           C  
ANISOU 3046  C   MET B  90     8848   2711   5989   -224  -1325    437       C  
ATOM   3047  O   MET B  90      81.489  59.091  36.249  1.00 46.80           O  
ANISOU 3047  O   MET B  90     9096   2646   6039   -277  -1328    498       O  
ATOM   3048  CB  MET B  90      82.740  56.478  36.543  1.00 39.81           C  
ANISOU 3048  CB  MET B  90     7789   2183   5153   -590   -844    581       C  
ATOM   3049  CG  MET B  90      83.770  55.421  36.143  1.00 42.62           C  
ANISOU 3049  CG  MET B  90     8090   2656   5449   -771   -640    675       C  
ATOM   3050  SD  MET B  90      84.693  54.804  37.568  1.00 46.81           S  
ANISOU 3050  SD  MET B  90     8389   3323   6073   -873   -463    647       S  
ATOM   3051  CE  MET B  90      85.600  56.248  38.055  1.00 43.68           C  
ANISOU 3051  CE  MET B  90     8131   2764   5701   -962   -499    669       C  
ATOM   3052  N   ASN B  91      79.604  57.985  35.653  1.00 44.12           N  
ANISOU 3052  N   ASN B  91     8454   2456   5855      9  -1541    244       N  
ATOM   3053  CA  ASN B  91      78.667  59.055  35.972  1.00 44.47           C  
ANISOU 3053  CA  ASN B  91     8510   2355   6030    247  -1800     71       C  
ATOM   3054  C   ASN B  91      77.868  58.722  37.222  1.00 49.07           C  
ANISOU 3054  C   ASN B  91     8666   3106   6874    311  -1665   -173       C  
ATOM   3055  O   ASN B  91      77.724  57.537  37.554  1.00 48.33           O  
ANISOU 3055  O   ASN B  91     8292   3212   6860    212  -1436   -226       O  
ATOM   3056  CB  ASN B  91      77.739  59.337  34.779  1.00 49.55           C  
ANISOU 3056  CB  ASN B  91     9332   2841   6654    503  -2197    -25       C  
ATOM   3057  CG  ASN B  91      78.407  59.871  33.515  1.00 71.62           C  
ANISOU 3057  CG  ASN B  91    12699   5395   9120    470  -2344    217       C  
ATOM   3058  OD1 ASN B  91      79.571  60.285  33.487  1.00 64.62           O  
ANISOU 3058  OD1 ASN B  91    12084   4416   8050    241  -2139    449       O  
ATOM   3059  ND2 ASN B  91      77.666  59.880  32.426  1.00 66.42           N  
ANISOU 3059  ND2 ASN B  91    12251   4606   8378    699  -2701    145       N  
ATOM   3060  N   SER B  92      77.360  59.775  37.933  1.00 45.47           N  
ANISOU 3060  N   SER B  92     8192   2545   6541    466  -1778   -327       N  
ATOM   3061  CA  SER B  92      76.565  59.654  39.174  1.00 44.92           C  
ANISOU 3061  CA  SER B  92     7765   2601   6701    530  -1608   -590       C  
ATOM   3062  C   SER B  92      77.247  58.769  40.223  1.00 48.25           C  
ANISOU 3062  C   SER B  92     8074   3211   7047    294  -1200   -499       C  
ATOM   3063  O   SER B  92      76.624  57.855  40.779  1.00 48.79           O  
ANISOU 3063  O   SER B  92     7859   3433   7245    256   -960   -650       O  
ATOM   3064  CB  SER B  92      75.146  59.176  38.871  1.00 48.89           C  
ANISOU 3064  CB  SER B  92     7914   3167   7494    715  -1715   -910       C  
ATOM   3065  OG  SER B  92      74.481  60.138  38.067  1.00 65.13           O  
ANISOU 3065  OG  SER B  92    10095   5015   9636   1005  -2167  -1048       O  
ATOM   3066  N   LEU B  93      78.552  59.034  40.456  1.00 42.85           N  
ANISOU 3066  N   LEU B  93     7635   2488   6158    133  -1134   -263       N  
ATOM   3067  CA  LEU B  93      79.398  58.308  41.395  1.00 41.06           C  
ANISOU 3067  CA  LEU B  93     7384   2392   5825    -49   -854   -166       C  
ATOM   3068  C   LEU B  93      78.920  58.493  42.820  1.00 45.91           C  
ANISOU 3068  C   LEU B  93     7910   3051   6484      7   -688   -343       C  
ATOM   3069  O   LEU B  93      78.517  59.582  43.204  1.00 46.23           O  
ANISOU 3069  O   LEU B  93     7991   2983   6591    143   -807   -477       O  
ATOM   3070  CB  LEU B  93      80.881  58.686  41.235  1.00 40.21           C  
ANISOU 3070  CB  LEU B  93     7511   2206   5560   -203   -887     53       C  
ATOM   3071  CG  LEU B  93      81.580  58.128  39.981  1.00 43.00           C  
ANISOU 3071  CG  LEU B  93     7946   2564   5827   -334   -895    236       C  
ATOM   3072  CD1 LEU B  93      82.787  58.959  39.601  1.00 41.68           C  
ANISOU 3072  CD1 LEU B  93     8016   2244   5578   -472   -941    384       C  
ATOM   3073  CD2 LEU B  93      81.991  56.673  40.154  1.00 44.09           C  
ANISOU 3073  CD2 LEU B  93     7931   2887   5934   -450   -685    284       C  
ATOM   3074  N   GLN B  94      78.894  57.399  43.573  1.00 43.38           N  
ANISOU 3074  N   GLN B  94     7500   2869   6115    -91   -402   -355       N  
ATOM   3075  CA  GLN B  94      78.436  57.322  44.954  1.00 42.96           C  
ANISOU 3075  CA  GLN B  94     7433   2857   6034    -72   -154   -509       C  
ATOM   3076  C   GLN B  94      79.554  56.786  45.860  1.00 45.62           C  
ANISOU 3076  C   GLN B  94     7994   3221   6118   -185    -33   -354       C  
ATOM   3077  O   GLN B  94      80.489  56.181  45.328  1.00 43.73           O  
ANISOU 3077  O   GLN B  94     7806   3006   5804   -286   -100   -168       O  
ATOM   3078  CB  GLN B  94      77.165  56.455  45.033  1.00 44.05           C  
ANISOU 3078  CB  GLN B  94     7302   3086   6348    -80    111   -708       C  
ATOM   3079  CG  GLN B  94      75.908  57.116  44.440  1.00 59.17           C  
ANISOU 3079  CG  GLN B  94     8945   4963   8573     94    -40   -979       C  
ATOM   3080  CD  GLN B  94      75.569  58.480  45.019  1.00 82.59           C  
ANISOU 3080  CD  GLN B  94    11953   7830  11599    269   -158  -1156       C  
ATOM   3081  OE1 GLN B  94      75.767  58.759  46.211  1.00 78.93           O  
ANISOU 3081  OE1 GLN B  94    11618   7367  11004    252     44  -1206       O  
ATOM   3082  NE2 GLN B  94      75.041  59.367  44.180  1.00 75.23           N  
ANISOU 3082  NE2 GLN B  94    10952   6787  10846    463   -513  -1264       N  
ATOM   3083  N   PRO B  95      79.519  57.015  47.208  1.00 43.38           N  
ANISOU 3083  N   PRO B  95     7868   2921   5694   -150    113   -447       N  
ATOM   3084  CA  PRO B  95      80.628  56.534  48.071  1.00 43.07           C  
ANISOU 3084  CA  PRO B  95     8098   2875   5391   -206    129   -319       C  
ATOM   3085  C   PRO B  95      80.995  55.066  47.908  1.00 47.77           C  
ANISOU 3085  C   PRO B  95     8722   3536   5894   -318    266   -176       C  
ATOM   3086  O   PRO B  95      82.156  54.725  48.087  1.00 48.08           O  
ANISOU 3086  O   PRO B  95     8915   3557   5796   -341    129    -51       O  
ATOM   3087  CB  PRO B  95      80.151  56.847  49.489  1.00 44.60           C  
ANISOU 3087  CB  PRO B  95     8488   3035   5422   -129    317   -479       C  
ATOM   3088  CG  PRO B  95      79.188  57.958  49.334  1.00 48.91           C  
ANISOU 3088  CG  PRO B  95     8858   3547   6177    -18    287   -685       C  
ATOM   3089  CD  PRO B  95      78.519  57.771  47.999  1.00 44.85           C  
ANISOU 3089  CD  PRO B  95     8021   3076   5942    -33    239   -697       C  
ATOM   3090  N   GLU B  96      80.031  54.222  47.486  1.00 44.55           N  
ANISOU 3090  N   GLU B  96     8134   3187   5605   -381    500   -220       N  
ATOM   3091  CA  GLU B  96      80.205  52.785  47.256  1.00 44.45           C  
ANISOU 3091  CA  GLU B  96     8138   3211   5539   -494    649   -103       C  
ATOM   3092  C   GLU B  96      81.061  52.461  46.024  1.00 46.92           C  
ANISOU 3092  C   GLU B  96     8342   3560   5927   -536    412     53       C  
ATOM   3093  O   GLU B  96      81.407  51.298  45.828  1.00 47.38           O  
ANISOU 3093  O   GLU B  96     8433   3637   5933   -610    485    152       O  
ATOM   3094  CB  GLU B  96      78.844  52.075  47.170  1.00 46.29           C  
ANISOU 3094  CB  GLU B  96     8176   3477   5936   -571    985   -247       C  
ATOM   3095  CG  GLU B  96      78.049  52.080  48.472  1.00 60.80           C  
ANISOU 3095  CG  GLU B  96    10158   5272   7673   -588   1357   -405       C  
ATOM   3096  CD  GLU B  96      77.319  53.361  48.852  1.00 84.71           C  
ANISOU 3096  CD  GLU B  96    13057   8297  10831   -472   1363   -639       C  
ATOM   3097  OE1 GLU B  96      77.045  54.198  47.959  1.00 71.18           O  
ANISOU 3097  OE1 GLU B  96    11084   6605   9355   -370   1078   -713       O  
ATOM   3098  OE2 GLU B  96      77.014  53.519  50.057  1.00 79.18           O  
ANISOU 3098  OE2 GLU B  96    12557   7554   9974   -474   1657   -756       O  
ATOM   3099  N   ASP B  97      81.410  53.470  45.205  1.00 41.01           N  
ANISOU 3099  N   ASP B  97     7501   2796   5284   -496    155     69       N  
ATOM   3100  CA  ASP B  97      82.274  53.297  44.032  1.00 39.02           C  
ANISOU 3100  CA  ASP B  97     7191   2559   5074   -557    -15    203       C  
ATOM   3101  C   ASP B  97      83.742  53.540  44.390  1.00 40.63           C  
ANISOU 3101  C   ASP B  97     7530   2726   5182   -580   -163    284       C  
ATOM   3102  O   ASP B  97      84.603  53.377  43.524  1.00 39.13           O  
ANISOU 3102  O   ASP B  97     7283   2546   5038   -655   -250    368       O  
ATOM   3103  CB  ASP B  97      81.853  54.209  42.877  1.00 40.05           C  
ANISOU 3103  CB  ASP B  97     7224   2652   5342   -521   -180    182       C  
ATOM   3104  CG  ASP B  97      80.421  54.020  42.430  1.00 44.87           C  
ANISOU 3104  CG  ASP B  97     7651   3289   6107   -455   -127     40       C  
ATOM   3105  OD1 ASP B  97      80.092  52.922  41.886  1.00 42.92           O  
ANISOU 3105  OD1 ASP B  97     7286   3109   5915   -510    -38     44       O  
ATOM   3106  OD2 ASP B  97      79.629  54.951  42.615  1.00 45.95           O  
ANISOU 3106  OD2 ASP B  97     7742   3374   6342   -341   -191   -108       O  
ATOM   3107  N   THR B  98      84.027  53.897  45.674  1.00 36.01           N  
ANISOU 3107  N   THR B  98     7116   2093   4472   -515   -184    227       N  
ATOM   3108  CA  THR B  98      85.375  54.125  46.192  1.00 35.60           C  
ANISOU 3108  CA  THR B  98     7171   1994   4364   -505   -375    235       C  
ATOM   3109  C   THR B  98      86.123  52.801  46.183  1.00 42.20           C  
ANISOU 3109  C   THR B  98     8028   2866   5140   -525   -374    303       C  
ATOM   3110  O   THR B  98      85.713  51.853  46.874  1.00 43.38           O  
ANISOU 3110  O   THR B  98     8342   3012   5129   -482   -243    320       O  
ATOM   3111  CB  THR B  98      85.326  54.788  47.571  1.00 39.51           C  
ANISOU 3111  CB  THR B  98     7882   2417   4715   -394   -430    127       C  
ATOM   3112  OG1 THR B  98      84.564  55.997  47.482  1.00 37.13           O  
ANISOU 3112  OG1 THR B  98     7533   2071   4502   -363   -438     46       O  
ATOM   3113  CG2 THR B  98      86.698  55.108  48.103  1.00 38.87           C  
ANISOU 3113  CG2 THR B  98     7883   2273   4614   -360   -694     82       C  
ATOM   3114  N   ALA B  99      87.185  52.712  45.355  1.00 37.73           N  
ANISOU 3114  N   ALA B  99     7309   2317   4710   -598   -491    332       N  
ATOM   3115  CA  ALA B  99      87.966  51.478  45.193  1.00 36.61           C  
ANISOU 3115  CA  ALA B  99     7135   2207   4567   -599   -520    362       C  
ATOM   3116  C   ALA B  99      89.192  51.744  44.333  1.00 41.12           C  
ANISOU 3116  C   ALA B  99     7492   2789   5343   -693   -627    324       C  
ATOM   3117  O   ALA B  99      89.234  52.756  43.632  1.00 39.45           O  
ANISOU 3117  O   ALA B  99     7190   2555   5245   -798   -607    325       O  
ATOM   3118  CB  ALA B  99      87.104  50.424  44.489  1.00 36.37           C  
ANISOU 3118  CB  ALA B  99     7057   2240   4523   -647   -313    448       C  
ATOM   3119  N   VAL B 100      90.156  50.797  44.317  1.00 37.97           N  
ANISOU 3119  N   VAL B 100     7021   2407   5000   -663   -714    280       N  
ATOM   3120  CA  VAL B 100      91.279  50.906  43.381  1.00 37.15           C  
ANISOU 3120  CA  VAL B 100     6656   2327   5132   -779   -732    206       C  
ATOM   3121  C   VAL B 100      90.725  50.251  42.103  1.00 39.29           C  
ANISOU 3121  C   VAL B 100     6858   2676   5395   -878   -510    321       C  
ATOM   3122  O   VAL B 100      90.271  49.095  42.170  1.00 39.66           O  
ANISOU 3122  O   VAL B 100     6972   2755   5343   -807   -463    376       O  
ATOM   3123  CB  VAL B 100      92.585  50.208  43.850  1.00 40.14           C  
ANISOU 3123  CB  VAL B 100     6926   2689   5638   -678   -950     42       C  
ATOM   3124  CG1 VAL B 100      93.658  50.286  42.767  1.00 39.27           C  
ANISOU 3124  CG1 VAL B 100     6483   2616   5822   -836   -875    -77       C  
ATOM   3125  CG2 VAL B 100      93.102  50.817  45.144  1.00 40.13           C  
ANISOU 3125  CG2 VAL B 100     7031   2596   5621   -540  -1239   -100       C  
ATOM   3126  N   TYR B 101      90.736  50.987  40.973  1.00 31.75           N  
ANISOU 3126  N   TYR B 101     5821   1722   4520  -1036   -382    355       N  
ATOM   3127  CA  TYR B 101      90.252  50.497  39.689  1.00 30.55           C  
ANISOU 3127  CA  TYR B 101     5655   1624   4328  -1115   -210    445       C  
ATOM   3128  C   TYR B 101      91.408  50.013  38.840  1.00 35.73           C  
ANISOU 3128  C   TYR B 101     6134   2316   5125  -1221   -116    368       C  
ATOM   3129  O   TYR B 101      92.376  50.744  38.641  1.00 34.40           O  
ANISOU 3129  O   TYR B 101     5853   2102   5114  -1346    -81    273       O  
ATOM   3130  CB  TYR B 101      89.436  51.566  38.937  1.00 31.26           C  
ANISOU 3130  CB  TYR B 101     5871   1657   4349  -1185   -147    535       C  
ATOM   3131  CG  TYR B 101      88.038  51.778  39.481  1.00 33.73           C  
ANISOU 3131  CG  TYR B 101     6300   1962   4556  -1062   -202    576       C  
ATOM   3132  CD1 TYR B 101      86.915  51.439  38.727  1.00 36.81           C  
ANISOU 3132  CD1 TYR B 101     6724   2380   4884  -1028   -158    622       C  
ATOM   3133  CD2 TYR B 101      87.834  52.311  40.755  1.00 33.48           C  
ANISOU 3133  CD2 TYR B 101     6326   1889   4506   -973   -297    527       C  
ATOM   3134  CE1 TYR B 101      85.623  51.633  39.225  1.00 39.17           C  
ANISOU 3134  CE1 TYR B 101     7051   2672   5161   -922   -189    594       C  
ATOM   3135  CE2 TYR B 101      86.551  52.507  41.263  1.00 33.62           C  
ANISOU 3135  CE2 TYR B 101     6417   1901   4455   -874   -289    521       C  
ATOM   3136  CZ  TYR B 101      85.447  52.175  40.493  1.00 43.30           C  
ANISOU 3136  CZ  TYR B 101     7614   3161   5677   -854   -226    542       C  
ATOM   3137  OH  TYR B 101      84.182  52.355  41.004  1.00 40.89           O  
ANISOU 3137  OH  TYR B 101     7307   2852   5376   -762   -199    473       O  
ATOM   3138  N   TYR B 102      91.305  48.766  38.343  1.00 34.37           N  
ANISOU 3138  N   TYR B 102     5921   2216   4921  -1182    -54    380       N  
ATOM   3139  CA  TYR B 102      92.314  48.144  37.481  1.00 35.78           C  
ANISOU 3139  CA  TYR B 102     5922   2441   5231  -1262     62    279       C  
ATOM   3140  C   TYR B 102      91.715  47.764  36.134  1.00 41.98           C  
ANISOU 3140  C   TYR B 102     6796   3265   5888  -1334    242    369       C  
ATOM   3141  O   TYR B 102      90.528  47.418  36.051  1.00 40.90           O  
ANISOU 3141  O   TYR B 102     6796   3140   5605  -1259    207    473       O  
ATOM   3142  CB  TYR B 102      92.865  46.822  38.090  1.00 37.67           C  
ANISOU 3142  CB  TYR B 102     6051   2709   5553  -1106    -72    172       C  
ATOM   3143  CG  TYR B 102      93.184  46.844  39.564  1.00 38.73           C  
ANISOU 3143  CG  TYR B 102     6219   2782   5714   -945   -333    103       C  
ATOM   3144  CD1 TYR B 102      94.488  47.033  40.008  1.00 39.77           C  
ANISOU 3144  CD1 TYR B 102     6143   2888   6081   -910   -491   -113       C  
ATOM   3145  CD2 TYR B 102      92.205  46.558  40.513  1.00 39.81           C  
ANISOU 3145  CD2 TYR B 102     6608   2875   5644   -816   -425    221       C  
ATOM   3146  CE1 TYR B 102      94.794  47.047  41.368  1.00 39.53           C  
ANISOU 3146  CE1 TYR B 102     6197   2780   6041   -721   -798   -197       C  
ATOM   3147  CE2 TYR B 102      92.499  46.557  41.875  1.00 40.81           C  
ANISOU 3147  CE2 TYR B 102     6865   2920   5721   -653   -662    164       C  
ATOM   3148  CZ  TYR B 102      93.799  46.793  42.299  1.00 48.35           C  
ANISOU 3148  CZ  TYR B 102     7654   3843   6875   -586   -883    -41       C  
ATOM   3149  OH  TYR B 102      94.100  46.803  43.645  1.00 51.16           O  
ANISOU 3149  OH  TYR B 102     8188   4100   7152   -388  -1182   -117       O  
ATOM   3150  N   CYS B 103      92.564  47.736  35.096  1.00 41.43           N  
ANISOU 3150  N   CYS B 103     6641   3213   5889  -1476    439    293       N  
ATOM   3151  CA  CYS B 103      92.182  47.183  33.814  1.00 43.46           C  
ANISOU 3151  CA  CYS B 103     7008   3505   6000  -1519    594    343       C  
ATOM   3152  C   CYS B 103      93.022  45.892  33.512  1.00 43.94           C  
ANISOU 3152  C   CYS B 103     6857   3643   6195  -1487    666    186       C  
ATOM   3153  O   CYS B 103      94.111  45.672  34.081  1.00 41.76           O  
ANISOU 3153  O   CYS B 103     6328   3379   6158  -1470    632     12       O  
ATOM   3154  CB  CYS B 103      92.194  48.199  32.675  1.00 46.25           C  
ANISOU 3154  CB  CYS B 103     7578   3782   6213  -1698    797    414       C  
ATOM   3155  SG  CYS B 103      93.836  48.795  32.214  1.00 52.22           S  
ANISOU 3155  SG  CYS B 103     8175   4494   7171  -1958   1114    253       S  
ATOM   3156  N   ALA B 104      92.436  44.994  32.733  1.00 38.76           N  
ANISOU 3156  N   ALA B 104     6296   3027   5406  -1438    704    220       N  
ATOM   3157  CA  ALA B 104      93.074  43.737  32.368  1.00 39.16           C  
ANISOU 3157  CA  ALA B 104     6186   3134   5560  -1385    760     74       C  
ATOM   3158  C   ALA B 104      92.796  43.470  30.907  1.00 43.60           C  
ANISOU 3158  C   ALA B 104     6911   3719   5936  -1463    955     88       C  
ATOM   3159  O   ALA B 104      91.770  43.921  30.379  1.00 41.91           O  
ANISOU 3159  O   ALA B 104     6958   3470   5494  -1474    925    230       O  
ATOM   3160  CB  ALA B 104      92.575  42.585  33.248  1.00 39.39           C  
ANISOU 3160  CB  ALA B 104     6198   3153   5617  -1193    535     89       C  
ATOM   3161  N   ALA B 105      93.735  42.784  30.244  1.00 40.60           N  
ANISOU 3161  N   ALA B 105     6386   3386   5653  -1502   1141    -88       N  
ATOM   3162  CA  ALA B 105      93.626  42.509  28.827  1.00 40.78           C  
ANISOU 3162  CA  ALA B 105     6598   3426   5471  -1578   1361   -106       C  
ATOM   3163  C   ALA B 105      93.673  41.037  28.534  1.00 45.37           C  
ANISOU 3163  C   ALA B 105     7077   4056   6105  -1446   1318   -234       C  
ATOM   3164  O   ALA B 105      94.602  40.349  28.955  1.00 46.21           O  
ANISOU 3164  O   ALA B 105     6893   4191   6473  -1382   1314   -420       O  
ATOM   3165  CB  ALA B 105      94.727  43.241  28.078  1.00 41.78           C  
ANISOU 3165  CB  ALA B 105     6704   3543   5628  -1802   1738   -217       C  
ATOM   3166  N   ASP B 106      92.660  40.543  27.825  1.00 42.21           N  
ANISOU 3166  N   ASP B 106     6912   3646   5478  -1385   1245   -160       N  
ATOM   3167  CA  ASP B 106      92.568  39.136  27.438  1.00 41.66           C  
ANISOU 3167  CA  ASP B 106     6792   3598   5440  -1268   1197   -281       C  
ATOM   3168  C   ASP B 106      92.986  39.022  25.981  1.00 45.88           C  
ANISOU 3168  C   ASP B 106     7481   4162   5789  -1353   1475   -394       C  
ATOM   3169  O   ASP B 106      92.309  39.621  25.142  1.00 46.53           O  
ANISOU 3169  O   ASP B 106     7905   4211   5564  -1405   1505   -287       O  
ATOM   3170  CB  ASP B 106      91.127  38.615  27.618  1.00 42.97           C  
ANISOU 3170  CB  ASP B 106     7094   3717   5516  -1158    934   -171       C  
ATOM   3171  CG  ASP B 106      90.948  37.103  27.546  1.00 47.54           C  
ANISOU 3171  CG  ASP B 106     7601   4273   6189  -1041    841   -287       C  
ATOM   3172  OD1 ASP B 106      91.923  36.399  27.197  1.00 48.32           O  
ANISOU 3172  OD1 ASP B 106     7579   4398   6382  -1015    965   -460       O  
ATOM   3173  OD2 ASP B 106      89.840  36.625  27.846  1.00 45.99           O  
ANISOU 3173  OD2 ASP B 106     7457   4016   5999   -984    658   -228       O  
ATOM   3174  N   PRO B 107      94.067  38.274  25.630  1.00 41.59           N  
ANISOU 3174  N   PRO B 107     6727   3668   5407  -1352   1671   -628       N  
ATOM   3175  CA  PRO B 107      94.441  38.161  24.207  1.00 41.29           C  
ANISOU 3175  CA  PRO B 107     6880   3655   5154  -1444   1994   -752       C  
ATOM   3176  C   PRO B 107      93.393  37.416  23.381  1.00 46.64           C  
ANISOU 3176  C   PRO B 107     7860   4307   5554  -1333   1837   -719       C  
ATOM   3177  O   PRO B 107      93.392  37.557  22.166  1.00 48.81           O  
ANISOU 3177  O   PRO B 107     8458   4572   5515  -1400   2042   -751       O  
ATOM   3178  CB  PRO B 107      95.800  37.465  24.245  1.00 43.11           C  
ANISOU 3178  CB  PRO B 107     6725   3946   5709  -1430   2194  -1057       C  
ATOM   3179  CG  PRO B 107      95.769  36.658  25.509  1.00 47.56           C  
ANISOU 3179  CG  PRO B 107     7000   4486   6584  -1228   1824  -1078       C  
ATOM   3180  CD  PRO B 107      94.981  37.490  26.489  1.00 43.34           C  
ANISOU 3180  CD  PRO B 107     6558   3907   6003  -1242   1591   -814       C  
ATOM   3181  N   PHE B 108      92.509  36.621  24.031  1.00 41.13           N  
ANISOU 3181  N   PHE B 108     7084   3577   4965  -1173   1485   -672       N  
ATOM   3182  CA  PHE B 108      91.382  35.974  23.356  1.00 39.73           C  
ANISOU 3182  CA  PHE B 108     7143   3358   4595  -1076   1285   -667       C  
ATOM   3183  C   PHE B 108      90.281  37.015  23.526  1.00 42.41           C  
ANISOU 3183  C   PHE B 108     7691   3653   4772  -1094   1092   -458       C  
ATOM   3184  O   PHE B 108      89.648  37.100  24.577  1.00 40.76           O  
ANISOU 3184  O   PHE B 108     7332   3416   4738  -1056    883   -356       O  
ATOM   3185  CB  PHE B 108      90.998  34.600  23.976  1.00 40.65           C  
ANISOU 3185  CB  PHE B 108     7060   3428   4959   -937   1052   -746       C  
ATOM   3186  CG  PHE B 108      92.051  33.523  23.862  1.00 41.06           C  
ANISOU 3186  CG  PHE B 108     6914   3492   5194   -869   1174   -972       C  
ATOM   3187  CD1 PHE B 108      92.307  32.903  22.649  1.00 43.30           C  
ANISOU 3187  CD1 PHE B 108     7329   3799   5325   -845   1318  -1160       C  
ATOM   3188  CD2 PHE B 108      92.775  33.114  24.975  1.00 42.21           C  
ANISOU 3188  CD2 PHE B 108     6769   3611   5659   -798   1112  -1018       C  
ATOM   3189  CE1 PHE B 108      93.283  31.906  22.547  1.00 43.79           C  
ANISOU 3189  CE1 PHE B 108     7183   3867   5588   -762   1427  -1405       C  
ATOM   3190  CE2 PHE B 108      93.753  32.125  24.871  1.00 43.82           C  
ANISOU 3190  CE2 PHE B 108     6781   3806   6063   -692   1172  -1262       C  
ATOM   3191  CZ  PHE B 108      94.001  31.527  23.661  1.00 41.97           C  
ANISOU 3191  CZ  PHE B 108     6630   3606   5711   -678   1341  -1461       C  
ATOM   3192  N   GLY B 109      90.177  37.880  22.527  1.00 39.85           N  
ANISOU 3192  N   GLY B 109     7731   3304   4105  -1155   1194   -405       N  
ATOM   3193  CA  GLY B 109      89.274  39.024  22.489  1.00 40.19           C  
ANISOU 3193  CA  GLY B 109     8039   3277   3954  -1152   1013   -231       C  
ATOM   3194  C   GLY B 109      87.791  38.754  22.628  1.00 45.27           C  
ANISOU 3194  C   GLY B 109     8698   3874   4629  -1001    605   -224       C  
ATOM   3195  O   GLY B 109      87.034  39.666  22.973  1.00 45.57           O  
ANISOU 3195  O   GLY B 109     8810   3861   4642   -973    417   -108       O  
ATOM   3196  N   GLU B 110      87.356  37.520  22.347  1.00 41.09           N  
ANISOU 3196  N   GLU B 110     8084   3348   4181   -906    467   -378       N  
ATOM   3197  CA  GLU B 110      85.944  37.176  22.446  1.00 40.73           C  
ANISOU 3197  CA  GLU B 110     7989   3248   4238   -790    105   -436       C  
ATOM   3198  C   GLU B 110      85.637  36.303  23.660  1.00 45.18           C  
ANISOU 3198  C   GLU B 110     8156   3809   5200   -803     58   -464       C  
ATOM   3199  O   GLU B 110      84.541  35.733  23.763  1.00 46.32           O  
ANISOU 3199  O   GLU B 110     8193   3898   5508   -749   -163   -568       O  
ATOM   3200  CB  GLU B 110      85.450  36.548  21.130  1.00 42.06           C  
ANISOU 3200  CB  GLU B 110     8425   3374   4184   -675    -68   -612       C  
ATOM   3201  CG  GLU B 110      85.445  37.508  19.947  1.00 51.51           C  
ANISOU 3201  CG  GLU B 110    10147   4515   4911   -628   -101   -567       C  
ATOM   3202  CD  GLU B 110      84.887  38.908  20.160  1.00 77.59           C  
ANISOU 3202  CD  GLU B 110    13629   7750   8100   -604   -259   -405       C  
ATOM   3203  OE1 GLU B 110      85.617  39.880  19.860  1.00 76.40           O  
ANISOU 3203  OE1 GLU B 110    13781   7567   7680   -700    -18   -255       O  
ATOM   3204  OE2 GLU B 110      83.731  39.038  20.628  1.00 70.39           O  
ANISOU 3204  OE2 GLU B 110    12552   6803   7391   -498   -603   -449       O  
ATOM   3205  N   ARG B 111      86.599  36.212  24.587  1.00 39.94           N  
ANISOU 3205  N   ARG B 111     7296   3182   4697   -876    265   -387       N  
ATOM   3206  CA  ARG B 111      86.463  35.374  25.765  1.00 39.05           C  
ANISOU 3206  CA  ARG B 111     6922   3026   4890   -881    242   -387       C  
ATOM   3207  C   ARG B 111      86.091  36.130  27.038  1.00 42.09           C  
ANISOU 3207  C   ARG B 111     7196   3397   5401   -921    216   -237       C  
ATOM   3208  O   ARG B 111      85.072  35.805  27.634  1.00 41.98           O  
ANISOU 3208  O   ARG B 111     7086   3316   5548   -926    113   -250       O  
ATOM   3209  CB  ARG B 111      87.735  34.514  25.981  1.00 36.93           C  
ANISOU 3209  CB  ARG B 111     6541   2767   4725   -871    406   -453       C  
ATOM   3210  CG  ARG B 111      87.803  33.837  27.350  1.00 30.90           C  
ANISOU 3210  CG  ARG B 111     5609   1918   4212   -857    374   -403       C  
ATOM   3211  CD  ARG B 111      89.007  32.954  27.522  1.00 34.85           C  
ANISOU 3211  CD  ARG B 111     6017   2396   4830   -788    445   -504       C  
ATOM   3212  NE  ARG B 111      90.196  33.735  27.858  1.00 35.29           N  
ANISOU 3212  NE  ARG B 111     5972   2535   4903   -798    561   -488       N  
ATOM   3213  CZ  ARG B 111      91.344  33.212  28.283  1.00 54.41           C  
ANISOU 3213  CZ  ARG B 111     8244   4937   7492   -714    579   -598       C  
ATOM   3214  NH1 ARG B 111      91.475  31.893  28.415  1.00 38.00           N  
ANISOU 3214  NH1 ARG B 111     6152   2745   5542   -598    483   -704       N  
ATOM   3215  NH2 ARG B 111      92.367  34.000  28.583  1.00 47.63           N  
ANISOU 3215  NH2 ARG B 111     7243   4153   6703   -735    670   -629       N  
ATOM   3216  N   LEU B 112      86.923  37.089  27.478  1.00 38.20           N  
ANISOU 3216  N   LEU B 112     6704   2955   4855   -964    332   -123       N  
ATOM   3217  CA  LEU B 112      86.801  37.768  28.776  1.00 38.29           C  
ANISOU 3217  CA  LEU B 112     6622   2951   4975   -991    318      3       C  
ATOM   3218  C   LEU B 112      85.380  38.191  29.196  1.00 41.93           C  
ANISOU 3218  C   LEU B 112     7071   3370   5489   -983    177     31       C  
ATOM   3219  O   LEU B 112      84.944  37.826  30.295  1.00 40.96           O  
ANISOU 3219  O   LEU B 112     6846   3192   5527  -1000    186     56       O  
ATOM   3220  CB  LEU B 112      87.756  38.972  28.883  1.00 38.15           C  
ANISOU 3220  CB  LEU B 112     6636   2985   4874  -1046    430     86       C  
ATOM   3221  CG  LEU B 112      87.826  39.693  30.233  1.00 42.87           C  
ANISOU 3221  CG  LEU B 112     7152   3566   5572  -1060    402    193       C  
ATOM   3222  CD1 LEU B 112      88.173  38.744  31.381  1.00 42.52           C  
ANISOU 3222  CD1 LEU B 112     6989   3473   5695  -1009    380    179       C  
ATOM   3223  CD2 LEU B 112      88.760  40.900  30.171  1.00 45.05           C  
ANISOU 3223  CD2 LEU B 112     7456   3873   5788  -1136    508    240       C  
ATOM   3224  N   CYS B 113      84.681  38.936  28.332  1.00 37.89           N  
ANISOU 3224  N   CYS B 113     6685   2866   4845   -950     52      8       N  
ATOM   3225  CA  CYS B 113      83.384  39.535  28.616  1.00 37.68           C  
ANISOU 3225  CA  CYS B 113     6612   2804   4900   -912   -114    -19       C  
ATOM   3226  C   CYS B 113      82.210  38.522  28.722  1.00 40.80           C  
ANISOU 3226  C   CYS B 113     6829   3144   5527   -904   -204   -186       C  
ATOM   3227  O   CYS B 113      81.105  38.930  29.103  1.00 41.07           O  
ANISOU 3227  O   CYS B 113     6740   3150   5716   -886   -304   -263       O  
ATOM   3228  CB  CYS B 113      83.097  40.651  27.619  1.00 38.75           C  
ANISOU 3228  CB  CYS B 113     6981   2929   4814   -837   -276     -9       C  
ATOM   3229  SG  CYS B 113      84.478  41.826  27.390  1.00 43.45           S  
ANISOU 3229  SG  CYS B 113     7818   3539   5151   -911    -92    172       S  
ATOM   3230  N   ILE B 114      82.448  37.212  28.436  1.00 34.91           N  
ANISOU 3230  N   ILE B 114     6048   2369   4846   -929   -149   -268       N  
ATOM   3231  CA  ILE B 114      81.445  36.155  28.618  1.00 33.44           C  
ANISOU 3231  CA  ILE B 114     5692   2095   4919   -969   -180   -432       C  
ATOM   3232  C   ILE B 114      81.257  35.965  30.152  1.00 37.10           C  
ANISOU 3232  C   ILE B 114     6041   2490   5565  -1078     17   -346       C  
ATOM   3233  O   ILE B 114      80.134  35.806  30.637  1.00 36.64           O  
ANISOU 3233  O   ILE B 114     5820   2365   5737  -1146     45   -460       O  
ATOM   3234  CB  ILE B 114      81.886  34.790  27.975  1.00 35.49           C  
ANISOU 3234  CB  ILE B 114     5990   2309   5188   -971   -159   -528       C  
ATOM   3235  CG1 ILE B 114      82.146  34.895  26.452  1.00 35.52           C  
ANISOU 3235  CG1 ILE B 114     6171   2370   4956   -865   -315   -624       C  
ATOM   3236  CG2 ILE B 114      80.883  33.658  28.300  1.00 33.96           C  
ANISOU 3236  CG2 ILE B 114     5623   1979   5300  -1059   -145   -691       C  
ATOM   3237  CD1 ILE B 114      82.918  33.617  25.852  1.00 40.28           C  
ANISOU 3237  CD1 ILE B 114     6835   2945   5525   -853   -245   -711       C  
ATOM   3238  N   ASP B 115      82.377  35.938  30.890  1.00 32.76           N  
ANISOU 3238  N   ASP B 115     5591   1943   4913  -1090    157   -174       N  
ATOM   3239  CA  ASP B 115      82.414  35.669  32.323  1.00 32.17           C  
ANISOU 3239  CA  ASP B 115     5535   1775   4915  -1160    323    -72       C  
ATOM   3240  C   ASP B 115      83.634  36.426  32.903  1.00 37.09           C  
ANISOU 3240  C   ASP B 115     6261   2461   5370  -1101    338     92       C  
ATOM   3241  O   ASP B 115      84.664  35.787  33.183  1.00 36.84           O  
ANISOU 3241  O   ASP B 115     6308   2389   5301  -1060    359    136       O  
ATOM   3242  CB  ASP B 115      82.558  34.146  32.496  1.00 32.91           C  
ANISOU 3242  CB  ASP B 115     5685   1717   5103  -1204    405   -109       C  
ATOM   3243  CG  ASP B 115      82.262  33.564  33.857  1.00 43.32           C  
ANISOU 3243  CG  ASP B 115     7113   2856   6492  -1300    593    -31       C  
ATOM   3244  OD1 ASP B 115      82.229  34.331  34.843  1.00 45.36           O  
ANISOU 3244  OD1 ASP B 115     7431   3122   6681  -1312    672     78       O  
ATOM   3245  OD2 ASP B 115      82.088  32.335  33.945  1.00 46.56           O  
ANISOU 3245  OD2 ASP B 115     7596   3093   7002  -1364    670    -75       O  
ATOM   3246  N   PRO B 116      83.544  37.781  33.069  1.00 33.36           N  
ANISOU 3246  N   PRO B 116     5777   2073   4825  -1084    301    150       N  
ATOM   3247  CA  PRO B 116      84.717  38.557  33.523  1.00 32.72           C  
ANISOU 3247  CA  PRO B 116     5763   2045   4625  -1046    301    265       C  
ATOM   3248  C   PRO B 116      85.287  38.180  34.891  1.00 36.89           C  
ANISOU 3248  C   PRO B 116     6376   2485   5155  -1029    355    346       C  
ATOM   3249  O   PRO B 116      86.510  38.110  35.018  1.00 35.11           O  
ANISOU 3249  O   PRO B 116     6171   2273   4896   -968    311    362       O  
ATOM   3250  CB  PRO B 116      84.229  40.008  33.477  1.00 33.71           C  
ANISOU 3250  CB  PRO B 116     5880   2230   4699  -1043    244    295       C  
ATOM   3251  CG  PRO B 116      83.078  40.003  32.571  1.00 37.40           C  
ANISOU 3251  CG  PRO B 116     6290   2701   5221  -1033    152    178       C  
ATOM   3252  CD  PRO B 116      82.415  38.689  32.764  1.00 34.30           C  
ANISOU 3252  CD  PRO B 116     5813   2229   4991  -1082    220     82       C  
ATOM   3253  N   ASN B 117      84.432  37.879  35.881  1.00 35.80           N  
ANISOU 3253  N   ASN B 117     6303   2241   5058  -1076    451    371       N  
ATOM   3254  CA  ASN B 117      84.903  37.499  37.220  1.00 36.32           C  
ANISOU 3254  CA  ASN B 117     6569   2180   5050  -1042    490    460       C  
ATOM   3255  C   ASN B 117      85.577  36.134  37.275  1.00 41.55           C  
ANISOU 3255  C   ASN B 117     7360   2710   5716   -988    458    458       C  
ATOM   3256  O   ASN B 117      86.426  35.932  38.133  1.00 44.45           O  
ANISOU 3256  O   ASN B 117     7908   2985   5995   -883    371    514       O  
ATOM   3257  CB  ASN B 117      83.801  37.616  38.268  1.00 34.30           C  
ANISOU 3257  CB  ASN B 117     6416   1827   4790  -1130    667    487       C  
ATOM   3258  CG  ASN B 117      83.514  39.061  38.578  1.00 43.55           C  
ANISOU 3258  CG  ASN B 117     7514   3104   5928  -1119    650    495       C  
ATOM   3259  OD1 ASN B 117      84.423  39.853  38.871  1.00 38.31           O  
ANISOU 3259  OD1 ASN B 117     6892   2497   5168  -1034    522    550       O  
ATOM   3260  ND2 ASN B 117      82.251  39.441  38.504  1.00 32.14           N  
ANISOU 3260  ND2 ASN B 117     5935   1677   4600  -1200    764    406       N  
ATOM   3261  N   THR B 118      85.255  35.218  36.370  1.00 35.64           N  
ANISOU 3261  N   THR B 118     6537   1937   5069  -1030    483    374       N  
ATOM   3262  CA  THR B 118      85.934  33.927  36.362  1.00 34.64           C  
ANISOU 3262  CA  THR B 118     6537   1667   4959   -957    430    354       C  
ATOM   3263  C   THR B 118      87.175  34.025  35.480  1.00 38.59           C  
ANISOU 3263  C   THR B 118     6887   2300   5474   -838    286    270       C  
ATOM   3264  O   THR B 118      88.249  33.601  35.899  1.00 38.97           O  
ANISOU 3264  O   THR B 118     7009   2280   5520   -700    165    254       O  
ATOM   3265  CB  THR B 118      84.990  32.797  35.866  1.00 39.37           C  
ANISOU 3265  CB  THR B 118     7137   2139   5683  -1070    539    277       C  
ATOM   3266  OG1 THR B 118      83.779  32.809  36.620  1.00 42.49           O  
ANISOU 3266  OG1 THR B 118     7604   2422   6119  -1227    742    308       O  
ATOM   3267  CG2 THR B 118      85.625  31.403  35.916  1.00 37.72           C  
ANISOU 3267  CG2 THR B 118     7108   1732   5492   -990    479    260       C  
ATOM   3268  N   PHE B 119      87.013  34.559  34.246  1.00 33.87           N  
ANISOU 3268  N   PHE B 119     6100   1875   4894   -886    303    194       N  
ATOM   3269  CA  PHE B 119      88.046  34.577  33.228  1.00 33.97           C  
ANISOU 3269  CA  PHE B 119     5991   2003   4911   -825    266     89       C  
ATOM   3270  C   PHE B 119      89.219  35.528  33.565  1.00 39.50           C  
ANISOU 3270  C   PHE B 119     6611   2797   5599   -774    231     94       C  
ATOM   3271  O   PHE B 119      90.320  35.313  33.058  1.00 38.64           O  
ANISOU 3271  O   PHE B 119     6385   2741   5554   -716    229    -30       O  
ATOM   3272  CB  PHE B 119      87.433  34.830  31.829  1.00 35.62           C  
ANISOU 3272  CB  PHE B 119     6134   2323   5076   -893    307     15       C  
ATOM   3273  CG  PHE B 119      86.425  33.793  31.332  1.00 36.96           C  
ANISOU 3273  CG  PHE B 119     6325   2403   5313   -928    297    -67       C  
ATOM   3274  CD1 PHE B 119      86.236  32.589  32.009  1.00 40.90           C  
ANISOU 3274  CD1 PHE B 119     6903   2718   5919   -925    307    -72       C  
ATOM   3275  CD2 PHE B 119      85.668  34.025  30.193  1.00 38.34           C  
ANISOU 3275  CD2 PHE B 119     6473   2650   5446   -960    259   -154       C  
ATOM   3276  CE1 PHE B 119      85.324  31.628  31.540  1.00 41.69           C  
ANISOU 3276  CE1 PHE B 119     7003   2713   6126   -988    315   -176       C  
ATOM   3277  CE2 PHE B 119      84.768  33.062  29.715  1.00 40.63           C  
ANISOU 3277  CE2 PHE B 119     6746   2850   5840   -988    214   -280       C  
ATOM   3278  CZ  PHE B 119      84.595  31.876  30.396  1.00 39.84           C  
ANISOU 3278  CZ  PHE B 119     6673   2575   5891  -1020    261   -296       C  
ATOM   3279  N   ALA B 120      89.016  36.505  34.484  1.00 37.58           N  
ANISOU 3279  N   ALA B 120     6413   2558   5307   -795    211    202       N  
ATOM   3280  CA  ALA B 120      90.057  37.414  34.984  1.00 37.68           C  
ANISOU 3280  CA  ALA B 120     6349   2625   5342   -755    150    189       C  
ATOM   3281  C   ALA B 120      91.181  36.619  35.648  1.00 39.73           C  
ANISOU 3281  C   ALA B 120     6601   2791   5702   -592     -4     93       C  
ATOM   3282  O   ALA B 120      92.333  37.032  35.596  1.00 38.38           O  
ANISOU 3282  O   ALA B 120     6250   2682   5650   -545    -58    -35       O  
ATOM   3283  CB  ALA B 120      89.466  38.380  35.997  1.00 38.85           C  
ANISOU 3283  CB  ALA B 120     6599   2752   5409   -784    129    312       C  
ATOM   3284  N   GLY B 121      90.830  35.477  36.238  1.00 37.16           N  
ANISOU 3284  N   GLY B 121     6476   2294   5349   -508    -76    132       N  
ATOM   3285  CA  GLY B 121      91.756  34.552  36.889  1.00 37.09           C  
ANISOU 3285  CA  GLY B 121     6556   2132   5406   -305   -286     47       C  
ATOM   3286  C   GLY B 121      92.732  33.893  35.935  1.00 43.22           C  
ANISOU 3286  C   GLY B 121     7101   2960   6362   -221   -316   -167       C  
ATOM   3287  O   GLY B 121      93.731  33.336  36.382  1.00 45.06           O  
ANISOU 3287  O   GLY B 121     7308   3097   6715    -17   -535   -310       O  
ATOM   3288  N   TYR B 122      92.451  33.942  34.614  1.00 39.61           N  
ANISOU 3288  N   TYR B 122     6488   2643   5920   -357   -112   -218       N  
ATOM   3289  CA  TYR B 122      93.284  33.356  33.560  1.00 39.05           C  
ANISOU 3289  CA  TYR B 122     6209   2637   5989   -307    -61   -439       C  
ATOM   3290  C   TYR B 122      94.300  34.373  32.991  1.00 44.79           C  
ANISOU 3290  C   TYR B 122     6643   3549   6828   -375     65   -591       C  
ATOM   3291  O   TYR B 122      95.254  33.983  32.314  1.00 45.11           O  
ANISOU 3291  O   TYR B 122     6465   3643   7030   -329    135   -827       O  
ATOM   3292  CB  TYR B 122      92.409  32.815  32.395  1.00 39.55           C  
ANISOU 3292  CB  TYR B 122     6330   2732   5965   -416    100   -429       C  
ATOM   3293  CG  TYR B 122      91.243  31.907  32.747  1.00 40.86           C  
ANISOU 3293  CG  TYR B 122     6737   2723   6066   -430     55   -308       C  
ATOM   3294  CD1 TYR B 122      91.292  31.070  33.859  1.00 42.74           C  
ANISOU 3294  CD1 TYR B 122     7182   2732   6327   -306   -104   -253       C  
ATOM   3295  CD2 TYR B 122      90.131  31.812  31.912  1.00 41.10           C  
ANISOU 3295  CD2 TYR B 122     6806   2787   6022   -564    168   -280       C  
ATOM   3296  CE1 TYR B 122      90.233  30.221  34.173  1.00 43.14           C  
ANISOU 3296  CE1 TYR B 122     7475   2585   6330   -370    -72   -148       C  
ATOM   3297  CE2 TYR B 122      89.081  30.934  32.198  1.00 41.05           C  
ANISOU 3297  CE2 TYR B 122     6963   2607   6028   -610    159   -223       C  
ATOM   3298  CZ  TYR B 122      89.121  30.168  33.350  1.00 48.34           C  
ANISOU 3298  CZ  TYR B 122     8091   3297   6978   -540     78   -146       C  
ATOM   3299  OH  TYR B 122      88.078  29.325  33.671  1.00 51.29           O  
ANISOU 3299  OH  TYR B 122     8650   3464   7372   -635    140    -89       O  
ATOM   3300  N   LEU B 123      94.081  35.670  33.266  1.00 41.92           N  
ANISOU 3300  N   LEU B 123     6276   3261   6390   -500    125   -473       N  
ATOM   3301  CA  LEU B 123      94.831  36.801  32.722  1.00 40.36           C  
ANISOU 3301  CA  LEU B 123     5865   3200   6269   -636    305   -572       C  
ATOM   3302  C   LEU B 123      96.071  37.159  33.477  1.00 47.06           C  
ANISOU 3302  C   LEU B 123     6467   4040   7373   -547    169   -760       C  
ATOM   3303  O   LEU B 123      96.050  37.293  34.698  1.00 48.27           O  
ANISOU 3303  O   LEU B 123     6707   4102   7531   -428    -87   -697       O  
ATOM   3304  CB  LEU B 123      93.926  38.033  32.593  1.00 39.28           C  
ANISOU 3304  CB  LEU B 123     5883   3114   5929   -812    420   -358       C  
ATOM   3305  CG  LEU B 123      92.547  37.854  31.928  1.00 42.35           C  
ANISOU 3305  CG  LEU B 123     6500   3501   6091   -876    480   -198       C  
ATOM   3306  CD1 LEU B 123      91.887  39.211  31.675  1.00 41.61           C  
ANISOU 3306  CD1 LEU B 123     6524   3447   5837  -1014    558    -49       C  
ATOM   3307  CD2 LEU B 123      92.631  37.010  30.625  1.00 42.34           C  
ANISOU 3307  CD2 LEU B 123     6496   3538   6054   -887    616   -321       C  
ATOM   3308  N   GLU B 124      97.153  37.340  32.742  1.00 45.04           N  
ANISOU 3308  N   GLU B 124     5905   3872   7336   -610    350  -1019       N  
ATOM   3309  CA  GLU B 124      98.444  37.746  33.292  1.00 45.77           C  
ANISOU 3309  CA  GLU B 124     5655   3969   7767   -552    247  -1290       C  
ATOM   3310  C   GLU B 124      98.691  39.270  33.148  1.00 49.48           C  
ANISOU 3310  C   GLU B 124     6023   4509   8269   -807    473  -1272       C  
ATOM   3311  O   GLU B 124      99.373  39.849  34.000  1.00 50.83           O  
ANISOU 3311  O   GLU B 124     6003   4648   8660   -764    294  -1403       O  
ATOM   3312  CB  GLU B 124      99.596  36.904  32.702  1.00 47.68           C  
ANISOU 3312  CB  GLU B 124     5543   4241   8332   -455    309  -1670       C  
ATOM   3313  CG  GLU B 124      99.565  36.721  31.188  1.00 61.39           C  
ANISOU 3313  CG  GLU B 124     7260   6084   9982   -644    748  -1728       C  
ATOM   3314  CD  GLU B 124     100.853  36.192  30.590  1.00 91.40           C  
ANISOU 3314  CD  GLU B 124    10648   9934  14146   -589    896  -2163       C  
ATOM   3315  OE1 GLU B 124     100.890  34.996  30.215  1.00 93.43           O  
ANISOU 3315  OE1 GLU B 124    10928  10159  14412   -417    826  -2265       O  
ATOM   3316  OE2 GLU B 124     101.827  36.975  30.500  1.00 87.51           O  
ANISOU 3316  OE2 GLU B 124     9788   9503  13961   -724   1095  -2430       O  
ATOM   3317  N   THR B 125      98.098  39.929  32.109  1.00 42.98           N  
ANISOU 3317  N   THR B 125     5375   3746   7207  -1056    827  -1106       N  
ATOM   3318  CA  THR B 125      98.300  41.364  31.892  1.00 41.12           C  
ANISOU 3318  CA  THR B 125     5125   3528   6972  -1311   1065  -1068       C  
ATOM   3319  C   THR B 125      97.243  42.214  32.637  1.00 42.27           C  
ANISOU 3319  C   THR B 125     5565   3618   6878  -1320    889   -761       C  
ATOM   3320  O   THR B 125      96.051  42.192  32.323  1.00 39.02           O  
ANISOU 3320  O   THR B 125     5471   3198   6156  -1327    892   -511       O  
ATOM   3321  CB  THR B 125      98.472  41.764  30.386  1.00 45.72           C  
ANISOU 3321  CB  THR B 125     5782   4158   7430  -1577   1556  -1094       C  
ATOM   3322  OG1 THR B 125      97.365  42.537  29.908  1.00 53.79           O  
ANISOU 3322  OG1 THR B 125     7236   5149   8052  -1684   1633   -775       O  
ATOM   3323  CG2 THR B 125      98.751  40.605  29.464  1.00 31.29           C  
ANISOU 3323  CG2 THR B 125     3851   2389   5649  -1520   1721  -1292       C  
ATOM   3324  N   TRP B 126      97.734  42.995  33.612  1.00 40.99           N  
ANISOU 3324  N   TRP B 126     5262   3414   6900  -1316    731   -829       N  
ATOM   3325  CA  TRP B 126      96.980  43.910  34.466  1.00 41.06           C  
ANISOU 3325  CA  TRP B 126     5487   3364   6749  -1314    561   -613       C  
ATOM   3326  C   TRP B 126      97.763  45.195  34.583  1.00 49.30           C  
ANISOU 3326  C   TRP B 126     6361   4375   7995  -1504    674   -731       C  
ATOM   3327  O   TRP B 126      98.983  45.202  34.359  1.00 50.92           O  
ANISOU 3327  O   TRP B 126     6209   4596   8540  -1587    797  -1031       O  
ATOM   3328  CB  TRP B 126      96.812  43.309  35.880  1.00 39.48           C  
ANISOU 3328  CB  TRP B 126     5335   3106   6561  -1038    146   -604       C  
ATOM   3329  CG  TRP B 126      95.909  42.099  35.963  1.00 39.84           C  
ANISOU 3329  CG  TRP B 126     5612   3130   6396   -878     42   -455       C  
ATOM   3330  CD1 TRP B 126      96.236  40.806  35.680  1.00 42.55           C  
ANISOU 3330  CD1 TRP B 126     5884   3469   6815   -746     -3   -572       C  
ATOM   3331  CD2 TRP B 126      94.525  42.087  36.360  1.00 39.46           C  
ANISOU 3331  CD2 TRP B 126     5887   3043   6064   -850     -8   -191       C  
ATOM   3332  NE1 TRP B 126      95.135  39.989  35.852  1.00 41.84           N  
ANISOU 3332  NE1 TRP B 126     6077   3323   6496   -661    -68   -378       N  
ATOM   3333  CE2 TRP B 126      94.077  40.748  36.284  1.00 42.99           C  
ANISOU 3333  CE2 TRP B 126     6446   3453   6435   -731    -57   -156       C  
ATOM   3334  CE3 TRP B 126      93.619  43.086  36.781  1.00 40.40           C  
ANISOU 3334  CE3 TRP B 126     6192   3144   6016   -916     -5    -11       C  
ATOM   3335  CZ2 TRP B 126      92.767  40.376  36.616  1.00 41.85           C  
ANISOU 3335  CZ2 TRP B 126     6569   3253   6080   -710    -68     41       C  
ATOM   3336  CZ3 TRP B 126      92.312  42.723  37.071  1.00 41.61           C  
ANISOU 3336  CZ3 TRP B 126     6583   3262   5964   -873    -22    167       C  
ATOM   3337  CH2 TRP B 126      91.894  41.382  36.982  1.00 42.08           C  
ANISOU 3337  CH2 TRP B 126     6725   3285   5976   -789    -34    187       C  
ATOM   3338  N   GLY B 127      97.062  46.273  34.935  1.00 45.58           N  
ANISOU 3338  N   GLY B 127     6123   3845   7350  -1575    637   -527       N  
ATOM   3339  CA  GLY B 127      97.672  47.560  35.220  1.00 45.01           C  
ANISOU 3339  CA  GLY B 127     5942   3701   7457  -1747    694   -616       C  
ATOM   3340  C   GLY B 127      97.948  47.664  36.708  1.00 50.54           C  
ANISOU 3340  C   GLY B 127     6527   4363   8313  -1547    289   -727       C  
ATOM   3341  O   GLY B 127      97.534  46.797  37.480  1.00 50.02           O  
ANISOU 3341  O   GLY B 127     6561   4307   8136  -1287     -2   -677       O  
ATOM   3342  N   GLN B 128      98.646  48.722  37.132  1.00 50.19           N  
ANISOU 3342  N   GLN B 128     6312   4248   8509  -1669    268   -883       N  
ATOM   3343  CA  GLN B 128      99.013  48.974  38.537  1.00 50.23           C  
ANISOU 3343  CA  GLN B 128     6220   4196   8668  -1481   -145  -1034       C  
ATOM   3344  C   GLN B 128      97.815  49.369  39.437  1.00 53.29           C  
ANISOU 3344  C   GLN B 128     7005   4536   8707  -1341   -364   -764       C  
ATOM   3345  O   GLN B 128      97.896  49.238  40.662  1.00 53.82           O  
ANISOU 3345  O   GLN B 128     7122   4560   8769  -1115   -731   -839       O  
ATOM   3346  CB  GLN B 128     100.149  50.022  38.608  1.00 51.57           C  
ANISOU 3346  CB  GLN B 128     6039   4296   9260  -1686    -80  -1338       C  
ATOM   3347  CG  GLN B 128      99.723  51.502  38.462  1.00 73.72           C  
ANISOU 3347  CG  GLN B 128     9039   6991  11979  -1947    121  -1183       C  
ATOM   3348  CD  GLN B 128      99.206  51.938  37.098  1.00 89.20           C  
ANISOU 3348  CD  GLN B 128    11234   8929  13728  -2231    602   -954       C  
ATOM   3349  OE1 GLN B 128      99.325  51.221  36.086  1.00 83.26           O  
ANISOU 3349  OE1 GLN B 128    10436   8253  12948  -2304    877   -962       O  
ATOM   3350  NE2 GLN B 128      98.624  53.150  37.049  1.00 68.57           N  
ANISOU 3350  NE2 GLN B 128     8922   6188  10944  -2376    687   -756       N  
ATOM   3351  N   GLY B 129      96.739  49.844  38.811  1.00 47.51           N  
ANISOU 3351  N   GLY B 129     6561   3800   7690  -1463   -143   -482       N  
ATOM   3352  CA  GLY B 129      95.529  50.305  39.476  1.00 46.44           C  
ANISOU 3352  CA  GLY B 129     6755   3626   7265  -1363   -272   -260       C  
ATOM   3353  C   GLY B 129      95.524  51.806  39.681  1.00 48.07           C  
ANISOU 3353  C   GLY B 129     7021   3724   7520  -1503   -258   -257       C  
ATOM   3354  O   GLY B 129      96.591  52.409  39.769  1.00 47.78           O  
ANISOU 3354  O   GLY B 129     6747   3628   7780  -1628   -258   -472       O  
ATOM   3355  N   THR B 130      94.324  52.423  39.736  1.00 43.69           N  
ANISOU 3355  N   THR B 130     6762   3129   6711  -1484   -247    -43       N  
ATOM   3356  CA  THR B 130      94.143  53.863  39.964  1.00 43.26           C  
ANISOU 3356  CA  THR B 130     6827   2943   6666  -1581   -263    -19       C  
ATOM   3357  C   THR B 130      93.054  54.081  41.033  1.00 46.84           C  
ANISOU 3357  C   THR B 130     7507   3385   6904  -1372   -469     73       C  
ATOM   3358  O   THR B 130      91.965  53.512  40.930  1.00 46.75           O  
ANISOU 3358  O   THR B 130     7645   3437   6679  -1265   -435    219       O  
ATOM   3359  CB  THR B 130      93.947  54.638  38.628  1.00 46.94           C  
ANISOU 3359  CB  THR B 130     7437   3317   7080  -1819     26    109       C  
ATOM   3360  OG1 THR B 130      94.425  55.971  38.787  1.00 48.00           O  
ANISOU 3360  OG1 THR B 130     7599   3281   7357  -1980     41     45       O  
ATOM   3361  CG2 THR B 130      92.500  54.617  38.077  1.00 40.29           C  
ANISOU 3361  CG2 THR B 130     6895   2484   5929  -1731     55    343       C  
ATOM   3362  N   GLN B 131      93.385  54.842  42.091  1.00 42.97           N  
ANISOU 3362  N   GLN B 131     7021   2812   6492  -1316   -673    -52       N  
ATOM   3363  CA  GLN B 131      92.473  55.145  43.199  1.00 42.17           C  
ANISOU 3363  CA  GLN B 131     7145   2688   6190  -1127   -838    -10       C  
ATOM   3364  C   GLN B 131      91.363  56.109  42.771  1.00 44.93           C  
ANISOU 3364  C   GLN B 131     7686   2967   6417  -1169   -734    133       C  
ATOM   3365  O   GLN B 131      91.644  57.154  42.206  1.00 44.84           O  
ANISOU 3365  O   GLN B 131     7691   2833   6515  -1330   -672    134       O  
ATOM   3366  CB  GLN B 131      93.246  55.742  44.401  1.00 42.84           C  
ANISOU 3366  CB  GLN B 131     7201   2687   6389  -1049  -1111   -218       C  
ATOM   3367  CG  GLN B 131      92.394  55.989  45.668  1.00 36.47           C  
ANISOU 3367  CG  GLN B 131     6672   1853   5334   -837  -1268   -205       C  
ATOM   3368  CD  GLN B 131      91.751  54.739  46.230  1.00 46.89           C  
ANISOU 3368  CD  GLN B 131     8164   3260   6392   -653  -1264   -120       C  
ATOM   3369  OE1 GLN B 131      92.419  53.764  46.584  1.00 45.53           O  
ANISOU 3369  OE1 GLN B 131     7968   3112   6221   -549  -1402   -190       O  
ATOM   3370  NE2 GLN B 131      90.434  54.740  46.329  1.00 37.13           N  
ANISOU 3370  NE2 GLN B 131     7111   2049   4946   -607  -1103     13       N  
ATOM   3371  N   VAL B 132      90.116  55.752  43.075  1.00 40.93           N  
ANISOU 3371  N   VAL B 132     7329   2518   5704  -1022   -716    229       N  
ATOM   3372  CA  VAL B 132      88.906  56.536  42.839  1.00 40.56           C  
ANISOU 3372  CA  VAL B 132     7431   2414   5565   -986   -677    307       C  
ATOM   3373  C   VAL B 132      88.271  56.713  44.237  1.00 46.42           C  
ANISOU 3373  C   VAL B 132     8292   3154   6190   -807   -773    228       C  
ATOM   3374  O   VAL B 132      88.034  55.718  44.941  1.00 47.16           O  
ANISOU 3374  O   VAL B 132     8423   3335   6161   -705   -747    220       O  
ATOM   3375  CB  VAL B 132      87.970  55.824  41.810  1.00 43.93           C  
ANISOU 3375  CB  VAL B 132     7862   2919   5912   -981   -539    427       C  
ATOM   3376  CG1 VAL B 132      86.565  56.419  41.799  1.00 43.93           C  
ANISOU 3376  CG1 VAL B 132     7967   2877   5848   -867   -563    437       C  
ATOM   3377  CG2 VAL B 132      88.572  55.846  40.405  1.00 43.07           C  
ANISOU 3377  CG2 VAL B 132     7729   2779   5858  -1155   -433    502       C  
ATOM   3378  N   THR B 133      88.067  57.971  44.663  1.00 43.17           N  
ANISOU 3378  N   THR B 133     7980   2622   5803   -778   -870    162       N  
ATOM   3379  CA  THR B 133      87.503  58.276  45.982  1.00 42.94           C  
ANISOU 3379  CA  THR B 133     8089   2576   5650   -613   -939     59       C  
ATOM   3380  C   THR B 133      86.276  59.179  45.863  1.00 46.21           C  
ANISOU 3380  C   THR B 133     8577   2925   6057   -535   -909     40       C  
ATOM   3381  O   THR B 133      86.389  60.294  45.384  1.00 45.25           O  
ANISOU 3381  O   THR B 133     8494   2659   6040   -584  -1000     36       O  
ATOM   3382  CB  THR B 133      88.593  58.822  46.923  1.00 52.13           C  
ANISOU 3382  CB  THR B 133     9295   3654   6859   -598  -1150    -84       C  
ATOM   3383  OG1 THR B 133      89.571  57.799  47.129  1.00 54.48           O  
ANISOU 3383  OG1 THR B 133     9508   4021   7172   -604  -1218   -110       O  
ATOM   3384  CG2 THR B 133      88.037  59.270  48.271  1.00 48.67           C  
ANISOU 3384  CG2 THR B 133     9066   3177   6247   -419  -1227   -204       C  
ATOM   3385  N   VAL B 134      85.104  58.680  46.274  1.00 43.59           N  
ANISOU 3385  N   VAL B 134     8262   2677   5623   -418   -774      8       N  
ATOM   3386  CA  VAL B 134      83.861  59.447  46.212  1.00 43.48           C  
ANISOU 3386  CA  VAL B 134     8252   2614   5656   -309   -753    -78       C  
ATOM   3387  C   VAL B 134      83.506  59.882  47.626  1.00 52.15           C  
ANISOU 3387  C   VAL B 134     9482   3688   6646   -181   -732   -240       C  
ATOM   3388  O   VAL B 134      83.143  59.051  48.454  1.00 53.11           O  
ANISOU 3388  O   VAL B 134     9663   3899   6617   -141   -551   -281       O  
ATOM   3389  CB  VAL B 134      82.699  58.697  45.513  1.00 46.16           C  
ANISOU 3389  CB  VAL B 134     8444   3052   6045   -281   -602    -68       C  
ATOM   3390  CG1 VAL B 134      81.488  59.605  45.338  1.00 45.15           C  
ANISOU 3390  CG1 VAL B 134     8269   2850   6038   -138   -658   -212       C  
ATOM   3391  CG2 VAL B 134      83.132  58.098  44.170  1.00 45.70           C  
ANISOU 3391  CG2 VAL B 134     8307   3024   6032   -399   -621     90       C  
ATOM   3392  N   SER B 135      83.655  61.183  47.909  1.00 51.41           N  
ANISOU 3392  N   SER B 135     9476   3448   6607   -127   -903   -334       N  
ATOM   3393  CA  SER B 135      83.392  61.773  49.220  1.00 51.97           C  
ANISOU 3393  CA  SER B 135     9703   3473   6571      7   -912   -515       C  
ATOM   3394  C   SER B 135      83.011  63.233  49.068  1.00 56.49           C  
ANISOU 3394  C   SER B 135    10305   3875   7286     90  -1074   -625       C  
ATOM   3395  O   SER B 135      83.449  63.889  48.116  1.00 55.10           O  
ANISOU 3395  O   SER B 135    10116   3568   7253      7  -1234   -532       O  
ATOM   3396  CB  SER B 135      84.626  61.653  50.113  1.00 56.65           C  
ANISOU 3396  CB  SER B 135    10458   4041   7027    -11  -1051   -535       C  
ATOM   3397  OG  SER B 135      84.432  62.293  51.365  1.00 71.53           O  
ANISOU 3397  OG  SER B 135    12549   5860   8770    131  -1092   -719       O  
ATOM   3398  N   SER B 136      82.196  63.740  50.011  1.00 54.90           N  
ANISOU 3398  N   SER B 136    10177   3651   7030    252  -1014   -830       N  
ATOM   3399  CA  SER B 136      81.790  65.151  50.057  1.00 55.46           C  
ANISOU 3399  CA  SER B 136    10301   3541   7231    376  -1185   -981       C  
ATOM   3400  C   SER B 136      82.374  65.811  51.278  1.00 60.98           C  
ANISOU 3400  C   SER B 136    11214   4152   7805    434  -1294  -1125       C  
ATOM   3401  O   SER B 136      82.686  65.133  52.260  1.00 61.60           O  
ANISOU 3401  O   SER B 136    11418   4332   7655    442  -1190  -1157       O  
ATOM   3402  CB  SER B 136      80.271  65.299  50.060  1.00 59.33           C  
ANISOU 3402  CB  SER B 136    10651   4068   7824    549  -1044  -1171       C  
ATOM   3403  OG  SER B 136      79.657  64.543  51.090  1.00 70.76           O  
ANISOU 3403  OG  SER B 136    12096   5673   9118    591   -722  -1308       O  
ATOM   3404  N   LEU B 137      82.521  67.137  51.221  1.00 58.59           N  
ANISOU 3404  N   LEU B 137    10996   3633   7633    487  -1526  -1220       N  
ATOM   3405  CA  LEU B 137      83.014  67.951  52.321  1.00 58.75           C  
ANISOU 3405  CA  LEU B 137    11217   3533   7572    561  -1678  -1401       C  
ATOM   3406  C   LEU B 137      82.005  67.941  53.464  1.00 61.83           C  
ANISOU 3406  C   LEU B 137    11695   4006   7790    763  -1479  -1637       C  
ATOM   3407  O   LEU B 137      82.394  68.081  54.620  1.00 60.45           O  
ANISOU 3407  O   LEU B 137    11744   3815   7408    833  -1517  -1776       O  
ATOM   3408  CB  LEU B 137      83.266  69.375  51.833  1.00 59.50           C  
ANISOU 3408  CB  LEU B 137    11379   3342   7886    558  -1946  -1445       C  
ATOM   3409  CG  LEU B 137      84.720  69.771  51.664  1.00 65.03           C  
ANISOU 3409  CG  LEU B 137    12122   3887   8701    340  -2149  -1348       C  
ATOM   3410  CD1 LEU B 137      85.328  69.138  50.417  1.00 65.58           C  
ANISOU 3410  CD1 LEU B 137    12063   3971   8882    127  -2082  -1084       C  
ATOM   3411  CD2 LEU B 137      84.843  71.267  51.602  1.00 67.81           C  
ANISOU 3411  CD2 LEU B 137    12624   3923   9217    361  -2382  -1474       C  
ATOM   3412  N   GLU B 138      80.711  67.749  53.124  1.00 59.58           N  
ANISOU 3412  N   GLU B 138    11234   3805   7599    857  -1263  -1709       N  
ATOM   3413  CA  GLU B 138      79.577  67.603  54.039  1.00 59.90           C  
ANISOU 3413  CA  GLU B 138    11271   3945   7541   1010   -955  -1960       C  
ATOM   3414  C   GLU B 138      79.825  66.382  54.964  1.00 61.48           C  
ANISOU 3414  C   GLU B 138    11654   4312   7393    934   -665  -1908       C  
ATOM   3415  O   GLU B 138      79.678  66.521  56.179  1.00 60.83           O  
ANISOU 3415  O   GLU B 138    11829   4224   7062   1032   -528  -2091       O  
ATOM   3416  CB  GLU B 138      78.279  67.418  53.239  1.00 61.86           C  
ANISOU 3416  CB  GLU B 138    11190   4264   8049   1073   -796  -2038       C  
ATOM   3417  CG  GLU B 138      77.036  67.937  53.943  1.00 77.81           C  
ANISOU 3417  CG  GLU B 138    13114   6287  10163   1276   -590  -2409       C  
ATOM   3418  CD  GLU B 138      75.751  67.271  53.483  1.00109.59           C  
ANISOU 3418  CD  GLU B 138    16759  10445  14436   1309   -332  -2548       C  
ATOM   3419  OE1 GLU B 138      75.222  66.422  54.237  1.00113.93           O  
ANISOU 3419  OE1 GLU B 138    17257  11157  14876   1240    125  -2658       O  
ATOM   3420  OE2 GLU B 138      75.276  67.588  52.367  1.00102.69           O  
ANISOU 3420  OE2 GLU B 138    15662   9491  13866   1401   -590  -2558       O  
ATOM   3421  N   VAL B 139      80.266  65.223  54.408  1.00 56.14           N  
ANISOU 3421  N   VAL B 139    10908   3753   6669    772   -595  -1659       N  
ATOM   3422  CA  VAL B 139      80.599  64.040  55.231  1.00 55.97           C  
ANISOU 3422  CA  VAL B 139    11128   3836   6301    713   -375  -1580       C  
ATOM   3423  C   VAL B 139      81.881  64.305  56.086  1.00 59.65           C  
ANISOU 3423  C   VAL B 139    11939   4203   6521    753   -684  -1575       C  
ATOM   3424  O   VAL B 139      81.881  64.063  57.295  1.00 59.68           O  
ANISOU 3424  O   VAL B 139    12307   4198   6170    841   -569  -1677       O  
ATOM   3425  CB  VAL B 139      80.673  62.704  54.429  1.00 59.77           C  
ANISOU 3425  CB  VAL B 139    11445   4447   6817    551   -230  -1343       C  
ATOM   3426  CG1 VAL B 139      81.095  61.534  55.315  1.00 59.00           C  
ANISOU 3426  CG1 VAL B 139    11677   4399   6342    512    -57  -1251       C  
ATOM   3427  CG2 VAL B 139      79.346  62.389  53.751  1.00 59.86           C  
ANISOU 3427  CG2 VAL B 139    11125   4551   7069    530     63  -1414       C  
ATOM   3428  N   LEU B 140      82.939  64.843  55.453  1.00 54.69           N  
ANISOU 3428  N   LEU B 140    11207   3480   6093    689  -1071  -1487       N  
ATOM   3429  CA  LEU B 140      84.225  65.156  56.072  1.00 52.99           C  
ANISOU 3429  CA  LEU B 140    11196   3158   5778    711  -1427  -1530       C  
ATOM   3430  C   LEU B 140      84.116  66.056  57.300  1.00 56.30           C  
ANISOU 3430  C   LEU B 140    11923   3463   6007    891  -1529  -1793       C  
ATOM   3431  O   LEU B 140      84.862  65.864  58.258  1.00 54.94           O  
ANISOU 3431  O   LEU B 140    12060   3248   5567    976  -1718  -1870       O  
ATOM   3432  CB  LEU B 140      85.172  65.756  55.013  1.00 52.57           C  
ANISOU 3432  CB  LEU B 140    10891   3002   6083    562  -1728  -1439       C  
ATOM   3433  CG  LEU B 140      86.537  66.282  55.472  1.00 57.09           C  
ANISOU 3433  CG  LEU B 140    11547   3437   6709    545  -2118  -1548       C  
ATOM   3434  CD1 LEU B 140      87.517  65.150  55.796  1.00 57.08           C  
ANISOU 3434  CD1 LEU B 140    11594   3521   6573    526  -2236  -1486       C  
ATOM   3435  CD2 LEU B 140      87.108  67.206  54.461  1.00 59.15           C  
ANISOU 3435  CD2 LEU B 140    11581   3539   7354    376  -2289  -1518       C  
ATOM   3436  N   PHE B 141      83.191  67.027  57.283  1.00 55.05           N  
ANISOU 3436  N   PHE B 141    11698   3242   5978    977  -1433  -1955       N  
ATOM   3437  CA  PHE B 141      83.050  67.982  58.377  1.00 54.81           C  
ANISOU 3437  CA  PHE B 141    11941   3090   5795   1156  -1527  -2232       C  
ATOM   3438  C   PHE B 141      81.885  67.699  59.350  1.00 60.46           C  
ANISOU 3438  C   PHE B 141    12880   3891   6202   1291  -1097  -2408       C  
ATOM   3439  O   PHE B 141      81.738  68.446  60.320  1.00 62.23           O  
ANISOU 3439  O   PHE B 141    13376   4021   6247   1451  -1136  -2657       O  
ATOM   3440  CB  PHE B 141      82.977  69.407  57.825  1.00 56.72           C  
ANISOU 3440  CB  PHE B 141    12011   3145   6394   1179  -1765  -2342       C  
ATOM   3441  CG  PHE B 141      84.274  69.927  57.245  1.00 58.40           C  
ANISOU 3441  CG  PHE B 141    12139   3200   6850   1036  -2171  -2255       C  
ATOM   3442  CD1 PHE B 141      85.291  70.386  58.073  1.00 60.98           C  
ANISOU 3442  CD1 PHE B 141    12676   3400   7096   1076  -2500  -2414       C  
ATOM   3443  CD2 PHE B 141      84.453  70.020  55.868  1.00 60.52           C  
ANISOU 3443  CD2 PHE B 141    12128   3424   7443    857  -2213  -2047       C  
ATOM   3444  CE1 PHE B 141      86.479  70.885  57.532  1.00 61.56           C  
ANISOU 3444  CE1 PHE B 141    12609   3313   7468    908  -2831  -2387       C  
ATOM   3445  CE2 PHE B 141      85.637  70.536  55.330  1.00 62.51           C  
ANISOU 3445  CE2 PHE B 141    12307   3506   7937    680  -2500  -1992       C  
ATOM   3446  CZ  PHE B 141      86.648  70.944  56.164  1.00 60.10           C  
ANISOU 3446  CZ  PHE B 141    12141   3087   7608    691  -2790  -2171       C  
ATOM   3447  N   GLN B 142      81.123  66.599  59.146  1.00 57.94           N  
ANISOU 3447  N   GLN B 142    12468   3735   5810   1212   -669  -2298       N  
ATOM   3448  CA  GLN B 142      79.998  66.158  59.987  1.00 72.36           C  
ANISOU 3448  CA  GLN B 142    14477   5643   7373   1267   -144  -2460       C  
ATOM   3449  C   GLN B 142      80.394  65.925  61.439  1.00113.69           C  
ANISOU 3449  C   GLN B 142    20325  10827  12045   1359    -94  -2524       C  
ATOM   3450  O   GLN B 142      79.743  66.453  62.339  1.00 87.88           O  
ANISOU 3450  O   GLN B 142    17327   7506   8557   1494     92  -2785       O  
ATOM   3451  CB  GLN B 142      79.323  64.886  59.426  1.00 73.29           C  
ANISOU 3451  CB  GLN B 142    14352   5920   7577   1108    282  -2311       C  
ATOM   3452  CG  GLN B 142      78.058  65.114  58.577  1.00 91.75           C  
ANISOU 3452  CG  GLN B 142    16214   8320  10326   1115    547  -2485       C  
ATOM   3453  CD  GLN B 142      77.012  66.050  59.168  1.00122.65           C  
ANISOU 3453  CD  GLN B 142    20173  12199  14227   1269    824  -2866       C  
ATOM   3454  OE1 GLN B 142      76.629  65.961  60.344  1.00123.01           O  
ANISOU 3454  OE1 GLN B 142    20604  12249  13884   1290   1193  -3002       O  
ATOM   3455  NE2 GLN B 142      76.515  66.969  58.351  1.00113.53           N  
ANISOU 3455  NE2 GLN B 142    18655  10991  13489   1392    655  -3058       N  
TER    3456      GLN B 142                                                      
ATOM   3457  N   CYS C   7      76.762  39.232 -13.425  1.00113.25           N  
ANISOU 3457  N   CYS C   7    28047   5415   9567  -2128   1113   1270       N  
ATOM   3458  CA  CYS C   7      76.711  37.963 -14.159  1.00112.77           C  
ANISOU 3458  CA  CYS C   7    27791   5600   9457  -2220   1199   1333       C  
ATOM   3459  C   CYS C   7      75.281  37.676 -14.647  1.00116.32           C  
ANISOU 3459  C   CYS C   7    28298   6051   9846  -1715    888   1428       C  
ATOM   3460  O   CYS C   7      74.689  36.661 -14.286  1.00115.61           O  
ANISOU 3460  O   CYS C   7    27660   6320   9945  -1465    796   1380       O  
ATOM   3461  CB  CYS C   7      77.261  36.820 -13.310  1.00112.81           C  
ANISOU 3461  CB  CYS C   7    27050   6089   9723  -2413   1396   1208       C  
ATOM   3462  SG  CYS C   7      78.833  37.192 -12.493  1.00116.53           S  
ANISOU 3462  SG  CYS C   7    27340   6593  10344  -2950   1679   1083       S  
ATOM   3463  N   GLU C   8      74.733  38.595 -15.467  1.00112.82           N  
ANISOU 3463  N   GLU C   8    28539   5186   9144  -1573    709   1566       N  
ATOM   3464  CA  GLU C   8      73.377  38.534 -16.027  1.00112.01           C  
ANISOU 3464  CA  GLU C   8    28616   4985   8958  -1099    356   1680       C  
ATOM   3465  C   GLU C   8      73.047  37.187 -16.697  1.00112.40           C  
ANISOU 3465  C   GLU C   8    28262   5396   9051  -1015    300   1701       C  
ATOM   3466  O   GLU C   8      71.956  36.655 -16.485  1.00110.61           O  
ANISOU 3466  O   GLU C   8    27704   5336   8989   -577     26   1699       O  
ATOM   3467  CB  GLU C   8      73.147  39.684 -17.027  1.00113.51           C  
ANISOU 3467  CB  GLU C   8    29686   4655   8788  -1137    243   1848       C  
ATOM   3468  CG  GLU C   8      73.146  41.078 -16.413  1.00129.88           C  
ANISOU 3468  CG  GLU C   8    32241   6302  10804  -1092    199   1848       C  
ATOM   3469  CD  GLU C   8      74.503  41.728 -16.206  1.00158.18           C  
ANISOU 3469  CD  GLU C   8    36040   9746  14317  -1651    545   1793       C  
ATOM   3470  OE1 GLU C   8      75.413  41.499 -17.036  1.00162.49           O  
ANISOU 3470  OE1 GLU C   8    36777  10278  14682  -2115    801   1846       O  
ATOM   3471  OE2 GLU C   8      74.652  42.479 -15.215  1.00150.11           O  
ANISOU 3471  OE2 GLU C   8    35003   8614  13418  -1630    564   1695       O  
ATOM   3472  N   ASN C   9      73.989  36.666 -17.515  1.00108.08           N  
ANISOU 3472  N   ASN C   9    27762   4948   8354  -1441    569   1721       N  
ATOM   3473  CA  ASN C   9      73.868  35.428 -18.290  1.00108.15           C  
ANISOU 3473  CA  ASN C   9    27507   5246   8340  -1439    565   1742       C  
ATOM   3474  C   ASN C   9      73.697  34.184 -17.430  1.00111.66           C  
ANISOU 3474  C   ASN C   9    27112   6182   9132  -1294    578   1606       C  
ATOM   3475  O   ASN C   9      72.790  33.396 -17.695  1.00111.50           O  
ANISOU 3475  O   ASN C   9    26851   6341   9173   -994    342   1630       O  
ATOM   3476  CB  ASN C   9      75.038  35.261 -19.279  1.00109.61           C  
ANISOU 3476  CB  ASN C   9    27983   5385   8278  -1950    920   1781       C  
ATOM   3477  CG  ASN C   9      76.422  35.410 -18.683  1.00132.41           C  
ANISOU 3477  CG  ASN C   9    30672   8356  11280  -2419   1339   1677       C  
ATOM   3478  OD1 ASN C   9      76.742  36.390 -17.986  1.00125.57           O  
ANISOU 3478  OD1 ASN C   9    29978   7280  10451  -2525   1384   1651       O  
ATOM   3479  ND2 ASN C   9      77.284  34.441 -18.967  1.00122.17           N  
ANISOU 3479  ND2 ASN C   9    29016   7357  10048  -2713   1646   1615       N  
ATOM   3480  N   TRP C  10      74.547  34.022 -16.394  1.00107.68           N  
ANISOU 3480  N   TRP C  10    26182   5880   8852  -1512    832   1469       N  
ATOM   3481  CA  TRP C  10      74.507  32.886 -15.479  1.00106.98           C  
ANISOU 3481  CA  TRP C  10    25329   6236   9082  -1409    866   1339       C  
ATOM   3482  C   TRP C  10      73.390  33.000 -14.434  1.00109.11           C  
ANISOU 3482  C   TRP C  10    25318   6565   9573   -944    598   1291       C  
ATOM   3483  O   TRP C  10      73.052  32.007 -13.791  1.00109.92           O  
ANISOU 3483  O   TRP C  10    24836   7016   9911   -771    557   1213       O  
ATOM   3484  CB  TRP C  10      75.881  32.641 -14.844  1.00105.84           C  
ANISOU 3484  CB  TRP C  10    24860   6275   9078  -1831   1218   1220       C  
ATOM   3485  CG  TRP C  10      76.756  31.741 -15.669  1.00107.03           C  
ANISOU 3485  CG  TRP C  10    24885   6613   9171  -2165   1490   1220       C  
ATOM   3486  CD1 TRP C  10      76.492  30.451 -16.037  1.00110.02           C  
ANISOU 3486  CD1 TRP C  10    24894   7295   9613  -2063   1476   1203       C  
ATOM   3487  CD2 TRP C  10      78.051  32.053 -16.202  1.00106.96           C  
ANISOU 3487  CD2 TRP C  10    25103   6494   9043  -2656   1842   1228       C  
ATOM   3488  NE1 TRP C  10      77.534  29.946 -16.779  1.00109.48           N  
ANISOU 3488  NE1 TRP C  10    24831   7303   9461  -2439   1804   1196       N  
ATOM   3489  CE2 TRP C  10      78.507  30.907 -16.896  1.00110.86           C  
ANISOU 3489  CE2 TRP C  10    25352   7237   9534  -2808   2044   1213       C  
ATOM   3490  CE3 TRP C  10      78.869  33.196 -16.171  1.00108.32           C  
ANISOU 3490  CE3 TRP C  10    25667   6373   9118  -2994   2016   1246       C  
ATOM   3491  CZ2 TRP C  10      79.754  30.864 -17.534  1.00110.15           C  
ANISOU 3491  CZ2 TRP C  10    25365   7123   9364  -3267   2441   1211       C  
ATOM   3492  CZ3 TRP C  10      80.101  33.155 -16.811  1.00109.89           C  
ANISOU 3492  CZ3 TRP C  10    25958   6553   9243  -3474   2396   1252       C  
ATOM   3493  CH2 TRP C  10      80.535  31.999 -17.477  1.00110.53           C  
ANISOU 3493  CH2 TRP C  10    25759   6897   9339  -3599   2617   1233       C  
ATOM   3494  N   LEU C  11      72.783  34.186 -14.313  1.00103.81           N  
ANISOU 3494  N   LEU C  11    25080   5541   8821   -734    427   1343       N  
ATOM   3495  CA  LEU C  11      71.656  34.460 -13.423  1.00103.24           C  
ANISOU 3495  CA  LEU C  11    24826   5460   8941   -264    195   1306       C  
ATOM   3496  C   LEU C  11      70.379  33.940 -14.086  1.00104.91           C  
ANISOU 3496  C   LEU C  11    24954   5727   9179    149   -129   1399       C  
ATOM   3497  O   LEU C  11      69.582  33.270 -13.430  1.00104.36           O  
ANISOU 3497  O   LEU C  11    24379   5909   9366    469   -248   1342       O  
ATOM   3498  CB  LEU C  11      71.542  35.981 -13.162  1.00103.60           C  
ANISOU 3498  CB  LEU C  11    25432   5061   8869   -195    141   1333       C  
ATOM   3499  CG  LEU C  11      70.409  36.450 -12.250  1.00108.77           C  
ANISOU 3499  CG  LEU C  11    25966   5651   9711    289    -45   1285       C  
ATOM   3500  CD1 LEU C  11      70.878  36.573 -10.810  1.00109.12           C  
ANISOU 3500  CD1 LEU C  11    25996   5633   9833    150    141   1151       C  
ATOM   3501  CD2 LEU C  11      69.855  37.776 -12.725  1.00112.01           C  
ANISOU 3501  CD2 LEU C  11    26928   5654   9978    632   -330   1417       C  
ATOM   3502  N   ALA C  12      70.183  34.272 -15.381  1.00100.19           N  
ANISOU 3502  N   ALA C  12    24870   4883   8314    129   -278   1544       N  
ATOM   3503  CA  ALA C  12      69.031  33.861 -16.186  1.00 99.17           C  
ANISOU 3503  CA  ALA C  12    24750   4760   8170    477   -635   1651       C  
ATOM   3504  C   ALA C  12      68.923  32.324 -16.252  1.00101.30           C  
ANISOU 3504  C   ALA C  12    24413   5475   8599    463   -623   1599       C  
ATOM   3505  O   ALA C  12      67.861  31.786 -15.928  1.00101.03           O  
ANISOU 3505  O   ALA C  12    23972   5620   8794    830   -863   1591       O  
ATOM   3506  CB  ALA C  12      69.130  34.455 -17.583  1.00 99.60           C  
ANISOU 3506  CB  ALA C  12    25538   4456   7851    356   -755   1811       C  
ATOM   3507  N   LEU C  13      70.040  31.628 -16.594  1.00 96.16           N  
ANISOU 3507  N   LEU C  13    23679   5004   7854     39   -325   1555       N  
ATOM   3508  CA  LEU C  13      70.118  30.164 -16.668  1.00 95.90           C  
ANISOU 3508  CA  LEU C  13    23118   5371   7950    -22   -267   1495       C  
ATOM   3509  C   LEU C  13      69.526  29.518 -15.413  1.00 97.63           C  
ANISOU 3509  C   LEU C  13    22648   5908   8538    235   -304   1383       C  
ATOM   3510  O   LEU C  13      68.661  28.653 -15.537  1.00 97.51           O  
ANISOU 3510  O   LEU C  13    22281   6104   8664    467   -508   1391       O  
ATOM   3511  CB  LEU C  13      71.580  29.695 -16.846  1.00 96.33           C  
ANISOU 3511  CB  LEU C  13    23136   5554   7910   -511    137   1432       C  
ATOM   3512  CG  LEU C  13      71.898  28.586 -17.882  1.00101.49           C  
ANISOU 3512  CG  LEU C  13    23784   6360   8419   -686    199   1459       C  
ATOM   3513  CD1 LEU C  13      73.210  27.905 -17.548  1.00101.64           C  
ANISOU 3513  CD1 LEU C  13    23515   6605   8499  -1081    622   1351       C  
ATOM   3514  CD2 LEU C  13      70.818  27.505 -17.954  1.00104.63           C  
ANISOU 3514  CD2 LEU C  13    23757   7018   8980   -379    -81   1454       C  
ATOM   3515  N   GLU C  14      69.973  29.972 -14.218  1.00 92.30           N  
ANISOU 3515  N   GLU C  14    21816   5247   8006    182   -114   1281       N  
ATOM   3516  CA  GLU C  14      69.557  29.514 -12.884  1.00 91.05           C  
ANISOU 3516  CA  GLU C  14    21085   5349   8161    387    -93   1165       C  
ATOM   3517  C   GLU C  14      68.036  29.535 -12.709  1.00 92.17           C  
ANISOU 3517  C   GLU C  14    21055   5493   8472    884   -409   1207       C  
ATOM   3518  O   GLU C  14      67.469  28.541 -12.276  1.00 91.36           O  
ANISOU 3518  O   GLU C  14    20419   5697   8597   1041   -456   1158       O  
ATOM   3519  CB  GLU C  14      70.231  30.387 -11.818  1.00 92.62           C  
ANISOU 3519  CB  GLU C  14    21381   5419   8390    263    103   1077       C  
ATOM   3520  CG  GLU C  14      70.211  29.806 -10.417  1.00103.68           C  
ANISOU 3520  CG  GLU C  14    22231   7109  10055    327    217    939       C  
ATOM   3521  CD  GLU C  14      70.370  30.833  -9.315  1.00123.00           C  
ANISOU 3521  CD  GLU C  14    24837   9368  12529    348    302    862       C  
ATOM   3522  OE1 GLU C  14      71.228  31.735  -9.454  1.00107.58           O  
ANISOU 3522  OE1 GLU C  14    23297   7170  10408     58    421    867       O  
ATOM   3523  OE2 GLU C  14      69.636  30.731  -8.307  1.00120.02           O  
ANISOU 3523  OE2 GLU C  14    24185   9081  12337    644    260    794       O  
ATOM   3524  N   ASN C  15      67.385  30.662 -13.050  1.00 88.43           N  
ANISOU 3524  N   ASN C  15    21029   4670   7900   1126   -623   1300       N  
ATOM   3525  CA  ASN C  15      65.932  30.829 -12.970  1.00 87.52           C  
ANISOU 3525  CA  ASN C  15    20779   4511   7963   1620   -940   1352       C  
ATOM   3526  C   ASN C  15      65.215  29.849 -13.912  1.00 89.64           C  
ANISOU 3526  C   ASN C  15    20843   4953   8262   1724  -1204   1433       C  
ATOM   3527  O   ASN C  15      64.206  29.277 -13.510  1.00 88.66           O  
ANISOU 3527  O   ASN C  15    20245   5030   8412   2030  -1363   1417       O  
ATOM   3528  CB  ASN C  15      65.523  32.278 -13.246  1.00 85.48           C  
ANISOU 3528  CB  ASN C  15    21103   3805   7572   1835  -1113   1440       C  
ATOM   3529  N   ILE C  16      65.758  29.627 -15.139  1.00 84.92           N  
ANISOU 3529  N   ILE C  16    20606   4279   7382   1449  -1234   1514       N  
ATOM   3530  CA  ILE C  16      65.216  28.666 -16.121  1.00 83.67           C  
ANISOU 3530  CA  ILE C  16    20343   4257   7190   1484  -1481   1587       C  
ATOM   3531  C   ILE C  16      65.354  27.230 -15.569  1.00 83.70           C  
ANISOU 3531  C   ILE C  16    19689   4702   7410   1381  -1328   1478       C  
ATOM   3532  O   ILE C  16      64.404  26.450 -15.661  1.00 83.47           O  
ANISOU 3532  O   ILE C  16    19295   4858   7560   1591  -1569   1497       O  
ATOM   3533  CB  ILE C  16      65.851  28.822 -17.548  1.00 86.54           C  
ANISOU 3533  CB  ILE C  16    21342   4391   7146   1193  -1504   1692       C  
ATOM   3534  CG1 ILE C  16      65.724  30.268 -18.065  1.00 87.15           C  
ANISOU 3534  CG1 ILE C  16    22107   4007   7000   1307  -1677   1811       C  
ATOM   3535  CG2 ILE C  16      65.226  27.834 -18.553  1.00 86.31           C  
ANISOU 3535  CG2 ILE C  16    21248   4490   7058   1226  -1779   1758       C  
ATOM   3536  CD1 ILE C  16      66.714  30.688 -19.218  1.00 95.17           C  
ANISOU 3536  CD1 ILE C  16    23841   4741   7578    917  -1524   1890       C  
ATOM   3537  N   LEU C  17      66.527  26.902 -14.979  1.00 77.47           N  
ANISOU 3537  N   LEU C  17    18749   4069   6618   1058   -944   1367       N  
ATOM   3538  CA  LEU C  17      66.809  25.582 -14.401  1.00 76.12           C  
ANISOU 3538  CA  LEU C  17    17999   4288   6636    942   -775   1262       C  
ATOM   3539  C   LEU C  17      65.894  25.246 -13.218  1.00 80.77           C  
ANISOU 3539  C   LEU C  17    18029   5086   7573   1256   -838   1196       C  
ATOM   3540  O   LEU C  17      65.496  24.098 -13.076  1.00 79.41           O  
ANISOU 3540  O   LEU C  17    17405   5197   7569   1298   -885   1165       O  
ATOM   3541  CB  LEU C  17      68.291  25.416 -13.998  1.00 75.41           C  
ANISOU 3541  CB  LEU C  17    17886   4287   6479    545   -375   1164       C  
ATOM   3542  CG  LEU C  17      69.361  25.427 -15.099  1.00 78.60           C  
ANISOU 3542  CG  LEU C  17    18714   4569   6581    173   -206   1203       C  
ATOM   3543  CD1 LEU C  17      70.749  25.324 -14.504  1.00 77.96           C  
ANISOU 3543  CD1 LEU C  17    18507   4590   6523   -178    180   1099       C  
ATOM   3544  CD2 LEU C  17      69.153  24.317 -16.114  1.00 80.16           C  
ANISOU 3544  CD2 LEU C  17    18871   4901   6686    121   -308   1241       C  
ATOM   3545  N   LYS C  18      65.551  26.242 -12.383  1.00 78.84           N  
ANISOU 3545  N   LYS C  18    17840   4686   7427   1473   -829   1175       N  
ATOM   3546  CA  LYS C  18      64.666  26.050 -11.240  1.00 79.31           C  
ANISOU 3546  CA  LYS C  18    17424   4908   7803   1784   -846   1112       C  
ATOM   3547  C   LYS C  18      63.205  25.909 -11.686  1.00 86.39           C  
ANISOU 3547  C   LYS C  18    18154   5802   8867   2164  -1204   1201       C  
ATOM   3548  O   LYS C  18      62.573  24.901 -11.376  1.00 87.18           O  
ANISOU 3548  O   LYS C  18    17738   6181   9204   2273  -1254   1173       O  
ATOM   3549  CB  LYS C  18      64.829  27.190 -10.226  1.00 81.47           C  
ANISOU 3549  CB  LYS C  18    17861   4993   8101   1882   -688   1049       C  
ATOM   3550  CG  LYS C  18      66.078  27.097  -9.350  1.00 94.51           C  
ANISOU 3550  CG  LYS C  18    19474   6735   9700   1547   -350    931       C  
ATOM   3551  CD  LYS C  18      66.267  28.390  -8.550  1.00106.98           C  
ANISOU 3551  CD  LYS C  18    21348   8054  11246   1622   -242    880       C  
ATOM   3552  CE  LYS C  18      67.385  28.320  -7.537  1.00118.69           C  
ANISOU 3552  CE  LYS C  18    22801   9609  12688   1291     43    764       C  
ATOM   3553  NZ  LYS C  18      67.478  29.568  -6.721  1.00122.92           N  
ANISOU 3553  NZ  LYS C  18    23662   9867  13174   1358    122    710       N  
ATOM   3554  N   LYS C  19      62.701  26.887 -12.452  1.00 84.98           N  
ANISOU 3554  N   LYS C  19    18414   5307   8568   2345  -1466   1314       N  
ATOM   3555  CA  LYS C  19      61.330  27.002 -12.965  1.00 85.90           C  
ANISOU 3555  CA  LYS C  19    18446   5353   8839   2727  -1864   1417       C  
ATOM   3556  C   LYS C  19      60.861  25.823 -13.826  1.00 91.55           C  
ANISOU 3556  C   LYS C  19    18909   6281   9596   2679  -2111   1472       C  
ATOM   3557  O   LYS C  19      59.783  25.300 -13.550  1.00 91.25           O  
ANISOU 3557  O   LYS C  19    18383   6421   9867   2938  -2285   1476       O  
ATOM   3558  CB  LYS C  19      61.155  28.344 -13.723  1.00 88.93           C  
ANISOU 3558  CB  LYS C  19    19471   5306   9013   2870  -2094   1535       C  
ATOM   3559  CG  LYS C  19      59.902  28.496 -14.594  1.00111.33           C  
ANISOU 3559  CG  LYS C  19    22325   8020  11953   3230  -2578   1668       C  
ATOM   3560  CD  LYS C  19      60.269  28.528 -16.091  1.00124.28           C  
ANISOU 3560  CD  LYS C  19    24523   9464  13235   3034  -2833   1797       C  
ATOM   3561  CE  LYS C  19      59.090  28.738 -17.016  1.00131.41           C  
ANISOU 3561  CE  LYS C  19    25491  10227  14212   3367  -3372   1939       C  
ATOM   3562  NZ  LYS C  19      58.572  30.132 -16.957  1.00133.78           N  
ANISOU 3562  NZ  LYS C  19    26107  10169  14554   3736  -3559   2010       N  
ATOM   3563  N   TYR C  20      61.616  25.445 -14.882  1.00 89.55           N  
ANISOU 3563  N   TYR C  20    18999   5990   9036   2355  -2130   1517       N  
ATOM   3564  CA  TYR C  20      61.182  24.386 -15.799  1.00 90.17           C  
ANISOU 3564  CA  TYR C  20    18933   6222   9104   2300  -2388   1569       C  
ATOM   3565  C   TYR C  20      62.004  23.098 -15.759  1.00 90.67           C  
ANISOU 3565  C   TYR C  20    18740   6582   9128   1956  -2124   1478       C  
ATOM   3566  O   TYR C  20      61.405  22.034 -15.868  1.00 91.34           O  
ANISOU 3566  O   TYR C  20    18384   6913   9407   2005  -2250   1462       O  
ATOM   3567  CB  TYR C  20      61.104  24.907 -17.245  1.00 93.45           C  
ANISOU 3567  CB  TYR C  20    19976   6336   9195   2267  -2711   1710       C  
ATOM   3568  CG  TYR C  20      59.985  24.317 -18.090  1.00 98.16           C  
ANISOU 3568  CG  TYR C  20    20437   6988   9871   2424  -3180   1801       C  
ATOM   3569  CD1 TYR C  20      59.887  22.938 -18.298  1.00100.41           C  
ANISOU 3569  CD1 TYR C  20    20362   7566  10222   2259  -3189   1755       C  
ATOM   3570  CD2 TYR C  20      59.089  25.142 -18.765  1.00 99.69           C  
ANISOU 3570  CD2 TYR C  20    20915   6915  10049   2716  -3639   1937       C  
ATOM   3571  CE1 TYR C  20      58.882  22.396 -19.100  1.00101.97           C  
ANISOU 3571  CE1 TYR C  20    20457   7801  10486   2372  -3644   1837       C  
ATOM   3572  CE2 TYR C  20      58.093  24.611 -19.588  1.00101.24           C  
ANISOU 3572  CE2 TYR C  20    21001   7151  10315   2840  -4116   2024       C  
ATOM   3573  CZ  TYR C  20      57.992  23.237 -19.750  1.00111.63           C  
ANISOU 3573  CZ  TYR C  20    21943   8768  11705   2656  -4118   1972       C  
ATOM   3574  OH  TYR C  20      57.003  22.720 -20.556  1.00116.63           O  
ANISOU 3574  OH  TYR C  20    22478   9429  12408   2755  -4612   2055       O  
ATOM   3575  N   TYR C  21      63.347  23.169 -15.645  1.00 83.39           N  
ANISOU 3575  N   TYR C  21    18085   5629   7971   1614  -1775   1421       N  
ATOM   3576  CA  TYR C  21      64.193  21.970 -15.633  1.00 81.26           C  
ANISOU 3576  CA  TYR C  21    17594   5616   7664   1299  -1515   1334       C  
ATOM   3577  C   TYR C  21      63.968  21.100 -14.383  1.00 81.42           C  
ANISOU 3577  C   TYR C  21    16948   5969   8021   1367  -1363   1226       C  
ATOM   3578  O   TYR C  21      63.557  19.952 -14.529  1.00 81.27           O  
ANISOU 3578  O   TYR C  21    16596   6169   8113   1355  -1459   1213       O  
ATOM   3579  CB  TYR C  21      65.678  22.327 -15.851  1.00 82.27           C  
ANISOU 3579  CB  TYR C  21    18104   5633   7523    943  -1161   1296       C  
ATOM   3580  CG  TYR C  21      66.663  21.227 -15.519  1.00 84.29           C  
ANISOU 3580  CG  TYR C  21    18061   6156   7809    655   -837   1186       C  
ATOM   3581  CD1 TYR C  21      66.817  20.124 -16.356  1.00 86.18           C  
ANISOU 3581  CD1 TYR C  21    18297   6510   7937    496   -860   1188       C  
ATOM   3582  CD2 TYR C  21      67.468  21.303 -14.385  1.00 85.13           C  
ANISOU 3582  CD2 TYR C  21    17914   6382   8048    544   -519   1079       C  
ATOM   3583  CE1 TYR C  21      67.727  19.110 -16.058  1.00 86.22           C  
ANISOU 3583  CE1 TYR C  21    18030   6745   7984    259   -562   1087       C  
ATOM   3584  CE2 TYR C  21      68.378  20.293 -14.075  1.00 85.98           C  
ANISOU 3584  CE2 TYR C  21    17737   6726   8203    302   -251    984       C  
ATOM   3585  CZ  TYR C  21      68.505  19.199 -14.916  1.00 92.38           C  
ANISOU 3585  CZ  TYR C  21    18530   7649   8922    170   -265    988       C  
ATOM   3586  OH  TYR C  21      69.413  18.208 -14.626  1.00 92.84           O  
ANISOU 3586  OH  TYR C  21    18317   7922   9035    -45      1    894       O  
ATOM   3587  N   LEU C  22      64.217  21.644 -13.173  1.00 75.19           N  
ANISOU 3587  N   LEU C  22    16000   5196   7372   1433  -1138   1151       N  
ATOM   3588  CA  LEU C  22      64.047  20.941 -11.895  1.00 73.14           C  
ANISOU 3588  CA  LEU C  22    15178   5215   7395   1494   -970   1049       C  
ATOM   3589  C   LEU C  22      62.611  20.495 -11.688  1.00 73.62           C  
ANISOU 3589  C   LEU C  22    14821   5410   7742   1804  -1219   1081       C  
ATOM   3590  O   LEU C  22      62.398  19.362 -11.295  1.00 70.37           O  
ANISOU 3590  O   LEU C  22    13979   5265   7495   1761  -1174   1034       O  
ATOM   3591  CB  LEU C  22      64.482  21.807 -10.695  1.00 72.73           C  
ANISOU 3591  CB  LEU C  22    15144   5094   7398   1528   -722    972       C  
ATOM   3592  CG  LEU C  22      65.970  22.039 -10.438  1.00 76.72           C  
ANISOU 3592  CG  LEU C  22    15842   5574   7735   1188   -410    899       C  
ATOM   3593  CD1 LEU C  22      66.166  22.753  -9.118  1.00 76.66           C  
ANISOU 3593  CD1 LEU C  22    15783   5522   7822   1259   -227    816       C  
ATOM   3594  CD2 LEU C  22      66.757  20.747 -10.423  1.00 78.36           C  
ANISOU 3594  CD2 LEU C  22    15759   6053   7961    929   -246    834       C  
ATOM   3595  N   SER C  23      61.630  21.379 -11.968  1.00 71.03           N  
ANISOU 3595  N   SER C  23    14613   4891   7486   2113  -1485   1164       N  
ATOM   3596  CA  SER C  23      60.205  21.077 -11.805  1.00 70.73           C  
ANISOU 3596  CA  SER C  23    14150   4962   7762   2430  -1737   1203       C  
ATOM   3597  C   SER C  23      59.757  19.870 -12.659  1.00 73.30           C  
ANISOU 3597  C   SER C  23    14285   5449   8115   2339  -1993   1252       C  
ATOM   3598  O   SER C  23      59.123  18.967 -12.106  1.00 72.97           O  
ANISOU 3598  O   SER C  23    13724   5659   8344   2399  -1994   1217       O  
ATOM   3599  CB  SER C  23      59.338  22.317 -12.040  1.00 73.22           C  
ANISOU 3599  CB  SER C  23    14664   5010   8147   2786  -1985   1287       C  
ATOM   3600  OG  SER C  23      59.182  22.640 -13.413  1.00 79.48           O  
ANISOU 3600  OG  SER C  23    15898   5578   8724   2784  -2328   1408       O  
ATOM   3601  N   ALA C  24      60.145  19.821 -13.964  1.00 68.01           N  
ANISOU 3601  N   ALA C  24    14059   4633   7147   2166  -2181   1324       N  
ATOM   3602  CA  ALA C  24      59.820  18.693 -14.850  1.00 67.79           C  
ANISOU 3602  CA  ALA C  24    13945   4724   7087   2048  -2427   1363       C  
ATOM   3603  C   ALA C  24      60.595  17.432 -14.475  1.00 70.56           C  
ANISOU 3603  C   ALA C  24    14043   5337   7429   1760  -2138   1261       C  
ATOM   3604  O   ALA C  24      59.984  16.369 -14.350  1.00 70.66           O  
ANISOU 3604  O   ALA C  24    13646   5563   7639   1768  -2245   1247       O  
ATOM   3605  CB  ALA C  24      60.075  19.053 -16.304  1.00 68.90           C  
ANISOU 3605  CB  ALA C  24    14703   4608   6867   1936  -2669   1460       C  
ATOM   3606  N   PHE C  25      61.928  17.539 -14.266  1.00 65.27           N  
ANISOU 3606  N   PHE C  25    13598   4649   6553   1510  -1777   1190       N  
ATOM   3607  CA  PHE C  25      62.744  16.396 -13.868  1.00 63.98           C  
ANISOU 3607  CA  PHE C  25    13203   4716   6392   1257  -1495   1091       C  
ATOM   3608  C   PHE C  25      62.187  15.757 -12.574  1.00 67.19           C  
ANISOU 3608  C   PHE C  25    13007   5380   7142   1380  -1392   1024       C  
ATOM   3609  O   PHE C  25      61.935  14.546 -12.560  1.00 66.70           O  
ANISOU 3609  O   PHE C  25    12639   5517   7187   1305  -1429   1001       O  
ATOM   3610  CB  PHE C  25      64.227  16.782 -13.725  1.00 65.81           C  
ANISOU 3610  CB  PHE C  25    13719   4876   6410   1009  -1131   1028       C  
ATOM   3611  CG  PHE C  25      65.233  15.714 -14.116  1.00 68.24           C  
ANISOU 3611  CG  PHE C  25    14052   5302   6574    707   -930    968       C  
ATOM   3612  CD1 PHE C  25      65.035  14.377 -13.766  1.00 71.14           C  
ANISOU 3612  CD1 PHE C  25    14002   5924   7105    662   -895    910       C  
ATOM   3613  CD2 PHE C  25      66.409  16.052 -14.773  1.00 71.28           C  
ANISOU 3613  CD2 PHE C  25    14868   5539   6676    467   -740    964       C  
ATOM   3614  CE1 PHE C  25      65.970  13.395 -14.111  1.00 71.99           C  
ANISOU 3614  CE1 PHE C  25    14139   6123   7092    410   -702    850       C  
ATOM   3615  CE2 PHE C  25      67.359  15.067 -15.093  1.00 74.26           C  
ANISOU 3615  CE2 PHE C  25    15240   6026   6951    211   -517    900       C  
ATOM   3616  CZ  PHE C  25      67.129  13.745 -14.763  1.00 71.78           C  
ANISOU 3616  CZ  PHE C  25    14519   5954   6801    197   -507    841       C  
ATOM   3617  N   TYR C  26      61.919  16.574 -11.528  1.00 63.18           N  
ANISOU 3617  N   TYR C  26    12362   4847   6798   1574  -1273    999       N  
ATOM   3618  CA  TYR C  26      61.344  16.093 -10.265  1.00 63.08           C  
ANISOU 3618  CA  TYR C  26    11831   5049   7090   1704  -1147    939       C  
ATOM   3619  C   TYR C  26      59.923  15.567 -10.440  1.00 66.61           C  
ANISOU 3619  C   TYR C  26    11906   5601   7801   1904  -1435    998       C  
ATOM   3620  O   TYR C  26      59.501  14.683  -9.688  1.00 65.18           O  
ANISOU 3620  O   TYR C  26    11280   5644   7842   1908  -1345    955       O  
ATOM   3621  CB  TYR C  26      61.381  17.165  -9.167  1.00 64.53           C  
ANISOU 3621  CB  TYR C  26    12026   5144   7349   1868   -946    894       C  
ATOM   3622  CG  TYR C  26      62.768  17.568  -8.717  1.00 67.12           C  
ANISOU 3622  CG  TYR C  26    12617   5410   7475   1644   -647    819       C  
ATOM   3623  CD1 TYR C  26      63.812  16.650  -8.701  1.00 69.88           C  
ANISOU 3623  CD1 TYR C  26    12925   5903   7724   1348   -473    760       C  
ATOM   3624  CD2 TYR C  26      63.021  18.848  -8.238  1.00 68.14           C  
ANISOU 3624  CD2 TYR C  26    13011   5338   7540   1733   -542    802       C  
ATOM   3625  CE1 TYR C  26      65.083  17.008  -8.261  1.00 71.77           C  
ANISOU 3625  CE1 TYR C  26    13351   6096   7822   1141   -218    693       C  
ATOM   3626  CE2 TYR C  26      64.291  19.221  -7.804  1.00 69.27           C  
ANISOU 3626  CE2 TYR C  26    13377   5425   7519   1503   -292    733       C  
ATOM   3627  CZ  TYR C  26      65.320  18.296  -7.819  1.00 76.95           C  
ANISOU 3627  CZ  TYR C  26    14268   6555   8416   1206   -137    681       C  
ATOM   3628  OH  TYR C  26      66.574  18.646  -7.388  1.00 80.27           O  
ANISOU 3628  OH  TYR C  26    14856   6929   8713    976     88    615       O  
ATOM   3629  N   GLY C  27      59.211  16.124 -11.424  1.00 63.47           N  
ANISOU 3629  N   GLY C  27    11704   5035   7378   2056  -1787   1099       N  
ATOM   3630  CA  GLY C  27      57.854  15.725 -11.779  1.00 63.11           C  
ANISOU 3630  CA  GLY C  27    11334   5059   7586   2241  -2137   1171       C  
ATOM   3631  C   GLY C  27      57.795  14.288 -12.261  1.00 65.18           C  
ANISOU 3631  C   GLY C  27    11414   5503   7847   2019  -2244   1165       C  
ATOM   3632  O   GLY C  27      57.017  13.495 -11.728  1.00 64.34           O  
ANISOU 3632  O   GLY C  27    10815   5602   8029   2064  -2260   1150       O  
ATOM   3633  N   ILE C  28      58.650  13.947 -13.259  1.00 60.73           N  
ANISOU 3633  N   ILE C  28    11268   4855   6951   1768  -2287   1173       N  
ATOM   3634  CA  ILE C  28      58.795  12.608 -13.854  1.00 59.94           C  
ANISOU 3634  CA  ILE C  28    11122   4879   6772   1531  -2369   1157       C  
ATOM   3635  C   ILE C  28      59.256  11.613 -12.771  1.00 60.38           C  
ANISOU 3635  C   ILE C  28    10800   5180   6960   1393  -2020   1053       C  
ATOM   3636  O   ILE C  28      58.709  10.514 -12.663  1.00 59.42           O  
ANISOU 3636  O   ILE C  28    10341   5229   7008   1338  -2107   1044       O  
ATOM   3637  CB  ILE C  28      59.762  12.633 -15.087  1.00 63.39           C  
ANISOU 3637  CB  ILE C  28    12157   5140   6789   1302  -2393   1172       C  
ATOM   3638  CG1 ILE C  28      59.344  13.693 -16.158  1.00 64.23           C  
ANISOU 3638  CG1 ILE C  28    12726   4964   6714   1431  -2728   1284       C  
ATOM   3639  CG2 ILE C  28      59.950  11.235 -15.711  1.00 64.08           C  
ANISOU 3639  CG2 ILE C  28    12240   5330   6777   1071  -2469   1146       C  
ATOM   3640  CD1 ILE C  28      57.986  13.471 -16.909  1.00 74.88           C  
ANISOU 3640  CD1 ILE C  28    13976   6273   8201   1597  -3266   1388       C  
ATOM   3641  N   GLU C  29      60.243  12.032 -11.958  1.00 54.79           N  
ANISOU 3641  N   GLU C  29    10167   4476   6177   1337  -1646    979       N  
ATOM   3642  CA  GLU C  29      60.791  11.274 -10.837  1.00 53.70           C  
ANISOU 3642  CA  GLU C  29     9732   4535   6137   1225  -1315    884       C  
ATOM   3643  C   GLU C  29      59.692  10.944  -9.825  1.00 56.09           C  
ANISOU 3643  C   GLU C  29     9516   5005   6790   1400  -1315    881       C  
ATOM   3644  O   GLU C  29      59.648   9.814  -9.341  1.00 54.09           O  
ANISOU 3644  O   GLU C  29     8968   4935   6647   1288  -1216    840       O  
ATOM   3645  CB  GLU C  29      61.882  12.093 -10.153  1.00 54.82           C  
ANISOU 3645  CB  GLU C  29    10069   4604   6155   1183   -995    823       C  
ATOM   3646  CG  GLU C  29      63.254  11.468 -10.222  1.00 60.91           C  
ANISOU 3646  CG  GLU C  29    10981   5424   6740    907   -752    751       C  
ATOM   3647  CD  GLU C  29      64.387  12.469 -10.297  1.00 66.85           C  
ANISOU 3647  CD  GLU C  29    12103   6014   7283    815   -565    728       C  
ATOM   3648  OE1 GLU C  29      65.199  12.343 -11.236  1.00 56.32           O  
ANISOU 3648  OE1 GLU C  29    11080   4597   5722    627   -532    730       O  
ATOM   3649  OE2 GLU C  29      64.470  13.370  -9.431  1.00 57.18           O  
ANISOU 3649  OE2 GLU C  29    10871   4737   6117    918   -440    706       O  
ATOM   3650  N   PHE C  30      58.790  11.929  -9.533  1.00 52.80           N  
ANISOU 3650  N   PHE C  30     8998   4514   6551   1677  -1416    926       N  
ATOM   3651  CA  PHE C  30      57.657  11.764  -8.612  1.00 52.09           C  
ANISOU 3651  CA  PHE C  30     8411   4564   6816   1873  -1391    927       C  
ATOM   3652  C   PHE C  30      56.702  10.668  -9.078  1.00 56.56           C  
ANISOU 3652  C   PHE C  30     8644   5268   7577   1830  -1654    975       C  
ATOM   3653  O   PHE C  30      56.386   9.782  -8.294  1.00 55.97           O  
ANISOU 3653  O   PHE C  30     8189   5383   7693   1773  -1507    939       O  
ATOM   3654  CB  PHE C  30      56.892  13.095  -8.349  1.00 52.79           C  
ANISOU 3654  CB  PHE C  30     8485   4516   7059   2205  -1453    966       C  
ATOM   3655  CG  PHE C  30      55.629  12.898  -7.531  1.00 53.58           C  
ANISOU 3655  CG  PHE C  30     8044   4759   7554   2420  -1426    972       C  
ATOM   3656  CD1 PHE C  30      55.698  12.581  -6.174  1.00 55.78           C  
ANISOU 3656  CD1 PHE C  30     8057   5182   7953   2416  -1055    892       C  
ATOM   3657  CD2 PHE C  30      54.375  12.942  -8.133  1.00 54.84           C  
ANISOU 3657  CD2 PHE C  30     7949   4916   7970   2606  -1775   1059       C  
ATOM   3658  CE1 PHE C  30      54.534  12.328  -5.432  1.00 55.64           C  
ANISOU 3658  CE1 PHE C  30     7541   5302   8299   2591   -984    897       C  
ATOM   3659  CE2 PHE C  30      53.212  12.687  -7.388  1.00 57.02           C  
ANISOU 3659  CE2 PHE C  30     7674   5343   8649   2785  -1721   1063       C  
ATOM   3660  CZ  PHE C  30      53.300  12.394  -6.041  1.00 54.43           C  
ANISOU 3660  CZ  PHE C  30     7100   5154   8426   2775  -1302    981       C  
ATOM   3661  N   ILE C  31      56.263  10.735 -10.348  1.00 54.67           N  
ANISOU 3661  N   ILE C  31     8579   4919   7275   1841  -2050   1057       N  
ATOM   3662  CA  ILE C  31      55.329   9.803 -10.984  1.00 55.86           C  
ANISOU 3662  CA  ILE C  31     8476   5158   7588   1790  -2391   1112       C  
ATOM   3663  C   ILE C  31      55.910   8.373 -11.108  1.00 62.13           C  
ANISOU 3663  C   ILE C  31     9261   6082   8264   1478  -2304   1060       C  
ATOM   3664  O   ILE C  31      55.298   7.441 -10.589  1.00 63.22           O  
ANISOU 3664  O   ILE C  31     8979   6397   8645   1426  -2277   1048       O  
ATOM   3665  CB  ILE C  31      54.842  10.396 -12.340  1.00 59.33           C  
ANISOU 3665  CB  ILE C  31     9217   5400   7925   1881  -2860   1213       C  
ATOM   3666  CG1 ILE C  31      53.755  11.466 -12.106  1.00 59.35           C  
ANISOU 3666  CG1 ILE C  31     9022   5324   8204   2238  -3025   1279       C  
ATOM   3667  CG2 ILE C  31      54.335   9.312 -13.296  1.00 61.33           C  
ANISOU 3667  CG2 ILE C  31     9402   5702   8197   1720  -3237   1258       C  
ATOM   3668  CD1 ILE C  31      53.956  12.736 -12.869  1.00 70.18           C  
ANISOU 3668  CD1 ILE C  31    10901   6419   9346   2376  -3230   1344       C  
ATOM   3669  N   VAL C  32      57.077   8.208 -11.786  1.00 58.17           N  
ANISOU 3669  N   VAL C  32     9221   5482   7399   1276  -2242   1028       N  
ATOM   3670  CA  VAL C  32      57.751   6.921 -12.023  1.00 56.76           C  
ANISOU 3670  CA  VAL C  32     9111   5385   7070   1000  -2154    973       C  
ATOM   3671  C   VAL C  32      58.098   6.229 -10.716  1.00 59.15           C  
ANISOU 3671  C   VAL C  32     9093   5871   7508    932  -1786    894       C  
ATOM   3672  O   VAL C  32      57.879   5.022 -10.590  1.00 60.50           O  
ANISOU 3672  O   VAL C  32     9052   6167   7768    790  -1798    875       O  
ATOM   3673  CB  VAL C  32      58.969   7.073 -12.982  1.00 60.53           C  
ANISOU 3673  CB  VAL C  32    10157   5701   7143    837  -2105    951       C  
ATOM   3674  CG1 VAL C  32      59.938   5.889 -12.889  1.00 60.33           C  
ANISOU 3674  CG1 VAL C  32    10182   5761   6980    592  -1864    866       C  
ATOM   3675  CG2 VAL C  32      58.505   7.270 -14.422  1.00 60.20           C  
ANISOU 3675  CG2 VAL C  32    10447   5490   6937    832  -2526   1032       C  
ATOM   3676  N   GLY C  33      58.592   6.997  -9.754  1.00 53.33           N  
ANISOU 3676  N   GLY C  33     8345   5135   6782   1031  -1486    853       N  
ATOM   3677  CA  GLY C  33      58.980   6.492  -8.442  1.00 52.55           C  
ANISOU 3677  CA  GLY C  33     8003   5184   6779    982  -1142    781       C  
ATOM   3678  C   GLY C  33      57.821   6.076  -7.559  1.00 55.43           C  
ANISOU 3678  C   GLY C  33     7878   5703   7480   1081  -1121    797       C  
ATOM   3679  O   GLY C  33      57.949   5.126  -6.787  1.00 53.70           O  
ANISOU 3679  O   GLY C  33     7456   5619   7330    963   -935    756       O  
ATOM   3680  N   MET C  34      56.696   6.806  -7.642  1.00 52.78           N  
ANISOU 3680  N   MET C  34     7352   5339   7362   1304  -1297    859       N  
ATOM   3681  CA  MET C  34      55.489   6.544  -6.858  1.00 52.67           C  
ANISOU 3681  CA  MET C  34     6837   5465   7710   1423  -1265    881       C  
ATOM   3682  C   MET C  34      54.746   5.353  -7.458  1.00 56.29           C  
ANISOU 3682  C   MET C  34     7057   6019   8311   1272  -1531    924       C  
ATOM   3683  O   MET C  34      54.297   4.478  -6.717  1.00 55.48           O  
ANISOU 3683  O   MET C  34     6612   6068   8398   1185  -1392    910       O  
ATOM   3684  CB  MET C  34      54.595   7.798  -6.804  1.00 55.18           C  
ANISOU 3684  CB  MET C  34     7035   5703   8228   1737  -1363    929       C  
ATOM   3685  CG  MET C  34      54.013   8.076  -5.435  1.00 59.26           C  
ANISOU 3685  CG  MET C  34     7194   6317   9005   1909  -1049    898       C  
ATOM   3686  SD  MET C  34      55.201   8.671  -4.201  1.00 63.48           S  
ANISOU 3686  SD  MET C  34     7998   6810   9312   1909   -582    796       S  
ATOM   3687  CE  MET C  34      54.082   9.361  -3.013  1.00 60.05           C  
ANISOU 3687  CE  MET C  34     7201   6410   9206   2219   -347    787       C  
ATOM   3688  N   LEU C  35      54.642   5.296  -8.799  1.00 53.23           N  
ANISOU 3688  N   LEU C  35     6888   5529   7808   1217  -1915    976       N  
ATOM   3689  CA  LEU C  35      54.004   4.159  -9.463  1.00 53.72           C  
ANISOU 3689  CA  LEU C  35     6789   5655   7968   1045  -2206   1012       C  
ATOM   3690  C   LEU C  35      54.870   2.901  -9.283  1.00 57.24           C  
ANISOU 3690  C   LEU C  35     7345   6166   8236    767  -2016    944       C  
ATOM   3691  O   LEU C  35      54.335   1.825  -9.006  1.00 58.25           O  
ANISOU 3691  O   LEU C  35     7176   6413   8541    632  -2036    947       O  
ATOM   3692  CB  LEU C  35      53.723   4.443 -10.959  1.00 54.12           C  
ANISOU 3692  CB  LEU C  35     7120   5552   7891   1049  -2682   1080       C  
ATOM   3693  CG  LEU C  35      52.541   5.381 -11.256  1.00 59.75           C  
ANISOU 3693  CG  LEU C  35     7605   6219   8877   1310  -3002   1169       C  
ATOM   3694  CD1 LEU C  35      52.687   6.048 -12.600  1.00 60.13           C  
ANISOU 3694  CD1 LEU C  35     8120   6053   8674   1358  -3379   1229       C  
ATOM   3695  CD2 LEU C  35      51.209   4.649 -11.192  1.00 63.83           C  
ANISOU 3695  CD2 LEU C  35     7594   6874   9783   1278  -3250   1219       C  
ATOM   3696  N   GLY C  36      56.192   3.067  -9.388  1.00 51.27           N  
ANISOU 3696  N   GLY C  36     6995   5328   7155    692  -1819    885       N  
ATOM   3697  CA  GLY C  36      57.164   1.988  -9.252  1.00 49.97           C  
ANISOU 3697  CA  GLY C  36     6975   5201   6811    467  -1628    817       C  
ATOM   3698  C   GLY C  36      57.260   1.415  -7.856  1.00 51.83           C  
ANISOU 3698  C   GLY C  36     6918   5582   7193    435  -1293    772       C  
ATOM   3699  O   GLY C  36      57.152   0.205  -7.684  1.00 50.68           O  
ANISOU 3699  O   GLY C  36     6646   5514   7097    268  -1276    758       O  
ATOM   3700  N   ASN C  37      57.452   2.276  -6.847  1.00 49.02           N  
ANISOU 3700  N   ASN C  37     6489   5248   6890    592  -1031    751       N  
ATOM   3701  CA  ASN C  37      57.574   1.844  -5.456  1.00 48.92           C  
ANISOU 3701  CA  ASN C  37     6258   5351   6978    573   -703    710       C  
ATOM   3702  C   ASN C  37      56.275   1.335  -4.858  1.00 54.49           C  
ANISOU 3702  C   ASN C  37     6512   6184   8008    594   -706    752       C  
ATOM   3703  O   ASN C  37      56.341   0.463  -4.000  1.00 54.48           O  
ANISOU 3703  O   ASN C  37     6370   6274   8055    480   -501    728       O  
ATOM   3704  CB  ASN C  37      58.202   2.911  -4.577  1.00 46.84           C  
ANISOU 3704  CB  ASN C  37     6106   5050   6639    716   -434    668       C  
ATOM   3705  CG  ASN C  37      59.697   2.909  -4.673  1.00 52.37           C  
ANISOU 3705  CG  ASN C  37     7157   5684   7056    605   -304    606       C  
ATOM   3706  OD1 ASN C  37      60.366   1.951  -4.283  1.00 47.53           O  
ANISOU 3706  OD1 ASN C  37     6564   5125   6372    453   -175    565       O  
ATOM   3707  ND2 ASN C  37      60.255   3.976  -5.198  1.00 39.78           N  
ANISOU 3707  ND2 ASN C  37     5843   3966   5307    678   -334    601       N  
ATOM   3708  N   PHE C  38      55.103   1.838  -5.301  1.00 52.05           N  
ANISOU 3708  N   PHE C  38     5969   5877   7930    732   -936    817       N  
ATOM   3709  CA  PHE C  38      53.848   1.320  -4.766  1.00 52.45           C  
ANISOU 3709  CA  PHE C  38     5539   6058   8331    735   -931    858       C  
ATOM   3710  C   PHE C  38      53.525  -0.078  -5.286  1.00 54.01           C  
ANISOU 3710  C   PHE C  38     5638   6309   8575    476  -1122    879       C  
ATOM   3711  O   PHE C  38      52.919  -0.857  -4.554  1.00 53.97           O  
ANISOU 3711  O   PHE C  38     5318   6417   8769    377   -974    887       O  
ATOM   3712  CB  PHE C  38      52.675   2.278  -4.952  1.00 55.49           C  
ANISOU 3712  CB  PHE C  38     5643   6437   9002    978  -1107    919       C  
ATOM   3713  CG  PHE C  38      52.446   3.181  -3.761  1.00 59.15           C  
ANISOU 3713  CG  PHE C  38     5946   6925   9602   1216   -772    896       C  
ATOM   3714  CD1 PHE C  38      52.212   2.649  -2.494  1.00 64.22           C  
ANISOU 3714  CD1 PHE C  38     6234   7698  10467   1204   -459    885       C  
ATOM   3715  CD2 PHE C  38      52.430   4.564  -3.908  1.00 62.54           C  
ANISOU 3715  CD2 PHE C  38     6604   7228   9930   1450   -763    886       C  
ATOM   3716  CE1 PHE C  38      51.990   3.489  -1.395  1.00 65.77           C  
ANISOU 3716  CE1 PHE C  38     6320   7900  10771   1432   -129    856       C  
ATOM   3717  CE2 PHE C  38      52.209   5.400  -2.810  1.00 65.99           C  
ANISOU 3717  CE2 PHE C  38     6929   7665  10481   1677   -452    856       C  
ATOM   3718  CZ  PHE C  38      51.985   4.857  -1.561  1.00 64.35           C  
ANISOU 3718  CZ  PHE C  38     6379   7588  10484   1671   -133    838       C  
ATOM   3719  N   THR C  39      53.972  -0.409  -6.517  1.00 47.98           N  
ANISOU 3719  N   THR C  39     5182   5447   7601    353  -1423    883       N  
ATOM   3720  CA  THR C  39      53.791  -1.721  -7.151  1.00 46.16           C  
ANISOU 3720  CA  THR C  39     4963   5225   7352     98  -1636    891       C  
ATOM   3721  C   THR C  39      54.602  -2.793  -6.425  1.00 46.26           C  
ANISOU 3721  C   THR C  39     5072   5275   7230    -85  -1345    832       C  
ATOM   3722  O   THR C  39      54.049  -3.841  -6.077  1.00 44.63           O  
ANISOU 3722  O   THR C  39     4639   5140   7177   -253  -1340    847       O  
ATOM   3723  CB  THR C  39      54.122  -1.641  -8.653  1.00 54.03           C  
ANISOU 3723  CB  THR C  39     6349   6075   8106     44  -1999    900       C  
ATOM   3724  OG1 THR C  39      53.294  -0.644  -9.243  1.00 51.18           O  
ANISOU 3724  OG1 THR C  39     5889   5672   7887    227  -2292    967       O  
ATOM   3725  CG2 THR C  39      53.905  -2.977  -9.391  1.00 55.07           C  
ANISOU 3725  CG2 THR C  39     6548   6184   8193   -219  -2248    902       C  
ATOM   3726  N   VAL C  40      55.897  -2.515  -6.177  1.00 42.64           N  
ANISOU 3726  N   VAL C  40     4940   4761   6502    -54  -1113    769       N  
ATOM   3727  CA  VAL C  40      56.826  -3.434  -5.508  1.00 42.72           C  
ANISOU 3727  CA  VAL C  40     5077   4786   6369   -192   -856    711       C  
ATOM   3728  C   VAL C  40      56.449  -3.655  -4.042  1.00 50.18           C  
ANISOU 3728  C   VAL C  40     5729   5845   7493   -174   -554    716       C  
ATOM   3729  O   VAL C  40      56.510  -4.798  -3.586  1.00 49.88           O  
ANISOU 3729  O   VAL C  40     5652   5839   7462   -339   -456    707       O  
ATOM   3730  CB  VAL C  40      58.326  -3.089  -5.687  1.00 45.20           C  
ANISOU 3730  CB  VAL C  40     5790   5010   6375   -172   -721    644       C  
ATOM   3731  CG1 VAL C  40      58.747  -3.202  -7.146  1.00 44.85           C  
ANISOU 3731  CG1 VAL C  40     6075   4845   6121   -250   -968    633       C  
ATOM   3732  CG2 VAL C  40      58.675  -1.724  -5.124  1.00 44.72           C  
ANISOU 3732  CG2 VAL C  40     5768   4938   6286     27   -552    632       C  
ATOM   3733  N   VAL C  41      56.024  -2.585  -3.324  1.00 49.36           N  
ANISOU 3733  N   VAL C  41     5446   5784   7524     26   -404    729       N  
ATOM   3734  CA  VAL C  41      55.588  -2.645  -1.918  1.00 49.95           C  
ANISOU 3734  CA  VAL C  41     5269   5952   7756     64    -87    731       C  
ATOM   3735  C   VAL C  41      54.366  -3.548  -1.791  1.00 56.82           C  
ANISOU 3735  C   VAL C  41     5766   6916   8909    -67   -141    787       C  
ATOM   3736  O   VAL C  41      54.399  -4.481  -0.982  1.00 55.93           O  
ANISOU 3736  O   VAL C  41     5601   6847   8805   -216     55    784       O  
ATOM   3737  CB  VAL C  41      55.377  -1.236  -1.292  1.00 53.49           C  
ANISOU 3737  CB  VAL C  41     5652   6401   8272    322     85    724       C  
ATOM   3738  CG1 VAL C  41      54.483  -1.276  -0.048  1.00 52.73           C  
ANISOU 3738  CG1 VAL C  41     5232   6403   8402    372    382    738       C  
ATOM   3739  CG2 VAL C  41      56.715  -0.592  -0.963  1.00 53.36           C  
ANISOU 3739  CG2 VAL C  41     6004   6300   7968    386    232    660       C  
ATOM   3740  N   PHE C  42      53.319  -3.301  -2.621  1.00 56.46           N  
ANISOU 3740  N   PHE C  42     5475   6890   9090    -26   -430    842       N  
ATOM   3741  CA  PHE C  42      52.090  -4.096  -2.634  1.00 58.43           C  
ANISOU 3741  CA  PHE C  42     5322   7227   9651   -166   -536    900       C  
ATOM   3742  C   PHE C  42      52.341  -5.542  -3.051  1.00 61.38           C  
ANISOU 3742  C   PHE C  42     5825   7573   9922   -463   -664    898       C  
ATOM   3743  O   PHE C  42      51.709  -6.451  -2.509  1.00 61.03           O  
ANISOU 3743  O   PHE C  42     5528   7599  10061   -634   -566    928       O  
ATOM   3744  CB  PHE C  42      50.984  -3.434  -3.472  1.00 62.10           C  
ANISOU 3744  CB  PHE C  42     5510   7705  10381    -46   -875    960       C  
ATOM   3745  CG  PHE C  42      50.442  -2.123  -2.928  1.00 66.38           C  
ANISOU 3745  CG  PHE C  42     5785   8291  11145    248   -713    974       C  
ATOM   3746  CD1 PHE C  42      50.497  -1.834  -1.564  1.00 71.83           C  
ANISOU 3746  CD1 PHE C  42     6281   9061  11949    316   -271    956       C  
ATOM   3747  CD2 PHE C  42      49.834  -1.199  -3.773  1.00 70.37           C  
ANISOU 3747  CD2 PHE C  42     6245   8744  11748    459  -1007   1009       C  
ATOM   3748  CE1 PHE C  42      50.007  -0.619  -1.065  1.00 73.56           C  
ANISOU 3748  CE1 PHE C  42     6279   9303  12367    602    -97    959       C  
ATOM   3749  CE2 PHE C  42      49.336   0.009  -3.273  1.00 74.49           C  
ANISOU 3749  CE2 PHE C  42     6530   9287  12485    753   -854   1018       C  
ATOM   3750  CZ  PHE C  42      49.427   0.291  -1.921  1.00 73.05           C  
ANISOU 3750  CZ  PHE C  42     6161   9182  12411    826   -388    989       C  
ATOM   3751  N   GLY C  43      53.304  -5.743  -3.954  1.00 56.40           N  
ANISOU 3751  N   GLY C  43     5607   6831   8991   -522   -845    859       N  
ATOM   3752  CA  GLY C  43      53.733  -7.066  -4.393  1.00 54.83           C  
ANISOU 3752  CA  GLY C  43     5621   6571   8642   -774   -949    839       C  
ATOM   3753  C   GLY C  43      54.257  -7.866  -3.218  1.00 55.27           C  
ANISOU 3753  C   GLY C  43     5720   6650   8630   -873   -603    813       C  
ATOM   3754  O   GLY C  43      53.804  -8.981  -2.982  1.00 55.91           O  
ANISOU 3754  O   GLY C  43     5673   6751   8820  -1079   -594    839       O  
ATOM   3755  N   TYR C  44      55.161  -7.271  -2.434  1.00 48.64           N  
ANISOU 3755  N   TYR C  44     5055   5803   7622   -730   -328    769       N  
ATOM   3756  CA  TYR C  44      55.730  -7.877  -1.228  1.00 47.20           C  
ANISOU 3756  CA  TYR C  44     4952   5631   7352   -788    -10    748       C  
ATOM   3757  C   TYR C  44      54.741  -8.006  -0.072  1.00 56.38           C  
ANISOU 3757  C   TYR C  44     5773   6895   8754   -815    236    796       C  
ATOM   3758  O   TYR C  44      54.916  -8.892   0.762  1.00 55.65           O  
ANISOU 3758  O   TYR C  44     5736   6797   8613   -946    433    800       O  
ATOM   3759  CB  TYR C  44      56.931  -7.072  -0.748  1.00 44.92           C  
ANISOU 3759  CB  TYR C  44     4923   5305   6840   -620    174    690       C  
ATOM   3760  CG  TYR C  44      58.269  -7.524  -1.282  1.00 40.73           C  
ANISOU 3760  CG  TYR C  44     4763   4673   6040   -669    109    632       C  
ATOM   3761  CD1 TYR C  44      58.390  -8.052  -2.566  1.00 40.67           C  
ANISOU 3761  CD1 TYR C  44     4902   4591   5958   -772   -156    622       C  
ATOM   3762  CD2 TYR C  44      59.434  -7.314  -0.550  1.00 39.99           C  
ANISOU 3762  CD2 TYR C  44     4876   4549   5768   -598    308    584       C  
ATOM   3763  CE1 TYR C  44      59.629  -8.442  -3.070  1.00 39.11           C  
ANISOU 3763  CE1 TYR C  44     5038   4297   5525   -798   -173    561       C  
ATOM   3764  CE2 TYR C  44      60.680  -7.644  -1.065  1.00 39.75           C  
ANISOU 3764  CE2 TYR C  44     5138   4433   5532   -621    261    528       C  
ATOM   3765  CZ  TYR C  44      60.773  -8.213  -2.322  1.00 44.81           C  
ANISOU 3765  CZ  TYR C  44     5909   5004   6111   -715     44    515       C  
ATOM   3766  OH  TYR C  44      62.008  -8.550  -2.796  1.00 46.61           O  
ANISOU 3766  OH  TYR C  44     6416   5146   6149   -725     47    454       O  
ATOM   3767  N   LEU C  45      53.749  -7.103   0.018  1.00 57.91           N  
ANISOU 3767  N   LEU C  45     5635   7170   9198   -679    246    831       N  
ATOM   3768  CA  LEU C  45      52.750  -7.142   1.087  1.00 60.66           C  
ANISOU 3768  CA  LEU C  45     5629   7618   9802   -688    519    872       C  
ATOM   3769  C   LEU C  45      51.619  -8.131   0.805  1.00 72.82           C  
ANISOU 3769  C   LEU C  45     6841   9212  11615   -919    390    935       C  
ATOM   3770  O   LEU C  45      51.070  -8.692   1.753  1.00 73.00           O  
ANISOU 3770  O   LEU C  45     6690   9285  11760  -1046    655    966       O  
ATOM   3771  CB  LEU C  45      52.158  -5.748   1.371  1.00 60.69           C  
ANISOU 3771  CB  LEU C  45     5399   7678   9982   -417    627    876       C  
ATOM   3772  CG  LEU C  45      53.002  -4.754   2.182  1.00 65.33           C  
ANISOU 3772  CG  LEU C  45     6238   8226  10359   -204    890    819       C  
ATOM   3773  CD1 LEU C  45      52.341  -3.391   2.201  1.00 65.40           C  
ANISOU 3773  CD1 LEU C  45     6045   8258  10545     69    913    821       C  
ATOM   3774  CD2 LEU C  45      53.224  -5.227   3.620  1.00 67.05           C  
ANISOU 3774  CD2 LEU C  45     6519   8459  10498   -267   1291    808       C  
ATOM   3775  N   PHE C  46      51.263  -8.334  -0.483  1.00 75.10           N  
ANISOU 3775  N   PHE C  46     7062   9480  11993   -988    -18    956       N  
ATOM   3776  CA  PHE C  46      50.160  -9.205  -0.893  1.00 77.40           C  
ANISOU 3776  CA  PHE C  46     7034   9814  12561  -1222   -217   1015       C  
ATOM   3777  C   PHE C  46      50.583 -10.580  -1.441  1.00 85.25           C  
ANISOU 3777  C   PHE C  46     8302  10708  13379  -1510   -397   1006       C  
ATOM   3778  O   PHE C  46      49.840 -11.546  -1.241  1.00 85.58           O  
ANISOU 3778  O   PHE C  46     8148  10774  13595  -1757   -367   1049       O  
ATOM   3779  CB  PHE C  46      49.242  -8.480  -1.886  1.00 79.87           C  
ANISOU 3779  CB  PHE C  46     7056  10163  13127  -1121   -584   1052       C  
ATOM   3780  CG  PHE C  46      48.452  -7.352  -1.257  1.00 82.53           C  
ANISOU 3780  CG  PHE C  46     6984  10609  13765   -874   -397   1079       C  
ATOM   3781  CD1 PHE C  46      48.959  -6.056  -1.224  1.00 86.45           C  
ANISOU 3781  CD1 PHE C  46     7624  11077  14144   -562   -342   1045       C  
ATOM   3782  CD2 PHE C  46      47.201  -7.586  -0.693  1.00 85.48           C  
ANISOU 3782  CD2 PHE C  46     6830  11104  14546   -953   -257   1135       C  
ATOM   3783  CE1 PHE C  46      48.234  -5.015  -0.632  1.00 87.57           C  
ANISOU 3783  CE1 PHE C  46     7414  11297  14560   -313   -157   1062       C  
ATOM   3784  CE2 PHE C  46      46.475  -6.544  -0.104  1.00 88.65           C  
ANISOU 3784  CE2 PHE C  46     6847  11598  15239   -699    -51   1151       C  
ATOM   3785  CZ  PHE C  46      46.996  -5.265  -0.080  1.00 86.77           C  
ANISOU 3785  CZ  PHE C  46     6783  11317  14868   -371     -7   1112       C  
ATOM   3786  N   CYS C  47      51.749 -10.683  -2.110  1.00 83.74           N  
ANISOU 3786  N   CYS C  47     8563  10398  12858  -1484   -564    949       N  
ATOM   3787  CA  CYS C  47      52.236 -11.957  -2.656  1.00 84.44           C  
ANISOU 3787  CA  CYS C  47     8963  10366  12755  -1720   -724    926       C  
ATOM   3788  C   CYS C  47      53.243 -12.618  -1.710  1.00 87.37           C  
ANISOU 3788  C   CYS C  47     9621  10679  12896  -1759   -409    891       C  
ATOM   3789  O   CYS C  47      53.000 -13.736  -1.245  1.00 87.37           O  
ANISOU 3789  O   CYS C  47     9618  10648  12933  -1983   -333    916       O  
ATOM   3790  CB  CYS C  47      52.818 -11.792  -4.061  1.00 85.65           C  
ANISOU 3790  CB  CYS C  47     9446  10407  12688  -1680  -1069    882       C  
ATOM   3791  SG  CYS C  47      51.866 -10.700  -5.151  1.00 90.07           S  
ANISOU 3791  SG  CYS C  47     9757  11008  13458  -1576  -1474    926       S  
ATOM   3792  N   MET C  48      54.363 -11.918  -1.419  1.00 82.69           N  
ANISOU 3792  N   MET C  48     9280  10063  12074  -1549   -243    838       N  
ATOM   3793  CA  MET C  48      55.462 -12.397  -0.566  1.00 81.68           C  
ANISOU 3793  CA  MET C  48     9442   9874  11719  -1546      9    802       C  
ATOM   3794  C   MET C  48      55.070 -12.632   0.895  1.00 84.92           C  
ANISOU 3794  C   MET C  48     9692  10345  12230  -1594    345    845       C  
ATOM   3795  O   MET C  48      54.663 -11.698   1.595  1.00 85.44           O  
ANISOU 3795  O   MET C  48     9524  10510  12427  -1458    536    864       O  
ATOM   3796  CB  MET C  48      56.675 -11.466  -0.657  1.00 83.56           C  
ANISOU 3796  CB  MET C  48     9939  10081  11730  -1318     70    737       C  
ATOM   3797  CG  MET C  48      57.200 -11.317  -2.049  1.00 86.89           C  
ANISOU 3797  CG  MET C  48    10590  10419  12004  -1290   -202    692       C  
ATOM   3798  SD  MET C  48      58.491 -12.501  -2.402  1.00 90.92           S  
ANISOU 3798  SD  MET C  48    11520  10776  12249  -1393   -226    629       S  
ATOM   3799  CE  MET C  48      58.916 -12.001  -3.970  1.00 87.45           C  
ANISOU 3799  CE  MET C  48    11306  10262  11660  -1323   -472    577       C  
ATOM   3800  N   LYS C  49      55.208 -13.886   1.350  1.00 79.30           N  
ANISOU 3800  N   LYS C  49     9137   9554  11438  -1786    426    860       N  
ATOM   3801  CA  LYS C  49      54.887 -14.281   2.721  1.00 77.89           C  
ANISOU 3801  CA  LYS C  49     8889   9400  11306  -1870    747    907       C  
ATOM   3802  C   LYS C  49      56.135 -14.656   3.536  1.00 76.82           C  
ANISOU 3802  C   LYS C  49     9140   9162  10887  -1826    910    879       C  
ATOM   3803  O   LYS C  49      56.209 -14.291   4.713  1.00 77.89           O  
ANISOU 3803  O   LYS C  49     9287   9325  10985  -1775   1195    899       O  
ATOM   3804  CB  LYS C  49      53.804 -15.385   2.769  1.00 80.84           C  
ANISOU 3804  CB  LYS C  49     9057   9772  11887  -2166    725    976       C  
ATOM   3805  CG  LYS C  49      54.073 -16.614   1.894  1.00 99.83           C  
ANISOU 3805  CG  LYS C  49    11702  12035  14194  -2377    462    965       C  
ATOM   3806  CD  LYS C  49      52.882 -17.570   1.887  1.00111.30           C  
ANISOU 3806  CD  LYS C  49    12922  13487  15879  -2692    430   1036       C  
ATOM   3807  CE  LYS C  49      53.098 -18.784   1.008  1.00121.40           C  
ANISOU 3807  CE  LYS C  49    14464  14604  17057  -2912    153   1020       C  
ATOM   3808  NZ  LYS C  49      52.952 -18.473  -0.440  1.00127.21           N  
ANISOU 3808  NZ  LYS C  49    15166  15334  17833  -2900   -235    983       N  
ATOM   3809  N   ASN C  50      57.109 -15.363   2.923  1.00 67.15           N  
ANISOU 3809  N   ASN C  50     8235   7814   9466  -1837    730    831       N  
ATOM   3810  CA  ASN C  50      58.327 -15.776   3.623  1.00 64.67           C  
ANISOU 3810  CA  ASN C  50     8261   7395   8914  -1779    838    805       C  
ATOM   3811  C   ASN C  50      59.528 -15.011   3.106  1.00 61.57           C  
ANISOU 3811  C   ASN C  50     8046   6985   8364  -1562    748    726       C  
ATOM   3812  O   ASN C  50      60.114 -15.373   2.090  1.00 61.74           O  
ANISOU 3812  O   ASN C  50     8230   6925   8303  -1564    558    678       O  
ATOM   3813  CB  ASN C  50      58.524 -17.308   3.580  1.00 68.89           C  
ANISOU 3813  CB  ASN C  50     9020   7780   9376  -1982    769    825       C  
ATOM   3814  CG  ASN C  50      58.882 -17.896   2.227  1.00 95.34           C  
ANISOU 3814  CG  ASN C  50    12506  11034  12686  -2043    486    777       C  
ATOM   3815  OD1 ASN C  50      58.178 -17.720   1.219  1.00 88.34           O  
ANISOU 3815  OD1 ASN C  50    11443  10191  11930  -2115    302    777       O  
ATOM   3816  ND2 ASN C  50      60.003 -18.602   2.185  1.00 86.66           N  
ANISOU 3816  ND2 ASN C  50    11739   9789  11400  -2005    442    733       N  
ATOM   3817  N   TRP C  51      59.879 -13.929   3.794  1.00 52.46           N  
ANISOU 3817  N   TRP C  51     6867   5898   7166  -1384    900    710       N  
ATOM   3818  CA  TRP C  51      60.957 -13.043   3.364  1.00 49.29           C  
ANISOU 3818  CA  TRP C  51     6591   5493   6644  -1192    837    640       C  
ATOM   3819  C   TRP C  51      62.341 -13.530   3.738  1.00 44.66           C  
ANISOU 3819  C   TRP C  51     6294   4804   5871  -1138    846    601       C  
ATOM   3820  O   TRP C  51      62.534 -14.078   4.817  1.00 43.32           O  
ANISOU 3820  O   TRP C  51     6238   4587   5633  -1173    968    632       O  
ATOM   3821  CB  TRP C  51      60.743 -11.627   3.932  1.00 48.38           C  
ANISOU 3821  CB  TRP C  51     6338   5477   6566  -1031    979    636       C  
ATOM   3822  CG  TRP C  51      59.578 -10.850   3.374  1.00 49.39           C  
ANISOU 3822  CG  TRP C  51     6172   5703   6890  -1006    935    660       C  
ATOM   3823  CD1 TRP C  51      58.470 -11.350   2.752  1.00 52.37           C  
ANISOU 3823  CD1 TRP C  51     6337   6111   7449  -1144    817    704       C  
ATOM   3824  CD2 TRP C  51      59.355  -9.443   3.515  1.00 49.09           C  
ANISOU 3824  CD2 TRP C  51     6010   5737   6904   -828   1007    647       C  
ATOM   3825  NE1 TRP C  51      57.606 -10.333   2.432  1.00 51.77           N  
ANISOU 3825  NE1 TRP C  51     5995   6128   7549  -1047    788    720       N  
ATOM   3826  CE2 TRP C  51      58.107  -9.154   2.915  1.00 53.09           C  
ANISOU 3826  CE2 TRP C  51     6220   6316   7637   -845    917    685       C  
ATOM   3827  CE3 TRP C  51      60.083  -8.395   4.099  1.00 50.29           C  
ANISOU 3827  CE3 TRP C  51     6282   5886   6938   -658   1124    605       C  
ATOM   3828  CZ2 TRP C  51      57.578  -7.859   2.870  1.00 52.08           C  
ANISOU 3828  CZ2 TRP C  51     5914   6253   7622   -671    950    685       C  
ATOM   3829  CZ3 TRP C  51      59.553  -7.115   4.062  1.00 51.79           C  
ANISOU 3829  CZ3 TRP C  51     6323   6133   7222   -506   1169    601       C  
ATOM   3830  CH2 TRP C  51      58.317  -6.857   3.450  1.00 52.35           C  
ANISOU 3830  CH2 TRP C  51     6101   6270   7520   -500   1087    641       C  
ATOM   3831  N   ASN C  52      63.309 -13.283   2.857  1.00 36.27           N  
ANISOU 3831  N   ASN C  52     5347   3704   4731  -1044    722    534       N  
ATOM   3832  CA  ASN C  52      64.722 -13.551   3.092  1.00 33.47           C  
ANISOU 3832  CA  ASN C  52     5208   3267   4241   -954    721    485       C  
ATOM   3833  C   ASN C  52      65.410 -12.178   3.321  1.00 33.27           C  
ANISOU 3833  C   ASN C  52     5157   3307   4178   -791    777    445       C  
ATOM   3834  O   ASN C  52      64.730 -11.152   3.337  1.00 31.52           O  
ANISOU 3834  O   ASN C  52     4785   3173   4020   -750    822    458       O  
ATOM   3835  CB  ASN C  52      65.355 -14.351   1.924  1.00 29.24           C  
ANISOU 3835  CB  ASN C  52     4821   2630   3660   -976    579    433       C  
ATOM   3836  CG  ASN C  52      65.446 -13.647   0.589  1.00 45.47           C  
ANISOU 3836  CG  ASN C  52     6850   4709   5716   -933    480    383       C  
ATOM   3837  OD1 ASN C  52      65.586 -12.427   0.494  1.00 46.08           O  
ANISOU 3837  OD1 ASN C  52     6842   4864   5802   -834    509    369       O  
ATOM   3838  ND2 ASN C  52      65.412 -14.410  -0.490  1.00 30.93           N  
ANISOU 3838  ND2 ASN C  52     5128   2779   3844  -1007    359    354       N  
ATOM   3839  N   SER C  53      66.737 -12.159   3.462  1.00 28.33           N  
ANISOU 3839  N   SER C  53     4669   2629   3465   -699    766    396       N  
ATOM   3840  CA  SER C  53      67.530 -10.958   3.702  1.00 27.05           C  
ANISOU 3840  CA  SER C  53     4502   2509   3267   -573    803    354       C  
ATOM   3841  C   SER C  53      67.416  -9.892   2.599  1.00 32.89           C  
ANISOU 3841  C   SER C  53     5163   3298   4036   -527    765    320       C  
ATOM   3842  O   SER C  53      67.214  -8.709   2.909  1.00 33.24           O  
ANISOU 3842  O   SER C  53     5143   3399   4087   -461    821    320       O  
ATOM   3843  CB  SER C  53      68.977 -11.343   3.949  1.00 28.01           C  
ANISOU 3843  CB  SER C  53     4753   2560   3331   -508    767    310       C  
ATOM   3844  OG  SER C  53      69.051 -12.265   5.022  1.00 25.34           O  
ANISOU 3844  OG  SER C  53     4518   2158   2951   -539    775    351       O  
ATOM   3845  N   SER C  54      67.492 -10.315   1.320  1.00 28.70           N  
ANISOU 3845  N   SER C  54     4672   2727   3507   -564    670    293       N  
ATOM   3846  CA  SER C  54      67.347  -9.433   0.168  1.00 28.06           C  
ANISOU 3846  CA  SER C  54     4573   2666   3423   -537    614    269       C  
ATOM   3847  C   SER C  54      65.969  -8.752   0.178  1.00 33.01           C  
ANISOU 3847  C   SER C  54     5042   3367   4135   -546    593    323       C  
ATOM   3848  O   SER C  54      65.895  -7.546  -0.044  1.00 34.21           O  
ANISOU 3848  O   SER C  54     5159   3551   4288   -466    599    317       O  
ATOM   3849  CB  SER C  54      67.573 -10.208  -1.126  1.00 29.95           C  
ANISOU 3849  CB  SER C  54     4937   2826   3619   -593    520    233       C  
ATOM   3850  OG  SER C  54      68.953 -10.487  -1.284  1.00 30.54           O  
ANISOU 3850  OG  SER C  54     5129   2838   3636   -540    573    169       O  
ATOM   3851  N   ASN C  55      64.898  -9.504   0.504  1.00 28.95           N  
ANISOU 3851  N   ASN C  55     4422   2873   3705   -639    578    378       N  
ATOM   3852  CA  ASN C  55      63.534  -8.987   0.652  1.00 28.73           C  
ANISOU 3852  CA  ASN C  55     4183   2924   3808   -646    577    434       C  
ATOM   3853  C   ASN C  55      63.452  -7.863   1.701  1.00 32.99           C  
ANISOU 3853  C   ASN C  55     4646   3524   4366   -527    736    441       C  
ATOM   3854  O   ASN C  55      62.836  -6.832   1.435  1.00 32.13           O  
ANISOU 3854  O   ASN C  55     4422   3458   4328   -444    722    453       O  
ATOM   3855  CB  ASN C  55      62.541 -10.118   1.016  1.00 27.10           C  
ANISOU 3855  CB  ASN C  55     3865   2726   3705   -795    575    491       C  
ATOM   3856  CG  ASN C  55      62.447 -11.222  -0.008  1.00 44.54           C  
ANISOU 3856  CG  ASN C  55     6161   4861   5902   -930    401    485       C  
ATOM   3857  OD1 ASN C  55      62.362 -12.408   0.337  1.00 41.74           O  
ANISOU 3857  OD1 ASN C  55     5856   4455   5549  -1056    411    505       O  
ATOM   3858  ND2 ASN C  55      62.481 -10.869  -1.287  1.00 30.95           N  
ANISOU 3858  ND2 ASN C  55     4501   3111   4146   -913    236    456       N  
ATOM   3859  N   VAL C  56      64.070  -8.075   2.888  1.00 29.84           N  
ANISOU 3859  N   VAL C  56     4337   3109   3891   -513    875    433       N  
ATOM   3860  CA  VAL C  56      64.088  -7.103   3.982  1.00 29.50           C  
ANISOU 3860  CA  VAL C  56     4290   3097   3823   -413   1030    431       C  
ATOM   3861  C   VAL C  56      64.739  -5.773   3.509  1.00 33.27           C  
ANISOU 3861  C   VAL C  56     4828   3565   4249   -293    995    382       C  
ATOM   3862  O   VAL C  56      64.117  -4.714   3.626  1.00 33.75           O  
ANISOU 3862  O   VAL C  56     4806   3656   4360   -201   1048    389       O  
ATOM   3863  CB  VAL C  56      64.711  -7.694   5.299  1.00 32.49           C  
ANISOU 3863  CB  VAL C  56     4814   3435   4095   -440   1141    434       C  
ATOM   3864  CG1 VAL C  56      64.882  -6.619   6.376  1.00 31.97           C  
ANISOU 3864  CG1 VAL C  56     4813   3376   3960   -339   1281    417       C  
ATOM   3865  CG2 VAL C  56      63.870  -8.848   5.834  1.00 31.57           C  
ANISOU 3865  CG2 VAL C  56     4650   3317   4028   -567   1210    495       C  
ATOM   3866  N   TYR C  57      65.925  -5.857   2.885  1.00 28.34           N  
ANISOU 3866  N   TYR C  57     4338   2890   3539   -298    910    334       N  
ATOM   3867  CA  TYR C  57      66.650  -4.695   2.366  1.00 27.20           C  
ANISOU 3867  CA  TYR C  57     4269   2724   3341   -222    887    289       C  
ATOM   3868  C   TYR C  57      65.918  -3.970   1.244  1.00 34.21           C  
ANISOU 3868  C   TYR C  57     5101   3619   4278   -185    801    305       C  
ATOM   3869  O   TYR C  57      65.874  -2.739   1.251  1.00 36.68           O  
ANISOU 3869  O   TYR C  57     5435   3923   4580    -95    826    296       O  
ATOM   3870  CB  TYR C  57      68.054  -5.083   1.907  1.00 26.78           C  
ANISOU 3870  CB  TYR C  57     4340   2620   3216   -252    844    237       C  
ATOM   3871  CG  TYR C  57      68.904  -5.779   2.951  1.00 27.07           C  
ANISOU 3871  CG  TYR C  57     4434   2635   3215   -268    880    223       C  
ATOM   3872  CD1 TYR C  57      69.038  -5.254   4.227  1.00 28.11           C  
ANISOU 3872  CD1 TYR C  57     4601   2772   3307   -231    951    227       C  
ATOM   3873  CD2 TYR C  57      69.664  -6.900   2.626  1.00 27.79           C  
ANISOU 3873  CD2 TYR C  57     4576   2683   3301   -309    830    202       C  
ATOM   3874  CE1 TYR C  57      69.853  -5.859   5.173  1.00 28.11           C  
ANISOU 3874  CE1 TYR C  57     4685   2738   3258   -243    942    219       C  
ATOM   3875  CE2 TYR C  57      70.510  -7.495   3.558  1.00 28.14           C  
ANISOU 3875  CE2 TYR C  57     4677   2694   3320   -301    829    193       C  
ATOM   3876  CZ  TYR C  57      70.612  -6.959   4.829  1.00 31.00           C  
ANISOU 3876  CZ  TYR C  57     5075   3064   3638   -273    869    205       C  
ATOM   3877  OH  TYR C  57      71.406  -7.544   5.784  1.00 27.75           O  
ANISOU 3877  OH  TYR C  57     4746   2608   3191   -267    828    206       O  
ATOM   3878  N   LEU C  58      65.359  -4.718   0.275  1.00 31.01           N  
ANISOU 3878  N   LEU C  58     4653   3212   3918   -254    679    328       N  
ATOM   3879  CA  LEU C  58      64.609  -4.152  -0.854  1.00 30.02           C  
ANISOU 3879  CA  LEU C  58     4495   3080   3833   -228    542    352       C  
ATOM   3880  C   LEU C  58      63.388  -3.382  -0.362  1.00 35.47           C  
ANISOU 3880  C   LEU C  58     4995   3826   4657   -137    568    399       C  
ATOM   3881  O   LEU C  58      63.193  -2.244  -0.780  1.00 34.57           O  
ANISOU 3881  O   LEU C  58     4901   3689   4546    -33    525    403       O  
ATOM   3882  CB  LEU C  58      64.191  -5.242  -1.857  1.00 29.16           C  
ANISOU 3882  CB  LEU C  58     4394   2948   3738   -342    382    367       C  
ATOM   3883  CG  LEU C  58      65.300  -5.778  -2.769  1.00 32.39           C  
ANISOU 3883  CG  LEU C  58     5025   3276   4006   -401    345    313       C  
ATOM   3884  CD1 LEU C  58      64.930  -7.139  -3.320  1.00 32.04           C  
ANISOU 3884  CD1 LEU C  58     5008   3197   3967   -527    235    319       C  
ATOM   3885  CD2 LEU C  58      65.716  -4.754  -3.863  1.00 30.40           C  
ANISOU 3885  CD2 LEU C  58     4934   2966   3652   -354    287    292       C  
ATOM   3886  N   PHE C  59      62.607  -3.971   0.584  1.00 32.50           N  
ANISOU 3886  N   PHE C  59     4445   3511   4392   -168    664    433       N  
ATOM   3887  CA  PHE C  59      61.447  -3.302   1.173  1.00 31.42           C  
ANISOU 3887  CA  PHE C  59     4099   3432   4409    -71    747    472       C  
ATOM   3888  C   PHE C  59      61.831  -1.973   1.859  1.00 36.39           C  
ANISOU 3888  C   PHE C  59     4817   4034   4974     81    888    439       C  
ATOM   3889  O   PHE C  59      61.135  -0.967   1.676  1.00 36.20           O  
ANISOU 3889  O   PHE C  59     4703   4010   5040    215    875    456       O  
ATOM   3890  CB  PHE C  59      60.731  -4.226   2.143  1.00 32.36           C  
ANISOU 3890  CB  PHE C  59     4054   3610   4632   -156    883    508       C  
ATOM   3891  CG  PHE C  59      59.391  -3.695   2.570  1.00 33.66           C  
ANISOU 3891  CG  PHE C  59     3947   3842   5002    -69    979    550       C  
ATOM   3892  CD1 PHE C  59      58.306  -3.714   1.697  1.00 36.48           C  
ANISOU 3892  CD1 PHE C  59     4066   4239   5557    -72    805    597       C  
ATOM   3893  CD2 PHE C  59      59.196  -3.209   3.863  1.00 35.26           C  
ANISOU 3893  CD2 PHE C  59     4129   4062   5207     15   1245    542       C  
ATOM   3894  CE1 PHE C  59      57.044  -3.259   2.113  1.00 37.61           C  
ANISOU 3894  CE1 PHE C  59     3901   4451   5938     20    903    636       C  
ATOM   3895  CE2 PHE C  59      57.938  -2.737   4.272  1.00 37.83           C  
ANISOU 3895  CE2 PHE C  59     4184   4448   5743    110   1378    575       C  
ATOM   3896  CZ  PHE C  59      56.874  -2.760   3.393  1.00 36.34           C  
ANISOU 3896  CZ  PHE C  59     3709   4310   5788    119   1210    623       C  
ATOM   3897  N   ASN C  60      62.956  -1.980   2.616  1.00 32.45           N  
ANISOU 3897  N   ASN C  60     4506   3501   4322     62    998    393       N  
ATOM   3898  CA  ASN C  60      63.530  -0.836   3.318  1.00 31.77           C  
ANISOU 3898  CA  ASN C  60     4560   3369   4141    166   1111    352       C  
ATOM   3899  C   ASN C  60      63.897   0.258   2.310  1.00 37.08           C  
ANISOU 3899  C   ASN C  60     5338   3979   4771    237    997    334       C  
ATOM   3900  O   ASN C  60      63.632   1.452   2.543  1.00 36.85           O  
ANISOU 3900  O   ASN C  60     5346   3910   4745    366   1051    325       O  
ATOM   3901  CB  ASN C  60      64.753  -1.280   4.092  1.00 29.05           C  
ANISOU 3901  CB  ASN C  60     4388   2995   3653     93   1169    312       C  
ATOM   3902  CG  ASN C  60      64.464  -1.567   5.535  1.00 41.51           C  
ANISOU 3902  CG  ASN C  60     5976   4587   5207     93   1344    319       C  
ATOM   3903  OD1 ASN C  60      64.538  -0.680   6.390  1.00 39.09           O  
ANISOU 3903  OD1 ASN C  60     5771   4246   4835    175   1463    293       O  
ATOM   3904  ND2 ASN C  60      64.118  -2.809   5.846  1.00 28.00           N  
ANISOU 3904  ND2 ASN C  60     4197   2912   3531     -8   1369    356       N  
ATOM   3905  N   LEU C  61      64.441  -0.176   1.153  1.00 32.29           N  
ANISOU 3905  N   LEU C  61     4801   3350   4116    153    846    330       N  
ATOM   3906  CA  LEU C  61      64.818   0.671   0.027  1.00 30.86           C  
ANISOU 3906  CA  LEU C  61     4758   3098   3870    183    736    321       C  
ATOM   3907  C   LEU C  61      63.586   1.447  -0.486  1.00 36.35           C  
ANISOU 3907  C   LEU C  61     5353   3784   4674    307    641    370       C  
ATOM   3908  O   LEU C  61      63.678   2.653  -0.682  1.00 37.08           O  
ANISOU 3908  O   LEU C  61     5562   3802   4725    408    633    365       O  
ATOM   3909  CB  LEU C  61      65.464  -0.218  -1.061  1.00 29.75           C  
ANISOU 3909  CB  LEU C  61     4705   2938   3660     58    625    309       C  
ATOM   3910  CG  LEU C  61      66.095   0.432  -2.273  1.00 32.90           C  
ANISOU 3910  CG  LEU C  61     5303   3250   3946     46    545    295       C  
ATOM   3911  CD1 LEU C  61      67.217   1.385  -1.888  1.00 32.02           C  
ANISOU 3911  CD1 LEU C  61     5339   3085   3742     55    661    248       C  
ATOM   3912  CD2 LEU C  61      66.588  -0.629  -3.258  1.00 32.86           C  
ANISOU 3912  CD2 LEU C  61     5385   3226   3876    -74    473    279       C  
ATOM   3913  N   SER C  62      62.421   0.787  -0.586  1.00 33.57           N  
ANISOU 3913  N   SER C  62     4774   3501   4480    306    574    419       N  
ATOM   3914  CA  SER C  62      61.163   1.413  -0.998  1.00 33.71           C  
ANISOU 3914  CA  SER C  62     4629   3523   4656    434    462    472       C  
ATOM   3915  C   SER C  62      60.664   2.404   0.058  1.00 40.30           C  
ANISOU 3915  C   SER C  62     5382   4358   5574    609    643    466       C  
ATOM   3916  O   SER C  62      60.190   3.467  -0.320  1.00 39.67           O  
ANISOU 3916  O   SER C  62     5312   4217   5542    764    572    484       O  
ATOM   3917  CB  SER C  62      60.100   0.357  -1.263  1.00 36.30           C  
ANISOU 3917  CB  SER C  62     4700   3933   5159    358    347    522       C  
ATOM   3918  OG  SER C  62      60.387  -0.360  -2.447  1.00 43.83           O  
ANISOU 3918  OG  SER C  62     5771   4853   6030    226    135    529       O  
ATOM   3919  N   ILE C  63      60.779   2.069   1.376  1.00 39.10           N  
ANISOU 3919  N   ILE C  63     5183   4253   5419    590    876    439       N  
ATOM   3920  CA  ILE C  63      60.365   2.973   2.467  1.00 39.44           C  
ANISOU 3920  CA  ILE C  63     5204   4278   5503    750   1089    419       C  
ATOM   3921  C   ILE C  63      61.155   4.290   2.408  1.00 43.25           C  
ANISOU 3921  C   ILE C  63     5964   4636   5831    844   1093    375       C  
ATOM   3922  O   ILE C  63      60.560   5.364   2.463  1.00 44.89           O  
ANISOU 3922  O   ILE C  63     6167   4785   6106   1027   1122    379       O  
ATOM   3923  CB  ILE C  63      60.396   2.299   3.864  1.00 42.34           C  
ANISOU 3923  CB  ILE C  63     5544   4699   5845    685   1334    399       C  
ATOM   3924  CG1 ILE C  63      59.295   1.224   3.965  1.00 42.07           C  
ANISOU 3924  CG1 ILE C  63     5201   4774   6011    617   1367    453       C  
ATOM   3925  CG2 ILE C  63      60.253   3.357   5.004  1.00 42.93           C  
ANISOU 3925  CG2 ILE C  63     5720   4714   5875    842   1570    357       C  
ATOM   3926  CD1 ILE C  63      59.459   0.294   5.170  1.00 48.36           C  
ANISOU 3926  CD1 ILE C  63     6026   5608   6740    493   1574    446       C  
ATOM   3927  N   SER C  64      62.476   4.192   2.235  1.00 38.39           N  
ANISOU 3927  N   SER C  64     5582   3977   5028    717   1057    336       N  
ATOM   3928  CA  SER C  64      63.397   5.313   2.074  1.00 37.78           C  
ANISOU 3928  CA  SER C  64     5775   3780   4800    743   1047    296       C  
ATOM   3929  C   SER C  64      62.981   6.163   0.833  1.00 42.27           C  
ANISOU 3929  C   SER C  64     6395   4269   5398    840    872    335       C  
ATOM   3930  O   SER C  64      62.804   7.399   0.942  1.00 41.98           O  
ANISOU 3930  O   SER C  64     6483   4126   5343    984    900    326       O  
ATOM   3931  CB  SER C  64      64.810   4.770   1.898  1.00 40.51           C  
ANISOU 3931  CB  SER C  64     6270   4121   4999    560   1016    259       C  
ATOM   3932  OG  SER C  64      65.740   5.824   1.765  1.00 50.14           O  
ANISOU 3932  OG  SER C  64     7728   5231   6092    551   1018    221       O  
ATOM   3933  N   ASP C  65      62.770   5.471  -0.325  1.00 37.26           N  
ANISOU 3933  N   ASP C  65     5690   3669   4799    765    684    379       N  
ATOM   3934  CA  ASP C  65      62.345   6.087  -1.573  1.00 36.92           C  
ANISOU 3934  CA  ASP C  65     5720   3545   4762    837    478    426       C  
ATOM   3935  C   ASP C  65      61.042   6.833  -1.410  1.00 44.62           C  
ANISOU 3935  C   ASP C  65     6533   4502   5918   1062    443    468       C  
ATOM   3936  O   ASP C  65      60.947   7.977  -1.864  1.00 44.58           O  
ANISOU 3936  O   ASP C  65     6693   4369   5876   1191    367    483       O  
ATOM   3937  CB  ASP C  65      62.155   5.051  -2.671  1.00 37.41           C  
ANISOU 3937  CB  ASP C  65     5724   3653   4836    715    281    464       C  
ATOM   3938  CG  ASP C  65      63.394   4.353  -3.168  1.00 42.30           C  
ANISOU 3938  CG  ASP C  65     6528   4261   5281    521    291    426       C  
ATOM   3939  OD1 ASP C  65      64.519   4.809  -2.834  1.00 42.00           O  
ANISOU 3939  OD1 ASP C  65     6670   4174   5115    473    424    375       O  
ATOM   3940  OD2 ASP C  65      63.248   3.341  -3.863  1.00 44.11           O  
ANISOU 3940  OD2 ASP C  65     6717   4530   5515    416    170    442       O  
ATOM   3941  N   LEU C  66      60.030   6.185  -0.778  1.00 42.35           N  
ANISOU 3941  N   LEU C  66     5919   4334   5838   1108    505    488       N  
ATOM   3942  CA  LEU C  66      58.708   6.777  -0.599  1.00 42.66           C  
ANISOU 3942  CA  LEU C  66     5722   4377   6108   1331    492    528       C  
ATOM   3943  C   LEU C  66      58.744   8.017   0.297  1.00 48.00           C  
ANISOU 3943  C   LEU C  66     6521   4956   6759   1523    697    485       C  
ATOM   3944  O   LEU C  66      58.176   9.042  -0.080  1.00 47.12           O  
ANISOU 3944  O   LEU C  66     6431   4745   6726   1728    607    511       O  
ATOM   3945  CB  LEU C  66      57.683   5.747  -0.132  1.00 42.57           C  
ANISOU 3945  CB  LEU C  66     5318   4521   6337   1302    546    557       C  
ATOM   3946  CG  LEU C  66      57.262   4.717  -1.197  1.00 47.59           C  
ANISOU 3946  CG  LEU C  66     5804   5222   7057   1162    268    614       C  
ATOM   3947  CD1 LEU C  66      56.704   3.460  -0.547  1.00 47.42           C  
ANISOU 3947  CD1 LEU C  66     5484   5346   7188   1027    380    624       C  
ATOM   3948  CD2 LEU C  66      56.282   5.310  -2.214  1.00 48.78           C  
ANISOU 3948  CD2 LEU C  66     5834   5326   7376   1319    -23    682       C  
ATOM   3949  N   ALA C  67      59.488   7.948   1.429  1.00 45.41           N  
ANISOU 3949  N   ALA C  67     6321   4634   6298   1452    947    417       N  
ATOM   3950  CA  ALA C  67      59.686   9.063   2.356  1.00 44.84           C  
ANISOU 3950  CA  ALA C  67     6439   4450   6148   1595   1148    361       C  
ATOM   3951  C   ALA C  67      60.219  10.289   1.574  1.00 49.45           C  
ANISOU 3951  C   ALA C  67     7336   4856   6598   1661   1005    360       C  
ATOM   3952  O   ALA C  67      59.688  11.384   1.742  1.00 49.76           O  
ANISOU 3952  O   ALA C  67     7438   4778   6691   1882   1044    357       O  
ATOM   3953  CB  ALA C  67      60.653   8.655   3.464  1.00 45.06           C  
ANISOU 3953  CB  ALA C  67     6622   4499   6001   1443   1348    294       C  
ATOM   3954  N   PHE C  68      61.179  10.074   0.635  1.00 46.29           N  
ANISOU 3954  N   PHE C  68     7124   4426   6038   1476    841    370       N  
ATOM   3955  CA  PHE C  68      61.723  11.142  -0.213  1.00 45.07           C  
ANISOU 3955  CA  PHE C  68     7284   4098   5741   1494    711    380       C  
ATOM   3956  C   PHE C  68      60.729  11.632  -1.291  1.00 49.01           C  
ANISOU 3956  C   PHE C  68     7734   4530   6359   1668    477    459       C  
ATOM   3957  O   PHE C  68      60.515  12.845  -1.392  1.00 48.21           O  
ANISOU 3957  O   PHE C  68     7814   4265   6240   1844    450    467       O  
ATOM   3958  CB  PHE C  68      63.090  10.767  -0.840  1.00 45.78           C  
ANISOU 3958  CB  PHE C  68     7588   4175   5630   1237    659    361       C  
ATOM   3959  CG  PHE C  68      63.587  11.801  -1.833  1.00 46.30           C  
ANISOU 3959  CG  PHE C  68     7980   4061   5551   1230    538    384       C  
ATOM   3960  CD1 PHE C  68      63.761  13.133  -1.451  1.00 49.04           C  
ANISOU 3960  CD1 PHE C  68     8575   4236   5824   1334    607    359       C  
ATOM   3961  CD2 PHE C  68      63.807  11.460  -3.163  1.00 47.39           C  
ANISOU 3961  CD2 PHE C  68     8208   4181   5616   1123    358    433       C  
ATOM   3962  CE1 PHE C  68      64.164  14.097  -2.377  1.00 50.13           C  
ANISOU 3962  CE1 PHE C  68     9036   4188   5824   1320    498    390       C  
ATOM   3963  CE2 PHE C  68      64.210  12.421  -4.094  1.00 50.59           C  
ANISOU 3963  CE2 PHE C  68     8948   4404   5870   1111    260    463       C  
ATOM   3964  CZ  PHE C  68      64.390  13.734  -3.697  1.00 49.36           C  
ANISOU 3964  CZ  PHE C  68     9026   4079   5649   1205    331    445       C  
ATOM   3965  N   LEU C  69      60.153  10.706  -2.102  1.00 44.56           N  
ANISOU 3965  N   LEU C  69     6953   4073   5905   1616    286    518       N  
ATOM   3966  CA  LEU C  69      59.211  11.028  -3.188  1.00 44.24           C  
ANISOU 3966  CA  LEU C  69     6856   3974   5978   1758      1    601       C  
ATOM   3967  C   LEU C  69      58.008  11.890  -2.760  1.00 53.48           C  
ANISOU 3967  C   LEU C  69     7839   5098   7382   2073     11    624       C  
ATOM   3968  O   LEU C  69      57.502  12.671  -3.563  1.00 52.66           O  
ANISOU 3968  O   LEU C  69     7824   4864   7319   2241   -212    684       O  
ATOM   3969  CB  LEU C  69      58.721   9.755  -3.902  1.00 43.14           C  
ANISOU 3969  CB  LEU C  69     6480   3973   5939   1629   -195    648       C  
ATOM   3970  CG  LEU C  69      59.744   8.968  -4.710  1.00 46.14           C  
ANISOU 3970  CG  LEU C  69     7077   4361   6095   1361   -269    637       C  
ATOM   3971  CD1 LEU C  69      59.356   7.505  -4.789  1.00 45.94           C  
ANISOU 3971  CD1 LEU C  69     6778   4499   6178   1215   -326    647       C  
ATOM   3972  CD2 LEU C  69      59.925   9.542  -6.095  1.00 46.61           C  
ANISOU 3972  CD2 LEU C  69     7453   4261   5995   1356   -527    690       C  
ATOM   3973  N   CYS C  70      57.552  11.743  -1.503  1.00 54.93           N  
ANISOU 3973  N   CYS C  70     7779   5375   7715   2160    278    578       N  
ATOM   3974  CA  CYS C  70      56.429  12.501  -0.932  1.00 56.66           C  
ANISOU 3974  CA  CYS C  70     7794   5559   8175   2470    371    583       C  
ATOM   3975  C   CYS C  70      56.708  13.994  -0.813  1.00 60.37           C  
ANISOU 3975  C   CYS C  70     8612   5801   8527   2664    416    558       C  
ATOM   3976  O   CYS C  70      55.765  14.794  -0.840  1.00 60.94           O  
ANISOU 3976  O   CYS C  70     8576   5785   8791   2960    373    585       O  
ATOM   3977  CB  CYS C  70      56.005  11.908   0.408  1.00 57.73           C  
ANISOU 3977  CB  CYS C  70     7643   5841   8450   2477    699    532       C  
ATOM   3978  SG  CYS C  70      55.262  10.265   0.277  1.00 62.07           S  
ANISOU 3978  SG  CYS C  70     7701   6637   9244   2323    632    583       S  
ATOM   3979  N   THR C  71      57.995  14.368  -0.662  1.00 55.99           N  
ANISOU 3979  N   THR C  71     8461   5140   7673   2499    503    504       N  
ATOM   3980  CA  THR C  71      58.423  15.770  -0.558  1.00 55.56           C  
ANISOU 3980  CA  THR C  71     8797   4847   7468   2627    545    476       C  
ATOM   3981  C   THR C  71      58.503  16.453  -1.918  1.00 60.93           C  
ANISOU 3981  C   THR C  71     9737   5355   8057   2661    239    552       C  
ATOM   3982  O   THR C  71      58.412  17.678  -1.966  1.00 62.61           O  
ANISOU 3982  O   THR C  71    10217   5351   8223   2847    221    554       O  
ATOM   3983  CB  THR C  71      59.758  15.900   0.187  1.00 55.13           C  
ANISOU 3983  CB  THR C  71     9049   4745   7151   2414    751    388       C  
ATOM   3984  OG1 THR C  71      60.832  15.462  -0.650  1.00 48.65           O  
ANISOU 3984  OG1 THR C  71     8408   3937   6138   2128    620    405       O  
ATOM   3985  CG2 THR C  71      59.756  15.183   1.527  1.00 51.58           C  
ANISOU 3985  CG2 THR C  71     8410   4446   6744   2361   1030    318       C  
ATOM   3986  N   LEU C  72      58.701  15.679  -3.014  1.00 56.94           N  
ANISOU 3986  N   LEU C  72     9206   4925   7503   2478      4    613       N  
ATOM   3987  CA  LEU C  72      58.831  16.213  -4.373  1.00 56.47           C  
ANISOU 3987  CA  LEU C  72     9445   4699   7311   2472   -290    690       C  
ATOM   3988  C   LEU C  72      57.695  17.181  -4.751  1.00 62.59           C  
ANISOU 3988  C   LEU C  72    10207   5319   8256   2819   -492    759       C  
ATOM   3989  O   LEU C  72      58.044  18.280  -5.191  1.00 62.97           O  
ANISOU 3989  O   LEU C  72    10663   5127   8135   2883   -568    782       O  
ATOM   3990  CB  LEU C  72      59.041  15.130  -5.446  1.00 56.06           C  
ANISOU 3990  CB  LEU C  72     9350   4757   7193   2244   -501    740       C  
ATOM   3991  CG  LEU C  72      60.390  14.376  -5.396  1.00 60.09           C  
ANISOU 3991  CG  LEU C  72    10004   5346   7480   1906   -342    681       C  
ATOM   3992  CD1 LEU C  72      60.477  13.330  -6.496  1.00 59.51           C  
ANISOU 3992  CD1 LEU C  72     9910   5353   7346   1721   -546    726       C  
ATOM   3993  CD2 LEU C  72      61.585  15.333  -5.485  1.00 62.06           C  
ANISOU 3993  CD2 LEU C  72    10708   5405   7465   1795   -233    650       C  
ATOM   3994  N   PRO C  73      56.374  16.906  -4.515  1.00 59.23           N  
ANISOU 3994  N   PRO C  73     9337   5001   8167   3057   -560    791       N  
ATOM   3995  CA  PRO C  73      55.353  17.923  -4.853  1.00 58.90           C  
ANISOU 3995  CA  PRO C  73     9285   4791   8305   3419   -758    855       C  
ATOM   3996  C   PRO C  73      55.609  19.309  -4.232  1.00 64.75           C  
ANISOU 3996  C   PRO C  73    10362   5292   8949   3617   -572    806       C  
ATOM   3997  O   PRO C  73      55.387  20.308  -4.925  1.00 64.65           O  
ANISOU 3997  O   PRO C  73    10631   5043   8890   3801   -792    868       O  
ATOM   3998  CB  PRO C  73      54.047  17.288  -4.372  1.00 60.27           C  
ANISOU 3998  CB  PRO C  73     8851   5162   8888   3604   -746    868       C  
ATOM   3999  CG  PRO C  73      54.298  15.826  -4.459  1.00 64.46           C  
ANISOU 3999  CG  PRO C  73     9144   5937   9411   3291   -738    861       C  
ATOM   4000  CD  PRO C  73      55.732  15.664  -4.031  1.00 60.12           C  
ANISOU 4000  CD  PRO C  73     8935   5382   8527   3007   -484    780       C  
ATOM   4001  N   MET C  74      56.131  19.374  -2.968  1.00 62.21           N  
ANISOU 4001  N   MET C  74    10068   5006   8563   3562   -188    696       N  
ATOM   4002  CA  MET C  74      56.493  20.632  -2.278  1.00 62.47           C  
ANISOU 4002  CA  MET C  74    10467   4804   8466   3702     12    631       C  
ATOM   4003  C   MET C  74      57.655  21.305  -3.007  1.00 67.55           C  
ANISOU 4003  C   MET C  74    11672   5233   8761   3496    -98    648       C  
ATOM   4004  O   MET C  74      57.596  22.506  -3.240  1.00 67.51           O  
ANISOU 4004  O   MET C  74    12013   4957   8682   3676   -168    668       O  
ATOM   4005  CB  MET C  74      56.910  20.395  -0.813  1.00 64.79           C  
ANISOU 4005  CB  MET C  74    10705   5192   8720   3621    414    510       C  
ATOM   4006  CG  MET C  74      55.771  20.291   0.156  1.00 68.30           C  
ANISOU 4006  CG  MET C  74    10750   5732   9468   3905    630    473       C  
ATOM   4007  SD  MET C  74      56.374  20.049   1.851  1.00 72.44           S  
ANISOU 4007  SD  MET C  74    11335   6328   9860   3776   1093    332       S  
ATOM   4008  CE  MET C  74      56.713  18.289   1.839  1.00 68.84           C  
ANISOU 4008  CE  MET C  74    10525   6207   9425   3425   1090    349       C  
ATOM   4009  N   LEU C  75      58.706  20.526  -3.365  1.00 65.45           N  
ANISOU 4009  N   LEU C  75    11494   5080   8292   3121   -100    641       N  
ATOM   4010  CA  LEU C  75      59.896  20.987  -4.092  1.00 66.10           C  
ANISOU 4010  CA  LEU C  75    12060   4997   8058   2870   -166    656       C  
ATOM   4011  C   LEU C  75      59.492  21.550  -5.456  1.00 70.69           C  
ANISOU 4011  C   LEU C  75    12877   5390   8593   2983   -506    774       C  
ATOM   4012  O   LEU C  75      59.974  22.614  -5.845  1.00 70.45           O  
ANISOU 4012  O   LEU C  75    13311   5089   8366   2986   -548    795       O  
ATOM   4013  CB  LEU C  75      60.883  19.825  -4.284  1.00 66.65           C  
ANISOU 4013  CB  LEU C  75    12058   5266   7998   2490   -107    632       C  
ATOM   4014  CG  LEU C  75      62.015  19.670  -3.278  1.00 72.41           C  
ANISOU 4014  CG  LEU C  75    12862   6054   8598   2253    179    526       C  
ATOM   4015  CD1 LEU C  75      61.512  19.084  -1.948  1.00 73.35           C  
ANISOU 4015  CD1 LEU C  75    12612   6359   8900   2350    391    453       C  
ATOM   4016  CD2 LEU C  75      63.088  18.735  -3.833  1.00 74.31           C  
ANISOU 4016  CD2 LEU C  75    13121   6421   8692   1898    177    523       C  
ATOM   4017  N   ILE C  76      58.577  20.852  -6.160  1.00 67.69           N  
ANISOU 4017  N   ILE C  76    12192   5136   8391   3077   -762    852       N  
ATOM   4018  CA  ILE C  76      58.048  21.263  -7.461  1.00 67.84           C  
ANISOU 4018  CA  ILE C  76    12402   4990   8383   3201  -1143    973       C  
ATOM   4019  C   ILE C  76      57.317  22.606  -7.329  1.00 73.25           C  
ANISOU 4019  C   ILE C  76    13246   5416   9169   3583  -1229   1006       C  
ATOM   4020  O   ILE C  76      57.649  23.523  -8.074  1.00 72.81           O  
ANISOU 4020  O   ILE C  76    13680   5084   8900   3596  -1381   1066       O  
ATOM   4021  CB  ILE C  76      57.191  20.141  -8.125  1.00 70.57           C  
ANISOU 4021  CB  ILE C  76    12345   5543   8927   3211  -1416   1040       C  
ATOM   4022  CG1 ILE C  76      58.085  18.941  -8.551  1.00 70.96           C  
ANISOU 4022  CG1 ILE C  76    12394   5772   8795   2816  -1369   1017       C  
ATOM   4023  CG2 ILE C  76      56.369  20.666  -9.313  1.00 69.95           C  
ANISOU 4023  CG2 ILE C  76    12422   5279   8877   3419  -1861   1169       C  
ATOM   4024  CD1 ILE C  76      57.424  17.564  -8.459  1.00 75.28           C  
ANISOU 4024  CD1 ILE C  76    12417   6606   9581   2771  -1433   1016       C  
ATOM   4025  N   ARG C  77      56.366  22.730  -6.365  1.00 71.74           N  
ANISOU 4025  N   ARG C  77    12665   5298   9293   3890  -1102    963       N  
ATOM   4026  CA  ARG C  77      55.603  23.968  -6.122  1.00 73.09           C  
ANISOU 4026  CA  ARG C  77    12936   5228   9606   4300  -1143    979       C  
ATOM   4027  C   ARG C  77      56.515  25.141  -5.759  1.00 76.40           C  
ANISOU 4027  C   ARG C  77    13920   5362   9746   4263   -953    925       C  
ATOM   4028  O   ARG C  77      56.386  26.204  -6.361  1.00 75.99           O  
ANISOU 4028  O   ARG C  77    14251   5009   9614   4449  -1143    990       O  
ATOM   4029  CB  ARG C  77      54.503  23.776  -5.058  1.00 78.28           C  
ANISOU 4029  CB  ARG C  77    13042   6043  10658   4609   -961    925       C  
ATOM   4030  CG  ARG C  77      53.361  22.853  -5.501  1.00 99.74           C  
ANISOU 4030  CG  ARG C  77    15190   8987  13719   4716  -1212   1000       C  
ATOM   4031  CD  ARG C  77      52.291  22.663  -4.429  1.00114.20           C  
ANISOU 4031  CD  ARG C  77    16453  10978  15960   5001   -983    947       C  
ATOM   4032  NE  ARG C  77      52.667  21.680  -3.405  1.00115.46           N  
ANISOU 4032  NE  ARG C  77    16356  11396  16117   4763   -604    846       N  
ATOM   4033  CZ  ARG C  77      51.955  20.597  -3.099  1.00123.53           C  
ANISOU 4033  CZ  ARG C  77    16800  12692  17444   4765   -523    841       C  
ATOM   4034  NH1 ARG C  77      52.369  19.771  -2.147  1.00109.20           N  
ANISOU 4034  NH1 ARG C  77    14836  11074  15580   4541   -176    754       N  
ATOM   4035  NH2 ARG C  77      50.823  20.334  -3.742  1.00105.59           N  
ANISOU 4035  NH2 ARG C  77    14098  10490  15531   4981   -800    927       N  
ATOM   4036  N   SER C  78      57.474  24.916  -4.830  1.00 72.60           N  
ANISOU 4036  N   SER C  78    13513   4963   9108   4001   -610    812       N  
ATOM   4037  CA  SER C  78      58.462  25.896  -4.373  1.00 72.35           C  
ANISOU 4037  CA  SER C  78    13991   4688   8810   3890   -416    746       C  
ATOM   4038  C   SER C  78      59.337  26.435  -5.519  1.00 77.81           C  
ANISOU 4038  C   SER C  78    15225   5154   9186   3659   -602    822       C  
ATOM   4039  O   SER C  78      59.528  27.648  -5.610  1.00 78.40           O  
ANISOU 4039  O   SER C  78    15762   4906   9120   3758   -622    834       O  
ATOM   4040  CB  SER C  78      59.334  25.310  -3.264  1.00 74.65           C  
ANISOU 4040  CB  SER C  78    14190   5157   9016   3615    -75    620       C  
ATOM   4041  N   TYR C  79      59.844  25.549  -6.395  1.00 74.49           N  
ANISOU 4041  N   TYR C  79    14772   4885   8647   3354   -719    872       N  
ATOM   4042  CA  TYR C  79      60.696  25.947  -7.516  1.00 74.67           C  
ANISOU 4042  CA  TYR C  79    15300   4712   8358   3102   -848    942       C  
ATOM   4043  C   TYR C  79      59.925  26.627  -8.644  1.00 80.38           C  
ANISOU 4043  C   TYR C  79    16291   5190   9059   3342  -1214   1078       C  
ATOM   4044  O   TYR C  79      60.450  27.561  -9.264  1.00 80.35           O  
ANISOU 4044  O   TYR C  79    16844   4888   8799   3259  -1281   1131       O  
ATOM   4045  CB  TYR C  79      61.546  24.772  -8.036  1.00 75.40           C  
ANISOU 4045  CB  TYR C  79    15289   5036   8324   2705   -807    938       C  
ATOM   4046  CG  TYR C  79      62.775  24.509  -7.190  1.00 76.92           C  
ANISOU 4046  CG  TYR C  79    15483   5334   8410   2387   -474    823       C  
ATOM   4047  CD1 TYR C  79      62.970  23.278  -6.573  1.00 78.68           C  
ANISOU 4047  CD1 TYR C  79    15262   5878   8755   2252   -322    751       C  
ATOM   4048  CD2 TYR C  79      63.744  25.491  -7.007  1.00 77.78           C  
ANISOU 4048  CD2 TYR C  79    16043   5210   8301   2213   -332    791       C  
ATOM   4049  CE1 TYR C  79      64.100  23.028  -5.796  1.00 79.62           C  
ANISOU 4049  CE1 TYR C  79    15380   6086   8787   1973    -58    652       C  
ATOM   4050  CE2 TYR C  79      64.873  25.257  -6.225  1.00 78.82           C  
ANISOU 4050  CE2 TYR C  79    16153   5437   8359   1916    -67    688       C  
ATOM   4051  CZ  TYR C  79      65.048  24.024  -5.619  1.00 86.94           C  
ANISOU 4051  CZ  TYR C  79    16728   6789   9517   1807     59    619       C  
ATOM   4052  OH  TYR C  79      66.164  23.796  -4.846  1.00 89.43           O  
ANISOU 4052  OH  TYR C  79    17019   7190   9769   1528    281    524       O  
ATOM   4053  N   ALA C  80      58.682  26.182  -8.893  1.00 77.67           N  
ANISOU 4053  N   ALA C  80    15558   4961   8990   3632  -1460   1138       N  
ATOM   4054  CA  ALA C  80      57.817  26.750  -9.928  1.00 78.02           C  
ANISOU 4054  CA  ALA C  80    15792   4790   9061   3900  -1868   1273       C  
ATOM   4055  C   ALA C  80      57.299  28.156  -9.553  1.00 83.02           C  
ANISOU 4055  C   ALA C  80    16682   5100   9761   4278  -1893   1283       C  
ATOM   4056  O   ALA C  80      57.037  28.966 -10.445  1.00 83.20           O  
ANISOU 4056  O   ALA C  80    17111   4829   9672   4427  -2193   1395       O  
ATOM   4057  CB  ALA C  80      56.656  25.809 -10.210  1.00 78.82           C  
ANISOU 4057  CB  ALA C  80    15340   5130   9479   4082  -2130   1324       C  
ATOM   4058  N   THR C  81      57.178  28.449  -8.239  1.00 79.50           N  
ANISOU 4058  N   THR C  81    16041   4689   9475   4431  -1577   1166       N  
ATOM   4059  CA  THR C  81      56.692  29.739  -7.729  1.00 78.98           C  
ANISOU 4059  CA  THR C  81    16202   4321   9486   4808  -1541   1150       C  
ATOM   4060  C   THR C  81      57.811  30.657  -7.195  1.00 83.36           C  
ANISOU 4060  C   THR C  81    17301   4629   9741   4611  -1264   1070       C  
ATOM   4061  O   THR C  81      57.593  31.864  -7.032  1.00 83.20           O  
ANISOU 4061  O   THR C  81    17653   4272   9688   4868  -1280   1075       O  
ATOM   4062  CB  THR C  81      55.617  29.523  -6.653  1.00 83.75           C  
ANISOU 4062  CB  THR C  81    16228   5096  10496   5174  -1384   1075       C  
ATOM   4063  OG1 THR C  81      56.183  28.774  -5.573  1.00 80.68           O  
ANISOU 4063  OG1 THR C  81    15573   4974  10106   4929  -1000    944       O  
ATOM   4064  CG2 THR C  81      54.356  28.852  -7.195  1.00 81.06           C  
ANISOU 4064  CG2 THR C  81    15354   4939  10508   5430  -1696   1166       C  
ATOM   4065  N   GLY C  82      58.969  30.073  -6.893  1.00 80.00           N  
ANISOU 4065  N   GLY C  82    16901   4370   9126   4172  -1020    994       N  
ATOM   4066  CA  GLY C  82      60.117  30.786  -6.343  1.00 79.90           C  
ANISOU 4066  CA  GLY C  82    17334   4173   8854   3919   -763    910       C  
ATOM   4067  C   GLY C  82      59.897  31.234  -4.911  1.00 83.90           C  
ANISOU 4067  C   GLY C  82    17750   4643   9484   4125   -481    778       C  
ATOM   4068  O   GLY C  82      60.434  32.264  -4.496  1.00 83.77           O  
ANISOU 4068  O   GLY C  82    18200   4334   9295   4100   -361    727       O  
ATOM   4069  N   ASN C  83      59.080  30.470  -4.154  1.00 80.42           N  
ANISOU 4069  N   ASN C  83    16732   4486   9339   4326   -370    721       N  
ATOM   4070  CA  ASN C  83      58.733  30.754  -2.764  1.00 80.10           C  
ANISOU 4070  CA  ASN C  83    16557   4445   9431   4544    -73    592       C  
ATOM   4071  C   ASN C  83      58.394  29.486  -1.979  1.00 84.54           C  
ANISOU 4071  C   ASN C  83    16501   5409  10211   4511    113    526       C  
ATOM   4072  O   ASN C  83      57.685  28.607  -2.484  1.00 85.17           O  
ANISOU 4072  O   ASN C  83    16128   5726  10505   4581    -46    597       O  
ATOM   4073  CB  ASN C  83      57.561  31.742  -2.697  1.00 81.20           C  
ANISOU 4073  CB  ASN C  83    16756   4327   9769   5080   -153    616       C  
ATOM   4074  CG  ASN C  83      57.620  32.656  -1.500  1.00 98.58           C  
ANISOU 4074  CG  ASN C  83    19225   6308  11923   5247    147    485       C  
ATOM   4075  OD1 ASN C  83      58.452  33.569  -1.426  1.00 86.47           O  
ANISOU 4075  OD1 ASN C  83    18269   4477  10108   5090    194    451       O  
ATOM   4076  ND2 ASN C  83      56.742  32.429  -0.535  1.00 91.65           N  
ANISOU 4076  ND2 ASN C  83    17951   5559  11311   5554    369    404       N  
ATOM   4077  N   TRP C  84      58.908  29.402  -0.738  1.00 79.39           N  
ANISOU 4077  N   TRP C  84    15862   4815   9490   4392    438    392       N  
ATOM   4078  CA  TRP C  84      58.664  28.315   0.201  1.00 77.80           C  
ANISOU 4078  CA  TRP C  84    15169   4945   9447   4353    666    316       C  
ATOM   4079  C   TRP C  84      57.527  28.760   1.113  1.00 81.56           C  
ANISOU 4079  C   TRP C  84    15478   5355  10156   4799    870    251       C  
ATOM   4080  O   TRP C  84      57.536  29.905   1.574  1.00 81.97           O  
ANISOU 4080  O   TRP C  84    15936   5102  10108   4977    982    189       O  
ATOM   4081  CB  TRP C  84      59.932  28.025   1.005  1.00 76.22           C  
ANISOU 4081  CB  TRP C  84    15146   4814   9000   3950    874    214       C  
ATOM   4082  CG  TRP C  84      59.782  26.886   1.966  1.00 77.13           C  
ANISOU 4082  CG  TRP C  84    14821   5249   9234   3879   1093    144       C  
ATOM   4083  CD1 TRP C  84      59.635  26.971   3.319  1.00 80.03           C  
ANISOU 4083  CD1 TRP C  84    15184   5619   9606   3976   1394     26       C  
ATOM   4084  CD2 TRP C  84      59.697  25.490   1.637  1.00 76.87           C  
ANISOU 4084  CD2 TRP C  84    14319   5562   9327   3712   1028    193       C  
ATOM   4085  NE1 TRP C  84      59.506  25.710   3.860  1.00 79.64           N  
ANISOU 4085  NE1 TRP C  84    14701   5895   9665   3860   1523      5       N  
ATOM   4086  CE2 TRP C  84      59.547  24.783   2.850  1.00 80.65           C  
ANISOU 4086  CE2 TRP C  84    14532   6236   9876   3697   1299    105       C  
ATOM   4087  CE3 TRP C  84      59.772  24.764   0.434  1.00 78.17           C  
ANISOU 4087  CE3 TRP C  84    14306   5870   9524   3557    768    300       C  
ATOM   4088  CZ2 TRP C  84      59.462  23.388   2.897  1.00 79.96           C  
ANISOU 4088  CZ2 TRP C  84    14000   6477   9903   3535   1314    126       C  
ATOM   4089  CZ3 TRP C  84      59.697  23.380   0.482  1.00 79.58           C  
ANISOU 4089  CZ3 TRP C  84    14045   6374   9817   3400    784    311       C  
ATOM   4090  CH2 TRP C  84      59.541  22.707   1.701  1.00 80.23           C  
ANISOU 4090  CH2 TRP C  84    13860   6643   9981   3391   1050    227       C  
ATOM   4091  N   THR C  85      56.521  27.894   1.337  1.00 77.43           N  
ANISOU 4091  N   THR C  85    14371   5100   9951   4987    925    265       N  
ATOM   4092  CA  THR C  85      55.341  28.262   2.141  1.00 77.57           C  
ANISOU 4092  CA  THR C  85    14155   5075  10242   5433   1147    209       C  
ATOM   4093  C   THR C  85      55.000  27.279   3.268  1.00 81.43           C  
ANISOU 4093  C   THR C  85    14211   5857  10873   5398   1485    125       C  
ATOM   4094  O   THR C  85      53.963  27.429   3.934  1.00 80.27           O  
ANISOU 4094  O   THR C  85    13806   5714  10978   5751   1718     79       O  
ATOM   4095  CB  THR C  85      54.118  28.453   1.217  1.00 86.37           C  
ANISOU 4095  CB  THR C  85    14961   6161  11693   5818    869    327       C  
ATOM   4096  OG1 THR C  85      53.949  27.289   0.400  1.00 87.18           O  
ANISOU 4096  OG1 THR C  85    14627   6564  11935   5636    630    426       O  
ATOM   4097  CG2 THR C  85      54.210  29.714   0.364  1.00 82.96           C  
ANISOU 4097  CG2 THR C  85    15031   5355  11137   5981    592    397       C  
ATOM   4098  N   TYR C  86      55.883  26.291   3.491  1.00 78.06           N  
ANISOU 4098  N   TYR C  86    13720   5660  10280   4976   1526    106       N  
ATOM   4099  CA  TYR C  86      55.674  25.193   4.435  1.00 77.18           C  
ANISOU 4099  CA  TYR C  86    13223   5838  10266   4874   1799     48       C  
ATOM   4100  C   TYR C  86      56.454  25.311   5.767  1.00 81.20           C  
ANISOU 4100  C   TYR C  86    14063   6285  10504   4707   2127    -90       C  
ATOM   4101  O   TYR C  86      56.396  24.401   6.597  1.00 80.52           O  
ANISOU 4101  O   TYR C  86    13737   6415  10441   4588   2353   -137       O  
ATOM   4102  CB  TYR C  86      55.976  23.865   3.722  1.00 77.62           C  
ANISOU 4102  CB  TYR C  86    12942   6195  10355   4550   1594    131       C  
ATOM   4103  CG  TYR C  86      55.433  23.781   2.310  1.00 78.36           C  
ANISOU 4103  CG  TYR C  86    12833   6312  10630   4645   1212    266       C  
ATOM   4104  CD1 TYR C  86      54.094  23.477   2.071  1.00 79.96           C  
ANISOU 4104  CD1 TYR C  86    12529   6633  11218   4941   1151    325       C  
ATOM   4105  CD2 TYR C  86      56.262  23.991   1.209  1.00 78.81           C  
ANISOU 4105  CD2 TYR C  86    13212   6262  10470   4430    907    336       C  
ATOM   4106  CE1 TYR C  86      53.592  23.392   0.773  1.00 80.21           C  
ANISOU 4106  CE1 TYR C  86    12398   6671  11406   5024    752    452       C  
ATOM   4107  CE2 TYR C  86      55.771  23.912  -0.094  1.00 79.29           C  
ANISOU 4107  CE2 TYR C  86    13152   6320  10656   4512    541    461       C  
ATOM   4108  CZ  TYR C  86      54.435  23.610  -0.307  1.00 84.87           C  
ANISOU 4108  CZ  TYR C  86    13369   7141  11737   4809    442    519       C  
ATOM   4109  OH  TYR C  86      53.957  23.522  -1.590  1.00 82.65           O  
ANISOU 4109  OH  TYR C  86    12988   6847  11568   4879     37    645       O  
ATOM   4110  N   GLY C  87      57.135  26.437   5.970  1.00 78.66           N  
ANISOU 4110  N   GLY C  87    14307   5654   9925   4701   2139   -150       N  
ATOM   4111  CA  GLY C  87      57.875  26.732   7.195  1.00 78.72           C  
ANISOU 4111  CA  GLY C  87    14708   5546   9657   4556   2398   -283       C  
ATOM   4112  C   GLY C  87      59.158  25.954   7.439  1.00 82.49           C  
ANISOU 4112  C   GLY C  87    15281   6174   9888   4076   2355   -307       C  
ATOM   4113  O   GLY C  87      59.599  25.166   6.598  1.00 81.85           O  
ANISOU 4113  O   GLY C  87    14996   6278   9825   3826   2128   -221       O  
ATOM   4114  N   ASP C  88      59.748  26.180   8.630  1.00 78.19           N  
ANISOU 4114  N   ASP C  88    15058   5537   9112   3960   2576   -428       N  
ATOM   4115  CA  ASP C  88      61.014  25.623   9.113  1.00 76.96           C  
ANISOU 4115  CA  ASP C  88    15066   5469   8706   3535   2548   -473       C  
ATOM   4116  C   ASP C  88      61.044  24.124   9.315  1.00 76.05           C  
ANISOU 4116  C   ASP C  88    14514   5705   8677   3344   2580   -441       C  
ATOM   4117  O   ASP C  88      62.053  23.521   8.981  1.00 76.25           O  
ANISOU 4117  O   ASP C  88    14525   5849   8598   3000   2404   -413       O  
ATOM   4118  CB  ASP C  88      61.442  26.302  10.431  1.00 79.50           C  
ANISOU 4118  CB  ASP C  88    15876   5566   8764   3515   2763   -614       C  
ATOM   4119  CG  ASP C  88      61.441  27.808  10.403  1.00 95.02           C  
ANISOU 4119  CG  ASP C  88    18364   7146  10593   3656   2738   -664       C  
ATOM   4120  OD1 ASP C  88      60.448  28.410  10.873  1.00 97.11           O  
ANISOU 4120  OD1 ASP C  88    18737   7235  10926   4032   2956   -719       O  
ATOM   4121  OD2 ASP C  88      62.435  28.390   9.922  1.00103.36           O  
ANISOU 4121  OD2 ASP C  88    19727   8066  11480   3389   2516   -649       O  
ATOM   4122  N   VAL C  89      60.003  23.532   9.938  1.00 69.71           N  
ANISOU 4122  N   VAL C  89    13382   5052   8052   3553   2827   -454       N  
ATOM   4123  CA  VAL C  89      59.957  22.097  10.278  1.00 68.54           C  
ANISOU 4123  CA  VAL C  89    12855   5215   7972   3375   2894   -429       C  
ATOM   4124  C   VAL C  89      59.865  21.238   9.021  1.00 72.20           C  
ANISOU 4124  C   VAL C  89    12896   5904   8635   3269   2630   -304       C  
ATOM   4125  O   VAL C  89      60.589  20.234   8.916  1.00 71.56           O  
ANISOU 4125  O   VAL C  89    12697   6007   8487   2964   2523   -278       O  
ATOM   4126  CB  VAL C  89      58.871  21.750  11.338  1.00 71.92           C  
ANISOU 4126  CB  VAL C  89    13085   5720   8521   3601   3269   -478       C  
ATOM   4127  CG1 VAL C  89      58.873  20.260  11.689  1.00 71.22           C  
ANISOU 4127  CG1 VAL C  89    12659   5926   8474   3383   3331   -446       C  
ATOM   4128  CG2 VAL C  89      59.062  22.586  12.604  1.00 71.79           C  
ANISOU 4128  CG2 VAL C  89    13570   5455   8252   3685   3537   -613       C  
ATOM   4129  N   LEU C  90      59.012  21.648   8.051  1.00 68.33           N  
ANISOU 4129  N   LEU C  90    12209   5379   8374   3520   2503   -229       N  
ATOM   4130  CA  LEU C  90      58.891  20.933   6.779  1.00 67.35           C  
ANISOU 4130  CA  LEU C  90    11747   5429   8412   3429   2220   -112       C  
ATOM   4131  C   LEU C  90      60.141  21.079   5.942  1.00 69.80           C  
ANISOU 4131  C   LEU C  90    12335   5674   8513   3134   1957    -82       C  
ATOM   4132  O   LEU C  90      60.493  20.125   5.265  1.00 69.58           O  
ANISOU 4132  O   LEU C  90    12091   5833   8512   2917   1793    -19       O  
ATOM   4133  CB  LEU C  90      57.629  21.296   5.989  1.00 67.17           C  
ANISOU 4133  CB  LEU C  90    11449   5381   8690   3773   2117    -35       C  
ATOM   4134  CG  LEU C  90      56.378  20.524   6.397  1.00 71.73           C  
ANISOU 4134  CG  LEU C  90    11501   6168   9585   3960   2297    -17       C  
ATOM   4135  CD1 LEU C  90      55.125  21.247   5.968  1.00 71.83           C  
ANISOU 4135  CD1 LEU C  90    11309   6085   9898   4373   2259     26       C  
ATOM   4136  CD2 LEU C  90      56.393  19.097   5.851  1.00 73.90           C  
ANISOU 4136  CD2 LEU C  90    11379   6735   9965   3711   2147     59       C  
ATOM   4137  N   CYS C  91      60.864  22.209   6.066  1.00 65.82           N  
ANISOU 4137  N   CYS C  91    12314   4906   7790   3100   1943   -134       N  
ATOM   4138  CA  CYS C  91      62.119  22.451   5.354  1.00 66.88           C  
ANISOU 4138  CA  CYS C  91    12732   4958   7723   2796   1737   -114       C  
ATOM   4139  C   CYS C  91      63.246  21.522   5.835  1.00 68.22           C  
ANISOU 4139  C   CYS C  91    12874   5295   7753   2428   1758   -153       C  
ATOM   4140  O   CYS C  91      64.009  21.002   5.009  1.00 67.46           O  
ANISOU 4140  O   CYS C  91    12719   5294   7620   2174   1587   -102       O  
ATOM   4141  CB  CYS C  91      62.524  23.919   5.442  1.00 68.97           C  
ANISOU 4141  CB  CYS C  91    13515   4881   7809   2851   1732   -160       C  
ATOM   4142  SG  CYS C  91      64.061  24.323   4.570  1.00 74.19           S  
ANISOU 4142  SG  CYS C  91    14527   5422   8241   2457   1515   -132       S  
ATOM   4143  N   ILE C  92      63.332  21.300   7.166  1.00 62.06           N  
ANISOU 4143  N   ILE C  92    12144   4542   6895   2410   1968   -242       N  
ATOM   4144  CA  ILE C  92      64.354  20.448   7.786  1.00 59.65           C  
ANISOU 4144  CA  ILE C  92    11831   4375   6459   2094   1974   -282       C  
ATOM   4145  C   ILE C  92      64.017  18.952   7.588  1.00 61.28           C  
ANISOU 4145  C   ILE C  92    11572   4885   6826   2030   1962   -221       C  
ATOM   4146  O   ILE C  92      64.905  18.194   7.193  1.00 60.79           O  
ANISOU 4146  O   ILE C  92    11423   4949   6727   1764   1827   -196       O  
ATOM   4147  CB  ILE C  92      64.604  20.872   9.269  1.00 62.01           C  
ANISOU 4147  CB  ILE C  92    12445   4546   6570   2090   2166   -397       C  
ATOM   4148  CG1 ILE C  92      65.080  22.367   9.388  1.00 62.14           C  
ANISOU 4148  CG1 ILE C  92    12972   4233   6403   2102   2140   -461       C  
ATOM   4149  CG2 ILE C  92      65.539  19.920  10.036  1.00 61.36           C  
ANISOU 4149  CG2 ILE C  92    12339   4609   6366   1797   2153   -431       C  
ATOM   4150  CD1 ILE C  92      66.353  22.831   8.491  1.00 65.47           C  
ANISOU 4150  CD1 ILE C  92    13599   4558   6721   1801   1893   -432       C  
ATOM   4151  N   SER C  93      62.744  18.536   7.810  1.00 56.28           N  
ANISOU 4151  N   SER C  93    10636   4360   6386   2270   2104   -198       N  
ATOM   4152  CA  SER C  93      62.331  17.137   7.616  1.00 55.22           C  
ANISOU 4152  CA  SER C  93    10069   4497   6415   2205   2092   -138       C  
ATOM   4153  C   SER C  93      62.493  16.684   6.163  1.00 55.65           C  
ANISOU 4153  C   SER C  93     9935   4644   6565   2102   1828    -45       C  
ATOM   4154  O   SER C  93      62.805  15.514   5.938  1.00 54.98           O  
ANISOU 4154  O   SER C  93     9633   4747   6508   1913   1761    -13       O  
ATOM   4155  CB  SER C  93      60.909  16.883   8.114  1.00 59.44           C  
ANISOU 4155  CB  SER C  93    10309   5114   7163   2470   2305   -129       C  
ATOM   4156  OG  SER C  93      59.922  17.442   7.262  1.00 71.20           O  
ANISOU 4156  OG  SER C  93    11650   6543   8859   2740   2232    -75       O  
ATOM   4157  N   ASN C  94      62.310  17.610   5.189  1.00 49.74           N  
ANISOU 4157  N   ASN C  94     9313   3744   5841   2224   1680     -4       N  
ATOM   4158  CA  ASN C  94      62.479  17.336   3.753  1.00 48.55           C  
ANISOU 4158  CA  ASN C  94     9077   3636   5733   2131   1426     83       C  
ATOM   4159  C   ASN C  94      63.958  17.080   3.452  1.00 50.47           C  
ANISOU 4159  C   ASN C  94     9506   3886   5784   1795   1341     66       C  
ATOM   4160  O   ASN C  94      64.286  16.140   2.716  1.00 48.43           O  
ANISOU 4160  O   ASN C  94     9072   3775   5553   1628   1226    112       O  
ATOM   4161  CB  ASN C  94      61.988  18.517   2.911  1.00 47.42           C  
ANISOU 4161  CB  ASN C  94     9117   3283   5616   2341   1294    128       C  
ATOM   4162  CG  ASN C  94      60.504  18.567   2.645  1.00 67.33           C  
ANISOU 4162  CG  ASN C  94    11346   5836   8400   2662   1258    185       C  
ATOM   4163  OD1 ASN C  94      59.689  17.964   3.353  1.00 58.07           O  
ANISOU 4163  OD1 ASN C  94     9852   4809   7403   2780   1415    171       O  
ATOM   4164  ND2 ASN C  94      60.117  19.318   1.619  1.00 62.40           N  
ANISOU 4164  ND2 ASN C  94    10832   5063   7812   2810   1048    255       N  
ATOM   4165  N   ARG C  95      64.844  17.926   4.048  1.00 46.60           N  
ANISOU 4165  N   ARG C  95     9368   3228   5109   1696   1404     -4       N  
ATOM   4166  CA  ARG C  95      66.301  17.842   3.930  1.00 45.66           C  
ANISOU 4166  CA  ARG C  95     9420   3096   4834   1379   1345    -31       C  
ATOM   4167  C   ARG C  95      66.821  16.536   4.544  1.00 48.87           C  
ANISOU 4167  C   ARG C  95     9596   3720   5252   1197   1387    -56       C  
ATOM   4168  O   ARG C  95      67.686  15.903   3.942  1.00 49.02           O  
ANISOU 4168  O   ARG C  95     9536   3832   5258    980   1295    -35       O  
ATOM   4169  CB  ARG C  95      66.969  19.056   4.571  1.00 43.03           C  
ANISOU 4169  CB  ARG C  95     9491   2529   4328   1328   1397   -105       C  
ATOM   4170  CG  ARG C  95      68.440  19.205   4.238  1.00 45.73           C  
ANISOU 4170  CG  ARG C  95    10008   2823   4544   1001   1311   -121       C  
ATOM   4171  CD  ARG C  95      69.070  20.262   5.117  1.00 48.45           C  
ANISOU 4171  CD  ARG C  95    10726   2954   4731    924   1356   -205       C  
ATOM   4172  NE  ARG C  95      69.011  21.581   4.492  1.00 59.02           N  
ANISOU 4172  NE  ARG C  95    12398   4030   5998    996   1316   -187       N  
ATOM   4173  CZ  ARG C  95      69.705  22.633   4.908  1.00 75.47           C  
ANISOU 4173  CZ  ARG C  95    14860   5883   7933    874   1316   -245       C  
ATOM   4174  NH1 ARG C  95      69.605  23.795   4.271  1.00 68.65           N  
ANISOU 4174  NH1 ARG C  95    14314   4767   7004    945   1277   -219       N  
ATOM   4175  NH2 ARG C  95      70.494  22.538   5.975  1.00 53.18           N  
ANISOU 4175  NH2 ARG C  95    12120   3064   5020    677   1336   -327       N  
ATOM   4176  N   TYR C  96      66.269  16.112   5.702  1.00 44.07           N  
ANISOU 4176  N   TYR C  96     8888   3184   4672   1295   1536    -96       N  
ATOM   4177  CA  TYR C  96      66.657  14.847   6.332  1.00 43.25           C  
ANISOU 4177  CA  TYR C  96     8593   3267   4573   1144   1571   -110       C  
ATOM   4178  C   TYR C  96      66.325  13.667   5.408  1.00 46.01           C  
ANISOU 4178  C   TYR C  96     8600   3811   5070   1109   1483    -35       C  
ATOM   4179  O   TYR C  96      67.199  12.870   5.091  1.00 44.42           O  
ANISOU 4179  O   TYR C  96     8323   3708   4848    904   1400    -28       O  
ATOM   4180  CB  TYR C  96      65.994  14.655   7.734  1.00 43.77           C  
ANISOU 4180  CB  TYR C  96     8659   3350   4621   1269   1772   -158       C  
ATOM   4181  CG  TYR C  96      66.111  13.225   8.235  1.00 44.44           C  
ANISOU 4181  CG  TYR C  96     8520   3631   4735   1148   1803   -146       C  
ATOM   4182  CD1 TYR C  96      67.347  12.693   8.604  1.00 45.75           C  
ANISOU 4182  CD1 TYR C  96     8760   3834   4790    909   1713   -174       C  
ATOM   4183  CD2 TYR C  96      65.015  12.366   8.210  1.00 45.40           C  
ANISOU 4183  CD2 TYR C  96     8333   3899   5016   1264   1895    -98       C  
ATOM   4184  CE1 TYR C  96      67.478  11.354   8.978  1.00 45.95           C  
ANISOU 4184  CE1 TYR C  96     8596   4020   4843    809   1716   -154       C  
ATOM   4185  CE2 TYR C  96      65.138  11.019   8.563  1.00 46.28           C  
ANISOU 4185  CE2 TYR C  96     8259   4174   5150   1136   1909    -78       C  
ATOM   4186  CZ  TYR C  96      66.367  10.523   8.970  1.00 52.37           C  
ANISOU 4186  CZ  TYR C  96     9148   4962   5789    919   1821   -106       C  
ATOM   4187  OH  TYR C  96      66.486   9.203   9.340  1.00 49.27           O  
ANISOU 4187  OH  TYR C  96     8602   4705   5412    812   1826    -82       O  
ATOM   4188  N   VAL C  97      65.049  13.570   5.009  1.00 43.59           N  
ANISOU 4188  N   VAL C  97     8088   3551   4922   1315   1498     17       N  
ATOM   4189  CA  VAL C  97      64.433  12.540   4.165  1.00 43.84           C  
ANISOU 4189  CA  VAL C  97     7798   3747   5111   1316   1403     90       C  
ATOM   4190  C   VAL C  97      65.111  12.436   2.777  1.00 46.84           C  
ANISOU 4190  C   VAL C  97     8227   4119   5452   1169   1206    133       C  
ATOM   4191  O   VAL C  97      65.138  11.352   2.197  1.00 45.70           O  
ANISOU 4191  O   VAL C  97     7889   4111   5365   1065   1126    169       O  
ATOM   4192  CB  VAL C  97      62.905  12.844   4.122  1.00 48.42           C  
ANISOU 4192  CB  VAL C  97     8188   4328   5881   1594   1449    128       C  
ATOM   4193  CG1 VAL C  97      62.360  13.074   2.723  1.00 48.46           C  
ANISOU 4193  CG1 VAL C  97     8113   4308   5991   1679   1235    206       C  
ATOM   4194  CG2 VAL C  97      62.090  11.826   4.907  1.00 47.99           C  
ANISOU 4194  CG2 VAL C  97     7831   4439   5965   1630   1599    134       C  
ATOM   4195  N   LEU C  98      65.671  13.560   2.268  1.00 43.38           N  
ANISOU 4195  N   LEU C  98     8077   3505   4901   1153   1146    126       N  
ATOM   4196  CA  LEU C  98      66.410  13.619   1.006  1.00 43.04           C  
ANISOU 4196  CA  LEU C  98     8152   3419   4782    999   1008    161       C  
ATOM   4197  C   LEU C  98      67.750  12.867   1.166  1.00 44.05           C  
ANISOU 4197  C   LEU C  98     8272   3631   4833    731   1037    119       C  
ATOM   4198  O   LEU C  98      67.988  11.880   0.475  1.00 43.98           O  
ANISOU 4198  O   LEU C  98     8124   3735   4853    621    977    146       O  
ATOM   4199  CB  LEU C  98      66.676  15.093   0.659  1.00 43.73           C  
ANISOU 4199  CB  LEU C  98     8584   3272   4758   1041    979    160       C  
ATOM   4200  CG  LEU C  98      67.253  15.431  -0.714  1.00 48.85           C  
ANISOU 4200  CG  LEU C  98     9426   3825   5309    914    858    208       C  
ATOM   4201  CD1 LEU C  98      66.751  16.778  -1.162  1.00 49.29           C  
ANISOU 4201  CD1 LEU C  98     9761   3652   5315   1078    792    244       C  
ATOM   4202  CD2 LEU C  98      68.772  15.473  -0.687  1.00 50.44           C  
ANISOU 4202  CD2 LEU C  98     9770   4005   5389    629    920    161       C  
ATOM   4203  N   HIS C  99      68.617  13.358   2.071  1.00 37.08           N  
ANISOU 4203  N   HIS C  99     7550   2681   3859    634   1117     53       N  
ATOM   4204  CA  HIS C  99      69.943  12.834   2.318  1.00 35.47           C  
ANISOU 4204  CA  HIS C  99     7337   2534   3607    396   1125     10       C  
ATOM   4205  C   HIS C  99      69.903  11.442   2.918  1.00 40.46           C  
ANISOU 4205  C   HIS C  99     7712   3351   4311    363   1147      3       C  
ATOM   4206  O   HIS C  99      70.801  10.647   2.630  1.00 40.16           O  
ANISOU 4206  O   HIS C  99     7578   3395   4284    199   1117     -5       O  
ATOM   4207  CB  HIS C  99      70.752  13.830   3.149  1.00 35.90           C  
ANISOU 4207  CB  HIS C  99     7640   2445   3555    308   1161    -55       C  
ATOM   4208  CG  HIS C  99      70.946  15.139   2.440  1.00 40.08           C  
ANISOU 4208  CG  HIS C  99     8449   2776   4005    294   1135    -43       C  
ATOM   4209  ND1 HIS C  99      70.127  16.236   2.693  1.00 41.74           N  
ANISOU 4209  ND1 HIS C  99     8862   2821   4175    490   1159    -43       N  
ATOM   4210  CD2 HIS C  99      71.830  15.478   1.471  1.00 41.64           C  
ANISOU 4210  CD2 HIS C  99     8759   2906   4155    111   1102    -27       C  
ATOM   4211  CE1 HIS C  99      70.545  17.190   1.884  1.00 40.85           C  
ANISOU 4211  CE1 HIS C  99     8996   2540   3984    417   1116    -23       C  
ATOM   4212  NE2 HIS C  99      71.575  16.788   1.145  1.00 41.29           N  
ANISOU 4212  NE2 HIS C  99     9013   2648   4028    178   1092    -12       N  
ATOM   4213  N   ALA C 100      68.846  11.119   3.716  1.00 38.37           N  
ANISOU 4213  N   ALA C 100     7333   3144   4102    523   1214      8       N  
ATOM   4214  CA  ALA C 100      68.660   9.775   4.285  1.00 38.20           C  
ANISOU 4214  CA  ALA C 100     7090   3283   4143    496   1245     13       C  
ATOM   4215  C   ALA C 100      68.402   8.803   3.148  1.00 41.61           C  
ANISOU 4215  C   ALA C 100     7320   3823   4666    463   1160     68       C  
ATOM   4216  O   ALA C 100      69.047   7.762   3.111  1.00 41.57           O  
ANISOU 4216  O   ALA C 100     7212   3910   4671    334   1135     63       O  
ATOM   4217  CB  ALA C 100      67.518   9.735   5.295  1.00 38.79           C  
ANISOU 4217  CB  ALA C 100     7103   3379   4257    665   1370     12       C  
ATOM   4218  N   ASN C 101      67.542   9.174   2.174  1.00 37.28           N  
ANISOU 4218  N   ASN C 101     6747   3244   4173    574   1096    119       N  
ATOM   4219  CA  ASN C 101      67.290   8.332   1.002  1.00 37.14           C  
ANISOU 4219  CA  ASN C 101     6596   3303   4214    531    985    170       C  
ATOM   4220  C   ASN C 101      68.576   8.034   0.223  1.00 41.61           C  
ANISOU 4220  C   ASN C 101     7256   3857   4696    341    948    151       C  
ATOM   4221  O   ASN C 101      68.845   6.886  -0.085  1.00 42.63           O  
ANISOU 4221  O   ASN C 101     7261   4081   4854    250    925    154       O  
ATOM   4222  CB  ASN C 101      66.240   8.933   0.071  1.00 37.21           C  
ANISOU 4222  CB  ASN C 101     6611   3251   4277    680    878    229       C  
ATOM   4223  CG  ASN C 101      65.940   8.041  -1.118  1.00 54.80           C  
ANISOU 4223  CG  ASN C 101     8735   5542   6543    624    734    279       C  
ATOM   4224  OD1 ASN C 101      65.931   8.490  -2.261  1.00 48.00           O  
ANISOU 4224  OD1 ASN C 101     8020   4595   5624    624    612    315       O  
ATOM   4225  ND2 ASN C 101      65.701   6.748  -0.887  1.00 43.25           N  
ANISOU 4225  ND2 ASN C 101     7057   4216   5161    565    738    284       N  
ATOM   4226  N   LEU C 102      69.363   9.064  -0.073  1.00 36.22           N  
ANISOU 4226  N   LEU C 102     6793   3050   3917    279    959    130       N  
ATOM   4227  CA  LEU C 102      70.639   8.963  -0.763  1.00 34.97           C  
ANISOU 4227  CA  LEU C 102     6723   2869   3695     93    971    108       C  
ATOM   4228  C   LEU C 102      71.566   7.926  -0.099  1.00 34.51           C  
ANISOU 4228  C   LEU C 102     6513   2922   3679    -29   1018     61       C  
ATOM   4229  O   LEU C 102      72.012   6.985  -0.754  1.00 31.56           O  
ANISOU 4229  O   LEU C 102     6052   2613   3327   -113   1014     61       O  
ATOM   4230  CB  LEU C 102      71.305  10.348  -0.671  1.00 35.48           C  
ANISOU 4230  CB  LEU C 102     7032   2778   3670     39   1009     83       C  
ATOM   4231  CG  LEU C 102      71.735  11.067  -1.943  1.00 41.94           C  
ANISOU 4231  CG  LEU C 102     8069   3470   4394    -47    997    110       C  
ATOM   4232  CD1 LEU C 102      70.563  11.284  -2.903  1.00 42.86           C  
ANISOU 4232  CD1 LEU C 102     8262   3533   4490    101    888    183       C  
ATOM   4233  CD2 LEU C 102      72.318  12.421  -1.588  1.00 44.85           C  
ANISOU 4233  CD2 LEU C 102     8675   3679   4688   -106   1040     84       C  
ATOM   4234  N   TYR C 103      71.833   8.104   1.212  1.00 30.66           N  
ANISOU 4234  N   TYR C 103     6017   2439   3195    -26   1054     21       N  
ATOM   4235  CA  TYR C 103      72.796   7.320   1.962  1.00 29.35           C  
ANISOU 4235  CA  TYR C 103     5746   2346   3059   -133   1062    -20       C  
ATOM   4236  C   TYR C 103      72.265   5.996   2.509  1.00 32.19           C  
ANISOU 4236  C   TYR C 103     5926   2827   3479    -81   1053     -4       C  
ATOM   4237  O   TYR C 103      73.085   5.128   2.752  1.00 31.71           O  
ANISOU 4237  O   TYR C 103     5770   2824   3454   -165   1035    -26       O  
ATOM   4238  CB  TYR C 103      73.446   8.188   3.049  1.00 30.22           C  
ANISOU 4238  CB  TYR C 103     5987   2377   3116   -182   1067    -69       C  
ATOM   4239  CG  TYR C 103      74.213   9.348   2.435  1.00 30.92           C  
ANISOU 4239  CG  TYR C 103     6245   2343   3160   -291   1076    -87       C  
ATOM   4240  CD1 TYR C 103      75.212   9.126   1.487  1.00 32.73           C  
ANISOU 4240  CD1 TYR C 103     6424   2585   3427   -440   1095    -93       C  
ATOM   4241  CD2 TYR C 103      73.913  10.667   2.770  1.00 30.71           C  
ANISOU 4241  CD2 TYR C 103     6444   2175   3050   -246   1086    -98       C  
ATOM   4242  CE1 TYR C 103      75.895  10.187   0.890  1.00 34.83           C  
ANISOU 4242  CE1 TYR C 103     6853   2731   3650   -564   1130   -102       C  
ATOM   4243  CE2 TYR C 103      74.577  11.734   2.169  1.00 31.77           C  
ANISOU 4243  CE2 TYR C 103     6761   2177   3134   -362   1096   -106       C  
ATOM   4244  CZ  TYR C 103      75.571  11.492   1.229  1.00 39.98           C  
ANISOU 4244  CZ  TYR C 103     7740   3237   4213   -532   1121   -106       C  
ATOM   4245  OH  TYR C 103      76.253  12.542   0.649  1.00 40.28           O  
ANISOU 4245  OH  TYR C 103     7965   3139   4201   -675   1157   -110       O  
ATOM   4246  N   THR C 104      70.936   5.798   2.651  1.00 29.16           N  
ANISOU 4246  N   THR C 104     5481   2476   3121     51   1065     36       N  
ATOM   4247  CA  THR C 104      70.414   4.490   3.058  1.00 29.63           C  
ANISOU 4247  CA  THR C 104     5375   2643   3241     69   1067     59       C  
ATOM   4248  C   THR C 104      70.342   3.611   1.816  1.00 35.53           C  
ANISOU 4248  C   THR C 104     6027   3438   4036     25   1008     86       C  
ATOM   4249  O   THR C 104      70.694   2.441   1.900  1.00 35.21           O  
ANISOU 4249  O   THR C 104     5894   3459   4027    -33    995     83       O  
ATOM   4250  CB  THR C 104      69.050   4.529   3.754  1.00 33.09           C  
ANISOU 4250  CB  THR C 104     5753   3105   3713    201   1128     90       C  
ATOM   4251  OG1 THR C 104      68.106   5.218   2.955  1.00 35.24           O  
ANISOU 4251  OG1 THR C 104     6016   3345   4029    307   1105    125       O  
ATOM   4252  CG2 THR C 104      69.108   5.070   5.147  1.00 27.65           C  
ANISOU 4252  CG2 THR C 104     5180   2370   2954    240   1215     55       C  
ATOM   4253  N   SER C 105      69.928   4.189   0.656  1.00 31.46           N  
ANISOU 4253  N   SER C 105     5572   2875   3508     54    964    113       N  
ATOM   4254  CA  SER C 105      69.822   3.486  -0.622  1.00 31.03           C  
ANISOU 4254  CA  SER C 105     5495   2836   3458      9    895    136       C  
ATOM   4255  C   SER C 105      71.110   2.770  -0.970  1.00 36.08           C  
ANISOU 4255  C   SER C 105     6143   3487   4079   -116    929     93       C  
ATOM   4256  O   SER C 105      71.089   1.582  -1.311  1.00 34.83           O  
ANISOU 4256  O   SER C 105     5908   3377   3950   -150    905     95       O  
ATOM   4257  CB  SER C 105      69.492   4.458  -1.755  1.00 33.64           C  
ANISOU 4257  CB  SER C 105     5978   3074   3731     42    836    165       C  
ATOM   4258  OG  SER C 105      68.132   4.855  -1.725  1.00 41.16           O  
ANISOU 4258  OG  SER C 105     6875   4023   4740    180    764    215       O  
ATOM   4259  N   ILE C 106      72.243   3.502  -0.910  1.00 32.00           N  
ANISOU 4259  N   ILE C 106     5718   2916   3524   -186    988     52       N  
ATOM   4260  CA  ILE C 106      73.525   2.910  -1.267  1.00 29.79           C  
ANISOU 4260  CA  ILE C 106     5408   2647   3263   -295   1042      8       C  
ATOM   4261  C   ILE C 106      73.943   1.835  -0.240  1.00 29.98           C  
ANISOU 4261  C   ILE C 106     5279   2746   3365   -297   1031    -14       C  
ATOM   4262  O   ILE C 106      74.557   0.863  -0.634  1.00 28.02           O  
ANISOU 4262  O   ILE C 106     4964   2523   3159   -336   1050    -36       O  
ATOM   4263  CB  ILE C 106      74.607   3.996  -1.541  1.00 31.47           C  
ANISOU 4263  CB  ILE C 106     5729   2784   3446   -390   1113    -25       C  
ATOM   4264  CG1 ILE C 106      75.797   3.392  -2.359  1.00 31.13           C  
ANISOU 4264  CG1 ILE C 106     5646   2746   3438   -498   1207    -66       C  
ATOM   4265  CG2 ILE C 106      75.034   4.717  -0.252  1.00 30.59           C  
ANISOU 4265  CG2 ILE C 106     5610   2659   3355   -402   1102    -51       C  
ATOM   4266  CD1 ILE C 106      76.794   4.339  -2.968  1.00 36.57           C  
ANISOU 4266  CD1 ILE C 106     6442   3355   4098   -619   1314    -90       C  
ATOM   4267  N   LEU C 107      73.572   1.991   1.053  1.00 26.17           N  
ANISOU 4267  N   LEU C 107     4770   2284   2888   -247   1004     -7       N  
ATOM   4268  CA  LEU C 107      73.925   1.018   2.089  1.00 25.59           C  
ANISOU 4268  CA  LEU C 107     4604   2259   2858   -249    975    -16       C  
ATOM   4269  C   LEU C 107      73.080  -0.246   1.971  1.00 29.12           C  
ANISOU 4269  C   LEU C 107     4975   2757   3331   -213    954     20       C  
ATOM   4270  O   LEU C 107      73.627  -1.348   2.040  1.00 29.33           O  
ANISOU 4270  O   LEU C 107     4940   2804   3401   -237    934      9       O  
ATOM   4271  CB  LEU C 107      73.854   1.638   3.493  1.00 25.80           C  
ANISOU 4271  CB  LEU C 107     4691   2268   2844   -223    961    -23       C  
ATOM   4272  CG  LEU C 107      75.158   2.247   4.040  1.00 30.25           C  
ANISOU 4272  CG  LEU C 107     5293   2791   3412   -303    924    -71       C  
ATOM   4273  CD1 LEU C 107      74.915   2.936   5.387  1.00 29.39           C  
ANISOU 4273  CD1 LEU C 107     5312   2637   3218   -277    902    -79       C  
ATOM   4274  CD2 LEU C 107      76.261   1.176   4.208  1.00 32.65           C  
ANISOU 4274  CD2 LEU C 107     5471   3131   3806   -351    863    -93       C  
ATOM   4275  N   PHE C 108      71.766  -0.103   1.695  1.00 25.23           N  
ANISOU 4275  N   PHE C 108     4480   2277   2828   -158    952     65       N  
ATOM   4276  CA  PHE C 108      70.900  -1.255   1.468  1.00 25.44           C  
ANISOU 4276  CA  PHE C 108     4426   2346   2892   -153    920    102       C  
ATOM   4277  C   PHE C 108      71.407  -2.033   0.292  1.00 31.04           C  
ANISOU 4277  C   PHE C 108     5148   3039   3604   -209    893     84       C  
ATOM   4278  O   PHE C 108      71.453  -3.259   0.374  1.00 31.86           O  
ANISOU 4278  O   PHE C 108     5211   3157   3737   -234    872     85       O  
ATOM   4279  CB  PHE C 108      69.418  -0.875   1.295  1.00 27.07           C  
ANISOU 4279  CB  PHE C 108     4588   2573   3126    -91    906    153       C  
ATOM   4280  CG  PHE C 108      68.789  -0.477   2.611  1.00 28.68           C  
ANISOU 4280  CG  PHE C 108     4762   2796   3339    -27    980    169       C  
ATOM   4281  CD1 PHE C 108      68.831  -1.331   3.709  1.00 31.33           C  
ANISOU 4281  CD1 PHE C 108     5075   3158   3671    -53   1022    175       C  
ATOM   4282  CD2 PHE C 108      68.142   0.749   2.751  1.00 30.18           C  
ANISOU 4282  CD2 PHE C 108     4977   2961   3529     66   1017    178       C  
ATOM   4283  CE1 PHE C 108      68.288  -0.939   4.934  1.00 32.87           C  
ANISOU 4283  CE1 PHE C 108     5291   3356   3843     -1   1121    185       C  
ATOM   4284  CE2 PHE C 108      67.575   1.124   3.974  1.00 32.47           C  
ANISOU 4284  CE2 PHE C 108     5266   3256   3817    136   1122    182       C  
ATOM   4285  CZ  PHE C 108      67.673   0.293   5.060  1.00 30.74           C  
ANISOU 4285  CZ  PHE C 108     5042   3064   3574     95   1183    184       C  
ATOM   4286  N   LEU C 109      71.890  -1.343  -0.761  1.00 27.48           N  
ANISOU 4286  N   LEU C 109     4786   2543   3112   -232    908     61       N  
ATOM   4287  CA  LEU C 109      72.423  -2.065  -1.896  1.00 28.41           C  
ANISOU 4287  CA  LEU C 109     4955   2631   3210   -284    919     34       C  
ATOM   4288  C   LEU C 109      73.781  -2.704  -1.620  1.00 33.34           C  
ANISOU 4288  C   LEU C 109     5529   3254   3885   -311    984    -20       C  
ATOM   4289  O   LEU C 109      74.053  -3.757  -2.209  1.00 32.79           O  
ANISOU 4289  O   LEU C 109     5471   3165   3824   -326    997    -43       O  
ATOM   4290  CB  LEU C 109      72.412  -1.262  -3.178  1.00 28.46           C  
ANISOU 4290  CB  LEU C 109     5107   2574   3132   -309    930     33       C  
ATOM   4291  CG  LEU C 109      71.188  -1.677  -3.984  1.00 32.75           C  
ANISOU 4291  CG  LEU C 109     5698   3107   3640   -299    814     78       C  
ATOM   4292  CD1 LEU C 109      70.406  -0.517  -4.471  1.00 32.51           C  
ANISOU 4292  CD1 LEU C 109     5755   3038   3560   -259    744    121       C  
ATOM   4293  CD2 LEU C 109      71.469  -2.880  -4.924  1.00 31.53           C  
ANISOU 4293  CD2 LEU C 109     5623   2916   3442   -357    809     49       C  
ATOM   4294  N   THR C 110      74.566  -2.156  -0.652  1.00 28.88           N  
ANISOU 4294  N   THR C 110     4908   2703   3363   -311   1004    -41       N  
ATOM   4295  CA  THR C 110      75.844  -2.737  -0.227  1.00 28.18           C  
ANISOU 4295  CA  THR C 110     4729   2618   3360   -322   1024    -86       C  
ATOM   4296  C   THR C 110      75.551  -4.061   0.488  1.00 32.19           C  
ANISOU 4296  C   THR C 110     5187   3144   3901   -280    955    -66       C  
ATOM   4297  O   THR C 110      76.205  -5.065   0.203  1.00 33.66           O  
ANISOU 4297  O   THR C 110     5336   3310   4144   -266    967    -94       O  
ATOM   4298  CB  THR C 110      76.643  -1.728   0.625  1.00 33.92           C  
ANISOU 4298  CB  THR C 110     5420   3346   4120   -350   1015   -106       C  
ATOM   4299  OG1 THR C 110      77.003  -0.613  -0.191  1.00 34.93           O  
ANISOU 4299  OG1 THR C 110     5615   3439   4219   -410   1095   -125       O  
ATOM   4300  CG2 THR C 110      77.900  -2.319   1.250  1.00 26.54           C  
ANISOU 4300  CG2 THR C 110     4357   2420   3305   -353    983   -144       C  
ATOM   4301  N   PHE C 111      74.547  -4.064   1.387  1.00 26.57           N  
ANISOU 4301  N   PHE C 111     4489   2456   3150   -257    901    -16       N  
ATOM   4302  CA  PHE C 111      74.159  -5.249   2.138  1.00 24.87           C  
ANISOU 4302  CA  PHE C 111     4260   2244   2944   -239    849     16       C  
ATOM   4303  C   PHE C 111      73.487  -6.272   1.237  1.00 28.54           C  
ANISOU 4303  C   PHE C 111     4747   2693   3405   -256    844     31       C  
ATOM   4304  O   PHE C 111      73.821  -7.455   1.365  1.00 28.52           O  
ANISOU 4304  O   PHE C 111     4748   2656   3431   -249    817     26       O  
ATOM   4305  CB  PHE C 111      73.356  -4.903   3.403  1.00 26.36           C  
ANISOU 4305  CB  PHE C 111     4475   2456   3086   -224    837     61       C  
ATOM   4306  CG  PHE C 111      74.253  -4.237   4.440  1.00 27.29           C  
ANISOU 4306  CG  PHE C 111     4618   2560   3190   -217    804     37       C  
ATOM   4307  CD1 PHE C 111      75.292  -4.939   5.038  1.00 29.63           C  
ANISOU 4307  CD1 PHE C 111     4900   2831   3528   -210    723     21       C  
ATOM   4308  CD2 PHE C 111      74.108  -2.888   4.750  1.00 28.00           C  
ANISOU 4308  CD2 PHE C 111     4757   2648   3232   -216    833     27       C  
ATOM   4309  CE1 PHE C 111      76.133  -4.319   5.963  1.00 30.37           C  
ANISOU 4309  CE1 PHE C 111     5018   2906   3615   -217    648      0       C  
ATOM   4310  CE2 PHE C 111      74.958  -2.267   5.669  1.00 29.55           C  
ANISOU 4310  CE2 PHE C 111     5004   2817   3408   -231    779      0       C  
ATOM   4311  CZ  PHE C 111      75.957  -2.987   6.280  1.00 27.36           C  
ANISOU 4311  CZ  PHE C 111     4702   2523   3172   -239    675    -12       C  
ATOM   4312  N   ILE C 112      72.670  -5.836   0.243  1.00 25.39           N  
ANISOU 4312  N   ILE C 112     4379   2298   2969   -278    852     44       N  
ATOM   4313  CA  ILE C 112      72.095  -6.763  -0.748  1.00 26.12           C  
ANISOU 4313  CA  ILE C 112     4520   2359   3045   -315    816     50       C  
ATOM   4314  C   ILE C 112      73.233  -7.523  -1.484  1.00 32.86           C  
ANISOU 4314  C   ILE C 112     5431   3151   3904   -313    861    -12       C  
ATOM   4315  O   ILE C 112      73.161  -8.735  -1.585  1.00 33.88           O  
ANISOU 4315  O   ILE C 112     5599   3234   4039   -322    833    -16       O  
ATOM   4316  CB  ILE C 112      71.056  -6.139  -1.736  1.00 28.29           C  
ANISOU 4316  CB  ILE C 112     4836   2637   3276   -338    770     78       C  
ATOM   4317  CG1 ILE C 112      69.809  -5.651  -0.991  1.00 28.98           C  
ANISOU 4317  CG1 ILE C 112     4826   2783   3401   -319    735    140       C  
ATOM   4318  CG2 ILE C 112      70.640  -7.148  -2.836  1.00 26.15           C  
ANISOU 4318  CG2 ILE C 112     4657   2311   2968   -396    702     73       C  
ATOM   4319  CD1 ILE C 112      68.984  -4.577  -1.765  1.00 36.23           C  
ANISOU 4319  CD1 ILE C 112     5758   3704   4303   -296    680    167       C  
ATOM   4320  N   SER C 113      74.285  -6.821  -1.932  1.00 30.07           N  
ANISOU 4320  N   SER C 113     5080   2787   3557   -301    946    -63       N  
ATOM   4321  CA  SER C 113      75.451  -7.415  -2.610  1.00 29.08           C  
ANISOU 4321  CA  SER C 113     4976   2607   3465   -285   1039   -130       C  
ATOM   4322  C   SER C 113      76.161  -8.425  -1.701  1.00 31.39           C  
ANISOU 4322  C   SER C 113     5180   2887   3859   -224   1012   -144       C  
ATOM   4323  O   SER C 113      76.602  -9.466  -2.186  1.00 31.86           O  
ANISOU 4323  O   SER C 113     5282   2880   3942   -190   1048   -183       O  
ATOM   4324  CB  SER C 113      76.445  -6.327  -3.017  1.00 31.10           C  
ANISOU 4324  CB  SER C 113     5206   2870   3742   -300   1155   -173       C  
ATOM   4325  OG  SER C 113      75.795  -5.261  -3.680  1.00 35.35           O  
ANISOU 4325  OG  SER C 113     5852   3404   4176   -349   1161   -149       O  
ATOM   4326  N   ILE C 114      76.282  -8.118  -0.384  1.00 27.10           N  
ANISOU 4326  N   ILE C 114     4543   2390   3364   -202    941   -113       N  
ATOM   4327  CA  ILE C 114      76.899  -9.048   0.571  1.00 26.31           C  
ANISOU 4327  CA  ILE C 114     4390   2263   3343   -141    872   -111       C  
ATOM   4328  C   ILE C 114      76.001 -10.299   0.677  1.00 29.23           C  
ANISOU 4328  C   ILE C 114     4861   2583   3663   -146    812    -71       C  
ATOM   4329  O   ILE C 114      76.510 -11.406   0.559  1.00 32.28           O  
ANISOU 4329  O   ILE C 114     5275   2895   4095    -93    801    -93       O  
ATOM   4330  CB  ILE C 114      77.214  -8.406   1.948  1.00 28.62           C  
ANISOU 4330  CB  ILE C 114     4617   2597   3661   -131    786    -85       C  
ATOM   4331  CG1 ILE C 114      78.288  -7.298   1.800  1.00 27.18           C  
ANISOU 4331  CG1 ILE C 114     4329   2446   3554   -146    830   -133       C  
ATOM   4332  CG2 ILE C 114      77.644  -9.517   2.941  1.00 29.03           C  
ANISOU 4332  CG2 ILE C 114     4670   2599   3760    -67    673    -65       C  
ATOM   4333  CD1 ILE C 114      78.513  -6.359   2.991  1.00 22.55           C  
ANISOU 4333  CD1 ILE C 114     3717   1889   2963   -167    737   -116       C  
ATOM   4334  N   ASP C 115      74.674 -10.113   0.816  1.00 22.92           N  
ANISOU 4334  N   ASP C 115     4109   1814   2783   -213    784    -14       N  
ATOM   4335  CA  ASP C 115      73.710 -11.195   0.837  1.00 22.08           C  
ANISOU 4335  CA  ASP C 115     4083   1665   2641   -258    735     29       C  
ATOM   4336  C   ASP C 115      73.834 -12.071  -0.419  1.00 28.66           C  
ANISOU 4336  C   ASP C 115     5017   2415   3459   -269    753    -17       C  
ATOM   4337  O   ASP C 115      73.813 -13.303  -0.295  1.00 29.39           O  
ANISOU 4337  O   ASP C 115     5191   2421   3554   -266    715    -12       O  
ATOM   4338  CB  ASP C 115      72.271 -10.683   1.012  1.00 22.54           C  
ANISOU 4338  CB  ASP C 115     4120   1786   2657   -333    720     91       C  
ATOM   4339  CG  ASP C 115      71.288 -11.808   1.306  1.00 29.05           C  
ANISOU 4339  CG  ASP C 115     4994   2573   3473   -407    674    146       C  
ATOM   4340  OD1 ASP C 115      71.507 -12.544   2.288  1.00 29.15           O  
ANISOU 4340  OD1 ASP C 115     5048   2542   3484   -396    657    174       O  
ATOM   4341  OD2 ASP C 115      70.320 -11.972   0.534  1.00 32.86           O  
ANISOU 4341  OD2 ASP C 115     5483   3057   3947   -484    642    163       O  
ATOM   4342  N   ARG C 116      73.989 -11.450  -1.614  1.00 26.04           N  
ANISOU 4342  N   ARG C 116     4715   2086   3092   -282    816    -63       N  
ATOM   4343  CA  ARG C 116      74.125 -12.209  -2.870  1.00 26.16           C  
ANISOU 4343  CA  ARG C 116     4880   2004   3056   -296    849   -115       C  
ATOM   4344  C   ARG C 116      75.451 -12.988  -2.939  1.00 31.22           C  
ANISOU 4344  C   ARG C 116     5532   2565   3766   -194    933   -184       C  
ATOM   4345  O   ARG C 116      75.454 -14.111  -3.435  1.00 31.62           O  
ANISOU 4345  O   ARG C 116     5723   2505   3788   -185    933   -214       O  
ATOM   4346  CB  ARG C 116      73.913 -11.339  -4.139  1.00 24.80           C  
ANISOU 4346  CB  ARG C 116     4793   1837   2793   -343    895   -141       C  
ATOM   4347  CG  ARG C 116      72.656 -10.396  -4.162  1.00 26.73           C  
ANISOU 4347  CG  ARG C 116     5007   2157   2994   -412    798    -73       C  
ATOM   4348  CD  ARG C 116      71.330 -11.014  -3.715  1.00 27.35           C  
ANISOU 4348  CD  ARG C 116     5055   2250   3087   -480    664     -4       C  
ATOM   4349  NE  ARG C 116      70.926 -12.136  -4.564  1.00 32.93           N  
ANISOU 4349  NE  ARG C 116     5923   2855   3734   -551    594    -21       N  
ATOM   4350  CZ  ARG C 116      69.899 -12.947  -4.318  1.00 42.76           C  
ANISOU 4350  CZ  ARG C 116     7164   4083   4999   -640    479     28       C  
ATOM   4351  NH1 ARG C 116      69.144 -12.767  -3.242  1.00 31.32           N  
ANISOU 4351  NH1 ARG C 116     5546   2721   3633   -664    452    100       N  
ATOM   4352  NH2 ARG C 116      69.613 -13.938  -5.153  1.00 28.98           N  
ANISOU 4352  NH2 ARG C 116     5597   2226   3188   -718    403      4       N  
ATOM   4353  N   TYR C 117      76.564 -12.427  -2.423  1.00 28.46           N  
ANISOU 4353  N   TYR C 117     5030   2261   3521   -115    993   -210       N  
ATOM   4354  CA  TYR C 117      77.840 -13.149  -2.423  1.00 28.93           C  
ANISOU 4354  CA  TYR C 117     5040   2253   3697      3   1062   -272       C  
ATOM   4355  C   TYR C 117      77.755 -14.379  -1.506  1.00 34.76           C  
ANISOU 4355  C   TYR C 117     5814   2920   4475     62    939   -237       C  
ATOM   4356  O   TYR C 117      78.226 -15.451  -1.870  1.00 34.72           O  
ANISOU 4356  O   TYR C 117     5888   2798   4505    145    973   -282       O  
ATOM   4357  CB  TYR C 117      79.017 -12.243  -1.996  1.00 30.35           C  
ANISOU 4357  CB  TYR C 117     5009   2508   4013     55   1118   -299       C  
ATOM   4358  CG  TYR C 117      80.312 -13.000  -1.769  1.00 32.96           C  
ANISOU 4358  CG  TYR C 117     5220   2785   4520    194   1148   -351       C  
ATOM   4359  CD1 TYR C 117      80.940 -13.676  -2.810  1.00 35.23           C  
ANISOU 4359  CD1 TYR C 117     5554   2982   4849    269   1314   -433       C  
ATOM   4360  CD2 TYR C 117      80.876 -13.094  -0.497  1.00 33.40           C  
ANISOU 4360  CD2 TYR C 117     5131   2863   4697    263   1003   -318       C  
ATOM   4361  CE1 TYR C 117      82.087 -14.435  -2.595  1.00 36.08           C  
ANISOU 4361  CE1 TYR C 117     5532   3030   5147    426   1344   -481       C  
ATOM   4362  CE2 TYR C 117      82.068 -13.783  -0.285  1.00 33.78           C  
ANISOU 4362  CE2 TYR C 117     5044   2856   4934    409    996   -360       C  
ATOM   4363  CZ  TYR C 117      82.679 -14.439  -1.342  1.00 45.73           C  
ANISOU 4363  CZ  TYR C 117     6565   4288   6520    500   1175   -443       C  
ATOM   4364  OH  TYR C 117      83.821 -15.178  -1.144  1.00 53.01           O  
ANISOU 4364  OH  TYR C 117     7334   5150   7658    673   1175   -486       O  
ATOM   4365  N   LEU C 118      77.154 -14.218  -0.319  1.00 31.81           N  
ANISOU 4365  N   LEU C 118     5407   2597   4083     23    811   -157       N  
ATOM   4366  CA  LEU C 118      77.040 -15.317   0.630  1.00 31.17           C  
ANISOU 4366  CA  LEU C 118     5397   2434   4012     61    696   -110       C  
ATOM   4367  C   LEU C 118      76.113 -16.432   0.137  1.00 35.65           C  
ANISOU 4367  C   LEU C 118     6161   2896   4488    -10    675    -93       C  
ATOM   4368  O   LEU C 118      76.439 -17.595   0.320  1.00 35.49           O  
ANISOU 4368  O   LEU C 118     6248   2747   4491     57    633    -97       O  
ATOM   4369  CB  LEU C 118      76.647 -14.809   2.023  1.00 30.43           C  
ANISOU 4369  CB  LEU C 118     5258   2409   3895     26    594    -30       C  
ATOM   4370  CG  LEU C 118      77.627 -13.835   2.698  1.00 32.26           C  
ANISOU 4370  CG  LEU C 118     5329   2717   4210     85    567    -45       C  
ATOM   4371  CD1 LEU C 118      77.062 -13.350   4.019  1.00 30.80           C  
ANISOU 4371  CD1 LEU C 118     5175   2582   3947     30    481     29       C  
ATOM   4372  CD2 LEU C 118      79.048 -14.473   2.879  1.00 29.76           C  
ANISOU 4372  CD2 LEU C 118     4930   2331   4048    234    513    -88       C  
ATOM   4373  N   LEU C 119      75.009 -16.073  -0.544  1.00 31.70           N  
ANISOU 4373  N   LEU C 119     5713   2437   3894   -141    690    -77       N  
ATOM   4374  CA  LEU C 119      74.036 -16.996  -1.110  1.00 30.44           C  
ANISOU 4374  CA  LEU C 119     5726   2187   3654   -247    645    -62       C  
ATOM   4375  C   LEU C 119      74.664 -17.818  -2.224  1.00 36.54           C  
ANISOU 4375  C   LEU C 119     6659   2819   4408   -186    707   -150       C  
ATOM   4376  O   LEU C 119      74.393 -19.016  -2.340  1.00 35.95           O  
ANISOU 4376  O   LEU C 119     6762   2602   4296   -210    658   -151       O  
ATOM   4377  CB  LEU C 119      72.803 -16.228  -1.612  1.00 29.56           C  
ANISOU 4377  CB  LEU C 119     5585   2167   3479   -387    620    -26       C  
ATOM   4378  CG  LEU C 119      71.562 -17.056  -1.962  1.00 31.46           C  
ANISOU 4378  CG  LEU C 119     5948   2342   3663   -539    527     12       C  
ATOM   4379  CD1 LEU C 119      70.933 -17.706  -0.724  1.00 29.37           C  
ANISOU 4379  CD1 LEU C 119     5669   2066   3424   -608    474     98       C  
ATOM   4380  CD2 LEU C 119      70.565 -16.212  -2.691  1.00 31.30           C  
ANISOU 4380  CD2 LEU C 119     5877   2407   3609   -641    483     30       C  
ATOM   4381  N   MET C 120      75.544 -17.201  -3.007  1.00 34.67           N  
ANISOU 4381  N   MET C 120     6375   2605   4194   -107    832   -228       N  
ATOM   4382  CA  MET C 120      76.288 -17.867  -4.090  1.00 35.36           C  
ANISOU 4382  CA  MET C 120     6612   2559   4264    -26    952   -327       C  
ATOM   4383  C   MET C 120      77.164 -18.998  -3.504  1.00 39.03           C  
ANISOU 4383  C   MET C 120     7093   2901   4837    131    950   -351       C  
ATOM   4384  O   MET C 120      77.234 -20.080  -4.063  1.00 37.73           O  
ANISOU 4384  O   MET C 120     7138   2569   4628    167    974   -399       O  
ATOM   4385  CB  MET C 120      77.161 -16.806  -4.756  1.00 38.45           C  
ANISOU 4385  CB  MET C 120     6894   3027   4689     26   1120   -391       C  
ATOM   4386  CG  MET C 120      77.914 -17.243  -5.992  1.00 42.92           C  
ANISOU 4386  CG  MET C 120     7610   3472   5227    103   1310   -501       C  
ATOM   4387  SD  MET C 120      78.770 -15.762  -6.615  1.00 47.14           S  
ANISOU 4387  SD  MET C 120     7992   4122   5797    109   1517   -548       S  
ATOM   4388  CE  MET C 120      79.889 -15.504  -5.337  1.00 43.85           C  
ANISOU 4388  CE  MET C 120     7229   3797   5634    240   1505   -533       C  
ATOM   4389  N   LYS C 121      77.795 -18.745  -2.352  1.00 36.90           N  
ANISOU 4389  N   LYS C 121     6623   2698   4698    224    898   -312       N  
ATOM   4390  CA  LYS C 121      78.654 -19.700  -1.656  1.00 35.88           C  
ANISOU 4390  CA  LYS C 121     6483   2459   4690    391    848   -318       C  
ATOM   4391  C   LYS C 121      77.838 -20.701  -0.823  1.00 39.06           C  
ANISOU 4391  C   LYS C 121     7062   2758   5019    331    683   -233       C  
ATOM   4392  O   LYS C 121      78.180 -21.878  -0.772  1.00 37.53           O  
ANISOU 4392  O   LYS C 121     7019   2391   4850    433    653   -251       O  
ATOM   4393  CB  LYS C 121      79.597 -18.942  -0.712  1.00 36.56           C  
ANISOU 4393  CB  LYS C 121     6297   2659   4933    490    806   -299       C  
ATOM   4394  CG  LYS C 121      80.628 -18.055  -1.379  1.00 34.29           C  
ANISOU 4394  CG  LYS C 121     5804   2456   4770    559    972   -381       C  
ATOM   4395  CD  LYS C 121      81.397 -17.328  -0.304  1.00 47.21           C  
ANISOU 4395  CD  LYS C 121     7183   4196   6559    617    871   -349       C  
ATOM   4396  CE  LYS C 121      82.557 -18.091   0.281  1.00 62.94           C  
ANISOU 4396  CE  LYS C 121     9057   6102   8756    823    800   -372       C  
ATOM   4397  NZ  LYS C 121      83.359 -17.239   1.194  1.00 70.98           N  
ANISOU 4397  NZ  LYS C 121     9833   7222   9914    853    656   -337       N  
ATOM   4398  N   PHE C 122      76.816 -20.202  -0.100  1.00 34.97           N  
ANISOU 4398  N   PHE C 122     6522   2342   4422    174    593   -140       N  
ATOM   4399  CA  PHE C 122      76.000 -20.971   0.834  1.00 34.06           C  
ANISOU 4399  CA  PHE C 122     6549   2154   4238     84    468    -46       C  
ATOM   4400  C   PHE C 122      74.503 -20.792   0.505  1.00 38.67           C  
ANISOU 4400  C   PHE C 122     7192   2791   4709   -143    462      1       C  
ATOM   4401  O   PHE C 122      73.822 -19.986   1.148  1.00 38.45           O  
ANISOU 4401  O   PHE C 122     7046   2900   4663   -238    447     68       O  
ATOM   4402  CB  PHE C 122      76.363 -20.557   2.274  1.00 34.87           C  
ANISOU 4402  CB  PHE C 122     6543   2323   4385    136    376     25       C  
ATOM   4403  CG  PHE C 122      77.852 -20.591   2.559  1.00 35.99           C  
ANISOU 4403  CG  PHE C 122     6568   2435   4673    354    344    -20       C  
ATOM   4404  CD1 PHE C 122      78.570 -19.412   2.731  1.00 38.15           C  
ANISOU 4404  CD1 PHE C 122     6601   2856   5039    406    363    -46       C  
ATOM   4405  CD2 PHE C 122      78.545 -21.807   2.615  1.00 38.08           C  
ANISOU 4405  CD2 PHE C 122     6954   2513   5002    510    287    -40       C  
ATOM   4406  CE1 PHE C 122      79.947 -19.442   2.994  1.00 39.14           C  
ANISOU 4406  CE1 PHE C 122     6575   2960   5337    593    316    -86       C  
ATOM   4407  CE2 PHE C 122      79.919 -21.838   2.896  1.00 40.34           C  
ANISOU 4407  CE2 PHE C 122     7087   2775   5465    727    240    -79       C  
ATOM   4408  CZ  PHE C 122      80.611 -20.654   3.088  1.00 38.17           C  
ANISOU 4408  CZ  PHE C 122     6538   2664   5299    759    250   -101       C  
ATOM   4409  N   PRO C 123      73.988 -21.521  -0.532  1.00 34.65           N  
ANISOU 4409  N   PRO C 123     6866   2168   4131   -229    468    -37       N  
ATOM   4410  CA  PRO C 123      72.593 -21.301  -0.979  1.00 33.19           C  
ANISOU 4410  CA  PRO C 123     6700   2041   3870   -447    430      3       C  
ATOM   4411  C   PRO C 123      71.504 -21.627   0.021  1.00 34.47           C  
ANISOU 4411  C   PRO C 123     6862   2217   4017   -607    359    114       C  
ATOM   4412  O   PRO C 123      70.381 -21.186  -0.160  1.00 32.66           O  
ANISOU 4412  O   PRO C 123     6547   2085   3777   -768    338    157       O  
ATOM   4413  CB  PRO C 123      72.474 -22.189  -2.232  1.00 34.38           C  
ANISOU 4413  CB  PRO C 123     7093   2025   3945   -492    422    -69       C  
ATOM   4414  CG  PRO C 123      73.872 -22.441  -2.656  1.00 38.43           C  
ANISOU 4414  CG  PRO C 123     7660   2447   4497   -274    525   -167       C  
ATOM   4415  CD  PRO C 123      74.670 -22.502  -1.410  1.00 34.82           C  
ANISOU 4415  CD  PRO C 123     7081   2004   4145   -125    511   -127       C  
ATOM   4416  N   PHE C 124      71.822 -22.421   1.041  1.00 31.65           N  
ANISOU 4416  N   PHE C 124     6609   1754   3663   -562    326    163       N  
ATOM   4417  CA  PHE C 124      70.837 -22.883   2.013  1.00 30.60           C  
ANISOU 4417  CA  PHE C 124     6530   1601   3496   -727    291    271       C  
ATOM   4418  C   PHE C 124      70.648 -21.935   3.218  1.00 34.26           C  
ANISOU 4418  C   PHE C 124     6825   2223   3972   -724    333    342       C  
ATOM   4419  O   PHE C 124      69.847 -22.241   4.090  1.00 35.50           O  
ANISOU 4419  O   PHE C 124     7029   2366   4092   -859    346    432       O  
ATOM   4420  CB  PHE C 124      71.165 -24.325   2.444  1.00 31.78           C  
ANISOU 4420  CB  PHE C 124     6954   1515   3605   -706    230    295       C  
ATOM   4421  CG  PHE C 124      70.874 -25.333   1.359  1.00 32.19           C  
ANISOU 4421  CG  PHE C 124     7216   1395   3618   -791    191    244       C  
ATOM   4422  CD1 PHE C 124      71.763 -25.521   0.297  1.00 34.96           C  
ANISOU 4422  CD1 PHE C 124     7645   1661   3975   -633    212    128       C  
ATOM   4423  CD2 PHE C 124      69.707 -26.085   1.381  1.00 32.93           C  
ANISOU 4423  CD2 PHE C 124     7439   1404   3668  -1040    145    306       C  
ATOM   4424  CE1 PHE C 124      71.479 -26.442  -0.730  1.00 34.78           C  
ANISOU 4424  CE1 PHE C 124     7868   1460   3887   -715    180     71       C  
ATOM   4425  CE2 PHE C 124      69.432 -27.019   0.360  1.00 34.35           C  
ANISOU 4425  CE2 PHE C 124     7847   1405   3798  -1137     84    252       C  
ATOM   4426  CZ  PHE C 124      70.323 -27.196  -0.681  1.00 32.00           C  
ANISOU 4426  CZ  PHE C 124     7666   1013   3479   -968     98    133       C  
ATOM   4427  N   ARG C 125      71.343 -20.781   3.240  1.00 29.12           N  
ANISOU 4427  N   ARG C 125     5994   1709   3362   -589    369    300       N  
ATOM   4428  CA  ARG C 125      71.270 -19.740   4.283  1.00 29.05           C  
ANISOU 4428  CA  ARG C 125     5849   1839   3348   -572    408    347       C  
ATOM   4429  C   ARG C 125      71.465 -20.282   5.702  1.00 34.85           C  
ANISOU 4429  C   ARG C 125     6732   2488   4022   -557    371    424       C  
ATOM   4430  O   ARG C 125      70.749 -19.882   6.613  1.00 34.88           O  
ANISOU 4430  O   ARG C 125     6724   2556   3974   -649    429    494       O  
ATOM   4431  CB  ARG C 125      69.968 -18.915   4.166  1.00 25.65           C  
ANISOU 4431  CB  ARG C 125     5266   1555   2924   -722    478    384       C  
ATOM   4432  CG  ARG C 125      69.875 -18.111   2.862  1.00 25.14           C  
ANISOU 4432  CG  ARG C 125     5066   1583   2904   -713    486    316       C  
ATOM   4433  CD  ARG C 125      68.580 -17.327   2.805  1.00 20.15           C  
ANISOU 4433  CD  ARG C 125     4269   1085   2302   -831    527    361       C  
ATOM   4434  NE  ARG C 125      68.516 -16.402   1.677  1.00 26.48           N  
ANISOU 4434  NE  ARG C 125     4961   1969   3129   -804    512    308       N  
ATOM   4435  CZ  ARG C 125      69.148 -15.236   1.614  1.00 30.80           C  
ANISOU 4435  CZ  ARG C 125     5418   2603   3681   -688    553    269       C  
ATOM   4436  NH1 ARG C 125      69.939 -14.848   2.603  1.00 24.26           N  
ANISOU 4436  NH1 ARG C 125     4580   1795   2843   -589    595    270       N  
ATOM   4437  NH2 ARG C 125      69.006 -14.457   0.556  1.00 21.74           N  
ANISOU 4437  NH2 ARG C 125     4214   1507   2539   -680    538    231       N  
ATOM   4438  N   GLU C 126      72.427 -21.203   5.890  1.00 32.24           N  
ANISOU 4438  N   GLU C 126     6559   1997   3692   -434    278    412       N  
ATOM   4439  CA  GLU C 126      72.656 -21.836   7.189  1.00 31.89           C  
ANISOU 4439  CA  GLU C 126     6713   1833   3570   -413    204    493       C  
ATOM   4440  C   GLU C 126      73.341 -20.934   8.208  1.00 37.75           C  
ANISOU 4440  C   GLU C 126     7395   2654   4293   -307    158    508       C  
ATOM   4441  O   GLU C 126      73.101 -21.129   9.390  1.00 38.91           O  
ANISOU 4441  O   GLU C 126     7713   2744   4327   -355    133    591       O  
ATOM   4442  CB  GLU C 126      73.403 -23.179   7.042  1.00 32.92           C  
ANISOU 4442  CB  GLU C 126     7055   1739   3712   -304     94    483       C  
ATOM   4443  CG  GLU C 126      72.543 -24.285   6.444  1.00 31.04           C  
ANISOU 4443  CG  GLU C 126     6997   1364   3433   -463    119    503       C  
ATOM   4444  CD  GLU C 126      73.292 -25.425   5.787  1.00 54.18           C  
ANISOU 4444  CD  GLU C 126    10101   4085   6399   -335     45    447       C  
ATOM   4445  OE1 GLU C 126      73.207 -26.578   6.283  1.00 48.95           O  
ANISOU 4445  OE1 GLU C 126     9717   3213   5670   -361    -25    507       O  
ATOM   4446  OE2 GLU C 126      73.945 -25.162   4.752  1.00 47.05           O  
ANISOU 4446  OE2 GLU C 126     9074   3216   5585   -211     73    341       O  
ATOM   4447  N   HIS C 127      74.180 -19.967   7.779  1.00 35.39           N  
ANISOU 4447  N   HIS C 127     6886   2471   4091   -180    145    429       N  
ATOM   4448  CA  HIS C 127      74.886 -19.091   8.712  1.00 35.81           C  
ANISOU 4448  CA  HIS C 127     6887   2589   4133    -96     72    436       C  
ATOM   4449  C   HIS C 127      73.930 -18.021   9.239  1.00 37.02           C  
ANISOU 4449  C   HIS C 127     6994   2878   4194   -225    191    471       C  
ATOM   4450  O   HIS C 127      73.055 -17.564   8.491  1.00 35.03           O  
ANISOU 4450  O   HIS C 127     6613   2729   3968   -319    322    452       O  
ATOM   4451  CB  HIS C 127      76.168 -18.487   8.086  1.00 37.90           C  
ANISOU 4451  CB  HIS C 127     6934   2916   4552     63     21    342       C  
ATOM   4452  CG  HIS C 127      77.128 -17.894   9.100  1.00 42.90           C  
ANISOU 4452  CG  HIS C 127     7539   3564   5198    158   -127    350       C  
ATOM   4453  ND1 HIS C 127      76.964 -16.599   9.597  1.00 44.57           N  
ANISOU 4453  ND1 HIS C 127     7685   3900   5351     97    -98    353       N  
ATOM   4454  CD2 HIS C 127      78.216 -18.449   9.700  1.00 45.30           C  
ANISOU 4454  CD2 HIS C 127     7888   3759   5566    305   -325    358       C  
ATOM   4455  CE1 HIS C 127      77.953 -16.412  10.460  1.00 43.89           C  
ANISOU 4455  CE1 HIS C 127     7617   3777   5282    189   -285    360       C  
ATOM   4456  NE2 HIS C 127      78.739 -17.486  10.552  1.00 44.53           N  
ANISOU 4456  NE2 HIS C 127     7746   3724   5448    318   -438    366       N  
ATOM   4457  N   ILE C 128      74.064 -17.661  10.539  1.00 33.35           N  
ANISOU 4457  N   ILE C 128     6657   2398   3616   -223    138    524       N  
ATOM   4458  CA  ILE C 128      73.224 -16.662  11.218  1.00 34.44           C  
ANISOU 4458  CA  ILE C 128     6797   2640   3650   -320    268    553       C  
ATOM   4459  C   ILE C 128      73.160 -15.306  10.455  1.00 36.05           C  
ANISOU 4459  C   ILE C 128     6743   3012   3943   -304    355    478       C  
ATOM   4460  O   ILE C 128      72.088 -14.697  10.399  1.00 34.41           O  
ANISOU 4460  O   ILE C 128     6469   2894   3709   -394    514    492       O  
ATOM   4461  CB  ILE C 128      73.637 -16.484  12.717  1.00 39.64           C  
ANISOU 4461  CB  ILE C 128     7687   3225   4148   -296    171    604       C  
ATOM   4462  CG1 ILE C 128      72.551 -15.743  13.539  1.00 40.18           C  
ANISOU 4462  CG1 ILE C 128     7847   3353   4067   -414    362    647       C  
ATOM   4463  CG2 ILE C 128      75.018 -15.811  12.869  1.00 42.91           C  
ANISOU 4463  CG2 ILE C 128     8017   3660   4627   -158    -21    546       C  
ATOM   4464  CD1 ILE C 128      71.154 -16.447  13.600  1.00 50.38           C  
ANISOU 4464  CD1 ILE C 128     9217   4617   5306   -575    562    719       C  
ATOM   4465  N   LEU C 129      74.290 -14.891   9.817  1.00 31.82           N  
ANISOU 4465  N   LEU C 129     6057   2507   3527   -191    260    403       N  
ATOM   4466  CA  LEU C 129      74.416 -13.655   9.047  1.00 31.66           C  
ANISOU 4466  CA  LEU C 129     5828   2617   3585   -176    327    334       C  
ATOM   4467  C   LEU C 129      73.562 -13.658   7.778  1.00 32.83           C  
ANISOU 4467  C   LEU C 129     5857   2826   3790   -239    453    312       C  
ATOM   4468  O   LEU C 129      73.361 -12.600   7.189  1.00 29.22           O  
ANISOU 4468  O   LEU C 129     5270   2468   3364   -247    525    275       O  
ATOM   4469  CB  LEU C 129      75.893 -13.344   8.691  1.00 32.31           C  
ANISOU 4469  CB  LEU C 129     5782   2701   3792    -61    209    264       C  
ATOM   4470  CG  LEU C 129      76.912 -13.080   9.817  1.00 38.27           C  
ANISOU 4470  CG  LEU C 129     6595   3416   4532      4     31    271       C  
ATOM   4471  CD1 LEU C 129      78.061 -12.262   9.297  1.00 39.46           C  
ANISOU 4471  CD1 LEU C 129     6532   3628   4834     64    -19    193       C  
ATOM   4472  CD2 LEU C 129      76.303 -12.343  11.024  1.00 40.11           C  
ANISOU 4472  CD2 LEU C 129     6991   3661   4587    -68     47    316       C  
ATOM   4473  N   GLN C 130      73.056 -14.840   7.381  1.00 29.62           N  
ANISOU 4473  N   GLN C 130     5524   2345   3387   -290    461    340       N  
ATOM   4474  CA  GLN C 130      72.225 -15.075   6.193  1.00 29.01           C  
ANISOU 4474  CA  GLN C 130     5379   2293   3352   -368    530    326       C  
ATOM   4475  C   GLN C 130      70.715 -15.123   6.505  1.00 31.07           C  
ANISOU 4475  C   GLN C 130     5643   2592   3571   -511    623    395       C  
ATOM   4476  O   GLN C 130      69.908 -15.286   5.577  1.00 29.22           O  
ANISOU 4476  O   GLN C 130     5338   2382   3382   -593    647    392       O  
ATOM   4477  CB  GLN C 130      72.635 -16.405   5.541  1.00 29.87           C  
ANISOU 4477  CB  GLN C 130     5585   2271   3492   -346    468    305       C  
ATOM   4478  CG  GLN C 130      73.966 -16.356   4.828  1.00 31.65           C  
ANISOU 4478  CG  GLN C 130     5751   2471   3804   -204    428    221       C  
ATOM   4479  CD  GLN C 130      74.187 -17.642   4.101  1.00 32.12           C  
ANISOU 4479  CD  GLN C 130     5926   2393   3887   -179    404    193       C  
ATOM   4480  OE1 GLN C 130      74.631 -18.637   4.679  1.00 31.00           O  
ANISOU 4480  OE1 GLN C 130     5914   2120   3743   -116    324    216       O  
ATOM   4481  NE2 GLN C 130      73.867 -17.658   2.826  1.00 21.64           N  
ANISOU 4481  NE2 GLN C 130     4583   1072   2565   -225    463    143       N  
ATOM   4482  N   LYS C 131      70.346 -15.007   7.804  1.00 26.97           N  
ANISOU 4482  N   LYS C 131     5209   2069   2968   -545    672    457       N  
ATOM   4483  CA  LYS C 131      68.959 -15.047   8.277  1.00 27.00           C  
ANISOU 4483  CA  LYS C 131     5201   2109   2948   -677    805    525       C  
ATOM   4484  C   LYS C 131      68.274 -13.703   8.158  1.00 33.81           C  
ANISOU 4484  C   LYS C 131     5885   3112   3850   -668    915    510       C  
ATOM   4485  O   LYS C 131      68.923 -12.656   8.304  1.00 32.86           O  
ANISOU 4485  O   LYS C 131     5737   3037   3710   -566    902    465       O  
ATOM   4486  CB  LYS C 131      68.861 -15.564   9.725  1.00 28.72           C  
ANISOU 4486  CB  LYS C 131     5636   2240   3036   -723    848    598       C  
ATOM   4487  CG  LYS C 131      69.538 -16.929  10.007  1.00 31.88           C  
ANISOU 4487  CG  LYS C 131     6260   2471   3381   -715    720    627       C  
ATOM   4488  CD  LYS C 131      68.996 -18.118   9.202  1.00 30.81           C  
ANISOU 4488  CD  LYS C 131     6147   2256   3303   -825    704    646       C  
ATOM   4489  CE  LYS C 131      69.729 -19.359   9.609  1.00 32.96           C  
ANISOU 4489  CE  LYS C 131     6675   2340   3508   -788    579    674       C  
ATOM   4490  NZ  LYS C 131      69.185 -20.560   8.955  1.00 44.56           N  
ANISOU 4490  NZ  LYS C 131     8222   3699   5010   -904    562    693       N  
ATOM   4491  N   LYS C 132      66.937 -13.739   7.925  1.00 32.06           N  
ANISOU 4491  N   LYS C 132     5538   2948   3697   -777   1017    550       N  
ATOM   4492  CA  LYS C 132      66.042 -12.574   7.788  1.00 31.60           C  
ANISOU 4492  CA  LYS C 132     5285   3012   3710   -762   1127    547       C  
ATOM   4493  C   LYS C 132      66.144 -11.667   9.052  1.00 36.79           C  
ANISOU 4493  C   LYS C 132     6024   3688   4267   -693   1256    552       C  
ATOM   4494  O   LYS C 132      66.159 -10.435   8.941  1.00 36.00           O  
ANISOU 4494  O   LYS C 132     5839   3655   4182   -600   1290    512       O  
ATOM   4495  CB  LYS C 132      64.613 -13.097   7.586  1.00 33.26           C  
ANISOU 4495  CB  LYS C 132     5352   3257   4029   -908   1207    606       C  
ATOM   4496  CG  LYS C 132      63.545 -12.036   7.437  1.00 49.69           C  
ANISOU 4496  CG  LYS C 132     7191   5460   6230   -885   1314    613       C  
ATOM   4497  CD  LYS C 132      62.145 -12.583   7.701  1.00 64.72           C  
ANISOU 4497  CD  LYS C 132     8942   7397   8252  -1036   1446    684       C  
ATOM   4498  CE  LYS C 132      61.810 -12.783   9.159  1.00 78.60           C  
ANISOU 4498  CE  LYS C 132    10817   9127   9921  -1082   1679    734       C  
ATOM   4499  NZ  LYS C 132      60.489 -13.445   9.316  1.00 92.37           N  
ANISOU 4499  NZ  LYS C 132    12388  10902  11806  -1255   1829    805       N  
ATOM   4500  N   GLU C 133      66.274 -12.309  10.240  1.00 33.91           N  
ANISOU 4500  N   GLU C 133     5870   3240   3776   -739   1314    598       N  
ATOM   4501  CA  GLU C 133      66.394 -11.667  11.557  1.00 32.60           C  
ANISOU 4501  CA  GLU C 133     5871   3054   3464   -696   1429    607       C  
ATOM   4502  C   GLU C 133      67.625 -10.793  11.637  1.00 35.21           C  
ANISOU 4502  C   GLU C 133     6275   3375   3728   -567   1296    540       C  
ATOM   4503  O   GLU C 133      67.517  -9.695  12.162  1.00 34.88           O  
ANISOU 4503  O   GLU C 133     6257   3365   3631   -509   1388    515       O  
ATOM   4504  CB  GLU C 133      66.388 -12.715  12.692  1.00 33.11           C  
ANISOU 4504  CB  GLU C 133     6204   2999   3378   -787   1477    677       C  
ATOM   4505  CG  GLU C 133      65.078 -13.477  12.820  1.00 40.28           C  
ANISOU 4505  CG  GLU C 133     7048   3912   4345   -947   1661    750       C  
ATOM   4506  CD  GLU C 133      64.755 -14.559  11.800  1.00 49.88           C  
ANISOU 4506  CD  GLU C 133     8147   5110   5696  -1053   1558    771       C  
ATOM   4507  OE1 GLU C 133      65.655 -14.937  11.024  1.00 34.80           O  
ANISOU 4507  OE1 GLU C 133     6263   3156   3804   -995   1345    731       O  
ATOM   4508  OE2 GLU C 133      63.600 -15.038  11.784  1.00 44.05           O  
ANISOU 4508  OE2 GLU C 133     7292   4396   5049  -1202   1698    825       O  
ATOM   4509  N   PHE C 134      68.785 -11.251  11.091  1.00 31.67           N  
ANISOU 4509  N   PHE C 134     5853   2880   3302   -523   1089    508       N  
ATOM   4510  CA  PHE C 134      70.017 -10.438  11.059  1.00 31.36           C  
ANISOU 4510  CA  PHE C 134     5829   2840   3244   -420    955    443       C  
ATOM   4511  C   PHE C 134      69.861  -9.234  10.115  1.00 34.39           C  
ANISOU 4511  C   PHE C 134     6015   3323   3727   -372    992    387       C  
ATOM   4512  O   PHE C 134      70.357  -8.156  10.429  1.00 34.56           O  
ANISOU 4512  O   PHE C 134     6068   3357   3706   -316    980    345       O  
ATOM   4513  CB  PHE C 134      71.252 -11.280  10.679  1.00 33.42           C  
ANISOU 4513  CB  PHE C 134     6119   3031   3548   -378    755    423       C  
ATOM   4514  CG  PHE C 134      72.543 -10.496  10.650  1.00 34.92           C  
ANISOU 4514  CG  PHE C 134     6279   3227   3761   -291    621    359       C  
ATOM   4515  CD1 PHE C 134      73.218 -10.192  11.828  1.00 39.57           C  
ANISOU 4515  CD1 PHE C 134     7040   3758   4237   -264    522    363       C  
ATOM   4516  CD2 PHE C 134      73.080 -10.051   9.447  1.00 36.22           C  
ANISOU 4516  CD2 PHE C 134     6256   3448   4057   -251    592    295       C  
ATOM   4517  CE1 PHE C 134      74.385  -9.410  11.803  1.00 40.42           C  
ANISOU 4517  CE1 PHE C 134     7092   3876   4391   -209    384    304       C  
ATOM   4518  CE2 PHE C 134      74.276  -9.327   9.418  1.00 39.10           C  
ANISOU 4518  CE2 PHE C 134     6569   3820   4466   -196    489    239       C  
ATOM   4519  CZ  PHE C 134      74.914  -8.998  10.597  1.00 37.78           C  
ANISOU 4519  CZ  PHE C 134     6535   3606   4214   -179    378    243       C  
ATOM   4520  N   ALA C 135      69.170  -9.416   8.972  1.00 29.55           N  
ANISOU 4520  N   ALA C 135     5227   2766   3234   -403   1022    388       N  
ATOM   4521  CA  ALA C 135      68.934  -8.340   8.021  1.00 29.41           C  
ANISOU 4521  CA  ALA C 135     5053   2823   3296   -359   1040    347       C  
ATOM   4522  C   ALA C 135      68.084  -7.204   8.637  1.00 31.87           C  
ANISOU 4522  C   ALA C 135     5344   3180   3583   -323   1187    354       C  
ATOM   4523  O   ALA C 135      68.326  -6.034   8.330  1.00 28.62           O  
ANISOU 4523  O   ALA C 135     4904   2792   3179   -255   1184    311       O  
ATOM   4524  CB  ALA C 135      68.274  -8.874   6.756  1.00 30.06           C  
ANISOU 4524  CB  ALA C 135     4997   2935   3488   -409   1010    357       C  
ATOM   4525  N   ILE C 136      67.097  -7.561   9.484  1.00 30.53           N  
ANISOU 4525  N   ILE C 136     5198   3013   3388   -368   1334    407       N  
ATOM   4526  CA  ILE C 136      66.221  -6.613  10.179  1.00 31.85           C  
ANISOU 4526  CA  ILE C 136     5353   3211   3537   -321   1523    413       C  
ATOM   4527  C   ILE C 136      67.077  -5.723  11.085  1.00 36.67           C  
ANISOU 4527  C   ILE C 136     6178   3765   3991   -255   1519    368       C  
ATOM   4528  O   ILE C 136      66.912  -4.507  11.047  1.00 37.89           O  
ANISOU 4528  O   ILE C 136     6316   3933   4146   -173   1581    330       O  
ATOM   4529  CB  ILE C 136      65.082  -7.342  10.962  1.00 35.55           C  
ANISOU 4529  CB  ILE C 136     5814   3684   4010   -404   1716    480       C  
ATOM   4530  CG1 ILE C 136      64.071  -7.984   9.981  1.00 36.42           C  
ANISOU 4530  CG1 ILE C 136     5666   3860   4311   -482   1709    520       C  
ATOM   4531  CG2 ILE C 136      64.367  -6.396  11.944  1.00 35.55           C  
ANISOU 4531  CG2 ILE C 136     5860   3691   3956   -339   1956    475       C  
ATOM   4532  CD1 ILE C 136      63.258  -9.182  10.555  1.00 39.86           C  
ANISOU 4532  CD1 ILE C 136     6108   4277   4762   -628   1836    594       C  
ATOM   4533  N   LEU C 137      68.016  -6.321  11.852  1.00 33.24           N  
ANISOU 4533  N   LEU C 137     5952   3252   3427   -289   1418    371       N  
ATOM   4534  CA  LEU C 137      68.930  -5.591  12.743  1.00 32.99           C  
ANISOU 4534  CA  LEU C 137     6142   3151   3241   -250   1354    331       C  
ATOM   4535  C   LEU C 137      69.909  -4.733  11.988  1.00 35.62           C  
ANISOU 4535  C   LEU C 137     6403   3499   3633   -203   1204    266       C  
ATOM   4536  O   LEU C 137      70.257  -3.668  12.462  1.00 37.09           O  
ANISOU 4536  O   LEU C 137     6707   3650   3736   -168   1205    222       O  
ATOM   4537  CB  LEU C 137      69.678  -6.525  13.705  1.00 33.38           C  
ANISOU 4537  CB  LEU C 137     6424   3105   3152   -298   1235    362       C  
ATOM   4538  CG  LEU C 137      68.841  -7.371  14.667  1.00 38.40           C  
ANISOU 4538  CG  LEU C 137     7225   3692   3674   -367   1393    433       C  
ATOM   4539  CD1 LEU C 137      69.727  -8.117  15.629  1.00 38.29           C  
ANISOU 4539  CD1 LEU C 137     7502   3557   3490   -395   1231    461       C  
ATOM   4540  CD2 LEU C 137      67.835  -6.523  15.454  1.00 41.59           C  
ANISOU 4540  CD2 LEU C 137     7717   4101   3986   -349   1666    430       C  
ATOM   4541  N   ILE C 138      70.338  -5.172  10.809  1.00 31.30           N  
ANISOU 4541  N   ILE C 138     5681   2990   3221   -212   1092    256       N  
ATOM   4542  CA  ILE C 138      71.228  -4.420   9.918  1.00 30.24           C  
ANISOU 4542  CA  ILE C 138     5458   2873   3161   -186    987    198       C  
ATOM   4543  C   ILE C 138      70.484  -3.214   9.353  1.00 35.59           C  
ANISOU 4543  C   ILE C 138     6060   3589   3875   -139   1095    179       C  
ATOM   4544  O   ILE C 138      71.049  -2.117   9.299  1.00 35.41           O  
ANISOU 4544  O   ILE C 138     6087   3541   3827   -117   1065    133       O  
ATOM   4545  CB  ILE C 138      71.823  -5.352   8.810  1.00 32.22           C  
ANISOU 4545  CB  ILE C 138     5573   3140   3530   -206    883    194       C  
ATOM   4546  CG1 ILE C 138      73.009  -6.187   9.363  1.00 31.91           C  
ANISOU 4546  CG1 ILE C 138     5608   3042   3476   -212    731    190       C  
ATOM   4547  CG2 ILE C 138      72.211  -4.608   7.524  1.00 32.96           C  
ANISOU 4547  CG2 ILE C 138     5545   3268   3712   -193    867    147       C  
ATOM   4548  CD1 ILE C 138      74.240  -5.430   9.943  1.00 37.45           C  
ANISOU 4548  CD1 ILE C 138     6378   3705   4145   -202    605    145       C  
ATOM   4549  N   SER C 139      69.221  -3.422   8.930  1.00 32.70           N  
ANISOU 4549  N   SER C 139     5571   3273   3579   -128   1206    218       N  
ATOM   4550  CA  SER C 139      68.380  -2.378   8.366  1.00 32.93           C  
ANISOU 4550  CA  SER C 139     5509   3334   3668    -60   1289    213       C  
ATOM   4551  C   SER C 139      68.171  -1.263   9.385  1.00 40.00           C  
ANISOU 4551  C   SER C 139     6551   4183   4463      7   1404    188       C  
ATOM   4552  O   SER C 139      68.346  -0.100   9.040  1.00 39.36           O  
ANISOU 4552  O   SER C 139     6502   4074   4379     63   1396    150       O  
ATOM   4553  CB  SER C 139      67.065  -2.952   7.858  1.00 34.51           C  
ANISOU 4553  CB  SER C 139     5529   3597   3987    -67   1357    266       C  
ATOM   4554  OG  SER C 139      67.309  -3.719   6.694  1.00 40.40           O  
ANISOU 4554  OG  SER C 139     6177   4364   4809   -123   1228    274       O  
ATOM   4555  N   LEU C 140      67.909  -1.623  10.655  1.00 39.25           N  
ANISOU 4555  N   LEU C 140     6593   4057   4262     -8   1508    205       N  
ATOM   4556  CA  LEU C 140      67.763  -0.660  11.748  1.00 39.87           C  
ANISOU 4556  CA  LEU C 140     6877   4068   4204     49   1633    173       C  
ATOM   4557  C   LEU C 140      69.057   0.131  11.964  1.00 39.96           C  
ANISOU 4557  C   LEU C 140     7071   4003   4111     35   1482    112       C  
ATOM   4558  O   LEU C 140      69.014   1.344  12.113  1.00 39.23           O  
ANISOU 4558  O   LEU C 140     7082   3855   3968     97   1533     68       O  
ATOM   4559  CB  LEU C 140      67.379  -1.387  13.025  1.00 41.44           C  
ANISOU 4559  CB  LEU C 140     7236   4233   4275      9   1762    206       C  
ATOM   4560  CG  LEU C 140      66.195  -0.776  13.740  1.00 50.07           C  
ANISOU 4560  CG  LEU C 140     8404   5302   5317     90   2035    200       C  
ATOM   4561  CD1 LEU C 140      64.867  -1.321  13.174  1.00 51.46           C  
ANISOU 4561  CD1 LEU C 140     8279   5577   5696    119   2204    251       C  
ATOM   4562  CD2 LEU C 140      66.301  -1.001  15.245  1.00 55.49           C  
ANISOU 4562  CD2 LEU C 140     9411   5898   5773     44   2140    206       C  
ATOM   4563  N   ALA C 141      70.203  -0.561  11.937  1.00 34.41           N  
ANISOU 4563  N   ALA C 141     6388   3290   3396    -45   1290    109       N  
ATOM   4564  CA  ALA C 141      71.535   0.004  12.084  1.00 33.10           C  
ANISOU 4564  CA  ALA C 141     6330   3066   3180    -87   1113     57       C  
ATOM   4565  C   ALA C 141      71.871   0.957  10.914  1.00 37.41           C  
ANISOU 4565  C   ALA C 141     6755   3627   3832    -77   1076     20       C  
ATOM   4566  O   ALA C 141      72.602   1.931  11.105  1.00 38.04           O  
ANISOU 4566  O   ALA C 141     6953   3641   3860   -103   1006    -29       O  
ATOM   4567  CB  ALA C 141      72.556  -1.127  12.180  1.00 33.36           C  
ANISOU 4567  CB  ALA C 141     6336   3101   3239   -154    927     74       C  
ATOM   4568  N   VAL C 142      71.318   0.698   9.713  1.00 33.25           N  
ANISOU 4568  N   VAL C 142     6023   3172   3438    -51   1118     46       N  
ATOM   4569  CA  VAL C 142      71.502   1.565   8.536  1.00 31.60           C  
ANISOU 4569  CA  VAL C 142     5739   2963   3303    -41   1099     23       C  
ATOM   4570  C   VAL C 142      70.755   2.894   8.775  1.00 36.16           C  
ANISOU 4570  C   VAL C 142     6431   3482   3825     47   1210      6       C  
ATOM   4571  O   VAL C 142      71.345   3.953   8.577  1.00 36.33           O  
ANISOU 4571  O   VAL C 142     6556   3435   3814     30   1170    -35       O  
ATOM   4572  CB  VAL C 142      71.113   0.843   7.225  1.00 34.83           C  
ANISOU 4572  CB  VAL C 142     5953   3445   3837    -42   1090     57       C  
ATOM   4573  CG1 VAL C 142      70.960   1.817   6.052  1.00 34.65           C  
ANISOU 4573  CG1 VAL C 142     5907   3405   3855    -14   1094     48       C  
ATOM   4574  CG2 VAL C 142      72.134  -0.253   6.890  1.00 34.56           C  
ANISOU 4574  CG2 VAL C 142     5844   3435   3852   -118    984     52       C  
ATOM   4575  N   TRP C 143      69.504   2.839   9.284  1.00 32.16           N  
ANISOU 4575  N   TRP C 143     5915   2992   3314    137   1359     34       N  
ATOM   4576  CA  TRP C 143      68.721   4.036   9.604  1.00 32.53           C  
ANISOU 4576  CA  TRP C 143     6062   2974   3323    255   1491     15       C  
ATOM   4577  C   TRP C 143      69.370   4.865  10.726  1.00 35.48           C  
ANISOU 4577  C   TRP C 143     6727   3230   3524    239   1497    -45       C  
ATOM   4578  O   TRP C 143      69.436   6.080  10.599  1.00 33.52           O  
ANISOU 4578  O   TRP C 143     6606   2892   3238    289   1511    -83       O  
ATOM   4579  CB  TRP C 143      67.265   3.681   9.937  1.00 31.54           C  
ANISOU 4579  CB  TRP C 143     5819   2903   3264    354   1674     57       C  
ATOM   4580  CG  TRP C 143      66.466   3.262   8.740  1.00 32.55           C  
ANISOU 4580  CG  TRP C 143     5674   3120   3574    386   1644    109       C  
ATOM   4581  CD1 TRP C 143      66.158   1.990   8.367  1.00 35.20           C  
ANISOU 4581  CD1 TRP C 143     5827   3548   4001    315   1609    158       C  
ATOM   4582  CD2 TRP C 143      65.862   4.122   7.764  1.00 32.48           C  
ANISOU 4582  CD2 TRP C 143     5576   3098   3667    493   1622    118       C  
ATOM   4583  NE1 TRP C 143      65.394   2.002   7.226  1.00 34.09           N  
ANISOU 4583  NE1 TRP C 143     5484   3457   4011    360   1557    194       N  
ATOM   4584  CE2 TRP C 143      65.210   3.295   6.823  1.00 35.61           C  
ANISOU 4584  CE2 TRP C 143     5729   3588   4213    474   1553    174       C  
ATOM   4585  CE3 TRP C 143      65.759   5.523   7.624  1.00 33.94           C  
ANISOU 4585  CE3 TRP C 143     5885   3185   3826    609   1644     88       C  
ATOM   4586  CZ2 TRP C 143      64.463   3.816   5.754  1.00 35.35           C  
ANISOU 4586  CZ2 TRP C 143     5569   3559   4302    567   1483    204       C  
ATOM   4587  CZ3 TRP C 143      65.043   6.038   6.548  1.00 35.39           C  
ANISOU 4587  CZ3 TRP C 143     5946   3366   4133    712   1586    121       C  
ATOM   4588  CH2 TRP C 143      64.404   5.190   5.628  1.00 35.96           C  
ANISOU 4588  CH2 TRP C 143     5773   3539   4352    692   1496    180       C  
ATOM   4589  N   VAL C 144      69.899   4.205  11.788  1.00 33.11           N  
ANISOU 4589  N   VAL C 144     6558   2914   3108    162   1459    -51       N  
ATOM   4590  CA  VAL C 144      70.593   4.882  12.892  1.00 33.76           C  
ANISOU 4590  CA  VAL C 144     6949   2875   3005    121   1414   -107       C  
ATOM   4591  C   VAL C 144      71.873   5.566  12.410  1.00 40.23           C  
ANISOU 4591  C   VAL C 144     7805   3643   3838     21   1216   -151       C  
ATOM   4592  O   VAL C 144      72.015   6.759  12.627  1.00 40.79           O  
ANISOU 4592  O   VAL C 144     8076   3601   3821     29   1223   -201       O  
ATOM   4593  CB  VAL C 144      70.872   3.960  14.094  1.00 37.26           C  
ANISOU 4593  CB  VAL C 144     7545   3302   3311     57   1382    -93       C  
ATOM   4594  CG1 VAL C 144      71.593   4.712  15.214  1.00 37.16           C  
ANISOU 4594  CG1 VAL C 144     7887   3147   3087      4   1292   -153       C  
ATOM   4595  CG2 VAL C 144      69.587   3.353  14.606  1.00 36.47           C  
ANISOU 4595  CG2 VAL C 144     7431   3237   3188    133   1622    -50       C  
ATOM   4596  N   LEU C 145      72.788   4.822  11.755  1.00 37.74           N  
ANISOU 4596  N   LEU C 145     7301   3401   3637    -76   1056   -133       N  
ATOM   4597  CA  LEU C 145      74.047   5.367  11.247  1.00 37.86           C  
ANISOU 4597  CA  LEU C 145     7297   3384   3704   -189    895   -171       C  
ATOM   4598  C   LEU C 145      73.824   6.545  10.291  1.00 41.50           C  
ANISOU 4598  C   LEU C 145     7761   3799   4206   -163    962   -187       C  
ATOM   4599  O   LEU C 145      74.475   7.583  10.459  1.00 41.60           O  
ANISOU 4599  O   LEU C 145     7935   3709   4164   -235    899   -235       O  
ATOM   4600  CB  LEU C 145      74.912   4.267  10.589  1.00 38.27           C  
ANISOU 4600  CB  LEU C 145     7107   3532   3903   -264    771   -148       C  
ATOM   4601  CG  LEU C 145      76.183   4.742   9.848  1.00 43.35           C  
ANISOU 4601  CG  LEU C 145     7653   4166   4654   -383    652   -183       C  
ATOM   4602  CD1 LEU C 145      77.286   5.212  10.839  1.00 43.23           C  
ANISOU 4602  CD1 LEU C 145     7782   4066   4578   -495    471   -229       C  
ATOM   4603  CD2 LEU C 145      76.671   3.696   8.833  1.00 43.02           C  
ANISOU 4603  CD2 LEU C 145     7343   4224   4778   -405    627   -160       C  
ATOM   4604  N   VAL C 146      72.899   6.397   9.310  1.00 35.82           N  
ANISOU 4604  N   VAL C 146     6888   3143   3578    -67   1071   -146       N  
ATOM   4605  CA  VAL C 146      72.600   7.458   8.351  1.00 34.30           C  
ANISOU 4605  CA  VAL C 146     6723   2894   3414    -24   1116   -148       C  
ATOM   4606  C   VAL C 146      72.015   8.679   9.084  1.00 40.18           C  
ANISOU 4606  C   VAL C 146     7721   3506   4040     70   1205   -183       C  
ATOM   4607  O   VAL C 146      72.450   9.785   8.785  1.00 40.67           O  
ANISOU 4607  O   VAL C 146     7932   3455   4064     30   1173   -214       O  
ATOM   4608  CB  VAL C 146      71.766   6.989   7.122  1.00 36.59           C  
ANISOU 4608  CB  VAL C 146     6811   3269   3821     54   1162    -91       C  
ATOM   4609  CG1 VAL C 146      71.231   8.168   6.298  1.00 35.65           C  
ANISOU 4609  CG1 VAL C 146     6777   3065   3704    134   1197    -84       C  
ATOM   4610  CG2 VAL C 146      72.587   6.046   6.238  1.00 36.08           C  
ANISOU 4610  CG2 VAL C 146     6570   3291   3847    -57   1078    -77       C  
ATOM   4611  N   THR C 147      71.116   8.492  10.084  1.00 36.83           N  
ANISOU 4611  N   THR C 147     7370   3078   3546    183   1328   -183       N  
ATOM   4612  CA  THR C 147      70.557   9.618  10.863  1.00 35.84           C  
ANISOU 4612  CA  THR C 147     7509   2810   3297    293   1448   -228       C  
ATOM   4613  C   THR C 147      71.662  10.396  11.558  1.00 39.60           C  
ANISOU 4613  C   THR C 147     8273   3147   3624    162   1334   -295       C  
ATOM   4614  O   THR C 147      71.674  11.598  11.449  1.00 39.47           O  
ANISOU 4614  O   THR C 147     8454   2992   3552    191   1352   -333       O  
ATOM   4615  CB  THR C 147      69.446   9.169  11.817  1.00 36.68           C  
ANISOU 4615  CB  THR C 147     7634   2943   3359    423   1640   -218       C  
ATOM   4616  OG1 THR C 147      68.446   8.510  11.051  1.00 38.39           O  
ANISOU 4616  OG1 THR C 147     7549   3288   3749    519   1718   -153       O  
ATOM   4617  CG2 THR C 147      68.804  10.322  12.548  1.00 29.49           C  
ANISOU 4617  CG2 THR C 147     6994   1879   2333    567   1807   -271       C  
ATOM   4618  N   LEU C 148      72.614   9.707  12.211  1.00 38.14           N  
ANISOU 4618  N   LEU C 148     8110   2993   3390     14   1191   -308       N  
ATOM   4619  CA  LEU C 148      73.783  10.317  12.858  1.00 38.01           C  
ANISOU 4619  CA  LEU C 148     8326   2856   3259   -143   1022   -368       C  
ATOM   4620  C   LEU C 148      74.670  11.039  11.809  1.00 43.19           C  
ANISOU 4620  C   LEU C 148     8912   3479   4020   -270    912   -379       C  
ATOM   4621  O   LEU C 148      75.248  12.085  12.100  1.00 44.10           O  
ANISOU 4621  O   LEU C 148     9261   3447   4049   -367    836   -432       O  
ATOM   4622  CB  LEU C 148      74.603   9.239  13.606  1.00 37.59           C  
ANISOU 4622  CB  LEU C 148     8237   2864   3181   -261    852   -361       C  
ATOM   4623  CG  LEU C 148      73.952   8.569  14.848  1.00 41.78           C  
ANISOU 4623  CG  LEU C 148     8942   3384   3550   -187    936   -353       C  
ATOM   4624  CD1 LEU C 148      74.788   7.394  15.327  1.00 41.50           C  
ANISOU 4624  CD1 LEU C 148     8832   3414   3521   -293    737   -325       C  
ATOM   4625  CD2 LEU C 148      73.819   9.551  16.030  1.00 42.84           C  
ANISOU 4625  CD2 LEU C 148     9514   3328   3436   -178    970   -422       C  
ATOM   4626  N   GLU C 149      74.750  10.491  10.591  1.00 39.50           N  
ANISOU 4626  N   GLU C 149     8148   3135   3724   -281    915   -329       N  
ATOM   4627  CA  GLU C 149      75.531  11.076   9.503  1.00 39.23           C  
ANISOU 4627  CA  GLU C 149     8045   3076   3784   -405    858   -331       C  
ATOM   4628  C   GLU C 149      74.881  12.370   8.943  1.00 43.12           C  
ANISOU 4628  C   GLU C 149     8724   3434   4227   -320    961   -335       C  
ATOM   4629  O   GLU C 149      75.589  13.247   8.464  1.00 41.84           O  
ANISOU 4629  O   GLU C 149     8665   3169   4063   -450    913   -355       O  
ATOM   4630  CB  GLU C 149      75.711  10.049   8.364  1.00 40.17           C  
ANISOU 4630  CB  GLU C 149     7840   3352   4070   -422    863   -280       C  
ATOM   4631  CG  GLU C 149      76.782   8.996   8.604  1.00 45.27           C  
ANISOU 4631  CG  GLU C 149     8293   4097   4809   -546    733   -284       C  
ATOM   4632  CD  GLU C 149      76.945   7.958   7.507  1.00 54.36           C  
ANISOU 4632  CD  GLU C 149     9160   5383   6111   -546    761   -245       C  
ATOM   4633  OE1 GLU C 149      76.206   8.019   6.498  1.00 39.02           O  
ANISOU 4633  OE1 GLU C 149     7175   3460   4189   -468    868   -210       O  
ATOM   4634  OE2 GLU C 149      77.819   7.075   7.657  1.00 49.86           O  
ANISOU 4634  OE2 GLU C 149     8424   4886   5636   -617    665   -250       O  
ATOM   4635  N   VAL C 150      73.539  12.457   8.979  1.00 40.06           N  
ANISOU 4635  N   VAL C 150     8364   3043   3814   -103   1101   -310       N  
ATOM   4636  CA  VAL C 150      72.736  13.548   8.411  1.00 39.32           C  
ANISOU 4636  CA  VAL C 150     8413   2826   3699     36   1192   -301       C  
ATOM   4637  C   VAL C 150      72.409  14.596   9.484  1.00 47.47           C  
ANISOU 4637  C   VAL C 150     9788   3673   4573    116   1255   -364       C  
ATOM   4638  O   VAL C 150      72.183  15.756   9.148  1.00 46.98           O  
ANISOU 4638  O   VAL C 150     9936   3448   4467    172   1283   -378       O  
ATOM   4639  CB  VAL C 150      71.478  12.986   7.665  1.00 40.96           C  
ANISOU 4639  CB  VAL C 150     8398   3145   4021    231   1282   -234       C  
ATOM   4640  CG1 VAL C 150      70.500  14.090   7.250  1.00 40.74           C  
ANISOU 4640  CG1 VAL C 150     8511   2982   3985    424   1357   -221       C  
ATOM   4641  CG2 VAL C 150      71.883  12.141   6.457  1.00 39.65           C  
ANISOU 4641  CG2 VAL C 150     7977   3113   3974    133   1209   -181       C  
ATOM   4642  N   LEU C 151      72.454  14.214  10.775  1.00 45.33           N  
ANISOU 4642  N   LEU C 151     9622   3405   4198    111   1270   -406       N  
ATOM   4643  CA  LEU C 151      72.177  15.174  11.845  1.00 45.20           C  
ANISOU 4643  CA  LEU C 151     9981   3195   3999    181   1343   -477       C  
ATOM   4644  C   LEU C 151      72.932  16.527  11.756  1.00 49.61           C  
ANISOU 4644  C   LEU C 151    10851   3537   4463     57   1249   -531       C  
ATOM   4645  O   LEU C 151      72.241  17.551  11.919  1.00 51.24           O  
ANISOU 4645  O   LEU C 151    11316   3568   4585    216   1367   -563       O  
ATOM   4646  CB  LEU C 151      72.382  14.565  13.229  1.00 44.75           C  
ANISOU 4646  CB  LEU C 151    10053   3150   3801    129   1328   -516       C  
ATOM   4647  CG  LEU C 151      71.182  13.922  13.880  1.00 48.46           C  
ANISOU 4647  CG  LEU C 151    10481   3687   4244    326   1542   -500       C  
ATOM   4648  CD1 LEU C 151      71.583  13.336  15.174  1.00 49.07           C  
ANISOU 4648  CD1 LEU C 151    10746   3750   4148    233   1498   -533       C  
ATOM   4649  CD2 LEU C 151      70.070  14.915  14.138  1.00 49.88           C  
ANISOU 4649  CD2 LEU C 151    10863   3723   4367    561   1770   -535       C  
ATOM   4650  N   PRO C 152      74.279  16.627  11.509  1.00 43.56           N  
ANISOU 4650  N   PRO C 152    10076   2759   3717   -213   1055   -543       N  
ATOM   4651  CA  PRO C 152      74.908  17.976  11.500  1.00 43.38           C  
ANISOU 4651  CA  PRO C 152    10375   2508   3600   -347    981   -596       C  
ATOM   4652  C   PRO C 152      74.291  19.005  10.538  1.00 48.29           C  
ANISOU 4652  C   PRO C 152    11114   2994   4240   -221   1084   -571       C  
ATOM   4653  O   PRO C 152      74.307  20.196  10.864  1.00 48.20           O  
ANISOU 4653  O   PRO C 152    11474   2744   4094   -219   1092   -624       O  
ATOM   4654  CB  PRO C 152      76.373  17.694  11.180  1.00 44.62           C  
ANISOU 4654  CB  PRO C 152    10368   2732   3855   -655    782   -593       C  
ATOM   4655  CG  PRO C 152      76.576  16.256  11.639  1.00 47.89           C  
ANISOU 4655  CG  PRO C 152    10504   3356   4335   -665    719   -572       C  
ATOM   4656  CD  PRO C 152      75.297  15.571  11.324  1.00 43.34           C  
ANISOU 4656  CD  PRO C 152     9757   2904   3805   -407    902   -518       C  
ATOM   4657  N   MET C 153      73.690  18.561   9.407  1.00 45.57           N  
ANISOU 4657  N   MET C 153    10494   2780   4043   -101   1150   -491       N  
ATOM   4658  CA  MET C 153      73.043  19.477   8.448  1.00 46.61           C  
ANISOU 4658  CA  MET C 153    10743   2778   4189     40   1214   -454       C  
ATOM   4659  C   MET C 153      71.587  19.853   8.829  1.00 55.40           C  
ANISOU 4659  C   MET C 153    11961   3814   5274    383   1371   -460       C  
ATOM   4660  O   MET C 153      70.948  20.617   8.107  1.00 56.65           O  
ANISOU 4660  O   MET C 153    12219   3850   5456    543   1407   -426       O  
ATOM   4661  CB  MET C 153      73.122  18.955   6.991  1.00 48.41           C  
ANISOU 4661  CB  MET C 153    10690   3141   4561     -1   1185   -367       C  
ATOM   4662  CG  MET C 153      72.364  17.657   6.744  1.00 51.00           C  
ANISOU 4662  CG  MET C 153    10653   3709   5017    143   1228   -313       C  
ATOM   4663  SD  MET C 153      71.950  17.357   5.011  1.00 54.23           S  
ANISOU 4663  SD  MET C 153    10866   4195   5544    196   1207   -214       S  
ATOM   4664  CE  MET C 153      73.550  16.902   4.350  1.00 50.52           C  
ANISOU 4664  CE  MET C 153    10289   3799   5106   -150   1129   -213       C  
ATOM   4665  N   LEU C 154      71.079  19.333   9.954  1.00 53.65           N  
ANISOU 4665  N   LEU C 154    11723   3653   5007    496   1470   -499       N  
ATOM   4666  CA  LEU C 154      69.713  19.602  10.425  1.00 53.58           C  
ANISOU 4666  CA  LEU C 154    11773   3588   4996    818   1665   -513       C  
ATOM   4667  C   LEU C 154      69.717  20.416  11.696  1.00 60.01           C  
ANISOU 4667  C   LEU C 154    13012   4187   5604    856   1752   -615       C  
ATOM   4668  O   LEU C 154      68.674  20.956  12.079  1.00 58.56           O  
ANISOU 4668  O   LEU C 154    12964   3888   5399   1131   1940   -645       O  
ATOM   4669  CB  LEU C 154      68.972  18.273  10.732  1.00 52.86           C  
ANISOU 4669  CB  LEU C 154    11329   3741   5014    924   1769   -476       C  
ATOM   4670  CG  LEU C 154      68.938  17.202   9.669  1.00 56.60           C  
ANISOU 4670  CG  LEU C 154    11385   4447   5674    873   1685   -385       C  
ATOM   4671  CD1 LEU C 154      68.412  15.920  10.242  1.00 56.86           C  
ANISOU 4671  CD1 LEU C 154    11154   4680   5770    918   1779   -365       C  
ATOM   4672  CD2 LEU C 154      68.146  17.640   8.441  1.00 57.23           C  
ANISOU 4672  CD2 LEU C 154    11354   4502   5890   1048   1675   -318       C  
ATOM   4673  N   THR C 155      70.869  20.445  12.389  1.00 59.97           N  
ANISOU 4673  N   THR C 155    13205   4128   5454    587   1617   -672       N  
ATOM   4674  CA  THR C 155      71.010  21.073  13.697  1.00 61.47           C  
ANISOU 4674  CA  THR C 155    13832   4115   5410    573   1660   -776       C  
ATOM   4675  C   THR C 155      72.019  22.216  13.717  1.00 70.12           C  
ANISOU 4675  C   THR C 155    15307   4963   6373    358   1498   -833       C  
ATOM   4676  O   THR C 155      71.731  23.243  14.330  1.00 71.63           O  
ANISOU 4676  O   THR C 155    15921   4895   6399    463   1585   -909       O  
ATOM   4677  CB  THR C 155      71.317  19.990  14.771  1.00 67.57           C  
ANISOU 4677  CB  THR C 155    14551   5025   6097    461   1632   -797       C  
ATOM   4678  OG1 THR C 155      72.445  19.211  14.365  1.00 69.52           O  
ANISOU 4678  OG1 THR C 155    14536   5438   6440    188   1399   -753       O  
ATOM   4679  CG2 THR C 155      70.141  19.040  15.007  1.00 60.74           C  
ANISOU 4679  CG2 THR C 155    13428   4336   5313    694   1857   -758       C  
ATOM   4680  N   PHE C 156      73.182  22.065  13.052  1.00 69.04           N  
ANISOU 4680  N   PHE C 156    15029   4891   6312     58   1281   -800       N  
ATOM   4681  CA  PHE C 156      74.219  23.102  13.091  1.00 69.89           C  
ANISOU 4681  CA  PHE C 156    15467   4772   6316   -197   1120   -852       C  
ATOM   4682  C   PHE C 156      74.567  23.731  11.736  1.00 76.65           C  
ANISOU 4682  C   PHE C 156    16270   5566   7286   -284   1078   -791       C  
ATOM   4683  O   PHE C 156      75.176  24.800  11.734  1.00 77.88           O  
ANISOU 4683  O   PHE C 156    16778   5472   7340   -427   1009   -833       O  
ATOM   4684  CB  PHE C 156      75.487  22.581  13.792  1.00 71.69           C  
ANISOU 4684  CB  PHE C 156    15669   5063   6507   -528    889   -887       C  
ATOM   4685  CG  PHE C 156      75.334  22.390  15.289  1.00 72.97           C  
ANISOU 4685  CG  PHE C 156    16098   5166   6460   -492    886   -965       C  
ATOM   4686  CD1 PHE C 156      75.777  23.360  16.179  1.00 75.09           C  
ANISOU 4686  CD1 PHE C 156    16877   5156   6496   -609    796  -1065       C  
ATOM   4687  CD2 PHE C 156      74.757  21.231  15.807  1.00 75.49           C  
ANISOU 4687  CD2 PHE C 156    16195   5691   6797   -355    973   -939       C  
ATOM   4688  CE1 PHE C 156      75.633  23.184  17.560  1.00 76.14           C  
ANISOU 4688  CE1 PHE C 156    17314   5215   6399   -580    795  -1139       C  
ATOM   4689  CE2 PHE C 156      74.615  21.056  17.189  1.00 77.99           C  
ANISOU 4689  CE2 PHE C 156    16809   5935   6890   -331    985  -1006       C  
ATOM   4690  CZ  PHE C 156      75.057  22.033  18.056  1.00 75.47           C  
ANISOU 4690  CZ  PHE C 156    17016   5336   6323   -440    896  -1106       C  
ATOM   4691  N   ILE C 157      74.190  23.109  10.602  1.00 73.81           N  
ANISOU 4691  N   ILE C 157    15522   5408   7115   -209   1118   -695       N  
ATOM   4692  CA  ILE C 157      74.443  23.671   9.255  1.00 74.12           C  
ANISOU 4692  CA  ILE C 157    15549   5380   7234   -281   1094   -630       C  
ATOM   4693  C   ILE C 157      73.074  23.866   8.562  1.00 80.03           C  
ANISOU 4693  C   ILE C 157    16268   6105   8035     81   1233   -572       C  
ATOM   4694  O   ILE C 157      72.668  23.052   7.718  1.00 79.58           O  
ANISOU 4694  O   ILE C 157    15860   6252   8124    173   1253   -491       O  
ATOM   4695  CB  ILE C 157      75.486  22.851   8.405  1.00 76.55           C  
ANISOU 4695  CB  ILE C 157    15491   5896   7697   -554    995   -570       C  
ATOM   4696  CG1 ILE C 157      76.784  22.567   9.197  1.00 76.49           C  
ANISOU 4696  CG1 ILE C 157    15450   5930   7684   -878    839   -628       C  
ATOM   4697  CG2 ILE C 157      75.828  23.572   7.101  1.00 76.70           C  
ANISOU 4697  CG2 ILE C 157    15596   5799   7748   -665    994   -511       C  
ATOM   4698  CD1 ILE C 157      77.279  21.142   9.138  1.00 76.43           C  
ANISOU 4698  CD1 ILE C 157    15003   6217   7820   -944    786   -602       C  
ATOM   4699  N   THR C 158      72.341  24.918   8.989  1.00 77.56           N  
ANISOU 4699  N   THR C 158    16327   5537   7605    295   1319   -618       N  
ATOM   4700  CA  THR C 158      70.985  25.250   8.523  1.00 78.46           C  
ANISOU 4700  CA  THR C 158    16442   5589   7781    677   1441   -576       C  
ATOM   4701  C   THR C 158      70.800  26.730   8.118  1.00 85.01           C  
ANISOU 4701  C   THR C 158    17709   6075   8516    762   1434   -580       C  
ATOM   4702  O   THR C 158      69.916  27.019   7.305  1.00 85.99           O  
ANISOU 4702  O   THR C 158    17794   6151   8726   1015   1457   -510       O  
ATOM   4703  CB  THR C 158      69.943  24.917   9.620  1.00 88.53           C  
ANISOU 4703  CB  THR C 158    17690   6906   9042    967   1617   -633       C  
ATOM   4704  OG1 THR C 158      70.227  25.672  10.801  1.00 92.46           O  
ANISOU 4704  OG1 THR C 158    18625   7175   9330    917   1656   -747       O  
ATOM   4705  CG2 THR C 158      69.864  23.435   9.949  1.00 84.73           C  
ANISOU 4705  CG2 THR C 158    16779   6750   8664    940   1646   -610       C  
ATOM   4706  N   SER C 159      71.596  27.657   8.713  1.00 81.16           N  
ANISOU 4706  N   SER C 159    17650   5336   7850    556   1384   -661       N  
ATOM   4707  CA  SER C 159      71.547  29.112   8.506  1.00 81.49           C  
ANISOU 4707  CA  SER C 159    18187   5008   7768    597   1374   -679       C  
ATOM   4708  C   SER C 159      71.484  29.581   7.038  1.00 86.47           C  
ANISOU 4708  C   SER C 159    18827   5563   8465    586   1303   -567       C  
ATOM   4709  O   SER C 159      72.066  28.954   6.152  1.00 85.00           O  
ANISOU 4709  O   SER C 159    18367   5563   8366    354   1225   -495       O  
ATOM   4710  CB  SER C 159      72.711  29.798   9.217  1.00 84.86           C  
ANISOU 4710  CB  SER C 159    19002   5226   8013    253   1280   -772       C  
ATOM   4711  N   THR C 160      70.778  30.715   6.809  1.00 84.23           N  
ANISOU 4711  N   THR C 160    18895   4983   8127    847   1336   -555       N  
ATOM   4712  CA  THR C 160      70.589  31.352   5.504  1.00121.52           C  
ANISOU 4712  CA  THR C 160    23739   9562  12870    884   1258   -447       C  
ATOM   4713  C   THR C 160      71.884  32.003   5.016  1.00150.18           C  
ANISOU 4713  C   THR C 160    27682  13006  16374    453   1163   -438       C  
ATOM   4714  O   THR C 160      72.728  31.335   4.422  1.00110.06           O  
ANISOU 4714  O   THR C 160    22351   8118  11347    132   1111   -393       O  
ATOM   4715  CB  THR C 160      69.463  32.386   5.593  1.00130.14           C  
ANISOU 4715  CB  THR C 160    25129  10374  13946   1320   1312   -445       C  
ATOM   4716  N   ASP C 166      60.854  31.334   5.598  1.00100.39           N  
ANISOU 4716  N   ASP C 166    19760   6949  11437   4160   1823   -313       N  
ATOM   4717  CA  ASP C 166      60.480  32.112   4.414  1.00 99.42           C  
ANISOU 4717  CA  ASP C 166    19793   6606  11375   4363   1589   -205       C  
ATOM   4718  C   ASP C 166      61.091  31.534   3.121  1.00 99.22           C  
ANISOU 4718  C   ASP C 166    19627   6737  11336   4067   1302    -71       C  
ATOM   4719  O   ASP C 166      60.609  31.828   2.020  1.00100.26           O  
ANISOU 4719  O   ASP C 166    19769   6769  11555   4242   1077     45       O  
ATOM   4720  CB  ASP C 166      60.838  33.597   4.597  1.00101.51           C  
ANISOU 4720  CB  ASP C 166    20739   6413  11416   4414   1596   -259       C  
ATOM   4721  CG  ASP C 166      62.325  33.869   4.706  1.00115.04           C  
ANISOU 4721  CG  ASP C 166    22874   8020  12815   3912   1553   -302       C  
ATOM   4722  OD1 ASP C 166      62.871  33.740   5.822  1.00115.19           O  
ANISOU 4722  OD1 ASP C 166    22953   8106  12710   3712   1727   -419       O  
ATOM   4723  OD2 ASP C 166      62.942  34.216   3.673  1.00124.11           O  
ANISOU 4723  OD2 ASP C 166    24301   9011  13845   3715   1344   -217       O  
ATOM   4724  N   SER C 167      62.151  30.720   3.264  1.00 90.26           N  
ANISOU 4724  N   SER C 167    18378   5834  10085   3630   1310    -88       N  
ATOM   4725  CA  SER C 167      62.857  30.080   2.151  1.00 87.52           C  
ANISOU 4725  CA  SER C 167    17901   5651   9704   3313   1099     17       C  
ATOM   4726  C   SER C 167      63.527  28.769   2.580  1.00 83.80           C  
ANISOU 4726  C   SER C 167    17079   5531   9231   2982   1181    -21       C  
ATOM   4727  O   SER C 167      64.043  28.677   3.696  1.00 82.50           O  
ANISOU 4727  O   SER C 167    16992   5388   8966   2840   1353   -130       O  
ATOM   4728  CB  SER C 167      63.898  31.030   1.559  1.00 91.09           C  
ANISOU 4728  CB  SER C 167    18889   5816   9905   3045    977     47       C  
ATOM   4729  OG  SER C 167      64.813  31.483   2.546  1.00 99.19           O  
ANISOU 4729  OG  SER C 167    20241   6713  10734   2793   1119    -68       O  
ATOM   4730  N   CYS C 168      63.513  27.764   1.690  1.00 75.32           N  
ANISOU 4730  N   CYS C 168    15650   4712   8256   2865   1042     70       N  
ATOM   4731  CA  CYS C 168      64.177  26.481   1.927  1.00 72.76           C  
ANISOU 4731  CA  CYS C 168    15004   4706   7935   2555   1092     47       C  
ATOM   4732  C   CYS C 168      65.369  26.388   0.976  1.00 75.28           C  
ANISOU 4732  C   CYS C 168    15489   5016   8098   2172    961     99       C  
ATOM   4733  O   CYS C 168      65.206  26.226  -0.236  1.00 75.52           O  
ANISOU 4733  O   CYS C 168    15483   5062   8151   2166    791    202       O  
ATOM   4734  CB  CYS C 168      63.220  25.304   1.765  1.00 71.72           C  
ANISOU 4734  CB  CYS C 168    14326   4878   8045   2711   1075     95       C  
ATOM   4735  SG  CYS C 168      63.746  23.796   2.623  1.00 74.77           S  
ANISOU 4735  SG  CYS C 168    14337   5616   8455   2444   1221     32       S  
ATOM   4736  N   VAL C 169      66.565  26.583   1.530  1.00 69.70           N  
ANISOU 4736  N   VAL C 169    14999   4256   7226   1856   1041     24       N  
ATOM   4737  CA  VAL C 169      67.821  26.601   0.794  1.00 68.36           C  
ANISOU 4737  CA  VAL C 169    14995   4059   6919   1467    973     54       C  
ATOM   4738  C   VAL C 169      68.467  25.212   0.827  1.00 68.88           C  
ANISOU 4738  C   VAL C 169    14669   4456   7045   1209    999     43       C  
ATOM   4739  O   VAL C 169      68.347  24.509   1.836  1.00 69.04           O  
ANISOU 4739  O   VAL C 169    14436   4658   7138   1239   1093    -23       O  
ATOM   4740  CB  VAL C 169      68.714  27.772   1.326  1.00 72.77           C  
ANISOU 4740  CB  VAL C 169    16035   4326   7290   1280   1022    -16       C  
ATOM   4741  CG1 VAL C 169      69.971  27.300   2.058  1.00 73.01           C  
ANISOU 4741  CG1 VAL C 169    15999   4480   7263    911   1091   -101       C  
ATOM   4742  CG2 VAL C 169      69.041  28.778   0.234  1.00 72.24           C  
ANISOU 4742  CG2 VAL C 169    16372   3984   7091   1178    921     63       C  
ATOM   4743  N   ASP C 170      69.098  24.796  -0.294  1.00 62.29           N  
ANISOU 4743  N   ASP C 170    13801   3690   6177    973    923    111       N  
ATOM   4744  CA  ASP C 170      69.785  23.506  -0.387  1.00 61.11           C  
ANISOU 4744  CA  ASP C 170    13308   3828   6085    731    950    102       C  
ATOM   4745  C   ASP C 170      70.953  23.525   0.611  1.00 60.78           C  
ANISOU 4745  C   ASP C 170    13303   3801   5988    456   1040      4       C  
ATOM   4746  O   ASP C 170      71.568  24.587   0.789  1.00 59.14           O  
ANISOU 4746  O   ASP C 170    13451   3359   5660    321   1052    -27       O  
ATOM   4747  CB  ASP C 170      70.273  23.224  -1.824  1.00 62.80           C  
ANISOU 4747  CB  ASP C 170    13555   4058   6246    544    882    186       C  
ATOM   4748  CG  ASP C 170      71.147  21.988  -1.956  1.00 74.40           C  
ANISOU 4748  CG  ASP C 170    14712   5788   7767    285    934    167       C  
ATOM   4749  OD1 ASP C 170      72.376  22.110  -1.775  1.00 74.49           O  
ANISOU 4749  OD1 ASP C 170    14791   5783   7728    -16   1008    123       O  
ATOM   4750  OD2 ASP C 170      70.597  20.892  -2.231  1.00 81.13           O  
ANISOU 4750  OD2 ASP C 170    15245   6856   8726    385    897    194       O  
ATOM   4751  N   TYR C 171      71.220  22.360   1.286  1.00 53.04           N  
ANISOU 4751  N   TYR C 171    11970   3084   5098    376   1082    -40       N  
ATOM   4752  CA  TYR C 171      72.294  22.186   2.269  1.00 50.83           C  
ANISOU 4752  CA  TYR C 171    11669   2854   4792    128   1121   -126       C  
ATOM   4753  C   TYR C 171      73.605  22.882   1.851  1.00 54.91           C  
ANISOU 4753  C   TYR C 171    12417   3223   5222   -211   1107   -135       C  
ATOM   4754  O   TYR C 171      74.230  23.528   2.689  1.00 53.68           O  
ANISOU 4754  O   TYR C 171    12465   2936   4996   -351   1105   -207       O  
ATOM   4755  CB  TYR C 171      72.558  20.683   2.580  1.00 50.27           C  
ANISOU 4755  CB  TYR C 171    11176   3090   4836     52   1131   -139       C  
ATOM   4756  CG  TYR C 171      73.990  20.416   3.009  1.00 48.82           C  
ANISOU 4756  CG  TYR C 171    10938   2963   4649   -277   1118   -194       C  
ATOM   4757  CD1 TYR C 171      74.486  20.919   4.217  1.00 49.83           C  
ANISOU 4757  CD1 TYR C 171    11234   2992   4706   -367   1103   -277       C  
ATOM   4758  CD2 TYR C 171      74.872  19.729   2.177  1.00 48.28           C  
ANISOU 4758  CD2 TYR C 171    10669   3026   4650   -498   1114   -165       C  
ATOM   4759  CE1 TYR C 171      75.825  20.761   4.570  1.00 49.15           C  
ANISOU 4759  CE1 TYR C 171    11093   2943   4639   -677   1048   -323       C  
ATOM   4760  CE2 TYR C 171      76.206  19.535   2.537  1.00 48.35           C  
ANISOU 4760  CE2 TYR C 171    10591   3082   4697   -789   1098   -214       C  
ATOM   4761  CZ  TYR C 171      76.680  20.065   3.727  1.00 55.09           C  
ANISOU 4761  CZ  TYR C 171    11590   3842   5500   -881   1046   -289       C  
ATOM   4762  OH  TYR C 171      77.987  19.862   4.092  1.00 54.43           O  
ANISOU 4762  OH  TYR C 171    11393   3808   5481  -1168    989   -334       O  
ATOM   4763  N   ALA C 172      74.036  22.710   0.580  1.00 52.52           N  
ANISOU 4763  N   ALA C 172    12084   2946   4926   -359   1104    -66       N  
ATOM   4764  CA  ALA C 172      75.273  23.289   0.058  1.00 52.99           C  
ANISOU 4764  CA  ALA C 172    12323   2883   4926   -701   1132    -65       C  
ATOM   4765  C   ALA C 172      75.322  24.838   0.096  1.00 58.04           C  
ANISOU 4765  C   ALA C 172    13449   3182   5423   -736   1120    -68       C  
ATOM   4766  O   ALA C 172      76.416  25.409   0.033  1.00 57.97           O  
ANISOU 4766  O   ALA C 172    13599   3055   5372  -1054   1146    -90       O  
ATOM   4767  CB  ALA C 172      75.554  22.765  -1.337  1.00 53.81           C  
ANISOU 4767  CB  ALA C 172    12331   3070   5044   -809   1169     12       C  
ATOM   4768  N   SER C 173      74.161  25.508   0.275  1.00 54.96           N  
ANISOU 4768  N   SER C 173    13282   2628   4972   -413   1084    -52       N  
ATOM   4769  CA  SER C 173      74.098  26.970   0.389  1.00 55.19           C  
ANISOU 4769  CA  SER C 173    13800   2308   4861   -394   1068    -60       C  
ATOM   4770  C   SER C 173      73.678  27.426   1.802  1.00 60.81           C  
ANISOU 4770  C   SER C 173    14640   2921   5542   -224   1074   -157       C  
ATOM   4771  O   SER C 173      73.222  28.556   1.979  1.00 61.71           O  
ANISOU 4771  O   SER C 173    15143   2749   5555    -65   1066   -167       O  
ATOM   4772  CB  SER C 173      73.237  27.580  -0.716  1.00 57.29           C  
ANISOU 4772  CB  SER C 173    14311   2395   5063   -174   1019     42       C  
ATOM   4773  OG  SER C 173      71.877  27.198  -0.658  1.00 63.88           O  
ANISOU 4773  OG  SER C 173    14984   3306   5981    237    974     66       O  
ATOM   4774  N   SER C 174      73.922  26.555   2.813  1.00 57.09           N  
ANISOU 4774  N   SER C 174    13878   2670   5143   -275   1091   -232       N  
ATOM   4775  CA  SER C 174      73.637  26.719   4.246  1.00 57.31           C  
ANISOU 4775  CA  SER C 174    13996   2652   5126   -154   1114   -332       C  
ATOM   4776  C   SER C 174      74.914  26.794   5.107  1.00 63.72           C  
ANISOU 4776  C   SER C 174    14874   3448   5889   -508   1065   -419       C  
ATOM   4777  O   SER C 174      75.952  26.255   4.723  1.00 63.55           O  
ANISOU 4777  O   SER C 174    14623   3576   5946   -810   1026   -403       O  
ATOM   4778  CB  SER C 174      72.806  25.537   4.749  1.00 60.25           C  
ANISOU 4778  CB  SER C 174    13980   3299   5613     92   1162   -337       C  
ATOM   4779  OG  SER C 174      71.431  25.857   4.862  1.00 70.39           O  
ANISOU 4779  OG  SER C 174    15327   4505   6913    491   1224   -324       O  
ATOM   4780  N   GLY C 175      74.789  27.402   6.292  1.00 61.89           N  
ANISOU 4780  N   GLY C 175    14938   3041   5537   -452   1064   -512       N  
ATOM   4781  CA  GLY C 175      75.831  27.522   7.315  1.00 61.50           C  
ANISOU 4781  CA  GLY C 175    15001   2948   5419   -746    977   -605       C  
ATOM   4782  C   GLY C 175      77.166  28.108   6.897  1.00 64.71           C  
ANISOU 4782  C   GLY C 175    15529   3238   5820  -1174    883   -605       C  
ATOM   4783  O   GLY C 175      77.285  28.714   5.826  1.00 64.62           O  
ANISOU 4783  O   GLY C 175    15649   3097   5805  -1254    911   -538       O  
ATOM   4784  N   ASN C 176      78.181  27.926   7.761  1.00 60.55           N  
ANISOU 4784  N   ASN C 176    14964   2750   5293  -1462    762   -678       N  
ATOM   4785  CA  ASN C 176      79.550  28.397   7.545  1.00 60.64           C  
ANISOU 4785  CA  ASN C 176    15022   2676   5341  -1908    655   -690       C  
ATOM   4786  C   ASN C 176      80.222  27.465   6.527  1.00 64.31           C  
ANISOU 4786  C   ASN C 176    15000   3416   6018  -2081    687   -612       C  
ATOM   4787  O   ASN C 176      80.349  26.278   6.807  1.00 65.39           O  
ANISOU 4787  O   ASN C 176    14734   3834   6279  -2046    658   -614       O  
ATOM   4788  CB  ASN C 176      80.322  28.411   8.873  1.00 63.05           C  
ANISOU 4788  CB  ASN C 176    15410   2949   5596  -2123    479   -793       C  
ATOM   4789  CG  ASN C 176      81.714  28.986   8.773  1.00 93.14           C  
ANISOU 4789  CG  ASN C 176    19286   6644   9460  -2595    340   -816       C  
ATOM   4790  OD1 ASN C 176      82.635  28.366   8.229  1.00 85.86           O  
ANISOU 4790  OD1 ASN C 176    17959   5921   8742  -2851    308   -778       O  
ATOM   4791  ND2 ASN C 176      81.904  30.185   9.312  1.00 86.55           N  
ANISOU 4791  ND2 ASN C 176    18958   5475   8451  -2725    261   -883       N  
ATOM   4792  N   PRO C 177      80.671  27.961   5.353  1.00 59.60           N  
ANISOU 4792  N   PRO C 177    14456   2731   5458  -2267    760   -546       N  
ATOM   4793  CA  PRO C 177      81.259  27.049   4.352  1.00 59.09           C  
ANISOU 4793  CA  PRO C 177    13954   2919   5578  -2405    835   -478       C  
ATOM   4794  C   PRO C 177      82.529  26.288   4.766  1.00 64.50           C  
ANISOU 4794  C   PRO C 177    14237   3812   6456  -2712    745   -518       C  
ATOM   4795  O   PRO C 177      82.731  25.184   4.261  1.00 63.80           O  
ANISOU 4795  O   PRO C 177    13724   3991   6526  -2690    805   -481       O  
ATOM   4796  CB  PRO C 177      81.508  27.954   3.140  1.00 60.04           C  
ANISOU 4796  CB  PRO C 177    14334   2833   5646  -2571    943   -408       C  
ATOM   4797  CG  PRO C 177      81.553  29.344   3.694  1.00 63.40           C  
ANISOU 4797  CG  PRO C 177    15281   2904   5906  -2670    871   -457       C  
ATOM   4798  CD  PRO C 177      80.585  29.344   4.834  1.00 59.37           C  
ANISOU 4798  CD  PRO C 177    14917   2357   5285  -2333    800   -523       C  
ATOM   4799  N   LYS C 178      83.366  26.858   5.659  1.00 62.57           N  
ANISOU 4799  N   LYS C 178    14127   3441   6205  -2985    589   -593       N  
ATOM   4800  CA  LYS C 178      84.623  26.258   6.144  1.00 62.99           C  
ANISOU 4800  CA  LYS C 178    13809   3664   6461  -3286    449   -633       C  
ATOM   4801  C   LYS C 178      84.391  24.936   6.860  1.00 67.13           C  
ANISOU 4801  C   LYS C 178    13985   4461   7061  -3076    363   -654       C  
ATOM   4802  O   LYS C 178      85.113  23.967   6.613  1.00 68.46           O  
ANISOU 4802  O   LYS C 178    13691   4871   7448  -3174    353   -637       O  
ATOM   4803  CB  LYS C 178      85.400  27.236   7.053  1.00 66.06           C  
ANISOU 4803  CB  LYS C 178    14483   3822   6796  -3600    251   -712       C  
ATOM   4804  N   TYR C 179      83.362  24.879   7.708  1.00 62.33           N  
ANISOU 4804  N   TYR C 179    13603   3806   6273  -2773    326   -687       N  
ATOM   4805  CA  TYR C 179      83.022  23.675   8.452  1.00 61.41           C  
ANISOU 4805  CA  TYR C 179    13230   3915   6188  -2565    261   -701       C  
ATOM   4806  C   TYR C 179      82.119  22.767   7.633  1.00 61.41           C  
ANISOU 4806  C   TYR C 179    12976   4115   6242  -2269    443   -628       C  
ATOM   4807  O   TYR C 179      82.210  21.543   7.747  1.00 59.04           O  
ANISOU 4807  O   TYR C 179    12305   4060   6068  -2202    420   -613       O  
ATOM   4808  CB  TYR C 179      82.390  24.029   9.804  1.00 64.07           C  
ANISOU 4808  CB  TYR C 179    13945   4100   6298  -2406    166   -775       C  
ATOM   4809  CG  TYR C 179      83.315  24.822  10.701  1.00 68.36           C  
ANISOU 4809  CG  TYR C 179    14755   4446   6772  -2712    -59   -855       C  
ATOM   4810  CD1 TYR C 179      84.372  24.205  11.366  1.00 70.98           C  
ANISOU 4810  CD1 TYR C 179    14837   4904   7230  -2937   -298   -888       C  
ATOM   4811  CD2 TYR C 179      83.161  26.197  10.851  1.00 69.71           C  
ANISOU 4811  CD2 TYR C 179    15435   4292   6760  -2785    -56   -898       C  
ATOM   4812  CE1 TYR C 179      85.256  24.941  12.158  1.00 73.10           C  
ANISOU 4812  CE1 TYR C 179    15342   4987   7447  -3245   -548   -960       C  
ATOM   4813  CE2 TYR C 179      84.028  26.939  11.652  1.00 71.51           C  
ANISOU 4813  CE2 TYR C 179    15930   4322   6918  -3095   -284   -976       C  
ATOM   4814  CZ  TYR C 179      85.065  26.303  12.318  1.00 82.13           C  
ANISOU 4814  CZ  TYR C 179    17010   5804   8391  -3329   -539  -1007       C  
ATOM   4815  OH  TYR C 179      85.922  27.026  13.114  1.00 87.29           O  
ANISOU 4815  OH  TYR C 179    17923   6259   8983  -3650   -805  -1082       O  
ATOM   4816  N   SER C 180      81.247  23.369   6.809  1.00 57.24           N  
ANISOU 4816  N   SER C 180    12663   3467   5619  -2096    602   -580       N  
ATOM   4817  CA  SER C 180      80.333  22.631   5.946  1.00 56.62           C  
ANISOU 4817  CA  SER C 180    12387   3545   5582  -1827    747   -506       C  
ATOM   4818  C   SER C 180      81.091  21.870   4.855  1.00 58.66           C  
ANISOU 4818  C   SER C 180    12267   3994   6026  -1991    812   -453       C  
ATOM   4819  O   SER C 180      80.660  20.783   4.476  1.00 57.71           O  
ANISOU 4819  O   SER C 180    11858   4084   5984  -1823    867   -416       O  
ATOM   4820  CB  SER C 180      79.295  23.561   5.337  1.00 60.64           C  
ANISOU 4820  CB  SER C 180    13238   3850   5952  -1623    853   -466       C  
ATOM   4821  OG  SER C 180      78.265  22.765   4.780  1.00 70.16           O  
ANISOU 4821  OG  SER C 180    14248   5215   7195  -1328    939   -406       O  
ATOM   4822  N   LEU C 181      82.240  22.418   4.384  1.00 54.36           N  
ANISOU 4822  N   LEU C 181    11724   3372   5558  -2330    816   -456       N  
ATOM   4823  CA  LEU C 181      83.100  21.766   3.395  1.00 53.45           C  
ANISOU 4823  CA  LEU C 181    11259   3420   5630  -2515    916   -419       C  
ATOM   4824  C   LEU C 181      83.702  20.503   4.001  1.00 55.78           C  
ANISOU 4824  C   LEU C 181    11115   3968   6111  -2536    819   -451       C  
ATOM   4825  O   LEU C 181      83.541  19.442   3.411  1.00 57.95           O  
ANISOU 4825  O   LEU C 181    11100   4437   6481  -2416    909   -416       O  
ATOM   4826  CB  LEU C 181      84.181  22.729   2.836  1.00 53.48           C  
ANISOU 4826  CB  LEU C 181    11376   3265   5681  -2889    969   -418       C  
ATOM   4827  CG  LEU C 181      85.193  22.180   1.798  1.00 58.56           C  
ANISOU 4827  CG  LEU C 181    11668   4052   6528  -3118   1125   -388       C  
ATOM   4828  CD1 LEU C 181      84.502  21.542   0.564  1.00 58.61           C  
ANISOU 4828  CD1 LEU C 181    11628   4151   6490  -2920   1319   -315       C  
ATOM   4829  CD2 LEU C 181      86.156  23.252   1.368  1.00 61.37           C  
ANISOU 4829  CD2 LEU C 181    12170   4226   6921  -3500   1191   -388       C  
ATOM   4830  N   ILE C 182      84.320  20.595   5.204  1.00 50.63           N  
ANISOU 4830  N   ILE C 182    10446   3297   5494  -2667    618   -517       N  
ATOM   4831  CA  ILE C 182      84.884  19.439   5.935  1.00 50.02           C  
ANISOU 4831  CA  ILE C 182     9994   3430   5579  -2671    473   -545       C  
ATOM   4832  C   ILE C 182      83.810  18.356   6.157  1.00 51.99           C  
ANISOU 4832  C   ILE C 182    10147   3836   5771  -2327    502   -521       C  
ATOM   4833  O   ILE C 182      84.060  17.183   5.854  1.00 53.13           O  
ANISOU 4833  O   ILE C 182     9930   4187   6071  -2276    531   -499       O  
ATOM   4834  CB  ILE C 182      85.620  19.839   7.255  1.00 52.82           C  
ANISOU 4834  CB  ILE C 182    10437   3697   5935  -2861    203   -617       C  
ATOM   4835  CG1 ILE C 182      86.791  20.806   6.967  1.00 53.50           C  
ANISOU 4835  CG1 ILE C 182    10522   3662   6145  -3251    164   -637       C  
ATOM   4836  CG2 ILE C 182      86.116  18.590   8.018  1.00 52.10           C  
ANISOU 4836  CG2 ILE C 182     9999   3810   5985  -2815     21   -634       C  
ATOM   4837  CD1 ILE C 182      87.153  21.802   8.163  1.00 61.43           C  
ANISOU 4837  CD1 ILE C 182    11877   4438   7025  -3444    -85   -708       C  
ATOM   4838  N   TYR C 183      82.615  18.754   6.641  1.00 45.55           N  
ANISOU 4838  N   TYR C 183     9651   2913   4741  -2093    514   -525       N  
ATOM   4839  CA  TYR C 183      81.493  17.830   6.842  1.00 44.31           C  
ANISOU 4839  CA  TYR C 183     9417   2887   4531  -1780    566   -498       C  
ATOM   4840  C   TYR C 183      81.028  17.165   5.530  1.00 47.87           C  
ANISOU 4840  C   TYR C 183     9659   3470   5061  -1657    737   -428       C  
ATOM   4841  O   TYR C 183      80.812  15.957   5.532  1.00 48.95           O  
ANISOU 4841  O   TYR C 183     9527   3794   5279  -1537    743   -409       O  
ATOM   4842  CB  TYR C 183      80.327  18.513   7.590  1.00 44.25           C  
ANISOU 4842  CB  TYR C 183     9786   2723   4304  -1564    583   -520       C  
ATOM   4843  CG  TYR C 183      79.009  17.766   7.539  1.00 44.28           C  
ANISOU 4843  CG  TYR C 183     9714   2838   4271  -1243    694   -480       C  
ATOM   4844  CD1 TYR C 183      78.860  16.527   8.158  1.00 45.70           C  
ANISOU 4844  CD1 TYR C 183     9663   3201   4499  -1149    653   -477       C  
ATOM   4845  CD2 TYR C 183      77.912  18.297   6.870  1.00 44.78           C  
ANISOU 4845  CD2 TYR C 183     9933   2817   4263  -1040    828   -441       C  
ATOM   4846  CE1 TYR C 183      77.655  15.827   8.094  1.00 44.77           C  
ANISOU 4846  CE1 TYR C 183     9459   3186   4366   -886    762   -438       C  
ATOM   4847  CE2 TYR C 183      76.700  17.614   6.808  1.00 45.32           C  
ANISOU 4847  CE2 TYR C 183     9889   2996   4335   -762    916   -402       C  
ATOM   4848  CZ  TYR C 183      76.575  16.380   7.426  1.00 50.49           C  
ANISOU 4848  CZ  TYR C 183    10303   3837   5043   -698    893   -403       C  
ATOM   4849  OH  TYR C 183      75.373  15.723   7.388  1.00 49.47           O  
ANISOU 4849  OH  TYR C 183    10059   3809   4928   -452    987   -364       O  
ATOM   4850  N   SER C 184      80.901  17.931   4.424  1.00 43.27           N  
ANISOU 4850  N   SER C 184     9226   2774   4439  -1700    860   -391       N  
ATOM   4851  CA  SER C 184      80.480  17.401   3.120  1.00 42.90           C  
ANISOU 4851  CA  SER C 184     9052   2818   4430  -1606   1003   -325       C  
ATOM   4852  C   SER C 184      81.476  16.380   2.563  1.00 47.49           C  
ANISOU 4852  C   SER C 184     9261   3581   5201  -1752   1047   -322       C  
ATOM   4853  O   SER C 184      81.060  15.374   1.997  1.00 44.98           O  
ANISOU 4853  O   SER C 184     8757   3407   4927  -1616   1112   -289       O  
ATOM   4854  CB  SER C 184      80.271  18.523   2.115  1.00 45.23           C  
ANISOU 4854  CB  SER C 184     9645   2920   4620  -1656   1101   -285       C  
ATOM   4855  OG  SER C 184      79.761  18.024   0.888  1.00 53.94           O  
ANISOU 4855  OG  SER C 184    10685   4090   5720  -1546   1209   -219       O  
ATOM   4856  N   LEU C 185      82.786  16.662   2.735  1.00 45.84           N  
ANISOU 4856  N   LEU C 185     8947   3355   5115  -2031   1012   -361       N  
ATOM   4857  CA  LEU C 185      83.929  15.826   2.370  1.00 45.08           C  
ANISOU 4857  CA  LEU C 185     8472   3413   5243  -2190   1052   -373       C  
ATOM   4858  C   LEU C 185      83.858  14.494   3.130  1.00 49.27           C  
ANISOU 4858  C   LEU C 185     8719   4131   5869  -2036    934   -389       C  
ATOM   4859  O   LEU C 185      83.930  13.434   2.489  1.00 49.15           O  
ANISOU 4859  O   LEU C 185     8454   4263   5959  -1963   1027   -371       O  
ATOM   4860  CB  LEU C 185      85.229  16.598   2.694  1.00 45.20           C  
ANISOU 4860  CB  LEU C 185     8451   3343   5378  -2515    990   -416       C  
ATOM   4861  CG  LEU C 185      86.135  17.102   1.537  1.00 49.51           C  
ANISOU 4861  CG  LEU C 185     8934   3845   6034  -2780   1191   -401       C  
ATOM   4862  CD1 LEU C 185      85.391  17.367   0.237  1.00 49.24           C  
ANISOU 4862  CD1 LEU C 185     9146   3728   5835  -2698   1408   -339       C  
ATOM   4863  CD2 LEU C 185      86.926  18.289   1.944  1.00 48.61           C  
ANISOU 4863  CD2 LEU C 185     8942   3572   5957  -3085   1114   -433       C  
ATOM   4864  N   CYS C 186      83.640  14.540   4.480  1.00 46.34           N  
ANISOU 4864  N   CYS C 186     8437   3736   5433  -1976    739   -422       N  
ATOM   4865  CA  CYS C 186      83.486  13.349   5.340  1.00 46.08           C  
ANISOU 4865  CA  CYS C 186     8214   3846   5446  -1829    611   -430       C  
ATOM   4866  C   CYS C 186      82.239  12.560   4.962  1.00 46.65           C  
ANISOU 4866  C   CYS C 186     8288   4004   5434  -1562    717   -384       C  
ATOM   4867  O   CYS C 186      82.285  11.328   4.920  1.00 44.81           O  
ANISOU 4867  O   CYS C 186     7807   3919   5300  -1475    709   -372       O  
ATOM   4868  CB  CYS C 186      83.474  13.717   6.818  1.00 47.51           C  
ANISOU 4868  CB  CYS C 186     8582   3945   5524  -1840    397   -472       C  
ATOM   4869  SG  CYS C 186      85.049  14.353   7.438  1.00 52.43           S  
ANISOU 4869  SG  CYS C 186     9134   4496   6290  -2172    184   -529       S  
ATOM   4870  N   LEU C 187      81.133  13.271   4.672  1.00 42.66           N  
ANISOU 4870  N   LEU C 187     8055   3395   4758  -1433    804   -359       N  
ATOM   4871  CA  LEU C 187      79.878  12.659   4.242  1.00 42.48           C  
ANISOU 4871  CA  LEU C 187     8027   3440   4673  -1194    890   -311       C  
ATOM   4872  C   LEU C 187      80.026  11.986   2.851  1.00 47.24           C  
ANISOU 4872  C   LEU C 187     8447   4136   5366  -1206   1015   -274       C  
ATOM   4873  O   LEU C 187      79.406  10.941   2.615  1.00 48.65           O  
ANISOU 4873  O   LEU C 187     8485   4432   5568  -1061   1037   -247       O  
ATOM   4874  CB  LEU C 187      78.738  13.696   4.274  1.00 42.33           C  
ANISOU 4874  CB  LEU C 187     8324   3274   4486  -1054    933   -295       C  
ATOM   4875  CG  LEU C 187      77.286  13.184   4.247  1.00 46.77           C  
ANISOU 4875  CG  LEU C 187     8881   3894   4995   -788    981   -254       C  
ATOM   4876  CD1 LEU C 187      76.974  12.257   5.443  1.00 47.08           C  
ANISOU 4876  CD1 LEU C 187     8814   4038   5038   -690    923   -271       C  
ATOM   4877  CD2 LEU C 187      76.308  14.347   4.240  1.00 47.35           C  
ANISOU 4877  CD2 LEU C 187     9246   3802   4942   -650   1023   -243       C  
ATOM   4878  N   THR C 188      80.889  12.539   1.961  1.00 41.93           N  
ANISOU 4878  N   THR C 188     7786   3405   4742  -1395   1106   -276       N  
ATOM   4879  CA  THR C 188      81.142  11.948   0.640  1.00 40.99           C  
ANISOU 4879  CA  THR C 188     7539   3350   4683  -1427   1253   -250       C  
ATOM   4880  C   THR C 188      81.936  10.651   0.835  1.00 43.78           C  
ANISOU 4880  C   THR C 188     7545   3869   5222  -1447   1239   -278       C  
ATOM   4881  O   THR C 188      81.590   9.637   0.218  1.00 43.19           O  
ANISOU 4881  O   THR C 188     7357   3887   5166  -1338   1304   -258       O  
ATOM   4882  CB  THR C 188      81.844  12.932  -0.320  1.00 43.91           C  
ANISOU 4882  CB  THR C 188     8049   3596   5037  -1636   1388   -243       C  
ATOM   4883  OG1 THR C 188      81.081  14.131  -0.409  1.00 46.80           O  
ANISOU 4883  OG1 THR C 188     8766   3788   5226  -1592   1373   -214       O  
ATOM   4884  CG2 THR C 188      82.037  12.354  -1.731  1.00 37.19           C  
ANISOU 4884  CG2 THR C 188     7135   2791   4205  -1664   1573   -218       C  
ATOM   4885  N   LEU C 189      82.973  10.681   1.713  1.00 39.07           N  
ANISOU 4885  N   LEU C 189     6791   3293   4759  -1578   1131   -323       N  
ATOM   4886  CA  LEU C 189      83.807   9.514   2.010  1.00 39.21           C  
ANISOU 4886  CA  LEU C 189     6471   3450   4976  -1582   1081   -349       C  
ATOM   4887  C   LEU C 189      83.015   8.370   2.677  1.00 42.24           C  
ANISOU 4887  C   LEU C 189     6799   3927   5323  -1366    975   -333       C  
ATOM   4888  O   LEU C 189      82.962   7.279   2.112  1.00 42.56           O  
ANISOU 4888  O   LEU C 189     6682   4060   5430  -1277   1048   -322       O  
ATOM   4889  CB  LEU C 189      85.074   9.898   2.824  1.00 39.42           C  
ANISOU 4889  CB  LEU C 189     6345   3466   5169  -1776    942   -395       C  
ATOM   4890  CG  LEU C 189      86.034   8.759   3.276  1.00 43.66           C  
ANISOU 4890  CG  LEU C 189     6511   4131   5946  -1771    836   -421       C  
ATOM   4891  CD1 LEU C 189      86.682   8.039   2.075  1.00 43.19           C  
ANISOU 4891  CD1 LEU C 189     6190   4154   6064  -1789   1059   -428       C  
ATOM   4892  CD2 LEU C 189      87.113   9.299   4.202  1.00 44.33           C  
ANISOU 4892  CD2 LEU C 189     6485   4183   6174  -1960    631   -460       C  
ATOM   4893  N   LEU C 190      82.375   8.623   3.832  1.00 38.59           N  
ANISOU 4893  N   LEU C 190     6494   3426   4741  -1288    826   -332       N  
ATOM   4894  CA  LEU C 190      81.628   7.582   4.567  1.00 38.15           C  
ANISOU 4894  CA  LEU C 190     6410   3446   4640  -1108    742   -313       C  
ATOM   4895  C   LEU C 190      80.318   7.189   3.921  1.00 39.57           C  
ANISOU 4895  C   LEU C 190     6667   3652   4715   -942    856   -267       C  
ATOM   4896  O   LEU C 190      79.974   6.009   3.921  1.00 37.74           O  
ANISOU 4896  O   LEU C 190     6313   3509   4516   -836    851   -247       O  
ATOM   4897  CB  LEU C 190      81.358   7.965   6.039  1.00 38.48           C  
ANISOU 4897  CB  LEU C 190     6629   3427   4567  -1085    578   -328       C  
ATOM   4898  CG  LEU C 190      82.529   8.502   6.845  1.00 44.18           C  
ANISOU 4898  CG  LEU C 190     7341   4092   5354  -1261    405   -373       C  
ATOM   4899  CD1 LEU C 190      82.045   9.503   7.897  1.00 44.97           C  
ANISOU 4899  CD1 LEU C 190     7773   4056   5256  -1268    319   -394       C  
ATOM   4900  CD2 LEU C 190      83.375   7.380   7.424  1.00 45.55           C  
ANISOU 4900  CD2 LEU C 190     7271   4356   5681  -1267    237   -381       C  
ATOM   4901  N   GLY C 191      79.566   8.180   3.450  1.00 35.27           N  
ANISOU 4901  N   GLY C 191     6333   3019   4050   -918    935   -248       N  
ATOM   4902  CA  GLY C 191      78.256   7.948   2.864  1.00 34.35           C  
ANISOU 4902  CA  GLY C 191     6285   2916   3849   -760   1005   -201       C  
ATOM   4903  C   GLY C 191      78.258   7.336   1.484  1.00 36.77           C  
ANISOU 4903  C   GLY C 191     6504   3270   4198   -763   1104   -178       C  
ATOM   4904  O   GLY C 191      77.400   6.509   1.185  1.00 37.09           O  
ANISOU 4904  O   GLY C 191     6500   3371   4222   -643   1108   -145       O  
ATOM   4905  N   PHE C 192      79.212   7.732   0.631  1.00 32.76           N  
ANISOU 4905  N   PHE C 192     5986   2725   3736   -910   1191   -196       N  
ATOM   4906  CA  PHE C 192      79.253   7.300  -0.757  1.00 32.00           C  
ANISOU 4906  CA  PHE C 192     5880   2641   3637   -926   1315   -179       C  
ATOM   4907  C   PHE C 192      80.486   6.461  -1.146  1.00 35.90           C  
ANISOU 4907  C   PHE C 192     6149   3207   4285  -1020   1403   -219       C  
ATOM   4908  O   PHE C 192      80.310   5.356  -1.654  1.00 33.08           O  
ANISOU 4908  O   PHE C 192     5703   2914   3952   -946   1440   -216       O  
ATOM   4909  CB  PHE C 192      79.092   8.528  -1.687  1.00 33.44           C  
ANISOU 4909  CB  PHE C 192     6316   2690   3700   -995   1398   -153       C  
ATOM   4910  CG  PHE C 192      79.360   8.335  -3.166  1.00 35.15           C  
ANISOU 4910  CG  PHE C 192     6600   2879   3877  -1063   1548   -140       C  
ATOM   4911  CD1 PHE C 192      78.764   7.291  -3.872  1.00 37.14           C  
ANISOU 4911  CD1 PHE C 192     6824   3190   4098   -962   1558   -122       C  
ATOM   4912  CD2 PHE C 192      80.177   9.223  -3.864  1.00 37.03           C  
ANISOU 4912  CD2 PHE C 192     6967   3015   4088  -1240   1684   -146       C  
ATOM   4913  CE1 PHE C 192      79.027   7.107  -5.237  1.00 37.82           C  
ANISOU 4913  CE1 PHE C 192     7026   3231   4114  -1029   1701   -116       C  
ATOM   4914  CE2 PHE C 192      80.416   9.053  -5.234  1.00 39.41           C  
ANISOU 4914  CE2 PHE C 192     7380   3275   4321  -1308   1851   -134       C  
ATOM   4915  CZ  PHE C 192      79.826   8.006  -5.915  1.00 37.43           C  
ANISOU 4915  CZ  PHE C 192     7123   3079   4021  -1196   1855   -121       C  
ATOM   4916  N   LEU C 193      81.707   6.987  -0.970  1.00 33.97           N  
ANISOU 4916  N   LEU C 193     5814   2941   4153  -1184   1443   -257       N  
ATOM   4917  CA  LEU C 193      82.902   6.293  -1.445  1.00 33.74           C  
ANISOU 4917  CA  LEU C 193     5543   2973   4303  -1269   1560   -298       C  
ATOM   4918  C   LEU C 193      83.208   4.995  -0.716  1.00 38.14           C  
ANISOU 4918  C   LEU C 193     5846   3639   5006  -1166   1454   -320       C  
ATOM   4919  O   LEU C 193      83.626   4.047  -1.375  1.00 38.80           O  
ANISOU 4919  O   LEU C 193     5790   3772   5181  -1130   1567   -340       O  
ATOM   4920  CB  LEU C 193      84.133   7.209  -1.486  1.00 33.69           C  
ANISOU 4920  CB  LEU C 193     5465   2920   4417  -1486   1633   -331       C  
ATOM   4921  CG  LEU C 193      83.991   8.466  -2.365  1.00 38.55           C  
ANISOU 4921  CG  LEU C 193     6357   3402   4888  -1618   1771   -306       C  
ATOM   4922  CD1 LEU C 193      85.120   9.454  -2.114  1.00 38.42           C  
ANISOU 4922  CD1 LEU C 193     6277   3328   4992  -1856   1802   -335       C  
ATOM   4923  CD2 LEU C 193      83.837   8.121  -3.840  1.00 39.95           C  
ANISOU 4923  CD2 LEU C 193     6647   3555   4975  -1612   1994   -289       C  
ATOM   4924  N   ILE C 194      82.966   4.911   0.603  1.00 34.12           N  
ANISOU 4924  N   ILE C 194     5312   3151   4500  -1109   1247   -316       N  
ATOM   4925  CA  ILE C 194      83.207   3.663   1.317  1.00 32.89           C  
ANISOU 4925  CA  ILE C 194     4961   3077   4458  -1007   1128   -325       C  
ATOM   4926  C   ILE C 194      82.151   2.582   0.881  1.00 35.03           C  
ANISOU 4926  C   ILE C 194     5293   3383   4634   -846   1163   -293       C  
ATOM   4927  O   ILE C 194      82.615   1.547   0.395  1.00 31.94           O  
ANISOU 4927  O   ILE C 194     4753   3033   4351   -802   1228   -313       O  
ATOM   4928  CB  ILE C 194      83.390   3.836   2.849  1.00 36.09           C  
ANISOU 4928  CB  ILE C 194     5355   3479   4879  -1011    893   -329       C  
ATOM   4929  CG1 ILE C 194      84.707   4.668   3.122  1.00 36.42           C  
ANISOU 4929  CG1 ILE C 194     5269   3493   5076  -1199    841   -370       C  
ATOM   4930  CG2 ILE C 194      83.413   2.442   3.561  1.00 36.84           C  
ANISOU 4930  CG2 ILE C 194     5316   3638   5045   -879    759   -321       C  
ATOM   4931  CD1 ILE C 194      85.027   5.046   4.625  1.00 40.19           C  
ANISOU 4931  CD1 ILE C 194     5778   3938   5553  -1245    568   -381       C  
ATOM   4932  N   PRO C 195      80.787   2.790   0.937  1.00 30.65           N  
ANISOU 4932  N   PRO C 195     4939   2805   3899   -764   1135   -249       N  
ATOM   4933  CA  PRO C 195      79.861   1.748   0.431  1.00 29.29           C  
ANISOU 4933  CA  PRO C 195     4794   2665   3668   -648   1159   -220       C  
ATOM   4934  C   PRO C 195      80.135   1.351  -1.025  1.00 35.19           C  
ANISOU 4934  C   PRO C 195     5543   3403   4426   -672   1322   -236       C  
ATOM   4935  O   PRO C 195      80.101   0.143  -1.332  1.00 36.56           O  
ANISOU 4935  O   PRO C 195     5651   3605   4637   -605   1339   -243       O  
ATOM   4936  CB  PRO C 195      78.476   2.401   0.566  1.00 29.76           C  
ANISOU 4936  CB  PRO C 195     5042   2695   3571   -588   1123   -172       C  
ATOM   4937  CG  PRO C 195      78.640   3.366   1.676  1.00 33.77           C  
ANISOU 4937  CG  PRO C 195     5608   3167   4056   -623   1044   -181       C  
ATOM   4938  CD  PRO C 195      80.025   3.927   1.499  1.00 30.02           C  
ANISOU 4938  CD  PRO C 195     5056   2667   3684   -766   1078   -226       C  
ATOM   4939  N   LEU C 196      80.442   2.336  -1.908  1.00 30.06           N  
ANISOU 4939  N   LEU C 196     4999   2693   3729   -774   1448   -243       N  
ATOM   4940  CA  LEU C 196      80.736   2.054  -3.318  1.00 30.93           C  
ANISOU 4940  CA  LEU C 196     5169   2771   3811   -814   1631   -261       C  
ATOM   4941  C   LEU C 196      81.946   1.138  -3.456  1.00 36.55           C  
ANISOU 4941  C   LEU C 196     5655   3525   4706   -823   1738   -319       C  
ATOM   4942  O   LEU C 196      81.876   0.166  -4.206  1.00 37.29           O  
ANISOU 4942  O   LEU C 196     5768   3616   4785   -765   1826   -336       O  
ATOM   4943  CB  LEU C 196      80.861   3.333  -4.190  1.00 31.06           C  
ANISOU 4943  CB  LEU C 196     5381   2696   3724   -937   1756   -251       C  
ATOM   4944  CG  LEU C 196      81.254   3.145  -5.689  1.00 35.83           C  
ANISOU 4944  CG  LEU C 196     6109   3244   4261  -1001   1978   -269       C  
ATOM   4945  CD1 LEU C 196      80.157   2.478  -6.475  1.00 35.88           C  
ANISOU 4945  CD1 LEU C 196     6312   3222   4098   -906   1930   -236       C  
ATOM   4946  CD2 LEU C 196      81.598   4.483  -6.348  1.00 35.75           C  
ANISOU 4946  CD2 LEU C 196     6281   3133   4168  -1155   2114   -258       C  
ATOM   4947  N   SER C 197      83.021   1.399  -2.680  1.00 33.54           N  
ANISOU 4947  N   SER C 197     5059   3177   4508   -885   1709   -350       N  
ATOM   4948  CA  SER C 197      84.222   0.554  -2.667  1.00 33.01           C  
ANISOU 4948  CA  SER C 197     4718   3155   4670   -871   1782   -404       C  
ATOM   4949  C   SER C 197      83.915  -0.824  -2.078  1.00 36.40           C  
ANISOU 4949  C   SER C 197     5063   3625   5144   -708   1646   -400       C  
ATOM   4950  O   SER C 197      84.461  -1.806  -2.583  1.00 39.21           O  
ANISOU 4950  O   SER C 197     5308   3985   5607   -642   1759   -440       O  
ATOM   4951  CB  SER C 197      85.386   1.237  -1.952  1.00 36.72           C  
ANISOU 4951  CB  SER C 197     4964   3647   5341   -986   1733   -431       C  
ATOM   4952  OG  SER C 197      85.172   1.302  -0.551  1.00 50.65           O  
ANISOU 4952  OG  SER C 197     6688   5436   7120   -946   1460   -408       O  
ATOM   4953  N   VAL C 198      82.992  -0.927  -1.084  1.00 29.54           N  
ANISOU 4953  N   VAL C 198     4276   2769   4177   -640   1432   -353       N  
ATOM   4954  CA  VAL C 198      82.602  -2.240  -0.532  1.00 29.28           C  
ANISOU 4954  CA  VAL C 198     4210   2757   4158   -505   1311   -338       C  
ATOM   4955  C   VAL C 198      81.918  -3.105  -1.619  1.00 35.58           C  
ANISOU 4955  C   VAL C 198     5142   3525   4852   -444   1424   -338       C  
ATOM   4956  O   VAL C 198      82.217  -4.296  -1.726  1.00 36.82           O  
ANISOU 4956  O   VAL C 198     5228   3674   5087   -356   1437   -361       O  
ATOM   4957  CB  VAL C 198      81.761  -2.177   0.782  1.00 31.37           C  
ANISOU 4957  CB  VAL C 198     4555   3034   4330   -465   1096   -286       C  
ATOM   4958  CG1 VAL C 198      81.284  -3.577   1.199  1.00 30.43           C  
ANISOU 4958  CG1 VAL C 198     4444   2918   4200   -348   1005   -262       C  
ATOM   4959  CG2 VAL C 198      82.553  -1.533   1.917  1.00 30.48           C  
ANISOU 4959  CG2 VAL C 198     4337   2931   4314   -520    952   -296       C  
ATOM   4960  N   MET C 199      81.028  -2.497  -2.440  1.00 33.01           N  
ANISOU 4960  N   MET C 199     5025   3169   4349   -492   1491   -313       N  
ATOM   4961  CA  MET C 199      80.330  -3.202  -3.523  1.00 32.23           C  
ANISOU 4961  CA  MET C 199     5091   3028   4128   -460   1563   -311       C  
ATOM   4962  C   MET C 199      81.313  -3.672  -4.565  1.00 37.32           C  
ANISOU 4962  C   MET C 199     5710   3633   4836   -470   1779   -377       C  
ATOM   4963  O   MET C 199      81.261  -4.837  -4.968  1.00 36.08           O  
ANISOU 4963  O   MET C 199     5587   3444   4676   -397   1814   -403       O  
ATOM   4964  CB  MET C 199      79.206  -2.362  -4.134  1.00 34.12           C  
ANISOU 4964  CB  MET C 199     5553   3234   4176   -505   1543   -264       C  
ATOM   4965  CG  MET C 199      78.038  -2.196  -3.213  1.00 38.20           C  
ANISOU 4965  CG  MET C 199     6090   3786   4640   -458   1359   -202       C  
ATOM   4966  SD  MET C 199      76.576  -1.429  -3.937  1.00 43.41           S  
ANISOU 4966  SD  MET C 199     6964   4407   5122   -464   1299   -142       S  
ATOM   4967  CE  MET C 199      77.159   0.312  -4.154  1.00 40.12           C  
ANISOU 4967  CE  MET C 199     6629   3943   4671   -549   1384   -146       C  
ATOM   4968  N   CYS C 200      82.270  -2.795  -4.915  1.00 36.54           N  
ANISOU 4968  N   CYS C 200     5543   3532   4811   -563   1934   -409       N  
ATOM   4969  CA  CYS C 200      83.361  -3.046  -5.872  1.00 38.02           C  
ANISOU 4969  CA  CYS C 200     5674   3686   5087   -589   2201   -478       C  
ATOM   4970  C   CYS C 200      84.221  -4.244  -5.429  1.00 41.24           C  
ANISOU 4970  C   CYS C 200     5830   4119   5719   -469   2211   -529       C  
ATOM   4971  O   CYS C 200      84.569  -5.108  -6.243  1.00 41.15           O  
ANISOU 4971  O   CYS C 200     5853   4058   5725   -406   2389   -583       O  
ATOM   4972  CB  CYS C 200      84.200  -1.781  -6.053  1.00 38.94           C  
ANISOU 4972  CB  CYS C 200     5723   3803   5271   -736   2346   -491       C  
ATOM   4973  SG  CYS C 200      83.443  -0.546  -7.139  1.00 43.12           S  
ANISOU 4973  SG  CYS C 200     6626   4242   5514   -868   2443   -449       S  
ATOM   4974  N   PHE C 201      84.508  -4.301  -4.115  1.00 37.54           N  
ANISOU 4974  N   PHE C 201     5143   3712   5407   -427   2002   -509       N  
ATOM   4975  CA  PHE C 201      85.237  -5.375  -3.469  1.00 36.82           C  
ANISOU 4975  CA  PHE C 201     4820   3637   5531   -297   1929   -538       C  
ATOM   4976  C   PHE C 201      84.452  -6.717  -3.537  1.00 39.98           C  
ANISOU 4976  C   PHE C 201     5375   3988   5829   -166   1854   -527       C  
ATOM   4977  O   PHE C 201      85.052  -7.728  -3.880  1.00 40.02           O  
ANISOU 4977  O   PHE C 201     5303   3951   5953    -55   1952   -579       O  
ATOM   4978  CB  PHE C 201      85.608  -4.983  -2.032  1.00 38.23           C  
ANISOU 4978  CB  PHE C 201     4804   3875   5846   -306   1679   -506       C  
ATOM   4979  CG  PHE C 201      86.266  -6.095  -1.253  1.00 40.36           C  
ANISOU 4979  CG  PHE C 201     4864   4147   6323   -159   1539   -520       C  
ATOM   4980  CD1 PHE C 201      87.499  -6.613  -1.650  1.00 43.68           C  
ANISOU 4980  CD1 PHE C 201     5028   4565   7004    -88   1686   -586       C  
ATOM   4981  CD2 PHE C 201      85.639  -6.652  -0.143  1.00 42.74           C  
ANISOU 4981  CD2 PHE C 201     5240   4443   6559    -81   1273   -465       C  
ATOM   4982  CE1 PHE C 201      88.098  -7.662  -0.939  1.00 44.70           C  
ANISOU 4982  CE1 PHE C 201     4968   4680   7336     77   1535   -595       C  
ATOM   4983  CE2 PHE C 201      86.247  -7.686   0.576  1.00 45.81           C  
ANISOU 4983  CE2 PHE C 201     5476   4810   7121     61   1123   -468       C  
ATOM   4984  CZ  PHE C 201      87.470  -8.187   0.170  1.00 43.81           C  
ANISOU 4984  CZ  PHE C 201     4961   4549   7136    149   1238   -532       C  
ATOM   4985  N   PHE C 202      83.122  -6.711  -3.262  1.00 35.50           N  
ANISOU 4985  N   PHE C 202     5019   3415   5054   -182   1699   -463       N  
ATOM   4986  CA  PHE C 202      82.284  -7.908  -3.330  1.00 35.33           C  
ANISOU 4986  CA  PHE C 202     5151   3341   4931   -100   1620   -446       C  
ATOM   4987  C   PHE C 202      82.052  -8.377  -4.767  1.00 42.95           C  
ANISOU 4987  C   PHE C 202     6324   4226   5771   -105   1808   -490       C  
ATOM   4988  O   PHE C 202      81.960  -9.585  -4.993  1.00 43.50           O  
ANISOU 4988  O   PHE C 202     6471   4224   5832    -19   1808   -513       O  
ATOM   4989  CB  PHE C 202      80.978  -7.752  -2.541  1.00 36.65           C  
ANISOU 4989  CB  PHE C 202     5434   3536   4956   -130   1412   -364       C  
ATOM   4990  CG  PHE C 202      81.198  -8.085  -1.083  1.00 37.81           C  
ANISOU 4990  CG  PHE C 202     5450   3711   5204    -70   1220   -330       C  
ATOM   4991  CD1 PHE C 202      81.083  -9.396  -0.627  1.00 40.99           C  
ANISOU 4991  CD1 PHE C 202     5876   4063   5635     25   1124   -318       C  
ATOM   4992  CD2 PHE C 202      81.643  -7.113  -0.189  1.00 37.89           C  
ANISOU 4992  CD2 PHE C 202     5340   3778   5278   -114   1133   -315       C  
ATOM   4993  CE1 PHE C 202      81.340  -9.713   0.718  1.00 41.06           C  
ANISOU 4993  CE1 PHE C 202     5807   4079   5716     79    936   -280       C  
ATOM   4994  CE2 PHE C 202      81.928  -7.440   1.141  1.00 40.15           C  
ANISOU 4994  CE2 PHE C 202     5547   4072   5636    -63    939   -286       C  
ATOM   4995  CZ  PHE C 202      81.751  -8.730   1.590  1.00 38.51           C  
ANISOU 4995  CZ  PHE C 202     5380   3814   5438     35    841   -264       C  
ATOM   4996  N   TYR C 203      82.059  -7.447  -5.739  1.00 41.84           N  
ANISOU 4996  N   TYR C 203     6296   4074   5526   -207   1971   -506       N  
ATOM   4997  CA  TYR C 203      82.007  -7.749  -7.171  1.00 43.51           C  
ANISOU 4997  CA  TYR C 203     6744   4193   5596   -228   2173   -555       C  
ATOM   4998  C   TYR C 203      83.308  -8.511  -7.542  1.00 45.93           C  
ANISOU 4998  C   TYR C 203     6915   4457   6080   -134   2404   -646       C  
ATOM   4999  O   TYR C 203      83.237  -9.519  -8.236  1.00 43.91           O  
ANISOU 4999  O   TYR C 203     6824   4104   5755    -66   2497   -695       O  
ATOM   5000  CB  TYR C 203      81.822  -6.456  -8.003  1.00 47.21           C  
ANISOU 5000  CB  TYR C 203     7377   4651   5910   -364   2285   -539       C  
ATOM   5001  CG  TYR C 203      82.224  -6.558  -9.460  1.00 53.39           C  
ANISOU 5001  CG  TYR C 203     8379   5333   6575   -402   2568   -604       C  
ATOM   5002  CD1 TYR C 203      81.609  -7.470 -10.312  1.00 55.47           C  
ANISOU 5002  CD1 TYR C 203     8930   5492   6654   -375   2580   -628       C  
ATOM   5003  CD2 TYR C 203      83.183  -5.706 -10.000  1.00 56.52           C  
ANISOU 5003  CD2 TYR C 203     8728   5726   7021   -487   2828   -639       C  
ATOM   5004  CE1 TYR C 203      81.988  -7.581 -11.647  1.00 57.64           C  
ANISOU 5004  CE1 TYR C 203     9461   5655   6786   -411   2852   -693       C  
ATOM   5005  CE2 TYR C 203      83.570  -5.806 -11.339  1.00 58.32           C  
ANISOU 5005  CE2 TYR C 203     9190   5850   7120   -529   3128   -699       C  
ATOM   5006  CZ  TYR C 203      82.954  -6.732 -12.163  1.00 69.46           C  
ANISOU 5006  CZ  TYR C 203    10916   7150   8326   -486   3139   -727       C  
ATOM   5007  OH  TYR C 203      83.306  -6.817 -13.491  1.00 77.34           O  
ANISOU 5007  OH  TYR C 203    12205   8026   9155   -533   3441   -789       O  
ATOM   5008  N   TYR C 204      84.472  -8.064  -7.008  1.00 43.36           N  
ANISOU 5008  N   TYR C 204     6277   4199   6000   -125   2479   -670       N  
ATOM   5009  CA  TYR C 204      85.762  -8.731  -7.179  1.00 43.62           C  
ANISOU 5009  CA  TYR C 204     6088   4210   6275    -15   2681   -753       C  
ATOM   5010  C   TYR C 204      85.713 -10.147  -6.551  1.00 49.35           C  
ANISOU 5010  C   TYR C 204     6765   4892   7094    165   2523   -760       C  
ATOM   5011  O   TYR C 204      86.201 -11.103  -7.170  1.00 48.35           O  
ANISOU 5011  O   TYR C 204     6676   4675   7020    284   2702   -833       O  
ATOM   5012  CB  TYR C 204      86.905  -7.907  -6.549  1.00 45.24           C  
ANISOU 5012  CB  TYR C 204     5922   4511   6757    -58   2711   -761       C  
ATOM   5013  CG  TYR C 204      88.198  -8.684  -6.415  1.00 48.73           C  
ANISOU 5013  CG  TYR C 204     6042   4951   7524     90   2833   -832       C  
ATOM   5014  CD1 TYR C 204      88.546  -9.295  -5.211  1.00 50.92           C  
ANISOU 5014  CD1 TYR C 204     6069   5262   8015    220   2568   -810       C  
ATOM   5015  CD2 TYR C 204      89.024  -8.897  -7.516  1.00 50.41           C  
ANISOU 5015  CD2 TYR C 204     6226   5109   7819    119   3214   -922       C  
ATOM   5016  CE1 TYR C 204      89.699 -10.073  -5.099  1.00 51.50           C  
ANISOU 5016  CE1 TYR C 204     5840   5321   8407    388   2649   -871       C  
ATOM   5017  CE2 TYR C 204      90.184  -9.667  -7.415  1.00 51.96           C  
ANISOU 5017  CE2 TYR C 204     6101   5297   8343    287   3340   -992       C  
ATOM   5018  CZ  TYR C 204      90.521 -10.245  -6.200  1.00 62.74           C  
ANISOU 5018  CZ  TYR C 204     7190   6702   9946    427   3040   -965       C  
ATOM   5019  OH  TYR C 204      91.666 -10.997  -6.094  1.00 69.77           O  
ANISOU 5019  OH  TYR C 204     7749   7578  11184    616   3136  -1029       O  
ATOM   5020  N   LYS C 205      85.154 -10.261  -5.310  1.00 45.81           N  
ANISOU 5020  N   LYS C 205     6256   4492   6656    185   2202   -684       N  
ATOM   5021  CA  LYS C 205      85.011 -11.525  -4.571  1.00 44.63           C  
ANISOU 5021  CA  LYS C 205     6100   4291   6568    333   2016   -668       C  
ATOM   5022  C   LYS C 205      84.152 -12.507  -5.362  1.00 48.55           C  
ANISOU 5022  C   LYS C 205     6923   4668   6856    359   2056   -684       C  
ATOM   5023  O   LYS C 205      84.496 -13.682  -5.462  1.00 47.69           O  
ANISOU 5023  O   LYS C 205     6841   4460   6821    502   2089   -728       O  
ATOM   5024  CB  LYS C 205      84.413 -11.288  -3.170  1.00 45.83           C  
ANISOU 5024  CB  LYS C 205     6203   4508   6702    305   1697   -575       C  
ATOM   5025  CG  LYS C 205      85.345 -10.552  -2.211  1.00 54.03           C  
ANISOU 5025  CG  LYS C 205     6934   5634   7959    302   1594   -565       C  
ATOM   5026  CD  LYS C 205      85.569 -11.279  -0.884  1.00 67.15           C  
ANISOU 5026  CD  LYS C 205     8497   7281   9735    418   1317   -521       C  
ATOM   5027  CE  LYS C 205      86.782 -12.192  -0.887  1.00 78.73           C  
ANISOU 5027  CE  LYS C 205     9743   8694  11476    602   1347   -577       C  
ATOM   5028  NZ  LYS C 205      88.068 -11.442  -0.809  1.00 86.03           N  
ANISOU 5028  NZ  LYS C 205    10313   9697  12680    590   1398   -618       N  
ATOM   5029  N   MET C 206      83.062 -12.008  -5.964  1.00 46.45           N  
ANISOU 5029  N   MET C 206     6912   4401   6337    221   2047   -651       N  
ATOM   5030  CA  MET C 206      82.145 -12.811  -6.772  1.00 46.38           C  
ANISOU 5030  CA  MET C 206     7231   4278   6113    203   2047   -661       C  
ATOM   5031  C   MET C 206      82.752 -13.336  -8.071  1.00 52.09           C  
ANISOU 5031  C   MET C 206     8117   4880   6795    255   2334   -765       C  
ATOM   5032  O   MET C 206      82.497 -14.493  -8.391  1.00 52.19           O  
ANISOU 5032  O   MET C 206     8328   4766   6737    323   2327   -799       O  
ATOM   5033  CB  MET C 206      80.866 -12.039  -7.066  1.00 48.44           C  
ANISOU 5033  CB  MET C 206     7683   4575   6147     46   1931   -595       C  
ATOM   5034  CG  MET C 206      79.995 -11.889  -5.880  1.00 52.32           C  
ANISOU 5034  CG  MET C 206     8091   5146   6642     12   1668   -500       C  
ATOM   5035  SD  MET C 206      78.497 -10.998  -6.259  1.00 56.90           S  
ANISOU 5035  SD  MET C 206     8842   5768   7008   -140   1546   -426       S  
ATOM   5036  CE  MET C 206      77.714 -12.171  -7.273  1.00 53.21           C  
ANISOU 5036  CE  MET C 206     8680   5166   6374   -167   1505   -447       C  
ATOM   5037  N   VAL C 207      83.546 -12.515  -8.824  1.00 49.81           N  
ANISOU 5037  N   VAL C 207     7772   4615   6540    216   2603   -818       N  
ATOM   5038  CA  VAL C 207      84.154 -12.988 -10.083  1.00 50.58           C  
ANISOU 5038  CA  VAL C 207     8049   4587   6582    263   2931   -924       C  
ATOM   5039  C   VAL C 207      85.212 -14.052  -9.784  1.00 53.50           C  
ANISOU 5039  C   VAL C 207     8217   4900   7210    474   3045   -998       C  
ATOM   5040  O   VAL C 207      85.242 -15.046 -10.493  1.00 53.88           O  
ANISOU 5040  O   VAL C 207     8499   4798   7176    563   3183  -1072       O  
ATOM   5041  CB  VAL C 207      84.648 -11.902 -11.094  1.00 55.23           C  
ANISOU 5041  CB  VAL C 207     8701   5187   7095    146   3231   -961       C  
ATOM   5042  CG1 VAL C 207      83.574 -10.844 -11.334  1.00 54.76           C  
ANISOU 5042  CG1 VAL C 207     8860   5164   6782    -37   3077   -879       C  
ATOM   5043  CG2 VAL C 207      85.960 -11.250 -10.664  1.00 55.53           C  
ANISOU 5043  CG2 VAL C 207     8323   5334   7441    167   3395   -982       C  
ATOM   5044  N   VAL C 208      85.998 -13.888  -8.694  1.00 49.41           N  
ANISOU 5044  N   VAL C 208     7293   4487   6994    558   2948   -975       N  
ATOM   5045  CA  VAL C 208      87.004 -14.851  -8.228  1.00 49.54           C  
ANISOU 5045  CA  VAL C 208     7068   4456   7299    781   2985  -1028       C  
ATOM   5046  C   VAL C 208      86.336 -16.191  -7.837  1.00 54.22           C  
ANISOU 5046  C   VAL C 208     7873   4924   7806    892   2768  -1008       C  
ATOM   5047  O   VAL C 208      86.880 -17.246  -8.167  1.00 55.71           O  
ANISOU 5047  O   VAL C 208     8108   4976   8082   1072   2903  -1086       O  
ATOM   5048  CB  VAL C 208      87.917 -14.276  -7.107  1.00 53.36           C  
ANISOU 5048  CB  VAL C 208     7081   5079   8114    823   2863   -994       C  
ATOM   5049  CG1 VAL C 208      88.867 -15.339  -6.541  1.00 52.99           C  
ANISOU 5049  CG1 VAL C 208     6783   4972   8379   1077   2843  -1038       C  
ATOM   5050  CG2 VAL C 208      88.710 -13.083  -7.616  1.00 53.20           C  
ANISOU 5050  CG2 VAL C 208     6857   5159   8198    700   3113  -1024       C  
ATOM   5051  N   PHE C 209      85.150 -16.148  -7.187  1.00 49.30           N  
ANISOU 5051  N   PHE C 209     7391   4331   7008    781   2459   -909       N  
ATOM   5052  CA  PHE C 209      84.401 -17.359  -6.822  1.00 48.35           C  
ANISOU 5052  CA  PHE C 209     7495   4089   6787    836   2256   -878       C  
ATOM   5053  C   PHE C 209      83.922 -18.091  -8.090  1.00 54.76           C  
ANISOU 5053  C   PHE C 209     8708   4731   7369    817   2413   -950       C  
ATOM   5054  O   PHE C 209      84.205 -19.282  -8.243  1.00 54.30           O  
ANISOU 5054  O   PHE C 209     8776   4510   7344    968   2454  -1006       O  
ATOM   5055  CB  PHE C 209      83.211 -17.045  -5.869  1.00 48.69           C  
ANISOU 5055  CB  PHE C 209     7581   4215   6704    694   1935   -755       C  
ATOM   5056  CG  PHE C 209      82.445 -18.272  -5.413  1.00 48.42           C  
ANISOU 5056  CG  PHE C 209     7758   4056   6584    724   1736   -714       C  
ATOM   5057  CD1 PHE C 209      82.880 -19.021  -4.322  1.00 49.76           C  
ANISOU 5057  CD1 PHE C 209     7805   4183   6916    867   1575   -679       C  
ATOM   5058  CD2 PHE C 209      81.323 -18.715  -6.111  1.00 48.73           C  
ANISOU 5058  CD2 PHE C 209     8133   4001   6380    602   1704   -710       C  
ATOM   5059  CE1 PHE C 209      82.203 -20.192  -3.941  1.00 49.28           C  
ANISOU 5059  CE1 PHE C 209     7977   3981   6766    883   1412   -639       C  
ATOM   5060  CE2 PHE C 209      80.638 -19.873  -5.713  1.00 49.76           C  
ANISOU 5060  CE2 PHE C 209     8462   4002   6441    604   1533   -672       C  
ATOM   5061  CZ  PHE C 209      81.082 -20.600  -4.633  1.00 46.86           C  
ANISOU 5061  CZ  PHE C 209     7990   3589   6227    742   1402   -636       C  
ATOM   5062  N   LEU C 210      83.239 -17.372  -9.005  1.00 53.85           N  
ANISOU 5062  N   LEU C 210     8812   4635   7016    640   2492   -952       N  
ATOM   5063  CA  LEU C 210      82.708 -17.942 -10.249  1.00 55.17           C  
ANISOU 5063  CA  LEU C 210     9406   4635   6921    588   2604  -1016       C  
ATOM   5064  C   LEU C 210      83.800 -18.478 -11.180  1.00 62.73           C  
ANISOU 5064  C   LEU C 210    10448   5456   7932    742   2970  -1152       C  
ATOM   5065  O   LEU C 210      83.581 -19.516 -11.811  1.00 62.63           O  
ANISOU 5065  O   LEU C 210    10770   5250   7777    793   3023  -1219       O  
ATOM   5066  CB  LEU C 210      81.771 -16.960 -10.987  1.00 55.05           C  
ANISOU 5066  CB  LEU C 210     9604   4669   6643    368   2564   -975       C  
ATOM   5067  CG  LEU C 210      80.531 -16.477 -10.204  1.00 59.60           C  
ANISOU 5067  CG  LEU C 210    10133   5360   7153    224   2220   -848       C  
ATOM   5068  CD1 LEU C 210      79.906 -15.274 -10.870  1.00 60.25           C  
ANISOU 5068  CD1 LEU C 210    10333   5510   7050     54   2206   -810       C  
ATOM   5069  CD2 LEU C 210      79.491 -17.572 -10.039  1.00 62.10           C  
ANISOU 5069  CD2 LEU C 210    10672   5566   7359    185   1990   -817       C  
ATOM   5070  N   LYS C 211      84.981 -17.808 -11.232  1.00 61.68           N  
ANISOU 5070  N   LYS C 211    10005   5412   8017    817   3228  -1198       N  
ATOM   5071  CA  LYS C 211      86.134 -18.244 -12.041  1.00 62.30           C  
ANISOU 5071  CA  LYS C 211    10084   5380   8207    979   3630  -1331       C  
ATOM   5072  C   LYS C 211      86.681 -19.589 -11.516  1.00 69.37           C  
ANISOU 5072  C   LYS C 211    10889   6152   9316   1238   3597  -1377       C  
ATOM   5073  O   LYS C 211      86.986 -20.474 -12.311  1.00 69.02           O  
ANISOU 5073  O   LYS C 211    11078   5921   9225   1372   3843  -1487       O  
ATOM   5074  CB  LYS C 211      87.235 -17.169 -12.091  1.00 63.74           C  
ANISOU 5074  CB  LYS C 211     9894   5708   8618    973   3894  -1353       C  
ATOM   5075  N   LYS C 212      86.755 -19.751 -10.182  1.00 68.79           N  
ANISOU 5075  N   LYS C 212    10523   6164   9451   1308   3287  -1290       N  
ATOM   5076  CA  LYS C 212      87.202 -20.987  -9.531  1.00 69.74           C  
ANISOU 5076  CA  LYS C 212    10571   6161   9767   1551   3184  -1308       C  
ATOM   5077  C   LYS C 212      86.124 -22.082  -9.659  1.00 77.50           C  
ANISOU 5077  C   LYS C 212    12010   6954  10481   1516   2998  -1293       C  
ATOM   5078  O   LYS C 212      86.466 -23.243  -9.886  1.00 77.11           O  
ANISOU 5078  O   LYS C 212    12126   6703  10470   1706   3078  -1367       O  
ATOM   5079  CB  LYS C 212      87.571 -20.736  -8.055  1.00 71.52           C  
ANISOU 5079  CB  LYS C 212    10377   6530  10268   1614   2889  -1210       C  
ATOM   5080  N   ARG C 213      84.827 -21.700  -9.537  1.00 77.11           N  
ANISOU 5080  N   ARG C 213    12159   6964  10176   1270   2755  -1200       N  
ATOM   5081  CA  ARG C 213      83.670 -22.596  -9.657  1.00 78.19           C  
ANISOU 5081  CA  ARG C 213    12699   6947  10060   1170   2552  -1172       C  
ATOM   5082  C   ARG C 213      83.547 -23.140 -11.093  1.00 86.32           C  
ANISOU 5082  C   ARG C 213    14174   7768  10857   1163   2785  -1292       C  
ATOM   5083  O   ARG C 213      83.200 -24.310 -11.262  1.00 86.26           O  
ANISOU 5083  O   ARG C 213    14475   7548  10754   1216   2719  -1325       O  
ATOM   5084  CB  ARG C 213      82.373 -21.903  -9.182  1.00 77.15           C  
ANISOU 5084  CB  ARG C 213    12592   6960   9761    907   2272  -1047       C  
ATOM   5085  CG  ARG C 213      81.144 -22.809  -9.114  1.00 87.11           C  
ANISOU 5085  CG  ARG C 213    14194   8091  10814    773   2031   -999       C  
ATOM   5086  CD  ARG C 213      80.501 -22.871  -7.735  1.00 96.33           C  
ANISOU 5086  CD  ARG C 213    15201   9346  12054    711   1723   -867       C  
ATOM   5087  NE  ARG C 213      81.302 -23.620  -6.759  1.00102.48           N  
ANISOU 5087  NE  ARG C 213    15834  10055  13047    926   1671   -858       N  
ATOM   5088  CZ  ARG C 213      80.887 -23.959  -5.540  1.00113.31           C  
ANISOU 5088  CZ  ARG C 213    17145  11441  14468    906   1423   -751       C  
ATOM   5089  NH1 ARG C 213      79.666 -23.631  -5.129  1.00100.04           N  
ANISOU 5089  NH1 ARG C 213    15506   9850  12655    681   1236   -650       N  
ATOM   5090  NH2 ARG C 213      81.691 -24.622  -4.719  1.00 96.50           N  
ANISOU 5090  NH2 ARG C 213    14914   9229  12523   1116   1364   -743       N  
ATOM   5091  N   SER C 214      83.875 -22.310 -12.115  1.00 85.09           N  
ANISOU 5091  N   SER C 214    14081   7652  10596   1096   3064  -1358       N  
ATOM   5092  CA  SER C 214      83.854 -22.701 -13.534  1.00 85.48           C  
ANISOU 5092  CA  SER C 214    14589   7500  10390   1081   3321  -1479       C  
ATOM   5093  C   SER C 214      84.941 -23.739 -13.836  1.00 90.51           C  
ANISOU 5093  C   SER C 214    15270   7944  11177   1366   3621  -1613       C  
ATOM   5094  O   SER C 214      84.660 -24.734 -14.509  1.00 90.74           O  
ANISOU 5094  O   SER C 214    15742   7726  11009   1400   3673  -1695       O  
ATOM   5095  CB  SER C 214      84.037 -21.483 -14.440  1.00 89.14           C  
ANISOU 5095  CB  SER C 214    15094   8058  10717    944   3559  -1504       C  
ATOM   5096  OG  SER C 214      82.994 -20.538 -14.271  1.00 98.57           O  
ANISOU 5096  OG  SER C 214    16268   9411  11774    705   3286  -1385       O  
ATOM   5097  N   GLN C 215      86.177 -23.505 -13.334  1.00 87.46           N  
ANISOU 5097  N   GLN C 215    14421   7661  11151   1572   3807  -1638       N  
ATOM   5098  CA  GLN C 215      87.331 -24.396 -13.521  1.00 87.55           C  
ANISOU 5098  CA  GLN C 215    14362   7514  11387   1884   4103  -1762       C  
ATOM   5099  C   GLN C 215      87.188 -25.721 -12.749  1.00 93.41           C  
ANISOU 5099  C   GLN C 215    15175   8089  12228   2065   3851  -1743       C  
ATOM   5100  O   GLN C 215      87.831 -26.710 -13.119  1.00 93.72           O  
ANISOU 5100  O   GLN C 215    15349   7912  12349   2314   4066  -1857       O  
ATOM   5101  CB  GLN C 215      88.647 -23.682 -13.166  1.00 88.46           C  
ANISOU 5101  CB  GLN C 215    13905   7810  11895   2029   4337  -1781       C  
ATOM   5102  N   GLN C 216      86.326 -25.744 -11.703  1.00 91.06           N  
ANISOU 5102  N   GLN C 216    14816   7873  11908   1939   3415  -1601       N  
ATOM   5103  CA  GLN C 216      86.054 -26.919 -10.864  1.00 91.41           C  
ANISOU 5103  CA  GLN C 216    14959   7763  12010   2058   3135  -1554       C  
ATOM   5104  C   GLN C 216      84.818 -27.691 -11.350  1.00 95.96           C  
ANISOU 5104  C   GLN C 216    16104   8131  12226   1881   2985  -1556       C  
ATOM   5105  O   GLN C 216      84.956 -28.816 -11.843  1.00 95.52           O  
ANISOU 5105  O   GLN C 216    16377   7802  12115   2030   3063  -1643       O  
ATOM   5106  CB  GLN C 216      85.912 -26.519  -9.380  1.00 92.70           C  
ANISOU 5106  CB  GLN C 216    14751   8120  12351   2014   2774  -1398       C  
ATOM   5107  N   GLN C 217      83.619 -27.079 -11.223  1.00 92.55           N  
ANISOU 5107  N   GLN C 217    15780   7823  11562   1564   2766  -1463       N  
ATOM   5108  CA  GLN C 217      82.336 -27.663 -11.624  1.00117.65           C  
ANISOU 5108  CA  GLN C 217    19437  10846  14420   1340   2573  -1446       C  
ATOM   5109  C   GLN C 217      81.813 -27.022 -12.909  1.00130.04           C  
ANISOU 5109  C   GLN C 217    21275  12432  15701   1131   2699  -1498       C  
ATOM   5110  O   GLN C 217      82.166 -27.451 -14.005  1.00 83.18           O  
ANISOU 5110  O   GLN C 217    15754   6278   9571   1161   2900  -1622       O  
ATOM   5111  CB  GLN C 217      81.305 -27.513 -10.493  1.00118.97           C  
ANISOU 5111  CB  GLN C 217    19486  11132  14583   1145   2175  -1282       C  
ATOM   5112  N   ASN C 224      76.792 -16.177 -13.927  1.00 69.65           N  
ANISOU 5112  N   ASN C 224    12792   6302   7370   -354   1818   -821       N  
ATOM   5113  CA  ASN C 224      76.680 -14.765 -14.272  1.00 68.70           C  
ANISOU 5113  CA  ASN C 224    12590   6300   7212   -414   1856   -774       C  
ATOM   5114  C   ASN C 224      75.493 -14.082 -13.586  1.00 71.44           C  
ANISOU 5114  C   ASN C 224    12748   6792   7603   -510   1538   -648       C  
ATOM   5115  O   ASN C 224      75.615 -12.917 -13.204  1.00 71.40           O  
ANISOU 5115  O   ASN C 224    12529   6922   7678   -509   1565   -597       O  
ATOM   5116  CB  ASN C 224      76.607 -14.585 -15.789  1.00 68.30           C  
ANISOU 5116  CB  ASN C 224    12979   6108   6866   -494   1980   -830       C  
ATOM   5117  N   LYS C 225      74.356 -14.802 -13.423  1.00 66.34           N  
ANISOU 5117  N   LYS C 225    12174   6113   6919   -595   1251   -599       N  
ATOM   5118  CA  LYS C 225      73.103 -14.308 -12.823  1.00 65.24           C  
ANISOU 5118  CA  LYS C 225    11855   6098   6838   -687    955   -484       C  
ATOM   5119  C   LYS C 225      73.292 -13.554 -11.476  1.00 66.80           C  
ANISOU 5119  C   LYS C 225    11631   6488   7264   -617    974   -416       C  
ATOM   5120  O   LYS C 225      72.744 -12.459 -11.379  1.00 65.75           O  
ANISOU 5120  O   LYS C 225    11398   6453   7131   -655    877   -349       O  
ATOM   5121  CB  LYS C 225      72.055 -15.432 -12.698  1.00 68.27           C  
ANISOU 5121  CB  LYS C 225    12317   6413   7211   -784    701   -455       C  
ATOM   5122  CG  LYS C 225      70.612 -14.941 -12.553  1.00 81.89           C  
ANISOU 5122  CG  LYS C 225    13942   8223   8949   -911    392   -349       C  
ATOM   5123  CD  LYS C 225      69.613 -16.101 -12.600  1.00 88.59           C  
ANISOU 5123  CD  LYS C 225    14883   8987   9791  -1042    153   -328       C  
ATOM   5124  CE  LYS C 225      68.189 -15.676 -12.320  1.00 94.22           C  
ANISOU 5124  CE  LYS C 225    15394   9810  10596  -1159   -135   -219       C  
ATOM   5125  NZ  LYS C 225      67.565 -14.996 -13.487  1.00101.64           N  
ANISOU 5125  NZ  LYS C 225    16535  10708  11376  -1238   -328   -201       N  
ATOM   5126  N   PRO C 226      74.061 -14.029 -10.451  1.00 62.73           N  
ANISOU 5126  N   PRO C 226    10887   6017   6931   -511   1083   -432       N  
ATOM   5127  CA  PRO C 226      74.209 -13.206  -9.229  1.00 61.28           C  
ANISOU 5127  CA  PRO C 226    10363   6000   6922   -463   1076   -369       C  
ATOM   5128  C   PRO C 226      75.019 -11.922  -9.412  1.00 61.37           C  
ANISOU 5128  C   PRO C 226    10290   6080   6948   -427   1246   -386       C  
ATOM   5129  O   PRO C 226      74.832 -10.991  -8.625  1.00 62.93           O  
ANISOU 5129  O   PRO C 226    10281   6400   7231   -426   1193   -327       O  
ATOM   5130  CB  PRO C 226      74.857 -14.162  -8.226  1.00 63.19           C  
ANISOU 5130  CB  PRO C 226    10456   6233   7319   -365   1115   -385       C  
ATOM   5131  CG  PRO C 226      75.606 -15.130  -9.059  1.00 68.24           C  
ANISOU 5131  CG  PRO C 226    11310   6715   7902   -305   1263   -483       C  
ATOM   5132  CD  PRO C 226      74.810 -15.303 -10.329  1.00 64.12           C  
ANISOU 5132  CD  PRO C 226    11122   6082   7159   -421   1194   -504       C  
ATOM   5133  N   LEU C 227      75.927 -11.867 -10.425  1.00 54.08           N  
ANISOU 5133  N   LEU C 227     9539   5069   5942   -405   1468   -470       N  
ATOM   5134  CA  LEU C 227      76.766 -10.682 -10.746  1.00 51.54           C  
ANISOU 5134  CA  LEU C 227     9167   4790   5627   -401   1667   -491       C  
ATOM   5135  C   LEU C 227      75.974  -9.473 -11.255  1.00 50.91           C  
ANISOU 5135  C   LEU C 227     9207   4734   5403   -497   1563   -428       C  
ATOM   5136  O   LEU C 227      76.445  -8.351 -11.102  1.00 49.44           O  
ANISOU 5136  O   LEU C 227     8919   4609   5257   -506   1661   -414       O  
ATOM   5137  CB  LEU C 227      77.842 -11.016 -11.794  1.00 51.18           C  
ANISOU 5137  CB  LEU C 227     9307   4627   5513   -370   1963   -597       C  
ATOM   5138  CG  LEU C 227      79.190 -11.539 -11.316  1.00 55.58           C  
ANISOU 5138  CG  LEU C 227     9637   5193   6287   -242   2184   -669       C  
ATOM   5139  CD1 LEU C 227      80.136 -11.693 -12.491  1.00 55.18           C  
ANISOU 5139  CD1 LEU C 227     9786   5025   6157   -221   2516   -773       C  
ATOM   5140  CD2 LEU C 227      79.825 -10.617 -10.289  1.00 58.16           C  
ANISOU 5140  CD2 LEU C 227     9604   5667   6825   -222   2207   -635       C  
ATOM   5141  N   ARG C 228      74.817  -9.708 -11.922  1.00 46.43           N  
ANISOU 5141  N   ARG C 228     8872   4102   4670   -572   1358   -393       N  
ATOM   5142  CA  ARG C 228      73.920  -8.692 -12.492  1.00 45.56           C  
ANISOU 5142  CA  ARG C 228     8902   3989   4419   -646   1201   -326       C  
ATOM   5143  C   ARG C 228      73.652  -7.550 -11.507  1.00 45.89           C  
ANISOU 5143  C   ARG C 228     8667   4169   4598   -620   1129   -251       C  
ATOM   5144  O   ARG C 228      73.917  -6.393 -11.847  1.00 46.14           O  
ANISOU 5144  O   ARG C 228     8762   4198   4570   -637   1205   -236       O  
ATOM   5145  CB  ARG C 228      72.566  -9.309 -12.882  1.00 46.65           C  
ANISOU 5145  CB  ARG C 228     9192   4074   4460   -716    906   -283       C  
ATOM   5146  CG  ARG C 228      72.426  -9.856 -14.290  1.00 57.04           C  
ANISOU 5146  CG  ARG C 228    10935   5214   5523   -789    887   -333       C  
ATOM   5147  CD  ARG C 228      70.985 -10.301 -14.581  1.00 67.77           C  
ANISOU 5147  CD  ARG C 228    12397   6535   6818   -879    530   -276       C  
ATOM   5148  NE  ARG C 228      70.379 -11.024 -13.454  1.00 79.52           N  
ANISOU 5148  NE  ARG C 228    13577   8118   8517   -874    395   -237       N  
ATOM   5149  CZ  ARG C 228      69.108 -11.415 -13.386  1.00 97.42           C  
ANISOU 5149  CZ  ARG C 228    15793  10399  10824   -957     97   -174       C  
ATOM   5150  NH1 ARG C 228      68.659 -12.045 -12.309  1.00 85.97           N  
ANISOU 5150  NH1 ARG C 228    14067   9032   9566   -962     33   -139       N  
ATOM   5151  NH2 ARG C 228      68.278 -11.180 -14.395  1.00 87.73           N  
ANISOU 5151  NH2 ARG C 228    14792   9097   9446  -1043   -145   -141       N  
ATOM   5152  N   LEU C 229      73.145  -7.887 -10.290  1.00 38.95           N  
ANISOU 5152  N   LEU C 229     7516   3394   3890   -582   1000   -207       N  
ATOM   5153  CA  LEU C 229      72.786  -6.933  -9.231  1.00 37.36           C  
ANISOU 5153  CA  LEU C 229     7070   3313   3813   -548    934   -142       C  
ATOM   5154  C   LEU C 229      73.946  -6.036  -8.778  1.00 39.81           C  
ANISOU 5154  C   LEU C 229     7265   3666   4195   -515   1128   -169       C  
ATOM   5155  O   LEU C 229      73.767  -4.817  -8.765  1.00 38.69           O  
ANISOU 5155  O   LEU C 229     7130   3545   4027   -523   1112   -132       O  
ATOM   5156  CB  LEU C 229      72.119  -7.621  -8.016  1.00 36.77           C  
ANISOU 5156  CB  LEU C 229     6765   3320   3885   -523    811   -100       C  
ATOM   5157  CG  LEU C 229      71.595  -6.657  -6.929  1.00 40.73           C  
ANISOU 5157  CG  LEU C 229     7053   3931   4491   -484    754    -36       C  
ATOM   5158  CD1 LEU C 229      70.195  -7.025  -6.476  1.00 41.04           C  
ANISOU 5158  CD1 LEU C 229     6988   4017   4589   -504    572     33       C  
ATOM   5159  CD2 LEU C 229      72.575  -6.509  -5.771  1.00 39.60           C  
ANISOU 5159  CD2 LEU C 229     6733   3849   4464   -430    878    -59       C  
ATOM   5160  N   VAL C 230      75.110  -6.620  -8.410  1.00 36.64           N  
ANISOU 5160  N   VAL C 230     6755   3270   3895   -477   1293   -233       N  
ATOM   5161  CA  VAL C 230      76.261  -5.853  -7.924  1.00 36.92           C  
ANISOU 5161  CA  VAL C 230     6639   3352   4037   -463   1451   -260       C  
ATOM   5162  C   VAL C 230      76.832  -4.942  -9.026  1.00 39.80           C  
ANISOU 5162  C   VAL C 230     7186   3650   4286   -529   1624   -287       C  
ATOM   5163  O   VAL C 230      77.056  -3.770  -8.734  1.00 39.30           O  
ANISOU 5163  O   VAL C 230     7069   3618   4244   -560   1650   -262       O  
ATOM   5164  CB  VAL C 230      77.354  -6.683  -7.183  1.00 41.44           C  
ANISOU 5164  CB  VAL C 230     7006   3952   4786   -396   1545   -313       C  
ATOM   5165  CG1 VAL C 230      78.160  -7.580  -8.115  1.00 41.00           C  
ANISOU 5165  CG1 VAL C 230     7056   3807   4715   -373   1733   -396       C  
ATOM   5166  CG2 VAL C 230      78.274  -5.783  -6.350  1.00 41.27           C  
ANISOU 5166  CG2 VAL C 230     6770   4004   4908   -394   1603   -317       C  
ATOM   5167  N   VAL C 231      77.006  -5.438 -10.274  1.00 36.53           N  
ANISOU 5167  N   VAL C 231     7022   3130   3729   -560   1738   -333       N  
ATOM   5168  CA  VAL C 231      77.521  -4.630 -11.400  1.00 36.86           C  
ANISOU 5168  CA  VAL C 231     7299   3085   3621   -638   1928   -355       C  
ATOM   5169  C   VAL C 231      76.588  -3.446 -11.629  1.00 40.73           C  
ANISOU 5169  C   VAL C 231     7938   3560   3978   -685   1762   -273       C  
ATOM   5170  O   VAL C 231      77.057  -2.315 -11.644  1.00 40.65           O  
ANISOU 5170  O   VAL C 231     7938   3544   3962   -734   1864   -259       O  
ATOM   5171  CB  VAL C 231      77.764  -5.435 -12.708  1.00 41.16           C  
ANISOU 5171  CB  VAL C 231     8150   3496   3991   -661   2080   -421       C  
ATOM   5172  CG1 VAL C 231      78.393  -4.554 -13.786  1.00 40.72           C  
ANISOU 5172  CG1 VAL C 231     8351   3346   3773   -754   2321   -442       C  
ATOM   5173  CG2 VAL C 231      78.636  -6.654 -12.448  1.00 41.29           C  
ANISOU 5173  CG2 VAL C 231     8015   3514   4159   -580   2241   -506       C  
ATOM   5174  N   LEU C 232      75.264  -3.706 -11.704  1.00 37.92           N  
ANISOU 5174  N   LEU C 232     7664   3197   3546   -667   1494   -215       N  
ATOM   5175  CA  LEU C 232      74.256  -2.668 -11.871  1.00 38.07           C  
ANISOU 5175  CA  LEU C 232     7789   3201   3475   -676   1297   -132       C  
ATOM   5176  C   LEU C 232      74.277  -1.645 -10.733  1.00 40.80           C  
ANISOU 5176  C   LEU C 232     7894   3640   3970   -636   1275    -93       C  
ATOM   5177  O   LEU C 232      74.248  -0.455 -11.007  1.00 40.00           O  
ANISOU 5177  O   LEU C 232     7917   3489   3791   -660   1279    -57       O  
ATOM   5178  CB  LEU C 232      72.851  -3.245 -12.102  1.00 38.39           C  
ANISOU 5178  CB  LEU C 232     7893   3230   3464   -660   1005    -82       C  
ATOM   5179  CG  LEU C 232      71.776  -2.224 -12.522  1.00 42.93           C  
ANISOU 5179  CG  LEU C 232     8603   3763   3943   -653    778      4       C  
ATOM   5180  CD1 LEU C 232      72.185  -1.457 -13.764  1.00 42.40           C  
ANISOU 5180  CD1 LEU C 232     8913   3553   3642   -718    866      4       C  
ATOM   5181  CD2 LEU C 232      70.462  -2.904 -12.771  1.00 46.48           C  
ANISOU 5181  CD2 LEU C 232     9075   4207   4380   -652    485     48       C  
ATOM   5182  N   ALA C 233      74.399  -2.095  -9.479  1.00 37.78           N  
ANISOU 5182  N   ALA C 233     7211   3368   3778   -582   1260   -103       N  
ATOM   5183  CA  ALA C 233      74.491  -1.192  -8.331  1.00 36.19           C  
ANISOU 5183  CA  ALA C 233     6814   3240   3697   -549   1246    -77       C  
ATOM   5184  C   ALA C 233      75.759  -0.331  -8.391  1.00 39.32           C  
ANISOU 5184  C   ALA C 233     7220   3611   4110   -614   1450   -115       C  
ATOM   5185  O   ALA C 233      75.649   0.877  -8.228  1.00 39.58           O  
ANISOU 5185  O   ALA C 233     7307   3619   4114   -630   1432    -82       O  
ATOM   5186  CB  ALA C 233      74.440  -1.978  -7.040  1.00 36.63           C  
ANISOU 5186  CB  ALA C 233     6604   3397   3916   -490   1194    -83       C  
ATOM   5187  N   VAL C 234      76.945  -0.926  -8.696  1.00 35.45           N  
ANISOU 5187  N   VAL C 234     6685   3112   3670   -654   1651   -186       N  
ATOM   5188  CA  VAL C 234      78.218  -0.182  -8.814  1.00 35.32           C  
ANISOU 5188  CA  VAL C 234     6637   3076   3706   -740   1869   -226       C  
ATOM   5189  C   VAL C 234      78.106   0.899  -9.915  1.00 38.94           C  
ANISOU 5189  C   VAL C 234     7408   3419   3969   -830   1944   -196       C  
ATOM   5190  O   VAL C 234      78.592   2.005  -9.732  1.00 38.07           O  
ANISOU 5190  O   VAL C 234     7305   3286   3876   -903   2015   -186       O  
ATOM   5191  CB  VAL C 234      79.444  -1.122  -9.023  1.00 38.24           C  
ANISOU 5191  CB  VAL C 234     6879   3458   4193   -746   2083   -308       C  
ATOM   5192  CG1 VAL C 234      80.641  -0.363  -9.592  1.00 37.93           C  
ANISOU 5192  CG1 VAL C 234     6861   3375   4178   -863   2353   -348       C  
ATOM   5193  CG2 VAL C 234      79.835  -1.821  -7.724  1.00 37.40           C  
ANISOU 5193  CG2 VAL C 234     6449   3453   4308   -666   2000   -329       C  
ATOM   5194  N   VAL C 235      77.432   0.563 -11.038  1.00 35.44           N  
ANISOU 5194  N   VAL C 235     7250   2887   3327   -831   1907   -180       N  
ATOM   5195  CA  VAL C 235      77.191   1.450 -12.166  1.00 34.33           C  
ANISOU 5195  CA  VAL C 235     7474   2613   2958   -906   1936   -142       C  
ATOM   5196  C   VAL C 235      76.161   2.547 -11.817  1.00 38.80           C  
ANISOU 5196  C   VAL C 235     8107   3158   3478   -862   1700    -55       C  
ATOM   5197  O   VAL C 235      76.493   3.724 -11.926  1.00 38.56           O  
ANISOU 5197  O   VAL C 235     8198   3058   3396   -928   1774    -31       O  
ATOM   5198  CB  VAL C 235      76.832   0.666 -13.457  1.00 36.68           C  
ANISOU 5198  CB  VAL C 235     8085   2807   3043   -921   1940   -155       C  
ATOM   5199  CG1 VAL C 235      76.382   1.618 -14.566  1.00 35.27           C  
ANISOU 5199  CG1 VAL C 235     8330   2474   2597   -986   1893    -95       C  
ATOM   5200  CG2 VAL C 235      78.015  -0.174 -13.923  1.00 36.12           C  
ANISOU 5200  CG2 VAL C 235     8006   2720   2998   -965   2251   -250       C  
ATOM   5201  N   ILE C 236      74.926   2.176 -11.415  1.00 35.57           N  
ANISOU 5201  N   ILE C 236     7621   2799   3096   -752   1432     -9       N  
ATOM   5202  CA  ILE C 236      73.886   3.160 -11.070  1.00 34.90           C  
ANISOU 5202  CA  ILE C 236     7567   2696   3000   -676   1217     69       C  
ATOM   5203  C   ILE C 236      74.420   4.195 -10.079  1.00 38.60           C  
ANISOU 5203  C   ILE C 236     7898   3189   3578   -682   1298     66       C  
ATOM   5204  O   ILE C 236      74.366   5.385 -10.381  1.00 40.26           O  
ANISOU 5204  O   ILE C 236     8311   3294   3693   -706   1295    105       O  
ATOM   5205  CB  ILE C 236      72.545   2.507 -10.610  1.00 36.82           C  
ANISOU 5205  CB  ILE C 236     7651   3016   3324   -560    956    110       C  
ATOM   5206  CG1 ILE C 236      71.876   1.789 -11.816  1.00 36.36           C  
ANISOU 5206  CG1 ILE C 236     7823   2882   3109   -579    812    130       C  
ATOM   5207  CG2 ILE C 236      71.598   3.577 -10.006  1.00 36.30           C  
ANISOU 5207  CG2 ILE C 236     7529   2951   3314   -452    790    178       C  
ATOM   5208  CD1 ILE C 236      70.482   1.099 -11.588  1.00 42.32           C  
ANISOU 5208  CD1 ILE C 236     8433   3701   3948   -499    527    177       C  
ATOM   5209  N   PHE C 237      75.008   3.742  -8.953  1.00 33.32           N  
ANISOU 5209  N   PHE C 237     6928   2638   3094   -673   1367     18       N  
ATOM   5210  CA  PHE C 237      75.538   4.629  -7.926  1.00 32.48           C  
ANISOU 5210  CA  PHE C 237     6699   2553   3089   -691   1415      7       C  
ATOM   5211  C   PHE C 237      76.753   5.444  -8.380  1.00 39.51           C  
ANISOU 5211  C   PHE C 237     7711   3360   3941   -843   1620    -20       C  
ATOM   5212  O   PHE C 237      76.803   6.623  -8.047  1.00 41.66           O  
ANISOU 5212  O   PHE C 237     8075   3564   4190   -871   1607      3       O  
ATOM   5213  CB  PHE C 237      75.795   3.895  -6.615  1.00 33.37           C  
ANISOU 5213  CB  PHE C 237     6499   2796   3385   -647   1396    -30       C  
ATOM   5214  CG  PHE C 237      74.486   3.624  -5.906  1.00 33.84           C  
ANISOU 5214  CG  PHE C 237     6466   2915   3479   -512   1209     13       C  
ATOM   5215  CD1 PHE C 237      73.765   4.662  -5.315  1.00 34.45           C  
ANISOU 5215  CD1 PHE C 237     6578   2962   3549   -438   1122     52       C  
ATOM   5216  CD2 PHE C 237      73.955   2.339  -5.858  1.00 34.42           C  
ANISOU 5216  CD2 PHE C 237     6424   3060   3594   -461   1137     15       C  
ATOM   5217  CE1 PHE C 237      72.544   4.415  -4.691  1.00 34.38           C  
ANISOU 5217  CE1 PHE C 237     6463   3009   3592   -311    991     90       C  
ATOM   5218  CE2 PHE C 237      72.734   2.094  -5.224  1.00 36.28           C  
ANISOU 5218  CE2 PHE C 237     6557   3350   3879   -359    992     59       C  
ATOM   5219  CZ  PHE C 237      72.031   3.135  -4.658  1.00 33.99           C  
ANISOU 5219  CZ  PHE C 237     6277   3043   3597   -282    931     96       C  
ATOM   5220  N   SER C 238      77.679   4.881  -9.172  1.00 35.99           N  
ANISOU 5220  N   SER C 238     7288   2904   3484   -942   1820    -68       N  
ATOM   5221  CA  SER C 238      78.788   5.680  -9.706  1.00 35.79           C  
ANISOU 5221  CA  SER C 238     7379   2794   3427  -1106   2049    -89       C  
ATOM   5222  C   SER C 238      78.272   6.750 -10.671  1.00 40.85           C  
ANISOU 5222  C   SER C 238     8417   3269   3835  -1152   2032    -24       C  
ATOM   5223  O   SER C 238      78.716   7.896 -10.589  1.00 41.09           O  
ANISOU 5223  O   SER C 238     8552   3216   3844  -1256   2107    -10       O  
ATOM   5224  CB  SER C 238      79.799   4.818 -10.451  1.00 38.17           C  
ANISOU 5224  CB  SER C 238     7637   3108   3759  -1186   2303   -154       C  
ATOM   5225  OG  SER C 238      80.480   3.933  -9.583  1.00 48.56           O  
ANISOU 5225  OG  SER C 238     8585   4555   5310  -1147   2330   -214       O  
ATOM   5226  N   VAL C 239      77.347   6.390 -11.590  1.00 37.43           N  
ANISOU 5226  N   VAL C 239     8226   2774   3222  -1083   1916     17       N  
ATOM   5227  CA  VAL C 239      76.849   7.351 -12.597  1.00 37.60           C  
ANISOU 5227  CA  VAL C 239     8668   2617   3001  -1117   1867     87       C  
ATOM   5228  C   VAL C 239      75.918   8.426 -11.972  1.00 42.23           C  
ANISOU 5228  C   VAL C 239     9297   3157   3592  -1009   1634    156       C  
ATOM   5229  O   VAL C 239      76.023   9.594 -12.332  1.00 40.26           O  
ANISOU 5229  O   VAL C 239     9320   2758   3221  -1074   1663    199       O  
ATOM   5230  CB  VAL C 239      76.219   6.644 -13.835  1.00 40.54           C  
ANISOU 5230  CB  VAL C 239     9323   2916   3164  -1091   1792    109       C  
ATOM   5231  CG1 VAL C 239      75.568   7.640 -14.784  1.00 39.81           C  
ANISOU 5231  CG1 VAL C 239     9677   2631   2818  -1099   1663    196       C  
ATOM   5232  CG2 VAL C 239      77.260   5.813 -14.578  1.00 40.15           C  
ANISOU 5232  CG2 VAL C 239     9327   2861   3068  -1210   2090     35       C  
ATOM   5233  N   LEU C 240      75.041   8.037 -11.025  1.00 40.36           N  
ANISOU 5233  N   LEU C 240     8799   3036   3498   -848   1429    163       N  
ATOM   5234  CA  LEU C 240      74.095   8.985 -10.421  1.00 39.43           C  
ANISOU 5234  CA  LEU C 240     8705   2876   3402   -715   1234    220       C  
ATOM   5235  C   LEU C 240      74.667   9.843  -9.287  1.00 41.39           C  
ANISOU 5235  C   LEU C 240     8833   3129   3763   -747   1313    191       C  
ATOM   5236  O   LEU C 240      74.353  11.030  -9.202  1.00 40.91           O  
ANISOU 5236  O   LEU C 240     8964   2940   3640   -714   1254    231       O  
ATOM   5237  CB  LEU C 240      72.812   8.263  -9.940  1.00 39.42           C  
ANISOU 5237  CB  LEU C 240     8493   2983   3502   -530   1003    245       C  
ATOM   5238  CG  LEU C 240      71.947   7.523 -10.990  1.00 43.41           C  
ANISOU 5238  CG  LEU C 240     9124   3467   3903   -484    834    286       C  
ATOM   5239  CD1 LEU C 240      70.615   7.141 -10.386  1.00 44.08           C  
ANISOU 5239  CD1 LEU C 240     8979   3645   4126   -312    599    322       C  
ATOM   5240  CD2 LEU C 240      71.714   8.357 -12.262  1.00 44.13           C  
ANISOU 5240  CD2 LEU C 240     9647   3360   3761   -512    758    352       C  
ATOM   5241  N   PHE C 241      75.473   9.259  -8.409  1.00 36.69           N  
ANISOU 5241  N   PHE C 241     7946   2665   3329   -806   1424    122       N  
ATOM   5242  CA  PHE C 241      75.984  10.010  -7.269  1.00 35.55           C  
ANISOU 5242  CA  PHE C 241     7698   2523   3286   -844   1456     91       C  
ATOM   5243  C   PHE C 241      77.257  10.812  -7.529  1.00 39.84           C  
ANISOU 5243  C   PHE C 241     8355   2972   3808  -1060   1644     65       C  
ATOM   5244  O   PHE C 241      77.448  11.801  -6.850  1.00 41.52           O  
ANISOU 5244  O   PHE C 241     8617   3117   4042  -1099   1628     59       O  
ATOM   5245  CB  PHE C 241      76.169   9.094  -6.045  1.00 35.99           C  
ANISOU 5245  CB  PHE C 241     7401   2749   3523   -795   1430     39       C  
ATOM   5246  CG  PHE C 241      74.901   8.695  -5.317  1.00 36.44           C  
ANISOU 5246  CG  PHE C 241     7340   2881   3625   -598   1260     65       C  
ATOM   5247  CD1 PHE C 241      73.650   8.849  -5.913  1.00 38.47           C  
ANISOU 5247  CD1 PHE C 241     7725   3088   3803   -464   1128    129       C  
ATOM   5248  CD2 PHE C 241      74.957   8.158  -4.036  1.00 36.91           C  
ANISOU 5248  CD2 PHE C 241     7158   3056   3811   -552   1231     29       C  
ATOM   5249  CE1 PHE C 241      72.485   8.476  -5.238  1.00 38.74           C  
ANISOU 5249  CE1 PHE C 241     7604   3200   3915   -294    997    152       C  
ATOM   5250  CE2 PHE C 241      73.789   7.787  -3.364  1.00 38.67           C  
ANISOU 5250  CE2 PHE C 241     7276   3342   4074   -387   1118     55       C  
ATOM   5251  CZ  PHE C 241      72.563   7.937  -3.975  1.00 36.45           C  
ANISOU 5251  CZ  PHE C 241     7080   3025   3745   -263   1016    114       C  
ATOM   5252  N   THR C 242      78.129  10.399  -8.450  1.00 35.48           N  
ANISOU 5252  N   THR C 242     7843   2412   3225  -1207   1833     44       N  
ATOM   5253  CA  THR C 242      79.395  11.092  -8.687  1.00 35.09           C  
ANISOU 5253  CA  THR C 242     7850   2288   3193  -1435   2048     17       C  
ATOM   5254  C   THR C 242      79.219  12.581  -9.099  1.00 40.11           C  
ANISOU 5254  C   THR C 242     8865   2713   3661  -1511   2045     74       C  
ATOM   5255  O   THR C 242      79.843  13.399  -8.424  1.00 40.69           O  
ANISOU 5255  O   THR C 242     8910   2742   3810  -1630   2077     53       O  
ATOM   5256  CB  THR C 242      80.314  10.314  -9.658  1.00 35.87           C  
ANISOU 5256  CB  THR C 242     7910   2419   3298  -1563   2298    -21       C  
ATOM   5257  OG1 THR C 242      80.633   9.062  -9.069  1.00 40.14           O  
ANISOU 5257  OG1 THR C 242     8084   3138   4030  -1493   2294    -80       O  
ATOM   5258  CG2 THR C 242      81.614  11.038  -9.948  1.00 34.95           C  
ANISOU 5258  CG2 THR C 242     7821   2231   3228  -1816   2555    -46       C  
ATOM   5259  N   PRO C 243      78.465  13.001 -10.162  1.00 36.80           N  
ANISOU 5259  N   PRO C 243     8819   2145   3016  -1461   1994    147       N  
ATOM   5260  CA  PRO C 243      78.464  14.444 -10.499  1.00 36.32           C  
ANISOU 5260  CA  PRO C 243     9134   1862   2804  -1547   2001    201       C  
ATOM   5261  C   PRO C 243      77.961  15.327  -9.356  1.00 43.71           C  
ANISOU 5261  C   PRO C 243    10053   2752   3802  -1438   1825    206       C  
ATOM   5262  O   PRO C 243      78.577  16.357  -9.062  1.00 43.07           O  
ANISOU 5262  O   PRO C 243    10101   2549   3717  -1590   1897    199       O  
ATOM   5263  CB  PRO C 243      77.622  14.530 -11.782  1.00 37.02           C  
ANISOU 5263  CB  PRO C 243     9609   1812   2645  -1467   1919    282       C  
ATOM   5264  CG  PRO C 243      77.666  13.114 -12.364  1.00 41.59           C  
ANISOU 5264  CG  PRO C 243    10039   2531   3232  -1448   1982    250       C  
ATOM   5265  CD  PRO C 243      77.684  12.221 -11.155  1.00 37.20           C  
ANISOU 5265  CD  PRO C 243     9006   2199   2931  -1349   1921    183       C  
ATOM   5266  N   TYR C 244      76.902  14.853  -8.645  1.00 42.70           N  
ANISOU 5266  N   TYR C 244     9744   2730   3749  -1190   1618    209       N  
ATOM   5267  CA  TYR C 244      76.290  15.523  -7.494  1.00 41.33           C  
ANISOU 5267  CA  TYR C 244     9540   2527   3636  -1046   1473    203       C  
ATOM   5268  C   TYR C 244      77.291  15.704  -6.357  1.00 44.92           C  
ANISOU 5268  C   TYR C 244     9798   3038   4231  -1193   1553    127       C  
ATOM   5269  O   TYR C 244      77.395  16.806  -5.837  1.00 44.76           O  
ANISOU 5269  O   TYR C 244     9953   2875   4179  -1234   1531    122       O  
ATOM   5270  CB  TYR C 244      75.030  14.767  -7.037  1.00 41.31           C  
ANISOU 5270  CB  TYR C 244     9337   2653   3706   -774   1291    217       C  
ATOM   5271  CG  TYR C 244      74.560  15.148  -5.651  1.00 42.12           C  
ANISOU 5271  CG  TYR C 244     9319   2778   3907   -636   1209    185       C  
ATOM   5272  CD1 TYR C 244      73.957  16.384  -5.409  1.00 43.80           C  
ANISOU 5272  CD1 TYR C 244     9785   2809   4050   -521   1133    214       C  
ATOM   5273  CD2 TYR C 244      74.757  14.294  -4.568  1.00 42.25           C  
ANISOU 5273  CD2 TYR C 244     9006   2976   4070   -621   1220    124       C  
ATOM   5274  CE1 TYR C 244      73.556  16.756  -4.122  1.00 41.25           C  
ANISOU 5274  CE1 TYR C 244     9389   2487   3797   -394   1093    174       C  
ATOM   5275  CE2 TYR C 244      74.395  14.673  -3.275  1.00 42.97           C  
ANISOU 5275  CE2 TYR C 244     9042   3068   4216   -515   1170     91       C  
ATOM   5276  CZ  TYR C 244      73.785  15.901  -3.059  1.00 44.83           C  
ANISOU 5276  CZ  TYR C 244     9534   3125   4377   -399   1119    112       C  
ATOM   5277  OH  TYR C 244      73.413  16.266  -1.790  1.00 43.76           O  
ANISOU 5277  OH  TYR C 244     9376   2975   4277   -286   1097     69       O  
ATOM   5278  N   HIS C 245      78.031  14.633  -5.976  1.00 41.12           N  
ANISOU 5278  N   HIS C 245     8974   2747   3904  -1271   1628     68       N  
ATOM   5279  CA  HIS C 245      79.028  14.726  -4.914  1.00 40.27           C  
ANISOU 5279  CA  HIS C 245     8661   2696   3943  -1414   1661     -1       C  
ATOM   5280  C   HIS C 245      80.206  15.628  -5.291  1.00 47.56           C  
ANISOU 5280  C   HIS C 245     9722   3491   4858  -1700   1813    -13       C  
ATOM   5281  O   HIS C 245      80.703  16.318  -4.408  1.00 47.74           O  
ANISOU 5281  O   HIS C 245     9744   3458   4937  -1805   1770    -49       O  
ATOM   5282  CB  HIS C 245      79.483  13.355  -4.430  1.00 39.71           C  
ANISOU 5282  CB  HIS C 245     8198   2844   4045  -1402   1672    -52       C  
ATOM   5283  CG  HIS C 245      78.461  12.684  -3.563  1.00 42.06           C  
ANISOU 5283  CG  HIS C 245     8353   3251   4378  -1169   1512    -53       C  
ATOM   5284  ND1 HIS C 245      77.429  11.955  -4.103  1.00 43.04           N  
ANISOU 5284  ND1 HIS C 245     8467   3433   4454   -990   1457    -12       N  
ATOM   5285  CD2 HIS C 245      78.329  12.692  -2.216  1.00 42.79           C  
ANISOU 5285  CD2 HIS C 245     8336   3386   4534  -1108   1406    -89       C  
ATOM   5286  CE1 HIS C 245      76.709  11.538  -3.077  1.00 42.00           C  
ANISOU 5286  CE1 HIS C 245     8193   3386   4379   -832   1343    -22       C  
ATOM   5287  NE2 HIS C 245      77.207  11.968  -1.924  1.00 42.20           N  
ANISOU 5287  NE2 HIS C 245     8177   3400   4457   -890   1318    -67       N  
ATOM   5288  N   ILE C 246      80.632  15.666  -6.580  1.00 45.34           N  
ANISOU 5288  N   ILE C 246     9586   3146   4496  -1838   1992     17       N  
ATOM   5289  CA  ILE C 246      81.723  16.564  -6.964  1.00 45.98           C  
ANISOU 5289  CA  ILE C 246     9805   3093   4571  -2133   2168     12       C  
ATOM   5290  C   ILE C 246      81.231  18.019  -6.849  1.00 51.08           C  
ANISOU 5290  C   ILE C 246    10856   3498   5056  -2138   2076     57       C  
ATOM   5291  O   ILE C 246      81.877  18.831  -6.190  1.00 49.58           O  
ANISOU 5291  O   ILE C 246    10693   3223   4922  -2310   2074     26       O  
ATOM   5292  CB  ILE C 246      82.355  16.290  -8.368  1.00 48.86           C  
ANISOU 5292  CB  ILE C 246    10265   3428   4869  -2298   2433     33       C  
ATOM   5293  CG1 ILE C 246      82.868  14.847  -8.509  1.00 49.26           C  
ANISOU 5293  CG1 ILE C 246     9940   3696   5082  -2275   2547    -19       C  
ATOM   5294  CG2 ILE C 246      83.494  17.299  -8.658  1.00 48.04           C  
ANISOU 5294  CG2 ILE C 246    10292   3182   4781  -2631   2640     30       C  
ATOM   5295  CD1 ILE C 246      83.180  14.417 -10.036  1.00 49.60           C  
ANISOU 5295  CD1 ILE C 246    10158   3695   4992  -2361   2811      2       C  
ATOM   5296  N   MET C 247      80.069  18.315  -7.469  1.00 49.67           N  
ANISOU 5296  N   MET C 247    10985   3204   4684  -1938   1978    129       N  
ATOM   5297  CA  MET C 247      79.470  19.646  -7.520  1.00 50.07           C  
ANISOU 5297  CA  MET C 247    11454   3001   4567  -1889   1882    183       C  
ATOM   5298  C   MET C 247      79.001  20.157  -6.174  1.00 53.79           C  
ANISOU 5298  C   MET C 247    11893   3446   5097  -1749   1711    145       C  
ATOM   5299  O   MET C 247      79.030  21.363  -5.992  1.00 54.71           O  
ANISOU 5299  O   MET C 247    12324   3341   5123  -1812   1687    158       O  
ATOM   5300  CB  MET C 247      78.364  19.732  -8.582  1.00 53.06           C  
ANISOU 5300  CB  MET C 247    12140   3270   4749  -1693   1793    273       C  
ATOM   5301  CG  MET C 247      78.908  19.766 -10.027  1.00 57.85           C  
ANISOU 5301  CG  MET C 247    13008   3776   5197  -1891   1982    324       C  
ATOM   5302  SD  MET C 247      80.185  21.041 -10.332  1.00 64.48           S  
ANISOU 5302  SD  MET C 247    14148   4385   5967  -2281   2216    331       S  
ATOM   5303  CE  MET C 247      81.636  20.024 -10.315  1.00 61.05           C  
ANISOU 5303  CE  MET C 247    13260   4183   5751  -2547   2497    246       C  
ATOM   5304  N   ARG C 248      78.638  19.278  -5.213  1.00 48.82           N  
ANISOU 5304  N   ARG C 248    10921   3021   4608  -1580   1610     95       N  
ATOM   5305  CA  ARG C 248      78.265  19.720  -3.867  1.00 48.06           C  
ANISOU 5305  CA  ARG C 248    10813   2898   4551  -1461   1481     49       C  
ATOM   5306  C   ARG C 248      79.512  20.260  -3.157  1.00 52.80           C  
ANISOU 5306  C   ARG C 248    11389   3449   5224  -1748   1526    -16       C  
ATOM   5307  O   ARG C 248      79.458  21.332  -2.553  1.00 51.51           O  
ANISOU 5307  O   ARG C 248    11482   3098   4990  -1772   1465    -34       O  
ATOM   5308  CB  ARG C 248      77.613  18.592  -3.039  1.00 44.79           C  
ANISOU 5308  CB  ARG C 248    10059   2708   4250  -1238   1389     17       C  
ATOM   5309  CG  ARG C 248      77.024  19.113  -1.720  1.00 46.51           C  
ANISOU 5309  CG  ARG C 248    10341   2868   4461  -1077   1282    -23       C  
ATOM   5310  CD  ARG C 248      76.407  18.029  -0.873  1.00 42.01           C  
ANISOU 5310  CD  ARG C 248     9466   2505   3990   -886   1223    -51       C  
ATOM   5311  NE  ARG C 248      77.413  17.149  -0.283  1.00 38.44           N  
ANISOU 5311  NE  ARG C 248     8718   2224   3664  -1053   1237   -107       N  
ATOM   5312  CZ  ARG C 248      77.161  15.924   0.160  1.00 46.19           C  
ANISOU 5312  CZ  ARG C 248     9405   3407   4740   -950   1208   -121       C  
ATOM   5313  NH1 ARG C 248      75.936  15.420   0.077  1.00 32.60           N  
ANISOU 5313  NH1 ARG C 248     7625   1752   3008   -705   1177    -84       N  
ATOM   5314  NH2 ARG C 248      78.130  15.196   0.700  1.00 35.64           N  
ANISOU 5314  NH2 ARG C 248     7825   2197   3518  -1095   1198   -168       N  
ATOM   5315  N   ASN C 249      80.634  19.522  -3.245  1.00 50.68           N  
ANISOU 5315  N   ASN C 249    10812   3338   5105  -1963   1625    -53       N  
ATOM   5316  CA  ASN C 249      81.901  19.939  -2.650  1.00 50.78           C  
ANISOU 5316  CA  ASN C 249    10736   3325   5233  -2260   1649   -112       C  
ATOM   5317  C   ASN C 249      82.470  21.196  -3.339  1.00 55.64           C  
ANISOU 5317  C   ASN C 249    11695   3695   5749  -2519   1762    -81       C  
ATOM   5318  O   ASN C 249      82.882  22.124  -2.640  1.00 55.48           O  
ANISOU 5318  O   ASN C 249    11833   3526   5720  -2670   1693   -115       O  
ATOM   5319  CB  ASN C 249      82.884  18.775  -2.601  1.00 48.76           C  
ANISOU 5319  CB  ASN C 249    10026   3305   5197  -2384   1718   -154       C  
ATOM   5320  CG  ASN C 249      82.454  17.714  -1.619  1.00 62.81           C  
ANISOU 5320  CG  ASN C 249    11517   5280   7068  -2169   1571   -191       C  
ATOM   5321  OD1 ASN C 249      82.347  17.961  -0.413  1.00 61.68           O  
ANISOU 5321  OD1 ASN C 249    11380   5121   6935  -2134   1414   -234       O  
ATOM   5322  ND2 ASN C 249      82.203  16.505  -2.101  1.00 47.83           N  
ANISOU 5322  ND2 ASN C 249     9396   3554   5221  -2030   1622   -175       N  
ATOM   5323  N   VAL C 250      82.399  21.264  -4.695  1.00 52.24           N  
ANISOU 5323  N   VAL C 250    11439   3197   5212  -2564   1922    -13       N  
ATOM   5324  CA  VAL C 250      82.834  22.425  -5.479  1.00 52.46           C  
ANISOU 5324  CA  VAL C 250    11851   2972   5108  -2803   2052     34       C  
ATOM   5325  C   VAL C 250      81.976  23.663  -5.091  1.00 58.19           C  
ANISOU 5325  C   VAL C 250    13026   3432   5650  -2668   1896     61       C  
ATOM   5326  O   VAL C 250      82.525  24.753  -4.878  1.00 57.73           O  
ANISOU 5326  O   VAL C 250    13220   3164   5552  -2896   1911     52       O  
ATOM   5327  CB  VAL C 250      82.827  22.155  -7.020  1.00 56.00           C  
ANISOU 5327  CB  VAL C 250    12447   3394   5437  -2847   2251    107       C  
ATOM   5328  CG1 VAL C 250      83.024  23.445  -7.820  1.00 55.49           C  
ANISOU 5328  CG1 VAL C 250    12884   3024   5177  -3052   2362    173       C  
ATOM   5329  CG2 VAL C 250      83.883  21.124  -7.414  1.00 55.79           C  
ANISOU 5329  CG2 VAL C 250    12017   3582   5597  -3027   2463     67       C  
ATOM   5330  N   ARG C 251      80.640  23.474  -4.997  1.00 54.67           N  
ANISOU 5330  N   ARG C 251    12667   2993   5113  -2298   1751     92       N  
ATOM   5331  CA  ARG C 251      79.682  24.518  -4.640  1.00 54.72           C  
ANISOU 5331  CA  ARG C 251    13055   2765   4972  -2092   1610    115       C  
ATOM   5332  C   ARG C 251      79.975  25.134  -3.250  1.00 60.69           C  
ANISOU 5332  C   ARG C 251    13834   3447   5778  -2150   1515     30       C  
ATOM   5333  O   ARG C 251      80.062  26.359  -3.148  1.00 61.41           O  
ANISOU 5333  O   ARG C 251    14319   3261   5752  -2244   1496     35       O  
ATOM   5334  CB  ARG C 251      78.234  23.991  -4.780  1.00 53.32           C  
ANISOU 5334  CB  ARG C 251    12842   2662   4755  -1681   1485    158       C  
ATOM   5335  CG  ARG C 251      77.148  24.825  -4.108  1.00 58.31           C  
ANISOU 5335  CG  ARG C 251    13724   3119   5312  -1390   1338    158       C  
ATOM   5336  CD  ARG C 251      76.811  26.132  -4.810  1.00 48.17           C  
ANISOU 5336  CD  ARG C 251    12970   1495   3839  -1368   1312    231       C  
ATOM   5337  NE  ARG C 251      75.883  26.871  -3.965  1.00 54.47           N  
ANISOU 5337  NE  ARG C 251    13953   2137   4606  -1081   1192    207       N  
ATOM   5338  CZ  ARG C 251      75.932  28.174  -3.729  1.00 70.39           C  
ANISOU 5338  CZ  ARG C 251    16402   3841   6504  -1116   1171    203       C  
ATOM   5339  NH1 ARG C 251      75.070  28.733  -2.892  1.00 52.35           N  
ANISOU 5339  NH1 ARG C 251    14253   1430   4206   -825   1086    167       N  
ATOM   5340  NH2 ARG C 251      76.839  28.934  -4.336  1.00 64.49           N  
ANISOU 5340  NH2 ARG C 251    15964   2890   5649  -1445   1253    233       N  
ATOM   5341  N   ILE C 252      80.169  24.291  -2.205  1.00 57.47           N  
ANISOU 5341  N   ILE C 252    13044   3267   5525  -2112   1452    -46       N  
ATOM   5342  CA  ILE C 252      80.489  24.752  -0.846  1.00 56.56           C  
ANISOU 5342  CA  ILE C 252    12959   3091   5439  -2180   1343   -132       C  
ATOM   5343  C   ILE C 252      81.829  25.495  -0.846  1.00 61.70           C  
ANISOU 5343  C   ILE C 252    13705   3610   6128  -2605   1390   -160       C  
ATOM   5344  O   ILE C 252      81.893  26.614  -0.331  1.00 61.92           O  
ANISOU 5344  O   ILE C 252    14084   3388   6054  -2691   1324   -187       O  
ATOM   5345  CB  ILE C 252      80.392  23.635   0.233  1.00 58.71           C  
ANISOU 5345  CB  ILE C 252    12839   3625   5844  -2047   1254   -196       C  
ATOM   5346  CG1 ILE C 252      79.012  22.945   0.172  1.00 57.69           C  
ANISOU 5346  CG1 ILE C 252    12625   3609   5685  -1649   1228   -162       C  
ATOM   5347  CG2 ILE C 252      80.651  24.214   1.652  1.00 59.85           C  
ANISOU 5347  CG2 ILE C 252    13110   3664   5965  -2114   1123   -284       C  
ATOM   5348  CD1 ILE C 252      78.854  21.676   0.989  1.00 53.51           C  
ANISOU 5348  CD1 ILE C 252    11705   3349   5279  -1525   1177   -202       C  
ATOM   5349  N   ALA C 253      82.862  24.917  -1.495  1.00 58.81           N  
ANISOU 5349  N   ALA C 253    13045   3393   5907  -2869   1519   -150       N  
ATOM   5350  CA  ALA C 253      84.178  25.539  -1.622  1.00 58.95           C  
ANISOU 5350  CA  ALA C 253    13075   3315   6009  -3298   1597   -169       C  
ATOM   5351  C   ALA C 253      84.111  26.870  -2.370  1.00 66.76           C  
ANISOU 5351  C   ALA C 253    14585   3972   6808  -3441   1681   -110       C  
ATOM   5352  O   ALA C 253      84.849  27.791  -1.999  1.00 66.72           O  
ANISOU 5352  O   ALA C 253    14753   3786   6811  -3741   1657   -142       O  
ATOM   5353  CB  ALA C 253      85.160  24.599  -2.288  1.00 59.42           C  
ANISOU 5353  CB  ALA C 253    12702   3601   6272  -3496   1767   -164       C  
ATOM   5354  N   SER C 254      83.190  27.007  -3.378  1.00 64.75           N  
ANISOU 5354  N   SER C 254    14611   3617   6373  -3225   1750    -23       N  
ATOM   5355  CA  SER C 254      83.005  28.265  -4.129  1.00 64.58           C  
ANISOU 5355  CA  SER C 254    15143   3254   6140  -3317   1809     48       C  
ATOM   5356  C   SER C 254      82.534  29.430  -3.217  1.00 71.32           C  
ANISOU 5356  C   SER C 254    16404   3828   6868  -3233   1641     13       C  
ATOM   5357  O   SER C 254      82.771  30.593  -3.541  1.00 71.16           O  
ANISOU 5357  O   SER C 254    16829   3497   6710  -3421   1676     47       O  
ATOM   5358  CB  SER C 254      82.075  28.073  -5.328  1.00 65.57           C  
ANISOU 5358  CB  SER C 254    15470   3341   6103  -3073   1863    150       C  
ATOM   5359  OG  SER C 254      80.689  28.215  -5.057  1.00 66.47           O  
ANISOU 5359  OG  SER C 254    15752   3394   6110  -2644   1688    170       O  
ATOM   5360  N   ARG C 255      81.895  29.098  -2.068  1.00 69.55           N  
ANISOU 5360  N   ARG C 255    16043   3701   6681  -2958   1476    -56       N  
ATOM   5361  CA  ARG C 255      81.400  30.037  -1.053  1.00 69.74           C  
ANISOU 5361  CA  ARG C 255    16419   3487   6591  -2831   1333   -111       C  
ATOM   5362  C   ARG C 255      82.526  30.536  -0.122  1.00 77.20           C  
ANISOU 5362  C   ARG C 255    17369   4358   7605  -3199   1265   -201       C  
ATOM   5363  O   ARG C 255      82.294  31.401   0.725  1.00 77.05           O  
ANISOU 5363  O   ARG C 255    17694   4108   7474  -3162   1151   -259       O  
ATOM   5364  CB  ARG C 255      80.213  29.442  -0.271  1.00 68.05           C  
ANISOU 5364  CB  ARG C 255    16071   3407   6377  -2378   1228   -144       C  
ATOM   5365  CG  ARG C 255      78.983  29.137  -1.140  1.00 70.19           C  
ANISOU 5365  CG  ARG C 255    16373   3710   6586  -2008   1250    -54       C  
ATOM   5366  CD  ARG C 255      77.729  28.927  -0.314  1.00 70.77           C  
ANISOU 5366  CD  ARG C 255    16410   3827   6654  -1570   1160    -86       C  
ATOM   5367  NE  ARG C 255      77.922  27.862   0.665  1.00 83.38           N  
ANISOU 5367  NE  ARG C 255    17578   5712   8389  -1552   1132   -164       N  
ATOM   5368  CZ  ARG C 255      77.585  27.936   1.947  1.00 89.92           C  
ANISOU 5368  CZ  ARG C 255    18438   6527   9202  -1401   1069   -247       C  
ATOM   5369  NH1 ARG C 255      76.985  29.017   2.422  1.00 65.32           N  
ANISOU 5369  NH1 ARG C 255    15742   3127   5950  -1225   1044   -274       N  
ATOM   5370  NH2 ARG C 255      77.820  26.914   2.759  1.00 83.11           N  
ANISOU 5370  NH2 ARG C 255    17209   5920   8448  -1409   1040   -305       N  
ATOM   5371  N   LEU C 256      83.753  30.022  -0.323  1.00 77.08           N  
ANISOU 5371  N   LEU C 256    16984   4522   7778  -3557   1334   -214       N  
ATOM   5372  CA  LEU C 256      84.974  30.456   0.351  1.00 78.57           C  
ANISOU 5372  CA  LEU C 256    17109   4661   8083  -3970   1262   -285       C  
ATOM   5373  C   LEU C 256      85.458  31.702  -0.443  1.00 88.22           C  
ANISOU 5373  C   LEU C 256    18760   5559   9202  -4305   1374   -234       C  
ATOM   5374  O   LEU C 256      84.830  32.751  -0.297  1.00 89.72           O  
ANISOU 5374  O   LEU C 256    19479   5429   9180  -4207   1311   -230       O  
ATOM   5375  CB  LEU C 256      86.037  29.333   0.327  1.00 78.43           C  
ANISOU 5375  CB  LEU C 256    16465   4983   8350  -4177   1304   -308       C  
ATOM   5376  CG  LEU C 256      86.284  28.402   1.536  1.00 82.12           C  
ANISOU 5376  CG  LEU C 256    16535   5687   8979  -4127   1106   -397       C  
ATOM   5377  CD1 LEU C 256      85.095  28.289   2.472  1.00 82.12           C  
ANISOU 5377  CD1 LEU C 256    16692   5686   8825  -3708    965   -433       C  
ATOM   5378  CD2 LEU C 256      86.739  27.042   1.064  1.00 82.43           C  
ANISOU 5378  CD2 LEU C 256    15980   6075   9265  -4147   1199   -384       C  
ATOM   5379  N   ASP C 257      86.508  31.596  -1.319  1.00 87.59           N  
ANISOU 5379  N   ASP C 257    18482   5541   9258  -4677   1562   -191       N  
ATOM   5380  CA  ASP C 257      87.024  32.761  -2.064  1.00 89.29           C  
ANISOU 5380  CA  ASP C 257    19110   5443   9375  -5037   1695   -138       C  
ATOM   5381  C   ASP C 257      87.340  32.505  -3.567  1.00 96.44           C  
ANISOU 5381  C   ASP C 257    19995   6378  10269  -5169   1993    -34       C  
ATOM   5382  O   ASP C 257      88.160  33.239  -4.150  1.00 95.42           O  
ANISOU 5382  O   ASP C 257    20077   6051  10126  -5571   2153      5       O  
ATOM   5383  CB  ASP C 257      88.255  33.379  -1.354  1.00 91.04           C  
ANISOU 5383  CB  ASP C 257    19240   5590   9763  -5527   1618   -209       C  
ATOM   5384  CG  ASP C 257      88.258  33.186   0.145  1.00100.09           C  
ANISOU 5384  CG  ASP C 257    20276   6791  10964  -5441   1322   -321       C  
ATOM   5385  OD1 ASP C 257      87.823  34.113   0.861  1.00 98.30           O  
ANISOU 5385  OD1 ASP C 257    20537   6267  10546  -5406   1167   -361       O  
ATOM   5386  OD2 ASP C 257      88.642  32.077   0.601  1.00107.05           O  
ANISOU 5386  OD2 ASP C 257    20614   8001  12058  -5382   1246   -369       O  
ATOM   5387  N   SER C 258      86.638  31.532  -4.206  1.00 95.06           N  
ANISOU 5387  N   SER C 258    19627   6419  10073  -4839   2071     12       N  
ATOM   5388  CA  SER C 258      86.803  31.188  -5.633  1.00 95.92           C  
ANISOU 5388  CA  SER C 258    19755   6561  10130  -4912   2344    105       C  
ATOM   5389  C   SER C 258      86.700  32.400  -6.605  1.00102.98           C  
ANISOU 5389  C   SER C 258    21307   7066  10755  -5061   2465    205       C  
ATOM   5390  O   SER C 258      87.460  32.477  -7.580  1.00103.18           O  
ANISOU 5390  O   SER C 258    21379   7043  10782  -5393   2735    259       O  
ATOM   5391  CB  SER C 258      85.803  30.111  -6.039  1.00 99.09           C  
ANISOU 5391  CB  SER C 258    19972   7188  10489  -4477   2326    135       C  
ATOM   5392  N   TRP C 259      85.765  33.340  -6.322  1.00100.04           N  
ANISOU 5392  N   TRP C 259    21449   6407  10153  -4811   2276    228       N  
ATOM   5393  CA  TRP C 259      85.493  34.527  -7.129  1.00126.07           C  
ANISOU 5393  CA  TRP C 259    25429   9300  13172  -4875   2330    328       C  
ATOM   5394  C   TRP C 259      84.856  35.616  -6.259  1.00143.75           C  
ANISOU 5394  C   TRP C 259    28117  11235  15268  -4681   2087    297       C  
ATOM   5395  O   TRP C 259      84.251  36.556  -6.773  1.00105.08           O  
ANISOU 5395  O   TRP C 259    23821   5978  10126  -4614   2067    377       O  
ATOM   5396  CB  TRP C 259      84.573  34.159  -8.312  1.00124.81           C  
ANISOU 5396  CB  TRP C 259    25453   9144  12824  -4581   2395    439       C  
ATOM   5397  N   GLY C 262      85.160  36.463 -13.059  1.00113.99           N  
ANISOU 5397  N   GLY C 262    25893   6824  10596  -5428   3176    877       N  
ATOM   5398  CA  GLY C 262      84.795  36.258 -11.662  1.00113.77           C  
ANISOU 5398  CA  GLY C 262    25632   6868  10726  -5162   2871    776       C  
ATOM   5399  C   GLY C 262      83.332  35.919 -11.455  1.00116.95           C  
ANISOU 5399  C   GLY C 262    26068   7323  11045  -4560   2571    792       C  
ATOM   5400  O   GLY C 262      82.760  36.241 -10.410  1.00116.87           O  
ANISOU 5400  O   GLY C 262    26044   7272  11091  -4298   2326    728       O  
ATOM   5401  N   CYS C 263      82.722  35.271 -12.466  1.00112.31           N  
ANISOU 5401  N   CYS C 263    25538   6814  10321  -4346   2594    876       N  
ATOM   5402  CA  CYS C 263      81.327  34.823 -12.483  1.00111.15           C  
ANISOU 5402  CA  CYS C 263    25380   6739  10113  -3795   2317    906       C  
ATOM   5403  C   CYS C 263      81.262  33.312 -12.230  1.00109.99           C  
ANISOU 5403  C   CYS C 263    24536   7060  10194  -3637   2329    831       C  
ATOM   5404  O   CYS C 263      80.233  32.674 -12.489  1.00109.14           O  
ANISOU 5404  O   CYS C 263    24345   7071  10052  -3248   2155    863       O  
ATOM   5405  CB  CYS C 263      80.663  35.203 -13.805  1.00112.11           C  
ANISOU 5405  CB  CYS C 263    26098   6590   9910  -3673   2276   1059       C  
ATOM   5406  SG  CYS C 263      80.233  36.958 -13.946  1.00116.34           S  
ANISOU 5406  SG  CYS C 263    27489   6547  10168  -3617   2108   1157       S  
ATOM   5407  N   SER C 264      82.376  32.753 -11.711  1.00102.95           N  
ANISOU 5407  N   SER C 264    23142   6424   9549  -3948   2521    732       N  
ATOM   5408  CA  SER C 264      82.553  31.339 -11.393  1.00100.79           C  
ANISOU 5408  CA  SER C 264    22198   6581   9516  -3861   2561    652       C  
ATOM   5409  C   SER C 264      81.525  30.829 -10.387  1.00100.30           C  
ANISOU 5409  C   SER C 264    21842   6697   9571  -3411   2270    593       C  
ATOM   5410  O   SER C 264      80.981  29.748 -10.592  1.00 99.52           O  
ANISOU 5410  O   SER C 264    21435   6850   9528  -3167   2222    591       O  
ATOM   5411  CB  SER C 264      83.972  31.071 -10.898  1.00103.67           C  
ANISOU 5411  CB  SER C 264    22125   7124  10140  -4274   2775    559       C  
ATOM   5412  OG  SER C 264      84.924  31.318 -11.920  1.00110.00           O  
ANISOU 5412  OG  SER C 264    23082   7837  10878  -4677   3107    610       O  
ATOM   5413  N   GLN C 265      81.225  31.618  -9.335  1.00 93.79           N  
ANISOU 5413  N   GLN C 265    21147   5722   8768  -3304   2091    547       N  
ATOM   5414  CA  GLN C 265      80.257  31.241  -8.302  1.00 92.28           C  
ANISOU 5414  CA  GLN C 265    20716   5669   8679  -2891   1854    487       C  
ATOM   5415  C   GLN C 265      78.871  30.900  -8.870  1.00 93.74           C  
ANISOU 5415  C   GLN C 265    21001   5859   8757  -2443   1688    565       C  
ATOM   5416  O   GLN C 265      78.329  29.844  -8.548  1.00 94.00           O  
ANISOU 5416  O   GLN C 265    20611   6181   8926  -2190   1608    529       O  
ATOM   5417  CB  GLN C 265      80.172  32.308  -7.195  1.00 93.43           C  
ANISOU 5417  CB  GLN C 265    21103   5582   8813  -2870   1726    427       C  
ATOM   5418  N   LYS C 266      78.329  31.760  -9.743  1.00 88.55           N  
ANISOU 5418  N   LYS C 266    20900   4882   7864  -2360   1627    675       N  
ATOM   5419  CA  LYS C 266      77.011  31.567 -10.365  1.00 87.22           C  
ANISOU 5419  CA  LYS C 266    20878   4671   7591  -1945   1424    764       C  
ATOM   5420  C   LYS C 266      77.023  30.390 -11.340  1.00 87.83           C  
ANISOU 5420  C   LYS C 266    20710   4997   7664  -1950   1484    804       C  
ATOM   5421  O   LYS C 266      76.047  29.635 -11.386  1.00 87.73           O  
ANISOU 5421  O   LYS C 266    20464   5153   7715  -1608   1310    815       O  
ATOM   5422  CB  LYS C 266      76.479  32.853 -11.048  1.00 89.72           C  
ANISOU 5422  CB  LYS C 266    21898   4546   7645  -1876   1322    881       C  
ATOM   5423  CG  LYS C 266      77.147  34.177 -10.636  1.00101.71           C  
ANISOU 5423  CG  LYS C 266    23828   5730   9086  -2100   1378    860       C  
ATOM   5424  CD  LYS C 266      76.749  34.687  -9.251  1.00111.79           C  
ANISOU 5424  CD  LYS C 266    25041   6953  10480  -1827   1227    769       C  
ATOM   5425  CE  LYS C 266      77.597  35.863  -8.814  1.00126.79           C  
ANISOU 5425  CE  LYS C 266    27325   8542  12308  -2113   1297    729       C  
ATOM   5426  NZ  LYS C 266      79.004  35.475  -8.518  1.00136.50           N  
ANISOU 5426  NZ  LYS C 266    28231   9957  13676  -2580   1496    637       N  
ATOM   5427  N   ALA C 267      78.141  30.217 -12.088  1.00 81.23           N  
ANISOU 5427  N   ALA C 267    19924   4179   6760  -2346   1745    820       N  
ATOM   5428  CA  ALA C 267      78.334  29.124 -13.049  1.00 79.42           C  
ANISOU 5428  CA  ALA C 267    19517   4158   6502  -2401   1858    846       C  
ATOM   5429  C   ALA C 267      78.340  27.780 -12.320  1.00 78.79           C  
ANISOU 5429  C   ALA C 267    18757   4488   6693  -2288   1854    742       C  
ATOM   5430  O   ALA C 267      77.624  26.876 -12.737  1.00 78.02           O  
ANISOU 5430  O   ALA C 267    18493   4552   6597  -2054   1740    764       O  
ATOM   5431  CB  ALA C 267      79.633  29.320 -13.816  1.00 80.16           C  
ANISOU 5431  CB  ALA C 267    19793   4172   6494  -2866   2197    865       C  
ATOM   5432  N   ILE C 268      79.092  27.686 -11.188  1.00 72.47           N  
ANISOU 5432  N   ILE C 268    17590   3832   6115  -2446   1943    634       N  
ATOM   5433  CA  ILE C 268      79.212  26.516 -10.301  1.00 69.96           C  
ANISOU 5433  CA  ILE C 268    16650   3872   6058  -2364   1932    532       C  
ATOM   5434  C   ILE C 268      77.837  26.167  -9.689  1.00 70.91           C  
ANISOU 5434  C   ILE C 268    16622   4085   6236  -1916   1660    528       C  
ATOM   5435  O   ILE C 268      77.517  24.998  -9.531  1.00 67.97           O  
ANISOU 5435  O   ILE C 268    15848   3988   5991  -1767   1621    495       O  
ATOM   5436  CB  ILE C 268      80.320  26.761  -9.225  1.00 71.98           C  
ANISOU 5436  CB  ILE C 268    16664   4184   6502  -2642   2034    432       C  
ATOM   5437  CG1 ILE C 268      81.735  26.601  -9.829  1.00 71.11           C  
ANISOU 5437  CG1 ILE C 268    16455   4120   6445  -3075   2336    419       C  
ATOM   5438  CG2 ILE C 268      80.154  25.847  -8.009  1.00 72.89           C  
ANISOU 5438  CG2 ILE C 268    16256   4590   6850  -2468   1921    335       C  
ATOM   5439  CD1 ILE C 268      82.910  27.142  -8.943  1.00 67.91           C  
ANISOU 5439  CD1 ILE C 268    15912   3685   6205  -3418   2417    342       C  
ATOM   5440  N   LYS C 269      77.027  27.186  -9.367  1.00 68.65           N  
ANISOU 5440  N   LYS C 269    16665   3557   5860  -1703   1486    561       N  
ATOM   5441  CA  LYS C 269      75.685  27.001  -8.804  1.00 68.66           C  
ANISOU 5441  CA  LYS C 269    16539   3617   5932  -1271   1256    560       C  
ATOM   5442  C   LYS C 269      74.760  26.294  -9.823  1.00 73.27           C  
ANISOU 5442  C   LYS C 269    17111   4275   6455  -1043   1127    645       C  
ATOM   5443  O   LYS C 269      74.122  25.308  -9.473  1.00 72.08           O  
ANISOU 5443  O   LYS C 269    16564   4374   6451   -832   1039    617       O  
ATOM   5444  CB  LYS C 269      75.124  28.358  -8.363  1.00 70.54           C  
ANISOU 5444  CB  LYS C 269    17182   3538   6083  -1106   1135    578       C  
ATOM   5445  CG  LYS C 269      73.861  28.312  -7.537  1.00 77.99           C  
ANISOU 5445  CG  LYS C 269    17959   4530   7142   -680    957    549       C  
ATOM   5446  CD  LYS C 269      73.649  29.677  -6.886  1.00 86.25           C  
ANISOU 5446  CD  LYS C 269    19413   5246   8111   -581    904    537       C  
ATOM   5447  CE  LYS C 269      72.234  29.847  -6.409  1.00 95.88           C  
ANISOU 5447  CE  LYS C 269    20565   6448   9419   -107    740    534       C  
ATOM   5448  NZ  LYS C 269      72.126  30.819  -5.296  1.00100.39           N  
ANISOU 5448  NZ  LYS C 269    21392   6781   9971    -10    745    467       N  
ATOM   5449  N   CYS C 270      74.735  26.776 -11.081  1.00 71.91           N  
ANISOU 5449  N   CYS C 270    17388   3878   6056  -1115   1115    750       N  
ATOM   5450  CA  CYS C 270      73.938  26.218 -12.179  1.00 72.78           C  
ANISOU 5450  CA  CYS C 270    17590   4006   6059   -943    964    840       C  
ATOM   5451  C   CYS C 270      74.346  24.783 -12.541  1.00 72.06           C  
ANISOU 5451  C   CYS C 270    17119   4222   6038  -1059   1079    802       C  
ATOM   5452  O   CYS C 270      73.482  23.963 -12.846  1.00 70.88           O  
ANISOU 5452  O   CYS C 270    16795   4210   5926   -835    905    828       O  
ATOM   5453  CB  CYS C 270      73.983  27.137 -13.394  1.00 74.58           C  
ANISOU 5453  CB  CYS C 270    18456   3891   5991  -1042    942    958       C  
ATOM   5454  SG  CYS C 270      73.228  28.752 -13.113  1.00 79.66           S  
ANISOU 5454  SG  CYS C 270    19584   4143   6541   -792    723   1026       S  
ATOM   5455  N   LEU C 271      75.656  24.495 -12.490  1.00 66.14           N  
ANISOU 5455  N   LEU C 271    16238   3570   5324  -1407   1366    739       N  
ATOM   5456  CA  LEU C 271      76.237  23.183 -12.748  1.00 65.43           C  
ANISOU 5456  CA  LEU C 271    15789   3753   5320  -1540   1527    686       C  
ATOM   5457  C   LEU C 271      75.899  22.212 -11.595  1.00 65.21           C  
ANISOU 5457  C   LEU C 271    15185   4031   5562  -1357   1444    598       C  
ATOM   5458  O   LEU C 271      75.696  21.032 -11.848  1.00 64.17           O  
ANISOU 5458  O   LEU C 271    14785   4107   5489  -1288   1428    583       O  
ATOM   5459  CB  LEU C 271      77.754  23.335 -12.993  1.00 66.18           C  
ANISOU 5459  CB  LEU C 271    15919   3826   5401  -1955   1867    648       C  
ATOM   5460  CG  LEU C 271      78.637  22.107 -13.324  1.00 72.56           C  
ANISOU 5460  CG  LEU C 271    16375   4881   6313  -2145   2115    583       C  
ATOM   5461  CD1 LEU C 271      78.006  21.140 -14.364  1.00 73.09           C  
ANISOU 5461  CD1 LEU C 271    16483   5029   6259  -2009   2058    621       C  
ATOM   5462  CD2 LEU C 271      80.007  22.566 -13.803  1.00 76.80           C  
ANISOU 5462  CD2 LEU C 271    17069   5311   6802  -2546   2455    574       C  
ATOM   5463  N   TYR C 272      75.758  22.728 -10.350  1.00 58.87           N  
ANISOU 5463  N   TYR C 272    14244   3228   4897  -1268   1381    545       N  
ATOM   5464  CA  TYR C 272      75.362  21.950  -9.175  1.00 56.58           C  
ANISOU 5464  CA  TYR C 272    13483   3186   4830  -1087   1302    469       C  
ATOM   5465  C   TYR C 272      73.883  21.553  -9.256  1.00 59.36           C  
ANISOU 5465  C   TYR C 272    13755   3590   5208   -720   1062    516       C  
ATOM   5466  O   TYR C 272      73.549  20.396  -8.978  1.00 57.46           O  
ANISOU 5466  O   TYR C 272    13133   3596   5103   -618   1026    484       O  
ATOM   5467  CB  TYR C 272      75.644  22.721  -7.864  1.00 56.42           C  
ANISOU 5467  CB  TYR C 272    13431   3106   4901  -1113   1312    400       C  
ATOM   5468  CG  TYR C 272      75.162  22.000  -6.617  1.00 56.40           C  
ANISOU 5468  CG  TYR C 272    13020   3323   5088   -915   1233    329       C  
ATOM   5469  CD1 TYR C 272      75.493  20.664  -6.384  1.00 57.37           C  
ANISOU 5469  CD1 TYR C 272    12715   3730   5353   -957   1286    280       C  
ATOM   5470  CD2 TYR C 272      74.388  22.656  -5.663  1.00 56.28           C  
ANISOU 5470  CD2 TYR C 272    13072   3214   5099   -686   1123    308       C  
ATOM   5471  CE1 TYR C 272      75.014  19.984  -5.267  1.00 56.45           C  
ANISOU 5471  CE1 TYR C 272    12265   3798   5385   -781   1218    225       C  
ATOM   5472  CE2 TYR C 272      73.935  21.996  -4.524  1.00 56.52           C  
ANISOU 5472  CE2 TYR C 272    12762   3433   5279   -515   1084    245       C  
ATOM   5473  CZ  TYR C 272      74.250  20.656  -4.330  1.00 60.71           C  
ANISOU 5473  CZ  TYR C 272    12886   4245   5937   -572   1127    208       C  
ATOM   5474  OH  TYR C 272      73.841  19.997  -3.200  1.00 55.57           O  
ANISOU 5474  OH  TYR C 272    11937   3765   5413   -425   1098    152       O  
ATOM   5475  N   ILE C 273      73.002  22.535  -9.580  1.00 56.88           N  
ANISOU 5475  N   ILE C 273    13790   3038   4783   -521    894    593       N  
ATOM   5476  CA  ILE C 273      71.549  22.376  -9.757  1.00 56.58           C  
ANISOU 5476  CA  ILE C 273    13704   3008   4787   -163    641    652       C  
ATOM   5477  C   ILE C 273      71.261  21.243 -10.756  1.00 60.16           C  
ANISOU 5477  C   ILE C 273    14046   3606   5207   -162    563    695       C  
ATOM   5478  O   ILE C 273      70.354  20.461 -10.507  1.00 60.29           O  
ANISOU 5478  O   ILE C 273    13752   3790   5366     55    415    696       O  
ATOM   5479  CB  ILE C 273      70.883  23.719 -10.198  1.00 59.43           C  
ANISOU 5479  CB  ILE C 273    14535   3038   5009      8    479    739       C  
ATOM   5480  CG1 ILE C 273      70.898  24.771  -9.073  1.00 59.41           C  
ANISOU 5480  CG1 ILE C 273    14627   2889   5059     80    525    686       C  
ATOM   5481  CG2 ILE C 273      69.459  23.528 -10.758  1.00 59.83           C  
ANISOU 5481  CG2 ILE C 273    14569   3073   5091    350    185    825       C  
ATOM   5482  CD1 ILE C 273      70.976  26.260  -9.643  1.00 57.41           C  
ANISOU 5482  CD1 ILE C 273    14984   2238   4591     53    480    760       C  
ATOM   5483  N   LEU C 274      72.025  21.165 -11.871  1.00 56.79           N  
ANISOU 5483  N   LEU C 274    13892   3099   4587   -410    674    730       N  
ATOM   5484  CA  LEU C 274      71.887  20.137 -12.917  1.00 57.05           C  
ANISOU 5484  CA  LEU C 274    13915   3228   4534   -447    627    763       C  
ATOM   5485  C   LEU C 274      72.131  18.703 -12.422  1.00 58.24           C  
ANISOU 5485  C   LEU C 274    13561   3696   4869   -486    721    678       C  
ATOM   5486  O   LEU C 274      71.422  17.774 -12.831  1.00 56.68           O  
ANISOU 5486  O   LEU C 274    13217   3619   4698   -369    570    697       O  
ATOM   5487  CB  LEU C 274      72.807  20.450 -14.114  1.00 57.76           C  
ANISOU 5487  CB  LEU C 274    14446   3140   4358   -732    801    804       C  
ATOM   5488  CG  LEU C 274      72.267  21.465 -15.105  1.00 63.76           C  
ANISOU 5488  CG  LEU C 274    15782   3580   4863   -667    626    924       C  
ATOM   5489  CD1 LEU C 274      73.396  22.250 -15.756  1.00 65.40           C  
ANISOU 5489  CD1 LEU C 274    16435   3572   4842   -994    891    947       C  
ATOM   5490  CD2 LEU C 274      71.438  20.795 -16.176  1.00 65.43           C  
ANISOU 5490  CD2 LEU C 274    16130   3785   4947   -535    377    999       C  
ATOM   5491  N   THR C 275      73.122  18.535 -11.533  1.00 53.37           N  
ANISOU 5491  N   THR C 275    12694   3202   4383   -652    947    586       N  
ATOM   5492  CA  THR C 275      73.504  17.235 -10.982  1.00 52.41           C  
ANISOU 5492  CA  THR C 275    12119   3359   4437   -698   1046    504       C  
ATOM   5493  C   THR C 275      72.522  16.691  -9.956  1.00 53.69           C  
ANISOU 5493  C   THR C 275    11910   3692   4800   -446    884    480       C  
ATOM   5494  O   THR C 275      72.428  15.478  -9.799  1.00 51.30           O  
ANISOU 5494  O   THR C 275    11296   3594   4603   -427    883    446       O  
ATOM   5495  CB  THR C 275      74.913  17.283 -10.401  1.00 58.18           C  
ANISOU 5495  CB  THR C 275    12711   4147   5247   -956   1308    423       C  
ATOM   5496  OG1 THR C 275      74.877  18.035  -9.194  1.00 53.36           O  
ANISOU 5496  OG1 THR C 275    12025   3508   4743   -900   1275    387       O  
ATOM   5497  CG2 THR C 275      75.953  17.851 -11.382  1.00 56.19           C  
ANISOU 5497  CG2 THR C 275    12798   3729   4824  -1237   1521    443       C  
ATOM   5498  N   ARG C 276      71.835  17.581  -9.227  1.00 51.50           N  
ANISOU 5498  N   ARG C 276    11672   3322   4574   -261    774    494       N  
ATOM   5499  CA  ARG C 276      70.877  17.211  -8.169  1.00 51.08           C  
ANISOU 5499  CA  ARG C 276    11285   3411   4712    -18    666    469       C  
ATOM   5500  C   ARG C 276      69.775  16.252  -8.635  1.00 51.68           C  
ANISOU 5500  C   ARG C 276    11169   3612   4856    153    482    514       C  
ATOM   5501  O   ARG C 276      69.664  15.214  -8.007  1.00 51.65           O  
ANISOU 5501  O   ARG C 276    10807   3820   4997    170    512    468       O  
ATOM   5502  CB  ARG C 276      70.267  18.443  -7.480  1.00 51.85           C  
ANISOU 5502  CB  ARG C 276    11527   3343   4830    174    599    480       C  
ATOM   5503  CG  ARG C 276      71.231  19.216  -6.596  1.00 59.74           C  
ANISOU 5503  CG  ARG C 276    12629   4257   5811     20    762    412       C  
ATOM   5504  CD  ARG C 276      70.517  19.800  -5.395  1.00 56.52           C  
ANISOU 5504  CD  ARG C 276    12166   3809   5499    245    731    376       C  
ATOM   5505  NE  ARG C 276      69.489  20.772  -5.770  1.00 53.85           N  
ANISOU 5505  NE  ARG C 276    12078   3263   5120    501    583    445       N  
ATOM   5506  CZ  ARG C 276      69.707  22.075  -5.911  1.00 71.77           C  
ANISOU 5506  CZ  ARG C 276    14751   5258   7261    488    582    464       C  
ATOM   5507  NH1 ARG C 276      68.710  22.889  -6.233  1.00 67.32           N  
ANISOU 5507  NH1 ARG C 276    14397   4503   6679    758    429    530       N  
ATOM   5508  NH2 ARG C 276      70.925  22.576  -5.736  1.00 52.18           N  
ANISOU 5508  NH2 ARG C 276    12464   2681   4679    203    726    421       N  
ATOM   5509  N   PRO C 277      68.968  16.523  -9.703  1.00 46.63           N  
ANISOU 5509  N   PRO C 277    10758   2845   4115    266    276    605       N  
ATOM   5510  CA  PRO C 277      67.939  15.537 -10.110  1.00 45.98           C  
ANISOU 5510  CA  PRO C 277    10462   2891   4118    398     73    643       C  
ATOM   5511  C   PRO C 277      68.510  14.231 -10.680  1.00 48.16           C  
ANISOU 5511  C   PRO C 277    10639   3313   4348    204    148    611       C  
ATOM   5512  O   PRO C 277      67.800  13.235 -10.745  1.00 47.50           O  
ANISOU 5512  O   PRO C 277    10311   3371   4366    277     18    618       O  
ATOM   5513  CB  PRO C 277      67.097  16.300 -11.144  1.00 47.73           C  
ANISOU 5513  CB  PRO C 277    11015   2901   4218    542   -189    749       C  
ATOM   5514  CG  PRO C 277      68.004  17.343 -11.683  1.00 50.68           C  
ANISOU 5514  CG  PRO C 277    11848   3043   4365    386    -72    768       C  
ATOM   5515  CD  PRO C 277      68.942  17.715 -10.584  1.00 46.17           C  
ANISOU 5515  CD  PRO C 277    11176   2507   3859    271    193    681       C  
ATOM   5516  N   LEU C 278      69.791  14.234 -11.084  1.00 44.42           N  
ANISOU 5516  N   LEU C 278    10348   2796   3731    -44    367    574       N  
ATOM   5517  CA  LEU C 278      70.485  13.051 -11.582  1.00 43.85           C  
ANISOU 5517  CA  LEU C 278    10196   2844   3620   -221    492    530       C  
ATOM   5518  C   LEU C 278      70.750  12.143 -10.386  1.00 46.97           C  
ANISOU 5518  C   LEU C 278    10144   3468   4234   -220    601    449       C  
ATOM   5519  O   LEU C 278      70.533  10.935 -10.488  1.00 46.23           O  
ANISOU 5519  O   LEU C 278     9847   3516   4203   -217    562    430       O  
ATOM   5520  CB  LEU C 278      71.796  13.428 -12.319  1.00 44.23           C  
ANISOU 5520  CB  LEU C 278    10553   2772   3482   -474    734    513       C  
ATOM   5521  CG  LEU C 278      72.630  12.267 -12.905  1.00 49.80           C  
ANISOU 5521  CG  LEU C 278    11206   3575   4141   -650    915    458       C  
ATOM   5522  CD1 LEU C 278      71.942  11.634 -14.103  1.00 50.61           C  
ANISOU 5522  CD1 LEU C 278    11518   3630   4083   -612    739    508       C  
ATOM   5523  CD2 LEU C 278      74.003  12.747 -13.324  1.00 52.20           C  
ANISOU 5523  CD2 LEU C 278    11723   3781   4330   -895   1216    429       C  
ATOM   5524  N   ALA C 279      71.145  12.731  -9.226  1.00 41.79           N  
ANISOU 5524  N   ALA C 279     9362   2832   3685   -215    711    404       N  
ATOM   5525  CA  ALA C 279      71.372  11.954  -8.014  1.00 40.50           C  
ANISOU 5525  CA  ALA C 279     8822   2861   3705   -207    789    335       C  
ATOM   5526  C   ALA C 279      70.055  11.426  -7.499  1.00 46.01           C  
ANISOU 5526  C   ALA C 279     9276   3666   4539      6    621    360       C  
ATOM   5527  O   ALA C 279      69.968  10.250  -7.164  1.00 45.06           O  
ANISOU 5527  O   ALA C 279     8891   3709   4520     -2    629    331       O  
ATOM   5528  CB  ALA C 279      72.036  12.799  -6.946  1.00 40.74           C  
ANISOU 5528  CB  ALA C 279     8841   2854   3783   -252    906    287       C  
ATOM   5529  N   PHE C 280      69.017  12.285  -7.471  1.00 43.87           N  
ANISOU 5529  N   PHE C 280     9093   3296   4282    197    473    416       N  
ATOM   5530  CA  PHE C 280      67.699  11.932  -6.934  1.00 43.28           C  
ANISOU 5530  CA  PHE C 280     8756   3315   4375    412    334    441       C  
ATOM   5531  C   PHE C 280      66.924  10.970  -7.822  1.00 45.86           C  
ANISOU 5531  C   PHE C 280     8991   3710   4723    438    148    490       C  
ATOM   5532  O   PHE C 280      65.884  10.477  -7.389  1.00 44.50           O  
ANISOU 5532  O   PHE C 280     8542   3644   4720    577     46    509       O  
ATOM   5533  CB  PHE C 280      66.876  13.196  -6.598  1.00 44.91           C  
ANISOU 5533  CB  PHE C 280     9066   3383   4616    629    253    479       C  
ATOM   5534  CG  PHE C 280      67.602  14.248  -5.782  1.00 46.76           C  
ANISOU 5534  CG  PHE C 280     9456   3508   4801    598    415    429       C  
ATOM   5535  CD1 PHE C 280      68.689  13.910  -4.980  1.00 50.57           C  
ANISOU 5535  CD1 PHE C 280     9852   4077   5286    424    600    350       C  
ATOM   5536  CD2 PHE C 280      67.193  15.573  -5.808  1.00 49.83           C  
ANISOU 5536  CD2 PHE C 280    10092   3696   5145    744    359    462       C  
ATOM   5537  CE1 PHE C 280      69.383  14.888  -4.261  1.00 51.78           C  
ANISOU 5537  CE1 PHE C 280    10169   4117   5387    367    715    303       C  
ATOM   5538  CE2 PHE C 280      67.885  16.549  -5.085  1.00 53.37           C  
ANISOU 5538  CE2 PHE C 280    10726   4022   5531    692    497    411       C  
ATOM   5539  CZ  PHE C 280      68.970  16.195  -4.305  1.00 51.15           C  
ANISOU 5539  CZ  PHE C 280    10355   3832   5248    494    668    331       C  
ATOM   5540  N   LEU C 281      67.442  10.664  -9.044  1.00 43.73           N  
ANISOU 5540  N   LEU C 281     8957   3377   4282    291    116    507       N  
ATOM   5541  CA  LEU C 281      66.838   9.692  -9.977  1.00 44.67           C  
ANISOU 5541  CA  LEU C 281     9055   3538   4379    277    -70    544       C  
ATOM   5542  C   LEU C 281      66.859   8.293  -9.357  1.00 48.15           C  
ANISOU 5542  C   LEU C 281     9154   4180   4960    222     -1    491       C  
ATOM   5543  O   LEU C 281      66.042   7.449  -9.713  1.00 48.90           O  
ANISOU 5543  O   LEU C 281     9118   4342   5120    250   -175    519       O  
ATOM   5544  CB  LEU C 281      67.551   9.718 -11.351  1.00 45.16           C  
ANISOU 5544  CB  LEU C 281     9511   3463   4184    115    -64    558       C  
ATOM   5545  CG  LEU C 281      67.057   8.760 -12.437  1.00 50.08           C  
ANISOU 5545  CG  LEU C 281    10216   4089   4722     71   -257    588       C  
ATOM   5546  CD1 LEU C 281      65.627   9.076 -12.859  1.00 50.66           C  
ANISOU 5546  CD1 LEU C 281    10290   4107   4852    250   -615    679       C  
ATOM   5547  CD2 LEU C 281      67.989   8.766 -13.633  1.00 52.02           C  
ANISOU 5547  CD2 LEU C 281    10878   4198   4689   -110   -155    580       C  
ATOM   5548  N   ASN C 282      67.763   8.086  -8.381  1.00 43.95           N  
ANISOU 5548  N   ASN C 282     8485   3734   4481    144    233    419       N  
ATOM   5549  CA  ASN C 282      67.939   6.881  -7.578  1.00 43.65           C  
ANISOU 5549  CA  ASN C 282     8150   3865   4570     99    323    368       C  
ATOM   5550  C   ASN C 282      66.611   6.333  -7.001  1.00 46.65           C  
ANISOU 5550  C   ASN C 282     8237   4355   5133    233    188    401       C  
ATOM   5551  O   ASN C 282      66.351   5.144  -7.141  1.00 44.92           O  
ANISOU 5551  O   ASN C 282     7877   4227   4964    178    135    398       O  
ATOM   5552  CB  ASN C 282      68.960   7.150  -6.448  1.00 41.90           C  
ANISOU 5552  CB  ASN C 282     7849   3682   4387     46    538    303       C  
ATOM   5553  CG  ASN C 282      68.921   6.142  -5.334  1.00 56.21           C  
ANISOU 5553  CG  ASN C 282     9367   5651   6341     51    598    266       C  
ATOM   5554  OD1 ASN C 282      69.421   5.024  -5.460  1.00 59.56           O  
ANISOU 5554  OD1 ASN C 282     9711   6147   6772    -45    641    235       O  
ATOM   5555  ND2 ASN C 282      68.285   6.505  -4.237  1.00 36.61           N  
ANISOU 5555  ND2 ASN C 282     6740   3208   3964    172    607    271       N  
ATOM   5556  N   SER C 283      65.787   7.196  -6.373  1.00 43.30           N  
ANISOU 5556  N   SER C 283     7726   3912   4813    403    147    432       N  
ATOM   5557  CA  SER C 283      64.517   6.807  -5.744  1.00 43.50           C  
ANISOU 5557  CA  SER C 283     7443   4042   5044    538     67    462       C  
ATOM   5558  C   SER C 283      63.449   6.341  -6.728  1.00 49.02           C  
ANISOU 5558  C   SER C 283     8082   4743   5801    572   -199    529       C  
ATOM   5559  O   SER C 283      62.511   5.657  -6.316  1.00 50.27           O  
ANISOU 5559  O   SER C 283     7941   5013   6145    619   -261    550       O  
ATOM   5560  CB  SER C 283      63.978   7.918  -4.848  1.00 47.10           C  
ANISOU 5560  CB  SER C 283     7842   4459   5596    726    130    468       C  
ATOM   5561  OG  SER C 283      63.934   9.152  -5.543  1.00 56.92           O  
ANISOU 5561  OG  SER C 283     9357   5531   6739    808     41    501       O  
ATOM   5562  N   ALA C 284      63.609   6.664  -8.022  1.00 44.70           N  
ANISOU 5562  N   ALA C 284     7828   4069   5088    529   -359    563       N  
ATOM   5563  CA  ALA C 284      62.688   6.254  -9.079  1.00 43.86           C  
ANISOU 5563  CA  ALA C 284     7732   3938   4996    540   -660    628       C  
ATOM   5564  C   ALA C 284      63.182   5.022  -9.848  1.00 46.58           C  
ANISOU 5564  C   ALA C 284     8182   4304   5212    341   -693    601       C  
ATOM   5565  O   ALA C 284      62.356   4.299 -10.414  1.00 46.06           O  
ANISOU 5565  O   ALA C 284     8032   4263   5204    319   -929    638       O  
ATOM   5566  CB  ALA C 284      62.442   7.414 -10.046  1.00 44.44           C  
ANISOU 5566  CB  ALA C 284     8115   3826   4944    635   -856    692       C  
ATOM   5567  N   VAL C 285      64.515   4.774  -9.872  1.00 42.33           N  
ANISOU 5567  N   VAL C 285     7821   3749   4512    198   -461    533       N  
ATOM   5568  CA  VAL C 285      65.084   3.661 -10.649  1.00 41.78           C  
ANISOU 5568  CA  VAL C 285     7896   3674   4305     28   -452    496       C  
ATOM   5569  C   VAL C 285      65.481   2.431  -9.801  1.00 44.76           C  
ANISOU 5569  C   VAL C 285     8023   4193   4791    -50   -285    434       C  
ATOM   5570  O   VAL C 285      65.380   1.313 -10.318  1.00 44.33           O  
ANISOU 5570  O   VAL C 285     7990   4150   4702   -148   -361    419       O  
ATOM   5571  CB  VAL C 285      66.254   4.085 -11.582  1.00 45.78           C  
ANISOU 5571  CB  VAL C 285     8808   4039   4546    -82   -325    469       C  
ATOM   5572  CG1 VAL C 285      65.824   5.186 -12.563  1.00 45.63           C  
ANISOU 5572  CG1 VAL C 285     9108   3851   4380    -21   -519    542       C  
ATOM   5573  CG2 VAL C 285      67.498   4.504 -10.793  1.00 45.66           C  
ANISOU 5573  CG2 VAL C 285     8767   4049   4533   -125     -9    405       C  
ATOM   5574  N   ASN C 286      65.890   2.622  -8.512  1.00 39.35           N  
ANISOU 5574  N   ASN C 286     7132   3595   4225     -8    -81    400       N  
ATOM   5575  CA  ASN C 286      66.338   1.536  -7.634  1.00 38.29           C  
ANISOU 5575  CA  ASN C 286     6796   3574   4178    -72     67    348       C  
ATOM   5576  C   ASN C 286      65.238   0.439  -7.383  1.00 43.27           C  
ANISOU 5576  C   ASN C 286     7184   4297   4959    -78    -71    379       C  
ATOM   5577  O   ASN C 286      65.658  -0.690  -7.064  1.00 42.92           O  
ANISOU 5577  O   ASN C 286     7075   4304   4930   -166     11    340       O  
ATOM   5578  CB  ASN C 286      66.994   2.041  -6.331  1.00 33.20           C  
ANISOU 5578  CB  ASN C 286     6037   2980   3598    -31    276    312       C  
ATOM   5579  CG  ASN C 286      66.075   2.646  -5.326  1.00 46.58           C  
ANISOU 5579  CG  ASN C 286     7533   4727   5439    104    266    345       C  
ATOM   5580  OD1 ASN C 286      64.887   2.341  -5.289  1.00 42.45           O  
ANISOU 5580  OD1 ASN C 286     6832   4255   5042    162    141    391       O  
ATOM   5581  ND2 ASN C 286      66.614   3.519  -4.477  1.00 38.14           N  
ANISOU 5581  ND2 ASN C 286     6489   3640   4362    151    409    317       N  
ATOM   5582  N   PRO C 287      63.891   0.638  -7.630  1.00 39.24           N  
ANISOU 5582  N   PRO C 287     6550   3798   4562     -4   -291    446       N  
ATOM   5583  CA  PRO C 287      62.958  -0.508  -7.558  1.00 38.80           C  
ANISOU 5583  CA  PRO C 287     6277   3819   4645    -64   -424    472       C  
ATOM   5584  C   PRO C 287      63.312  -1.642  -8.550  1.00 41.80           C  
ANISOU 5584  C   PRO C 287     6853   4143   4887   -222   -518    444       C  
ATOM   5585  O   PRO C 287      62.820  -2.767  -8.384  1.00 41.82           O  
ANISOU 5585  O   PRO C 287     6713   4197   4981   -309   -585    448       O  
ATOM   5586  CB  PRO C 287      61.608   0.126  -7.931  1.00 40.06           C  
ANISOU 5586  CB  PRO C 287     6307   3972   4941     44   -673    549       C  
ATOM   5587  CG  PRO C 287      61.735   1.524  -7.483  1.00 44.06           C  
ANISOU 5587  CG  PRO C 287     6843   4445   5453    206   -574    558       C  
ATOM   5588  CD  PRO C 287      63.130   1.869  -7.931  1.00 40.17           C  
ANISOU 5588  CD  PRO C 287     6691   3857   4715    137   -436    505       C  
ATOM   5589  N   ILE C 288      64.190  -1.372  -9.557  1.00 36.31           N  
ANISOU 5589  N   ILE C 288     6504   3331   3963   -267   -500    411       N  
ATOM   5590  CA  ILE C 288      64.637  -2.393 -10.532  1.00 36.03           C  
ANISOU 5590  CA  ILE C 288     6713   3215   3761   -404   -543    370       C  
ATOM   5591  C   ILE C 288      65.318  -3.602  -9.846  1.00 36.61           C  
ANISOU 5591  C   ILE C 288     6690   3345   3875   -477   -353    307       C  
ATOM   5592  O   ILE C 288      65.263  -4.720 -10.349  1.00 34.69           O  
ANISOU 5592  O   ILE C 288     6545   3060   3576   -580   -426    282       O  
ATOM   5593  CB  ILE C 288      65.534  -1.782 -11.672  1.00 39.60           C  
ANISOU 5593  CB  ILE C 288     7572   3524   3952   -432   -487    343       C  
ATOM   5594  CG1 ILE C 288      65.541  -2.650 -12.940  1.00 40.30           C  
ANISOU 5594  CG1 ILE C 288     7974   3496   3844   -554   -616    319       C  
ATOM   5595  CG2 ILE C 288      66.973  -1.456 -11.217  1.00 40.46           C  
ANISOU 5595  CG2 ILE C 288     7723   3639   4010   -431   -155    277       C  
ATOM   5596  CD1 ILE C 288      64.279  -2.538 -13.799  1.00 50.05           C  
ANISOU 5596  CD1 ILE C 288     9301   4666   5051   -566  -1003    391       C  
ATOM   5597  N   PHE C 289      65.960  -3.351  -8.695  1.00 31.88           N  
ANISOU 5597  N   PHE C 289     5926   2825   3363   -422   -127    282       N  
ATOM   5598  CA  PHE C 289      66.722  -4.341  -7.973  1.00 30.57           C  
ANISOU 5598  CA  PHE C 289     5686   2698   3232   -465     44    228       C  
ATOM   5599  C   PHE C 289      65.858  -5.488  -7.430  1.00 35.66           C  
ANISOU 5599  C   PHE C 289     6140   3400   4009   -520    -48    254       C  
ATOM   5600  O   PHE C 289      66.378  -6.582  -7.190  1.00 33.04           O  
ANISOU 5600  O   PHE C 289     5830   3056   3668   -578     31    213       O  
ATOM   5601  CB  PHE C 289      67.559  -3.656  -6.904  1.00 30.96           C  
ANISOU 5601  CB  PHE C 289     5630   2802   3332   -395    254    203       C  
ATOM   5602  CG  PHE C 289      68.720  -2.890  -7.471  1.00 31.31           C  
ANISOU 5602  CG  PHE C 289     5873   2776   3248   -394    386    160       C  
ATOM   5603  CD1 PHE C 289      69.790  -3.552  -8.059  1.00 32.65           C  
ANISOU 5603  CD1 PHE C 289     6197   2886   3323   -456    510     94       C  
ATOM   5604  CD2 PHE C 289      68.769  -1.497  -7.380  1.00 34.01           C  
ANISOU 5604  CD2 PHE C 289     6246   3104   3574   -332    408    184       C  
ATOM   5605  CE1 PHE C 289      70.876  -2.833  -8.578  1.00 33.60           C  
ANISOU 5605  CE1 PHE C 289     6474   2946   3346   -472    668     55       C  
ATOM   5606  CE2 PHE C 289      69.865  -0.784  -7.884  1.00 35.63           C  
ANISOU 5606  CE2 PHE C 289     6634   3237   3666   -361    546    148       C  
ATOM   5607  CZ  PHE C 289      70.908  -1.460  -8.479  1.00 32.85           C  
ANISOU 5607  CZ  PHE C 289     6407   2839   3234   -438    683     85       C  
ATOM   5608  N   TYR C 290      64.531  -5.249  -7.307  1.00 34.14           N  
ANISOU 5608  N   TYR C 290     5767   3260   3946   -505   -219    323       N  
ATOM   5609  CA  TYR C 290      63.535  -6.255  -6.921  1.00 34.40           C  
ANISOU 5609  CA  TYR C 290     5603   3344   4124   -585   -324    360       C  
ATOM   5610  C   TYR C 290      63.479  -7.402  -7.943  1.00 39.59           C  
ANISOU 5610  C   TYR C 290     6457   3906   4679   -726   -478    337       C  
ATOM   5611  O   TYR C 290      63.123  -8.526  -7.577  1.00 40.95           O  
ANISOU 5611  O   TYR C 290     6543   4090   4927   -827   -501    342       O  
ATOM   5612  CB  TYR C 290      62.143  -5.615  -6.881  1.00 34.73           C  
ANISOU 5612  CB  TYR C 290     5415   3446   4334   -536   -497    437       C  
ATOM   5613  CG  TYR C 290      61.781  -4.981  -5.563  1.00 35.44           C  
ANISOU 5613  CG  TYR C 290     5231   3643   4591   -427   -332    465       C  
ATOM   5614  CD1 TYR C 290      62.271  -3.727  -5.212  1.00 36.87           C  
ANISOU 5614  CD1 TYR C 290     5454   3825   4732   -287   -203    452       C  
ATOM   5615  CD2 TYR C 290      60.880  -5.596  -4.697  1.00 35.69           C  
ANISOU 5615  CD2 TYR C 290     4982   3763   4817   -473   -302    504       C  
ATOM   5616  CE1 TYR C 290      61.905  -3.116  -4.014  1.00 36.99           C  
ANISOU 5616  CE1 TYR C 290     5261   3917   4877   -182    -47    470       C  
ATOM   5617  CE2 TYR C 290      60.491  -4.987  -3.506  1.00 36.45           C  
ANISOU 5617  CE2 TYR C 290     4856   3945   5049   -369   -123    526       C  
ATOM   5618  CZ  TYR C 290      61.008  -3.747  -3.169  1.00 45.16           C  
ANISOU 5618  CZ  TYR C 290     6030   5039   6091   -217      1    505       C  
ATOM   5619  OH  TYR C 290      60.622  -3.144  -2.005  1.00 47.67           O  
ANISOU 5619  OH  TYR C 290     6174   5420   6519   -111    184    518       O  
ATOM   5620  N   PHE C 291      63.775  -7.086  -9.225  1.00 35.42           N  
ANISOU 5620  N   PHE C 291     6222   3270   3967   -739   -586    314       N  
ATOM   5621  CA  PHE C 291      63.734  -7.973 -10.393  1.00 35.78           C  
ANISOU 5621  CA  PHE C 291     6547   3191   3859   -864   -746    284       C  
ATOM   5622  C   PHE C 291      65.094  -8.640 -10.702  1.00 39.73           C  
ANISOU 5622  C   PHE C 291     7314   3597   4183   -885   -532    190       C  
ATOM   5623  O   PHE C 291      65.249  -9.285 -11.738  1.00 38.18           O  
ANISOU 5623  O   PHE C 291     7418   3272   3817   -970   -611    148       O  
ATOM   5624  CB  PHE C 291      63.163  -7.213 -11.623  1.00 37.38           C  
ANISOU 5624  CB  PHE C 291     6947   3311   3945   -864  -1004    320       C  
ATOM   5625  CG  PHE C 291      61.849  -6.525 -11.331  1.00 39.83           C  
ANISOU 5625  CG  PHE C 291     6960   3709   4463   -808  -1221    412       C  
ATOM   5626  CD1 PHE C 291      60.675  -7.261 -11.187  1.00 43.94           C  
ANISOU 5626  CD1 PHE C 291     7251   4277   5168   -905  -1441    459       C  
ATOM   5627  CD2 PHE C 291      61.794  -5.147 -11.128  1.00 43.33           C  
ANISOU 5627  CD2 PHE C 291     7328   4188   4946   -656  -1184    449       C  
ATOM   5628  CE1 PHE C 291      59.467  -6.629 -10.858  1.00 45.47           C  
ANISOU 5628  CE1 PHE C 291     7108   4564   5603   -838  -1610    541       C  
ATOM   5629  CE2 PHE C 291      60.586  -4.514 -10.796  1.00 46.19           C  
ANISOU 5629  CE2 PHE C 291     7388   4629   5533   -572  -1357    529       C  
ATOM   5630  CZ  PHE C 291      59.428  -5.256 -10.677  1.00 44.53           C  
ANISOU 5630  CZ  PHE C 291     6918   4478   5525   -657  -1564    574       C  
ATOM   5631  N   LEU C 292      66.061  -8.509  -9.784  1.00 36.48           N  
ANISOU 5631  N   LEU C 292     6792   3245   3823   -805   -266    156       N  
ATOM   5632  CA  LEU C 292      67.403  -9.062  -9.985  1.00 35.86           C  
ANISOU 5632  CA  LEU C 292     6900   3093   3634   -795    -48     69       C  
ATOM   5633  C   LEU C 292      67.819 -10.003  -8.844  1.00 40.49           C  
ANISOU 5633  C   LEU C 292     7316   3724   4346   -782     81     50       C  
ATOM   5634  O   LEU C 292      69.015 -10.245  -8.651  1.00 40.79           O  
ANISOU 5634  O   LEU C 292     7403   3735   4361   -728    280    -13       O  
ATOM   5635  CB  LEU C 292      68.424  -7.905 -10.135  1.00 35.11           C  
ANISOU 5635  CB  LEU C 292     6870   3001   3470   -710    142     41       C  
ATOM   5636  CG  LEU C 292      68.321  -7.004 -11.385  1.00 38.24           C  
ANISOU 5636  CG  LEU C 292     7540   3306   3682   -727     67     50       C  
ATOM   5637  CD1 LEU C 292      69.348  -5.916 -11.327  1.00 37.52           C  
ANISOU 5637  CD1 LEU C 292     7481   3222   3553   -666    285     27       C  
ATOM   5638  CD2 LEU C 292      68.525  -7.781 -12.648  1.00 38.87           C  
ANISOU 5638  CD2 LEU C 292     7978   3236   3557   -811     43     -7       C  
ATOM   5639  N   VAL C 293      66.839 -10.549  -8.104  1.00 36.35           N  
ANISOU 5639  N   VAL C 293     6595   3260   3959   -835    -34    107       N  
ATOM   5640  CA  VAL C 293      67.137 -11.422  -6.967  1.00 35.71           C  
ANISOU 5640  CA  VAL C 293     6385   3206   3978   -832     71    105       C  
ATOM   5641  C   VAL C 293      66.633 -12.884  -7.179  1.00 40.71           C  
ANISOU 5641  C   VAL C 293     7115   3748   4605   -961    -44    103       C  
ATOM   5642  O   VAL C 293      66.382 -13.601  -6.211  1.00 39.99           O  
ANISOU 5642  O   VAL C 293     6896   3682   4616   -999    -24    136       O  
ATOM   5643  CB  VAL C 293      66.686 -10.797  -5.609  1.00 37.84           C  
ANISOU 5643  CB  VAL C 293     6362   3612   4402   -780    124    169       C  
ATOM   5644  CG1 VAL C 293      67.609  -9.653  -5.209  1.00 36.69           C  
ANISOU 5644  CG1 VAL C 293     6179   3519   4245   -657    277    146       C  
ATOM   5645  CG2 VAL C 293      65.229 -10.338  -5.633  1.00 37.26           C  
ANISOU 5645  CG2 VAL C 293     6115   3609   4431   -828    -37    245       C  
ATOM   5646  N   GLY C 294      66.549 -13.297  -8.450  1.00 38.75           N  
ANISOU 5646  N   GLY C 294     7133   3376   4215  -1033   -156     61       N  
ATOM   5647  CA  GLY C 294      66.232 -14.653  -8.923  1.00 38.58           C  
ANISOU 5647  CA  GLY C 294     7303   3222   4136  -1161   -270     37       C  
ATOM   5648  C   GLY C 294      65.001 -15.400  -8.443  1.00 42.42           C  
ANISOU 5648  C   GLY C 294     7641   3726   4750  -1314   -443    106       C  
ATOM   5649  O   GLY C 294      64.972 -16.624  -8.552  1.00 41.84           O  
ANISOU 5649  O   GLY C 294     7724   3533   4642  -1413   -483     81       O  
ATOM   5650  N   ASP C 295      63.966 -14.697  -7.952  1.00 40.40           N  
ANISOU 5650  N   ASP C 295     7091   3608   4650  -1341   -540    190       N  
ATOM   5651  CA  ASP C 295      62.735 -15.310  -7.417  1.00 40.94           C  
ANISOU 5651  CA  ASP C 295     6952   3718   4886  -1496   -670    264       C  
ATOM   5652  C   ASP C 295      61.557 -15.379  -8.387  1.00 47.67           C  
ANISOU 5652  C   ASP C 295     7806   4541   5765  -1649   -981    298       C  
ATOM   5653  O   ASP C 295      60.540 -15.990  -8.051  1.00 48.08           O  
ANISOU 5653  O   ASP C 295     7677   4618   5973  -1808  -1100    355       O  
ATOM   5654  CB  ASP C 295      62.288 -14.581  -6.126  1.00 42.25           C  
ANISOU 5654  CB  ASP C 295     6754   4056   5242  -1427   -540    336       C  
ATOM   5655  CG  ASP C 295      62.143 -13.069  -6.250  1.00 45.37           C  
ANISOU 5655  CG  ASP C 295     7001   4561   5675  -1288   -541    357       C  
ATOM   5656  OD1 ASP C 295      62.212 -12.552  -7.387  1.00 43.11           O  
ANISOU 5656  OD1 ASP C 295     6878   4224   5278  -1262   -676    332       O  
ATOM   5657  OD2 ASP C 295      61.966 -12.407  -5.213  1.00 49.49           O  
ANISOU 5657  OD2 ASP C 295     7279   5203   6322  -1206   -404    399       O  
ATOM   5658  N   HIS C 296      61.687 -14.742  -9.564  1.00 45.91           N  
ANISOU 5658  N   HIS C 296     7784   4263   5397  -1610  -1119    268       N  
ATOM   5659  CA  HIS C 296      60.672 -14.591 -10.617  1.00 46.78           C  
ANISOU 5659  CA  HIS C 296     7939   4333   5501  -1727  -1463    300       C  
ATOM   5660  C   HIS C 296      59.499 -13.690 -10.148  1.00 50.97           C  
ANISOU 5660  C   HIS C 296     8042   5032   6291  -1702  -1584    399       C  
ATOM   5661  O   HIS C 296      58.344 -13.905 -10.529  1.00 50.36           O  
ANISOU 5661  O   HIS C 296     7830   4960   6342  -1841  -1876    452       O  
ATOM   5662  CB  HIS C 296      60.216 -15.947 -11.202  1.00 48.07           C  
ANISOU 5662  CB  HIS C 296     8309   4347   5608  -1953  -1672    279       C  
ATOM   5663  CG  HIS C 296      61.230 -16.540 -12.123  1.00 51.96           C  
ANISOU 5663  CG  HIS C 296     9296   4643   5805  -1951  -1623    174       C  
ATOM   5664  ND1 HIS C 296      61.123 -16.403 -13.497  1.00 53.77           N  
ANISOU 5664  ND1 HIS C 296     9869   4739   5821  -2004  -1851    140       N  
ATOM   5665  CD2 HIS C 296      62.376 -17.204 -11.836  1.00 53.96           C  
ANISOU 5665  CD2 HIS C 296     9748   4808   5947  -1882  -1356     97       C  
ATOM   5666  CE1 HIS C 296      62.189 -17.002 -14.001  1.00 53.25           C  
ANISOU 5666  CE1 HIS C 296    10205   4509   5517  -1973  -1684     37       C  
ATOM   5667  NE2 HIS C 296      62.973 -17.500 -13.042  1.00 53.76           N  
ANISOU 5667  NE2 HIS C 296    10177   4598   5651  -1891  -1388      8       N  
ATOM   5668  N   PHE C 297      59.829 -12.643  -9.348  1.00 48.06           N  
ANISOU 5668  N   PHE C 297     7467   4791   6002  -1516  -1364    418       N  
ATOM   5669  CA  PHE C 297      58.891 -11.636  -8.822  1.00 47.80           C  
ANISOU 5669  CA  PHE C 297     7050   4909   6203  -1431  -1405    497       C  
ATOM   5670  C   PHE C 297      58.098 -10.952  -9.952  1.00 53.34           C  
ANISOU 5670  C   PHE C 297     7772   5583   6911  -1427  -1750    536       C  
ATOM   5671  O   PHE C 297      56.902 -10.702  -9.793  1.00 50.73           O  
ANISOU 5671  O   PHE C 297     7103   5342   6829  -1447  -1923    609       O  
ATOM   5672  CB  PHE C 297      59.645 -10.603  -7.965  1.00 49.02           C  
ANISOU 5672  CB  PHE C 297     7125   5150   6352  -1224  -1108    486       C  
ATOM   5673  CG  PHE C 297      58.831  -9.476  -7.378  1.00 50.18           C  
ANISOU 5673  CG  PHE C 297     6929   5428   6710  -1097  -1099    551       C  
ATOM   5674  CD1 PHE C 297      57.765  -9.736  -6.522  1.00 52.56           C  
ANISOU 5674  CD1 PHE C 297     6854   5839   7279  -1150  -1073    612       C  
ATOM   5675  CD2 PHE C 297      59.167  -8.151  -7.630  1.00 52.52           C  
ANISOU 5675  CD2 PHE C 297     7290   5727   6939   -919  -1083    549       C  
ATOM   5676  CE1 PHE C 297      57.026  -8.691  -5.960  1.00 53.64           C  
ANISOU 5676  CE1 PHE C 297     6672   6088   7621  -1008  -1028    664       C  
ATOM   5677  CE2 PHE C 297      58.452  -7.105  -7.038  1.00 55.46           C  
ANISOU 5677  CE2 PHE C 297     7367   6200   7504   -777  -1055    602       C  
ATOM   5678  CZ  PHE C 297      57.377  -7.381  -6.216  1.00 53.26           C  
ANISOU 5678  CZ  PHE C 297     6705   6031   7499   -811  -1024    656       C  
ATOM   5679  N   ARG C 298      58.763 -10.695 -11.101  1.00 54.07           N  
ANISOU 5679  N   ARG C 298     8271   5542   6732  -1404  -1850    487       N  
ATOM   5680  CA  ARG C 298      58.166 -10.092 -12.293  1.00 56.04           C  
ANISOU 5680  CA  ARG C 298     8660   5721   6912  -1404  -2199    521       C  
ATOM   5681  C   ARG C 298      56.986 -10.962 -12.757  1.00 63.03           C  
ANISOU 5681  C   ARG C 298     9442   6577   7929  -1612  -2565    562       C  
ATOM   5682  O   ARG C 298      55.901 -10.434 -13.011  1.00 63.21           O  
ANISOU 5682  O   ARG C 298     9213   6656   8147  -1601  -2851    638       O  
ATOM   5683  CB  ARG C 298      59.233  -9.942 -13.399  1.00 58.71           C  
ANISOU 5683  CB  ARG C 298     9532   5891   6883  -1386  -2175    448       C  
ATOM   5684  CG  ARG C 298      58.722  -9.355 -14.727  1.00 70.04           C  
ANISOU 5684  CG  ARG C 298    11232   7211   8169  -1402  -2547    480       C  
ATOM   5685  CD  ARG C 298      59.717  -9.538 -15.862  1.00 82.24           C  
ANISOU 5685  CD  ARG C 298    13360   8563   9323  -1441  -2499    400       C  
ATOM   5686  NE  ARG C 298      60.942  -8.756 -15.653  1.00 94.49           N  
ANISOU 5686  NE  ARG C 298    15046  10118  10738  -1285  -2150    360       N  
ATOM   5687  CZ  ARG C 298      62.171  -9.268 -15.625  1.00108.96           C  
ANISOU 5687  CZ  ARG C 298    17077  11904  12419  -1277  -1806    270       C  
ATOM   5688  NH1 ARG C 298      62.361 -10.569 -15.815  1.00 95.96           N  
ANISOU 5688  NH1 ARG C 298    15556  10187  10718  -1395  -1757    205       N  
ATOM   5689  NH2 ARG C 298      63.219  -8.481 -15.422  1.00 94.24           N  
ANISOU 5689  NH2 ARG C 298    15286  10052  10469  -1152  -1515    243       N  
ATOM   5690  N   ASP C 299      57.198 -12.293 -12.809  1.00 61.40           N  
ANISOU 5690  N   ASP C 299     9407   6283   7640  -1797  -2551    513       N  
ATOM   5691  CA  ASP C 299      56.202 -13.300 -13.175  1.00 62.32           C  
ANISOU 5691  CA  ASP C 299     9464   6351   7866  -2040  -2871    540       C  
ATOM   5692  C   ASP C 299      55.110 -13.393 -12.094  1.00 68.61           C  
ANISOU 5692  C   ASP C 299     9679   7324   9064  -2091  -2856    623       C  
ATOM   5693  O   ASP C 299      53.935 -13.529 -12.433  1.00 67.63           O  
ANISOU 5693  O   ASP C 299     9323   7225   9147  -2221  -3196    685       O  
ATOM   5694  CB  ASP C 299      56.881 -14.673 -13.398  1.00 64.30           C  
ANISOU 5694  CB  ASP C 299    10082   6443   7908  -2200  -2785    456       C  
ATOM   5695  CG  ASP C 299      57.849 -14.745 -14.577  1.00 76.11           C  
ANISOU 5695  CG  ASP C 299    12169   7738   9010  -2181  -2808    366       C  
ATOM   5696  OD1 ASP C 299      58.613 -13.775 -14.787  1.00 76.39           O  
ANISOU 5696  OD1 ASP C 299    12348   7781   8897  -1991  -2628    341       O  
ATOM   5697  OD2 ASP C 299      57.857 -15.780 -15.276  1.00 84.47           O  
ANISOU 5697  OD2 ASP C 299    13562   8625   9907  -2362  -2984    317       O  
ATOM   5698  N   MET C 300      55.504 -13.297 -10.797  1.00 67.96           N  
ANISOU 5698  N   MET C 300     9365   7362   9094  -1991  -2461    624       N  
ATOM   5699  CA  MET C 300      54.588 -13.333  -9.650  1.00 69.15           C  
ANISOU 5699  CA  MET C 300     9000   7677   9596  -2022  -2346    696       C  
ATOM   5700  C   MET C 300      53.626 -12.133  -9.690  1.00 76.87           C  
ANISOU 5700  C   MET C 300     9600   8781  10825  -1882  -2501    770       C  
ATOM   5701  O   MET C 300      52.425 -12.321  -9.490  1.00 76.76           O  
ANISOU 5701  O   MET C 300     9184   8854  11128  -1990  -2656    838       O  
ATOM   5702  CB  MET C 300      55.356 -13.376  -8.312  1.00 71.69           C  
ANISOU 5702  CB  MET C 300     9259   8070   9909  -1919  -1889    674       C  
ATOM   5703  CG  MET C 300      56.129 -14.668  -8.075  1.00 75.95           C  
ANISOU 5703  CG  MET C 300    10087   8492  10276  -2055  -1744    619       C  
ATOM   5704  SD  MET C 300      56.670 -14.891  -6.351  1.00 80.58           S  
ANISOU 5704  SD  MET C 300    10524   9165  10928  -1992  -1291    627       S  
ATOM   5705  CE  MET C 300      58.298 -14.356  -6.452  1.00 77.18           C  
ANISOU 5705  CE  MET C 300    10427   8682  10217  -1762  -1083    544       C  
ATOM   5706  N   LEU C 301      54.155 -10.916  -9.990  1.00 75.96           N  
ANISOU 5706  N   LEU C 301     9621   8663  10579  -1645  -2468    757       N  
ATOM   5707  CA  LEU C 301      53.411  -9.651 -10.093  1.00 77.14           C  
ANISOU 5707  CA  LEU C 301     9493   8896  10921  -1460  -2611    820       C  
ATOM   5708  C   LEU C 301      52.350  -9.685 -11.182  1.00 85.17           C  
ANISOU 5708  C   LEU C 301    10439   9867  12055  -1561  -3120    875       C  
ATOM   5709  O   LEU C 301      51.187  -9.379 -10.913  1.00 84.87           O  
ANISOU 5709  O   LEU C 301     9932   9941  12373  -1535  -3260    949       O  
ATOM   5710  CB  LEU C 301      54.361  -8.467 -10.367  1.00 76.95           C  
ANISOU 5710  CB  LEU C 301     9758   8821  10656  -1223  -2495    787       C  
ATOM   5711  CG  LEU C 301      54.708  -7.539  -9.206  1.00 81.11           C  
ANISOU 5711  CG  LEU C 301    10098   9457  11264  -1007  -2115    785       C  
ATOM   5712  CD1 LEU C 301      55.723  -6.508  -9.647  1.00 81.20           C  
ANISOU 5712  CD1 LEU C 301    10464   9384  11003   -836  -2035    746       C  
ATOM   5713  CD2 LEU C 301      53.479  -6.819  -8.673  1.00 82.75           C  
ANISOU 5713  CD2 LEU C 301     9811   9795  11836   -881  -2157    860       C  
ATOM   5714  N   PHE C 302      52.753 -10.058 -12.410  1.00 85.26           N  
ANISOU 5714  N   PHE C 302    10917   9707  11770  -1673  -3396    838       N  
ATOM   5715  CA  PHE C 302      51.879 -10.121 -13.579  1.00 86.97           C  
ANISOU 5715  CA  PHE C 302    11181   9840  12022  -1786  -3933    884       C  
ATOM   5716  C   PHE C 302      50.726 -11.123 -13.435  1.00 93.49           C  
ANISOU 5716  C   PHE C 302    11631  10722  13167  -2038  -4162    930       C  
ATOM   5717  O   PHE C 302      49.647 -10.874 -13.978  1.00 94.02           O  
ANISOU 5717  O   PHE C 302    11455  10807  13461  -2074  -4586   1000       O  
ATOM   5718  CB  PHE C 302      52.694 -10.375 -14.860  1.00 89.33           C  
ANISOU 5718  CB  PHE C 302    12147   9920  11875  -1864  -4118    819       C  
ATOM   5719  CG  PHE C 302      53.664  -9.278 -15.254  1.00 91.57           C  
ANISOU 5719  CG  PHE C 302    12801  10130  11860  -1642  -3973    790       C  
ATOM   5720  CD1 PHE C 302      53.419  -7.948 -14.917  1.00 95.14           C  
ANISOU 5720  CD1 PHE C 302    13028  10666  12455  -1397  -3958    849       C  
ATOM   5721  CD2 PHE C 302      54.791  -9.565 -16.013  1.00 94.42           C  
ANISOU 5721  CD2 PHE C 302    13747  10324  11804  -1684  -3857    704       C  
ATOM   5722  CE1 PHE C 302      54.313  -6.937 -15.283  1.00 96.22           C  
ANISOU 5722  CE1 PHE C 302    13527  10719  12313  -1219  -3825    826       C  
ATOM   5723  CE2 PHE C 302      55.670  -8.548 -16.403  1.00 97.48           C  
ANISOU 5723  CE2 PHE C 302    14469  10641  11929  -1507  -3710    681       C  
ATOM   5724  CZ  PHE C 302      55.428  -7.243 -16.030  1.00 95.54           C  
ANISOU 5724  CZ  PHE C 302    14002  10477  11821  -1287  -3701    745       C  
ATOM   5725  N   SER C 303      50.939 -12.227 -12.688  1.00 90.87           N  
ANISOU 5725  N   SER C 303    11241  10415  12871  -2214  -3893    897       N  
ATOM   5726  CA  SER C 303      49.913 -13.242 -12.425  1.00 91.12           C  
ANISOU 5726  CA  SER C 303    10923  10496  13204  -2486  -4043    940       C  
ATOM   5727  C   SER C 303      48.798 -12.665 -11.527  1.00 96.26           C  
ANISOU 5727  C   SER C 303    10873  11360  14340  -2400  -3957   1027       C  
ATOM   5728  O   SER C 303      47.617 -12.939 -11.770  1.00 96.34           O  
ANISOU 5728  O   SER C 303    10506  11422  14679  -2562  -4275   1092       O  
ATOM   5729  CB  SER C 303      50.531 -14.474 -11.765  1.00 94.26           C  
ANISOU 5729  CB  SER C 303    11494  10841  13479  -2669  -3730    885       C  
ATOM   5730  OG  SER C 303      51.607 -14.994 -12.528  1.00102.42           O  
ANISOU 5730  OG  SER C 303    13155  11674  14088  -2722  -3768    797       O  
ATOM   5731  N   LYS C 304      49.182 -11.845 -10.515  1.00 92.47           N  
ANISOU 5731  N   LYS C 304    10228  10999  13908  -2144  -3529   1025       N  
ATOM   5732  CA  LYS C 304      48.274 -11.204  -9.561  1.00114.77           C  
ANISOU 5732  CA  LYS C 304    12440  14014  17152  -2014  -3348   1091       C  
ATOM   5733  C   LYS C 304      47.472 -10.072 -10.204  1.00139.59           C  
ANISOU 5733  C   LYS C 304    15329  17197  20512  -1820  -3700   1152       C  
ATOM   5734  O   LYS C 304      48.026  -9.246 -10.927  1.00103.90           O  
ANISOU 5734  O   LYS C 304    11151  12582  15743  -1636  -3857   1135       O  
ATOM   5735  CB  LYS C 304      49.049 -10.696  -8.334  1.00117.19           C  
ANISOU 5735  CB  LYS C 304    12755  14396  17375  -1806  -2793   1056       C  
TER    5736      LYS C 304                                                      
ATOM   5737  N   GLU D   9      50.188 -28.800 -12.809  1.00105.62           N  
ANISOU 5737  N   GLU D   9    13817  10136  16177  -4173  -8199   1237       N  
ATOM   5738  CA  GLU D   9      49.465 -29.892 -12.156  1.00105.33           C  
ANISOU 5738  CA  GLU D   9    13271   9976  16774  -4529  -8217   1326       C  
ATOM   5739  C   GLU D   9      50.233 -31.222 -12.258  1.00108.22           C  
ANISOU 5739  C   GLU D   9    14423  10143  16554  -4732  -8196   1015       C  
ATOM   5740  O   GLU D   9      49.783 -32.161 -12.921  1.00107.64           O  
ANISOU 5740  O   GLU D   9    14672   9757  16470  -5091  -8969    953       O  
ATOM   5741  CB  GLU D   9      48.025 -30.017 -12.705  1.00106.70           C  
ANISOU 5741  CB  GLU D   9    12807   9954  17781  -4870  -9148   1618       C  
ATOM   5742  CG  GLU D   9      46.998 -30.456 -11.672  1.00117.17           C  
ANISOU 5742  CG  GLU D   9    13101  11284  20136  -5115  -8886   1899       C  
ATOM   5743  CD  GLU D   9      47.061 -31.910 -11.244  1.00139.91           C  
ANISOU 5743  CD  GLU D   9    16198  13957  23006  -5497  -8811   1787       C  
ATOM   5744  OE1 GLU D   9      46.347 -32.741 -11.851  1.00137.33           O  
ANISOU 5744  OE1 GLU D   9    15912  13306  22963  -5947  -9681   1829       O  
ATOM   5745  OE2 GLU D   9      47.826 -32.217 -10.300  1.00132.57           O  
ANISOU 5745  OE2 GLU D   9    15426  13157  21787  -5351  -7931   1662       O  
ATOM   5746  N   VAL D  10      51.401 -31.287 -11.594  1.00104.03           N  
ANISOU 5746  N   VAL D  10    14214   9763  15550  -4488  -7344    816       N  
ATOM   5747  CA  VAL D  10      52.261 -32.477 -11.560  1.00103.12           C  
ANISOU 5747  CA  VAL D  10    14805   9473  14904  -4586  -7189    521       C  
ATOM   5748  C   VAL D  10      52.313 -32.988 -10.114  1.00104.21           C  
ANISOU 5748  C   VAL D  10    14475   9679  15442  -4630  -6482    600       C  
ATOM   5749  O   VAL D  10      52.539 -32.194  -9.198  1.00103.93           O  
ANISOU 5749  O   VAL D  10    14005   9915  15568  -4361  -5790    710       O  
ATOM   5750  CB  VAL D  10      53.683 -32.192 -12.142  1.00107.27           C  
ANISOU 5750  CB  VAL D  10    16222  10073  14462  -4245  -6876    212       C  
ATOM   5751  CG1 VAL D  10      54.560 -33.442 -12.135  1.00106.93           C  
ANISOU 5751  CG1 VAL D  10    16890   9816  13925  -4305  -6740    -96       C  
ATOM   5752  CG2 VAL D  10      53.601 -31.620 -13.555  1.00107.24           C  
ANISOU 5752  CG2 VAL D  10    16717  10008  14022  -4190  -7506    182       C  
ATOM   5753  N   GLN D  11      52.077 -34.301  -9.913  1.00 98.21           N  
ANISOU 5753  N   GLN D  11    13851   8638  14826  -4977  -6685    553       N  
ATOM   5754  CA  GLN D  11      52.119 -34.938  -8.590  1.00 96.77           C  
ANISOU 5754  CA  GLN D  11    13344   8454  14970  -5069  -6076    647       C  
ATOM   5755  C   GLN D  11      53.471 -35.625  -8.360  1.00 96.72           C  
ANISOU 5755  C   GLN D  11    14107   8378  14262  -4884  -5655    328       C  
ATOM   5756  O   GLN D  11      54.068 -36.122  -9.316  1.00 95.88           O  
ANISOU 5756  O   GLN D  11    14770   8072  13587  -4875  -6029     43       O  
ATOM   5757  CB  GLN D  11      50.962 -35.935  -8.419  1.00 98.27           C  
ANISOU 5757  CB  GLN D  11    13135   8344  15860  -5597  -6561    858       C  
ATOM   5758  CG  GLN D  11      49.596 -35.278  -8.195  1.00113.93           C  
ANISOU 5758  CG  GLN D  11    14091  10426  18772  -5771  -6774   1261       C  
ATOM   5759  CD  GLN D  11      49.080 -35.476  -6.786  1.00133.88           C  
ANISOU 5759  CD  GLN D  11    15839  13121  21909  -5771  -5968   1564       C  
ATOM   5760  OE1 GLN D  11      48.835 -36.601  -6.333  1.00129.59           O  
ANISOU 5760  OE1 GLN D  11    15229  12393  21614  -6065  -5776   1661       O  
ATOM   5761  NE2 GLN D  11      48.886 -34.381  -6.065  1.00125.77           N  
ANISOU 5761  NE2 GLN D  11    14247  12420  21120  -5434  -5466   1730       N  
ATOM   5762  N   LEU D  12      53.955 -35.641  -7.094  1.00 90.55           N  
ANISOU 5762  N   LEU D  12    13140   7745  13518  -4716  -4883    378       N  
ATOM   5763  CA  LEU D  12      55.243 -36.241  -6.694  1.00 88.64           C  
ANISOU 5763  CA  LEU D  12    13514   7446  12718  -4510  -4460    121       C  
ATOM   5764  C   LEU D  12      55.103 -37.345  -5.612  1.00 89.66           C  
ANISOU 5764  C   LEU D  12    13550   7388  13128  -4726  -4178    233       C  
ATOM   5765  O   LEU D  12      54.273 -37.211  -4.709  1.00 88.68           O  
ANISOU 5765  O   LEU D  12    12785   7354  13555  -4865  -3892    541       O  
ATOM   5766  CB  LEU D  12      56.191 -35.127  -6.204  1.00 88.14           C  
ANISOU 5766  CB  LEU D  12    13448   7720  12320  -4049  -3840     58       C  
ATOM   5767  CG  LEU D  12      57.272 -34.559  -7.161  1.00 91.80           C  
ANISOU 5767  CG  LEU D  12    14479   8268  12132  -3741  -3886   -209       C  
ATOM   5768  CD1 LEU D  12      56.706 -34.111  -8.495  1.00 91.77           C  
ANISOU 5768  CD1 LEU D  12    14574   8232  12062  -3833  -4511   -206       C  
ATOM   5769  CD2 LEU D  12      57.958 -33.366  -6.539  1.00 92.64           C  
ANISOU 5769  CD2 LEU D  12    14407   8685  12107  -3372  -3312   -187       C  
ATOM   5770  N   VAL D  13      55.914 -38.427  -5.706  1.00 85.05           N  
ANISOU 5770  N   VAL D  13    13626   6526  12165  -4739  -4234     -5       N  
ATOM   5771  CA  VAL D  13      55.926 -39.541  -4.732  1.00 84.52           C  
ANISOU 5771  CA  VAL D  13    13606   6224  12284  -4925  -4001     90       C  
ATOM   5772  C   VAL D  13      57.358 -39.991  -4.339  1.00 85.70           C  
ANISOU 5772  C   VAL D  13    14361   6314  11889  -4589  -3623   -163       C  
ATOM   5773  O   VAL D  13      58.146 -40.349  -5.219  1.00 85.50           O  
ANISOU 5773  O   VAL D  13    14950   6133  11402  -4434  -3855   -479       O  
ATOM   5774  CB  VAL D  13      55.051 -40.775  -5.128  1.00 89.50           C  
ANISOU 5774  CB  VAL D  13    14306   6413  13286  -5445  -4607    164       C  
ATOM   5775  CG1 VAL D  13      53.567 -40.521  -4.885  1.00 89.67           C  
ANISOU 5775  CG1 VAL D  13    13489   6485  14095  -5830  -4789    557       C  
ATOM   5776  CG2 VAL D  13      55.302 -41.237  -6.562  1.00 89.56           C  
ANISOU 5776  CG2 VAL D  13    15016   6128  12883  -5489  -5296   -174       C  
ATOM   5777  N   GLU D  14      57.666 -39.999  -3.016  1.00 80.20           N  
ANISOU 5777  N   GLU D  14    13499   5716  11258  -4472  -3050    -12       N  
ATOM   5778  CA  GLU D  14      58.937 -40.461  -2.422  1.00 80.01           C  
ANISOU 5778  CA  GLU D  14    13948   5613  10841  -4178  -2719   -178       C  
ATOM   5779  C   GLU D  14      58.783 -41.950  -2.015  1.00 84.85           C  
ANISOU 5779  C   GLU D  14    14858   5785  11597  -4465  -2866   -119       C  
ATOM   5780  O   GLU D  14      57.664 -42.345  -1.671  1.00 84.60           O  
ANISOU 5780  O   GLU D  14    14476   5628  12038  -4873  -2963    164       O  
ATOM   5781  CB  GLU D  14      59.297 -39.628  -1.181  1.00 81.52           C  
ANISOU 5781  CB  GLU D  14    13859   6105  11009  -3921  -2113    -26       C  
ATOM   5782  CG  GLU D  14      59.584 -38.160  -1.440  1.00 93.20           C  
ANISOU 5782  CG  GLU D  14    15103   7970  12340  -3614  -1937    -87       C  
ATOM   5783  CD  GLU D  14      58.351 -37.294  -1.572  1.00115.43           C  
ANISOU 5783  CD  GLU D  14    17313  10992  15554  -3768  -1970    138       C  
ATOM   5784  OE1 GLU D  14      57.934 -36.697  -0.557  1.00102.77           O  
ANISOU 5784  OE1 GLU D  14    15331   9573  14146  -3704  -1539    349       O  
ATOM   5785  OE2 GLU D  14      57.794 -37.222  -2.690  1.00117.86           O  
ANISOU 5785  OE2 GLU D  14    17550  11255  15977  -3937  -2440    102       O  
ATOM   5786  N   SER D  15      59.874 -42.779  -2.032  1.00 82.16           N  
ANISOU 5786  N   SER D  15    15125   5186  10907  -4259  -2875   -358       N  
ATOM   5787  CA  SER D  15      59.674 -44.204  -1.720  1.00 83.15           C  
ANISOU 5787  CA  SER D  15    15572   4835  11186  -4543  -3074   -297       C  
ATOM   5788  C   SER D  15      60.804 -45.003  -0.992  1.00 88.70           C  
ANISOU 5788  C   SER D  15    16757   5305  11642  -4282  -2850   -382       C  
ATOM   5789  O   SER D  15      60.507 -46.080  -0.449  1.00 89.23           O  
ANISOU 5789  O   SER D  15    16990   5007  11905  -4548  -2916   -214       O  
ATOM   5790  CB  SER D  15      59.323 -44.967  -2.998  1.00 86.00           C  
ANISOU 5790  CB  SER D  15    16321   4828  11528  -4773  -3712   -518       C  
ATOM   5791  OG  SER D  15      60.380 -44.897  -3.941  1.00 93.64           O  
ANISOU 5791  OG  SER D  15    17824   5769  11984  -4376  -3789   -919       O  
ATOM   5792  N   GLY D  16      62.055 -44.541  -1.030  1.00 83.86           N  
ANISOU 5792  N   GLY D  16    16358   4853  10650  -3796  -2639   -620       N  
ATOM   5793  CA  GLY D  16      63.163 -45.314  -0.461  1.00 82.58           C  
ANISOU 5793  CA  GLY D  16    16632   4440  10307  -3517  -2521   -714       C  
ATOM   5794  C   GLY D  16      63.357 -45.321   1.042  1.00 84.27           C  
ANISOU 5794  C   GLY D  16    16746   4696  10576  -3473  -2174   -438       C  
ATOM   5795  O   GLY D  16      64.367 -45.843   1.518  1.00 83.48           O  
ANISOU 5795  O   GLY D  16    16990   4411  10317  -3189  -2119   -514       O  
ATOM   5796  N   GLY D  17      62.405 -44.751   1.781  1.00 80.15           N  
ANISOU 5796  N   GLY D  17    15785   4399  10269  -3726  -1940   -116       N  
ATOM   5797  CA  GLY D  17      62.470 -44.582   3.230  1.00 79.92           C  
ANISOU 5797  CA  GLY D  17    15701   4451  10216  -3683  -1551    162       C  
ATOM   5798  C   GLY D  17      62.321 -45.810   4.103  1.00 84.71           C  
ANISOU 5798  C   GLY D  17    16660   4633  10894  -3889  -1554    390       C  
ATOM   5799  O   GLY D  17      61.627 -46.767   3.749  1.00 85.02           O  
ANISOU 5799  O   GLY D  17    16788   4329  11187  -4269  -1803    480       O  
ATOM   5800  N   GLY D  18      62.949 -45.748   5.272  1.00 80.81           N  
ANISOU 5800  N   GLY D  18    16385   4144  10176  -3658  -1305    505       N  
ATOM   5801  CA  GLY D  18      62.916 -46.818   6.256  1.00 80.59           C  
ANISOU 5801  CA  GLY D  18    16762   3719  10138  -3805  -1273    760       C  
ATOM   5802  C   GLY D  18      64.022 -46.763   7.288  1.00 84.20           C  
ANISOU 5802  C   GLY D  18    17590   4144  10257  -3427  -1168    778       C  
ATOM   5803  O   GLY D  18      64.721 -45.750   7.422  1.00 83.00           O  
ANISOU 5803  O   GLY D  18    17311   4323   9901  -3082  -1058    637       O  
ATOM   5804  N   LEU D  19      64.178 -47.873   8.026  1.00 81.33           N  
ANISOU 5804  N   LEU D  19    17708   3342   9852  -3513  -1253    970       N  
ATOM   5805  CA  LEU D  19      65.173 -48.030   9.089  1.00 81.22           C  
ANISOU 5805  CA  LEU D  19    18140   3189   9532  -3197  -1258   1043       C  
ATOM   5806  C   LEU D  19      66.567 -48.368   8.546  1.00 84.46           C  
ANISOU 5806  C   LEU D  19    18783   3423   9886  -2754  -1641    698       C  
ATOM   5807  O   LEU D  19      66.709 -49.291   7.739  1.00 86.53           O  
ANISOU 5807  O   LEU D  19    19218   3347  10314  -2778  -1927    529       O  
ATOM   5808  CB  LEU D  19      64.709 -49.108  10.093  1.00 81.09           C  
ANISOU 5808  CB  LEU D  19    18572   2739   9501  -3495  -1194   1440       C  
ATOM   5809  CG  LEU D  19      65.458 -49.182  11.434  1.00 85.09           C  
ANISOU 5809  CG  LEU D  19    19574   3135   9623  -3264  -1117   1649       C  
ATOM   5810  CD1 LEU D  19      65.060 -48.026  12.376  1.00 85.14           C  
ANISOU 5810  CD1 LEU D  19    19424   3547   9378  -3289   -616   1859       C  
ATOM   5811  CD2 LEU D  19      65.217 -50.499  12.099  1.00 83.69           C  
ANISOU 5811  CD2 LEU D  19    19948   2404   9446  -3503  -1208   1972       C  
ATOM   5812  N   VAL D  20      67.586 -47.637   9.021  1.00 77.13           N  
ANISOU 5812  N   VAL D  20    17868   2692   8746  -2349  -1646    606       N  
ATOM   5813  CA  VAL D  20      68.997 -47.829   8.673  1.00 75.80           C  
ANISOU 5813  CA  VAL D  20    17822   2392   8587  -1885  -1956    334       C  
ATOM   5814  C   VAL D  20      69.853 -47.742   9.916  1.00 78.28           C  
ANISOU 5814  C   VAL D  20    18435   2620   8687  -1617  -2068    483       C  
ATOM   5815  O   VAL D  20      69.555 -46.951  10.810  1.00 77.12           O  
ANISOU 5815  O   VAL D  20    18276   2718   8309  -1679  -1860    662       O  
ATOM   5816  CB  VAL D  20      69.569 -46.880   7.579  1.00 79.44           C  
ANISOU 5816  CB  VAL D  20    17835   3215   9134  -1619  -1944    -22       C  
ATOM   5817  CG1 VAL D  20      69.806 -47.632   6.275  1.00 79.88           C  
ANISOU 5817  CG1 VAL D  20    17944   3045   9364  -1575  -2110   -299       C  
ATOM   5818  CG2 VAL D  20      68.712 -45.639   7.366  1.00 78.52           C  
ANISOU 5818  CG2 VAL D  20    17265   3598   8972  -1799  -1643      2       C  
ATOM   5819  N   GLN D  21      70.945 -48.520   9.952  1.00 73.97           N  
ANISOU 5819  N   GLN D  21    18173   1712   8220  -1291  -2421    396       N  
ATOM   5820  CA  GLN D  21      71.895 -48.481  11.057  1.00 73.55           C  
ANISOU 5820  CA  GLN D  21    18407   1528   8012   -999  -2666    523       C  
ATOM   5821  C   GLN D  21      72.842 -47.245  10.946  1.00 75.18           C  
ANISOU 5821  C   GLN D  21    18191   2124   8250   -661  -2721    319       C  
ATOM   5822  O   GLN D  21      73.130 -46.805   9.824  1.00 73.18           O  
ANISOU 5822  O   GLN D  21    17486   2106   8214   -537  -2634     38       O  
ATOM   5823  CB  GLN D  21      72.692 -49.791  11.116  1.00 75.32           C  
ANISOU 5823  CB  GLN D  21    19038   1189   8390   -760  -3063    524       C  
ATOM   5824  CG  GLN D  21      71.918 -50.943  11.752  1.00 98.63           C  
ANISOU 5824  CG  GLN D  21    22541   3686  11248  -1103  -3074    831       C  
ATOM   5825  CD  GLN D  21      72.829 -52.027  12.272  1.00134.32           C  
ANISOU 5825  CD  GLN D  21    27565   7632  15838   -825  -3514    916       C  
ATOM   5826  OE1 GLN D  21      73.840 -51.761  12.935  1.00136.06           O  
ANISOU 5826  OE1 GLN D  21    27995   7774  15928   -548  -3791   1034       O  
ATOM   5827  NE2 GLN D  21      72.486 -53.280  11.999  1.00126.86           N  
ANISOU 5827  NE2 GLN D  21    26861   6234  15106   -893  -3638    861       N  
ATOM   5828  N   PRO D  22      73.332 -46.677  12.087  1.00 71.61           N  
ANISOU 5828  N   PRO D  22    17915   1719   7572   -529  -2878    464       N  
ATOM   5829  CA  PRO D  22      74.265 -45.537  12.012  1.00 71.04           C  
ANISOU 5829  CA  PRO D  22    17445   1955   7590   -247  -3002    288       C  
ATOM   5830  C   PRO D  22      75.531 -45.849  11.210  1.00 74.62           C  
ANISOU 5830  C   PRO D  22    17577   2301   8474    147  -3268     51       C  
ATOM   5831  O   PRO D  22      76.204 -46.844  11.473  1.00 75.50           O  
ANISOU 5831  O   PRO D  22    17953   2001   8732    368  -3600     97       O  
ATOM   5832  CB  PRO D  22      74.585 -45.246  13.485  1.00 72.69           C  
ANISOU 5832  CB  PRO D  22    18101   2054   7465   -186  -3267    510       C  
ATOM   5833  CG  PRO D  22      73.448 -45.801  14.235  1.00 77.24           C  
ANISOU 5833  CG  PRO D  22    19212   2464   7673   -516  -3024    802       C  
ATOM   5834  CD  PRO D  22      73.092 -47.054  13.494  1.00 73.34           C  
ANISOU 5834  CD  PRO D  22    18761   1678   7428   -632  -2982    799       C  
ATOM   5835  N   GLY D  23      75.812 -45.005  10.222  1.00 69.72           N  
ANISOU 5835  N   GLY D  23    16392   2038   8061    238  -3080   -184       N  
ATOM   5836  CA  GLY D  23      76.938 -45.144   9.307  1.00 68.79           C  
ANISOU 5836  CA  GLY D  23    15881   1896   8361    607  -3166   -412       C  
ATOM   5837  C   GLY D  23      76.502 -45.688   7.963  1.00 70.91           C  
ANISOU 5837  C   GLY D  23    16061   2153   8727    566  -2870   -621       C  
ATOM   5838  O   GLY D  23      77.257 -45.621   6.987  1.00 70.09           O  
ANISOU 5838  O   GLY D  23    15621   2107   8901    852  -2776   -840       O  
ATOM   5839  N   GLY D  24      75.271 -46.206   7.925  1.00 66.64           N  
ANISOU 5839  N   GLY D  24    15837   1527   7957    200  -2720   -541       N  
ATOM   5840  CA  GLY D  24      74.643 -46.796   6.749  1.00 65.81           C  
ANISOU 5840  CA  GLY D  24    15775   1344   7885     69  -2536   -717       C  
ATOM   5841  C   GLY D  24      74.412 -45.857   5.581  1.00 69.10           C  
ANISOU 5841  C   GLY D  24    15770   2175   8310     28  -2240   -929       C  
ATOM   5842  O   GLY D  24      74.781 -44.686   5.627  1.00 68.85           O  
ANISOU 5842  O   GLY D  24    15348   2506   8305    125  -2142   -949       O  
ATOM   5843  N   SER D  25      73.808 -46.398   4.514  1.00 65.07           N  
ANISOU 5843  N   SER D  25    15386   1570   7768   -122  -2141  -1084       N  
ATOM   5844  CA  SER D  25      73.467 -45.725   3.258  1.00 63.85           C  
ANISOU 5844  CA  SER D  25    14973   1727   7560   -185  -1912  -1286       C  
ATOM   5845  C   SER D  25      72.016 -46.010   2.882  1.00 65.96           C  
ANISOU 5845  C   SER D  25    15406   1955   7701   -648  -1910  -1242       C  
ATOM   5846  O   SER D  25      71.504 -47.108   3.119  1.00 64.02           O  
ANISOU 5846  O   SER D  25    15539   1314   7470   -836  -2081  -1169       O  
ATOM   5847  CB  SER D  25      74.374 -46.206   2.128  1.00 67.02           C  
ANISOU 5847  CB  SER D  25    15416   1981   8066    207  -1843  -1587       C  
ATOM   5848  OG  SER D  25      75.584 -45.472   2.089  1.00 74.62           O  
ANISOU 5848  OG  SER D  25    16000   3135   9217    597  -1740  -1630       O  
ATOM   5849  N   LEU D  26      71.359 -45.021   2.297  1.00 62.60           N  
ANISOU 5849  N   LEU D  26    14680   1913   7193   -839  -1749  -1266       N  
ATOM   5850  CA  LEU D  26      69.978 -45.141   1.841  1.00 62.83           C  
ANISOU 5850  CA  LEU D  26    14748   1946   7178  -1275  -1789  -1217       C  
ATOM   5851  C   LEU D  26      69.865 -44.335   0.551  1.00 66.58           C  
ANISOU 5851  C   LEU D  26    15017   2719   7560  -1242  -1690  -1420       C  
ATOM   5852  O   LEU D  26      70.483 -43.274   0.448  1.00 66.14           O  
ANISOU 5852  O   LEU D  26    14644   3009   7478  -1035  -1504  -1449       O  
ATOM   5853  CB  LEU D  26      69.011 -44.540   2.889  1.00 63.16           C  
ANISOU 5853  CB  LEU D  26    14572   2192   7233  -1611  -1687   -897       C  
ATOM   5854  CG  LEU D  26      68.035 -45.432   3.678  1.00 67.94           C  
ANISOU 5854  CG  LEU D  26    15413   2493   7909  -1971  -1761   -628       C  
ATOM   5855  CD1 LEU D  26      66.886 -44.603   4.223  1.00 67.76           C  
ANISOU 5855  CD1 LEU D  26    15065   2766   7915  -2293  -1537   -358       C  
ATOM   5856  CD2 LEU D  26      67.476 -46.583   2.856  1.00 69.28           C  
ANISOU 5856  CD2 LEU D  26    15876   2269   8177  -2214  -2007   -716       C  
ATOM   5857  N   ARG D  27      69.074 -44.825  -0.416  1.00 63.24           N  
ANISOU 5857  N   ARG D  27    14812   2137   7082  -1463  -1851  -1544       N  
ATOM   5858  CA  ARG D  27      68.829 -44.134  -1.671  1.00 62.98           C  
ANISOU 5858  CA  ARG D  27    14695   2337   6899  -1474  -1823  -1714       C  
ATOM   5859  C   ARG D  27      67.349 -43.786  -1.787  1.00 68.26           C  
ANISOU 5859  C   ARG D  27    15166   3127   7642  -1950  -1978  -1540       C  
ATOM   5860  O   ARG D  27      66.504 -44.677  -1.733  1.00 69.32           O  
ANISOU 5860  O   ARG D  27    15496   2951   7892  -2281  -2233  -1470       O  
ATOM   5861  CB  ARG D  27      69.298 -44.956  -2.872  1.00 63.69           C  
ANISOU 5861  CB  ARG D  27    15275   2115   6809  -1277  -1924  -2043       C  
ATOM   5862  CG  ARG D  27      69.460 -44.115  -4.141  1.00 77.31           C  
ANISOU 5862  CG  ARG D  27    16986   4106   8283  -1154  -1804  -2229       C  
ATOM   5863  CD  ARG D  27      69.781 -44.969  -5.338  1.00 88.18           C  
ANISOU 5863  CD  ARG D  27    18966   5138   9398   -971  -1887  -2563       C  
ATOM   5864  NE  ARG D  27      68.580 -45.264  -6.118  1.00103.76           N  
ANISOU 5864  NE  ARG D  27    21254   6927  11244  -1372  -2294  -2618       N  
ATOM   5865  CZ  ARG D  27      67.936 -46.427  -6.118  1.00120.15           C  
ANISOU 5865  CZ  ARG D  27    23702   8542  13408  -1642  -2674  -2645       C  
ATOM   5866  NH1 ARG D  27      68.374 -47.440  -5.378  1.00110.13           N  
ANISOU 5866  NH1 ARG D  27    22584   6938  12322  -1536  -2671  -2618       N  
ATOM   5867  NH2 ARG D  27      66.850 -46.589  -6.863  1.00106.23           N  
ANISOU 5867  NH2 ARG D  27    22170   6619  11574  -2033  -3104  -2682       N  
ATOM   5868  N   LEU D  28      67.039 -42.486  -1.913  1.00 65.36           N  
ANISOU 5868  N   LEU D  28    14381   3187   7266  -1986  -1832  -1449       N  
ATOM   5869  CA  LEU D  28      65.664 -41.996  -2.053  1.00 64.51           C  
ANISOU 5869  CA  LEU D  28    13982   3233   7297  -2379  -1958  -1269       C  
ATOM   5870  C   LEU D  28      65.360 -41.656  -3.508  1.00 68.54           C  
ANISOU 5870  C   LEU D  28    14593   3810   7639  -2421  -2163  -1447       C  
ATOM   5871  O   LEU D  28      66.263 -41.255  -4.250  1.00 67.77           O  
ANISOU 5871  O   LEU D  28    14638   3825   7285  -2105  -2030  -1650       O  
ATOM   5872  CB  LEU D  28      65.381 -40.777  -1.142  1.00 63.69           C  
ANISOU 5872  CB  LEU D  28    13377   3514   7307  -2380  -1680  -1032       C  
ATOM   5873  CG  LEU D  28      65.610 -40.933   0.375  1.00 66.67           C  
ANISOU 5873  CG  LEU D  28    13711   3854   7767  -2340  -1470   -833       C  
ATOM   5874  CD1 LEU D  28      65.308 -39.661   1.086  1.00 65.41           C  
ANISOU 5874  CD1 LEU D  28    13156   4049   7649  -2316  -1209   -659       C  
ATOM   5875  CD2 LEU D  28      64.764 -42.066   0.989  1.00 67.83           C  
ANISOU 5875  CD2 LEU D  28    13997   3679   8095  -2683  -1579   -638       C  
ATOM   5876  N   SER D  29      64.088 -41.833  -3.909  1.00 65.13           N  
ANISOU 5876  N   SER D  29    14093   3289   7363  -2820  -2495  -1351       N  
ATOM   5877  CA  SER D  29      63.597 -41.568  -5.263  1.00 64.71           C  
ANISOU 5877  CA  SER D  29    14187   3250   7150  -2924  -2819  -1487       C  
ATOM   5878  C   SER D  29      62.429 -40.587  -5.222  1.00 68.89           C  
ANISOU 5878  C   SER D  29    14164   4062   7948  -3191  -2920  -1234       C  
ATOM   5879  O   SER D  29      61.621 -40.622  -4.295  1.00 67.26           O  
ANISOU 5879  O   SER D  29    13551   3882   8125  -3440  -2865   -962       O  
ATOM   5880  CB  SER D  29      63.148 -42.862  -5.936  1.00 68.09           C  
ANISOU 5880  CB  SER D  29    15130   3198   7544  -3167  -3294  -1641       C  
ATOM   5881  OG  SER D  29      64.111 -43.896  -5.826  1.00 79.03           O  
ANISOU 5881  OG  SER D  29    17022   4256   8752  -2918  -3200  -1857       O  
ATOM   5882  N   CYS D  30      62.353 -39.713  -6.232  1.00 67.41           N  
ANISOU 5882  N   CYS D  30    13977   4073   7564  -3118  -3043  -1310       N  
ATOM   5883  CA  CYS D  30      61.287 -38.730  -6.412  1.00 67.91           C  
ANISOU 5883  CA  CYS D  30    13552   4378   7873  -3318  -3209  -1095       C  
ATOM   5884  C   CYS D  30      60.690 -38.961  -7.813  1.00 75.21           C  
ANISOU 5884  C   CYS D  30    14827   5120   8628  -3505  -3801  -1222       C  
ATOM   5885  O   CYS D  30      61.320 -38.651  -8.829  1.00 74.33           O  
ANISOU 5885  O   CYS D  30    15155   5039   8049  -3277  -3827  -1435       O  
ATOM   5886  CB  CYS D  30      61.825 -37.311  -6.240  1.00 67.69           C  
ANISOU 5886  CB  CYS D  30    13217   4755   7748  -3017  -2814  -1036       C  
ATOM   5887  SG  CYS D  30      60.563 -36.009  -6.306  1.00 71.07           S  
ANISOU 5887  SG  CYS D  30    13016   5467   8522  -3178  -2962   -760       S  
ATOM   5888  N   GLU D  31      59.518 -39.606  -7.858  1.00 74.65           N  
ANISOU 5888  N   GLU D  31    14620   4816   8927  -3931  -4285  -1091       N  
ATOM   5889  CA  GLU D  31      58.853 -39.913  -9.116  1.00 75.95           C  
ANISOU 5889  CA  GLU D  31    15141   4744   8972  -4167  -4980  -1199       C  
ATOM   5890  C   GLU D  31      57.747 -38.905  -9.386  1.00 82.72           C  
ANISOU 5890  C   GLU D  31    15411   5821  10196  -4364  -5288   -936       C  
ATOM   5891  O   GLU D  31      56.937 -38.623  -8.496  1.00 82.72           O  
ANISOU 5891  O   GLU D  31    14686   5956  10787  -4546  -5151   -627       O  
ATOM   5892  CB  GLU D  31      58.326 -41.357  -9.127  1.00 77.24           C  
ANISOU 5892  CB  GLU D  31    15623   4409   9316  -4533  -5446  -1259       C  
ATOM   5893  N   ALA D  32      57.746 -38.337 -10.609  1.00 80.48           N  
ANISOU 5893  N   ALA D  32    15463   5568   9548  -4294  -5670  -1049       N  
ATOM   5894  CA  ALA D  32      56.783 -37.340 -11.078  1.00110.19           C  
ANISOU 5894  CA  ALA D  32    18770   9504  13595  -4428  -6060   -821       C  
ATOM   5895  C   ALA D  32      55.447 -37.992 -11.391  1.00131.32           C  
ANISOU 5895  C   ALA D  32    21300  11861  16734  -4924  -6881   -697       C  
ATOM   5896  O   ALA D  32      55.417 -39.128 -11.846  1.00 94.73           O  
ANISOU 5896  O   ALA D  32    17296   6826  11871  -5115  -7347   -910       O  
ATOM   5897  CB  ALA D  32      57.321 -36.648 -12.318  1.00110.94           C  
ANISOU 5897  CB  ALA D  32    19393   9707  13052  -4160  -6170   -980       C  
ATOM   5898  N   LEU D  37      60.770 -33.986 -13.645  1.00 85.15           N  
ANISOU 5898  N   LEU D  37    17279   7090   7985  -2972  -4851  -1312       N  
ATOM   5899  CA  LEU D  37      60.990 -34.019 -15.095  1.00 85.12           C  
ANISOU 5899  CA  LEU D  37    18107   6946   7288  -2902  -5150  -1464       C  
ATOM   5900  C   LEU D  37      61.928 -32.892 -15.602  1.00 87.76           C  
ANISOU 5900  C   LEU D  37    18648   7533   7165  -2546  -4556  -1452       C  
ATOM   5901  O   LEU D  37      62.201 -31.941 -14.867  1.00 86.87           O  
ANISOU 5901  O   LEU D  37    17953   7699   7355  -2399  -4044  -1300       O  
ATOM   5902  CB  LEU D  37      59.655 -34.034 -15.865  1.00 85.27           C  
ANISOU 5902  CB  LEU D  37    18153   6835   7410  -3206  -6036  -1319       C  
ATOM   5903  N   ALA D  38      62.393 -33.018 -16.870  1.00 83.20           N  
ANISOU 5903  N   ALA D  38    18939   6826   5849  -2424  -4636  -1607       N  
ATOM   5904  CA  ALA D  38      63.351 -32.180 -17.607  1.00 82.46           C  
ANISOU 5904  CA  ALA D  38    19213   6899   5217  -2110  -4065  -1604       C  
ATOM   5905  C   ALA D  38      63.407 -30.683 -17.235  1.00 84.08           C  
ANISOU 5905  C   ALA D  38    18810   7437   5699  -2039  -3794  -1289       C  
ATOM   5906  O   ALA D  38      64.462 -30.232 -16.785  1.00 83.83           O  
ANISOU 5906  O   ALA D  38    18570   7598   5684  -1805  -3090  -1262       O  
ATOM   5907  CB  ALA D  38      63.131 -32.325 -19.106  1.00 83.36           C  
ANISOU 5907  CB  ALA D  38    20365   6793   4516  -2087  -4413  -1735       C  
ATOM   5908  N   ASN D  39      62.301 -29.926 -17.440  1.00 78.18           N  
ANISOU 5908  N   ASN D  39    17782   6725   5199  -2233  -4375  -1052       N  
ATOM   5909  CA  ASN D  39      62.220 -28.475 -17.193  1.00 76.72           C  
ANISOU 5909  CA  ASN D  39    17099   6788   5264  -2163  -4222   -755       C  
ATOM   5910  C   ASN D  39      62.189 -28.033 -15.717  1.00 75.08           C  
ANISOU 5910  C   ASN D  39    15944   6786   5797  -2145  -3880   -623       C  
ATOM   5911  O   ASN D  39      62.514 -26.879 -15.438  1.00 74.55           O  
ANISOU 5911  O   ASN D  39    15557   6904   5867  -2018  -3574   -440       O  
ATOM   5912  CB  ASN D  39      61.016 -27.871 -17.925  1.00 79.87           C  
ANISOU 5912  CB  ASN D  39    17583   7104   5658  -2334  -5007   -552       C  
ATOM   5913  CG  ASN D  39      61.072 -28.030 -19.422  1.00115.90           C  
ANISOU 5913  CG  ASN D  39    23179  11465   9395  -2331  -5366   -643       C  
ATOM   5914  OD1 ASN D  39      61.897 -27.413 -20.110  1.00111.19           O  
ANISOU 5914  OD1 ASN D  39    23094  10932   8222  -2134  -4950   -609       O  
ATOM   5915  ND2 ASN D  39      60.188 -28.863 -19.959  1.00112.43           N  
ANISOU 5915  ND2 ASN D  39    23097  10753   8869  -2563  -6153   -751       N  
ATOM   5916  N   TYR D  40      61.767 -28.913 -14.794  1.00 67.48           N  
ANISOU 5916  N   TYR D  40    14595   5763   5281  -2276  -3948   -707       N  
ATOM   5917  CA  TYR D  40      61.641 -28.604 -13.361  1.00 65.26           C  
ANISOU 5917  CA  TYR D  40    13519   5641   5636  -2263  -3636   -593       C  
ATOM   5918  C   TYR D  40      62.957 -28.630 -12.590  1.00 63.96           C  
ANISOU 5918  C   TYR D  40    13272   5592   5437  -2042  -2926   -695       C  
ATOM   5919  O   TYR D  40      63.902 -29.321 -12.974  1.00 63.19           O  
ANISOU 5919  O   TYR D  40    13638   5413   4957  -1927  -2668   -895       O  
ATOM   5920  CB  TYR D  40      60.647 -29.575 -12.672  1.00 66.57           C  
ANISOU 5920  CB  TYR D  40    13341   5676   6277  -2514  -3965   -602       C  
ATOM   5921  CG  TYR D  40      59.189 -29.310 -12.977  1.00 69.58           C  
ANISOU 5921  CG  TYR D  40    13403   5998   7036  -2745  -4626   -401       C  
ATOM   5922  CD1 TYR D  40      58.611 -29.756 -14.167  1.00 72.28           C  
ANISOU 5922  CD1 TYR D  40    14233   6118   7113  -2934  -5323   -448       C  
ATOM   5923  CD2 TYR D  40      58.373 -28.650 -12.063  1.00 70.32           C  
ANISOU 5923  CD2 TYR D  40    12714   6233   7773  -2764  -4572   -165       C  
ATOM   5924  CE1 TYR D  40      57.267 -29.521 -14.453  1.00 73.85           C  
ANISOU 5924  CE1 TYR D  40    14077   6242   7740  -3157  -6012   -240       C  
ATOM   5925  CE2 TYR D  40      57.025 -28.409 -12.337  1.00 71.59           C  
ANISOU 5925  CE2 TYR D  40    12484   6336   8382  -2951  -5165     44       C  
ATOM   5926  CZ  TYR D  40      56.476 -28.846 -13.536  1.00 82.22           C  
ANISOU 5926  CZ  TYR D  40    14255   7464   9519  -3159  -5916     18       C  
ATOM   5927  OH  TYR D  40      55.151 -28.616 -13.823  1.00 85.90           O  
ANISOU 5927  OH  TYR D  40    14286   7854  10497  -3353  -6581    246       O  
ATOM   5928  N   ALA D  41      62.983 -27.895 -11.467  1.00 56.83           N  
ANISOU 5928  N   ALA D  41    11773   4852   4969  -1974  -2636   -560       N  
ATOM   5929  CA  ALA D  41      64.064 -27.878 -10.496  1.00 54.76           C  
ANISOU 5929  CA  ALA D  41    11327   4679   4802  -1804  -2083   -624       C  
ATOM   5930  C   ALA D  41      63.557 -28.767  -9.353  1.00 55.79           C  
ANISOU 5930  C   ALA D  41    11143   4744   5311  -1918  -2105   -658       C  
ATOM   5931  O   ALA D  41      62.419 -28.594  -8.901  1.00 55.66           O  
ANISOU 5931  O   ALA D  41    10738   4742   5670  -2059  -2329   -514       O  
ATOM   5932  CB  ALA D  41      64.301 -26.461  -9.989  1.00 55.18           C  
ANISOU 5932  CB  ALA D  41    11015   4898   5053  -1680  -1840   -452       C  
ATOM   5933  N   ILE D  42      64.355 -29.748  -8.922  1.00 50.05           N  
ANISOU 5933  N   ILE D  42    10588   3925   4503  -1856  -1874   -827       N  
ATOM   5934  CA  ILE D  42      63.917 -30.635  -7.841  1.00 49.11           C  
ANISOU 5934  CA  ILE D  42    10246   3714   4700  -1974  -1884   -831       C  
ATOM   5935  C   ILE D  42      64.805 -30.453  -6.634  1.00 50.73           C  
ANISOU 5935  C   ILE D  42    10242   3996   5038  -1799  -1461   -833       C  
ATOM   5936  O   ILE D  42      66.023 -30.410  -6.763  1.00 49.83           O  
ANISOU 5936  O   ILE D  42    10295   3901   4736  -1603  -1200   -934       O  
ATOM   5937  CB  ILE D  42      63.733 -32.151  -8.243  1.00 52.01           C  
ANISOU 5937  CB  ILE D  42    10998   3817   4947  -2123  -2142   -995       C  
ATOM   5938  CG1 ILE D  42      63.066 -32.348  -9.643  1.00 52.18           C  
ANISOU 5938  CG1 ILE D  42    11412   3710   4706  -2275  -2632  -1048       C  
ATOM   5939  CG2 ILE D  42      62.978 -32.937  -7.160  1.00 52.46           C  
ANISOU 5939  CG2 ILE D  42    10761   3769   5404  -2328  -2214   -906       C  
ATOM   5940  CD1 ILE D  42      61.573 -31.943  -9.784  1.00 57.23           C  
ANISOU 5940  CD1 ILE D  42    11708   4366   5672  -2534  -3111   -842       C  
ATOM   5941  N   GLY D  43      64.181 -30.347  -5.474  1.00 46.47           N  
ANISOU 5941  N   GLY D  43     9343   3487   4826  -1869  -1400   -710       N  
ATOM   5942  CA  GLY D  43      64.881 -30.183  -4.213  1.00 46.17           C  
ANISOU 5942  CA  GLY D  43     9168   3486   4887  -1725  -1079   -702       C  
ATOM   5943  C   GLY D  43      64.402 -31.167  -3.173  1.00 49.41           C  
ANISOU 5943  C   GLY D  43     9528   3770   5476  -1848  -1056   -664       C  
ATOM   5944  O   GLY D  43      63.231 -31.548  -3.181  1.00 47.70           O  
ANISOU 5944  O   GLY D  43     9165   3501   5457  -2066  -1226   -559       O  
ATOM   5945  N   TRP D  44      65.319 -31.597  -2.295  1.00 46.02           N  
ANISOU 5945  N   TRP D  44     9215   3270   4999  -1720   -864   -725       N  
ATOM   5946  CA  TRP D  44      65.068 -32.494  -1.175  1.00 45.58           C  
ANISOU 5946  CA  TRP D  44     9196   3073   5050  -1802   -798   -668       C  
ATOM   5947  C   TRP D  44      65.093 -31.682   0.115  1.00 49.32           C  
ANISOU 5947  C   TRP D  44     9506   3642   5593  -1694   -556   -560       C  
ATOM   5948  O   TRP D  44      65.997 -30.871   0.334  1.00 48.32           O  
ANISOU 5948  O   TRP D  44     9385   3591   5383  -1498   -466   -614       O  
ATOM   5949  CB  TRP D  44      66.074 -33.652  -1.152  1.00 44.08           C  
ANISOU 5949  CB  TRP D  44     9344   2679   4724  -1714   -825   -816       C  
ATOM   5950  CG  TRP D  44      65.715 -34.739  -2.123  1.00 45.10           C  
ANISOU 5950  CG  TRP D  44     9719   2619   4796  -1866  -1066   -914       C  
ATOM   5951  CD1 TRP D  44      66.162 -34.877  -3.404  1.00 48.09           C  
ANISOU 5951  CD1 TRP D  44    10339   2964   4966  -1789  -1175  -1086       C  
ATOM   5952  CD2 TRP D  44      64.747 -35.780  -1.921  1.00 44.92           C  
ANISOU 5952  CD2 TRP D  44     9756   2392   4918  -2143  -1241   -838       C  
ATOM   5953  NE1 TRP D  44      65.545 -35.952  -4.013  1.00 47.41           N  
ANISOU 5953  NE1 TRP D  44    10521   2644   4850  -1986  -1452  -1157       N  
ATOM   5954  CE2 TRP D  44      64.677 -36.529  -3.120  1.00 48.67           C  
ANISOU 5954  CE2 TRP D  44    10542   2687   5262  -2225  -1521   -999       C  
ATOM   5955  CE3 TRP D  44      63.942 -36.166  -0.834  1.00 46.05           C  
ANISOU 5955  CE3 TRP D  44     9746   2467   5285  -2336  -1167   -637       C  
ATOM   5956  CZ2 TRP D  44      63.837 -37.635  -3.260  1.00 47.67           C  
ANISOU 5956  CZ2 TRP D  44    10559   2291   5261  -2520  -1803   -974       C  
ATOM   5957  CZ3 TRP D  44      63.115 -37.267  -0.975  1.00 47.18           C  
ANISOU 5957  CZ3 TRP D  44     9976   2367   5585  -2638  -1386   -575       C  
ATOM   5958  CH2 TRP D  44      63.059 -37.977  -2.180  1.00 47.88           C  
ANISOU 5958  CH2 TRP D  44    10354   2259   5581  -2741  -1737   -746       C  
ATOM   5959  N   PHE D  45      64.055 -31.866   0.933  1.00 46.64           N  
ANISOU 5959  N   PHE D  45     9027   3281   5414  -1831   -445   -399       N  
ATOM   5960  CA  PHE D  45      63.824 -31.199   2.216  1.00 46.42           C  
ANISOU 5960  CA  PHE D  45     8922   3308   5406  -1735   -165   -289       C  
ATOM   5961  C   PHE D  45      63.541 -32.254   3.283  1.00 52.43           C  
ANISOU 5961  C   PHE D  45     9858   3902   6160  -1844    -28   -179       C  
ATOM   5962  O   PHE D  45      62.970 -33.301   2.984  1.00 51.12           O  
ANISOU 5962  O   PHE D  45     9698   3608   6116  -2069   -135   -118       O  
ATOM   5963  CB  PHE D  45      62.631 -30.228   2.101  1.00 47.78           C  
ANISOU 5963  CB  PHE D  45     8715   3634   5804  -1765    -57   -153       C  
ATOM   5964  CG  PHE D  45      62.888 -29.101   1.128  1.00 49.61           C  
ANISOU 5964  CG  PHE D  45     8822   4004   6026  -1650   -196   -225       C  
ATOM   5965  CD1 PHE D  45      62.649 -29.265  -0.237  1.00 52.57           C  
ANISOU 5965  CD1 PHE D  45     9135   4400   6439  -1768   -487   -254       C  
ATOM   5966  CD2 PHE D  45      63.393 -27.882   1.568  1.00 50.90           C  
ANISOU 5966  CD2 PHE D  45     8993   4236   6109  -1433    -64   -261       C  
ATOM   5967  CE1 PHE D  45      62.937 -28.244  -1.139  1.00 52.58           C  
ANISOU 5967  CE1 PHE D  45     9094   4508   6377  -1665   -602   -291       C  
ATOM   5968  CE2 PHE D  45      63.684 -26.866   0.665  1.00 53.57           C  
ANISOU 5968  CE2 PHE D  45     9246   4666   6441  -1350   -192   -298       C  
ATOM   5969  CZ  PHE D  45      63.448 -27.051  -0.681  1.00 51.94           C  
ANISOU 5969  CZ  PHE D  45     8983   4497   6254  -1463   -439   -299       C  
ATOM   5970  N   ARG D  46      63.944 -31.983   4.521  1.00 50.49           N  
ANISOU 5970  N   ARG D  46     9808   3625   5753  -1697    180   -147       N  
ATOM   5971  CA  ARG D  46      63.713 -32.902   5.630  1.00 50.09           C  
ANISOU 5971  CA  ARG D  46    10007   3403   5623  -1782    345    -11       C  
ATOM   5972  C   ARG D  46      63.160 -32.151   6.834  1.00 56.26           C  
ANISOU 5972  C   ARG D  46    10821   4240   6313  -1681    730    119       C  
ATOM   5973  O   ARG D  46      63.495 -30.981   7.054  1.00 55.53           O  
ANISOU 5973  O   ARG D  46    10734   4251   6116  -1469    785     30       O  
ATOM   5974  CB  ARG D  46      64.986 -33.698   5.978  1.00 46.15           C  
ANISOU 5974  CB  ARG D  46     9919   2707   4910  -1683    143   -116       C  
ATOM   5975  CG  ARG D  46      66.077 -32.941   6.752  1.00 46.55           C  
ANISOU 5975  CG  ARG D  46    10200   2756   4732  -1419    107   -209       C  
ATOM   5976  CD  ARG D  46      67.276 -33.840   6.947  1.00 47.76           C  
ANISOU 5976  CD  ARG D  46    10662   2698   4787  -1329   -156   -286       C  
ATOM   5977  NE  ARG D  46      68.414 -33.179   7.580  1.00 51.03           N  
ANISOU 5977  NE  ARG D  46    11235   3086   5069  -1102   -313   -375       N  
ATOM   5978  CZ  ARG D  46      69.652 -33.668   7.579  1.00 62.48           C  
ANISOU 5978  CZ  ARG D  46    12812   4387   6539   -966   -598   -461       C  
ATOM   5979  NH1 ARG D  46      69.924 -34.806   6.951  1.00 46.59           N  
ANISOU 5979  NH1 ARG D  46    10829   2240   4635   -996   -710   -495       N  
ATOM   5980  NH2 ARG D  46      70.631 -33.013   8.191  1.00 48.30           N  
ANISOU 5980  NH2 ARG D  46    11106   2555   4691   -793   -795   -516       N  
ATOM   5981  N   GLN D  47      62.273 -32.809   7.575  1.00 55.01           N  
ANISOU 5981  N   GLN D  47    10699   3997   6205  -1837   1019    336       N  
ATOM   5982  CA  GLN D  47      61.702 -32.254   8.792  1.00 55.35           C  
ANISOU 5982  CA  GLN D  47    10854   4066   6112  -1727   1488    478       C  
ATOM   5983  C   GLN D  47      61.635 -33.313   9.885  1.00 61.22           C  
ANISOU 5983  C   GLN D  47    12018   4599   6646  -1832   1692    661       C  
ATOM   5984  O   GLN D  47      61.012 -34.368   9.700  1.00 60.25           O  
ANISOU 5984  O   GLN D  47    11771   4373   6749  -2115   1719    839       O  
ATOM   5985  CB  GLN D  47      60.348 -31.560   8.564  1.00 56.11           C  
ANISOU 5985  CB  GLN D  47    10412   4337   6569  -1770   1820    625       C  
ATOM   5986  CG  GLN D  47      59.848 -30.904   9.849  1.00 64.42           C  
ANISOU 5986  CG  GLN D  47    11624   5406   7447  -1581   2396    746       C  
ATOM   5987  CD  GLN D  47      58.517 -30.229   9.713  1.00 86.21           C  
ANISOU 5987  CD  GLN D  47    13801   8327  10626  -1563   2766    897       C  
ATOM   5988  OE1 GLN D  47      58.426 -28.993   9.700  1.00 79.82           O  
ANISOU 5988  OE1 GLN D  47    12868   7628   9833  -1308   2840    785       O  
ATOM   5989  NE2 GLN D  47      57.450 -31.027   9.645  1.00 77.58           N  
ANISOU 5989  NE2 GLN D  47    12320   7227   9930  -1834   2996   1171       N  
ATOM   5990  N   ALA D  48      62.317 -33.032  11.011  1.00 60.31           N  
ANISOU 5990  N   ALA D  48    12448   4384   6084  -1618   1779    621       N  
ATOM   5991  CA  ALA D  48      62.347 -33.894  12.196  1.00 61.37           C  
ANISOU 5991  CA  ALA D  48    13125   4296   5897  -1667   1970    804       C  
ATOM   5992  C   ALA D  48      61.274 -33.410  13.183  1.00 70.20           C  
ANISOU 5992  C   ALA D  48    14309   5470   6895  -1613   2648   1012       C  
ATOM   5993  O   ALA D  48      60.926 -32.224  13.148  1.00 70.27           O  
ANISOU 5993  O   ALA D  48    14095   5652   6952  -1424   2867    925       O  
ATOM   5994  CB  ALA D  48      63.722 -33.851  12.843  1.00 61.88           C  
ANISOU 5994  CB  ALA D  48    13791   4194   5526  -1451   1604    644       C  
ATOM   5995  N   PRO D  49      60.703 -34.286  14.046  1.00 70.83           N  
ANISOU 5995  N   PRO D  49    14686   5393   6832  -1763   3034   1300       N  
ATOM   5996  CA  PRO D  49      59.661 -33.811  14.977  1.00 71.69           C  
ANISOU 5996  CA  PRO D  49    14851   5564   6826  -1681   3796   1513       C  
ATOM   5997  C   PRO D  49      60.162 -32.725  15.919  1.00 78.36           C  
ANISOU 5997  C   PRO D  49    16289   6392   7093  -1296   3934   1336       C  
ATOM   5998  O   PRO D  49      61.157 -32.922  16.621  1.00 78.95           O  
ANISOU 5998  O   PRO D  49    17086   6265   6645  -1184   3634   1249       O  
ATOM   5999  CB  PRO D  49      59.236 -35.076  15.722  1.00 73.09           C  
ANISOU 5999  CB  PRO D  49    15339   5531   6903  -1938   4113   1865       C  
ATOM   6000  CG  PRO D  49      60.378 -36.012  15.566  1.00 77.55           C  
ANISOU 6000  CG  PRO D  49    16315   5862   7289  -2024   3456   1769       C  
ATOM   6001  CD  PRO D  49      60.960 -35.730  14.225  1.00 72.76           C  
ANISOU 6001  CD  PRO D  49    15248   5379   7019  -2001   2841   1461       C  
ATOM   6002  N   GLY D  50      59.500 -31.573  15.861  1.00 75.83           N  
ANISOU 6002  N   GLY D  50    15654   6254   6904  -1092   4310   1271       N  
ATOM   6003  CA  GLY D  50      59.821 -30.406  16.674  1.00 75.97           C  
ANISOU 6003  CA  GLY D  50    16213   6235   6419   -715   4467   1076       C  
ATOM   6004  C   GLY D  50      60.722 -29.385  16.003  1.00 79.19           C  
ANISOU 6004  C   GLY D  50    16508   6704   6878   -538   3885    727       C  
ATOM   6005  O   GLY D  50      60.984 -28.322  16.578  1.00 79.86           O  
ANISOU 6005  O   GLY D  50    17004   6730   6608   -239   3949    541       O  
ATOM   6006  N   LYS D  51      61.213 -29.701  14.791  1.00 73.41           N  
ANISOU 6006  N   LYS D  51    15262   6061   6568   -722   3327    637       N  
ATOM   6007  CA  LYS D  51      62.106 -28.814  14.037  1.00 71.76           C  
ANISOU 6007  CA  LYS D  51    14898   5912   6454   -598   2796    351       C  
ATOM   6008  C   LYS D  51      61.429 -28.253  12.773  1.00 71.54           C  
ANISOU 6008  C   LYS D  51    14059   6115   7006   -661   2790    340       C  
ATOM   6009  O   LYS D  51      60.416 -28.782  12.313  1.00 71.41           O  
ANISOU 6009  O   LYS D  51    13547   6202   7385   -861   3021    540       O  
ATOM   6010  CB  LYS D  51      63.428 -29.545  13.676  1.00 74.43           C  
ANISOU 6010  CB  LYS D  51    15449   6128   6703   -691   2117    230       C  
ATOM   6011  CG  LYS D  51      64.281 -30.048  14.862  1.00 86.22           C  
ANISOU 6011  CG  LYS D  51    17766   7359   7636   -596   1939    218       C  
ATOM   6012  CD  LYS D  51      64.804 -28.950  15.819  1.00102.22           C  
ANISOU 6012  CD  LYS D  51    20354   9268   9216   -311   1904     40       C  
ATOM   6013  CE  LYS D  51      65.874 -28.035  15.248  1.00121.28           C  
ANISOU 6013  CE  LYS D  51    22674  11664  11744   -222   1287   -216       C  
ATOM   6014  NZ  LYS D  51      65.302 -26.776  14.690  1.00130.56           N  
ANISOU 6014  NZ  LYS D  51    23320  13029  13260   -153   1418   -322       N  
ATOM   6015  N   GLU D  52      61.995 -27.182  12.213  1.00 65.37           N  
ANISOU 6015  N   GLU D  52    13166   5388   6285   -507   2487    125       N  
ATOM   6016  CA  GLU D  52      61.500 -26.557  10.985  1.00 63.30           C  
ANISOU 6016  CA  GLU D  52    12236   5313   6504   -542   2392    107       C  
ATOM   6017  C   GLU D  52      62.008 -27.365   9.801  1.00 61.97           C  
ANISOU 6017  C   GLU D  52    11781   5196   6570   -791   1914     88       C  
ATOM   6018  O   GLU D  52      62.942 -28.152   9.957  1.00 60.33           O  
ANISOU 6018  O   GLU D  52    11896   4871   6156   -864   1627     34       O  
ATOM   6019  CB  GLU D  52      61.985 -25.095  10.885  1.00 64.54           C  
ANISOU 6019  CB  GLU D  52    12472   5457   6592   -291   2235    -99       C  
ATOM   6020  N   ARG D  53      61.407 -27.163   8.619  1.00 56.91           N  
ANISOU 6020  N   ARG D  53    10573   4708   6344   -896   1812    127       N  
ATOM   6021  CA  ARG D  53      61.803 -27.843   7.390  1.00 56.03           C  
ANISOU 6021  CA  ARG D  53    10244   4634   6410  -1106   1385     88       C  
ATOM   6022  C   ARG D  53      63.180 -27.343   6.945  1.00 56.91           C  
ANISOU 6022  C   ARG D  53    10547   4725   6353  -1000    998   -123       C  
ATOM   6023  O   ARG D  53      63.398 -26.141   6.833  1.00 56.26           O  
ANISOU 6023  O   ARG D  53    10424   4683   6269   -836    962   -210       O  
ATOM   6024  CB  ARG D  53      60.742 -27.649   6.303  1.00 57.26           C  
ANISOU 6024  CB  ARG D  53     9822   4931   7003  -1232   1346    192       C  
ATOM   6025  CG  ARG D  53      60.827 -28.651   5.150  1.00 64.21           C  
ANISOU 6025  CG  ARG D  53    10559   5804   8035  -1497    967    190       C  
ATOM   6026  CD  ARG D  53      60.039 -28.166   3.940  1.00 74.60           C  
ANISOU 6026  CD  ARG D  53    11412   7241   9692  -1571    760    236       C  
ATOM   6027  NE  ARG D  53      60.427 -26.810   3.529  1.00 78.42           N  
ANISOU 6027  NE  ARG D  53    11873   7808  10114  -1348    673    126       N  
ATOM   6028  CZ  ARG D  53      59.577 -25.802   3.354  1.00 91.04           C  
ANISOU 6028  CZ  ARG D  53    13136   9490  11966  -1230    765    209       C  
ATOM   6029  NH1 ARG D  53      58.272 -25.989   3.515  1.00 74.03           N  
ANISOU 6029  NH1 ARG D  53    10566   7371  10192  -1304    956    408       N  
ATOM   6030  NH2 ARG D  53      60.024 -24.603   2.998  1.00 78.62           N  
ANISOU 6030  NH2 ARG D  53    11611   7945  10316  -1039    662    114       N  
ATOM   6031  N   GLU D  54      64.110 -28.282   6.744  1.00 51.78           N  
ANISOU 6031  N   GLU D  54    10099   3985   5592  -1087    731   -189       N  
ATOM   6032  CA  GLU D  54      65.505 -28.045   6.385  1.00 50.12           C  
ANISOU 6032  CA  GLU D  54    10023   3735   5284   -999    401   -353       C  
ATOM   6033  C   GLU D  54      65.785 -28.579   4.976  1.00 52.10           C  
ANISOU 6033  C   GLU D  54    10049   4049   5698  -1120    172   -400       C  
ATOM   6034  O   GLU D  54      65.593 -29.771   4.709  1.00 52.96           O  
ANISOU 6034  O   GLU D  54    10188   4092   5843  -1266    121   -367       O  
ATOM   6035  CB  GLU D  54      66.423 -28.745   7.430  1.00 51.19           C  
ANISOU 6035  CB  GLU D  54    10603   3679   5169   -943    295   -383       C  
ATOM   6036  CG  GLU D  54      67.914 -28.480   7.281  1.00 58.67           C  
ANISOU 6036  CG  GLU D  54    11640   4558   6092   -835    -49   -522       C  
ATOM   6037  CD  GLU D  54      68.855 -29.649   7.520  1.00 76.91           C  
ANISOU 6037  CD  GLU D  54    14148   6710   8366   -839   -279   -543       C  
ATOM   6038  OE1 GLU D  54      68.880 -30.187   8.651  1.00 66.74           O  
ANISOU 6038  OE1 GLU D  54    13247   5249   6862   -800   -311   -493       O  
ATOM   6039  OE2 GLU D  54      69.587 -30.015   6.572  1.00 75.77           O  
ANISOU 6039  OE2 GLU D  54    13803   6593   8391   -856   -422   -607       O  
ATOM   6040  N   GLY D  55      66.251 -27.699   4.101  1.00 45.97           N  
ANISOU 6040  N   GLY D  55     9109   3369   4991  -1057     42   -476       N  
ATOM   6041  CA  GLY D  55      66.653 -28.061   2.746  1.00 43.99           C  
ANISOU 6041  CA  GLY D  55     8740   3168   4804  -1126   -133   -535       C  
ATOM   6042  C   GLY D  55      67.933 -28.860   2.799  1.00 44.03           C  
ANISOU 6042  C   GLY D  55     8938   3058   4735  -1068   -262   -633       C  
ATOM   6043  O   GLY D  55      68.852 -28.529   3.546  1.00 43.07           O  
ANISOU 6043  O   GLY D  55     8933   2862   4570   -945   -319   -671       O  
ATOM   6044  N   VAL D  56      68.004 -29.904   2.016  1.00 40.42           N  
ANISOU 6044  N   VAL D  56     8522   2554   4280  -1145   -337   -677       N  
ATOM   6045  CA  VAL D  56      69.134 -30.816   2.041  1.00 40.68           C  
ANISOU 6045  CA  VAL D  56     8726   2446   4284  -1053   -432   -770       C  
ATOM   6046  C   VAL D  56      69.950 -30.742   0.745  1.00 44.93           C  
ANISOU 6046  C   VAL D  56     9190   3039   4840   -972   -449   -872       C  
ATOM   6047  O   VAL D  56      71.166 -30.566   0.790  1.00 43.38           O  
ANISOU 6047  O   VAL D  56     8951   2818   4715   -817   -457   -919       O  
ATOM   6048  CB  VAL D  56      68.564 -32.229   2.391  1.00 45.03           C  
ANISOU 6048  CB  VAL D  56     9481   2825   4804  -1177   -462   -739       C  
ATOM   6049  CG1 VAL D  56      69.374 -33.379   1.828  1.00 44.68           C  
ANISOU 6049  CG1 VAL D  56     9607   2616   4752  -1108   -572   -859       C  
ATOM   6050  CG2 VAL D  56      68.397 -32.373   3.889  1.00 45.57           C  
ANISOU 6050  CG2 VAL D  56     9724   2785   4804  -1170   -409   -636       C  
ATOM   6051  N   SER D  57      69.276 -30.830  -0.399  1.00 43.91           N  
ANISOU 6051  N   SER D  57     9049   2979   4655  -1077   -453   -890       N  
ATOM   6052  CA  SER D  57      69.929 -30.869  -1.706  1.00 45.16           C  
ANISOU 6052  CA  SER D  57     9254   3172   4734   -999   -418   -985       C  
ATOM   6053  C   SER D  57      68.998 -30.396  -2.810  1.00 48.67           C  
ANISOU 6053  C   SER D  57     9691   3727   5075  -1131   -475   -952       C  
ATOM   6054  O   SER D  57      67.791 -30.541  -2.691  1.00 48.73           O  
ANISOU 6054  O   SER D  57     9660   3731   5122  -1303   -598   -884       O  
ATOM   6055  CB  SER D  57      70.416 -32.286  -2.003  1.00 49.85           C  
ANISOU 6055  CB  SER D  57    10099   3575   5267   -930   -442  -1117       C  
ATOM   6056  OG  SER D  57      71.370 -32.230  -3.046  1.00 62.95           O  
ANISOU 6056  OG  SER D  57    11804   5261   6854   -765   -297  -1213       O  
ATOM   6057  N   CYS D  58      69.546 -29.825  -3.872  1.00 45.40           N  
ANISOU 6057  N   CYS D  58     9305   3399   4547  -1054   -392   -977       N  
ATOM   6058  CA  CYS D  58      68.726 -29.288  -4.956  1.00 46.01           C  
ANISOU 6058  CA  CYS D  58     9436   3563   4483  -1164   -498   -926       C  
ATOM   6059  C   CYS D  58      69.414 -29.534  -6.275  1.00 47.41           C  
ANISOU 6059  C   CYS D  58     9898   3725   4391  -1068   -393  -1023       C  
ATOM   6060  O   CYS D  58      70.641 -29.538  -6.343  1.00 45.24           O  
ANISOU 6060  O   CYS D  58     9612   3450   4128   -890   -138  -1067       O  
ATOM   6061  CB  CYS D  58      68.458 -27.797  -4.723  1.00 47.74           C  
ANISOU 6061  CB  CYS D  58     9391   3925   4822  -1170   -476   -774       C  
ATOM   6062  SG  CYS D  58      67.299 -27.030  -5.894  1.00 52.58           S  
ANISOU 6062  SG  CYS D  58    10030   4621   5327  -1294   -692   -661       S  
ATOM   6063  N   ILE D  59      68.618 -29.746  -7.322  1.00 46.15           N  
ANISOU 6063  N   ILE D  59    10002   3536   3995  -1181   -591  -1047       N  
ATOM   6064  CA  ILE D  59      69.084 -29.962  -8.693  1.00 46.56           C  
ANISOU 6064  CA  ILE D  59    10465   3553   3672  -1094   -501  -1142       C  
ATOM   6065  C   ILE D  59      68.285 -29.078  -9.650  1.00 53.06           C  
ANISOU 6065  C   ILE D  59    11404   4458   4298  -1213   -713  -1021       C  
ATOM   6066  O   ILE D  59      67.067 -28.957  -9.522  1.00 52.57           O  
ANISOU 6066  O   ILE D  59    11226   4390   4360  -1399  -1075   -940       O  
ATOM   6067  CB  ILE D  59      69.153 -31.459  -9.112  1.00 48.84           C  
ANISOU 6067  CB  ILE D  59    11188   3618   3752  -1061   -569  -1365       C  
ATOM   6068  CG1 ILE D  59      70.001 -31.635 -10.404  1.00 48.75           C  
ANISOU 6068  CG1 ILE D  59    11635   3567   3322   -861   -293  -1490       C  
ATOM   6069  CG2 ILE D  59      67.758 -32.126  -9.199  1.00 49.17           C  
ANISOU 6069  CG2 ILE D  59    11381   3517   3785  -1326  -1050  -1389       C  
ATOM   6070  CD1 ILE D  59      70.387 -33.119 -10.818  1.00 57.86           C  
ANISOU 6070  CD1 ILE D  59    13288   4455   4242   -723   -253  -1759       C  
ATOM   6071  N   SER D  60      68.991 -28.403 -10.552  1.00 52.23           N  
ANISOU 6071  N   SER D  60    11487   4425   3932  -1100   -474   -974       N  
ATOM   6072  CA  SER D  60      68.377 -27.501 -11.521  1.00 53.01           C  
ANISOU 6072  CA  SER D  60    11772   4580   3791  -1186   -667   -831       C  
ATOM   6073  C   SER D  60      68.065 -28.245 -12.795  1.00 60.66           C  
ANISOU 6073  C   SER D  60    13388   5408   4249  -1209   -860   -964       C  
ATOM   6074  O   SER D  60      68.601 -29.339 -13.015  1.00 60.76           O  
ANISOU 6074  O   SER D  60    13726   5291   4067  -1101   -702  -1177       O  
ATOM   6075  CB  SER D  60      69.299 -26.320 -11.804  1.00 54.46           C  
ANISOU 6075  CB  SER D  60    11854   4891   3950  -1078   -295   -666       C  
ATOM   6076  OG  SER D  60      70.506 -26.763 -12.398  1.00 62.48           O  
ANISOU 6076  OG  SER D  60    13128   5886   4725   -898    160   -757       O  
ATOM   6077  N   SER D  61      67.217 -27.637 -13.655  1.00 59.81           N  
ANISOU 6077  N   SER D  61    13519   5299   3909  -1329  -1223   -843       N  
ATOM   6078  CA  SER D  61      66.830 -28.176 -14.963  1.00 60.31           C  
ANISOU 6078  CA  SER D  61    14305   5203   3409  -1370  -1516   -950       C  
ATOM   6079  C   SER D  61      68.055 -28.406 -15.836  1.00 66.54           C  
ANISOU 6079  C   SER D  61    15635   5966   3682  -1137   -979  -1060       C  
ATOM   6080  O   SER D  61      68.101 -29.388 -16.575  1.00 67.52           O  
ANISOU 6080  O   SER D  61    16395   5902   3359  -1084  -1044  -1283       O  
ATOM   6081  CB  SER D  61      65.857 -27.237 -15.663  1.00 64.38           C  
ANISOU 6081  CB  SER D  61    14929   5732   3801  -1512  -1997   -741       C  
ATOM   6082  OG  SER D  61      66.369 -25.914 -15.730  1.00 77.15           O  
ANISOU 6082  OG  SER D  61    16352   7508   5452  -1426  -1691   -507       O  
ATOM   6083  N   GLY D  62      69.046 -27.521 -15.705  1.00 64.06           N  
ANISOU 6083  N   GLY D  62    15053   5819   3467   -997   -435   -904       N  
ATOM   6084  CA  GLY D  62      70.311 -27.595 -16.431  1.00 64.33           C  
ANISOU 6084  CA  GLY D  62    15437   5866   3140   -762    214   -941       C  
ATOM   6085  C   GLY D  62      71.260 -28.651 -15.891  1.00 68.60           C  
ANISOU 6085  C   GLY D  62    15856   6348   3860   -557    624  -1164       C  
ATOM   6086  O   GLY D  62      72.317 -28.886 -16.480  1.00 69.73           O  
ANISOU 6086  O   GLY D  62    16279   6476   3741   -318   1198  -1228       O  
ATOM   6087  N   GLY D  63      70.893 -29.274 -14.771  1.00 63.16           N  
ANISOU 6087  N   GLY D  63    14750   5617   3630   -633    357  -1263       N  
ATOM   6088  CA  GLY D  63      71.678 -30.331 -14.147  1.00 62.43           C  
ANISOU 6088  CA  GLY D  63    14533   5429   3758   -449    628  -1460       C  
ATOM   6089  C   GLY D  63      72.519 -29.950 -12.944  1.00 64.71           C  
ANISOU 6089  C   GLY D  63    14100   5847   4641   -371    914  -1348       C  
ATOM   6090  O   GLY D  63      72.927 -30.846 -12.203  1.00 65.15           O  
ANISOU 6090  O   GLY D  63    14000   5800   4951   -252    983  -1489       O  
ATOM   6091  N   SER D  64      72.808 -28.635 -12.740  1.00 58.59           N  
ANISOU 6091  N   SER D  64    12916   5256   4089   -437   1039  -1094       N  
ATOM   6092  CA  SER D  64      73.639 -28.164 -11.619  1.00 56.66           C  
ANISOU 6092  CA  SER D  64    12026   5100   4403   -390   1233   -982       C  
ATOM   6093  C   SER D  64      73.036 -28.513 -10.250  1.00 54.12           C  
ANISOU 6093  C   SER D  64    11379   4733   4451   -501    843  -1034       C  
ATOM   6094  O   SER D  64      71.821 -28.450 -10.067  1.00 51.81           O  
ANISOU 6094  O   SER D  64    11142   4431   4113   -690    435  -1022       O  
ATOM   6095  CB  SER D  64      73.982 -26.680 -11.744  1.00 60.57           C  
ANISOU 6095  CB  SER D  64    12239   5742   5034   -467   1395   -708       C  
ATOM   6096  OG  SER D  64      72.871 -25.845 -11.474  1.00 74.07           O  
ANISOU 6096  OG  SER D  64    13878   7494   6772   -679    966   -588       O  
ATOM   6097  N   THR D  65      73.906 -28.935  -9.316  1.00 48.69           N  
ANISOU 6097  N   THR D  65    10369   4002   4128   -368    984  -1082       N  
ATOM   6098  CA  THR D  65      73.559 -29.454  -7.984  1.00 47.55           C  
ANISOU 6098  CA  THR D  65    10010   3779   4279   -425    692  -1136       C  
ATOM   6099  C   THR D  65      74.085 -28.622  -6.806  1.00 49.94           C  
ANISOU 6099  C   THR D  65     9822   4145   5008   -442    668   -996       C  
ATOM   6100  O   THR D  65      75.234 -28.161  -6.821  1.00 50.23           O  
ANISOU 6100  O   THR D  65     9594   4217   5272   -327    926   -917       O  
ATOM   6101  CB  THR D  65      74.100 -30.899  -7.844  1.00 52.84           C  
ANISOU 6101  CB  THR D  65    10849   4264   4965   -235    775  -1335       C  
ATOM   6102  OG1 THR D  65      75.529 -30.858  -7.846  1.00 55.17           O  
ANISOU 6102  OG1 THR D  65    10894   4569   5499      7   1155  -1312       O  
ATOM   6103  CG2 THR D  65      73.595 -31.854  -8.947  1.00 47.05           C  
ANISOU 6103  CG2 THR D  65    10698   3391   3788   -212    743  -1523       C  
ATOM   6104  N   VAL D  66      73.252 -28.474  -5.768  1.00 43.71           N  
ANISOU 6104  N   VAL D  66     8926   3345   4336   -584    360   -966       N  
ATOM   6105  CA  VAL D  66      73.617 -27.763  -4.538  1.00 42.46           C  
ANISOU 6105  CA  VAL D  66     8439   3194   4500   -599    267   -873       C  
ATOM   6106  C   VAL D  66      73.298 -28.642  -3.319  1.00 44.84           C  
ANISOU 6106  C   VAL D  66     8783   3368   4887   -602     59   -948       C  
ATOM   6107  O   VAL D  66      72.373 -29.458  -3.355  1.00 43.09           O  
ANISOU 6107  O   VAL D  66     8779   3088   4505   -682    -55  -1015       O  
ATOM   6108  CB  VAL D  66      73.084 -26.293  -4.403  1.00 45.44           C  
ANISOU 6108  CB  VAL D  66     8671   3669   4924   -729    177   -722       C  
ATOM   6109  CG1 VAL D  66      73.881 -25.331  -5.279  1.00 44.94           C  
ANISOU 6109  CG1 VAL D  66     8495   3682   4899   -713    400   -596       C  
ATOM   6110  CG2 VAL D  66      71.597 -26.187  -4.711  1.00 44.84           C  
ANISOU 6110  CG2 VAL D  66     8752   3637   4650   -865      4   -707       C  
ATOM   6111  N   TYR D  67      74.103 -28.486  -2.256  1.00 41.91           N  
ANISOU 6111  N   TYR D  67     8222   2930   4774   -528    -12   -920       N  
ATOM   6112  CA  TYR D  67      74.009 -29.248  -1.013  1.00 40.65           C  
ANISOU 6112  CA  TYR D  67     8153   2625   4669   -509   -208   -960       C  
ATOM   6113  C   TYR D  67      74.104 -28.354   0.189  1.00 42.93           C  
ANISOU 6113  C   TYR D  67     8337   2890   5085   -544   -380   -883       C  
ATOM   6114  O   TYR D  67      74.833 -27.362   0.157  1.00 43.28           O  
ANISOU 6114  O   TYR D  67     8162   2967   5315   -528   -384   -819       O  
ATOM   6115  CB  TYR D  67      75.151 -30.290  -0.942  1.00 41.75           C  
ANISOU 6115  CB  TYR D  67     8280   2616   4966   -313   -184  -1036       C  
ATOM   6116  CG  TYR D  67      75.116 -31.300  -2.061  1.00 41.93           C  
ANISOU 6116  CG  TYR D  67     8505   2599   4826   -229     -3  -1157       C  
ATOM   6117  CD1 TYR D  67      74.384 -32.476  -1.941  1.00 43.78           C  
ANISOU 6117  CD1 TYR D  67     9056   2685   4893   -274   -117  -1248       C  
ATOM   6118  CD2 TYR D  67      75.792 -31.070  -3.255  1.00 42.55           C  
ANISOU 6118  CD2 TYR D  67     8509   2760   4899   -111    295  -1176       C  
ATOM   6119  CE1 TYR D  67      74.309 -33.393  -2.995  1.00 44.20           C  
ANISOU 6119  CE1 TYR D  67     9382   2649   4762   -203     -2  -1390       C  
ATOM   6120  CE2 TYR D  67      75.731 -31.982  -4.311  1.00 42.84           C  
ANISOU 6120  CE2 TYR D  67     8846   2728   4703     -7    474  -1317       C  
ATOM   6121  CZ  TYR D  67      74.983 -33.139  -4.177  1.00 48.95           C  
ANISOU 6121  CZ  TYR D  67     9970   3330   5299    -53    292  -1440       C  
ATOM   6122  OH  TYR D  67      74.938 -34.043  -5.212  1.00 52.15           O  
ANISOU 6122  OH  TYR D  67    10746   3614   5454     51    419  -1608       O  
ATOM   6123  N   SER D  68      73.380 -28.708   1.264  1.00 39.07           N  
ANISOU 6123  N   SER D  68     8041   2318   4487   -598   -516   -881       N  
ATOM   6124  CA  SER D  68      73.463 -27.978   2.518  1.00 39.38           C  
ANISOU 6124  CA  SER D  68     8120   2287   4555   -598   -682   -838       C  
ATOM   6125  C   SER D  68      74.777 -28.388   3.194  1.00 44.59           C  
ANISOU 6125  C   SER D  68     8753   2781   5408   -471   -897   -852       C  
ATOM   6126  O   SER D  68      75.287 -29.478   2.935  1.00 44.13           O  
ANISOU 6126  O   SER D  68     8702   2644   5422   -375   -894   -892       O  
ATOM   6127  CB  SER D  68      72.256 -28.257   3.412  1.00 43.27           C  
ANISOU 6127  CB  SER D  68     8867   2741   4831   -673   -671   -814       C  
ATOM   6128  OG  SER D  68      72.223 -29.585   3.908  1.00 54.23           O  
ANISOU 6128  OG  SER D  68    10474   3987   6145   -660   -726   -825       O  
ATOM   6129  N   GLU D  69      75.343 -27.501   4.010  1.00 42.50           N  
ANISOU 6129  N   GLU D  69     8458   2437   5254   -462  -1120   -820       N  
ATOM   6130  CA  GLU D  69      76.608 -27.728   4.701  1.00 43.39           C  
ANISOU 6130  CA  GLU D  69     8504   2370   5613   -362  -1435   -810       C  
ATOM   6131  C   GLU D  69      76.642 -29.026   5.526  1.00 49.95           C  
ANISOU 6131  C   GLU D  69     9633   3021   6324   -275  -1605   -828       C  
ATOM   6132  O   GLU D  69      77.693 -29.652   5.634  1.00 50.53           O  
ANISOU 6132  O   GLU D  69     9576   2964   6660   -144  -1795   -821       O  
ATOM   6133  CB  GLU D  69      76.956 -26.512   5.579  1.00 44.47           C  
ANISOU 6133  CB  GLU D  69     8684   2401   5810   -413  -1736   -784       C  
ATOM   6134  CG  GLU D  69      77.344 -25.263   4.798  1.00 52.98           C  
ANISOU 6134  CG  GLU D  69     9417   3577   7137   -497  -1656   -733       C  
ATOM   6135  CD  GLU D  69      78.691 -25.364   4.116  1.00 71.40           C  
ANISOU 6135  CD  GLU D  69    11280   5899   9951   -455  -1689   -661       C  
ATOM   6136  OE1 GLU D  69      78.714 -25.701   2.912  1.00 47.41           O  
ANISOU 6136  OE1 GLU D  69     8014   3018   6983   -417  -1322   -642       O  
ATOM   6137  OE2 GLU D  69      79.723 -25.132   4.786  1.00 75.44           O  
ANISOU 6137  OE2 GLU D  69    11659   6229  10776   -454  -2081   -620       O  
ATOM   6138  N   SER D  70      75.490 -29.427   6.084  1.00 47.90           N  
ANISOU 6138  N   SER D  70     9749   2745   5705   -343  -1518   -827       N  
ATOM   6139  CA  SER D  70      75.305 -30.623   6.910  1.00 49.02           C  
ANISOU 6139  CA  SER D  70    10256   2702   5669   -304  -1634   -805       C  
ATOM   6140  C   SER D  70      75.357 -31.939   6.130  1.00 56.94           C  
ANISOU 6140  C   SER D  70    11210   3670   6755   -254  -1509   -834       C  
ATOM   6141  O   SER D  70      75.540 -33.002   6.731  1.00 59.60           O  
ANISOU 6141  O   SER D  70    11805   3796   7045   -188  -1670   -807       O  
ATOM   6142  CB  SER D  70      73.972 -30.532   7.641  1.00 52.76           C  
ANISOU 6142  CB  SER D  70    11090   3190   5765   -419  -1463   -758       C  
ATOM   6143  OG  SER D  70      72.917 -30.184   6.757  1.00 60.61           O  
ANISOU 6143  OG  SER D  70    11901   4399   6730   -536  -1122   -762       O  
ATOM   6144  N   VAL D  71      75.157 -31.896   4.807  1.00 52.79           N  
ANISOU 6144  N   VAL D  71    10430   3314   6313   -281  -1239   -892       N  
ATOM   6145  CA  VAL D  71      75.124 -33.119   4.001  1.00 51.82           C  
ANISOU 6145  CA  VAL D  71    10355   3125   6210   -228  -1119   -958       C  
ATOM   6146  C   VAL D  71      76.182 -33.133   2.887  1.00 58.41           C  
ANISOU 6146  C   VAL D  71    10871   4007   7313    -54   -998  -1033       C  
ATOM   6147  O   VAL D  71      76.146 -34.027   2.039  1.00 57.24           O  
ANISOU 6147  O   VAL D  71    10803   3809   7139     16   -845  -1124       O  
ATOM   6148  CB  VAL D  71      73.702 -33.412   3.464  1.00 54.22           C  
ANISOU 6148  CB  VAL D  71    10807   3513   6279   -426   -917   -964       C  
ATOM   6149  CG1 VAL D  71      72.686 -33.511   4.606  1.00 53.74           C  
ANISOU 6149  CG1 VAL D  71    11010   3395   6012   -580   -944   -854       C  
ATOM   6150  CG2 VAL D  71      73.264 -32.382   2.417  1.00 53.41           C  
ANISOU 6150  CG2 VAL D  71    10469   3662   6163   -511   -722   -985       C  
ATOM   6151  N   LYS D  72      77.141 -32.169   2.892  1.00 57.61           N  
ANISOU 6151  N   LYS D  72    10432   3978   7480     16  -1051   -990       N  
ATOM   6152  CA  LYS D  72      78.203 -32.164   1.874  1.00 58.58           C  
ANISOU 6152  CA  LYS D  72    10201   4149   7908    189   -851  -1018       C  
ATOM   6153  C   LYS D  72      79.156 -33.353   2.105  1.00 64.67           C  
ANISOU 6153  C   LYS D  72    10944   4688   8939    449   -965  -1054       C  
ATOM   6154  O   LYS D  72      79.286 -33.833   3.240  1.00 64.89           O  
ANISOU 6154  O   LYS D  72    11144   4515   8994    483  -1322  -1014       O  
ATOM   6155  CB  LYS D  72      78.954 -30.817   1.810  1.00 60.75           C  
ANISOU 6155  CB  LYS D  72    10068   4541   8471    152   -865   -920       C  
ATOM   6156  CG  LYS D  72      79.872 -30.543   3.007  1.00 78.58           C  
ANISOU 6156  CG  LYS D  72    12189   6632  11036    190  -1307   -839       C  
ATOM   6157  CD  LYS D  72      80.401 -29.111   3.027  1.00 85.57           C  
ANISOU 6157  CD  LYS D  72    12697   7592  12225     89  -1379   -735       C  
ATOM   6158  CE  LYS D  72      81.254 -28.865   4.249  1.00 94.48           C  
ANISOU 6158  CE  LYS D  72    13744   8505  13651    103  -1927   -668       C  
ATOM   6159  NZ  LYS D  72      81.514 -27.418   4.462  1.00107.17           N  
ANISOU 6159  NZ  LYS D  72    15022  10131  15568    -45  -2071   -568       N  
ATOM   6160  N   ASP D  73      79.797 -33.841   1.030  1.00 61.99           N  
ANISOU 6160  N   ASP D  73    10435   4357   8762    654   -649  -1128       N  
ATOM   6161  CA  ASP D  73      80.744 -34.983   1.054  1.00 62.17           C  
ANISOU 6161  CA  ASP D  73    10389   4149   9082    973   -670  -1180       C  
ATOM   6162  C   ASP D  73      80.095 -36.326   1.440  1.00 63.21           C  
ANISOU 6162  C   ASP D  73    11027   4030   8959   1003   -834  -1269       C  
ATOM   6163  O   ASP D  73      80.814 -37.326   1.553  1.00 64.72           O  
ANISOU 6163  O   ASP D  73    11221   3974   9395   1278   -925  -1305       O  
ATOM   6164  CB  ASP D  73      81.993 -34.708   1.942  1.00 64.75           C  
ANISOU 6164  CB  ASP D  73    10286   4363   9952   1117  -1001  -1050       C  
ATOM   6165  CG  ASP D  73      82.536 -33.291   1.904  1.00 80.57           C  
ANISOU 6165  CG  ASP D  73    11810   6553  12249    994   -989   -919       C  
ATOM   6166  OD1 ASP D  73      82.741 -32.759   0.783  1.00 82.41           O  
ANISOU 6166  OD1 ASP D  73    11795   6981  12538   1001   -530   -915       O  
ATOM   6167  OD2 ASP D  73      82.755 -32.712   2.992  1.00 87.82           O  
ANISOU 6167  OD2 ASP D  73    12650   7396  13322    884  -1452   -816       O  
ATOM   6168  N   ARG D  74      78.754 -36.367   1.631  1.00 55.71           N  
ANISOU 6168  N   ARG D  74    10476   3119   7573    726   -870  -1285       N  
ATOM   6169  CA  ARG D  74      78.086 -37.612   1.999  1.00 54.16           C  
ANISOU 6169  CA  ARG D  74    10744   2667   7169    692  -1017  -1329       C  
ATOM   6170  C   ARG D  74      76.724 -37.829   1.311  1.00 55.05           C  
ANISOU 6170  C   ARG D  74    11170   2846   6899    434   -862  -1400       C  
ATOM   6171  O   ARG D  74      76.185 -38.928   1.400  1.00 56.25           O  
ANISOU 6171  O   ARG D  74    11691   2762   6922    385   -954  -1444       O  
ATOM   6172  CB  ARG D  74      77.989 -37.776   3.531  1.00 53.54           C  
ANISOU 6172  CB  ARG D  74    10850   2418   7073    618  -1416  -1183       C  
ATOM   6173  CG  ARG D  74      77.120 -36.784   4.266  1.00 54.08           C  
ANISOU 6173  CG  ARG D  74    10983   2666   6901    332  -1486  -1069       C  
ATOM   6174  CD  ARG D  74      77.177 -37.050   5.758  1.00 55.57           C  
ANISOU 6174  CD  ARG D  74    11450   2644   7018    321  -1852   -936       C  
ATOM   6175  NE  ARG D  74      76.326 -36.101   6.472  1.00 66.43           N  
ANISOU 6175  NE  ARG D  74    12957   4171   8114     88  -1844   -847       N  
ATOM   6176  CZ  ARG D  74      75.143 -36.395   6.998  1.00 75.68           C  
ANISOU 6176  CZ  ARG D  74    14487   5307   8962   -116  -1758   -767       C  
ATOM   6177  NH1 ARG D  74      74.678 -37.639   6.953  1.00 57.85           N  
ANISOU 6177  NH1 ARG D  74    12509   2844   6626   -162  -1737   -745       N  
ATOM   6178  NH2 ARG D  74      74.423 -35.451   7.592  1.00 57.48           N  
ANISOU 6178  NH2 ARG D  74    12260   3147   6434   -270  -1675   -699       N  
ATOM   6179  N   PHE D  75      76.176 -36.827   0.635  1.00 49.45           N  
ANISOU 6179  N   PHE D  75    10319   2421   6048    265   -675  -1396       N  
ATOM   6180  CA  PHE D  75      74.916 -36.964  -0.106  1.00 49.26           C  
ANISOU 6180  CA  PHE D  75    10535   2458   5724     26   -595  -1450       C  
ATOM   6181  C   PHE D  75      75.199 -36.610  -1.557  1.00 55.45           C  
ANISOU 6181  C   PHE D  75    11259   3385   6426    124   -313  -1570       C  
ATOM   6182  O   PHE D  75      76.079 -35.789  -1.811  1.00 56.40           O  
ANISOU 6182  O   PHE D  75    11055   3664   6710    268   -136  -1535       O  
ATOM   6183  CB  PHE D  75      73.783 -36.064   0.439  1.00 50.40           C  
ANISOU 6183  CB  PHE D  75    10618   2793   5740   -277   -660  -1309       C  
ATOM   6184  CG  PHE D  75      73.035 -36.475   1.700  1.00 51.74           C  
ANISOU 6184  CG  PHE D  75    10974   2830   5853   -446   -836  -1181       C  
ATOM   6185  CD1 PHE D  75      71.736 -36.031   1.930  1.00 54.03           C  
ANISOU 6185  CD1 PHE D  75    11265   3244   6020   -717   -805  -1074       C  
ATOM   6186  CD2 PHE D  75      73.670 -37.200   2.711  1.00 52.71           C  
ANISOU 6186  CD2 PHE D  75    11253   2711   6063   -315  -1013  -1137       C  
ATOM   6187  CE1 PHE D  75      71.065 -36.355   3.119  1.00 54.33           C  
ANISOU 6187  CE1 PHE D  75    11471   3172   5998   -859   -864   -926       C  
ATOM   6188  CE2 PHE D  75      73.011 -37.490   3.913  1.00 54.90           C  
ANISOU 6188  CE2 PHE D  75    11763   2869   6228   -469  -1129   -986       C  
ATOM   6189  CZ  PHE D  75      71.710 -37.074   4.105  1.00 52.85           C  
ANISOU 6189  CZ  PHE D  75    11513   2745   5824   -741  -1011   -881       C  
ATOM   6190  N   THR D  76      74.486 -37.252  -2.504  1.00 51.99           N  
ANISOU 6190  N   THR D  76    11165   2859   5729     41   -285  -1700       N  
ATOM   6191  CA  THR D  76      74.612 -37.028  -3.947  1.00 51.95           C  
ANISOU 6191  CA  THR D  76    11275   2948   5515    125    -36  -1826       C  
ATOM   6192  C   THR D  76      73.223 -36.998  -4.571  1.00 56.39           C  
ANISOU 6192  C   THR D  76    12110   3540   5776   -183   -201  -1846       C  
ATOM   6193  O   THR D  76      72.452 -37.955  -4.438  1.00 57.19           O  
ANISOU 6193  O   THR D  76    12512   3414   5804   -340   -441  -1901       O  
ATOM   6194  CB  THR D  76      75.523 -38.091  -4.614  1.00 66.57           C  
ANISOU 6194  CB  THR D  76    13377   4559   7359    472    163  -2029       C  
ATOM   6195  OG1 THR D  76      76.747 -38.220  -3.885  1.00 74.10           O  
ANISOU 6195  OG1 THR D  76    14013   5442   8699    753    228  -1979       O  
ATOM   6196  CG2 THR D  76      75.826 -37.782  -6.082  1.00 61.89           C  
ANISOU 6196  CG2 THR D  76    12932   4074   6507    621    527  -2146       C  
ATOM   6197  N   ILE D  77      72.921 -35.905  -5.269  1.00 53.43           N  
ANISOU 6197  N   ILE D  77    11619   3419   5262   -278   -104  -1784       N  
ATOM   6198  CA  ILE D  77      71.668 -35.704  -5.996  1.00 53.52           C  
ANISOU 6198  CA  ILE D  77    11838   3477   5020   -547   -300  -1781       C  
ATOM   6199  C   ILE D  77      71.933 -35.947  -7.485  1.00 60.59           C  
ANISOU 6199  C   ILE D  77    13153   4314   5553   -410   -155  -1958       C  
ATOM   6200  O   ILE D  77      72.977 -35.555  -8.006  1.00 61.02           O  
ANISOU 6200  O   ILE D  77    13154   4467   5565   -155    216  -1981       O  
ATOM   6201  CB  ILE D  77      70.955 -34.343  -5.653  1.00 55.69           C  
ANISOU 6201  CB  ILE D  77    11751   4027   5383   -753   -371  -1571       C  
ATOM   6202  CG1 ILE D  77      69.504 -34.290  -6.206  1.00 54.69           C  
ANISOU 6202  CG1 ILE D  77    11764   3902   5114  -1048   -675  -1536       C  
ATOM   6203  CG2 ILE D  77      71.773 -33.123  -6.071  1.00 56.09           C  
ANISOU 6203  CG2 ILE D  77    11572   4305   5434   -609    -91  -1496       C  
ATOM   6204  CD1 ILE D  77      68.553 -33.254  -5.557  1.00 45.44           C  
ANISOU 6204  CD1 ILE D  77    10207   2922   4136  -1246   -786  -1323       C  
ATOM   6205  N   SER D  78      71.037 -36.677  -8.139  1.00 59.81           N  
ANISOU 6205  N   SER D  78    13504   4021   5201   -573   -439  -2081       N  
ATOM   6206  CA  SER D  78      71.147 -36.992  -9.567  1.00 61.29           C  
ANISOU 6206  CA  SER D  78    14253   4097   4938   -459   -370  -2278       C  
ATOM   6207  C   SER D  78      69.760 -37.123 -10.143  1.00 71.62           C  
ANISOU 6207  C   SER D  78    15868   5313   6033   -799   -863  -2288       C  
ATOM   6208  O   SER D  78      68.809 -37.339  -9.397  1.00 70.62           O  
ANISOU 6208  O   SER D  78    15531   5131   6170  -1092  -1217  -2179       O  
ATOM   6209  CB  SER D  78      71.936 -38.278  -9.792  1.00 61.50           C  
ANISOU 6209  CB  SER D  78    14694   3803   4871   -164   -207  -2533       C  
ATOM   6210  OG  SER D  78      71.320 -39.342  -9.089  1.00 66.09           O  
ANISOU 6210  OG  SER D  78    15388   4096   5625   -337   -576  -2577       O  
ATOM   6211  N   ARG D  79      69.638 -36.956 -11.456  1.00 74.23           N  
ANISOU 6211  N   ARG D  79    16679   5626   5900   -768   -888  -2391       N  
ATOM   6212  CA  ARG D  79      68.352 -37.039 -12.127  1.00 77.04           C  
ANISOU 6212  CA  ARG D  79    17354   5873   6046  -1091  -1447  -2396       C  
ATOM   6213  C   ARG D  79      68.448 -37.959 -13.321  1.00 87.27           C  
ANISOU 6213  C   ARG D  79    19516   6835   6808   -992  -1575  -2696       C  
ATOM   6214  O   ARG D  79      69.447 -37.923 -14.044  1.00 87.35           O  
ANISOU 6214  O   ARG D  79    19899   6838   6451   -643  -1110  -2845       O  
ATOM   6215  CB  ARG D  79      67.823 -35.623 -12.501  1.00 77.88           C  
ANISOU 6215  CB  ARG D  79    17205   6287   6099  -1220  -1524  -2166       C  
ATOM   6216  CG  ARG D  79      68.510 -34.900 -13.681  1.00 83.39           C  
ANISOU 6216  CG  ARG D  79    18299   7098   6288   -996  -1198  -2197       C  
ATOM   6217  CD  ARG D  79      68.108 -33.436 -13.828  1.00 81.84           C  
ANISOU 6217  CD  ARG D  79    17778   7190   6128  -1114  -1255  -1924       C  
ATOM   6218  NE  ARG D  79      66.661 -33.260 -13.964  1.00 82.79           N  
ANISOU 6218  NE  ARG D  79    17823   7271   6363  -1456  -1921  -1810       N  
ATOM   6219  CZ  ARG D  79      65.973 -32.232 -13.472  1.00 96.26           C  
ANISOU 6219  CZ  ARG D  79    18940   9185   8450  -1611  -2073  -1552       C  
ATOM   6220  NH1 ARG D  79      66.593 -31.262 -12.810  1.00 74.26           N  
ANISOU 6220  NH1 ARG D  79    15660   6641   5914  -1475  -1645  -1397       N  
ATOM   6221  NH2 ARG D  79      64.662 -32.168 -13.634  1.00 90.15           N  
ANISOU 6221  NH2 ARG D  79    18061   8352   7842  -1895  -2668  -1446       N  
ATOM   6222  N   ASP D  80      67.435 -38.811 -13.509  1.00 88.83           N  
ANISOU 6222  N   ASP D  80    20042   6727   6980  -1294  -2187  -2786       N  
ATOM   6223  CA  ASP D  80      67.377 -39.701 -14.669  1.00 90.88           C  
ANISOU 6223  CA  ASP D  80    21234   6601   6697  -1249  -2446  -3096       C  
ATOM   6224  C   ASP D  80      66.878 -38.909 -15.856  1.00 98.54           C  
ANISOU 6224  C   ASP D  80    22606   7656   7180  -1346  -2715  -3066       C  
ATOM   6225  O   ASP D  80      67.391 -39.114 -16.950  1.00100.98           O  
ANISOU 6225  O   ASP D  80    23701   7814   6851  -1102  -2549  -3295       O  
ATOM   6226  CB  ASP D  80      66.456 -40.894 -14.429  1.00 93.28           C  
ANISOU 6226  CB  ASP D  80    21743   6492   7208  -1583  -3080  -3190       C  
ATOM   6227  CG  ASP D  80      66.706 -42.008 -15.412  1.00110.31           C  
ANISOU 6227  CG  ASP D  80    24904   8164   8844  -1437  -3238  -3577       C  
ATOM   6228  OD1 ASP D  80      66.216 -41.909 -16.560  1.00113.58           O  
ANISOU 6228  OD1 ASP D  80    25986   8427   8741  -1532  -3633  -3707       O  
ATOM   6229  OD2 ASP D  80      67.395 -42.983 -15.040  1.00118.52           O  
ANISOU 6229  OD2 ASP D  80    26110   8945   9975  -1212  -2991  -3756       O  
ATOM   6230  N   ASN D  81      65.884 -38.004 -15.627  1.00 95.75           N  
ANISOU 6230  N   ASN D  81    21731   7528   7119  -1673  -3110  -2776       N  
ATOM   6231  CA  ASN D  81      65.182 -37.111 -16.564  1.00 96.50           C  
ANISOU 6231  CA  ASN D  81    22037   7718   6908  -1834  -3518  -2654       C  
ATOM   6232  C   ASN D  81      63.930 -37.773 -17.154  1.00105.07           C  
ANISOU 6232  C   ASN D  81    23521   8451   7950  -2225  -4444  -2725       C  
ATOM   6233  O   ASN D  81      62.978 -37.081 -17.529  1.00106.34           O  
ANISOU 6233  O   ASN D  81    23557   8686   8162  -2475  -4982  -2534       O  
ATOM   6234  CB  ASN D  81      66.097 -36.533 -17.651  1.00 95.82           C  
ANISOU 6234  CB  ASN D  81    22585   7717   6106  -1501  -3079  -2746       C  
ATOM   6235  CG  ASN D  81      66.491 -35.095 -17.478  1.00117.43           C  
ANISOU 6235  CG  ASN D  81    24792  10878   8947  -1372  -2601  -2464       C  
ATOM   6236  OD1 ASN D  81      65.821 -34.302 -16.809  1.00112.96           O  
ANISOU 6236  OD1 ASN D  81    23514  10540   8866  -1575  -2797  -2186       O  
ATOM   6237  ND2 ASN D  81      67.590 -34.722 -18.112  1.00110.06           N  
ANISOU 6237  ND2 ASN D  81    24222  10035   7561  -1026  -1943  -2524       N  
ATOM   6238  N   ALA D  82      63.937 -39.120 -17.223  1.00102.42           N  
ANISOU 6238  N   ALA D  82    23650   7701   7564  -2280  -4665  -2990       N  
ATOM   6239  CA  ALA D  82      62.826 -39.964 -17.656  1.00101.47           C  
ANISOU 6239  CA  ALA D  82    23894   7160   7499  -2687  -5568  -3078       C  
ATOM   6240  C   ALA D  82      61.902 -40.246 -16.423  1.00105.15           C  
ANISOU 6240  C   ALA D  82    23419   7664   8871  -3061  -5800  -2812       C  
ATOM   6241  O   ALA D  82      61.551 -41.403 -16.163  1.00105.93           O  
ANISOU 6241  O   ALA D  82    23616   7413   9218  -3236  -6017  -2917       O  
ATOM   6242  CB  ALA D  82      63.355 -41.264 -18.254  1.00101.69           C  
ANISOU 6242  CB  ALA D  82    24913   6689   7036  -2535  -5621  -3497       C  
ATOM   6243  N   LYS D  83      61.588 -39.156 -15.645  1.00 98.52           N  
ANISOU 6243  N   LYS D  83    21689   7250   8495  -3143  -5665  -2459       N  
ATOM   6244  CA  LYS D  83      60.670 -38.956 -14.507  1.00 96.76           C  
ANISOU 6244  CA  LYS D  83    20483   7193   9088  -3440  -5758  -2127       C  
ATOM   6245  C   LYS D  83      61.294 -39.040 -13.080  1.00 96.49           C  
ANISOU 6245  C   LYS D  83    19907   7313   9440  -3288  -5078  -2050       C  
ATOM   6246  O   LYS D  83      60.592 -38.655 -12.137  1.00 96.72           O  
ANISOU 6246  O   LYS D  83    19168   7504  10076  -3491  -5055  -1766       O  
ATOM   6247  CB  LYS D  83      59.401 -39.852 -14.588  1.00 99.62           C  
ANISOU 6247  CB  LYS D  83    20784   7203   9865  -3956  -6615  -2052       C  
ATOM   6248  CG  LYS D  83      59.393 -41.150 -13.768  1.00116.47           C  
ANISOU 6248  CG  LYS D  83    23010   8957  12284  -4153  -6691  -2147       C  
ATOM   6249  CD  LYS D  83      57.983 -41.735 -13.685  1.00127.03           C  
ANISOU 6249  CD  LYS D  83    23985  10034  14245  -4724  -7466  -1941       C  
ATOM   6250  CE  LYS D  83      57.851 -42.793 -12.616  1.00134.20           C  
ANISOU 6250  CE  LYS D  83    24774  10636  15579  -4950  -7412  -1916       C  
ATOM   6251  NZ  LYS D  83      56.455 -42.886 -12.114  1.00141.80           N  
ANISOU 6251  NZ  LYS D  83    24976  11525  17375  -5488  -7866  -1554       N  
ATOM   6252  N   ILE D  85      62.567 -39.471 -12.894  1.00 88.58           N  
ANISOU 6252  N   ILE D  85    19266   6278   8113  -2914  -4517  -2273       N  
ATOM   6253  CA  ILE D  85      63.078 -39.599 -11.514  1.00 85.78           C  
ANISOU 6253  CA  ILE D  85    18422   6030   8139  -2791  -3997  -2180       C  
ATOM   6254  C   ILE D  85      64.320 -38.755 -11.127  1.00 83.31           C  
ANISOU 6254  C   ILE D  85    17879   6067   7707  -2366  -3278  -2164       C  
ATOM   6255  O   ILE D  85      65.197 -38.496 -11.947  1.00 82.55           O  
ANISOU 6255  O   ILE D  85    18204   6015   7146  -2061  -3010  -2335       O  
ATOM   6256  CB  ILE D  85      63.355 -41.094 -11.188  1.00 88.51           C  
ANISOU 6256  CB  ILE D  85    19212   5934   8483  -2802  -4066  -2389       C  
ATOM   6257  N   VAL D  86      64.384 -38.364  -9.837  1.00 75.31           N  
ANISOU 6257  N   VAL D  86    16210   5273   7130  -2361  -2968  -1949       N  
ATOM   6258  CA  VAL D  86      65.550 -37.733  -9.215  1.00 73.28           C  
ANISOU 6258  CA  VAL D  86    15687   5275   6880  -2014  -2375  -1920       C  
ATOM   6259  C   VAL D  86      65.910 -38.573  -8.002  1.00 73.08           C  
ANISOU 6259  C   VAL D  86    15519   5105   7145  -1980  -2209  -1903       C  
ATOM   6260  O   VAL D  86      65.035 -38.907  -7.202  1.00 71.44           O  
ANISOU 6260  O   VAL D  86    15041   4823   7280  -2267  -2401  -1734       O  
ATOM   6261  CB  VAL D  86      65.571 -36.187  -8.941  1.00 76.69           C  
ANISOU 6261  CB  VAL D  86    15594   6116   7430  -1950  -2143  -1702       C  
ATOM   6262  CG1 VAL D  86      65.001 -35.375 -10.101  1.00 76.28           C  
ANISOU 6262  CG1 VAL D  86    15710   6167   7106  -2015  -2385  -1675       C  
ATOM   6263  CG2 VAL D  86      64.917 -35.809  -7.620  1.00 76.31           C  
ANISOU 6263  CG2 VAL D  86    14930   6203   7860  -2135  -2139  -1448       C  
ATOM   6264  N   TYR D  87      67.184 -38.964  -7.914  1.00 68.73           N  
ANISOU 6264  N   TYR D  87    15165   4486   6463  -1630  -1859  -2062       N  
ATOM   6265  CA  TYR D  87      67.735 -39.805  -6.848  1.00 67.78           C  
ANISOU 6265  CA  TYR D  87    15001   4186   6568  -1527  -1727  -2064       C  
ATOM   6266  C   TYR D  87      68.527 -39.004  -5.833  1.00 68.31           C  
ANISOU 6266  C   TYR D  87    14597   4521   6837  -1321  -1364  -1917       C  
ATOM   6267  O   TYR D  87      69.187 -38.025  -6.190  1.00 67.51           O  
ANISOU 6267  O   TYR D  87    14336   4674   6642  -1114  -1099  -1918       O  
ATOM   6268  CB  TYR D  87      68.666 -40.885  -7.436  1.00 69.20           C  
ANISOU 6268  CB  TYR D  87    15742   4032   6517  -1234  -1643  -2355       C  
ATOM   6269  CG  TYR D  87      68.028 -41.794  -8.461  1.00 70.56           C  
ANISOU 6269  CG  TYR D  87    16536   3848   6427  -1400  -2034  -2562       C  
ATOM   6270  CD1 TYR D  87      67.275 -42.897  -8.071  1.00 72.04           C  
ANISOU 6270  CD1 TYR D  87    16911   3663   6797  -1693  -2422  -2554       C  
ATOM   6271  CD2 TYR D  87      68.215 -41.581  -9.823  1.00 71.66           C  
ANISOU 6271  CD2 TYR D  87    17135   3982   6112  -1268  -2027  -2765       C  
ATOM   6272  CE1 TYR D  87      66.708 -43.754  -9.010  1.00 73.21           C  
ANISOU 6272  CE1 TYR D  87    17669   3425   6722  -1871  -2859  -2758       C  
ATOM   6273  CE2 TYR D  87      67.636 -42.424 -10.775  1.00 72.75           C  
ANISOU 6273  CE2 TYR D  87    17946   3744   5951  -1421  -2456  -2982       C  
ATOM   6274  CZ  TYR D  87      66.884 -43.510 -10.362  1.00 82.78           C  
ANISOU 6274  CZ  TYR D  87    19374   4630   7450  -1730  -2902  -2987       C  
ATOM   6275  OH  TYR D  87      66.331 -44.367 -11.288  1.00 90.49           O  
ANISOU 6275  OH  TYR D  87    21048   5179   8153  -1904  -3396  -3214       O  
ATOM   6276  N   LEU D  88      68.494 -39.450  -4.568  1.00 62.51           N  
ANISOU 6276  N   LEU D  88    13690   3695   6366  -1386  -1372  -1784       N  
ATOM   6277  CA  LEU D  88      69.277 -38.859  -3.481  1.00 60.34           C  
ANISOU 6277  CA  LEU D  88    13074   3592   6262  -1195  -1123  -1661       C  
ATOM   6278  C   LEU D  88      70.015 -40.003  -2.771  1.00 63.73           C  
ANISOU 6278  C   LEU D  88    13716   3709   6788  -1028  -1133  -1714       C  
ATOM   6279  O   LEU D  88      69.383 -40.803  -2.068  1.00 63.42           O  
ANISOU 6279  O   LEU D  88    13796   3448   6852  -1240  -1309  -1615       O  
ATOM   6280  CB  LEU D  88      68.422 -38.004  -2.499  1.00 59.08           C  
ANISOU 6280  CB  LEU D  88    12513   3658   6277  -1417  -1118  -1404       C  
ATOM   6281  CG  LEU D  88      69.150 -37.400  -1.250  1.00 61.37           C  
ANISOU 6281  CG  LEU D  88    12558   4069   6689  -1244   -936  -1287       C  
ATOM   6282  CD1 LEU D  88      70.052 -36.235  -1.611  1.00 60.47           C  
ANISOU 6282  CD1 LEU D  88    12221   4202   6553  -1014   -751  -1327       C  
ATOM   6283  CD2 LEU D  88      68.165 -36.983  -0.168  1.00 60.85           C  
ANISOU 6283  CD2 LEU D  88    12284   4100   6737  -1464   -921  -1061       C  
ATOM   6284  N   GLN D  89      71.335 -40.127  -3.020  1.00 59.58           N  
ANISOU 6284  N   GLN D  89    13240   3142   6256   -647   -942  -1857       N  
ATOM   6285  CA  GLN D  89      72.128 -41.159  -2.352  1.00 59.63           C  
ANISOU 6285  CA  GLN D  89    13413   2840   6404   -427   -976  -1900       C  
ATOM   6286  C   GLN D  89      72.653 -40.556  -1.059  1.00 62.73           C  
ANISOU 6286  C   GLN D  89    13456   3374   7004   -351   -943  -1705       C  
ATOM   6287  O   GLN D  89      73.448 -39.610  -1.088  1.00 60.27           O  
ANISOU 6287  O   GLN D  89    12818   3306   6776   -169   -773  -1686       O  
ATOM   6288  CB  GLN D  89      73.264 -41.707  -3.245  1.00 60.96           C  
ANISOU 6288  CB  GLN D  89    13790   2846   6524    -18   -787  -2147       C  
ATOM   6289  CG  GLN D  89      74.125 -42.811  -2.585  1.00 66.60           C  
ANISOU 6289  CG  GLN D  89    14652   3206   7448    269   -845  -2191       C  
ATOM   6290  CD  GLN D  89      73.354 -44.047  -2.183  1.00 73.84           C  
ANISOU 6290  CD  GLN D  89    16000   3715   8341     55  -1158  -2189       C  
ATOM   6291  OE1 GLN D  89      72.554 -44.586  -2.939  1.00 71.26           O  
ANISOU 6291  OE1 GLN D  89    16050   3204   7822   -134  -1290  -2320       O  
ATOM   6292  NE2 GLN D  89      73.579 -44.525  -0.978  1.00 62.53           N  
ANISOU 6292  NE2 GLN D  89    14552   2104   7102     62  -1316  -2024       N  
ATOM   6293  N   MET D  90      72.155 -41.075   0.072  1.00 60.22           N  
ANISOU 6293  N   MET D  90    13242   2886   6752   -523  -1122  -1545       N  
ATOM   6294  CA  MET D  90      72.514 -40.594   1.408  1.00 59.89           C  
ANISOU 6294  CA  MET D  90    13018   2919   6816   -481  -1154  -1356       C  
ATOM   6295  C   MET D  90      73.481 -41.570   2.031  1.00 63.69           C  
ANISOU 6295  C   MET D  90    13693   3072   7434   -218  -1299  -1368       C  
ATOM   6296  O   MET D  90      73.148 -42.738   2.175  1.00 63.57           O  
ANISOU 6296  O   MET D  90    14035   2718   7401   -291  -1441  -1365       O  
ATOM   6297  CB  MET D  90      71.276 -40.448   2.304  1.00 61.90           C  
ANISOU 6297  CB  MET D  90    13305   3212   7001   -836  -1198  -1135       C  
ATOM   6298  CG  MET D  90      70.143 -39.671   1.685  1.00 65.16           C  
ANISOU 6298  CG  MET D  90    13516   3891   7352  -1105  -1099  -1103       C  
ATOM   6299  SD  MET D  90      68.808 -39.360   2.859  1.00 69.25           S  
ANISOU 6299  SD  MET D  90    13955   4487   7871  -1438  -1029   -813       S  
ATOM   6300  CE  MET D  90      68.159 -40.979   3.076  1.00 65.95           C  
ANISOU 6300  CE  MET D  90    13901   3655   7504  -1680  -1181   -726       C  
ATOM   6301  N   ASN D  91      74.686 -41.107   2.357  1.00 60.27           N  
ANISOU 6301  N   ASN D  91    13013   2709   7179     84  -1296  -1371       N  
ATOM   6302  CA  ASN D  91      75.709 -41.948   2.970  1.00 60.09           C  
ANISOU 6302  CA  ASN D  91    13098   2373   7359    381  -1488  -1361       C  
ATOM   6303  C   ASN D  91      76.080 -41.404   4.350  1.00 63.93           C  
ANISOU 6303  C   ASN D  91    13493   2895   7902    386  -1710  -1160       C  
ATOM   6304  O   ASN D  91      75.792 -40.240   4.653  1.00 61.94           O  
ANISOU 6304  O   ASN D  91    13032   2936   7565    235  -1650  -1081       O  
ATOM   6305  CB  ASN D  91      76.946 -42.038   2.060  1.00 61.02           C  
ANISOU 6305  CB  ASN D  91    12987   2475   7723    785  -1329  -1544       C  
ATOM   6306  CG  ASN D  91      76.711 -42.653   0.691  1.00 80.06           C  
ANISOU 6306  CG  ASN D  91    15625   4790  10002    850  -1105  -1778       C  
ATOM   6307  OD1 ASN D  91      75.691 -43.295   0.409  1.00 69.49           O  
ANISOU 6307  OD1 ASN D  91    14673   3292   8437    604  -1179  -1824       O  
ATOM   6308  ND2 ASN D  91      77.675 -42.480  -0.194  1.00 72.55           N  
ANISOU 6308  ND2 ASN D  91    14457   3912   9196   1184   -827  -1925       N  
ATOM   6309  N   SER D  92      76.719 -42.249   5.183  1.00 61.30           N  
ANISOU 6309  N   SER D  92    13371   2228   7695    572  -1999  -1083       N  
ATOM   6310  CA  SER D  92      77.165 -41.911   6.543  1.00 61.94           C  
ANISOU 6310  CA  SER D  92    13498   2249   7785    605  -2315   -895       C  
ATOM   6311  C   SER D  92      76.011 -41.299   7.365  1.00 65.10           C  
ANISOU 6311  C   SER D  92    14116   2801   7817    246  -2262   -731       C  
ATOM   6312  O   SER D  92      76.158 -40.208   7.913  1.00 64.31           O  
ANISOU 6312  O   SER D  92    13874   2902   7660    217  -2317   -672       O  
ATOM   6313  CB  SER D  92      78.373 -40.966   6.501  1.00 66.48           C  
ANISOU 6313  CB  SER D  92    13579   3001   8681    844  -2404   -924       C  
ATOM   6314  OG  SER D  92      79.398 -41.461   5.654  1.00 77.51           O  
ANISOU 6314  OG  SER D  92    14701   4282  10467   1199  -2348  -1055       O  
ATOM   6315  N   LEU D  93      74.848 -41.982   7.397  1.00 60.83           N  
ANISOU 6315  N   LEU D  93    13903   2153   7057    -25  -2132   -662       N  
ATOM   6316  CA  LEU D  93      73.664 -41.507   8.118  1.00 60.09           C  
ANISOU 6316  CA  LEU D  93    13976   2191   6664   -351  -1977   -486       C  
ATOM   6317  C   LEU D  93      73.803 -41.733   9.622  1.00 64.18           C  
ANISOU 6317  C   LEU D  93    14928   2490   6969   -341  -2200   -267       C  
ATOM   6318  O   LEU D  93      74.294 -42.775  10.056  1.00 64.74           O  
ANISOU 6318  O   LEU D  93    15328   2196   7076   -224  -2462   -194       O  
ATOM   6319  CB  LEU D  93      72.380 -42.177   7.595  1.00 59.95           C  
ANISOU 6319  CB  LEU D  93    14084   2114   6580   -666  -1768   -451       C  
ATOM   6320  CG  LEU D  93      71.933 -41.824   6.174  1.00 64.26           C  
ANISOU 6320  CG  LEU D  93    14299   2891   7224   -759  -1571   -635       C  
ATOM   6321  CD1 LEU D  93      71.009 -42.891   5.632  1.00 64.18           C  
ANISOU 6321  CD1 LEU D  93    14500   2657   7228  -1024  -1560   -622       C  
ATOM   6322  CD2 LEU D  93      71.259 -40.454   6.112  1.00 63.91           C  
ANISOU 6322  CD2 LEU D  93    13931   3253   7098   -904  -1346   -601       C  
ATOM   6323  N   GLN D  94      73.360 -40.765  10.414  1.00 59.35           N  
ANISOU 6323  N   GLN D  94    14376   2069   6105   -449  -2100   -163       N  
ATOM   6324  CA  GLN D  94      73.436 -40.838  11.873  1.00 59.06           C  
ANISOU 6324  CA  GLN D  94    14853   1835   5752   -438  -2286     39       C  
ATOM   6325  C   GLN D  94      72.046 -40.501  12.471  1.00 65.01           C  
ANISOU 6325  C   GLN D  94    15834   2711   6155   -727  -1870    217       C  
ATOM   6326  O   GLN D  94      71.203 -39.981  11.732  1.00 64.09           O  
ANISOU 6326  O   GLN D  94    15352   2873   6127   -893  -1517    158       O  
ATOM   6327  CB  GLN D  94      74.531 -39.875  12.408  1.00 59.74           C  
ANISOU 6327  CB  GLN D  94    14869   1978   5852   -204  -2635    -26       C  
ATOM   6328  CG  GLN D  94      75.928 -39.990  11.766  1.00 58.05           C  
ANISOU 6328  CG  GLN D  94    14262   1696   6097     89  -2984   -178       C  
ATOM   6329  CD  GLN D  94      76.639 -41.309  11.998  1.00 75.48           C  
ANISOU 6329  CD  GLN D  94    16716   3500   8463    279  -3330   -114       C  
ATOM   6330  OE1 GLN D  94      76.676 -41.850  13.106  1.00 70.67           O  
ANISOU 6330  OE1 GLN D  94    16655   2597   7601    285  -3610     73       O  
ATOM   6331  NE2 GLN D  94      77.235 -41.857  10.945  1.00 66.31           N  
ANISOU 6331  NE2 GLN D  94    15192   2293   7709    463  -3310   -265       N  
ATOM   6332  N   PRO D  95      71.766 -40.762  13.779  1.00 64.30           N  
ANISOU 6332  N   PRO D  95    16338   2419   5673   -780  -1876    448       N  
ATOM   6333  CA  PRO D  95      70.442 -40.413  14.331  1.00 64.97           C  
ANISOU 6333  CA  PRO D  95    16596   2634   5455  -1024  -1364    631       C  
ATOM   6334  C   PRO D  95      69.924 -38.994  14.033  1.00 68.89           C  
ANISOU 6334  C   PRO D  95    16703   3525   5946  -1039  -1042    509       C  
ATOM   6335  O   PRO D  95      68.724 -38.869  13.799  1.00 69.14           O  
ANISOU 6335  O   PRO D  95    16536   3721   6014  -1256   -575    603       O  
ATOM   6336  CB  PRO D  95      70.623 -40.651  15.826  1.00 67.25           C  
ANISOU 6336  CB  PRO D  95    17647   2652   5254   -963  -1491    847       C  
ATOM   6337  CG  PRO D  95      71.606 -41.815  15.874  1.00 71.54           C  
ANISOU 6337  CG  PRO D  95    18429   2816   5937   -828  -2018    877       C  
ATOM   6338  CD  PRO D  95      72.602 -41.421  14.809  1.00 66.82           C  
ANISOU 6338  CD  PRO D  95    17224   2364   5801   -615  -2324    578       C  
ATOM   6339  N   GLU D  96      70.804 -37.950  13.959  1.00 63.87           N  
ANISOU 6339  N   GLU D  96    15904   3024   5340   -823  -1305    311       N  
ATOM   6340  CA  GLU D  96      70.396 -36.559  13.657  1.00 62.70           C  
ANISOU 6340  CA  GLU D  96    15416   3202   5204   -817  -1052    188       C  
ATOM   6341  C   GLU D  96      69.714 -36.429  12.293  1.00 66.36           C  
ANISOU 6341  C   GLU D  96    15253   3923   6037   -962   -779    104       C  
ATOM   6342  O   GLU D  96      68.903 -35.521  12.109  1.00 67.22           O  
ANISOU 6342  O   GLU D  96    15127   4271   6143  -1028   -440     98       O  
ATOM   6343  CB  GLU D  96      71.590 -35.583  13.727  1.00 63.83           C  
ANISOU 6343  CB  GLU D  96    15471   3379   5404   -596  -1471      2       C  
ATOM   6344  CG  GLU D  96      71.944 -35.106  15.126  1.00 76.83           C  
ANISOU 6344  CG  GLU D  96    17742   4847   6604   -477  -1695     48       C  
ATOM   6345  CD  GLU D  96      71.271 -33.828  15.604  1.00113.74           C  
ANISOU 6345  CD  GLU D  96    22547   9678  10989   -465  -1387     -1       C  
ATOM   6346  OE1 GLU D  96      71.188 -32.850  14.822  1.00104.68           O  
ANISOU 6346  OE1 GLU D  96    20901   8772  10102   -459  -1286   -150       O  
ATOM   6347  OE2 GLU D  96      70.851 -33.799  16.783  1.00115.55           O  
ANISOU 6347  OE2 GLU D  96    23433   9763  10706   -441  -1243    112       O  
ATOM   6348  N   ASP D  97      70.064 -37.321  11.335  1.00 60.46           N  
ANISOU 6348  N   ASP D  97    14276   3101   5594   -985   -954     33       N  
ATOM   6349  CA  ASP D  97      69.527 -37.362   9.969  1.00 58.97           C  
ANISOU 6349  CA  ASP D  97    13607   3093   5708  -1116   -803    -64       C  
ATOM   6350  C   ASP D  97      68.116 -37.958   9.869  1.00 62.52           C  
ANISOU 6350  C   ASP D  97    14027   3534   6193  -1418   -481    110       C  
ATOM   6351  O   ASP D  97      67.531 -37.932   8.789  1.00 61.37           O  
ANISOU 6351  O   ASP D  97    13509   3528   6281  -1556   -403     45       O  
ATOM   6352  CB  ASP D  97      70.492 -38.099   9.026  1.00 59.81           C  
ANISOU 6352  CB  ASP D  97    13585   3075   6064   -990  -1095   -225       C  
ATOM   6353  CG  ASP D  97      71.837 -37.424   8.881  1.00 61.50           C  
ANISOU 6353  CG  ASP D  97    13626   3347   6392   -716  -1352   -380       C  
ATOM   6354  OD1 ASP D  97      71.862 -36.204   8.614  1.00 59.69           O  
ANISOU 6354  OD1 ASP D  97    13112   3374   6194   -690  -1263   -455       O  
ATOM   6355  OD2 ASP D  97      72.867 -38.117   9.032  1.00 63.93           O  
ANISOU 6355  OD2 ASP D  97    14058   3426   6805   -529  -1651   -410       O  
ATOM   6356  N   THR D  98      67.580 -38.504  10.984  1.00 59.99           N  
ANISOU 6356  N   THR D  98    14104   3036   5653  -1534   -309    349       N  
ATOM   6357  CA  THR D  98      66.227 -39.054  11.069  1.00 59.39           C  
ANISOU 6357  CA  THR D  98    13974   2933   5659  -1849     44    582       C  
ATOM   6358  C   THR D  98      65.236 -37.909  10.848  1.00 64.26           C  
ANISOU 6358  C   THR D  98    14161   3882   6371  -1910    420    599       C  
ATOM   6359  O   THR D  98      65.281 -36.895  11.559  1.00 63.35           O  
ANISOU 6359  O   THR D  98    14152   3899   6020  -1739    602    590       O  
ATOM   6360  CB  THR D  98      65.999 -39.681  12.435  1.00 66.04           C  
ANISOU 6360  CB  THR D  98    15378   3528   6185  -1911    214    858       C  
ATOM   6361  OG1 THR D  98      66.996 -40.677  12.668  1.00 70.75           O  
ANISOU 6361  OG1 THR D  98    16388   3792   6701  -1808   -202    843       O  
ATOM   6362  CG2 THR D  98      64.590 -40.255  12.602  1.00 65.07           C  
ANISOU 6362  CG2 THR D  98    15165   3362   6199  -2265    645   1159       C  
ATOM   6363  N   ALA D  99      64.358 -38.076   9.848  1.00 60.76           N  
ANISOU 6363  N   ALA D  99    13262   3540   6283  -2141    488    617       N  
ATOM   6364  CA  ALA D  99      63.329 -37.108   9.471  1.00 59.83           C  
ANISOU 6364  CA  ALA D  99    12653   3711   6370  -2213    782    656       C  
ATOM   6365  C   ALA D  99      62.434 -37.716   8.408  1.00 62.06           C  
ANISOU 6365  C   ALA D  99    12531   3981   7067  -2527    694    714       C  
ATOM   6366  O   ALA D  99      62.729 -38.788   7.891  1.00 60.68           O  
ANISOU 6366  O   ALA D  99    12504   3579   6974  -2657    386    667       O  
ATOM   6367  CB  ALA D  99      63.985 -35.847   8.908  1.00 60.52           C  
ANISOU 6367  CB  ALA D  99    12536   4033   6423  -1953    635    401       C  
ATOM   6368  N   VAL D 100      61.353 -37.008   8.071  1.00 59.06           N  
ANISOU 6368  N   VAL D 100    11657   3821   6963  -2631    922    808       N  
ATOM   6369  CA  VAL D 100      60.475 -37.322   6.952  1.00 58.57           C  
ANISOU 6369  CA  VAL D 100    11146   3778   7330  -2915    736    844       C  
ATOM   6370  C   VAL D 100      61.095 -36.486   5.832  1.00 59.86           C  
ANISOU 6370  C   VAL D 100    11164   4126   7454  -2713    424    551       C  
ATOM   6371  O   VAL D 100      61.295 -35.281   6.007  1.00 59.83           O  
ANISOU 6371  O   VAL D 100    11049   4340   7343  -2471    579    481       O  
ATOM   6372  CB  VAL D 100      58.990 -36.946   7.206  1.00 62.87           C  
ANISOU 6372  CB  VAL D 100    11170   4458   8260  -3110   1123   1130       C  
ATOM   6373  CG1 VAL D 100      58.156 -37.116   5.937  1.00 62.86           C  
ANISOU 6373  CG1 VAL D 100    10677   4470   8737  -3395    781   1146       C  
ATOM   6374  CG2 VAL D 100      58.401 -37.772   8.347  1.00 62.37           C  
ANISOU 6374  CG2 VAL D 100    11264   4217   8216  -3306   1543   1462       C  
ATOM   6375  N   TYR D 101      61.468 -37.137   4.724  1.00 54.29           N  
ANISOU 6375  N   TYR D 101    10535   3300   6795  -2798      4    379       N  
ATOM   6376  CA  TYR D 101      62.117 -36.498   3.578  1.00 52.52           C  
ANISOU 6376  CA  TYR D 101    10253   3215   6486  -2622   -263    119       C  
ATOM   6377  C   TYR D 101      61.127 -36.260   2.449  1.00 58.26           C  
ANISOU 6377  C   TYR D 101    10601   4031   7505  -2832   -471    145       C  
ATOM   6378  O   TYR D 101      60.511 -37.205   1.944  1.00 58.85           O  
ANISOU 6378  O   TYR D 101    10665   3911   7783  -3129   -714    201       O  
ATOM   6379  CB  TYR D 101      63.314 -37.337   3.091  1.00 51.79           C  
ANISOU 6379  CB  TYR D 101    10573   2917   6190  -2507   -544   -107       C  
ATOM   6380  CG  TYR D 101      64.557 -37.223   3.950  1.00 51.13           C  
ANISOU 6380  CG  TYR D 101    10783   2796   5848  -2210   -455   -182       C  
ATOM   6381  CD1 TYR D 101      64.577 -37.714   5.254  1.00 52.54           C  
ANISOU 6381  CD1 TYR D 101    11213   2818   5931  -2222   -297    -17       C  
ATOM   6382  CD2 TYR D 101      65.735 -36.684   3.439  1.00 50.79           C  
ANISOU 6382  CD2 TYR D 101    10779   2848   5672  -1930   -555   -398       C  
ATOM   6383  CE1 TYR D 101      65.713 -37.600   6.052  1.00 51.97           C  
ANISOU 6383  CE1 TYR D 101    11431   2686   5628  -1955   -315    -77       C  
ATOM   6384  CE2 TYR D 101      66.891 -36.609   4.213  1.00 51.00           C  
ANISOU 6384  CE2 TYR D 101    11014   2814   5549  -1678   -554   -449       C  
ATOM   6385  CZ  TYR D 101      66.878 -37.076   5.518  1.00 57.25           C  
ANISOU 6385  CZ  TYR D 101    12068   3442   6241  -1690   -479   -296       C  
ATOM   6386  OH  TYR D 101      68.010 -37.000   6.296  1.00 55.76           O  
ANISOU 6386  OH  TYR D 101    12110   3166   5911  -1449   -574   -336       O  
ATOM   6387  N   TYR D 102      60.970 -34.985   2.069  1.00 55.52           N  
ANISOU 6387  N   TYR D 102     9962   3944   7188  -2685   -421    114       N  
ATOM   6388  CA  TYR D 102      60.080 -34.536   1.000  1.00 55.62           C  
ANISOU 6388  CA  TYR D 102     9614   4058   7459  -2829   -665    149       C  
ATOM   6389  C   TYR D 102      60.896 -33.986  -0.145  1.00 60.40           C  
ANISOU 6389  C   TYR D 102    10387   4749   7816  -2652   -922    -87       C  
ATOM   6390  O   TYR D 102      61.910 -33.327   0.093  1.00 57.10           O  
ANISOU 6390  O   TYR D 102    10117   4432   7145  -2374   -763   -207       O  
ATOM   6391  CB  TYR D 102      59.158 -33.391   1.464  1.00 56.16           C  
ANISOU 6391  CB  TYR D 102     9198   4346   7794  -2768   -380    340       C  
ATOM   6392  CG  TYR D 102      58.401 -33.615   2.751  1.00 56.85           C  
ANISOU 6392  CG  TYR D 102     9106   4409   8085  -2850     63    594       C  
ATOM   6393  CD1 TYR D 102      58.968 -33.285   3.980  1.00 58.46           C  
ANISOU 6393  CD1 TYR D 102     9564   4643   8006  -2614    479    595       C  
ATOM   6394  CD2 TYR D 102      57.074 -34.032   2.738  1.00 57.60           C  
ANISOU 6394  CD2 TYR D 102     8759   4456   8670  -3154     82    854       C  
ATOM   6395  CE1 TYR D 102      58.261 -33.444   5.170  1.00 60.35           C  
ANISOU 6395  CE1 TYR D 102     9720   4857   8353  -2662    956    837       C  
ATOM   6396  CE2 TYR D 102      56.364 -34.225   3.924  1.00 58.94           C  
ANISOU 6396  CE2 TYR D 102     8751   4610   9036  -3225    593   1124       C  
ATOM   6397  CZ  TYR D 102      56.959 -33.919   5.140  1.00 67.24           C  
ANISOU 6397  CZ  TYR D 102    10144   5692   9711  -2963   1062   1111       C  
ATOM   6398  OH  TYR D 102      56.265 -34.068   6.320  1.00 66.49           O  
ANISOU 6398  OH  TYR D 102     9962   5578   9724  -3002   1632   1381       O  
ATOM   6399  N   CYS D 103      60.438 -34.237  -1.387  1.00 60.48           N  
ANISOU 6399  N   CYS D 103    10383   4700   7897  -2825  -1326   -136       N  
ATOM   6400  CA  CYS D 103      61.020 -33.632  -2.572  1.00 62.17           C  
ANISOU 6400  CA  CYS D 103    10769   5001   7852  -2676  -1539   -315       C  
ATOM   6401  C   CYS D 103      60.008 -32.585  -3.073  1.00 62.37           C  
ANISOU 6401  C   CYS D 103    10382   5195   8122  -2728  -1687   -169       C  
ATOM   6402  O   CYS D 103      58.803 -32.760  -2.865  1.00 61.76           O  
ANISOU 6402  O   CYS D 103     9927   5088   8453  -2957  -1790     29       O  
ATOM   6403  CB  CYS D 103      61.420 -34.646  -3.650  1.00 64.83           C  
ANISOU 6403  CB  CYS D 103    11567   5113   7952  -2762  -1890   -518       C  
ATOM   6404  SG  CYS D 103      60.048 -35.591  -4.370  1.00 70.68           S  
ANISOU 6404  SG  CYS D 103    12261   5611   8984  -3201  -2437   -433       S  
ATOM   6405  N   ALA D 104      60.495 -31.456  -3.615  1.00 56.19           N  
ANISOU 6405  N   ALA D 104     9622   4580   7146  -2506  -1664   -232       N  
ATOM   6406  CA  ALA D 104      59.635 -30.394  -4.139  1.00 55.49           C  
ANISOU 6406  CA  ALA D 104     9192   4624   7266  -2508  -1837    -94       C  
ATOM   6407  C   ALA D 104      60.047 -30.017  -5.549  1.00 58.91           C  
ANISOU 6407  C   ALA D 104     9946   5064   7374  -2459  -2161   -209       C  
ATOM   6408  O   ALA D 104      61.228 -30.111  -5.886  1.00 58.12           O  
ANISOU 6408  O   ALA D 104    10251   4953   6877  -2308  -2038   -387       O  
ATOM   6409  CB  ALA D 104      59.682 -29.178  -3.234  1.00 56.07           C  
ANISOU 6409  CB  ALA D 104     8978   4874   7453  -2270  -1445      0       C  
ATOM   6410  N   ALA D 105      59.077 -29.577  -6.368  1.00 56.21           N  
ANISOU 6410  N   ALA D 105     9420   4730   7209  -2574  -2564    -87       N  
ATOM   6411  CA  ALA D 105      59.300 -29.181  -7.766  1.00 55.67           C  
ANISOU 6411  CA  ALA D 105     9714   4646   6791  -2545  -2922   -156       C  
ATOM   6412  C   ALA D 105      59.009 -27.707  -8.071  1.00 58.10           C  
ANISOU 6412  C   ALA D 105     9784   5103   7190  -2392  -2961     -1       C  
ATOM   6413  O   ALA D 105      57.933 -27.181  -7.754  1.00 57.38           O  
ANISOU 6413  O   ALA D 105     9172   5057   7573  -2425  -3062    198       O  
ATOM   6414  CB  ALA D 105      58.510 -30.086  -8.702  1.00 56.41           C  
ANISOU 6414  CB  ALA D 105     9999   4533   6899  -2835  -3534   -174       C  
ATOM   6415  N   ASP D 106      59.987 -27.044  -8.695  1.00 54.28           N  
ANISOU 6415  N   ASP D 106     9673   4676   6275  -2213  -2856    -79       N  
ATOM   6416  CA  ASP D 106      59.881 -25.644  -9.112  1.00 53.37           C  
ANISOU 6416  CA  ASP D 106     9457   4656   6166  -2067  -2905     65       C  
ATOM   6417  C   ASP D 106      59.707 -25.593 -10.644  1.00 56.51           C  
ANISOU 6417  C   ASP D 106    10303   4967   6203  -2147  -3404     77       C  
ATOM   6418  O   ASP D 106      60.610 -26.049 -11.354  1.00 55.57           O  
ANISOU 6418  O   ASP D 106    10751   4797   5565  -2124  -3333    -84       O  
ATOM   6419  CB  ASP D 106      61.126 -24.843  -8.666  1.00 54.57           C  
ANISOU 6419  CB  ASP D 106     9701   4911   6121  -1832  -2399     14       C  
ATOM   6420  CG  ASP D 106      60.997 -23.325  -8.710  1.00 64.38           C  
ANISOU 6420  CG  ASP D 106    10762   6218   7480  -1675  -2369    180       C  
ATOM   6421  OD1 ASP D 106      60.010 -22.823  -9.290  1.00 66.24           O  
ANISOU 6421  OD1 ASP D 106    10863   6426   7880  -1710  -2761    338       O  
ATOM   6422  OD2 ASP D 106      61.877 -22.641  -8.161  1.00 66.76           O  
ANISOU 6422  OD2 ASP D 106    11059   6570   7738  -1521  -1997    156       O  
ATOM   6423  N   PRO D 107      58.574 -25.053 -11.182  1.00 53.07           N  
ANISOU 6423  N   PRO D 107     9655   4495   6016  -2219  -3910    269       N  
ATOM   6424  CA  PRO D 107      58.428 -24.970 -12.660  1.00 52.94           C  
ANISOU 6424  CA  PRO D 107    10173   4366   5575  -2292  -4450    289       C  
ATOM   6425  C   PRO D 107      59.459 -24.042 -13.320  1.00 57.65           C  
ANISOU 6425  C   PRO D 107    11236   5022   5648  -2097  -4187    299       C  
ATOM   6426  O   PRO D 107      59.621 -24.078 -14.544  1.00 57.39           O  
ANISOU 6426  O   PRO D 107    11822   4894   5091  -2131  -4483    281       O  
ATOM   6427  CB  PRO D 107      56.990 -24.484 -12.881  1.00 54.45           C  
ANISOU 6427  CB  PRO D 107     9910   4506   6273  -2383  -5046    533       C  
ATOM   6428  CG  PRO D 107      56.375 -24.368 -11.531  1.00 59.01           C  
ANISOU 6428  CG  PRO D 107     9692   5170   7557  -2368  -4755    626       C  
ATOM   6429  CD  PRO D 107      57.425 -24.444 -10.481  1.00 54.35           C  
ANISOU 6429  CD  PRO D 107     9106   4702   6843  -2205  -4001    484       C  
ATOM   6430  N   PHE D 108      60.157 -23.215 -12.495  1.00 53.52           N  
ANISOU 6430  N   PHE D 108    10442   4632   5259  -1905  -3631    336       N  
ATOM   6431  CA  PHE D 108      61.247 -22.344 -12.920  1.00 52.50           C  
ANISOU 6431  CA  PHE D 108    10650   4553   4745  -1751  -3289    369       C  
ATOM   6432  C   PHE D 108      62.536 -23.113 -12.621  1.00 55.27           C  
ANISOU 6432  C   PHE D 108    11231   4944   4824  -1705  -2767    150       C  
ATOM   6433  O   PHE D 108      63.081 -23.021 -11.525  1.00 54.29           O  
ANISOU 6433  O   PHE D 108    10773   4895   4961  -1621  -2357     99       O  
ATOM   6434  CB  PHE D 108      61.205 -20.971 -12.212  1.00 53.80           C  
ANISOU 6434  CB  PHE D 108    10388   4780   5273  -1594  -3084    543       C  
ATOM   6435  CG  PHE D 108      60.013 -20.107 -12.551  1.00 54.80           C  
ANISOU 6435  CG  PHE D 108    10278   4845   5699  -1576  -3570    773       C  
ATOM   6436  CD1 PHE D 108      59.876 -19.545 -13.813  1.00 58.07           C  
ANISOU 6436  CD1 PHE D 108    11122   5171   5771  -1590  -3964    929       C  
ATOM   6437  CD2 PHE D 108      59.035 -19.843 -11.604  1.00 56.33           C  
ANISOU 6437  CD2 PHE D 108     9830   5054   6519  -1520  -3616    849       C  
ATOM   6438  CE1 PHE D 108      58.765 -18.754 -14.131  1.00 58.75           C  
ANISOU 6438  CE1 PHE D 108    10972   5172   6177  -1552  -4480   1159       C  
ATOM   6439  CE2 PHE D 108      57.934 -19.037 -11.917  1.00 58.97           C  
ANISOU 6439  CE2 PHE D 108     9881   5317   7208  -1460  -4057   1073       C  
ATOM   6440  CZ  PHE D 108      57.805 -18.504 -13.180  1.00 57.06           C  
ANISOU 6440  CZ  PHE D 108    10045   4977   6660  -1478  -4525   1227       C  
ATOM   6441  N   GLY D 109      62.963 -23.912 -13.597  1.00 51.96           N  
ANISOU 6441  N   GLY D 109    11409   4447   3888  -1747  -2826     17       N  
ATOM   6442  CA  GLY D 109      64.136 -24.781 -13.532  1.00 52.03           C  
ANISOU 6442  CA  GLY D 109    11697   4454   3619  -1671  -2375   -200       C  
ATOM   6443  C   GLY D 109      65.412 -24.228 -12.927  1.00 55.91           C  
ANISOU 6443  C   GLY D 109    11999   5060   4183  -1507  -1757   -188       C  
ATOM   6444  O   GLY D 109      66.132 -24.959 -12.240  1.00 55.48           O  
ANISOU 6444  O   GLY D 109    11851   5013   4215  -1443  -1434   -347       O  
ATOM   6445  N   GLU D 110      65.707 -22.945 -13.177  1.00 51.87           N  
ANISOU 6445  N   GLU D 110    11430   4608   3670  -1447  -1634     15       N  
ATOM   6446  CA  GLU D 110      66.922 -22.314 -12.659  1.00 51.24           C  
ANISOU 6446  CA  GLU D 110    11148   4604   3716  -1335  -1114     61       C  
ATOM   6447  C   GLU D 110      66.672 -21.397 -11.440  1.00 52.74           C  
ANISOU 6447  C   GLU D 110    10783   4829   4428  -1315  -1109    160       C  
ATOM   6448  O   GLU D 110      67.534 -20.568 -11.111  1.00 52.56           O  
ANISOU 6448  O   GLU D 110    10612   4825   4533  -1258   -811    246       O  
ATOM   6449  CB  GLU D 110      67.676 -21.567 -13.788  1.00 52.71           C  
ANISOU 6449  CB  GLU D 110    11728   4793   3507  -1293   -874    221       C  
ATOM   6450  CG  GLU D 110      68.258 -22.445 -14.893  1.00 64.96           C  
ANISOU 6450  CG  GLU D 110    13892   6306   4486  -1244   -678     99       C  
ATOM   6451  CD  GLU D 110      69.121 -23.638 -14.504  1.00 90.84           C  
ANISOU 6451  CD  GLU D 110    17153   9586   7776  -1138   -302   -146       C  
ATOM   6452  OE1 GLU D 110      68.943 -24.712 -15.123  1.00 87.22           O  
ANISOU 6452  OE1 GLU D 110    17148   9033   6957  -1120   -408   -342       O  
ATOM   6453  OE2 GLU D 110      69.974 -23.505 -13.595  1.00 83.26           O  
ANISOU 6453  OE2 GLU D 110    15754   8690   7192  -1068     55   -144       O  
ATOM   6454  N   ARG D 111      65.505 -21.546 -10.768  1.00 46.04           N  
ANISOU 6454  N   ARG D 111     9636   3968   3890  -1362  -1424    149       N  
ATOM   6455  CA  ARG D 111      65.172 -20.703  -9.627  1.00 44.36           C  
ANISOU 6455  CA  ARG D 111     8977   3764   4115  -1300  -1385    220       C  
ATOM   6456  C   ARG D 111      65.535 -21.328  -8.270  1.00 46.95           C  
ANISOU 6456  C   ARG D 111     9050   4109   4679  -1265  -1145     64       C  
ATOM   6457  O   ARG D 111      66.448 -20.833  -7.621  1.00 45.92           O  
ANISOU 6457  O   ARG D 111     8824   3974   4649  -1191   -889     54       O  
ATOM   6458  CB  ARG D 111      63.700 -20.237  -9.663  1.00 41.35           C  
ANISOU 6458  CB  ARG D 111     8378   3351   3983  -1319  -1782    351       C  
ATOM   6459  CG  ARG D 111      63.247 -19.547  -8.360  1.00 41.85           C  
ANISOU 6459  CG  ARG D 111     7998   3407   4497  -1207  -1670    381       C  
ATOM   6460  CD  ARG D 111      61.865 -18.945  -8.430  1.00 46.25           C  
ANISOU 6460  CD  ARG D 111     8277   3925   5369  -1165  -1989    537       C  
ATOM   6461  NE  ARG D 111      60.797 -19.943  -8.455  1.00 49.47           N  
ANISOU 6461  NE  ARG D 111     8492   4351   5952  -1283  -2243    522       N  
ATOM   6462  CZ  ARG D 111      59.517 -19.662  -8.247  1.00 63.60           C  
ANISOU 6462  CZ  ARG D 111     9886   6117   8161  -1251  -2480    656       C  
ATOM   6463  NH1 ARG D 111      59.137 -18.420  -7.978  1.00 53.35           N  
ANISOU 6463  NH1 ARG D 111     8379   4771   7119  -1063  -2479    792       N  
ATOM   6464  NH2 ARG D 111      58.605 -20.621  -8.304  1.00 56.31           N  
ANISOU 6464  NH2 ARG D 111     8752   5196   7450  -1407  -2723    666       N  
ATOM   6465  N   LEU D 112      64.815 -22.388  -7.853  1.00 44.13           N  
ANISOU 6465  N   LEU D 112     8605   3745   4415  -1335  -1267    -34       N  
ATOM   6466  CA  LEU D 112      64.877 -23.091  -6.560  1.00 43.74           C  
ANISOU 6466  CA  LEU D 112     8363   3689   4567  -1322  -1098   -146       C  
ATOM   6467  C   LEU D 112      66.261 -23.226  -5.922  1.00 48.07           C  
ANISOU 6467  C   LEU D 112     8966   4230   5070  -1233   -789   -250       C  
ATOM   6468  O   LEU D 112      66.393 -22.987  -4.720  1.00 46.79           O  
ANISOU 6468  O   LEU D 112     8633   4047   5098  -1168   -666   -269       O  
ATOM   6469  CB  LEU D 112      64.220 -24.502  -6.662  1.00 43.14           C  
ANISOU 6469  CB  LEU D 112     8352   3568   4471  -1464  -1272   -232       C  
ATOM   6470  CG  LEU D 112      64.038 -25.298  -5.341  1.00 47.49           C  
ANISOU 6470  CG  LEU D 112     8722   4086   5235  -1486  -1126   -293       C  
ATOM   6471  CD1 LEU D 112      63.105 -24.579  -4.347  1.00 48.00           C  
ANISOU 6471  CD1 LEU D 112     8412   4182   5643  -1445  -1066   -166       C  
ATOM   6472  CD2 LEU D 112      63.597 -26.730  -5.595  1.00 47.92           C  
ANISOU 6472  CD2 LEU D 112     8917   4048   5244  -1653  -1301   -372       C  
ATOM   6473  N   CYS D 113      67.265 -23.634  -6.700  1.00 45.34           N  
ANISOU 6473  N   CYS D 113     8863   3884   4480  -1217   -672   -313       N  
ATOM   6474  CA  CYS D 113      68.589 -23.937  -6.177  1.00 46.05           C  
ANISOU 6474  CA  CYS D 113     8939   3954   4602  -1127   -412   -400       C  
ATOM   6475  C   CYS D 113      69.438 -22.714  -5.845  1.00 47.70           C  
ANISOU 6475  C   CYS D 113     8989   4167   4967  -1068   -272   -300       C  
ATOM   6476  O   CYS D 113      70.508 -22.882  -5.250  1.00 47.56           O  
ANISOU 6476  O   CYS D 113     8881   4114   5074  -1008   -127   -351       O  
ATOM   6477  CB  CYS D 113      69.318 -24.896  -7.108  1.00 47.83           C  
ANISOU 6477  CB  CYS D 113     9444   4162   4566  -1094   -283   -505       C  
ATOM   6478  SG  CYS D 113      68.369 -26.380  -7.535  1.00 52.55           S  
ANISOU 6478  SG  CYS D 113    10318   4676   4974  -1190   -523   -648       S  
ATOM   6479  N   ILE D 114      68.965 -21.492  -6.188  1.00 42.35           N  
ANISOU 6479  N   ILE D 114     8271   3497   4323  -1091   -362   -150       N  
ATOM   6480  CA  ILE D 114      69.625 -20.235  -5.835  1.00 41.19           C  
ANISOU 6480  CA  ILE D 114     7994   3298   4359  -1067   -290    -44       C  
ATOM   6481  C   ILE D 114      69.451 -20.049  -4.305  1.00 44.31           C  
ANISOU 6481  C   ILE D 114     8231   3615   4988  -1012   -349   -124       C  
ATOM   6482  O   ILE D 114      70.418 -19.746  -3.606  1.00 44.97           O  
ANISOU 6482  O   ILE D 114     8241   3621   5225   -992   -302   -145       O  
ATOM   6483  CB  ILE D 114      69.024 -19.016  -6.606  1.00 44.22           C  
ANISOU 6483  CB  ILE D 114     8432   3662   4709  -1093   -411    143       C  
ATOM   6484  CG1 ILE D 114      69.160 -19.157  -8.138  1.00 44.58           C  
ANISOU 6484  CG1 ILE D 114     8751   3761   4425  -1145   -373    240       C  
ATOM   6485  CG2 ILE D 114      69.608 -17.665  -6.105  1.00 44.00           C  
ANISOU 6485  CG2 ILE D 114     8289   3516   4914  -1086   -381    250       C  
ATOM   6486  CD1 ILE D 114      68.415 -18.043  -8.934  1.00 51.28           C  
ANISOU 6486  CD1 ILE D 114     9714   4566   5205  -1170   -579    446       C  
ATOM   6487  N   ASP D 115      68.218 -20.255  -3.804  1.00 38.20           N  
ANISOU 6487  N   ASP D 115     7419   2850   4243   -991   -454   -158       N  
ATOM   6488  CA  ASP D 115      67.849 -20.063  -2.401  1.00 36.76           C  
ANISOU 6488  CA  ASP D 115     7170   2593   4203   -912   -446   -222       C  
ATOM   6489  C   ASP D 115      66.803 -21.144  -2.013  1.00 39.16           C  
ANISOU 6489  C   ASP D 115     7440   2949   4491   -933   -440   -271       C  
ATOM   6490  O   ASP D 115      65.617 -20.800  -1.876  1.00 37.92           O  
ANISOU 6490  O   ASP D 115     7156   2804   4449   -902   -467   -205       O  
ATOM   6491  CB  ASP D 115      67.245 -18.639  -2.282  1.00 37.63           C  
ANISOU 6491  CB  ASP D 115     7226   2626   4447   -833   -506   -128       C  
ATOM   6492  CG  ASP D 115      67.255 -18.006  -0.905  1.00 43.99           C  
ANISOU 6492  CG  ASP D 115     8074   3289   5353   -711   -466   -205       C  
ATOM   6493  OD1 ASP D 115      67.218 -18.759   0.103  1.00 45.13           O  
ANISOU 6493  OD1 ASP D 115     8279   3421   5445   -678   -386   -313       O  
ATOM   6494  OD2 ASP D 115      67.280 -16.757  -0.830  1.00 44.64           O  
ANISOU 6494  OD2 ASP D 115     8186   3241   5534   -644   -523   -157       O  
ATOM   6495  N   PRO D 116      67.193 -22.454  -1.858  1.00 35.03           N  
ANISOU 6495  N   PRO D 116     7000   2435   3872   -987   -404   -365       N  
ATOM   6496  CA  PRO D 116      66.189 -23.492  -1.618  1.00 33.95           C  
ANISOU 6496  CA  PRO D 116     6834   2315   3749  -1060   -418   -375       C  
ATOM   6497  C   PRO D 116      65.235 -23.268  -0.460  1.00 37.42           C  
ANISOU 6497  C   PRO D 116     7165   2728   4327  -1006   -305   -336       C  
ATOM   6498  O   PRO D 116      64.049 -23.538  -0.631  1.00 36.57           O  
ANISOU 6498  O   PRO D 116     6886   2660   4351  -1073   -326   -253       O  
ATOM   6499  CB  PRO D 116      67.032 -24.758  -1.417  1.00 36.40           C  
ANISOU 6499  CB  PRO D 116     7307   2576   3947  -1088   -388   -487       C  
ATOM   6500  CG  PRO D 116      68.251 -24.516  -2.187  1.00 40.78           C  
ANISOU 6500  CG  PRO D 116     7928   3142   4423  -1045   -371   -519       C  
ATOM   6501  CD  PRO D 116      68.534 -23.061  -2.003  1.00 36.56           C  
ANISOU 6501  CD  PRO D 116     7297   2606   3990   -983   -356   -445       C  
ATOM   6502  N   ASN D 117      65.733 -22.771   0.690  1.00 34.41           N  
ANISOU 6502  N   ASN D 117     6888   2263   3922   -884   -190   -388       N  
ATOM   6503  CA  ASN D 117      64.942 -22.607   1.899  1.00 34.62           C  
ANISOU 6503  CA  ASN D 117     6923   2241   3991   -792      0   -370       C  
ATOM   6504  C   ASN D 117      63.936 -21.470   1.821  1.00 40.88           C  
ANISOU 6504  C   ASN D 117     7521   3049   4961   -678     73   -285       C  
ATOM   6505  O   ASN D 117      62.912 -21.541   2.508  1.00 42.24           O  
ANISOU 6505  O   ASN D 117     7586   3224   5240   -613    293   -227       O  
ATOM   6506  CB  ASN D 117      65.833 -22.514   3.159  1.00 32.46           C  
ANISOU 6506  CB  ASN D 117     6946   1832   3555   -691     47   -472       C  
ATOM   6507  CG  ASN D 117      66.433 -23.865   3.528  1.00 50.73           C  
ANISOU 6507  CG  ASN D 117     9426   4106   5744   -773     10   -518       C  
ATOM   6508  OD1 ASN D 117      65.797 -24.927   3.433  1.00 45.05           O  
ANISOU 6508  OD1 ASN D 117     8659   3420   5038   -882     77   -467       O  
ATOM   6509  ND2 ASN D 117      67.673 -23.866   3.955  1.00 38.99           N  
ANISOU 6509  ND2 ASN D 117     8127   2515   4172   -728   -133   -601       N  
ATOM   6510  N   THR D 118      64.184 -20.457   0.975  1.00 36.49           N  
ANISOU 6510  N   THR D 118     6910   2494   4462   -644    -83   -256       N  
ATOM   6511  CA  THR D 118      63.248 -19.349   0.801  1.00 36.12           C  
ANISOU 6511  CA  THR D 118     6681   2429   4615   -510    -64   -164       C  
ATOM   6512  C   THR D 118      62.298 -19.668  -0.352  1.00 41.98           C  
ANISOU 6512  C   THR D 118     7139   3283   5529   -620   -233    -27       C  
ATOM   6513  O   THR D 118      61.099 -19.431  -0.236  1.00 42.43           O  
ANISOU 6513  O   THR D 118     6918   3355   5847   -541   -169     77       O  
ATOM   6514  CB  THR D 118      64.007 -18.013   0.530  1.00 37.33           C  
ANISOU 6514  CB  THR D 118     6966   2467   4750   -426   -189   -177       C  
ATOM   6515  OG1 THR D 118      64.962 -17.771   1.564  1.00 39.49           O  
ANISOU 6515  OG1 THR D 118     7517   2602   4887   -364   -136   -310       O  
ATOM   6516  CG2 THR D 118      63.086 -16.814   0.376  1.00 31.30           C  
ANISOU 6516  CG2 THR D 118     6057   1633   4201   -252   -194    -85       C  
ATOM   6517  N   PHE D 119      62.841 -20.164  -1.473  1.00 38.88           N  
ANISOU 6517  N   PHE D 119     6828   2949   4996   -787   -457    -21       N  
ATOM   6518  CA  PHE D 119      62.077 -20.368  -2.696  1.00 39.71           C  
ANISOU 6518  CA  PHE D 119     6789   3118   5183   -900   -724     95       C  
ATOM   6519  C   PHE D 119      61.098 -21.540  -2.613  1.00 48.80           C  
ANISOU 6519  C   PHE D 119     7738   4312   6490  -1043   -768    134       C  
ATOM   6520  O   PHE D 119      60.105 -21.548  -3.354  1.00 49.00           O  
ANISOU 6520  O   PHE D 119     7545   4358   6717  -1118  -1027    260       O  
ATOM   6521  CB  PHE D 119      63.014 -20.461  -3.913  1.00 40.93           C  
ANISOU 6521  CB  PHE D 119     7205   3290   5056  -1004   -906     79       C  
ATOM   6522  CG  PHE D 119      63.811 -19.206  -4.245  1.00 41.26           C  
ANISOU 6522  CG  PHE D 119     7379   3277   5021   -916   -897    123       C  
ATOM   6523  CD1 PHE D 119      63.556 -18.002  -3.601  1.00 44.54           C  
ANISOU 6523  CD1 PHE D 119     7696   3599   5628   -752   -834    169       C  
ATOM   6524  CD2 PHE D 119      64.822 -19.237  -5.188  1.00 43.12           C  
ANISOU 6524  CD2 PHE D 119     7852   3528   5005   -994   -921    128       C  
ATOM   6525  CE1 PHE D 119      64.268 -16.844  -3.929  1.00 45.49           C  
ANISOU 6525  CE1 PHE D 119     7950   3621   5712   -707   -866    230       C  
ATOM   6526  CE2 PHE D 119      65.531 -18.076  -5.522  1.00 46.40           C  
ANISOU 6526  CE2 PHE D 119     8359   3875   5394   -954   -895    218       C  
ATOM   6527  CZ  PHE D 119      65.245 -16.886  -4.896  1.00 44.30           C  
ANISOU 6527  CZ  PHE D 119     7991   3496   5344   -830   -899    273       C  
ATOM   6528  N   ALA D 120      61.318 -22.472  -1.651  1.00 47.72           N  
ANISOU 6528  N   ALA D 120     7664   4164   6303  -1087   -542     51       N  
ATOM   6529  CA  ALA D 120      60.449 -23.617  -1.387  1.00 47.93           C  
ANISOU 6529  CA  ALA D 120     7511   4195   6505  -1251   -530    111       C  
ATOM   6530  C   ALA D 120      59.087 -23.150  -0.870  1.00 53.63           C  
ANISOU 6530  C   ALA D 120     7797   4937   7643  -1174   -380    276       C  
ATOM   6531  O   ALA D 120      58.106 -23.892  -0.963  1.00 53.73           O  
ANISOU 6531  O   ALA D 120     7517   4955   7942  -1344   -446    399       O  
ATOM   6532  CB  ALA D 120      61.089 -24.507  -0.350  1.00 48.67           C  
ANISOU 6532  CB  ALA D 120     7831   4239   6422  -1278   -290     11       C  
ATOM   6533  N   GLY D 121      59.060 -21.941  -0.303  1.00 50.59           N  
ANISOU 6533  N   GLY D 121     7367   4537   7318   -914   -168    282       N  
ATOM   6534  CA  GLY D 121      57.863 -21.320   0.241  1.00 50.87           C  
ANISOU 6534  CA  GLY D 121     7001   4575   7753   -746     61    423       C  
ATOM   6535  C   GLY D 121      56.929 -20.783  -0.822  1.00 56.63           C  
ANISOU 6535  C   GLY D 121     7345   5326   8848   -748   -291    586       C  
ATOM   6536  O   GLY D 121      55.817 -20.362  -0.495  1.00 56.97           O  
ANISOU 6536  O   GLY D 121     6940   5369   9335   -610   -138    735       O  
ATOM   6537  N   TYR D 122      57.373 -20.782  -2.100  1.00 53.47           N  
ANISOU 6537  N   TYR D 122     7126   4928   8261   -887   -757    570       N  
ATOM   6538  CA  TYR D 122      56.589 -20.291  -3.238  1.00 53.10           C  
ANISOU 6538  CA  TYR D 122     6835   4871   8468   -908  -1209    729       C  
ATOM   6539  C   TYR D 122      55.895 -21.454  -3.971  1.00 60.52           C  
ANISOU 6539  C   TYR D 122     7587   5824   9583  -1218  -1602    819       C  
ATOM   6540  O   TYR D 122      54.928 -21.237  -4.709  1.00 61.00           O  
ANISOU 6540  O   TYR D 122     7307   5861  10008  -1260  -2000    994       O  
ATOM   6541  CB  TYR D 122      57.488 -19.557  -4.259  1.00 52.57           C  
ANISOU 6541  CB  TYR D 122     7184   4770   8021   -886  -1494    679       C  
ATOM   6542  CG  TYR D 122      58.427 -18.477  -3.751  1.00 51.95           C  
ANISOU 6542  CG  TYR D 122     7369   4634   7735   -665  -1224    586       C  
ATOM   6543  CD1 TYR D 122      58.116 -17.722  -2.620  1.00 53.70           C  
ANISOU 6543  CD1 TYR D 122     7434   4797   8173   -404   -865    573       C  
ATOM   6544  CD2 TYR D 122      59.571 -18.133  -4.466  1.00 51.42           C  
ANISOU 6544  CD2 TYR D 122     7713   4542   7281   -713  -1343    529       C  
ATOM   6545  CE1 TYR D 122      58.954 -16.699  -2.180  1.00 53.13           C  
ANISOU 6545  CE1 TYR D 122     7651   4615   7921   -224   -706    478       C  
ATOM   6546  CE2 TYR D 122      60.398 -17.093  -4.053  1.00 51.45           C  
ANISOU 6546  CE2 TYR D 122     7915   4456   7176   -556  -1163    477       C  
ATOM   6547  CZ  TYR D 122      60.104 -16.398  -2.893  1.00 57.21           C  
ANISOU 6547  CZ  TYR D 122     8525   5101   8111   -325   -884    438       C  
ATOM   6548  OH  TYR D 122      60.946 -15.399  -2.469  1.00 56.67           O  
ANISOU 6548  OH  TYR D 122     8707   4894   7931   -198   -776    367       O  
ATOM   6549  N   LEU D 123      56.410 -22.680  -3.769  1.00 57.46           N  
ANISOU 6549  N   LEU D 123     7443   5439   8951  -1435  -1538    701       N  
ATOM   6550  CA  LEU D 123      56.010 -23.917  -4.438  1.00 56.80           C  
ANISOU 6550  CA  LEU D 123     7353   5309   8921  -1760  -1923    724       C  
ATOM   6551  C   LEU D 123      54.715 -24.559  -3.952  1.00 64.93           C  
ANISOU 6551  C   LEU D 123     7811   6319  10540  -1926  -1904    913       C  
ATOM   6552  O   LEU D 123      54.484 -24.670  -2.742  1.00 65.03           O  
ANISOU 6552  O   LEU D 123     7598   6365  10745  -1844  -1378    960       O  
ATOM   6553  CB  LEU D 123      57.156 -24.950  -4.358  1.00 55.63           C  
ANISOU 6553  CB  LEU D 123     7725   5126   8285  -1884  -1821    511       C  
ATOM   6554  CG  LEU D 123      58.563 -24.478  -4.731  1.00 57.99           C  
ANISOU 6554  CG  LEU D 123     8533   5447   8055  -1738  -1736    336       C  
ATOM   6555  CD1 LEU D 123      59.546 -25.604  -4.642  1.00 57.51           C  
ANISOU 6555  CD1 LEU D 123     8870   5336   7645  -1837  -1638    152       C  
ATOM   6556  CD2 LEU D 123      58.596 -23.843  -6.109  1.00 58.27           C  
ANISOU 6556  CD2 LEU D 123     8761   5472   7907  -1733  -2149    371       C  
ATOM   6557  N   GLU D 124      53.908 -25.046  -4.924  1.00 63.54           N  
ANISOU 6557  N   GLU D 124     7449   6068  10627  -2185  -2496   1027       N  
ATOM   6558  CA  GLU D 124      52.640 -25.754  -4.716  1.00 64.15           C  
ANISOU 6558  CA  GLU D 124     6935   6091  11349  -2434  -2631   1243       C  
ATOM   6559  C   GLU D 124      52.841 -27.278  -4.860  1.00 68.79           C  
ANISOU 6559  C   GLU D 124     7818   6548  11769  -2800  -2820   1151       C  
ATOM   6560  O   GLU D 124      52.102 -28.047  -4.249  1.00 68.44           O  
ANISOU 6560  O   GLU D 124     7385   6452  12167  -3013  -2668   1303       O  
ATOM   6561  CB  GLU D 124      51.573 -25.275  -5.722  1.00 65.80           C  
ANISOU 6561  CB  GLU D 124     6725   6247  12031  -2509  -3299   1446       C  
ATOM   6562  CG  GLU D 124      51.086 -23.849  -5.504  1.00 81.41           C  
ANISOU 6562  CG  GLU D 124     8270   8303  14357  -2149  -3149   1595       C  
ATOM   6563  CD  GLU D 124      49.958 -23.624  -4.509  1.00108.94           C  
ANISOU 6563  CD  GLU D 124    10973  11852  18569  -2000  -2619   1816       C  
ATOM   6564  OE1 GLU D 124      49.470 -24.606  -3.900  1.00 97.31           O  
ANISOU 6564  OE1 GLU D 124     9143  10361  17469  -2243  -2427   1933       O  
ATOM   6565  OE2 GLU D 124      49.558 -22.448  -4.344  1.00104.60           O  
ANISOU 6565  OE2 GLU D 124    10178  11346  18219  -1628  -2372   1881       O  
ATOM   6566  N   THR D 125      53.839 -27.702  -5.671  1.00 65.43           N  
ANISOU 6566  N   THR D 125     8089   6049  10722  -2863  -3124    914       N  
ATOM   6567  CA  THR D 125      54.160 -29.107  -5.954  1.00 64.77           C  
ANISOU 6567  CA  THR D 125     8417   5792  10400  -3157  -3354    775       C  
ATOM   6568  C   THR D 125      55.161 -29.684  -4.941  1.00 67.81           C  
ANISOU 6568  C   THR D 125     9127   6188  10450  -3068  -2769    621       C  
ATOM   6569  O   THR D 125      56.350 -29.360  -4.961  1.00 66.90           O  
ANISOU 6569  O   THR D 125     9465   6134   9818  -2839  -2544    424       O  
ATOM   6570  CB  THR D 125      54.599 -29.275  -7.427  1.00 72.04           C  
ANISOU 6570  CB  THR D 125     9940   6595  10835  -3234  -3974    603       C  
ATOM   6571  OG1 THR D 125      53.521 -28.872  -8.277  1.00 72.77           O  
ANISOU 6571  OG1 THR D 125     9722   6637  11289  -3357  -4608    784       O  
ATOM   6572  CG2 THR D 125      55.002 -30.698  -7.766  1.00 70.10           C  
ANISOU 6572  CG2 THR D 125    10207   6126  10303  -3488  -4210    417       C  
ATOM   6573  N   TRP D 126      54.654 -30.569  -4.077  1.00 65.12           N  
ANISOU 6573  N   TRP D 126     8539   5763  10439  -3272  -2558    738       N  
ATOM   6574  CA  TRP D 126      55.421 -31.262  -3.040  1.00 64.64           C  
ANISOU 6574  CA  TRP D 126     8769   5664  10127  -3232  -2072    647       C  
ATOM   6575  C   TRP D 126      55.123 -32.748  -3.073  1.00 71.69           C  
ANISOU 6575  C   TRP D 126     9788   6306  11144  -3604  -2312    667       C  
ATOM   6576  O   TRP D 126      54.283 -33.207  -3.852  1.00 72.50           O  
ANISOU 6576  O   TRP D 126     9749   6261  11536  -3905  -2869    740       O  
ATOM   6577  CB  TRP D 126      55.102 -30.666  -1.649  1.00 62.32           C  
ANISOU 6577  CB  TRP D 126     8085   5512  10082  -3049  -1410    819       C  
ATOM   6578  CG  TRP D 126      55.757 -29.329  -1.432  1.00 62.45           C  
ANISOU 6578  CG  TRP D 126     8197   5706   9827  -2654  -1122    719       C  
ATOM   6579  CD1 TRP D 126      55.321 -28.117  -1.882  1.00 64.95           C  
ANISOU 6579  CD1 TRP D 126     8213   6139  10327  -2473  -1215    788       C  
ATOM   6580  CD2 TRP D 126      57.021 -29.090  -0.793  1.00 62.07           C  
ANISOU 6580  CD2 TRP D 126     8605   5691   9287  -2410   -783    531       C  
ATOM   6581  NE1 TRP D 126      56.219 -27.133  -1.538  1.00 63.84           N  
ANISOU 6581  NE1 TRP D 126     8331   6090   9834  -2147   -928    653       N  
ATOM   6582  CE2 TRP D 126      57.280 -27.705  -0.884  1.00 65.19           C  
ANISOU 6582  CE2 TRP D 126     8954   6217   9599  -2115   -682    493       C  
ATOM   6583  CE3 TRP D 126      57.951 -29.911  -0.126  1.00 63.08           C  
ANISOU 6583  CE3 TRP D 126     9166   5725   9075  -2413   -591    407       C  
ATOM   6584  CZ2 TRP D 126      58.428 -27.123  -0.333  1.00 64.14           C  
ANISOU 6584  CZ2 TRP D 126     9175   6118   9079  -1862   -418    334       C  
ATOM   6585  CZ3 TRP D 126      59.098 -29.333   0.397  1.00 63.90           C  
ANISOU 6585  CZ3 TRP D 126     9599   5879   8801  -2139   -353    252       C  
ATOM   6586  CH2 TRP D 126      59.326 -27.957   0.291  1.00 64.15           C  
ANISOU 6586  CH2 TRP D 126     9558   6037   8778  -1886   -277    217       C  
ATOM   6587  N   GLY D 127      55.827 -33.491  -2.239  1.00 69.25           N  
ANISOU 6587  N   GLY D 127     9778   5916  10619  -3587  -1945    606       N  
ATOM   6588  CA  GLY D 127      55.601 -34.915  -2.075  1.00 69.16           C  
ANISOU 6588  CA  GLY D 127     9916   5629  10733  -3923  -2096    648       C  
ATOM   6589  C   GLY D 127      54.875 -35.184  -0.773  1.00 73.02           C  
ANISOU 6589  C   GLY D 127     9996   6117  11631  -4051  -1604    947       C  
ATOM   6590  O   GLY D 127      54.715 -34.282   0.061  1.00 72.08           O  
ANISOU 6590  O   GLY D 127     9590   6214  11585  -3813  -1083   1065       O  
ATOM   6591  N   GLN D 128      54.438 -36.437  -0.591  1.00 69.54           N  
ANISOU 6591  N   GLN D 128     9574   5406  11441  -4427  -1746   1073       N  
ATOM   6592  CA  GLN D 128      53.741 -36.899   0.609  1.00 69.68           C  
ANISOU 6592  CA  GLN D 128     9262   5371  11842  -4615  -1263   1398       C  
ATOM   6593  C   GLN D 128      54.742 -37.093   1.765  1.00 72.93           C  
ANISOU 6593  C   GLN D 128    10173   5780  11755  -4368   -719   1327       C  
ATOM   6594  O   GLN D 128      54.338 -37.098   2.936  1.00 72.63           O  
ANISOU 6594  O   GLN D 128     9955   5782  11860  -4371   -144   1580       O  
ATOM   6595  CB  GLN D 128      53.038 -38.239   0.318  1.00 71.66           C  
ANISOU 6595  CB  GLN D 128     9444   5273  12510  -5141  -1676   1555       C  
ATOM   6596  CG  GLN D 128      51.962 -38.167  -0.760  1.00 95.58           C  
ANISOU 6596  CG  GLN D 128    11962   8247  16107  -5451  -2312   1664       C  
ATOM   6597  CD  GLN D 128      50.603 -37.899  -0.170  1.00116.43           C  
ANISOU 6597  CD  GLN D 128    13695  10983  19558  -5657  -2001   2105       C  
ATOM   6598  OE1 GLN D 128      50.289 -36.779   0.261  1.00112.28           O  
ANISOU 6598  OE1 GLN D 128    12713  10764  19185  -5360  -1545   2220       O  
ATOM   6599  NE2 GLN D 128      49.768 -38.928  -0.138  1.00105.56           N  
ANISOU 6599  NE2 GLN D 128    12030   9325  18753  -6168  -2226   2369       N  
ATOM   6600  N   GLY D 129      56.017 -37.302   1.408  1.00 68.30           N  
ANISOU 6600  N   GLY D 129    10218   5125  10608  -4161   -918   1000       N  
ATOM   6601  CA  GLY D 129      57.112 -37.545   2.341  1.00 67.75           C  
ANISOU 6601  CA  GLY D 129    10659   5012  10070  -3918   -578    900       C  
ATOM   6602  C   GLY D 129      57.415 -39.012   2.583  1.00 70.40           C  
ANISOU 6602  C   GLY D 129    11430   4986  10334  -4140   -716    912       C  
ATOM   6603  O   GLY D 129      56.570 -39.883   2.327  1.00 68.24           O  
ANISOU 6603  O   GLY D 129    11002   4480  10444  -4545   -948   1080       O  
ATOM   6604  N   THR D 130      58.647 -39.290   3.074  1.00 67.18           N  
ANISOU 6604  N   THR D 130    11565   4496   9464  -3876   -614    740       N  
ATOM   6605  CA  THR D 130      59.102 -40.646   3.401  1.00 66.47           C  
ANISOU 6605  CA  THR D 130    11956   4035   9266  -4006   -732    743       C  
ATOM   6606  C   THR D 130      59.939 -40.623   4.687  1.00 68.86           C  
ANISOU 6606  C   THR D 130    12616   4334   9214  -3737   -356    785       C  
ATOM   6607  O   THR D 130      60.935 -39.898   4.772  1.00 67.02           O  
ANISOU 6607  O   THR D 130    12539   4269   8655  -3365   -308    581       O  
ATOM   6608  CB  THR D 130      59.774 -41.360   2.193  1.00 72.95           C  
ANISOU 6608  CB  THR D 130    13162   4617   9939  -3999  -1270    427       C  
ATOM   6609  OG1 THR D 130      59.766 -42.770   2.419  1.00 74.84           O  
ANISOU 6609  OG1 THR D 130    13757   4427  10250  -4243  -1438    497       O  
ATOM   6610  CG2 THR D 130      61.201 -40.859   1.872  1.00 68.88           C  
ANISOU 6610  CG2 THR D 130    12970   4219   8982  -3539  -1285     99       C  
ATOM   6611  N   GLN D 131      59.498 -41.403   5.698  1.00 65.48           N  
ANISOU 6611  N   GLN D 131    12322   3693   8863  -3949   -110   1076       N  
ATOM   6612  CA  GLN D 131      60.170 -41.510   6.994  1.00 65.28           C  
ANISOU 6612  CA  GLN D 131    12728   3601   8476  -3743    201   1168       C  
ATOM   6613  C   GLN D 131      61.503 -42.249   6.840  1.00 69.66           C  
ANISOU 6613  C   GLN D 131    13840   3897   8730  -3530   -158    922       C  
ATOM   6614  O   GLN D 131      61.551 -43.315   6.225  1.00 70.00           O  
ANISOU 6614  O   GLN D 131    14072   3625   8899  -3707   -504    858       O  
ATOM   6615  CB  GLN D 131      59.250 -42.192   8.041  1.00 66.52           C  
ANISOU 6615  CB  GLN D 131    12905   3573   8796  -4066    578   1589       C  
ATOM   6616  CG  GLN D 131      59.808 -42.300   9.466  1.00 70.22           C  
ANISOU 6616  CG  GLN D 131    13898   3954   8830  -3877    929   1740       C  
ATOM   6617  CD  GLN D 131      60.152 -40.966  10.085  1.00 87.82           C  
ANISOU 6617  CD  GLN D 131    16117   6514  10736  -3505   1265   1661       C  
ATOM   6618  OE1 GLN D 131      59.279 -40.196  10.503  1.00 83.60           O  
ANISOU 6618  OE1 GLN D 131    15233   6207  10325  -3527   1739   1837       O  
ATOM   6619  NE2 GLN D 131      61.441 -40.668  10.161  1.00 76.25           N  
ANISOU 6619  NE2 GLN D 131    15032   5054   8885  -3148   1017   1396       N  
ATOM   6620  N   VAL D 132      62.581 -41.643   7.358  1.00 65.63           N  
ANISOU 6620  N   VAL D 132    13571   3504   7861  -3139    -99    778       N  
ATOM   6621  CA  VAL D 132      63.944 -42.178   7.371  1.00 65.17           C  
ANISOU 6621  CA  VAL D 132    13962   3233   7566  -2863   -394    575       C  
ATOM   6622  C   VAL D 132      64.350 -42.187   8.844  1.00 71.96           C  
ANISOU 6622  C   VAL D 132    15211   4008   8124  -2725   -192    761       C  
ATOM   6623  O   VAL D 132      64.408 -41.122   9.449  1.00 72.66           O  
ANISOU 6623  O   VAL D 132    15226   4352   8031  -2563     59    786       O  
ATOM   6624  CB  VAL D 132      64.904 -41.326   6.490  1.00 67.86           C  
ANISOU 6624  CB  VAL D 132    14152   3802   7828  -2530   -577    235       C  
ATOM   6625  CG1 VAL D 132      66.375 -41.627   6.789  1.00 67.18           C  
ANISOU 6625  CG1 VAL D 132    14426   3553   7547  -2183   -782     83       C  
ATOM   6626  CG2 VAL D 132      64.601 -41.519   5.009  1.00 67.45           C  
ANISOU 6626  CG2 VAL D 132    13902   3753   7973  -2651   -819     46       C  
ATOM   6627  N   THR D 133      64.537 -43.381   9.437  1.00 70.01           N  
ANISOU 6627  N   THR D 133    15423   3371   7805  -2806   -307    906       N  
ATOM   6628  CA  THR D 133      64.926 -43.550  10.844  1.00 70.18           C  
ANISOU 6628  CA  THR D 133    15941   3239   7485  -2693   -183   1112       C  
ATOM   6629  C   THR D 133      66.314 -44.176  10.909  1.00 74.02           C  
ANISOU 6629  C   THR D 133    16842   3442   7841  -2395   -626    952       C  
ATOM   6630  O   THR D 133      66.570 -45.176  10.244  1.00 73.37           O  
ANISOU 6630  O   THR D 133    16866   3065   7946  -2440   -913    866       O  
ATOM   6631  CB  THR D 133      63.879 -44.371  11.648  1.00 78.43           C  
ANISOU 6631  CB  THR D 133    17190   4056   8555  -3066    133   1523       C  
ATOM   6632  OG1 THR D 133      62.570 -43.847  11.414  1.00 82.56           O  
ANISOU 6632  OG1 THR D 133    17193   4845   9332  -3333    540   1672       O  
ATOM   6633  CG2 THR D 133      64.148 -44.356  13.152  1.00 74.04           C  
ANISOU 6633  CG2 THR D 133    17214   3374   7543  -2945    337   1762       C  
ATOM   6634  N   VAL D 134      67.214 -43.568  11.691  1.00 70.74           N  
ANISOU 6634  N   VAL D 134    16653   3093   7133  -2078   -706    906       N  
ATOM   6635  CA  VAL D 134      68.583 -44.047  11.872  1.00 69.88           C  
ANISOU 6635  CA  VAL D 134    16867   2726   6957  -1759  -1154    787       C  
ATOM   6636  C   VAL D 134      68.757 -44.363  13.348  1.00 74.73           C  
ANISOU 6636  C   VAL D 134    18105   3095   7194  -1723  -1178   1061       C  
ATOM   6637  O   VAL D 134      68.720 -43.460  14.182  1.00 75.52           O  
ANISOU 6637  O   VAL D 134    18340   3375   6978  -1651  -1004   1132       O  
ATOM   6638  CB  VAL D 134      69.656 -43.068  11.309  1.00 72.63           C  
ANISOU 6638  CB  VAL D 134    16880   3329   7386  -1413  -1364    475       C  
ATOM   6639  CG1 VAL D 134      71.040 -43.701  11.331  1.00 72.10           C  
ANISOU 6639  CG1 VAL D 134    17013   2973   7409  -1089  -1824    364       C  
ATOM   6640  CG2 VAL D 134      69.308 -42.620   9.891  1.00 72.28           C  
ANISOU 6640  CG2 VAL D 134    16284   3559   7619  -1479  -1251    250       C  
ATOM   6641  N   SER D 135      68.868 -45.653  13.672  1.00 73.03           N  
ANISOU 6641  N   SER D 135    18332   2438   6979  -1784  -1385   1225       N  
ATOM   6642  CA  SER D 135      68.991 -46.157  15.043  1.00108.31           C  
ANISOU 6642  CA  SER D 135    23500   6594  11060  -1775  -1445   1532       C  
ATOM   6643  C   SER D 135      69.888 -47.383  15.100  1.00131.46           C  
ANISOU 6643  C   SER D 135    26829   9030  14092  -1621  -1947   1556       C  
ATOM   6644  O   SER D 135      69.990 -48.108  14.116  1.00 92.08           O  
ANISOU 6644  O   SER D 135    21628   3883   9474  -1640  -2101   1403       O  
ATOM   6645  CB  SER D 135      67.616 -46.500  15.609  1.00111.90           C  
ANISOU 6645  CB  SER D 135    24146   7008  11362  -2183   -913   1901       C  
ATOM   6646  OG  SER D 135      67.669 -46.675  17.015  1.00120.54           O  
ANISOU 6646  OG  SER D 135    25963   7880  11955  -2153   -858   2206       O  
TER    6647      SER D 135                                                      
HETATM 6648  C24 OLC A 401      84.945  -9.899  14.415  1.00 76.49           C  
ANISOU 6648  C24 OLC A 401    10977   7499  10585    176   2095  -1540       C  
HETATM 6649  C5  OLC A 401      79.811  -2.678  16.625  1.00 59.95           C  
ANISOU 6649  C5  OLC A 401     8923   6202   7652   -171   1249   -706       C  
HETATM 6650  C4  OLC A 401      79.845  -4.107  15.999  1.00 61.67           C  
ANISOU 6650  C4  OLC A 401     9241   6321   7869   -191   1344   -805       C  
HETATM 6651  C3  OLC A 401      81.202  -4.836  16.225  1.00 64.23           C  
ANISOU 6651  C3  OLC A 401     9455   6550   8400    -78   1456   -904       C  
HETATM 6652  C2  OLC A 401      81.016  -6.376  16.339  1.00 68.52           C  
ANISOU 6652  C2  OLC A 401    10063   6974   8998    -37   1455   -949       C  
HETATM 6653  C21 OLC A 401      84.205  -8.278  16.270  1.00 75.09           C  
ANISOU 6653  C21 OLC A 401    10632   7514  10383    236   1760  -1258       C  
HETATM 6654  C1  OLC A 401      82.159  -7.193  15.772  1.00 73.71           C  
ANISOU 6654  C1  OLC A 401    10691   7519   9797     14   1631  -1100       C  
HETATM 6655  C22 OLC A 401      84.201  -9.750  15.771  1.00 74.74           C  
ANISOU 6655  C22 OLC A 401    10685   7314  10398    263   1833  -1358       C  
HETATM 6656  O19 OLC A 401      82.380  -7.213  14.570  1.00 77.35           O  
ANISOU 6656  O19 OLC A 401    11250   7966  10173    -80   1794  -1207       O  
HETATM 6657  O25 OLC A 401      85.683 -11.137  14.375  1.00 77.45           O  
ANISOU 6657  O25 OLC A 401    11000   7465  10960    300   2215  -1684       O  
HETATM 6658  O23 OLC A 401      84.793 -10.604  16.765  1.00 74.59           O  
ANISOU 6658  O23 OLC A 401    10534   7168  10639    438   1760  -1366       O  
HETATM 6659  O20 OLC A 401      82.868  -7.906  16.672  1.00 74.99           O  
ANISOU 6659  O20 OLC A 401    10724   7589  10179    164   1591  -1110       O  
HETATM 6660  C24 OLC A 402      55.854   1.166  26.601  1.00 67.02           C  
ANISOU 6660  C24 OLC A 402     8136   7812   9515   -852    302   -541       C  
HETATM 6661  C4  OLC A 402      60.496   8.033  25.327  1.00 46.83           C  
ANISOU 6661  C4  OLC A 402     5827   5179   6787   -180    -88   -270       C  
HETATM 6662  C3  OLC A 402      59.571   7.078  26.141  1.00 49.94           C  
ANISOU 6662  C3  OLC A 402     6128   5604   7242   -262     37   -342       C  
HETATM 6663  C2  OLC A 402      58.962   5.927  25.287  1.00 54.00           C  
ANISOU 6663  C2  OLC A 402     6638   6123   7755   -352    -41   -342       C  
HETATM 6664  C21 OLC A 402      57.239   2.936  25.336  1.00 64.98           C  
ANISOU 6664  C21 OLC A 402     7974   7539   9177   -631     66   -433       C  
HETATM 6665  C1  OLC A 402      57.928   5.091  26.013  1.00 60.90           C  
ANISOU 6665  C1  OLC A 402     7404   7021   8714   -446     77   -418       C  
HETATM 6666  C22 OLC A 402      55.835   2.311  25.553  1.00 67.46           C  
ANISOU 6666  C22 OLC A 402     8114   7871   9646   -738     98   -515       C  
HETATM 6667  O19 OLC A 402      57.839   5.078  27.229  1.00 65.26           O  
ANISOU 6667  O19 OLC A 402     7933   7587   9274   -463    247   -463       O  
HETATM 6668  O25 OLC A 402      54.569   0.523  26.601  1.00 66.86           O  
ANISOU 6668  O25 OLC A 402     7962   7805   9635   -971    322   -617       O  
HETATM 6669  O23 OLC A 402      54.876   3.317  25.929  1.00 70.94           O  
ANISOU 6669  O23 OLC A 402     8318   8331  10303   -691    100   -585       O  
HETATM 6670  O20 OLC A 402      57.106   4.371  25.231  1.00 63.29           O  
ANISOU 6670  O20 OLC A 402     7647   7326   9074   -521    -15   -435       O  
HETATM 6671  C18 OLC A 403      90.404   9.042  21.911  1.00 82.01           C  
ANISOU 6671  C18 OLC A 403    10072   9371  11716    -21   1242   -761       C  
HETATM 6672  C10 OLC A 403      86.979  15.339  23.941  1.00 77.18           C  
ANISOU 6672  C10 OLC A 403     9948   8845  10533   -264    826   -365       C  
HETATM 6673  C9  OLC A 403      88.085  14.655  24.264  1.00 77.52           C  
ANISOU 6673  C9  OLC A 403     9831   8897  10726   -218    839   -435       C  
HETATM 6674  C17 OLC A 403      90.153  10.535  22.246  1.00 82.74           C  
ANISOU 6674  C17 OLC A 403    10260   9502  11676   -128   1230   -695       C  
HETATM 6675  C11 OLC A 403      86.025  14.998  22.819  1.00 77.65           C  
ANISOU 6675  C11 OLC A 403    10168   8893  10442   -293    877   -321       C  
HETATM 6676  C8  OLC A 403      89.062  14.986  25.370  1.00 78.55           C  
ANISOU 6676  C8  OLC A 403     9797   9036  11013   -194    756   -478       C  
HETATM 6677  C24 OLC A 403      84.747  21.274  20.257  1.00 86.05           C  
ANISOU 6677  C24 OLC A 403    11848   9702  11144   -715    878    -60       C  
HETATM 6678  C16 OLC A 403      88.906  10.726  23.151  1.00 83.94           C  
ANISOU 6678  C16 OLC A 403    10515   9675  11703    -77   1025   -579       C  
HETATM 6679  C12 OLC A 403      85.078  13.846  23.236  1.00 78.69           C  
ANISOU 6679  C12 OLC A 403    10327   9041  10531   -194    785   -291       C  
HETATM 6680  C7  OLC A 403      90.525  14.806  24.872  1.00 80.36           C  
ANISOU 6680  C7  OLC A 403     9853   9258  11421   -232    886   -580       C  
HETATM 6681  C15 OLC A 403      87.867  11.661  22.469  1.00 84.75           C  
ANISOU 6681  C15 OLC A 403    10818   9788  11593   -168   1051   -504       C  
HETATM 6682  C13 OLC A 403      85.427  12.528  22.496  1.00 80.70           C  
ANISOU 6682  C13 OLC A 403    10578   9290  10793   -185    885   -339       C  
HETATM 6683  C6  OLC A 403      90.902  15.750  23.691  1.00 81.54           C  
ANISOU 6683  C6  OLC A 403    10046   9394  11541   -381   1073   -608       C  
HETATM 6684  C14 OLC A 403      86.533  11.756  23.269  1.00 83.41           C  
ANISOU 6684  C14 OLC A 403    10749   9634  11310   -109    881   -408       C  
HETATM 6685  C5  OLC A 403      91.506  17.105  24.161  1.00 82.32           C  
ANISOU 6685  C5  OLC A 403    10100   9487  11691   -460   1039   -612       C  
HETATM 6686  C4  OLC A 403      92.057  17.922  22.958  1.00 82.74           C  
ANISOU 6686  C4  OLC A 403    10197   9515  11725   -624   1243   -645       C  
HETATM 6687  C3  OLC A 403      91.099  19.077  22.548  1.00 84.31           C  
ANISOU 6687  C3  OLC A 403    10622   9679  11732   -702   1224   -547       C  
HETATM 6688  C2  OLC A 403      89.700  18.569  22.080  1.00 86.24           C  
ANISOU 6688  C2  OLC A 403    11060   9919  11787   -650   1183   -462       C  
HETATM 6689  C21 OLC A 403      86.665  19.880  21.254  1.00 86.85           C  
ANISOU 6689  C21 OLC A 403    11611   9913  11476   -667   1008   -228       C  
HETATM 6690  C1  OLC A 403      88.983  19.494  21.118  1.00 87.93           C  
ANISOU 6690  C1  OLC A 403    11497  10083  11828   -757   1231   -387       C  
HETATM 6691  C22 OLC A 403      86.258  20.915  20.174  1.00 86.12           C  
ANISOU 6691  C22 OLC A 403    11726   9748  11249   -785   1044   -156       C  
HETATM 6692  O19 OLC A 403      89.492  20.523  20.694  1.00 88.71           O  
ANISOU 6692  O19 OLC A 403    11638  10143  11925   -883   1318   -391       O  
HETATM 6693  O25 OLC A 403      84.472  22.406  19.409  1.00 86.29           O  
ANISOU 6693  O25 OLC A 403    12065   9645  11078   -818    878     13       O  
HETATM 6694  O23 OLC A 403      87.064  22.098  20.313  1.00 86.33           O  
ANISOU 6694  O23 OLC A 403    11735   9730  11334   -884   1098   -174       O  
HETATM 6695  O20 OLC A 403      87.756  19.082  20.754  1.00 87.99           O  
ANISOU 6695  O20 OLC A 403    11656  10086  11691   -709   1164   -314       O  
HETATM 6696  C10 OLC A 404      77.600   9.390  45.887  1.00 76.13           C  
ANISOU 6696  C10 OLC A 404    11715   8657   8555   -400   -278    -52       C  
HETATM 6697  C9  OLC A 404      77.291   8.085  45.878  1.00 74.24           C  
ANISOU 6697  C9  OLC A 404    11562   8377   8267   -411   -286     24       C  
HETATM 6698  C11 OLC A 404      76.700  10.527  46.333  1.00 78.41           C  
ANISOU 6698  C11 OLC A 404    12041   8983   8768   -479   -104   -161       C  
HETATM 6699  C8  OLC A 404      75.970   7.491  46.306  1.00 73.31           C  
ANISOU 6699  C8  OLC A 404    11599   8252   8004   -522   -115     20       C  
HETATM 6700  C24 OLC A 404      71.404  -1.257  41.903  1.00 64.58           C  
ANISOU 6700  C24 OLC A 404    10535   6863   7142   -645    345    311       C  
HETATM 6701  C12 OLC A 404      77.516  11.844  46.472  1.00 78.09           C  
ANISOU 6701  C12 OLC A 404    11938   8956   8776   -458   -186   -219       C  
HETATM 6702  C7  OLC A 404      76.146   5.988  46.647  1.00 73.17           C  
ANISOU 6702  C7  OLC A 404    11743   8156   7901   -541   -224    134       C  
HETATM 6703  C6  OLC A 404      75.031   5.503  47.616  1.00 72.66           C  
ANISOU 6703  C6  OLC A 404    11912   8070   7625   -699    -70    134       C  
HETATM 6704  C5  OLC A 404      74.706   4.004  47.372  1.00 72.05           C  
ANISOU 6704  C5  OLC A 404    11884   7935   7558   -705    -56    216       C  
HETATM 6705  C4  OLC A 404      73.222   3.660  47.670  1.00 70.40           C  
ANISOU 6705  C4  OLC A 404    11786   7736   7228   -855    192    174       C  
HETATM 6706  C3  OLC A 404      72.871   2.307  47.001  1.00 69.67           C  
ANISOU 6706  C3  OLC A 404    11681   7594   7198   -847    217    240       C  
HETATM 6707  C2  OLC A 404      71.626   2.391  46.074  1.00 69.56           C  
ANISOU 6707  C2  OLC A 404    11457   7649   7323   -854    445    151       C  
HETATM 6708  C21 OLC A 404      70.118  -0.245  43.917  1.00 66.31           C  
ANISOU 6708  C21 OLC A 404    10845   7190   7161   -860    620    190       C  
HETATM 6709  C1  OLC A 404      71.331   1.049  45.456  1.00 70.77           C  
ANISOU 6709  C1  OLC A 404    11590   7751   7548   -841    445    212       C  
HETATM 6710  C22 OLC A 404      70.207  -0.384  42.375  1.00 65.94           C  
ANISOU 6710  C22 OLC A 404    10596   7146   7311   -707    517    204       C  
HETATM 6711  O19 OLC A 404      71.781   0.031  45.974  1.00 75.37           O  
ANISOU 6711  O19 OLC A 404    12339   8238   8062   -842    306    317       O  
HETATM 6712  O25 OLC A 404      70.973  -2.576  41.494  1.00 64.58           O  
ANISOU 6712  O25 OLC A 404    10527   6818   7193   -679    408    323       O  
HETATM 6713  O23 OLC A 404      68.977  -0.951  41.915  1.00 67.45           O  
ANISOU 6713  O23 OLC A 404    10630   7385   7613   -734    656    143       O  
HETATM 6714  O20 OLC A 404      70.571   1.063  44.339  1.00 67.46           O  
ANISOU 6714  O20 OLC A 404    10967   7390   7276   -828    591    144       O  
HETATM 6715  C18 OLC A 405      95.326   7.912  36.028  1.00 94.44           C  
ANISOU 6715  C18 OLC A 405    10972  10734  14175    720  -1252   -443       C  
HETATM 6716  C10 OLC A 405      90.406   1.608  36.637  1.00 97.47           C  
ANISOU 6716  C10 OLC A 405    12402  10791  13839    936  -1259    -26       C  
HETATM 6717  C9  OLC A 405      90.367   0.512  35.859  1.00 96.77           C  
ANISOU 6717  C9  OLC A 405    12301  10617  13849   1011  -1195    -40       C  
HETATM 6718  C17 OLC A 405      94.763   7.156  34.795  1.00 95.09           C  
ANISOU 6718  C17 OLC A 405    11054  10802  14274    754  -1002   -472       C  
HETATM 6719  C11 OLC A 405      91.616   2.492  36.864  1.00 97.54           C  
ANISOU 6719  C11 OLC A 405    12205  10830  14027    953  -1368    -85       C  
HETATM 6720  C8  OLC A 405      89.176  -0.384  35.618  1.00 96.08           C  
ANISOU 6720  C8  OLC A 405    12415  10495  13595    983  -1092     12       C  
HETATM 6721  C24 OLC A 405      86.740 -11.181  41.331  1.00102.32           C  
ANISOU 6721  C24 OLC A 405    15195   9865  13818   1150  -2359    958       C  
HETATM 6722  C16 OLC A 405      94.410   5.684  35.152  1.00 96.48           C  
ANISOU 6722  C16 OLC A 405    11317  10881  14461    872  -1113   -412       C  
HETATM 6723  C12 OLC A 405      91.734   3.558  35.739  1.00 97.15           C  
ANISOU 6723  C12 OLC A 405    11983  10880  14048    895  -1127   -190       C  
HETATM 6724  C7  OLC A 405      89.058  -1.404  36.782  1.00 96.72           C  
ANISOU 6724  C7  OLC A 405    12682  10451  13614   1026  -1319    123       C  
HETATM 6725  C15 OLC A 405      94.026   4.838  33.900  1.00 97.10           C  
ANISOU 6725  C15 OLC A 405    11417  10939  14537    896   -869   -445       C  
HETATM 6726  C13 OLC A 405      92.324   2.973  34.422  1.00 96.71           C  
ANISOU 6726  C13 OLC A 405    11749  10784  14211    964   -956   -285       C  
HETATM 6727  C6  OLC A 405      89.428  -2.840  36.322  1.00 97.44           C  
ANISOU 6727  C6  OLC A 405    12752  10398  13873   1138  -1327    113       C  
HETATM 6728  C14 OLC A 405      93.826   3.333  34.244  1.00 96.86           C  
ANISOU 6728  C14 OLC A 405    11473  10794  14533   1011   -984   -390       C  
HETATM 6729  C5  OLC A 405      89.595  -3.806  37.525  1.00 98.47           C  
ANISOU 6729  C5  OLC A 405    13038  10376  14001   1203  -1607    225       C  
HETATM 6730  C4  OLC A 405      88.470  -4.879  37.559  1.00 99.54           C  
ANISOU 6730  C4  OLC A 405    13427  10430  13962   1161  -1555    303       C  
HETATM 6731  C3  OLC A 405      88.525  -5.714  38.870  1.00100.38           C  
ANISOU 6731  C3  OLC A 405    13757  10396  13986   1181  -1836    440       C  
HETATM 6732  C2  OLC A 405      87.103  -6.014  39.423  1.00101.00           C  
ANISOU 6732  C2  OLC A 405    14145  10470  13761   1046  -1764    534       C  
HETATM 6733  C21 OLC A 405      86.681  -8.635  41.011  1.00102.04           C  
ANISOU 6733  C21 OLC A 405    14812  10216  13741   1066  -2127    793       C  
HETATM 6734  C1  OLC A 405      87.114  -6.312  40.904  1.00101.82           C  
ANISOU 6734  C1  OLC A 405    14503  10489  13696   1003  -2016    671       C  
HETATM 6735  C22 OLC A 405      87.011  -9.798  41.984  1.00101.89           C  
ANISOU 6735  C22 OLC A 405    15032   9979  13701   1112  -2422    936       C  
HETATM 6736  O19 OLC A 405      86.732  -5.488  41.726  1.00101.61           O  
ANISOU 6736  O19 OLC A 405    14595  10557  13455    887  -2030    706       O  
HETATM 6737  O25 OLC A 405      85.833 -11.933  42.158  1.00101.97           O  
ANISOU 6737  O25 OLC A 405    15484   9793  13467    980  -2303   1062       O  
HETATM 6738  O23 OLC A 405      88.371  -9.720  42.451  1.00102.06           O  
ANISOU 6738  O23 OLC A 405    14906   9916  13956   1266  -2709    944       O  
HETATM 6739  O20 OLC A 405      87.585  -7.530  41.234  1.00102.51           O  
ANISOU 6739  O20 OLC A 405    14683  10382  13885   1101  -2222    746       O  
HETATM 6740  C18 OLC A 406      62.664   6.328  17.307  1.00 60.68           C  
ANISOU 6740  C18 OLC A 406     8476   6795   7786   -454   -751     29       C  
HETATM 6741  C10 OLC A 406      58.800  -0.049  18.658  1.00 64.21           C  
ANISOU 6741  C10 OLC A 406     8637   7303   8458   -877   -575   -263       C  
HETATM 6742  C9  OLC A 406      59.263  -1.280  18.384  1.00 64.20           C  
ANISOU 6742  C9  OLC A 406     8780   7268   8344   -955   -496   -285       C  
HETATM 6743  C17 OLC A 406      63.802   5.271  17.343  1.00 62.97           C  
ANISOU 6743  C17 OLC A 406     8904   7088   7933   -507   -589      1       C  
HETATM 6744  C11 OLC A 406      59.394   1.277  18.233  1.00 65.23           C  
ANISOU 6744  C11 OLC A 406     8818   7431   8537   -779   -636   -204       C  
HETATM 6745  C8  OLC A 406      58.644  -2.583  18.829  1.00 65.20           C  
ANISOU 6745  C8  OLC A 406     8872   7382   8520  -1064   -433   -340       C  
HETATM 6746  C24 OLC A 406      59.218 -12.945  13.663  1.00 96.25           C  
ANISOU 6746  C24 OLC A 406    14185  10689  11698  -1955   -264   -770       C  
HETATM 6747  C16 OLC A 406      63.620   4.247  18.506  1.00 64.86           C  
ANISOU 6747  C16 OLC A 406     9040   7356   8249   -493   -438    -52       C  
HETATM 6748  C12 OLC A 406      60.764   1.090  17.514  1.00 66.20           C  
ANISOU 6748  C12 OLC A 406     9175   7520   8458   -784   -574   -177       C  
HETATM 6749  C7  OLC A 406      59.357  -3.742  18.099  1.00 67.50           C  
ANISOU 6749  C7  OLC A 406     9383   7611   8653  -1124   -364   -352       C  
HETATM 6750  C15 OLC A 406      64.261   2.850  18.218  1.00 63.97           C  
ANISOU 6750  C15 OLC A 406     9055   7226   8025   -557   -330    -86       C  
HETATM 6751  C13 OLC A 406      61.772   2.217  17.878  1.00 64.44           C  
ANISOU 6751  C13 OLC A 406     8994   7297   8193   -684   -550   -125       C  
HETATM 6752  C6  OLC A 406      58.362  -4.536  17.212  1.00 71.68           C  
ANISOU 6752  C6  OLC A 406     9963   8119   9153  -1258   -497   -393       C  
HETATM 6753  C14 OLC A 406      63.235   1.702  17.993  1.00 62.80           C  
ANISOU 6753  C14 OLC A 406     8867   7078   7915   -639   -354   -129       C  
HETATM 6754  C5  OLC A 406      58.330  -6.026  17.640  1.00 76.99           C  
ANISOU 6754  C5  OLC A 406    10677   8743   9832  -1363   -386   -443       C  
HETATM 6755  C4  OLC A 406      59.222  -6.911  16.722  1.00 82.27           C  
ANISOU 6755  C4  OLC A 406    11591   9332  10334  -1404   -334   -462       C  
HETATM 6756  C3  OLC A 406      58.466  -7.394  15.450  1.00 87.64           C  
ANISOU 6756  C3  OLC A 406    12357   9991  10952  -1539   -485   -508       C  
HETATM 6757  C2  OLC A 406      56.996  -7.816  15.746  1.00 92.06           C  
ANISOU 6757  C2  OLC A 406    12749  10573  11656  -1658   -571   -550       C  
HETATM 6758  C21 OLC A 406      57.732 -11.364  15.003  1.00 96.68           C  
ANISOU 6758  C21 OLC A 406    13804  10918  12014  -1916   -386   -687       C  
HETATM 6759  C1  OLC A 406      56.707  -9.272  15.466  1.00 96.39           C  
ANISOU 6759  C1  OLC A 406    13418  11050  12154  -1808   -562   -614       C  
HETATM 6760  C22 OLC A 406      59.194 -11.760  14.668  1.00 96.66           C  
ANISOU 6760  C22 OLC A 406    14018  10835  11873  -1833   -252   -689       C  
HETATM 6761  O19 OLC A 406      55.602  -9.623  15.055  1.00 99.06           O  
ANISOU 6761  O19 OLC A 406    13706  11400  12534  -1929   -716   -655       O  
HETATM 6762  O25 OLC A 406      60.530 -13.073  13.089  1.00 96.20           O  
ANISOU 6762  O25 OLC A 406    14358  10619  11575  -1870   -146   -787       O  
HETATM 6763  O23 OLC A 406      59.927 -10.617  14.180  1.00 97.16           O  
ANISOU 6763  O23 OLC A 406    14088  10954  11874  -1713   -277   -643       O  
HETATM 6764  O20 OLC A 406      57.738 -10.107  15.716  1.00 96.70           O  
ANISOU 6764  O20 OLC A 406    13617  11008  12116  -1796   -385   -624       O  
HETATM 6765  C18 OLC A 407      80.384   7.505  42.772  1.00 70.41           C  
ANISOU 6765  C18 OLC A 407    10491   7868   8394    -40   -622    103       C  
HETATM 6766  C10 OLC A 407      79.335  17.245  45.280  1.00 83.61           C  
ANISOU 6766  C10 OLC A 407    12183   9683   9902   -358   -220   -495       C  
HETATM 6767  C9  OLC A 407      80.102  18.337  45.143  1.00 84.77           C  
ANISOU 6767  C9  OLC A 407    12264   9816  10129   -358   -279   -540       C  
HETATM 6768  C17 OLC A 407      79.596   8.789  43.148  1.00 72.11           C  
ANISOU 6768  C17 OLC A 407    10748   8138   8511   -121   -493     27       C  
HETATM 6769  C11 OLC A 407      79.220  16.077  44.326  1.00 81.91           C  
ANISOU 6769  C11 OLC A 407    11866   9485   9772   -284   -223   -406       C  
HETATM 6770  C8  OLC A 407      81.044  18.667  44.004  1.00 86.49           C  
ANISOU 6770  C8  OLC A 407    12288  10035  10537   -291   -350   -511       C  
HETATM 6771  C24 OLC A 407      90.114  25.535  42.943  1.00 89.88           C  
ANISOU 6771  C24 OLC A 407    11935  10328  11887   -637  -1064   -807       C  
HETATM 6772  C16 OLC A 407      80.480  10.070  43.112  1.00 73.63           C  
ANISOU 6772  C16 OLC A 407    10824   8361   8791   -100   -548    -30       C  
HETATM 6773  C12 OLC A 407      80.295  14.998  44.637  1.00 80.78           C  
ANISOU 6773  C12 OLC A 407    11768   9329   9596   -274   -421   -319       C  
HETATM 6774  C7  OLC A 407      82.267  17.698  43.980  1.00 87.68           C  
ANISOU 6774  C7  OLC A 407    12401  10193  10720   -268   -544   -433       C  
HETATM 6775  C15 OLC A 407      80.124  11.067  44.256  1.00 74.99           C  
ANISOU 6775  C15 OLC A 407    11136   8546   8810   -196   -526    -88       C  
HETATM 6776  C13 OLC A 407      79.696  13.564  44.599  1.00 79.34           C  
ANISOU 6776  C13 OLC A 407    11662   9141   9343   -269   -394   -247       C  
HETATM 6777  C6  OLC A 407      83.500  18.302  43.247  1.00 86.73           C  
ANISOU 6777  C6  OLC A 407    12103  10070  10779   -238   -626   -437       C  
HETATM 6778  C14 OLC A 407      80.650  12.506  43.977  1.00 76.78           C  
ANISOU 6778  C14 OLC A 407    11237   8800   9134   -185   -527   -161       C  
HETATM 6779  C5  OLC A 407      83.962  19.607  43.950  1.00 85.86           C  
ANISOU 6779  C5  OLC A 407    12032   9938  10652   -312   -676   -516       C  
HETATM 6780  C4  OLC A 407      85.057  20.353  43.146  1.00 85.92           C  
ANISOU 6780  C4  OLC A 407    11860   9941  10845   -303   -739   -527       C  
HETATM 6781  C3  OLC A 407      86.167  20.866  44.100  1.00 87.65           C  
ANISOU 6781  C3  OLC A 407    12119  10144  11040   -378   -917   -572       C  
HETATM 6782  C2  OLC A 407      86.995  22.030  43.484  1.00 88.83           C  
ANISOU 6782  C2  OLC A 407    12128  10275  11348   -411   -913   -624       C  
HETATM 6783  C21 OLC A 407      87.510  25.306  43.013  1.00 89.49           C  
ANISOU 6783  C21 OLC A 407    12136  10265  11600   -547   -799   -776       C  
HETATM 6784  C1  OLC A 407      86.346  23.380  43.666  1.00 89.55           C  
ANISOU 6784  C1  OLC A 407    12302  10326  11395   -462   -787   -700       C  
HETATM 6785  C22 OLC A 407      88.761  26.111  43.457  1.00 90.04           C  
ANISOU 6785  C22 OLC A 407    12163  10314  11735   -643   -942   -838       C  
HETATM 6786  O19 OLC A 407      85.149  23.549  43.473  1.00 90.43           O  
ANISOU 6786  O19 OLC A 407    12474  10428  11456   -432   -630   -706       O  
HETATM 6787  O25 OLC A 407      89.916  24.527  41.935  1.00 89.36           O  
ANISOU 6787  O25 OLC A 407    11746  10290  11915   -551   -954   -741       O  
HETATM 6788  O23 OLC A 407      88.625  27.501  43.109  1.00 90.41           O  
ANISOU 6788  O23 OLC A 407    12222  10297  11833   -701   -842   -899       O  
HETATM 6789  O20 OLC A 407      87.189  24.356  44.047  1.00 89.33           O  
ANISOU 6789  O20 OLC A 407    12265  10269  11406   -540   -867   -764       O  
HETATM 6790  C10 OLC A 408      57.505   4.666  41.162  1.00 65.01           C  
ANISOU 6790  C10 OLC A 408     8705   7573   8422  -1258   2242   -973       C  
HETATM 6791  C9  OLC A 408      56.502   3.845  41.517  1.00 66.80           C  
ANISOU 6791  C9  OLC A 408     8873   7806   8702  -1411   2415  -1041       C  
HETATM 6792  C11 OLC A 408      58.038   5.887  41.884  1.00 63.29           C  
ANISOU 6792  C11 OLC A 408     8505   7360   8182  -1189   2286  -1037       C  
HETATM 6793  C8  OLC A 408      56.065   2.650  40.696  1.00 70.23           C  
ANISOU 6793  C8  OLC A 408     9302   8226   9156  -1477   2348   -972       C  
HETATM 6794  C24 OLC A 408      58.395  -6.674  41.494  1.00 81.83           C  
ANISOU 6794  C24 OLC A 408    12364   9142   9586  -2125   2117   -251       C  
HETATM 6795  C12 OLC A 408      59.510   6.175  41.459  1.00 61.00           C  
ANISOU 6795  C12 OLC A 408     8370   7050   7758  -1062   2061   -909       C  
HETATM 6796  C7  OLC A 408      55.291   1.606  41.542  1.00 74.42           C  
ANISOU 6796  C7  OLC A 408     9926   8740   9609  -1708   2591  -1024       C  
HETATM 6797  C13 OLC A 408      59.649   7.451  40.582  1.00 59.24           C  
ANISOU 6797  C13 OLC A 408     7940   6840   7729   -877   1884   -903       C  
HETATM 6798  C6  OLC A 408      56.229   0.471  42.045  1.00 78.51           C  
ANISOU 6798  C6  OLC A 408    10807   9191   9833  -1800   2554   -882       C  
HETATM 6799  C14 OLC A 408      60.939   7.432  39.713  1.00 57.57           C  
ANISOU 6799  C14 OLC A 408     7867   6610   7397   -767   1679   -784       C  
HETATM 6800  C5  OLC A 408      56.557   0.622  43.563  1.00 80.01           C  
ANISOU 6800  C5  OLC A 408    11258   9358   9784  -1899   2706   -892       C  
HETATM 6801  C4  OLC A 408      58.082   0.546  43.861  1.00 80.13           C  
ANISOU 6801  C4  OLC A 408    11544   9326   9577  -1805   2498   -741       C  
HETATM 6802  C3  OLC A 408      58.630  -0.856  43.488  1.00 83.04           C  
ANISOU 6802  C3  OLC A 408    12100   9620   9831  -1836   2356   -591       C  
HETATM 6803  C2  OLC A 408      58.186  -1.946  44.506  1.00 86.04           C  
ANISOU 6803  C2  OLC A 408    12739   9936  10017  -2073   2536   -571       C  
HETATM 6804  C21 OLC A 408      58.425  -4.825  43.259  1.00 85.97           C  
ANISOU 6804  C21 OLC A 408    12938   9760   9966  -2151   2317   -349       C  
HETATM 6805  C1  OLC A 408      57.183  -2.933  43.953  1.00 88.79           C  
ANISOU 6805  C1  OLC A 408    12992  10268  10475  -2192   2621   -593       C  
HETATM 6806  C22 OLC A 408      57.972  -6.274  42.928  1.00 84.79           C  
ANISOU 6806  C22 OLC A 408    12868   9530   9817  -2282   2339   -302       C  
HETATM 6807  O19 OLC A 408      56.170  -2.553  43.383  1.00 90.81           O  
ANISOU 6807  O19 OLC A 408    12953  10589  10960  -2195   2711   -711       O  
HETATM 6808  O25 OLC A 408      59.335  -7.761  41.507  1.00 80.17           O  
ANISOU 6808  O25 OLC A 408    12415   8802   9245  -2128   1986   -114       O  
HETATM 6809  O23 OLC A 408      58.438  -7.227  43.906  1.00 86.64           O  
ANISOU 6809  O23 OLC A 408    13472   9644   9803  -2415   2356   -191       O  
HETATM 6810  O20 OLC A 408      57.470  -4.234  44.168  1.00 88.03           O  
ANISOU 6810  O20 OLC A 408    13159  10074  10213  -2297   2583   -477       O  
HETATM 6811  C1  GOL A 409      69.390 -11.809  28.675  1.00 60.61           C  
ANISOU 6811  C1  GOL A 409     9690   5768   7569   -562    509     19       C  
HETATM 6812  O1  GOL A 409      68.385 -12.541  29.408  1.00 61.60           O  
ANISOU 6812  O1  GOL A 409     9922   5843   7639   -703    547     52       O  
HETATM 6813  C2  GOL A 409      69.371 -10.309  29.087  1.00 57.43           C  
ANISOU 6813  C2  GOL A 409     9151   5521   7150   -528    501     30       C  
HETATM 6814  O2  GOL A 409      69.655 -10.156  30.502  1.00 57.41           O  
ANISOU 6814  O2  GOL A 409     9212   5498   7102   -513    474    105       O  
HETATM 6815  C3  GOL A 409      70.312  -9.440  28.190  1.00 52.68           C  
ANISOU 6815  C3  GOL A 409     8433   4981   6601   -408    477    -12       C  
HETATM 6816  O3  GOL A 409      69.688  -8.183  27.849  1.00 47.57           O  
ANISOU 6816  O3  GOL A 409     7652   4483   5941   -434    489    -35       O  
HETATM 6817  C01 H95 A 410      86.151  28.847  21.323  1.00 77.08           C  
ANISOU 6817  C01 H95 A 410    11017   8100  10172  -1092    784     48       C  
HETATM 6818  C02 H95 A 410      85.761  27.638  22.195  1.00 76.60           C  
ANISOU 6818  C02 H95 A 410    10786   8159  10160   -937    722     -4       C  
HETATM 6819  C03 H95 A 410      86.367  27.822  23.595  1.00 71.22           C  
ANISOU 6819  C03 H95 A 410     9934   7516   9612   -899    685    -90       C  
HETATM 6820  C04 H95 A 410      86.761  26.466  24.180  1.00 64.58           C  
ANISOU 6820  C04 H95 A 410     8913   6801   8825   -817    690   -157       C  
HETATM 6821  C05 H95 A 410      87.818  25.674  23.387  1.00 60.38           C  
ANISOU 6821  C05 H95 A 410     8299   6325   8316   -895    840   -202       C  
HETATM 6822  C06 H95 A 410      88.828  26.499  22.568  1.00 64.24           C  
ANISOU 6822  C06 H95 A 410     8822   6760   8825  -1073    986   -221       C  
HETATM 6823  O07 H95 A 410      88.542  24.934  24.314  1.00 57.47           O  
ANISOU 6823  O07 H95 A 410     7734   6039   8065   -834    816   -282       O  
HETATM 6824  O08 H95 A 410      84.371  27.462  22.325  1.00 78.43           O  
ANISOU 6824  O08 H95 A 410    11079   8377  10343   -811    591     52       O  
HETATM 6825 H012 H95 A 410      85.656  28.817  20.489  1.00 77.23           H  
ANISOU 6825 H012 H95 A 410    11172   8078  10093  -1110    773    115       H  
HETATM 6826 H011 H95 A 410      87.102  28.816  21.135  1.00 77.00           H  
ANISOU 6826 H011 H95 A 410    10958   8110  10188  -1189    899      4       H  
HETATM 6827 H013 H95 A 410      85.941  29.668  21.795  1.00 77.06           H  
ANISOU 6827 H013 H95 A 410    11037   8033  10208  -1081    719     55       H  
HETATM 6828 H021 H95 A 410      86.113  26.842  21.772  1.00 76.58           H  
ANISOU 6828 H021 H95 A 410    10743   8214  10139   -957    799    -26       H  
HETATM 6829 H032 H95 A 410      85.709  28.230  24.179  1.00 70.61           H  
ANISOU 6829 H032 H95 A 410     9882   7404   9543   -833    591    -77       H  
HETATM 6830 H031 H95 A 410      87.138  28.407  23.551  1.00 71.84           H  
ANISOU 6830 H031 H95 A 410     9997   7566   9732   -993    744   -117       H  
HETATM 6831 H042 H95 A 410      87.083  26.609  25.083  1.00 64.91           H  
ANISOU 6831 H042 H95 A 410     8864   6861   8937   -791    644   -203       H  
HETATM 6832 H041 H95 A 410      85.962  25.923  24.228  1.00 64.23           H  
ANISOU 6832 H041 H95 A 410     8892   6777   8733   -732    636   -129       H  
HETATM 6833 H051 H95 A 410      87.361  25.063  22.788  1.00 60.36           H  
ANISOU 6833 H051 H95 A 410     8356   6338   8242   -873    861   -171       H  
HETATM 6834 H063 H95 A 410      89.089  27.296  23.041  1.00 64.24           H  
ANISOU 6834 H063 H95 A 410     8803   6725   8879  -1106    956   -237       H  
HETATM 6835 H062 H95 A 410      88.431  26.749  21.720  1.00 64.39           H  
ANISOU 6835 H062 H95 A 410     8990   6727   8746  -1126   1021   -163       H  
HETATM 6836 H061 H95 A 410      89.616  25.963  22.395  1.00 64.11           H  
ANISOU 6836 H061 H95 A 410     8702   6792   8866  -1107   1079   -278       H  
HETATM 6837 H071 H95 A 410      88.020  24.419  24.744  1.00 57.49           H  
ANISOU 6837 H071 H95 A 410     7725   6071   8048   -746    748   -272       H  
HETATM 6838 H081 H95 A 410      84.033  28.194  22.589  1.00 78.44           H  
ANISOU 6838 H081 H95 A 410    11125   8317  10362   -796    531     71       H  
HETATM 6839  C24 OLC C 401      79.473 -11.126  15.271  1.00 70.31           C  
ANISOU 6839  C24 OLC C 401    10716   6795   9205   -103   1546  -1158       C  
HETATM 6840  C6  OLC C 401      74.712  -2.608  14.680  1.00 61.00           C  
ANISOU 6840  C6  OLC C 401     9520   6447   7209   -561    864   -541       C  
HETATM 6841  C5  OLC C 401      75.198  -3.982  14.136  1.00 61.13           C  
ANISOU 6841  C5  OLC C 401     9638   6370   7220   -587    993   -653       C  
HETATM 6842  C4  OLC C 401      74.058  -5.018  13.920  1.00 59.12           C  
ANISOU 6842  C4  OLC C 401     9468   6077   6917   -652    913   -660       C  
HETATM 6843  C3  OLC C 401      74.147  -6.126  14.998  1.00 61.67           C  
ANISOU 6843  C3  OLC C 401     9710   6331   7389   -555    923   -664       C  
HETATM 6844  C2  OLC C 401      74.894  -7.413  14.542  1.00 66.14           C  
ANISOU 6844  C2  OLC C 401    10361   6775   7995   -546   1058   -779       C  
HETATM 6845  C21 OLC C 401      78.193  -8.888  15.501  1.00 69.46           C  
ANISOU 6845  C21 OLC C 401    10586   6958   8847   -233   1348   -955       C  
HETATM 6846  C1  OLC C 401      76.356  -7.477  14.941  1.00 68.79           C  
ANISOU 6846  C1  OLC C 401    10603   7058   8476   -425   1186   -834       C  
HETATM 6847  C22 OLC C 401      78.634 -10.036  14.549  1.00 70.10           C  
ANISOU 6847  C22 OLC C 401    10775   6912   8946   -256   1506  -1105       C  
HETATM 6848  O19 OLC C 401      77.088  -6.504  14.812  1.00 70.09           O  
ANISOU 6848  O19 OLC C 401    10707   7276   8647   -406   1243   -838       O  
HETATM 6849  O25 OLC C 401      79.628 -12.286  14.420  1.00 70.21           O  
ANISOU 6849  O25 OLC C 401    10826   6647   9203   -132   1670  -1291       O  
HETATM 6850  O23 OLC C 401      77.507 -10.630  13.883  1.00 71.48           O  
ANISOU 6850  O23 OLC C 401    11124   7063   8973   -382   1472  -1120       O  
HETATM 6851  O20 OLC C 401      76.761  -8.675  15.418  1.00 68.84           O  
ANISOU 6851  O20 OLC C 401    10599   6948   8610   -347   1225   -878       O  
HETATM 6852  C18 OLC C 402      77.436   1.061  14.977  1.00 78.85           C  
ANISOU 6852  C18 OLC C 402    11574   8822   9564   -476   1030   -492       C  
HETATM 6853  C10 OLC C 402      67.972   1.663  16.962  1.00 90.82           C  
ANISOU 6853  C10 OLC C 402    12851  10538  11120   -573     12   -137       C  
HETATM 6854  C9  OLC C 402      67.894   2.941  17.389  1.00 93.16           C  
ANISOU 6854  C9  OLC C 402    13062  10864  11470   -514    -39    -90       C  
HETATM 6855  C17 OLC C 402      75.961   0.652  14.710  1.00 79.21           C  
ANISOU 6855  C17 OLC C 402    11715   8874   9508   -534    892   -450       C  
HETATM 6856  C11 OLC C 402      68.810   0.535  17.524  1.00 86.09           C  
ANISOU 6856  C11 OLC C 402    12276   9902  10532   -546    158   -182       C  
HETATM 6857  C8  OLC C 402      67.067   4.064  16.774  1.00 93.57           C  
ANISOU 6857  C8  OLC C 402    13097  10928  11527   -532   -204    -42       C  
HETATM 6858  C24 OLC C 402      66.490  16.168  18.333  1.00 86.66           C  
ANISOU 6858  C24 OLC C 402    11919   9781  11228    -33   -809    323       C  
HETATM 6859  C16 OLC C 402      74.972   1.345  15.693  1.00 79.02           C  
ANISOU 6859  C16 OLC C 402    11599   8905   9519   -492    718   -346       C  
HETATM 6860  C12 OLC C 402      70.271   1.022  17.732  1.00 82.51           C  
ANISOU 6860  C12 OLC C 402    11830   9441  10080   -479    264   -185       C  
HETATM 6861  C7  OLC C 402      67.946   5.350  16.659  1.00 92.63           C  
ANISOU 6861  C7  OLC C 402    13007  10804  11383   -490   -200      2       C  
HETATM 6862  C15 OLC C 402      73.678   0.504  15.877  1.00 78.17           C  
ANISOU 6862  C15 OLC C 402    11485   8793   9423   -494    616   -329       C  
HETATM 6863  C13 OLC C 402      71.201   0.680  16.536  1.00 79.89           C  
ANISOU 6863  C13 OLC C 402    11642   9068   9644   -533    353   -235       C  
HETATM 6864  C6  OLC C 402      67.490   6.363  15.567  1.00 89.95           C  
ANISOU 6864  C6  OLC C 402    12721  10447  11008   -521   -378     60       C  
HETATM 6865  C14 OLC C 402      72.637   1.230  16.769  1.00 78.30           C  
ANISOU 6865  C14 OLC C 402    11414   8865   9471   -474    463   -245       C  
HETATM 6866  C5  OLC C 402      68.065   7.784  15.838  1.00 85.95           C  
ANISOU 6866  C5  OLC C 402    12238   9924  10496   -478   -367    107       C  
HETATM 6867  C4  OLC C 402      67.473   8.370  17.148  1.00 84.31           C  
ANISOU 6867  C4  OLC C 402    11845   9734  10454   -373   -379    116       C  
HETATM 6868  C3  OLC C 402      66.241   9.289  16.912  1.00 84.25           C  
ANISOU 6868  C3  OLC C 402    11760   9709  10544   -347   -574    154       C  
HETATM 6869  C2  OLC C 402      66.447  10.608  17.707  1.00 85.86           C  
ANISOU 6869  C2  OLC C 402    11828   9909  10886   -247   -559    160       C  
HETATM 6870  C21 OLC C 402      66.243  13.666  17.869  1.00 87.50           C  
ANISOU 6870  C21 OLC C 402    12037  10000  11209   -137   -737    264       C  
HETATM 6871  C1  OLC C 402      65.267  11.548  17.761  1.00 87.12           C  
ANISOU 6871  C1  OLC C 402    11910  10028  11162   -200   -740    196       C  
HETATM 6872  C22 OLC C 402      66.087  15.096  17.288  1.00 87.24           C  
ANISOU 6872  C22 OLC C 402    12068   9877  11202   -111   -891    338       C  
HETATM 6873  O19 OLC C 402      64.252  11.261  18.376  1.00 88.14           O  
ANISOU 6873  O19 OLC C 402    11879  10173  11438   -163   -793    161       O  
HETATM 6874  O25 OLC C 402      65.741  17.364  18.070  1.00 86.70           O  
ANISOU 6874  O25 OLC C 402    11888   9698  11355     32   -980    364       O  
HETATM 6875  O23 OLC C 402      66.888  15.253  16.105  1.00 88.01           O  
ANISOU 6875  O23 OLC C 402    12395   9934  11111   -205   -921    404       O  
HETATM 6876  O20 OLC C 402      65.446  12.721  17.123  1.00 87.28           O  
ANISOU 6876  O20 OLC C 402    12044   9987  11131   -201   -828    263       O  
HETATM 6877  C1  CLR C 403      84.310  -7.398   4.405  1.00 73.62           C  
ANISOU 6877  C1  CLR C 403     9409   8318  10244     24    367   -266       C  
HETATM 6878  C2  CLR C 403      85.095  -8.741   4.333  1.00 74.55           C  
ANISOU 6878  C2  CLR C 403     9391   8385  10549    182    315   -284       C  
HETATM 6879  C3  CLR C 403      85.753  -9.080   5.697  1.00 76.31           C  
ANISOU 6879  C3  CLR C 403     9562   8572  10860    247      0   -248       C  
HETATM 6880  C4  CLR C 403      84.705  -9.078   6.842  1.00 75.19           C  
ANISOU 6880  C4  CLR C 403     9720   8395  10453    207   -159   -170       C  
HETATM 6881  C5  CLR C 403      83.920  -7.771   6.905  1.00 73.75           C  
ANISOU 6881  C5  CLR C 403     9666   8268  10089     57    -71   -164       C  
HETATM 6882  C6  CLR C 403      83.793  -7.152   8.092  1.00 72.78           C  
ANISOU 6882  C6  CLR C 403     9678   8130   9845     -4   -249   -130       C  
HETATM 6883  C7  CLR C 403      83.058  -5.854   8.304  1.00 73.73           C  
ANISOU 6883  C7  CLR C 403     9950   8280   9787   -127   -176   -127       C  
HETATM 6884  C8  CLR C 403      82.182  -5.426   7.088  1.00 73.76           C  
ANISOU 6884  C8  CLR C 403     9971   8329   9724   -165    100   -142       C  
HETATM 6885  C9  CLR C 403      82.930  -5.718   5.742  1.00 73.18           C  
ANISOU 6885  C9  CLR C 403     9674   8285   9848   -141    250   -197       C  
HETATM 6886  C10 CLR C 403      83.293  -7.245   5.600  1.00 73.37           C  
ANISOU 6886  C10 CLR C 403     9623   8268   9987     -7    210   -195       C  
HETATM 6887  C11 CLR C 403      82.129  -5.138   4.524  1.00 71.66           C  
ANISOU 6887  C11 CLR C 403     9548   8121   9560   -197    490   -210       C  
HETATM 6888  C12 CLR C 403      81.737  -3.640   4.709  1.00 69.27           C  
ANISOU 6888  C12 CLR C 403     9346   7832   9143   -305    516   -207       C  
HETATM 6889  C13 CLR C 403      80.892  -3.420   6.002  1.00 68.59           C  
ANISOU 6889  C13 CLR C 403     9455   7723   8884   -302    390   -158       C  
HETATM 6890  C14 CLR C 403      81.808  -3.911   7.168  1.00 71.11           C  
ANISOU 6890  C14 CLR C 403     9729   8012   9277   -275    159   -154       C  
HETATM 6891  C15 CLR C 403      81.127  -3.402   8.455  1.00 70.43           C  
ANISOU 6891  C15 CLR C 403     9884   7887   8990   -301     58   -119       C  
HETATM 6892  C16 CLR C 403      80.578  -2.016   8.006  1.00 69.57           C  
ANISOU 6892  C16 CLR C 403     9847   7790   8797   -377    201   -140       C  
HETATM 6893  C17 CLR C 403      80.672  -1.923   6.438  1.00 68.18           C  
ANISOU 6893  C17 CLR C 403     9520   7657   8727   -389    386   -166       C  
HETATM 6894  C18 CLR C 403      79.528  -4.182   5.906  1.00 66.34           C  
ANISOU 6894  C18 CLR C 403     9302   7438   8467   -243    461   -108       C  
HETATM 6895  C19 CLR C 403      81.999  -8.081   5.328  1.00 73.66           C  
ANISOU 6895  C19 CLR C 403     9857   8274   9856     30    296   -153       C  
HETATM 6896  C20 CLR C 403      79.535  -1.069   5.758  1.00 64.37           C  
ANISOU 6896  C20 CLR C 403     9162   7178   8119   -405    553   -154       C  
HETATM 6897  C21 CLR C 403      79.832  -0.808   4.252  1.00 62.82           C  
ANISOU 6897  C21 CLR C 403     8871   6997   8000   -443    706   -182       C  
HETATM 6898  C22 CLR C 403      79.258   0.263   6.544  1.00 63.85           C  
ANISOU 6898  C22 CLR C 403     9262   7067   7933   -456    521   -160       C  
HETATM 6899  C23 CLR C 403      79.917   1.569   6.000  1.00 63.58           C  
ANISOU 6899  C23 CLR C 403     9205   7002   7950   -567    549   -203       C  
HETATM 6900  C24 CLR C 403      79.655   2.780   6.940  1.00 61.83           C  
ANISOU 6900  C24 CLR C 403     9196   6708   7591   -609    502   -212       C  
HETATM 6901  C25 CLR C 403      80.893   3.694   7.158  1.00 60.67           C  
ANISOU 6901  C25 CLR C 403     9020   6511   7519   -755    403   -260       C  
HETATM 6902  C26 CLR C 403      80.597   4.692   8.317  1.00 61.67           C  
ANISOU 6902  C26 CLR C 403     9415   6540   7476   -786    323   -274       C  
HETATM 6903  C27 CLR C 403      82.177   2.889   7.493  1.00 60.34           C  
ANISOU 6903  C27 CLR C 403     8769   6504   7652   -794    231   -277       C  
HETATM 6904  O1  CLR C 403      86.390 -10.371   5.597  1.00 78.46           O  
ANISOU 6904  O1  CLR C 403     9733   8777  11301    421    -54   -258       O  
HETATM 6905  C18 OLC C 404      61.471   7.481   7.607  1.00 77.89           C  
ANISOU 6905  C18 OLC C 404    10978   8734   9883   1268   2030    156       C  
HETATM 6906  C10 OLC C 404      62.727  -1.998   9.673  1.00 75.50           C  
ANISOU 6906  C10 OLC C 404    10398   8888   9399    132   2013    355       C  
HETATM 6907  C9  OLC C 404      63.015  -3.087   8.941  1.00 74.02           C  
ANISOU 6907  C9  OLC C 404    10143   8728   9252     10   1849    384       C  
HETATM 6908  C17 OLC C 404      61.129   6.341   8.607  1.00 77.29           C  
ANISOU 6908  C17 OLC C 404    10790   8762   9814   1167   2205    167       C  
HETATM 6909  C11 OLC C 404      63.391  -0.642   9.588  1.00 75.77           C  
ANISOU 6909  C11 OLC C 404    10581   8859   9350    248   1963    293       C  
HETATM 6910  C8  OLC C 404      62.327  -4.433   9.031  1.00 72.30           C  
ANISOU 6910  C8  OLC C 404     9806   8551   9114   -123   1896    446       C  
HETATM 6911  C24 OLC C 404      53.505 -10.057   4.951  1.00 78.86           C  
ANISOU 6911  C24 OLC C 404     8356   9851  11755  -1219   1507    908       C  
HETATM 6912  C16 OLC C 404      62.406   5.582   9.060  1.00 76.96           C  
ANISOU 6912  C16 OLC C 404    11001   8701   9541    972   2167    133       C  
HETATM 6913  C12 OLC C 404      62.303   0.473   9.563  1.00 75.87           C  
ANISOU 6913  C12 OLC C 404    10468   8877   9482    414   2115    289       C  
HETATM 6914  C7  OLC C 404      60.854  -4.354   8.536  1.00 70.19           C  
ANISOU 6914  C7  OLC C 404     9216   8368   9086   -103   1969    489       C  
HETATM 6915  C15 OLC C 404      62.054   4.292   9.857  1.00 76.31           C  
ANISOU 6915  C15 OLC C 404    10837   8706   9452    857   2301    161       C  
HETATM 6916  C13 OLC C 404      62.882   1.883   9.883  1.00 74.40           C  
ANISOU 6916  C13 OLC C 404    10523   8587   9161    534   2153    222       C  
HETATM 6917  C6  OLC C 404      60.464  -5.581   7.665  1.00 69.51           C  
ANISOU 6917  C6  OLC C 404     8960   8322   9130   -252   1814    537       C  
HETATM 6918  C14 OLC C 404      62.233   2.996   9.016  1.00 74.31           C  
ANISOU 6918  C14 OLC C 404    10385   8561   9289    697   2118    218       C  
HETATM 6919  C5  OLC C 404      59.892  -6.782   8.473  1.00 71.28           C  
ANISOU 6919  C5  OLC C 404     9170   8548   9367   -414   1962    593       C  
HETATM 6920  C4  OLC C 404      59.963  -8.082   7.615  1.00 74.96           C  
ANISOU 6920  C4  OLC C 404     9578   9008   9894   -579   1758    625       C  
HETATM 6921  C3  OLC C 404      58.942  -9.198   7.996  1.00 78.17           C  
ANISOU 6921  C3  OLC C 404     9861   9431  10408   -762   1885    695       C  
HETATM 6922  C2  OLC C 404      58.211  -9.705   6.720  1.00 81.24           C  
ANISOU 6922  C2  OLC C 404     9969   9874  11025   -864   1702    728       C  
HETATM 6923  C21 OLC C 404      55.908 -11.032   5.111  1.00 83.84           C  
ANISOU 6923  C21 OLC C 404     9754  10282  11818  -1222   1417    831       C  
HETATM 6924  C1  OLC C 404      57.615 -11.099   6.758  1.00 84.27           C  
ANISOU 6924  C1  OLC C 404    10330  10226  11461  -1101   1688    784       C  
HETATM 6925  C22 OLC C 404      55.026  -9.767   4.858  1.00 81.98           C  
ANISOU 6925  C22 OLC C 404     9164  10159  11826  -1073   1434    839       C  
HETATM 6926  O19 OLC C 404      58.285 -12.100   6.985  1.00 85.31           O  
ANISOU 6926  O19 OLC C 404    10724  10262  11428  -1191   1645    784       O  
HETATM 6927  O25 OLC C 404      52.988 -10.209   3.620  1.00 76.48           O  
ANISOU 6927  O25 OLC C 404     7817   9589  11652  -1223   1177    920       O  
HETATM 6928  O23 OLC C 404      55.379  -8.626   5.670  1.00 82.34           O  
ANISOU 6928  O23 OLC C 404     9259  10226  11803   -853   1659    806       O  
HETATM 6929  O20 OLC C 404      56.290 -11.141   6.502  1.00 85.04           O  
ANISOU 6929  O20 OLC C 404    10093  10402  11817  -1204   1715    835       O  
HETATM 6930  C18 OLC C 405      89.964  12.428  -5.057  1.00 80.38           C  
ANISOU 6930  C18 OLC C 405    11298   8403  10839  -3043   2815   -408       C  
HETATM 6931  C10 OLC C 405      85.440   3.769  -5.742  1.00 80.91           C  
ANISOU 6931  C10 OLC C 405    11197   8998  10548  -1387   2488   -422       C  
HETATM 6932  C9  OLC C 405      85.821   2.577  -6.231  1.00 82.45           C  
ANISOU 6932  C9  OLC C 405    11248   9236  10845  -1298   2619   -468       C  
HETATM 6933  C17 OLC C 405      89.177  11.143  -4.670  1.00 80.58           C  
ANISOU 6933  C17 OLC C 405    11246   8551  10819  -2713   2646   -412       C  
HETATM 6934  C11 OLC C 405      86.315   4.770  -5.020  1.00 80.34           C  
ANISOU 6934  C11 OLC C 405    10973   8926  10627  -1550   2437   -430       C  
HETATM 6935  C8  OLC C 405      87.204   1.956  -6.184  1.00 83.19           C  
ANISOU 6935  C8  OLC C 405    10961   9396  11253  -1312   2758   -535       C  
HETATM 6936  C24 OLC C 405      91.784  -9.630  -2.286  1.00 99.95           C  
ANISOU 6936  C24 OLC C 405    11051  11632  15295    487   2045   -819       C  
HETATM 6937  C16 OLC C 405      88.463  10.490  -5.890  1.00 80.38           C  
ANISOU 6937  C16 OLC C 405    11458   8506  10578  -2563   2847   -384       C  
HETATM 6938  C12 OLC C 405      87.111   5.635  -6.039  1.00 80.74           C  
ANISOU 6938  C12 OLC C 405    11084   8901  10693  -1769   2736   -445       C  
HETATM 6939  C7  OLC C 405      87.336   0.972  -4.986  1.00 83.23           C  
ANISOU 6939  C7  OLC C 405    10706   9488  11430  -1144   2503   -545       C  
HETATM 6940  C15 OLC C 405      88.922   9.020  -6.102  1.00 79.47           C  
ANISOU 6940  C15 OLC C 405    11020   8532  10643  -2433   2979   -431       C  
HETATM 6941  C13 OLC C 405      87.450   7.039  -5.457  1.00 80.26           C  
ANISOU 6941  C13 OLC C 405    11084   8775  10638  -1961   2651   -424       C  
HETATM 6942  C6  OLC C 405      87.747  -0.458  -5.441  1.00 85.05           C  
ANISOU 6942  C6  OLC C 405    10807   9737  11771   -989   2639   -596       C  
HETATM 6943  C14 OLC C 405      87.755   8.101  -6.551  1.00 79.28           C  
ANISOU 6943  C14 OLC C 405    11200   8524  10400  -2176   2930   -408       C  
HETATM 6944  C5  OLC C 405      87.856  -1.445  -4.243  1.00 86.49           C  
ANISOU 6944  C5  OLC C 405    10749   9984  12131   -826   2373   -598       C  
HETATM 6945  C4  OLC C 405      87.717  -2.928  -4.689  1.00 88.06           C  
ANISOU 6945  C4  OLC C 405    10955  10163  12341   -639   2453   -632       C  
HETATM 6946  C3  OLC C 405      89.096  -3.558  -5.032  1.00 90.08           C  
ANISOU 6946  C3  OLC C 405    10869  10439  12919   -583   2658   -708       C  
HETATM 6947  C2  OLC C 405      89.206  -5.018  -4.508  1.00 92.44           C  
ANISOU 6947  C2  OLC C 405    11048  10734  13341   -354   2530   -727       C  
HETATM 6948  C21 OLC C 405      91.656  -7.462  -3.706  1.00 98.04           C  
ANISOU 6948  C21 OLC C 405    10939  11462  14849     83   2486   -841       C  
HETATM 6949  C1  OLC C 405      90.560  -5.638  -4.759  1.00 94.63           C  
ANISOU 6949  C1  OLC C 405    10959  11026  13970   -260   2712   -802       C  
HETATM 6950  C22 OLC C 405      91.350  -8.138  -2.341  1.00 99.57           C  
ANISOU 6950  C22 OLC C 405    11103  11655  15075    220   2055   -782       C  
HETATM 6951  O19 OLC C 405      91.039  -5.690  -5.886  1.00 94.73           O  
ANISOU 6951  O19 OLC C 405    10962  11005  14026   -283   3078   -865       O  
HETATM 6952  O25 OLC C 405      90.994 -10.317  -1.293  1.00 99.91           O  
ANISOU 6952  O25 OLC C 405    11230  11585  15147    582   1689   -748       O  
HETATM 6953  O23 OLC C 405      91.941  -7.382  -1.268  1.00100.24           O  
ANISOU 6953  O23 OLC C 405    10917  11814  15356    134   1792   -751       O  
HETATM 6954  O20 OLC C 405      91.175  -6.099  -3.651  1.00 96.33           O  
ANISOU 6954  O20 OLC C 405    10875  11284  14440   -149   2444   -793       O  
HETATM 6955  C18 OLC C 406      86.629  18.592  -4.746  1.00 58.19           C  
ANISOU 6955  C18 OLC C 406    10763   4561   6786  -3266   2397   -177       C  
HETATM 6956  C10 OLC C 406      84.255   9.806  -7.189  1.00 72.68           C  
ANISOU 6956  C10 OLC C 406    11453   7390   8773  -1957   2575   -230       C  
HETATM 6957  C9  OLC C 406      83.681   8.614  -7.453  1.00 73.11           C  
ANISOU 6957  C9  OLC C 406    11451   7528   8799  -1774   2540   -234       C  
HETATM 6958  C17 OLC C 406      86.774  17.044  -4.720  1.00 60.72           C  
ANISOU 6958  C17 OLC C 406    10620   5147   7304  -3101   2362   -221       C  
HETATM 6959  C11 OLC C 406      83.549  11.073  -6.738  1.00 68.98           C  
ANISOU 6959  C11 OLC C 406    11257   6793   8157  -1963   2407   -181       C  
HETATM 6960  C8  OLC C 406      84.409   7.369  -7.895  1.00 72.88           C  
ANISOU 6960  C8  OLC C 406    11180   7598   8912  -1754   2717   -290       C  
HETATM 6961  C24 OLC C 406      86.868  -4.482 -10.212  1.00 80.42           C  
ANISOU 6961  C24 OLC C 406    11105   8827  10623   -628   3556   -781       C  
HETATM 6962  C16 OLC C 406      85.521  16.300  -4.182  1.00 60.91           C  
ANISOU 6962  C16 OLC C 406    10711   5246   7187  -2736   2206   -198       C  
HETATM 6963  C12 OLC C 406      84.439  11.865  -5.747  1.00 64.83           C  
ANISOU 6963  C12 OLC C 406    10575   6260   7799  -2129   2348   -216       C  
HETATM 6964  C7  OLC C 406      83.528   6.506  -8.836  1.00 74.08           C  
ANISOU 6964  C7  OLC C 406    11558   7724   8865  -1624   2754   -271       C  
HETATM 6965  C15 OLC C 406      85.311  14.990  -4.991  1.00 62.57           C  
ANISOU 6965  C15 OLC C 406    10639   5645   7492  -2615   2325   -210       C  
HETATM 6966  C13 OLC C 406      83.645  13.040  -5.132  1.00 63.45           C  
ANISOU 6966  C13 OLC C 406    10713   5932   7462  -2119   2186   -177       C  
HETATM 6967  C6  OLC C 406      84.404   5.434  -9.552  1.00 74.25           C  
ANISOU 6967  C6  OLC C 406    11412   7799   9001  -1627   3006   -338       C  
HETATM 6968  C14 OLC C 406      84.536  13.905  -4.198  1.00 63.29           C  
ANISOU 6968  C14 OLC C 406    10596   5873   7578  -2312   2114   -216       C  
HETATM 6969  C5  OLC C 406      83.581   4.380 -10.348  1.00 72.27           C  
ANISOU 6969  C5  OLC C 406    11341   7535   8581  -1477   2983   -335       C  
HETATM 6970  C4  OLC C 406      83.713   2.957  -9.735  1.00 69.93           C  
ANISOU 6970  C4  OLC C 406    10728   7363   8480  -1330   2928   -389       C  
HETATM 6971  C3  OLC C 406      83.651   1.852 -10.822  1.00 69.93           C  
ANISOU 6971  C3  OLC C 406    10889   7320   8361  -1260   3080   -425       C  
HETATM 6972  C2  OLC C 406      84.845   0.883 -10.645  1.00 73.27           C  
ANISOU 6972  C2  OLC C 406    10993   7807   9038  -1227   3299   -513       C  
HETATM 6973  C21 OLC C 406      86.201  -2.055 -10.799  1.00 81.59           C  
ANISOU 6973  C21 OLC C 406    11611   8934  10456   -942   3551   -677       C  
HETATM 6974  C1  OLC C 406      84.786  -0.327 -11.545  1.00 78.52           C  
ANISOU 6974  C1  OLC C 406    11797   8430   9609  -1118   3407   -559       C  
HETATM 6975  C22 OLC C 406      86.195  -3.173  -9.720  1.00 81.52           C  
ANISOU 6975  C22 OLC C 406    11305   9007  10661   -762   3335   -693       C  
HETATM 6976  O19 OLC C 406      84.692  -0.221 -12.761  1.00 79.41           O  
ANISOU 6976  O19 OLC C 406    12266   8429   9479  -1168   3569   -563       O  
HETATM 6977  O25 OLC C 406      86.747  -5.465  -9.173  1.00 79.81           O  
ANISOU 6977  O25 OLC C 406    10892   8786  10645   -458   3297   -774       O  
HETATM 6978  O23 OLC C 406      86.814  -2.721  -8.503  1.00 82.00           O  
ANISOU 6978  O23 OLC C 406    10989   9170  10999   -783   3207   -685       O  
HETATM 6979  O20 OLC C 406      84.864  -1.510 -10.902  1.00 81.33           O  
ANISOU 6979  O20 OLC C 406    11891   8862  10147   -967   3303   -595       O  
HETATM 6980  C18 OLC C 407      63.625  14.641  11.667  1.00 76.49           C  
ANISOU 6980  C18 OLC C 407    12904   7467   8692   1719   2557   -292       C  
HETATM 6981  C10 OLC C 407      65.424   6.315  12.668  1.00 81.25           C  
ANISOU 6981  C10 OLC C 407    12627   8935   9310    718   2259    -53       C  
HETATM 6982  C9  OLC C 407      65.552   4.996  12.902  1.00 83.86           C  
ANISOU 6982  C9  OLC C 407    12884   9351   9629    594   2235    -12       C  
HETATM 6983  C17 OLC C 407      64.873  13.721  11.725  1.00 77.51           C  
ANISOU 6983  C17 OLC C 407    13228   7606   8617   1426   2411   -321       C  
HETATM 6984  C11 OLC C 407      64.259   7.015  11.996  1.00 78.19           C  
ANISOU 6984  C11 OLC C 407    12024   8568   9115    903   2368    -33       C  
HETATM 6985  C8  OLC C 407      64.563   3.911  12.533  1.00 86.68           C  
ANISOU 6985  C8  OLC C 407    12937   9841  10156    584   2324     61       C  
HETATM 6986  C24 OLC C 407      60.084  -6.000  11.956  1.00101.88           C  
ANISOU 6986  C24 OLC C 407    13530  12312  12870   -345   2611    581       C  
HETATM 6987  C16 OLC C 407      64.909  12.913  13.052  1.00 78.66           C  
ANISOU 6987  C16 OLC C 407    13351   7852   8685   1353   2557   -327       C  
HETATM 6988  C12 OLC C 407      64.448   8.554  12.072  1.00 76.34           C  
ANISOU 6988  C12 OLC C 407    12019   8177   8811   1030   2379    -95       C  
HETATM 6989  C7  OLC C 407      63.846   3.377  13.803  1.00 89.95           C  
ANISOU 6989  C7  OLC C 407    13449  10244  10484    595   2601     70       C  
HETATM 6990  C15 OLC C 407      64.844  11.382  12.784  1.00 77.60           C  
ANISOU 6990  C15 OLC C 407    12831   7944   8709   1238   2464   -242       C  
HETATM 6991  C13 OLC C 407      63.359   9.248  12.942  1.00 75.92           C  
ANISOU 6991  C13 OLC C 407    12173   8014   8657   1184   2671   -149       C  
HETATM 6992  C6  OLC C 407      62.362   3.845  13.902  1.00 92.55           C  
ANISOU 6992  C6  OLC C 407    13574  10606  10985    761   2881     82       C  
HETATM 6993  C14 OLC C 407      63.401  10.808  12.899  1.00 76.05           C  
ANISOU 6993  C14 OLC C 407    12370   7866   8658   1365   2711   -203       C  
HETATM 6994  C5  OLC C 407      61.380   2.871  13.185  1.00 94.59           C  
ANISOU 6994  C5  OLC C 407    13423  11014  11501    721   2892    162       C  
HETATM 6995  C4  OLC C 407      60.817   1.767  14.130  1.00 95.84           C  
ANISOU 6995  C4  OLC C 407    13572  11213  11632    623   3128    205       C  
HETATM 6996  C3  OLC C 407      61.784   0.557  14.270  1.00 97.38           C  
ANISOU 6996  C3  OLC C 407    13888  11416  11697    417   2945    241       C  
HETATM 6997  C2  OLC C 407      61.425  -0.597  13.294  1.00 98.81           C  
ANISOU 6997  C2  OLC C 407    13731  11717  12095    311   2813    313       C  
HETATM 6998  C21 OLC C 407      60.720  -3.644  12.781  1.00100.63           C  
ANISOU 6998  C21 OLC C 407    13656  12075  12505    -50   2720    464       C  
HETATM 6999  C1  OLC C 407      60.446  -1.574  13.895  1.00100.35           C  
ANISOU 6999  C1  OLC C 407    13829  11957  12344    208   3040    374       C  
HETATM 7000  C22 OLC C 407      60.146  -5.036  13.172  1.00101.28           C  
ANISOU 7000  C22 OLC C 407    13674  12178  12628   -224   2850    539       C  
HETATM 7001  O19 OLC C 407      59.347  -1.202  14.283  1.00101.32           O  
ANISOU 7001  O19 OLC C 407    13811  12107  12577    280   3328    383       O  
HETATM 7002  O25 OLC C 407      59.548  -7.266  12.384  1.00102.33           O  
ANISOU 7002  O25 OLC C 407    13565  12365  12952   -524   2735    651       O  
HETATM 7003  O23 OLC C 407      60.880  -5.631  14.260  1.00100.57           O  
ANISOU 7003  O23 OLC C 407    13950  11987  12275   -310   2911    549       O  
HETATM 7004  O20 OLC C 407      60.877  -2.847  13.976  1.00100.50           O  
ANISOU 7004  O20 OLC C 407    13924  11974  12289     37   2916    418       O  
HETATM 7005  C18 OLC C 408      81.119   2.033  11.770  1.00 77.49           C  
ANISOU 7005  C18 OLC C 408    11596   8512   9334   -676   -254   -224       C  
HETATM 7006  C10 OLC C 408      77.884  -2.959  10.316  1.00 70.32           C  
ANISOU 7006  C10 OLC C 408    10455   7819   8444   -273    246    -15       C  
HETATM 7007  C9  OLC C 408      78.657  -3.926  10.836  1.00 68.95           C  
ANISOU 7007  C9  OLC C 408    10270   7613   8315   -251     75      1       C  
HETATM 7008  C17 OLC C 408      81.038   0.486  11.743  1.00 78.48           C  
ANISOU 7008  C17 OLC C 408    11626   8690   9502   -566   -268   -173       C  
HETATM 7009  C11 OLC C 408      76.587  -2.420  10.875  1.00 70.42           C  
ANISOU 7009  C11 OLC C 408    10658   7816   8283   -263    383      8       C  
HETATM 7010  C8  OLC C 408      78.418  -4.716  12.102  1.00 66.67           C  
ANISOU 7010  C8  OLC C 408    10199   7253   7880   -231    -37     52       C  
HETATM 7011  C24 OLC C 408      74.044 -11.334   4.412  1.00 49.61           C  
ANISOU 7011  C24 OLC C 408     7584   5162   6103   -205    615    134       C  
HETATM 7012  C16 OLC C 408      80.071  -0.007  10.629  1.00 80.51           C  
ANISOU 7012  C16 OLC C 408    11759   9025   9805   -488    -17   -149       C  
HETATM 7013  C12 OLC C 408      75.853  -1.574   9.803  1.00 70.40           C  
ANISOU 7013  C12 OLC C 408    10581   7855   8314   -257    549    -11       C  
HETATM 7014  C7  OLC C 408      79.410  -5.910  12.172  1.00 63.21           C  
ANISOU 7014  C7  OLC C 408     9673   6781   7565   -181   -237     68       C  
HETATM 7015  C15 OLC C 408      78.585   0.397  10.878  1.00 81.30           C  
ANISOU 7015  C15 OLC C 408    12062   9109   9717   -437    174   -127       C  
HETATM 7016  C13 OLC C 408      76.197  -0.071   9.923  1.00 73.50           C  
ANISOU 7016  C13 OLC C 408    11060   8200   8666   -302    525    -61       C  
HETATM 7017  C6  OLC C 408      78.747  -7.196  11.611  1.00 60.75           C  
ANISOU 7017  C6  OLC C 408     9336   6470   7277   -127   -137    112       C  
HETATM 7018  C14 OLC C 408      77.699   0.198   9.604  1.00 78.88           C  
ANISOU 7018  C14 OLC C 408    11617   8876   9477   -379    375   -104       C  
HETATM 7019  C5  OLC C 408      79.750  -8.115  10.857  1.00 56.50           C  
ANISOU 7019  C5  OLC C 408     8595   5923   6949    -52   -240     94       C  
HETATM 7020  C4  OLC C 408      79.658  -7.992   9.304  1.00 52.71           C  
ANISOU 7020  C4  OLC C 408     7893   5517   6617    -46    -56     47       C  
HETATM 7021  C3  OLC C 408      78.210  -8.124   8.758  1.00 49.99           C  
ANISOU 7021  C3  OLC C 408     7619   5206   6169    -80    153     73       C  
HETATM 7022  C2  OLC C 408      78.179  -8.001   7.211  1.00 50.17           C  
ANISOU 7022  C2  OLC C 408     7477   5281   6304    -82    300     26       C  
HETATM 7023  C21 OLC C 408      75.458 -10.220   6.247  1.00 55.87           C  
ANISOU 7023  C21 OLC C 408     8368   5965   6895   -128    495    123       C  
HETATM 7024  C1  OLC C 408      76.832  -8.364   6.621  1.00 53.58           C  
ANISOU 7024  C1  OLC C 408     7969   5731   6658   -111    439     57       C  
HETATM 7025  C22 OLC C 408      74.655 -10.014   4.944  1.00 54.18           C  
ANISOU 7025  C22 OLC C 408     8104   5796   6687   -174    609    110       C  
HETATM 7026  O19 OLC C 408      75.886  -7.608   6.611  1.00 57.90           O  
ANISOU 7026  O19 OLC C 408     8559   6318   7121   -154    524     74       O  
HETATM 7027  O25 OLC C 408      72.623 -11.197   4.493  1.00 48.30           O  
ANISOU 7027  O25 OLC C 408     7428   5038   5886   -286    669    186       O  
HETATM 7028  O23 OLC C 408      73.654  -9.009   5.164  1.00 57.31           O  
ANISOU 7028  O23 OLC C 408     8499   6256   7020   -216    675    136       O  
HETATM 7029  O20 OLC C 408      76.739  -9.575   6.092  1.00 55.59           O  
ANISOU 7029  O20 OLC C 408     8222   5947   6953    -85    452     63       O  
HETATM 7030  C1  GOL C 409      69.528  26.305  -3.215  1.00 74.62           C  
ANISOU 7030  C1  GOL C 409    16144   4763   7443    768    720    310       C  
HETATM 7031  O1  GOL C 409      68.458  26.960  -2.520  1.00 76.19           O  
ANISOU 7031  O1  GOL C 409    16281   4916   7751   1172    680    297       O  
HETATM 7032  C2  GOL C 409      69.478  26.793  -4.682  1.00 73.71           C  
ANISOU 7032  C2  GOL C 409    16311   4483   7212    763    591    433       C  
HETATM 7033  O2  GOL C 409      69.986  28.144  -4.784  1.00 73.75           O  
ANISOU 7033  O2  GOL C 409    16839   4145   7037    635    606    449       O  
HETATM 7034  C3  GOL C 409      70.138  25.799  -5.674  1.00 68.95           C  
ANISOU 7034  C3  GOL C 409    15517   4090   6591    522    596    479       C  
HETATM 7035  O3  GOL C 409      71.520  25.618  -5.323  1.00 66.18           O  
ANISOU 7035  O3  GOL C 409    15168   3790   6187    126    764    419       O  
HETATM 7036  O   HOH A 501      62.213  -5.233  35.125  1.00 34.13           O  
ANISOU 7036  O   HOH A 501     5730   3186   4051  -1180   1123   -116       O  
HETATM 7037  O   HOH A 502      85.850  10.670  26.185  1.00 43.58           O  
ANISOU 7037  O   HOH A 502     5631   4601   6328     99    541   -339       O  
HETATM 7038  O   HOH A 503      74.230  -4.157  28.995  1.00 44.95           O  
ANISOU 7038  O   HOH A 503     7013   4310   5758      8    329     11       O  
HETATM 7039  O   HOH A 504      81.816  36.833  35.852  1.00 32.04           O  
ANISOU 7039  O   HOH A 504     5263   1848   5062   -468     81   -818       O  
HETATM 7040  O   HOH A 505      61.260  -9.273  25.400  1.00 37.38           O  
ANISOU 7040  O   HOH A 505     6003   3435   4764  -1242    550   -293       O  
HETATM 7041  O   HOH A 506      86.050  23.908  30.456  1.00 22.84           O  
ANISOU 7041  O   HOH A 506     3222   1783   3673   -366    217   -347       O  
HETATM 7042  O   HOH A 507      74.063  28.814  37.529  1.00 36.06           O  
ANISOU 7042  O   HOH A 507     5357   3020   5324    141    379   -842       O  
HETATM 7043  O   HOH A 508      68.965  -0.511  31.838  1.00 37.25           O  
ANISOU 7043  O   HOH A 508     5854   3703   4597   -322    502     -9       O  
HETATM 7044  O   HOH A 509      67.981  12.766  35.490  1.00 22.03           O  
ANISOU 7044  O   HOH A 509     3305   2019   3044    -25    643   -408       O  
HETATM 7045  O   HOH A 510      78.302  26.967  23.784  1.00 45.24           O  
ANISOU 7045  O   HOH A 510     6893   4112   6185   -251     57    165       O  
HETATM 7046  O   HOH A 511      83.192 -18.856  28.887  1.00 50.30           O  
ANISOU 7046  O   HOH A 511     8325   2720   8066   1168   -227   -154       O  
HETATM 7047  O   HOH A 512      75.693  31.840  35.360  1.00 33.25           O  
ANISOU 7047  O   HOH A 512     5100   2363   5170    104    204   -717       O  
HETATM 7048  O   HOH A 513      85.054  25.691  26.705  1.00 32.95           O  
ANISOU 7048  O   HOH A 513     4804   2876   4840   -530    431   -186       O  
HETATM 7049  O   HOH A 514      80.357  30.422  39.747  1.00 31.32           O  
ANISOU 7049  O   HOH A 514     4998   2449   4454   -290     91   -914       O  
HETATM 7050  O   HOH A 515      76.166   6.908  30.286  1.00 44.12           O  
ANISOU 7050  O   HOH A 515     6321   4715   5728    127    245    -45       O  
HETATM 7051  O   HOH A 516      75.219  38.818  26.993  1.00 60.17           O  
ANISOU 7051  O   HOH A 516     9253   4587   9023     76   -416      9       O  
HETATM 7052  O   HOH A 517      75.675  27.581  40.729  1.00 54.65           O  
ANISOU 7052  O   HOH A 517     7925   5553   7288    -68    413   -975       O  
HETATM 7053  O   HOH A 518      76.312  32.042  28.082  1.00 41.81           O  
ANISOU 7053  O   HOH A 518     6398   3245   6242     21   -102    -91       O  
HETATM 7054  O   HOH A 519      79.830 -17.822  37.809  1.00 67.91           O  
ANISOU 7054  O   HOH A 519    11795   5000   9010    555  -1158    911       O  
HETATM 7055  O   HOH A 520      61.009 -15.660  12.426  1.00 91.69           O  
ANISOU 7055  O   HOH A 520    14129   9794  10914  -2020     20   -941       O  
HETATM 7056  O   HOH A 521      76.142 -18.452  36.284  1.00 61.32           O  
ANISOU 7056  O   HOH A 521    11126   4351   7822     64   -571    797       O  
HETATM 7057  O   HOH A 522      85.956  27.846  32.747  1.00 29.28           O  
ANISOU 7057  O   HOH A 522     4206   2397   4522   -491     87   -469       O  
HETATM 7058  O   HOH A 523      91.481  22.303  41.796  1.00 65.51           O  
ANISOU 7058  O   HOH A 523     8515   7337   9038   -440  -1200   -659       O  
HETATM 7059  O   HOH A 524      78.910  43.557  40.997  1.00 46.20           O  
ANISOU 7059  O   HOH A 524     7437   3546   6570  -1206   1108     87       O  
HETATM 7060  O   HOH A 525      70.193 -15.601  25.497  1.00 47.08           O  
ANISOU 7060  O   HOH A 525     8268   3625   5993   -559    574   -181       O  
HETATM 7061  O   HOH A 526      77.995   6.882  37.501  1.00 46.28           O  
ANISOU 7061  O   HOH A 526     6954   4912   5720     91   -105     29       O  
HETATM 7062  O   HOH A 527      76.291  40.628  35.564  1.00 40.23           O  
ANISOU 7062  O   HOH A 527     6492   2145   6650     53    121   -972       O  
HETATM 7063  O   HOH A 528      81.705 -19.620  36.987  1.00 58.53           O  
ANISOU 7063  O   HOH A 528    10527   3399   8315    913  -1389    867       O  
HETATM 7064  O   HOH A 529      92.829  28.949  36.307  1.00 73.62           O  
ANISOU 7064  O   HOH A 529     9254   8109  10610   -917   -368   -836       O  
HETATM 7065  O   HOH A 530      75.354 -11.894  40.621  1.00 66.26           O  
ANISOU 7065  O   HOH A 530    11600   5863   7712   -267   -530    887       O  
HETATM 7066  O   HOH A 531      66.522  -7.023  29.176  1.00 39.38           O  
ANISOU 7066  O   HOH A 531     6466   3641   4855   -684    583    -43       O  
HETATM 7067  O   HOH A 532      89.458  35.209  39.573  1.00 71.01           O  
ANISOU 7067  O   HOH A 532     9803   7267   9910  -1094   -355  -1092       O  
HETATM 7068  O   HOH A 533      72.205 -11.245  30.924  1.00 79.21           O  
ANISOU 7068  O   HOH A 533    12101   8029   9965   -272    320    171       O  
HETATM 7069  O   HOH A 534      69.297 -20.778  18.676  1.00 53.01           O  
ANISOU 7069  O   HOH A 534     9629   3822   6691   -973    875   -820       O  
HETATM 7070  O   HOH A 535      69.856   4.212  22.558  1.00 22.62           O  
ANISOU 7070  O   HOH A 535     3768   1990   2836   -209    204    -67       O  
HETATM 7071  O   HOH A 536      61.900 -12.469  28.625  1.00 50.32           O  
ANISOU 7071  O   HOH A 536     8141   4731   6249  -1414    808   -156       O  
HETATM 7072  O   HOH A 537      74.941  35.668  17.326  1.00 75.88           O  
ANISOU 7072  O   HOH A 537    12238   6587  10008   -418   -940    988       O  
HETATM 7073  O   HOH A 538      71.573 -10.646  38.235  1.00 57.48           O  
ANISOU 7073  O   HOH A 538    10063   5172   6603   -575    130    588       O  
HETATM 7074  O   HOH A 539      77.863 -13.187  45.303  1.00 74.75           O  
ANISOU 7074  O   HOH A 539    13623   6408   8372   -243  -1443   1395       O  
HETATM 7075  O   HOH A 540      59.173 -12.381  33.558  1.00 54.20           O  
ANISOU 7075  O   HOH A 540     8736   5261   6596  -1903   1307   -112       O  
HETATM 7076  O   HOH A 541      74.712 -17.738  19.086  1.00 43.96           O  
ANISOU 7076  O   HOH A 541     7988   2820   5895   -257   1001   -841       O  
HETATM 7077  O   HOH A 542      85.464  -3.435  36.386  1.00 46.58           O  
ANISOU 7077  O   HOH A 542     6897   4045   6756    837   -996    256       O  
HETATM 7078  O   HOH A 543      66.144  13.437  37.325  1.00 27.80           O  
ANISOU 7078  O   HOH A 543     3985   2751   3826   -101    898   -595       O  
HETATM 7079  O   HOH A 544      78.724 -14.193  40.273  1.00 53.84           O  
ANISOU 7079  O   HOH A 544    10060   3775   6620    223  -1124   1017       O  
HETATM 7080  O   HOH A 545      80.474  -8.894  44.633  1.00 45.35           O  
ANISOU 7080  O   HOH A 545     9029   3186   5018    109  -1606   1123       O  
HETATM 7081  O   HOH A 546      75.575   4.567  31.665  1.00 50.55           O  
ANISOU 7081  O   HOH A 546     7277   5465   6464    107    222     -4       O  
HETATM 7082  O   HOH A 547      70.130  33.758  41.892  1.00 61.59           O  
ANISOU 7082  O   HOH A 547     8681   5723   8997    282    958  -1658       O  
HETATM 7083  O   HOH A 548      70.752  -3.014  34.038  1.00 29.31           O  
ANISOU 7083  O   HOH A 548     5242   2463   3433   -316    409    136       O  
HETATM 7084  O   HOH A 549      86.899 -10.330  11.711  1.00 89.96           O  
ANISOU 7084  O   HOH A 549    12665   9085  12429     74   2779  -2019       O  
HETATM 7085  O   HOH A 550      51.674   0.615  27.614  1.00 64.52           O  
ANISOU 7085  O   HOH A 550     7143   7568   9805  -1141    503   -852       O  
HETATM 7086  O   HOH A 551      66.386  -7.656  46.128  1.00 59.17           O  
ANISOU 7086  O   HOH A 551    11164   5713   5605  -1729   1028    532       O  
HETATM 7087  O   HOH A 552      83.285  28.599  31.928  1.00 38.79           O  
ANISOU 7087  O   HOH A 552     5608   3480   5650   -365    129   -387       O  
HETATM 7088  O   HOH A 553      61.465 -25.314  16.028  1.00 83.65           O  
ANISOU 7088  O   HOH A 553    14010   7501  10273  -2346    684  -1125       O  
HETATM 7089  O   HOH A 554      72.791  26.403  37.579  1.00 55.51           O  
ANISOU 7089  O   HOH A 554     7724   5661   7706    175    452   -802       O  
HETATM 7090  O   HOH A 555      79.518  30.451  26.342  1.00 44.30           O  
ANISOU 7090  O   HOH A 555     6763   3772   6297   -292     67     16       O  
HETATM 7091  O   HOH A 556      65.834 -19.939   8.998  1.00 51.62           O  
ANISOU 7091  O   HOH A 556    10104   4010   5500  -1984    749  -1496       O  
HETATM 7092  O   HOH A 557      52.483 -10.413  34.018  1.00 46.29           O  
ANISOU 7092  O   HOH A 557     6587   4723   6279  -2531   1912   -657       O  
HETATM 7093  O   HOH A 558      73.158  -2.898  31.148  1.00 46.53           O  
ANISOU 7093  O   HOH A 558     7231   4612   5837    -70    304     81       O  
HETATM 7094  O   HOH A 559      85.395  32.619  23.715  1.00 52.23           O  
ANISOU 7094  O   HOH A 559     7971   4640   7232  -1029    500     40       O  
HETATM 7095  O   HOH A 560      72.206 -20.024  20.127  1.00 64.02           O  
ANISOU 7095  O   HOH A 560    10848   5149   8329   -539    877   -728       O  
HETATM 7096  O   HOH A 561      72.648  -8.566  31.002  1.00 56.28           O  
ANISOU 7096  O   HOH A 561     8931   5380   7072   -168    299    145       O  
HETATM 7097  O   HOH A 562      86.625  -7.899  23.873  1.00 85.81           O  
ANISOU 7097  O   HOH A 562    11365   8748  12490    900    753   -764       O  
HETATM 7098  O   HOH A 563      63.993 -19.088  13.544  1.00 64.25           O  
ANISOU 7098  O   HOH A 563    11083   5804   7525  -1836    526  -1081       O  
HETATM 7099  O   HOH A 564      81.889  31.884  42.666  1.00 51.62           O  
ANISOU 7099  O   HOH A 564     7793   4962   6856   -509    -13  -1151       O  
HETATM 7100  O   HOH A 565      76.832 -13.106  27.496  1.00 57.32           O  
ANISOU 7100  O   HOH A 565     9154   4867   7757    246    310   -101       O  
HETATM 7101  O   HOH A 566     119.768  23.007  27.011  1.00 75.25           O  
ANISOU 7101  O   HOH A 566     1979   8687  17927  -2077   1769  -3695       O  
HETATM 7102  O   HOH A 567      55.501 -12.267  34.118  1.00 60.64           O  
ANISOU 7102  O   HOH A 567     9134   6251   7657  -2371   1685   -356       O  
HETATM 7103  O   HOH A 568      81.301  35.617  41.156  1.00 65.46           O  
ANISOU 7103  O   HOH A 568     9601   6318   8952   -501    102  -1230       O  
HETATM 7104  O   HOH A 569      87.806  22.981  16.666  1.00 67.51           O  
ANISOU 7104  O   HOH A 569     9790   7218   8643  -1308   1489   -129       O  
HETATM 7105  O   HOH A 570      53.773  -3.749  45.414  1.00 77.00           O  
ANISOU 7105  O   HOH A 570    11403   8792   9061  -2799   3386   -887       O  
HETATM 7106  O   HOH A 571      84.329  -8.408  20.390  1.00 51.56           O  
ANISOU 7106  O   HOH A 571     7407   4484   7701    557   1198   -933       O  
HETATM 7107  O   HOH A 572      51.953   3.375  27.757  1.00 68.44           O  
ANISOU 7107  O   HOH A 572     7470   8071  10461   -847    425   -861       O  
HETATM 7108  O   HOH A 573      62.369  12.799  22.254  1.00 54.61           O  
ANISOU 7108  O   HOH A 573     7055   5961   7735     70   -597    -25       O  
HETATM 7109  O   HOH A 574      83.074   2.592  40.720  1.00 69.01           O  
ANISOU 7109  O   HOH A 574    10142   7378   8699    321  -1047    313       O  
HETATM 7110  O   HOH A 575      81.241  -1.074  45.371  1.00 77.20           O  
ANISOU 7110  O   HOH A 575    12398   8035   8899    -17  -1369    714       O  
HETATM 7111  O   HOH A 576      98.762  22.042  40.350  1.00 65.64           O  
ANISOU 7111  O   HOH A 576     7153   7380  10408   -548  -1644   -928       O  
HETATM 7112  O   HOH A 577      87.013  -3.395  21.110  1.00 56.49           O  
ANISOU 7112  O   HOH A 577     7444   5489   8528    561   1209   -912       O  
HETATM 7113  O   HOH A 578      67.152 -16.654  26.724  1.00 74.09           O  
ANISOU 7113  O   HOH A 578    11848   7028   9277   -970    632   -110       O  
HETATM 7114  O   HOH A 579      86.966  -5.045  23.255  1.00 55.02           O  
ANISOU 7114  O   HOH A 579     7263   5137   8506    774    858   -778       O  
HETATM 7115  O   HOH A 580     110.376  16.842  30.736  1.00 88.38           O  
ANISOU 7115  O   HOH A 580     6412  10219  16949   -358    -30  -2171       O  
HETATM 7116  O   HOH A 581      61.983 -12.712  36.894  1.00 62.08           O  
ANISOU 7116  O   HOH A 581    10400   6019   7169  -1759   1234    188       O  
HETATM 7117  O   HOH A 582      84.993 -10.711  21.705  1.00 66.87           O  
ANISOU 7117  O   HOH A 582     9340   6111   9958    801   1002   -910       O  
HETATM 7118  O   HOH A 583      85.458  33.323  19.203  1.00 67.84           O  
ANISOU 7118  O   HOH A 583    10568   6389   8819  -1413    685    334       O  
HETATM 7119  O   HOH A 584      46.028 -11.990  27.025  1.00 69.96           O  
ANISOU 7119  O   HOH A 584     8109   7927  10547  -3056   1094  -1214       O  
HETATM 7120  O   HOH A 585      73.422  -4.360  34.606  1.00 46.85           O  
ANISOU 7120  O   HOH A 585     7628   4478   5694   -136    181    241       O  
HETATM 7121  O   HOH A 586      63.586  16.210  38.080  1.00 65.62           O  
ANISOU 7121  O   HOH A 586     8443   7456   9034     -6   1133   -907       O  
HETATM 7122  O   HOH A 587      56.433   8.416  29.855  1.00 45.43           O  
ANISOU 7122  O   HOH A 587     4974   5078   7208   -290    509   -702       O  
HETATM 7123  O   HOH A 588      76.889 -17.661  23.296  1.00 48.65           O  
ANISOU 7123  O   HOH A 588     8388   3226   6872    195    672   -516       O  
HETATM 7124  O   HOH A 589      79.120  32.992  25.266  1.00 46.33           O  
ANISOU 7124  O   HOH A 589     7281   3704   6618   -343    -38    120       O  
HETATM 7125  O   HOH A 590      88.974  -2.692  26.439  1.00 48.71           O  
ANISOU 7125  O   HOH A 590     6068   4457   7983    930    392   -624       O  
HETATM 7126  O   HOH A 591      88.853  -4.075  28.759  1.00 68.14           O  
ANISOU 7126  O   HOH A 591     8635   6740  10514   1100    -39   -449       O  
HETATM 7127  O   HOH A 592     117.264  16.723  29.707  1.00 80.08           O  
ANISOU 7127  O   HOH A 592     2934   9122  18370   -548    328  -3196       O  
HETATM 7128  O   HOH A 593      89.090  -7.796  33.165  1.00 64.54           O  
ANISOU 7128  O   HOH A 593     8650   5742  10131   1405   -970    -36       O  
HETATM 7129  O   HOH A 594      71.246  19.298  49.472  1.00 62.20           O  
ANISOU 7129  O   HOH A 594     9969   6907   6757   -774   1178  -1231       O  
HETATM 7130  O   HOH A 595      50.626  -2.297  33.520  1.00 61.33           O  
ANISOU 7130  O   HOH A 595     7065   7137   9100  -1794   1766  -1070       O  
HETATM 7131  O   HOH A 596      60.988 -13.164  31.627  1.00 65.08           O  
ANISOU 7131  O   HOH A 596    10214   6518   7996  -1653   1040    -67       O  
HETATM 7132  O   HOH A 597      68.165  18.844  42.320  1.00 52.98           O  
ANISOU 7132  O   HOH A 597     7566   5782   6781   -169   1144  -1001       O  
HETATM 7133  O   HOH A 598      60.359  16.306  25.611  1.00 48.37           O  
ANISOU 7133  O   HOH A 598     5722   5061   7597    360   -428   -279       O  
HETATM 7134  O   HOH A 599      77.459  34.446  27.153  1.00 37.78           O  
ANISOU 7134  O   HOH A 599     6135   2448   5771   -125   -144    -10       O  
HETATM 7135  O   HOH A 600      73.720  26.385  17.396  1.00 54.54           O  
ANISOU 7135  O   HOH A 600     8763   4992   6968   -299   -587    668       O  
HETATM 7136  O   HOH A 601      87.241 -10.882  46.585  1.00 91.05           O  
ANISOU 7136  O   HOH A 601    14771   8171  11651    896  -3290   1476       O  
HETATM 7137  O   HOH A 602      93.620   5.810  30.576  1.00 65.43           O  
ANISOU 7137  O   HOH A 602     7326   7053  10482    714   -157   -626       O  
HETATM 7138  O   HOH A 603      71.236  23.457  48.451  1.00 66.15           O  
ANISOU 7138  O   HOH A 603    10127   7251   7756   -555   1241  -1481       O  
HETATM 7139  O   HOH A 604      92.184   3.625  28.994  1.00 60.29           O  
ANISOU 7139  O   HOH A 604     6896   6307   9703    778     75   -624       O  
HETATM 7140  O   HOH A 605      61.663 -15.327  25.313  1.00 75.76           O  
ANISOU 7140  O   HOH A 605    11590   7704   9493  -1570    698   -304       O  
HETATM 7141  O   HOH A 606      86.438  -6.951  12.534  1.00 76.45           O  
ANISOU 7141  O   HOH A 606    10825   7731  10493    -39   2542  -1710       O  
HETATM 7142  O   HOH A 607      59.520  20.560  25.340  1.00 55.24           O  
ANISOU 7142  O   HOH A 607     6440   5604   8944    670   -720   -290       O  
HETATM 7143  O   HOH A 608      74.000  -3.627  47.666  1.00 84.04           O  
ANISOU 7143  O   HOH A 608    14270   8884   8780   -906   -291    741       O  
HETATM 7144  O   HOH A 609      61.729  39.260  30.496  1.00 89.17           O  
ANISOU 7144  O   HOH A 609    11246   7732  14902   1691   -668   -907       O  
HETATM 7145  O   HOH A 610      85.657  -4.174  16.866  1.00 69.74           O  
ANISOU 7145  O   HOH A 610     9593   7162   9744    199   1743  -1141       O  
HETATM 7146  O   HOH A 611      71.383   8.937  49.370  1.00 53.53           O  
ANISOU 7146  O   HOH A 611     9503   5827   5009  -1025    755   -352       O  
HETATM 7147  O   HOH A 612      68.222  34.627  39.503  1.00 63.15           O  
ANISOU 7147  O   HOH A 612     8579   5702   9712    582    810  -1547       O  
HETATM 7148  O   HOH A 613      53.590   7.936  34.806  1.00 60.20           O  
ANISOU 7148  O   HOH A 613     6523   7020   9330   -618   1469  -1185       O  
HETATM 7149  O   HOH A 614      84.485  -1.238  40.957  1.00 76.15           O  
ANISOU 7149  O   HOH A 614    11178   7927   9827    535  -1386    479       O  
HETATM 7150  O   HOH A 615      61.850  10.553  44.064  1.00 60.15           O  
ANISOU 7150  O   HOH A 615     8520   6904   7430   -852   2036  -1055       O  
HETATM 7151  O   HOH A 616      68.051  17.185  48.499  1.00 54.63           O  
ANISOU 7151  O   HOH A 616     8689   6032   6038   -774   1636  -1236       O  
HETATM 7152  O   HOH A 617      85.167  16.057  17.782  1.00 65.77           O  
ANISOU 7152  O   HOH A 617     9294   7271   8424   -714   1229   -226       O  
HETATM 7153  O   HOH A 618      50.397  -5.829  22.516  1.00 60.98           O  
ANISOU 7153  O   HOH A 618     7150   6961   9058  -1799   -116   -811       O  
HETATM 7154  O   HOH A 619     110.233  36.582  34.075  1.00 83.58           O  
ANISOU 7154  O   HOH A 619     7600   9237  14920  -3200     54  -2173       O  
HETATM 7155  O   HOH A 620      88.216   1.223  40.130  1.00 72.10           O  
ANISOU 7155  O   HOH A 620     9933   7520   9942    757  -1632    272       O  
HETATM 7156  O   HOH A 621      73.577  44.772  21.293  1.00 70.89           O  
ANISOU 7156  O   HOH A 621    11798   4517  10618     99  -1370    798       O  
HETATM 7157  O   HOH A 622      64.687  18.650  37.528  1.00 53.22           O  
ANISOU 7157  O   HOH A 622     6876   5775   7572    148    964   -896       O  
HETATM 7158  O   HOH A 623      55.993  10.213  39.273  1.00 57.28           O  
ANISOU 7158  O   HOH A 623     6774   6609   8380   -657   2036  -1311       O  
HETATM 7159  O   HOH A 624      55.894  10.105  24.892  1.00 67.60           O  
ANISOU 7159  O   HOH A 624     7700   7761  10225    -71   -392   -473       O  
HETATM 7160  O   HOH B 201      77.887  36.024  29.217  1.00 34.95           O  
ANISOU 7160  O   HOH B 201     5283   2135   5860  -1055   -366   -939       O  
HETATM 7161  O   HOH B 202      89.161  45.578  18.884  1.00 69.70           O  
ANISOU 7161  O   HOH B 202    14566   6207   5709  -1528   1449    547       O  
HETATM 7162  O   HOH B 203      83.152  47.068  45.561  1.00 59.26           O  
ANISOU 7162  O   HOH B 203    10256   5074   7185   -764    600    493       O  
HETATM 7163  O   HOH B 204      91.167  49.124  47.941  1.00 50.99           O  
ANISOU 7163  O   HOH B 204     9420   3806   6147   -116  -1296    120       O  
HETATM 7164  O   HOH B 205      83.772  50.107  45.252  1.00 44.10           O  
ANISOU 7164  O   HOH B 205     8141   3223   5392   -647    197    395       O  
HETATM 7165  O   HOH B 206      96.394  38.568  29.959  1.00 41.69           O  
ANISOU 7165  O   HOH B 206     5730   3631   6477  -1110   1126   -861       O  
HETATM 7166  O   HOH B 207     100.930  44.831  32.492  1.00 63.64           O  
ANISOU 7166  O   HOH B 207     7294   6297  10591  -1935   1536  -1533       O  
HETATM 7167  O   HOH B 208      75.930  46.722  26.394  1.00 65.40           O  
ANISOU 7167  O   HOH B 208    10564   5757   8528    358  -2511   -812       O  
HETATM 7168  O   HOH B 209     100.600  42.278  34.281  1.00 43.52           O  
ANISOU 7168  O   HOH B 209     4650   3747   8137  -1139    536  -1645       O  
HETATM 7169  O   HOH B 210      83.894  55.567  27.646  1.00 55.91           O  
ANISOU 7169  O   HOH B 210    12039   3593   5612   -772   -894   1174       O  
HETATM 7170  O   HOH B 211      80.949  42.034  39.449  1.00 37.84           O  
ANISOU 7170  O   HOH B 211     6507   2509   5364  -1170    804    311       O  
HETATM 7171  O   HOH B 212      77.874  62.483  37.026  1.00 46.71           O  
ANISOU 7171  O   HOH B 212     9164   2112   6472    660  -2317   -146       O  
HETATM 7172  O   HOH B 213      74.868  42.439  34.157  1.00 32.79           O  
ANISOU 7172  O   HOH B 213     4389   1978   6092   -924    -67  -1030       O  
HETATM 7173  O   HOH B 214      90.604  47.765  19.536  1.00191.42           O  
ANISOU 7173  O   HOH B 214    30132  21405  21193  -2025   2122    786       O  
HETATM 7174  O   HOH B 215      92.217  45.292  51.161  1.00 57.48           O  
ANISOU 7174  O   HOH B 215    11783   4037   6021    670  -2007    168       O  
HETATM 7175  O   HOH B 216      81.655  30.750  31.661  1.00 34.46           O  
ANISOU 7175  O   HOH B 216     5236   2702   5154   -318    118   -378       O  
HETATM 7176  O   HOH B 217     104.903  42.546  25.777  1.00 73.59           O  
ANISOU 7176  O   HOH B 217     7640   7850  12469  -2923   4423  -3026       O  
HETATM 7177  O   HOH B 218      85.760  45.401  45.973  1.00 37.47           O  
ANISOU 7177  O   HOH B 218     7862   2179   4196   -603    204    642       O  
HETATM 7178  O   HOH B 219      88.552  35.026  21.643  1.00 61.63           O  
ANISOU 7178  O   HOH B 219    10488   6006   6922   -860    716   -726       O  
HETATM 7179  O   HOH B 220      94.731  37.071  37.284  1.00 58.36           O  
ANISOU 7179  O   HOH B 220     8596   5096   8482   -198   -534   -338       O  
HETATM 7180  O   HOH B 221      98.517  44.629  39.168  1.00 54.98           O  
ANISOU 7180  O   HOH B 221     7024   4883   8982   -712   -694  -1005       O  
HETATM 7181  O   HOH B 222      78.255  50.522  43.076  1.00 44.44           O  
ANISOU 7181  O   HOH B 222     7229   3386   6270   -667    612   -194       O  
HETATM 7182  O   HOH B 223      89.909  65.127  41.160  1.00 48.73           O  
ANISOU 7182  O   HOH B 223     9494   1955   7067  -1639   -897    308       O  
HETATM 7183  O   HOH B 224      92.304  59.225  22.082  1.00 85.22           O  
ANISOU 7183  O   HOH B 224    18966   5721   7693  -3437   2877   2017       O  
HETATM 7184  O   HOH B 225      84.118  38.461  42.647  1.00 59.18           O  
ANISOU 7184  O   HOH B 225    10458   4640   7387  -1025    851    750       O  
HETATM 7185  O   HOH B 226      85.245  43.344  34.061  1.00 44.48           O  
ANISOU 7185  O   HOH B 226     7367   3658   5876  -1032    168    473       O  
HETATM 7186  O   HOH B 227     101.201  46.264  36.076  1.00 62.47           O  
ANISOU 7186  O   HOH B 227     6925   5967  10842  -1523    370  -1665       O  
HETATM 7187  O   HOH B 228      85.068  39.099  25.327  1.00 55.84           O  
ANISOU 7187  O   HOH B 228     9475   5150   6590   -871    -13   -116       O  
HETATM 7188  O   HOH B 229      78.436  38.691  27.651  1.00 45.38           O  
ANISOU 7188  O   HOH B 229     7058   3608   6578   -704   -853   -779       O  
HETATM 7189  O   HOH B 230      77.211  45.090  23.284  1.00 76.74           O  
ANISOU 7189  O   HOH B 230    12915   7134   9110    393  -2651   -720       O  
HETATM 7190  O   HOH B 231      73.775  51.407  38.802  1.00 68.07           O  
ANISOU 7190  O   HOH B 231     9028   6358  10477   -150   -347  -1189       O  
HETATM 7191  O   HOH B 232      75.755  43.592  30.636  1.00 64.30           O  
ANISOU 7191  O   HOH B 232     8952   5973   9504   -444  -1085   -935       O  
HETATM 7192  O   HOH B 233      71.345  56.337  36.694  1.00 71.88           O  
ANISOU 7192  O   HOH B 233     9586   6312  11415   1078  -2139  -1922       O  
HETATM 7193  O   HOH B 234      83.634  51.563  49.326  1.00 56.16           O  
ANISOU 7193  O   HOH B 234    10476   4533   6330   -396    276    206       O  
HETATM 7194  O   HOH B 235      89.873  52.122  48.151  1.00 50.27           O  
ANISOU 7194  O   HOH B 235     9281   3734   6086   -277  -1116     90       O  
HETATM 7195  O   HOH B 236      79.998  66.313  37.050  1.00 73.13           O  
ANISOU 7195  O   HOH B 236    13744   4556   9487    460  -2537    275       O  
HETATM 7196  O   HOH B 237      97.621  52.436  42.988  1.00 59.40           O  
ANISOU 7196  O   HOH B 237     8110   5001   9459  -1133  -1180   -901       O  
HETATM 7197  O   HOH B 238      82.532  49.205  50.120  1.00 64.42           O  
ANISOU 7197  O   HOH B 238    11933   5465   7077   -522    859    303       O  
HETATM 7198  O   HOH B 239      78.018  48.307  22.311  1.00 68.78           O  
ANISOU 7198  O   HOH B 239    13253   5694   7188    603  -2902   -225       O  
HETATM 7199  O   HOH B 240      77.124  66.805  39.738  1.00 61.83           O  
ANISOU 7199  O   HOH B 240    11384   3385   8721   1138  -2779   -583       O  
HETATM 7200  O   HOH B 241      78.240  58.575  28.915  1.00 80.90           O  
ANISOU 7200  O   HOH B 241    15085   6247   9407    679  -2915    463       O  
HETATM 7201  O   HOH B 242      74.517  58.361  34.124  1.00 66.02           O  
ANISOU 7201  O   HOH B 242    10656   5051   9376   1081  -2778   -802       O  
HETATM 7202  O   HOH B 243      96.682  35.448  29.246  1.00 71.79           O  
ANISOU 7202  O   HOH B 243     9460   7395  10421   -759    980  -1175       O  
HETATM 7203  O   HOH B 244      79.403  61.621  29.674  1.00 68.81           O  
ANISOU 7203  O   HOH B 244    14348   4144   7651    513  -2819    819       O  
HETATM 7204  O   HOH B 245      99.832  43.897  20.780  1.00 83.56           O  
ANISOU 7204  O   HOH B 245    12816   8690  10244  -3263   5125  -1150       O  
HETATM 7205  O   HOH B 246      84.750  42.728  54.712  1.00 79.68           O  
ANISOU 7205  O   HOH B 246    17259   6107   6910   -149    909    993       O  
HETATM 7206  O   HOH B 247      82.429  67.781  47.488  1.00 75.49           O  
ANISOU 7206  O   HOH B 247    13034   5477  10172    230  -1769   -736       O  
HETATM 7207  O   HOH B 248      80.033  63.690  31.560  1.00 65.56           O  
ANISOU 7207  O   HOH B 248    13872   3491   7546    391  -2692    838       O  
HETATM 7208  O   HOH B 249     105.768  45.953  27.069  1.00 94.90           O  
ANISOU 7208  O   HOH B 249    10178  10265  15615  -3617   4736  -2983       O  
HETATM 7209  O   HOH B 250      93.215  40.642  43.234  1.00 64.42           O  
ANISOU 7209  O   HOH B 250    10477   5532   8465     -4  -1114    141       O  
HETATM 7210  O   HOH B 251      96.068  34.310  21.525  1.00 47.23           O  
ANISOU 7210  O   HOH B 251     7487   4517   5941  -1192   2472  -1609       O  
HETATM 7211  O   HOH B 252     100.601  52.489  41.837  1.00 81.35           O  
ANISOU 7211  O   HOH B 252     9849   7784  13277  -1460  -1013  -1636       O  
HETATM 7212  O   HOH B 253      83.419  58.232  19.127  1.00 97.05           O  
ANISOU 7212  O   HOH B 253    22626   6821   7428   -248  -1631   1945       O  
HETATM 7213  O   HOH B 254      91.278  61.572  21.131  1.00 89.51           O  
ANISOU 7213  O   HOH B 254    21244   5364   7402  -3310   2521   2479       O  
HETATM 7214  O   HOH B 255      80.523  47.859  55.060  1.00 70.30           O  
ANISOU 7214  O   HOH B 255    14644   5627   6439   -611   2253    228       O  
HETATM 7215  O   HOH B 256      95.007  42.786  40.045  1.00 67.39           O  
ANISOU 7215  O   HOH B 256     9695   6339   9571   -447   -750   -233       O  
HETATM 7216  O   HOH C 501      60.328 -14.150  -0.227  1.00 44.39           O  
ANISOU 7216  O   HOH C 501     7153   3091   6623    295   -245    214       O  
HETATM 7217  O   HOH C 502      70.904 -11.693   6.832  1.00 26.76           O  
ANISOU 7217  O   HOH C 502     4851   2292   3025   -395    737    329       O  
HETATM 7218  O   HOH C 503      76.740  24.219   3.159  1.00 54.65           O  
ANISOU 7218  O   HOH C 503    12755   2932   5078  -1022   1058   -291       O  
HETATM 7219  O   HOH C 504      61.949  -9.412  -5.297  1.00 22.45           O  
ANISOU 7219  O   HOH C 504     3678   1922   2930   -886   -349    421       O  
HETATM 7220  O   HOH C 505      62.882 -13.328  -2.898  1.00 29.71           O  
ANISOU 7220  O   HOH C 505     4718   2724   3844  -1168    -19    404       O  
HETATM 7221  O   HOH C 506      63.820 -10.812  -8.739  1.00 62.38           O  
ANISOU 7221  O   HOH C 506     9696   6591   7415  -1043   -574    246       O  
HETATM 7222  O   HOH C 507      68.044 -21.102   1.131  1.00 28.87           O  
ANISOU 7222  O   HOH C 507     6379   1390   3201   -754   -319   -477       O  
HETATM 7223  O   HOH C 508      71.994  18.424  -1.080  1.00 42.03           O  
ANISOU 7223  O   HOH C 508     9604   2413   3951     55   1030     84       O  
HETATM 7224  O   HOH C 509      71.487 -10.579  -9.905  1.00 48.32           O  
ANISOU 7224  O   HOH C 509     8723   4517   5119   -658    658   -181       O  
HETATM 7225  O   HOH C 510      75.711   5.655   3.112  1.00 26.77           O  
ANISOU 7225  O   HOH C 510     5166   2142   2862   -414   1000   -114       O  
HETATM 7226  O   HOH C 511      72.938 -19.321  -4.596  1.00 34.01           O  
ANISOU 7226  O   HOH C 511     6834   2253   3834   -443    616   -206       O  
HETATM 7227  O   HOH C 512      45.027 -13.181 -12.569  1.00 85.75           O  
ANISOU 7227  O   HOH C 512     8354  10168  14059  -2855  -5167   1240       O  
HETATM 7228  O   HOH C 513      54.693  17.302  -0.775  1.00 74.88           O  
ANISOU 7228  O   HOH C 513    10571   7164  10714   3593    338    599       O  
HETATM 7229  O   HOH C 514      73.626  25.231  -3.624  1.00 53.06           O  
ANISOU 7229  O   HOH C 514    13212   2329   4618   -383   1018    231       O  
HETATM 7230  O   HOH C 515      63.477  28.087  -1.247  1.00 81.19           O  
ANISOU 7230  O   HOH C 515    16610   5292   8946   2820    567    316       O  
HETATM 7231  O   HOH C 516      74.480  13.640 -10.027  1.00 38.61           O  
ANISOU 7231  O   HOH C 516     9341   2253   3077   -808   1271    321       O  
HETATM 7232  O   HOH C 517      67.364 -14.774   4.649  1.00 34.84           O  
ANISOU 7232  O   HOH C 517     5798   3241   4197   -806    738    446       O  
HETATM 7233  O   HOH C 518      70.848  30.076  -2.932  1.00 79.70           O  
ANISOU 7233  O   HOH C 518    18160   4469   7654    488    766    288       O  
HETATM 7234  O   HOH C 519      63.385  16.494  -0.012  1.00 52.23           O  
ANISOU 7234  O   HOH C 519     9539   4171   6135   1757    808    287       O  
HETATM 7235  O   HOH C 520      72.962 -14.938   1.856  1.00 27.88           O  
ANISOU 7235  O   HOH C 520     5094   2152   3348   -319    588    116       O  
HETATM 7236  O   HOH C 521      56.366  23.299   9.226  1.00 77.37           O  
ANISOU 7236  O   HOH C 521    13194   6254   9951   4482   3073   -320       O  
HETATM 7237  O   HOH C 522      64.465   8.759   3.244  1.00 49.32           O  
ANISOU 7237  O   HOH C 522     7850   4898   5990    959   1241    182       O  
HETATM 7238  O   HOH C 523      58.705  15.892   5.166  1.00 63.38           O  
ANISOU 7238  O   HOH C 523     9853   5902   8326   2733   1837    126       O  
HETATM 7239  O   HOH C 524      83.995 -23.010  -5.391  1.00 80.70           O  
ANISOU 7239  O   HOH C 524    12275   7465  10923   1377   1747   -871       O  
HETATM 7240  O   HOH C 525      77.328   5.488   5.287  1.00 35.14           O  
ANISOU 7240  O   HOH C 525     6201   3195   3955   -538    831   -183       O  
HETATM 7241  O   HOH C 526      65.985 -12.223 -11.189  1.00 50.89           O  
ANISOU 7241  O   HOH C 526     9140   4763   5434  -1108   -452     39       O  
HETATM 7242  O   HOH C 527      65.522 -13.177  -3.202  1.00 28.60           O  
ANISOU 7242  O   HOH C 527     4947   2466   3453   -960    153    268       O  
HETATM 7243  O   HOH C 528      70.542 -22.889  10.248  1.00 52.66           O  
ANISOU 7243  O   HOH C 528     9855   4298   5855   -812    332    790       O  
HETATM 7244  O   HOH C 529      87.771 -10.232   8.264  1.00 71.32           O  
ANISOU 7244  O   HOH C 529     8737   7816  10546    464   -762   -183       O  
HETATM 7245  O   HOH C 530      81.059 -22.806  -0.630  1.00 53.58           O  
ANISOU 7245  O   HOH C 530     8842   4250   7267    951    720   -377       O  
HETATM 7246  O   HOH C 531      74.429 -23.538   2.159  1.00 38.31           O  
ANISOU 7246  O   HOH C 531     7581   2367   4608   -128    267    123       O  
HETATM 7247  O   HOH C 532      63.937 -13.926 -11.453  1.00 64.67           O  
ANISOU 7247  O   HOH C 532    10845   6440   7287  -1402   -918    106       O  
HETATM 7248  O   HOH C 533      78.636  41.451 -12.412  1.00106.96           O  
ANISOU 7248  O   HOH C 533    28153   3910   8576  -2928   1388   1227       O  
HETATM 7249  O   HOH C 534      84.333 -19.932   2.389  1.00 60.57           O  
ANISOU 7249  O   HOH C 534     8650   5575   8788   1229    366   -306       O  
HETATM 7250  O   HOH C 535      62.634  21.036   1.004  1.00 70.38           O  
ANISOU 7250  O   HOH C 535    12810   5655   8275   2401    947    214       O  
HETATM 7251  O   HOH C 536      68.986  20.268   0.662  1.00 45.18           O  
ANISOU 7251  O   HOH C 536    10246   2519   4400    837   1019     68       O  
HETATM 7252  O   HOH C 537      65.671 -16.466   7.041  1.00 39.09           O  
ANISOU 7252  O   HOH C 537     6512   3674   4667  -1089    945    636       O  
HETATM 7253  O   HOH C 538      65.859  21.540   2.500  1.00 44.95           O  
ANISOU 7253  O   HOH C 538    10209   2298   4573   1717   1189     18       O  
HETATM 7254  O   HOH C 539      75.599 -22.134  11.099  1.00 63.19           O  
ANISOU 7254  O   HOH C 539    11131   5520   7359     -4   -300    648       O  
HETATM 7255  O   HOH C 540      61.455 -12.840 -13.677  1.00 53.90           O  
ANISOU 7255  O   HOH C 540     9611   5008   5858  -1600  -1757    229       O  
HETATM 7256  O   HOH C 541      63.884 -16.780   9.042  1.00 46.24           O  
ANISOU 7256  O   HOH C 541     7411   4604   5554  -1323   1286    784       O  
HETATM 7257  O   HOH C 542      74.099 -17.945 -14.238  1.00 66.54           O  
ANISOU 7257  O   HOH C 542    12792   5739   6751   -630   1161   -734       O  
HETATM 7258  O   HOH C 543      63.565 -16.668  14.685  1.00 56.24           O  
ANISOU 7258  O   HOH C 543     9584   5634   6151  -1415   1963    995       O  
HETATM 7259  O   HOH C 544      46.125 -10.538 -13.685  1.00 73.97           O  
ANISOU 7259  O   HOH C 544     7432   8574  12100  -2155  -5295   1226       O  
HETATM 7260  O   HOH C 545      62.141 -11.046 -11.812  1.00 54.57           O  
ANISOU 7260  O   HOH C 545     9180   5368   6186  -1283  -1288    274       O  
HETATM 7261  O   HOH C 546      77.154 -25.032  -1.874  1.00 44.38           O  
ANISOU 7261  O   HOH C 546     8632   2736   5495    361    597   -294       O  
HETATM 7262  O   HOH C 547      86.158  20.961  -3.157  1.00 63.58           O  
ANISOU 7262  O   HOH C 547    11997   4873   7287  -3386   2025   -194       O  
HETATM 7263  O   HOH C 548      83.833  27.173  15.941  1.00 88.95           O  
ANISOU 7263  O   HOH C 548    19098   6169   8530  -3158   -904  -1247       O  
HETATM 7264  O   HOH C 549      64.169 -14.317 -14.369  1.00 58.47           O  
ANISOU 7264  O   HOH C 549    10949   5294   5973  -1544  -1199     -6       O  
HETATM 7265  O   HOH C 550      65.730  19.380   0.815  1.00 63.77           O  
ANISOU 7265  O   HOH C 550    12017   5079   7134   1559    969    158       O  
HETATM 7266  O   HOH C 551      70.128 -14.313  -8.759  1.00 51.35           O  
ANISOU 7266  O   HOH C 551     9107   4765   5640   -792    381   -163       O  
HETATM 7267  O   HOH C 552      66.653  -7.136 -16.061  1.00 87.49           O  
ANISOU 7267  O   HOH C 552    15009   9055   9179  -1010   -636     63       O  
HETATM 7268  O   HOH C 553      68.397 -24.192   7.887  1.00 95.69           O  
ANISOU 7268  O   HOH C 553    15158   9727  11473  -1172    428    747       O  
HETATM 7269  O   HOH C 554      73.616 -17.356  -6.385  1.00 41.69           O  
ANISOU 7269  O   HOH C 554     7788   3343   4711   -404    798   -302       O  
HETATM 7270  O   HOH C 555      75.323  16.930  15.789  1.00 75.74           O  
ANISOU 7270  O   HOH C 555    15104   6499   7177   -451    797   -760       O  
HETATM 7271  O   HOH C 556      62.346   1.878 -13.558  1.00 59.49           O  
ANISOU 7271  O   HOH C 556    10357   5786   6459    -77  -1424    638       O  
HETATM 7272  O   HOH C 557      77.944 -20.836   6.500  1.00 48.57           O  
ANISOU 7272  O   HOH C 557     8344   3958   6151    377    -73    228       O  
HETATM 7273  O   HOH C 558      56.013   1.174 -13.028  1.00 77.95           O  
ANISOU 7273  O   HOH C 558    11099   8452  10067    227  -2785    946       O  
HETATM 7274  O   HOH C 559      79.656  12.392   8.760  1.00 58.38           O  
ANISOU 7274  O   HOH C 559    10353   5386   6444  -1091    484   -422       O  
HETATM 7275  O   HOH C 560      51.698  15.556  -0.293  1.00 80.66           O  
ANISOU 7275  O   HOH C 560     9878   8373  12395   3877    371    684       O  
HETATM 7276  O   HOH C 561      78.706   9.858  13.132  1.00 67.45           O  
ANISOU 7276  O   HOH C 561    11837   6581   7209   -850    171   -444       O  
HETATM 7277  O   HOH C 562      86.955  12.882  -0.453  1.00 47.34           O  
ANISOU 7277  O   HOH C 562     7579   4168   6242  -2483   1585   -387       O  
HETATM 7278  O   HOH C 563      60.980   0.204 -11.903  1.00 69.81           O  
ANISOU 7278  O   HOH C 563    10870   7394   8259   -103  -1430    628       O  
HETATM 7279  O   HOH C 564      49.138  -1.085  -8.250  1.00 74.72           O  
ANISOU 7279  O   HOH C 564     7178   9024  12189    387  -2538   1144       O  
HETATM 7280  O   HOH C 565      87.933   4.615  -0.500  1.00 59.10           O  
ANISOU 7280  O   HOH C 565     7483   6430   8541  -1540   1574   -477       O  
HETATM 7281  O   HOH C 566      87.121  -2.204   1.118  1.00 56.98           O  
ANISOU 7281  O   HOH C 566     6845   6347   8458   -592   1141   -458       O  
HETATM 7282  O   HOH C 567      72.677  29.298  12.758  1.00 89.74           O  
ANISOU 7282  O   HOH C 567    19957   5830   8309    315   1403  -1035       O  
HETATM 7283  O   HOH C 568      64.506  16.612 -17.927  1.00 76.68           O  
ANISOU 7283  O   HOH C 568    16479   5752   6902    660  -1647   1243       O  
HETATM 7284  O   HOH C 569      55.649  15.488   3.699  1.00 77.42           O  
ANISOU 7284  O   HOH C 569    10700   7861  10854   3224   1600    300       O  
HETATM 7285  O   HOH C 570      52.045  12.236  -2.009  1.00 85.15           O  
ANISOU 7285  O   HOH C 570    10040   9357  12957   3149   -155    802       O  
HETATM 7286  O   HOH C 571      65.894  23.330 -19.646  1.00 96.30           O  
ANISOU 7286  O   HOH C 571    21471   6738   8380    672  -1596   1585       O  
HETATM 7287  O   HOH C 572      50.386  15.937  -5.833  1.00 88.69           O  
ANISOU 7287  O   HOH C 572    11065   9090  13545   3993  -1656   1117       O  
HETATM 7288  O   HOH C 573      90.390  -7.720   4.043  1.00 47.93           O  
ANISOU 7288  O   HOH C 573     4718   5145   8348    202    265   -476       O  
HETATM 7289  O   HOH C 574      89.021  17.548   4.514  1.00 76.36           O  
ANISOU 7289  O   HOH C 574    11863   7252   9899  -3373    524   -560       O  
HETATM 7290  O   HOH C 575      72.144   5.169 -15.039  1.00 59.29           O  
ANISOU 7290  O   HOH C 575    11967   5248   5315   -739    822    273       O  
HETATM 7291  O   HOH C 576      53.811  24.207 -11.513  1.00 93.24           O  
ANISOU 7291  O   HOH C 576    16078   7319  12028   4540  -2986   1512       O  
HETATM 7292  O   HOH C 577      52.914  16.628  -8.577  1.00 81.87           O  
ANISOU 7292  O   HOH C 577    11779   7746  11583   3518  -2150   1194       O  
HETATM 7293  O   HOH C 578      74.441  34.012  -1.642  1.00 85.46           O  
ANISOU 7293  O   HOH C 578    20437   4164   7870   -660    961    106       O  
HETATM 7294  O   HOH C 579      89.085  -6.768   8.587  1.00 66.14           O  
ANISOU 7294  O   HOH C 579     7752   7332  10045     51   -832   -265       O  
HETATM 7295  O   HOH C 580      88.403  -5.206   5.930  1.00 69.06           O  
ANISOU 7295  O   HOH C 580     8054   7829  10358   -167    -50   -363       O  
HETATM 7296  O   HOH C 581      80.028   7.450  12.861  1.00 77.98           O  
ANISOU 7296  O   HOH C 581    12601   8177   8852   -879    -35   -373       O  
HETATM 7297  O   HOH C 582      54.663   3.959   3.756  1.00 65.73           O  
ANISOU 7297  O   HOH C 582     7189   7840   9944   1350   1482    564       O  
HETATM 7298  O   HOH C 583      52.288  28.314 -17.108  1.00108.41           O  
ANISOU 7298  O   HOH C 583    20600   7525  13066   5310  -5186   2221       O  
HETATM 7299  O   HOH D 201      67.513 -14.960  -2.750  1.00 43.23           O  
ANISOU 7299  O   HOH D 201     8001   2983   5443   -726   -703    140       O  
HETATM 7300  O   HOH D 202      72.175 -39.796  -6.547  1.00 63.68           O  
ANISOU 7300  O   HOH D 202    14387   3720   6089   -225   -534  -2359       O  
HETATM 7301  O   HOH D 203      60.266 -38.016  11.852  1.00 76.26           O  
ANISOU 7301  O   HOH D 203    14815   5630   8532  -2753   2160   1586       O  
HETATM 7302  O   HOH D 204      69.238 -26.280   5.076  1.00 44.70           O  
ANISOU 7302  O   HOH D 204     9268   3013   4702   -752   -346   -682       O  
HETATM 7303  O   HOH D 205      73.051 -22.026  -5.991  1.00 44.65           O  
ANISOU 7303  O   HOH D 205     8335   3741   4889   -950    300   -198       O  
HETATM 7304  O   HOH D 206      72.899 -33.573   9.733  1.00 61.46           O  
ANISOU 7304  O   HOH D 206    13247   3799   6306   -485  -1495   -529       O  
HETATM 7305  O   HOH D 207      76.436 -25.235   1.345  1.00 42.80           O  
ANISOU 7305  O   HOH D 207     7720   2781   5760   -565   -728   -672       O  
HETATM 7306  O   HOH D 208      56.326 -18.263  -8.157  1.00 64.08           O  
ANISOU 7306  O   HOH D 208     8796   6073   9479  -1010  -3089   1119       O  
HETATM 7307  O   HOH D 209      72.116 -36.431 -12.877  1.00 76.24           O  
ANISOU 7307  O   HOH D 209    17277   6032   5658    -47    235  -2542       O  
HETATM 7308  O   HOH D 210      64.150 -30.746  10.480  1.00 51.97           O  
ANISOU 7308  O   HOH D 210    11428   3500   4819  -1126   1261    125       O  
HETATM 7309  O   HOH D 211      67.531 -24.228  -9.776  1.00 48.80           O  
ANISOU 7309  O   HOH D 211    10130   4304   4106  -1272   -779   -324       O  
HETATM 7310  O   HOH D 212      62.806 -24.978   4.059  1.00 43.38           O  
ANISOU 7310  O   HOH D 212     8049   3302   5134   -927    568   -202       O  
HETATM 7311  O   HOH D 213      55.095 -40.097  -1.459  1.00116.58           O  
ANISOU 7311  O   HOH D 213    16800  10356  17140  -5154  -2744    793       O  
HETATM 7312  O   HOH D 214      51.765 -20.403  -4.546  1.00 74.60           O  
ANISOU 7312  O   HOH D 214     7450   7553  13344  -1071  -2215   1542       O  
HETATM 7313  O   HOH D 215      66.328 -28.181  -1.386  1.00 62.76           O  
ANISOU 7313  O   HOH D 215    10917   5743   7185  -1333   -498   -606       O  
HETATM 7314  O   HOH D 216      66.660 -47.501  -0.246  1.00 93.03           O  
ANISOU 7314  O   HOH D 216    19245   4938  11165  -2499  -2537  -1269       O  
HETATM 7315  O   HOH D 217      77.884 -35.222  -4.723  1.00 69.09           O  
ANISOU 7315  O   HOH D 217    12428   5489   8334    785    830  -1687       O  
HETATM 7316  O   HOH D 218      52.326 -22.300  -2.477  1.00 63.15           O  
ANISOU 7316  O   HOH D 218     6154   6196  11643  -1256  -1078   1362       O  
HETATM 7317  O   HOH D 219      55.164 -24.201   0.558  1.00 63.07           O  
ANISOU 7317  O   HOH D 219     7543   6173  10249  -1369    113    860       O  
HETATM 7318  O   HOH D 220      75.510 -28.636 -14.729  1.00 80.43           O  
ANISOU 7318  O   HOH D 220    16121   8065   6374    116   2526  -1054       O  
HETATM 7319  O   HOH D 221      65.375 -23.453   7.369  1.00 67.51           O  
ANISOU 7319  O   HOH D 221    12356   5914   7381   -439    544   -550       O  
HETATM 7320  O   HOH D 222      58.317 -25.553   7.994  1.00 69.65           O  
ANISOU 7320  O   HOH D 222    11155   6565   8746   -703   2543    409       O  
HETATM 7321  O   HOH D 223      77.578 -29.101 -10.167  1.00 69.49           O  
ANISOU 7321  O   HOH D 223    12524   6686   7194    200   2252   -976       O  
HETATM 7322  O   HOH D 224      66.365 -32.323  10.475  1.00 84.05           O  
ANISOU 7322  O   HOH D 224    15952   7252   8732  -1138    482    -18       O  
HETATM 7323  O   HOH D 225      76.586 -31.002 -11.842  1.00 88.07           O  
ANISOU 7323  O   HOH D 225    16090   8780   8592    408   2288  -1423       O  
HETATM 7324  O   HOH D 226      66.129 -38.755  16.485  1.00 97.27           O  
ANISOU 7324  O   HOH D 226    21111   7221   8628  -1499    636   1231       O  
HETATM 7325  O   HOH D 227      67.573 -27.328 -19.810  1.00 88.92           O  
ANISOU 7325  O   HOH D 227    20579   8581   4625  -1143  -1432   -886       O  
HETATM 7326  O   HOH D 228      69.198 -37.578  17.584  1.00 72.47           O  
ANISOU 7326  O   HOH D 228    18814   3798   4922   -876   -634    849       O  
HETATM 7327  O   HOH D 229      56.870 -42.844  12.262  1.00 86.78           O  
ANISOU 7327  O   HOH D 229    15784   5981  11208  -4515   2756   3010       O  
HETATM 7328  O   HOH D 230      57.518 -30.050   5.607  1.00 78.14           O  
ANISOU 7328  O   HOH D 230    11346   7568  10775  -2019   1539    828       O  
HETATM 7329  O   HOH D 231      56.330 -29.890   3.148  1.00 64.37           O  
ANISOU 7329  O   HOH D 231     8763   5934   9761  -2310    740    890       O  
HETATM 7330  O   HOH D 232      54.363 -24.879   5.154  1.00 57.84           O  
ANISOU 7330  O   HOH D 232     7059   5449   9470  -1008   2258   1062       O  
HETATM 7331  O   HOH D 233      55.832 -21.911 -15.878  1.00 87.29           O  
ANISOU 7331  O   HOH D 233    14507   8459  10200  -2248  -6543   1109       O  
HETATM 7332  O   HOH D 234      48.680 -23.286   1.023  1.00 87.06           O  
ANISOU 7332  O   HOH D 234     7191   9313  16576  -1149    578   2070       O  
HETATM 7333  O   HOH D 235      68.824 -40.916  19.413  1.00 85.44           O  
ANISOU 7333  O   HOH D 235    21923   4560   5979  -1189   -611   1628       O  
HETATM 7334  O   HOH D 236      72.672 -41.639 -17.612  1.00121.75           O  
ANISOU 7334  O   HOH D 236    27485  10085   8691    896    325  -4137       O  
CONECT   12 1960                                                                
CONECT  696 1276                                                                
CONECT 1276  696                                                                
CONECT 1960   12                                                                
CONECT 2597 3155                                                                
CONECT 2801 3229                                                                
CONECT 3155 2597                                                                
CONECT 3229 2801                                                                
CONECT 3462 5406                                                                
CONECT 4142 4735                                                                
CONECT 4735 4142                                                                
CONECT 5406 3462                                                                
CONECT 5887 6404                                                                
CONECT 6062 6478                                                                
CONECT 6404 5887                                                                
CONECT 6478 6062                                                                
CONECT 6648 6655 6657                                                           
CONECT 6649 6650                                                                
CONECT 6650 6649 6651                                                           
CONECT 6651 6650 6652                                                           
CONECT 6652 6651 6654                                                           
CONECT 6653 6655 6659                                                           
CONECT 6654 6652 6656 6659                                                      
CONECT 6655 6648 6653 6658                                                      
CONECT 6656 6654                                                                
CONECT 6657 6648                                                                
CONECT 6658 6655                                                                
CONECT 6659 6653 6654                                                           
CONECT 6660 6666 6668                                                           
CONECT 6661 6662                                                                
CONECT 6662 6661 6663                                                           
CONECT 6663 6662 6665                                                           
CONECT 6664 6666 6670                                                           
CONECT 6665 6663 6667 6670                                                      
CONECT 6666 6660 6664 6669                                                      
CONECT 6667 6665                                                                
CONECT 6668 6660                                                                
CONECT 6669 6666                                                                
CONECT 6670 6664 6665                                                           
CONECT 6671 6674                                                                
CONECT 6672 6673 6675                                                           
CONECT 6673 6672 6676                                                           
CONECT 6674 6671 6678                                                           
CONECT 6675 6672 6679                                                           
CONECT 6676 6673 6680                                                           
CONECT 6677 6691 6693                                                           
CONECT 6678 6674 6681                                                           
CONECT 6679 6675 6682                                                           
CONECT 6680 6676 6683                                                           
CONECT 6681 6678 6684                                                           
CONECT 6682 6679 6684                                                           
CONECT 6683 6680 6685                                                           
CONECT 6684 6681 6682                                                           
CONECT 6685 6683 6686                                                           
CONECT 6686 6685 6687                                                           
CONECT 6687 6686 6688                                                           
CONECT 6688 6687 6690                                                           
CONECT 6689 6691 6695                                                           
CONECT 6690 6688 6692 6695                                                      
CONECT 6691 6677 6689 6694                                                      
CONECT 6692 6690                                                                
CONECT 6693 6677                                                                
CONECT 6694 6691                                                                
CONECT 6695 6689 6690                                                           
CONECT 6696 6697 6698                                                           
CONECT 6697 6696 6699                                                           
CONECT 6698 6696 6701                                                           
CONECT 6699 6697 6702                                                           
CONECT 6700 6710 6712                                                           
CONECT 6701 6698                                                                
CONECT 6702 6699 6703                                                           
CONECT 6703 6702 6704                                                           
CONECT 6704 6703 6705                                                           
CONECT 6705 6704 6706                                                           
CONECT 6706 6705 6707                                                           
CONECT 6707 6706 6709                                                           
CONECT 6708 6710 6714                                                           
CONECT 6709 6707 6711 6714                                                      
CONECT 6710 6700 6708 6713                                                      
CONECT 6711 6709                                                                
CONECT 6712 6700                                                                
CONECT 6713 6710                                                                
CONECT 6714 6708 6709                                                           
CONECT 6715 6718                                                                
CONECT 6716 6717 6719                                                           
CONECT 6717 6716 6720                                                           
CONECT 6718 6715 6722                                                           
CONECT 6719 6716 6723                                                           
CONECT 6720 6717 6724                                                           
CONECT 6721 6735 6737                                                           
CONECT 6722 6718 6725                                                           
CONECT 6723 6719 6726                                                           
CONECT 6724 6720 6727                                                           
CONECT 6725 6722 6728                                                           
CONECT 6726 6723 6728                                                           
CONECT 6727 6724 6729                                                           
CONECT 6728 6725 6726                                                           
CONECT 6729 6727 6730                                                           
CONECT 6730 6729 6731                                                           
CONECT 6731 6730 6732                                                           
CONECT 6732 6731 6734                                                           
CONECT 6733 6735 6739                                                           
CONECT 6734 6732 6736 6739                                                      
CONECT 6735 6721 6733 6738                                                      
CONECT 6736 6734                                                                
CONECT 6737 6721                                                                
CONECT 6738 6735                                                                
CONECT 6739 6733 6734                                                           
CONECT 6740 6743                                                                
CONECT 6741 6742 6744                                                           
CONECT 6742 6741 6745                                                           
CONECT 6743 6740 6747                                                           
CONECT 6744 6741 6748                                                           
CONECT 6745 6742 6749                                                           
CONECT 6746 6760 6762                                                           
CONECT 6747 6743 6750                                                           
CONECT 6748 6744 6751                                                           
CONECT 6749 6745 6752                                                           
CONECT 6750 6747 6753                                                           
CONECT 6751 6748 6753                                                           
CONECT 6752 6749 6754                                                           
CONECT 6753 6750 6751                                                           
CONECT 6754 6752 6755                                                           
CONECT 6755 6754 6756                                                           
CONECT 6756 6755 6757                                                           
CONECT 6757 6756 6759                                                           
CONECT 6758 6760 6764                                                           
CONECT 6759 6757 6761 6764                                                      
CONECT 6760 6746 6758 6763                                                      
CONECT 6761 6759                                                                
CONECT 6762 6746                                                                
CONECT 6763 6760                                                                
CONECT 6764 6758 6759                                                           
CONECT 6765 6768                                                                
CONECT 6766 6767 6769                                                           
CONECT 6767 6766 6770                                                           
CONECT 6768 6765 6772                                                           
CONECT 6769 6766 6773                                                           
CONECT 6770 6767 6774                                                           
CONECT 6771 6785 6787                                                           
CONECT 6772 6768 6775                                                           
CONECT 6773 6769 6776                                                           
CONECT 6774 6770 6777                                                           
CONECT 6775 6772 6778                                                           
CONECT 6776 6773 6778                                                           
CONECT 6777 6774 6779                                                           
CONECT 6778 6775 6776                                                           
CONECT 6779 6777 6780                                                           
CONECT 6780 6779 6781                                                           
CONECT 6781 6780 6782                                                           
CONECT 6782 6781 6784                                                           
CONECT 6783 6785 6789                                                           
CONECT 6784 6782 6786 6789                                                      
CONECT 6785 6771 6783 6788                                                      
CONECT 6786 6784                                                                
CONECT 6787 6771                                                                
CONECT 6788 6785                                                                
CONECT 6789 6783 6784                                                           
CONECT 6790 6791 6792                                                           
CONECT 6791 6790 6793                                                           
CONECT 6792 6790 6795                                                           
CONECT 6793 6791 6796                                                           
CONECT 6794 6806 6808                                                           
CONECT 6795 6792 6797                                                           
CONECT 6796 6793 6798                                                           
CONECT 6797 6795 6799                                                           
CONECT 6798 6796 6800                                                           
CONECT 6799 6797                                                                
CONECT 6800 6798 6801                                                           
CONECT 6801 6800 6802                                                           
CONECT 6802 6801 6803                                                           
CONECT 6803 6802 6805                                                           
CONECT 6804 6806 6810                                                           
CONECT 6805 6803 6807 6810                                                      
CONECT 6806 6794 6804 6809                                                      
CONECT 6807 6805                                                                
CONECT 6808 6794                                                                
CONECT 6809 6806                                                                
CONECT 6810 6804 6805                                                           
CONECT 6811 6812 6813                                                           
CONECT 6812 6811                                                                
CONECT 6813 6811 6814 6815                                                      
CONECT 6814 6813                                                                
CONECT 6815 6813 6816                                                           
CONECT 6816 6815                                                                
CONECT 6817 6818 6825 6826 6827                                                 
CONECT 6818 6817 6819 6824 6828                                                 
CONECT 6819 6818 6820 6829 6830                                                 
CONECT 6820 6819 6821 6831 6832                                                 
CONECT 6821 6820 6822 6823 6833                                                 
CONECT 6822 6821 6834 6835 6836                                                 
CONECT 6823 6821 6837                                                           
CONECT 6824 6818 6838                                                           
CONECT 6825 6817                                                                
CONECT 6826 6817                                                                
CONECT 6827 6817                                                                
CONECT 6828 6818                                                                
CONECT 6829 6819                                                                
CONECT 6830 6819                                                                
CONECT 6831 6820                                                                
CONECT 6832 6820                                                                
CONECT 6833 6821                                                                
CONECT 6834 6822                                                                
CONECT 6835 6822                                                                
CONECT 6836 6822                                                                
CONECT 6837 6823                                                                
CONECT 6838 6824                                                                
CONECT 6839 6847 6849                                                           
CONECT 6840 6841                                                                
CONECT 6841 6840 6842                                                           
CONECT 6842 6841 6843                                                           
CONECT 6843 6842 6844                                                           
CONECT 6844 6843 6846                                                           
CONECT 6845 6847 6851                                                           
CONECT 6846 6844 6848 6851                                                      
CONECT 6847 6839 6845 6850                                                      
CONECT 6848 6846                                                                
CONECT 6849 6839                                                                
CONECT 6850 6847                                                                
CONECT 6851 6845 6846                                                           
CONECT 6852 6855                                                                
CONECT 6853 6854 6856                                                           
CONECT 6854 6853 6857                                                           
CONECT 6855 6852 6859                                                           
CONECT 6856 6853 6860                                                           
CONECT 6857 6854 6861                                                           
CONECT 6858 6872 6874                                                           
CONECT 6859 6855 6862                                                           
CONECT 6860 6856 6863                                                           
CONECT 6861 6857 6864                                                           
CONECT 6862 6859 6865                                                           
CONECT 6863 6860 6865                                                           
CONECT 6864 6861 6866                                                           
CONECT 6865 6862 6863                                                           
CONECT 6866 6864 6867                                                           
CONECT 6867 6866 6868                                                           
CONECT 6868 6867 6869                                                           
CONECT 6869 6868 6871                                                           
CONECT 6870 6872 6876                                                           
CONECT 6871 6869 6873 6876                                                      
CONECT 6872 6858 6870 6875                                                      
CONECT 6873 6871                                                                
CONECT 6874 6858                                                                
CONECT 6875 6872                                                                
CONECT 6876 6870 6871                                                           
CONECT 6877 6878 6886                                                           
CONECT 6878 6877 6879                                                           
CONECT 6879 6878 6880 6904                                                      
CONECT 6880 6879 6881                                                           
CONECT 6881 6880 6882 6886                                                      
CONECT 6882 6881 6883                                                           
CONECT 6883 6882 6884                                                           
CONECT 6884 6883 6885 6890                                                      
CONECT 6885 6884 6886 6887                                                      
CONECT 6886 6877 6881 6885 6895                                                 
CONECT 6887 6885 6888                                                           
CONECT 6888 6887 6889                                                           
CONECT 6889 6888 6890 6893 6894                                                 
CONECT 6890 6884 6889 6891                                                      
CONECT 6891 6890 6892                                                           
CONECT 6892 6891 6893                                                           
CONECT 6893 6889 6892 6896                                                      
CONECT 6894 6889                                                                
CONECT 6895 6886                                                                
CONECT 6896 6893 6897 6898                                                      
CONECT 6897 6896                                                                
CONECT 6898 6896 6899                                                           
CONECT 6899 6898 6900                                                           
CONECT 6900 6899 6901                                                           
CONECT 6901 6900 6902 6903                                                      
CONECT 6902 6901                                                                
CONECT 6903 6901                                                                
CONECT 6904 6879                                                                
CONECT 6905 6908                                                                
CONECT 6906 6907 6909                                                           
CONECT 6907 6906 6910                                                           
CONECT 6908 6905 6912                                                           
CONECT 6909 6906 6913                                                           
CONECT 6910 6907 6914                                                           
CONECT 6911 6925 6927                                                           
CONECT 6912 6908 6915                                                           
CONECT 6913 6909 6916                                                           
CONECT 6914 6910 6917                                                           
CONECT 6915 6912 6918                                                           
CONECT 6916 6913 6918                                                           
CONECT 6917 6914 6919                                                           
CONECT 6918 6915 6916                                                           
CONECT 6919 6917 6920                                                           
CONECT 6920 6919 6921                                                           
CONECT 6921 6920 6922                                                           
CONECT 6922 6921 6924                                                           
CONECT 6923 6925 6929                                                           
CONECT 6924 6922 6926 6929                                                      
CONECT 6925 6911 6923 6928                                                      
CONECT 6926 6924                                                                
CONECT 6927 6911                                                                
CONECT 6928 6925                                                                
CONECT 6929 6923 6924                                                           
CONECT 6930 6933                                                                
CONECT 6931 6932 6934                                                           
CONECT 6932 6931 6935                                                           
CONECT 6933 6930 6937                                                           
CONECT 6934 6931 6938                                                           
CONECT 6935 6932 6939                                                           
CONECT 6936 6950 6952                                                           
CONECT 6937 6933 6940                                                           
CONECT 6938 6934 6941                                                           
CONECT 6939 6935 6942                                                           
CONECT 6940 6937 6943                                                           
CONECT 6941 6938 6943                                                           
CONECT 6942 6939 6944                                                           
CONECT 6943 6940 6941                                                           
CONECT 6944 6942 6945                                                           
CONECT 6945 6944 6946                                                           
CONECT 6946 6945 6947                                                           
CONECT 6947 6946 6949                                                           
CONECT 6948 6950 6954                                                           
CONECT 6949 6947 6951 6954                                                      
CONECT 6950 6936 6948 6953                                                      
CONECT 6951 6949                                                                
CONECT 6952 6936                                                                
CONECT 6953 6950                                                                
CONECT 6954 6948 6949                                                           
CONECT 6955 6958                                                                
CONECT 6956 6957 6959                                                           
CONECT 6957 6956 6960                                                           
CONECT 6958 6955 6962                                                           
CONECT 6959 6956 6963                                                           
CONECT 6960 6957 6964                                                           
CONECT 6961 6975 6977                                                           
CONECT 6962 6958 6965                                                           
CONECT 6963 6959 6966                                                           
CONECT 6964 6960 6967                                                           
CONECT 6965 6962 6968                                                           
CONECT 6966 6963 6968                                                           
CONECT 6967 6964 6969                                                           
CONECT 6968 6965 6966                                                           
CONECT 6969 6967 6970                                                           
CONECT 6970 6969 6971                                                           
CONECT 6971 6970 6972                                                           
CONECT 6972 6971 6974                                                           
CONECT 6973 6975 6979                                                           
CONECT 6974 6972 6976 6979                                                      
CONECT 6975 6961 6973 6978                                                      
CONECT 6976 6974                                                                
CONECT 6977 6961                                                                
CONECT 6978 6975                                                                
CONECT 6979 6973 6974                                                           
CONECT 6980 6983                                                                
CONECT 6981 6982 6984                                                           
CONECT 6982 6981 6985                                                           
CONECT 6983 6980 6987                                                           
CONECT 6984 6981 6988                                                           
CONECT 6985 6982 6989                                                           
CONECT 6986 7000 7002                                                           
CONECT 6987 6983 6990                                                           
CONECT 6988 6984 6991                                                           
CONECT 6989 6985 6992                                                           
CONECT 6990 6987 6993                                                           
CONECT 6991 6988 6993                                                           
CONECT 6992 6989 6994                                                           
CONECT 6993 6990 6991                                                           
CONECT 6994 6992 6995                                                           
CONECT 6995 6994 6996                                                           
CONECT 6996 6995 6997                                                           
CONECT 6997 6996 6999                                                           
CONECT 6998 7000 7004                                                           
CONECT 6999 6997 7001 7004                                                      
CONECT 7000 6986 6998 7003                                                      
CONECT 7001 6999                                                                
CONECT 7002 6986                                                                
CONECT 7003 7000                                                                
CONECT 7004 6998 6999                                                           
CONECT 7005 7008                                                                
CONECT 7006 7007 7009                                                           
CONECT 7007 7006 7010                                                           
CONECT 7008 7005 7012                                                           
CONECT 7009 7006 7013                                                           
CONECT 7010 7007 7014                                                           
CONECT 7011 7025 7027                                                           
CONECT 7012 7008 7015                                                           
CONECT 7013 7009 7016                                                           
CONECT 7014 7010 7017                                                           
CONECT 7015 7012 7018                                                           
CONECT 7016 7013 7018                                                           
CONECT 7017 7014 7019                                                           
CONECT 7018 7015 7016                                                           
CONECT 7019 7017 7020                                                           
CONECT 7020 7019 7021                                                           
CONECT 7021 7020 7022                                                           
CONECT 7022 7021 7024                                                           
CONECT 7023 7025 7029                                                           
CONECT 7024 7022 7026 7029                                                      
CONECT 7025 7011 7023 7028                                                      
CONECT 7026 7024                                                                
CONECT 7027 7011                                                                
CONECT 7028 7025                                                                
CONECT 7029 7023 7024                                                           
CONECT 7030 7031 7032                                                           
CONECT 7031 7030                                                                
CONECT 7032 7030 7033 7034                                                      
CONECT 7033 7032                                                                
CONECT 7034 7032 7035                                                           
CONECT 7035 7034                                                                
MASTER      579    0   19   41   24    0   44    6 7316    4  404   76          
END