HEADER    MEMBRANE PROTEIN                        06-AUG-19   6KNM              
TITLE     APELIN RECEPTOR IN COMPLEX WITH SINGLE DOMAIN ANTIBODY                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APELIN RECEPTOR,RUBREDOXIN,APELIN RECEPTOR;                
COMPND   3 CHAIN: B;                                                            
COMPND   4 SYNONYM: ANGIOTENSIN RECEPTOR-LIKE 1,G-PROTEIN COUPLED RECEPTOR APJ, 
COMPND   5 G-PROTEIN COUPLED RECEPTOR HG11,RD,ANGIOTENSIN RECEPTOR-LIKE 1,G-    
COMPND   6 PROTEIN COUPLED RECEPTOR APJ,G-PROTEIN COUPLED RECEPTOR HG11;        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: SINGLE DOMAIN ANTIBODY JN241;                              
COMPND  11 CHAIN: A;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, CLOSTRIDIUM PASTEURIANUM;         
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 1501;                                          
SOURCE   5 GENE: APLNR, AGTRL1, APJ;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: CAMELUS BACTRIANUS;                             
SOURCE  10 ORGANISM_TAXID: 9837;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GPCR, SINGLE-DOMAIN ANTIBODY, ANTAGONIST, AGONIST, MEMBRANE PROTEIN   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.B.MA,Y.DING,X.SONG,X.MA,X.LI,N.ZHANG,Y.SONG,Y.SUN,Y.SHEN,W.ZHONG,   
AUTHOR   2 L.A.HU,Y.L.MA,M.Y.ZHANG                                              
REVDAT   2   12-FEB-20 6KNM    1       SPRSDE JRNL                              
REVDAT   1   29-JAN-20 6KNM    0                                                
JRNL        AUTH   Y.MA,Y.DING,X.SONG,X.MA,X.LI,N.ZHANG,Y.SONG,Y.SUN,Y.SHEN,    
JRNL        AUTH 2 W.ZHONG,L.A.HU,Y.MA,M.Y.ZHANG                                
JRNL        TITL   STRUCTURE-GUIDED DISCOVERY OF A SINGLE-DOMAIN ANTIBODY       
JRNL        TITL 2 AGONIST AGAINST HUMAN APELIN RECEPTOR.                       
JRNL        REF    SCI ADV                       V.   6 X7379 2020              
JRNL        REFN                   ESSN 2375-2548                               
JRNL        PMID   31998837                                                     
JRNL        DOI    10.1126/SCIADV.AAX7379                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.64                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.860                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 12361                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.260                           
REMARK   3   R VALUE            (WORKING SET) : 0.258                           
REMARK   3   FREE R VALUE                     : 0.305                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 619                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.6400 -  5.0787    0.97     3236   171  0.2370 0.2576        
REMARK   3     2  5.0787 -  4.0318    0.97     3084   162  0.2244 0.2814        
REMARK   3     3  4.0318 -  3.5224    0.97     3041   161  0.2911 0.3876        
REMARK   3     4  3.5224 -  3.2004    0.77     2381   125  0.3790 0.4392        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.670           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 95.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.6352  14.0224 -43.9990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7684 T22:   0.7122                                     
REMARK   3      T33:   0.6866 T12:   0.0264                                     
REMARK   3      T13:   0.0127 T23:   0.0127                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0748 L22:   0.0821                                     
REMARK   3      L33:   0.0197 L12:  -0.0491                                     
REMARK   3      L13:   0.0200 L23:   0.0099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1000 S12:  -0.1242 S13:  -0.0238                       
REMARK   3      S21:  -0.2154 S22:  -0.0286 S23:   0.0074                       
REMARK   3      S31:  -0.0835 S32:   0.0799 S33:  -0.0417                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6KNM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-AUG-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300013335.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12402                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.641                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.19000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.3800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.84                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.860                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4NC2, 5VBL                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.1, 26% PEG500 DME, 125   
REMARK 280  MM MGCL2, 100 MM NACL, LIPIDIC CUBIC PHASE, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       22.39000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      175.05000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.19500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      175.05000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.39000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.19500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET B   -17                                                      
REMARK 465     LYS B   -16                                                      
REMARK 465     THR B   -15                                                      
REMARK 465     ILE B   -14                                                      
REMARK 465     ILE B   -13                                                      
REMARK 465     ALA B   -12                                                      
REMARK 465     LEU B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     TYR B    -9                                                      
REMARK 465     ILE B    -8                                                      
REMARK 465     PHE B    -7                                                      
REMARK 465     CYS B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     VAL B    -4                                                      
REMARK 465     PHE B    -3                                                      
REMARK 465     ALA B    -2                                                      
REMARK 465     ASP B    -1                                                      
REMARK 465     TYR B     0                                                      
REMARK 465     LYS B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     PHE B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     ASN B     9                                                      
REMARK 465     TYR B    10                                                      
REMARK 465     TYR B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     ASP B    14                                                      
REMARK 465     ASN B    15                                                      
REMARK 465     GLN B    16                                                      
REMARK 465     SER B    17                                                      
REMARK 465     GLN B   328                                                      
REMARK 465     SER B   329                                                      
REMARK 465     ARG B   330                                                      
REMARK 465     LEU B   331                                                      
REMARK 465     GLU B   332                                                      
REMARK 465     VAL B   333                                                      
REMARK 465     LEU B   334                                                      
REMARK 465     PHE B   335                                                      
REMARK 465     GLN B   336                                                      
REMARK 465     GLY B   337                                                      
REMARK 465     PRO B   338                                                      
REMARK 465     HIS B   339                                                      
REMARK 465     HIS B   340                                                      
REMARK 465     HIS B   341                                                      
REMARK 465     HIS B   342                                                      
REMARK 465     HIS B   343                                                      
REMARK 465     HIS B   344                                                      
REMARK 465     HIS B   345                                                      
REMARK 465     HIS B   346                                                      
REMARK 465     HIS B   347                                                      
REMARK 465     HIS B   348                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS A    33     SG   CYS A   109              1.43            
REMARK 500   O    TRP B  1037     CE   LYS B  1046              1.66            
REMARK 500   O    TYR A    29     NH1  ARG A   100              1.92            
REMARK 500   N    TYR A    93     O    THR A   123              1.96            
REMARK 500   O    VAL B   203     OG1  THR B   207              2.01            
REMARK 500   OE2  GLU B   174     N    ARG A    53              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS B 181   CA  -  CB  -  SG  ANGL. DEV. =   7.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR B  35      -38.04    -37.38                                   
REMARK 500    VAL B  49       -9.75    -59.63                                   
REMARK 500    ALA B  64       45.13    -78.54                                   
REMARK 500    ARG B  91       31.62    -78.00                                   
REMARK 500    ASP B  92       65.78     39.39                                   
REMARK 500    TYR B  93       75.70     66.83                                   
REMARK 500    ARG B 133       72.22     52.75                                   
REMARK 500    ARG B 141       70.47     29.99                                   
REMARK 500    ASN B 175       77.10     60.09                                   
REMARK 500    TYR B 185       22.20    -76.70                                   
REMARK 500    ALA B 229      -70.50    -42.66                                   
REMARK 500    ASN B1025      159.60    -44.22                                   
REMARK 500    GLU B1050      109.76   -160.07                                   
REMARK 500    GLU B1054       83.73    -62.53                                   
REMARK 500    ARG B 243       93.14    -38.78                                   
REMARK 500    HIS B 278       63.50     69.95                                   
REMARK 500    PRO B 280      153.36    -41.93                                   
REMARK 500    ASN B 301       -8.66    -58.06                                   
REMARK 500    CYS B 303       28.89    -76.71                                   
REMARK 500    PHE B 312      -25.04   -144.58                                   
REMARK 500    LEU B 325      -58.80    -29.02                                   
REMARK 500    PHE A  37     -159.90   -116.74                                   
REMARK 500    LYS A  43     -163.06   -117.00                                   
REMARK 500    VAL A  48      -76.21   -116.39                                   
REMARK 500    SER A  54      -68.74    -94.00                                   
REMARK 500    ASP A  72       82.48   -152.06                                   
REMARK 500    ASN A  76       79.07     45.87                                   
REMARK 500    SER A  84       70.84     61.16                                   
REMARK 500    ARG A 100     -157.07    -93.89                                   
REMARK 500    TRP A 119     -166.46   -117.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ASN A 112         15.13                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1006   SG                                                     
REMARK 620 2 CYS B1009   SG  102.9                                              
REMARK 620 3 CYS B1039   SG  114.0  87.0                                        
REMARK 620 4 CYS B1042   SG  134.5 108.4 100.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1101                 
DBREF  6KNM B    7   229  UNP    P35414   APJ_HUMAN        7    229             
DBREF  6KNM B 1001  1054  UNP    P00268   RUBR_CLOPA       1     54             
DBREF  6KNM B  243   330  UNP    P35414   APJ_HUMAN      243    330             
DBREF  6KNM A    1   129  PDB    6KNM     6KNM             1    129             
SEQADV 6KNM MET B  -17  UNP  P35414              INITIATING METHIONINE          
SEQADV 6KNM LYS B  -16  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM THR B  -15  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM ILE B  -14  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM ILE B  -13  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM ALA B  -12  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM LEU B  -11  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM SER B  -10  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM TYR B   -9  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM ILE B   -8  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM PHE B   -7  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM CYS B   -6  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM LEU B   -5  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM VAL B   -4  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM PHE B   -3  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM ALA B   -2  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM ASP B   -1  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM TYR B    0  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM LYS B    1  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM ASP B    2  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM ASP B    3  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM ASP B    4  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM ASP B    5  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM LYS B    6  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM ALA B  117  UNP  P35414    VAL   117 ENGINEERED MUTATION            
SEQADV 6KNM ASN B  177  UNP  P35414    THR   177 ENGINEERED MUTATION            
SEQADV 6KNM LYS B  261  UNP  P35414    TRP   261 ENGINEERED MUTATION            
SEQADV 6KNM LEU B  325  UNP  P35414    CYS   325 ENGINEERED MUTATION            
SEQADV 6KNM MET B  326  UNP  P35414    CYS   326 ENGINEERED MUTATION            
SEQADV 6KNM LEU B  331  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM GLU B  332  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM VAL B  333  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM LEU B  334  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM PHE B  335  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM GLN B  336  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM GLY B  337  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM PRO B  338  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM HIS B  339  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM HIS B  340  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM HIS B  341  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM HIS B  342  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM HIS B  343  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM HIS B  344  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM HIS B  345  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM HIS B  346  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM HIS B  347  UNP  P35414              EXPRESSION TAG                 
SEQADV 6KNM HIS B  348  UNP  P35414              EXPRESSION TAG                 
SEQRES   1 B  407  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 B  407  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP LYS PHE ASP          
SEQRES   3 B  407  ASN TYR TYR GLY ALA ASP ASN GLN SER GLU CYS GLU TYR          
SEQRES   4 B  407  THR ASP TRP LYS SER SER GLY ALA LEU ILE PRO ALA ILE          
SEQRES   5 B  407  TYR MET LEU VAL PHE LEU LEU GLY THR THR GLY ASN GLY          
SEQRES   6 B  407  LEU VAL LEU TRP THR VAL PHE ARG SER SER ARG GLU LYS          
SEQRES   7 B  407  ARG ARG SER ALA ASP ILE PHE ILE ALA SER LEU ALA VAL          
SEQRES   8 B  407  ALA ASP LEU THR PHE VAL VAL THR LEU PRO LEU TRP ALA          
SEQRES   9 B  407  THR TYR THR TYR ARG ASP TYR ASP TRP PRO PHE GLY THR          
SEQRES  10 B  407  PHE PHE CYS LYS LEU SER SER TYR LEU ILE PHE VAL ASN          
SEQRES  11 B  407  MET TYR ALA SER ALA PHE CYS LEU THR GLY LEU SER PHE          
SEQRES  12 B  407  ASP ARG TYR LEU ALA ILE VAL ARG PRO VAL ALA ASN ALA          
SEQRES  13 B  407  ARG LEU ARG LEU ARG VAL SER GLY ALA VAL ALA THR ALA          
SEQRES  14 B  407  VAL LEU TRP VAL LEU ALA ALA LEU LEU ALA MET PRO VAL          
SEQRES  15 B  407  MET VAL LEU ARG THR THR GLY ASP LEU GLU ASN THR ASN          
SEQRES  16 B  407  LYS VAL GLN CYS TYR MET ASP TYR SER MET VAL ALA THR          
SEQRES  17 B  407  VAL SER SER GLU TRP ALA TRP GLU VAL GLY LEU GLY VAL          
SEQRES  18 B  407  SER SER THR THR VAL GLY PHE VAL VAL PRO PHE THR ILE          
SEQRES  19 B  407  MET LEU THR CYS TYR PHE PHE ILE ALA GLN THR ILE ALA          
SEQRES  20 B  407  MET LYS LYS TYR THR CYS THR VAL CYS GLY TYR ILE TYR          
SEQRES  21 B  407  ASN PRO GLU ASP GLY ASP PRO ASP ASN GLY VAL ASN PRO          
SEQRES  22 B  407  GLY THR ASP PHE LYS ASP ILE PRO ASP ASP TRP VAL CYS          
SEQRES  23 B  407  PRO LEU CYS GLY VAL GLY LYS ASP GLN PHE GLU GLU VAL          
SEQRES  24 B  407  GLU GLU ARG ARG ARG LEU LEU SER ILE ILE VAL VAL LEU          
SEQRES  25 B  407  VAL VAL THR PHE ALA LEU CYS LYS MET PRO TYR HIS LEU          
SEQRES  26 B  407  VAL LYS THR LEU TYR MET LEU GLY SER LEU LEU HIS TRP          
SEQRES  27 B  407  PRO CYS ASP PHE ASP LEU PHE LEU MET ASN ILE PHE PRO          
SEQRES  28 B  407  TYR CYS THR CYS ILE SER TYR VAL ASN SER CYS LEU ASN          
SEQRES  29 B  407  PRO PHE LEU TYR ALA PHE PHE ASP PRO ARG PHE ARG GLN          
SEQRES  30 B  407  ALA CYS THR SER MET LEU LEU MET GLY GLN SER ARG LEU          
SEQRES  31 B  407  GLU VAL LEU PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS          
SEQRES  32 B  407  HIS HIS HIS HIS                                              
SEQRES   1 A  129  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN          
SEQRES   2 A  129  SER GLY GLY SER LEU THR LEU SER CYS ALA ALA SER GLY          
SEQRES   3 A  129  SER THR TYR SER SER HIS CYS MET GLY TRP PHE ARG GLN          
SEQRES   4 A  129  ALA PRO GLY LYS GLU ARG GLU GLY VAL ALA LEU MET THR          
SEQRES   5 A  129  ARG SER ARG GLY THR SER TYR ALA ASP SER VAL LYS GLY          
SEQRES   6 A  129  ARG PHE THR ILE SER GLN ASP ASN THR LYS ASN ILE LEU          
SEQRES   7 A  129  TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 A  129  MET TYR TYR CYS ALA ALA VAL PRO ARG ALA GLY ILE GLU          
SEQRES   9 A  129  SER GLY ALA TYR CYS LYS TRP ASN MET LYS ASP SER GLY          
SEQRES  10 A  129  SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER              
HET     ZN  B1101       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   3   ZN    ZN 2+                                                        
HELIX    1 AA1 ALA B   29  SER B   56  1                                  28    
HELIX    2 AA2 ARG B   62  ALA B   64  5                                   3    
HELIX    3 AA3 ASP B   65  VAL B   80  1                                  16    
HELIX    4 AA4 THR B   81  ARG B   91  1                                  11    
HELIX    5 AA5 PHE B   97  ARG B  133  1                                  37    
HELIX    6 AA6 ARG B  141  LEU B  160  1                                  20    
HELIX    7 AA7 ALA B  161  LEU B  167  1                                   7    
HELIX    8 AA8 SER B  193  PHE B  210  1                                  18    
HELIX    9 AA9 PHE B  210  ALA B  229  1                                  20    
HELIX   10 AB1 ASP B 1019  GLY B 1023  5                                   5    
HELIX   11 AB2 ASP B 1029  ILE B 1033  5                                   5    
HELIX   12 AB3 GLY B 1045  ASP B 1047  5                                   3    
HELIX   13 AB4 ARG B  245  SER B  275  1                                  31    
HELIX   14 AB5 PRO B  280  ASN B  301  1                                  22    
HELIX   15 AB6 LEU B  304  ASP B  313  1                                  10    
HELIX   16 AB7 ASP B  313  GLY B  327  1                                  15    
HELIX   17 AB8 LYS A   86  THR A   90  5                                   5    
SHEET    1 AA1 2 ARG B 168  GLY B 171  0                                        
SHEET    2 AA1 2 GLN B 180  MET B 183 -1  O  TYR B 182   N  THR B 169           
SHEET    1 AA2 3 ILE B1012  TYR B1013  0                                        
SHEET    2 AA2 3 TYR B1004  CYS B1006 -1  N  TYR B1004   O  TYR B1013           
SHEET    3 AA2 3 PHE B1049  GLU B1051 -1  O  GLU B1050   N  THR B1005           
SHEET    1 AA3 4 GLN A   3  SER A   7  0                                        
SHEET    2 AA3 4 SER A  21  SER A  25 -1  O  ALA A  23   N  VAL A   5           
SHEET    3 AA3 4 ILE A  77  ASN A  83 -1  O  LEU A  78   N  CYS A  22           
SHEET    4 AA3 4 SER A  17  THR A  19 -1  N  LEU A  18   O  MET A  82           
SHEET    1 AA4 4 GLN A   3  SER A   7  0                                        
SHEET    2 AA4 4 SER A  21  SER A  25 -1  O  ALA A  23   N  VAL A   5           
SHEET    3 AA4 4 ILE A  77  ASN A  83 -1  O  LEU A  78   N  CYS A  22           
SHEET    4 AA4 4 PHE A  67  GLN A  71 -1  N  THR A  68   O  GLN A  81           
SHEET    1 AA5 3 SER A  11  GLN A  13  0                                        
SHEET    2 AA5 3 THR A 123  SER A 128  1  O  THR A 126   N  VAL A  12           
SHEET    3 AA5 3 ALA A  91  TYR A  93 -1  N  TYR A  93   O  THR A 123           
SHEET    1 AA6 4 THR A  57  TYR A  59  0                                        
SHEET    2 AA6 4 ALA A  49  MET A  51 -1  N  LEU A  50   O  SER A  58           
SHEET    3 AA6 4 HIS A  32  TRP A  36 -1  N  MET A  34   O  MET A  51           
SHEET    4 AA6 4 CYS A  95  PRO A  99 -1  O  VAL A  98   N  CYS A  33           
SSBOND   1 CYS B   19    CYS B  281                          1555   1555  2.05  
SSBOND   2 CYS B  102    CYS B  181                          1555   1555  2.03  
SSBOND   3 CYS A   22    CYS A   95                          1555   1555  2.04  
LINK         SG  CYS B1006                ZN    ZN B1101     1555   1555  2.09  
LINK         SG  CYS B1009                ZN    ZN B1101     1555   1555  2.30  
LINK         SG  CYS B1039                ZN    ZN B1101     1555   1555  2.53  
LINK         SG  CYS B1042                ZN    ZN B1101     1555   1555  2.47  
CISPEP   1 ALA A   40    PRO A   41          0       -25.98                     
SITE     1 AC1  4 CYS B1006  CYS B1009  CYS B1039  CYS B1042                    
CRYST1   44.780   48.390  350.100  90.00  90.00  90.00 P 21 21 21    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      0.022331  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020665  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002856        0.00000                         
ATOM      1  N   GLU B  18      12.540  18.200 -70.428  1.00168.19           N  
ANISOU    1  N   GLU B  18    23453  20100  20351   -263    614    426       N  
ATOM      2  CA  GLU B  18      13.061  16.897 -70.821  1.00176.17           C  
ANISOU    2  CA  GLU B  18    24456  21114  21365   -251    685    460       C  
ATOM      3  C   GLU B  18      12.433  15.783 -69.984  1.00192.15           C  
ANISOU    3  C   GLU B  18    26407  23177  23424   -219    695    459       C  
ATOM      4  O   GLU B  18      13.016  14.703 -69.847  1.00189.26           O  
ANISOU    4  O   GLU B  18    26000  22839  23070   -209    759    493       O  
ATOM      5  CB  GLU B  18      14.585  16.865 -70.685  1.00100.02           C  
ANISOU    5  CB  GLU B  18    14782  11507  11714   -274    753    508       C  
ATOM      6  CG  GLU B  18      15.315  17.773 -71.662  1.00100.32           C  
ANISOU    6  CG  GLU B  18    14897  11503  11718   -305    757    516       C  
ATOM      7  CD  GLU B  18      16.817  17.768 -71.448  1.00100.45           C  
ANISOU    7  CD  GLU B  18    14878  11560  11730   -327    823    562       C  
ATOM      8  OE1 GLU B  18      17.271  17.213 -70.427  1.00100.30           O  
ANISOU    8  OE1 GLU B  18    14770  11604  11734   -320    859    585       O  
ATOM      9  OE2 GLU B  18      17.542  18.323 -72.300  1.00100.72           O  
ANISOU    9  OE2 GLU B  18    14971  11560  11736   -352    840    576       O  
ATOM     10  N   CYS B  19      11.221  16.046 -69.474  1.00141.65           N  
ANISOU   10  N   CYS B  19    19996  16779  17044   -202    630    418       N  
ATOM     11  CA  CYS B  19      10.722  15.440 -68.235  1.00134.97           C  
ANISOU   11  CA  CYS B  19    19058  15990  16233   -177    627    415       C  
ATOM     12  C   CYS B  19       9.209  15.220 -68.253  1.00123.57           C  
ANISOU   12  C   CYS B  19    17630  14517  14804   -151    569    372       C  
ATOM     13  O   CYS B  19       8.449  16.149 -68.540  1.00128.81           O  
ANISOU   13  O   CYS B  19    18342  15142  15456   -155    503    334       O  
ATOM     14  CB  CYS B  19      11.089  16.336 -67.039  1.00147.62           C  
ANISOU   14  CB  CYS B  19    20594  17651  17844   -190    608    414       C  
ATOM     15  SG  CYS B  19      10.078  17.870 -66.832  1.00155.55           S  
ANISOU   15  SG  CYS B  19    21630  18632  18841   -198    508    360       S  
ATOM     16  N   GLU B  20       8.764  14.019 -67.885  1.00115.70           N  
ANISOU   16  N   GLU B  20    16587  13541  13834   -122    593    378       N  
ATOM     17  CA  GLU B  20       7.355  13.676 -68.023  1.00122.01           C  
ANISOU   17  CA  GLU B  20    17405  14307  14648    -96    544    340       C  
ATOM     18  C   GLU B  20       6.890  12.873 -66.807  1.00116.18           C  
ANISOU   18  C   GLU B  20    16570  13626  13947    -69    551    342       C  
ATOM     19  O   GLU B  20       7.695  12.344 -66.034  1.00 97.87           O  
ANISOU   19  O   GLU B  20    14177  11366  11642    -68    604    377       O  
ATOM     20  CB  GLU B  20       7.117  12.922 -69.348  1.00130.98           C  
ANISOU   20  CB  GLU B  20    18617  15378  15771    -87    562    341       C  
ATOM     21  CG  GLU B  20       7.359  13.767 -70.647  1.00103.97           C  
ANISOU   21  CG  GLU B  20    15301  11890  12311   -111    544    332       C  
ATOM     22  CD  GLU B  20       8.773  13.629 -71.267  1.00114.00           C  
ANISOU   22  CD  GLU B  20    16596  13161  13559   -133    612    376       C  
ATOM     23  OE1 GLU B  20       9.499  14.652 -71.348  1.00136.07           O  
ANISOU   23  OE1 GLU B  20    19410  15959  16333   -162    608    383       O  
ATOM     24  OE2 GLU B  20       9.148  12.507 -71.694  1.00 98.69           O  
ANISOU   24  OE2 GLU B  20    14656  11218  11623   -123    669    402       O  
ATOM     25  N   TYR B  21       5.566  12.772 -66.658  1.00118.14           N  
ANISOU   25  N   TYR B  21    16821  13855  14212    -47    497    304       N  
ATOM     26  CA  TYR B  21       4.934  12.444 -65.382  1.00105.09           C  
ANISOU   26  CA  TYR B  21    15080  12255  12593    -24    481    294       C  
ATOM     27  C   TYR B  21       4.016  11.234 -65.494  1.00110.79           C  
ANISOU   27  C   TYR B  21    15792  12963  13341      8    486    286       C  
ATOM     28  O   TYR B  21       3.042  11.267 -66.250  1.00111.23           O  
ANISOU   28  O   TYR B  21    15910  12959  13393     18    443    253       O  
ATOM     29  CB  TYR B  21       4.127  13.632 -64.877  1.00 96.69           C  
ANISOU   29  CB  TYR B  21    14017  11192  11529    -27    403    252       C  
ATOM     30  CG  TYR B  21       3.522  14.566 -65.949  1.00112.05           C  
ANISOU   30  CG  TYR B  21    16063  13063  13448    -39    344    215       C  
ATOM     31  CD1 TYR B  21       4.280  15.588 -66.519  1.00111.05           C  
ANISOU   31  CD1 TYR B  21    15990  12915  13290    -71    339    220       C  
ATOM     32  CD2 TYR B  21       2.180  14.464 -66.345  1.00103.26           C  
ANISOU   32  CD2 TYR B  21    14988  11902  12343    -20    290    175       C  
ATOM     33  CE1 TYR B  21       3.738  16.479 -67.417  1.00107.83           C  
ANISOU   33  CE1 TYR B  21    15670  12443  12858    -81    284    187       C  
ATOM     34  CE2 TYR B  21       1.628  15.357 -67.269  1.00105.07           C  
ANISOU   34  CE2 TYR B  21    15307  12067  12548    -31    233    140       C  
ATOM     35  CZ  TYR B  21       2.421  16.361 -67.792  1.00109.11           C  
ANISOU   35  CZ  TYR B  21    15869  12560  13027    -61    231    147       C  
ATOM     36  OH  TYR B  21       1.929  17.270 -68.700  1.00114.03           O  
ANISOU   36  OH  TYR B  21    16581  13120  13626    -73    177    115       O  
ATOM     37  N   THR B  22       4.283  10.215 -64.669  1.00118.42           N  
ANISOU   37  N   THR B  22    16677  13984  14334     25    534    314       N  
ATOM     38  CA  THR B  22       3.633   8.905 -64.732  1.00121.43           C  
ANISOU   38  CA  THR B  22    17038  14357  14741     55    554    316       C  
ATOM     39  C   THR B  22       3.917   8.068 -63.487  1.00115.89           C  
ANISOU   39  C   THR B  22    16231  13731  14072     71    597    344       C  
ATOM     40  O   THR B  22       4.994   8.161 -62.896  1.00111.18           O  
ANISOU   40  O   THR B  22    15585  13185  13471     58    639    377       O  
ATOM     41  CB  THR B  22       4.061   8.145 -65.990  1.00124.51           C  
ANISOU   41  CB  THR B  22    17493  14699  15117     53    599    336       C  
ATOM     42  OG1 THR B  22       5.447   8.393 -66.284  1.00131.56           O  
ANISOU   42  OG1 THR B  22    18397  15604  15986     27    649    372       O  
ATOM     43  CG2 THR B  22       3.210   8.524 -67.131  1.00106.09           C  
ANISOU   43  CG2 THR B  22    15255  12287  12767     53    548    299       C  
ATOM     44  N   ASP B  23       2.954   7.207 -63.138  1.00116.91           N  
ANISOU   44  N   ASP B  23    16326  13862  14231    101    587    332       N  
ATOM     45  CA  ASP B  23       2.882   6.571 -61.820  1.00125.13           C  
ANISOU   45  CA  ASP B  23    17264  14973  15305    121    608    347       C  
ATOM     46  C   ASP B  23       4.024   5.569 -61.608  1.00132.03           C  
ANISOU   46  C   ASP B  23    18091  15889  16187    121    693    399       C  
ATOM     47  O   ASP B  23       4.671   5.106 -62.556  1.00132.56           O  
ANISOU   47  O   ASP B  23    18205  15925  16239    112    735    421       O  
ATOM     48  CB  ASP B  23       1.532   5.853 -61.652  1.00131.86           C  
ANISOU   48  CB  ASP B  23    18102  15810  16188    153    578    321       C  
ATOM     49  CG  ASP B  23       1.241   5.437 -60.199  1.00130.44           C  
ANISOU   49  CG  ASP B  23    17818  15702  16043    173    583    328       C  
ATOM     50  OD1 ASP B  23       1.947   5.917 -59.289  1.00128.28           O  
ANISOU   50  OD1 ASP B  23    17487  15486  15766    163    596    345       O  
ATOM     51  OD2 ASP B  23       0.317   4.617 -59.963  1.00138.44           O  
ANISOU   51  OD2 ASP B  23    18804  16712  17085    201    575    317       O  
ATOM     52  N   TRP B  24       4.268   5.243 -60.331  1.00128.43           N  
ANISOU   52  N   TRP B  24    17539  15505  15753    131    716    418       N  
ATOM     53  CA  TRP B  24       5.156   4.142 -59.949  1.00132.75           C  
ANISOU   53  CA  TRP B  24    18028  16098  16315    138    792    465       C  
ATOM     54  C   TRP B  24       4.466   2.794 -60.155  1.00133.04           C  
ANISOU   54  C   TRP B  24    18054  16117  16379    167    812    468       C  
ATOM     55  O   TRP B  24       3.238   2.693 -60.247  1.00140.85           O  
ANISOU   55  O   TRP B  24    19058  17076  17383    186    765    434       O  
ATOM     56  CB  TRP B  24       5.579   4.227 -58.473  1.00116.11           C  
ANISOU   56  CB  TRP B  24    15819  14073  14224    142    808    483       C  
ATOM     57  CG  TRP B  24       6.516   5.353 -58.060  1.00128.80           C  
ANISOU   57  CG  TRP B  24    17415  15714  15809    114    805    492       C  
ATOM     58  CD1 TRP B  24       6.701   6.564 -58.681  1.00131.53           C  
ANISOU   58  CD1 TRP B  24    17828  16024  16124     88    769    473       C  
ATOM     59  CD2 TRP B  24       7.389   5.354 -56.922  1.00140.72           C  
ANISOU   59  CD2 TRP B  24    18841  17300  17327    111    841    522       C  
ATOM     60  NE1 TRP B  24       7.629   7.315 -57.989  1.00139.52           N  
ANISOU   60  NE1 TRP B  24    18801  17085  17126     69    779    489       N  
ATOM     61  CE2 TRP B  24       8.067   6.592 -56.909  1.00138.60           C  
ANISOU   61  CE2 TRP B  24    18592  17038  17033     82    823    519       C  
ATOM     62  CE3 TRP B  24       7.664   4.424 -55.911  1.00143.25           C  
ANISOU   62  CE3 TRP B  24    19070  17683  17674    130    886    552       C  
ATOM     63  CZ2 TRP B  24       9.001   6.922 -55.923  1.00130.75           C  
ANISOU   63  CZ2 TRP B  24    17530  16110  16039     72    848    543       C  
ATOM     64  CZ3 TRP B  24       8.590   4.755 -54.932  1.00135.45           C  
ANISOU   64  CZ3 TRP B  24    18016  16762  16686    120    911    576       C  
ATOM     65  CH2 TRP B  24       9.247   5.992 -54.947  1.00128.01           C  
ANISOU   65  CH2 TRP B  24    17095  15824  15718     92    892    571       C  
ATOM     66  N   LYS B  25       5.285   1.744 -60.190  1.00128.47           N  
ANISOU   66  N   LYS B  25    17445  15559  15808    172    884    510       N  
ATOM     67  CA  LYS B  25       4.777   0.392 -60.385  1.00137.30           C  
ANISOU   67  CA  LYS B  25    18551  16665  16954    198    911    518       C  
ATOM     68  C   LYS B  25       3.716   0.078 -59.335  1.00138.57           C  
ANISOU   68  C   LYS B  25    18643  16857  17148    226    880    499       C  
ATOM     69  O   LYS B  25       3.979   0.164 -58.132  1.00135.64           O  
ANISOU   69  O   LYS B  25    18192  16554  16792    229    890    513       O  
ATOM     70  CB  LYS B  25       5.928  -0.615 -60.295  1.00141.24           C  
ANISOU   70  CB  LYS B  25    19008  17198  17457    198    994    569       C  
ATOM     71  CG  LYS B  25       7.308  -0.064 -60.670  1.00141.27           C  
ANISOU   71  CG  LYS B  25    19037  17210  17429    167   1031    596       C  
ATOM     72  CD  LYS B  25       8.083   0.337 -59.410  1.00139.79           C  
ANISOU   72  CD  LYS B  25    18768  17101  17246    159   1050    618       C  
ATOM     73  CE  LYS B  25       9.458   0.912 -59.724  1.00135.27           C  
ANISOU   73  CE  LYS B  25    18215  16537  16643    128   1086    645       C  
ATOM     74  NZ  LYS B  25      10.258   1.096 -58.466  1.00121.74           N  
ANISOU   74  NZ  LYS B  25    16414  14904  14939    123   1112    671       N  
ATOM     75  N   SER B  26       2.514  -0.277 -59.796  1.00142.66           N  
ANISOU   75  N   SER B  26    19195  17329  17682    245    842    468       N  
ATOM     76  CA  SER B  26       1.365  -0.372 -58.902  1.00123.39           C  
ANISOU   76  CA  SER B  26    16702  14910  15272    269    801    443       C  
ATOM     77  C   SER B  26       1.628  -1.342 -57.757  1.00117.26           C  
ANISOU   77  C   SER B  26    15824  14202  14527    288    849    476       C  
ATOM     78  O   SER B  26       2.409  -2.290 -57.874  1.00108.62           O  
ANISOU   78  O   SER B  26    14709  13123  13438    291    914    515       O  
ATOM     79  CB  SER B  26       0.113  -0.813 -59.660  1.00118.82           C  
ANISOU   79  CB  SER B  26    16173  14266  14706    288    763    410       C  
ATOM     80  OG  SER B  26      -0.977  -0.978 -58.764  1.00115.60           O  
ANISOU   80  OG  SER B  26    15711  13882  14331    312    727    388       O  
ATOM     81  N   SER B  27       0.966  -1.073 -56.632  1.00136.36           N  
ANISOU   81  N   SER B  27    18181  16663  16966    302    815    460       N  
ATOM     82  CA  SER B  27       1.041  -1.874 -55.417  1.00126.77           C  
ANISOU   82  CA  SER B  27    16866  15516  15783    323    851    486       C  
ATOM     83  C   SER B  27       0.023  -3.010 -55.403  1.00 98.52           C  
ANISOU   83  C   SER B  27    13270  11923  12242    354    851    479       C  
ATOM     84  O   SER B  27      -0.109  -3.707 -54.389  1.00 87.41           O  
ANISOU   84  O   SER B  27    11780  10568  10864    374    874    497       O  
ATOM     85  CB  SER B  27       0.869  -0.962 -54.187  1.00112.63           C  
ANISOU   85  CB  SER B  27    15018  13782  13995    322    814    473       C  
ATOM     86  OG  SER B  27      -0.242  -0.074 -54.317  1.00 95.51           O  
ANISOU   86  OG  SER B  27    12888  11579  11823    323    737    424       O  
ATOM     87  N   GLY B  28      -0.681  -3.217 -56.513  1.00102.18           N  
ANISOU   87  N   GLY B  28    13806  12313  12703    358    827    455       N  
ATOM     88  CA  GLY B  28      -1.690  -4.247 -56.605  1.00109.35           C  
ANISOU   88  CA  GLY B  28    14703  13198  13645    387    823    445       C  
ATOM     89  C   GLY B  28      -2.883  -3.959 -55.724  1.00101.92           C  
ANISOU   89  C   GLY B  28    13720  12276  12729    406    768    413       C  
ATOM     90  O   GLY B  28      -3.587  -2.961 -55.913  1.00 95.36           O  
ANISOU   90  O   GLY B  28    12930  11416  11886    399    703    373       O  
ATOM     91  N   ALA B  29      -3.119  -4.837 -54.751  1.00104.41           N  
ANISOU   91  N   ALA B  29    13951  12639  13079    430    794    432       N  
ATOM     92  CA  ALA B  29      -4.186  -4.655 -53.776  1.00100.51           C  
ANISOU   92  CA  ALA B  29    13405  12173  12611    450    749    407       C  
ATOM     93  C   ALA B  29      -3.634  -4.394 -52.385  1.00 90.16           C  
ANISOU   93  C   ALA B  29    12006  10946  11305    450    768    429       C  
ATOM     94  O   ALA B  29      -4.363  -4.540 -51.400  1.00 85.39           O  
ANISOU   94  O   ALA B  29    11339  10378  10728    471    749    420       O  
ATOM     95  CB  ALA B  29      -5.108  -5.875 -53.758  1.00109.75           C  
ANISOU   95  CB  ALA B  29    14551  13327  13822    480    757    405       C  
ATOM     96  N   LEU B  30      -2.356  -4.012 -52.304  1.00 91.41           N  
ANISOU   96  N   LEU B  30    12159  11135  11437    428    804    457       N  
ATOM     97  CA  LEU B  30      -1.696  -3.847 -51.015  1.00 87.73           C  
ANISOU   97  CA  LEU B  30    11608  10751  10974    428    829    483       C  
ATOM     98  C   LEU B  30      -2.433  -2.851 -50.136  1.00 88.50           C  
ANISOU   98  C   LEU B  30    11678  10875  11074    432    767    449       C  
ATOM     99  O   LEU B  30      -2.758  -3.151 -48.978  1.00 85.16           O  
ANISOU   99  O   LEU B  30    11174  10506  10675    452    770    456       O  
ATOM    100  CB  LEU B  30      -0.248  -3.408 -51.213  1.00 89.87           C  
ANISOU  100  CB  LEU B  30    11892  11040  11213    400    868    512       C  
ATOM    101  CG  LEU B  30       0.570  -3.712 -49.956  1.00 94.74           C  
ANISOU  101  CG  LEU B  30    12414  11743  11841    405    915    550       C  
ATOM    102  CD1 LEU B  30       0.591  -5.215 -49.698  1.00102.53           C  
ANISOU  102  CD1 LEU B  30    13349  12749  12860    429    972    583       C  
ATOM    103  CD2 LEU B  30       1.988  -3.160 -50.065  1.00 80.85           C  
ANISOU  103  CD2 LEU B  30    10663  10005  10050    377    949    576       C  
ATOM    104  N   ILE B  31      -2.696  -1.660 -50.662  1.00 89.47           N  
ANISOU  104  N   ILE B  31    11865  10960  11171    414    711    414       N  
ATOM    105  CA  ILE B  31      -3.432  -0.677 -49.877  1.00 87.34           C  
ANISOU  105  CA  ILE B  31    11572  10711  10902    417    649    380       C  
ATOM    106  C   ILE B  31      -4.810  -1.250 -49.571  1.00 84.46           C  
ANISOU  106  C   ILE B  31    11183  10335  10572    448    618    356       C  
ATOM    107  O   ILE B  31      -5.069  -1.550 -48.390  1.00 82.00           O  
ANISOU  107  O   ILE B  31    10790  10083  10285    467    624    365       O  
ATOM    108  CB  ILE B  31      -3.463   0.713 -50.546  1.00 82.86           C  
ANISOU  108  CB  ILE B  31    11081  10102  10300    392    593    346       C  
ATOM    109  CG1 ILE B  31      -2.160   1.464 -50.264  1.00 82.54           C  
ANISOU  109  CG1 ILE B  31    11031  10101  10231    365    617    369       C  
ATOM    110  CG2 ILE B  31      -4.636   1.542 -50.055  1.00 81.52           C  
ANISOU  110  CG2 ILE B  31    10907   9929  10137    401    518    300       C  
ATOM    111  CD1 ILE B  31      -1.024   1.091 -51.162  1.00 87.17           C  
ANISOU  111  CD1 ILE B  31    11658  10665  10797    346    672    401       C  
ATOM    112  N   PRO B  32      -5.693  -1.488 -50.553  1.00 81.77           N  
ANISOU  112  N   PRO B  32    10907   9925  10238    454    589    329       N  
ATOM    113  CA  PRO B  32      -7.064  -1.882 -50.191  1.00 83.02           C  
ANISOU  113  CA  PRO B  32    11041  10073  10430    482    552    302       C  
ATOM    114  C   PRO B  32      -7.114  -3.045 -49.212  1.00 81.24           C  
ANISOU  114  C   PRO B  32    10724   9903  10241    508    598    333       C  
ATOM    115  O   PRO B  32      -7.986  -3.073 -48.329  1.00 79.90           O  
ANISOU  115  O   PRO B  32    10501   9761  10096    529    570    317       O  
ATOM    116  CB  PRO B  32      -7.683  -2.230 -51.542  1.00 82.60           C  
ANISOU  116  CB  PRO B  32    11071   9936  10377    483    534    280       C  
ATOM    117  CG  PRO B  32      -6.943  -1.371 -52.488  1.00 83.53           C  
ANISOU  117  CG  PRO B  32    11267  10017  10453    452    527    276       C  
ATOM    118  CD  PRO B  32      -5.530  -1.443 -52.011  1.00 79.94           C  
ANISOU  118  CD  PRO B  32    10770   9619   9984    437    587    321       C  
ATOM    119  N   ALA B  33      -6.165  -3.978 -49.313  1.00 85.27           N  
ANISOU  119  N   ALA B  33    11213  10432  10755    507    668    377       N  
ATOM    120  CA  ALA B  33      -5.983  -4.980 -48.271  1.00 85.21           C  
ANISOU  120  CA  ALA B  33    11112  10487  10777    529    718    412       C  
ATOM    121  C   ALA B  33      -5.864  -4.324 -46.901  1.00 81.01           C  
ANISOU  121  C   ALA B  33    10507  10029  10245    532    704    414       C  
ATOM    122  O   ALA B  33      -6.669  -4.584 -45.998  1.00 79.96           O  
ANISOU  122  O   ALA B  33    10314   9927  10140    556    688    406       O  
ATOM    123  CB  ALA B  33      -4.747  -5.824 -48.582  1.00 82.70           C  
ANISOU  123  CB  ALA B  33    10786  10182  10453    521    794    461       C  
ATOM    124  N   ILE B  34      -4.867  -3.451 -46.737  1.00 81.34           N  
ANISOU  124  N   ILE B  34    10553  10098  10255    508    710    424       N  
ATOM    125  CA  ILE B  34      -4.637  -2.811 -45.442  1.00 80.48           C  
ANISOU  125  CA  ILE B  34    10374  10061  10144    510    700    427       C  
ATOM    126  C   ILE B  34      -5.891  -2.085 -44.971  1.00 78.96           C  
ANISOU  126  C   ILE B  34    10176   9864   9960    522    628    382       C  
ATOM    127  O   ILE B  34      -6.381  -2.318 -43.860  1.00 77.69           O  
ANISOU  127  O   ILE B  34     9942   9754   9823    545    624    383       O  
ATOM    128  CB  ILE B  34      -3.426  -1.868 -45.530  1.00 78.26           C  
ANISOU  128  CB  ILE B  34    10113   9797   9825    479    710    439       C  
ATOM    129  CG1 ILE B  34      -2.145  -2.695 -45.621  1.00 76.89           C  
ANISOU  129  CG1 ILE B  34     9917   9649   9648    472    789    490       C  
ATOM    130  CG2 ILE B  34      -3.415  -0.910 -44.358  1.00 74.56           C  
ANISOU  130  CG2 ILE B  34     9592   9388   9350    479    678    427       C  
ATOM    131  CD1 ILE B  34      -0.949  -1.892 -46.001  1.00 76.57           C  
ANISOU  131  CD1 ILE B  34     9912   9611   9572    441    802    502       C  
ATOM    132  N   TYR B  35      -6.432  -1.202 -45.822  1.00 76.97           N  
ANISOU  132  N   TYR B  35    10003   9551   9689    508    571    341       N  
ATOM    133  CA  TYR B  35      -7.727  -0.553 -45.619  1.00 78.07           C  
ANISOU  133  CA  TYR B  35    10152   9671   9837    519    498    294       C  
ATOM    134  C   TYR B  35      -8.794  -1.454 -44.990  1.00 81.34           C  
ANISOU  134  C   TYR B  35    10511  10100  10294    553    496    290       C  
ATOM    135  O   TYR B  35      -9.615  -0.978 -44.200  1.00 81.24           O  
ANISOU  135  O   TYR B  35    10464  10111  10293    567    451    264       O  
ATOM    136  CB  TYR B  35      -8.280  -0.025 -46.949  1.00 79.50           C  
ANISOU  136  CB  TYR B  35    10436   9767  10002    505    451    256       C  
ATOM    137  CG  TYR B  35      -7.708   1.287 -47.441  1.00 81.40           C  
ANISOU  137  CG  TYR B  35    10736   9989  10203    474    421    240       C  
ATOM    138  CD1 TYR B  35      -6.776   1.996 -46.697  1.00 81.40           C  
ANISOU  138  CD1 TYR B  35    10700  10046  10184    459    432    257       C  
ATOM    139  CD2 TYR B  35      -8.151   1.842 -48.645  1.00 81.75           C  
ANISOU  139  CD2 TYR B  35    10876   9958  10230    460    377    207       C  
ATOM    140  CE1 TYR B  35      -6.273   3.220 -47.156  1.00 88.23           C  
ANISOU  140  CE1 TYR B  35    11620  10892  11013    430    403    241       C  
ATOM    141  CE2 TYR B  35      -7.666   3.056 -49.111  1.00 85.10           C  
ANISOU  141  CE2 TYR B  35    11356  10362  10618    432    348    192       C  
ATOM    142  CZ  TYR B  35      -6.724   3.746 -48.369  1.00 91.85           C  
ANISOU  142  CZ  TYR B  35    12172  11273  11454    416    361    209       C  
ATOM    143  OH  TYR B  35      -6.235   4.959 -48.829  1.00 92.79           O  
ANISOU  143  OH  TYR B  35    12347  11373  11538    388    332    194       O  
ATOM    144  N   MET B  36      -8.831  -2.739 -45.365  1.00 83.66           N  
ANISOU  144  N   MET B  36    10798  10377  10611    567    541    314       N  
ATOM    145  CA  MET B  36      -9.851  -3.643 -44.832  1.00 80.91           C  
ANISOU  145  CA  MET B  36    10400  10038  10304    599    540    311       C  
ATOM    146  C   MET B  36      -9.418  -4.221 -43.496  1.00 83.89           C  
ANISOU  146  C   MET B  36    10675  10499  10700    616    586    347       C  
ATOM    147  O   MET B  36     -10.218  -4.321 -42.554  1.00 84.93           O  
ANISOU  147  O   MET B  36    10749  10665  10857    639    566    337       O  
ATOM    148  CB  MET B  36     -10.135  -4.768 -45.829  1.00 83.08           C  
ANISOU  148  CB  MET B  36    10713  10257  10598    607    566    318       C  
ATOM    149  CG  MET B  36     -10.832  -4.340 -47.113  1.00 87.11           C  
ANISOU  149  CG  MET B  36    11321  10681  11098    598    516    278       C  
ATOM    150  SD  MET B  36     -12.363  -3.397 -46.853  1.00 98.88           S  
ANISOU  150  SD  MET B  36    12825  12149  12597    608    424    218       S  
ATOM    151  CE  MET B  36     -13.183  -4.369 -45.577  1.00100.92           C  
ANISOU  151  CE  MET B  36    12980  12460  12904    646    439    229       C  
ATOM    152  N   LEU B  37      -8.161  -4.651 -43.437  1.00 85.29           N  
ANISOU  152  N   LEU B  37    10832  10709  10867    605    649    391       N  
ATOM    153  CA  LEU B  37      -7.487  -4.976 -42.194  1.00 80.71           C  
ANISOU  153  CA  LEU B  37    10161  10211  10295    615    693    427       C  
ATOM    154  C   LEU B  37      -7.797  -3.921 -41.137  1.00 81.97           C  
ANISOU  154  C   LEU B  37    10281  10419  10447    617    647    405       C  
ATOM    155  O   LEU B  37      -8.198  -4.239 -40.012  1.00 82.89           O  
ANISOU  155  O   LEU B  37    10320  10588  10586    641    650    412       O  
ATOM    156  CB  LEU B  37      -5.991  -5.054 -42.506  1.00 77.34           C  
ANISOU  156  CB  LEU B  37     9744   9800   9842    592    749    466       C  
ATOM    157  CG  LEU B  37      -4.969  -5.691 -41.592  1.00 77.53           C  
ANISOU  157  CG  LEU B  37     9689   9897   9873    598    815    515       C  
ATOM    158  CD1 LEU B  37      -4.548  -4.692 -40.516  1.00 79.42           C  
ANISOU  158  CD1 LEU B  37     9881  10200  10095    592    797    513       C  
ATOM    159  CD2 LEU B  37      -5.577  -6.948 -41.014  1.00 78.21           C  
ANISOU  159  CD2 LEU B  37     9711  10004  10000    630    843    532       C  
ATOM    160  N   VAL B  38      -7.662  -2.648 -41.512  1.00 80.22           N  
ANISOU  160  N   VAL B  38    10112  10175  10193    594    601    377       N  
ATOM    161  CA  VAL B  38      -7.853  -1.551 -40.571  1.00 80.76           C  
ANISOU  161  CA  VAL B  38    10148  10287  10250    593    556    355       C  
ATOM    162  C   VAL B  38      -9.326  -1.351 -40.251  1.00 83.35           C  
ANISOU  162  C   VAL B  38    10468  10600  10600    614    497    314       C  
ATOM    163  O   VAL B  38      -9.697  -1.190 -39.086  1.00 84.68           O  
ANISOU  163  O   VAL B  38    10568  10824  10781    632    483    311       O  
ATOM    164  CB  VAL B  38      -7.213  -0.274 -41.126  1.00 76.95           C  
ANISOU  164  CB  VAL B  38     9728   9784   9728    561    528    338       C  
ATOM    165  CG1 VAL B  38      -7.759   0.963 -40.431  1.00 74.84           C  
ANISOU  165  CG1 VAL B  38     9447   9537   9450    560    463    301       C  
ATOM    166  CG2 VAL B  38      -5.712  -0.375 -40.964  1.00 73.52           C  
ANISOU  166  CG2 VAL B  38     9271   9390   9274    543    587    381       C  
ATOM    167  N   PHE B  39     -10.187  -1.337 -41.268  1.00 79.44           N  
ANISOU  167  N   PHE B  39    10042  10031  10109    613    460    282       N  
ATOM    168  CA  PHE B  39     -11.621  -1.365 -40.999  1.00 80.11           C  
ANISOU  168  CA  PHE B  39    10117  10100  10221    637    410    247       C  
ATOM    169  C   PHE B  39     -11.983  -2.521 -40.084  1.00 81.52           C  
ANISOU  169  C   PHE B  39    10211  10324  10438    668    447    273       C  
ATOM    170  O   PHE B  39     -12.878  -2.400 -39.243  1.00 81.40           O  
ANISOU  170  O   PHE B  39    10150  10336  10443    689    415    254       O  
ATOM    171  CB  PHE B  39     -12.410  -1.492 -42.299  1.00 75.17           C  
ANISOU  171  CB  PHE B  39     9575   9387   9599    633    378    217       C  
ATOM    172  CG  PHE B  39     -13.771  -2.124 -42.124  1.00 78.11           C  
ANISOU  172  CG  PHE B  39     9928   9741  10011    662    354    197       C  
ATOM    173  CD1 PHE B  39     -14.880  -1.340 -41.851  1.00 76.86           C  
ANISOU  173  CD1 PHE B  39     9776   9572   9857    670    285    151       C  
ATOM    174  CD2 PHE B  39     -13.936  -3.506 -42.232  1.00 83.54           C  
ANISOU  174  CD2 PHE B  39    10589  10422  10730    682    400    223       C  
ATOM    175  CE1 PHE B  39     -16.123  -1.909 -41.697  1.00 78.03           C  
ANISOU  175  CE1 PHE B  39     9905   9702  10041    696    262    133       C  
ATOM    176  CE2 PHE B  39     -15.175  -4.082 -42.064  1.00 88.34           C  
ANISOU  176  CE2 PHE B  39    11176  11013  11374    708    378    204       C  
ATOM    177  CZ  PHE B  39     -16.274  -3.280 -41.799  1.00 81.05           C  
ANISOU  177  CZ  PHE B  39    10260  10078  10455    715    309    159       C  
ATOM    178  N   LEU B  40     -11.326  -3.666 -40.267  1.00 87.22           N  
ANISOU  178  N   LEU B  40    10913  11053  11171    672    514    315       N  
ATOM    179  CA  LEU B  40     -11.652  -4.845 -39.475  1.00 88.06           C  
ANISOU  179  CA  LEU B  40    10943  11199  11316    702    553    341       C  
ATOM    180  C   LEU B  40     -11.237  -4.647 -38.023  1.00 83.10           C  
ANISOU  180  C   LEU B  40    10226  10660  10689    712    569    361       C  
ATOM    181  O   LEU B  40     -12.068  -4.711 -37.107  1.00 82.33           O  
ANISOU  181  O   LEU B  40    10073  10595  10615    735    548    350       O  
ATOM    182  CB  LEU B  40     -10.967  -6.079 -40.079  1.00 89.46           C  
ANISOU  182  CB  LEU B  40    11125  11361  11504    701    621    381       C  
ATOM    183  CG  LEU B  40     -11.340  -7.490 -39.597  1.00 88.51           C  
ANISOU  183  CG  LEU B  40    10942  11262  11426    731    665    409       C  
ATOM    184  CD1 LEU B  40     -10.806  -8.477 -40.589  1.00 98.53           C  
ANISOU  184  CD1 LEU B  40    12248  12491  12700    725    715    436       C  
ATOM    185  CD2 LEU B  40     -10.809  -7.847 -38.219  1.00 84.41           C  
ANISOU  185  CD2 LEU B  40    10324  10830  10916    745    706    446       C  
ATOM    186  N   LEU B  41      -9.938  -4.433 -37.795  1.00 84.40           N  
ANISOU  186  N   LEU B  41    10375  10864  10828    695    608    392       N  
ATOM    187  CA  LEU B  41      -9.455  -4.175 -36.443  1.00 85.66           C  
ANISOU  187  CA  LEU B  41    10453  11108  10985    703    623    411       C  
ATOM    188  C   LEU B  41     -10.043  -2.882 -35.883  1.00 92.51           C  
ANISOU  188  C   LEU B  41    11320  11990  11839    701    555    370       C  
ATOM    189  O   LEU B  41     -10.314  -2.806 -34.684  1.00 94.53           O  
ANISOU  189  O   LEU B  41    11504  12307  12107    720    549    372       O  
ATOM    190  CB  LEU B  41      -7.924  -4.121 -36.441  1.00 86.47           C  
ANISOU  190  CB  LEU B  41    10550  11243  11062    682    675    449       C  
ATOM    191  CG  LEU B  41      -7.243  -5.215 -37.261  1.00 88.10           C  
ANISOU  191  CG  LEU B  41    10777  11421  11274    676    737    485       C  
ATOM    192  CD1 LEU B  41      -5.736  -5.107 -37.179  1.00 89.02           C  
ANISOU  192  CD1 LEU B  41    10883  11574  11365    656    786    521       C  
ATOM    193  CD2 LEU B  41      -7.702  -6.549 -36.711  1.00 87.18           C  
ANISOU  193  CD2 LEU B  41    10597  11328  11198    707    775    510       C  
ATOM    194  N   GLY B  42     -10.277  -1.875 -36.735  1.00 88.61           N  
ANISOU  194  N   GLY B  42    10905  11442  11322    680    502    333       N  
ATOM    195  CA  GLY B  42     -10.715  -0.576 -36.241  1.00 83.81           C  
ANISOU  195  CA  GLY B  42    10299  10848  10698    675    438    295       C  
ATOM    196  C   GLY B  42     -12.144  -0.576 -35.727  1.00 88.25           C  
ANISOU  196  C   GLY B  42    10836  11409  11287    702    391    262       C  
ATOM    197  O   GLY B  42     -12.415  -0.094 -34.621  1.00 91.71           O  
ANISOU  197  O   GLY B  42    11217  11901  11727    715    369    253       O  
ATOM    198  N   THR B  43     -13.084  -1.089 -36.534  1.00 88.30           N  
ANISOU  198  N   THR B  43    10885  11352  11314    710    374    243       N  
ATOM    199  CA  THR B  43     -14.483  -1.161 -36.107  1.00 88.64           C  
ANISOU  199  CA  THR B  43    10905  11388  11385    735    330    212       C  
ATOM    200  C   THR B  43     -14.632  -2.002 -34.840  1.00 90.57           C  
ANISOU  200  C   THR B  43    11051  11703  11660    765    366    241       C  
ATOM    201  O   THR B  43     -15.463  -1.710 -33.968  1.00 93.41           O  
ANISOU  201  O   THR B  43    11365  12093  12033    785    332    220       O  
ATOM    202  CB  THR B  43     -15.353  -1.727 -37.242  1.00 88.42           C  
ANISOU  202  CB  THR B  43    10939  11281  11377    739    314    192       C  
ATOM    203  OG1 THR B  43     -14.838  -2.999 -37.679  1.00 93.90           O  
ANISOU  203  OG1 THR B  43    11628  11965  12086    743    379    232       O  
ATOM    204  CG2 THR B  43     -15.402  -0.768 -38.427  1.00 86.87           C  
ANISOU  204  CG2 THR B  43    10840  11014  11150    712    266    157       C  
ATOM    205  N   THR B  44     -13.825  -3.042 -34.716  1.00 92.42           N  
ANISOU  205  N   THR B  44    11248  11964  11903    770    436    288       N  
ATOM    206  CA  THR B  44     -13.878  -3.907 -33.556  1.00 94.18           C  
ANISOU  206  CA  THR B  44    11378  12252  12153    798    477    319       C  
ATOM    207  C   THR B  44     -13.007  -3.413 -32.409  1.00 93.82           C  
ANISOU  207  C   THR B  44    11269  12288  12089    796    494    340       C  
ATOM    208  O   THR B  44     -13.210  -3.840 -31.273  1.00 93.96           O  
ANISOU  208  O   THR B  44    11207  12367  12127    821    512    357       O  
ATOM    209  CB  THR B  44     -13.469  -5.320 -33.980  1.00 94.96           C  
ANISOU  209  CB  THR B  44    11467  12339  12274    804    544    360       C  
ATOM    210  OG1 THR B  44     -12.127  -5.294 -34.489  1.00 92.45           O  
ANISOU  210  OG1 THR B  44    11176  12022  11928    779    586    389       O  
ATOM    211  CG2 THR B  44     -14.401  -5.822 -35.088  1.00 95.98           C  
ANISOU  211  CG2 THR B  44    11657  12388  12424    807    523    337       C  
ATOM    212  N   GLY B  45     -12.055  -2.524 -32.670  1.00 87.74           N  
ANISOU  212  N   GLY B  45    10533  11522  11282    769    490    340       N  
ATOM    213  CA  GLY B  45     -11.147  -2.080 -31.630  1.00 89.71           C  
ANISOU  213  CA  GLY B  45    10724  11847  11514    766    509    361       C  
ATOM    214  C   GLY B  45     -11.641  -0.827 -30.938  1.00 91.05           C  
ANISOU  214  C   GLY B  45    10883  12042  11670    767    446    324       C  
ATOM    215  O   GLY B  45     -11.593  -0.714 -29.713  1.00 89.48           O  
ANISOU  215  O   GLY B  45    10611  11912  11475    784    450    333       O  
ATOM    216  N   ASN B  46     -12.098   0.146 -31.711  1.00 88.14           N  
ANISOU  216  N   ASN B  46    10588  11618  11284    750    387    281       N  
ATOM    217  CA  ASN B  46     -12.751   1.282 -31.084  1.00 91.63           C  
ANISOU  217  CA  ASN B  46    11020  12078  11717    754    322    241       C  
ATOM    218  C   ASN B  46     -14.120   0.907 -30.569  1.00 95.05           C  
ANISOU  218  C   ASN B  46    11418  12513  12183    784    294    221       C  
ATOM    219  O   ASN B  46     -14.594   1.507 -29.596  1.00 93.24           O  
ANISOU  219  O   ASN B  46    11146  12328  11955    798    260    202       O  
ATOM    220  CB  ASN B  46     -12.846   2.452 -32.056  1.00 88.23           C  
ANISOU  220  CB  ASN B  46    10678  11587  11258    725    266    201       C  
ATOM    221  CG  ASN B  46     -11.551   3.222 -32.132  1.00 98.18           C  
ANISOU  221  CG  ASN B  46    11955  12866  12482    697    279    214       C  
ATOM    222  OD1 ASN B  46     -11.277   4.079 -31.272  1.00 89.15           O  
ANISOU  222  OD1 ASN B  46    10777  11773  11324    695    258    207       O  
ATOM    223  ND2 ASN B  46     -10.734   2.923 -33.144  1.00 93.14           N  
ANISOU  223  ND2 ASN B  46    11369  12189  11831    675    314    235       N  
ATOM    224  N   GLY B  47     -14.746  -0.090 -31.196  1.00 91.01           N  
ANISOU  224  N   GLY B  47    10925  11956  11699    796    310    224       N  
ATOM    225  CA  GLY B  47     -15.989  -0.620 -30.671  1.00 89.72           C  
ANISOU  225  CA  GLY B  47    10720  11797  11571    827    292    211       C  
ATOM    226  C   GLY B  47     -15.903  -0.891 -29.185  1.00 92.17           C  
ANISOU  226  C   GLY B  47    10932  12195  11894    852    316    234       C  
ATOM    227  O   GLY B  47     -16.875  -0.691 -28.451  1.00 93.18           O  
ANISOU  227  O   GLY B  47    11023  12343  12038    874    281    212       O  
ATOM    228  N   LEU B  48     -14.721  -1.317 -28.710  1.00 95.07           N  
ANISOU  228  N   LEU B  48    11255  12614  12252    849    376    280       N  
ATOM    229  CA  LEU B  48     -14.536  -1.701 -27.305  1.00 96.58           C  
ANISOU  229  CA  LEU B  48    11351  12890  12455    873    408    307       C  
ATOM    230  C   LEU B  48     -14.361  -0.491 -26.401  1.00 91.83           C  
ANISOU  230  C   LEU B  48    10722  12341  11829    871    370    288       C  
ATOM    231  O   LEU B  48     -15.105  -0.307 -25.431  1.00 92.04           O  
ANISOU  231  O   LEU B  48    10696  12407  11868    895    344    274       O  
ATOM    232  CB  LEU B  48     -13.312  -2.601 -27.146  1.00100.62           C  
ANISOU  232  CB  LEU B  48    11826  13438  12966    871    486    363       C  
ATOM    233  CG  LEU B  48     -13.437  -4.117 -27.261  1.00 94.91           C  
ANISOU  233  CG  LEU B  48    11074  12709  12278    889    542    398       C  
ATOM    234  CD1 LEU B  48     -14.229  -4.506 -28.502  1.00 97.05           C  
ANISOU  234  CD1 LEU B  48    11415  12894  12565    885    523    376       C  
ATOM    235  CD2 LEU B  48     -12.055  -4.732 -27.238  1.00 90.68           C  
ANISOU  235  CD2 LEU B  48    10517  12205  11732    879    613    448       C  
ATOM    236  N   VAL B  49     -13.344   0.326 -26.690  1.00 91.22           N  
ANISOU  236  N   VAL B  49    10677  12265  11716    843    368    289       N  
ATOM    237  CA  VAL B  49     -13.009   1.488 -25.881  1.00 90.60           C  
ANISOU  237  CA  VAL B  49    10575  12236  11612    838    335    274       C  
ATOM    238  C   VAL B  49     -14.205   2.423 -25.851  1.00 91.23           C  
ANISOU  238  C   VAL B  49    10680  12291  11692    843    258    220       C  
ATOM    239  O   VAL B  49     -14.234   3.386 -25.078  1.00101.61           O  
ANISOU  239  O   VAL B  49    11970  13646  12991    845    221    200       O  
ATOM    240  CB  VAL B  49     -11.755   2.205 -26.408  1.00 91.48           C  
ANISOU  240  CB  VAL B  49    10730  12340  11688    803    344    282       C  
ATOM    241  CG1 VAL B  49     -10.693   1.180 -26.784  1.00 88.43           C  
ANISOU  241  CG1 VAL B  49    10338  11958  11304    796    419    331       C  
ATOM    242  CG2 VAL B  49     -12.102   3.078 -27.582  1.00 91.39           C  
ANISOU  242  CG2 VAL B  49    10813  12253  11659    778    290    241       C  
ATOM    243  N   LEU B  50     -15.207   2.144 -26.683  1.00 88.11           N  
ANISOU  243  N   LEU B  50    10334  11829  11316    846    231    195       N  
ATOM    244  CA  LEU B  50     -16.471   2.843 -26.524  1.00 95.04           C  
ANISOU  244  CA  LEU B  50    11223  12688  12201    857    162    147       C  
ATOM    245  C   LEU B  50     -17.398   2.126 -25.542  1.00101.65           C  
ANISOU  245  C   LEU B  50    11986  13564  13072    894    168    152       C  
ATOM    246  O   LEU B  50     -18.126   2.781 -24.788  1.00 97.45           O  
ANISOU  246  O   LEU B  50    11426  13059  12542    909    122    123       O  
ATOM    247  CB  LEU B  50     -17.142   3.015 -27.882  1.00 90.23           C  
ANISOU  247  CB  LEU B  50    10703  11986  11592    841    124    113       C  
ATOM    248  CG  LEU B  50     -17.066   4.501 -28.222  1.00 91.64           C  
ANISOU  248  CG  LEU B  50    10938  12142  11738    817     62     74       C  
ATOM    249  CD1 LEU B  50     -17.775   4.798 -29.515  1.00 94.22           C  
ANISOU  249  CD1 LEU B  50    11355  12380  12064    802     18     37       C  
ATOM    250  CD2 LEU B  50     -17.600   5.351 -27.065  1.00 95.14           C  
ANISOU  250  CD2 LEU B  50    11333  12639  12179    833     16     47       C  
ATOM    251  N   TRP B  51     -17.373   0.790 -25.511  1.00102.42           N  
ANISOU  251  N   TRP B  51    12050  13668  13198    910    224    188       N  
ATOM    252  CA  TRP B  51     -18.105   0.098 -24.459  1.00 97.98           C  
ANISOU  252  CA  TRP B  51    11409  13152  12667    946    237    199       C  
ATOM    253  C   TRP B  51     -17.372   0.220 -23.132  1.00101.90           C  
ANISOU  253  C   TRP B  51    11825  13741  13153    958    265    226       C  
ATOM    254  O   TRP B  51     -18.004   0.489 -22.111  1.00108.51           O  
ANISOU  254  O   TRP B  51    12608  14623  13998    981    240    213       O  
ATOM    255  CB  TRP B  51     -18.367  -1.374 -24.829  1.00 97.80           C  
ANISOU  255  CB  TRP B  51    11374  13106  12679    960    287    228       C  
ATOM    256  CG  TRP B  51     -19.384  -2.069 -23.875  1.00122.06           C  
ANISOU  256  CG  TRP B  51    14374  16214  15789    998    290    232       C  
ATOM    257  CD1 TRP B  51     -20.745  -1.879 -23.852  1.00136.13           C  
ANISOU  257  CD1 TRP B  51    16162  17968  17591   1014    239    194       C  
ATOM    258  CD2 TRP B  51     -19.114  -3.074 -22.867  1.00126.74           C  
ANISOU  258  CD2 TRP B  51    14880  16872  16402   1024    348    277       C  
ATOM    259  NE1 TRP B  51     -21.326  -2.666 -22.879  1.00124.81           N  
ANISOU  259  NE1 TRP B  51    14652  16581  16191   1047    261    212       N  
ATOM    260  CE2 TRP B  51     -20.353  -3.411 -22.265  1.00121.46           C  
ANISOU  260  CE2 TRP B  51    14170  16213  15766   1054    328    262       C  
ATOM    261  CE3 TRP B  51     -17.950  -3.706 -22.406  1.00125.85           C  
ANISOU  261  CE3 TRP B  51    14722  16812  16284   1024    415    327       C  
ATOM    262  CZ2 TRP B  51     -20.455  -4.350 -21.224  1.00121.15           C  
ANISOU  262  CZ2 TRP B  51    14045  16233  15753   1084    372    297       C  
ATOM    263  CZ3 TRP B  51     -18.058  -4.645 -21.383  1.00123.19           C  
ANISOU  263  CZ3 TRP B  51    14300  16533  15973   1054    459    361       C  
ATOM    264  CH2 TRP B  51     -19.301  -4.944 -20.795  1.00120.76           C  
ANISOU  264  CH2 TRP B  51    13953  16234  15697   1084    437    346       C  
ATOM    265  N   THR B  52     -16.036   0.078 -23.127  1.00100.48           N  
ANISOU  265  N   THR B  52    11637  13588  12953    942    313    263       N  
ATOM    266  CA  THR B  52     -15.303   0.071 -21.859  1.00100.04           C  
ANISOU  266  CA  THR B  52    11502  13621  12889    955    345    292       C  
ATOM    267  C   THR B  52     -15.446   1.386 -21.106  1.00101.45           C  
ANISOU  267  C   THR B  52    11666  13836  13044    955    290    259       C  
ATOM    268  O   THR B  52     -15.491   1.389 -19.864  1.00 98.36           O  
ANISOU  268  O   THR B  52    11200  13515  12656    978    297    269       O  
ATOM    269  CB  THR B  52     -13.817  -0.200 -22.064  1.00 87.12           C  
ANISOU  269  CB  THR B  52     9866  12003  11233    935    402    333       C  
ATOM    270  OG1 THR B  52     -13.189   0.970 -22.596  1.00 88.60           O  
ANISOU  270  OG1 THR B  52    10111  12169  11385    903    370    312       O  
ATOM    271  CG2 THR B  52     -13.615  -1.352 -23.005  1.00 87.53           C  
ANISOU  271  CG2 THR B  52     9947  12008  11303    929    451    361       C  
ATOM    272  N   VAL B  53     -15.505   2.508 -21.830  1.00 97.07           N  
ANISOU  272  N   VAL B  53    11182  13235  12465    929    237    221       N  
ATOM    273  CA  VAL B  53     -15.728   3.778 -21.150  1.00103.27           C  
ANISOU  273  CA  VAL B  53    11956  14051  13230    929    180    186       C  
ATOM    274  C   VAL B  53     -17.192   3.922 -20.751  1.00112.90           C  
ANISOU  274  C   VAL B  53    13161  15265  14472    954    130    150       C  
ATOM    275  O   VAL B  53     -17.505   4.548 -19.733  1.00119.98           O  
ANISOU  275  O   VAL B  53    14012  16213  15363    970    100    134       O  
ATOM    276  CB  VAL B  53     -15.255   4.949 -22.025  1.00 96.04           C  
ANISOU  276  CB  VAL B  53    11120  13091  12282    893    140    158       C  
ATOM    277  CG1 VAL B  53     -15.708   6.289 -21.446  1.00 93.69           C  
ANISOU  277  CG1 VAL B  53    10820  12813  11967    894     72    115       C  
ATOM    278  CG2 VAL B  53     -13.753   4.915 -22.140  1.00 96.96           C  
ANISOU  278  CG2 VAL B  53    11235  13229  12374    872    189    195       C  
ATOM    279  N   PHE B  54     -18.109   3.325 -21.504  1.00111.06           N  
ANISOU  279  N   PHE B  54    12963  14972  14265    960    122    138       N  
ATOM    280  CA  PHE B  54     -19.515   3.449 -21.154  1.00113.34           C  
ANISOU  280  CA  PHE B  54    13237  15252  14574    983     74    103       C  
ATOM    281  C   PHE B  54     -20.047   2.260 -20.360  1.00122.59           C  
ANISOU  281  C   PHE B  54    14333  16462  15782   1019    114    131       C  
ATOM    282  O   PHE B  54     -21.098   2.393 -19.719  1.00129.49           O  
ANISOU  282  O   PHE B  54    15174  17352  16673   1043     80    108       O  
ATOM    283  CB  PHE B  54     -20.355   3.681 -22.417  1.00108.42           C  
ANISOU  283  CB  PHE B  54    12698  14538  13958    969     29     65       C  
ATOM    284  CG  PHE B  54     -20.152   5.052 -23.043  1.00123.36           C  
ANISOU  284  CG  PHE B  54    14661  16394  15816    940    -27     26       C  
ATOM    285  CD1 PHE B  54     -19.176   5.923 -22.563  1.00117.54           C  
ANISOU  285  CD1 PHE B  54    13913  15702  15047    925    -30     30       C  
ATOM    286  CD2 PHE B  54     -20.941   5.474 -24.102  1.00130.03           C  
ANISOU  286  CD2 PHE B  54    15583  17159  16662    927    -78    -14       C  
ATOM    287  CE1 PHE B  54     -18.986   7.175 -23.133  1.00113.92           C  
ANISOU  287  CE1 PHE B  54    13517  15209  14558    897    -81     -4       C  
ATOM    288  CE2 PHE B  54     -20.756   6.731 -24.674  1.00133.57           C  
ANISOU  288  CE2 PHE B  54    16096  17575  17080    900   -130    -49       C  
ATOM    289  CZ  PHE B  54     -19.778   7.577 -24.191  1.00126.79           C  
ANISOU  289  CZ  PHE B  54    15225  16761  16190    885   -130    -43       C  
ATOM    290  N   ARG B  55     -19.349   1.113 -20.367  1.00120.32           N  
ANISOU  290  N   ARG B  55    14018  16192  15508   1022    184    180       N  
ATOM    291  CA  ARG B  55     -19.685   0.028 -19.440  1.00117.88           C  
ANISOU  291  CA  ARG B  55    13628  15932  15230   1056    227    211       C  
ATOM    292  C   ARG B  55     -19.703   0.547 -18.017  1.00124.66           C  
ANISOU  292  C   ARG B  55    14413  16873  16080   1077    215    210       C  
ATOM    293  O   ARG B  55     -20.646   0.292 -17.261  1.00140.48           O  
ANISOU  293  O   ARG B  55    16368  18902  18107   1107    203    203       O  
ATOM    294  CB  ARG B  55     -18.692  -1.129 -19.573  1.00112.76           C  
ANISOU  294  CB  ARG B  55    12956  15298  14588   1054    306    266       C  
ATOM    295  CG  ARG B  55     -18.524  -1.973 -18.340  1.00117.36           C  
ANISOU  295  CG  ARG B  55    13445  15958  15189   1085    356    307       C  
ATOM    296  CD  ARG B  55     -17.556  -3.091 -18.605  1.00114.51           C  
ANISOU  296  CD  ARG B  55    13070  15603  14835   1080    431    359       C  
ATOM    297  NE  ARG B  55     -16.856  -3.496 -17.401  1.00114.28           N  
ANISOU  297  NE  ARG B  55    12957  15658  14804   1098    478    399       N  
ATOM    298  CZ  ARG B  55     -17.394  -4.254 -16.451  1.00121.95           C  
ANISOU  298  CZ  ARG B  55    13856  16676  15803   1132    501    418       C  
ATOM    299  NH1 ARG B  55     -16.690  -4.578 -15.370  1.00120.59           N  
ANISOU  299  NH1 ARG B  55    13610  16582  15627   1148    544    455       N  
ATOM    300  NH2 ARG B  55     -18.646  -4.684 -16.578  1.00131.33           N  
ANISOU  300  NH2 ARG B  55    15044  17832  17024   1150    481    400       N  
ATOM    301  N   SER B  56     -18.664   1.296 -17.644  1.00124.08           N  
ANISOU  301  N   SER B  56    14332  16839  15972   1062    218    217       N  
ATOM    302  CA  SER B  56     -18.726   2.121 -16.444  1.00127.27           C  
ANISOU  302  CA  SER B  56    14684  17311  16362   1077    189    203       C  
ATOM    303  C   SER B  56     -19.854   3.139 -16.578  1.00140.00           C  
ANISOU  303  C   SER B  56    16331  18890  17971   1077    110    146       C  
ATOM    304  O   SER B  56     -19.954   3.858 -17.579  1.00144.46           O  
ANISOU  304  O   SER B  56    16973  19393  18522   1051     69    113       O  
ATOM    305  CB  SER B  56     -17.387   2.832 -16.201  1.00125.09           C  
ANISOU  305  CB  SER B  56    14407  17074  16049   1056    201    216       C  
ATOM    306  OG  SER B  56     -17.427   3.646 -15.034  1.00126.01           O  
ANISOU  306  OG  SER B  56    14473  17256  16151   1070    172    202       O  
ATOM    307  N   SER B  57     -20.718   3.176 -15.566  1.00152.50           N  
ANISOU  307  N   SER B  57    17857  20516  19570   1108     90    133       N  
ATOM    308  CA  SER B  57     -21.849   4.092 -15.504  1.00149.50           C  
ANISOU  308  CA  SER B  57    17498  20115  19190   1114     16     80       C  
ATOM    309  C   SER B  57     -21.619   5.220 -14.515  1.00138.44           C  
ANISOU  309  C   SER B  57    16065  18775  17762   1118    -19     62       C  
ATOM    310  O   SER B  57     -22.477   6.100 -14.368  1.00143.28           O  
ANISOU  310  O   SER B  57    16691  19377  18371   1123    -82     17       O  
ATOM    311  CB  SER B  57     -23.118   3.329 -15.103  1.00165.98           C  
ANISOU  311  CB  SER B  57    19546  22203  21316   1147     14     77       C  
ATOM    312  OG  SER B  57     -23.050   2.946 -13.733  1.00143.75           O  
ANISOU  312  OG  SER B  57    16640  19472  18508   1178     44    103       O  
ATOM    313  N   ARG B  58     -20.491   5.214 -13.833  1.00133.23           N  
ANISOU  313  N   ARG B  58    15361  18177  17083   1117     20     95       N  
ATOM    314  CA  ARG B  58     -20.373   5.993 -12.624  1.00146.22           C  
ANISOU  314  CA  ARG B  58    16952  19894  18711   1132     -2     85       C  
ATOM    315  C   ARG B  58     -19.936   7.421 -12.917  1.00141.93           C  
ANISOU  315  C   ARG B  58    16457  19337  18131   1105    -55     50       C  
ATOM    316  O   ARG B  58     -19.762   7.838 -14.065  1.00131.58           O  
ANISOU  316  O   ARG B  58    15225  17960  16810   1074    -75     32       O  
ATOM    317  CB  ARG B  58     -19.407   5.299 -11.664  1.00140.81           C  
ANISOU  317  CB  ARG B  58    16191  19287  18023   1147     63    136       C  
ATOM    318  CG  ARG B  58     -19.817   3.883 -11.307  1.00142.48           C  
ANISOU  318  CG  ARG B  58    16350  19516  18270   1176    116    173       C  
ATOM    319  CD  ARG B  58     -21.295   3.856 -10.918  1.00155.21           C  
ANISOU  319  CD  ARG B  58    17943  21123  19908   1203     77    143       C  
ATOM    320  NE  ARG B  58     -21.586   4.758  -9.799  1.00176.83           N  
ANISOU  320  NE  ARG B  58    20636  23920  22630   1221     37    119       N  
ATOM    321  CZ  ARG B  58     -22.783   5.284  -9.545  1.00179.77           C  
ANISOU  321  CZ  ARG B  58    21008  24283  23012   1237    -19     78       C  
ATOM    322  NH1 ARG B  58     -23.811   5.008 -10.336  1.00174.60           N  
ANISOU  322  NH1 ARG B  58    20396  23562  22383   1236    -42     55       N  
ATOM    323  NH2 ARG B  58     -22.953   6.092  -8.504  1.00170.80           N  
ANISOU  323  NH2 ARG B  58    19830  23204  21861   1253    -52     58       N  
ATOM    324  N   GLU B  59     -19.814   8.191 -11.838  1.00140.82           N  
ANISOU  324  N   GLU B  59    16270  19260  17973   1117    -78     38       N  
ATOM    325  CA  GLU B  59     -18.905   9.319 -11.784  1.00142.78           C  
ANISOU  325  CA  GLU B  59    16539  19525  18186   1094   -101     26       C  
ATOM    326  C   GLU B  59     -17.498   8.871 -11.382  1.00139.23           C  
ANISOU  326  C   GLU B  59    16050  19127  17723   1089    -38     75       C  
ATOM    327  O   GLU B  59     -16.749   9.645 -10.778  1.00123.43           O  
ANISOU  327  O   GLU B  59    14028  17173  15695   1083    -47     74       O  
ATOM    328  CB  GLU B  59     -19.446  10.393 -10.832  1.00136.57           C  
ANISOU  328  CB  GLU B  59    15723  18782  17387   1110   -160    -12       C  
ATOM    329  CG  GLU B  59     -20.966  10.580 -10.919  1.00135.95           C  
ANISOU  329  CG  GLU B  59    15658  18669  17328   1126   -213    -53       C  
ATOM    330  CD  GLU B  59     -21.555  11.396  -9.766  1.00144.11           C  
ANISOU  330  CD  GLU B  59    16644  19757  18354   1150   -259    -83       C  
ATOM    331  OE1 GLU B  59     -22.203  12.421 -10.068  1.00145.18           O  
ANISOU  331  OE1 GLU B  59    16822  19858  18480   1142   -327   -132       O  
ATOM    332  OE2 GLU B  59     -21.359  11.051  -8.574  1.00135.07           O  
ANISOU  332  OE2 GLU B  59    15420  18689  17211   1178   -231    -59       O  
ATOM    333  N   LYS B  60     -17.154   7.608 -11.662  1.00137.05           N  
ANISOU  333  N   LYS B  60    15761  18846  17466   1092     27    119       N  
ATOM    334  CA  LYS B  60     -15.779   7.127 -11.713  1.00127.59           C  
ANISOU  334  CA  LYS B  60    14550  17673  16257   1078     88    165       C  
ATOM    335  C   LYS B  60     -15.207   7.183 -13.130  1.00121.55           C  
ANISOU  335  C   LYS B  60    13868  16834  15482   1040     95    165       C  
ATOM    336  O   LYS B  60     -14.315   6.394 -13.475  1.00121.36           O  
ANISOU  336  O   LYS B  60    13842  16809  15459   1030    154    207       O  
ATOM    337  CB  LYS B  60     -15.695   5.707 -11.146  1.00125.76           C  
ANISOU  337  CB  LYS B  60    14252  17481  16050   1105    157    214       C  
ATOM    338  CG  LYS B  60     -16.154   5.572  -9.699  1.00139.52           C  
ANISOU  338  CG  LYS B  60    15909  19301  17802   1144    158    219       C  
ATOM    339  CD  LYS B  60     -16.211   4.108  -9.271  1.00139.06           C  
ANISOU  339  CD  LYS B  60    15792  19272  17772   1170    224    266       C  
ATOM    340  CE  LYS B  60     -16.367   3.953  -7.767  1.00140.43           C  
ANISOU  340  CE  LYS B  60    15874  19533  17949   1207    236    280       C  
ATOM    341  NZ  LYS B  60     -16.110   2.545  -7.390  1.00106.48           N  
ANISOU  341  NZ  LYS B  60    11520  15264  13673   1228    308    332       N  
ATOM    342  N   ARG B  61     -15.720   8.088 -13.964  1.00120.83           N  
ANISOU  342  N   ARG B  61    13848  16680  15380   1020     35    121       N  
ATOM    343  CA  ARG B  61     -15.123   8.380 -15.261  1.00116.97           C  
ANISOU  343  CA  ARG B  61    13441  16125  14877    982     33    117       C  
ATOM    344  C   ARG B  61     -13.877   9.228 -15.047  1.00108.26           C  
ANISOU  344  C   ARG B  61    12339  15054  13740    960     35    123       C  
ATOM    345  O   ARG B  61     -13.969  10.329 -14.495  1.00 99.00           O  
ANISOU  345  O   ARG B  61    11159  13908  12550    960    -14     92       O  
ATOM    346  CB  ARG B  61     -16.109   9.133 -16.156  1.00129.01           C  
ANISOU  346  CB  ARG B  61    15041  17576  16401    968    -34     65       C  
ATOM    347  CG  ARG B  61     -17.571   8.771 -15.973  1.00133.99           C  
ANISOU  347  CG  ARG B  61    15658  18191  17061    996    -62     42       C  
ATOM    348  CD  ARG B  61     -18.434   9.384 -17.070  1.00127.89           C  
ANISOU  348  CD  ARG B  61    14968  17335  16288    978   -122     -5       C  
ATOM    349  NE  ARG B  61     -18.490   8.517 -18.245  1.00130.24           N  
ANISOU  349  NE  ARG B  61    15317  17566  16603    966    -93     10       N  
ATOM    350  CZ  ARG B  61     -19.209   7.399 -18.316  1.00121.71           C  
ANISOU  350  CZ  ARG B  61    14217  16472  15555    987    -67     24       C  
ATOM    351  NH1 ARG B  61     -19.941   7.011 -17.282  1.00121.08           N  
ANISOU  351  NH1 ARG B  61    14069  16440  15497   1021    -66     26       N  
ATOM    352  NH2 ARG B  61     -19.202   6.666 -19.421  1.00115.07           N  
ANISOU  352  NH2 ARG B  61    13426  15568  14726    974    -42     35       N  
ATOM    353  N   ARG B  62     -12.721   8.735 -15.489  1.00105.87           N  
ANISOU  353  N   ARG B  62    12047  14750  13430    941     89    161       N  
ATOM    354  CA  ARG B  62     -11.494   9.493 -15.299  1.00 96.21           C  
ANISOU  354  CA  ARG B  62    10822  13556  12176    919     94    169       C  
ATOM    355  C   ARG B  62     -11.541  10.789 -16.107  1.00 93.01           C  
ANISOU  355  C   ARG B  62    10495  13096  11748    888     32    126       C  
ATOM    356  O   ARG B  62     -12.250  10.900 -17.113  1.00 97.15           O  
ANISOU  356  O   ARG B  62    11085  13548  12278    876      2    100       O  
ATOM    357  CB  ARG B  62     -10.279   8.642 -15.666  1.00 93.90           C  
ANISOU  357  CB  ARG B  62    10526  13268  11882    905    167    220       C  
ATOM    358  CG  ARG B  62     -10.180   8.243 -17.095  1.00 92.56           C  
ANISOU  358  CG  ARG B  62    10433  13019  11717    880    181    224       C  
ATOM    359  CD  ARG B  62      -9.515   6.903 -17.219  1.00 92.74           C  
ANISOU  359  CD  ARG B  62    10430  13053  11755    885    259    277       C  
ATOM    360  NE  ARG B  62      -8.063   7.002 -17.225  1.00103.70           N  
ANISOU  360  NE  ARG B  62    11812  14467  13121    864    300    308       N  
ATOM    361  CZ  ARG B  62      -7.252   5.949 -17.240  1.00108.30           C  
ANISOU  361  CZ  ARG B  62    12368  15068  13712    865    370    356       C  
ATOM    362  NH1 ARG B  62      -7.766   4.736 -17.263  1.00100.48           N  
ANISOU  362  NH1 ARG B  62    11356  14073  12751    886    406    378       N  
ATOM    363  NH2 ARG B  62      -5.930   6.101 -17.231  1.00100.48           N  
ANISOU  363  NH2 ARG B  62    11373  14103  12703    846    404    383       N  
ATOM    364  N   SER B  63     -10.836  11.803 -15.596  1.00 96.95           N  
ANISOU  364  N   SER B  63    10981  13633  12221    877     11    117       N  
ATOM    365  CA  SER B  63     -10.773  13.111 -16.237  1.00 97.49           C  
ANISOU  365  CA  SER B  63    11117  13658  12266    848    -47     77       C  
ATOM    366  C   SER B  63     -10.601  12.966 -17.732  1.00 92.37           C  
ANISOU  366  C   SER B  63    10554  12927  11616    817    -40     77       C  
ATOM    367  O   SER B  63     -11.473  13.341 -18.522  1.00 90.21           O  
ANISOU  367  O   SER B  63    10341  12589  11345    809    -87     41       O  
ATOM    368  CB  SER B  63      -9.595  13.911 -15.677  1.00 95.47           C  
ANISOU  368  CB  SER B  63    10839  13452  11984    834    -44     85       C  
ATOM    369  OG  SER B  63      -8.367  13.348 -16.133  1.00 96.49           O  
ANISOU  369  OG  SER B  63    10975  13579  12107    814     17    128       O  
ATOM    370  N   ALA B  64      -9.476  12.387 -18.127  1.00 86.38           N  
ANISOU  370  N   ALA B  64     9800  12169  10852    801     19    118       N  
ATOM    371  CA  ALA B  64      -9.181  12.256 -19.538  1.00 86.91           C  
ANISOU  371  CA  ALA B  64     9947  12160  10914    770     29    121       C  
ATOM    372  C   ALA B  64      -9.965  11.095 -20.134  1.00 84.96           C  
ANISOU  372  C   ALA B  64     9716  11871  10696    784     53    131       C  
ATOM    373  O   ALA B  64      -9.398  10.296 -20.872  1.00 80.81           O  
ANISOU  373  O   ALA B  64     9214  11317  10174    771    103    162       O  
ATOM    374  CB  ALA B  64      -7.675  12.067 -19.748  1.00 85.25           C  
ANISOU  374  CB  ALA B  64     9737  11967  10689    748     84    161       C  
ATOM    375  N   ASP B  65     -11.255  10.970 -19.824  1.00 85.44           N  
ANISOU  375  N   ASP B  65     9762  11926  10776    809     19    105       N  
ATOM    376  CA  ASP B  65     -12.061   9.945 -20.479  1.00 88.83           C  
ANISOU  376  CA  ASP B  65    10212  12308  11232    819     35    109       C  
ATOM    377  C   ASP B  65     -13.052  10.518 -21.472  1.00 83.20           C  
ANISOU  377  C   ASP B  65     9577  11515  10519    807    -25     63       C  
ATOM    378  O   ASP B  65     -13.346   9.874 -22.488  1.00 84.43           O  
ANISOU  378  O   ASP B  65     9781  11610  10687    800    -12     67       O  
ATOM    379  CB  ASP B  65     -12.822   9.089 -19.458  1.00 95.89           C  
ANISOU  379  CB  ASP B  65    11029  13251  12155    859     53    122       C  
ATOM    380  CG  ASP B  65     -12.280   7.654 -19.375  1.00 97.45           C  
ANISOU  380  CG  ASP B  65    11186  13469  12371    871    132    175       C  
ATOM    381  OD1 ASP B  65     -11.340   7.333 -20.142  1.00 94.80           O  
ANISOU  381  OD1 ASP B  65    10885  13109  12026    847    172    201       O  
ATOM    382  OD2 ASP B  65     -12.756   6.857 -18.525  1.00 99.76           O  
ANISOU  382  OD2 ASP B  65    11412  13806  12687    903    156    192       O  
ATOM    383  N   ILE B  66     -13.563  11.719 -21.212  1.00 77.10           N  
ANISOU  383  N   ILE B  66     8818  10743   9734    805    -93     19       N  
ATOM    384  CA  ILE B  66     -14.442  12.356 -22.183  1.00 77.39           C  
ANISOU  384  CA  ILE B  66     8934  10704   9769    791   -153    -26       C  
ATOM    385  C   ILE B  66     -13.731  12.479 -23.527  1.00 76.76           C  
ANISOU  385  C   ILE B  66     8935  10559   9673    755   -141    -20       C  
ATOM    386  O   ILE B  66     -14.371  12.447 -24.585  1.00 77.40           O  
ANISOU  386  O   ILE B  66     9083  10567   9758    746   -165    -42       O  
ATOM    387  CB  ILE B  66     -14.901  13.719 -21.632  1.00 70.19           C  
ANISOU  387  CB  ILE B  66     8020   9808   8841    792   -224    -71       C  
ATOM    388  CG1 ILE B  66     -15.913  14.380 -22.546  1.00 73.78           C  
ANISOU  388  CG1 ILE B  66     8551  10187   9295    781   -289   -120       C  
ATOM    389  CG2 ILE B  66     -13.720  14.667 -21.507  1.00 71.83           C  
ANISOU  389  CG2 ILE B  66     8236  10040   9017    767   -227    -68       C  
ATOM    390  CD1 ILE B  66     -16.438  15.634 -21.932  1.00 76.17           C  
ANISOU  390  CD1 ILE B  66     8847  10508   9585    785   -358   -164       C  
ATOM    391  N   PHE B  67     -12.401  12.591 -23.515  1.00 79.38           N  
ANISOU  391  N   PHE B  67     9261  10916   9984    736   -102     10       N  
ATOM    392  CA  PHE B  67     -11.682  12.693 -24.770  1.00 78.63           C  
ANISOU  392  CA  PHE B  67     9242  10762   9873    702    -88     18       C  
ATOM    393  C   PHE B  67     -11.391  11.336 -25.370  1.00 80.19           C  
ANISOU  393  C   PHE B  67     9444  10938  10087    704    -23     58       C  
ATOM    394  O   PHE B  67     -11.346  11.214 -26.602  1.00 82.65           O  
ANISOU  394  O   PHE B  67     9828  11180  10395    683    -21     54       O  
ATOM    395  CB  PHE B  67     -10.375  13.444 -24.603  1.00 74.74           C  
ANISOU  395  CB  PHE B  67     8748  10299   9352    678    -77     32       C  
ATOM    396  CG  PHE B  67     -10.542  14.809 -24.088  1.00 74.51           C  
ANISOU  396  CG  PHE B  67     8718  10288   9304    672   -140     -6       C  
ATOM    397  CD1 PHE B  67     -10.989  15.807 -24.920  1.00 74.54           C  
ANISOU  397  CD1 PHE B  67     8798  10230   9294    651   -200    -48       C  
ATOM    398  CD2 PHE B  67     -10.218  15.115 -22.789  1.00 76.33           C  
ANISOU  398  CD2 PHE B  67     8874  10597   9531    688   -138      0       C  
ATOM    399  CE1 PHE B  67     -11.146  17.088 -24.467  1.00 76.17           C  
ANISOU  399  CE1 PHE B  67     9006  10452   9484    646   -259    -84       C  
ATOM    400  CE2 PHE B  67     -10.371  16.398 -22.319  1.00 77.65           C  
ANISOU  400  CE2 PHE B  67     9042  10781   9681    683   -198    -36       C  
ATOM    401  CZ  PHE B  67     -10.833  17.392 -23.163  1.00 75.86           C  
ANISOU  401  CZ  PHE B  67     8891  10491   9441    662   -259    -78       C  
ATOM    402  N   ILE B  68     -11.186  10.309 -24.543  1.00 82.72           N  
ANISOU  402  N   ILE B  68     9689  11315  10427    728     31     95       N  
ATOM    403  CA  ILE B  68     -10.929   8.989 -25.121  1.00 81.49           C  
ANISOU  403  CA  ILE B  68     9537  11137  10288    731     93    133       C  
ATOM    404  C   ILE B  68     -12.169   8.452 -25.819  1.00 87.01           C  
ANISOU  404  C   ILE B  68    10274  11775  11011    742     72    111       C  
ATOM    405  O   ILE B  68     -12.067   7.779 -26.858  1.00 89.95           O  
ANISOU  405  O   ILE B  68    10694  12093  11390    731     99    124       O  
ATOM    406  CB  ILE B  68     -10.417   8.002 -24.065  1.00 86.50           C  
ANISOU  406  CB  ILE B  68    10082  11846  10938    755    156    179       C  
ATOM    407  CG1 ILE B  68      -9.062   8.453 -23.542  1.00 84.38           C  
ANISOU  407  CG1 ILE B  68     9785  11632  10645    740    183    203       C  
ATOM    408  CG2 ILE B  68     -10.332   6.588 -24.641  1.00 86.17           C  
ANISOU  408  CG2 ILE B  68    10043  11780  10918    761    216    214       C  
ATOM    409  CD1 ILE B  68      -8.689   7.745 -22.279  1.00 85.51           C  
ANISOU  409  CD1 ILE B  68     9833  11857  10800    767    229    239       C  
ATOM    410  N   ALA B  69     -13.352   8.724 -25.256  1.00 85.70           N  
ANISOU  410  N   ALA B  69    10085  11617  10859    765     24     79       N  
ATOM    411  CA  ALA B  69     -14.585   8.464 -25.987  1.00 86.28           C  
ANISOU  411  CA  ALA B  69    10203  11625  10952    772     -9     49       C  
ATOM    412  C   ALA B  69     -14.584   9.217 -27.313  1.00 86.88           C  
ANISOU  412  C   ALA B  69    10379  11622  11009    741    -47     20       C  
ATOM    413  O   ALA B  69     -14.666   8.607 -28.386  1.00 83.36           O  
ANISOU  413  O   ALA B  69     9985  11116  10570    731    -30     26       O  
ATOM    414  CB  ALA B  69     -15.800   8.842 -25.144  1.00 79.25           C  
ANISOU  414  CB  ALA B  69     9276  10758  10077    799    -60     15       C  
ATOM    415  N   SER B  70     -14.442  10.546 -27.268  1.00 82.23           N  
ANISOU  415  N   SER B  70     9817  11033  10394    723    -99    -11       N  
ATOM    416  CA  SER B  70     -14.431  11.307 -28.515  1.00 81.20           C  
ANISOU  416  CA  SER B  70     9782  10828  10243    693   -136    -39       C  
ATOM    417  C   SER B  70     -13.374  10.792 -29.494  1.00 84.65           C  
ANISOU  417  C   SER B  70    10261  11232  10668    668    -83     -4       C  
ATOM    418  O   SER B  70     -13.629  10.711 -30.705  1.00 84.75           O  
ANISOU  418  O   SER B  70    10349  11171  10679    654    -94    -17       O  
ATOM    419  CB  SER B  70     -14.239  12.795 -28.234  1.00 74.15           C  
ANISOU  419  CB  SER B  70     8904   9947   9322    677   -191    -70       C  
ATOM    420  OG  SER B  70     -15.505  13.423 -28.146  1.00 77.17           O  
ANISOU  420  OG  SER B  70     9302  10306   9712    688   -260   -119       O  
ATOM    421  N   LEU B  71     -12.190  10.415 -28.995  1.00 87.34           N  
ANISOU  421  N   LEU B  71    10557  11627  11003    665    -25     39       N  
ATOM    422  CA  LEU B  71     -11.197   9.818 -29.885  1.00 87.47           C  
ANISOU  422  CA  LEU B  71    10609  11615  11011    644     30     74       C  
ATOM    423  C   LEU B  71     -11.760   8.589 -30.593  1.00 86.85           C  
ANISOU  423  C   LEU B  71    10550  11491  10959    656     59     86       C  
ATOM    424  O   LEU B  71     -11.534   8.398 -31.792  1.00 84.66           O  
ANISOU  424  O   LEU B  71    10342  11152  10674    636     69     88       O  
ATOM    425  CB  LEU B  71      -9.928   9.450 -29.111  1.00 85.77           C  
ANISOU  425  CB  LEU B  71    10330  11470  10789    644     91    120       C  
ATOM    426  CG  LEU B  71      -8.840   8.770 -29.965  1.00 92.06           C  
ANISOU  426  CG  LEU B  71    11158  12243  11579    623    153    160       C  
ATOM    427  CD1 LEU B  71      -7.471   9.169 -29.479  1.00 91.38           C  
ANISOU  427  CD1 LEU B  71    11043  12208  11471    607    184    187       C  
ATOM    428  CD2 LEU B  71      -8.956   7.230 -29.972  1.00 88.16           C  
ANISOU  428  CD2 LEU B  71    10630  11753  11113    644    213    196       C  
ATOM    429  N   ALA B  72     -12.485   7.736 -29.860  1.00 86.56           N  
ANISOU  429  N   ALA B  72    10452  11485  10952    688     73     94       N  
ATOM    430  CA  ALA B  72     -12.991   6.498 -30.443  1.00 88.38           C  
ANISOU  430  CA  ALA B  72    10693  11678  11210    701    104    108       C  
ATOM    431  C   ALA B  72     -14.079   6.753 -31.471  1.00 89.16           C  
ANISOU  431  C   ALA B  72    10866  11695  11314    697     51     66       C  
ATOM    432  O   ALA B  72     -14.180   6.016 -32.457  1.00 88.36           O  
ANISOU  432  O   ALA B  72    10810  11540  11222    693     73     75       O  
ATOM    433  CB  ALA B  72     -13.532   5.576 -29.356  1.00 87.48           C  
ANISOU  433  CB  ALA B  72    10493  11619  11128    738    130    126       C  
ATOM    434  N   VAL B  73     -14.901   7.779 -31.258  1.00 88.35           N  
ANISOU  434  N   VAL B  73    10778  11584  11205    699    -18     21       N  
ATOM    435  CA  VAL B  73     -16.050   7.996 -32.129  1.00 86.24           C  
ANISOU  435  CA  VAL B  73    10576  11244  10947    699    -71    -21       C  
ATOM    436  C   VAL B  73     -15.591   8.471 -33.507  1.00 85.33           C  
ANISOU  436  C   VAL B  73    10557  11059  10807    666    -83    -31       C  
ATOM    437  O   VAL B  73     -16.069   7.986 -34.537  1.00 90.29           O  
ANISOU  437  O   VAL B  73    11240  11620  11444    663    -85    -40       O  
ATOM    438  CB  VAL B  73     -17.027   8.990 -31.478  1.00 82.13           C  
ANISOU  438  CB  VAL B  73    10043  10736  10427    710   -142    -67       C  
ATOM    439  CG1 VAL B  73     -18.374   8.938 -32.159  1.00 80.63           C  
ANISOU  439  CG1 VAL B  73     9901  10481  10256    719   -191   -106       C  
ATOM    440  CG2 VAL B  73     -17.176   8.686 -30.032  1.00 84.32           C  
ANISOU  440  CG2 VAL B  73    10223  11094  10720    739   -127    -52       C  
ATOM    441  N   ALA B  74     -14.650   9.416 -33.553  1.00 85.33           N  
ANISOU  441  N   ALA B  74    10577  11071  10775    640    -89    -30       N  
ATOM    442  CA  ALA B  74     -14.187   9.916 -34.844  1.00 84.25           C  
ANISOU  442  CA  ALA B  74    10531  10868  10612    608   -100    -39       C  
ATOM    443  C   ALA B  74     -13.342   8.879 -35.572  1.00 84.24           C  
ANISOU  443  C   ALA B  74    10547  10848  10612    599    -31      3       C  
ATOM    444  O   ALA B  74     -13.460   8.731 -36.797  1.00 85.68           O  
ANISOU  444  O   ALA B  74    10804  10961  10790    585    -35     -5       O  
ATOM    445  CB  ALA B  74     -13.407  11.213 -34.659  1.00 88.89           C  
ANISOU  445  CB  ALA B  74    11133  11476  11167    583   -125    -49       C  
ATOM    446  N   ASP B  75     -12.473   8.164 -34.845  1.00 85.30           N  
ANISOU  446  N   ASP B  75    10614  11044  10753    607     32     49       N  
ATOM    447  CA  ASP B  75     -11.796   7.022 -35.455  1.00 88.43           C  
ANISOU  447  CA  ASP B  75    11018  11425  11155    603    100     90       C  
ATOM    448  C   ASP B  75     -12.792   6.001 -35.971  1.00 88.90           C  
ANISOU  448  C   ASP B  75    11092  11440  11246    623    104     84       C  
ATOM    449  O   ASP B  75     -12.545   5.361 -37.002  1.00 89.10           O  
ANISOU  449  O   ASP B  75    11167  11416  11272    613    133     99       O  
ATOM    450  CB  ASP B  75     -10.834   6.349 -34.479  1.00 88.17           C  
ANISOU  450  CB  ASP B  75    10903  11469  11128    612    165    138       C  
ATOM    451  CG  ASP B  75      -9.517   7.093 -34.350  1.00 94.64           C  
ANISOU  451  CG  ASP B  75    11724  12318  11916    586    182    155       C  
ATOM    452  OD1 ASP B  75      -9.044   7.653 -35.363  1.00 99.46           O  
ANISOU  452  OD1 ASP B  75    12409  12879  12503    558    172    147       O  
ATOM    453  OD2 ASP B  75      -8.939   7.104 -33.239  1.00 86.45           O  
ANISOU  453  OD2 ASP B  75    10613  11354  10878    595    206    178       O  
ATOM    454  N   LEU B  76     -13.931   5.855 -35.291  1.00 87.39           N  
ANISOU  454  N   LEU B  76    10860  11264  11080    650     73     63       N  
ATOM    455  CA  LEU B  76     -14.931   4.887 -35.728  1.00 90.12           C  
ANISOU  455  CA  LEU B  76    11215  11568  11457    670     74     57       C  
ATOM    456  C   LEU B  76     -15.656   5.364 -36.985  1.00 86.05           C  
ANISOU  456  C   LEU B  76    10794  10966  10935    656     22     16       C  
ATOM    457  O   LEU B  76     -15.608   4.697 -38.028  1.00 87.81           O  
ANISOU  457  O   LEU B  76    11068  11135  11163    650     45     25       O  
ATOM    458  CB  LEU B  76     -15.919   4.605 -34.599  1.00 85.85           C  
ANISOU  458  CB  LEU B  76    10601  11071  10946    703     58     47       C  
ATOM    459  CG  LEU B  76     -16.406   3.165 -34.584  1.00 83.34           C  
ANISOU  459  CG  LEU B  76    10250  10749  10666    728     99     70       C  
ATOM    460  CD1 LEU B  76     -15.224   2.226 -34.664  1.00 78.98           C  
ANISOU  460  CD1 LEU B  76     9676  10220  10113    722    178    123       C  
ATOM    461  CD2 LEU B  76     -17.158   2.917 -33.300  1.00 89.67           C  
ANISOU  461  CD2 LEU B  76    10969  11609  11495    760     91     68       C  
ATOM    462  N   THR B  77     -16.339   6.517 -36.910  1.00 81.55           N  
ANISOU  462  N   THR B  77    10250  10381  10353    652    -48    -29       N  
ATOM    463  CA  THR B  77     -17.074   7.009 -38.071  1.00 83.12           C  
ANISOU  463  CA  THR B  77    10538  10498  10545    640   -101    -70       C  
ATOM    464  C   THR B  77     -16.193   7.020 -39.313  1.00 88.72           C  
ANISOU  464  C   THR B  77    11323  11157  11230    612    -77    -56       C  
ATOM    465  O   THR B  77     -16.693   6.903 -40.442  1.00 89.66           O  
ANISOU  465  O   THR B  77    11513  11202  11349    606    -97    -76       O  
ATOM    466  CB  THR B  77     -17.624   8.419 -37.823  1.00 83.57           C  
ANISOU  466  CB  THR B  77    10615  10551  10586    634   -177   -117       C  
ATOM    467  OG1 THR B  77     -16.545   9.322 -37.549  1.00 86.86           O  
ANISOU  467  OG1 THR B  77    11032  11002  10970    611   -173   -107       O  
ATOM    468  CG2 THR B  77     -18.624   8.436 -36.676  1.00 80.98           C  
ANISOU  468  CG2 THR B  77    10220  10267  10283    663   -206   -135       C  
ATOM    469  N   PHE B  78     -14.877   7.132 -39.125  1.00 87.55           N  
ANISOU  469  N   PHE B  78    11159  11045  11060    594    -33    -22       N  
ATOM    470  CA  PHE B  78     -13.954   7.065 -40.252  1.00 85.41           C  
ANISOU  470  CA  PHE B  78    10954  10732  10766    567     -3     -4       C  
ATOM    471  C   PHE B  78     -13.872   5.653 -40.819  1.00 87.87           C  
ANISOU  471  C   PHE B  78    11268  11020  11099    578     54     27       C  
ATOM    472  O   PHE B  78     -14.176   5.424 -41.996  1.00 88.08           O  
ANISOU  472  O   PHE B  78    11366  10976  11124    570     45     15       O  
ATOM    473  CB  PHE B  78     -12.573   7.544 -39.810  1.00 84.40           C  
ANISOU  473  CB  PHE B  78    10802  10655  10612    548     31     26       C  
ATOM    474  CG  PHE B  78     -11.480   7.225 -40.789  1.00 84.71           C  
ANISOU  474  CG  PHE B  78    10890  10664  10632    524     79     56       C  
ATOM    475  CD1 PHE B  78     -11.663   7.430 -42.145  1.00 85.05           C  
ANISOU  475  CD1 PHE B  78    11026  10628  10661    507     58     37       C  
ATOM    476  CD2 PHE B  78     -10.257   6.739 -40.347  1.00 84.26           C  
ANISOU  476  CD2 PHE B  78    10785  10658  10570    519    145    103       C  
ATOM    477  CE1 PHE B  78     -10.660   7.147 -43.030  1.00 85.41           C  
ANISOU  477  CE1 PHE B  78    11116  10648  10689    485    102     64       C  
ATOM    478  CE2 PHE B  78      -9.246   6.455 -41.240  1.00 83.73           C  
ANISOU  478  CE2 PHE B  78    10763  10565  10486    497    189    131       C  
ATOM    479  CZ  PHE B  78      -9.449   6.662 -42.575  1.00 84.37           C  
ANISOU  479  CZ  PHE B  78    10936  10568  10553    480    168    111       C  
ATOM    480  N   VAL B  79     -13.461   4.691 -39.985  1.00 88.22           N  
ANISOU  480  N   VAL B  79    11234  11123  11163    595    111     67       N  
ATOM    481  CA  VAL B  79     -13.082   3.368 -40.460  1.00 85.34           C  
ANISOU  481  CA  VAL B  79    10866  10745  10814    601    175    104       C  
ATOM    482  C   VAL B  79     -14.256   2.610 -41.027  1.00 85.50           C  
ANISOU  482  C   VAL B  79    10910  10712  10864    620    159     85       C  
ATOM    483  O   VAL B  79     -14.063   1.631 -41.755  1.00 86.73           O  
ANISOU  483  O   VAL B  79    11088  10835  11031    621    200    106       O  
ATOM    484  CB  VAL B  79     -12.448   2.560 -39.325  1.00 86.20           C  
ANISOU  484  CB  VAL B  79    10880  10933  10940    617    236    149       C  
ATOM    485  CG1 VAL B  79     -11.185   3.235 -38.856  1.00 85.16           C  
ANISOU  485  CG1 VAL B  79    10728  10851  10779    597    257    170       C  
ATOM    486  CG2 VAL B  79     -13.441   2.406 -38.200  1.00 85.59           C  
ANISOU  486  CG2 VAL B  79    10732  10897  10890    648    213    135       C  
ATOM    487  N   VAL B  80     -15.476   3.020 -40.690  1.00 82.55           N  
ANISOU  487  N   VAL B  80    10530  10329  10506    636    100     45       N  
ATOM    488  CA  VAL B  80     -16.642   2.372 -41.267  1.00 83.64           C  
ANISOU  488  CA  VAL B  80    10695  10413  10672    653     79     24       C  
ATOM    489  C   VAL B  80     -16.727   2.646 -42.765  1.00 86.93           C  
ANISOU  489  C   VAL B  80    11214  10743  11070    633     56      2       C  
ATOM    490  O   VAL B  80     -17.253   1.821 -43.525  1.00 85.58           O  
ANISOU  490  O   VAL B  80    11075  10523  10920    642     63     -1       O  
ATOM    491  CB  VAL B  80     -17.894   2.838 -40.513  1.00 80.08           C  
ANISOU  491  CB  VAL B  80    10212   9975  10240    674     20    -14       C  
ATOM    492  CG1 VAL B  80     -19.160   2.496 -41.292  1.00 83.39           C  
ANISOU  492  CG1 VAL B  80    10678  10324  10682    686    -18    -48       C  
ATOM    493  CG2 VAL B  80     -17.910   2.225 -39.134  1.00 78.71           C  
ANISOU  493  CG2 VAL B  80     9936   9880  10092    699     53     12       C  
ATOM    494  N   THR B  81     -16.189   3.785 -43.220  1.00 86.05           N  
ANISOU  494  N   THR B  81    11158  10615  10922    605     28    -13       N  
ATOM    495  CA  THR B  81     -16.213   4.142 -44.635  1.00 86.89           C  
ANISOU  495  CA  THR B  81    11364  10642  11007    585      4    -34       C  
ATOM    496  C   THR B  81     -15.126   3.448 -45.443  1.00 86.43           C  
ANISOU  496  C   THR B  81    11337  10566  10937    570     67      5       C  
ATOM    497  O   THR B  81     -15.194   3.454 -46.674  1.00 90.18           O  
ANISOU  497  O   THR B  81    11893  10972  11400    557     57     -8       O  
ATOM    498  CB  THR B  81     -16.060   5.659 -44.808  1.00 87.93           C  
ANISOU  498  CB  THR B  81    11544  10762  11104    561    -50    -65       C  
ATOM    499  OG1 THR B  81     -14.668   6.007 -44.891  1.00 83.83           O  
ANISOU  499  OG1 THR B  81    11031  10266  10553    535    -12    -35       O  
ATOM    500  CG2 THR B  81     -16.690   6.393 -43.633  1.00 90.37           C  
ANISOU  500  CG2 THR B  81    11797  11119  11420    573    -96    -90       C  
ATOM    501  N   LEU B  82     -14.131   2.864 -44.791  1.00 83.66           N  
ANISOU  501  N   LEU B  82    10925  10274  10588    571    131     51       N  
ATOM    502  CA  LEU B  82     -12.990   2.247 -45.468  1.00 85.51           C  
ANISOU  502  CA  LEU B  82    11183  10499  10810    556    194     90       C  
ATOM    503  C   LEU B  82     -13.334   1.083 -46.407  1.00 90.29           C  
ANISOU  503  C   LEU B  82    11822  11049  11434    566    220     98       C  
ATOM    504  O   LEU B  82     -12.551   0.791 -47.322  1.00 90.35           O  
ANISOU  504  O   LEU B  82    11878  11026  11425    549    256    118       O  
ATOM    505  CB  LEU B  82     -11.974   1.799 -44.420  1.00 85.30           C  
ANISOU  505  CB  LEU B  82    11072  10552  10786    559    255    137       C  
ATOM    506  CG  LEU B  82     -11.233   3.018 -43.880  1.00 86.62           C  
ANISOU  506  CG  LEU B  82    11230  10761  10923    539    238    134       C  
ATOM    507  CD1 LEU B  82     -10.452   2.699 -42.587  1.00 86.56           C  
ANISOU  507  CD1 LEU B  82    11126  10841  10921    547    286    173       C  
ATOM    508  CD2 LEU B  82     -10.310   3.556 -44.993  1.00 85.52           C  
ANISOU  508  CD2 LEU B  82    11170  10578  10747    506    247    139       C  
ATOM    509  N   PRO B  83     -14.452   0.374 -46.222  1.00 86.95           N  
ANISOU  509  N   PRO B  83    11375  10614  11047    593    206     84       N  
ATOM    510  CA  PRO B  83     -14.952  -0.443 -47.332  1.00 85.45           C  
ANISOU  510  CA  PRO B  83    11240  10356  10872    599    212     78       C  
ATOM    511  C   PRO B  83     -15.171   0.362 -48.590  1.00 87.03           C  
ANISOU  511  C   PRO B  83    11543  10481  11045    579    164     43       C  
ATOM    512  O   PRO B  83     -14.984  -0.172 -49.687  1.00 90.36           O  
ANISOU  512  O   PRO B  83    12022  10848  11461    573    185     50       O  
ATOM    513  CB  PRO B  83     -16.273  -0.996 -46.794  1.00 88.27           C  
ANISOU  513  CB  PRO B  83    11554  10714  11270    630    186     58       C  
ATOM    514  CG  PRO B  83     -16.067  -1.080 -45.345  1.00 86.29           C  
ANISOU  514  CG  PRO B  83    11207  10548  11033    644    207     80       C  
ATOM    515  CD  PRO B  83     -15.119   0.026 -44.955  1.00 86.71           C  
ANISOU  515  CD  PRO B  83    11257  10640  11049    620    203     85       C  
ATOM    516  N   LEU B  84     -15.566   1.632 -48.473  1.00 84.39           N  
ANISOU  516  N   LEU B  84    11234  10140  10691    568    102      6       N  
ATOM    517  CA  LEU B  84     -15.733   2.449 -49.670  1.00 89.29           C  
ANISOU  517  CA  LEU B  84    11954  10689  11284    548     57    -27       C  
ATOM    518  C   LEU B  84     -14.381   2.784 -50.298  1.00 86.41           C  
ANISOU  518  C   LEU B  84    11631  10318  10881    518     92     -1       C  
ATOM    519  O   LEU B  84     -14.168   2.552 -51.497  1.00 84.14           O  
ANISOU  519  O   LEU B  84    11417   9973  10581    507    102      0       O  
ATOM    520  CB  LEU B  84     -16.525   3.719 -49.345  1.00 80.58           C  
ANISOU  520  CB  LEU B  84    10864   9581  10172    545    -20    -74       C  
ATOM    521  CG  LEU B  84     -17.827   3.607 -48.541  1.00 78.63           C  
ANISOU  521  CG  LEU B  84    10567   9349   9959    573    -61   -101       C  
ATOM    522  CD1 LEU B  84     -18.550   4.938 -48.548  1.00 82.75           C  
ANISOU  522  CD1 LEU B  84    11126   9850  10466    565   -140   -151       C  
ATOM    523  CD2 LEU B  84     -18.730   2.524 -49.062  1.00 79.95           C  
ANISOU  523  CD2 LEU B  84    10747   9472  10160    595    -58   -108       C  
ATOM    524  N   TRP B  85     -13.440   3.310 -49.500  1.00 87.91           N  
ANISOU  524  N   TRP B  85    11778  10571  11055    506    114     21       N  
ATOM    525  CA  TRP B  85     -12.116   3.626 -50.034  1.00 88.90           C  
ANISOU  525  CA  TRP B  85    11938  10695  11145    477    150     48       C  
ATOM    526  C   TRP B  85     -11.300   2.391 -50.352  1.00 89.43           C  
ANISOU  526  C   TRP B  85    11991  10768  11220    480    227     94       C  
ATOM    527  O   TRP B  85     -10.274   2.504 -51.031  1.00 88.33           O  
ANISOU  527  O   TRP B  85    11894  10615  11055    457    259    115       O  
ATOM    528  CB  TRP B  85     -11.331   4.512 -49.073  1.00 88.04           C  
ANISOU  528  CB  TRP B  85    11782  10650  11017    464    151     59       C  
ATOM    529  CG  TRP B  85     -11.956   5.814 -48.951  1.00 86.66           C  
ANISOU  529  CG  TRP B  85    11635  10464  10829    456     78     15       C  
ATOM    530  CD1 TRP B  85     -12.554   6.329 -47.858  1.00 87.34           C  
ANISOU  530  CD1 TRP B  85    11666  10594  10927    469     40     -5       C  
ATOM    531  CD2 TRP B  85     -12.098   6.777 -49.986  1.00 85.86           C  
ANISOU  531  CD2 TRP B  85    11625  10299  10698    434     30    -17       C  
ATOM    532  NE1 TRP B  85     -13.056   7.574 -48.136  1.00 90.59           N  
ANISOU  532  NE1 TRP B  85    12128  10974  11319    456    -29    -48       N  
ATOM    533  CE2 TRP B  85     -12.786   7.875 -49.441  1.00 87.62           C  
ANISOU  533  CE2 TRP B  85    11842  10531  10917    435    -36    -56       C  
ATOM    534  CE3 TRP B  85     -11.707   6.819 -51.326  1.00 89.20           C  
ANISOU  534  CE3 TRP B  85    12135  10658  11098    415     38    -16       C  
ATOM    535  CZ2 TRP B  85     -13.094   9.010 -50.180  1.00 91.71           C  
ANISOU  535  CZ2 TRP B  85    12438  10996  11410    416    -95    -94       C  
ATOM    536  CZ3 TRP B  85     -12.009   7.946 -52.068  1.00 93.41           C  
ANISOU  536  CZ3 TRP B  85    12746  11140  11606    397    -21    -53       C  
ATOM    537  CH2 TRP B  85     -12.698   9.030 -51.490  1.00 95.02           C  
ANISOU  537  CH2 TRP B  85    12942  11354  11807    397    -87    -92       C  
ATOM    538  N   ALA B  86     -11.730   1.221 -49.877  1.00 89.21           N  
ANISOU  538  N   ALA B  86    11906  10760  11229    506    257    110       N  
ATOM    539  CA  ALA B  86     -11.033  -0.014 -50.224  1.00 87.41           C  
ANISOU  539  CA  ALA B  86    11667  10533  11010    510    328    152       C  
ATOM    540  C   ALA B  86     -11.362  -0.450 -51.649  1.00 90.10           C  
ANISOU  540  C   ALA B  86    12092  10792  11348    508    324    140       C  
ATOM    541  O   ALA B  86     -10.482  -0.916 -52.379  1.00 88.72           O  
ANISOU  541  O   ALA B  86    11949  10600  11159    496    372    168       O  
ATOM    542  CB  ALA B  86     -11.368  -1.123 -49.224  1.00 91.85           C  
ANISOU  542  CB  ALA B  86    12139  11146  11614    540    363    175       C  
ATOM    543  N   THR B  87     -12.625  -0.299 -52.070  1.00 89.84           N  
ANISOU  543  N   THR B  87    12098  10709  11329    520    266     97       N  
ATOM    544  CA  THR B  87     -12.962  -0.579 -53.466  1.00 88.41           C  
ANISOU  544  CA  THR B  87    12004  10447  11142    516    255     81       C  
ATOM    545  C   THR B  87     -12.381   0.480 -54.400  1.00 89.78           C  
ANISOU  545  C   THR B  87    12262  10580  11271    485    234     68       C  
ATOM    546  O   THR B  87     -11.729   0.138 -55.388  1.00 87.92           O  
ANISOU  546  O   THR B  87    12080  10307  11017    473    267     85       O  
ATOM    547  CB  THR B  87     -14.479  -0.690 -53.662  1.00 88.16           C  
ANISOU  547  CB  THR B  87    11990  10370  11136    537    198     38       C  
ATOM    548  OG1 THR B  87     -15.055   0.613 -53.838  1.00 89.33           O  
ANISOU  548  OG1 THR B  87    12185  10491  11264    526    126     -7       O  
ATOM    549  CG2 THR B  87     -15.125  -1.382 -52.480  1.00 82.65           C  
ANISOU  549  CG2 THR B  87    11200   9723  10480    566    206     45       C  
ATOM    550  N   TYR B  88     -12.589   1.771 -54.094  1.00 87.74           N  
ANISOU  550  N   TYR B  88    12016  10328  10992    473    179     39       N  
ATOM    551  CA  TYR B  88     -12.169   2.844 -55.001  1.00 89.56           C  
ANISOU  551  CA  TYR B  88    12332  10516  11183    444    151     22       C  
ATOM    552  C   TYR B  88     -10.681   2.755 -55.329  1.00 88.56           C  
ANISOU  552  C   TYR B  88    12215  10405  11028    422    212     64       C  
ATOM    553  O   TYR B  88     -10.289   2.870 -56.491  1.00 90.70           O  
ANISOU  553  O   TYR B  88    12564  10623  11275    405    218     64       O  
ATOM    554  CB  TYR B  88     -12.516   4.210 -54.402  1.00 90.00           C  
ANISOU  554  CB  TYR B  88    12382  10590  11224    435     89    -10       C  
ATOM    555  CG  TYR B  88     -11.987   5.438 -55.150  1.00 87.15           C  
ANISOU  555  CG  TYR B  88    12097  10195  10820    404     61    -25       C  
ATOM    556  CD1 TYR B  88     -10.729   5.951 -54.868  1.00 88.03           C  
ANISOU  556  CD1 TYR B  88    12195  10347  10906    381     93      4       C  
ATOM    557  CD2 TYR B  88     -12.770   6.114 -56.074  1.00 87.51           C  
ANISOU  557  CD2 TYR B  88    12225  10171  10852    398     -1    -68       C  
ATOM    558  CE1 TYR B  88     -10.253   7.057 -55.498  1.00 93.72           C  
ANISOU  558  CE1 TYR B  88    12981  11040  11590    353     68     -8       C  
ATOM    559  CE2 TYR B  88     -12.296   7.232 -56.714  1.00 88.96           C  
ANISOU  559  CE2 TYR B  88    12477  10327  10998    371    -27    -80       C  
ATOM    560  CZ  TYR B  88     -11.031   7.700 -56.425  1.00 92.72           C  
ANISOU  560  CZ  TYR B  88    12937  10843  11450    348      8    -50       C  
ATOM    561  OH  TYR B  88     -10.538   8.824 -57.059  1.00 90.52           O  
ANISOU  561  OH  TYR B  88    12724  10535  11133    320    -16    -61       O  
ATOM    562  N   THR B  89      -9.832   2.547 -54.327  1.00 89.88           N  
ANISOU  562  N   THR B  89    12306  10645  11200    421    259    101       N  
ATOM    563  CA  THR B  89      -8.423   2.350 -54.641  1.00 90.88           C  
ANISOU  563  CA  THR B  89    12439  10787  11304    401    321    143       C  
ATOM    564  C   THR B  89      -8.168   0.998 -55.305  1.00 90.78           C  
ANISOU  564  C   THR B  89    12436  10750  11305    411    378    171       C  
ATOM    565  O   THR B  89      -7.184   0.863 -56.037  1.00 87.40           O  
ANISOU  565  O   THR B  89    12048  10307  10855    393    419    196       O  
ATOM    566  CB  THR B  89      -7.568   2.494 -53.373  1.00 89.50           C  
ANISOU  566  CB  THR B  89    12179  10697  11131    398    355    174       C  
ATOM    567  OG1 THR B  89      -8.261   1.939 -52.247  1.00 88.35           O  
ANISOU  567  OG1 THR B  89    11950  10599  11022    426    353    174       O  
ATOM    568  CG2 THR B  89      -7.240   3.963 -53.099  1.00 91.24           C  
ANISOU  568  CG2 THR B  89    12413  10932  11321    375    314    156       C  
ATOM    569  N   TYR B  90      -9.056   0.016 -55.084  1.00 87.15           N  
ANISOU  569  N   TYR B  90    11944  10286  10883    440    379    167       N  
ATOM    570  CA  TYR B  90      -8.919  -1.332 -55.647  1.00 91.56           C  
ANISOU  570  CA  TYR B  90    12505  10823  11459    452    431    192       C  
ATOM    571  C   TYR B  90      -9.140  -1.345 -57.159  1.00 92.79           C  
ANISOU  571  C   TYR B  90    12764  10895  11598    444    415    173       C  
ATOM    572  O   TYR B  90      -8.332  -1.906 -57.914  1.00 95.35           O  
ANISOU  572  O   TYR B  90    13119  11200  11910    435    464    201       O  
ATOM    573  CB  TYR B  90      -9.923  -2.250 -54.961  1.00 83.36           C  
ANISOU  573  CB  TYR B  90    11405   9802  10466    485    429    187       C  
ATOM    574  CG  TYR B  90      -9.997  -3.688 -55.412  1.00 91.58           C  
ANISOU  574  CG  TYR B  90    12441  10822  11533    503    475    209       C  
ATOM    575  CD1 TYR B  90      -8.867  -4.394 -55.815  1.00 99.47           C  
ANISOU  575  CD1 TYR B  90    13443  11827  12522    494    544    252       C  
ATOM    576  CD2 TYR B  90     -11.217  -4.359 -55.387  1.00 96.24           C  
ANISOU  576  CD2 TYR B  90    13020  11387  12159    529    451    188       C  
ATOM    577  CE1 TYR B  90      -8.960  -5.726 -56.198  1.00106.32           C  
ANISOU  577  CE1 TYR B  90    14304  12678  13416    512    586    271       C  
ATOM    578  CE2 TYR B  90     -11.321  -5.675 -55.762  1.00105.22           C  
ANISOU  578  CE2 TYR B  90    14149  12506  13322    547    492    207       C  
ATOM    579  CZ  TYR B  90     -10.194  -6.357 -56.166  1.00108.22           C  
ANISOU  579  CZ  TYR B  90    14534  12893  13693    538    559    248       C  
ATOM    580  OH  TYR B  90     -10.308  -7.675 -56.538  1.00106.25           O  
ANISOU  580  OH  TYR B  90    14277  12625  13470    555    599    267       O  
ATOM    581  N   ARG B  91     -10.248  -0.757 -57.618  1.00 87.45           N  
ANISOU  581  N   ARG B  91    12139  10168  10921    448    347    126       N  
ATOM    582  CA  ARG B  91     -10.536  -0.661 -59.041  1.00 89.99           C  
ANISOU  582  CA  ARG B  91    12559  10407  11224    441    324    103       C  
ATOM    583  C   ARG B  91      -9.720   0.452 -59.677  1.00 96.11           C  
ANISOU  583  C   ARG B  91    13400  11164  11954    409    314    101       C  
ATOM    584  O   ARG B  91     -10.168   1.074 -60.641  1.00 99.49           O  
ANISOU  584  O   ARG B  91    13910  11529  12361    400    268     68       O  
ATOM    585  CB  ARG B  91     -12.029  -0.429 -59.265  1.00 83.84           C  
ANISOU  585  CB  ARG B  91    11810   9582  10463    457    253     53       C  
ATOM    586  CG  ARG B  91     -12.889  -1.537 -58.720  1.00 79.97           C  
ANISOU  586  CG  ARG B  91    11261   9105  10020    489    261     54       C  
ATOM    587  CD  ARG B  91     -14.138  -1.024 -58.056  1.00 83.55           C  
ANISOU  587  CD  ARG B  91    11688   9562  10493    504    196     13       C  
ATOM    588  NE  ARG B  91     -15.146  -0.634 -59.041  1.00 91.88           N  
ANISOU  588  NE  ARG B  91    12824  10541  11544    506    134    -33       N  
ATOM    589  CZ  ARG B  91     -16.445  -0.904 -58.934  1.00 90.19           C  
ANISOU  589  CZ  ARG B  91    12603  10303  11362    528     91    -65       C  
ATOM    590  NH1 ARG B  91     -16.907  -1.588 -57.896  1.00 89.95           N  
ANISOU  590  NH1 ARG B  91    12488  10319  11370    552    105    -55       N  
ATOM    591  NH2 ARG B  91     -17.280  -0.513 -59.886  1.00 87.28           N  
ANISOU  591  NH2 ARG B  91    12312   9863  10986    529     36   -107       N  
ATOM    592  N   ASP B  92      -8.521   0.693 -59.149  1.00 91.45           N  
ANISOU  592  N   ASP B  92    12773  10628  11347    392    357    136       N  
ATOM    593  CA  ASP B  92      -7.685   1.826 -59.522  1.00 91.11           C  
ANISOU  593  CA  ASP B  92    12776  10579  11262    361    348    137       C  
ATOM    594  C   ASP B  92      -8.525   3.082 -59.727  1.00 89.77           C  
ANISOU  594  C   ASP B  92    12657  10375  11078    353    267     87       C  
ATOM    595  O   ASP B  92      -8.642   3.567 -60.850  1.00 93.01           O  
ANISOU  595  O   ASP B  92    13155  10721  11463    340    240     66       O  
ATOM    596  CB  ASP B  92      -6.871   1.510 -60.779  1.00 99.48           C  
ANISOU  596  CB  ASP B  92    13908  11594  12297    345    388    157       C  
ATOM    597  CG  ASP B  92      -5.567   2.293 -60.835  1.00 98.97           C  
ANISOU  597  CG  ASP B  92    13857  11552  12197    315    413    181       C  
ATOM    598  OD1 ASP B  92      -4.728   2.085 -59.934  1.00 95.20           O  
ANISOU  598  OD1 ASP B  92    13308  11141  11725    312    459    215       O  
ATOM    599  OD2 ASP B  92      -5.395   3.139 -61.743  1.00 92.09           O  
ANISOU  599  OD2 ASP B  92    13065  10633  11292    294    387    164       O  
ATOM    600  N   TYR B  93      -9.140   3.588 -58.662  1.00 92.95           N  
ANISOU  600  N   TYR B  93    13005  10817  11497    362    228     68       N  
ATOM    601  CA  TYR B  93      -9.893   4.843 -58.673  1.00 90.71           C  
ANISOU  601  CA  TYR B  93    12757  10510  11200    355    151     22       C  
ATOM    602  C   TYR B  93     -11.160   4.707 -59.554  1.00 97.98           C  
ANISOU  602  C   TYR B  93    13741  11356  12129    369    100    -20       C  
ATOM    603  O   TYR B  93     -11.241   5.213 -60.664  1.00103.83           O  
ANISOU  603  O   TYR B  93    14571  12036  12846    355     73    -40       O  
ATOM    604  CB  TYR B  93      -8.994   6.011 -59.111  1.00 97.44           C  
ANISOU  604  CB  TYR B  93    13660  11353  12009    322    143     24       C  
ATOM    605  CG  TYR B  93      -7.706   6.163 -58.297  1.00 98.28           C  
ANISOU  605  CG  TYR B  93    13707  11529  12106    307    194     64       C  
ATOM    606  CD1 TYR B  93      -6.551   5.456 -58.633  1.00102.03           C  
ANISOU  606  CD1 TYR B  93    14178  12015  12572    298    266    109       C  
ATOM    607  CD2 TYR B  93      -7.630   7.061 -57.241  1.00 99.38           C  
ANISOU  607  CD2 TYR B  93    13796  11721  12243    301    167     57       C  
ATOM    608  CE1 TYR B  93      -5.382   5.599 -57.905  1.00108.92           C  
ANISOU  608  CE1 TYR B  93    14997  12951  13436    284    311    145       C  
ATOM    609  CE2 TYR B  93      -6.467   7.213 -56.508  1.00 95.60           C  
ANISOU  609  CE2 TYR B  93    13263  11305  11756    288    211     92       C  
ATOM    610  CZ  TYR B  93      -5.344   6.480 -56.847  1.00107.29           C  
ANISOU  610  CZ  TYR B  93    14741  12796  13229    279    283    137       C  
ATOM    611  OH  TYR B  93      -4.180   6.628 -56.123  1.00107.49           O  
ANISOU  611  OH  TYR B  93    14712  12883  13246    266    327    172       O  
ATOM    612  N   ASP B  94     -12.141   4.013 -58.979  1.00 97.25           N  
ANISOU  612  N   ASP B  94    13600  11276  12076    397     88    -31       N  
ATOM    613  CA  ASP B  94     -13.499   3.906 -59.525  1.00 94.72           C  
ANISOU  613  CA  ASP B  94    13321  10896  11772    414     33    -74       C  
ATOM    614  C   ASP B  94     -14.510   3.971 -58.387  1.00 94.18           C  
ANISOU  614  C   ASP B  94    13184  10865  11736    436     -4    -96       C  
ATOM    615  O   ASP B  94     -14.598   3.036 -57.588  1.00 92.23           O  
ANISOU  615  O   ASP B  94    12860  10661  11521    456     31    -74       O  
ATOM    616  CB  ASP B  94     -13.694   2.598 -60.289  1.00 93.17           C  
ANISOU  616  CB  ASP B  94    13145  10660  11594    431     69    -62       C  
ATOM    617  CG  ASP B  94     -14.463   2.780 -61.584  1.00100.05           C  
ANISOU  617  CG  ASP B  94    14113  11445  12455    431     23    -99       C  
ATOM    618  OD1 ASP B  94     -15.637   3.212 -61.536  1.00109.84           O  
ANISOU  618  OD1 ASP B  94    15367  12660  13708    442    -42   -142       O  
ATOM    619  OD2 ASP B  94     -13.897   2.469 -62.645  1.00 97.46           O  
ANISOU  619  OD2 ASP B  94    13846  11077  12108    421     51    -85       O  
ATOM    620  N   TRP B  95     -15.295   5.051 -58.333  1.00 96.11           N  
ANISOU  620  N   TRP B  95    13455  11089  11972    433    -76   -140       N  
ATOM    621  CA  TRP B  95     -16.225   5.308 -57.232  1.00 99.13           C  
ANISOU  621  CA  TRP B  95    13775  11509  12382    451   -117   -163       C  
ATOM    622  C   TRP B  95     -17.665   5.063 -57.674  1.00100.42           C  
ANISOU  622  C   TRP B  95    13969  11616  12568    472   -169   -205       C  
ATOM    623  O   TRP B  95     -18.323   5.981 -58.189  1.00 98.51           O  
ANISOU  623  O   TRP B  95    13788  11328  12312    465   -234   -247       O  
ATOM    624  CB  TRP B  95     -16.066   6.741 -56.712  1.00 98.10           C  
ANISOU  624  CB  TRP B  95    13644  11403  12227    432   -161   -182       C  
ATOM    625  CG  TRP B  95     -16.932   7.024 -55.529  1.00 94.63           C  
ANISOU  625  CG  TRP B  95    13136  11005  11812    450   -200   -204       C  
ATOM    626  CD1 TRP B  95     -18.169   7.590 -55.546  1.00 97.96           C  
ANISOU  626  CD1 TRP B  95    13580  11396  12243    460   -271   -253       C  
ATOM    627  CD2 TRP B  95     -16.616   6.798 -54.158  1.00 94.11           C  
ANISOU  627  CD2 TRP B  95    12972  11021  11764    460   -171   -180       C  
ATOM    628  NE1 TRP B  95     -18.661   7.705 -54.277  1.00100.77           N  
ANISOU  628  NE1 TRP B  95    13856  11809  12622    477   -287   -259       N  
ATOM    629  CE2 TRP B  95     -17.725   7.231 -53.399  1.00 97.31           C  
ANISOU  629  CE2 TRP B  95    13343  11440  12189    477   -227   -215       C  
ATOM    630  CE3 TRP B  95     -15.511   6.259 -53.491  1.00 96.20           C  
ANISOU  630  CE3 TRP B  95    13173  11348  12029    458   -102   -131       C  
ATOM    631  CZ2 TRP B  95     -17.765   7.145 -51.994  1.00 99.81           C  
ANISOU  631  CZ2 TRP B  95    13565  11833  12527    491   -216   -203       C  
ATOM    632  CZ3 TRP B  95     -15.549   6.171 -52.085  1.00 91.77           C  
ANISOU  632  CZ3 TRP B  95    12517  10862  11489    472    -92   -119       C  
ATOM    633  CH2 TRP B  95     -16.671   6.618 -51.358  1.00 94.46           C  
ANISOU  633  CH2 TRP B  95    12826  11215  11848    489   -149   -155       C  
ATOM    634  N   PRO B  96     -18.225   3.858 -57.455  1.00 93.60           N  
ANISOU  634  N   PRO B  96    13063  10756  11743    498   -146   -196       N  
ATOM    635  CA  PRO B  96     -19.582   3.577 -57.944  1.00 95.64           C  
ANISOU  635  CA  PRO B  96    13355  10959  12027    518   -194   -236       C  
ATOM    636  C   PRO B  96     -20.676   3.904 -56.944  1.00 97.79           C  
ANISOU  636  C   PRO B  96    13572  11257  12325    536   -243   -266       C  
ATOM    637  O   PRO B  96     -21.747   3.287 -56.969  1.00 96.08           O  
ANISOU  637  O   PRO B  96    13346  11017  12143    560   -264   -286       O  
ATOM    638  CB  PRO B  96     -19.536   2.075 -58.218  1.00 96.99           C  
ANISOU  638  CB  PRO B  96    13505  11120  12225    536   -139   -208       C  
ATOM    639  CG  PRO B  96     -18.605   1.568 -57.171  1.00 94.31           C  
ANISOU  639  CG  PRO B  96    13079  10860  11894    537    -74   -160       C  
ATOM    640  CD  PRO B  96     -17.594   2.656 -56.888  1.00 94.85           C  
ANISOU  640  CD  PRO B  96    13151  10964  11925    510    -72   -149       C  
ATOM    641  N   PHE B  97     -20.429   4.875 -56.068  1.00104.73           N  
ANISOU  641  N   PHE B  97    14415  12185  13191    526   -263   -270       N  
ATOM    642  CA  PHE B  97     -21.340   5.175 -54.969  1.00100.57           C  
ANISOU  642  CA  PHE B  97    13826  11696  12689    544   -303   -293       C  
ATOM    643  C   PHE B  97     -21.964   6.559 -55.080  1.00100.44           C  
ANISOU  643  C   PHE B  97    13855  11654  12654    533   -382   -341       C  
ATOM    644  O   PHE B  97     -22.463   7.094 -54.085  1.00 98.45           O  
ANISOU  644  O   PHE B  97    13551  11442  12412    542   -415   -358       O  
ATOM    645  CB  PHE B  97     -20.623   5.041 -53.626  1.00100.32           C  
ANISOU  645  CB  PHE B  97    13699  11753  12665    547   -260   -257       C  
ATOM    646  CG  PHE B  97     -20.003   3.696 -53.395  1.00105.94           C  
ANISOU  646  CG  PHE B  97    14359  12496  13397    558   -183   -209       C  
ATOM    647  CD1 PHE B  97     -20.780   2.632 -52.962  1.00100.76           C  
ANISOU  647  CD1 PHE B  97    13651  11850  12785    587   -170   -206       C  
ATOM    648  CD2 PHE B  97     -18.643   3.496 -53.599  1.00104.13           C  
ANISOU  648  CD2 PHE B  97    14132  12288  13145    539   -123   -167       C  
ATOM    649  CE1 PHE B  97     -20.214   1.399 -52.731  1.00 97.48           C  
ANISOU  649  CE1 PHE B  97    13186  11463  12388    597   -100   -162       C  
ATOM    650  CE2 PHE B  97     -18.067   2.257 -53.370  1.00 93.98           C  
ANISOU  650  CE2 PHE B  97    12797  11031  11878    550    -52   -123       C  
ATOM    651  CZ  PHE B  97     -18.854   1.209 -52.935  1.00 91.91           C  
ANISOU  651  CZ  PHE B  97    12484  10778  11659    579    -41   -120       C  
ATOM    652  N   GLY B  98     -21.939   7.159 -56.258  1.00 98.92           N  
ANISOU  652  N   GLY B  98    13756  11396  12432    516   -412   -362       N  
ATOM    653  CA  GLY B  98     -22.559   8.459 -56.410  1.00108.14           C  
ANISOU  653  CA  GLY B  98    14970  12537  13582    506   -487   -408       C  
ATOM    654  C   GLY B  98     -21.863   9.602 -55.699  1.00 98.54           C  
ANISOU  654  C   GLY B  98    13731  11370  12339    486   -498   -405       C  
ATOM    655  O   GLY B  98     -20.975   9.390 -54.866  1.00101.21           O  
ANISOU  655  O   GLY B  98    14004  11773  12677    483   -448   -367       O  
ATOM    656  N   THR B  99     -22.284  10.827 -56.023  1.00 95.45           N  
ANISOU  656  N   THR B  99    13394  10946  11926    473   -564   -445       N  
ATOM    657  CA  THR B  99     -21.615  12.022 -55.513  1.00112.03           C  
ANISOU  657  CA  THR B  99    15487  13083  13997    451   -579   -445       C  
ATOM    658  C   THR B  99     -21.783  12.168 -54.001  1.00107.35           C  
ANISOU  658  C   THR B  99    14797  12568  13425    464   -582   -441       C  
ATOM    659  O   THR B  99     -20.829  12.521 -53.292  1.00101.90           O  
ANISOU  659  O   THR B  99    14063  11935  12720    452   -553   -415       O  
ATOM    660  CB  THR B  99     -22.164  13.251 -56.233  1.00114.10           C  
ANISOU  660  CB  THR B  99    15830  13287  14234    437   -653   -491       C  
ATOM    661  OG1 THR B  99     -21.711  13.233 -57.590  1.00 99.24           O  
ANISOU  661  OG1 THR B  99    14038  11343  12327    419   -643   -487       O  
ATOM    662  CG2 THR B  99     -21.695  14.539 -55.564  1.00109.74           C  
ANISOU  662  CG2 THR B  99    15262  12775  13658    418   -680   -498       C  
ATOM    663  N   PHE B 100     -22.991  11.901 -53.496  1.00108.54           N  
ANISOU  663  N   PHE B 100    14912  12720  13608    490   -617   -468       N  
ATOM    664  CA  PHE B 100     -23.285  12.054 -52.074  1.00107.09           C  
ANISOU  664  CA  PHE B 100    14638  12606  13444    506   -625   -469       C  
ATOM    665  C   PHE B 100     -22.231  11.392 -51.200  1.00106.91           C  
ANISOU  665  C   PHE B 100    14537  12658  13428    507   -551   -417       C  
ATOM    666  O   PHE B 100     -21.571  12.054 -50.391  1.00100.90           O  
ANISOU  666  O   PHE B 100    13734  11951  12650    496   -546   -406       O  
ATOM    667  CB  PHE B 100     -24.671  11.482 -51.772  1.00108.17           C  
ANISOU  667  CB  PHE B 100    14747  12731  13622    536   -655   -496       C  
ATOM    668  CG  PHE B 100     -25.034  11.525 -50.330  1.00104.38           C  
ANISOU  668  CG  PHE B 100    14172  12321  13164    555   -661   -496       C  
ATOM    669  CD1 PHE B 100     -24.819  12.671 -49.579  1.00106.12           C  
ANISOU  669  CD1 PHE B 100    14372  12584  13367    544   -692   -509       C  
ATOM    670  CD2 PHE B 100     -25.599  10.421 -49.723  1.00104.05           C  
ANISOU  670  CD2 PHE B 100    14065  12305  13163    583   -635   -484       C  
ATOM    671  CE1 PHE B 100     -25.145  12.710 -48.232  1.00 99.10           C  
ANISOU  671  CE1 PHE B 100    13394  11760  12497    562   -697   -509       C  
ATOM    672  CE2 PHE B 100     -25.931  10.443 -48.378  1.00112.65           C  
ANISOU  672  CE2 PHE B 100    15067  13461  14273    601   -638   -483       C  
ATOM    673  CZ  PHE B 100     -25.708  11.593 -47.627  1.00104.59           C  
ANISOU  673  CZ  PHE B 100    14024  12482  13232    591   -670   -495       C  
ATOM    674  N   PHE B 101     -22.062  10.079 -51.339  1.00101.73           N  
ANISOU  674  N   PHE B 101    13856  12003  12792    521   -495   -385       N  
ATOM    675  CA  PHE B 101     -21.113   9.386 -50.480  1.00100.16           C  
ANISOU  675  CA  PHE B 101    13580  11876  12602    524   -425   -336       C  
ATOM    676  C   PHE B 101     -19.710   9.924 -50.690  1.00100.05           C  
ANISOU  676  C   PHE B 101    13587  11879  12550    495   -392   -308       C  
ATOM    677  O   PHE B 101     -19.011  10.274 -49.731  1.00103.13           O  
ANISOU  677  O   PHE B 101    13918  12335  12933    489   -373   -288       O  
ATOM    678  CB  PHE B 101     -21.156   7.884 -50.733  1.00101.60           C  
ANISOU  678  CB  PHE B 101    13741  12049  12812    542   -370   -307       C  
ATOM    679  CG  PHE B 101     -22.405   7.224 -50.234  1.00109.60           C  
ANISOU  679  CG  PHE B 101    14710  13064  13868    574   -389   -326       C  
ATOM    680  CD1 PHE B 101     -23.470   7.984 -49.768  1.00103.77           C  
ANISOU  680  CD1 PHE B 101    13964  12324  13138    584   -457   -369       C  
ATOM    681  CD2 PHE B 101     -22.536   5.845 -50.285  1.00106.93           C  
ANISOU  681  CD2 PHE B 101    14342  12726  13561    593   -342   -300       C  
ATOM    682  CE1 PHE B 101     -24.620   7.388 -49.338  1.00 97.19           C  
ANISOU  682  CE1 PHE B 101    13091  11491  12344    612   -475   -386       C  
ATOM    683  CE2 PHE B 101     -23.691   5.240 -49.859  1.00104.49           C  
ANISOU  683  CE2 PHE B 101    13994  12416  13292    622   -360   -317       C  
ATOM    684  CZ  PHE B 101     -24.736   6.017 -49.383  1.00106.04           C  
ANISOU  684  CZ  PHE B 101    14182  12612  13497    631   -427   -360       C  
ATOM    685  N   CYS B 102     -19.302  10.042 -51.958  1.00100.35           N  
ANISOU  685  N   CYS B 102    13710  11856  12564    475   -388   -308       N  
ATOM    686  CA  CYS B 102     -18.002  10.625 -52.252  1.00 96.11           C  
ANISOU  686  CA  CYS B 102    13199  11328  11989    445   -361   -284       C  
ATOM    687  C   CYS B 102     -17.836  11.985 -51.577  1.00 97.31           C  
ANISOU  687  C   CYS B 102    13339  11514  12121    431   -404   -303       C  
ATOM    688  O   CYS B 102     -16.758  12.292 -51.060  1.00100.71           O  
ANISOU  688  O   CYS B 102    13737  11994  12535    416   -371   -274       O  
ATOM    689  CB  CYS B 102     -17.807  10.718 -53.759  1.00 92.30           C  
ANISOU  689  CB  CYS B 102    12819  10769  11483    428   -366   -291       C  
ATOM    690  SG  CYS B 102     -16.659  11.987 -54.308  1.00107.70           S  
ANISOU  690  SG  CYS B 102    14830  12708  13383    389   -371   -287       S  
ATOM    691  N   LYS B 103     -18.894  12.802 -51.536  1.00 94.55           N  
ANISOU  691  N   LYS B 103    13011  11139  11773    436   -477   -351       N  
ATOM    692  CA  LYS B 103     -18.854  13.996 -50.688  1.00100.17           C  
ANISOU  692  CA  LYS B 103    13695  11891  12472    428   -518   -369       C  
ATOM    693  C   LYS B 103     -18.758  13.602 -49.217  1.00 93.45           C  
ANISOU  693  C   LYS B 103    12737  11124  11644    447   -491   -348       C  
ATOM    694  O   LYS B 103     -17.786  13.927 -48.522  1.00 88.29           O  
ANISOU  694  O   LYS B 103    12040  10528  10977    435   -462   -322       O  
ATOM    695  CB  LYS B 103     -20.094  14.879 -50.917  1.00100.78           C  
ANISOU  695  CB  LYS B 103    13817  11926  12551    432   -603   -426       C  
ATOM    696  CG  LYS B 103     -20.236  15.522 -52.291  1.00 97.27           C  
ANISOU  696  CG  LYS B 103    13480  11399  12080    412   -641   -453       C  
ATOM    697  CD  LYS B 103     -21.618  16.159 -52.486  1.00 93.52           C  
ANISOU  697  CD  LYS B 103    13040  10881  11613    423   -722   -508       C  
ATOM    698  CE  LYS B 103     -21.563  17.658 -52.289  1.00 90.97           C  
ANISOU  698  CE  LYS B 103    12740  10561  11264    404   -778   -537       C  
ATOM    699  NZ  LYS B 103     -20.555  18.306 -53.182  1.00 90.06           N  
ANISOU  699  NZ  LYS B 103    12695  10414  11109    371   -769   -525       N  
ATOM    700  N   LEU B 104     -19.768  12.885 -48.735  1.00 93.19           N  
ANISOU  700  N   LEU B 104    12660  11100  11647    476   -499   -359       N  
ATOM    701  CA  LEU B 104     -19.864  12.601 -47.315  1.00 92.57           C  
ANISOU  701  CA  LEU B 104    12481  11099  11591    496   -483   -346       C  
ATOM    702  C   LEU B 104     -18.681  11.771 -46.838  1.00 89.04           C  
ANISOU  702  C   LEU B 104    11977  10708  11146    495   -402   -290       C  
ATOM    703  O   LEU B 104     -18.005  12.132 -45.864  1.00 86.45           O  
ANISOU  703  O   LEU B 104    11591  10445  10811    491   -385   -272       O  
ATOM    704  CB  LEU B 104     -21.181  11.883 -47.027  1.00 99.06           C  
ANISOU  704  CB  LEU B 104    13273  11912  12452    528   -503   -366       C  
ATOM    705  CG  LEU B 104     -21.362  11.334 -45.608  1.00 91.80           C  
ANISOU  705  CG  LEU B 104    12249  11070  11562    553   -479   -348       C  
ATOM    706  CD1 LEU B 104     -22.802  11.498 -45.190  1.00 90.55           C  
ANISOU  706  CD1 LEU B 104    12072  10902  11429    577   -538   -390       C  
ATOM    707  CD2 LEU B 104     -20.972   9.863 -45.542  1.00 81.90           C  
ANISOU  707  CD2 LEU B 104    10952   9834  10331    567   -406   -303       C  
ATOM    708  N   SER B 105     -18.440  10.633 -47.496  1.00 89.97           N  
ANISOU  708  N   SER B 105    12110  10800  11275    499   -352   -263       N  
ATOM    709  CA  SER B 105     -17.322   9.784 -47.111  1.00 89.77           C  
ANISOU  709  CA  SER B 105    12033  10824  11252    499   -273   -209       C  
ATOM    710  C   SER B 105     -16.040  10.589 -47.041  1.00 89.61           C  
ANISOU  710  C   SER B 105    12020  10830  11196    470   -255   -190       C  
ATOM    711  O   SER B 105     -15.266  10.450 -46.094  1.00 88.12           O  
ANISOU  711  O   SER B 105    11763  10711  11009    471   -216   -158       O  
ATOM    712  CB  SER B 105     -17.164   8.623 -48.092  1.00 92.12           C  
ANISOU  712  CB  SER B 105    12366  11076  11559    501   -227   -187       C  
ATOM    713  OG  SER B 105     -15.857   8.090 -48.013  1.00 92.52           O  
ANISOU  713  OG  SER B 105    12391  11162  11599    491   -156   -138       O  
ATOM    714  N   SER B 106     -15.804  11.450 -48.030  1.00 88.28           N  
ANISOU  714  N   SER B 106    11937  10609  10997    445   -285   -209       N  
ATOM    715  CA  SER B 106     -14.629  12.306 -47.967  1.00 86.80           C  
ANISOU  715  CA  SER B 106    11758  10444  10776    417   -273   -193       C  
ATOM    716  C   SER B 106     -14.698  13.207 -46.759  1.00 82.98           C  
ANISOU  716  C   SER B 106    11217  10020  10291    419   -306   -207       C  
ATOM    717  O   SER B 106     -13.731  13.320 -45.999  1.00 80.12           O  
ANISOU  717  O   SER B 106    10802   9719   9921    412   -271   -177       O  
ATOM    718  CB  SER B 106     -14.508  13.146 -49.230  1.00 95.96           C  
ANISOU  718  CB  SER B 106    13021  11535  11906    390   -308   -215       C  
ATOM    719  OG  SER B 106     -14.606  12.336 -50.387  1.00 95.50           O  
ANISOU  719  OG  SER B 106    13021  11416  11850    391   -285   -208       O  
ATOM    720  N   TYR B 107     -15.852  13.844 -46.564  1.00 86.18           N  
ANISOU  720  N   TYR B 107    11631  10408  10704    429   -375   -252       N  
ATOM    721  CA  TYR B 107     -16.026  14.801 -45.478  1.00 86.44           C  
ANISOU  721  CA  TYR B 107    11617  10492  10734    432   -415   -272       C  
ATOM    722  C   TYR B 107     -15.606  14.231 -44.132  1.00 85.50           C  
ANISOU  722  C   TYR B 107    11394  10459  10634    449   -370   -239       C  
ATOM    723  O   TYR B 107     -15.197  14.985 -43.239  1.00 87.32           O  
ANISOU  723  O   TYR B 107    11581  10742  10853    444   -381   -239       O  
ATOM    724  CB  TYR B 107     -17.485  15.244 -45.426  1.00 90.23           C  
ANISOU  724  CB  TYR B 107    12112  10942  11229    448   -488   -323       C  
ATOM    725  CG  TYR B 107     -17.811  16.156 -44.272  1.00 87.29           C  
ANISOU  725  CG  TYR B 107    11688  10622  10858    454   -532   -346       C  
ATOM    726  CD1 TYR B 107     -17.362  17.465 -44.255  1.00 89.76           C  
ANISOU  726  CD1 TYR B 107    12028  10937  11141    431   -568   -362       C  
ATOM    727  CD2 TYR B 107     -18.563  15.702 -43.200  1.00 86.28           C  
ANISOU  727  CD2 TYR B 107    11483  10540  10759    484   -536   -351       C  
ATOM    728  CE1 TYR B 107     -17.662  18.310 -43.216  1.00 89.48           C  
ANISOU  728  CE1 TYR B 107    11946  10947  11105    437   -609   -384       C  
ATOM    729  CE2 TYR B 107     -18.867  16.530 -42.153  1.00 87.60           C  
ANISOU  729  CE2 TYR B 107    11604  10755  10927    491   -576   -372       C  
ATOM    730  CZ  TYR B 107     -18.411  17.839 -42.160  1.00 90.74           C  
ANISOU  730  CZ  TYR B 107    12030  11154  11295    468   -613   -389       C  
ATOM    731  OH  TYR B 107     -18.710  18.685 -41.111  1.00 87.08           O  
ANISOU  731  OH  TYR B 107    11520  10737  10831    475   -654   -411       O  
ATOM    732  N   LEU B 108     -15.684  12.906 -43.980  1.00 81.76           N  
ANISOU  732  N   LEU B 108    10879   9999  10186    469   -319   -211       N  
ATOM    733  CA  LEU B 108     -15.378  12.226 -42.730  1.00 79.31           C  
ANISOU  733  CA  LEU B 108    10470   9767   9895    489   -274   -179       C  
ATOM    734  C   LEU B 108     -13.909  11.848 -42.590  1.00 76.48           C  
ANISOU  734  C   LEU B 108    10086   9450   9524    475   -204   -128       C  
ATOM    735  O   LEU B 108     -13.460  11.603 -41.471  1.00 73.94           O  
ANISOU  735  O   LEU B 108     9684   9200   9211    486   -172   -103       O  
ATOM    736  CB  LEU B 108     -16.259  10.988 -42.617  1.00 75.90           C  
ANISOU  736  CB  LEU B 108    10007   9330   9501    519   -257   -174       C  
ATOM    737  CG  LEU B 108     -17.668  11.445 -42.265  1.00 75.38           C  
ANISOU  737  CG  LEU B 108     9937   9253   9453    538   -326   -222       C  
ATOM    738  CD1 LEU B 108     -18.669  10.432 -42.698  1.00 76.23           C  
ANISOU  738  CD1 LEU B 108    10052   9320   9591    560   -324   -230       C  
ATOM    739  CD2 LEU B 108     -17.769  11.657 -40.774  1.00 74.74           C  
ANISOU  739  CD2 LEU B 108     9764   9251   9383    556   -330   -219       C  
ATOM    740  N   ILE B 109     -13.149  11.797 -43.689  1.00 84.03           N  
ANISOU  740  N   ILE B 109    11107  10361  10459    451   -178   -113       N  
ATOM    741  CA  ILE B 109     -11.687  11.708 -43.590  1.00 86.15           C  
ANISOU  741  CA  ILE B 109    11358  10665  10709    432   -120    -70       C  
ATOM    742  C   ILE B 109     -11.145  12.873 -42.763  1.00 81.50           C  
ANISOU  742  C   ILE B 109    10740  10127  10101    419   -143    -76       C  
ATOM    743  O   ILE B 109     -10.385  12.682 -41.797  1.00 79.03           O  
ANISOU  743  O   ILE B 109    10355   9883   9790    423   -104    -45       O  
ATOM    744  CB  ILE B 109     -11.047  11.647 -45.002  1.00 83.70           C  
ANISOU  744  CB  ILE B 109    11135  10292  10377    407    -98    -59       C  
ATOM    745  CG1 ILE B 109     -11.048  10.230 -45.561  1.00 81.35           C  
ANISOU  745  CG1 ILE B 109    10840   9971  10098    420    -45    -31       C  
ATOM    746  CG2 ILE B 109      -9.604  12.136 -45.027  1.00 79.32           C  
ANISOU  746  CG2 ILE B 109    10583   9763   9794    379    -63    -29       C  
ATOM    747  CD1 ILE B 109     -12.364   9.769 -46.009  1.00 85.63           C  
ANISOU  747  CD1 ILE B 109    11409  10465  10663    440    -78    -61       C  
ATOM    748  N   PHE B 110     -11.575  14.095 -43.106  1.00 82.04           N  
ANISOU  748  N   PHE B 110    10861  10159  10150    405   -209   -117       N  
ATOM    749  CA  PHE B 110     -11.027  15.311 -42.514  1.00 81.95           C  
ANISOU  749  CA  PHE B 110    10835  10184  10117    388   -236   -126       C  
ATOM    750  C   PHE B 110     -11.652  15.633 -41.158  1.00 79.62           C  
ANISOU  750  C   PHE B 110    10464   9949   9838    410   -268   -144       C  
ATOM    751  O   PHE B 110     -10.958  16.134 -40.260  1.00 78.80           O  
ANISOU  751  O   PHE B 110    10310   9906   9726    405   -260   -132       O  
ATOM    752  CB  PHE B 110     -11.203  16.464 -43.497  1.00 87.34           C  
ANISOU  752  CB  PHE B 110    11610  10803  10774    363   -292   -162       C  
ATOM    753  CG  PHE B 110     -10.140  16.508 -44.563  1.00 91.68           C  
ANISOU  753  CG  PHE B 110    12222  11315  11298    333   -257   -138       C  
ATOM    754  CD1 PHE B 110      -8.918  17.118 -44.316  1.00 86.99           C  
ANISOU  754  CD1 PHE B 110    11616  10753  10681    310   -235   -116       C  
ATOM    755  CD2 PHE B 110     -10.346  15.920 -45.795  1.00 92.69           C  
ANISOU  755  CD2 PHE B 110    12419  11376  11425    329   -245   -137       C  
ATOM    756  CE1 PHE B 110      -7.932  17.165 -45.277  1.00 86.11           C  
ANISOU  756  CE1 PHE B 110    11561  10609  10547    283   -202    -93       C  
ATOM    757  CE2 PHE B 110      -9.354  15.960 -46.766  1.00 99.48           C  
ANISOU  757  CE2 PHE B 110    13335  12202  12260    303   -211   -114       C  
ATOM    758  CZ  PHE B 110      -8.149  16.586 -46.505  1.00 94.04           C  
ANISOU  758  CZ  PHE B 110    12635  11547  11549    280   -190    -92       C  
ATOM    759  N   VAL B 111     -12.952  15.361 -40.998  1.00 81.81           N  
ANISOU  759  N   VAL B 111    10734  10212  10139    435   -304   -173       N  
ATOM    760  CA  VAL B 111     -13.587  15.415 -39.679  1.00 80.53           C  
ANISOU  760  CA  VAL B 111    10492  10109   9996    461   -325   -184       C  
ATOM    761  C   VAL B 111     -12.739  14.664 -38.661  1.00 79.56           C  
ANISOU  761  C   VAL B 111    10282  10065   9884    472   -259   -138       C  
ATOM    762  O   VAL B 111     -12.249  15.242 -37.686  1.00 79.87           O  
ANISOU  762  O   VAL B 111    10269  10164   9915    471   -262   -133       O  
ATOM    763  CB  VAL B 111     -15.019  14.850 -39.741  1.00 78.59           C  
ANISOU  763  CB  VAL B 111    10246   9835   9780    488   -354   -211       C  
ATOM    764  CG1 VAL B 111     -15.484  14.326 -38.380  1.00 78.18           C  
ANISOU  764  CG1 VAL B 111    10097   9853   9756    520   -344   -203       C  
ATOM    765  CG2 VAL B 111     -15.981  15.901 -40.251  1.00 81.09           C  
ANISOU  765  CG2 VAL B 111    10625  10098  10088    482   -435   -265       C  
ATOM    766  N   ASN B 112     -12.537  13.363 -38.897  1.00 86.96           N  
ANISOU  766  N   ASN B 112    11203  11001  10839    483   -200   -103       N  
ATOM    767  CA  ASN B 112     -11.708  12.553 -38.012  1.00 83.29           C  
ANISOU  767  CA  ASN B 112    10657  10605  10383    494   -133    -56       C  
ATOM    768  C   ASN B 112     -10.346  13.189 -37.782  1.00 81.98           C  
ANISOU  768  C   ASN B 112    10483  10476  10191    469   -109    -33       C  
ATOM    769  O   ASN B 112      -9.839  13.195 -36.653  1.00 82.00           O  
ANISOU  769  O   ASN B 112    10411  10551  10196    478    -88    -14       O  
ATOM    770  CB  ASN B 112     -11.541  11.147 -38.592  1.00 86.52           C  
ANISOU  770  CB  ASN B 112    11071  10994  10811    502    -72    -22       C  
ATOM    771  CG  ASN B 112     -10.332  10.412 -38.017  1.00 85.26           C  
ANISOU  771  CG  ASN B 112    10850  10894  10652    502      4     31       C  
ATOM    772  OD1 ASN B 112      -9.216  10.517 -38.530  1.00 87.13           O  
ANISOU  772  OD1 ASN B 112    11114  11124  10867    478     38     55       O  
ATOM    773  ND2 ASN B 112     -10.549   9.689 -36.931  1.00 83.99           N  
ANISOU  773  ND2 ASN B 112    10605  10793  10516    530     29     49       N  
ATOM    774  N   MET B 113      -9.741  13.739 -38.833  1.00 79.21           N  
ANISOU  774  N   MET B 113    10207  10075   9813    439   -113    -36       N  
ATOM    775  CA  MET B 113      -8.374  14.216 -38.696  1.00 79.11           C  
ANISOU  775  CA  MET B 113    10188  10095   9777    415    -83     -9       C  
ATOM    776  C   MET B 113      -8.295  15.449 -37.809  1.00 76.96           C  
ANISOU  776  C   MET B 113     9886   9864   9492    410   -128    -31       C  
ATOM    777  O   MET B 113      -7.342  15.600 -37.035  1.00 75.76           O  
ANISOU  777  O   MET B 113     9681   9773   9332    405    -98     -6       O  
ATOM    778  CB  MET B 113      -7.793  14.508 -40.061  1.00 80.09           C  
ANISOU  778  CB  MET B 113    10401  10152   9877    384    -77     -7       C  
ATOM    779  CG  MET B 113      -6.737  15.552 -40.019  1.00 78.44           C  
ANISOU  779  CG  MET B 113    10205   9960   9639    355    -81     -2       C  
ATOM    780  SD  MET B 113      -6.643  16.155 -41.669  1.00 81.04           S  
ANISOU  780  SD  MET B 113    10654  10196   9943    323   -105    -20       S  
ATOM    781  CE  MET B 113      -5.634  17.607 -41.437  1.00 82.60           C  
ANISOU  781  CE  MET B 113    10860  10415  10109    292   -127    -24       C  
ATOM    782  N   TYR B 114      -9.279  16.345 -37.908  1.00 80.72           N  
ANISOU  782  N   TYR B 114    10395  10310   9964    411   -201    -79       N  
ATOM    783  CA  TYR B 114      -9.315  17.481 -36.989  1.00 77.29           C  
ANISOU  783  CA  TYR B 114     9928   9918   9520    410   -247   -103       C  
ATOM    784  C   TYR B 114      -9.676  17.034 -35.577  1.00 76.84           C  
ANISOU  784  C   TYR B 114     9774   9937   9486    442   -238    -96       C  
ATOM    785  O   TYR B 114      -9.069  17.490 -34.602  1.00 76.86           O  
ANISOU  785  O   TYR B 114     9721  10002   9482    442   -233    -86       O  
ATOM    786  CB  TYR B 114     -10.309  18.535 -37.473  1.00 77.20           C  
ANISOU  786  CB  TYR B 114     9978   9854   9501    403   -328   -157       C  
ATOM    787  CG  TYR B 114      -9.942  19.128 -38.789  1.00 77.82           C  
ANISOU  787  CG  TYR B 114    10152   9862   9555    371   -342   -166       C  
ATOM    788  CD1 TYR B 114      -8.617  19.348 -39.112  1.00 77.71           C  
ANISOU  788  CD1 TYR B 114    10154   9855   9519    344   -304   -136       C  
ATOM    789  CD2 TYR B 114     -10.915  19.441 -39.725  1.00 80.39           C  
ANISOU  789  CD2 TYR B 114    10551  10115   9879    368   -393   -204       C  
ATOM    790  CE1 TYR B 114      -8.265  19.884 -40.331  1.00 78.04           C  
ANISOU  790  CE1 TYR B 114    10283   9832   9538    315   -315   -144       C  
ATOM    791  CE2 TYR B 114     -10.577  19.973 -40.941  1.00 80.79           C  
ANISOU  791  CE2 TYR B 114    10689  10101   9905    340   -406   -212       C  
ATOM    792  CZ  TYR B 114      -9.244  20.192 -41.245  1.00 79.27           C  
ANISOU  792  CZ  TYR B 114    10512   9916   9691    313   -366   -181       C  
ATOM    793  OH  TYR B 114      -8.884  20.716 -42.475  1.00 79.40           O  
ANISOU  793  OH  TYR B 114    10617   9868   9684    284   -377   -187       O  
ATOM    794  N   ALA B 115     -10.668  16.152 -35.449  1.00 77.58           N  
ANISOU  794  N   ALA B 115     9847  10024   9608    469   -236   -101       N  
ATOM    795  CA  ALA B 115     -11.034  15.650 -34.133  1.00 78.44           C  
ANISOU  795  CA  ALA B 115     9864  10203   9739    501   -224    -92       C  
ATOM    796  C   ALA B 115      -9.847  14.974 -33.465  1.00 80.82           C  
ANISOU  796  C   ALA B 115    10100  10569  10041    503   -152    -40       C  
ATOM    797  O   ALA B 115      -9.465  15.339 -32.343  1.00 79.34           O  
ANISOU  797  O   ALA B 115     9847  10449   9850    510   -151    -34       O  
ATOM    798  CB  ALA B 115     -12.215  14.686 -34.247  1.00 78.91           C  
ANISOU  798  CB  ALA B 115     9915  10238   9828    528   -225   -100       C  
ATOM    799  N   SER B 116      -9.234  14.001 -34.161  1.00 82.39           N  
ANISOU  799  N   SER B 116    10316  10745  10242    496    -92     -4       N  
ATOM    800  CA  SER B 116      -8.130  13.230 -33.592  1.00 77.76           C  
ANISOU  800  CA  SER B 116     9669  10216   9659    499    -19     47       C  
ATOM    801  C   SER B 116      -7.043  14.145 -33.059  1.00 78.56           C  
ANISOU  801  C   SER B 116     9750  10363   9736    480    -18     55       C  
ATOM    802  O   SER B 116      -6.500  13.918 -31.969  1.00 78.68           O  
ANISOU  802  O   SER B 116     9688  10451   9756    492     13     80       O  
ATOM    803  CB  SER B 116      -7.541  12.281 -34.636  1.00 80.38           C  
ANISOU  803  CB  SER B 116    10042  10508   9992    487     38     80       C  
ATOM    804  OG  SER B 116      -6.987  13.005 -35.723  1.00 81.69           O  
ANISOU  804  OG  SER B 116    10288  10620  10131    453     24     71       O  
ATOM    805  N   ALA B 117      -6.728  15.202 -33.806  1.00 73.58           N  
ANISOU  805  N   ALA B 117     9187   9690   9080    450    -53     35       N  
ATOM    806  CA  ALA B 117      -5.808  16.209 -33.299  1.00 73.74           C  
ANISOU  806  CA  ALA B 117     9191   9748   9078    431    -62     36       C  
ATOM    807  C   ALA B 117      -6.399  16.933 -32.085  1.00 74.73           C  
ANISOU  807  C   ALA B 117     9260   9925   9207    450   -111      8       C  
ATOM    808  O   ALA B 117      -5.760  17.024 -31.028  1.00 75.11           O  
ANISOU  808  O   ALA B 117     9240  10045   9255    456    -91     27       O  
ATOM    809  CB  ALA B 117      -5.459  17.181 -34.427  1.00 70.25           C  
ANISOU  809  CB  ALA B 117     8838   9243   8609    396    -92     18       C  
ATOM    810  N   PHE B 118      -7.634  17.430 -32.214  1.00 76.09           N  
ANISOU  810  N   PHE B 118     9461  10065   9385    459   -175    -37       N  
ATOM    811  CA  PHE B 118      -8.186  18.284 -31.171  1.00 77.14           C  
ANISOU  811  CA  PHE B 118     9551  10240   9519    473   -228    -68       C  
ATOM    812  C   PHE B 118      -8.400  17.500 -29.898  1.00 77.36           C  
ANISOU  812  C   PHE B 118     9484  10342   9569    507   -199    -49       C  
ATOM    813  O   PHE B 118      -8.298  18.067 -28.806  1.00 78.35           O  
ANISOU  813  O   PHE B 118     9553  10526   9690    517   -218    -56       O  
ATOM    814  CB  PHE B 118      -9.512  18.921 -31.604  1.00 79.14           C  
ANISOU  814  CB  PHE B 118     9856  10441   9775    477   -302   -121       C  
ATOM    815  CG  PHE B 118      -9.401  19.900 -32.778  1.00 79.73           C  
ANISOU  815  CG  PHE B 118    10024  10444   9825    444   -342   -147       C  
ATOM    816  CD1 PHE B 118      -8.168  20.292 -33.286  1.00 79.70           C  
ANISOU  816  CD1 PHE B 118    10052  10431   9798    413   -317   -125       C  
ATOM    817  CD2 PHE B 118     -10.554  20.418 -33.369  1.00 79.12           C  
ANISOU  817  CD2 PHE B 118    10005  10309   9750    445   -406   -192       C  
ATOM    818  CE1 PHE B 118      -8.090  21.166 -34.355  1.00 79.98           C  
ANISOU  818  CE1 PHE B 118    10173  10402   9812    383   -353   -148       C  
ATOM    819  CE2 PHE B 118     -10.482  21.295 -34.431  1.00 80.50           C  
ANISOU  819  CE2 PHE B 118    10265  10418   9903    416   -443   -216       C  
ATOM    820  CZ  PHE B 118      -9.251  21.672 -34.929  1.00 81.57           C  
ANISOU  820  CZ  PHE B 118    10432  10546  10015    385   -416   -194       C  
ATOM    821  N   CYS B 119      -8.708  16.204 -30.012  1.00 76.29           N  
ANISOU  821  N   CYS B 119     9329  10202   9456    526   -155    -25       N  
ATOM    822  CA  CYS B 119      -8.793  15.363 -28.819  1.00 77.20           C  
ANISOU  822  CA  CYS B 119     9352  10389   9592    558   -119      0       C  
ATOM    823  C   CYS B 119      -7.434  15.229 -28.156  1.00 77.41           C  
ANISOU  823  C   CYS B 119     9325  10479   9608    552    -66     41       C  
ATOM    824  O   CYS B 119      -7.280  15.526 -26.966  1.00 76.88           O  
ANISOU  824  O   CYS B 119     9190  10480   9542    566    -71     43       O  
ATOM    825  CB  CYS B 119      -9.344  13.982 -29.165  1.00 78.33           C  
ANISOU  825  CB  CYS B 119     9490  10510   9762    577    -80     19       C  
ATOM    826  SG  CYS B 119     -11.087  13.969 -29.604  1.00 84.56           S  
ANISOU  826  SG  CYS B 119    10317  11242  10572    595   -140    -27       S  
ATOM    827  N   LEU B 120      -6.430  14.806 -28.928  1.00 77.19           N  
ANISOU  827  N   LEU B 120     9329  10428   9571    530    -16     74       N  
ATOM    828  CA  LEU B 120      -5.117  14.508 -28.373  1.00 75.36           C  
ANISOU  828  CA  LEU B 120     9046  10253   9332    524     42    117       C  
ATOM    829  C   LEU B 120      -4.462  15.697 -27.689  1.00 77.42           C  
ANISOU  829  C   LEU B 120     9286  10557   9572    511     15    107       C  
ATOM    830  O   LEU B 120      -3.511  15.483 -26.931  1.00 77.45           O  
ANISOU  830  O   LEU B 120     9232  10623   9573    514     57    139       O  
ATOM    831  CB  LEU B 120      -4.171  13.980 -29.453  1.00 75.81           C  
ANISOU  831  CB  LEU B 120     9152  10271   9382    499     95    150       C  
ATOM    832  CG  LEU B 120      -4.140  12.452 -29.474  1.00 75.73           C  
ANISOU  832  CG  LEU B 120     9109  10270   9394    518    160    189       C  
ATOM    833  CD1 LEU B 120      -5.496  11.888 -29.825  1.00 77.63           C  
ANISOU  833  CD1 LEU B 120     9369  10469   9657    539    137    167       C  
ATOM    834  CD2 LEU B 120      -3.063  11.929 -30.360  1.00 75.23           C  
ANISOU  834  CD2 LEU B 120     9082  10180   9322    495    217    225       C  
ATOM    835  N   THR B 121      -4.916  16.929 -27.947  1.00 75.87           N  
ANISOU  835  N   THR B 121     9136  10330   9361    498    -53     63       N  
ATOM    836  CA  THR B 121      -4.405  18.066 -27.191  1.00 76.03           C  
ANISOU  836  CA  THR B 121     9130  10394   9364    489    -84     49       C  
ATOM    837  C   THR B 121      -5.279  18.384 -25.982  1.00 76.51           C  
ANISOU  837  C   THR B 121     9130  10505   9435    519   -125     23       C  
ATOM    838  O   THR B 121      -4.750  18.810 -24.952  1.00 77.52           O  
ANISOU  838  O   THR B 121     9199  10698   9556    525   -125     29       O  
ATOM    839  CB  THR B 121      -4.264  19.311 -28.086  1.00 78.98           C  
ANISOU  839  CB  THR B 121     9585  10711   9714    455   -133     18       C  
ATOM    840  OG1 THR B 121      -5.492  20.055 -28.131  1.00 79.82           O  
ANISOU  840  OG1 THR B 121     9719  10787   9822    463   -207    -32       O  
ATOM    841  CG2 THR B 121      -3.895  18.910 -29.511  1.00 80.18           C  
ANISOU  841  CG2 THR B 121     9813  10792   9859    431   -105     33       C  
ATOM    842  N   GLY B 122      -6.596  18.172 -26.073  1.00 73.82           N  
ANISOU  842  N   GLY B 122     8800  10138   9111    539   -160     -5       N  
ATOM    843  CA  GLY B 122      -7.430  18.249 -24.883  1.00 74.43           C  
ANISOU  843  CA  GLY B 122     8812  10268   9202    571   -189    -23       C  
ATOM    844  C   GLY B 122      -7.123  17.125 -23.912  1.00 75.85           C  
ANISOU  844  C   GLY B 122     8905  10515   9398    599   -128     18       C  
ATOM    845  O   GLY B 122      -7.097  17.326 -22.692  1.00 75.79           O  
ANISOU  845  O   GLY B 122     8828  10577   9393    619   -134     19       O  
ATOM    846  N   LEU B 123      -6.890  15.924 -24.445  1.00 73.83           N  
ANISOU  846  N   LEU B 123     8654  10241   9156    601    -69     54       N  
ATOM    847  CA  LEU B 123      -6.237  14.878 -23.676  1.00 73.61           C  
ANISOU  847  CA  LEU B 123     8553  10276   9141    619     -1    101       C  
ATOM    848  C   LEU B 123      -4.977  15.399 -22.996  1.00 74.61           C  
ANISOU  848  C   LEU B 123     8640  10461   9248    607     18    121       C  
ATOM    849  O   LEU B 123      -4.739  15.108 -21.822  1.00 76.00           O  
ANISOU  849  O   LEU B 123     8737  10710   9431    630     41    139       O  
ATOM    850  CB  LEU B 123      -5.914  13.700 -24.595  1.00 72.54           C  
ANISOU  850  CB  LEU B 123     8446  10102   9016    612     58    136       C  
ATOM    851  CG  LEU B 123      -6.202  12.304 -24.062  1.00 70.69           C  
ANISOU  851  CG  LEU B 123     8150   9901   8809    643    110    168       C  
ATOM    852  CD1 LEU B 123      -7.583  12.243 -23.487  1.00 69.66           C  
ANISOU  852  CD1 LEU B 123     7992   9778   8698    674     69    139       C  
ATOM    853  CD2 LEU B 123      -6.030  11.268 -25.150  1.00 71.97           C  
ANISOU  853  CD2 LEU B 123     8355  10010   8981    634    157    194       C  
ATOM    854  N   SER B 124      -4.161  16.183 -23.708  1.00 72.61           N  
ANISOU  854  N   SER B 124     8441  10176   8972    573     10    117       N  
ATOM    855  CA  SER B 124      -2.957  16.728 -23.088  1.00 72.67           C  
ANISOU  855  CA  SER B 124     8413  10236   8962    560     26    135       C  
ATOM    856  C   SER B 124      -3.266  17.912 -22.187  1.00 73.97           C  
ANISOU  856  C   SER B 124     8551  10439   9117    567    -35     99       C  
ATOM    857  O   SER B 124      -2.750  17.987 -21.072  1.00 78.02           O  
ANISOU  857  O   SER B 124     8993  11023   9627    580    -20    113       O  
ATOM    858  CB  SER B 124      -1.928  17.131 -24.136  1.00 76.13           C  
ANISOU  858  CB  SER B 124     8916  10630   9381    521     41    146       C  
ATOM    859  OG  SER B 124      -1.439  15.990 -24.807  1.00 78.06           O  
ANISOU  859  OG  SER B 124     9173  10854   9634    516    106    185       O  
ATOM    860  N   PHE B 125      -4.090  18.858 -22.640  1.00 74.33           N  
ANISOU  860  N   PHE B 125     8650  10437   9155    558   -103     52       N  
ATOM    861  CA  PHE B 125      -4.409  20.001 -21.783  1.00 76.06           C  
ANISOU  861  CA  PHE B 125     8844  10691   9365    565   -163     16       C  
ATOM    862  C   PHE B 125      -5.076  19.574 -20.492  1.00 80.54           C  
ANISOU  862  C   PHE B 125     9329  11324   9949    605   -164     16       C  
ATOM    863  O   PHE B 125      -5.148  20.365 -19.543  1.00 80.96           O  
ANISOU  863  O   PHE B 125     9342  11425   9995    615   -200     -5       O  
ATOM    864  CB  PHE B 125      -5.323  20.978 -22.494  1.00 73.67           C  
ANISOU  864  CB  PHE B 125     8612  10325   9055    552   -236    -35       C  
ATOM    865  CG  PHE B 125      -5.360  22.336 -21.876  1.00 74.86           C  
ANISOU  865  CG  PHE B 125     8753  10499   9190    548   -297    -70       C  
ATOM    866  CD1 PHE B 125      -4.327  23.230 -22.083  1.00 80.48           C  
ANISOU  866  CD1 PHE B 125     9489  11210   9881    518   -303    -69       C  
ATOM    867  CD2 PHE B 125      -6.452  22.736 -21.117  1.00 78.58           C  
ANISOU  867  CD2 PHE B 125     9196  10993   9669    573   -349   -106       C  
ATOM    868  CE1 PHE B 125      -4.377  24.510 -21.538  1.00 79.66           C  
ANISOU  868  CE1 PHE B 125     9378  11126   9762    513   -361   -103       C  
ATOM    869  CE2 PHE B 125      -6.513  24.018 -20.559  1.00 80.69           C  
ANISOU  869  CE2 PHE B 125     9455  11280   9921    569   -408   -141       C  
ATOM    870  CZ  PHE B 125      -5.475  24.904 -20.765  1.00 77.46           C  
ANISOU  870  CZ  PHE B 125     9070  10870   9492    539   -414   -140       C  
ATOM    871  N   ASP B 126      -5.598  18.352 -20.453  1.00 78.93           N  
ANISOU  871  N   ASP B 126     9100  11122   9767    628   -127     36       N  
ATOM    872  CA  ASP B 126      -5.993  17.740 -19.190  1.00 76.95           C  
ANISOU  872  CA  ASP B 126     8763  10942   9533    666   -110     48       C  
ATOM    873  C   ASP B 126      -4.791  17.615 -18.262  1.00 77.19           C  
ANISOU  873  C   ASP B 126     8726  11047   9555    670    -66     84       C  
ATOM    874  O   ASP B 126      -4.760  18.205 -17.184  1.00 80.27           O  
ANISOU  874  O   ASP B 126     9064  11496   9940    684    -90     72       O  
ATOM    875  CB  ASP B 126      -6.616  16.378 -19.492  1.00 80.59           C  
ANISOU  875  CB  ASP B 126     9218  11384  10020    686    -70     69       C  
ATOM    876  CG  ASP B 126      -7.464  15.866 -18.385  1.00 82.64           C  
ANISOU  876  CG  ASP B 126     9405  11696  10299    726    -72     68       C  
ATOM    877  OD1 ASP B 126      -8.353  16.624 -17.935  1.00 83.84           O  
ANISOU  877  OD1 ASP B 126     9552  11853  10450    738   -132     27       O  
ATOM    878  OD2 ASP B 126      -7.278  14.681 -18.034  1.00 78.77           O  
ANISOU  878  OD2 ASP B 126     8867  11236   9825    745    -13    107       O  
ATOM    879  N   ARG B 127      -3.759  16.903 -18.710  1.00 73.41           N  
ANISOU  879  N   ARG B 127     8252  10565   9076    655     -3    127       N  
ATOM    880  CA  ARG B 127      -2.586  16.692 -17.884  1.00 73.03           C  
ANISOU  880  CA  ARG B 127     8141  10587   9022    658     44    163       C  
ATOM    881  C   ARG B 127      -1.819  17.977 -17.609  1.00 75.55           C  
ANISOU  881  C   ARG B 127     8464  10925   9316    637     11    147       C  
ATOM    882  O   ARG B 127      -1.093  18.031 -16.620  1.00 76.37           O  
ANISOU  882  O   ARG B 127     8504  11098   9415    647     32    166       O  
ATOM    883  CB  ARG B 127      -1.653  15.670 -18.521  1.00 74.00           C  
ANISOU  883  CB  ARG B 127     8273  10695   9148    645    118    211       C  
ATOM    884  CG  ARG B 127      -2.327  14.545 -19.265  1.00 73.52           C  
ANISOU  884  CG  ARG B 127     8239  10588   9108    653    145    223       C  
ATOM    885  CD  ARG B 127      -2.615  13.387 -18.358  1.00 73.12           C  
ANISOU  885  CD  ARG B 127     8111  10592   9079    690    188    252       C  
ATOM    886  NE  ARG B 127      -3.728  13.680 -17.464  1.00 76.38           N  
ANISOU  886  NE  ARG B 127     8485  11035   9502    719    142    221       N  
ATOM    887  CZ  ARG B 127      -3.783  13.341 -16.175  1.00 82.93           C  
ANISOU  887  CZ  ARG B 127     9231  11941  10340    751    157    235       C  
ATOM    888  NH1 ARG B 127      -2.766  12.715 -15.565  1.00 82.52           N  
ANISOU  888  NH1 ARG B 127     9122  11945  10287    757    217    279       N  
ATOM    889  NH2 ARG B 127      -4.866  13.652 -15.483  1.00 83.40           N  
ANISOU  889  NH2 ARG B 127     9263  12019  10407    776    112    204       N  
ATOM    890  N   TYR B 128      -1.921  19.018 -18.437  1.00 70.46           N  
ANISOU  890  N   TYR B 128     7892  10224   8657    608    -38    113       N  
ATOM    891  CA  TYR B 128      -1.261  20.267 -18.038  1.00 71.07           C  
ANISOU  891  CA  TYR B 128     7966  10325   8713    592    -73     96       C  
ATOM    892  C   TYR B 128      -2.029  20.964 -16.925  1.00 73.46           C  
ANISOU  892  C   TYR B 128     8222  10675   9016    617   -128     61       C  
ATOM    893  O   TYR B 128      -1.438  21.414 -15.936  1.00 76.21           O  
ANISOU  893  O   TYR B 128     8515  11085   9355    624   -130     65       O  
ATOM    894  CB  TYR B 128      -1.080  21.225 -19.216  1.00 74.07           C  
ANISOU  894  CB  TYR B 128     8434  10633   9076    553   -110     71       C  
ATOM    895  CG  TYR B 128      -0.963  22.725 -18.829  1.00 76.22           C  
ANISOU  895  CG  TYR B 128     8714  10918   9330    541   -173     34       C  
ATOM    896  CD1 TYR B 128       0.269  23.310 -18.522  1.00 75.90           C  
ANISOU  896  CD1 TYR B 128     8655  10910   9274    522   -160     48       C  
ATOM    897  CD2 TYR B 128      -2.088  23.563 -18.829  1.00 76.15           C  
ANISOU  897  CD2 TYR B 128     8731  10883   9320    546   -246    -16       C  
ATOM    898  CE1 TYR B 128       0.368  24.688 -18.184  1.00 78.52           C  
ANISOU  898  CE1 TYR B 128     8993  11250   9590    510   -219     13       C  
ATOM    899  CE2 TYR B 128      -1.996  24.931 -18.504  1.00 84.18           C  
ANISOU  899  CE2 TYR B 128     9756  11909  10321    535   -305    -51       C  
ATOM    900  CZ  TYR B 128      -0.770  25.491 -18.186  1.00 86.24           C  
ANISOU  900  CZ  TYR B 128     9998  12203  10567    517   -291    -36       C  
ATOM    901  OH  TYR B 128      -0.693  26.848 -17.877  1.00 82.42           O  
ANISOU  901  OH  TYR B 128     9521  11725  10068    505   -351    -71       O  
ATOM    902  N   LEU B 129      -3.341  21.122 -17.106  1.00 80.63           N  
ANISOU  902  N   LEU B 129     9155  11549   9932    630   -176     25       N  
ATOM    903  CA  LEU B 129      -4.179  21.641 -16.037  1.00 83.61           C  
ANISOU  903  CA  LEU B 129     9486  11971  10313    658   -225     -7       C  
ATOM    904  C   LEU B 129      -3.979  20.815 -14.780  1.00 85.08           C  
ANISOU  904  C   LEU B 129     9578  12239  10510    692   -180     25       C  
ATOM    905  O   LEU B 129      -3.734  21.354 -13.695  1.00 90.44           O  
ANISOU  905  O   LEU B 129    10201  12981  11180    706   -197     18       O  
ATOM    906  CB  LEU B 129      -5.647  21.617 -16.466  1.00 88.09           C  
ANISOU  906  CB  LEU B 129    10089  12488  10893    670   -269    -42       C  
ATOM    907  CG  LEU B 129      -6.230  22.742 -17.333  1.00 94.30           C  
ANISOU  907  CG  LEU B 129    10955  13206  11668    647   -339    -90       C  
ATOM    908  CD1 LEU B 129      -7.563  22.294 -17.956  1.00 86.90           C  
ANISOU  908  CD1 LEU B 129    10057  12214  10749    658   -361   -112       C  
ATOM    909  CD2 LEU B 129      -6.423  24.032 -16.521  1.00 89.26           C  
ANISOU  909  CD2 LEU B 129    10297  12602  11017    651   -402   -129       C  
ATOM    910  N   ALA B 130      -4.044  19.491 -14.919  1.00 81.16           N  
ANISOU  910  N   ALA B 130     9063  11743  10031    706   -123     60       N  
ATOM    911  CA  ALA B 130      -3.892  18.614 -13.765  1.00 79.61           C  
ANISOU  911  CA  ALA B 130     8778  11622   9847    740    -78     93       C  
ATOM    912  C   ALA B 130      -2.498  18.740 -13.160  1.00 82.26           C  
ANISOU  912  C   ALA B 130     9071  12016  10169    732    -41    123       C  
ATOM    913  O   ALA B 130      -2.341  19.100 -11.986  1.00 85.04           O  
ANISOU  913  O   ALA B 130     9359  12436  10515    751    -52    120       O  
ATOM    914  CB  ALA B 130      -4.182  17.168 -14.170  1.00 75.75           C  
ANISOU  914  CB  ALA B 130     8286  11116   9381    752    -22    126       C  
ATOM    915  N   ILE B 131      -1.464  18.476 -13.965  1.00 81.11           N  
ANISOU  915  N   ILE B 131     8958  11842  10017    703      2    152       N  
ATOM    916  CA  ILE B 131      -0.137  18.227 -13.419  1.00 80.50           C  
ANISOU  916  CA  ILE B 131     8834  11821   9933    700     53    192       C  
ATOM    917  C   ILE B 131       0.719  19.493 -13.296  1.00 81.98           C  
ANISOU  917  C   ILE B 131     9033  12020  10097    675     22    176       C  
ATOM    918  O   ILE B 131       1.861  19.417 -12.817  1.00 81.91           O  
ANISOU  918  O   ILE B 131     8984  12057  10081    670     59    205       O  
ATOM    919  CB  ILE B 131       0.457  17.077 -14.259  1.00 77.51           C  
ANISOU  919  CB  ILE B 131     8476  11411   9563    687    122    235       C  
ATOM    920  CG1 ILE B 131      -0.482  15.859 -14.117  1.00 78.57           C  
ANISOU  920  CG1 ILE B 131     8585  11547   9722    718    148    249       C  
ATOM    921  CG2 ILE B 131       1.864  16.732 -13.849  1.00 77.62           C  
ANISOU  921  CG2 ILE B 131     8447  11474   9571    681    180    279       C  
ATOM    922  CD1 ILE B 131      -0.100  14.557 -14.887  1.00 78.77           C  
ANISOU  922  CD1 ILE B 131     8626  11543   9762    712    217    292       C  
ATOM    923  N   VAL B 132       0.187  20.669 -13.630  1.00 82.70           N  
ANISOU  923  N   VAL B 132     9171  12073  10177    660    -47    129       N  
ATOM    924  CA  VAL B 132       0.923  21.887 -13.301  1.00 83.47           C  
ANISOU  924  CA  VAL B 132     9268  12192  10255    642    -80    112       C  
ATOM    925  C   VAL B 132       0.030  22.829 -12.507  1.00 87.74           C  
ANISOU  925  C   VAL B 132     9789  12757  10792    661   -151     66       C  
ATOM    926  O   VAL B 132       0.519  23.578 -11.656  1.00 90.06           O  
ANISOU  926  O   VAL B 132    10043  13102  11074    664   -171     57       O  
ATOM    927  CB  VAL B 132       1.489  22.580 -14.551  1.00 85.84           C  
ANISOU  927  CB  VAL B 132     9651  12423  10541    598    -93    104       C  
ATOM    928  CG1 VAL B 132       1.815  24.030 -14.240  1.00 86.77           C  
ANISOU  928  CG1 VAL B 132     9776  12551  10640    582   -150     71       C  
ATOM    929  CG2 VAL B 132       2.732  21.857 -15.038  1.00 85.20           C  
ANISOU  929  CG2 VAL B 132     9574  12340  10460    579    -22    152       C  
ATOM    930  N   ARG B 133      -1.282  22.778 -12.752  1.00 85.99           N  
ANISOU  930  N   ARG B 133     9591  12501  10580    675   -188     37       N  
ATOM    931  CA  ARG B 133      -2.234  23.592 -12.004  1.00 86.99           C  
ANISOU  931  CA  ARG B 133     9697  12649  10705    695   -254     -7       C  
ATOM    932  C   ARG B 133      -1.822  25.058 -12.036  1.00 94.36           C  
ANISOU  932  C   ARG B 133    10659  13575  11618    671   -309    -40       C  
ATOM    933  O   ARG B 133      -1.350  25.579 -11.019  1.00 98.48           O  
ANISOU  933  O   ARG B 133    11128  14159  12131    681   -319    -43       O  
ATOM    934  CB  ARG B 133      -2.318  23.111 -10.553  1.00 96.42           C  
ANISOU  934  CB  ARG B 133    10798  13932  11907    736   -234      7       C  
ATOM    935  CG  ARG B 133      -2.763  21.664 -10.364  1.00 98.91           C  
ANISOU  935  CG  ARG B 133    11076  14262  12243    763   -181     40       C  
ATOM    936  CD  ARG B 133      -2.211  21.045  -9.055  1.00101.85           C  
ANISOU  936  CD  ARG B 133    11355  14725  12619    793   -136     74       C  
ATOM    937  NE  ARG B 133      -1.028  20.217  -9.317  1.00 93.65           N  
ANISOU  937  NE  ARG B 133    10305  13696  11581    781    -64    125       N  
ATOM    938  CZ  ARG B 133       0.046  20.140  -8.534  1.00 94.30           C  
ANISOU  938  CZ  ARG B 133    10332  13842  11656    785    -29    153       C  
ATOM    939  NH1 ARG B 133       0.115  20.840  -7.407  1.00 95.07           N  
ANISOU  939  NH1 ARG B 133    10377  14001  11743    802    -60    136       N  
ATOM    940  NH2 ARG B 133       1.058  19.355  -8.883  1.00 96.15           N  
ANISOU  940  NH2 ARG B 133    10563  14078  11893    772     36    198       N  
ATOM    941  N   PRO B 134      -1.959  25.753 -13.169  1.00 97.54           N  
ANISOU  941  N   PRO B 134    11145  13904  12013    639   -344    -65       N  
ATOM    942  CA  PRO B 134      -1.577  27.179 -13.204  1.00 98.49           C  
ANISOU  942  CA  PRO B 134    11292  14015  12115    616   -398    -97       C  
ATOM    943  C   PRO B 134      -2.365  28.048 -12.237  1.00101.27           C  
ANISOU  943  C   PRO B 134    11611  14404  12463    638   -463   -140       C  
ATOM    944  O   PRO B 134      -1.795  28.980 -11.659  1.00106.49           O  
ANISOU  944  O   PRO B 134    12251  15099  13112    632   -489   -153       O  
ATOM    945  CB  PRO B 134      -1.853  27.573 -14.656  1.00 98.88           C  
ANISOU  945  CB  PRO B 134    11439  13973  12160    583   -423   -116       C  
ATOM    946  CG  PRO B 134      -2.939  26.619 -15.096  1.00100.54           C  
ANISOU  946  CG  PRO B 134    11665  14148  12387    600   -412   -116       C  
ATOM    947  CD  PRO B 134      -2.610  25.318 -14.418  1.00 89.55           C  
ANISOU  947  CD  PRO B 134    10204  12813  11010    626   -343    -70       C  
ATOM    948  N   VAL B 135      -3.651  27.769 -12.039  1.00100.28           N  
ANISOU  948  N   VAL B 135    11479  14272  12350    665   -489   -162       N  
ATOM    949  CA  VAL B 135      -4.470  28.477 -11.066  1.00111.97           C  
ANISOU  949  CA  VAL B 135    12923  15791  13830    691   -546   -200       C  
ATOM    950  C   VAL B 135      -4.726  27.554  -9.865  1.00122.35           C  
ANISOU  950  C   VAL B 135    14150  17181  15157    733   -511   -178       C  
ATOM    951  O   VAL B 135      -4.415  26.359  -9.889  1.00120.83           O  
ANISOU  951  O   VAL B 135    13932  17002  14975    742   -446   -135       O  
ATOM    952  CB  VAL B 135      -5.792  28.973 -11.692  1.00108.40           C  
ANISOU  952  CB  VAL B 135    12529  15278  13382    690   -609   -247       C  
ATOM    953  CG1 VAL B 135      -6.421  30.115 -10.867  1.00110.06           C  
ANISOU  953  CG1 VAL B 135    12718  15517  13584    704   -681   -294       C  
ATOM    954  CG2 VAL B 135      -5.556  29.403 -13.128  1.00109.11           C  
ANISOU  954  CG2 VAL B 135    12710  15282  13463    648   -621   -255       C  
ATOM    955  N   ALA B 136      -5.287  28.128  -8.794  1.00114.00           N  
ANISOU  955  N   ALA B 136    13045  16173  14096    760   -555   -206       N  
ATOM    956  CA  ALA B 136      -5.702  27.356  -7.630  1.00120.23           C  
ANISOU  956  CA  ALA B 136    13753  17031  14897    803   -531   -191       C  
ATOM    957  C   ALA B 136      -6.901  26.465  -7.975  1.00121.55           C  
ANISOU  957  C   ALA B 136    13931  17166  15084    822   -524   -193       C  
ATOM    958  O   ALA B 136      -7.628  26.705  -8.942  1.00120.31           O  
ANISOU  958  O   ALA B 136    13842  16940  14932    806   -557   -218       O  
ATOM    959  CB  ALA B 136      -6.043  28.287  -6.468  1.00112.53           C  
ANISOU  959  CB  ALA B 136    12731  16112  13912    825   -584   -225       C  
ATOM    960  N   ASN B 137      -7.132  25.452  -7.132  1.00117.02           N  
ANISOU  960  N   ASN B 137    13290  16648  14525    857   -482   -165       N  
ATOM    961  CA  ASN B 137      -7.883  24.268  -7.557  1.00111.21           C  
ANISOU  961  CA  ASN B 137    12560  15885  13811    871   -449   -148       C  
ATOM    962  C   ASN B 137      -9.388  24.514  -7.675  1.00120.63           C  
ANISOU  962  C   ASN B 137    13775  17044  15014    886   -504   -190       C  
ATOM    963  O   ASN B 137     -10.050  23.843  -8.478  1.00118.23           O  
ANISOU  963  O   ASN B 137    13509  16686  14726    884   -493   -187       O  
ATOM    964  CB  ASN B 137      -7.552  23.116  -6.603  1.00105.24           C  
ANISOU  964  CB  ASN B 137    11722  15199  13066    902   -384   -103       C  
ATOM    965  CG  ASN B 137      -6.043  22.863  -6.526  1.00106.49           C  
ANISOU  965  CG  ASN B 137    11860  15388  13213    886   -329    -61       C  
ATOM    966  OD1 ASN B 137      -5.255  23.639  -7.074  1.00112.80           O  
ANISOU  966  OD1 ASN B 137    12701  16160  13996    852   -343    -68       O  
ATOM    967  ND2 ASN B 137      -5.637  21.797  -5.848  1.00 92.77           N  
ANISOU  967  ND2 ASN B 137    10058  13704  11485    909   -268    -17       N  
ATOM    968  N   ALA B 138      -9.947  25.463  -6.914  1.00124.14           N  
ANISOU  968  N   ALA B 138    14198  17518  15451    902   -563   -230       N  
ATOM    969  CA  ALA B 138     -11.353  25.825  -7.116  1.00126.59           C  
ANISOU  969  CA  ALA B 138    14536  17791  15770    913   -621   -274       C  
ATOM    970  C   ALA B 138     -11.569  26.490  -8.479  1.00128.58           C  
ANISOU  970  C   ALA B 138    14885  17953  16018    876   -661   -303       C  
ATOM    971  O   ALA B 138     -12.525  26.156  -9.194  1.00120.99           O  
ANISOU  971  O   ALA B 138    13965  16936  15070    877   -674   -317       O  
ATOM    972  CB  ALA B 138     -11.844  26.739  -5.991  1.00111.80           C  
ANISOU  972  CB  ALA B 138    12620  15971  13888    937   -676   -310       C  
ATOM    973  N   ARG B 139     -10.677  27.412  -8.870  1.00127.06           N  
ANISOU  973  N   ARG B 139    14729  17745  15805    844   -679   -311       N  
ATOM    974  CA  ARG B 139     -10.748  28.102 -10.161  1.00119.24           C  
ANISOU  974  CA  ARG B 139    13829  16670  14807    807   -715   -336       C  
ATOM    975  C   ARG B 139     -10.230  27.277 -11.339  1.00115.36           C  
ANISOU  975  C   ARG B 139    13388  16124  14321    781   -662   -302       C  
ATOM    976  O   ARG B 139     -10.299  27.749 -12.483  1.00118.11           O  
ANISOU  976  O   ARG B 139    13814  16400  14664    751   -688   -320       O  
ATOM    977  CB  ARG B 139      -9.984  29.435 -10.095  1.00123.63           C  
ANISOU  977  CB  ARG B 139    14403  17231  15339    782   -755   -358       C  
ATOM    978  CG  ARG B 139     -10.656  30.523  -9.257  1.00132.47           C  
ANISOU  978  CG  ARG B 139    15500  18380  16451    799   -825   -405       C  
ATOM    979  CD  ARG B 139     -11.995  31.020  -9.844  1.00119.34           C  
ANISOU  979  CD  ARG B 139    13891  16657  14794    799   -889   -453       C  
ATOM    980  NE  ARG B 139     -12.291  30.550 -11.205  1.00119.67           N  
ANISOU  980  NE  ARG B 139    14006  16617  14845    777   -877   -448       N  
ATOM    981  CZ  ARG B 139     -11.779  31.073 -12.318  1.00124.04           C  
ANISOU  981  CZ  ARG B 139    14634  17109  15388    738   -888   -453       C  
ATOM    982  NH1 ARG B 139     -10.935  32.091 -12.241  1.00124.66           N  
ANISOU  982  NH1 ARG B 139    14723  17196  15447    716   -910   -462       N  
ATOM    983  NH2 ARG B 139     -12.107  30.573 -13.509  1.00118.79           N  
ANISOU  983  NH2 ARG B 139    14032  16371  14730    722   -875   -449       N  
ATOM    984  N   LEU B 140      -9.726  26.068 -11.099  1.00111.23           N  
ANISOU  984  N   LEU B 140    12821  15633  13809    794   -591   -254       N  
ATOM    985  CA  LEU B 140      -9.158  25.272 -12.176  1.00107.01           C  
ANISOU  985  CA  LEU B 140    12331  15050  13279    770   -538   -219       C  
ATOM    986  C   LEU B 140     -10.234  24.650 -13.059  1.00113.23           C  
ANISOU  986  C   LEU B 140    13165  15773  14085    773   -543   -229       C  
ATOM    987  O   LEU B 140      -9.944  24.324 -14.218  1.00106.75           O  
ANISOU  987  O   LEU B 140    12404  14890  13264    747   -521   -216       O  
ATOM    988  CB  LEU B 140      -8.243  24.197 -11.588  1.00103.55           C  
ANISOU  988  CB  LEU B 140    11828  14669  12846    783   -460   -165       C  
ATOM    989  CG  LEU B 140      -7.117  23.584 -12.421  1.00 99.82           C  
ANISOU  989  CG  LEU B 140    11384  14171  12370    755   -399   -122       C  
ATOM    990  CD1 LEU B 140      -5.897  24.491 -12.426  1.00 95.46           C  
ANISOU  990  CD1 LEU B 140    10843  13632  11797    727   -405   -120       C  
ATOM    991  CD2 LEU B 140      -6.757  22.242 -11.829  1.00 96.72           C  
ANISOU  991  CD2 LEU B 140    10927  13830  11993    779   -327    -73       C  
ATOM    992  N   ARG B 141     -11.468  24.528 -12.542  1.00115.82           N  
ANISOU  992  N   ARG B 141    13467  16111  14426    804   -574   -254       N  
ATOM    993  CA  ARG B 141     -12.641  24.005 -13.246  1.00106.05           C  
ANISOU  993  CA  ARG B 141    12269  14817  13209    811   -586   -269       C  
ATOM    994  C   ARG B 141     -12.261  22.969 -14.304  1.00 96.87           C  
ANISOU  994  C   ARG B 141    11144  13605  12055    794   -530   -233       C  
ATOM    995  O   ARG B 141     -12.364  23.228 -15.504  1.00 91.32           O  
ANISOU  995  O   ARG B 141    10520  12828  11348    767   -548   -247       O  
ATOM    996  CB  ARG B 141     -13.462  25.159 -13.857  1.00 94.61           C  
ANISOU  996  CB  ARG B 141    10886  13310  11752    796   -666   -324       C  
ATOM    997  CG  ARG B 141     -12.676  26.244 -14.620  1.00102.40           C  
ANISOU  997  CG  ARG B 141    11936  14256  12715    756   -694   -339       C  
ATOM    998  CD  ARG B 141     -13.575  27.383 -15.156  1.00105.44           C  
ANISOU  998  CD  ARG B 141    12383  14586  13093    744   -775   -396       C  
ATOM    999  NE  ARG B 141     -14.653  26.926 -16.053  1.00113.10           N  
ANISOU  999  NE  ARG B 141    13405  15488  14080    746   -789   -412       N  
ATOM   1000  CZ  ARG B 141     -14.768  27.237 -17.349  1.00118.56           C  
ANISOU 1000  CZ  ARG B 141    14182  16099  14766    716   -810   -427       C  
ATOM   1001  NH1 ARG B 141     -13.877  28.024 -17.942  1.00113.99           N  
ANISOU 1001  NH1 ARG B 141    13651  15494  14166    682   -819   -429       N  
ATOM   1002  NH2 ARG B 141     -15.791  26.768 -18.050  1.00115.65           N  
ANISOU 1002  NH2 ARG B 141    13853  15676  14414    722   -822   -442       N  
ATOM   1003  N   LEU B 142     -11.822  21.788 -13.864  1.00102.34           N  
ANISOU 1003  N   LEU B 142    11783  14340  12761    811   -462   -187       N  
ATOM   1004  CA  LEU B 142     -11.140  20.856 -14.755  1.00 95.77           C  
ANISOU 1004  CA  LEU B 142    10980  13473  11934    793   -401   -147       C  
ATOM   1005  C   LEU B 142     -12.116  20.004 -15.564  1.00 92.94           C  
ANISOU 1005  C   LEU B 142    10658  13057  11598    800   -394   -149       C  
ATOM   1006  O   LEU B 142     -11.866  19.725 -16.748  1.00 95.40           O  
ANISOU 1006  O   LEU B 142    11034  13305  11910    775   -377   -140       O  
ATOM   1007  CB  LEU B 142     -10.206  19.962 -13.949  1.00 93.63           C  
ANISOU 1007  CB  LEU B 142    10636  13272  11666    808   -330    -95       C  
ATOM   1008  CG  LEU B 142      -9.573  18.842 -14.761  1.00 88.14           C  
ANISOU 1008  CG  LEU B 142     9961  12547  10980    795   -262    -51       C  
ATOM   1009  CD1 LEU B 142      -8.605  19.430 -15.780  1.00 91.34           C  
ANISOU 1009  CD1 LEU B 142    10434  12905  11365    753   -261    -49       C  
ATOM   1010  CD2 LEU B 142      -8.885  17.828 -13.878  1.00 84.77           C  
ANISOU 1010  CD2 LEU B 142     9456  12191  10562    816   -193     -2       C  
ATOM   1011  N   ARG B 143     -13.222  19.571 -14.956  1.00 92.70           N  
ANISOU 1011  N   ARG B 143    10588  13045  11587    833   -406   -160       N  
ATOM   1012  CA  ARG B 143     -14.212  18.817 -15.720  1.00 93.58           C  
ANISOU 1012  CA  ARG B 143    10735  13099  11723    840   -405   -166       C  
ATOM   1013  C   ARG B 143     -14.794  19.651 -16.855  1.00 94.29           C  
ANISOU 1013  C   ARG B 143    10914  13107  11805    815   -465   -210       C  
ATOM   1014  O   ARG B 143     -14.822  19.214 -18.011  1.00 89.77           O  
ANISOU 1014  O   ARG B 143    10403  12469  11238    797   -450   -203       O  
ATOM   1015  CB  ARG B 143     -15.319  18.325 -14.803  1.00 95.92           C  
ANISOU 1015  CB  ARG B 143    10970  13432  12041    880   -413   -174       C  
ATOM   1016  CG  ARG B 143     -14.805  17.390 -13.783  1.00102.11           C  
ANISOU 1016  CG  ARG B 143    11670  14291  12834    905   -352   -129       C  
ATOM   1017  CD  ARG B 143     -13.922  16.328 -14.437  1.00106.36           C  
ANISOU 1017  CD  ARG B 143    12220  14813  13378    891   -280    -81       C  
ATOM   1018  NE  ARG B 143     -13.612  15.251 -13.496  1.00110.40           N  
ANISOU 1018  NE  ARG B 143    12650  15392  13904    919   -218    -37       N  
ATOM   1019  CZ  ARG B 143     -13.923  13.968 -13.677  1.00104.72           C  
ANISOU 1019  CZ  ARG B 143    11915  14663  13211    934   -171     -7       C  
ATOM   1020  NH1 ARG B 143     -14.513  13.570 -14.810  1.00102.53           N  
ANISOU 1020  NH1 ARG B 143    11699  14310  12947    923   -176    -17       N  
ATOM   1021  NH2 ARG B 143     -13.604  13.081 -12.735  1.00101.57           N  
ANISOU 1021  NH2 ARG B 143    11439  14330  12822    960   -118     32       N  
ATOM   1022  N   VAL B 144     -15.290  20.846 -16.526  1.00 97.37           N  
ANISOU 1022  N   VAL B 144    11313  13500  12183    815   -533   -254       N  
ATOM   1023  CA  VAL B 144     -15.821  21.766 -17.527  1.00 92.77           C  
ANISOU 1023  CA  VAL B 144    10814  12843  11591    791   -594   -298       C  
ATOM   1024  C   VAL B 144     -14.788  22.028 -18.616  1.00 90.40           C  
ANISOU 1024  C   VAL B 144    10581  12496  11273    751   -577   -285       C  
ATOM   1025  O   VAL B 144     -15.048  21.819 -19.809  1.00 87.51           O  
ANISOU 1025  O   VAL B 144    10284  12057  10910    734   -580   -290       O  
ATOM   1026  CB  VAL B 144     -16.272  23.069 -16.844  1.00 91.25           C  
ANISOU 1026  CB  VAL B 144    10611  12674  11385    797   -665   -344       C  
ATOM   1027  CG1 VAL B 144     -17.273  23.824 -17.697  1.00 91.85           C  
ANISOU 1027  CG1 VAL B 144    10761  12677  11460    785   -733   -394       C  
ATOM   1028  CG2 VAL B 144     -16.870  22.744 -15.487  1.00 89.25           C  
ANISOU 1028  CG2 VAL B 144    10272  12493  11146    837   -664   -343       C  
ATOM   1029  N   SER B 145     -13.596  22.486 -18.221  1.00 92.44           N  
ANISOU 1029  N   SER B 145    10817  12794  11510    737   -559   -266       N  
ATOM   1030  CA  SER B 145     -12.521  22.664 -19.188  1.00 92.89           C  
ANISOU 1030  CA  SER B 145    10931  12813  11551    700   -536   -248       C  
ATOM   1031  C   SER B 145     -12.236  21.371 -19.938  1.00 93.05           C  
ANISOU 1031  C   SER B 145    10967  12804  11585    696   -471   -208       C  
ATOM   1032  O   SER B 145     -11.810  21.410 -21.098  1.00 89.91           O  
ANISOU 1032  O   SER B 145    10638  12346  11178    667   -462   -203       O  
ATOM   1033  CB  SER B 145     -11.264  23.179 -18.491  1.00 95.80           C  
ANISOU 1033  CB  SER B 145    11261  13241  11900    690   -518   -229       C  
ATOM   1034  OG  SER B 145     -11.584  24.300 -17.684  1.00 98.89           O  
ANISOU 1034  OG  SER B 145    11628  13665  12280    698   -577   -266       O  
ATOM   1035  N   GLY B 146     -12.477  20.219 -19.305  1.00 91.17           N  
ANISOU 1035  N   GLY B 146    10666  12605  11368    726   -425   -180       N  
ATOM   1036  CA  GLY B 146     -12.499  18.974 -20.050  1.00 90.81           C  
ANISOU 1036  CA  GLY B 146    10639  12524  11339    726   -373   -149       C  
ATOM   1037  C   GLY B 146     -13.719  18.840 -20.941  1.00 88.35           C  
ANISOU 1037  C   GLY B 146    10387  12141  11043    728   -408   -179       C  
ATOM   1038  O   GLY B 146     -13.630  18.267 -22.030  1.00 83.50           O  
ANISOU 1038  O   GLY B 146     9825  11467  10432    712   -384   -167       O  
ATOM   1039  N   ALA B 147     -14.864  19.378 -20.507  1.00 90.46           N  
ANISOU 1039  N   ALA B 147    10645  12408  11316    746   -467   -221       N  
ATOM   1040  CA  ALA B 147     -16.125  19.147 -21.200  1.00 89.19           C  
ANISOU 1040  CA  ALA B 147    10528  12185  11174    753   -500   -249       C  
ATOM   1041  C   ALA B 147     -16.482  20.255 -22.177  1.00 87.05           C  
ANISOU 1041  C   ALA B 147    10344  11845  10887    727   -564   -294       C  
ATOM   1042  O   ALA B 147     -17.021  19.960 -23.247  1.00 86.56           O  
ANISOU 1042  O   ALA B 147    10344  11712  10833    718   -573   -305       O  
ATOM   1043  CB  ALA B 147     -17.264  18.973 -20.199  1.00 93.78           C  
ANISOU 1043  CB  ALA B 147    11051  12806  11776    791   -525   -268       C  
ATOM   1044  N   VAL B 148     -16.228  21.525 -21.838  1.00 85.81           N  
ANISOU 1044  N   VAL B 148    10193  11704  10708    715   -611   -321       N  
ATOM   1045  CA  VAL B 148     -16.353  22.581 -22.850  1.00 86.59           C  
ANISOU 1045  CA  VAL B 148    10378  11734  10788    685   -666   -357       C  
ATOM   1046  C   VAL B 148     -15.352  22.360 -23.986  1.00 85.99           C  
ANISOU 1046  C   VAL B 148    10362  11612  10699    652   -627   -330       C  
ATOM   1047  O   VAL B 148     -15.645  22.629 -25.164  1.00 84.53           O  
ANISOU 1047  O   VAL B 148    10257  11352  10509    631   -653   -350       O  
ATOM   1048  CB  VAL B 148     -16.202  23.968 -22.188  1.00 90.26           C  
ANISOU 1048  CB  VAL B 148    10832  12231  11233    679   -721   -389       C  
ATOM   1049  CG1 VAL B 148     -16.151  25.069 -23.222  1.00 87.75           C  
ANISOU 1049  CG1 VAL B 148    10601  11845  10893    645   -772   -421       C  
ATOM   1050  CG2 VAL B 148     -17.384  24.213 -21.299  1.00 80.33           C  
ANISOU 1050  CG2 VAL B 148     9531  11002   9989    710   -767   -422       C  
ATOM   1051  N   ALA B 149     -14.162  21.857 -23.647  1.00 88.19           N  
ANISOU 1051  N   ALA B 149    10600  11935  10972    647   -565   -285       N  
ATOM   1052  CA  ALA B 149     -13.216  21.397 -24.651  1.00 83.18           C  
ANISOU 1052  CA  ALA B 149    10012  11263  10329    620   -516   -252       C  
ATOM   1053  C   ALA B 149     -13.870  20.411 -25.607  1.00 81.92           C  
ANISOU 1053  C   ALA B 149     9894  11043  10188    624   -498   -247       C  
ATOM   1054  O   ALA B 149     -13.714  20.525 -26.827  1.00 82.72           O  
ANISOU 1054  O   ALA B 149    10073  11077  10281    599   -501   -251       O  
ATOM   1055  CB  ALA B 149     -12.002  20.758 -23.971  1.00 83.51           C  
ANISOU 1055  CB  ALA B 149     9991  11370  10369    623   -447   -202       C  
ATOM   1056  N   THR B 150     -14.609  19.431 -25.075  1.00 81.11           N  
ANISOU 1056  N   THR B 150     9741  10964  10112    656   -477   -237       N  
ATOM   1057  CA  THR B 150     -15.075  18.349 -25.933  1.00 79.99           C  
ANISOU 1057  CA  THR B 150     9631  10771   9991    660   -449   -225       C  
ATOM   1058  C   THR B 150     -16.198  18.827 -26.841  1.00 80.66           C  
ANISOU 1058  C   THR B 150     9789  10780  10078    655   -511   -271       C  
ATOM   1059  O   THR B 150     -16.390  18.275 -27.930  1.00 81.86           O  
ANISOU 1059  O   THR B 150     9997  10868  10236    645   -497   -267       O  
ATOM   1060  CB  THR B 150     -15.564  17.151 -25.119  1.00 69.67           C  
ANISOU 1060  CB  THR B 150     8249   9508   8713    696   -410   -201       C  
ATOM   1061  OG1 THR B 150     -15.432  15.970 -25.901  1.00 69.15           O  
ANISOU 1061  OG1 THR B 150     8205   9408   8663    695   -357   -171       O  
ATOM   1062  CG2 THR B 150     -17.063  17.270 -24.863  1.00 70.30           C  
ANISOU 1062  CG2 THR B 150     8324   9575   8813    721   -463   -241       C  
ATOM   1063  N   ALA B 151     -16.941  19.853 -26.429  1.00 80.38           N  
ANISOU 1063  N   ALA B 151     9756  10748  10038    660   -578   -316       N  
ATOM   1064  CA  ALA B 151     -18.049  20.307 -27.258  1.00 80.99           C  
ANISOU 1064  CA  ALA B 151     9900  10753  10119    656   -639   -361       C  
ATOM   1065  C   ALA B 151     -17.549  21.147 -28.431  1.00 82.16           C  
ANISOU 1065  C   ALA B 151    10138  10838  10241    619   -663   -375       C  
ATOM   1066  O   ALA B 151     -17.765  20.800 -29.597  1.00 82.52           O  
ANISOU 1066  O   ALA B 151    10251  10815  10289    606   -660   -378       O  
ATOM   1067  CB  ALA B 151     -19.047  21.088 -26.406  1.00 83.01           C  
ANISOU 1067  CB  ALA B 151    10126  11035  10379    676   -703   -403       C  
ATOM   1068  N   VAL B 152     -16.854  22.249 -28.137  1.00 82.43           N  
ANISOU 1068  N   VAL B 152    10174  10894  10249    600   -687   -384       N  
ATOM   1069  CA  VAL B 152     -16.327  23.111 -29.191  1.00 81.78           C  
ANISOU 1069  CA  VAL B 152    10175  10756  10142    564   -710   -397       C  
ATOM   1070  C   VAL B 152     -15.347  22.360 -30.080  1.00 81.23           C  
ANISOU 1070  C   VAL B 152    10138  10658  10066    544   -647   -356       C  
ATOM   1071  O   VAL B 152     -15.146  22.731 -31.240  1.00 82.24           O  
ANISOU 1071  O   VAL B 152    10347  10722  10179    517   -659   -364       O  
ATOM   1072  CB  VAL B 152     -15.685  24.358 -28.566  1.00 80.90           C  
ANISOU 1072  CB  VAL B 152    10048  10683  10007    550   -741   -410       C  
ATOM   1073  CG1 VAL B 152     -15.503  25.436 -29.620  1.00 85.75           C  
ANISOU 1073  CG1 VAL B 152    10752  11233  10598    516   -785   -437       C  
ATOM   1074  CG2 VAL B 152     -16.542  24.847 -27.404  1.00 80.63           C  
ANISOU 1074  CG2 VAL B 152     9957  10696   9982    577   -788   -441       C  
ATOM   1075  N   LEU B 153     -14.729  21.299 -29.562  1.00 80.33           N  
ANISOU 1075  N   LEU B 153     9965  10593   9964    557   -578   -310       N  
ATOM   1076  CA  LEU B 153     -13.935  20.383 -30.374  1.00 79.61           C  
ANISOU 1076  CA  LEU B 153     9899  10477   9872    543   -514   -269       C  
ATOM   1077  C   LEU B 153     -14.750  19.884 -31.557  1.00 80.45           C  
ANISOU 1077  C   LEU B 153    10073  10504   9990    542   -524   -283       C  
ATOM   1078  O   LEU B 153     -14.400  20.156 -32.712  1.00 81.04           O  
ANISOU 1078  O   LEU B 153    10225  10518  10048    515   -528   -286       O  
ATOM   1079  CB  LEU B 153     -13.447  19.199 -29.530  1.00 78.18           C  
ANISOU 1079  CB  LEU B 153     9635  10361   9709    565   -443   -222       C  
ATOM   1080  CG  LEU B 153     -12.732  17.998 -30.160  1.00 79.83           C  
ANISOU 1080  CG  LEU B 153     9853  10555   9924    559   -369   -176       C  
ATOM   1081  CD1 LEU B 153     -11.680  17.549 -29.192  1.00 80.23           C  
ANISOU 1081  CD1 LEU B 153     9826  10683   9974    565   -311   -132       C  
ATOM   1082  CD2 LEU B 153     -13.688  16.841 -30.442  1.00 79.63           C  
ANISOU 1082  CD2 LEU B 153     9825  10503   9928    582   -354   -173       C  
ATOM   1083  N   TRP B 154     -15.848  19.169 -31.265  1.00 79.08           N  
ANISOU 1083  N   TRP B 154     9872  10331   9844    571   -531   -293       N  
ATOM   1084  CA  TRP B 154     -16.653  18.559 -32.320  1.00 79.43           C  
ANISOU 1084  CA  TRP B 154     9973  10304   9903    573   -537   -304       C  
ATOM   1085  C   TRP B 154     -17.223  19.598 -33.275  1.00 82.50           C  
ANISOU 1085  C   TRP B 154    10449  10620  10275    554   -605   -351       C  
ATOM   1086  O   TRP B 154     -17.486  19.286 -34.442  1.00 83.65           O  
ANISOU 1086  O   TRP B 154    10664  10698  10422    544   -606   -356       O  
ATOM   1087  CB  TRP B 154     -17.781  17.724 -31.713  1.00 78.63           C  
ANISOU 1087  CB  TRP B 154     9821  10220   9835    610   -538   -310       C  
ATOM   1088  CG  TRP B 154     -17.337  16.352 -31.288  1.00 79.29           C  
ANISOU 1088  CG  TRP B 154     9843  10344   9938    627   -462   -261       C  
ATOM   1089  CD1 TRP B 154     -17.204  15.890 -30.012  1.00 79.21           C  
ANISOU 1089  CD1 TRP B 154     9743  10413   9942    651   -432   -238       C  
ATOM   1090  CD2 TRP B 154     -16.943  15.272 -32.143  1.00 76.85           C  
ANISOU 1090  CD2 TRP B 154     9561  10000   9637    621   -406   -228       C  
ATOM   1091  NE1 TRP B 154     -16.767  14.585 -30.021  1.00 76.73           N  
ANISOU 1091  NE1 TRP B 154     9397  10114   9645    661   -361   -193       N  
ATOM   1092  CE2 TRP B 154     -16.601  14.188 -31.320  1.00 77.11           C  
ANISOU 1092  CE2 TRP B 154     9517  10093   9690    643   -345   -187       C  
ATOM   1093  CE3 TRP B 154     -16.849  15.117 -33.521  1.00 76.94           C  
ANISOU 1093  CE3 TRP B 154     9657   9937   9642    600   -403   -230       C  
ATOM   1094  CZ2 TRP B 154     -16.177  12.972 -31.837  1.00 79.29           C  
ANISOU 1094  CZ2 TRP B 154     9794  10354   9977    643   -282   -148       C  
ATOM   1095  CZ3 TRP B 154     -16.431  13.908 -34.026  1.00 76.35           C  
ANISOU 1095  CZ3 TRP B 154     9583   9848   9578    602   -340   -192       C  
ATOM   1096  CH2 TRP B 154     -16.100  12.856 -33.193  1.00 77.56           C  
ANISOU 1096  CH2 TRP B 154     9658  10061   9751    623   -281   -152       C  
ATOM   1097  N   VAL B 155     -17.392  20.839 -32.814  1.00 82.31           N  
ANISOU 1097  N   VAL B 155    10426  10612  10237    548   -662   -384       N  
ATOM   1098  CA  VAL B 155     -17.977  21.873 -33.663  1.00 82.54           C  
ANISOU 1098  CA  VAL B 155    10536  10575  10252    531   -730   -430       C  
ATOM   1099  C   VAL B 155     -16.942  22.459 -34.630  1.00 83.81           C  
ANISOU 1099  C   VAL B 155    10765  10696  10382    493   -722   -421       C  
ATOM   1100  O   VAL B 155     -17.247  22.699 -35.808  1.00 83.42           O  
ANISOU 1100  O   VAL B 155    10799  10573  10325    477   -748   -440       O  
ATOM   1101  CB  VAL B 155     -18.631  22.952 -32.781  1.00 85.77           C  
ANISOU 1101  CB  VAL B 155    10916  11013  10658    541   -796   -471       C  
ATOM   1102  CG1 VAL B 155     -18.648  24.291 -33.497  1.00 88.29           C  
ANISOU 1102  CG1 VAL B 155    11311  11282  10951    513   -857   -508       C  
ATOM   1103  CG2 VAL B 155     -20.044  22.530 -32.396  1.00 87.11           C  
ANISOU 1103  CG2 VAL B 155    11060  11182  10857    573   -826   -497       C  
ATOM   1104  N   LEU B 156     -15.715  22.712 -34.159  1.00 79.03           N  
ANISOU 1104  N   LEU B 156    10128  10139   9760    479   -688   -391       N  
ATOM   1105  CA  LEU B 156     -14.634  23.035 -35.086  1.00 78.95           C  
ANISOU 1105  CA  LEU B 156    10178  10095   9726    445   -666   -373       C  
ATOM   1106  C   LEU B 156     -14.471  21.947 -36.140  1.00 78.15           C  
ANISOU 1106  C   LEU B 156    10118   9946   9631    440   -617   -347       C  
ATOM   1107  O   LEU B 156     -14.707  22.175 -37.334  1.00 76.71           O  
ANISOU 1107  O   LEU B 156    10019   9690   9438    423   -639   -364       O  
ATOM   1108  CB  LEU B 156     -13.313  23.212 -34.344  1.00 72.67           C  
ANISOU 1108  CB  LEU B 156     9330   9365   8917    434   -625   -339       C  
ATOM   1109  CG  LEU B 156     -12.975  24.595 -33.841  1.00 73.24           C  
ANISOU 1109  CG  LEU B 156     9399   9461   8969    420   -671   -362       C  
ATOM   1110  CD1 LEU B 156     -11.468  24.677 -33.704  1.00 72.74           C  
ANISOU 1110  CD1 LEU B 156     9318   9433   8888    398   -621   -323       C  
ATOM   1111  CD2 LEU B 156     -13.486  25.647 -34.801  1.00 74.27           C  
ANISOU 1111  CD2 LEU B 156     9617   9520   9083    399   -736   -405       C  
ATOM   1112  N   ALA B 157     -14.074  20.747 -35.695  1.00 80.42           N  
ANISOU 1112  N   ALA B 157    10348  10274   9935    456   -551   -305       N  
ATOM   1113  CA  ALA B 157     -13.649  19.688 -36.595  1.00 78.08           C  
ANISOU 1113  CA  ALA B 157    10082   9942   9643    450   -494   -272       C  
ATOM   1114  C   ALA B 157     -14.713  19.358 -37.624  1.00 80.01           C  
ANISOU 1114  C   ALA B 157    10391  10110   9898    455   -522   -298       C  
ATOM   1115  O   ALA B 157     -14.387  18.860 -38.708  1.00 79.94           O  
ANISOU 1115  O   ALA B 157    10438  10051   9884    441   -493   -282       O  
ATOM   1116  CB  ALA B 157     -13.281  18.452 -35.780  1.00 79.54           C  
ANISOU 1116  CB  ALA B 157    10185  10189   9850    473   -426   -228       C  
ATOM   1117  N   ALA B 158     -15.989  19.618 -37.309  1.00 79.92           N  
ANISOU 1117  N   ALA B 158    10373  10090   9901    475   -578   -338       N  
ATOM   1118  CA  ALA B 158     -17.024  19.509 -38.335  1.00 82.03           C  
ANISOU 1118  CA  ALA B 158    10710  10280  10177    477   -615   -369       C  
ATOM   1119  C   ALA B 158     -17.095  20.771 -39.170  1.00 80.82           C  
ANISOU 1119  C   ALA B 158    10640  10070   9996    450   -673   -405       C  
ATOM   1120  O   ALA B 158     -17.095  20.696 -40.405  1.00 81.27           O  
ANISOU 1120  O   ALA B 158    10775  10059  10044    434   -675   -409       O  
ATOM   1121  CB  ALA B 158     -18.391  19.224 -37.726  1.00 73.02           C  
ANISOU 1121  CB  ALA B 158     9531   9149   9065    509   -650   -397       C  
ATOM   1122  N   LEU B 159     -17.161  21.937 -38.520  1.00 80.17           N  
ANISOU 1122  N   LEU B 159    10543  10016   9902    446   -722   -431       N  
ATOM   1123  CA  LEU B 159     -17.215  23.174 -39.286  1.00 81.91           C  
ANISOU 1123  CA  LEU B 159    10841  10183  10097    420   -779   -466       C  
ATOM   1124  C   LEU B 159     -16.058  23.255 -40.270  1.00 82.14           C  
ANISOU 1124  C   LEU B 159    10929  10179  10101    388   -743   -439       C  
ATOM   1125  O   LEU B 159     -16.267  23.244 -41.490  1.00 83.09           O  
ANISOU 1125  O   LEU B 159    11129  10227  10212    375   -755   -450       O  
ATOM   1126  CB  LEU B 159     -17.208  24.401 -38.384  1.00 84.76           C  
ANISOU 1126  CB  LEU B 159    11172  10586  10446    417   -828   -491       C  
ATOM   1127  CG  LEU B 159     -18.604  24.980 -38.151  1.00 83.64           C  
ANISOU 1127  CG  LEU B 159    11036  10426  10316    434   -902   -543       C  
ATOM   1128  CD1 LEU B 159     -18.514  26.488 -37.841  1.00 82.74           C  
ANISOU 1128  CD1 LEU B 159    10937  10320  10181    418   -962   -575       C  
ATOM   1129  CD2 LEU B 159     -19.559  24.658 -39.300  1.00 82.39           C  
ANISOU 1129  CD2 LEU B 159    10951  10187  10166    436   -928   -567       C  
ATOM   1130  N   LEU B 160     -14.819  23.298 -39.761  1.00 83.94           N  
ANISOU 1130  N   LEU B 160    11116  10459  10317    376   -698   -403       N  
ATOM   1131  CA  LEU B 160     -13.745  23.535 -40.718  1.00 83.49           C  
ANISOU 1131  CA  LEU B 160    11119  10368  10234    343   -671   -382       C  
ATOM   1132  C   LEU B 160     -13.532  22.369 -41.684  1.00 85.40           C  
ANISOU 1132  C   LEU B 160    11397  10570  10482    342   -617   -353       C  
ATOM   1133  O   LEU B 160     -12.742  22.514 -42.628  1.00 85.96           O  
ANISOU 1133  O   LEU B 160    11526  10602  10532    316   -596   -337       O  
ATOM   1134  CB  LEU B 160     -12.425  23.879 -40.023  1.00 74.55           C  
ANISOU 1134  CB  LEU B 160     9941   9297   9088    329   -635   -350       C  
ATOM   1135  CG  LEU B 160     -11.638  22.939 -39.133  1.00 73.45           C  
ANISOU 1135  CG  LEU B 160     9717   9229   8960    342   -564   -303       C  
ATOM   1136  CD1 LEU B 160     -10.189  23.112 -39.492  1.00 73.14           C  
ANISOU 1136  CD1 LEU B 160     9694   9196   8899    312   -519   -268       C  
ATOM   1137  CD2 LEU B 160     -11.834  23.289 -37.675  1.00 73.31           C  
ANISOU 1137  CD2 LEU B 160     9615   9286   8953    361   -583   -312       C  
ATOM   1138  N   ALA B 161     -14.235  21.249 -41.523  1.00 84.01           N  
ANISOU 1138  N   ALA B 161    11190  10397  10334    370   -596   -346       N  
ATOM   1139  CA  ALA B 161     -14.151  20.152 -42.481  1.00 83.32           C  
ANISOU 1139  CA  ALA B 161    11139  10265  10253    370   -550   -323       C  
ATOM   1140  C   ALA B 161     -15.074  20.310 -43.697  1.00 85.82           C  
ANISOU 1140  C   ALA B 161    11544  10495  10567    366   -596   -358       C  
ATOM   1141  O   ALA B 161     -15.055  19.446 -44.572  1.00 86.58           O  
ANISOU 1141  O   ALA B 161    11678  10550  10669    367   -563   -343       O  
ATOM   1142  CB  ALA B 161     -14.454  18.826 -41.776  1.00 83.70           C  
ANISOU 1142  CB  ALA B 161    11112  10356  10333    401   -505   -298       C  
ATOM   1143  N   MET B 162     -15.859  21.389 -43.790  1.00 86.19           N  
ANISOU 1143  N   MET B 162    11627  10515  10607    363   -670   -405       N  
ATOM   1144  CA  MET B 162     -16.925  21.592 -44.780  1.00 85.34           C  
ANISOU 1144  CA  MET B 162    11596  10329  10500    364   -722   -445       C  
ATOM   1145  C   MET B 162     -16.505  21.772 -46.242  1.00 85.96           C  
ANISOU 1145  C   MET B 162    11772  10335  10555    338   -719   -444       C  
ATOM   1146  O   MET B 162     -17.177  21.234 -47.143  1.00 86.58           O  
ANISOU 1146  O   MET B 162    11901  10354  10641    344   -726   -455       O  
ATOM   1147  CB  MET B 162     -17.772  22.804 -44.389  1.00 85.44           C  
ANISOU 1147  CB  MET B 162    11616  10339  10509    366   -803   -495       C  
ATOM   1148  CG  MET B 162     -18.973  22.444 -43.566  1.00 90.82           C  
ANISOU 1148  CG  MET B 162    12242  11044  11221    399   -830   -518       C  
ATOM   1149  SD  MET B 162     -20.108  21.451 -44.546  1.00105.87           S  
ANISOU 1149  SD  MET B 162    14196  12880  13151    417   -837   -533       S  
ATOM   1150  CE  MET B 162     -20.523  20.179 -43.344  1.00 91.48           C  
ANISOU 1150  CE  MET B 162    12266  11123  11367    454   -794   -510       C  
ATOM   1151  N   PRO B 163     -15.461  22.556 -46.543  1.00 86.68           N  
ANISOU 1151  N   PRO B 163    11894  10424  10616    308   -712   -432       N  
ATOM   1152  CA  PRO B 163     -15.057  22.685 -47.948  1.00 88.09           C  
ANISOU 1152  CA  PRO B 163    12166  10534  10772    284   -706   -428       C  
ATOM   1153  C   PRO B 163     -14.819  21.338 -48.584  1.00 89.29           C  
ANISOU 1153  C   PRO B 163    12326  10665  10933    291   -644   -395       C  
ATOM   1154  O   PRO B 163     -14.918  21.205 -49.809  1.00 92.24           O  
ANISOU 1154  O   PRO B 163    12779  10971  11296    281   -647   -401       O  
ATOM   1155  CB  PRO B 163     -13.764  23.511 -47.874  1.00 83.50           C  
ANISOU 1155  CB  PRO B 163    11589   9975  10161    254   -689   -408       C  
ATOM   1156  CG  PRO B 163     -13.779  24.146 -46.566  1.00 85.24           C  
ANISOU 1156  CG  PRO B 163    11737  10262  10387    261   -713   -417       C  
ATOM   1157  CD  PRO B 163     -14.489  23.212 -45.654  1.00 85.05           C  
ANISOU 1157  CD  PRO B 163    11638  10281  10397    295   -699   -414       C  
ATOM   1158  N   VAL B 164     -14.517  20.326 -47.779  1.00 79.60           N  
ANISOU 1158  N   VAL B 164    11021   9495   9728    309   -589   -361       N  
ATOM   1159  CA  VAL B 164     -14.413  18.983 -48.307  1.00 82.58           C  
ANISOU 1159  CA  VAL B 164    11401   9855  10119    320   -532   -332       C  
ATOM   1160  C   VAL B 164     -15.796  18.377 -48.500  1.00 86.26           C  
ANISOU 1160  C   VAL B 164    11875  10287  10613    346   -563   -360       C  
ATOM   1161  O   VAL B 164     -15.989  17.519 -49.370  1.00 86.06           O  
ANISOU 1161  O   VAL B 164    11888  10215  10594    351   -539   -352       O  
ATOM   1162  CB  VAL B 164     -13.520  18.142 -47.384  1.00 80.66           C  
ANISOU 1162  CB  VAL B 164    11071   9686   9888    328   -461   -283       C  
ATOM   1163  CG1 VAL B 164     -13.491  16.694 -47.838  1.00 83.29           C  
ANISOU 1163  CG1 VAL B 164    11402  10005  10241    342   -403   -254       C  
ATOM   1164  CG2 VAL B 164     -12.114  18.738 -47.358  1.00 82.73           C  
ANISOU 1164  CG2 VAL B 164    11337   9974  10123    299   -431   -256       C  
ATOM   1165  N   MET B 165     -16.791  18.822 -47.736  1.00 85.37           N  
ANISOU 1165  N   MET B 165    11728  10192  10515    364   -616   -395       N  
ATOM   1166  CA  MET B 165     -18.140  18.340 -48.000  1.00 86.89           C  
ANISOU 1166  CA  MET B 165    11936  10346  10733    388   -650   -425       C  
ATOM   1167  C   MET B 165     -18.707  19.000 -49.240  1.00 88.80           C  
ANISOU 1167  C   MET B 165    12279  10504  10958    374   -704   -463       C  
ATOM   1168  O   MET B 165     -19.260  18.325 -50.119  1.00 95.33           O  
ANISOU 1168  O   MET B 165    13150  11275  11794    382   -703   -469       O  
ATOM   1169  CB  MET B 165     -19.062  18.613 -46.818  1.00 88.34           C  
ANISOU 1169  CB  MET B 165    12053  10574  10939    411   -691   -451       C  
ATOM   1170  CG  MET B 165     -20.513  18.323 -47.136  1.00 90.45           C  
ANISOU 1170  CG  MET B 165    12342  10795  11230    433   -737   -489       C  
ATOM   1171  SD  MET B 165     -20.680  16.580 -47.524  1.00 96.88           S  
ANISOU 1171  SD  MET B 165    13141  11595  12074    454   -675   -458       S  
ATOM   1172  CE  MET B 165     -21.490  16.004 -46.047  1.00 90.77           C  
ANISOU 1172  CE  MET B 165    12261  10889  11340    490   -674   -459       C  
ATOM   1173  N   VAL B 166     -18.554  20.317 -49.336  1.00 82.58           N  
ANISOU 1173  N   VAL B 166    11527   9705  10144    353   -752   -487       N  
ATOM   1174  CA  VAL B 166     -19.202  21.063 -50.407  1.00 87.37           C  
ANISOU 1174  CA  VAL B 166    12226  10235  10734    341   -812   -527       C  
ATOM   1175  C   VAL B 166     -18.500  20.864 -51.752  1.00 90.72           C  
ANISOU 1175  C   VAL B 166    12732  10602  11136    320   -782   -509       C  
ATOM   1176  O   VAL B 166     -19.160  20.679 -52.778  1.00 95.16           O  
ANISOU 1176  O   VAL B 166    13363  11097  11698    322   -805   -530       O  
ATOM   1177  CB  VAL B 166     -19.275  22.542 -50.002  1.00 89.07           C  
ANISOU 1177  CB  VAL B 166    12449  10460  10931    327   -873   -559       C  
ATOM   1178  CG1 VAL B 166     -19.489  23.412 -51.211  1.00 91.83           C  
ANISOU 1178  CG1 VAL B 166    12902  10734  11255    306   -921   -590       C  
ATOM   1179  CG2 VAL B 166     -20.396  22.717 -49.018  1.00 83.42           C  
ANISOU 1179  CG2 VAL B 166    11680   9775  10241    353   -920   -592       C  
ATOM   1180  N   LEU B 167     -17.166  20.872 -51.767  1.00 90.87           N  
ANISOU 1180  N   LEU B 167    12743  10648  11135    299   -729   -469       N  
ATOM   1181  CA  LEU B 167     -16.389  20.959 -52.997  1.00 92.13           C  
ANISOU 1181  CA  LEU B 167    12982  10756  11266    274   -706   -454       C  
ATOM   1182  C   LEU B 167     -16.027  19.611 -53.594  1.00 88.02           C  
ANISOU 1182  C   LEU B 167    12468  10221  10756    281   -641   -418       C  
ATOM   1183  O   LEU B 167     -15.985  19.470 -54.822  1.00 85.63           O  
ANISOU 1183  O   LEU B 167    12244   9854  10438    271   -638   -420       O  
ATOM   1184  CB  LEU B 167     -15.097  21.723 -52.752  1.00 97.66           C  
ANISOU 1184  CB  LEU B 167    13675  11491  11939    246   -684   -429       C  
ATOM   1185  CG  LEU B 167     -15.064  23.215 -53.012  1.00 94.26           C  
ANISOU 1185  CG  LEU B 167    13297  11036  11482    222   -743   -460       C  
ATOM   1186  CD1 LEU B 167     -16.113  23.888 -52.176  1.00 92.56           C  
ANISOU 1186  CD1 LEU B 167    13048  10839  11281    238   -810   -502       C  
ATOM   1187  CD2 LEU B 167     -13.676  23.713 -52.647  1.00 92.83           C  
ANISOU 1187  CD2 LEU B 167    13092  10898  11280    198   -707   -427       C  
ATOM   1188  N   ARG B 168     -15.695  18.633 -52.770  1.00 83.96           N  
ANISOU 1188  N   ARG B 168    11873   9765  10263    297   -585   -384       N  
ATOM   1189  CA  ARG B 168     -15.399  17.325 -53.327  1.00 90.94           C  
ANISOU 1189  CA  ARG B 168    12761  10633  11157    305   -524   -352       C  
ATOM   1190  C   ARG B 168     -16.575  16.835 -54.156  1.00 95.39           C  
ANISOU 1190  C   ARG B 168    13376  11130  11736    322   -556   -381       C  
ATOM   1191  O   ARG B 168     -17.714  16.808 -53.684  1.00 96.66           O  
ANISOU 1191  O   ARG B 168    13512  11293  11922    344   -598   -412       O  
ATOM   1192  CB  ARG B 168     -15.066  16.334 -52.209  1.00 95.18           C  
ANISOU 1192  CB  ARG B 168    13198  11244  11721    325   -467   -315       C  
ATOM   1193  CG  ARG B 168     -13.580  16.181 -51.990  1.00 88.03           C  
ANISOU 1193  CG  ARG B 168    12266  10383  10801    307   -402   -267       C  
ATOM   1194  CD  ARG B 168     -13.198  14.726 -52.079  1.00 90.73           C  
ANISOU 1194  CD  ARG B 168    12576  10737  11161    320   -330   -227       C  
ATOM   1195  NE  ARG B 168     -11.750  14.527 -52.070  1.00 95.32           N  
ANISOU 1195  NE  ARG B 168    13142  11349  11725    302   -265   -180       N  
ATOM   1196  CZ  ARG B 168     -11.145  13.394 -52.428  1.00 90.45           C  
ANISOU 1196  CZ  ARG B 168    12519  10734  11115    305   -198   -141       C  
ATOM   1197  NH1 ARG B 168      -9.824  13.313 -52.401  1.00 85.13           N  
ANISOU 1197  NH1 ARG B 168    11832  10089  10425    287   -142   -101       N  
ATOM   1198  NH2 ARG B 168     -11.853  12.336 -52.807  1.00 87.76           N  
ANISOU 1198  NH2 ARG B 168    12183  10364  10798    327   -186   -143       N  
ATOM   1199  N   THR B 169     -16.309  16.515 -55.417  1.00 94.69           N  
ANISOU 1199  N   THR B 169    13364  10983  11633    311   -538   -374       N  
ATOM   1200  CA  THR B 169     -17.305  15.879 -56.273  1.00 94.47           C  
ANISOU 1200  CA  THR B 169    13384  10891  11619    328   -557   -396       C  
ATOM   1201  C   THR B 169     -16.680  14.672 -56.957  1.00 97.01           C  
ANISOU 1201  C   THR B 169    13719  11196  11943    329   -489   -358       C  
ATOM   1202  O   THR B 169     -15.480  14.408 -56.835  1.00 94.54           O  
ANISOU 1202  O   THR B 169    13384  10918  11618    316   -429   -316       O  
ATOM   1203  CB  THR B 169     -17.876  16.830 -57.340  1.00 99.89           C  
ANISOU 1203  CB  THR B 169    14169  11502  12282    314   -623   -439       C  
ATOM   1204  OG1 THR B 169     -17.012  16.840 -58.483  1.00100.63           O  
ANISOU 1204  OG1 THR B 169    14335  11554  12346    292   -593   -419       O  
ATOM   1205  CG2 THR B 169     -18.061  18.263 -56.806  1.00102.26           C  
ANISOU 1205  CG2 THR B 169    14469  11818  12567    302   -683   -469       C  
ATOM   1206  N   THR B 170     -17.522  13.933 -57.672  1.00107.70           N  
ANISOU 1206  N   THR B 170    15109  12499  13314    346   -498   -373       N  
ATOM   1207  CA  THR B 170     -17.093  12.848 -58.540  1.00 99.94           C  
ANISOU 1207  CA  THR B 170    14156  11486  12332    348   -444   -345       C  
ATOM   1208  C   THR B 170     -16.904  13.349 -59.975  1.00104.30           C  
ANISOU 1208  C   THR B 170    14817  11963  12851    328   -462   -358       C  
ATOM   1209  O   THR B 170     -17.301  14.461 -60.347  1.00105.39           O  
ANISOU 1209  O   THR B 170    15009  12066  12968    316   -522   -394       O  
ATOM   1210  CB  THR B 170     -18.101  11.689 -58.528  1.00 98.03           C  
ANISOU 1210  CB  THR B 170    13890  11227  12128    380   -441   -353       C  
ATOM   1211  OG1 THR B 170     -19.435  12.193 -58.663  1.00 99.26           O  
ANISOU 1211  OG1 THR B 170    14076  11345  12295    391   -516   -405       O  
ATOM   1212  CG2 THR B 170     -18.013  10.912 -57.252  1.00101.02           C  
ANISOU 1212  CG2 THR B 170    14164  11681  12539    399   -401   -326       C  
ATOM   1213  N   GLY B 171     -16.292  12.503 -60.790  1.00105.72           N  
ANISOU 1213  N   GLY B 171    15027  12118  13023    325   -409   -329       N  
ATOM   1214  CA  GLY B 171     -16.101  12.845 -62.183  1.00109.59           C  
ANISOU 1214  CA  GLY B 171    15620  12537  13483    308   -420   -338       C  
ATOM   1215  C   GLY B 171     -14.969  12.083 -62.836  1.00112.77           C  
ANISOU 1215  C   GLY B 171    16041  12935  13871    297   -347   -294       C  
ATOM   1216  O   GLY B 171     -13.888  11.945 -62.251  1.00113.26           O  
ANISOU 1216  O   GLY B 171    16052  13052  13928    287   -294   -254       O  
ATOM   1217  N   ASP B 172     -15.206  11.565 -64.038  1.00111.55           N  
ANISOU 1217  N   ASP B 172    15958  12716  13711    301   -344   -299       N  
ATOM   1218  CA  ASP B 172     -14.155  10.896 -64.802  1.00112.98           C  
ANISOU 1218  CA  ASP B 172    16168  12883  13874    290   -278   -260       C  
ATOM   1219  C   ASP B 172     -13.215  11.969 -65.328  1.00115.08           C  
ANISOU 1219  C   ASP B 172    16490  13137  14097    258   -279   -253       C  
ATOM   1220  O   ASP B 172     -13.478  12.598 -66.359  1.00121.12           O  
ANISOU 1220  O   ASP B 172    17344  13839  14837    247   -318   -278       O  
ATOM   1221  CB  ASP B 172     -14.745  10.061 -65.940  1.00109.17           C  
ANISOU 1221  CB  ASP B 172    15748  12334  13399    305   -278   -271       C  
ATOM   1222  CG  ASP B 172     -13.694   9.622 -66.992  1.00117.55           C  
ANISOU 1222  CG  ASP B 172    16864  13367  14433    290   -222   -238       C  
ATOM   1223  OD1 ASP B 172     -13.351  10.426 -67.888  1.00121.53           O  
ANISOU 1223  OD1 ASP B 172    17447  13828  14900    269   -240   -247       O  
ATOM   1224  OD2 ASP B 172     -13.232   8.461 -66.952  1.00114.25           O  
ANISOU 1224  OD2 ASP B 172    16411  12967  14031    301   -160   -204       O  
ATOM   1225  N   LEU B 173     -12.122  12.203 -64.613  1.00115.26           N  
ANISOU 1225  N   LEU B 173    16462  13220  14111    242   -238   -219       N  
ATOM   1226  CA  LEU B 173     -11.027  12.933 -65.227  1.00120.99           C  
ANISOU 1226  CA  LEU B 173    17239  13933  14797    211   -221   -201       C  
ATOM   1227  C   LEU B 173     -10.335  12.051 -66.253  1.00113.48           C  
ANISOU 1227  C   LEU B 173    16333  12951  13835    208   -162   -170       C  
ATOM   1228  O   LEU B 173     -10.357  10.817 -66.161  1.00107.86           O  
ANISOU 1228  O   LEU B 173    15585  12250  13147    227   -118   -149       O  
ATOM   1229  CB  LEU B 173     -10.010  13.391 -64.185  1.00123.48           C  
ANISOU 1229  CB  LEU B 173    17487  14323  15108    195   -191   -172       C  
ATOM   1230  CG  LEU B 173     -10.519  13.921 -62.860  1.00110.88           C  
ANISOU 1230  CG  LEU B 173    15816  12780  13531    203   -228   -190       C  
ATOM   1231  CD1 LEU B 173      -9.358  14.582 -62.187  1.00105.20           C  
ANISOU 1231  CD1 LEU B 173    15058  12116  12796    181   -201   -162       C  
ATOM   1232  CD2 LEU B 173     -11.635  14.928 -63.085  1.00102.42           C  
ANISOU 1232  CD2 LEU B 173    14793  11667  12455    204   -313   -243       C  
ATOM   1233  N   GLU B 174      -9.749  12.692 -67.256  1.00104.28           N  
ANISOU 1233  N   GLU B 174    15247  11742  12632    184   -164   -168       N  
ATOM   1234  CA  GLU B 174      -8.665  12.104 -68.019  1.00105.78           C  
ANISOU 1234  CA  GLU B 174    15468  11922  12803    173    -98   -129       C  
ATOM   1235  C   GLU B 174      -9.089  11.076 -69.086  1.00106.93           C  
ANISOU 1235  C   GLU B 174    15666  12009  12953    189    -82   -131       C  
ATOM   1236  O   GLU B 174      -8.204  10.470 -69.755  1.00104.14           O  
ANISOU 1236  O   GLU B 174    15337  11646  12586    182    -24    -98       O  
ATOM   1237  CB  GLU B 174      -7.663  11.532 -67.003  1.00 89.59           C  
ANISOU 1237  CB  GLU B 174    13325   9948  10766    171    -30    -83       C  
ATOM   1238  CG  GLU B 174      -6.387  11.030 -67.558  1.00102.41           C  
ANISOU 1238  CG  GLU B 174    14965  11575  12371    157     42    -38       C  
ATOM   1239  CD  GLU B 174      -5.211  11.681 -66.931  1.00100.26           C  
ANISOU 1239  CD  GLU B 174    14655  11357  12084    132     71     -9       C  
ATOM   1240  OE1 GLU B 174      -5.352  12.803 -66.412  1.00 98.28           O  
ANISOU 1240  OE1 GLU B 174    14396  11121  11825    120     25    -29       O  
ATOM   1241  OE2 GLU B 174      -4.147  11.053 -66.954  1.00 94.30           O  
ANISOU 1241  OE2 GLU B 174    13877  10627  11324    126    139     34       O  
ATOM   1242  N   ASN B 175     -10.393  10.886 -69.336  1.00114.78           N  
ANISOU 1242  N   ASN B 175    16683  12963  13966    211   -133   -171       N  
ATOM   1243  CA  ASN B 175     -10.899   9.998 -70.394  1.00112.64           C  
ANISOU 1243  CA  ASN B 175    16467  12631  13699    227   -128   -179       C  
ATOM   1244  C   ASN B 175     -10.444   8.553 -70.185  1.00118.99           C  
ANISOU 1244  C   ASN B 175    17218  13465  14527    243    -56   -140       C  
ATOM   1245  O   ASN B 175      -9.559   8.047 -70.882  1.00104.93           O  
ANISOU 1245  O   ASN B 175    15467  11672  12729    235     -1   -108       O  
ATOM   1246  CB  ASN B 175     -10.451  10.439 -71.787  1.00106.95           C  
ANISOU 1246  CB  ASN B 175    15851  11848  12937    208   -129   -180       C  
ATOM   1247  CG  ASN B 175     -11.074   9.595 -72.871  1.00120.67           C  
ANISOU 1247  CG  ASN B 175    17648  13521  14679    227   -131   -194       C  
ATOM   1248  OD1 ASN B 175     -12.069   8.909 -72.629  1.00140.08           O  
ANISOU 1248  OD1 ASN B 175    20081  15974  17171    253   -151   -213       O  
ATOM   1249  ND2 ASN B 175     -10.469   9.593 -74.058  1.00115.27           N  
ANISOU 1249  ND2 ASN B 175    17043  12791  13963    214   -109   -182       N  
ATOM   1250  N   THR B 176     -11.107   7.880 -69.247  1.00120.19           N  
ANISOU 1250  N   THR B 176    17293  13653  14719    267    -57   -143       N  
ATOM   1251  CA  THR B 176     -10.628   6.554 -68.884  1.00106.09           C  
ANISOU 1251  CA  THR B 176    15446  11904  12958    281     13   -104       C  
ATOM   1252  C   THR B 176     -11.695   5.551 -68.474  1.00108.72           C  
ANISOU 1252  C   THR B 176    15734  12239  13335    314      4   -118       C  
ATOM   1253  O   THR B 176     -11.329   4.418 -68.154  1.00107.18           O  
ANISOU 1253  O   THR B 176    15487  12074  13163    327     62    -85       O  
ATOM   1254  CB  THR B 176      -9.586   6.700 -67.769  1.00106.22           C  
ANISOU 1254  CB  THR B 176    15383  12001  12976    269     58    -66       C  
ATOM   1255  OG1 THR B 176      -8.859   5.474 -67.631  1.00114.12           O  
ANISOU 1255  OG1 THR B 176    16339  13032  13991    277    133    -22       O  
ATOM   1256  CG2 THR B 176     -10.238   7.093 -66.464  1.00110.53           C  
ANISOU 1256  CG2 THR B 176    15853  12597  13547    279     21    -84       C  
ATOM   1257  N   ASN B 177     -12.987   5.898 -68.495  1.00110.90           N  
ANISOU 1257  N   ASN B 177    16029  12482  13625    328    -65   -164       N  
ATOM   1258  CA  ASN B 177     -14.066   4.978 -68.106  1.00111.87           C  
ANISOU 1258  CA  ASN B 177    16108  12604  13791    359    -77   -179       C  
ATOM   1259  C   ASN B 177     -13.968   4.590 -66.624  1.00106.76           C  
ANISOU 1259  C   ASN B 177    15350  12038  13177    370    -51   -158       C  
ATOM   1260  O   ASN B 177     -14.319   3.476 -66.238  1.00104.90           O  
ANISOU 1260  O   ASN B 177    15061  11818  12976    393    -24   -146       O  
ATOM   1261  CB  ASN B 177     -14.087   3.720 -68.991  1.00119.76           C  
ANISOU 1261  CB  ASN B 177    17138  13564  14802    374    -38   -166       C  
ATOM   1262  CG  ASN B 177     -15.496   3.176 -69.233  1.00129.44           C  
ANISOU 1262  CG  ASN B 177    18375  14746  16059    402    -82   -203       C  
ATOM   1263  OD1 ASN B 177     -16.430   3.923 -69.545  1.00105.60           O  
ANISOU 1263  OD1 ASN B 177    15402  11686  13036    404   -151   -247       O  
ATOM   1264  ND2 ASN B 177     -15.655   1.863 -69.066  1.00145.90           N  
ANISOU 1264  ND2 ASN B 177    20416  16841  18179    424    -41   -184       N  
ATOM   1265  N   LYS B 178     -13.485   5.517 -65.794  1.00110.63           N  
ANISOU 1265  N   LYS B 178    15802  12577  13654    353    -59   -152       N  
ATOM   1266  CA  LYS B 178     -13.353   5.327 -64.354  1.00102.34           C  
ANISOU 1266  CA  LYS B 178    14648  11606  12630    362    -38   -134       C  
ATOM   1267  C   LYS B 178     -13.669   6.644 -63.650  1.00102.84           C  
ANISOU 1267  C   LYS B 178    14698  11693  12684    351    -96   -161       C  
ATOM   1268  O   LYS B 178     -13.052   7.672 -63.947  1.00105.70           O  
ANISOU 1268  O   LYS B 178    15102  12048  13011    326   -109   -163       O  
ATOM   1269  CB  LYS B 178     -11.938   4.865 -63.979  1.00 97.04           C  
ANISOU 1269  CB  LYS B 178    13931  10989  11951    350     40    -79       C  
ATOM   1270  CG  LYS B 178     -11.523   3.516 -64.515  1.00 94.03           C  
ANISOU 1270  CG  LYS B 178    13551  10596  11581    361    103    -47       C  
ATOM   1271  CD  LYS B 178     -10.204   3.086 -63.908  1.00 97.59           C  
ANISOU 1271  CD  LYS B 178    13941  11110  12028    351    178      5       C  
ATOM   1272  CE  LYS B 178      -9.060   3.631 -64.725  1.00 92.78           C  
ANISOU 1272  CE  LYS B 178    13394  10483  11378    322    203     24       C  
ATOM   1273  NZ  LYS B 178      -7.950   4.153 -63.896  1.00 89.43           N  
ANISOU 1273  NZ  LYS B 178    12917  10123  10939    303    235     54       N  
ATOM   1274  N   VAL B 179     -14.609   6.612 -62.714  1.00106.81           N  
ANISOU 1274  N   VAL B 179    15142  12223  13218    371   -129   -182       N  
ATOM   1275  CA  VAL B 179     -14.965   7.809 -61.959  1.00110.36           C  
ANISOU 1275  CA  VAL B 179    15571  12698  13661    364   -184   -209       C  
ATOM   1276  C   VAL B 179     -13.907   8.073 -60.894  1.00102.83           C  
ANISOU 1276  C   VAL B 179    14545  11822  12702    352   -144   -174       C  
ATOM   1277  O   VAL B 179     -13.326   7.144 -60.317  1.00 96.70           O  
ANISOU 1277  O   VAL B 179    13704  11094  11943    360    -83   -135       O  
ATOM   1278  CB  VAL B 179     -16.363   7.661 -61.328  1.00110.93           C  
ANISOU 1278  CB  VAL B 179    15605  12772  13770    391   -234   -245       C  
ATOM   1279  CG1 VAL B 179     -16.877   9.016 -60.831  1.00103.93           C  
ANISOU 1279  CG1 VAL B 179    14721  11894  12872    383   -303   -282       C  
ATOM   1280  CG2 VAL B 179     -17.340   7.045 -62.316  1.00 99.03           C  
ANISOU 1280  CG2 VAL B 179    14156  11195  12277    408   -258   -271       C  
ATOM   1281  N   GLN B 180     -13.654   9.348 -60.631  1.00 95.54           N  
ANISOU 1281  N   GLN B 180    13634  10912  11754    331   -180   -189       N  
ATOM   1282  CA  GLN B 180     -12.760   9.752 -59.566  1.00 93.16           C  
ANISOU 1282  CA  GLN B 180    13265  10685  11448    320   -153   -162       C  
ATOM   1283  C   GLN B 180     -13.476  10.719 -58.642  1.00100.21           C  
ANISOU 1283  C   GLN B 180    14123  11605  12347    324   -215   -196       C  
ATOM   1284  O   GLN B 180     -14.191  11.619 -59.098  1.00 98.77           O  
ANISOU 1284  O   GLN B 180    13998  11379  12153    318   -280   -237       O  
ATOM   1285  CB  GLN B 180     -11.488  10.392 -60.109  1.00 95.18           C  
ANISOU 1285  CB  GLN B 180    13564  10937  11664    288   -126   -139       C  
ATOM   1286  CG  GLN B 180     -10.377   9.394 -60.331  1.00 98.63           C  
ANISOU 1286  CG  GLN B 180    13984  11391  12098    284    -44    -88       C  
ATOM   1287  CD  GLN B 180     -10.265   8.971 -61.778  1.00107.16           C  
ANISOU 1287  CD  GLN B 180    15152  12402  13163    279    -29    -87       C  
ATOM   1288  OE1 GLN B 180     -10.215   9.815 -62.674  1.00112.36           O  
ANISOU 1288  OE1 GLN B 180    15891  13009  13790    260    -62   -106       O  
ATOM   1289  NE2 GLN B 180     -10.236   7.660 -62.021  1.00106.93           N  
ANISOU 1289  NE2 GLN B 180    15107  12367  13154    296     19    -64       N  
ATOM   1290  N   CYS B 181     -13.297  10.491 -57.344  1.00 93.24           N  
ANISOU 1290  N   CYS B 181    13147  10797  11485    334   -193   -177       N  
ATOM   1291  CA  CYS B 181     -13.678  11.426 -56.301  1.00 86.00           C  
ANISOU 1291  CA  CYS B 181    12184   9921  10571    335   -239   -200       C  
ATOM   1292  C   CYS B 181     -12.521  12.400 -56.145  1.00 88.46           C  
ANISOU 1292  C   CYS B 181    12500  10260  10849    306   -229   -184       C  
ATOM   1293  O   CYS B 181     -11.354  11.993 -56.155  1.00 87.97           O  
ANISOU 1293  O   CYS B 181    12422  10225  10778    294   -166   -141       O  
ATOM   1294  CB  CYS B 181     -13.953  10.652 -55.006  1.00 85.83           C  
ANISOU 1294  CB  CYS B 181    12059   9967  10586    361   -215   -185       C  
ATOM   1295  SG  CYS B 181     -14.836  11.426 -53.610  1.00108.44           S  
ANISOU 1295  SG  CYS B 181    14853  12882  13468    376   -273   -217       S  
ATOM   1296  N   TYR B 182     -12.834  13.690 -56.068  1.00 92.90           N  
ANISOU 1296  N   TYR B 182    13090  10812  11395    293   -290   -218       N  
ATOM   1297  CA  TYR B 182     -11.759  14.675 -56.093  1.00 86.95           C  
ANISOU 1297  CA  TYR B 182    12354  10074  10608    263   -285   -205       C  
ATOM   1298  C   TYR B 182     -12.266  16.039 -55.656  1.00 85.39           C  
ANISOU 1298  C   TYR B 182    12163   9880  10401    255   -356   -245       C  
ATOM   1299  O   TYR B 182     -13.463  16.336 -55.721  1.00 84.29           O  
ANISOU 1299  O   TYR B 182    12043   9710  10272    268   -417   -287       O  
ATOM   1300  CB  TYR B 182     -11.144  14.792 -57.483  1.00 86.99           C  
ANISOU 1300  CB  TYR B 182    12451  10017  10583    240   -269   -196       C  
ATOM   1301  CG  TYR B 182     -12.034  15.542 -58.433  1.00 95.64           C  
ANISOU 1301  CG  TYR B 182    13635  11039  11664    235   -337   -242       C  
ATOM   1302  CD1 TYR B 182     -13.325  15.102 -58.687  1.00 97.25           C  
ANISOU 1302  CD1 TYR B 182    13855  11205  11891    259   -375   -274       C  
ATOM   1303  CD2 TYR B 182     -11.604  16.703 -59.054  1.00106.12           C  
ANISOU 1303  CD2 TYR B 182    15028  12335  12956    207   -366   -254       C  
ATOM   1304  CE1 TYR B 182     -14.162  15.773 -59.540  1.00103.47           C  
ANISOU 1304  CE1 TYR B 182    14722  11925  12666    255   -438   -317       C  
ATOM   1305  CE2 TYR B 182     -12.438  17.389 -59.920  1.00109.11           C  
ANISOU 1305  CE2 TYR B 182    15488  12646  13322    203   -430   -297       C  
ATOM   1306  CZ  TYR B 182     -13.721  16.914 -60.158  1.00107.46           C  
ANISOU 1306  CZ  TYR B 182    15294  12400  13136    228   -466   -329       C  
ATOM   1307  OH  TYR B 182     -14.564  17.582 -61.023  1.00102.89           O  
ANISOU 1307  OH  TYR B 182    14796  11754  12545    225   -530   -371       O  
ATOM   1308  N   MET B 183     -11.319  16.871 -55.239  1.00 89.84           N  
ANISOU 1308  N   MET B 183    12712  10481  10944    233   -349   -230       N  
ATOM   1309  CA  MET B 183     -11.610  18.256 -54.923  1.00 88.96           C  
ANISOU 1309  CA  MET B 183    12613  10370  10818    220   -414   -265       C  
ATOM   1310  C   MET B 183     -11.690  19.052 -56.214  1.00 98.04           C  
ANISOU 1310  C   MET B 183    13869  11444  11938    199   -452   -289       C  
ATOM   1311  O   MET B 183     -10.770  19.010 -57.039  1.00 93.40           O  
ANISOU 1311  O   MET B 183    13329  10831  11327    178   -415   -264       O  
ATOM   1312  CB  MET B 183     -10.530  18.828 -54.021  1.00 93.35           C  
ANISOU 1312  CB  MET B 183    13114  10992  11363    204   -390   -240       C  
ATOM   1313  CG  MET B 183     -10.555  18.231 -52.649  1.00 94.04           C  
ANISOU 1313  CG  MET B 183    13096  11156  11478    226   -364   -223       C  
ATOM   1314  SD  MET B 183     -10.608  19.552 -51.453  1.00 84.81           S  
ANISOU 1314  SD  MET B 183    11878  10041  10305    221   -415   -246       S  
ATOM   1315  CE  MET B 183     -12.335  20.008 -51.597  1.00 88.69           C  
ANISOU 1315  CE  MET B 183    12402  10486  10809    239   -502   -307       C  
ATOM   1316  N   ASP B 184     -12.791  19.774 -56.392  1.00 99.44           N  
ANISOU 1316  N   ASP B 184    14084  11584  12116    204   -525   -337       N  
ATOM   1317  CA  ASP B 184     -13.065  20.498 -57.632  1.00101.36           C  
ANISOU 1317  CA  ASP B 184    14429  11750  12333    187   -568   -364       C  
ATOM   1318  C   ASP B 184     -13.176  21.985 -57.304  1.00 96.48           C  
ANISOU 1318  C   ASP B 184    13825  11136  11699    171   -630   -395       C  
ATOM   1319  O   ASP B 184     -14.209  22.460 -56.818  1.00 95.12           O  
ANISOU 1319  O   ASP B 184    13638  10964  11539    184   -690   -434       O  
ATOM   1320  CB  ASP B 184     -14.328  19.954 -58.290  1.00 99.38           C  
ANISOU 1320  CB  ASP B 184    14220  11442  12099    209   -601   -395       C  
ATOM   1321  CG  ASP B 184     -14.889  20.889 -59.349  1.00111.78           C  
ANISOU 1321  CG  ASP B 184    15888  12937  13646    196   -665   -435       C  
ATOM   1322  OD1 ASP B 184     -15.697  21.769 -58.982  1.00112.91           O  
ANISOU 1322  OD1 ASP B 184    16033  13077  13792    199   -731   -475       O  
ATOM   1323  OD2 ASP B 184     -14.547  20.740 -60.552  1.00109.56           O  
ANISOU 1323  OD2 ASP B 184    15683  12600  13343    183   -648   -427       O  
ATOM   1324  N   TYR B 185     -12.116  22.724 -57.565  1.00 89.69           N  
ANISOU 1324  N   TYR B 185    12992  10278  10810    141   -616   -378       N  
ATOM   1325  CA  TYR B 185     -12.134  24.131 -57.217  1.00 99.16           C  
ANISOU 1325  CA  TYR B 185    14200  11484  11993    125   -671   -404       C  
ATOM   1326  C   TYR B 185     -12.943  24.967 -58.178  1.00105.67           C  
ANISOU 1326  C   TYR B 185    15115  12234  12801    117   -740   -448       C  
ATOM   1327  O   TYR B 185     -12.747  26.183 -58.249  1.00 97.12           O  
ANISOU 1327  O   TYR B 185    14063  11141  11697     96   -780   -466       O  
ATOM   1328  CB  TYR B 185     -10.704  24.646 -57.118  1.00104.95           C  
ANISOU 1328  CB  TYR B 185    14926  12247  12703     96   -633   -370       C  
ATOM   1329  CG  TYR B 185      -9.875  23.829 -56.170  1.00104.44           C  
ANISOU 1329  CG  TYR B 185    14772  12256  12654    103   -565   -326       C  
ATOM   1330  CD1 TYR B 185     -10.117  23.877 -54.794  1.00100.63           C  
ANISOU 1330  CD1 TYR B 185    14200  11842  12194    119   -574   -330       C  
ATOM   1331  CD2 TYR B 185      -8.897  22.962 -56.634  1.00105.41           C  
ANISOU 1331  CD2 TYR B 185    14898  12382  12771     96   -491   -281       C  
ATOM   1332  CE1 TYR B 185      -9.375  23.126 -53.902  1.00 99.14           C  
ANISOU 1332  CE1 TYR B 185    13929  11722  12020    127   -513   -291       C  
ATOM   1333  CE2 TYR B 185      -8.153  22.198 -55.741  1.00 96.17           C  
ANISOU 1333  CE2 TYR B 185    13644  11280  11616    104   -430   -242       C  
ATOM   1334  CZ  TYR B 185      -8.400  22.286 -54.383  1.00 89.75           C  
ANISOU 1334  CZ  TYR B 185    12744  10533  10824    119   -441   -246       C  
ATOM   1335  OH  TYR B 185      -7.661  21.530 -53.511  1.00 81.15           O  
ANISOU 1335  OH  TYR B 185    11574   9512   9750    127   -380   -207       O  
ATOM   1336  N   SER B 186     -13.870  24.356 -58.903  1.00105.60           N  
ANISOU 1336  N   SER B 186    15149  12173  12802    134   -756   -468       N  
ATOM   1337  CA  SER B 186     -14.543  25.065 -59.980  1.00106.89           C  
ANISOU 1337  CA  SER B 186    15407  12259  12947    126   -815   -506       C  
ATOM   1338  C   SER B 186     -15.644  25.988 -59.483  1.00105.40           C  
ANISOU 1338  C   SER B 186    15214  12067  12766    134   -896   -556       C  
ATOM   1339  O   SER B 186     -15.916  27.002 -60.136  1.00112.31           O  
ANISOU 1339  O   SER B 186    16160  12893  13620    119   -949   -586       O  
ATOM   1340  CB  SER B 186     -15.095  24.062 -60.986  1.00 90.24           C  
ANISOU 1340  CB  SER B 186    13349  10094  10845    141   -802   -508       C  
ATOM   1341  OG  SER B 186     -14.131  23.052 -61.193  1.00 94.26           O  
ANISOU 1341  OG  SER B 186    13841  10621  11354    139   -722   -460       O  
ATOM   1342  N   MET B 187     -16.288  25.677 -58.355  1.00104.28           N  
ANISOU 1342  N   MET B 187    14993  11974  12654    158   -907   -566       N  
ATOM   1343  CA  MET B 187     -17.102  26.706 -57.732  1.00111.33           C  
ANISOU 1343  CA  MET B 187    15873  12874  13551    162   -980   -609       C  
ATOM   1344  C   MET B 187     -16.234  27.918 -57.431  1.00116.77           C  
ANISOU 1344  C   MET B 187    16564  13588  14216    134   -992   -605       C  
ATOM   1345  O   MET B 187     -16.402  28.986 -58.029  1.00111.49           O  
ANISOU 1345  O   MET B 187    15962  12875  13526    117  -1043   -632       O  
ATOM   1346  CB  MET B 187     -17.762  26.197 -56.450  1.00125.85           C  
ANISOU 1346  CB  MET B 187    17618  14773  15426    191   -983   -615       C  
ATOM   1347  CG  MET B 187     -18.495  27.324 -55.684  1.00120.07           C  
ANISOU 1347  CG  MET B 187    16865  14058  14697    194  -1056   -657       C  
ATOM   1348  SD  MET B 187     -18.889  27.048 -53.928  1.00113.92           S  
ANISOU 1348  SD  MET B 187    15963  13368  13952    220  -1055   -658       S  
ATOM   1349  CE  MET B 187     -18.815  28.724 -53.291  1.00127.81           C  
ANISOU 1349  CE  MET B 187    17719  15150  15694    203  -1118   -688       C  
ATOM   1350  N   VAL B 188     -15.223  27.728 -56.581  1.00117.32           N  
ANISOU 1350  N   VAL B 188    16564  13726  14289    128   -940   -567       N  
ATOM   1351  CA  VAL B 188     -14.567  28.857 -55.931  1.00109.67           C  
ANISOU 1351  CA  VAL B 188    15571  12794  13304    108   -957   -567       C  
ATOM   1352  C   VAL B 188     -13.594  29.577 -56.855  1.00104.28           C  
ANISOU 1352  C   VAL B 188    14959  12075  12587     74   -948   -553       C  
ATOM   1353  O   VAL B 188     -13.370  30.784 -56.694  1.00105.83           O  
ANISOU 1353  O   VAL B 188    15171  12274  12767     55   -987   -570       O  
ATOM   1354  CB  VAL B 188     -13.859  28.382 -54.643  1.00112.57           C  
ANISOU 1354  CB  VAL B 188    15834  13249  13688    116   -906   -533       C  
ATOM   1355  CG1 VAL B 188     -14.848  28.275 -53.476  1.00107.47           C  
ANISOU 1355  CG1 VAL B 188    15116  12648  13072    145   -940   -558       C  
ATOM   1356  CG2 VAL B 188     -13.139  27.051 -54.878  1.00105.82           C  
ANISOU 1356  CG2 VAL B 188    14959  12407  12840    121   -824   -485       C  
ATOM   1357  N   ALA B 189     -12.991  28.875 -57.811  1.00104.68           N  
ANISOU 1357  N   ALA B 189    15054  12093  12626     66   -896   -523       N  
ATOM   1358  CA  ALA B 189     -11.804  29.387 -58.476  1.00108.81           C  
ANISOU 1358  CA  ALA B 189    15625  12600  13119     34   -868   -498       C  
ATOM   1359  C   ALA B 189     -12.073  29.719 -59.930  1.00119.45           C  
ANISOU 1359  C   ALA B 189    17080  13861  14442     21   -895   -515       C  
ATOM   1360  O   ALA B 189     -13.132  29.413 -60.488  1.00118.24           O  
ANISOU 1360  O   ALA B 189    16968  13661  14297     38   -928   -544       O  
ATOM   1361  CB  ALA B 189     -10.655  28.380 -58.400  1.00 99.51           C  
ANISOU 1361  CB  ALA B 189    14408  11458  11942     31   -780   -443       C  
ATOM   1362  N   THR B 190     -11.075  30.377 -60.523  1.00130.49           N  
ANISOU 1362  N   THR B 190    18526  15243  15812    -10   -879   -497       N  
ATOM   1363  CA  THR B 190     -10.827  30.418 -61.960  1.00136.41           C  
ANISOU 1363  CA  THR B 190    19373  15921  16535    -26   -872   -493       C  
ATOM   1364  C   THR B 190      -9.534  29.648 -62.232  1.00116.56           C  
ANISOU 1364  C   THR B 190    16848  13426  14012    -37   -787   -438       C  
ATOM   1365  O   THR B 190      -8.749  29.393 -61.315  1.00109.26           O  
ANISOU 1365  O   THR B 190    15848  12568  13098    -39   -743   -408       O  
ATOM   1366  CB  THR B 190     -10.720  31.865 -62.463  1.00120.88           C  
ANISOU 1366  CB  THR B 190    17473  13916  14541    -52   -925   -516       C  
ATOM   1367  OG1 THR B 190      -9.369  32.328 -62.336  1.00127.02           O  
ANISOU 1367  OG1 THR B 190    18239  14723  15301    -80   -885   -481       O  
ATOM   1368  CG2 THR B 190     -11.629  32.776 -61.626  1.00112.93           C  
ANISOU 1368  CG2 THR B 190    16437  12926  13545    -44   -999   -560       C  
ATOM   1369  N   VAL B 191      -9.300  29.291 -63.498  1.00104.03           N  
ANISOU 1369  N   VAL B 191    15339  11781  12407    -45   -764   -427       N  
ATOM   1370  CA  VAL B 191      -8.316  28.250 -63.815  1.00114.53           C  
ANISOU 1370  CA  VAL B 191    16657  13124  13734    -48   -681   -378       C  
ATOM   1371  C   VAL B 191      -6.899  28.628 -63.379  1.00110.43           C  
ANISOU 1371  C   VAL B 191    16102  12652  13202    -73   -635   -339       C  
ATOM   1372  O   VAL B 191      -6.095  27.748 -63.049  1.00 91.28           O  
ANISOU 1372  O   VAL B 191    13627  10268  10785    -71   -566   -298       O  
ATOM   1373  CB  VAL B 191      -8.359  27.916 -65.320  1.00109.15           C  
ANISOU 1373  CB  VAL B 191    16073  12368  13032    -53   -671   -376       C  
ATOM   1374  CG1 VAL B 191      -7.289  26.884 -65.682  1.00106.63           C  
ANISOU 1374  CG1 VAL B 191    15745  12061  12708    -57   -585   -325       C  
ATOM   1375  CG2 VAL B 191      -9.744  27.438 -65.728  1.00119.67           C  
ANISOU 1375  CG2 VAL B 191    17436  13655  14379    -26   -713   -413       C  
ATOM   1376  N   SER B 192      -6.555  29.918 -63.373  1.00115.77           N  
ANISOU 1376  N   SER B 192    16804  13323  13860    -98   -670   -351       N  
ATOM   1377  CA  SER B 192      -5.233  30.331 -62.900  1.00104.05           C  
ANISOU 1377  CA  SER B 192    15283  11885  12365   -122   -630   -316       C  
ATOM   1378  C   SER B 192      -5.143  30.456 -61.379  1.00 97.30           C  
ANISOU 1378  C   SER B 192    14326  11111  11534   -113   -632   -314       C  
ATOM   1379  O   SER B 192      -4.108  30.107 -60.798  1.00 96.81           O  
ANISOU 1379  O   SER B 192    14205  11101  11475   -120   -574   -275       O  
ATOM   1380  CB  SER B 192      -4.820  31.667 -63.537  1.00105.70           C  
ANISOU 1380  CB  SER B 192    15560  12055  12544   -153   -664   -326       C  
ATOM   1381  OG  SER B 192      -4.497  31.543 -64.906  1.00106.08           O  
ANISOU 1381  OG  SER B 192    15697  12040  12567   -167   -644   -315       O  
ATOM   1382  N   SER B 193      -6.183  30.974 -60.723  1.00100.66           N  
ANISOU 1382  N   SER B 193    14729  11545  11974    -99   -696   -355       N  
ATOM   1383  CA  SER B 193      -6.262  30.961 -59.270  1.00104.86           C  
ANISOU 1383  CA  SER B 193    15162  12151  12530    -85   -700   -356       C  
ATOM   1384  C   SER B 193      -6.639  29.592 -58.702  1.00102.89           C  
ANISOU 1384  C   SER B 193    14848  11938  12309    -54   -661   -342       C  
ATOM   1385  O   SER B 193      -6.684  29.445 -57.478  1.00101.46           O  
ANISOU 1385  O   SER B 193    14580  11822  12149    -40   -657   -339       O  
ATOM   1386  CB  SER B 193      -7.265  32.023 -58.790  1.00106.14           C  
ANISOU 1386  CB  SER B 193    15324  12308  12696    -80   -784   -407       C  
ATOM   1387  OG  SER B 193      -6.642  33.270 -58.491  1.00111.99           O  
ANISOU 1387  OG  SER B 193    16066  13064  13422   -105   -808   -410       O  
ATOM   1388  N   GLU B 194      -6.889  28.584 -59.543  1.00102.02           N  
ANISOU 1388  N   GLU B 194    14774  11789  12201    -42   -632   -332       N  
ATOM   1389  CA  GLU B 194      -7.372  27.300 -59.038  1.00 95.20           C  
ANISOU 1389  CA  GLU B 194    13852  10953  11366    -11   -601   -323       C  
ATOM   1390  C   GLU B 194      -6.347  26.655 -58.112  1.00 97.78           C  
ANISOU 1390  C   GLU B 194    14092  11356  11705    -10   -533   -277       C  
ATOM   1391  O   GLU B 194      -6.686  26.220 -57.005  1.00 95.66           O  
ANISOU 1391  O   GLU B 194    13741  11142  11462     12   -529   -277       O  
ATOM   1392  CB  GLU B 194      -7.718  26.353 -60.194  1.00 96.21           C  
ANISOU 1392  CB  GLU B 194    14040  11022  11491     -2   -579   -318       C  
ATOM   1393  CG  GLU B 194      -8.703  25.249 -59.801  1.00103.77           C  
ANISOU 1393  CG  GLU B 194    14955  11991  12481     33   -577   -327       C  
ATOM   1394  CD  GLU B 194      -9.716  24.906 -60.900  1.00106.67           C  
ANISOU 1394  CD  GLU B 194    15399  12283  12848     45   -608   -355       C  
ATOM   1395  OE1 GLU B 194      -9.282  24.593 -62.023  1.00107.51           O  
ANISOU 1395  OE1 GLU B 194    15571  12343  12936     34   -579   -339       O  
ATOM   1396  OE2 GLU B 194     -10.945  24.987 -60.658  1.00 98.72           O  
ANISOU 1396  OE2 GLU B 194    14388  11264  11858     65   -662   -394       O  
ATOM   1397  N   TRP B 195      -5.084  26.583 -58.543  1.00103.87           N  
ANISOU 1397  N   TRP B 195    14878  12129  12457    -33   -478   -238       N  
ATOM   1398  CA  TRP B 195      -4.061  26.015 -57.676  1.00100.00           C  
ANISOU 1398  CA  TRP B 195    14307  11710  11978    -33   -413   -195       C  
ATOM   1399  C   TRP B 195      -3.916  26.795 -56.394  1.00 93.80           C  
ANISOU 1399  C   TRP B 195    13451  10987  11201    -35   -438   -203       C  
ATOM   1400  O   TRP B 195      -3.399  26.244 -55.423  1.00 93.15           O  
ANISOU 1400  O   TRP B 195    13287  10972  11135    -25   -395   -176       O  
ATOM   1401  CB  TRP B 195      -2.700  25.948 -58.369  1.00 95.56           C  
ANISOU 1401  CB  TRP B 195    13777  11139  11394    -59   -354   -154       C  
ATOM   1402  CG  TRP B 195      -2.107  27.302 -58.591  1.00100.29           C  
ANISOU 1402  CG  TRP B 195    14415  11725  11968    -91   -382   -161       C  
ATOM   1403  CD1 TRP B 195      -2.155  28.036 -59.745  1.00103.46           C  
ANISOU 1403  CD1 TRP B 195    14910  12058  12342   -111   -412   -177       C  
ATOM   1404  CD2 TRP B 195      -1.398  28.097 -57.644  1.00113.65           C  
ANISOU 1404  CD2 TRP B 195    16052  13472  13658   -105   -385   -153       C  
ATOM   1405  NE1 TRP B 195      -1.515  29.237 -59.573  1.00108.19           N  
ANISOU 1405  NE1 TRP B 195    15517  12666  12925   -138   -432   -179       N  
ATOM   1406  CE2 TRP B 195      -1.044  29.300 -58.290  1.00108.55           C  
ANISOU 1406  CE2 TRP B 195    15471  12786  12985   -135   -417   -165       C  
ATOM   1407  CE3 TRP B 195      -1.019  27.911 -56.318  1.00109.75           C  
ANISOU 1407  CE3 TRP B 195    15460  13056  13183    -96   -363   -137       C  
ATOM   1408  CZ2 TRP B 195      -0.338  30.306 -57.651  1.00103.02           C  
ANISOU 1408  CZ2 TRP B 195    14742  12122  12279   -155   -428   -162       C  
ATOM   1409  CZ3 TRP B 195      -0.337  28.916 -55.685  1.00104.85           C  
ANISOU 1409  CZ3 TRP B 195    14812  12472  12556   -115   -376   -135       C  
ATOM   1410  CH2 TRP B 195       0.001  30.102 -56.350  1.00102.29           C  
ANISOU 1410  CH2 TRP B 195    14553  12106  12205   -145   -408   -148       C  
ATOM   1411  N   ALA B 196      -4.335  28.066 -56.362  1.00 96.40           N  
ANISOU 1411  N   ALA B 196    13811  11299  11520    -46   -506   -240       N  
ATOM   1412  CA  ALA B 196      -4.276  28.812 -55.102  1.00 97.50           C  
ANISOU 1412  CA  ALA B 196    13880  11498  11667    -46   -534   -251       C  
ATOM   1413  C   ALA B 196      -5.189  28.195 -54.049  1.00 92.76           C  
ANISOU 1413  C   ALA B 196    13205  10943  11098    -12   -546   -265       C  
ATOM   1414  O   ALA B 196      -4.767  27.970 -52.913  1.00 87.51           O  
ANISOU 1414  O   ALA B 196    12454  10347  10447     -3   -520   -247       O  
ATOM   1415  CB  ALA B 196      -4.632  30.282 -55.314  1.00100.70           C  
ANISOU 1415  CB  ALA B 196    14336  11871  12056    -64   -607   -290       C  
ATOM   1416  N   TRP B 197      -6.427  27.873 -54.421  1.00100.15           N  
ANISOU 1416  N   TRP B 197    14171  11838  12045      9   -584   -297       N  
ATOM   1417  CA  TRP B 197      -7.369  27.299 -53.470  1.00 94.50           C  
ANISOU 1417  CA  TRP B 197    13387  11159  11358     41   -598   -312       C  
ATOM   1418  C   TRP B 197      -6.987  25.882 -53.066  1.00 88.10           C  
ANISOU 1418  C   TRP B 197    12515  10391  10568     60   -526   -272       C  
ATOM   1419  O   TRP B 197      -7.347  25.438 -51.975  1.00 85.99           O  
ANISOU 1419  O   TRP B 197    12168  10179  10325     83   -522   -271       O  
ATOM   1420  CB  TRP B 197      -8.769  27.308 -54.067  1.00 94.71           C  
ANISOU 1420  CB  TRP B 197    13467  11128  11392     57   -656   -356       C  
ATOM   1421  CG  TRP B 197      -9.246  28.678 -54.200  1.00 98.60           C  
ANISOU 1421  CG  TRP B 197    14004  11592  11870     44   -730   -397       C  
ATOM   1422  CD1 TRP B 197      -8.768  29.622 -55.058  1.00 95.39           C  
ANISOU 1422  CD1 TRP B 197    13671  11140  11434     14   -750   -403       C  
ATOM   1423  CD2 TRP B 197     -10.229  29.319 -53.399  1.00 97.62           C  
ANISOU 1423  CD2 TRP B 197    13849  11485  11759     58   -795   -438       C  
ATOM   1424  NE1 TRP B 197      -9.431  30.804 -54.877  1.00 99.72           N  
ANISOU 1424  NE1 TRP B 197    14240  11674  11977     10   -824   -446       N  
ATOM   1425  CE2 TRP B 197     -10.332  30.649 -53.856  1.00101.69           C  
ANISOU 1425  CE2 TRP B 197    14424  11961  12251     37   -854   -469       C  
ATOM   1426  CE3 TRP B 197     -11.054  28.897 -52.355  1.00 91.04           C  
ANISOU 1426  CE3 TRP B 197    12942  10695  10953     88   -810   -453       C  
ATOM   1427  CZ2 TRP B 197     -11.222  31.566 -53.292  1.00 98.87           C  
ANISOU 1427  CZ2 TRP B 197    14058  11609  11900     44   -927   -513       C  
ATOM   1428  CZ3 TRP B 197     -11.941  29.806 -51.803  1.00105.14           C  
ANISOU 1428  CZ3 TRP B 197    14719  12485  12743     95   -882   -497       C  
ATOM   1429  CH2 TRP B 197     -12.017  31.124 -52.269  1.00 95.82           C  
ANISOU 1429  CH2 TRP B 197    13599  11266  11541     73   -940   -527       C  
ATOM   1430  N   GLU B 198      -6.295  25.146 -53.932  1.00 89.49           N  
ANISOU 1430  N   GLU B 198    12726  10541  10735     50   -469   -239       N  
ATOM   1431  CA  GLU B 198      -5.690  23.900 -53.494  1.00 87.00           C  
ANISOU 1431  CA  GLU B 198    12348  10272  10436     63   -395   -195       C  
ATOM   1432  C   GLU B 198      -4.654  24.160 -52.419  1.00 88.00           C  
ANISOU 1432  C   GLU B 198    12399  10473  10563     55   -363   -167       C  
ATOM   1433  O   GLU B 198      -4.584  23.427 -51.425  1.00 87.87           O  
ANISOU 1433  O   GLU B 198    12300  10517  10569     75   -331   -148       O  
ATOM   1434  CB  GLU B 198      -5.056  23.179 -54.673  1.00 90.49           C  
ANISOU 1434  CB  GLU B 198    12847  10669  10864     52   -341   -165       C  
ATOM   1435  CG  GLU B 198      -3.876  22.334 -54.284  1.00 90.18           C  
ANISOU 1435  CG  GLU B 198    12753  10682  10831     50   -260   -113       C  
ATOM   1436  CD  GLU B 198      -3.027  21.923 -55.475  1.00108.59           C  
ANISOU 1436  CD  GLU B 198    15147  12971  13142     31   -210    -83       C  
ATOM   1437  OE1 GLU B 198      -2.656  22.807 -56.307  1.00107.76           O  
ANISOU 1437  OE1 GLU B 198    15113  12821  13009      5   -229    -90       O  
ATOM   1438  OE2 GLU B 198      -2.740  20.700 -55.568  1.00112.86           O  
ANISOU 1438  OE2 GLU B 198    15664  13523  13695     44   -150    -51       O  
ATOM   1439  N   VAL B 199      -3.859  25.221 -52.589  1.00 87.69           N  
ANISOU 1439  N   VAL B 199    12387  10431  10500     25   -374   -165       N  
ATOM   1440  CA  VAL B 199      -2.769  25.497 -51.658  1.00 83.44           C  
ANISOU 1440  CA  VAL B 199    11782   9960   9960     14   -341   -137       C  
ATOM   1441  C   VAL B 199      -3.291  26.087 -50.339  1.00 80.96           C  
ANISOU 1441  C   VAL B 199    11399   9701   9662     29   -386   -162       C  
ATOM   1442  O   VAL B 199      -2.903  25.641 -49.251  1.00 78.91           O  
ANISOU 1442  O   VAL B 199    11054   9511   9418     41   -353   -140       O  
ATOM   1443  CB  VAL B 199      -1.723  26.399 -52.344  1.00 80.92           C  
ANISOU 1443  CB  VAL B 199    11518   9616   9612    -22   -335   -125       C  
ATOM   1444  CG1 VAL B 199      -0.633  26.769 -51.401  1.00 79.59           C  
ANISOU 1444  CG1 VAL B 199    11283   9514   9443    -34   -308   -100       C  
ATOM   1445  CG2 VAL B 199      -1.085  25.658 -53.456  1.00 86.45           C  
ANISOU 1445  CG2 VAL B 199    12269  10276  10300    -33   -279    -93       C  
ATOM   1446  N   GLY B 200      -4.189  27.071 -50.413  1.00 82.10           N  
ANISOU 1446  N   GLY B 200    11578   9815   9801     28   -462   -208       N  
ATOM   1447  CA  GLY B 200      -4.739  27.660 -49.203  1.00 79.42           C  
ANISOU 1447  CA  GLY B 200    11176   9525   9474     42   -508   -235       C  
ATOM   1448  C   GLY B 200      -5.570  26.678 -48.401  1.00 80.76           C  
ANISOU 1448  C   GLY B 200    11279   9731   9674     78   -500   -237       C  
ATOM   1449  O   GLY B 200      -5.407  26.563 -47.182  1.00 83.14           O  
ANISOU 1449  O   GLY B 200    11497  10103   9991     92   -489   -228       O  
ATOM   1450  N   LEU B 201      -6.463  25.943 -49.065  1.00 79.29           N  
ANISOU 1450  N   LEU B 201    11130   9500   9498     94   -505   -249       N  
ATOM   1451  CA  LEU B 201      -7.267  24.984 -48.319  1.00 78.08           C  
ANISOU 1451  CA  LEU B 201    10913   9379   9374    129   -497   -251       C  
ATOM   1452  C   LEU B 201      -6.439  23.806 -47.821  1.00 78.02           C  
ANISOU 1452  C   LEU B 201    10839   9424   9380    138   -417   -201       C  
ATOM   1453  O   LEU B 201      -6.886  23.075 -46.924  1.00 77.62           O  
ANISOU 1453  O   LEU B 201    10717   9419   9354    166   -404   -196       O  
ATOM   1454  CB  LEU B 201      -8.432  24.485 -49.165  1.00 69.22           C  
ANISOU 1454  CB  LEU B 201     9845   8193   8261    144   -523   -277       C  
ATOM   1455  CG  LEU B 201      -9.538  25.511 -49.415  1.00 70.17           C  
ANISOU 1455  CG  LEU B 201    10014   8270   8376    144   -609   -331       C  
ATOM   1456  CD1 LEU B 201     -10.858  24.811 -49.693  1.00 70.22           C  
ANISOU 1456  CD1 LEU B 201    10035   8242   8404    171   -633   -356       C  
ATOM   1457  CD2 LEU B 201      -9.677  26.505 -48.282  1.00 70.36           C  
ANISOU 1457  CD2 LEU B 201     9987   8344   8402    145   -653   -353       C  
ATOM   1458  N   GLY B 202      -5.244  23.618 -48.374  1.00 84.51           N  
ANISOU 1458  N   GLY B 202    11683  10241  10186    116   -363   -164       N  
ATOM   1459  CA  GLY B 202      -4.335  22.600 -47.893  1.00 83.76           C  
ANISOU 1459  CA  GLY B 202    11526  10198  10101    122   -286   -116       C  
ATOM   1460  C   GLY B 202      -3.494  23.073 -46.724  1.00 80.88           C  
ANISOU 1460  C   GLY B 202    11088   9908   9736    117   -273    -99       C  
ATOM   1461  O   GLY B 202      -3.335  22.334 -45.750  1.00 78.52           O  
ANISOU 1461  O   GLY B 202    10707   9670   9456    137   -236    -76       O  
ATOM   1462  N   VAL B 203      -2.946  24.293 -46.798  1.00 84.64           N  
ANISOU 1462  N   VAL B 203    11590  10380  10191     90   -301   -109       N  
ATOM   1463  CA  VAL B 203      -2.133  24.796 -45.690  1.00 84.24           C  
ANISOU 1463  CA  VAL B 203    11469  10399  10139     85   -291    -95       C  
ATOM   1464  C   VAL B 203      -3.013  25.232 -44.530  1.00 81.30           C  
ANISOU 1464  C   VAL B 203    11039  10070   9782    107   -343   -127       C  
ATOM   1465  O   VAL B 203      -2.537  25.290 -43.394  1.00 81.15           O  
ANISOU 1465  O   VAL B 203    10942  10119   9770    114   -327   -113       O  
ATOM   1466  CB  VAL B 203      -1.205  25.956 -46.107  1.00 79.66           C  
ANISOU 1466  CB  VAL B 203    10933   9804   9533     49   -302    -94       C  
ATOM   1467  CG1 VAL B 203      -0.199  26.266 -45.009  1.00 77.81           C  
ANISOU 1467  CG1 VAL B 203    10623   9643   9298     43   -277    -70       C  
ATOM   1468  CG2 VAL B 203      -0.476  25.632 -47.404  1.00 83.99           C  
ANISOU 1468  CG2 VAL B 203    11551  10298  10063     26   -260    -68       C  
ATOM   1469  N   SER B 204      -4.292  25.533 -44.767  1.00 80.09           N  
ANISOU 1469  N   SER B 204    10920   9877   9634    119   -404   -170       N  
ATOM   1470  CA  SER B 204      -5.211  25.595 -43.637  1.00 82.70           C  
ANISOU 1470  CA  SER B 204    11186  10251   9984    147   -441   -195       C  
ATOM   1471  C   SER B 204      -5.202  24.243 -42.944  1.00 78.79           C  
ANISOU 1471  C   SER B 204    10617   9806   9514    175   -385   -164       C  
ATOM   1472  O   SER B 204      -4.643  24.136 -41.854  1.00 77.04           O  
ANISOU 1472  O   SER B 204    10318   9655   9300    182   -359   -144       O  
ATOM   1473  CB  SER B 204      -6.632  25.959 -44.054  1.00 81.48           C  
ANISOU 1473  CB  SER B 204    11080  10045   9835    158   -510   -244       C  
ATOM   1474  OG  SER B 204      -7.549  25.557 -43.048  1.00 81.60           O  
ANISOU 1474  OG  SER B 204    11028  10101   9874    191   -527   -259       O  
ATOM   1475  N   SER B 205      -5.750  23.205 -43.594  1.00 79.14           N  
ANISOU 1475  N   SER B 205    10685   9813   9570    189   -363   -158       N  
ATOM   1476  CA  SER B 205      -5.946  21.887 -42.990  1.00 78.27           C  
ANISOU 1476  CA  SER B 205    10509   9743   9487    218   -315   -133       C  
ATOM   1477  C   SER B 205      -4.784  21.476 -42.097  1.00 79.28           C  
ANISOU 1477  C   SER B 205    10560   9945   9617    218   -254    -89       C  
ATOM   1478  O   SER B 205      -4.966  21.271 -40.892  1.00 77.63           O  
ANISOU 1478  O   SER B 205    10271   9800   9425    240   -252    -86       O  
ATOM   1479  CB  SER B 205      -6.107  20.789 -44.035  1.00 84.63           C  
ANISOU 1479  CB  SER B 205    11359  10497  10298    222   -278   -116       C  
ATOM   1480  OG  SER B 205      -4.871  20.105 -44.227  1.00 83.48           O  
ANISOU 1480  OG  SER B 205    11201  10371  10147    210   -203    -67       O  
ATOM   1481  N   THR B 206      -3.583  21.363 -42.674  1.00 83.77           N  
ANISOU 1481  N   THR B 206    11153  10506  10170    194   -205    -55       N  
ATOM   1482  CA  THR B 206      -2.441  20.911 -41.886  1.00 79.90           C  
ANISOU 1482  CA  THR B 206    10592  10084   9683    193   -143    -11       C  
ATOM   1483  C   THR B 206      -2.079  21.917 -40.792  1.00 80.23           C  
ANISOU 1483  C   THR B 206    10581  10183   9718    189   -171    -21       C  
ATOM   1484  O   THR B 206      -1.728  21.507 -39.675  1.00 80.38           O  
ANISOU 1484  O   THR B 206    10517  10273   9751    205   -141      0       O  
ATOM   1485  CB  THR B 206      -1.250  20.609 -42.805  1.00 78.57           C  
ANISOU 1485  CB  THR B 206    10466   9890   9498    167    -87     26       C  
ATOM   1486  OG1 THR B 206      -0.091  20.293 -42.029  1.00 80.25           O  
ANISOU 1486  OG1 THR B 206    10611  10169   9713    165    -31     67       O  
ATOM   1487  CG2 THR B 206      -0.946  21.774 -43.708  1.00 78.38           C  
ANISOU 1487  CG2 THR B 206    10522   9812   9446    135   -123      7       C  
ATOM   1488  N   THR B 207      -2.219  23.227 -41.043  1.00 73.82           N  
ANISOU 1488  N   THR B 207     9816   9344   8889    170   -231    -55       N  
ATOM   1489  CA  THR B 207      -1.861  24.178 -39.984  1.00 75.54           C  
ANISOU 1489  CA  THR B 207     9983   9618   9102    166   -257    -64       C  
ATOM   1490  C   THR B 207      -2.778  24.035 -38.757  1.00 72.07           C  
ANISOU 1490  C   THR B 207     9469   9229   8683    199   -285    -84       C  
ATOM   1491  O   THR B 207      -2.317  23.724 -37.651  1.00 71.48           O  
ANISOU 1491  O   THR B 207     9313   9227   8619    213   -256    -62       O  
ATOM   1492  CB  THR B 207      -1.832  25.621 -40.518  1.00 86.93           C  
ANISOU 1492  CB  THR B 207    11489  11018  10522    138   -316    -97       C  
ATOM   1493  OG1 THR B 207      -2.891  25.776 -41.476  1.00 82.13           O  
ANISOU 1493  OG1 THR B 207    10956  10337   9911    139   -362   -131       O  
ATOM   1494  CG2 THR B 207      -0.492  25.892 -41.178  1.00 79.95           C  
ANISOU 1494  CG2 THR B 207    10641  10120   9618    105   -277    -66       C  
ATOM   1495  N   VAL B 208      -4.076  24.299 -38.928  1.00 75.41           N  
ANISOU 1495  N   VAL B 208     9920   9617   9113    213   -344   -126       N  
ATOM   1496  CA  VAL B 208      -5.046  24.043 -37.864  1.00 74.50           C  
ANISOU 1496  CA  VAL B 208     9740   9545   9020    247   -368   -144       C  
ATOM   1497  C   VAL B 208      -5.022  22.585 -37.434  1.00 73.72           C  
ANISOU 1497  C   VAL B 208     9583   9484   8944    272   -306   -108       C  
ATOM   1498  O   VAL B 208      -5.142  22.278 -36.245  1.00 75.01           O  
ANISOU 1498  O   VAL B 208     9664   9712   9122    296   -297   -101       O  
ATOM   1499  CB  VAL B 208      -6.462  24.459 -38.302  1.00 73.22           C  
ANISOU 1499  CB  VAL B 208     9627   9330   8862    256   -438   -193       C  
ATOM   1500  CG1 VAL B 208      -6.771  23.919 -39.662  1.00 74.96           C  
ANISOU 1500  CG1 VAL B 208     9926   9474   9081    248   -427   -193       C  
ATOM   1501  CG2 VAL B 208      -7.505  23.889 -37.336  1.00 72.30           C  
ANISOU 1501  CG2 VAL B 208     9445   9252   8772    293   -451   -206       C  
ATOM   1502  N   GLY B 209      -4.931  21.713 -38.416  1.00 76.87           N  
ANISOU 1502  N   GLY B 209    10025   9837   9345    268   -267    -88       N  
ATOM   1503  CA  GLY B 209      -4.889  20.286 -38.197  1.00 75.71           C  
ANISOU 1503  CA  GLY B 209     9832   9714   9219    290   -206    -53       C  
ATOM   1504  C   GLY B 209      -3.689  19.678 -37.525  1.00 74.57           C  
ANISOU 1504  C   GLY B 209     9622   9634   9078    290   -136     -5       C  
ATOM   1505  O   GLY B 209      -3.831  18.772 -36.749  1.00 72.65           O  
ANISOU 1505  O   GLY B 209     9311   9437   8854    316   -103     15       O  
ATOM   1506  N   PHE B 210      -2.496  20.137 -37.855  1.00 77.74           N  
ANISOU 1506  N   PHE B 210    10044  10036   9458    261   -112     16       N  
ATOM   1507  CA  PHE B 210      -1.312  19.535 -37.282  1.00 75.29           C  
ANISOU 1507  CA  PHE B 210     9673   9783   9150    261    -44     63       C  
ATOM   1508  C   PHE B 210      -0.289  20.395 -36.589  1.00 73.55           C  
ANISOU 1508  C   PHE B 210     9418   9612   8915    244    -43     72       C  
ATOM   1509  O   PHE B 210       0.179  20.037 -35.546  1.00 75.20           O  
ANISOU 1509  O   PHE B 210     9550   9890   9133    258    -12     95       O  
ATOM   1510  CB  PHE B 210      -0.598  18.768 -38.363  1.00 77.11           C  
ANISOU 1510  CB  PHE B 210     9951   9974   9375    245     13     97       C  
ATOM   1511  CG  PHE B 210       0.307  17.707 -37.856  1.00 76.79           C  
ANISOU 1511  CG  PHE B 210     9846   9985   9344    253     90    146       C  
ATOM   1512  CD1 PHE B 210      -0.199  16.568 -37.318  1.00 79.74           C  
ANISOU 1512  CD1 PHE B 210    10166  10388   9743    284    118    161       C  
ATOM   1513  CD2 PHE B 210       1.658  17.837 -37.966  1.00 79.81           C  
ANISOU 1513  CD2 PHE B 210    10227  10386   9713    230    133    179       C  
ATOM   1514  CE1 PHE B 210       0.628  15.584 -36.858  1.00 81.27           C  
ANISOU 1514  CE1 PHE B 210    10302  10629   9946    293    189    207       C  
ATOM   1515  CE2 PHE B 210       2.498  16.855 -37.523  1.00 79.62           C  
ANISOU 1515  CE2 PHE B 210    10146  10409   9698    238    204    225       C  
ATOM   1516  CZ  PHE B 210       1.980  15.727 -36.963  1.00 81.39           C  
ANISOU 1516  CZ  PHE B 210    10314  10663   9947    270    231    239       C  
ATOM   1517  N   VAL B 211       0.068  21.530 -37.152  1.00 71.99           N  
ANISOU 1517  N   VAL B 211     9278   9381   8696    215    -78     54       N  
ATOM   1518  CA  VAL B 211       1.146  22.304 -36.528  1.00 75.74           C  
ANISOU 1518  CA  VAL B 211     9718   9902   9156    198    -72     66       C  
ATOM   1519  C   VAL B 211       0.632  23.042 -35.283  1.00 76.80           C  
ANISOU 1519  C   VAL B 211     9794  10089   9296    215   -122     37       C  
ATOM   1520  O   VAL B 211       1.334  23.134 -34.273  1.00 77.75           O  
ANISOU 1520  O   VAL B 211     9847  10277   9419    219   -102     55       O  
ATOM   1521  CB  VAL B 211       1.808  23.292 -37.509  1.00 68.86           C  
ANISOU 1521  CB  VAL B 211     8923   8980   8259    159    -88     59       C  
ATOM   1522  CG1 VAL B 211       0.785  24.089 -38.231  1.00 69.45           C  
ANISOU 1522  CG1 VAL B 211     9072   8991   8327    153   -158     13       C  
ATOM   1523  CG2 VAL B 211       2.800  24.213 -36.790  1.00 82.11           C  
ANISOU 1523  CG2 VAL B 211    10565  10707   9927    143    -92     66       C  
ATOM   1524  N   VAL B 212      -0.582  23.580 -35.320  1.00 76.27           N  
ANISOU 1524  N   VAL B 212     9753   9994   9233    225   -188     -8       N  
ATOM   1525  CA  VAL B 212      -1.137  24.179 -34.105  1.00 77.01           C  
ANISOU 1525  CA  VAL B 212     9787  10140   9333    244   -234    -35       C  
ATOM   1526  C   VAL B 212      -1.343  23.109 -33.034  1.00 75.21           C  
ANISOU 1526  C   VAL B 212     9472   9978   9128    279   -196    -13       C  
ATOM   1527  O   VAL B 212      -0.823  23.268 -31.916  1.00 74.51           O  
ANISOU 1527  O   VAL B 212     9311   9958   9041    288   -186     -1       O  
ATOM   1528  CB  VAL B 212      -2.438  24.951 -34.376  1.00 68.11           C  
ANISOU 1528  CB  VAL B 212     8706   8968   8205    249   -313    -88       C  
ATOM   1529  CG1 VAL B 212      -3.313  24.940 -33.132  1.00 68.03           C  
ANISOU 1529  CG1 VAL B 212     8625   9013   8213    282   -344   -109       C  
ATOM   1530  CG2 VAL B 212      -2.114  26.386 -34.747  1.00 68.95           C  
ANISOU 1530  CG2 VAL B 212     8863   9047   8289    219   -363   -114       C  
ATOM   1531  N   PRO B 213      -2.061  22.010 -33.297  1.00 73.76           N  
ANISOU 1531  N   PRO B 213     9287   9775   8962    300   -175     -6       N  
ATOM   1532  CA  PRO B 213      -2.225  21.022 -32.222  1.00 75.36           C  
ANISOU 1532  CA  PRO B 213     9403  10043   9187    333   -139     17       C  
ATOM   1533  C   PRO B 213      -0.897  20.483 -31.746  1.00 75.01           C  
ANISOU 1533  C   PRO B 213     9306  10054   9142    329    -70     65       C  
ATOM   1534  O   PRO B 213      -0.631  20.486 -30.540  1.00 74.14           O  
ANISOU 1534  O   PRO B 213     9118  10015   9036    345    -61     75       O  
ATOM   1535  CB  PRO B 213      -3.098  19.941 -32.873  1.00 71.17           C  
ANISOU 1535  CB  PRO B 213     8898   9469   8674    350   -124     18       C  
ATOM   1536  CG  PRO B 213      -3.844  20.665 -33.915  1.00 71.88           C  
ANISOU 1536  CG  PRO B 213     9076   9483   8754    334   -181    -22       C  
ATOM   1537  CD  PRO B 213      -2.792  21.575 -34.496  1.00 72.32           C  
ANISOU 1537  CD  PRO B 213     9178   9517   8783    298   -182    -17       C  
ATOM   1538  N   PHE B 214      -0.026  20.069 -32.669  1.00 78.34           N  
ANISOU 1538  N   PHE B 214     9768  10442   9554    306    -21     96       N  
ATOM   1539  CA  PHE B 214       1.130  19.296 -32.241  1.00 79.15           C  
ANISOU 1539  CA  PHE B 214     9817  10595   9660    307     51    145       C  
ATOM   1540  C   PHE B 214       2.083  20.139 -31.409  1.00 79.90           C  
ANISOU 1540  C   PHE B 214     9870  10747   9743    296     48    151       C  
ATOM   1541  O   PHE B 214       2.695  19.630 -30.464  1.00 80.54           O  
ANISOU 1541  O   PHE B 214     9875  10894   9831    309     90    181       O  
ATOM   1542  CB  PHE B 214       1.874  18.681 -33.421  1.00 83.73           C  
ANISOU 1542  CB  PHE B 214    10452  11128  10233    285    104    176       C  
ATOM   1543  CG  PHE B 214       2.826  17.612 -33.004  1.00 82.84           C  
ANISOU 1543  CG  PHE B 214    10281  11064  10129    293    182    227       C  
ATOM   1544  CD1 PHE B 214       2.567  16.860 -31.877  1.00 83.10           C  
ANISOU 1544  CD1 PHE B 214    10231  11160  10182    325    203    242       C  
ATOM   1545  CD2 PHE B 214       4.030  17.442 -33.644  1.00 83.42           C  
ANISOU 1545  CD2 PHE B 214    10379  11125  10190    267    231    261       C  
ATOM   1546  CE1 PHE B 214       3.451  15.894 -31.450  1.00 84.48           C  
ANISOU 1546  CE1 PHE B 214    10351  11382  10366    332    274    289       C  
ATOM   1547  CE2 PHE B 214       4.926  16.481 -33.215  1.00 84.22           C  
ANISOU 1547  CE2 PHE B 214    10426  11273  10300    274    302    308       C  
ATOM   1548  CZ  PHE B 214       4.638  15.710 -32.118  1.00 87.40           C  
ANISOU 1548  CZ  PHE B 214    10746  11737  10723    307    323    321       C  
ATOM   1549  N   THR B 215       2.224  21.422 -31.731  1.00 76.42           N  
ANISOU 1549  N   THR B 215     9474  10279   9283    271     -1    123       N  
ATOM   1550  CA  THR B 215       3.019  22.266 -30.848  1.00 78.39           C  
ANISOU 1550  CA  THR B 215     9678  10584   9522    263    -10    125       C  
ATOM   1551  C   THR B 215       2.308  22.519 -29.534  1.00 80.58           C  
ANISOU 1551  C   THR B 215     9887  10921   9811    292    -47    102       C  
ATOM   1552  O   THR B 215       2.973  22.677 -28.508  1.00 81.09           O  
ANISOU 1552  O   THR B 215     9883  11051   9875    299    -33    117       O  
ATOM   1553  CB  THR B 215       3.318  23.616 -31.461  1.00 79.28           C  
ANISOU 1553  CB  THR B 215     9854  10656   9614    230    -57     99       C  
ATOM   1554  OG1 THR B 215       2.106  24.386 -31.457  1.00 84.84           O  
ANISOU 1554  OG1 THR B 215    10586  11333  10318    237   -132     49       O  
ATOM   1555  CG2 THR B 215       3.895  23.459 -32.885  1.00 78.31           C  
ANISOU 1555  CG2 THR B 215     9811  10466   9478    199    -28    116       C  
ATOM   1556  N   ILE B 216       0.974  22.615 -29.545  1.00 78.91           N  
ANISOU 1556  N   ILE B 216     9690  10684   9608    310    -97     66       N  
ATOM   1557  CA  ILE B 216       0.238  22.703 -28.283  1.00 77.94           C  
ANISOU 1557  CA  ILE B 216     9497  10619   9497    342   -127     47       C  
ATOM   1558  C   ILE B 216       0.602  21.530 -27.379  1.00 76.34           C  
ANISOU 1558  C   ILE B 216     9211  10483   9311    369    -65     87       C  
ATOM   1559  O   ILE B 216       1.033  21.713 -26.239  1.00 76.00           O  
ANISOU 1559  O   ILE B 216     9098  10510   9269    381    -59     96       O  
ATOM   1560  CB  ILE B 216      -1.277  22.756 -28.535  1.00 72.40           C  
ANISOU 1560  CB  ILE B 216     8826   9876   8805    359   -181      6       C  
ATOM   1561  CG1 ILE B 216      -1.704  24.134 -28.999  1.00 79.40           C  
ANISOU 1561  CG1 ILE B 216     9774  10718   9676    339   -255    -40       C  
ATOM   1562  CG2 ILE B 216      -2.012  22.452 -27.272  1.00 70.88           C  
ANISOU 1562  CG2 ILE B 216     8555   9745   8630    396   -193     -2       C  
ATOM   1563  CD1 ILE B 216      -3.202  24.293 -29.002  1.00 79.36           C  
ANISOU 1563  CD1 ILE B 216     9786  10685   9681    359   -313    -83       C  
ATOM   1564  N   MET B 217       0.441  20.302 -27.885  1.00 74.56           N  
ANISOU 1564  N   MET B 217     8993  10237   9100    378    -17    113       N  
ATOM   1565  CA  MET B 217       0.838  19.125 -27.125  1.00 73.07           C  
ANISOU 1565  CA  MET B 217     8730  10107   8927    401     47    155       C  
ATOM   1566  C   MET B 217       2.314  19.141 -26.775  1.00 76.61           C  
ANISOU 1566  C   MET B 217     9144  10601   9366    386     95    192       C  
ATOM   1567  O   MET B 217       2.693  18.665 -25.711  1.00 77.67           O  
ANISOU 1567  O   MET B 217     9199  10804   9508    406    127    216       O  
ATOM   1568  CB  MET B 217       0.522  17.854 -27.899  1.00 79.85           C  
ANISOU 1568  CB  MET B 217     9612  10926   9800    409     91    177       C  
ATOM   1569  CG  MET B 217      -0.863  17.781 -28.443  1.00 79.72           C  
ANISOU 1569  CG  MET B 217     9640  10856   9795    420     47    142       C  
ATOM   1570  SD  MET B 217      -0.983  16.369 -29.539  1.00 77.39           S  
ANISOU 1570  SD  MET B 217     9384  10508   9514    421    102    171       S  
ATOM   1571  CE  MET B 217      -1.403  17.097 -31.135  1.00 80.16           C  
ANISOU 1571  CE  MET B 217     9852  10756   9847    391     56    137       C  
ATOM   1572  N   LEU B 218       3.172  19.629 -27.665  1.00 82.07           N  
ANISOU 1572  N   LEU B 218     9891  11252  10039    351    104    199       N  
ATOM   1573  CA  LEU B 218       4.556  19.835 -27.255  1.00 81.30           C  
ANISOU 1573  CA  LEU B 218     9759  11199   9931    336    141    229       C  
ATOM   1574  C   LEU B 218       4.653  20.912 -26.187  1.00 82.97           C  
ANISOU 1574  C   LEU B 218     9926  11463  10135    340     96    206       C  
ATOM   1575  O   LEU B 218       5.404  20.749 -25.223  1.00 84.18           O  
ANISOU 1575  O   LEU B 218    10010  11684  10290    349    127    230       O  
ATOM   1576  CB  LEU B 218       5.451  20.193 -28.441  1.00 84.41           C  
ANISOU 1576  CB  LEU B 218    10224  11539  10307    297    158    241       C  
ATOM   1577  CG  LEU B 218       5.708  19.084 -29.443  1.00 84.57           C  
ANISOU 1577  CG  LEU B 218    10282  11518  10333    291    215    273       C  
ATOM   1578  CD1 LEU B 218       7.031  19.361 -30.109  1.00 85.87           C  
ANISOU 1578  CD1 LEU B 218    10480  11666  10481    256    250    298       C  
ATOM   1579  CD2 LEU B 218       5.714  17.730 -28.757  1.00 82.47           C  
ANISOU 1579  CD2 LEU B 218     9946  11301  10088    321    272    307       C  
ATOM   1580  N   THR B 219       3.918  22.021 -26.334  1.00 78.10           N  
ANISOU 1580  N   THR B 219     9348  10816   9510    333     24    160       N  
ATOM   1581  CA  THR B 219       3.935  23.057 -25.298  1.00 79.31           C  
ANISOU 1581  CA  THR B 219     9459  11019   9657    338    -22    135       C  
ATOM   1582  C   THR B 219       3.453  22.498 -23.965  1.00 81.36           C  
ANISOU 1582  C   THR B 219     9631  11351   9933    378    -16    139       C  
ATOM   1583  O   THR B 219       4.147  22.607 -22.949  1.00 82.25           O  
ANISOU 1583  O   THR B 219     9676  11530  10043    386      1    155       O  
ATOM   1584  CB  THR B 219       3.091  24.262 -25.725  1.00 79.86           C  
ANISOU 1584  CB  THR B 219     9587  11039   9716    327   -102     83       C  
ATOM   1585  OG1 THR B 219       3.661  24.815 -26.907  1.00 80.59           O  
ANISOU 1585  OG1 THR B 219     9758  11070   9793    289   -105     82       O  
ATOM   1586  CG2 THR B 219       3.071  25.349 -24.667  1.00 86.48           C  
ANISOU 1586  CG2 THR B 219    10383  11928  10549    333   -152     55       C  
ATOM   1587  N   CYS B 220       2.280  21.864 -23.963  1.00 82.47           N  
ANISOU 1587  N   CYS B 220     9769  11477  10088    403    -27    127       N  
ATOM   1588  CA  CYS B 220       1.818  21.159 -22.773  1.00 81.41           C  
ANISOU 1588  CA  CYS B 220     9552  11408   9971    442    -12    136       C  
ATOM   1589  C   CYS B 220       2.888  20.192 -22.262  1.00 80.72           C  
ANISOU 1589  C   CYS B 220     9405  11376   9890    449     65    188       C  
ATOM   1590  O   CYS B 220       3.299  20.279 -21.101  1.00 84.74           O  
ANISOU 1590  O   CYS B 220     9842  11957  10400    465     73    198       O  
ATOM   1591  CB  CYS B 220       0.506  20.424 -23.076  1.00 75.54           C  
ANISOU 1591  CB  CYS B 220     8825  10632   9246    464    -22    122       C  
ATOM   1592  SG  CYS B 220      -1.037  21.335 -22.657  1.00 93.15           S  
ANISOU 1592  SG  CYS B 220    11062  12853  11479    483   -113     61       S  
ATOM   1593  N   TYR B 221       3.385  19.292 -23.125  1.00 82.05           N  
ANISOU 1593  N   TYR B 221     9603  11512  10062    437    121    222       N  
ATOM   1594  CA  TYR B 221       4.331  18.268 -22.676  1.00 82.40           C  
ANISOU 1594  CA  TYR B 221     9590  11605  10114    445    196    273       C  
ATOM   1595  C   TYR B 221       5.585  18.868 -22.056  1.00 82.04           C  
ANISOU 1595  C   TYR B 221     9506  11610  10054    432    209    288       C  
ATOM   1596  O   TYR B 221       6.266  18.192 -21.278  1.00 84.13           O  
ANISOU 1596  O   TYR B 221     9704  11936  10326    446    259    324       O  
ATOM   1597  CB  TYR B 221       4.769  17.357 -23.821  1.00 91.47           C  
ANISOU 1597  CB  TYR B 221    10785  12704  11266    429    250    304       C  
ATOM   1598  CG  TYR B 221       5.675  16.232 -23.352  1.00 92.05           C  
ANISOU 1598  CG  TYR B 221    10799  12828  11349    440    328    356       C  
ATOM   1599  CD1 TYR B 221       5.295  15.407 -22.310  1.00 88.63           C  
ANISOU 1599  CD1 TYR B 221    10289  12453  10933    476    350    371       C  
ATOM   1600  CD2 TYR B 221       6.960  16.078 -23.869  1.00 82.07           C  
ANISOU 1600  CD2 TYR B 221     9550  11557  10075    414    377    390       C  
ATOM   1601  CE1 TYR B 221       6.122  14.400 -21.855  1.00 83.68           C  
ANISOU 1601  CE1 TYR B 221     9607  11874  10316    487    419    419       C  
ATOM   1602  CE2 TYR B 221       7.802  15.085 -23.407  1.00 79.39           C  
ANISOU 1602  CE2 TYR B 221     9155  11266   9745    424    446    437       C  
ATOM   1603  CZ  TYR B 221       7.374  14.248 -22.403  1.00 81.99           C  
ANISOU 1603  CZ  TYR B 221     9410  11650  10091    461    467    451       C  
ATOM   1604  OH  TYR B 221       8.201  13.249 -21.943  1.00 93.21           O  
ANISOU 1604  OH  TYR B 221    10775  13118  11521    471    536    497       O  
ATOM   1605  N   PHE B 222       5.916  20.115 -22.385  1.00 81.34           N  
ANISOU 1605  N   PHE B 222     9460  11498   9948    404    166    263       N  
ATOM   1606  CA  PHE B 222       7.102  20.750 -21.819  1.00 83.83           C  
ANISOU 1606  CA  PHE B 222     9742  11859  10252    390    176    276       C  
ATOM   1607  C   PHE B 222       6.897  21.148 -20.355  1.00 86.30           C  
ANISOU 1607  C   PHE B 222     9976  12247  10566    417    148    262       C  
ATOM   1608  O   PHE B 222       7.525  20.585 -19.446  1.00 84.45           O  
ANISOU 1608  O   PHE B 222     9669  12079  10337    434    191    293       O  
ATOM   1609  CB  PHE B 222       7.466  21.968 -22.659  1.00 80.77           C  
ANISOU 1609  CB  PHE B 222     9425  11419   9844    352    136    252       C  
ATOM   1610  CG  PHE B 222       8.709  22.691 -22.204  1.00 86.12           C  
ANISOU 1610  CG  PHE B 222    10076  12135  10510    334    143    264       C  
ATOM   1611  CD1 PHE B 222       9.969  22.123 -22.378  1.00 91.16           C  
ANISOU 1611  CD1 PHE B 222    10700  12789  11147    320    210    308       C  
ATOM   1612  CD2 PHE B 222       8.621  23.966 -21.649  1.00 93.72           C  
ANISOU 1612  CD2 PHE B 222    11031  13115  11462    329     83    228       C  
ATOM   1613  CE1 PHE B 222      11.117  22.805 -21.986  1.00100.53           C  
ANISOU 1613  CE1 PHE B 222    11863  14009  12323    302    216    318       C  
ATOM   1614  CE2 PHE B 222       9.758  24.659 -21.253  1.00102.77           C  
ANISOU 1614  CE2 PHE B 222    12155  14296  12599    311     88    238       C  
ATOM   1615  CZ  PHE B 222      11.009  24.081 -21.421  1.00107.68           C  
ANISOU 1615  CZ  PHE B 222    12761  14932  13219    297    154    283       C  
ATOM   1616  N   PHE B 223       6.012  22.126 -20.131  1.00 90.43           N  
ANISOU 1616  N   PHE B 223    10514  12761  11085    422     77    215       N  
ATOM   1617  CA  PHE B 223       5.699  22.615 -18.791  1.00 92.33           C  
ANISOU 1617  CA  PHE B 223    10687  13068  11326    447     42    196       C  
ATOM   1618  C   PHE B 223       5.367  21.487 -17.819  1.00 89.58           C  
ANISOU 1618  C   PHE B 223    10262  12780  10996    487     80    220       C  
ATOM   1619  O   PHE B 223       5.566  21.633 -16.602  1.00 90.38           O  
ANISOU 1619  O   PHE B 223    10291  12953  11097    508     77    222       O  
ATOM   1620  CB  PHE B 223       4.535  23.604 -18.882  1.00 90.97           C  
ANISOU 1620  CB  PHE B 223    10551  12863  11150    449    -38    142       C  
ATOM   1621  CG  PHE B 223       4.936  24.970 -19.381  1.00 90.38           C  
ANISOU 1621  CG  PHE B 223    10530  12754  11057    416    -86    114       C  
ATOM   1622  CD1 PHE B 223       5.810  25.107 -20.445  1.00 87.13           C  
ANISOU 1622  CD1 PHE B 223    10176  12295  10636    379    -61    131       C  
ATOM   1623  CD2 PHE B 223       4.388  26.119 -18.824  1.00101.76           C  
ANISOU 1623  CD2 PHE B 223    11965  14208  12491    420   -156     70       C  
ATOM   1624  CE1 PHE B 223       6.176  26.350 -20.903  1.00 94.28           C  
ANISOU 1624  CE1 PHE B 223    11130  13168  11525    348   -104    107       C  
ATOM   1625  CE2 PHE B 223       4.742  27.380 -19.304  1.00 98.42           C  
ANISOU 1625  CE2 PHE B 223    11592  13750  12052    389   -200     45       C  
ATOM   1626  CZ  PHE B 223       5.637  27.489 -20.342  1.00 93.65           C  
ANISOU 1626  CZ  PHE B 223    11043  13100  11439    353   -174     64       C  
ATOM   1627  N   ILE B 224       4.859  20.359 -18.331  1.00 89.56           N  
ANISOU 1627  N   ILE B 224    10272  12749  11007    498    115    238       N  
ATOM   1628  CA  ILE B 224       4.640  19.202 -17.468  1.00 90.22           C  
ANISOU 1628  CA  ILE B 224    10282  12888  11108    534    158    266       C  
ATOM   1629  C   ILE B 224       5.964  18.640 -16.957  1.00 93.89           C  
ANISOU 1629  C   ILE B 224    10693  13408  11572    533    223    313       C  
ATOM   1630  O   ILE B 224       6.056  18.202 -15.803  1.00 94.48           O  
ANISOU 1630  O   ILE B 224    10690  13554  11654    562    244    329       O  
ATOM   1631  CB  ILE B 224       3.787  18.125 -18.174  1.00 78.94           C  
ANISOU 1631  CB  ILE B 224     8883  11414   9697    545    180    273       C  
ATOM   1632  CG1 ILE B 224       2.382  18.668 -18.489  1.00 79.24           C  
ANISOU 1632  CG1 ILE B 224     8963  11407   9738    551    112    225       C  
ATOM   1633  CG2 ILE B 224       3.768  16.820 -17.349  1.00 76.88           C  
ANISOU 1633  CG2 ILE B 224     8547  11211   9455    579    236    311       C  
ATOM   1634  CD1 ILE B 224       1.330  17.604 -18.662  1.00 76.79           C  
ANISOU 1634  CD1 ILE B 224     8650  11077   9449    576    126    229       C  
ATOM   1635  N   ALA B 225       7.017  18.670 -17.777  1.00 94.30           N  
ANISOU 1635  N   ALA B 225    10785  13430  11616    501    256    335       N  
ATOM   1636  CA  ALA B 225       8.273  18.080 -17.315  1.00 95.24           C  
ANISOU 1636  CA  ALA B 225    10852  13601  11735    500    320    381       C  
ATOM   1637  C   ALA B 225       9.046  18.983 -16.341  1.00 93.23           C  
ANISOU 1637  C   ALA B 225    10549  13405  11467    498    302    375       C  
ATOM   1638  O   ALA B 225       9.742  18.470 -15.457  1.00 92.06           O  
ANISOU 1638  O   ALA B 225    10332  13323  11324    514    344    406       O  
ATOM   1639  CB  ALA B 225       9.154  17.697 -18.511  1.00 90.71           C  
ANISOU 1639  CB  ALA B 225    10332  12975  11156    468    367    409       C  
ATOM   1640  N   GLN B 226       8.955  20.309 -16.475  1.00 87.44           N  
ANISOU 1640  N   GLN B 226     9850  12651  10720    480    241    337       N  
ATOM   1641  CA  GLN B 226       9.727  21.191 -15.604  1.00 96.47           C  
ANISOU 1641  CA  GLN B 226    10953  13850  11853    476    223    331       C  
ATOM   1642  C   GLN B 226       9.086  21.391 -14.239  1.00 98.55           C  
ANISOU 1642  C   GLN B 226    11146  14180  12121    512    191    312       C  
ATOM   1643  O   GLN B 226       9.700  22.013 -13.358  1.00106.28           O  
ANISOU 1643  O   GLN B 226    12078  15212  13091    516    179    309       O  
ATOM   1644  CB  GLN B 226       9.937  22.557 -16.257  1.00 99.73           C  
ANISOU 1644  CB  GLN B 226    11428  14216  12250    441    170    298       C  
ATOM   1645  CG  GLN B 226       8.882  23.583 -15.888  1.00 98.20           C  
ANISOU 1645  CG  GLN B 226    11243  14018  12051    451     91    246       C  
ATOM   1646  CD  GLN B 226       9.116  24.910 -16.567  1.00108.69           C  
ANISOU 1646  CD  GLN B 226    12634  15298  13364    416     40    215       C  
ATOM   1647  OE1 GLN B 226       9.997  25.038 -17.424  1.00102.79           O  
ANISOU 1647  OE1 GLN B 226    11932  14514  12610    383     65    233       O  
ATOM   1648  NE2 GLN B 226       8.326  25.910 -16.191  1.00104.16           N  
ANISOU 1648  NE2 GLN B 226    12066  14724  12785    422    -30    170       N  
ATOM   1649  N   THR B 227       7.862  20.911 -14.051  1.00 96.54           N  
ANISOU 1649  N   THR B 227    10883  13921  11878    540    175    298       N  
ATOM   1650  CA  THR B 227       7.338  20.747 -12.710  1.00 95.13           C  
ANISOU 1650  CA  THR B 227    10627  13812  11705    579    163    292       C  
ATOM   1651  C   THR B 227       7.410  19.295 -12.246  1.00 95.92           C  
ANISOU 1651  C   THR B 227    10671  13953  11821    607    230    335       C  
ATOM   1652  O   THR B 227       7.671  19.059 -11.066  1.00104.36           O  
ANISOU 1652  O   THR B 227    11664  15095  12892    633    246    349       O  
ATOM   1653  CB  THR B 227       5.906  21.281 -12.629  1.00 91.19           C  
ANISOU 1653  CB  THR B 227    10148  13292  11208    595     96    244       C  
ATOM   1654  OG1 THR B 227       5.085  20.558 -13.543  1.00 90.62           O  
ANISOU 1654  OG1 THR B 227    10123  13160  11148    595    105    245       O  
ATOM   1655  CG2 THR B 227       5.879  22.770 -13.000  1.00 91.34           C  
ANISOU 1655  CG2 THR B 227    10219  13276  11212    568     28    201       C  
ATOM   1656  N   ILE B 228       7.210  18.385 -13.178  1.00 86.87           N  
ANISOU 1656  N   ILE B 228     9564  12758  10686    601    266    355       N  
ATOM   1657  CA  ILE B 228       7.454  16.989 -12.913  1.00 86.41           C  
ANISOU 1657  CA  ILE B 228     9460  12729  10642    621    336    400       C  
ATOM   1658  C   ILE B 228       8.947  16.849 -12.624  1.00 93.94           C  
ANISOU 1658  C   ILE B 228    10380  13725  11590    608    386    438       C  
ATOM   1659  O   ILE B 228       9.377  15.905 -12.009  1.00105.62           O  
ANISOU 1659  O   ILE B 228    11801  15253  13078    628    439    475       O  
ATOM   1660  CB  ILE B 228       7.294  16.188 -14.199  1.00 98.61           C  
ANISOU 1660  CB  ILE B 228    11067  14205  12197    605    368    416       C  
ATOM   1661  CG1 ILE B 228       5.851  15.850 -14.470  1.00 98.44           C  
ANISOU 1661  CG1 ILE B 228    11068  14147  12188    623    340    392       C  
ATOM   1662  CG2 ILE B 228       8.076  14.890 -14.149  1.00105.22           C  
ANISOU 1662  CG2 ILE B 228    11868  15067  13045    612    449    470       C  
ATOM   1663  CD1 ILE B 228       5.720  14.824 -15.567  1.00 96.12           C  
ANISOU 1663  CD1 ILE B 228    10820  13796  11907    614    383    415       C  
ATOM   1664  N   ALA B 229       9.734  17.764 -13.162  1.00100.67           N  
ANISOU 1664  N   ALA B 229    11273  14550  12425    574    370    429       N  
ATOM   1665  CA  ALA B 229      11.165  17.786 -13.047  1.00101.32           C  
ANISOU 1665  CA  ALA B 229    11335  14661  12501    556    411    460       C  
ATOM   1666  C   ALA B 229      11.714  17.474 -11.686  1.00 96.42           C  
ANISOU 1666  C   ALA B 229    10624  14130  11883    583    438    483       C  
ATOM   1667  O   ALA B 229      12.324  16.430 -11.491  1.00 96.36           O  
ANISOU 1667  O   ALA B 229    10578  14152  11884    593    502    526       O  
ATOM   1668  CB  ALA B 229      11.668  19.138 -13.497  1.00100.94           C  
ANISOU 1668  CB  ALA B 229    11334  14584  12435    522    367    433       C  
ATOM   1669  N   MET B1001      11.524  18.391 -10.747  1.00 95.09           N  
ANISOU 1669  N   MET B1001    10419  14004  11706    596    388    454       N  
ATOM   1670  CA  MET B1001      12.063  18.188  -9.414  1.00101.21           C  
ANISOU 1670  CA  MET B1001    11108  14866  12482    622    409    473       C  
ATOM   1671  C   MET B1001      11.370  17.038  -8.735  1.00 98.28           C  
ANISOU 1671  C   MET B1001    10683  14533  12126    662    439    491       C  
ATOM   1672  O   MET B1001      10.191  16.838  -8.922  1.00104.96           O  
ANISOU 1672  O   MET B1001    11548  15352  12981    676    415    472       O  
ATOM   1673  CB  MET B1001      12.032  19.452  -8.595  1.00 97.24           C  
ANISOU 1673  CB  MET B1001    10583  14400  11966    626    349    436       C  
ATOM   1674  CG  MET B1001      13.400  19.754  -8.025  1.00 89.81           C  
ANISOU 1674  CG  MET B1001     9599  13508  11017    617    373    457       C  
ATOM   1675  SD  MET B1001      13.892  21.394  -8.510  1.00118.86           S  
ANISOU 1675  SD  MET B1001    13332  17152  14678    577    314    421       S  
ATOM   1676  CE  MET B1001      12.274  22.068  -8.829  1.00108.24           C  
ANISOU 1676  CE  MET B1001    12036  15759  13332    584    237    366       C  
ATOM   1677  N   LYS B1002      12.089  16.332  -7.879  1.00 96.41           N  
ANISOU 1677  N   LYS B1002    10375  14362  11893    681    490    529       N  
ATOM   1678  CA  LYS B1002      11.564  15.088  -7.322  1.00101.39           C  
ANISOU 1678  CA  LYS B1002    10956  15027  12540    718    529    554       C  
ATOM   1679  C   LYS B1002      11.378  15.190  -5.808  1.00 97.79           C  
ANISOU 1679  C   LYS B1002    10417  14655  12083    755    516    550       C  
ATOM   1680  O   LYS B1002      12.272  15.668  -5.097  1.00 95.50           O  
ANISOU 1680  O   LYS B1002    10087  14417  11783    755    517    556       O  
ATOM   1681  CB  LYS B1002      12.500  13.919  -7.642  1.00 98.36           C  
ANISOU 1681  CB  LYS B1002    10558  14648  12165    712    609    608       C  
ATOM   1682  CG  LYS B1002      12.820  13.741  -9.113  1.00 93.74           C  
ANISOU 1682  CG  LYS B1002    10052  13985  11581    675    630    617       C  
ATOM   1683  CD  LYS B1002      11.573  13.597  -9.959  1.00 96.23           C  
ANISOU 1683  CD  LYS B1002    10425  14233  11904    674    602    592       C  
ATOM   1684  CE  LYS B1002      11.933  13.479 -11.436  1.00 95.45           C  
ANISOU 1684  CE  LYS B1002    10407  14057  11805    637    621    600       C  
ATOM   1685  NZ  LYS B1002      10.812  13.871 -12.327  1.00 90.41           N  
ANISOU 1685  NZ  LYS B1002     9838  13346  11166    628    573    563       N  
ATOM   1686  N   LYS B1003      10.224  14.723  -5.318  1.00 91.13           N  
ANISOU 1686  N   LYS B1003     9547  13826  11250    789    504    541       N  
ATOM   1687  CA  LYS B1003      10.057  14.445  -3.897  1.00 87.67           C  
ANISOU 1687  CA  LYS B1003     9025  13471  10815    829    509    549       C  
ATOM   1688  C   LYS B1003      11.004  13.331  -3.470  1.00 87.25           C  
ANISOU 1688  C   LYS B1003     8918  13466  10769    841    585    603       C  
ATOM   1689  O   LYS B1003      11.534  12.573  -4.280  1.00 87.22           O  
ANISOU 1689  O   LYS B1003     8939  13428  10772    823    635    634       O  
ATOM   1690  CB  LYS B1003       8.629  14.004  -3.562  1.00 82.17           C  
ANISOU 1690  CB  LYS B1003     8314  12775  10131    862    489    533       C  
ATOM   1691  CG  LYS B1003       7.525  15.008  -3.820  1.00 90.86           C  
ANISOU 1691  CG  LYS B1003     9459  13837  11227    858    413    479       C  
ATOM   1692  CD  LYS B1003       6.175  14.282  -3.812  1.00 96.05           C  
ANISOU 1692  CD  LYS B1003    10113  14479  11901    885    409    473       C  
ATOM   1693  CE  LYS B1003       5.015  15.203  -4.151  1.00 94.55           C  
ANISOU 1693  CE  LYS B1003     9970  14244  11708    882    335    420       C  
ATOM   1694  NZ  LYS B1003       4.358  15.626  -2.895  1.00 99.14           N  
ANISOU 1694  NZ  LYS B1003    10495  14888  12287    917    297    397       N  
ATOM   1695  N   TYR B1004      11.176  13.207  -2.164  1.00 96.54           N  
ANISOU 1695  N   TYR B1004    10016  14722  11944    873    592    613       N  
ATOM   1696  CA  TYR B1004      12.138  12.254  -1.617  1.00 96.04           C  
ANISOU 1696  CA  TYR B1004     9894  14712  11885    886    661    663       C  
ATOM   1697  C   TYR B1004      11.675  11.842  -0.224  1.00 92.82           C  
ANISOU 1697  C   TYR B1004     9405  14382  11481    933    664    669       C  
ATOM   1698  O   TYR B1004      11.469  12.710   0.630  1.00 90.62           O  
ANISOU 1698  O   TYR B1004     9098  14144  11191    947    617    640       O  
ATOM   1699  CB  TYR B1004      13.521  12.895  -1.578  1.00 95.00           C  
ANISOU 1699  CB  TYR B1004     9758  14597  11738    861    669    671       C  
ATOM   1700  CG  TYR B1004      14.422  12.522  -2.730  1.00 94.47           C  
ANISOU 1700  CG  TYR B1004     9740  14479  11673    824    713    698       C  
ATOM   1701  CD1 TYR B1004      15.189  11.372  -2.685  1.00 91.87           C  
ANISOU 1701  CD1 TYR B1004     9379  14173  11354    830    786    748       C  
ATOM   1702  CD2 TYR B1004      14.513  13.323  -3.846  1.00 97.36           C  
ANISOU 1702  CD2 TYR B1004    10183  14776  12032    785    682    674       C  
ATOM   1703  CE1 TYR B1004      16.022  11.032  -3.702  1.00 92.53           C  
ANISOU 1703  CE1 TYR B1004     9506  14213  11440    797    827    773       C  
ATOM   1704  CE2 TYR B1004      15.345  12.987  -4.882  1.00 96.17           C  
ANISOU 1704  CE2 TYR B1004    10077  14581  11884    752    724    699       C  
ATOM   1705  CZ  TYR B1004      16.102  11.838  -4.797  1.00 93.45           C  
ANISOU 1705  CZ  TYR B1004     9697  14260  11548    759    796    748       C  
ATOM   1706  OH  TYR B1004      16.940  11.483  -5.825  1.00 99.10           O  
ANISOU 1706  OH  TYR B1004    10456  14932  12265    727    839    774       O  
ATOM   1707  N   THR B1005      11.492  10.537   0.006  1.00 84.98           N  
ANISOU 1707  N   THR B1005     8376  13409  10505    957    719    706       N  
ATOM   1708  CA  THR B1005      11.038  10.037   1.297  1.00 85.89           C  
ANISOU 1708  CA  THR B1005     8413  13596  10624   1002    727    717       C  
ATOM   1709  C   THR B1005      12.211   9.482   2.098  1.00 85.83           C  
ANISOU 1709  C   THR B1005     8340  13658  10615   1015    782    759       C  
ATOM   1710  O   THR B1005      13.059   8.756   1.562  1.00 86.79           O  
ANISOU 1710  O   THR B1005     8470  13765  10743    999    838    797       O  
ATOM   1711  CB  THR B1005       9.941   8.972   1.158  1.00 84.01           C  
ANISOU 1711  CB  THR B1005     8172  13341  10408   1026    747    728       C  
ATOM   1712  OG1 THR B1005      10.521   7.718   0.803  1.00 84.53           O  
ANISOU 1712  OG1 THR B1005     8228  13402  10488   1024    820    777       O  
ATOM   1713  CG2 THR B1005       8.889   9.362   0.148  1.00 80.34           C  
ANISOU 1713  CG2 THR B1005     7781  12798   9948   1009    703    692       C  
ATOM   1714  N   CYS B1006      12.261   9.854   3.380  1.00 87.80           N  
ANISOU 1714  N   CYS B1006     8525  13980  10854   1044    764    752       N  
ATOM   1715  CA  CYS B1006      13.241   9.293   4.295  1.00 88.74           C  
ANISOU 1715  CA  CYS B1006     8574  14172  10971   1063    813    791       C  
ATOM   1716  C   CYS B1006      12.876   7.848   4.603  1.00 88.68           C  
ANISOU 1716  C   CYS B1006     8525  14187  10983   1093    870    831       C  
ATOM   1717  O   CYS B1006      11.805   7.568   5.158  1.00 89.35           O  
ANISOU 1717  O   CYS B1006     8584  14290  11075   1125    855    822       O  
ATOM   1718  CB  CYS B1006      13.307  10.107   5.579  1.00 90.91           C  
ANISOU 1718  CB  CYS B1006     8794  14519  11230   1087    774    770       C  
ATOM   1719  SG  CYS B1006      14.096   9.181   6.905  1.00 89.08           S  
ANISOU 1719  SG  CYS B1006     8465  14383  10999   1125    834    818       S  
ATOM   1720  N   THR B1007      13.771   6.933   4.244  1.00 84.18           N  
ANISOU 1720  N   THR B1007     7950  13615  10421   1083    935    876       N  
ATOM   1721  CA  THR B1007      13.458   5.519   4.332  1.00 85.25           C  
ANISOU 1721  CA  THR B1007     8055  13759  10576   1106    991    915       C  
ATOM   1722  C   THR B1007      13.389   5.014   5.771  1.00 91.09           C  
ANISOU 1722  C   THR B1007     8708  14586  11317   1152   1011    936       C  
ATOM   1723  O   THR B1007      12.863   3.916   5.993  1.00 97.99           O  
ANISOU 1723  O   THR B1007     9553  15472  12208   1178   1048    962       O  
ATOM   1724  CB  THR B1007      14.501   4.736   3.537  1.00 90.51           C  
ANISOU 1724  CB  THR B1007     8741  14398  11250   1081   1055    957       C  
ATOM   1725  OG1 THR B1007      14.042   3.400   3.331  1.00 91.36           O  
ANISOU 1725  OG1 THR B1007     8838  14495  11379   1098   1104    989       O  
ATOM   1726  CG2 THR B1007      15.772   4.672   4.312  1.00 93.10           C  
ANISOU 1726  CG2 THR B1007     9014  14792  11569   1087   1088    985       C  
ATOM   1727  N   VAL B1008      13.897   5.786   6.734  1.00 87.17           N  
ANISOU 1727  N   VAL B1008     8169  14150  10802   1163    986    924       N  
ATOM   1728  CA  VAL B1008      13.993   5.377   8.143  1.00 88.85           C  
ANISOU 1728  CA  VAL B1008     8296  14450  11012   1206   1005    944       C  
ATOM   1729  C   VAL B1008      12.901   6.020   8.986  1.00 91.26           C  
ANISOU 1729  C   VAL B1008     8578  14786  11310   1236    948    906       C  
ATOM   1730  O   VAL B1008      12.231   5.342   9.767  1.00 87.79           O  
ANISOU 1730  O   VAL B1008     8089  14387  10879   1274    962    919       O  
ATOM   1731  CB  VAL B1008      15.389   5.716   8.720  1.00 84.20           C  
ANISOU 1731  CB  VAL B1008     7670  13913  10408   1201   1022    960       C  
ATOM   1732  CG1 VAL B1008      15.366   5.596  10.216  1.00 86.76           C  
ANISOU 1732  CG1 VAL B1008     7912  14327  10725   1245   1025    968       C  
ATOM   1733  CG2 VAL B1008      16.447   4.798   8.177  1.00 83.43           C  
ANISOU 1733  CG2 VAL B1008     7575  13804  10320   1183   1092   1007       C  
ATOM   1734  N   CYS B1009      12.715   7.338   8.838  1.00 90.86           N  
ANISOU 1734  N   CYS B1009     8563  14716  11245   1218    882    859       N  
ATOM   1735  CA  CYS B1009      11.791   8.086   9.676  1.00 88.56           C  
ANISOU 1735  CA  CYS B1009     8248  14457  10944   1245    824    820       C  
ATOM   1736  C   CYS B1009      10.546   8.596   8.956  1.00 86.78           C  
ANISOU 1736  C   CYS B1009     8082  14167  10724   1235    771    778       C  
ATOM   1737  O   CYS B1009       9.609   9.021   9.635  1.00 87.71           O  
ANISOU 1737  O   CYS B1009     8179  14309  10838   1261    728    749       O  
ATOM   1738  CB  CYS B1009      12.504   9.279  10.320  1.00 86.30           C  
ANISOU 1738  CB  CYS B1009     7944  14212  10635   1241    784    796       C  
ATOM   1739  SG  CYS B1009      12.331  10.772   9.383  1.00 81.55           S  
ANISOU 1739  SG  CYS B1009     7423  13542  10022   1199    712    741       S  
ATOM   1740  N   GLY B1010      10.502   8.584   7.619  1.00 90.85           N  
ANISOU 1740  N   GLY B1010     8670  14601  11247   1198    772    773       N  
ATOM   1741  CA  GLY B1010       9.271   8.795   6.878  1.00 88.44           C  
ANISOU 1741  CA  GLY B1010     8420  14233  10951   1190    733    741       C  
ATOM   1742  C   GLY B1010       9.081  10.187   6.296  1.00 84.98           C  
ANISOU 1742  C   GLY B1010     8042  13747  10498   1160    664    690       C  
ATOM   1743  O   GLY B1010       8.279  10.348   5.357  1.00 81.73           O  
ANISOU 1743  O   GLY B1010     7691  13267  10094   1143    637    666       O  
ATOM   1744  N   TYR B1011       9.793  11.189   6.817  1.00 83.80           N  
ANISOU 1744  N   TYR B1011     7877  13633  10329   1154    634    673       N  
ATOM   1745  CA  TYR B1011       9.616  12.566   6.359  1.00 85.56           C  
ANISOU 1745  CA  TYR B1011     8153  13817  10539   1128    566    623       C  
ATOM   1746  C   TYR B1011       9.893  12.656   4.866  1.00 84.53           C  
ANISOU 1746  C   TYR B1011     8104  13601  10412   1082    571    622       C  
ATOM   1747  O   TYR B1011      10.866  12.085   4.361  1.00 86.20           O  
ANISOU 1747  O   TYR B1011     8323  13800  10628   1062    623    657       O  
ATOM   1748  CB  TYR B1011      10.552  13.505   7.135  1.00 84.23           C  
ANISOU 1748  CB  TYR B1011     7951  13702  10350   1126    544    613       C  
ATOM   1749  CG  TYR B1011      11.034  14.763   6.423  1.00 85.63           C  
ANISOU 1749  CG  TYR B1011     8187  13834  10514   1085    498    579       C  
ATOM   1750  CD1 TYR B1011      10.295  15.945   6.480  1.00 85.89           C  
ANISOU 1750  CD1 TYR B1011     8245  13851  10536   1083    424    527       C  
ATOM   1751  CD2 TYR B1011      12.245  14.781   5.726  1.00 84.86           C  
ANISOU 1751  CD2 TYR B1011     8117  13712  10414   1050    529    601       C  
ATOM   1752  CE1 TYR B1011      10.743  17.111   5.846  1.00 93.59           C  
ANISOU 1752  CE1 TYR B1011     9273  14785  11500   1046    381    497       C  
ATOM   1753  CE2 TYR B1011      12.699  15.938   5.068  1.00 85.27           C  
ANISOU 1753  CE2 TYR B1011     8223  13723  10455   1012    488    571       C  
ATOM   1754  CZ  TYR B1011      11.945  17.100   5.137  1.00 89.85           C  
ANISOU 1754  CZ  TYR B1011     8828  14287  11025   1010    414    520       C  
ATOM   1755  OH  TYR B1011      12.393  18.245   4.507  1.00 91.37           O  
ANISOU 1755  OH  TYR B1011     9071  14438  11206    973    373    491       O  
ATOM   1756  N   ILE B1012       9.033  13.363   4.147  1.00 85.16           N  
ANISOU 1756  N   ILE B1012     8245  13621  10492   1065    517    581       N  
ATOM   1757  CA  ILE B1012       9.203  13.501   2.711  1.00 85.52           C  
ANISOU 1757  CA  ILE B1012     8370  13582  10540   1023    518    576       C  
ATOM   1758  C   ILE B1012       9.687  14.913   2.407  1.00 89.08           C  
ANISOU 1758  C   ILE B1012     8862  14012  10973    991    465    540       C  
ATOM   1759  O   ILE B1012       9.247  15.889   3.027  1.00 91.43           O  
ANISOU 1759  O   ILE B1012     9147  14332  11259   1002    407    502       O  
ATOM   1760  CB  ILE B1012       7.925  13.147   1.923  1.00 85.55           C  
ANISOU 1760  CB  ILE B1012     8424  13523  10560   1023    502    560       C  
ATOM   1761  CG1 ILE B1012       7.333  11.819   2.392  1.00 88.54           C  
ANISOU 1761  CG1 ILE B1012     8755  13929  10957   1058    548    591       C  
ATOM   1762  CG2 ILE B1012       8.263  12.954   0.490  1.00 89.35           C  
ANISOU 1762  CG2 ILE B1012     8978  13925  11046    983    521    569       C  
ATOM   1763  CD1 ILE B1012       5.933  11.559   1.867  1.00 87.31           C  
ANISOU 1763  CD1 ILE B1012     8634  13722  10816   1066    524    570       C  
ATOM   1764  N   TYR B1013      10.600  15.009   1.439  1.00 94.59           N  
ANISOU 1764  N   TYR B1013     9606  14664  11668    952    486    553       N  
ATOM   1765  CA  TYR B1013      11.282  16.244   1.066  1.00 94.69           C  
ANISOU 1765  CA  TYR B1013     9657  14656  11666    919    448    528       C  
ATOM   1766  C   TYR B1013      10.804  16.668  -0.319  1.00 93.19           C  
ANISOU 1766  C   TYR B1013     9557  14374  11477    883    419    503       C  
ATOM   1767  O   TYR B1013      11.293  16.166  -1.331  1.00 93.56           O  
ANISOU 1767  O   TYR B1013     9646  14372  11529    857    458    527       O  
ATOM   1768  CB  TYR B1013      12.795  16.043   1.070  1.00 94.22           C  
ANISOU 1768  CB  TYR B1013     9578  14619  11601    901    497    564       C  
ATOM   1769  CG  TYR B1013      13.546  17.260   0.603  1.00101.61           C  
ANISOU 1769  CG  TYR B1013    10555  15528  12522    864    462    541       C  
ATOM   1770  CD1 TYR B1013      13.868  18.259   1.508  1.00 97.11           C  
ANISOU 1770  CD1 TYR B1013     9950  15008  11939    871    421    517       C  
ATOM   1771  CD2 TYR B1013      13.937  17.417  -0.730  1.00 96.78           C  
ANISOU 1771  CD2 TYR B1013    10018  14843  11911    821    469    543       C  
ATOM   1772  CE1 TYR B1013      14.550  19.385   1.112  1.00 92.54           C  
ANISOU 1772  CE1 TYR B1013     9408  14406  11348    838    388    496       C  
ATOM   1773  CE2 TYR B1013      14.618  18.550  -1.139  1.00 96.99           C  
ANISOU 1773  CE2 TYR B1013    10080  14845  11925    788    437    522       C  
ATOM   1774  CZ  TYR B1013      14.922  19.533  -0.207  1.00 96.98           C  
ANISOU 1774  CZ  TYR B1013    10042  14894  11911    796    396    498       C  
ATOM   1775  OH  TYR B1013      15.602  20.676  -0.557  1.00102.62           O  
ANISOU 1775  OH  TYR B1013    10789  15588  12614    763    362    477       O  
ATOM   1776  N   ASN B1014       9.877  17.593  -0.357  1.00 91.61           N  
ANISOU 1776  N   ASN B1014     9386  14151  11271    884    351    456       N  
ATOM   1777  CA  ASN B1014       9.424  18.192  -1.604  1.00 93.78           C  
ANISOU 1777  CA  ASN B1014     9746  14340  11544    850    314    426       C  
ATOM   1778  C   ASN B1014      10.291  19.399  -1.954  1.00 94.58           C  
ANISOU 1778  C   ASN B1014     9882  14424  11630    815    283    407       C  
ATOM   1779  O   ASN B1014      10.483  20.282  -1.112  1.00 98.93           O  
ANISOU 1779  O   ASN B1014    10400  15019  12169    823    244    384       O  
ATOM   1780  CB  ASN B1014       7.961  18.600  -1.498  1.00101.14           C  
ANISOU 1780  CB  ASN B1014    10694  15254  12479    868    255    383       C  
ATOM   1781  CG  ASN B1014       7.589  19.693  -2.477  1.00100.92           C  
ANISOU 1781  CG  ASN B1014    10747  15155  12444    835    196    341       C  
ATOM   1782  OD1 ASN B1014       7.696  20.863  -2.149  1.00102.98           O  
ANISOU 1782  OD1 ASN B1014    11010  15427  12691    828    144    308       O  
ATOM   1783  ND2 ASN B1014       7.164  19.321  -3.685  1.00101.52           N  
ANISOU 1783  ND2 ASN B1014    10888  15156  12528    815    204    342       N  
ATOM   1784  N   PRO B1015      10.831  19.472  -3.172  1.00 94.14           N  
ANISOU 1784  N   PRO B1015     9891  14304  11573    776    297    415       N  
ATOM   1785  CA  PRO B1015      11.703  20.604  -3.519  1.00 92.44           C  
ANISOU 1785  CA  PRO B1015     9708  14071  11344    741    270    399       C  
ATOM   1786  C   PRO B1015      10.986  21.944  -3.609  1.00 99.04           C  
ANISOU 1786  C   PRO B1015    10581  14879  12169    732    188    343       C  
ATOM   1787  O   PRO B1015      11.666  22.978  -3.567  1.00103.54           O  
ANISOU 1787  O   PRO B1015    11161  15452  12727    711    159    326       O  
ATOM   1788  CB  PRO B1015      12.294  20.190  -4.878  1.00 94.00           C  
ANISOU 1788  CB  PRO B1015     9969  14201  11545    704    310    423       C  
ATOM   1789  CG  PRO B1015      12.179  18.708  -4.907  1.00 94.20           C  
ANISOU 1789  CG  PRO B1015     9969  14236  11585    723    375    464       C  
ATOM   1790  CD  PRO B1015      10.883  18.414  -4.196  1.00 97.56           C  
ANISOU 1790  CD  PRO B1015    10362  14687  12019    762    351    446       C  
ATOM   1791  N   GLU B1016       9.654  21.977  -3.742  1.00 99.92           N  
ANISOU 1791  N   GLU B1016    10715  14964  12286    747    150    314       N  
ATOM   1792  CA  GLU B1016       8.952  23.259  -3.661  1.00101.24           C  
ANISOU 1792  CA  GLU B1016    10909  15114  12443    743     71    261       C  
ATOM   1793  C   GLU B1016       9.107  23.865  -2.274  1.00102.53           C  
ANISOU 1793  C   GLU B1016    11003  15356  12598    769     43    246       C  
ATOM   1794  O   GLU B1016       9.440  25.047  -2.124  1.00 96.77           O  
ANISOU 1794  O   GLU B1016    10283  14629  11856    754     -4    217       O  
ATOM   1795  CB  GLU B1016       7.458  23.108  -3.976  1.00104.29           C  
ANISOU 1795  CB  GLU B1016    11325  15461  12838    757     37    233       C  
ATOM   1796  CG  GLU B1016       7.050  22.953  -5.429  1.00112.01           C  
ANISOU 1796  CG  GLU B1016    12387  16350  13821    729     37    228       C  
ATOM   1797  CD  GLU B1016       5.535  22.855  -5.569  1.00114.72           C  
ANISOU 1797  CD  GLU B1016    12751  16663  14173    747     -1    198       C  
ATOM   1798  OE1 GLU B1016       5.002  21.729  -5.454  1.00115.33           O  
ANISOU 1798  OE1 GLU B1016    12805  16749  14266    771     36    220       O  
ATOM   1799  OE2 GLU B1016       4.882  23.901  -5.805  1.00120.96           O  
ANISOU 1799  OE2 GLU B1016    13581  17421  14956    738    -68    152       O  
ATOM   1800  N   ASP B1017       8.853  23.061  -1.245  1.00 95.24           N  
ANISOU 1800  N   ASP B1017    10008  14497  11681    809     70    265       N  
ATOM   1801  CA  ASP B1017       8.938  23.548   0.121  1.00 93.54           C  
ANISOU 1801  CA  ASP B1017     9724  14359  11457    838     45    252       C  
ATOM   1802  C   ASP B1017      10.394  23.669   0.569  1.00104.56           C  
ANISOU 1802  C   ASP B1017    11082  15801  12846    828     77    279       C  
ATOM   1803  O   ASP B1017      10.787  24.680   1.164  1.00109.45           O  
ANISOU 1803  O   ASP B1017    11683  16451  13453    827     38    255       O  
ATOM   1804  CB  ASP B1017       8.146  22.619   1.045  1.00 84.90           C  
ANISOU 1804  CB  ASP B1017     8569  13317  10373    884     66    265       C  
ATOM   1805  CG  ASP B1017       6.648  22.589   0.726  1.00 92.38           C  
ANISOU 1805  CG  ASP B1017     9547  14225  11328    897     28    235       C  
ATOM   1806  OD1 ASP B1017       6.250  21.872  -0.210  1.00104.48           O  
ANISOU 1806  OD1 ASP B1017    11123  15702  12873    886     53    248       O  
ATOM   1807  OD2 ASP B1017       5.856  23.262   1.418  1.00102.40           O  
ANISOU 1807  OD2 ASP B1017    10798  15518  12592    918    -27    198       O  
ATOM   1808  N   GLY B1018      11.213  22.651   0.284  1.00105.01           N  
ANISOU 1808  N   GLY B1018    11128  15861  12910    822    148    327       N  
ATOM   1809  CA  GLY B1018      12.605  22.658   0.716  1.00 97.48           C  
ANISOU 1809  CA  GLY B1018    10135  14952  11950    814    184    355       C  
ATOM   1810  C   GLY B1018      12.783  22.229   2.169  1.00 99.89           C  
ANISOU 1810  C   GLY B1018    10350  15350  12255    856    203    372       C  
ATOM   1811  O   GLY B1018      11.965  21.500   2.738  1.00 95.43           O  
ANISOU 1811  O   GLY B1018     9748  14814  11697    891    214    379       O  
ATOM   1812  N   ASP B1019      13.896  22.676   2.770  1.00105.29           N  
ANISOU 1812  N   ASP B1019    10996  16080  12929    852    209    381       N  
ATOM   1813  CA  ASP B1019      14.122  22.530   4.209  1.00105.96           C  
ANISOU 1813  CA  ASP B1019    10996  16254  13009    890    216    389       C  
ATOM   1814  C   ASP B1019      14.847  23.777   4.708  1.00103.00           C  
ANISOU 1814  C   ASP B1019    10608  15907  12621    879    172    364       C  
ATOM   1815  O   ASP B1019      15.979  23.703   5.211  1.00105.29           O  
ANISOU 1815  O   ASP B1019    10856  16242  12907    879    203    388       O  
ATOM   1816  CB  ASP B1019      14.920  21.260   4.530  1.00101.44           C  
ANISOU 1816  CB  ASP B1019    10374  15723  12444    904    295    445       C  
ATOM   1817  CG  ASP B1019      15.250  21.125   6.018  1.00101.16           C  
ANISOU 1817  CG  ASP B1019    10251  15782  12404    943    304    456       C  
ATOM   1818  OD1 ASP B1019      14.640  21.852   6.836  1.00 93.53           O  
ANISOU 1818  OD1 ASP B1019     9259  14850  11429    966    250    420       O  
ATOM   1819  OD2 ASP B1019      16.144  20.317   6.353  1.00108.18           O  
ANISOU 1819  OD2 ASP B1019    11098  16710  13297    950    363    499       O  
ATOM   1820  N   PRO B1020      14.218  24.946   4.591  1.00100.19           N  
ANISOU 1820  N   PRO B1020    10286  15525  12257    871    101    314       N  
ATOM   1821  CA  PRO B1020      14.949  26.196   4.819  1.00102.58           C  
ANISOU 1821  CA  PRO B1020    10590  15838  12547    852     58    289       C  
ATOM   1822  C   PRO B1020      15.314  26.411   6.272  1.00104.85           C  
ANISOU 1822  C   PRO B1020    10796  16214  12826    886     50    287       C  
ATOM   1823  O   PRO B1020      16.181  27.244   6.568  1.00106.95           O  
ANISOU 1823  O   PRO B1020    11051  16501  13085    872     30    277       O  
ATOM   1824  CB  PRO B1020      13.962  27.253   4.325  1.00109.60           C  
ANISOU 1824  CB  PRO B1020    11536  16674  13432    839    -16    236       C  
ATOM   1825  CG  PRO B1020      12.622  26.654   4.700  1.00116.66           C  
ANISOU 1825  CG  PRO B1020    12414  17579  14331    875    -23    228       C  
ATOM   1826  CD  PRO B1020      12.759  25.155   4.558  1.00107.07           C  
ANISOU 1826  CD  PRO B1020    11179  16373  13129    887     53    279       C  
ATOM   1827  N   ASP B1021      14.687  25.676   7.183  1.00 98.99           N  
ANISOU 1827  N   ASP B1021     9998  15526  12087    929     65    298       N  
ATOM   1828  CA  ASP B1021      15.030  25.767   8.595  1.00105.07           C  
ANISOU 1828  CA  ASP B1021    10689  16384  12849    965     63    300       C  
ATOM   1829  C   ASP B1021      16.446  25.283   8.859  1.00109.67           C  
ANISOU 1829  C   ASP B1021    11233  17005  13432    959    120    342       C  
ATOM   1830  O   ASP B1021      17.032  25.639   9.890  1.00106.21           O  
ANISOU 1830  O   ASP B1021    10738  16633  12986    977    112    340       O  
ATOM   1831  CB  ASP B1021      14.033  24.945   9.412  1.00100.35           C  
ANISOU 1831  CB  ASP B1021    10042  15830  12254   1012     74    307       C  
ATOM   1832  CG  ASP B1021      12.672  25.601   9.490  1.00106.59           C  
ANISOU 1832  CG  ASP B1021    10856  16603  13042   1026      9    259       C  
ATOM   1833  OD1 ASP B1021      12.234  26.172   8.468  1.00116.22           O  
ANISOU 1833  OD1 ASP B1021    12145  17749  14263    995    -26    233       O  
ATOM   1834  OD2 ASP B1021      12.029  25.512  10.550  1.00 97.41           O  
ANISOU 1834  OD2 ASP B1021     9640  15497  11875   1067     -7    249       O  
ATOM   1835  N   ASN B1022      17.004  24.486   7.945  1.00107.87           N  
ANISOU 1835  N   ASN B1022    11035  16738  13214    934    177    380       N  
ATOM   1836  CA  ASN B1022      18.300  23.850   8.123  1.00 95.25           C  
ANISOU 1836  CA  ASN B1022     9400  15172  11618    929    239    425       C  
ATOM   1837  C   ASN B1022      19.316  24.343   7.113  1.00 90.79           C  
ANISOU 1837  C   ASN B1022     8888  14555  11055    880    247    430       C  
ATOM   1838  O   ASN B1022      20.287  23.650   6.809  1.00 94.65           O  
ANISOU 1838  O   ASN B1022     9369  15044  11549    866    306    471       O  
ATOM   1839  CB  ASN B1022      18.153  22.334   8.058  1.00 97.45           C  
ANISOU 1839  CB  ASN B1022     9658  15459  11909    948    309    471       C  
ATOM   1840  CG  ASN B1022      17.225  21.809   9.139  1.00102.28           C  
ANISOU 1840  CG  ASN B1022    10212  16129  12520    998    306    470       C  
ATOM   1841  OD1 ASN B1022      16.248  21.123   8.857  1.00102.71           O  
ANISOU 1841  OD1 ASN B1022    10281  16161  12584   1011    316    474       O  
ATOM   1842  ND2 ASN B1022      17.528  22.148  10.397  1.00103.66           N  
ANISOU 1842  ND2 ASN B1022    10320  16379  12685   1027    291    464       N  
ATOM   1843  N   GLY B1023      19.108  25.554   6.610  1.00 96.24           N  
ANISOU 1843  N   GLY B1023     9629  15200  11738    854    186    388       N  
ATOM   1844  CA  GLY B1023      19.949  26.140   5.606  1.00100.63           C  
ANISOU 1844  CA  GLY B1023    10239  15700  12294    806    185    388       C  
ATOM   1845  C   GLY B1023      19.425  26.005   4.190  1.00 93.20           C  
ANISOU 1845  C   GLY B1023     9381  14671  11360    774    187    384       C  
ATOM   1846  O   GLY B1023      19.521  26.965   3.425  1.00 93.11           O  
ANISOU 1846  O   GLY B1023     9428  14606  11345    740    148    358       O  
ATOM   1847  N   VAL B1024      18.847  24.856   3.837  1.00 98.77           N  
ANISOU 1847  N   VAL B1024    10093  15360  12075    787    229    409       N  
ATOM   1848  CA  VAL B1024      18.589  24.503   2.432  1.00 97.22           C  
ANISOU 1848  CA  VAL B1024     9972  15082  11886    755    247    417       C  
ATOM   1849  C   VAL B1024      17.202  25.025   2.052  1.00100.08           C  
ANISOU 1849  C   VAL B1024    10381  15399  12247    758    187    374       C  
ATOM   1850  O   VAL B1024      16.174  24.376   2.253  1.00 99.43           O  
ANISOU 1850  O   VAL B1024    10288  15321  12170    785    190    373       O  
ATOM   1851  CB  VAL B1024      18.761  23.003   2.172  1.00 94.77           C  
ANISOU 1851  CB  VAL B1024     9648  14773  11588    765    324    468       C  
ATOM   1852  CG1 VAL B1024      18.057  22.175   3.231  1.00 94.87           C  
ANISOU 1852  CG1 VAL B1024     9595  14847  11604    814    339    478       C  
ATOM   1853  CG2 VAL B1024      18.291  22.627   0.771  1.00 93.12           C  
ANISOU 1853  CG2 VAL B1024     9516  14479  11386    738    336    471       C  
ATOM   1854  N   ASN B1025      17.198  26.232   1.466  1.00104.63           N  
ANISOU 1854  N   ASN B1025    11012  15928  12816    727    133    338       N  
ATOM   1855  CA  ASN B1025      16.129  27.003   0.825  1.00103.47           C  
ANISOU 1855  CA  ASN B1025    10927  15721  12666    715     71    293       C  
ATOM   1856  C   ASN B1025      15.226  26.207  -0.111  1.00105.38           C  
ANISOU 1856  C   ASN B1025    11218  15905  12918    712     90    300       C  
ATOM   1857  O   ASN B1025      15.620  25.145  -0.606  1.00105.91           O  
ANISOU 1857  O   ASN B1025    11289  15958  12993    706    153    342       O  
ATOM   1858  CB  ASN B1025      16.781  28.135   0.039  1.00 99.99           C  
ANISOU 1858  CB  ASN B1025    10542  15231  12219    670     39    273       C  
ATOM   1859  CG  ASN B1025      17.979  27.639  -0.742  1.00103.72           C  
ANISOU 1859  CG  ASN B1025    11035  15678  12696    638    100    315       C  
ATOM   1860  OD1 ASN B1025      18.802  26.906  -0.191  1.00100.18           O  
ANISOU 1860  OD1 ASN B1025    10533  15280  12250    651    154    352       O  
ATOM   1861  ND2 ASN B1025      18.041  27.946  -2.041  1.00109.88           N  
ANISOU 1861  ND2 ASN B1025    11894  16380  13477    599     95    309       N  
ATOM   1862  N   PRO B1026      14.024  26.708  -0.395  1.00102.42           N  
ANISOU 1862  N   PRO B1026    10881  15492  12541    715     35    261       N  
ATOM   1863  CA  PRO B1026      13.117  26.016  -1.327  1.00104.18           C  
ANISOU 1863  CA  PRO B1026    11155  15656  12774    711     47    264       C  
ATOM   1864  C   PRO B1026      13.580  26.071  -2.783  1.00 97.59           C  
ANISOU 1864  C   PRO B1026    10399  14741  11940    666     64    273       C  
ATOM   1865  O   PRO B1026      14.527  26.762  -3.168  1.00103.94           O  
ANISOU 1865  O   PRO B1026    11226  15528  12737    634     60    273       O  
ATOM   1866  CB  PRO B1026      11.788  26.757  -1.139  1.00103.83           C  
ANISOU 1866  CB  PRO B1026    11128  15597  12726    726    -25    213       C  
ATOM   1867  CG  PRO B1026      11.890  27.386   0.216  1.00106.19           C  
ANISOU 1867  CG  PRO B1026    11361  15971  13017    753    -58    195       C  
ATOM   1868  CD  PRO B1026      13.329  27.744   0.386  1.00 98.82           C  
ANISOU 1868  CD  PRO B1026    10408  15063  12077    733    -37    214       C  
ATOM   1869  N   GLY B1027      12.873  25.311  -3.611  1.00100.37           N  
ANISOU 1869  N   GLY B1027    10792  15043  12302    664     84    282       N  
ATOM   1870  CA  GLY B1027      13.218  25.240  -5.014  1.00105.65           C  
ANISOU 1870  CA  GLY B1027    11536  15635  12972    624    103    293       C  
ATOM   1871  C   GLY B1027      14.505  24.507  -5.312  1.00106.02           C  
ANISOU 1871  C   GLY B1027    11572  15689  13022    608    175    342       C  
ATOM   1872  O   GLY B1027      14.877  24.387  -6.494  1.00 96.04           O  
ANISOU 1872  O   GLY B1027    10369  14363  11759    575    196    354       O  
ATOM   1873  N   THR B1028      15.199  24.020  -4.284  1.00101.18           N  
ANISOU 1873  N   THR B1028    10883  15150  12410    630    212    370       N  
ATOM   1874  CA  THR B1028      16.395  23.215  -4.464  1.00 98.36           C  
ANISOU 1874  CA  THR B1028    10508  14807  12058    619    284    419       C  
ATOM   1875  C   THR B1028      16.019  21.749  -4.615  1.00 92.16           C  
ANISOU 1875  C   THR B1028     9710  14022  11286    639    342    455       C  
ATOM   1876  O   THR B1028      15.076  21.261  -3.990  1.00 97.13           O  
ANISOU 1876  O   THR B1028    10305  14679  11921    674    335    449       O  
ATOM   1877  CB  THR B1028      17.332  23.377  -3.279  1.00 90.81           C  
ANISOU 1877  CB  THR B1028     9476  13931  11097    634    296    433       C  
ATOM   1878  OG1 THR B1028      16.576  23.117  -2.103  1.00 95.32           O  
ANISOU 1878  OG1 THR B1028     9985  14562  11669    679    282    424       O  
ATOM   1879  CG2 THR B1028      17.873  24.788  -3.210  1.00 91.12           C  
ANISOU 1879  CG2 THR B1028     9530  13966  11124    611    245    402       C  
ATOM   1880  N   ASP B1029      16.756  21.052  -5.464  1.00 93.06           N  
ANISOU 1880  N   ASP B1029     9850  14103  11404    616    398    491       N  
ATOM   1881  CA  ASP B1029      16.568  19.623  -5.611  1.00 93.88           C  
ANISOU 1881  CA  ASP B1029     9939  14210  11522    634    459    529       C  
ATOM   1882  C   ASP B1029      17.563  18.887  -4.725  1.00 96.75           C  
ANISOU 1882  C   ASP B1029    10226  14645  11888    651    517    571       C  
ATOM   1883  O   ASP B1029      18.485  19.474  -4.154  1.00 95.43           O  
ANISOU 1883  O   ASP B1029    10027  14518  11714    646    513    573       O  
ATOM   1884  CB  ASP B1029      16.698  19.203  -7.079  1.00 91.25           C  
ANISOU 1884  CB  ASP B1029     9680  13798  11193    601    488    544       C  
ATOM   1885  CG  ASP B1029      16.345  17.735  -7.297  1.00109.38           C  
ANISOU 1885  CG  ASP B1029    11966  16090  13505    619    546    579       C  
ATOM   1886  OD1 ASP B1029      15.591  17.180  -6.458  1.00110.80           O  
ANISOU 1886  OD1 ASP B1029    12096  16312  13692    657    546    579       O  
ATOM   1887  OD2 ASP B1029      16.789  17.147  -8.306  1.00 99.26           O  
ANISOU 1887  OD2 ASP B1029    10726  14762  12227    597    589    604       O  
ATOM   1888  N   PHE B1030      17.369  17.570  -4.644  1.00 94.16           N  
ANISOU 1888  N   PHE B1030     9873  14331  11574    673    571    606       N  
ATOM   1889  CA  PHE B1030      17.946  16.778  -3.569  1.00 97.59           C  
ANISOU 1889  CA  PHE B1030    10225  14843  12013    702    619    641       C  
ATOM   1890  C   PHE B1030      19.458  16.602  -3.709  1.00 98.23           C  
ANISOU 1890  C   PHE B1030    10294  14939  12092    681    669    677       C  
ATOM   1891  O   PHE B1030      20.190  16.733  -2.719  1.00 98.62           O  
ANISOU 1891  O   PHE B1030    10281  15054  12137    694    679    688       O  
ATOM   1892  CB  PHE B1030      17.250  15.427  -3.519  1.00 97.46           C  
ANISOU 1892  CB  PHE B1030    10188  14830  12011    730    661    667       C  
ATOM   1893  CG  PHE B1030      17.661  14.590  -2.359  1.00 97.09           C  
ANISOU 1893  CG  PHE B1030    10057  14864  11970    765    706    702       C  
ATOM   1894  CD1 PHE B1030      17.276  14.935  -1.071  1.00 93.15           C  
ANISOU 1894  CD1 PHE B1030     9496  14432  11467    799    675    685       C  
ATOM   1895  CD2 PHE B1030      18.451  13.470  -2.549  1.00 96.28           C  
ANISOU 1895  CD2 PHE B1030     9934  14770  11876    763    779    751       C  
ATOM   1896  CE1 PHE B1030      17.662  14.169   0.009  1.00 93.75           C  
ANISOU 1896  CE1 PHE B1030     9492  14582  11546    831    716    717       C  
ATOM   1897  CE2 PHE B1030      18.846  12.703  -1.477  1.00 91.76           C  
ANISOU 1897  CE2 PHE B1030     9284  14272  11309    795    820    783       C  
ATOM   1898  CZ  PHE B1030      18.450  13.049  -0.189  1.00 90.20           C  
ANISOU 1898  CZ  PHE B1030     9025  14141  11106    830    789    766       C  
ATOM   1899  N   LYS B1031      19.947  16.271  -4.911  1.00 89.28           N  
ANISOU 1899  N   LYS B1031     9215  13745  10961    648    703    697       N  
ATOM   1900  CA  LYS B1031      21.375  15.993  -5.086  1.00 88.06           C  
ANISOU 1900  CA  LYS B1031     9049  13603  10806    628    757    734       C  
ATOM   1901  C   LYS B1031      22.246  17.228  -4.876  1.00 96.98           C  
ANISOU 1901  C   LYS B1031    10179  14746  11924    605    724    715       C  
ATOM   1902  O   LYS B1031      23.454  17.090  -4.626  1.00115.74           O  
ANISOU 1902  O   LYS B1031    12523  17154  14299    597    762    744       O  
ATOM   1903  CB  LYS B1031      21.624  15.402  -6.476  1.00105.73           C  
ANISOU 1903  CB  LYS B1031    11352  15770  13050    598    797    756       C  
ATOM   1904  CG  LYS B1031      21.157  13.972  -6.613  1.00107.04           C  
ANISOU 1904  CG  LYS B1031    11506  15934  13231    620    849    787       C  
ATOM   1905  CD  LYS B1031      22.131  13.051  -5.919  1.00104.48           C  
ANISOU 1905  CD  LYS B1031    11114  15672  12913    636    914    834       C  
ATOM   1906  CE  LYS B1031      21.421  11.858  -5.300  1.00100.43           C  
ANISOU 1906  CE  LYS B1031    10552  15194  12414    676    945    855       C  
ATOM   1907  NZ  LYS B1031      20.891  12.175  -3.934  1.00 99.29           N  
ANISOU 1907  NZ  LYS B1031    10342  15117  12265    713    910    836       N  
ATOM   1908  N   ASP B1032      21.660  18.423  -4.969  1.00 94.38           N  
ANISOU 1908  N   ASP B1032     9883  14392  11585    595    654    669       N  
ATOM   1909  CA  ASP B1032      22.363  19.655  -4.654  1.00 95.03           C  
ANISOU 1909  CA  ASP B1032     9961  14490  11656    578    615    647       C  
ATOM   1910  C   ASP B1032      22.433  19.942  -3.162  1.00100.65           C  
ANISOU 1910  C   ASP B1032    10593  15286  12364    611    595    639       C  
ATOM   1911  O   ASP B1032      23.314  20.706  -2.742  1.00108.11           O  
ANISOU 1911  O   ASP B1032    11515  16258  13301    600    582    633       O  
ATOM   1912  CB  ASP B1032      21.700  20.857  -5.335  1.00 91.57           C  
ANISOU 1912  CB  ASP B1032     9590  13991  11209    554    546    599       C  
ATOM   1913  CG  ASP B1032      21.169  20.538  -6.711  1.00 95.93           C  
ANISOU 1913  CG  ASP B1032    10223  14462  11766    531    553    599       C  
ATOM   1914  OD1 ASP B1032      21.962  20.070  -7.557  1.00101.98           O  
ANISOU 1914  OD1 ASP B1032    11018  15194  12534    505    602    629       O  
ATOM   1915  OD2 ASP B1032      19.962  20.781  -6.941  1.00 99.46           O  
ANISOU 1915  OD2 ASP B1032    10703  14877  12213    539    509    567       O  
ATOM   1916  N   ILE B1033      21.525  19.386  -2.356  1.00 94.95           N  
ANISOU 1916  N   ILE B1033     9827  14604  11647    651    591    636       N  
ATOM   1917  CA  ILE B1033      21.587  19.608  -0.915  1.00 91.51           C  
ANISOU 1917  CA  ILE B1033     9313  14250  11206    685    575    630       C  
ATOM   1918  C   ILE B1033      22.964  19.149  -0.463  1.00 91.37           C  
ANISOU 1918  C   ILE B1033     9246  14282  11190    685    631    670       C  
ATOM   1919  O   ILE B1033      23.328  17.984  -0.683  1.00 90.15           O  
ANISOU 1919  O   ILE B1033     9078  14130  11045    689    695    713       O  
ATOM   1920  CB  ILE B1033      20.486  18.871  -0.137  1.00 92.65           C  
ANISOU 1920  CB  ILE B1033     9414  14432  11356    730    575    630       C  
ATOM   1921  CG1 ILE B1033      19.132  18.972  -0.823  1.00 96.39           C  
ANISOU 1921  CG1 ILE B1033     9944  14847  11833    729    538    600       C  
ATOM   1922  CG2 ILE B1033      20.323  19.504   1.224  1.00 91.19           C  
ANISOU 1922  CG2 ILE B1033     9167  14318  11163    761    534    607       C  
ATOM   1923  CD1 ILE B1033      18.023  18.296  -0.029  1.00 91.58           C  
ANISOU 1923  CD1 ILE B1033     9292  14275  11231    774    535    598       C  
ATOM   1924  N   PRO B1034      23.759  20.044   0.119  1.00 97.13           N  
ANISOU 1924  N   PRO B1034     9948  15046  11911    678    607    659       N  
ATOM   1925  CA  PRO B1034      25.099  19.677   0.590  1.00 95.37           C  
ANISOU 1925  CA  PRO B1034     9675  14871  11689    677    657    695       C  
ATOM   1926  C   PRO B1034      25.121  18.318   1.283  1.00 91.32           C  
ANISOU 1926  C   PRO B1034     9100  14412  11185    713    716    736       C  
ATOM   1927  O   PRO B1034      24.271  18.007   2.120  1.00 89.89           O  
ANISOU 1927  O   PRO B1034     8878  14271  11004    751    703    728       O  
ATOM   1928  CB  PRO B1034      25.442  20.815   1.558  1.00 94.04           C  
ANISOU 1928  CB  PRO B1034     9468  14752  11511    684    606    666       C  
ATOM   1929  CG  PRO B1034      24.704  21.989   1.006  1.00 96.10           C  
ANISOU 1929  CG  PRO B1034     9789  14959  11764    664    536    617       C  
ATOM   1930  CD  PRO B1034      23.427  21.451   0.411  1.00 94.95           C  
ANISOU 1930  CD  PRO B1034     9685  14769  11624    672    531    609       C  
ATOM   1931  N   ASP B1035      26.118  17.507   0.921  1.00 94.63           N  
ANISOU 1931  N   ASP B1035     9513  14832  11612    700    782    780       N  
ATOM   1932  CA  ASP B1035      26.206  16.104   1.309  1.00 92.19           C  
ANISOU 1932  CA  ASP B1035     9156  14558  11312    728    847    824       C  
ATOM   1933  C   ASP B1035      26.349  15.908   2.822  1.00 98.78           C  
ANISOU 1933  C   ASP B1035     9903  15485  12144    769    850    831       C  
ATOM   1934  O   ASP B1035      26.272  14.770   3.309  1.00 92.00           O  
ANISOU 1934  O   ASP B1035     8999  14664  11293    798    898    865       O  
ATOM   1935  CB  ASP B1035      27.366  15.479   0.523  1.00 87.74           C  
ANISOU 1935  CB  ASP B1035     8611  13971  10756    699    911    865       C  
ATOM   1936  CG  ASP B1035      27.345  15.868  -0.977  1.00 94.48           C  
ANISOU 1936  CG  ASP B1035     9555  14735  11610    654    902    854       C  
ATOM   1937  OD1 ASP B1035      26.249  16.032  -1.567  1.00 97.33           O  
ANISOU 1937  OD1 ASP B1035     9965  15045  11969    652    869    829       O  
ATOM   1938  OD2 ASP B1035      28.437  16.014  -1.568  1.00 93.20           O  
ANISOU 1938  OD2 ASP B1035     9414  14551  11447    622    929    872       O  
ATOM   1939  N   ASP B1036      26.536  16.990   3.576  1.00 98.57           N  
ANISOU 1939  N   ASP B1036     9851  15495  12107    774    800    801       N  
ATOM   1940  CA  ASP B1036      26.438  16.956   5.029  1.00 92.30           C  
ANISOU 1940  CA  ASP B1036     8978  14784  11308    816    790    799       C  
ATOM   1941  C   ASP B1036      25.002  17.047   5.529  1.00 94.12           C  
ANISOU 1941  C   ASP B1036     9201  15025  11536    848    746    769       C  
ATOM   1942  O   ASP B1036      24.773  16.945   6.737  1.00 97.04           O  
ANISOU 1942  O   ASP B1036     9506  15464  11901    887    737    768       O  
ATOM   1943  CB  ASP B1036      27.268  18.097   5.629  1.00 97.94           C  
ANISOU 1943  CB  ASP B1036     9668  15533  12011    808    753    778       C  
ATOM   1944  CG  ASP B1036      26.638  19.484   5.412  1.00103.57           C  
ANISOU 1944  CG  ASP B1036    10424  16211  12715    792    674    724       C  
ATOM   1945  OD1 ASP B1036      25.514  19.597   4.876  1.00 99.82           O  
ANISOU 1945  OD1 ASP B1036     9996  15691  12241    791    643    700       O  
ATOM   1946  OD2 ASP B1036      27.277  20.488   5.794  1.00104.15           O  
ANISOU 1946  OD2 ASP B1036    10486  16306  12781    782    640    704       O  
ATOM   1947  N   TRP B1037      24.045  17.293   4.643  1.00 94.13           N  
ANISOU 1947  N   TRP B1037     9266  14959  11538    833    715    744       N  
ATOM   1948  CA  TRP B1037      22.656  17.429   5.054  1.00 90.93           C  
ANISOU 1948  CA  TRP B1037     8858  14559  11131    861    671    714       C  
ATOM   1949  C   TRP B1037      22.164  16.106   5.591  1.00 90.61           C  
ANISOU 1949  C   TRP B1037     8771  14556  11101    899    718    746       C  
ATOM   1950  O   TRP B1037      22.501  15.041   5.060  1.00 88.20           O  
ANISOU 1950  O   TRP B1037     8472  14234  10807    893    779    786       O  
ATOM   1951  CB  TRP B1037      21.783  17.822   3.872  1.00 84.46           C  
ANISOU 1951  CB  TRP B1037     8121  13655  10314    835    637    686       C  
ATOM   1952  CG  TRP B1037      20.376  18.178   4.210  1.00 82.36           C  
ANISOU 1952  CG  TRP B1037     7859  13388  10046    859    582    647       C  
ATOM   1953  CD1 TRP B1037      19.930  19.388   4.629  1.00 84.19           C  
ANISOU 1953  CD1 TRP B1037     8095  13628  10267    862    512    601       C  
ATOM   1954  CD2 TRP B1037      19.229  17.331   4.142  1.00 80.07           C  
ANISOU 1954  CD2 TRP B1037     7571  13086   9765    883    593    652       C  
ATOM   1955  NE1 TRP B1037      18.576  19.353   4.820  1.00 85.37           N  
ANISOU 1955  NE1 TRP B1037     8249  13771  10418    885    478    576       N  
ATOM   1956  CE2 TRP B1037      18.120  18.100   4.526  1.00 80.17           C  
ANISOU 1956  CE2 TRP B1037     7589  13100   9773    899    527    607       C  
ATOM   1957  CE3 TRP B1037      19.033  16.000   3.798  1.00 79.10           C  
ANISOU 1957  CE3 TRP B1037     7445  12952   9657    892    652    690       C  
ATOM   1958  CZ2 TRP B1037      16.836  17.588   4.567  1.00 79.36           C  
ANISOU 1958  CZ2 TRP B1037     7488  12987   9677    923    518    598       C  
ATOM   1959  CZ3 TRP B1037      17.757  15.493   3.846  1.00 78.29           C  
ANISOU 1959  CZ3 TRP B1037     7346  12840   9563    917    642    681       C  
ATOM   1960  CH2 TRP B1037      16.673  16.284   4.228  1.00 78.44           C  
ANISOU 1960  CH2 TRP B1037     7369  12859   9575    932    576    636       C  
ATOM   1961  N   VAL B1038      21.342  16.175   6.633  1.00 88.10           N  
ANISOU 1961  N   VAL B1038     8407  14289  10780    939    688    729       N  
ATOM   1962  CA  VAL B1038      20.721  14.986   7.199  1.00 84.64           C  
ANISOU 1962  CA  VAL B1038     7924  13885  10350    978    726    755       C  
ATOM   1963  C   VAL B1038      19.245  15.262   7.422  1.00 82.82           C  
ANISOU 1963  C   VAL B1038     7703  13647  10120   1000    676    719       C  
ATOM   1964  O   VAL B1038      18.782  16.405   7.379  1.00 83.02           O  
ANISOU 1964  O   VAL B1038     7756  13653  10135    991    610    674       O  
ATOM   1965  CB  VAL B1038      21.370  14.527   8.520  1.00 89.57           C  
ANISOU 1965  CB  VAL B1038     8461  14600  10971   1013    757    782       C  
ATOM   1966  CG1 VAL B1038      22.729  13.898   8.245  1.00 90.27           C  
ANISOU 1966  CG1 VAL B1038     8538  14695  11064    995    822    827       C  
ATOM   1967  CG2 VAL B1038      21.449  15.667   9.525  1.00 97.67           C  
ANISOU 1967  CG2 VAL B1038     9452  15677  11981   1027    701    747       C  
ATOM   1968  N   CYS B1039      18.518  14.183   7.674  1.00 80.91           N  
ANISOU 1968  N   CYS B1039     7435  13418   9888   1030    707    741       N  
ATOM   1969  CA  CYS B1039      17.079  14.242   7.798  1.00 81.87           C  
ANISOU 1969  CA  CYS B1039     7567  13528  10013   1051    669    712       C  
ATOM   1970  C   CYS B1039      16.727  15.202   8.918  1.00 84.70           C  
ANISOU 1970  C   CYS B1039     7886  13941  10357   1077    610    676       C  
ATOM   1971  O   CYS B1039      17.216  15.025  10.040  1.00 92.90           O  
ANISOU 1971  O   CYS B1039     8855  15054  11389   1105    626    692       O  
ATOM   1972  CB  CYS B1039      16.510  12.854   8.084  1.00 86.14           C  
ANISOU 1972  CB  CYS B1039     8072  14088  10568   1084    719    747       C  
ATOM   1973  SG  CYS B1039      14.702  12.792   8.206  1.00 84.82           S  
ANISOU 1973  SG  CYS B1039     7916  13905  10409   1111    677    716       S  
ATOM   1974  N   PRO B1040      15.919  16.230   8.668  1.00 82.30           N  
ANISOU 1974  N   PRO B1040     7622  13602  10046   1068    543    627       N  
ATOM   1975  CA  PRO B1040      15.519  17.125   9.758  1.00 86.11           C  
ANISOU 1975  CA  PRO B1040     8066  14138  10515   1094    486    591       C  
ATOM   1976  C   PRO B1040      14.840  16.403  10.927  1.00 88.89           C  
ANISOU 1976  C   PRO B1040     8348  14556  10869   1146    500    604       C  
ATOM   1977  O   PRO B1040      14.895  16.895  12.071  1.00 91.13           O  
ANISOU 1977  O   PRO B1040     8579  14906  11141   1174    474    589       O  
ATOM   1978  CB  PRO B1040      14.559  18.104   9.069  1.00 86.31           C  
ANISOU 1978  CB  PRO B1040     8156  14100  10537   1075    419    541       C  
ATOM   1979  CG  PRO B1040      14.145  17.438   7.852  1.00 87.69           C  
ANISOU 1979  CG  PRO B1040     8389  14203  10727   1054    445    554       C  
ATOM   1980  CD  PRO B1040      15.294  16.611   7.405  1.00 85.31           C  
ANISOU 1980  CD  PRO B1040     8086  13897  10432   1035    514    602       C  
ATOM   1981  N   LEU B1041      14.230  15.240  10.686  1.00 90.05           N  
ANISOU 1981  N   LEU B1041     8493  14689  11031   1160    542    631       N  
ATOM   1982  CA  LEU B1041      13.432  14.598  11.722  1.00 87.67           C  
ANISOU 1982  CA  LEU B1041     8132  14445  10733   1209    551    639       C  
ATOM   1983  C   LEU B1041      14.220  13.580  12.546  1.00 90.16           C  
ANISOU 1983  C   LEU B1041     8377  14828  11052   1235    616    689       C  
ATOM   1984  O   LEU B1041      14.000  13.475  13.763  1.00 91.57           O  
ANISOU 1984  O   LEU B1041     8491  15079  11224   1275    612    690       O  
ATOM   1985  CB  LEU B1041      12.197  13.939  11.099  1.00 83.83           C  
ANISOU 1985  CB  LEU B1041     7678  13909  10263   1214    555    637       C  
ATOM   1986  CG  LEU B1041      11.121  14.878  10.526  1.00 86.92           C  
ANISOU 1986  CG  LEU B1041     8129  14245  10653   1200    485    585       C  
ATOM   1987  CD1 LEU B1041       9.733  14.277  10.710  1.00 88.85           C  
ANISOU 1987  CD1 LEU B1041     8364  14485  10910   1231    480    580       C  
ATOM   1988  CD2 LEU B1041      11.181  16.293  11.108  1.00 83.78           C  
ANISOU 1988  CD2 LEU B1041     7725  13872  10236   1200    418    540       C  
ATOM   1989  N   CYS B1042      15.138  12.825  11.926  1.00 88.97           N  
ANISOU 1989  N   CYS B1042     8236  14658  10909   1213    675    729       N  
ATOM   1990  CA  CYS B1042      15.917  11.850  12.686  1.00 90.61           C  
ANISOU 1990  CA  CYS B1042     8378  14929  11120   1237    737    777       C  
ATOM   1991  C   CYS B1042      17.418  12.029  12.543  1.00 92.85           C  
ANISOU 1991  C   CYS B1042     8658  15223  11398   1212    764    797       C  
ATOM   1992  O   CYS B1042      18.163  11.779  13.495  1.00102.05           O  
ANISOU 1992  O   CYS B1042     9760  16457  12556   1234    790    820       O  
ATOM   1993  CB  CYS B1042      15.545  10.426  12.274  1.00 81.83           C  
ANISOU 1993  CB  CYS B1042     7266  13798  10028   1246    797    817       C  
ATOM   1994  SG  CYS B1042      15.937  10.053  10.584  1.00 82.87           S  
ANISOU 1994  SG  CYS B1042     7478  13836  10174   1196    829    833       S  
ATOM   1995  N   GLY B1043      17.888  12.447  11.387  1.00 83.14           N  
ANISOU 1995  N   GLY B1043     7492  13927  10169   1167    760    790       N  
ATOM   1996  CA  GLY B1043      19.281  12.756  11.206  1.00 83.76           C  
ANISOU 1996  CA  GLY B1043     7572  14011  10242   1140    779    805       C  
ATOM   1997  C   GLY B1043      20.120  11.705  10.520  1.00 83.09           C  
ANISOU 1997  C   GLY B1043     7497  13905  10170   1121    851    853       C  
ATOM   1998  O   GLY B1043      21.340  11.663  10.764  1.00 83.93           O  
ANISOU 1998  O   GLY B1043     7575  14041  10272   1113    881    876       O  
ATOM   1999  N   VAL B1044      19.514  10.846   9.685  1.00 89.40           N  
ANISOU 1999  N   VAL B1044     8332  14653  10985   1115    880    869       N  
ATOM   2000  CA  VAL B1044      20.262  10.017   8.745  1.00 88.03           C  
ANISOU 2000  CA  VAL B1044     8185  14439  10822   1088    941    908       C  
ATOM   2001  C   VAL B1044      20.640  10.866   7.538  1.00 88.70           C  
ANISOU 2001  C   VAL B1044     8347  14452  10904   1039    915    886       C  
ATOM   2002  O   VAL B1044      19.915  11.792   7.154  1.00 86.26           O  
ANISOU 2002  O   VAL B1044     8083  14103  10589   1026    856    842       O  
ATOM   2003  CB  VAL B1044      19.444   8.778   8.328  1.00 79.76           C  
ANISOU 2003  CB  VAL B1044     7147  13365   9794   1102    980    932       C  
ATOM   2004  CG1 VAL B1044      19.529   7.689   9.398  1.00 82.60           C  
ANISOU 2004  CG1 VAL B1044     7428  13797  10160   1144   1029    971       C  
ATOM   2005  CG2 VAL B1044      17.993   9.154   8.030  1.00 80.79           C  
ANISOU 2005  CG2 VAL B1044     7315  13455   9927   1107    928    893       C  
ATOM   2006  N   GLY B1045      21.808  10.561   6.938  1.00 92.30           N  
ANISOU 2006  N   GLY B1045     8818  14891  11363   1010    961    916       N  
ATOM   2007  CA  GLY B1045      22.295  11.299   5.786  1.00 96.93           C  
ANISOU 2007  CA  GLY B1045     9474  15410  11946    963    944    900       C  
ATOM   2008  C   GLY B1045      21.648  10.866   4.484  1.00 96.12           C  
ANISOU 2008  C   GLY B1045     9441  15225  11854    940    953    900       C  
ATOM   2009  O   GLY B1045      21.092   9.772   4.391  1.00 97.67           O  
ANISOU 2009  O   GLY B1045     9629  15417  12064    959    990    924       O  
ATOM   2010  N   LYS B1046      21.953  11.633   3.452  1.00 96.07           N  
ANISOU 2010  N   LYS B1046     9502  15157  11843    899    930    881       N  
ATOM   2011  CA  LYS B1046      21.345  11.520   2.145  1.00 94.47           C  
ANISOU 2011  CA  LYS B1046     9376  14871  11648    873    926    871       C  
ATOM   2012  C   LYS B1046      21.489  10.124   1.622  1.00 93.70           C  
ANISOU 2012  C   LYS B1046     9280  14755  11565    874    995    916       C  
ATOM   2013  O   LYS B1046      20.743   9.694   0.767  1.00 92.51           O  
ANISOU 2013  O   LYS B1046     9178  14548  11425    867    999    914       O  
ATOM   2014  CB  LYS B1046      22.017  12.501   1.204  1.00 97.14           C  
ANISOU 2014  CB  LYS B1046     9777  15156  11977    826    902    853       C  
ATOM   2015  CG  LYS B1046      22.156  13.898   1.779  1.00 98.04           C  
ANISOU 2015  CG  LYS B1046     9882  15293  12076    822    839    814       C  
ATOM   2016  CD  LYS B1046      23.440  14.089   2.592  1.00 98.55           C  
ANISOU 2016  CD  LYS B1046     9891  15421  12134    825    860    832       C  
ATOM   2017  CE  LYS B1046      23.288  13.937   4.105  1.00 97.89           C  
ANISOU 2017  CE  LYS B1046     9722  15424  12047    870    855    835       C  
ATOM   2018  NZ  LYS B1046      24.001  12.734   4.612  1.00 97.77           N  
ANISOU 2018  NZ  LYS B1046     9650  15459  12040    890    926    885       N  
ATOM   2019  N   ASP B1047      22.381   9.369   2.232  1.00 93.50           N  
ANISOU 2019  N   ASP B1047     9198  14784  11544    889   1050    957       N  
ATOM   2020  CA  ASP B1047      22.665   8.000   1.919  1.00 94.91           C  
ANISOU 2020  CA  ASP B1047     9365  14958  11737    894   1121   1004       C  
ATOM   2021  C   ASP B1047      21.426   7.106   2.019  1.00 94.54           C  
ANISOU 2021  C   ASP B1047     9310  14906  11704    924   1129   1008       C  
ATOM   2022  O   ASP B1047      21.304   6.158   1.284  1.00 88.79           O  
ANISOU 2022  O   ASP B1047     8606  14140  10990    918   1171   1033       O  
ATOM   2023  CB  ASP B1047      23.694   7.558   2.935  1.00 98.11           C  
ANISOU 2023  CB  ASP B1047     9695  15440  12141    914   1163   1038       C  
ATOM   2024  CG  ASP B1047      24.147   6.171   2.725  1.00105.91           C  
ANISOU 2024  CG  ASP B1047    10665  16433  13144    920   1239   1089       C  
ATOM   2025  OD1 ASP B1047      23.732   5.567   1.729  1.00103.50           O  
ANISOU 2025  OD1 ASP B1047    10407  16068  12850    906   1259   1097       O  
ATOM   2026  OD2 ASP B1047      24.928   5.679   3.554  1.00109.46           O  
ANISOU 2026  OD2 ASP B1047    11051  16945  13594    938   1277   1120       O  
ATOM   2027  N   GLN B1048      20.528   7.371   2.953  1.00 96.01           N  
ANISOU 2027  N   GLN B1048     9459  15132  11887    957   1090    985       N  
ATOM   2028  CA  GLN B1048      19.331   6.587   3.124  1.00 88.11           C  
ANISOU 2028  CA  GLN B1048     8448  14130  10900    986   1095    988       C  
ATOM   2029  C   GLN B1048      18.016   7.093   2.537  1.00 86.59           C  
ANISOU 2029  C   GLN B1048     8311  13881  10710    981   1040    946       C  
ATOM   2030  O   GLN B1048      16.980   6.568   2.907  1.00 83.59           O  
ANISOU 2030  O   GLN B1048     7911  13511  10340   1011   1036    944       O  
ATOM   2031  CB  GLN B1048      19.122   6.410   4.599  1.00 81.75           C  
ANISOU 2031  CB  GLN B1048     7560  13409  10091   1031   1093    993       C  
ATOM   2032  CG  GLN B1048      20.320   5.820   5.275  1.00 85.45           C  
ANISOU 2032  CG  GLN B1048     7969  13938  10559   1042   1148   1035       C  
ATOM   2033  CD  GLN B1048      20.300   4.321   5.190  1.00 93.48           C  
ANISOU 2033  CD  GLN B1048     8964  14960  11596   1058   1216   1082       C  
ATOM   2034  OE1 GLN B1048      19.248   3.725   4.975  1.00 94.87           O  
ANISOU 2034  OE1 GLN B1048     9151  15112  11785   1073   1217   1081       O  
ATOM   2035  NE2 GLN B1048      21.459   3.696   5.365  1.00111.37           N  
ANISOU 2035  NE2 GLN B1048    11196  17257  13864   1056   1273   1123       N  
ATOM   2036  N   PHE B1049      18.005   8.087   1.655  1.00 92.05           N  
ANISOU 2036  N   PHE B1049     9069  14513  11391    946    997    913       N  
ATOM   2037  CA  PHE B1049      16.710   8.570   1.200  1.00 87.80           C  
ANISOU 2037  CA  PHE B1049     8578  13926  10855    944    943    872       C  
ATOM   2038  C   PHE B1049      16.231   7.732   0.006  1.00 87.42           C  
ANISOU 2038  C   PHE B1049     8585  13807  10823    930    971    885       C  
ATOM   2039  O   PHE B1049      16.829   6.708  -0.339  1.00 86.31           O  
ANISOU 2039  O   PHE B1049     8439  13663  10693    926   1034    927       O  
ATOM   2040  CB  PHE B1049      16.786  10.061   0.890  1.00 87.38           C  
ANISOU 2040  CB  PHE B1049     8570  13846  10785    917    878    827       C  
ATOM   2041  CG  PHE B1049      16.712  10.935   2.109  1.00 88.98           C  
ANISOU 2041  CG  PHE B1049     8723  14113  10975    939    832    801       C  
ATOM   2042  CD1 PHE B1049      17.654  10.819   3.121  1.00 88.72           C  
ANISOU 2042  CD1 PHE B1049     8622  14153  10936    956    859    824       C  
ATOM   2043  CD2 PHE B1049      15.676  11.842   2.265  1.00 85.72           C  
ANISOU 2043  CD2 PHE B1049     8328  13687  10555    946    763    753       C  
ATOM   2044  CE1 PHE B1049      17.584  11.619   4.232  1.00 88.61           C  
ANISOU 2044  CE1 PHE B1049     8562  14197  10908    977    816    800       C  
ATOM   2045  CE2 PHE B1049      15.598  12.640   3.387  1.00 87.05           C  
ANISOU 2045  CE2 PHE B1049     8450  13915  10711    967    721    729       C  
ATOM   2046  CZ  PHE B1049      16.548  12.525   4.365  1.00 90.15           C  
ANISOU 2046  CZ  PHE B1049     8777  14379  11097    983    747    752       C  
ATOM   2047  N   GLU B1050      15.141   8.157  -0.644  1.00 92.35           N  
ANISOU 2047  N   GLU B1050     9265  14375  11449    922    925    849       N  
ATOM   2048  CA  GLU B1050      14.493   7.351  -1.686  1.00 91.18           C  
ANISOU 2048  CA  GLU B1050     9166  14161  11317    914    946    858       C  
ATOM   2049  C   GLU B1050      13.626   8.236  -2.567  1.00 94.65           C  
ANISOU 2049  C   GLU B1050     9680  14531  11753    892    884    811       C  
ATOM   2050  O   GLU B1050      12.563   8.686  -2.131  1.00 92.22           O  
ANISOU 2050  O   GLU B1050     9366  14228  11443    911    835    778       O  
ATOM   2051  CB  GLU B1050      13.633   6.266  -1.061  1.00 89.72           C  
ANISOU 2051  CB  GLU B1050     8933  14007  11150    954    970    876       C  
ATOM   2052  CG  GLU B1050      12.689   5.612  -2.033  1.00 86.43           C  
ANISOU 2052  CG  GLU B1050     8567  13523  10751    950    976    874       C  
ATOM   2053  CD  GLU B1050      12.562   4.138  -1.773  1.00 92.22           C  
ANISOU 2053  CD  GLU B1050     9258  14278  11504    976   1038    917       C  
ATOM   2054  OE1 GLU B1050      13.089   3.348  -2.577  1.00 88.64           O  
ANISOU 2054  OE1 GLU B1050     8828  13790  11060    959   1088    948       O  
ATOM   2055  OE2 GLU B1050      11.897   3.761  -0.789  1.00 95.90           O  
ANISOU 2055  OE2 GLU B1050     9667  14793  11977   1014   1036    920       O  
ATOM   2056  N   GLU B1051      14.037   8.448  -3.806  1.00 97.27           N  
ANISOU 2056  N   GLU B1051    10082  14796  12082    853    889    810       N  
ATOM   2057  CA  GLU B1051      13.187   9.169  -4.740  1.00 93.78           C  
ANISOU 2057  CA  GLU B1051     9714  14281  11636    832    835    768       C  
ATOM   2058  C   GLU B1051      11.892   8.407  -5.008  1.00 90.23           C  
ANISOU 2058  C   GLU B1051     9277  13801  11204    852    834    764       C  
ATOM   2059  O   GLU B1051      11.911   7.208  -5.310  1.00 85.88           O  
ANISOU 2059  O   GLU B1051     8720  13241  10670    860    888    798       O  
ATOM   2060  CB  GLU B1051      13.935   9.397  -6.044  1.00 96.14           C  
ANISOU 2060  CB  GLU B1051    10085  14515  11930    788    848    773       C  
ATOM   2061  CG  GLU B1051      13.058   9.765  -7.213  1.00 97.12           C  
ANISOU 2061  CG  GLU B1051    10291  14555  12055    767    810    741       C  
ATOM   2062  CD  GLU B1051      13.846   9.798  -8.506  1.00100.64           C  
ANISOU 2062  CD  GLU B1051    10804  14939  12496    726    833    753       C  
ATOM   2063  OE1 GLU B1051      14.955  10.377  -8.504  1.00101.70           O  
ANISOU 2063  OE1 GLU B1051    10938  15086  12618    704    839    759       O  
ATOM   2064  OE2 GLU B1051      13.368   9.243  -9.522  1.00112.61           O  
ANISOU 2064  OE2 GLU B1051    12372  16393  14022    716    846    756       O  
ATOM   2065  N   VAL B1052      10.765   9.103  -4.898  1.00 92.72           N  
ANISOU 2065  N   VAL B1052     9610  14100  11518    861    771    720       N  
ATOM   2066  CA  VAL B1052       9.482   8.571  -5.348  1.00 94.83           C  
ANISOU 2066  CA  VAL B1052     9905  14325  11802    874    760    708       C  
ATOM   2067  C   VAL B1052       9.286   8.903  -6.824  1.00 96.40           C  
ANISOU 2067  C   VAL B1052    10196  14433  11999    837    741    689       C  
ATOM   2068  O   VAL B1052       9.451  10.058  -7.239  1.00 95.94           O  
ANISOU 2068  O   VAL B1052    10183  14346  11925    811    695    657       O  
ATOM   2069  CB  VAL B1052       8.318   9.116  -4.499  1.00 89.14           C  
ANISOU 2069  CB  VAL B1052     9157  13632  11081    903    703    671       C  
ATOM   2070  CG1 VAL B1052       8.205   8.331  -3.209  1.00 87.81           C  
ANISOU 2070  CG1 VAL B1052     8901  13542  10922    945    734    697       C  
ATOM   2071  CG2 VAL B1052       8.513  10.597  -4.209  1.00 95.44           C  
ANISOU 2071  CG2 VAL B1052     9966  14441  11857    889    641    632       C  
ATOM   2072  N   GLU B1053       8.963   7.880  -7.598  1.00100.52           N  
ANISOU 2072  N   GLU B1053    10745  14912  12538    836    778    709       N  
ATOM   2073  CA  GLU B1053       8.683   8.016  -8.998  1.00 98.83           C  
ANISOU 2073  CA  GLU B1053    10615  14610  12324    805    765    694       C  
ATOM   2074  C   GLU B1053       7.239   7.646  -8.989  1.00 98.46           C  
ANISOU 2074  C   GLU B1053    10573  14543  12294    829    740    674       C  
ATOM   2075  O   GLU B1053       6.878   6.493  -9.040  1.00 92.57           O  
ANISOU 2075  O   GLU B1053     9810  13796  11568    847    780    700       O  
ATOM   2076  CB  GLU B1053       9.529   7.059  -9.818  1.00 98.82           C  
ANISOU 2076  CB  GLU B1053    10635  14582  12330    788    832    737       C  
ATOM   2077  CG  GLU B1053      10.780   7.736 -10.359  1.00114.65           C  
ANISOU 2077  CG  GLU B1053    12674  16572  14317    750    839    742       C  
ATOM   2078  CD  GLU B1053      11.824   6.775 -10.882  1.00123.75           C  
ANISOU 2078  CD  GLU B1053    13827  17718  15475    737    912    789       C  
ATOM   2079  OE1 GLU B1053      12.149   6.869 -12.079  1.00121.54           O  
ANISOU 2079  OE1 GLU B1053    13615  17374  15190    705    919    789       O  
ATOM   2080  OE2 GLU B1053      12.335   5.943 -10.105  1.00116.24           O  
ANISOU 2080  OE2 GLU B1053    12809  16824  14531    758    962    827       O  
ATOM   2081  N   GLU B1054       6.439   8.687  -8.822  1.00101.38           N  
ANISOU 2081  N   GLU B1054    10961  14903  12655    831    671    628       N  
ATOM   2082  CA  GLU B1054       4.995   8.641  -8.712  1.00 93.78           C  
ANISOU 2082  CA  GLU B1054    10003  13923  11704    853    632    599       C  
ATOM   2083  C   GLU B1054       4.291   8.118  -9.920  1.00 99.66           C  
ANISOU 2083  C   GLU B1054    10813  14590  12464    841    634    594       C  
ATOM   2084  O   GLU B1054       3.796   8.879 -10.724  1.00105.63           O  
ANISOU 2084  O   GLU B1054    11635  15286  13213    820    586    557       O  
ATOM   2085  CB  GLU B1054       4.476  10.036  -8.450  1.00 96.89           C  
ANISOU 2085  CB  GLU B1054    10415  14316  12083    849    555    548       C  
ATOM   2086  CG  GLU B1054       5.439  11.119  -8.852  1.00 97.32           C  
ANISOU 2086  CG  GLU B1054    10506  14355  12114    813    534    535       C  
ATOM   2087  CD  GLU B1054       5.931  11.899  -7.670  1.00111.14           C  
ANISOU 2087  CD  GLU B1054    12201  16178  13851    825    513    527       C  
ATOM   2088  OE1 GLU B1054       7.150  12.093  -7.539  1.00106.16           O  
ANISOU 2088  OE1 GLU B1054    11555  15572  13208    809    539    548       O  
ATOM   2089  OE2 GLU B1054       5.090  12.325  -6.873  1.00118.93           O  
ANISOU 2089  OE2 GLU B1054    13157  17195  14838    849    470    499       O  
ATOM   2090  N   ARG B 243       4.205   6.808 -10.005  1.00110.56           N  
ANISOU 2090  N   ARG B 243    12171  15971  13864    856    689    629       N  
ATOM   2091  CA  ARG B 243       3.582   6.111 -11.108  1.00110.17           C  
ANISOU 2091  CA  ARG B 243    12176  15851  13831    849    701    631       C  
ATOM   2092  C   ARG B 243       2.322   6.677 -11.723  1.00112.99           C  
ANISOU 2092  C   ARG B 243    12591  16148  14192    845    639    584       C  
ATOM   2093  O   ARG B 243       1.241   6.382 -11.260  1.00110.66           O  
ANISOU 2093  O   ARG B 243    12271  15864  13913    873    620    571       O  
ATOM   2094  CB  ARG B 243       3.242   4.715 -10.635  1.00106.18           C  
ANISOU 2094  CB  ARG B 243    11617  15375  13351    881    752    666       C  
ATOM   2095  CG  ARG B 243       2.410   4.710  -9.371  1.00113.36           C  
ANISOU 2095  CG  ARG B 243    12460  16344  14269    920    730    655       C  
ATOM   2096  CD  ARG B 243       2.182   3.297  -8.874  1.00114.80           C  
ANISOU 2096  CD  ARG B 243    12585  16557  14476    951    786    695       C  
ATOM   2097  NE  ARG B 243       3.391   2.735  -8.296  1.00121.64           N  
ANISOU 2097  NE  ARG B 243    13398  17481  15339    955    846    740       N  
ATOM   2098  CZ  ARG B 243       3.597   1.436  -8.128  1.00126.72           C  
ANISOU 2098  CZ  ARG B 243    14003  18144  16002    972    909    784       C  
ATOM   2099  NH1 ARG B 243       2.666   0.572  -8.499  1.00125.84           N  
ANISOU 2099  NH1 ARG B 243    13901  17998  15915    986    919    787       N  
ATOM   2100  NH2 ARG B 243       4.731   1.005  -7.593  1.00121.30           N  
ANISOU 2100  NH2 ARG B 243    13268  17509  15310    975    960    823       N  
ATOM   2101  N   ARG B 244       2.460   7.477 -12.772  1.00110.58           N  
ANISOU 2101  N   ARG B 244    12362  15781  13872    810    607    559       N  
ATOM   2102  CA  ARG B 244       1.301   7.980 -13.519  1.00108.56           C  
ANISOU 2102  CA  ARG B 244    12169  15459  13619    804    549    515       C  
ATOM   2103  C   ARG B 244       1.066   7.178 -14.777  1.00104.90           C  
ANISOU 2103  C   ARG B 244    11765  14923  13169    790    576    526       C  
ATOM   2104  O   ARG B 244       2.006   6.921 -15.510  1.00104.86           O  
ANISOU 2104  O   ARG B 244    11791  14894  13158    765    614    551       O  
ATOM   2105  CB  ARG B 244       1.513   9.413 -13.972  1.00101.44           C  
ANISOU 2105  CB  ARG B 244    11323  14526  12693    773    493    477       C  
ATOM   2106  CG  ARG B 244       2.126  10.337 -12.958  1.00 99.01           C  
ANISOU 2106  CG  ARG B 244    10970  14282  12367    776    471    469       C  
ATOM   2107  CD  ARG B 244       1.541  11.715 -13.143  1.00101.23           C  
ANISOU 2107  CD  ARG B 244    11295  14534  12633    762    393    416       C  
ATOM   2108  NE  ARG B 244       2.131  12.679 -12.237  1.00 94.03           N  
ANISOU 2108  NE  ARG B 244    10345  13678  11703    762    368    405       N  
ATOM   2109  CZ  ARG B 244       3.427  12.799 -12.042  1.00100.21           C  
ANISOU 2109  CZ  ARG B 244    11109  14493  12474    748    401    431       C  
ATOM   2110  NH1 ARG B 244       3.886  13.705 -11.207  1.00113.23           N  
ANISOU 2110  NH1 ARG B 244    12723  16192  14107    749    375    418       N  
ATOM   2111  NH2 ARG B 244       4.258  12.014 -12.686  1.00103.16           N  
ANISOU 2111  NH2 ARG B 244    11497  14848  12851    732    461    470       N  
ATOM   2112  N   ARG B 245      -0.169   6.775 -15.048  1.00100.84           N  
ANISOU 2112  N   ARG B 245    11267  14374  12674    806    555    508       N  
ATOM   2113  CA  ARG B 245      -0.389   6.056 -16.290  1.00 97.22           C  
ANISOU 2113  CA  ARG B 245    10867  13843  12227    792    578    517       C  
ATOM   2114  C   ARG B 245      -1.168   6.912 -17.273  1.00 97.21           C  
ANISOU 2114  C   ARG B 245    10949  13768  12219    772    515    469       C  
ATOM   2115  O   ARG B 245      -0.949   6.800 -18.483  1.00 95.07           O  
ANISOU 2115  O   ARG B 245    10746  13432  11945    746    524    471       O  
ATOM   2116  CB  ARG B 245      -1.106   4.723 -16.042  1.00102.71           C  
ANISOU 2116  CB  ARG B 245    11525  14548  12954    823    614    539       C  
ATOM   2117  CG  ARG B 245      -0.415   3.803 -15.016  1.00118.30           C  
ANISOU 2117  CG  ARG B 245    13415  16598  14937    846    676    586       C  
ATOM   2118  CD  ARG B 245       0.821   3.052 -15.562  1.00128.25           C  
ANISOU 2118  CD  ARG B 245    14682  17852  16195    828    744    632       C  
ATOM   2119  NE  ARG B 245       1.286   2.004 -14.642  1.00127.00           N  
ANISOU 2119  NE  ARG B 245    14443  17759  16050    854    805    677       N  
ATOM   2120  CZ  ARG B 245       2.104   2.204 -13.602  1.00124.88           C  
ANISOU 2120  CZ  ARG B 245    14113  17564  15771    863    823    696       C  
ATOM   2121  NH1 ARG B 245       2.540   3.423 -13.297  1.00117.64           N  
ANISOU 2121  NH1 ARG B 245    13201  16667  14829    848    784    673       N  
ATOM   2122  NH2 ARG B 245       2.466   1.185 -12.831  1.00120.85           N  
ANISOU 2122  NH2 ARG B 245    13533  17109  15275    887    879    738       N  
ATOM   2123  N   LEU B 246      -2.032   7.800 -16.767  1.00 93.43           N  
ANISOU 2123  N   LEU B 246    10465  13298  11736    783    451    428       N  
ATOM   2124  CA  LEU B 246      -2.705   8.763 -17.627  1.00 91.11           C  
ANISOU 2124  CA  LEU B 246    10247  12937  11432    763    387    381       C  
ATOM   2125  C   LEU B 246      -1.708   9.496 -18.502  1.00 87.45           C  
ANISOU 2125  C   LEU B 246     9845  12438  10944    723    385    379       C  
ATOM   2126  O   LEU B 246      -1.878   9.568 -19.722  1.00 89.99           O  
ANISOU 2126  O   LEU B 246    10242  12686  11263    700    374    367       O  
ATOM   2127  CB  LEU B 246      -3.509   9.747 -16.791  1.00 96.10           C  
ANISOU 2127  CB  LEU B 246    10857  13599  12059    778    322    339       C  
ATOM   2128  CG  LEU B 246      -4.723   9.117 -16.122  1.00105.64           C  
ANISOU 2128  CG  LEU B 246    12020  14827  13293    816    313    333       C  
ATOM   2129  CD1 LEU B 246      -4.597   9.067 -14.553  1.00 92.92           C  
ANISOU 2129  CD1 LEU B 246    10314  13310  11683    847    323    346       C  
ATOM   2130  CD2 LEU B 246      -5.968   9.861 -16.609  1.00 90.19           C  
ANISOU 2130  CD2 LEU B 246    10115  12816  11337    814    242    280       C  
ATOM   2131  N   LEU B 247      -0.636  10.017 -17.909  1.00 82.98           N  
ANISOU 2131  N   LEU B 247     9246  11921  10360    713    396    393       N  
ATOM   2132  CA  LEU B 247       0.318  10.760 -18.720  1.00 78.44           C  
ANISOU 2132  CA  LEU B 247     8729  11313   9763    675    393    391       C  
ATOM   2133  C   LEU B 247       1.072   9.829 -19.657  1.00 78.14           C  
ANISOU 2133  C   LEU B 247     8721  11239   9728    658    456    430       C  
ATOM   2134  O   LEU B 247       1.326  10.177 -20.815  1.00 77.29           O  
ANISOU 2134  O   LEU B 247     8688  11068   9609    628    448    421       O  
ATOM   2135  CB  LEU B 247       1.324  11.502 -17.855  1.00 76.73           C  
ANISOU 2135  CB  LEU B 247     8468  11157   9527    669    393    398       C  
ATOM   2136  CG  LEU B 247       2.098  12.519 -18.686  1.00 73.30           C  
ANISOU 2136  CG  LEU B 247     8099  10683   9070    629    372    385       C  
ATOM   2137  CD1 LEU B 247       1.056  13.374 -19.356  1.00 75.08           C  
ANISOU 2137  CD1 LEU B 247     8390  10846   9290    619    302    335       C  
ATOM   2138  CD2 LEU B 247       3.085  13.360 -17.906  1.00 72.39           C  
ANISOU 2138  CD2 LEU B 247     7945  10623   8936    621    367    388       C  
ATOM   2139  N   SER B 248       1.433   8.638 -19.184  1.00 88.03           N  
ANISOU 2139  N   SER B 248     9918  12533  10998    677    519    472       N  
ATOM   2140  CA  SER B 248       2.258   7.766 -20.013  1.00 85.40           C  
ANISOU 2140  CA  SER B 248     9609  12173  10667    661    581    511       C  
ATOM   2141  C   SER B 248       1.488   7.213 -21.215  1.00 83.09           C  
ANISOU 2141  C   SER B 248     9383  11801  10387    656    579    502       C  
ATOM   2142  O   SER B 248       2.100   6.867 -22.237  1.00 83.29           O  
ANISOU 2142  O   SER B 248     9457  11782  10408    633    611    520       O  
ATOM   2143  CB  SER B 248       2.825   6.618 -19.185  1.00 80.90           C  
ANISOU 2143  CB  SER B 248     8961  11665  10111    684    648    559       C  
ATOM   2144  OG  SER B 248       3.145   5.535 -20.038  1.00 87.49           O  
ANISOU 2144  OG  SER B 248     9821  12464  10958    677    703    591       O  
ATOM   2145  N   ILE B 249       0.160   7.111 -21.125  1.00 84.67           N  
ANISOU 2145  N   ILE B 249     9585  11982  10602    677    541    474       N  
ATOM   2146  CA  ILE B 249      -0.593   6.720 -22.311  1.00 83.30           C  
ANISOU 2146  CA  ILE B 249     9480  11730  10439    669    531    460       C  
ATOM   2147  C   ILE B 249      -0.697   7.898 -23.276  1.00 82.09           C  
ANISOU 2147  C   ILE B 249     9411  11515  10265    638    477    421       C  
ATOM   2148  O   ILE B 249      -0.475   7.759 -24.486  1.00 81.18           O  
ANISOU 2148  O   ILE B 249     9364  11336  10144    615    488    424       O  
ATOM   2149  CB  ILE B 249      -1.982   6.191 -21.910  1.00 83.82           C  
ANISOU 2149  CB  ILE B 249     9520  11796  10531    702    510    444       C  
ATOM   2150  CG1 ILE B 249      -1.867   5.160 -20.783  1.00 87.24           C  
ANISOU 2150  CG1 ILE B 249     9863  12301  10985    735    560    481       C  
ATOM   2151  CG2 ILE B 249      -2.645   5.532 -23.099  1.00 83.31           C  
ANISOU 2151  CG2 ILE B 249     9517  11655  10481    698    514    438       C  
ATOM   2152  CD1 ILE B 249      -3.101   5.064 -19.884  1.00 92.12           C  
ANISOU 2152  CD1 ILE B 249    10432  12947  11621    770    528    460       C  
ATOM   2153  N   ILE B 250      -1.007   9.083 -22.739  1.00 83.21           N  
ANISOU 2153  N   ILE B 250     9548  11674  10393    637    417    386       N  
ATOM   2154  CA  ILE B 250      -1.257  10.252 -23.560  1.00 79.25           C  
ANISOU 2154  CA  ILE B 250     9124  11115   9873    610    359    345       C  
ATOM   2155  C   ILE B 250      -0.063  10.598 -24.429  1.00 78.48           C  
ANISOU 2155  C   ILE B 250     9077  10988   9754    574    381    360       C  
ATOM   2156  O   ILE B 250      -0.240  11.228 -25.471  1.00 79.71           O  
ANISOU 2156  O   ILE B 250     9311  11077   9897    549    348    335       O  
ATOM   2157  CB  ILE B 250      -1.702  11.412 -22.639  1.00 73.91           C  
ANISOU 2157  CB  ILE B 250     8420  10476   9187    619    296    308       C  
ATOM   2158  CG1 ILE B 250      -3.120  11.121 -22.120  1.00 73.69           C  
ANISOU 2158  CG1 ILE B 250     8365  10454   9180    652    264    284       C  
ATOM   2159  CG2 ILE B 250      -1.616  12.764 -23.336  1.00 74.79           C  
ANISOU 2159  CG2 ILE B 250     8602  10541   9275    587    240    271       C  
ATOM   2160  CD1 ILE B 250      -3.780  12.249 -21.381  1.00 73.25           C  
ANISOU 2160  CD1 ILE B 250     8293  10421   9116    661    196    241       C  
ATOM   2161  N   VAL B 251       1.147  10.166 -24.072  1.00 77.92           N  
ANISOU 2161  N   VAL B 251     8966  10961   9679    569    439    402       N  
ATOM   2162  CA  VAL B 251       2.263  10.395 -24.991  1.00 78.40           C  
ANISOU 2162  CA  VAL B 251     9078  10989   9721    534    466    419       C  
ATOM   2163  C   VAL B 251       2.398   9.262 -25.991  1.00 80.11           C  
ANISOU 2163  C   VAL B 251     9330  11159   9948    529    517    447       C  
ATOM   2164  O   VAL B 251       2.630   9.518 -27.176  1.00 79.67           O  
ANISOU 2164  O   VAL B 251     9351  11040   9881    502    513    441       O  
ATOM   2165  CB  VAL B 251       3.592  10.637 -24.252  1.00 75.74           C  
ANISOU 2165  CB  VAL B 251     8690  10716   9372    526    499    448       C  
ATOM   2166  CG1 VAL B 251       3.390  11.593 -23.082  1.00 80.26           C  
ANISOU 2166  CG1 VAL B 251     9213  11343   9937    538    452    423       C  
ATOM   2167  CG2 VAL B 251       4.281   9.348 -23.855  1.00 75.21           C  
ANISOU 2167  CG2 VAL B 251     8566  10691   9319    541    576    499       C  
ATOM   2168  N   VAL B 252       2.224   8.008 -25.557  1.00 76.33           N  
ANISOU 2168  N   VAL B 252     8800  10709   9493    556    564    477       N  
ATOM   2169  CA  VAL B 252       2.333   6.898 -26.497  1.00 75.68           C  
ANISOU 2169  CA  VAL B 252     8749  10582   9422    552    613    503       C  
ATOM   2170  C   VAL B 252       1.270   7.036 -27.585  1.00 76.06           C  
ANISOU 2170  C   VAL B 252     8876  10550   9474    546    571    469       C  
ATOM   2171  O   VAL B 252       1.513   6.735 -28.760  1.00 77.19           O  
ANISOU 2171  O   VAL B 252     9083  10634   9613    527    589    476       O  
ATOM   2172  CB  VAL B 252       2.247   5.551 -25.751  1.00 79.26           C  
ANISOU 2172  CB  VAL B 252     9130  11084   9902    584    667    539       C  
ATOM   2173  CG1 VAL B 252       0.824   5.119 -25.533  1.00 84.87           C  
ANISOU 2173  CG1 VAL B 252     9828  11782  10636    613    638    518       C  
ATOM   2174  CG2 VAL B 252       3.018   4.457 -26.476  1.00 75.96           C  
ANISOU 2174  CG2 VAL B 252     8726  10646   9490    575    736    582       C  
ATOM   2175  N   LEU B 253       0.097   7.557 -27.223  1.00 76.70           N  
ANISOU 2175  N   LEU B 253     8955  10627   9561    561    510    429       N  
ATOM   2176  CA  LEU B 253      -0.866   7.990 -28.224  1.00 77.96           C  
ANISOU 2176  CA  LEU B 253     9192  10709   9718    552    459    389       C  
ATOM   2177  C   LEU B 253      -0.248   9.050 -29.120  1.00 77.20           C  
ANISOU 2177  C   LEU B 253     9170  10569   9594    515    434    373       C  
ATOM   2178  O   LEU B 253      -0.127   8.859 -30.338  1.00 77.49           O  
ANISOU 2178  O   LEU B 253     9277  10541   9624    495    444    375       O  
ATOM   2179  CB  LEU B 253      -2.117   8.529 -27.536  1.00 79.64           C  
ANISOU 2179  CB  LEU B 253     9384  10934   9940    574    396    348       C  
ATOM   2180  CG  LEU B 253      -3.028   7.446 -26.968  1.00 79.30           C  
ANISOU 2180  CG  LEU B 253     9289  10912   9928    610    412    357       C  
ATOM   2181  CD1 LEU B 253      -4.230   8.027 -26.232  1.00 77.26           C  
ANISOU 2181  CD1 LEU B 253     9007  10669   9678    632    350    316       C  
ATOM   2182  CD2 LEU B 253      -3.455   6.564 -28.105  1.00 77.02           C  
ANISOU 2182  CD2 LEU B 253     9054  10557   9654    608    432    362       C  
ATOM   2183  N   VAL B 254       0.192  10.164 -28.524  1.00 73.75           N  
ANISOU 2183  N   VAL B 254     8717  10166   9138    504    403    359       N  
ATOM   2184  CA  VAL B 254       0.693  11.284 -29.322  1.00 77.62           C  
ANISOU 2184  CA  VAL B 254     9277  10615   9602    469    373    340       C  
ATOM   2185  C   VAL B 254       1.902  10.869 -30.158  1.00 79.36           C  
ANISOU 2185  C   VAL B 254     9530  10813   9811    443    430    377       C  
ATOM   2186  O   VAL B 254       1.996  11.207 -31.348  1.00 78.68           O  
ANISOU 2186  O   VAL B 254     9523  10660   9711    418    419    366       O  
ATOM   2187  CB  VAL B 254       1.014  12.496 -28.435  1.00 69.83           C  
ANISOU 2187  CB  VAL B 254     8258   9674   8598    463    334    321       C  
ATOM   2188  CG1 VAL B 254       1.923  13.461 -29.193  1.00 70.22           C  
ANISOU 2188  CG1 VAL B 254     8368   9692   8622    425    324    317       C  
ATOM   2189  CG2 VAL B 254      -0.278  13.203 -28.075  1.00 70.26           C  
ANISOU 2189  CG2 VAL B 254     8317   9722   8658    478    261    273       C  
ATOM   2190  N   VAL B 255       2.844  10.131 -29.559  1.00 78.50           N  
ANISOU 2190  N   VAL B 255     9359  10759   9707    450    493    421       N  
ATOM   2191  CA  VAL B 255       4.059   9.847 -30.310  1.00 77.73           C  
ANISOU 2191  CA  VAL B 255     9292  10644   9598    424    546    455       C  
ATOM   2192  C   VAL B 255       3.811   8.835 -31.418  1.00 77.75           C  
ANISOU 2192  C   VAL B 255     9344  10588   9611    423    579    468       C  
ATOM   2193  O   VAL B 255       4.538   8.848 -32.418  1.00 80.97           O  
ANISOU 2193  O   VAL B 255     9807  10953  10004    397    603    482       O  
ATOM   2194  CB  VAL B 255       5.213   9.433 -29.383  1.00 68.24           C  
ANISOU 2194  CB  VAL B 255     8013   9517   8397    429    602    497       C  
ATOM   2195  CG1 VAL B 255       6.477   9.187 -30.187  1.00 67.94           C  
ANISOU 2195  CG1 VAL B 255     8008   9458   8346    402    656    531       C  
ATOM   2196  CG2 VAL B 255       5.495  10.561 -28.410  1.00 73.02           C  
ANISOU 2196  CG2 VAL B 255     8581  10174   8990    427    565    480       C  
ATOM   2197  N   THR B 256       2.780   7.989 -31.327  1.00 79.90           N  
ANISOU 2197  N   THR B 256     9601  10851   9907    451    578    464       N  
ATOM   2198  CA  THR B 256       2.405   7.298 -32.562  1.00 81.11           C  
ANISOU 2198  CA  THR B 256     9818  10933  10066    446    592    465       C  
ATOM   2199  C   THR B 256       1.473   8.135 -33.428  1.00 84.47           C  
ANISOU 2199  C   THR B 256    10323  11289  10482    434    525    417       C  
ATOM   2200  O   THR B 256       1.549   8.037 -34.663  1.00 85.88           O  
ANISOU 2200  O   THR B 256    10577  11402  10652    415    530    416       O  
ATOM   2201  CB  THR B 256       1.754   5.931 -32.311  1.00 79.94           C  
ANISOU 2201  CB  THR B 256     9630  10795   9949    477    626    483       C  
ATOM   2202  OG1 THR B 256       0.349   6.105 -32.069  1.00 82.60           O  
ANISOU 2202  OG1 THR B 256     9967  11117  10300    498    571    445       O  
ATOM   2203  CG2 THR B 256       2.454   5.143 -31.179  1.00 80.71           C  
ANISOU 2203  CG2 THR B 256     9635  10972  10059    496    683    525       C  
ATOM   2204  N   PHE B 257       0.606   8.961 -32.818  1.00 80.79           N  
ANISOU 2204  N   PHE B 257     9845  10835  10016    444    462    379       N  
ATOM   2205  CA  PHE B 257      -0.200   9.889 -33.613  1.00 81.41           C  
ANISOU 2205  CA  PHE B 257     9999  10849  10083    431    395    332       C  
ATOM   2206  C   PHE B 257       0.678  10.693 -34.549  1.00 80.35           C  
ANISOU 2206  C   PHE B 257     9934  10675   9921    393    392    331       C  
ATOM   2207  O   PHE B 257       0.456  10.711 -35.755  1.00 80.42           O  
ANISOU 2207  O   PHE B 257    10021  10613   9922    378    382    320       O  
ATOM   2208  CB  PHE B 257      -0.999  10.850 -32.735  1.00 83.10           C  
ANISOU 2208  CB  PHE B 257    10187  11091  10298    443    329    293       C  
ATOM   2209  CG  PHE B 257      -1.469  12.105 -33.471  1.00 78.88           C  
ANISOU 2209  CG  PHE B 257     9729  10498   9743    421    260    247       C  
ATOM   2210  CD1 PHE B 257      -2.590  12.073 -34.293  1.00 78.94           C  
ANISOU 2210  CD1 PHE B 257     9796  10439   9757    425    221    215       C  
ATOM   2211  CD2 PHE B 257      -0.789  13.315 -33.336  1.00 77.36           C  
ANISOU 2211  CD2 PHE B 257     9549  10318   9526    397    234    236       C  
ATOM   2212  CE1 PHE B 257      -3.021  13.220 -34.962  1.00 75.09           C  
ANISOU 2212  CE1 PHE B 257     9379   9899   9251    405    158    174       C  
ATOM   2213  CE2 PHE B 257      -1.215  14.463 -34.016  1.00 77.33           C  
ANISOU 2213  CE2 PHE B 257     9616  10261   9505    377    171    195       C  
ATOM   2214  CZ  PHE B 257      -2.334  14.410 -34.824  1.00 75.64           C  
ANISOU 2214  CZ  PHE B 257     9460   9981   9296    382    133    164       C  
ATOM   2215  N   ALA B 258       1.680  11.374 -33.999  1.00 81.40           N  
ANISOU 2215  N   ALA B 258    10039  10852  10037    378    400    343       N  
ATOM   2216  CA  ALA B 258       2.574  12.195 -34.798  1.00 81.97           C  
ANISOU 2216  CA  ALA B 258    10171  10891  10082    342    397    343       C  
ATOM   2217  C   ALA B 258       3.612  11.375 -35.554  1.00 82.81           C  
ANISOU 2217  C   ALA B 258    10298  10982  10185    327    467    386       C  
ATOM   2218  O   ALA B 258       4.453  11.958 -36.250  1.00 83.49           O  
ANISOU 2218  O   ALA B 258    10433  11041  10250    297    473    392       O  
ATOM   2219  CB  ALA B 258       3.263  13.231 -33.910  1.00 81.35           C  
ANISOU 2219  CB  ALA B 258    10053  10867   9990    332    379    340       C  
ATOM   2220  N   LEU B 259       3.579  10.046 -35.447  1.00 81.24           N  
ANISOU 2220  N   LEU B 259    10064  10796  10007    348    520    417       N  
ATOM   2221  CA  LEU B 259       4.419   9.245 -36.331  1.00 79.23           C  
ANISOU 2221  CA  LEU B 259     9840  10515   9749    334    582    453       C  
ATOM   2222  C   LEU B 259       3.692   8.774 -37.594  1.00 80.36           C  
ANISOU 2222  C   LEU B 259    10059  10579   9896    332    574    440       C  
ATOM   2223  O   LEU B 259       4.320   8.657 -38.654  1.00 84.87           O  
ANISOU 2223  O   LEU B 259    10689  11106  10453    310    601    454       O  
ATOM   2224  CB  LEU B 259       5.011   8.060 -35.564  1.00 75.87           C  
ANISOU 2224  CB  LEU B 259     9336  10150   9342    353    651    499       C  
ATOM   2225  CG  LEU B 259       6.509   8.276 -35.396  1.00 73.95           C  
ANISOU 2225  CG  LEU B 259     9073   9943   9083    332    695    532       C  
ATOM   2226  CD1 LEU B 259       6.772   9.515 -34.579  1.00 79.92           C  
ANISOU 2226  CD1 LEU B 259     9801  10739   9825    323    654    514       C  
ATOM   2227  CD2 LEU B 259       7.146   7.073 -34.762  1.00 74.65           C  
ANISOU 2227  CD2 LEU B 259     9090  10085   9189    349    765    579       C  
ATOM   2228  N   CYS B 260       2.380   8.510 -37.508  1.00 84.13           N  
ANISOU 2228  N   CYS B 260    10537  11038  10391    356    538    412       N  
ATOM   2229  CA  CYS B 260       1.596   8.170 -38.696  1.00 83.16           C  
ANISOU 2229  CA  CYS B 260    10488  10838  10272    355    522    394       C  
ATOM   2230  C   CYS B 260       1.131   9.407 -39.456  1.00 82.10           C  
ANISOU 2230  C   CYS B 260    10433  10645  10115    334    455    350       C  
ATOM   2231  O   CYS B 260       1.087   9.397 -40.693  1.00 83.09           O  
ANISOU 2231  O   CYS B 260    10637  10703  10230    318    453    344       O  
ATOM   2232  CB  CYS B 260       0.370   7.332 -38.330  1.00 77.62           C  
ANISOU 2232  CB  CYS B 260     9755  10137   9600    389    512    383       C  
ATOM   2233  SG  CYS B 260       0.697   5.737 -37.556  1.00 86.19           S  
ANISOU 2233  SG  CYS B 260    10754  11280  10715    417    588    432       S  
ATOM   2234  N   LYS B 261       0.768  10.470 -38.747  1.00 72.95           N  
ANISOU 2234  N   LYS B 261     9255   9511   8950    334    400    320       N  
ATOM   2235  CA  LYS B 261       0.218  11.654 -39.382  1.00 74.22           C  
ANISOU 2235  CA  LYS B 261     9487   9619   9093    317    332    276       C  
ATOM   2236  C   LYS B 261       1.283  12.625 -39.882  1.00 78.26           C  
ANISOU 2236  C   LYS B 261    10043  10117   9575    281    331    280       C  
ATOM   2237  O   LYS B 261       0.933  13.619 -40.532  1.00 83.69           O  
ANISOU 2237  O   LYS B 261    10797  10756  10245    263    278    246       O  
ATOM   2238  CB  LYS B 261      -0.715  12.395 -38.426  1.00 68.98           C  
ANISOU 2238  CB  LYS B 261     8788   8985   8437    333    269    239       C  
ATOM   2239  CG  LYS B 261      -2.195  12.386 -38.768  1.00 71.06           C  
ANISOU 2239  CG  LYS B 261     9085   9202   8713    350    216    198       C  
ATOM   2240  CD  LYS B 261      -2.836  11.025 -38.597  1.00 70.36           C  
ANISOU 2240  CD  LYS B 261     8960   9119   8655    380    248    213       C  
ATOM   2241  CE  LYS B 261      -4.300  11.206 -38.178  1.00 69.14           C  
ANISOU 2241  CE  LYS B 261     8794   8958   8518    404    188    172       C  
ATOM   2242  NZ  LYS B 261      -5.076   9.929 -38.122  1.00 68.79           N  
ANISOU 2242  NZ  LYS B 261     8724   8909   8505    433    212    182       N  
ATOM   2243  N   MET B 262       2.571  12.379 -39.608  1.00 83.90           N  
ANISOU 2243  N   MET B 262    10723  10873  10283    270    388    321       N  
ATOM   2244  CA  MET B 262       3.591  13.285 -40.132  1.00 81.65           C  
ANISOU 2244  CA  MET B 262    10481  10572   9970    235    389    326       C  
ATOM   2245  C   MET B 262       3.778  13.138 -41.638  1.00 79.33           C  
ANISOU 2245  C   MET B 262    10278  10202   9662    214    402    329       C  
ATOM   2246  O   MET B 262       3.751  14.161 -42.342  1.00 83.17           O  
ANISOU 2246  O   MET B 262    10831  10641  10126    191    361    304       O  
ATOM   2247  CB  MET B 262       4.909  13.090 -39.385  1.00 89.12           C  
ANISOU 2247  CB  MET B 262    11363  11584  10914    229    445    367       C  
ATOM   2248  CG  MET B 262       5.991  14.017 -39.833  1.00 90.02           C  
ANISOU 2248  CG  MET B 262    11515  11687  11003    194    447    374       C  
ATOM   2249  SD  MET B 262       6.732  14.625 -38.311  1.00139.79           S  
ANISOU 2249  SD  MET B 262    17726  18081  17306    196    448    384       S  
ATOM   2250  CE  MET B 262       5.591  15.938 -37.858  1.00 96.45           C  
ANISOU 2250  CE  MET B 262    12248  12585  11812    201    353    326       C  
ATOM   2251  N   PRO B 263       3.970  11.928 -42.197  1.00 77.00           N  
ANISOU 2251  N   PRO B 263     9991   9889   9377    221    458    358       N  
ATOM   2252  CA  PRO B 263       4.187  11.808 -43.647  1.00 79.71           C  
ANISOU 2252  CA  PRO B 263    10422  10159   9704    201    471    362       C  
ATOM   2253  C   PRO B 263       3.178  12.561 -44.504  1.00 81.23           C  
ANISOU 2253  C   PRO B 263    10696  10281   9886    194    403    315       C  
ATOM   2254  O   PRO B 263       3.537  13.504 -45.216  1.00 80.04           O  
ANISOU 2254  O   PRO B 263    10609  10093   9711    167    379    303       O  
ATOM   2255  CB  PRO B 263       4.081  10.290 -43.878  1.00 80.15           C  
ANISOU 2255  CB  PRO B 263    10460  10211   9781    221    526    390       C  
ATOM   2256  CG  PRO B 263       3.484   9.739 -42.642  1.00 77.55           C  
ANISOU 2256  CG  PRO B 263    10046   9941   9479    253    526    391       C  
ATOM   2257  CD  PRO B 263       4.016  10.603 -41.569  1.00 77.70           C  
ANISOU 2257  CD  PRO B 263    10010  10021   9491    247    512    391       C  
ATOM   2258  N   TYR B 264       1.910  12.142 -44.423  1.00 82.41           N  
ANISOU 2258  N   TYR B 264    10843  10414  10055    219    372    290       N  
ATOM   2259  CA  TYR B 264       0.822  12.802 -45.140  1.00 80.71           C  
ANISOU 2259  CA  TYR B 264    10698  10134   9833    217    304    244       C  
ATOM   2260  C   TYR B 264       0.814  14.301 -44.898  1.00 81.54           C  
ANISOU 2260  C   TYR B 264    10821  10242   9919    199    245    212       C  
ATOM   2261  O   TYR B 264       0.406  15.067 -45.771  1.00 86.99           O  
ANISOU 2261  O   TYR B 264    11589  10872  10593    183    199    182       O  
ATOM   2262  CB  TYR B 264      -0.511  12.187 -44.698  1.00 85.94           C  
ANISOU 2262  CB  TYR B 264    11331  10799  10524    251    279    222       C  
ATOM   2263  CG  TYR B 264      -1.779  12.898 -45.138  1.00 88.50           C  
ANISOU 2263  CG  TYR B 264    11710  11070  10847    254    202    170       C  
ATOM   2264  CD1 TYR B 264      -2.312  13.948 -44.404  1.00 84.18           C  
ANISOU 2264  CD1 TYR B 264    11143  10545  10297    256    141    136       C  
ATOM   2265  CD2 TYR B 264      -2.456  12.488 -46.267  1.00 90.24           C  
ANISOU 2265  CD2 TYR B 264    12000  11220  11069    256    191    155       C  
ATOM   2266  CE1 TYR B 264      -3.472  14.579 -44.800  1.00 83.73           C  
ANISOU 2266  CE1 TYR B 264    11136  10440  10239    259     72     89       C  
ATOM   2267  CE2 TYR B 264      -3.616  13.105 -46.666  1.00 87.34           C  
ANISOU 2267  CE2 TYR B 264    11682  10803  10699    259    122    108       C  
ATOM   2268  CZ  TYR B 264      -4.124  14.149 -45.938  1.00 88.02           C  
ANISOU 2268  CZ  TYR B 264    11748  10911  10783    261     62     75       C  
ATOM   2269  OH  TYR B 264      -5.286  14.755 -46.371  1.00 97.12           O  
ANISOU 2269  OH  TYR B 264    12952  12014  11936    264     -7     28       O  
ATOM   2270  N   HIS B 265       1.234  14.745 -43.715  1.00 82.88           N  
ANISOU 2270  N   HIS B 265    10920  10480  10091    201    243    219       N  
ATOM   2271  CA  HIS B 265       1.274  16.171 -43.453  1.00 82.41           C  
ANISOU 2271  CA  HIS B 265    10874  10424  10014    184    188    190       C  
ATOM   2272  C   HIS B 265       2.607  16.800 -43.820  1.00 82.69           C  
ANISOU 2272  C   HIS B 265    10934  10460  10025    151    213    212       C  
ATOM   2273  O   HIS B 265       2.685  18.030 -43.909  1.00 85.35           O  
ANISOU 2273  O   HIS B 265    11302  10784  10344    131    166    187       O  
ATOM   2274  CB  HIS B 265       0.943  16.459 -41.992  1.00 75.27           C  
ANISOU 2274  CB  HIS B 265     9885   9590   9124    204    164    179       C  
ATOM   2275  CG  HIS B 265      -0.521  16.385 -41.690  1.00 78.61           C  
ANISOU 2275  CG  HIS B 265    10300  10002   9565    230    112    142       C  
ATOM   2276  ND1 HIS B 265      -1.014  16.010 -40.456  1.00 81.09           N  
ANISOU 2276  ND1 HIS B 265    10532  10377   9902    259    110    141       N  
ATOM   2277  CD2 HIS B 265      -1.602  16.627 -42.468  1.00 78.95           C  
ANISOU 2277  CD2 HIS B 265    10408   9981   9607    232     62    105       C  
ATOM   2278  CE1 HIS B 265      -2.335  16.027 -40.487  1.00 78.08           C  
ANISOU 2278  CE1 HIS B 265    10164   9969   9533    278     61    105       C  
ATOM   2279  NE2 HIS B 265      -2.716  16.396 -41.697  1.00 78.50           N  
ANISOU 2279  NE2 HIS B 265    10306   9946   9573    262     31     82       N  
ATOM   2280  N   LEU B 266       3.650  16.008 -44.071  1.00 77.93           N  
ANISOU 2280  N   LEU B 266    10320   9869   9420    143    284    256       N  
ATOM   2281  CA  LEU B 266       4.859  16.639 -44.582  1.00 79.65           C  
ANISOU 2281  CA  LEU B 266    10572  10077   9614    110    305    274       C  
ATOM   2282  C   LEU B 266       4.806  16.786 -46.105  1.00 83.29           C  
ANISOU 2282  C   LEU B 266    11135  10455  10056     90    298    266       C  
ATOM   2283  O   LEU B 266       5.214  17.820 -46.654  1.00 83.45           O  
ANISOU 2283  O   LEU B 266    11209  10446  10054     62    273    255       O  
ATOM   2284  CB  LEU B 266       6.098  15.859 -44.139  1.00 77.60           C  
ANISOU 2284  CB  LEU B 266    10255   9871   9360    109    382    326       C  
ATOM   2285  CG  LEU B 266       7.377  16.623 -44.496  1.00 77.49           C  
ANISOU 2285  CG  LEU B 266    10266   9855   9322     74    400    343       C  
ATOM   2286  CD1 LEU B 266       8.344  16.678 -43.345  1.00 79.51           C  
ANISOU 2286  CD1 LEU B 266    10438  10189   9582     74    433    371       C  
ATOM   2287  CD2 LEU B 266       8.055  15.994 -45.675  1.00 78.14           C  
ANISOU 2287  CD2 LEU B 266    10404   9893   9394     58    453    372       C  
ATOM   2288  N   VAL B 267       4.279  15.784 -46.805  1.00 79.12           N  
ANISOU 2288  N   VAL B 267    10636   9888   9537    104    318    271       N  
ATOM   2289  CA  VAL B 267       4.343  15.808 -48.261  1.00 76.71           C  
ANISOU 2289  CA  VAL B 267    10426   9507   9214     85    321    268       C  
ATOM   2290  C   VAL B 267       3.307  16.771 -48.837  1.00 79.87           C  
ANISOU 2290  C   VAL B 267    10894   9849   9603     80    243    218       C  
ATOM   2291  O   VAL B 267       3.644  17.624 -49.665  1.00 86.80           O  
ANISOU 2291  O   VAL B 267    11842  10683  10456     53    223    208       O  
ATOM   2292  CB  VAL B 267       4.209  14.382 -48.837  1.00 78.27           C  
ANISOU 2292  CB  VAL B 267    10631   9682   9425    101    372    291       C  
ATOM   2293  CG1 VAL B 267       2.812  13.822 -48.689  1.00 82.47           C  
ANISOU 2293  CG1 VAL B 267    11155  10200   9980    132    339    264       C  
ATOM   2294  CG2 VAL B 267       4.592  14.375 -50.286  1.00 81.96           C  
ANISOU 2294  CG2 VAL B 267    11190  10082   9871     80    388    298       C  
ATOM   2295  N   LYS B 268       2.044  16.689 -48.393  1.00 75.83           N  
ANISOU 2295  N   LYS B 268    10364   9337   9109    105    197    186       N  
ATOM   2296  CA  LYS B 268       1.046  17.659 -48.841  1.00 81.29           C  
ANISOU 2296  CA  LYS B 268    11117   9979   9792    101    120    137       C  
ATOM   2297  C   LYS B 268       1.537  19.085 -48.611  1.00 85.67           C  
ANISOU 2297  C   LYS B 268    11683  10543  10326     75     83    122       C  
ATOM   2298  O   LYS B 268       1.181  20.002 -49.364  1.00 83.05           O  
ANISOU 2298  O   LYS B 268    11423  10156   9976     59     33     92       O  
ATOM   2299  CB  LYS B 268      -0.301  17.422 -48.133  1.00 75.66           C  
ANISOU 2299  CB  LYS B 268    10365   9279   9103    132     77    106       C  
ATOM   2300  CG  LYS B 268      -1.408  18.397 -48.556  1.00 77.44           C  
ANISOU 2300  CG  LYS B 268    10650   9453   9321    130     -4     53       C  
ATOM   2301  CD  LYS B 268      -2.588  18.459 -47.583  1.00 77.96           C  
ANISOU 2301  CD  LYS B 268    10665   9548   9410    158    -52     21       C  
ATOM   2302  CE  LYS B 268      -3.837  17.762 -48.115  1.00 85.11           C  
ANISOU 2302  CE  LYS B 268    11601  10406  10333    180    -73     -1       C  
ATOM   2303  NZ  LYS B 268      -5.043  18.660 -47.989  1.00 86.68           N  
ANISOU 2303  NZ  LYS B 268    11822  10581  10533    187   -155    -54       N  
ATOM   2304  N   THR B 269       2.395  19.277 -47.600  1.00 88.29           N  
ANISOU 2304  N   THR B 269    11943  10942  10659     72    108    144       N  
ATOM   2305  CA  THR B 269       2.961  20.590 -47.313  1.00 82.69           C  
ANISOU 2305  CA  THR B 269    11237  10247   9932     47     77    134       C  
ATOM   2306  C   THR B 269       4.164  20.899 -48.187  1.00 85.92           C  
ANISOU 2306  C   THR B 269    11698  10630  10318     14    112    160       C  
ATOM   2307  O   THR B 269       4.357  22.051 -48.582  1.00 90.65           O  
ANISOU 2307  O   THR B 269    12345  11201  10896    -10     74    141       O  
ATOM   2308  CB  THR B 269       3.313  20.688 -45.832  1.00 77.98           C  
ANISOU 2308  CB  THR B 269    10544   9736   9350     59     85    144       C  
ATOM   2309  OG1 THR B 269       2.112  20.968 -45.110  1.00 79.68           O  
ANISOU 2309  OG1 THR B 269    10730   9965   9579     82     27    106       O  
ATOM   2310  CG2 THR B 269       4.325  21.796 -45.562  1.00 80.26           C  
ANISOU 2310  CG2 THR B 269    10828  10048   9620     31     78    150       C  
ATOM   2311  N   LEU B 270       4.957  19.902 -48.551  1.00 82.75           N  
ANISOU 2311  N   LEU B 270    11290  10233   9917     13    183    202       N  
ATOM   2312  CA  LEU B 270       6.012  20.182 -49.518  1.00 84.75           C  
ANISOU 2312  CA  LEU B 270    11602  10453  10147    -19    215    224       C  
ATOM   2313  C   LEU B 270       5.442  20.409 -50.927  1.00 88.19           C  
ANISOU 2313  C   LEU B 270    12141  10802  10567    -29    186    201       C  
ATOM   2314  O   LEU B 270       5.892  21.312 -51.646  1.00 90.30           O  
ANISOU 2314  O   LEU B 270    12469  11031  10809    -57    170    196       O  
ATOM   2315  CB  LEU B 270       7.052  19.058 -49.486  1.00 74.52           C  
ANISOU 2315  CB  LEU B 270    10269   9188   8858    -17    300    276       C  
ATOM   2316  CG  LEU B 270       8.332  19.390 -48.724  1.00 71.78           C  
ANISOU 2316  CG  LEU B 270     9864   8902   8508    -33    335    306       C  
ATOM   2317  CD1 LEU B 270       7.907  19.981 -47.436  1.00 72.29           C  
ANISOU 2317  CD1 LEU B 270     9862   9021   8584    -20    293    284       C  
ATOM   2318  CD2 LEU B 270       9.201  18.155 -48.492  1.00 70.95           C  
ANISOU 2318  CD2 LEU B 270     9708   8836   8414    -25    417    355       C  
ATOM   2319  N   TYR B 271       4.426  19.632 -51.329  1.00 88.25           N  
ANISOU 2319  N   TYR B 271    12170  10776  10586     -7    177    187       N  
ATOM   2320  CA  TYR B 271       3.922  19.733 -52.704  1.00102.12           C  
ANISOU 2320  CA  TYR B 271    14024  12449  12326    -15    155    168       C  
ATOM   2321  C   TYR B 271       3.197  21.051 -52.953  1.00 99.61           C  
ANISOU 2321  C   TYR B 271    13759  12094  11995    -26     75    122       C  
ATOM   2322  O   TYR B 271       3.124  21.505 -54.105  1.00 99.59           O  
ANISOU 2322  O   TYR B 271    13843  12025  11971    -44     55    109       O  
ATOM   2323  CB  TYR B 271       2.993  18.551 -53.055  1.00 89.68           C  
ANISOU 2323  CB  TYR B 271    12457  10849  10770     13    164    164       C  
ATOM   2324  CG  TYR B 271       2.155  18.698 -54.341  1.00 94.58           C  
ANISOU 2324  CG  TYR B 271    13174  11384  11377     11    126    134       C  
ATOM   2325  CD1 TYR B 271       2.641  18.263 -55.576  1.00 98.89           C  
ANISOU 2325  CD1 TYR B 271    13787  11879  11907     -2    163    153       C  
ATOM   2326  CD2 TYR B 271       0.887  19.284 -54.322  1.00 94.53           C  
ANISOU 2326  CD2 TYR B 271    13193  11350  11376     21     52     86       C  
ATOM   2327  CE1 TYR B 271       1.876  18.388 -56.750  1.00103.24           C  
ANISOU 2327  CE1 TYR B 271    14428  12353  12446     -3    128    125       C  
ATOM   2328  CE2 TYR B 271       0.113  19.392 -55.482  1.00106.66           C  
ANISOU 2328  CE2 TYR B 271    14816  12809  12901     20     17     58       C  
ATOM   2329  CZ  TYR B 271       0.619  18.950 -56.693  1.00109.37           C  
ANISOU 2329  CZ  TYR B 271    15225  13103  13228      8     55     78       C  
ATOM   2330  OH  TYR B 271      -0.145  19.072 -57.833  1.00101.81           O  
ANISOU 2330  OH  TYR B 271    14355  12071  12259      8     19     50       O  
ATOM   2331  N   MET B 272       2.632  21.669 -51.919  1.00 88.55           N  
ANISOU 2331  N   MET B 272    12309  10731  10605    -16     26     95       N  
ATOM   2332  CA  MET B 272       2.028  22.975 -52.139  1.00 88.76           C  
ANISOU 2332  CA  MET B 272    12384  10722  10617    -28    -49     52       C  
ATOM   2333  C   MET B 272       3.016  24.101 -51.894  1.00 92.82           C  
ANISOU 2333  C   MET B 272    12896  11257  11114    -57    -55     59       C  
ATOM   2334  O   MET B 272       2.739  25.253 -52.251  1.00 91.84           O  
ANISOU 2334  O   MET B 272    12823  11098  10974    -74   -111     28       O  
ATOM   2335  CB  MET B 272       0.763  23.130 -51.291  1.00 90.49           C  
ANISOU 2335  CB  MET B 272    12565  10962  10857     -2   -106     13       C  
ATOM   2336  CG  MET B 272      -0.349  22.223 -51.818  1.00 99.29           C  
ANISOU 2336  CG  MET B 272    13705  12034  11985     23   -114     -2       C  
ATOM   2337  SD  MET B 272      -1.825  22.144 -50.798  1.00 99.16           S  
ANISOU 2337  SD  MET B 272    13634  12045  11997     58   -170    -41       S  
ATOM   2338  CE  MET B 272      -2.635  20.687 -51.466  1.00 90.28           C  
ANISOU 2338  CE  MET B 272    12529  10881  10891     84   -144    -37       C  
ATOM   2339  N   LEU B 273       4.165  23.769 -51.311  1.00 89.27           N  
ANISOU 2339  N   LEU B 273    12388  10863  10668    -64      3     99       N  
ATOM   2340  CA  LEU B 273       5.386  24.543 -51.464  1.00 97.84           C  
ANISOU 2340  CA  LEU B 273    13486  11955  11733    -96     21    119       C  
ATOM   2341  C   LEU B 273       6.090  24.218 -52.774  1.00108.28           C  
ANISOU 2341  C   LEU B 273    14880  13224  13036   -116     65    144       C  
ATOM   2342  O   LEU B 273       6.867  25.046 -53.273  1.00115.04           O  
ANISOU 2342  O   LEU B 273    15777  14061  13872   -146     65    151       O  
ATOM   2343  CB  LEU B 273       6.305  24.257 -50.272  1.00 98.31           C  
ANISOU 2343  CB  LEU B 273    13451  12097  11806    -92     66    151       C  
ATOM   2344  CG  LEU B 273       7.366  25.232 -49.772  1.00100.29           C  
ANISOU 2344  CG  LEU B 273    13676  12383  12046   -117     68    162       C  
ATOM   2345  CD1 LEU B 273       7.780  24.796 -48.384  1.00 88.37           C  
ANISOU 2345  CD1 LEU B 273    12061  10958  10556   -100     97    183       C  
ATOM   2346  CD2 LEU B 273       8.576  25.231 -50.698  1.00103.66           C  
ANISOU 2346  CD2 LEU B 273    14149  12783  12453   -146    118    197       C  
ATOM   2347  N   GLY B 274       5.797  23.038 -53.345  1.00103.30           N  
ANISOU 2347  N   GLY B 274    14265  12570  12413   -100    101    158       N  
ATOM   2348  CA  GLY B 274       6.477  22.576 -54.552  1.00106.89           C  
ANISOU 2348  CA  GLY B 274    14783  12979  12851   -116    150    185       C  
ATOM   2349  C   GLY B 274       5.953  23.162 -55.858  1.00122.30           C  
ANISOU 2349  C   GLY B 274    16840  14848  14780   -129    108    158       C  
ATOM   2350  O   GLY B 274       6.637  23.096 -56.892  1.00121.66           O  
ANISOU 2350  O   GLY B 274    16819  14727  14680   -149    141    179       O  
ATOM   2351  N   SER B 275       4.729  23.710 -55.845  1.00114.98           N  
ANISOU 2351  N   SER B 275    15938  13894  13856   -119     37    112       N  
ATOM   2352  CA  SER B 275       4.249  24.542 -56.945  1.00125.74           C  
ANISOU 2352  CA  SER B 275    17398  15182  15197   -134    -13     82       C  
ATOM   2353  C   SER B 275       4.704  25.994 -56.786  1.00122.44           C  
ANISOU 2353  C   SER B 275    16995  14766  14762   -162    -51     69       C  
ATOM   2354  O   SER B 275       4.681  26.754 -57.771  1.00123.91           O  
ANISOU 2354  O   SER B 275    17263  14893  14925   -182    -80     54       O  
ATOM   2355  CB  SER B 275       2.710  24.459 -57.041  1.00124.78           C  
ANISOU 2355  CB  SER B 275    17298  15027  15086   -110    -73     38       C  
ATOM   2356  OG  SER B 275       2.165  25.240 -58.098  1.00111.99           O  
ANISOU 2356  OG  SER B 275    15772  13335  13446   -123   -124      6       O  
ATOM   2357  N   LEU B 276       5.160  26.376 -55.581  1.00107.31           N  
ANISOU 2357  N   LEU B 276    15000  12917  12856   -163    -51     76       N  
ATOM   2358  CA  LEU B 276       5.418  27.770 -55.237  1.00106.55           C  
ANISOU 2358  CA  LEU B 276    14907  12828  12749   -185    -96     57       C  
ATOM   2359  C   LEU B 276       6.837  28.030 -54.739  1.00106.91           C  
ANISOU 2359  C   LEU B 276    14907  12923  12790   -206    -50     94       C  
ATOM   2360  O   LEU B 276       7.120  29.134 -54.266  1.00105.37           O  
ANISOU 2360  O   LEU B 276    14700  12745  12589   -222    -84     81       O  
ATOM   2361  CB  LEU B 276       4.396  28.233 -54.204  1.00101.57           C  
ANISOU 2361  CB  LEU B 276    14229  12228  12135   -165   -159     18       C  
ATOM   2362  CG  LEU B 276       2.977  28.326 -54.766  1.00 99.29           C  
ANISOU 2362  CG  LEU B 276    13996  11882  11846   -150   -219    -25       C  
ATOM   2363  CD1 LEU B 276       3.041  28.814 -56.197  1.00107.08           C  
ANISOU 2363  CD1 LEU B 276    15088  12791  12806   -172   -232    -32       C  
ATOM   2364  CD2 LEU B 276       2.229  27.010 -54.669  1.00 93.34           C  
ANISOU 2364  CD2 LEU B 276    13217  11134  11114   -117   -197    -22       C  
ATOM   2365  N   LEU B 277       7.723  27.041 -54.802  1.00111.14           N  
ANISOU 2365  N   LEU B 277    15416  13482  13329   -205     25    138       N  
ATOM   2366  CA  LEU B 277       9.157  27.283 -54.882  1.00101.79           C  
ANISOU 2366  CA  LEU B 277    14224  12317  12134   -232     74    176       C  
ATOM   2367  C   LEU B 277       9.764  26.811 -56.198  1.00117.10           C  
ANISOU 2367  C   LEU B 277    16234  14205  14055   -248    123    203       C  
ATOM   2368  O   LEU B 277      10.944  27.095 -56.453  1.00117.39           O  
ANISOU 2368  O   LEU B 277    16278  14246  14079   -273    161    233       O  
ATOM   2369  CB  LEU B 277       9.912  26.602 -53.730  1.00 95.75           C  
ANISOU 2369  CB  LEU B 277    13360  11633  11389   -222    128    210       C  
ATOM   2370  CG  LEU B 277      10.433  27.552 -52.662  1.00 97.63           C  
ANISOU 2370  CG  LEU B 277    13540  11926  11631   -233    107    206       C  
ATOM   2371  CD1 LEU B 277      11.620  26.920 -51.929  1.00 88.60           C  
ANISOU 2371  CD1 LEU B 277    12319  10847  10497   -233    177    251       C  
ATOM   2372  CD2 LEU B 277      10.791  28.899 -53.272  1.00105.84           C  
ANISOU 2372  CD2 LEU B 277    14642  12924  12647   -266     70    192       C  
ATOM   2373  N   HIS B 278       8.992  26.101 -57.031  1.00110.94           N  
ANISOU 2373  N   HIS B 278    15504  13374  13273   -233    122    194       N  
ATOM   2374  CA  HIS B 278       9.412  25.583 -58.327  1.00104.84           C  
ANISOU 2374  CA  HIS B 278    14802  12548  12482   -244    164    216       C  
ATOM   2375  C   HIS B 278      10.421  24.452 -58.180  1.00100.56           C  
ANISOU 2375  C   HIS B 278    14215  12045  11949   -241    249    265       C  
ATOM   2376  O   HIS B 278      11.569  24.548 -58.628  1.00111.01           O  
ANISOU 2376  O   HIS B 278    15555  13365  13257   -264    294    297       O  
ATOM   2377  CB  HIS B 278       9.938  26.725 -59.190  1.00 97.76           C  
ANISOU 2377  CB  HIS B 278    13981  11605  11557   -278    144    212       C  
ATOM   2378  CG  HIS B 278       9.209  28.010 -58.959  1.00118.96           C  
ANISOU 2378  CG  HIS B 278    16687  14275  14239   -284     63    167       C  
ATOM   2379  ND1 HIS B 278       9.785  29.091 -58.325  1.00111.14           N  
ANISOU 2379  ND1 HIS B 278    15668  13315  13245   -304     42    165       N  
ATOM   2380  CD2 HIS B 278       7.930  28.367 -59.222  1.00132.36           C  
ANISOU 2380  CD2 HIS B 278    18425  15931  15935   -272     -3    123       C  
ATOM   2381  CE1 HIS B 278       8.903  30.072 -58.245  1.00122.76           C  
ANISOU 2381  CE1 HIS B 278    17166  14763  14713   -305    -33    121       C  
ATOM   2382  NE2 HIS B 278       7.767  29.658 -58.780  1.00147.85           N  
ANISOU 2382  NE2 HIS B 278    20386  17898  17892   -285    -62     95       N  
ATOM   2383  N   TRP B 279       9.968  23.364 -57.567  1.00103.43           N  
ANISOU 2383  N   TRP B 279    14520  12443  12336   -211    270    271       N  
ATOM   2384  CA  TRP B 279      10.802  22.192 -57.401  1.00103.18           C  
ANISOU 2384  CA  TRP B 279    14442  12447  12314   -204    349    317       C  
ATOM   2385  C   TRP B 279      11.070  21.542 -58.757  1.00 98.38           C  
ANISOU 2385  C   TRP B 279    13909  11782  11691   -211    390    335       C  
ATOM   2386  O   TRP B 279      10.232  21.605 -59.659  1.00100.76           O  
ANISOU 2386  O   TRP B 279    14282  12020  11982   -207    355    309       O  
ATOM   2387  CB  TRP B 279      10.138  21.175 -56.461  1.00105.70           C  
ANISOU 2387  CB  TRP B 279    14686  12812  12663   -169    358    316       C  
ATOM   2388  CG  TRP B 279      10.372  21.442 -54.972  1.00101.31           C  
ANISOU 2388  CG  TRP B 279    14033  12334  12124   -162    353    319       C  
ATOM   2389  CD1 TRP B 279       9.608  22.214 -54.128  1.00 94.03           C  
ANISOU 2389  CD1 TRP B 279    13082  11435  11212   -154    289    283       C  
ATOM   2390  CD2 TRP B 279      11.473  20.974 -54.187  1.00115.59           C  
ANISOU 2390  CD2 TRP B 279    15766  14208  13943   -164    413    359       C  
ATOM   2391  NE1 TRP B 279      10.159  22.238 -52.874  1.00 94.19           N  
ANISOU 2391  NE1 TRP B 279    13012  11529  11246   -150    307    299       N  
ATOM   2392  CE2 TRP B 279      11.306  21.488 -52.882  1.00107.31           C  
ANISOU 2392  CE2 TRP B 279    14645  13219  12909   -156    382    345       C  
ATOM   2393  CE3 TRP B 279      12.587  20.167 -54.460  1.00127.83           C  
ANISOU 2393  CE3 TRP B 279    17305  15774  15493   -172    490    406       C  
ATOM   2394  CZ2 TRP B 279      12.206  21.215 -51.858  1.00106.69           C  
ANISOU 2394  CZ2 TRP B 279    14482  13212  12842   -154    425    376       C  
ATOM   2395  CZ3 TRP B 279      13.479  19.894 -53.435  1.00127.01           C  
ANISOU 2395  CZ3 TRP B 279    17117  15741  15402   -170    533    436       C  
ATOM   2396  CH2 TRP B 279      13.282  20.416 -52.149  1.00114.73           C  
ANISOU 2396  CH2 TRP B 279    15490  14243  13860   -162    500    422       C  
ATOM   2397  N   PRO B 280      12.249  20.933 -58.925  1.00 93.25           N  
ANISOU 2397  N   PRO B 280    13242  11151  11037   -221    462    380       N  
ATOM   2398  CA  PRO B 280      12.519  20.126 -60.116  1.00 96.00           C  
ANISOU 2398  CA  PRO B 280    13650  11452  11373   -223    508    402       C  
ATOM   2399  C   PRO B 280      11.365  19.238 -60.544  1.00104.01           C  
ANISOU 2399  C   PRO B 280    14689  12432  12398   -194    495    383       C  
ATOM   2400  O   PRO B 280      10.517  18.854 -59.735  1.00103.36           O  
ANISOU 2400  O   PRO B 280    14555  12378  12339   -168    472    365       O  
ATOM   2401  CB  PRO B 280      13.728  19.293 -59.679  1.00 98.32           C  
ANISOU 2401  CB  PRO B 280    13881  11799  11676   -224    589    451       C  
ATOM   2402  CG  PRO B 280      14.490  20.228 -58.827  1.00 98.77           C  
ANISOU 2402  CG  PRO B 280    13891  11904  11733   -243    582    458       C  
ATOM   2403  CD  PRO B 280      13.463  21.094 -58.107  1.00102.16           C  
ANISOU 2403  CD  PRO B 280    14304  12343  12171   -235    504    413       C  
ATOM   2404  N   CYS B 281      11.331  18.936 -61.843  1.00108.58           N  
ANISOU 2404  N   CYS B 281    15350  12947  12959   -199    509    386       N  
ATOM   2405  CA  CYS B 281      10.366  17.990 -62.390  1.00101.36           C  
ANISOU 2405  CA  CYS B 281    14464  11995  12052   -174    505    372       C  
ATOM   2406  C   CYS B 281      10.405  16.662 -61.647  1.00101.16           C  
ANISOU 2406  C   CYS B 281    14359  12020  12055   -148    554    397       C  
ATOM   2407  O   CYS B 281       9.357  16.037 -61.450  1.00102.17           O  
ANISOU 2407  O   CYS B 281    14473  12143  12202   -120    533    377       O  
ATOM   2408  CB  CYS B 281      10.662  17.778 -63.876  1.00 96.47           C  
ANISOU 2408  CB  CYS B 281    13938  11310  11409   -186    529    383       C  
ATOM   2409  SG  CYS B 281       9.252  17.524 -64.987  1.00138.18           S  
ANISOU 2409  SG  CYS B 281    19306  16510  16684   -168    481    343       S  
ATOM   2410  N   ASP B 282      11.602  16.214 -61.242  1.00104.58           N  
ANISOU 2410  N   ASP B 282    14741  12502  12493   -156    620    440       N  
ATOM   2411  CA  ASP B 282      11.736  14.957 -60.510  1.00102.88           C  
ANISOU 2411  CA  ASP B 282    14448  12337  12304   -132    670    466       C  
ATOM   2412  C   ASP B 282      10.791  14.924 -59.324  1.00 99.53           C  
ANISOU 2412  C   ASP B 282    13956  11956  11907   -108    629    442       C  
ATOM   2413  O   ASP B 282      10.026  13.968 -59.131  1.00 97.29           O  
ANISOU 2413  O   ASP B 282    13648  11675  11644    -79    633    437       O  
ATOM   2414  CB  ASP B 282      13.166  14.781 -59.993  1.00107.57           C  
ANISOU 2414  CB  ASP B 282    14986  12987  12898   -147    735    512       C  
ATOM   2415  CG  ASP B 282      14.217  15.145 -61.006  1.00118.38           C  
ANISOU 2415  CG  ASP B 282    16418  14322  14240   -177    768    535       C  
ATOM   2416  OD1 ASP B 282      14.468  16.358 -61.197  1.00116.66           O  
ANISOU 2416  OD1 ASP B 282    16235  14088  14003   -201    735    521       O  
ATOM   2417  OD2 ASP B 282      14.818  14.208 -61.580  1.00110.91           O  
ANISOU 2417  OD2 ASP B 282    15483  13367  13291   -175    830    567       O  
ATOM   2418  N   PHE B 283      10.828  15.992 -58.530  1.00 99.63           N  
ANISOU 2418  N   PHE B 283    13937  11999  11918   -118    589    426       N  
ATOM   2419  CA  PHE B 283      10.300  15.959 -57.180  1.00 98.62           C  
ANISOU 2419  CA  PHE B 283    13725  11930  11815    -98    566    413       C  
ATOM   2420  C   PHE B 283       8.782  15.863 -57.191  1.00 95.86           C  
ANISOU 2420  C   PHE B 283    13392  11552  11479    -73    507    371       C  
ATOM   2421  O   PHE B 283       8.206  14.939 -56.610  1.00 93.26           O  
ANISOU 2421  O   PHE B 283    13011  11249  11174    -45    517    373       O  
ATOM   2422  CB  PHE B 283      10.755  17.210 -56.438  1.00 94.98           C  
ANISOU 2422  CB  PHE B 283    13236  11505  11347   -117    535    405       C  
ATOM   2423  CG  PHE B 283      11.246  16.944 -55.050  1.00110.90           C  
ANISOU 2423  CG  PHE B 283    15149  13605  13385   -107    561    426       C  
ATOM   2424  CD1 PHE B 283      12.537  16.482 -54.840  1.00117.97           C  
ANISOU 2424  CD1 PHE B 283    16005  14539  14280   -117    631    471       C  
ATOM   2425  CD2 PHE B 283      10.414  17.112 -53.960  1.00104.70           C  
ANISOU 2425  CD2 PHE B 283    14305  12858  12619    -86    519    401       C  
ATOM   2426  CE1 PHE B 283      12.996  16.234 -53.566  1.00129.22           C  
ANISOU 2426  CE1 PHE B 283    17335  16040  15723   -108    655    491       C  
ATOM   2427  CE2 PHE B 283      10.865  16.854 -52.694  1.00101.66           C  
ANISOU 2427  CE2 PHE B 283    13826  12549  12252    -76    544    420       C  
ATOM   2428  CZ  PHE B 283      12.159  16.415 -52.496  1.00128.35           C  
ANISOU 2428  CZ  PHE B 283    17169  15968  15632    -87    611    465       C  
ATOM   2429  N   ASP B 284       8.117  16.820 -57.844  1.00 90.43           N  
ANISOU 2429  N   ASP B 284    12776  10810  10774    -84    445    334       N  
ATOM   2430  CA  ASP B 284       6.659  16.892 -57.792  1.00 92.34           C  
ANISOU 2430  CA  ASP B 284    13032  11025  11027    -62    382    290       C  
ATOM   2431  C   ASP B 284       6.023  15.546 -58.115  1.00 91.08           C  
ANISOU 2431  C   ASP B 284    12873  10848  10886    -35    407    295       C  
ATOM   2432  O   ASP B 284       5.144  15.067 -57.391  1.00 93.49           O  
ANISOU 2432  O   ASP B 284    13128  11177  11216     -8    388    280       O  
ATOM   2433  CB  ASP B 284       6.151  17.983 -58.739  1.00 98.40           C  
ANISOU 2433  CB  ASP B 284    13892  11724  11770    -80    321    254       C  
ATOM   2434  CG  ASP B 284       6.596  19.385 -58.319  1.00110.39           C  
ANISOU 2434  CG  ASP B 284    15409  13261  13275   -104    285    243       C  
ATOM   2435  OD1 ASP B 284       6.975  19.562 -57.141  1.00105.23           O  
ANISOU 2435  OD1 ASP B 284    14675  12673  12634   -102    292    252       O  
ATOM   2436  OD2 ASP B 284       6.584  20.307 -59.170  1.00116.40           O  
ANISOU 2436  OD2 ASP B 284    16246  13969  14011   -126    251    225       O  
ATOM   2437  N   LEU B 285       6.480  14.903 -59.185  1.00 92.63           N  
ANISOU 2437  N   LEU B 285    13121  11003  11070    -41    451    317       N  
ATOM   2438  CA  LEU B 285       5.955  13.584 -59.498  1.00 97.15           C  
ANISOU 2438  CA  LEU B 285    13692  11561  11661    -15    479    324       C  
ATOM   2439  C   LEU B 285       6.280  12.599 -58.390  1.00105.01           C  
ANISOU 2439  C   LEU B 285    14588  12628  12685      4    528    354       C  
ATOM   2440  O   LEU B 285       5.427  11.787 -58.003  1.00109.05           O  
ANISOU 2440  O   LEU B 285    15065  13149  13222     32    523    346       O  
ATOM   2441  CB  LEU B 285       6.509  13.079 -60.823  1.00 84.70           C  
ANISOU 2441  CB  LEU B 285    12186   9931  10064    -26    522    345       C  
ATOM   2442  CG  LEU B 285       6.077  11.630 -60.962  1.00 95.15           C  
ANISOU 2442  CG  LEU B 285    13492  11251  11410      2    558    357       C  
ATOM   2443  CD1 LEU B 285       4.755  11.531 -61.699  1.00124.34           C  
ANISOU 2443  CD1 LEU B 285    17250  14884  15109     17    506    317       C  
ATOM   2444  CD2 LEU B 285       7.168  10.799 -61.585  1.00 96.62           C  
ANISOU 2444  CD2 LEU B 285    13690  11434  11588     -6    634    401       C  
ATOM   2445  N   PHE B 286       7.511  12.647 -57.871  1.00106.42           N  
ANISOU 2445  N   PHE B 286    14719  12856  12858    -11    577    391       N  
ATOM   2446  CA  PHE B 286       7.872  11.790 -56.747  1.00 98.68           C  
ANISOU 2446  CA  PHE B 286    13641  11948  11904      7    622    420       C  
ATOM   2447  C   PHE B 286       6.797  11.871 -55.674  1.00 96.19           C  
ANISOU 2447  C   PHE B 286    13268  11665  11613     31    575    391       C  
ATOM   2448  O   PHE B 286       6.074  10.900 -55.419  1.00 89.99           O  
ANISOU 2448  O   PHE B 286    12452  10886  10853     59    582    389       O  
ATOM   2449  CB  PHE B 286       9.242  12.202 -56.191  1.00104.14           C  
ANISOU 2449  CB  PHE B 286    14290  12691  12587    -15    662    453       C  
ATOM   2450  CG  PHE B 286       9.769  11.287 -55.129  1.00 96.86           C  
ANISOU 2450  CG  PHE B 286    13272  11842  11689      1    716    488       C  
ATOM   2451  CD1 PHE B 286       9.302  11.359 -53.837  1.00 98.80           C  
ANISOU 2451  CD1 PHE B 286    13439  12144  11956     19    693    477       C  
ATOM   2452  CD2 PHE B 286      10.752  10.358 -55.423  1.00100.76           C  
ANISOU 2452  CD2 PHE B 286    13754  12346  12182     -2    791    532       C  
ATOM   2453  CE1 PHE B 286       9.797  10.508 -52.859  1.00 96.91           C  
ANISOU 2453  CE1 PHE B 286    13112  11972  11738     35    744    510       C  
ATOM   2454  CE2 PHE B 286      11.252   9.503 -54.449  1.00100.91           C  
ANISOU 2454  CE2 PHE B 286    13685  12432  12223     13    842    564       C  
ATOM   2455  CZ  PHE B 286      10.772   9.580 -53.170  1.00103.35           C  
ANISOU 2455  CZ  PHE B 286    13918  12798  12555     31    818    554       C  
ATOM   2456  N   LEU B 287       6.622  13.068 -55.111  1.00 94.44           N  
ANISOU 2456  N   LEU B 287    13038  11461  11385     21    522    366       N  
ATOM   2457  CA  LEU B 287       5.660  13.310 -54.047  1.00 89.00           C  
ANISOU 2457  CA  LEU B 287    12293  10805  10716     41    473    337       C  
ATOM   2458  C   LEU B 287       4.225  12.964 -54.431  1.00 89.62           C  
ANISOU 2458  C   LEU B 287    12405  10839  10808     64    429    302       C  
ATOM   2459  O   LEU B 287       3.388  12.839 -53.528  1.00 88.92           O  
ANISOU 2459  O   LEU B 287    12262  10781  10742     87    400    283       O  
ATOM   2460  CB  LEU B 287       5.710  14.776 -53.603  1.00 87.44           C  
ANISOU 2460  CB  LEU B 287    12099  10621  10505     23    419    312       C  
ATOM   2461  CG  LEU B 287       7.040  15.526 -53.424  1.00 93.54           C  
ANISOU 2461  CG  LEU B 287    12860  11421  11258     -6    443    336       C  
ATOM   2462  CD1 LEU B 287       6.795  16.971 -52.974  1.00 87.46           C  
ANISOU 2462  CD1 LEU B 287    12095  10658  10478    -20    377    303       C  
ATOM   2463  CD2 LEU B 287       7.969  14.823 -52.455  1.00 93.80           C  
ANISOU 2463  CD2 LEU B 287    12805  11529  11307      0    506    378       C  
ATOM   2464  N   MET B 288       3.905  12.827 -55.723  1.00 86.46           N  
ANISOU 2464  N   MET B 288    12090  10366  10394     59    422    291       N  
ATOM   2465  CA  MET B 288       2.560  12.404 -56.089  1.00 85.87           C  
ANISOU 2465  CA  MET B 288    12044  10248  10334     82    383    258       C  
ATOM   2466  C   MET B 288       2.393  10.901 -55.974  1.00 89.00           C  
ANISOU 2466  C   MET B 288    12400  10658  10756    108    433    282       C  
ATOM   2467  O   MET B 288       1.366  10.428 -55.483  1.00 85.97           O  
ANISOU 2467  O   MET B 288    11983  10282  10398    135    410    263       O  
ATOM   2468  CB  MET B 288       2.223  12.789 -57.524  1.00 88.57           C  
ANISOU 2468  CB  MET B 288    12494  10507  10653     69    355    236       C  
ATOM   2469  CG  MET B 288       2.168  14.244 -57.861  1.00 94.63           C  
ANISOU 2469  CG  MET B 288    13316  11244  11393     45    298    207       C  
ATOM   2470  SD  MET B 288       2.317  14.345 -59.667  1.00103.60           S  
ANISOU 2470  SD  MET B 288    14574  12289  12498     26    300    203       S  
ATOM   2471  CE  MET B 288       2.204  16.114 -59.892  1.00104.38           C  
ANISOU 2471  CE  MET B 288    14729  12360  12570     -1    229    168       C  
ATOM   2472  N   ASN B 289       3.353  10.137 -56.479  1.00 98.02           N  
ANISOU 2472  N   ASN B 289    13551  11800  11893    101    500    322       N  
ATOM   2473  CA  ASN B 289       3.257   8.691 -56.411  1.00107.23           C  
ANISOU 2473  CA  ASN B 289    14680  12977  13084    125    550    346       C  
ATOM   2474  C   ASN B 289       3.756   8.161 -55.080  1.00100.30           C  
ANISOU 2474  C   ASN B 289    13699  12183  12229    137    591    376       C  
ATOM   2475  O   ASN B 289       3.839   6.940 -54.897  1.00 90.93           O  
ANISOU 2475  O   ASN B 289    12471  11015  11063    156    640    402       O  
ATOM   2476  CB  ASN B 289       4.020   8.034 -57.570  1.00 90.25           C  
ANISOU 2476  CB  ASN B 289    12585  10787  10918    114    605    375       C  
ATOM   2477  CG  ASN B 289       4.009   8.870 -58.867  1.00115.19           C  
ANISOU 2477  CG  ASN B 289    15849  13873  14044     91    573    353       C  
ATOM   2478  OD1 ASN B 289       5.061   9.280 -59.349  1.00122.24           O  
ANISOU 2478  OD1 ASN B 289    16773  14761  14913     65    602    375       O  
ATOM   2479  ND2 ASN B 289       2.823   9.098 -59.437  1.00120.82           N  
ANISOU 2479  ND2 ASN B 289    16617  14531  14757    100    516    312       N  
ATOM   2480  N   ILE B 290       4.103   9.066 -54.165  1.00 98.34           N  
ANISOU 2480  N   ILE B 290    13407  11983  11976    127    572    373       N  
ATOM   2481  CA  ILE B 290       4.378   8.732 -52.776  1.00 86.96           C  
ANISOU 2481  CA  ILE B 290    11863  10621  10555    141    596    393       C  
ATOM   2482  C   ILE B 290       3.101   8.786 -51.947  1.00 89.97           C  
ANISOU 2482  C   ILE B 290    12204  11020  10961    167    543    360       C  
ATOM   2483  O   ILE B 290       2.984   8.083 -50.941  1.00 91.98           O  
ANISOU 2483  O   ILE B 290    12379  11330  11241    189    566    375       O  
ATOM   2484  CB  ILE B 290       5.425   9.713 -52.223  1.00 90.36           C  
ANISOU 2484  CB  ILE B 290    12270  11095  10969    117    600    406       C  
ATOM   2485  CG1 ILE B 290       6.317   9.048 -51.196  1.00 82.19           C  
ANISOU 2485  CG1 ILE B 290    11144  10136   9948    124    660    447       C  
ATOM   2486  CG2 ILE B 290       4.757  10.882 -51.554  1.00 96.13           C  
ANISOU 2486  CG2 ILE B 290    12989  11840  11698    116    529    367       C  
ATOM   2487  CD1 ILE B 290       7.451   8.348 -51.820  1.00 82.91           C  
ANISOU 2487  CD1 ILE B 290    11248  10222  10030    112    731    490       C  
ATOM   2488  N   PHE B 291       2.130   9.589 -52.383  1.00 93.97           N  
ANISOU 2488  N   PHE B 291    12766  11479  11460    165    474    315       N  
ATOM   2489  CA  PHE B 291       1.051  10.021 -51.497  1.00 92.15           C  
ANISOU 2489  CA  PHE B 291    12498  11271  11246    183    416    280       C  
ATOM   2490  C   PHE B 291       0.114   8.895 -51.096  1.00 90.37           C  
ANISOU 2490  C   PHE B 291    12228  11054  11054    217    423    278       C  
ATOM   2491  O   PHE B 291      -0.158   8.760 -49.887  1.00 86.35           O  
ANISOU 2491  O   PHE B 291    11640  10604  10566    236    419    279       O  
ATOM   2492  CB  PHE B 291       0.281  11.158 -52.159  1.00 96.04           C  
ANISOU 2492  CB  PHE B 291    13066  11705  11720    171    342    233       C  
ATOM   2493  CG  PHE B 291      -0.421  12.057 -51.202  1.00 91.13           C  
ANISOU 2493  CG  PHE B 291    12407  11113  11104    178    280    200       C  
ATOM   2494  CD1 PHE B 291      -1.654  11.701 -50.681  1.00 91.72           C  
ANISOU 2494  CD1 PHE B 291    12451  11193  11206    207    246    174       C  
ATOM   2495  CD2 PHE B 291       0.115  13.291 -50.879  1.00 87.83           C  
ANISOU 2495  CD2 PHE B 291    11991  10714  10667    156    254    191       C  
ATOM   2496  CE1 PHE B 291      -2.321  12.537 -49.815  1.00 91.17           C  
ANISOU 2496  CE1 PHE B 291    12349  11151  11142    214    189    142       C  
ATOM   2497  CE2 PHE B 291      -0.547  14.145 -50.014  1.00 91.99           C  
ANISOU 2497  CE2 PHE B 291    12486  11267  11198    162    196    159       C  
ATOM   2498  CZ  PHE B 291      -1.770  13.768 -49.482  1.00 95.52           C  
ANISOU 2498  CZ  PHE B 291    12900  11721  11671    191    163    134       C  
ATOM   2499  N   PRO B 292      -0.434   8.050 -52.030  1.00 90.44           N  
ANISOU 2499  N   PRO B 292    12284  11008  11071    228    432    275       N  
ATOM   2500  CA  PRO B 292      -1.444   7.049 -51.627  1.00 95.50           C  
ANISOU 2500  CA  PRO B 292    12885  11656  11746    261    431    268       C  
ATOM   2501  C   PRO B 292      -0.995   6.189 -50.463  1.00 90.32           C  
ANISOU 2501  C   PRO B 292    12129  11076  11115    279    483    304       C  
ATOM   2502  O   PRO B 292      -1.812   5.659 -49.701  1.00 84.49           O  
ANISOU 2502  O   PRO B 292    11335  10364  10405    306    473    297       O  
ATOM   2503  CB  PRO B 292      -1.629   6.197 -52.888  1.00 97.10           C  
ANISOU 2503  CB  PRO B 292    13152  11793  11949    264    453    273       C  
ATOM   2504  CG  PRO B 292      -0.366   6.392 -53.645  1.00 99.97           C  
ANISOU 2504  CG  PRO B 292    13558  12141  12283    236    494    300       C  
ATOM   2505  CD  PRO B 292      -0.021   7.839 -53.427  1.00 93.59           C  
ANISOU 2505  CD  PRO B 292    12767  11344  11450    212    454    283       C  
ATOM   2506  N   TYR B 293       0.324   6.068 -50.332  1.00 92.72           N  
ANISOU 2506  N   TYR B 293    12411  11414  11406    263    540    344       N  
ATOM   2507  CA  TYR B 293       0.915   5.451 -49.154  1.00 89.76           C  
ANISOU 2507  CA  TYR B 293    11939  11116  11049    276    588    380       C  
ATOM   2508  C   TYR B 293       0.678   6.285 -47.899  1.00 87.10           C  
ANISOU 2508  C   TYR B 293    11542  10837  10716    280    549    363       C  
ATOM   2509  O   TYR B 293       0.089   5.808 -46.917  1.00 82.90           O  
ANISOU 2509  O   TYR B 293    10941  10347  10210    307    547    362       O  
ATOM   2510  CB  TYR B 293       2.411   5.235 -49.382  1.00 83.64           C  
ANISOU 2510  CB  TYR B 293    11162  10362  10257    255    654    424       C  
ATOM   2511  CG  TYR B 293       2.721   4.113 -50.339  1.00 97.00           C  
ANISOU 2511  CG  TYR B 293    12887  12016  11952    257    707    449       C  
ATOM   2512  CD1 TYR B 293       1.703   3.383 -50.936  1.00 93.36           C  
ANISOU 2512  CD1 TYR B 293    12457  11506  11508    276    693    432       C  
ATOM   2513  CD2 TYR B 293       4.033   3.759 -50.616  1.00101.15           C  
ANISOU 2513  CD2 TYR B 293    13412  12556  12466    241    771    491       C  
ATOM   2514  CE1 TYR B 293       1.987   2.352 -51.810  1.00117.40           C  
ANISOU 2514  CE1 TYR B 293    15534  14517  14556    279    741    455       C  
ATOM   2515  CE2 TYR B 293       4.329   2.726 -51.480  1.00113.05           C  
ANISOU 2515  CE2 TYR B 293    14948  14029  13975    244    820    514       C  
ATOM   2516  CZ  TYR B 293       3.302   2.022 -52.084  1.00129.10           C  
ANISOU 2516  CZ  TYR B 293    17015  16014  16025    263    805    496       C  
ATOM   2517  OH  TYR B 293       3.588   0.990 -52.968  1.00138.84           O  
ANISOU 2517  OH  TYR B 293    18280  17213  17261    266    853    519       O  
ATOM   2518  N   CYS B 294       1.162   7.526 -47.896  1.00 85.07           N  
ANISOU 2518  N   CYS B 294    11309  10582  10433    256    520    351       N  
ATOM   2519  CA  CYS B 294       1.120   8.312 -46.671  1.00 85.23           C  
ANISOU 2519  CA  CYS B 294    11267  10661  10454    259    490    339       C  
ATOM   2520  C   CYS B 294      -0.303   8.437 -46.154  1.00 84.43           C  
ANISOU 2520  C   CYS B 294    11148  10558  10373    283    431    300       C  
ATOM   2521  O   CYS B 294      -0.539   8.353 -44.942  1.00 82.61           O  
ANISOU 2521  O   CYS B 294    10840  10389  10161    302    428    302       O  
ATOM   2522  CB  CYS B 294       1.740   9.680 -46.916  1.00 85.44           C  
ANISOU 2522  CB  CYS B 294    11335  10679  10450    227    460    327       C  
ATOM   2523  SG  CYS B 294       3.519   9.583 -47.209  1.00 92.75           S  
ANISOU 2523  SG  CYS B 294    12262  11625  11356    200    532    376       S  
ATOM   2524  N   THR B 295      -1.267   8.615 -47.064  1.00 83.07           N  
ANISOU 2524  N   THR B 295    11047  10318  10200    284    386    266       N  
ATOM   2525  CA  THR B 295      -2.672   8.475 -46.701  1.00 81.09           C  
ANISOU 2525  CA  THR B 295    10781  10059   9972    310    339    232       C  
ATOM   2526  C   THR B 295      -2.898   7.190 -45.930  1.00 82.40           C  
ANISOU 2526  C   THR B 295    10869  10269  10171    341    382    257       C  
ATOM   2527  O   THR B 295      -3.453   7.198 -44.824  1.00 81.29           O  
ANISOU 2527  O   THR B 295    10662  10176  10050    361    363    248       O  
ATOM   2528  CB  THR B 295      -3.546   8.470 -47.949  1.00 79.11           C  
ANISOU 2528  CB  THR B 295    10618   9724   9718    309    303    201       C  
ATOM   2529  OG1 THR B 295      -3.116   9.507 -48.834  1.00 89.57           O  
ANISOU 2529  OG1 THR B 295    12021  11004  11009    279    277    187       O  
ATOM   2530  CG2 THR B 295      -4.988   8.683 -47.584  1.00 86.52           C  
ANISOU 2530  CG2 THR B 295    11548  10651  10675    331    240    159       C  
ATOM   2531  N   CYS B 296      -2.443   6.072 -46.498  1.00 89.65           N  
ANISOU 2531  N   CYS B 296    11795  11171  11096    343    441    290       N  
ATOM   2532  CA  CYS B 296      -2.846   4.774 -45.981  1.00 87.50           C  
ANISOU 2532  CA  CYS B 296    11463  10926  10858    373    477    310       C  
ATOM   2533  C   CYS B 296      -2.241   4.525 -44.597  1.00 88.45           C  
ANISOU 2533  C   CYS B 296    11483  11134  10990    384    513    340       C  
ATOM   2534  O   CYS B 296      -2.929   3.998 -43.713  1.00 86.34           O  
ANISOU 2534  O   CYS B 296    11152  10902  10750    412    510    339       O  
ATOM   2535  CB  CYS B 296      -2.478   3.681 -46.995  1.00 87.43           C  
ANISOU 2535  CB  CYS B 296    11491  10876  10853    372    530    336       C  
ATOM   2536  SG  CYS B 296      -3.061   1.977 -46.641  1.00 88.45           S  
ANISOU 2536  SG  CYS B 296    11562  11020  11025    408    574    359       S  
ATOM   2537  N   ILE B 297      -0.991   4.956 -44.346  1.00 81.85           N  
ANISOU 2537  N   ILE B 297    10631  10334  10133    363    544    366       N  
ATOM   2538  CA  ILE B 297      -0.465   4.770 -42.989  1.00 78.56           C  
ANISOU 2538  CA  ILE B 297    10120  10002   9728    375    574    392       C  
ATOM   2539  C   ILE B 297      -1.145   5.730 -42.017  1.00 76.20           C  
ANISOU 2539  C   ILE B 297     9786   9737   9431    383    513    359       C  
ATOM   2540  O   ILE B 297      -1.584   5.324 -40.938  1.00 75.73           O  
ANISOU 2540  O   ILE B 297     9651   9729   9393    409    515    362       O  
ATOM   2541  CB  ILE B 297       1.082   4.865 -42.924  1.00 68.21           C  
ANISOU 2541  CB  ILE B 297     8794   8725   8397    353    627    431       C  
ATOM   2542  CG1 ILE B 297       1.605   6.300 -42.934  1.00 68.66           C  
ANISOU 2542  CG1 ILE B 297     8879   8784   8424    325    591    414       C  
ATOM   2543  CG2 ILE B 297       1.755   4.017 -43.971  1.00 68.09           C  
ANISOU 2543  CG2 ILE B 297     8821   8673   8378    343    683    462       C  
ATOM   2544  CD1 ILE B 297       3.009   6.380 -42.406  1.00 68.34           C  
ANISOU 2544  CD1 ILE B 297     8794   8798   8372    311    640    452       C  
ATOM   2545  N   SER B 298      -1.284   7.001 -42.388  1.00 80.70           N  
ANISOU 2545  N   SER B 298    10409  10277   9977    363    457    325       N  
ATOM   2546  CA  SER B 298      -1.979   7.926 -41.503  1.00 81.33           C  
ANISOU 2546  CA  SER B 298    10459  10386  10058    371    397    291       C  
ATOM   2547  C   SER B 298      -3.422   7.483 -41.271  1.00 78.15           C  
ANISOU 2547  C   SER B 298    10042   9969   9682    401    362    263       C  
ATOM   2548  O   SER B 298      -4.002   7.770 -40.217  1.00 78.28           O  
ANISOU 2548  O   SER B 298    10002  10029   9711    419    332    248       O  
ATOM   2549  CB  SER B 298      -1.907   9.344 -42.078  1.00 79.80           C  
ANISOU 2549  CB  SER B 298    10333  10153   9834    343    343    258       C  
ATOM   2550  OG  SER B 298      -2.952   9.583 -42.991  1.00 82.99           O  
ANISOU 2550  OG  SER B 298    10809  10486  10237    343    293    220       O  
ATOM   2551  N   TYR B 299      -3.995   6.750 -42.228  1.00 78.16           N  
ANISOU 2551  N   TYR B 299    10092   9911   9694    407    367    259       N  
ATOM   2552  CA  TYR B 299      -5.318   6.169 -42.034  1.00 81.83           C  
ANISOU 2552  CA  TYR B 299    10540  10362  10188    436    342    237       C  
ATOM   2553  C   TYR B 299      -5.315   5.069 -40.977  1.00 80.68           C  
ANISOU 2553  C   TYR B 299    10302  10280  10073    464    389    269       C  
ATOM   2554  O   TYR B 299      -6.321   4.900 -40.280  1.00 81.01           O  
ANISOU 2554  O   TYR B 299    10303  10340  10138    489    361    251       O  
ATOM   2555  CB  TYR B 299      -5.873   5.631 -43.362  1.00 89.93           C  
ANISOU 2555  CB  TYR B 299    11643  11308  11218    434    338    226       C  
ATOM   2556  CG  TYR B 299      -6.531   6.641 -44.305  1.00 85.04           C  
ANISOU 2556  CG  TYR B 299    11112  10619  10580    419    271    180       C  
ATOM   2557  CD1 TYR B 299      -6.509   8.008 -44.038  1.00 82.02           C  
ANISOU 2557  CD1 TYR B 299    10743  10243  10175    403    219    152       C  
ATOM   2558  CD2 TYR B 299      -7.205   6.207 -45.458  1.00 84.98           C  
ANISOU 2558  CD2 TYR B 299    11174  10537  10578    421    259    163       C  
ATOM   2559  CE1 TYR B 299      -7.135   8.925 -44.899  1.00 89.50           C  
ANISOU 2559  CE1 TYR B 299    11773  11127  11106    389    157    110       C  
ATOM   2560  CE2 TYR B 299      -7.827   7.119 -46.329  1.00 88.90           C  
ANISOU 2560  CE2 TYR B 299    11752  10969  11056    407    197    121       C  
ATOM   2561  CZ  TYR B 299      -7.789   8.474 -46.036  1.00 94.05           C  
ANISOU 2561  CZ  TYR B 299    12417  11631  11687    391    146     94       C  
ATOM   2562  OH  TYR B 299      -8.383   9.385 -46.872  1.00 90.97           O  
ANISOU 2562  OH  TYR B 299    12107  11179  11280    378     85     53       O  
ATOM   2563  N   VAL B 300      -4.224   4.298 -40.844  1.00 76.84           N  
ANISOU 2563  N   VAL B 300     9782   9827   9587    461    459    316       N  
ATOM   2564  CA  VAL B 300      -4.212   3.232 -39.820  1.00 76.95           C  
ANISOU 2564  CA  VAL B 300     9706   9901   9629    488    505    347       C  
ATOM   2565  C   VAL B 300      -4.108   3.799 -38.404  1.00 77.33           C  
ANISOU 2565  C   VAL B 300     9678  10027   9679    498    491    347       C  
ATOM   2566  O   VAL B 300      -4.497   3.134 -37.441  1.00 74.93           O  
ANISOU 2566  O   VAL B 300     9299   9770   9399    525    507    359       O  
ATOM   2567  CB  VAL B 300      -3.082   2.195 -40.020  1.00 68.98           C  
ANISOU 2567  CB  VAL B 300     8678   8910   8623    484    586    399       C  
ATOM   2568  CG1 VAL B 300      -2.962   1.828 -41.477  1.00 73.77           C  
ANISOU 2568  CG1 VAL B 300     9368   9442   9221    469    600    400       C  
ATOM   2569  CG2 VAL B 300      -1.751   2.668 -39.439  1.00 68.70           C  
ANISOU 2569  CG2 VAL B 300     8606   8929   8565    467    617    427       C  
ATOM   2570  N   ASN B 301      -3.640   5.030 -38.255  1.00 79.73           N  
ANISOU 2570  N   ASN B 301     9996  10341   9955    477    459    332       N  
ATOM   2571  CA  ASN B 301      -3.444   5.619 -36.942  1.00 78.31           C  
ANISOU 2571  CA  ASN B 301     9746  10235   9774    484    447    331       C  
ATOM   2572  C   ASN B 301      -4.750   5.640 -36.148  1.00 82.28           C  
ANISOU 2572  C   ASN B 301    10208  10756  10299    513    402    302       C  
ATOM   2573  O   ASN B 301      -4.755   5.944 -34.941  1.00 85.06           O  
ANISOU 2573  O   ASN B 301    10491  11172  10655    527    393    302       O  
ATOM   2574  CB  ASN B 301      -2.874   7.033 -37.083  1.00 77.40           C  
ANISOU 2574  CB  ASN B 301     9668  10116   9626    455    410    312       C  
ATOM   2575  CG  ASN B 301      -2.597   7.690 -35.741  1.00 85.11           C  
ANISOU 2575  CG  ASN B 301    10572  11168  10599    462    397    312       C  
ATOM   2576  OD1 ASN B 301      -3.267   8.656 -35.351  1.00 88.50           O  
ANISOU 2576  OD1 ASN B 301    11003  11600  11023    464    335    274       O  
ATOM   2577  ND2 ASN B 301      -1.612   7.158 -35.018  1.00 83.38           N  
ANISOU 2577  ND2 ASN B 301    10289  11011  10383    466    454    354       N  
ATOM   2578  N   SER B 302      -5.865   5.305 -36.804  1.00 85.25           N  
ANISOU 2578  N   SER B 302    10625  11075  10691    524    374    277       N  
ATOM   2579  CA  SER B 302      -7.115   5.140 -36.072  1.00 86.46           C  
ANISOU 2579  CA  SER B 302    10737  11245  10870    554    339    253       C  
ATOM   2580  C   SER B 302      -7.124   3.820 -35.314  1.00 87.40           C  
ANISOU 2580  C   SER B 302    10778  11411  11019    582    394    290       C  
ATOM   2581  O   SER B 302      -7.262   3.799 -34.084  1.00 87.59           O  
ANISOU 2581  O   SER B 302    10726  11501  11055    602    395    295       O  
ATOM   2582  CB  SER B 302      -8.295   5.211 -37.025  1.00 79.08           C  
ANISOU 2582  CB  SER B 302     9871  10233   9943    556    290    214       C  
ATOM   2583  OG  SER B 302      -8.171   4.173 -37.954  1.00 83.05           O  
ANISOU 2583  OG  SER B 302    10408  10691  10455    555    332    235       O  
ATOM   2584  N   CYS B 303      -6.945   2.704 -36.026  1.00 83.30           N  
ANISOU 2584  N   CYS B 303    10276  10860  10513    584    442    316       N  
ATOM   2585  CA  CYS B 303      -7.040   1.385 -35.401  1.00 85.62           C  
ANISOU 2585  CA  CYS B 303    10502  11193  10839    612    494    349       C  
ATOM   2586  C   CYS B 303      -5.801   1.022 -34.580  1.00 86.81           C  
ANISOU 2586  C   CYS B 303    10585  11416  10985    611    555    396       C  
ATOM   2587  O   CYS B 303      -5.482  -0.158 -34.422  1.00 86.13           O  
ANISOU 2587  O   CYS B 303    10460  11349  10918    625    614    434       O  
ATOM   2588  CB  CYS B 303      -7.314   0.308 -36.465  1.00 79.28           C  
ANISOU 2588  CB  CYS B 303     9742  10330  10052    615    522    359       C  
ATOM   2589  SG  CYS B 303      -5.879  -0.305 -37.405  1.00 73.41           S  
ANISOU 2589  SG  CYS B 303     9034   9566   9292    591    593    403       S  
ATOM   2590  N   LEU B 304      -5.109   2.015 -34.031  1.00 86.47           N  
ANISOU 2590  N   LEU B 304    10526  11412  10916    597    542    394       N  
ATOM   2591  CA  LEU B 304      -3.993   1.773 -33.125  1.00 82.46           C  
ANISOU 2591  CA  LEU B 304     9948  10977  10404    598    593    434       C  
ATOM   2592  C   LEU B 304      -4.270   2.210 -31.694  1.00 85.19           C  
ANISOU 2592  C   LEU B 304    10218  11396  10755    618    571    427       C  
ATOM   2593  O   LEU B 304      -3.872   1.510 -30.763  1.00 85.05           O  
ANISOU 2593  O   LEU B 304    10124  11441  10751    636    616    461       O  
ATOM   2594  CB  LEU B 304      -2.737   2.482 -33.636  1.00 77.87           C  
ANISOU 2594  CB  LEU B 304     9406  10389   9789    564    607    445       C  
ATOM   2595  CG  LEU B 304      -2.393   2.138 -35.075  1.00 77.25           C  
ANISOU 2595  CG  LEU B 304     9409  10241   9703    543    628    452       C  
ATOM   2596  CD1 LEU B 304      -1.079   2.779 -35.471  1.00 78.05           C  
ANISOU 2596  CD1 LEU B 304     9539  10343   9772    511    647    468       C  
ATOM   2597  CD2 LEU B 304      -2.329   0.636 -35.225  1.00 75.24           C  
ANISOU 2597  CD2 LEU B 304     9128   9985   9473    560    689    488       C  
ATOM   2598  N   ASN B 305      -4.927   3.356 -31.488  1.00 91.25           N  
ANISOU 2598  N   ASN B 305    11003  12157  11512    615    503    384       N  
ATOM   2599  CA  ASN B 305      -5.321   3.745 -30.137  1.00 90.37           C  
ANISOU 2599  CA  ASN B 305    10819  12111  11407    637    478    373       C  
ATOM   2600  C   ASN B 305      -6.084   2.638 -29.426  1.00 91.33           C  
ANISOU 2600  C   ASN B 305    10877  12263  11564    673    501    387       C  
ATOM   2601  O   ASN B 305      -5.842   2.442 -28.223  1.00 88.97           O  
ANISOU 2601  O   ASN B 305    10497  12036  11271    691    521    407       O  
ATOM   2602  CB  ASN B 305      -6.148   5.042 -30.138  1.00 87.67           C  
ANISOU 2602  CB  ASN B 305    10511  11746  11052    631    397    320       C  
ATOM   2603  CG  ASN B 305      -5.548   6.123 -31.011  1.00 91.80           C  
ANISOU 2603  CG  ASN B 305    11109  12228  11543    595    371    303       C  
ATOM   2604  OD1 ASN B 305      -6.271   6.902 -31.642  1.00 95.00           O  
ANISOU 2604  OD1 ASN B 305    11576  12580  11940    585    312    261       O  
ATOM   2605  ND2 ASN B 305      -4.220   6.164 -31.077  1.00 96.08           N  
ANISOU 2605  ND2 ASN B 305    11648  12792  12067    575    414    335       N  
ATOM   2606  N   PRO B 306      -6.989   1.886 -30.071  1.00 88.74           N  
ANISOU 2606  N   PRO B 306    10576  11883  11258    684    498    379       N  
ATOM   2607  CA  PRO B 306      -7.508   0.679 -29.408  1.00 86.48           C  
ANISOU 2607  CA  PRO B 306    10224  11628  11006    717    533    402       C  
ATOM   2608  C   PRO B 306      -6.412  -0.266 -28.961  1.00 85.95           C  
ANISOU 2608  C   PRO B 306    10102  11612  10945    722    610    456       C  
ATOM   2609  O   PRO B 306      -6.474  -0.771 -27.837  1.00 87.64           O  
ANISOU 2609  O   PRO B 306    10235  11889  11175    747    633    476       O  
ATOM   2610  CB  PRO B 306      -8.411   0.066 -30.476  1.00 86.08           C  
ANISOU 2610  CB  PRO B 306    10230  11502  10975    720    522    386       C  
ATOM   2611  CG  PRO B 306      -8.948   1.245 -31.170  1.00 89.20           C  
ANISOU 2611  CG  PRO B 306    10698  11842  11350    702    453    337       C  
ATOM   2612  CD  PRO B 306      -7.814   2.242 -31.240  1.00 89.18           C  
ANISOU 2612  CD  PRO B 306    10717  11855  11312    672    451    341       C  
ATOM   2613  N   PHE B 307      -5.393  -0.504 -29.793  1.00 87.80           N  
ANISOU 2613  N   PHE B 307    10376  11821  11164    698    650    481       N  
ATOM   2614  CA  PHE B 307      -4.302  -1.373 -29.358  1.00 88.53           C  
ANISOU 2614  CA  PHE B 307    10415  11962  11260    702    723    533       C  
ATOM   2615  C   PHE B 307      -3.467  -0.716 -28.260  1.00 89.74           C  
ANISOU 2615  C   PHE B 307    10511  12191  11396    700    729    545       C  
ATOM   2616  O   PHE B 307      -3.028  -1.392 -27.324  1.00 91.27           O  
ANISOU 2616  O   PHE B 307    10629  12447  11600    718    774    580       O  
ATOM   2617  CB  PHE B 307      -3.392  -1.746 -30.524  1.00 93.50           C  
ANISOU 2617  CB  PHE B 307    11102  12546  11877    676    764    555       C  
ATOM   2618  CG  PHE B 307      -3.935  -2.825 -31.442  1.00101.24           C  
ANISOU 2618  CG  PHE B 307    12117  13468  12880    683    785    561       C  
ATOM   2619  CD1 PHE B 307      -4.836  -2.516 -32.451  1.00108.89           C  
ANISOU 2619  CD1 PHE B 307    13161  14362  13851    676    738    523       C  
ATOM   2620  CD2 PHE B 307      -3.497  -4.136 -31.332  1.00 99.81           C  
ANISOU 2620  CD2 PHE B 307    11896  13306  12720    696    852    605       C  
ATOM   2621  CE1 PHE B 307      -5.298  -3.503 -33.329  1.00 99.18           C  
ANISOU 2621  CE1 PHE B 307    11966  13077  12641    682    757    528       C  
ATOM   2622  CE2 PHE B 307      -3.960  -5.124 -32.194  1.00112.47           C  
ANISOU 2622  CE2 PHE B 307    13534  14856  14346    703    872    610       C  
ATOM   2623  CZ  PHE B 307      -4.862  -4.806 -33.193  1.00109.40           C  
ANISOU 2623  CZ  PHE B 307    13219  14392  13957    696    824    571       C  
ATOM   2624  N   LEU B 308      -3.221   0.597 -28.356  1.00 89.80           N  
ANISOU 2624  N   LEU B 308    10553  12193  11375    678    683    517       N  
ATOM   2625  CA  LEU B 308      -2.372   1.247 -27.355  1.00 88.76           C  
ANISOU 2625  CA  LEU B 308    10369  12131  11225    675    688    528       C  
ATOM   2626  C   LEU B 308      -3.006   1.209 -25.967  1.00 94.41           C  
ANISOU 2626  C   LEU B 308    11003  12912  11956    707    673    524       C  
ATOM   2627  O   LEU B 308      -2.312   0.954 -24.975  1.00 93.92           O  
ANISOU 2627  O   LEU B 308    10871  12920  11894    718    710    554       O  
ATOM   2628  CB  LEU B 308      -2.056   2.684 -27.763  1.00 83.76           C  
ANISOU 2628  CB  LEU B 308     9790  11474  10559    645    639    497       C  
ATOM   2629  CG  LEU B 308      -1.027   2.835 -28.878  1.00 83.02           C  
ANISOU 2629  CG  LEU B 308     9762  11338  10445    611    664    510       C  
ATOM   2630  CD1 LEU B 308      -1.214   4.167 -29.590  1.00 86.47           C  
ANISOU 2630  CD1 LEU B 308    10273  11725  10856    584    601    468       C  
ATOM   2631  CD2 LEU B 308       0.377   2.702 -28.315  1.00 84.88           C  
ANISOU 2631  CD2 LEU B 308     9950  11633  10670    603    718    552       C  
ATOM   2632  N   TYR B 309      -4.316   1.466 -25.870  1.00 93.38           N  
ANISOU 2632  N   TYR B 309    10880  12760  11838    723    620    486       N  
ATOM   2633  CA  TYR B 309      -4.987   1.325 -24.581  1.00 93.13           C  
ANISOU 2633  CA  TYR B 309    10771  12789  11824    756    609    483       C  
ATOM   2634  C   TYR B 309      -4.831  -0.091 -24.029  1.00 89.67           C  
ANISOU 2634  C   TYR B 309    10268  12391  11413    781    675    528       C  
ATOM   2635  O   TYR B 309      -4.751  -0.269 -22.807  1.00 92.16           O  
ANISOU 2635  O   TYR B 309    10504  12777  11734    804    689    544       O  
ATOM   2636  CB  TYR B 309      -6.475   1.685 -24.689  1.00 92.21           C  
ANISOU 2636  CB  TYR B 309    10679  12637  11721    769    546    437       C  
ATOM   2637  CG  TYR B 309      -6.775   3.098 -25.151  1.00 85.48           C  
ANISOU 2637  CG  TYR B 309     9888  11746  10844    747    475    390       C  
ATOM   2638  CD1 TYR B 309      -6.026   4.174 -24.706  1.00 83.40           C  
ANISOU 2638  CD1 TYR B 309     9618  11519  10553    731    457    383       C  
ATOM   2639  CD2 TYR B 309      -7.839   3.359 -26.012  1.00 85.73           C  
ANISOU 2639  CD2 TYR B 309     9984  11708  10882    743    426    351       C  
ATOM   2640  CE1 TYR B 309      -6.308   5.483 -25.133  1.00 84.82           C  
ANISOU 2640  CE1 TYR B 309     9854  11663  10711    711    391    339       C  
ATOM   2641  CE2 TYR B 309      -8.131   4.657 -26.436  1.00 87.90           C  
ANISOU 2641  CE2 TYR B 309    10316  11948  11135    724    361    307       C  
ATOM   2642  CZ  TYR B 309      -7.362   5.718 -25.992  1.00 84.35           C  
ANISOU 2642  CZ  TYR B 309     9859  11533  10657    708    344    301       C  
ATOM   2643  OH  TYR B 309      -7.649   7.006 -26.407  1.00 85.81           O  
ANISOU 2643  OH  TYR B 309    10100  11683  10821    688    279    258       O  
ATOM   2644  N   ALA B 310      -4.766  -1.106 -24.899  1.00 85.93           N  
ANISOU 2644  N   ALA B 310     9822  11872  10953    778    715    550       N  
ATOM   2645  CA  ALA B 310      -4.553  -2.467 -24.416  1.00 90.37           C  
ANISOU 2645  CA  ALA B 310    10324  12471  11542    801    780    594       C  
ATOM   2646  C   ALA B 310      -3.165  -2.621 -23.807  1.00 96.11           C  
ANISOU 2646  C   ALA B 310    11003  13261  12255    795    833    636       C  
ATOM   2647  O   ALA B 310      -3.027  -2.974 -22.629  1.00 99.02           O  
ANISOU 2647  O   ALA B 310    11291  13699  12632    819    856    658       O  
ATOM   2648  CB  ALA B 310      -4.761  -3.470 -25.545  1.00 86.68           C  
ANISOU 2648  CB  ALA B 310     9902  11939  11092    797    809    606       C  
ATOM   2649  N   PHE B 311      -2.122  -2.335 -24.582  1.00 96.53           N  
ANISOU 2649  N   PHE B 311    11102  13288  12285    765    852    647       N  
ATOM   2650  CA  PHE B 311      -0.765  -2.476 -24.072  1.00 90.44           C  
ANISOU 2650  CA  PHE B 311    10289  12573  11501    758    903    686       C  
ATOM   2651  C   PHE B 311      -0.430  -1.499 -22.942  1.00 88.22           C  
ANISOU 2651  C   PHE B 311     9960  12359  11202    761    877    677       C  
ATOM   2652  O   PHE B 311       0.638  -1.636 -22.334  1.00 85.96           O  
ANISOU 2652  O   PHE B 311     9626  12127  10907    759    919    710       O  
ATOM   2653  CB  PHE B 311       0.220  -2.306 -25.231  1.00 97.07           C  
ANISOU 2653  CB  PHE B 311    11195  13366  12320    722    924    696       C  
ATOM   2654  CG  PHE B 311       0.820  -3.600 -25.712  1.00103.38           C  
ANISOU 2654  CG  PHE B 311    11991  14155  13133    723    995    740       C  
ATOM   2655  CD1 PHE B 311       0.007  -4.609 -26.214  1.00105.07           C  
ANISOU 2655  CD1 PHE B 311    12218  14328  13375    739   1007    743       C  
ATOM   2656  CD2 PHE B 311       2.198  -3.793 -25.708  1.00105.33           C  
ANISOU 2656  CD2 PHE B 311    12224  14429  13366    708   1047    777       C  
ATOM   2657  CE1 PHE B 311       0.550  -5.802 -26.663  1.00102.12           C  
ANISOU 2657  CE1 PHE B 311    11841  13944  13016    740   1071    782       C  
ATOM   2658  CE2 PHE B 311       2.748  -4.985 -26.161  1.00111.49           C  
ANISOU 2658  CE2 PHE B 311    13001  15199  14160    709   1112    817       C  
ATOM   2659  CZ  PHE B 311       1.922  -5.990 -26.640  1.00100.94           C  
ANISOU 2659  CZ  PHE B 311    11677  13823  12851    725   1124    819       C  
ATOM   2660  N   PHE B 312      -1.297  -0.521 -22.635  1.00 89.06           N  
ANISOU 2660  N   PHE B 312    10075  12462  11302    765    810    633       N  
ATOM   2661  CA  PHE B 312      -0.859   0.517 -21.710  1.00 87.28           C  
ANISOU 2661  CA  PHE B 312     9814  12293  11055    763    784    622       C  
ATOM   2662  C   PHE B 312      -1.929   1.057 -20.765  1.00 87.73           C  
ANISOU 2662  C   PHE B 312     9833  12381  11119    788    731    590       C  
ATOM   2663  O   PHE B 312      -1.543   1.586 -19.718  1.00 84.06           O  
ANISOU 2663  O   PHE B 312     9315  11981  10643    796    724    592       O  
ATOM   2664  CB  PHE B 312      -0.266   1.709 -22.469  1.00 89.88           C  
ANISOU 2664  CB  PHE B 312    10211  12586  11354    726    751    599       C  
ATOM   2665  CG  PHE B 312       1.017   1.409 -23.202  1.00 90.69           C  
ANISOU 2665  CG  PHE B 312    10343  12672  11444    700    803    633       C  
ATOM   2666  CD1 PHE B 312       0.988   0.930 -24.507  1.00 90.69           C  
ANISOU 2666  CD1 PHE B 312    10410  12600  11447    683    819    636       C  
ATOM   2667  CD2 PHE B 312       2.248   1.567 -22.585  1.00 89.67           C  
ANISOU 2667  CD2 PHE B 312    10171  12600  11300    693    837    661       C  
ATOM   2668  CE1 PHE B 312       2.159   0.654 -25.201  1.00 88.65           C  
ANISOU 2668  CE1 PHE B 312    10179  12326  11177    659    867    666       C  
ATOM   2669  CE2 PHE B 312       3.433   1.283 -23.278  1.00 91.87           C  
ANISOU 2669  CE2 PHE B 312    10476  12863  11568    668    885    692       C  
ATOM   2670  CZ  PHE B 312       3.380   0.825 -24.590  1.00 90.67           C  
ANISOU 2670  CZ  PHE B 312    10394  12639  11419    651    900    694       C  
ATOM   2671  N   ASP B 313      -3.238   1.005 -21.071  1.00 89.09           N  
ANISOU 2671  N   ASP B 313    10031  12512  11308    800    691    559       N  
ATOM   2672  CA  ASP B 313      -4.226   1.537 -20.123  1.00 95.24           C  
ANISOU 2672  CA  ASP B 313    10771  13324  12093    824    641    528       C  
ATOM   2673  C   ASP B 313      -4.675   0.468 -19.154  1.00 96.44           C  
ANISOU 2673  C   ASP B 313    10844  13527  12273    861    675    554       C  
ATOM   2674  O   ASP B 313      -5.340  -0.504 -19.561  1.00 93.62           O  
ANISOU 2674  O   ASP B 313    10493  13137  11942    874    694    562       O  
ATOM   2675  CB  ASP B 313      -5.450   2.138 -20.818  1.00 98.96           C  
ANISOU 2675  CB  ASP B 313    11304  13730  12567    819    575    478       C  
ATOM   2676  CG  ASP B 313      -6.274   3.049 -19.858  1.00 99.00           C  
ANISOU 2676  CG  ASP B 313    11277  13770  12569    837    514    441       C  
ATOM   2677  OD1 ASP B 313      -5.821   3.270 -18.709  1.00105.38           O  
ANISOU 2677  OD1 ASP B 313    12018  14652  13369    850    523    454       O  
ATOM   2678  OD2 ASP B 313      -7.390   3.506 -20.204  1.00 89.79           O  
ANISOU 2678  OD2 ASP B 313    10148  12562  11408    840    458    400       O  
ATOM   2679  N   PRO B 314      -4.402   0.607 -17.868  1.00 87.87           N  
ANISOU 2679  N   PRO B 314     9683  12519  11184    881    683    566       N  
ATOM   2680  CA  PRO B 314      -4.940  -0.313 -16.872  1.00 82.61           C  
ANISOU 2680  CA  PRO B 314     8940  11903  10543    918    709    587       C  
ATOM   2681  C   PRO B 314      -6.464  -0.389 -16.836  1.00 90.19           C  
ANISOU 2681  C   PRO B 314     9905  12837  11526    939    666    555       C  
ATOM   2682  O   PRO B 314      -7.014  -1.487 -16.967  1.00100.10           O  
ANISOU 2682  O   PRO B 314    11146  14078  12811    957    695    572       O  
ATOM   2683  CB  PRO B 314      -4.369   0.236 -15.561  1.00 93.36           C  
ANISOU 2683  CB  PRO B 314    10234  13350  11889    930    708    595       C  
ATOM   2684  CG  PRO B 314      -3.177   1.071 -15.976  1.00 96.98           C  
ANISOU 2684  CG  PRO B 314    10729  13804  12317    896    707    595       C  
ATOM   2685  CD  PRO B 314      -3.541   1.647 -17.277  1.00 94.88           C  
ANISOU 2685  CD  PRO B 314    10554  13454  12043    868    667    561       C  
ATOM   2686  N   ARG B 315      -7.156   0.745 -16.645  1.00 92.88           N  
ANISOU 2686  N   ARG B 315    10263  13172  11855    938    598    509       N  
ATOM   2687  CA  ARG B 315      -8.623   0.736 -16.602  1.00 96.81           C  
ANISOU 2687  CA  ARG B 315    10766  13645  12374    958    554    476       C  
ATOM   2688  C   ARG B 315      -9.213  -0.035 -17.773  1.00 98.27           C  
ANISOU 2688  C   ARG B 315    11006  13753  12581    953    563    475       C  
ATOM   2689  O   ARG B 315     -10.233  -0.726 -17.630  1.00 95.88           O  
ANISOU 2689  O   ARG B 315    10683  13441  12307    977    562    472       O  
ATOM   2690  CB  ARG B 315      -9.166   2.167 -16.604  1.00100.14           C  
ANISOU 2690  CB  ARG B 315    11222  14051  12775    948    476    423       C  
ATOM   2691  CG  ARG B 315     -10.658   2.316 -16.941  1.00101.33           C  
ANISOU 2691  CG  ARG B 315    11404  14153  12945    960    423    382       C  
ATOM   2692  CD  ARG B 315     -11.184   3.715 -16.586  1.00110.31           C  
ANISOU 2692  CD  ARG B 315    12553  15296  14063    957    349    333       C  
ATOM   2693  NE  ARG B 315     -10.639   4.206 -15.313  1.00111.64           N  
ANISOU 2693  NE  ARG B 315    12655  15547  14216    969    350    341       N  
ATOM   2694  CZ  ARG B 315     -11.357   4.530 -14.232  1.00107.65           C  
ANISOU 2694  CZ  ARG B 315    12096  15090  13715    997    320    323       C  
ATOM   2695  NH1 ARG B 315     -12.683   4.437 -14.241  1.00111.99           N  
ANISOU 2695  NH1 ARG B 315    12650  15615  14286   1015    284    295       N  
ATOM   2696  NH2 ARG B 315     -10.742   4.964 -13.132  1.00112.54           N  
ANISOU 2696  NH2 ARG B 315    12657  15784  14318   1007    325    333       N  
ATOM   2697  N   PHE B 316      -8.572   0.063 -18.937  1.00 91.71           N  
ANISOU 2697  N   PHE B 316    10243  12867  11736    921    573    477       N  
ATOM   2698  CA  PHE B 316      -9.058  -0.621 -20.123  1.00 95.60           C  
ANISOU 2698  CA  PHE B 316    10793  13284  12246    913    580    475       C  
ATOM   2699  C   PHE B 316      -8.900  -2.133 -19.997  1.00 94.46           C  
ANISOU 2699  C   PHE B 316    10605  13154  12130    932    649    521       C  
ATOM   2700  O   PHE B 316      -9.895  -2.865 -20.023  1.00 91.52           O  
ANISOU 2700  O   PHE B 316    10222  12762  11788    953    649    518       O  
ATOM   2701  CB  PHE B 316      -8.334  -0.075 -21.354  1.00 97.21           C  
ANISOU 2701  CB  PHE B 316    11079  13429  12425    875    574    466       C  
ATOM   2702  CG  PHE B 316      -8.754  -0.718 -22.639  1.00 93.17           C  
ANISOU 2702  CG  PHE B 316    10633  12839  11930    865    581    463       C  
ATOM   2703  CD1 PHE B 316     -10.033  -0.532 -23.132  1.00 95.03           C  
ANISOU 2703  CD1 PHE B 316    10909  13020  12179    871    530    424       C  
ATOM   2704  CD2 PHE B 316      -7.861  -1.497 -23.356  1.00 90.54           C  
ANISOU 2704  CD2 PHE B 316    10321  12484  11596    850    639    499       C  
ATOM   2705  CE1 PHE B 316     -10.421  -1.134 -24.300  1.00 95.94           C  
ANISOU 2705  CE1 PHE B 316    11082  13062  12308    863    536    420       C  
ATOM   2706  CE2 PHE B 316      -8.236  -2.095 -24.519  1.00 88.58           C  
ANISOU 2706  CE2 PHE B 316    10132  12165  11362    842    645    496       C  
ATOM   2707  CZ  PHE B 316      -9.521  -1.914 -25.000  1.00 89.79           C  
ANISOU 2707  CZ  PHE B 316    10323  12264  11528    849    594    456       C  
ATOM   2708  N   ARG B 317      -7.656  -2.619 -19.831  1.00 95.43           N  
ANISOU 2708  N   ARG B 317    10702  13313  12245    925    709    565       N  
ATOM   2709  CA  ARG B 317      -7.400  -4.063 -19.815  1.00 88.97           C  
ANISOU 2709  CA  ARG B 317     9848  12504  11453    939    777    610       C  
ATOM   2710  C   ARG B 317      -8.326  -4.785 -18.844  1.00 92.58           C  
ANISOU 2710  C   ARG B 317    10235  13000  11941    978    784    618       C  
ATOM   2711  O   ARG B 317      -8.857  -5.861 -19.150  1.00 96.71           O  
ANISOU 2711  O   ARG B 317    10753  13497  12494    992    810    633       O  
ATOM   2712  CB  ARG B 317      -5.953  -4.363 -19.417  1.00 82.61           C  
ANISOU 2712  CB  ARG B 317     9005  11751  10633    932    836    655       C  
ATOM   2713  CG  ARG B 317      -4.908  -3.440 -19.966  1.00 80.95           C  
ANISOU 2713  CG  ARG B 317     8843  11526  10387    897    828    649       C  
ATOM   2714  CD  ARG B 317      -3.598  -3.583 -19.200  1.00 80.45           C  
ANISOU 2714  CD  ARG B 317     8724  11533  10311    896    878    690       C  
ATOM   2715  NE  ARG B 317      -2.921  -4.835 -19.536  1.00 87.82           N  
ANISOU 2715  NE  ARG B 317     9645  12464  11258    897    949    736       N  
ATOM   2716  CZ  ARG B 317      -1.688  -4.899 -20.038  1.00 96.68           C  
ANISOU 2716  CZ  ARG B 317    10789  13582  12364    873    988    762       C  
ATOM   2717  NH1 ARG B 317      -1.002  -3.779 -20.234  1.00102.81           N  
ANISOU 2717  NH1 ARG B 317    11598  14356  13108    846    962    745       N  
ATOM   2718  NH2 ARG B 317      -1.138  -6.075 -20.340  1.00 92.09           N  
ANISOU 2718  NH2 ARG B 317    10196  12997  11797    875   1052    803       N  
ATOM   2719  N   GLN B 318      -8.514  -4.208 -17.656  1.00 87.77           N  
ANISOU 2719  N   GLN B 318     9569  12454  11325    996    760    609       N  
ATOM   2720  CA  GLN B 318      -9.366  -4.822 -16.649  1.00106.04           C  
ANISOU 2720  CA  GLN B 318    11813  14811  13666   1033    766    616       C  
ATOM   2721  C   GLN B 318     -10.816  -4.877 -17.106  1.00116.90           C  
ANISOU 2721  C   GLN B 318    13220  16131  15065   1043    722    580       C  
ATOM   2722  O   GLN B 318     -11.473  -5.919 -16.995  1.00110.63           O  
ANISOU 2722  O   GLN B 318    12398  15333  14304   1066    746    596       O  
ATOM   2723  CB  GLN B 318      -9.272  -4.041 -15.346  1.00101.92           C  
ANISOU 2723  CB  GLN B 318    11233  14366  13128   1048    743    608       C  
ATOM   2724  CG  GLN B 318     -10.213  -4.559 -14.253  1.00108.87           C  
ANISOU 2724  CG  GLN B 318    12040  15292  14034   1088    744    612       C  
ATOM   2725  CD  GLN B 318     -11.334  -3.582 -13.917  1.00126.89           C  
ANISOU 2725  CD  GLN B 318    14329  17570  16314   1097    671    562       C  
ATOM   2726  OE1 GLN B 318     -11.755  -2.781 -14.759  1.00137.97           O  
ANISOU 2726  OE1 GLN B 318    15802  18913  17706   1076    619    521       O  
ATOM   2727  NE2 GLN B 318     -11.809  -3.631 -12.678  1.00127.32           N  
ANISOU 2727  NE2 GLN B 318    14311  17687  16377   1129    667    565       N  
ATOM   2728  N   ALA B 319     -11.343  -3.752 -17.598  1.00114.09           N  
ANISOU 2728  N   ALA B 319    12921  15734  14693   1027    655    532       N  
ATOM   2729  CA  ALA B 319     -12.739  -3.717 -18.012  1.00109.65           C  
ANISOU 2729  CA  ALA B 319    12390  15121  14152   1037    609    495       C  
ATOM   2730  C   ALA B 319     -13.038  -4.744 -19.096  1.00104.44           C  
ANISOU 2730  C   ALA B 319    11772  14394  13518   1033    635    506       C  
ATOM   2731  O   ALA B 319     -14.215  -5.029 -19.348  1.00109.70           O  
ANISOU 2731  O   ALA B 319    12450  15022  14210   1046    609    484       O  
ATOM   2732  CB  ALA B 319     -13.116  -2.309 -18.485  1.00106.30           C  
ANISOU 2732  CB  ALA B 319    12028  14658  13703   1016    535    442       C  
ATOM   2733  N   CYS B 320     -12.002  -5.308 -19.734  1.00110.76           N  
ANISOU 2733  N   CYS B 320    12593  15179  14311   1014    687    539       N  
ATOM   2734  CA  CYS B 320     -12.177  -6.369 -20.727  1.00115.85           C  
ANISOU 2734  CA  CYS B 320    13272  15765  14980   1011    718    554       C  
ATOM   2735  C   CYS B 320     -12.307  -7.737 -20.068  1.00114.22           C  
ANISOU 2735  C   CYS B 320    12994  15595  14807   1041    775    596       C  
ATOM   2736  O   CYS B 320     -13.327  -8.422 -20.217  1.00116.94           O  
ANISOU 2736  O   CYS B 320    13335  15911  15185   1059    771    590       O  
ATOM   2737  CB  CYS B 320     -10.998  -6.403 -21.710  1.00120.41           C  
ANISOU 2737  CB  CYS B 320    13904  16310  15536    979    750    573       C  
ATOM   2738  SG  CYS B 320     -10.393  -4.833 -22.379  1.00107.48           S  
ANISOU 2738  SG  CYS B 320    12341  14643  13853    941    701    538       S  
ATOM   2739  N   THR B 321     -11.400  -8.046 -19.185  1.00106.30           N  
ANISOU 2739  N   THR B 321    11928  14662  13798   1049    822    635       N  
ATOM   2740  CA  THR B 321     -11.445  -9.342 -18.605  1.00118.55           C  
ANISOU 2740  CA  THR B 321    13416  16249  15381   1076    878    676       C  
ATOM   2741  C   THR B 321     -12.801  -9.521 -17.998  1.00117.88           C  
ANISOU 2741  C   THR B 321    13294  16171  15325   1106    848    657       C  
ATOM   2742  O   THR B 321     -13.419 -10.565 -18.122  1.00112.54           O  
ANISOU 2742  O   THR B 321    12602  15476  14683   1124    872    671       O  
ATOM   2743  CB  THR B 321     -10.502  -9.335 -17.438  1.00106.55           C  
ANISOU 2743  CB  THR B 321    11822  14814  13846   1086    914    710       C  
ATOM   2744  OG1 THR B 321     -10.884  -8.243 -16.603  1.00109.90           O  
ANISOU 2744  OG1 THR B 321    12225  15278  14253   1094    863    679       O  
ATOM   2745  CG2 THR B 321      -9.100  -9.107 -17.920  1.00 93.24           C  
ANISOU 2745  CG2 THR B 321    10167  13130  12132   1057    944    730       C  
ATOM   2746  N   SER B 322     -13.311  -8.467 -17.413  1.00115.07           N  
ANISOU 2746  N   SER B 322    12931  15838  14955   1111    794    622       N  
ATOM   2747  CA  SER B 322     -14.557  -8.592 -16.718  1.00118.32           C  
ANISOU 2747  CA  SER B 322    13301  16264  15391   1141    766    605       C  
ATOM   2748  C   SER B 322     -15.746  -9.063 -17.524  1.00126.55           C  
ANISOU 2748  C   SER B 322    14383  17235  16466   1146    744    582       C  
ATOM   2749  O   SER B 322     -16.444  -9.972 -17.090  1.00135.73           O  
ANISOU 2749  O   SER B 322    15499  18409  17663   1173    764    597       O  
ATOM   2750  CB  SER B 322     -14.929  -7.226 -16.188  1.00116.50           C  
ANISOU 2750  CB  SER B 322    13073  16055  15137   1140    702    563       C  
ATOM   2751  OG  SER B 322     -15.485  -6.456 -17.231  1.00124.26           O  
ANISOU 2751  OG  SER B 322    14138  16965  16111   1118    645    517       O  
ATOM   2752  N   MET B 323     -15.983  -8.503 -18.697  1.00127.21           N  
ANISOU 2752  N   MET B 323    14550  17245  16539   1121    704    548       N  
ATOM   2753  CA  MET B 323     -17.147  -8.956 -19.444  1.00140.55           C  
ANISOU 2753  CA  MET B 323    16276  18867  18259   1127    681    525       C  
ATOM   2754  C   MET B 323     -16.946 -10.394 -19.841  1.00144.69           C  
ANISOU 2754  C   MET B 323    16789  19374  18814   1134    743    565       C  
ATOM   2755  O   MET B 323     -17.857 -11.219 -19.796  1.00145.91           O  
ANISOU 2755  O   MET B 323    16921  19511  19005   1156    749    568       O  
ATOM   2756  CB  MET B 323     -17.410  -8.104 -20.675  1.00146.01           C  
ANISOU 2756  CB  MET B 323    17062  19481  18933   1099    627    481       C  
ATOM   2757  CG  MET B 323     -18.808  -8.298 -21.241  1.00132.67           C  
ANISOU 2757  CG  MET B 323    15406  17730  17274   1109    587    447       C  
ATOM   2758  SD  MET B 323     -20.078  -7.779 -20.079  1.00143.36           S  
ANISOU 2758  SD  MET B 323    16704  19124  18642   1139    536    416       S  
ATOM   2759  CE  MET B 323     -21.528  -7.857 -21.116  1.00146.10           C  
ANISOU 2759  CE  MET B 323    17114  19379  19017   1140    485    371       C  
ATOM   2760  N   LEU B 324     -15.710 -10.671 -20.211  1.00136.06           N  
ANISOU 2760  N   LEU B 324    15709  18286  17703   1116    789    597       N  
ATOM   2761  CA  LEU B 324     -15.291 -12.001 -20.656  1.00132.74           C  
ANISOU 2761  CA  LEU B 324    15281  17849  17306   1118    853    639       C  
ATOM   2762  C   LEU B 324     -15.893 -13.109 -19.793  1.00152.42           C  
ANISOU 2762  C   LEU B 324    17696  20378  19838   1154    886    666       C  
ATOM   2763  O   LEU B 324     -16.712 -13.910 -20.263  1.00147.64           O  
ANISOU 2763  O   LEU B 324    17100  19727  19267   1165    889    664       O  
ATOM   2764  CB  LEU B 324     -13.758 -12.087 -20.642  1.00133.68           C  
ANISOU 2764  CB  LEU B 324    15394  18001  17398   1101    904    677       C  
ATOM   2765  CG  LEU B 324     -13.042 -13.427 -20.864  1.00131.11           C  
ANISOU 2765  CG  LEU B 324    15047  17678  17091   1104    978    727       C  
ATOM   2766  CD1 LEU B 324     -11.930 -13.245 -21.869  1.00128.90           C  
ANISOU 2766  CD1 LEU B 324    14829  17365  16784   1071    998    736       C  
ATOM   2767  CD2 LEU B 324     -12.483 -14.013 -19.557  1.00126.70           C  
ANISOU 2767  CD2 LEU B 324    14394  17206  16539   1127   1030    772       C  
ATOM   2768  N   LEU B 325     -15.453 -13.167 -18.537  1.00139.69           N  
ANISOU 2768  N   LEU B 325    16006  18847  18220   1171    913    693       N  
ATOM   2769  CA  LEU B 325     -15.990 -14.033 -17.498  1.00140.53           C  
ANISOU 2769  CA  LEU B 325    16031  19003  18360   1207    941    719       C  
ATOM   2770  C   LEU B 325     -17.469 -14.356 -17.687  1.00147.98           C  
ANISOU 2770  C   LEU B 325    16981  19904  19341   1225    908    692       C  
ATOM   2771  O   LEU B 325     -17.847 -15.526 -17.842  1.00142.17           O  
ANISOU 2771  O   LEU B 325    16226  19151  18643   1240    943    715       O  
ATOM   2772  CB  LEU B 325     -15.777 -13.340 -16.149  1.00142.96           C  
ANISOU 2772  CB  LEU B 325    16276  19394  18648   1221    931    720       C  
ATOM   2773  CG  LEU B 325     -15.950 -13.940 -14.749  1.00140.69           C  
ANISOU 2773  CG  LEU B 325    15893  19185  18380   1257    963    751       C  
ATOM   2774  CD1 LEU B 325     -15.696 -12.829 -13.742  1.00149.11           C  
ANISOU 2774  CD1 LEU B 325    16925  20315  19413   1261    933    737       C  
ATOM   2775  CD2 LEU B 325     -17.323 -14.558 -14.505  1.00139.60           C  
ANISOU 2775  CD2 LEU B 325    15727  19031  18284   1285    950    742       C  
ATOM   2776  N   MET B 326     -18.289 -13.300 -17.717  1.00146.99           N  
ANISOU 2776  N   MET B 326    16884  19759  19205   1222    840    643       N  
ATOM   2777  CA  MET B 326     -19.713 -13.405 -17.398  1.00156.21           C  
ANISOU 2777  CA  MET B 326    18032  20916  20405   1247    804    617       C  
ATOM   2778  C   MET B 326     -20.423 -14.421 -18.284  1.00149.04           C  
ANISOU 2778  C   MET B 326    17152  19939  19536   1251    816    619       C  
ATOM   2779  O   MET B 326     -20.954 -15.426 -17.792  1.00128.82           O  
ANISOU 2779  O   MET B 326    14537  17395  17013   1277    846    642       O  
ATOM   2780  CB  MET B 326     -20.378 -12.029 -17.523  1.00144.81           C  
ANISOU 2780  CB  MET B 326    16631  19451  18940   1237    726    561       C  
ATOM   2781  CG  MET B 326     -19.577 -10.881 -16.925  1.00143.94           C  
ANISOU 2781  CG  MET B 326    16513  19393  18786   1225    709    554       C  
ATOM   2782  SD  MET B 326     -18.611 -11.391 -15.480  1.00166.69           S  
ANISOU 2782  SD  MET B 326    19294  22379  21661   1246    772    608       S  
ATOM   2783  CE  MET B 326     -19.870 -11.619 -14.218  1.00135.69           C  
ANISOU 2783  CE  MET B 326    15290  18501  17766   1288    756    602       C  
ATOM   2784  N   GLY B 327     -20.440 -14.164 -19.592  1.00144.50           N  
ANISOU 2784  N   GLY B 327    16662  19289  18954   1225    792    594       N  
ATOM   2785  CA  GLY B 327     -21.224 -14.909 -20.564  1.00131.86           C  
ANISOU 2785  CA  GLY B 327    15101  17613  17387   1226    788    583       C  
ATOM   2786  C   GLY B 327     -21.733 -16.297 -20.217  1.00150.74           C  
ANISOU 2786  C   GLY B 327    17437  20012  19826   1254    832    615       C  
ATOM   2787  O   GLY B 327     -22.779 -16.442 -19.580  1.00154.18           O  
ANISOU 2787  O   GLY B 327    17831  20461  20290   1279    813    604       O  
TER    2788      GLY B 327                                                      
ATOM   2789  N   GLN A   1      -4.061  34.500 -66.884  1.00112.80           N  
ANISOU 2789  N   GLN A   1    16746  12766  13347   -233   -738   -351       N  
ATOM   2790  CA  GLN A   1      -2.665  34.705 -66.509  1.00117.05           C  
ANISOU 2790  CA  GLN A   1    17247  13348  13879   -256   -685   -309       C  
ATOM   2791  C   GLN A   1      -1.823  33.588 -67.140  1.00125.41           C  
ANISOU 2791  C   GLN A   1    18315  14403  14930   -257   -604   -264       C  
ATOM   2792  O   GLN A   1      -0.675  33.357 -66.752  1.00119.27           O  
ANISOU 2792  O   GLN A   1    17492  13670  14153   -270   -545   -223       O  
ATOM   2793  CB  GLN A   1      -2.513  34.727 -64.973  1.00131.46           C  
ANISOU 2793  CB  GLN A   1    18964  15255  15730   -248   -682   -306       C  
ATOM   2794  CG  GLN A   1      -1.345  35.587 -64.392  1.00149.36           C  
ANISOU 2794  CG  GLN A   1    21196  17564  17990   -276   -667   -284       C  
ATOM   2795  CD  GLN A   1      -1.767  36.962 -63.812  1.00145.53           C  
ANISOU 2795  CD  GLN A   1    20705  17085  17505   -286   -741   -321       C  
ATOM   2796  OE1 GLN A   1      -2.798  37.528 -64.187  1.00151.14           O  
ANISOU 2796  OE1 GLN A   1    21465  17750  18211   -280   -807   -363       O  
ATOM   2797  NE2 GLN A   1      -0.961  37.486 -62.883  1.00136.72           N  
ANISOU 2797  NE2 GLN A   1    19526  16025  16394   -299   -729   -306       N  
ATOM   2798  N   VAL A   2      -2.397  32.907 -68.132  1.00113.34           N  
ANISOU 2798  N   VAL A   2    16847  12820  13395   -244   -601   -271       N  
ATOM   2799  CA  VAL A   2      -1.812  31.692 -68.683  1.00 94.71           C  
ANISOU 2799  CA  VAL A   2    14494  10458  11034   -238   -528   -232       C  
ATOM   2800  C   VAL A   2      -1.841  31.754 -70.209  1.00 97.44           C  
ANISOU 2800  C   VAL A   2    14947  10725  11350   -248   -529   -234       C  
ATOM   2801  O   VAL A   2      -2.919  31.777 -70.819  1.00 96.61           O  
ANISOU 2801  O   VAL A   2    14897  10567  11242   -234   -577   -270       O  
ATOM   2802  CB  VAL A   2      -2.546  30.446 -68.178  1.00 88.83           C  
ANISOU 2802  CB  VAL A   2    13694   9738  10319   -204   -513   -236       C  
ATOM   2803  CG1 VAL A   2      -4.059  30.613 -68.336  1.00101.43           C  
ANISOU 2803  CG1 VAL A   2    15321  11293  11923   -183   -586   -287       C  
ATOM   2804  CG2 VAL A   2      -2.024  29.246 -68.899  1.00 92.49           C  
ANISOU 2804  CG2 VAL A   2    14176  10188  10778   -198   -443   -200       C  
ATOM   2805  N   GLN A   3      -0.666  31.774 -70.831  1.00 91.18           N  
ANISOU 2805  N   GLN A   3    14185   9923  10535   -271   -476   -196       N  
ATOM   2806  CA  GLN A   3      -0.593  31.859 -72.279  1.00102.87           C  
ANISOU 2806  CA  GLN A   3    15768  11331  11985   -281   -473   -195       C  
ATOM   2807  C   GLN A   3       0.235  30.704 -72.821  1.00104.64           C  
ANISOU 2807  C   GLN A   3    15996  11558  12205   -279   -391   -151       C  
ATOM   2808  O   GLN A   3       1.121  30.173 -72.140  1.00 99.28           O  
ANISOU 2808  O   GLN A   3    15247  10936  11538   -282   -333   -114       O  
ATOM   2809  CB  GLN A   3      -0.016  33.201 -72.760  1.00106.16           C  
ANISOU 2809  CB  GLN A   3    16241  11720  12374   -315   -497   -196       C  
ATOM   2810  CG  GLN A   3      -1.069  34.307 -72.889  1.00124.25           C  
ANISOU 2810  CG  GLN A   3    18578  13972  14659   -315   -586   -247       C  
ATOM   2811  CD  GLN A   3      -0.521  35.604 -73.498  1.00117.12           C  
ANISOU 2811  CD  GLN A   3    17740  13034  13727   -348   -609   -248       C  
ATOM   2812  OE1 GLN A   3       0.389  36.225 -72.946  1.00 97.89           O  
ANISOU 2812  OE1 GLN A   3    15267  10636  11290   -370   -593   -228       O  
ATOM   2813  NE2 GLN A   3      -1.102  36.027 -74.630  1.00113.91           N  
ANISOU 2813  NE2 GLN A   3    17429  12554  13297   -350   -649   -272       N  
ATOM   2814  N   LEU A   4      -0.089  30.312 -74.058  1.00 92.92           N  
ANISOU 2814  N   LEU A   4    14593  10009  10702   -274   -389   -155       N  
ATOM   2815  CA  LEU A   4       0.518  29.176 -74.738  1.00 86.33           C  
ANISOU 2815  CA  LEU A   4    13775   9165   9861   -269   -318   -119       C  
ATOM   2816  C   LEU A   4       0.699  29.564 -76.198  1.00 98.11           C  
ANISOU 2816  C   LEU A   4    15377  10585  11317   -284   -321   -119       C  
ATOM   2817  O   LEU A   4      -0.286  29.873 -76.872  1.00100.22           O  
ANISOU 2817  O   LEU A   4    15710  10795  11574   -275   -377   -156       O  
ATOM   2818  CB  LEU A   4      -0.380  27.945 -74.593  1.00 86.00           C  
ANISOU 2818  CB  LEU A   4    13706   9126   9844   -234   -313   -130       C  
ATOM   2819  CG  LEU A   4      -0.919  27.680 -73.172  1.00 92.53           C  
ANISOU 2819  CG  LEU A   4    14433  10015  10708   -214   -330   -143       C  
ATOM   2820  CD1 LEU A   4      -2.173  26.829 -73.146  1.00 85.92           C  
ANISOU 2820  CD1 LEU A   4    13589   9162   9893   -180   -355   -171       C  
ATOM   2821  CD2 LEU A   4       0.141  27.027 -72.307  1.00 85.77           C  
ANISOU 2821  CD2 LEU A   4    13490   9231   9868   -217   -259    -98       C  
ATOM   2822  N   VAL A   5       1.939  29.572 -76.695  1.00 95.86           N  
ANISOU 2822  N   VAL A   5    15112  10300  11011   -306   -263    -78       N  
ATOM   2823  CA  VAL A   5       2.233  30.079 -78.040  1.00 90.68           C  
ANISOU 2823  CA  VAL A   5    14559   9577  10317   -324   -265    -75       C  
ATOM   2824  C   VAL A   5       2.878  28.988 -78.897  1.00 87.86           C  
ANISOU 2824  C   VAL A   5    14231   9204   9949   -320   -193    -39       C  
ATOM   2825  O   VAL A   5       3.998  28.541 -78.620  1.00 84.46           O  
ANISOU 2825  O   VAL A   5    13756   8814   9520   -330   -125      4       O  
ATOM   2826  CB  VAL A   5       3.104  31.342 -78.001  1.00 92.94           C  
ANISOU 2826  CB  VAL A   5    14859   9869  10585   -359   -271    -63       C  
ATOM   2827  CG1 VAL A   5       4.410  31.093 -77.252  1.00 92.14           C  
ANISOU 2827  CG1 VAL A   5    14682   9833  10493   -374   -203    -17       C  
ATOM   2828  CG2 VAL A   5       3.388  31.796 -79.432  1.00102.68           C  
ANISOU 2828  CG2 VAL A   5    16201  11033  11780   -376   -270    -59       C  
ATOM   2829  N   GLU A   6       2.187  28.596 -79.970  1.00 90.61           N  
ANISOU 2829  N   GLU A   6    14656   9490  10283   -305   -209    -57       N  
ATOM   2830  CA  GLU A   6       2.607  27.490 -80.827  1.00 84.24           C  
ANISOU 2830  CA  GLU A   6    13881   8662   9466   -296   -148    -28       C  
ATOM   2831  C   GLU A   6       3.504  27.986 -81.956  1.00 82.33           C  
ANISOU 2831  C   GLU A   6    13720   8378   9184   -322   -120     -5       C  
ATOM   2832  O   GLU A   6       3.114  28.879 -82.713  1.00 84.09           O  
ANISOU 2832  O   GLU A   6    14021   8546   9383   -331   -169    -29       O  
ATOM   2833  CB  GLU A   6       1.382  26.784 -81.411  1.00 85.89           C  
ANISOU 2833  CB  GLU A   6    14131   8824   9680   -265   -179    -61       C  
ATOM   2834  CG  GLU A   6       0.321  26.361 -80.386  1.00 84.51           C  
ANISOU 2834  CG  GLU A   6    13886   8682   9543   -239   -216    -90       C  
ATOM   2835  CD  GLU A   6      -0.764  27.406 -80.169  1.00 85.65           C  
ANISOU 2835  CD  GLU A   6    14051   8803   9689   -237   -304   -140       C  
ATOM   2836  OE1 GLU A   6      -1.927  27.013 -79.924  1.00 86.28           O  
ANISOU 2836  OE1 GLU A   6    14117   8875   9790   -211   -345   -173       O  
ATOM   2837  OE2 GLU A   6      -0.455  28.616 -80.235  1.00 86.66           O  
ANISOU 2837  OE2 GLU A   6    14207   8922   9799   -262   -334   -146       O  
ATOM   2838  N   SER A   7       4.695  27.395 -82.081  1.00 83.27           N  
ANISOU 2838  N   SER A   7    13820   8522   9298   -332    -42     43       N  
ATOM   2839  CA  SER A   7       5.658  27.822 -83.096  1.00 86.03           C  
ANISOU 2839  CA  SER A   7    14238   8837   9611   -357     -9     70       C  
ATOM   2840  C   SER A   7       6.397  26.627 -83.685  1.00 83.94           C  
ANISOU 2840  C   SER A   7    13980   8573   9340   -350     70    109       C  
ATOM   2841  O   SER A   7       7.032  25.854 -82.961  1.00 80.67           O  
ANISOU 2841  O   SER A   7    13489   8215   8947   -346    126    140       O  
ATOM   2842  CB  SER A   7       6.677  28.805 -82.524  1.00 80.70           C  
ANISOU 2842  CB  SER A   7    13530   8199   8932   -389      3     92       C  
ATOM   2843  OG  SER A   7       7.878  28.123 -82.201  1.00 82.88           O  
ANISOU 2843  OG  SER A   7    13753   8524   9215   -397     83    140       O  
ATOM   2844  N   GLY A   8       6.372  26.514 -85.005  1.00 91.64           N  
ANISOU 2844  N   GLY A   8    15049   9486  10285   -349     77    110       N  
ATOM   2845  CA  GLY A   8       7.162  25.503 -85.675  1.00 96.33           C  
ANISOU 2845  CA  GLY A   8    15659  10076  10869   -346    152    148       C  
ATOM   2846  C   GLY A   8       6.536  24.980 -86.948  1.00 95.35           C  
ANISOU 2846  C   GLY A   8    15623   9883  10723   -328    143    133       C  
ATOM   2847  O   GLY A   8       7.223  24.417 -87.801  1.00 94.11           O  
ANISOU 2847  O   GLY A   8    15505   9705  10545   -330    199    162       O  
ATOM   2848  N   GLY A   9       5.233  25.181 -87.094  1.00 92.14           N  
ANISOU 2848  N   GLY A   9    15248   9439  10321   -310     73     86       N  
ATOM   2849  CA  GLY A   9       4.472  24.478 -88.101  1.00 92.74           C  
ANISOU 2849  CA  GLY A   9    15391   9459  10387   -285     63     67       C  
ATOM   2850  C   GLY A   9       4.202  25.261 -89.358  1.00101.73           C  
ANISOU 2850  C   GLY A   9    16642  10524  11486   -294     25     49       C  
ATOM   2851  O   GLY A   9       3.454  26.235 -89.342  1.00102.10           O  
ANISOU 2851  O   GLY A   9    16720  10546  11529   -298    -45     12       O  
ATOM   2852  N   GLY A  10       4.800  24.849 -90.454  1.00 93.46           N  
ANISOU 2852  N   GLY A  10    15659   9442  10411   -297     71     73       N  
ATOM   2853  CA  GLY A  10       4.444  25.371 -91.750  1.00100.21           C  
ANISOU 2853  CA  GLY A  10    16624  10222  11228   -299     39     55       C  
ATOM   2854  C   GLY A  10       4.091  24.216 -92.670  1.00106.97           C  
ANISOU 2854  C   GLY A  10    17526  11040  12077   -272     62     54       C  
ATOM   2855  O   GLY A  10       3.482  23.213 -92.248  1.00 98.49           O  
ANISOU 2855  O   GLY A  10    16406   9983  11032   -245     64     43       O  
ATOM   2856  N   SER A  11       4.525  24.344 -93.923  1.00101.83           N  
ANISOU 2856  N   SER A  11    16965  10339  11387   -280     82     67       N  
ATOM   2857  CA  SER A  11       4.297  23.337 -94.946  1.00 93.98           C  
ANISOU 2857  CA  SER A  11    16027   9303  10380   -256    106     67       C  
ATOM   2858  C   SER A  11       5.511  22.420 -95.087  1.00 95.94           C  
ANISOU 2858  C   SER A  11    16249   9581  10625   -260    198    119       C  
ATOM   2859  O   SER A  11       6.646  22.904 -95.199  1.00 89.11           O  
ANISOU 2859  O   SER A  11    15387   8729   9740   -287    240    154       O  
ATOM   2860  CB  SER A  11       3.971  24.018 -96.268  1.00 99.11           C  
ANISOU 2860  CB  SER A  11    16794   9877  10988   -260     69     48       C  
ATOM   2861  OG  SER A  11       3.688  23.054 -97.261  1.00103.52           O  
ANISOU 2861  OG  SER A  11    17408  10393  11534   -236     88     46       O  
ATOM   2862  N   VAL A  12       5.256  21.094 -95.067  1.00102.38           N  
ANISOU 2862  N   VAL A  12    17035  10404  11459   -233    229    123       N  
ATOM   2863  CA  VAL A  12       6.232  20.022 -95.302  1.00103.00           C  
ANISOU 2863  CA  VAL A  12    17094  10505  11536   -230    314    167       C  
ATOM   2864  C   VAL A  12       5.580  18.941 -96.161  1.00 96.12           C  
ANISOU 2864  C   VAL A  12    16269   9589  10661   -198    317    152       C  
ATOM   2865  O   VAL A  12       4.359  18.760 -96.138  1.00 95.09           O  
ANISOU 2865  O   VAL A  12    16148   9434  10546   -175    261    111       O  
ATOM   2866  CB  VAL A  12       6.765  19.359 -93.999  1.00102.50           C  
ANISOU 2866  CB  VAL A  12    16913  10521  11513   -229    360    193       C  
ATOM   2867  CG1 VAL A  12       8.064  18.590 -94.261  1.00104.89           C  
ANISOU 2867  CG1 VAL A  12    17201  10848  11806   -237    451    245       C  
ATOM   2868  CG2 VAL A  12       6.973  20.372 -92.895  1.00 97.64           C  
ANISOU 2868  CG2 VAL A  12    16237   9951  10911   -252    335    192       C  
ATOM   2869  N   GLN A  13       6.407  18.202 -96.904  1.00100.80           N  
ANISOU 2869  N   GLN A  13    16890  10174  11236   -196    384    187       N  
ATOM   2870  CA  GLN A  13       5.976  17.113 -97.779  1.00104.44           C  
ANISOU 2870  CA  GLN A  13    17395  10595  11691   -167    399    180       C  
ATOM   2871  C   GLN A  13       6.160  15.754 -97.110  1.00104.28           C  
ANISOU 2871  C   GLN A  13    17291  10622  11706   -148    451    200       C  
ATOM   2872  O   GLN A  13       6.986  15.587 -96.209  1.00105.36           O  
ANISOU 2872  O   GLN A  13    17348  10821  11863   -161    497    232       O  
ATOM   2873  CB  GLN A  13       6.738  17.134 -99.106  1.00109.07           C  
ANISOU 2873  CB  GLN A  13    18072  11139  12232   -176    439    204       C  
ATOM   2874  CG  GLN A  13       5.932  17.651-100.276  1.00125.44           C  
ANISOU 2874  CG  GLN A  13    20254  13134  14272   -167    383    168       C  
ATOM   2875  CD  GLN A  13       6.444  17.120-101.617  1.00111.04           C  
ANISOU 2875  CD  GLN A  13    18511  11266  12411   -161    428    188       C  
ATOM   2876  OE1 GLN A  13       6.229  15.944-101.967  1.00102.62           O  
ANISOU 2876  OE1 GLN A  13    17446  10190  11354   -134    454    189       O  
ATOM   2877  NE2 GLN A  13       7.109  17.992-102.386  1.00100.25           N  
ANISOU 2877  NE2 GLN A  13    17214   9872  11004   -184    437    203       N  
ATOM   2878  N   SER A  14       5.400  14.771 -97.609  1.00104.59           N  
ANISOU 2878  N   SER A  14    17355  10631  11754   -117    444    181       N  
ATOM   2879  CA  SER A  14       5.162  13.503 -96.918  1.00 99.23           C  
ANISOU 2879  CA  SER A  14    16597   9989  11116    -93    471    186       C  
ATOM   2880  C   SER A  14       6.461  12.836 -96.473  1.00 87.36           C  
ANISOU 2880  C   SER A  14    15030   8542   9621   -104    558    239       C  
ATOM   2881  O   SER A  14       7.499  12.932 -97.136  1.00 86.33           O  
ANISOU 2881  O   SER A  14    14938   8405   9460   -120    608    272       O  
ATOM   2882  CB  SER A  14       4.369  12.558 -97.827  1.00 97.33           C  
ANISOU 2882  CB  SER A  14    16411   9696  10873    -60    461    164       C  
ATOM   2883  OG  SER A  14       2.998  12.924 -97.900  1.00104.88           O  
ANISOU 2883  OG  SER A  14    17398  10615  11838    -45    380    112       O  
ATOM   2884  N   GLY A  15       6.394  12.149 -95.334  1.00 88.52           N  
ANISOU 2884  N   GLY A  15    15078   8746   9810    -94    575    246       N  
ATOM   2885  CA  GLY A  15       7.587  11.603 -94.718  1.00 92.11           C  
ANISOU 2885  CA  GLY A  15    15460   9261  10277   -105    652    294       C  
ATOM   2886  C   GLY A  15       8.499  12.615 -94.056  1.00100.36           C  
ANISOU 2886  C   GLY A  15    16468  10348  11315   -139    665    318       C  
ATOM   2887  O   GLY A  15       9.625  12.264 -93.694  1.00 94.51           O  
ANISOU 2887  O   GLY A  15    15678   9653  10578   -151    732    361       O  
ATOM   2888  N   GLY A  16       8.050  13.861 -93.878  1.00109.58           N  
ANISOU 2888  N   GLY A  16    17657  11503  12474   -154    603    291       N  
ATOM   2889  CA  GLY A  16       8.878  14.904 -93.309  1.00 96.43           C  
ANISOU 2889  CA  GLY A  16    15965   9874  10802   -187    609    311       C  
ATOM   2890  C   GLY A  16       8.974  14.821 -91.797  1.00 89.75           C  
ANISOU 2890  C   GLY A  16    15005   9100   9996   -189    614    318       C  
ATOM   2891  O   GLY A  16       8.325  14.002 -91.147  1.00 86.04           O  
ANISOU 2891  O   GLY A  16    14477   8654   9561   -166    608    306       O  
ATOM   2892  N   SER A  17       9.810  15.704 -91.236  1.00 95.35           N  
ANISOU 2892  N   SER A  17    15683   9846  10701   -219    626    339       N  
ATOM   2893  CA  SER A  17      10.111  15.757 -89.799  1.00 96.24           C  
ANISOU 2893  CA  SER A  17    15688  10032  10848   -226    636    351       C  
ATOM   2894  C   SER A  17       9.807  17.143 -89.228  1.00103.44           C  
ANISOU 2894  C   SER A  17    16594  10950  11759   -246    574    327       C  
ATOM   2895  O   SER A  17      10.683  18.014 -89.192  1.00105.89           O  
ANISOU 2895  O   SER A  17    16910  11273  12052   -275    588    348       O  
ATOM   2896  CB  SER A  17      11.578  15.387 -89.529  1.00108.17           C  
ANISOU 2896  CB  SER A  17    17152  11591  12358   -243    719    405       C  
ATOM   2897  OG  SER A  17      11.810  13.998 -89.643  1.00105.62           O  
ANISOU 2897  OG  SER A  17    16802  11280  12048   -223    777    427       O  
ATOM   2898  N   LEU A  18       8.592  17.344 -88.728  1.00101.94           N  
ANISOU 2898  N   LEU A  18    16389  10756  11590   -230    507    285       N  
ATOM   2899  CA  LEU A  18       8.235  18.604 -88.088  1.00 96.45           C  
ANISOU 2899  CA  LEU A  18    15679  10070  10897   -246    446    260       C  
ATOM   2900  C   LEU A  18       8.299  18.487 -86.575  1.00 91.96           C  
ANISOU 2900  C   LEU A  18    14998   9575  10366   -245    450    266       C  
ATOM   2901  O   LEU A  18       8.139  17.406 -86.005  1.00 89.81           O  
ANISOU 2901  O   LEU A  18    14662   9337  10124   -224    477    274       O  
ATOM   2902  CB  LEU A  18       6.835  19.070 -88.493  1.00 93.12           C  
ANISOU 2902  CB  LEU A  18    15316   9595  10472   -231    363    207       C  
ATOM   2903  CG  LEU A  18       6.815  20.356 -89.311  1.00 95.21           C  
ANISOU 2903  CG  LEU A  18    15670   9808  10700   -253    320    192       C  
ATOM   2904  CD1 LEU A  18       5.391  20.846 -89.534  1.00 94.47           C  
ANISOU 2904  CD1 LEU A  18    15620   9667  10606   -238    234    137       C  
ATOM   2905  CD2 LEU A  18       7.659  21.403 -88.612  1.00 91.19           C  
ANISOU 2905  CD2 LEU A  18    15122   9339  10188   -285    325    210       C  
ATOM   2906  N   THR A  19       8.525  19.625 -85.932  1.00 97.00           N  
ANISOU 2906  N   THR A  19    15612  10238  11005   -268    421    262       N  
ATOM   2907  CA  THR A  19       8.505  19.675 -84.483  1.00 95.20           C  
ANISOU 2907  CA  THR A  19    15282  10078  10812   -267    415    262       C  
ATOM   2908  C   THR A  19       7.919  21.023 -84.057  1.00 90.08           C  
ANISOU 2908  C   THR A  19    14640   9424  10161   -280    339    227       C  
ATOM   2909  O   THR A  19       8.279  22.073 -84.603  1.00 86.71           O  
ANISOU 2909  O   THR A  19    14272   8968   9707   -305    322    226       O  
ATOM   2910  CB  THR A  19       9.910  19.413 -83.914  1.00 95.97           C  
ANISOU 2910  CB  THR A  19    15314  10235  10914   -285    489    312       C  
ATOM   2911  OG1 THR A  19       9.808  19.087 -82.528  1.00 93.77           O  
ANISOU 2911  OG1 THR A  19    14931  10024  10674   -276    492    314       O  
ATOM   2912  CG2 THR A  19      10.833  20.623 -84.090  1.00 94.54           C  
ANISOU 2912  CG2 THR A  19    15160  10052  10707   -321    493    328       C  
ATOM   2913  N   LEU A  20       6.971  20.971 -83.113  1.00 86.80           N  
ANISOU 2913  N   LEU A  20    14168   9034   9777   -263    294    197       N  
ATOM   2914  CA  LEU A  20       6.103  22.103 -82.775  1.00 89.23           C  
ANISOU 2914  CA  LEU A  20    14488   9328  10086   -267    212    155       C  
ATOM   2915  C   LEU A  20       6.219  22.423 -81.292  1.00 90.99           C  
ANISOU 2915  C   LEU A  20    14612   9623  10339   -272    204    156       C  
ATOM   2916  O   LEU A  20       5.736  21.658 -80.455  1.00 89.70           O  
ANISOU 2916  O   LEU A  20    14378   9497  10209   -249    206    151       O  
ATOM   2917  CB  LEU A  20       4.640  21.803 -83.117  1.00 83.33           C  
ANISOU 2917  CB  LEU A  20    13778   8537   9348   -239    154    110       C  
ATOM   2918  CG  LEU A  20       4.071  21.928 -84.526  1.00 86.42           C  
ANISOU 2918  CG  LEU A  20    14280   8848   9709   -234    125     87       C  
ATOM   2919  CD1 LEU A  20       4.929  21.236 -85.549  1.00 91.94           C  
ANISOU 2919  CD1 LEU A  20    15026   9522  10384   -237    192    123       C  
ATOM   2920  CD2 LEU A  20       2.680  21.315 -84.519  1.00 90.35           C  
ANISOU 2920  CD2 LEU A  20    14780   9322  10228   -201     79     48       C  
ATOM   2921  N   SER A  21       6.815  23.568 -80.970  1.00 86.84           N  
ANISOU 2921  N   SER A  21    14080   9112   9802   -300    191    162       N  
ATOM   2922  CA  SER A  21       6.855  24.042 -79.594  1.00 80.19           C  
ANISOU 2922  CA  SER A  21    13150   8332   8985   -305    172    158       C  
ATOM   2923  C   SER A  21       5.530  24.663 -79.187  1.00 80.47           C  
ANISOU 2923  C   SER A  21    13187   8355   9034   -293     87    106       C  
ATOM   2924  O   SER A  21       4.814  25.248 -80.003  1.00 82.56           O  
ANISOU 2924  O   SER A  21    13532   8559   9279   -293     35     75       O  
ATOM   2925  CB  SER A  21       7.971  25.067 -79.394  1.00 78.53           C  
ANISOU 2925  CB  SER A  21    12934   8144   8760   -340    187    181       C  
ATOM   2926  OG  SER A  21       9.182  24.620 -79.962  1.00 85.86           O  
ANISOU 2926  OG  SER A  21    13877   9074   9672   -354    262    226       O  
ATOM   2927  N   CYS A  22       5.203  24.507 -77.901  1.00 86.31           N  
ANISOU 2927  N   CYS A  22    13836   9151   9806   -281     75     98       N  
ATOM   2928  CA  CYS A  22       4.114  25.226 -77.234  1.00 87.37           C  
ANISOU 2928  CA  CYS A  22    13952   9288   9955   -273     -3     53       C  
ATOM   2929  C   CYS A  22       4.759  25.904 -76.027  1.00 88.77           C  
ANISOU 2929  C   CYS A  22    14052   9531  10146   -290     -1     66       C  
ATOM   2930  O   CYS A  22       4.759  25.350 -74.926  1.00 84.92           O  
ANISOU 2930  O   CYS A  22    13474   9104   9688   -277     17     74       O  
ATOM   2931  CB  CYS A  22       2.957  24.287 -76.837  1.00 92.88           C  
ANISOU 2931  CB  CYS A  22    14616   9992  10683   -238    -23     29       C  
ATOM   2932  SG  CYS A  22       1.788  24.927 -75.589  1.00 92.20           S  
ANISOU 2932  SG  CYS A  22    14470   9938  10626   -224   -102    -17       S  
ATOM   2933  N   ALA A  23       5.355  27.075 -76.256  1.00 91.56           N  
ANISOU 2933  N   ALA A  23    14439   9873  10477   -320    -15     69       N  
ATOM   2934  CA  ALA A  23       5.954  27.835 -75.170  1.00 94.62           C  
ANISOU 2934  CA  ALA A  23    14758  10317  10874   -338    -18     77       C  
ATOM   2935  C   ALA A  23       4.850  28.348 -74.261  1.00 99.78           C  
ANISOU 2935  C   ALA A  23    15373  10988  11550   -324    -90     34       C  
ATOM   2936  O   ALA A  23       3.841  28.883 -74.729  1.00 86.31           O  
ANISOU 2936  O   ALA A  23    13725   9233   9836   -318   -155     -6       O  
ATOM   2937  CB  ALA A  23       6.795  28.988 -75.711  1.00 85.40           C  
ANISOU 2937  CB  ALA A  23    13643   9126   9677   -373    -20     89       C  
ATOM   2938  N   ALA A  24       5.018  28.149 -72.963  1.00 98.39           N  
ANISOU 2938  N   ALA A  24    15100  10882  11402   -318    -79     42       N  
ATOM   2939  CA  ALA A  24       3.932  28.366 -72.032  1.00 91.67           C  
ANISOU 2939  CA  ALA A  24    14202  10054  10575   -299   -138      4       C  
ATOM   2940  C   ALA A  24       4.358  29.364 -70.966  1.00100.76           C  
ANISOU 2940  C   ALA A  24    15296  11256  11734   -316   -159      2       C  
ATOM   2941  O   ALA A  24       5.546  29.504 -70.654  1.00103.78           O  
ANISOU 2941  O   ALA A  24    15643  11675  12113   -336   -112     38       O  
ATOM   2942  CB  ALA A  24       3.489  27.049 -71.403  1.00 90.18           C  
ANISOU 2942  CB  ALA A  24    13946   9902  10417   -267   -111      9       C  
ATOM   2943  N   SER A  25       3.369  30.067 -70.423  1.00103.02           N  
ANISOU 2943  N   SER A  25    15571  11542  12031   -308   -232    -40       N  
ATOM   2944  CA  SER A  25       3.591  31.138 -69.470  1.00103.35           C  
ANISOU 2944  CA  SER A  25    15567  11624  12079   -323   -265    -50       C  
ATOM   2945  C   SER A  25       2.505  31.083 -68.413  1.00 97.37           C  
ANISOU 2945  C   SER A  25    14748  10900  11350   -298   -314    -85       C  
ATOM   2946  O   SER A  25       1.343  30.788 -68.716  1.00 95.34           O  
ANISOU 2946  O   SER A  25    14520  10608  11098   -276   -353   -117       O  
ATOM   2947  CB  SER A  25       3.555  32.493 -70.150  1.00109.22           C  
ANISOU 2947  CB  SER A  25    16386  12316  12795   -348   -316    -72       C  
ATOM   2948  OG  SER A  25       2.536  32.482 -71.137  1.00110.50           O  
ANISOU 2948  OG  SER A  25    16630  12410  12945   -337   -358   -103       O  
ATOM   2949  N   GLY A  26       2.896  31.379 -67.169  1.00103.67           N  
ANISOU 2949  N   GLY A  26    15461  11765  12165   -301   -311    -78       N  
ATOM   2950  CA  GLY A  26       2.005  31.319 -66.024  1.00103.26           C  
ANISOU 2950  CA  GLY A  26    15339  11754  12140   -277   -351   -105       C  
ATOM   2951  C   GLY A  26       1.773  29.902 -65.543  1.00 97.97           C  
ANISOU 2951  C   GLY A  26    14609  11120  11496   -248   -307    -89       C  
ATOM   2952  O   GLY A  26       1.611  29.652 -64.345  1.00111.08           O  
ANISOU 2952  O   GLY A  26    16183  12841  13181   -233   -307    -90       O  
ATOM   2953  N   SER A  27       1.769  28.961 -66.480  1.00100.74           N  
ANISOU 2953  N   SER A  27    15004  11433  11840   -240   -269    -74       N  
ATOM   2954  CA  SER A  27       1.480  27.573 -66.160  1.00107.13           C  
ANISOU 2954  CA  SER A  27    15765  12268  12673   -212   -230    -61       C  
ATOM   2955  C   SER A  27       2.593  26.965 -65.308  1.00104.88           C  
ANISOU 2955  C   SER A  27    15394  12053  12401   -214   -160    -15       C  
ATOM   2956  O   SER A  27       3.743  27.417 -65.295  1.00108.89           O  
ANISOU 2956  O   SER A  27    15897  12580  12895   -239   -127     13       O  
ATOM   2957  CB  SER A  27       1.266  26.758 -67.447  1.00106.47           C  
ANISOU 2957  CB  SER A  27    15755  12123  12577   -204   -206    -55       C  
ATOM   2958  OG  SER A  27       2.472  26.215 -67.972  1.00 97.05           O  
ANISOU 2958  OG  SER A  27    14571  10932  11370   -218   -132     -8       O  
ATOM   2959  N   THR A  28       2.227  25.942 -64.565  1.00 97.41           N  
ANISOU 2959  N   THR A  28    14380  11149  11483   -187   -138     -9       N  
ATOM   2960  CA  THR A  28       3.189  25.194 -63.789  1.00103.44           C  
ANISOU 2960  CA  THR A  28    15063  11979  12261   -185    -69     33       C  
ATOM   2961  C   THR A  28       3.047  23.741 -64.183  1.00104.05           C  
ANISOU 2961  C   THR A  28    15137  12047  12350   -163    -20     53       C  
ATOM   2962  O   THR A  28       1.932  23.263 -64.404  1.00102.19           O  
ANISOU 2962  O   THR A  28    14919  11784  12126   -140    -49     26       O  
ATOM   2963  CB  THR A  28       2.946  25.342 -62.281  1.00119.02           C  
ANISOU 2963  CB  THR A  28    16939  14022  14260   -172    -88     25       C  
ATOM   2964  OG1 THR A  28       2.035  24.326 -61.844  1.00106.91           O  
ANISOU 2964  OG1 THR A  28    15364  12504  12753   -139    -89     15       O  
ATOM   2965  CG2 THR A  28       2.351  26.719 -61.945  1.00120.53           C  
ANISOU 2965  CG2 THR A  28    17144  14206  14446   -181   -167    -17       C  
ATOM   2966  N   TYR A  29       4.170  23.038 -64.284  1.00104.92           N  
ANISOU 2966  N   TYR A  29    15226  12182  12458   -171     55     99       N  
ATOM   2967  CA  TYR A  29       4.073  21.588 -64.340  1.00 98.99           C  
ANISOU 2967  CA  TYR A  29    14448  11440  11724   -147    106    120       C  
ATOM   2968  C   TYR A  29       3.308  21.065 -63.139  1.00 99.14           C  
ANISOU 2968  C   TYR A  29    14383  11510  11777   -118     91    108       C  
ATOM   2969  O   TYR A  29       2.428  20.209 -63.276  1.00102.59           O  
ANISOU 2969  O   TYR A  29    14820  11930  12230    -92     86     95       O  
ATOM   2970  CB  TYR A  29       5.458  20.966 -64.390  1.00106.25           C  
ANISOU 2970  CB  TYR A  29    15341  12389  12638   -159    189    173       C  
ATOM   2971  CG  TYR A  29       5.483  19.539 -63.921  1.00103.24           C  
ANISOU 2971  CG  TYR A  29    14897  12046  12283   -134    242    198       C  
ATOM   2972  CD1 TYR A  29       4.685  18.584 -64.530  1.00100.10           C  
ANISOU 2972  CD1 TYR A  29    14530  11611  11894   -111    245    188       C  
ATOM   2973  CD2 TYR A  29       6.313  19.137 -62.880  1.00107.93           C  
ANISOU 2973  CD2 TYR A  29    15403  12714  12894   -133    291    231       C  
ATOM   2974  CE1 TYR A  29       4.685  17.297 -64.108  1.00 94.79           C  
ANISOU 2974  CE1 TYR A  29    13799  10970  11245    -88    292    211       C  
ATOM   2975  CE2 TYR A  29       6.332  17.811 -62.463  1.00112.35           C  
ANISOU 2975  CE2 TYR A  29    15905  13307  13477   -110    341    255       C  
ATOM   2976  CZ  TYR A  29       5.508  16.894 -63.096  1.00100.58           C  
ANISOU 2976  CZ  TYR A  29    14446  11776  11995    -87    341    244       C  
ATOM   2977  OH  TYR A  29       5.482  15.567 -62.722  1.00 95.74           O  
ANISOU 2977  OH  TYR A  29    13779  11192  11406    -63    389    267       O  
ATOM   2978  N   SER A  30       3.626  21.587 -61.954  1.00103.50           N  
ANISOU 2978  N   SER A  30    14862  12124  12340   -122     83    110       N  
ATOM   2979  CA  SER A  30       3.000  21.122 -60.721  1.00101.05           C  
ANISOU 2979  CA  SER A  30    14465  11869  12061    -96     73    101       C  
ATOM   2980  C   SER A  30       1.479  21.164 -60.787  1.00101.38           C  
ANISOU 2980  C   SER A  30    14529  11877  12115    -73      8     55       C  
ATOM   2981  O   SER A  30       0.808  20.253 -60.293  1.00 99.33           O  
ANISOU 2981  O   SER A  30    14222  11637  11881    -45     14     52       O  
ATOM   2982  CB  SER A  30       3.476  21.964 -59.544  1.00107.80           C  
ANISOU 2982  CB  SER A  30    15254  12786  12921   -106     59    103       C  
ATOM   2983  OG  SER A  30       2.619  21.775 -58.430  1.00117.43           O  
ANISOU 2983  OG  SER A  30    16403  14047  14167    -81     29     82       O  
ATOM   2984  N   SER A  31       0.911  22.223 -61.358  1.00 97.96           N  
ANISOU 2984  N   SER A  31    14164  11394  11664    -85    -56     18       N  
ATOM   2985  CA  SER A  31      -0.532  22.406 -61.318  1.00102.09           C  
ANISOU 2985  CA  SER A  31    14703  11888  12198    -65   -124    -29       C  
ATOM   2986  C   SER A  31      -1.227  22.100 -62.631  1.00 98.15           C  
ANISOU 2986  C   SER A  31    14293  11310  11687    -60   -141    -48       C  
ATOM   2987  O   SER A  31      -2.457  21.970 -62.637  1.00 94.18           O  
ANISOU 2987  O   SER A  31    13801  10784  11199    -38   -189    -83       O  
ATOM   2988  CB  SER A  31      -0.889  23.845 -60.887  1.00109.71           C  
ANISOU 2988  CB  SER A  31    15675  12855  13155    -78   -195    -65       C  
ATOM   2989  OG  SER A  31      -0.880  24.758 -61.979  1.00 99.75           O  
ANISOU 2989  OG  SER A  31    14508  11529  11865   -100   -229    -82       O  
ATOM   2990  N   HIS A  32      -0.487  21.955 -63.732  1.00 98.66           N  
ANISOU 2990  N   HIS A  32    14423  11334  11729    -77   -104    -25       N  
ATOM   2991  CA  HIS A  32      -1.085  21.928 -65.059  1.00 98.56           C  
ANISOU 2991  CA  HIS A  32    14507  11242  11699    -76   -128    -45       C  
ATOM   2992  C   HIS A  32      -0.517  20.802 -65.910  1.00 96.00           C  
ANISOU 2992  C   HIS A  32    14209  10896  11369    -74    -61    -11       C  
ATOM   2993  O   HIS A  32       0.665  20.466 -65.813  1.00 98.47           O  
ANISOU 2993  O   HIS A  32    14496  11241  11676    -86      3     31       O  
ATOM   2994  CB  HIS A  32      -0.877  23.268 -65.781  1.00 93.38           C  
ANISOU 2994  CB  HIS A  32    13929  10542  11011   -105   -169    -63       C  
ATOM   2995  CG  HIS A  32      -1.778  24.357 -65.296  1.00 97.20           C  
ANISOU 2995  CG  HIS A  32    14413  11022  11498   -104   -250   -108       C  
ATOM   2996  ND1 HIS A  32      -3.152  24.295 -65.418  1.00 96.20           N  
ANISOU 2996  ND1 HIS A  32    14307  10862  11384    -82   -307   -150       N  
ATOM   2997  CD2 HIS A  32      -1.508  25.534 -64.688  1.00 99.62           C  
ANISOU 2997  CD2 HIS A  32    14700  11353  11798   -122   -283   -119       C  
ATOM   2998  CE1 HIS A  32      -3.686  25.388 -64.906  1.00 99.26           C  
ANISOU 2998  CE1 HIS A  32    14689  11254  11771    -87   -372   -185       C  
ATOM   2999  NE2 HIS A  32      -2.710  26.154 -64.451  1.00103.97           N  
ANISOU 2999  NE2 HIS A  32    15262  11887  12357   -111   -359   -166       N  
ATOM   3000  N   CYS A  33      -1.375  20.239 -66.761  1.00 93.67           N  
ANISOU 3000  N   CYS A  33    13970  10546  11076    -57    -77    -30       N  
ATOM   3001  CA  CYS A  33      -0.990  19.301 -67.812  1.00 94.76           C  
ANISOU 3001  CA  CYS A  33    14155  10646  11204    -54    -26     -6       C  
ATOM   3002  C   CYS A  33      -1.173  19.943 -69.189  1.00 91.96           C  
ANISOU 3002  C   CYS A  33    13912  10213  10816    -69    -58    -26       C  
ATOM   3003  O   CYS A  33      -1.838  20.966 -69.344  1.00 89.96           O  
ANISOU 3003  O   CYS A  33    13700   9929  10553    -75   -125    -63       O  
ATOM   3004  CB  CYS A  33      -1.811  18.008 -67.713  1.00104.96           C  
ANISOU 3004  CB  CYS A  33    15418  11936  12524    -21    -14    -10       C  
ATOM   3005  SG  CYS A  33      -2.074  17.374 -66.023  1.00113.63           S  
ANISOU 3005  SG  CYS A  33    16389  13121  13665      3     -1     -3       S  
ATOM   3006  N   MET A  34      -0.590  19.312 -70.208  1.00 84.54           N  
ANISOU 3006  N   MET A  34    13023   9239   9860    -74     -9      0       N  
ATOM   3007  CA  MET A  34      -0.455  19.912 -71.529  1.00 82.77           C  
ANISOU 3007  CA  MET A  34    12903   8946   9601    -92    -24     -8       C  
ATOM   3008  C   MET A  34      -0.779  18.870 -72.585  1.00 81.48           C  
ANISOU 3008  C   MET A  34    12793   8732   9434    -75     -1     -6       C  
ATOM   3009  O   MET A  34      -0.474  17.693 -72.402  1.00 82.93           O  
ANISOU 3009  O   MET A  34    12933   8941   9634    -60     55     22       O  
ATOM   3010  CB  MET A  34       0.967  20.415 -71.729  1.00 76.29           C  
ANISOU 3010  CB  MET A  34    12092   8141   8755   -123     21     29       C  
ATOM   3011  CG  MET A  34       1.397  21.375 -70.664  1.00 78.76           C  
ANISOU 3011  CG  MET A  34    12348   8507   9072   -140      4     30       C  
ATOM   3012  SD  MET A  34       0.959  23.006 -71.193  1.00 91.40           S  
ANISOU 3012  SD  MET A  34    14026  10056  10645   -161    -75    -10       S  
ATOM   3013  CE  MET A  34       2.238  23.277 -72.405  1.00 81.89           C  
ANISOU 3013  CE  MET A  34    12899   8815   9402   -192    -26     25       C  
ATOM   3014  N   GLY A  35      -1.395  19.300 -73.688  1.00 77.89           N  
ANISOU 3014  N   GLY A  35    12432   8206   8958    -76    -44    -35       N  
ATOM   3015  CA  GLY A  35      -1.803  18.386 -74.745  1.00 81.88           C  
ANISOU 3015  CA  GLY A  35    12994   8657   9459    -59    -30    -38       C  
ATOM   3016  C   GLY A  35      -1.910  19.128 -76.057  1.00 80.90           C  
ANISOU 3016  C   GLY A  35    12981   8460   9299    -74    -62    -56       C  
ATOM   3017  O   GLY A  35      -1.739  20.346 -76.097  1.00 83.47           O  
ANISOU 3017  O   GLY A  35    13335   8776   9604    -96    -98    -68       O  
ATOM   3018  N   TRP A  36      -2.200  18.383 -77.138  1.00 74.46           N  
ANISOU 3018  N   TRP A  36    12227   7590   8474    -61    -50    -58       N  
ATOM   3019  CA  TRP A  36      -2.235  18.931 -78.500  1.00 75.96           C  
ANISOU 3019  CA  TRP A  36    12527   7708   8628    -73    -71    -71       C  
ATOM   3020  C   TRP A  36      -3.511  18.527 -79.214  1.00 76.79           C  
ANISOU 3020  C   TRP A  36    12686   7753   8737    -47   -117   -109       C  
ATOM   3021  O   TRP A  36      -3.882  17.353 -79.182  1.00 81.03           O  
ANISOU 3021  O   TRP A  36    13198   8294   9298    -23    -93   -105       O  
ATOM   3022  CB  TRP A  36      -1.073  18.429 -79.348  1.00 78.30           C  
ANISOU 3022  CB  TRP A  36    12860   7992   8899    -85      0    -28       C  
ATOM   3023  CG  TRP A  36       0.221  19.077 -79.119  1.00 80.18           C  
ANISOU 3023  CG  TRP A  36    13082   8263   9119   -115     38      6       C  
ATOM   3024  CD1 TRP A  36       1.300  18.521 -78.508  1.00 80.28           C  
ANISOU 3024  CD1 TRP A  36    13027   8334   9141   -122    107     51       C  
ATOM   3025  CD2 TRP A  36       0.617  20.402 -79.512  1.00 88.46           C  
ANISOU 3025  CD2 TRP A  36    14185   9289  10136   -144      9      1       C  
ATOM   3026  NE1 TRP A  36       2.346  19.414 -78.487  1.00 85.38           N  
ANISOU 3026  NE1 TRP A  36    13680   8995   9765   -153    124     73       N  
ATOM   3027  CE2 TRP A  36       1.951  20.577 -79.096  1.00 89.03           C  
ANISOU 3027  CE2 TRP A  36    14216   9408  10202   -168     65     43       C  
ATOM   3028  CE3 TRP A  36      -0.028  21.461 -80.166  1.00 90.07           C  
ANISOU 3028  CE3 TRP A  36    14467   9438  10318   -153    -58    -36       C  
ATOM   3029  CZ2 TRP A  36       2.656  21.769 -79.316  1.00 89.06           C  
ANISOU 3029  CZ2 TRP A  36    14255   9405  10178   -199     56     50       C  
ATOM   3030  CZ3 TRP A  36       0.676  22.649 -80.384  1.00 84.50           C  
ANISOU 3030  CZ3 TRP A  36    13797   8726   9585   -184    -67    -29       C  
ATOM   3031  CH2 TRP A  36       2.001  22.788 -79.963  1.00 86.91           C  
ANISOU 3031  CH2 TRP A  36    14059   9078   9885   -207    -10     14       C  
ATOM   3032  N   PHE A  37      -4.149  19.465 -79.910  1.00 80.77           N  
ANISOU 3032  N   PHE A  37    13268   8200   9219    -54   -180   -146       N  
ATOM   3033  CA  PHE A  37      -5.317  19.085 -80.686  1.00 90.53           C  
ANISOU 3033  CA  PHE A  37    14563   9377  10459    -30   -222   -182       C  
ATOM   3034  C   PHE A  37      -4.972  19.350 -82.154  1.00 95.79           C  
ANISOU 3034  C   PHE A  37    15337   9976  11083    -42   -217   -179       C  
ATOM   3035  O   PHE A  37      -3.791  19.480 -82.503  1.00 92.21           O  
ANISOU 3035  O   PHE A  37    14899   9530  10605    -64   -166   -142       O  
ATOM   3036  CB  PHE A  37      -6.550  19.878 -80.256  1.00102.73           C  
ANISOU 3036  CB  PHE A  37    16107  10908  12015    -23   -307   -232       C  
ATOM   3037  CG  PHE A  37      -7.314  19.264 -79.108  1.00104.47           C  
ANISOU 3037  CG  PHE A  37    16239  11174  12281      2   -320   -245       C  
ATOM   3038  CD1 PHE A  37      -6.727  18.318 -78.284  1.00105.07           C  
ANISOU 3038  CD1 PHE A  37    16229  11312  12382      9   -258   -210       C  
ATOM   3039  CD2 PHE A  37      -8.643  19.600 -78.888  1.00104.86           C  
ANISOU 3039  CD2 PHE A  37    16293  11202  12346     18   -393   -294       C  
ATOM   3040  CE1 PHE A  37      -7.423  17.793 -77.211  1.00104.40           C  
ANISOU 3040  CE1 PHE A  37    16061  11269  12337     31   -269   -221       C  
ATOM   3041  CE2 PHE A  37      -9.356  19.055 -77.830  1.00103.13           C  
ANISOU 3041  CE2 PHE A  37    15992  11024  12168     40   -404   -305       C  
ATOM   3042  CZ  PHE A  37      -8.742  18.149 -76.994  1.00 97.92           C  
ANISOU 3042  CZ  PHE A  37    15246  10427  11532     47   -342   -269       C  
ATOM   3043  N   ARG A  38      -5.998  19.472 -83.002  1.00 94.70           N  
ANISOU 3043  N   ARG A  38    15273   9773  10937    -29   -271   -218       N  
ATOM   3044  CA  ARG A  38      -5.844  19.978 -84.369  1.00 97.11           C  
ANISOU 3044  CA  ARG A  38    15687  10010  11200    -41   -283   -224       C  
ATOM   3045  C   ARG A  38      -7.225  20.081 -85.007  1.00107.85           C  
ANISOU 3045  C   ARG A  38    17110  11307  12561    -20   -353   -274       C  
ATOM   3046  O   ARG A  38      -8.197  19.526 -84.489  1.00 96.37           O  
ANISOU 3046  O   ARG A  38    15615   9861  11141      5   -380   -299       O  
ATOM   3047  CB  ARG A  38      -4.909  19.101 -85.225  1.00 91.87           C  
ANISOU 3047  CB  ARG A  38    15056   9333  10519    -42   -209   -184       C  
ATOM   3048  CG  ARG A  38      -5.347  17.658 -85.396  1.00 93.26           C  
ANISOU 3048  CG  ARG A  38    15213   9502  10717    -11   -180   -181       C  
ATOM   3049  CD  ARG A  38      -4.311  16.849 -86.187  1.00102.19           C  
ANISOU 3049  CD  ARG A  38    16373  10626  11830    -15   -104   -139       C  
ATOM   3050  NE  ARG A  38      -4.747  15.474 -86.438  1.00 94.39           N  
ANISOU 3050  NE  ARG A  38    15374   9627  10863     15    -79   -138       N  
ATOM   3051  CZ  ARG A  38      -3.978  14.530 -86.972  1.00 86.95           C  
ANISOU 3051  CZ  ARG A  38    14441   8684   9914     18    -11   -103       C  
ATOM   3052  NH1 ARG A  38      -2.731  14.809 -87.315  1.00 92.36           N  
ANISOU 3052  NH1 ARG A  38    15144   9378  10569     -6     40    -65       N  
ATOM   3053  NH2 ARG A  38      -4.455  13.306 -87.168  1.00 89.13           N  
ANISOU 3053  NH2 ARG A  38    14706   8949  10211     46      7   -105       N  
ATOM   3054  N   GLN A  39      -7.306  20.827 -86.120  1.00109.51           N  
ANISOU 3054  N   GLN A  39    17420  11455  12735    -31   -385   -290       N  
ATOM   3055  CA  GLN A  39      -8.507  20.885 -86.952  1.00106.51           C  
ANISOU 3055  CA  GLN A  39    17114  11007  12350    -13   -446   -335       C  
ATOM   3056  C   GLN A  39      -8.133  20.989 -88.437  1.00111.60           C  
ANISOU 3056  C   GLN A  39    17865  11586  12950    -20   -434   -328       C  
ATOM   3057  O   GLN A  39      -7.216  21.731 -88.808  1.00 98.46           O  
ANISOU 3057  O   GLN A  39    16237   9919  11255    -47   -415   -306       O  
ATOM   3058  CB  GLN A  39      -9.427  22.048 -86.551  1.00 94.89           C  
ANISOU 3058  CB  GLN A  39    15648   9523  10881    -17   -531   -380       C  
ATOM   3059  CG  GLN A  39     -10.876  21.802 -86.965  1.00107.90           C  
ANISOU 3059  CG  GLN A  39    17335  11120  12542     11   -593   -429       C  
ATOM   3060  CD  GLN A  39     -11.811  22.941 -86.628  1.00111.50           C  
ANISOU 3060  CD  GLN A  39    17803  11562  13002      8   -677   -474       C  
ATOM   3061  OE1 GLN A  39     -11.411  23.933 -86.011  1.00119.83           O  
ANISOU 3061  OE1 GLN A  39    18832  12647  14050    -14   -691   -471       O  
ATOM   3062  NE2 GLN A  39     -13.066  22.819 -87.065  1.00111.71           N  
ANISOU 3062  NE2 GLN A  39    17869  11539  13037     31   -735   -518       N  
ATOM   3063  N   ALA A  40      -8.851  20.220 -89.250  1.00113.71           N  
ANISOU 3063  N   ALA A  40    18181  11805  13220      5   -445   -347       N  
ATOM   3064  CA  ALA A  40      -8.572  19.964 -90.671  1.00112.56           C  
ANISOU 3064  CA  ALA A  40    18130  11599  13039      6   -425   -340       C  
ATOM   3065  C   ALA A  40      -8.490  21.031 -91.764  1.00125.71           C  
ANISOU 3065  C   ALA A  40    19901  13205  14658    -11   -459   -353       C  
ATOM   3066  O   ALA A  40      -7.664  20.913 -92.659  1.00113.07           O  
ANISOU 3066  O   ALA A  40    18355  11581  13025    -21   -415   -325       O  
ATOM   3067  CB  ALA A  40      -9.511  18.871 -91.147  1.00119.28           C  
ANISOU 3067  CB  ALA A  40    18999  12415  13908     40   -435   -362       C  
ATOM   3068  N   PRO A  41      -9.382  22.016 -91.769  1.00136.75           N  
ANISOU 3068  N   PRO A  41    21333  14574  16053    -13   -537   -395       N  
ATOM   3069  CA  PRO A  41     -10.735  22.038 -91.235  1.00128.17           C  
ANISOU 3069  CA  PRO A  41    20220  13482  14998      8   -603   -442       C  
ATOM   3070  C   PRO A  41     -11.724  21.377 -92.158  1.00125.54           C  
ANISOU 3070  C   PRO A  41    19948  13086  14666     37   -632   -473       C  
ATOM   3071  O   PRO A  41     -11.391  20.654 -93.078  1.00112.99           O  
ANISOU 3071  O   PRO A  41    18406  11466  13059     45   -594   -457       O  
ATOM   3072  CB  PRO A  41     -11.045  23.520 -91.089  1.00125.84           C  
ANISOU 3072  CB  PRO A  41    19953  13173  14688    -11   -669   -469       C  
ATOM   3073  CG  PRO A  41     -10.108  24.202 -92.003  1.00124.92           C  
ANISOU 3073  CG  PRO A  41    19911  13028  14525    -36   -648   -446       C  
ATOM   3074  CD  PRO A  41      -8.875  23.370 -92.028  1.00140.85           C  
ANISOU 3074  CD  PRO A  41    21899  15080  16538    -43   -558   -393       C  
ATOM   3075  N   GLY A  42     -12.986  21.592 -91.833  1.00125.31           N  
ANISOU 3075  N   GLY A  42    19912  13041  14660     54   -702   -519       N  
ATOM   3076  CA  GLY A  42     -14.104  20.942 -92.500  1.00119.96           C  
ANISOU 3076  CA  GLY A  42    19277  12310  13991     84   -737   -554       C  
ATOM   3077  C   GLY A  42     -14.576  19.730 -91.700  1.00126.81           C  
ANISOU 3077  C   GLY A  42    20059  13215  14907    110   -717   -554       C  
ATOM   3078  O   GLY A  42     -15.617  19.151 -91.969  1.00131.55           O  
ANISOU 3078  O   GLY A  42    20674  13782  15527    137   -750   -586       O  
ATOM   3079  N   LYS A  43     -13.794  19.399 -90.681  1.00125.31           N  
ANISOU 3079  N   LYS A  43    19779  13096  14737    101   -664   -518       N  
ATOM   3080  CA  LYS A  43     -13.985  18.347 -89.735  1.00126.59           C  
ANISOU 3080  CA  LYS A  43    19847  13307  14943    119   -634   -507       C  
ATOM   3081  C   LYS A  43     -14.139  18.999 -88.381  1.00122.96           C  
ANISOU 3081  C   LYS A  43    19306  12906  14509    110   -659   -514       C  
ATOM   3082  O   LYS A  43     -14.407  20.183 -88.252  1.00122.73           O  
ANISOU 3082  O   LYS A  43    19299  12867  14467     95   -713   -538       O  
ATOM   3083  CB  LYS A  43     -12.758  17.441 -89.694  1.00117.84           C  
ANISOU 3083  CB  LYS A  43    18703  12237  13833    114   -543   -453       C  
ATOM   3084  CG  LYS A  43     -12.858  16.221 -90.591  1.00124.19           C  
ANISOU 3084  CG  LYS A  43    19543  13004  14638    137   -510   -447       C  
ATOM   3085  CD  LYS A  43     -12.152  15.021 -89.982  1.00124.14           C  
ANISOU 3085  CD  LYS A  43    19458  13054  14658    144   -433   -405       C  
ATOM   3086  CE  LYS A  43     -12.464  13.735 -90.733  1.00134.78           C  
ANISOU 3086  CE  LYS A  43    20830  14366  16014    171   -408   -405       C  
ATOM   3087  NZ  LYS A  43     -13.837  13.226 -90.485  1.00140.66           N  
ANISOU 3087  NZ  LYS A  43    21555  15092  16796    200   -458   -446       N  
ATOM   3088  N   GLU A  44     -13.975  18.187 -87.363  1.00124.13           N  
ANISOU 3088  N   GLU A  44    19358  13114  14693    119   -620   -493       N  
ATOM   3089  CA  GLU A  44     -14.103  18.624 -85.982  1.00120.61           C  
ANISOU 3089  CA  GLU A  44    18823  12729  14275    114   -637   -497       C  
ATOM   3090  C   GLU A  44     -12.721  18.785 -85.344  1.00119.64           C  
ANISOU 3090  C   GLU A  44    18647  12669  14144     89   -574   -448       C  
ATOM   3091  O   GLU A  44     -11.688  18.615 -85.997  1.00116.30           O  
ANISOU 3091  O   GLU A  44    18257  12238  13692     75   -520   -413       O  
ATOM   3092  CB  GLU A  44     -14.949  17.618 -85.208  1.00130.99           C  
ANISOU 3092  CB  GLU A  44    20063  14069  15637    143   -640   -509       C  
ATOM   3093  CG  GLU A  44     -16.252  17.269 -85.900  1.00127.95           C  
ANISOU 3093  CG  GLU A  44    19731  13622  15264    170   -693   -553       C  
ATOM   3094  CD  GLU A  44     -17.404  18.101 -85.387  1.00132.81           C  
ANISOU 3094  CD  GLU A  44    20338  14229  15894    175   -775   -602       C  
ATOM   3095  OE1 GLU A  44     -17.604  18.135 -84.149  1.00130.25           O  
ANISOU 3095  OE1 GLU A  44    19926  13962  15602    178   -780   -602       O  
ATOM   3096  OE2 GLU A  44     -18.091  18.738 -86.216  1.00137.30           O  
ANISOU 3096  OE2 GLU A  44    20988  14736  16443    177   -834   -638       O  
ATOM   3097  N   ARG A  45     -12.694  19.122 -84.047  1.00115.12           N  
ANISOU 3097  N   ARG A  45    17988  12158  13595     84   -580   -446       N  
ATOM   3098  CA  ARG A  45     -11.446  19.090 -83.293  1.00110.72           C  
ANISOU 3098  CA  ARG A  45    17364  11667  13037     65   -517   -399       C  
ATOM   3099  C   ARG A  45     -11.176  17.676 -82.800  1.00112.34           C  
ANISOU 3099  C   ARG A  45    17498  11914  13274     83   -454   -369       C  
ATOM   3100  O   ARG A  45     -12.102  16.907 -82.522  1.00111.71           O  
ANISOU 3100  O   ARG A  45    17386  11831  13226    110   -470   -389       O  
ATOM   3101  CB  ARG A  45     -11.479  20.061 -82.111  1.00124.59           C  
ANISOU 3101  CB  ARG A  45    19059  13473  14805     51   -550   -408       C  
ATOM   3102  CG  ARG A  45     -10.772  21.404 -82.371  1.00131.45           C  
ANISOU 3102  CG  ARG A  45    19973  14334  15637     18   -564   -403       C  
ATOM   3103  CD  ARG A  45     -11.100  22.483 -81.318  1.00113.59           C  
ANISOU 3103  CD  ARG A  45    17664  12108  13386      8   -616   -425       C  
ATOM   3104  NE  ARG A  45     -11.171  21.939 -79.966  1.00104.68           N  
ANISOU 3104  NE  ARG A  45    16426  11050  12298     20   -597   -415       N  
ATOM   3105  CZ  ARG A  45     -11.553  22.636 -78.897  1.00114.07           C  
ANISOU 3105  CZ  ARG A  45    17559  12278  13504     17   -637   -434       C  
ATOM   3106  NH1 ARG A  45     -11.891  23.923 -79.021  1.00128.85           N  
ANISOU 3106  NH1 ARG A  45    19474  14126  15358      3   -699   -464       N  
ATOM   3107  NH2 ARG A  45     -11.582  22.055 -77.691  1.00107.73           N  
ANISOU 3107  NH2 ARG A  45    16657  11541  12737     30   -615   -422       N  
ATOM   3108  N   GLU A  46      -9.893  17.323 -82.710  1.00112.27           N  
ANISOU 3108  N   GLU A  46    17462  11941  13254     68   -380   -320       N  
ATOM   3109  CA  GLU A  46      -9.514  15.958 -82.362  1.00105.22           C  
ANISOU 3109  CA  GLU A  46    16508  11085  12387     84   -314   -288       C  
ATOM   3110  C   GLU A  46      -8.250  15.950 -81.517  1.00 99.82           C  
ANISOU 3110  C   GLU A  46    15752  10471  11704     65   -252   -241       C  
ATOM   3111  O   GLU A  46      -7.262  16.609 -81.849  1.00 98.79           O  
ANISOU 3111  O   GLU A  46    15652  10342  11542     39   -229   -218       O  
ATOM   3112  CB  GLU A  46      -9.307  15.090 -83.618  1.00100.85           C  
ANISOU 3112  CB  GLU A  46    16022  10481  11817     94   -278   -275       C  
ATOM   3113  CG  GLU A  46      -8.098  15.442 -84.500  1.00102.62           C  
ANISOU 3113  CG  GLU A  46    16307  10686  11997     69   -235   -243       C  
ATOM   3114  CD  GLU A  46      -7.782  14.362 -85.550  1.00104.39           C  
ANISOU 3114  CD  GLU A  46    16579  10875  12211     81   -185   -224       C  
ATOM   3115  OE1 GLU A  46      -7.912  13.149 -85.242  1.00123.58           O  
ANISOU 3115  OE1 GLU A  46    18958  13326  14671    103   -150   -211       O  
ATOM   3116  OE2 GLU A  46      -7.396  14.735 -86.685  1.00 98.24           O  
ANISOU 3116  OE2 GLU A  46    15887  10047  11392     69   -182   -220       O  
ATOM   3117  N   GLY A  47      -8.290  15.201 -80.421  1.00 94.35           N  
ANISOU 3117  N   GLY A  47    14963   9838  11050     79   -225   -227       N  
ATOM   3118  CA  GLY A  47      -7.087  15.036 -79.627  1.00 88.02           C  
ANISOU 3118  CA  GLY A  47    14090   9103  10251     64   -162   -181       C  
ATOM   3119  C   GLY A  47      -5.991  14.365 -80.432  1.00 88.46           C  
ANISOU 3119  C   GLY A  47    14177   9149  10286     56    -89   -139       C  
ATOM   3120  O   GLY A  47      -6.246  13.486 -81.263  1.00 90.31           O  
ANISOU 3120  O   GLY A  47    14451   9343  10519     73    -72   -140       O  
ATOM   3121  N   VAL A  48      -4.750  14.776 -80.174  1.00 89.32           N  
ANISOU 3121  N   VAL A  48    14265   9295  10376     30    -45   -103       N  
ATOM   3122  CA  VAL A  48      -3.591  14.216 -80.856  1.00 87.37           C  
ANISOU 3122  CA  VAL A  48    14043   9045  10109     20     28    -60       C  
ATOM   3123  C   VAL A  48      -2.682  13.504 -79.856  1.00 85.11           C  
ANISOU 3123  C   VAL A  48    13660   8834   9845     19     96    -16       C  
ATOM   3124  O   VAL A  48      -2.660  12.268 -79.789  1.00 83.30           O  
ANISOU 3124  O   VAL A  48    13396   8618   9637     39    140      2       O  
ATOM   3125  CB  VAL A  48      -2.836  15.316 -81.616  1.00 79.62           C  
ANISOU 3125  CB  VAL A  48    13134   8035   9084    -10     24    -53       C  
ATOM   3126  CG1 VAL A  48      -1.560  14.775 -82.241  1.00 79.37           C  
ANISOU 3126  CG1 VAL A  48    13121   8006   9031    -23    102     -6       C  
ATOM   3127  CG2 VAL A  48      -3.738  15.893 -82.666  1.00 82.85           C  
ANISOU 3127  CG2 VAL A  48    13640   8367   9470     -7    -39    -94       C  
ATOM   3128  N   ALA A  49      -1.922  14.266 -79.075  1.00 85.57           N  
ANISOU 3128  N   ALA A  49    13672   8941   9898     -4    106      2       N  
ATOM   3129  CA  ALA A  49      -0.992  13.686 -78.111  1.00 83.70           C  
ANISOU 3129  CA  ALA A  49    13344   8777   9680     -7    170     44       C  
ATOM   3130  C   ALA A  49      -1.089  14.496 -76.825  1.00 82.70           C  
ANISOU 3130  C   ALA A  49    13147   8706   9570    -15    139     34       C  
ATOM   3131  O   ALA A  49      -0.672  15.658 -76.785  1.00 83.17           O  
ANISOU 3131  O   ALA A  49    13227   8767   9608    -40    117     31       O  
ATOM   3132  CB  ALA A  49       0.439  13.668 -78.652  1.00 75.18           C  
ANISOU 3132  CB  ALA A  49    12288   7703   8573    -30    236     88       C  
ATOM   3133  N   LEU A  50      -1.652  13.899 -75.786  1.00 84.70           N  
ANISOU 3133  N   LEU A  50    13319   9003   9862      6    135     29       N  
ATOM   3134  CA  LEU A  50      -1.773  14.563 -74.499  1.00 82.57           C  
ANISOU 3134  CA  LEU A  50    12975   8788   9608      2    107     20       C  
ATOM   3135  C   LEU A  50      -0.714  14.055 -73.538  1.00 82.65           C  
ANISOU 3135  C   LEU A  50    12895   8873   9633     -3    174     65       C  
ATOM   3136  O   LEU A  50       0.035  13.118 -73.824  1.00 82.92           O  
ANISOU 3136  O   LEU A  50    12921   8917   9668     -1    240    102       O  
ATOM   3137  CB  LEU A  50      -3.155  14.356 -73.879  1.00 74.68           C  
ANISOU 3137  CB  LEU A  50    11941   7791   8642     28     53    -18       C  
ATOM   3138  CG  LEU A  50      -4.377  14.333 -74.772  1.00 73.67           C  
ANISOU 3138  CG  LEU A  50    11887   7592   8512     45     -3    -61       C  
ATOM   3139  CD1 LEU A  50      -5.601  14.198 -73.906  1.00 73.40           C  
ANISOU 3139  CD1 LEU A  50    11801   7576   8513     69    -52    -95       C  
ATOM   3140  CD2 LEU A  50      -4.434  15.577 -75.647  1.00 75.06           C  
ANISOU 3140  CD2 LEU A  50    12155   7714   8651     23    -51    -85       C  
ATOM   3141  N   MET A  51      -0.664  14.694 -72.376  1.00 74.48           N  
ANISOU 3141  N   MET A  51    11794   7892   8611    -10    154     62       N  
ATOM   3142  CA  MET A  51       0.191  14.259 -71.289  1.00 73.40           C  
ANISOU 3142  CA  MET A  51    11563   7832   8493    -12    208     99       C  
ATOM   3143  C   MET A  51      -0.774  13.881 -70.167  1.00 90.26           C  
ANISOU 3143  C   MET A  51    13622  10006  10667     14    180     79       C  
ATOM   3144  O   MET A  51      -1.469  14.738 -69.607  1.00101.89           O  
ANISOU 3144  O   MET A  51    15082  11485  12145     14    119     46       O  
ATOM   3145  CB  MET A  51       1.178  15.339 -70.889  1.00 71.51           C  
ANISOU 3145  CB  MET A  51    11311   7625   8234    -42    214    115       C  
ATOM   3146  CG  MET A  51       2.330  15.537 -71.863  1.00 74.01           C  
ANISOU 3146  CG  MET A  51    11687   7915   8517    -67    258    145       C  
ATOM   3147  SD  MET A  51       3.744  14.403 -71.750  1.00 74.83           S  
ANISOU 3147  SD  MET A  51    11742   8064   8625    -71    361    207       S  
ATOM   3148  CE  MET A  51       3.588  13.751 -70.084  1.00100.76           C  
ANISOU 3148  CE  MET A  51    14897  11433  11952    -50    377    217       C  
ATOM   3149  N   THR A  52      -0.846  12.583 -69.883  1.00 99.96           N  
ANISOU 3149  N   THR A  52    14802  11257  11922     37    224     98       N  
ATOM   3150  CA  THR A  52      -1.805  12.042 -68.937  1.00 99.22           C  
ANISOU 3150  CA  THR A  52    14639  11194  11866     65    202     81       C  
ATOM   3151  C   THR A  52      -1.170  11.798 -67.570  1.00 97.59           C  
ANISOU 3151  C   THR A  52    14327  11072  11681     66    240    111       C  
ATOM   3152  O   THR A  52       0.047  11.872 -67.381  1.00 93.10           O  
ANISOU 3152  O   THR A  52    13735  10539  11101     47    291    148       O  
ATOM   3153  CB  THR A  52      -2.425  10.733 -69.464  1.00100.20           C  
ANISOU 3153  CB  THR A  52    14774  11287  12009     92    221     80       C  
ATOM   3154  OG1 THR A  52      -1.454   9.941 -70.172  1.00106.95           O  
ANISOU 3154  OG1 THR A  52    15651  12133  12852     86    291    119       O  
ATOM   3155  CG2 THR A  52      -3.660  10.997 -70.344  1.00 96.43           C  
ANISOU 3155  CG2 THR A  52    14376  10737  11527    103    156     33       C  
ATOM   3156  N   ARG A  53      -2.049  11.523 -66.608  1.00101.81           N  
ANISOU 3156  N   ARG A  53    14797  11638  12248     89    214     93       N  
ATOM   3157  CA  ARG A  53      -1.684  11.127 -65.255  1.00102.95           C  
ANISOU 3157  CA  ARG A  53    14836  11862  12418     97    246    117       C  
ATOM   3158  C   ARG A  53      -1.236   9.669 -65.215  1.00108.19           C  
ANISOU 3158  C   ARG A  53    15459  12547  13100    113    318    155       C  
ATOM   3159  O   ARG A  53      -0.220   9.333 -64.592  1.00110.31           O  
ANISOU 3159  O   ARG A  53    15668  12871  13373    106    374    194       O  
ATOM   3160  CB  ARG A  53      -2.902  11.351 -64.339  1.00106.46           C  
ANISOU 3160  CB  ARG A  53    15234  12325  12889    117    187     80       C  
ATOM   3161  CG  ARG A  53      -3.784  10.075 -64.168  1.00112.97           C  
ANISOU 3161  CG  ARG A  53    16025  13148  13749    151    196     76       C  
ATOM   3162  CD  ARG A  53      -5.317  10.276 -64.224  1.00121.38           C  
ANISOU 3162  CD  ARG A  53    17112  14176  14831    171    124     26       C  
ATOM   3163  NE  ARG A  53      -6.062   9.184 -63.588  1.00140.05           N  
ANISOU 3163  NE  ARG A  53    19413  16564  17234    202    134     26       N  
ATOM   3164  CZ  ARG A  53      -6.365   7.985 -64.088  1.00140.37           C  
ANISOU 3164  CZ  ARG A  53    19462  16579  17292    221    163     34       C  
ATOM   3165  NH1 ARG A  53      -7.023   7.113 -63.308  1.00124.48           N  
ANISOU 3165  NH1 ARG A  53    17381  14598  15319    249    169     35       N  
ATOM   3166  NH2 ARG A  53      -6.089   7.679 -65.358  1.00137.20           N  
ANISOU 3166  NH2 ARG A  53    19138  16121  16871    214    182     40       N  
ATOM   3167  N   SER A  54      -1.970   8.794 -65.902  1.00103.22           N  
ANISOU 3167  N   SER A  54    14862  11872  12483    133    317    144       N  
ATOM   3168  CA  SER A  54      -1.850   7.355 -65.687  1.00106.10           C  
ANISOU 3168  CA  SER A  54    15179  12261  12875    155    374    173       C  
ATOM   3169  C   SER A  54      -0.853   6.786 -66.698  1.00111.89           C  
ANISOU 3169  C   SER A  54    15958  12967  13587    143    435    206       C  
ATOM   3170  O   SER A  54       0.250   6.408 -66.319  1.00109.03           O  
ANISOU 3170  O   SER A  54    15552  12651  13225    135    497    248       O  
ATOM   3171  CB  SER A  54      -3.225   6.692 -65.744  1.00 98.75           C  
ANISOU 3171  CB  SER A  54    14247  11300  11972    185    339    142       C  
ATOM   3172  OG  SER A  54      -4.082   7.331 -66.676  1.00 99.77           O  
ANISOU 3172  OG  SER A  54    14462  11359  12086    183    277     99       O  
ATOM   3173  N   ARG A  55      -1.227   6.779 -67.981  1.00113.82           N  
ANISOU 3173  N   ARG A  55    16294  13139  13814    142    417    188       N  
ATOM   3174  CA  ARG A  55      -0.243   6.435 -68.997  1.00101.52           C  
ANISOU 3174  CA  ARG A  55    14789  11554  12231    128    470    218       C  
ATOM   3175  C   ARG A  55       0.648   7.633 -69.322  1.00109.87           C  
ANISOU 3175  C   ARG A  55    15888  12607  13250     95    466    225       C  
ATOM   3176  O   ARG A  55       0.357   8.783 -68.971  1.00108.71           O  
ANISOU 3176  O   ARG A  55    15747  12464  13095     83    413    199       O  
ATOM   3177  CB  ARG A  55      -0.907   5.898 -70.266  1.00101.89           C  
ANISOU 3177  CB  ARG A  55    14916  11525  12271    141    457    199       C  
ATOM   3178  CG  ARG A  55      -2.146   6.631 -70.702  1.00114.74           C  
ANISOU 3178  CG  ARG A  55    16602  13099  13894    146    376    147       C  
ATOM   3179  CD  ARG A  55      -3.157   5.643 -71.299  1.00137.31           C  
ANISOU 3179  CD  ARG A  55    19488  15912  16773    174    364    127       C  
ATOM   3180  NE  ARG A  55      -4.541   6.074 -71.122  1.00149.74           N  
ANISOU 3180  NE  ARG A  55    21072  17461  18363    189    289     79       N  
ATOM   3181  CZ  ARG A  55      -5.590   5.254 -71.111  1.00136.50           C  
ANISOU 3181  CZ  ARG A  55    19382  15765  16716    217    271     59       C  
ATOM   3182  NH1 ARG A  55      -5.416   3.944 -71.261  1.00119.91           N  
ANISOU 3182  NH1 ARG A  55    17258  13667  14634    234    324     84       N  
ATOM   3183  NH2 ARG A  55      -6.817   5.739 -70.946  1.00159.59           N  
ANISOU 3183  NH2 ARG A  55    22317  18667  19652    229    200     14       N  
ATOM   3184  N   GLY A  56       1.821   7.368 -69.850  1.00114.48           N  
ANISOU 3184  N   GLY A  56    16491  13192  13814     79    526    262       N  
ATOM   3185  CA  GLY A  56       2.714   8.486 -69.989  1.00101.90           C  
ANISOU 3185  CA  GLY A  56    14924  11603  12190     47    526    271       C  
ATOM   3186  C   GLY A  56       2.163   9.559 -70.865  1.00 91.70           C  
ANISOU 3186  C   GLY A  56    13723  10248  10870     35    463    234       C  
ATOM   3187  O   GLY A  56       2.136  10.702 -70.487  1.00 99.23           O  
ANISOU 3187  O   GLY A  56    14678  11213  11814     18    422    217       O  
ATOM   3188  N   THR A  57       1.642   9.168 -72.001  1.00 89.77           N  
ANISOU 3188  N   THR A  57    13554   9939  10616     44    453    219       N  
ATOM   3189  CA  THR A  57       1.131  10.099 -72.957  1.00 87.09           C  
ANISOU 3189  CA  THR A  57    13307   9534  10249     33    396    184       C  
ATOM   3190  C   THR A  57       0.058   9.376 -73.684  1.00 95.74           C  
ANISOU 3190  C   THR A  57    14447  10575  11355     59    373    158       C  
ATOM   3191  O   THR A  57       0.264   8.264 -74.086  1.00106.80           O  
ANISOU 3191  O   THR A  57    15848  11968  12763     72    420    179       O  
ATOM   3192  CB  THR A  57       2.230  10.452 -73.953  1.00 85.30           C  
ANISOU 3192  CB  THR A  57    13147   9279   9983      7    433    209       C  
ATOM   3193  OG1 THR A  57       3.129   9.352 -74.131  1.00 81.11           O  
ANISOU 3193  OG1 THR A  57    12593   8767   9456     11    511    253       O  
ATOM   3194  CG2 THR A  57       3.038  11.578 -73.446  1.00 92.90           C  
ANISOU 3194  CG2 THR A  57    14092  10276  10929    -21    430    220       C  
ATOM   3195  N   SER A  58      -1.082   9.989 -73.910  1.00 94.17           N  
ANISOU 3195  N   SER A  58    14289  10335  11155     65    300    112       N  
ATOM   3196  CA  SER A  58      -2.117   9.267 -74.603  1.00 97.15           C  
ANISOU 3196  CA  SER A  58    14708  10661  11544     90    277     86       C  
ATOM   3197  C   SER A  58      -2.245   9.759 -76.000  1.00 92.91           C  
ANISOU 3197  C   SER A  58    14282  10049  10972     81    252     68       C  
ATOM   3198  O   SER A  58      -2.958  10.702 -76.252  1.00 90.43           O  
ANISOU 3198  O   SER A  58    14015   9700  10646     76    186     31       O  
ATOM   3199  CB  SER A  58      -3.441   9.464 -73.904  1.00102.55           C  
ANISOU 3199  CB  SER A  58    15360  11349  12256    110    212     45       C  
ATOM   3200  OG  SER A  58      -4.508   9.176 -74.773  1.00105.21           O  
ANISOU 3200  OG  SER A  58    15760  11620  12595    128    172     11       O  
ATOM   3201  N   TYR A  59      -1.641   9.035 -76.919  1.00 86.35           N  
ANISOU 3201  N   TYR A  59    13492   9190  10125     81    303     93       N  
ATOM   3202  CA  TYR A  59      -1.643   9.373 -78.330  1.00 87.44           C  
ANISOU 3202  CA  TYR A  59    13738   9257  10228     72    288     81       C  
ATOM   3203  C   TYR A  59      -2.970   8.944 -78.933  1.00 86.01           C  
ANISOU 3203  C   TYR A  59    13602   9019  10059     98    241     41       C  
ATOM   3204  O   TYR A  59      -3.727   8.166 -78.345  1.00 87.24           O  
ANISOU 3204  O   TYR A  59    13704   9191  10251    123    234     30       O  
ATOM   3205  CB  TYR A  59      -0.502   8.676 -79.070  1.00 80.47           C  
ANISOU 3205  CB  TYR A  59    12879   8368   9326     65    364    124       C  
ATOM   3206  CG  TYR A  59       0.902   9.069 -78.635  1.00 82.03           C  
ANISOU 3206  CG  TYR A  59    13043   8617   9510     38    416    166       C  
ATOM   3207  CD1 TYR A  59       1.432   8.597 -77.436  1.00 84.70           C  
ANISOU 3207  CD1 TYR A  59    13279   9028   9874     40    457    195       C  
ATOM   3208  CD2 TYR A  59       1.709   9.886 -79.426  1.00 83.78           C  
ANISOU 3208  CD2 TYR A  59    13331   8812   9690     10    424    177       C  
ATOM   3209  CE1 TYR A  59       2.718   8.921 -77.033  1.00 84.85           C  
ANISOU 3209  CE1 TYR A  59    13265   9093   9881     16    505    233       C  
ATOM   3210  CE2 TYR A  59       3.008  10.226 -79.017  1.00 87.04           C  
ANISOU 3210  CE2 TYR A  59    13709   9270  10091    -14    473    216       C  
ATOM   3211  CZ  TYR A  59       3.501   9.734 -77.816  1.00 88.71           C  
ANISOU 3211  CZ  TYR A  59    13820   9556  10332    -11    513    243       C  
ATOM   3212  OH  TYR A  59       4.777  10.045 -77.391  1.00 89.95           O  
ANISOU 3212  OH  TYR A  59    13940   9759  10478    -35    561    282       O  
ATOM   3213  N   ALA A  60      -3.265   9.476 -80.105  1.00 79.98           N  
ANISOU 3213  N   ALA A  60    12937   8188   9265     93    206     18       N  
ATOM   3214  CA  ALA A  60      -4.405   8.984 -80.852  1.00 82.66           C  
ANISOU 3214  CA  ALA A  60    13328   8468   9612    117    168    -17       C  
ATOM   3215  C   ALA A  60      -3.945   7.858 -81.769  1.00 87.34           C  
ANISOU 3215  C   ALA A  60    13954   9033  10198    127    225      8       C  
ATOM   3216  O   ALA A  60      -2.774   7.785 -82.160  1.00 87.35           O  
ANISOU 3216  O   ALA A  60    13971   9043  10175    110    282     45       O  
ATOM   3217  CB  ALA A  60      -5.066  10.110 -81.644  1.00 85.22           C  
ANISOU 3217  CB  ALA A  60    13742   8731   9908    108     97    -58       C  
ATOM   3218  N   ASP A  61      -4.876   6.961 -82.089  1.00 96.72           N  
ANISOU 3218  N   ASP A  61    15151  10190  11408    156    211    -13       N  
ATOM   3219  CA  ASP A  61      -4.522   5.755 -82.830  1.00 95.57           C  
ANISOU 3219  CA  ASP A  61    15026  10023  11263    170    265     10       C  
ATOM   3220  C   ASP A  61      -3.782   6.070 -84.130  1.00 92.39           C  
ANISOU 3220  C   ASP A  61    14718   9573  10814    153    286     22       C  
ATOM   3221  O   ASP A  61      -2.867   5.335 -84.526  1.00 87.70           O  
ANISOU 3221  O   ASP A  61    14125   8986  10210    151    353     59       O  
ATOM   3222  CB  ASP A  61      -5.786   4.938 -83.109  1.00101.02           C  
ANISOU 3222  CB  ASP A  61    15726  10674  11980    202    232    -23       C  
ATOM   3223  CG  ASP A  61      -6.351   4.272 -81.854  1.00110.05           C  
ANISOU 3223  CG  ASP A  61    16769  11870  13174    222    232    -24       C  
ATOM   3224  OD1 ASP A  61      -5.559   3.729 -81.045  1.00105.00           O  
ANISOU 3224  OD1 ASP A  61    16053  11292  12551    219    290     15       O  
ATOM   3225  OD2 ASP A  61      -7.590   4.306 -81.670  1.00111.90           O  
ANISOU 3225  OD2 ASP A  61    17001  12083  13431    240    174    -64       O  
ATOM   3226  N   SER A  62      -4.146   7.174 -84.796  1.00 88.54           N  
ANISOU 3226  N   SER A  62    14308   9038  10295    141    231     -8       N  
ATOM   3227  CA  SER A  62      -3.565   7.477 -86.102  1.00 86.78           C  
ANISOU 3227  CA  SER A  62    14181   8764  10028    127    245      0       C  
ATOM   3228  C   SER A  62      -2.125   7.968 -85.976  1.00 91.09           C  
ANISOU 3228  C   SER A  62    14716   9346  10548     97    298     43       C  
ATOM   3229  O   SER A  62      -1.232   7.481 -86.679  1.00101.36           O  
ANISOU 3229  O   SER A  62    16047  10638  11828     92    356     75       O  
ATOM   3230  CB  SER A  62      -4.421   8.511 -86.827  1.00 93.32           C  
ANISOU 3230  CB  SER A  62    15094   9530  10832    124    168    -45       C  
ATOM   3231  OG  SER A  62      -4.449   9.727 -86.109  1.00 92.21           O  
ANISOU 3231  OG  SER A  62    14933   9416  10688    104    129    -57       O  
ATOM   3232  N   VAL A  63      -1.877   8.938 -85.086  1.00 94.05           N  
ANISOU 3232  N   VAL A  63    15048   9763  10923     77    280     44       N  
ATOM   3233  CA  VAL A  63      -0.535   9.512 -84.942  1.00 94.59           C  
ANISOU 3233  CA  VAL A  63    15106   9866  10968     46    325     83       C  
ATOM   3234  C   VAL A  63       0.409   8.625 -84.152  1.00 87.21           C  
ANISOU 3234  C   VAL A  63    14084   8997  10054     47    401    129       C  
ATOM   3235  O   VAL A  63       1.620   8.885 -84.139  1.00 85.20           O  
ANISOU 3235  O   VAL A  63    13823   8769   9780     24    449    165       O  
ATOM   3236  CB  VAL A  63      -0.558  10.880 -84.237  1.00 90.17           C  
ANISOU 3236  CB  VAL A  63    14530   9330  10403     24    279     68       C  
ATOM   3237  CG1 VAL A  63      -1.691  11.730 -84.769  1.00 92.53           C  
ANISOU 3237  CG1 VAL A  63    14898   9571  10689     28    196     18       C  
ATOM   3238  CG2 VAL A  63      -0.689  10.692 -82.752  1.00 85.83           C  
ANISOU 3238  CG2 VAL A  63    13870   8850   9892     30    281     73       C  
ATOM   3239  N   LYS A  64      -0.124   7.599 -83.493  1.00 88.83           N  
ANISOU 3239  N   LYS A  64    14223   9228  10299     72    410    127       N  
ATOM   3240  CA  LYS A  64       0.664   6.691 -82.676  1.00 85.19           C  
ANISOU 3240  CA  LYS A  64    13675   8831   9863     75    479    169       C  
ATOM   3241  C   LYS A  64       1.894   6.192 -83.425  1.00 83.08           C  
ANISOU 3241  C   LYS A  64    13436   8559   9571     64    552    211       C  
ATOM   3242  O   LYS A  64       1.837   5.897 -84.619  1.00 83.80           O  
ANISOU 3242  O   LYS A  64    13606   8594   9640     70    558    207       O  
ATOM   3243  CB  LYS A  64      -0.208   5.507 -82.274  1.00 89.29           C  
ANISOU 3243  CB  LYS A  64    14145   9358  10423    108    478    158       C  
ATOM   3244  CG  LYS A  64       0.128   4.884 -80.941  1.00 83.59           C  
ANISOU 3244  CG  LYS A  64    13310   8712   9738    114    517    184       C  
ATOM   3245  CD  LYS A  64      -1.062   4.060 -80.461  1.00 80.66           C  
ANISOU 3245  CD  LYS A  64    12896   8341   9408    146    490    160       C  
ATOM   3246  CE  LYS A  64      -0.737   3.306 -79.208  1.00 76.81           C  
ANISOU 3246  CE  LYS A  64    12299   7927   8958    155    533    188       C  
ATOM   3247  NZ  LYS A  64      -0.063   4.217 -78.233  1.00 76.15           N  
ANISOU 3247  NZ  LYS A  64    12163   7901   8870    132    536    203       N  
ATOM   3248  N   GLY A  65       3.014   6.095 -82.705  1.00 85.10           N  
ANISOU 3248  N   GLY A  65    13627   8877   9831     49    609    252       N  
ATOM   3249  CA  GLY A  65       4.256   5.613 -83.273  1.00 87.33           C  
ANISOU 3249  CA  GLY A  65    13926   9164  10093     38    683    296       C  
ATOM   3250  C   GLY A  65       4.947   6.546 -84.246  1.00 91.17           C  
ANISOU 3250  C   GLY A  65    14496   9613  10533     11    684    302       C  
ATOM   3251  O   GLY A  65       6.095   6.282 -84.615  1.00 95.06           O  
ANISOU 3251  O   GLY A  65    14995  10115  11007     -2    747    341       O  
ATOM   3252  N   ARG A  66       4.299   7.616 -84.686  1.00 82.99           N  
ANISOU 3252  N   ARG A  66    13523   8533   9476      3    618    266       N  
ATOM   3253  CA  ARG A  66       4.940   8.591 -85.554  1.00 82.73           C  
ANISOU 3253  CA  ARG A  66    13568   8466   9399    -23    616    272       C  
ATOM   3254  C   ARG A  66       5.305   9.864 -84.812  1.00 83.98           C  
ANISOU 3254  C   ARG A  66    13700   8659   9551    -50    592    272       C  
ATOM   3255  O   ARG A  66       6.432  10.354 -84.922  1.00 86.02           O  
ANISOU 3255  O   ARG A  66    13964   8933   9786    -76    630    302       O  
ATOM   3256  CB  ARG A  66       4.025   8.912 -86.747  1.00 82.08           C  
ANISOU 3256  CB  ARG A  66    13590   8304   9294    -14    562    233       C  
ATOM   3257  CG  ARG A  66       3.639   7.699 -87.597  1.00 86.84           C  
ANISOU 3257  CG  ARG A  66    14229   8867   9900     13    582    230       C  
ATOM   3258  CD  ARG A  66       2.954   8.096 -88.900  1.00 90.83           C  
ANISOU 3258  CD  ARG A  66    14845   9292  10375     18    535    197       C  
ATOM   3259  NE  ARG A  66       1.525   8.371 -88.742  1.00 87.41           N  
ANISOU 3259  NE  ARG A  66    14422   8830   9958     36    457    146       N  
ATOM   3260  CZ  ARG A  66       0.945   9.548 -89.002  1.00 96.24           C  
ANISOU 3260  CZ  ARG A  66    15593   9914  11058     25    390    112       C  
ATOM   3261  NH1 ARG A  66       1.665  10.598 -89.399  1.00 89.05           N  
ANISOU 3261  NH1 ARG A  66    14729   8994  10111     -3    391    123       N  
ATOM   3262  NH2 ARG A  66      -0.366   9.694 -88.835  1.00104.22           N  
ANISOU 3262  NH2 ARG A  66    16609  10901  12087     43    322     67       N  
ATOM   3263  N   PHE A  67       4.375  10.397 -84.039  1.00 86.81           N  
ANISOU 3263  N   PHE A  67    14026   9029   9930    -44    530    238       N  
ATOM   3264  CA  PHE A  67       4.632  11.594 -83.261  1.00 86.92           C  
ANISOU 3264  CA  PHE A  67    14008   9076   9940    -68    502    235       C  
ATOM   3265  C   PHE A  67       5.328  11.258 -81.941  1.00 86.18           C  
ANISOU 3265  C   PHE A  67    13805   9063   9875    -72    546    266       C  
ATOM   3266  O   PHE A  67       5.098  10.203 -81.332  1.00 83.22           O  
ANISOU 3266  O   PHE A  67    13366   8721   9533    -50    571    274       O  
ATOM   3267  CB  PHE A  67       3.320  12.323 -82.985  1.00 86.71           C  
ANISOU 3267  CB  PHE A  67    13994   9027   9923    -60    416    184       C  
ATOM   3268  CG  PHE A  67       2.689  12.924 -84.204  1.00 91.32           C  
ANISOU 3268  CG  PHE A  67    14687   9535  10478    -60    365    151       C  
ATOM   3269  CD1 PHE A  67       3.223  12.705 -85.466  1.00 96.10           C  
ANISOU 3269  CD1 PHE A  67    15372  10093  11050    -66    398    167       C  
ATOM   3270  CD2 PHE A  67       1.564  13.729 -84.091  1.00 91.27           C  
ANISOU 3270  CD2 PHE A  67    14703   9501  10474    -56    285    104       C  
ATOM   3271  CE1 PHE A  67       2.643  13.268 -86.593  1.00 97.24           C  
ANISOU 3271  CE1 PHE A  67    15616  10165  11164    -66    352    137       C  
ATOM   3272  CE2 PHE A  67       0.977  14.299 -85.222  1.00 95.06           C  
ANISOU 3272  CE2 PHE A  67    15283   9909  10925    -57    237     74       C  
ATOM   3273  CZ  PHE A  67       1.521  14.064 -86.470  1.00 94.19           C  
ANISOU 3273  CZ  PHE A  67    15252   9753  10782    -62    271     90       C  
ATOM   3274  N   THR A  68       6.199  12.169 -81.505  1.00 90.28           N  
ANISOU 3274  N   THR A  68    14305   9616  10382   -100    556    284       N  
ATOM   3275  CA  THR A  68       6.793  12.114 -80.176  1.00 88.16           C  
ANISOU 3275  CA  THR A  68    13934   9424  10137   -106    585    309       C  
ATOM   3276  C   THR A  68       6.507  13.431 -79.471  1.00 94.26           C  
ANISOU 3276  C   THR A  68    14690  10214  10910   -123    526    285       C  
ATOM   3277  O   THR A  68       6.518  14.493 -80.101  1.00100.03           O  
ANISOU 3277  O   THR A  68    15489  10905  11611   -142    491    269       O  
ATOM   3278  CB  THR A  68       8.308  11.861 -80.222  1.00 95.12           C  
ANISOU 3278  CB  THR A  68    14795  10339  11007   -126    664    360       C  
ATOM   3279  OG1 THR A  68       8.603  10.814 -81.158  1.00105.91           O  
ANISOU 3279  OG1 THR A  68    16200  11675  12364   -114    714    380       O  
ATOM   3280  CG2 THR A  68       8.808  11.440 -78.838  1.00 93.67           C  
ANISOU 3280  CG2 THR A  68    14499  10237  10856   -124    700    386       C  
ATOM   3281  N   ILE A  69       6.264  13.361 -78.160  1.00 98.13           N  
ANISOU 3281  N   ILE A  69    15089  10763  11432   -115    516    282       N  
ATOM   3282  CA  ILE A  69       5.788  14.498 -77.367  1.00 94.24           C  
ANISOU 3282  CA  ILE A  69    14572  10289  10945   -124    454    253       C  
ATOM   3283  C   ILE A  69       6.613  14.598 -76.090  1.00 91.47           C  
ANISOU 3283  C   ILE A  69    14125  10018  10613   -135    487    282       C  
ATOM   3284  O   ILE A  69       6.994  13.575 -75.513  1.00 90.89           O  
ANISOU 3284  O   ILE A  69    13983   9989  10563   -122    539    309       O  
ATOM   3285  CB  ILE A  69       4.286  14.333 -77.052  1.00 84.86           C  
ANISOU 3285  CB  ILE A  69    13375   9085   9781    -97    391    208       C  
ATOM   3286  CG1 ILE A  69       3.794  15.340 -76.026  1.00 86.66           C  
ANISOU 3286  CG1 ILE A  69    13559   9345  10022   -103    332    182       C  
ATOM   3287  CG2 ILE A  69       4.004  12.942 -76.571  1.00 87.49           C  
ANISOU 3287  CG2 ILE A  69    13646   9448  10149    -68    426    220       C  
ATOM   3288  CD1 ILE A  69       2.344  15.110 -75.671  1.00 85.96           C  
ANISOU 3288  CD1 ILE A  69    13456   9244   9959    -75    274    140       C  
ATOM   3289  N   SER A  70       6.906  15.823 -75.648  1.00 85.39           N  
ANISOU 3289  N   SER A  70    13347   9264   9832   -158    457    275       N  
ATOM   3290  CA  SER A  70       7.646  15.963 -74.400  1.00 91.62           C  
ANISOU 3290  CA  SER A  70    14044  10129  10639   -167    484    299       C  
ATOM   3291  C   SER A  70       7.387  17.322 -73.762  1.00 95.91           C  
ANISOU 3291  C   SER A  70    14576  10686  11180   -183    423    273       C  
ATOM   3292  O   SER A  70       7.164  18.321 -74.459  1.00102.54           O  
ANISOU 3292  O   SER A  70    15488  11477  11994   -199    379    251       O  
ATOM   3293  CB  SER A  70       9.152  15.768 -74.608  1.00 86.76           C  
ANISOU 3293  CB  SER A  70    13419   9536  10009   -188    559    349       C  
ATOM   3294  OG  SER A  70       9.570  16.258 -75.853  1.00 85.14           O  
ANISOU 3294  OG  SER A  70    13307   9274   9768   -208    564    353       O  
ATOM   3295  N   GLN A  71       7.433  17.334 -72.422  1.00 95.56           N  
ANISOU 3295  N   GLN A  71    14438  10708  11162   -178    422    277       N  
ATOM   3296  CA  GLN A  71       7.375  18.529 -71.587  1.00 91.65           C  
ANISOU 3296  CA  GLN A  71    13912  10242  10669   -193    375    259       C  
ATOM   3297  C   GLN A  71       8.795  18.967 -71.213  1.00 93.84           C  
ANISOU 3297  C   GLN A  71    14155  10562  10937   -220    422    297       C  
ATOM   3298  O   GLN A  71       9.754  18.197 -71.310  1.00 96.62           O  
ANISOU 3298  O   GLN A  71    14486  10936  11290   -223    493    339       O  
ATOM   3299  CB  GLN A  71       6.543  18.255 -70.326  1.00 94.50           C  
ANISOU 3299  CB  GLN A  71    14190  10651  11066   -169    346    239       C  
ATOM   3300  CG  GLN A  71       5.912  19.460 -69.626  1.00 89.98           C  
ANISOU 3300  CG  GLN A  71    13602  10089  10496   -175    273    203       C  
ATOM   3301  CD  GLN A  71       4.390  19.321 -69.469  1.00 88.58           C  
ANISOU 3301  CD  GLN A  71    13429   9891  10338   -148    211    158       C  
ATOM   3302  OE1 GLN A  71       3.717  18.857 -70.378  1.00 97.36           O  
ANISOU 3302  OE1 GLN A  71    14601  10947  11444   -135    199    142       O  
ATOM   3303  NE2 GLN A  71       3.853  19.718 -68.317  1.00 80.77           N  
ANISOU 3303  NE2 GLN A  71    12375   8944   9370   -140    171    137       N  
ATOM   3304  N   ASP A  72       8.934  20.242 -70.819  1.00 91.34           N  
ANISOU 3304  N   ASP A  72    13837  10256  10612   -241    381    283       N  
ATOM   3305  CA  ASP A  72      10.243  20.741 -70.356  1.00106.36           C  
ANISOU 3305  CA  ASP A  72    15702  12202  12508   -268    420    317       C  
ATOM   3306  C   ASP A  72       9.988  21.882 -69.368  1.00109.22           C  
ANISOU 3306  C   ASP A  72    16024  12597  12879   -277    364    293       C  
ATOM   3307  O   ASP A  72      10.058  23.065 -69.709  1.00100.14           O  
ANISOU 3307  O   ASP A  72    14921  11418  11708   -299    325    277       O  
ATOM   3308  CB  ASP A  72      11.150  21.191 -71.503  1.00102.15           C  
ANISOU 3308  CB  ASP A  72    15246  11625  11941   -295    448    338       C  
ATOM   3309  CG  ASP A  72      12.582  21.543 -71.039  1.00103.62           C  
ANISOU 3309  CG  ASP A  72    15389  11859  12124   -321    497    377       C  
ATOM   3310  OD1 ASP A  72      12.841  21.707 -69.827  1.00101.08           O  
ANISOU 3310  OD1 ASP A  72    14984  11601  11823   -322    498    383       O  
ATOM   3311  OD2 ASP A  72      13.474  21.642 -71.905  1.00108.80           O  
ANISOU 3311  OD2 ASP A  72    16095  12489  12756   -342    537    404       O  
ATOM   3312  N   ASN A  73       9.718  21.499 -68.118  1.00106.44           N  
ANISOU 3312  N   ASN A  73    15581  12305  12556   -259    362    291       N  
ATOM   3313  CA  ASN A  73       9.454  22.455 -67.052  1.00 94.46           C  
ANISOU 3313  CA  ASN A  73    14014  10826  11050   -264    312    268       C  
ATOM   3314  C   ASN A  73      10.563  23.490 -66.900  1.00 96.39           C  
ANISOU 3314  C   ASN A  73    14255  11088  11279   -297    322    286       C  
ATOM   3315  O   ASN A  73      10.293  24.607 -66.435  1.00105.62           O  
ANISOU 3315  O   ASN A  73    15420  12264  12447   -307    267    260       O  
ATOM   3316  CB  ASN A  73       9.255  21.697 -65.739  1.00100.65           C  
ANISOU 3316  CB  ASN A  73    14694  11680  11868   -240    328    275       C  
ATOM   3317  CG  ASN A  73       8.289  22.387 -64.797  1.00104.66           C  
ANISOU 3317  CG  ASN A  73    15164  12209  12391   -229    258    235       C  
ATOM   3318  OD1 ASN A  73       7.480  23.221 -65.218  1.00101.94           O  
ANISOU 3318  OD1 ASN A  73    14877  11820  12037   -232    193    197       O  
ATOM   3319  ND2 ASN A  73       8.346  22.018 -63.508  1.00 98.64           N  
ANISOU 3319  ND2 ASN A  73    14306  11517  11656   -215    271    244       N  
ATOM   3320  N   THR A  74      11.800  23.145 -67.268  1.00 99.83           N  
ANISOU 3320  N   THR A  74    14693  11534  11704   -313    390    329       N  
ATOM   3321  CA  THR A  74      12.898  24.096 -67.149  1.00100.42           C  
ANISOU 3321  CA  THR A  74    14765  11625  11765   -345    402    348       C  
ATOM   3322  C   THR A  74      12.583  25.377 -67.906  1.00100.57           C  
ANISOU 3322  C   THR A  74    14867  11586  11759   -366    344    319       C  
ATOM   3323  O   THR A  74      12.506  26.456 -67.309  1.00 96.21           O  
ANISOU 3323  O   THR A  74    14297  11050  11208   -378    298    300       O  
ATOM   3324  CB  THR A  74      14.199  23.477 -67.650  1.00 95.18           C  
ANISOU 3324  CB  THR A  74    14105  10968  11092   -359    484    398       C  
ATOM   3325  OG1 THR A  74      14.220  22.079 -67.328  1.00100.84           O  
ANISOU 3325  OG1 THR A  74    14770  11716  11828   -334    535    420       O  
ATOM   3326  CG2 THR A  74      15.377  24.177 -67.008  1.00 98.93           C  
ANISOU 3326  CG2 THR A  74    14533  11489  11566   -385    507    423       C  
ATOM   3327  N   LYS A  75      12.373  25.275 -69.221  1.00 96.23           N  
ANISOU 3327  N   LYS A  75    14408  10968  11186   -369    344    315       N  
ATOM   3328  CA  LYS A  75      11.875  26.397 -70.008  1.00 99.38           C  
ANISOU 3328  CA  LYS A  75    14893  11307  11562   -384    283    284       C  
ATOM   3329  C   LYS A  75      10.361  26.393 -70.174  1.00 94.36           C  
ANISOU 3329  C   LYS A  75    14288  10633  10930   -361    217    237       C  
ATOM   3330  O   LYS A  75       9.833  27.235 -70.913  1.00 94.99           O  
ANISOU 3330  O   LYS A  75    14444  10657  10991   -370    165    208       O  
ATOM   3331  CB  LYS A  75      12.528  26.436 -71.390  1.00 95.62           C  
ANISOU 3331  CB  LYS A  75    14503  10774  11053   -403    317    305       C  
ATOM   3332  CG  LYS A  75      14.030  26.619 -71.400  1.00 93.19           C  
ANISOU 3332  CG  LYS A  75    14179  10492  10737   -431    378    349       C  
ATOM   3333  CD  LYS A  75      14.580  26.616 -72.827  1.00 90.82           C  
ANISOU 3333  CD  LYS A  75    13971  10133  10405   -447    409    368       C  
ATOM   3334  CE  LYS A  75      14.822  25.203 -73.326  1.00107.69           C  
ANISOU 3334  CE  LYS A  75    16108  12265  12542   -430    474    396       C  
ATOM   3335  NZ  LYS A  75      13.594  24.378 -73.449  1.00117.64           N  
ANISOU 3335  NZ  LYS A  75    17378  13506  13815   -397    449    369       N  
ATOM   3336  N   ASN A  76       9.657  25.477 -69.505  1.00 89.84           N  
ANISOU 3336  N   ASN A  76    13659  10091  10385   -331    217    228       N  
ATOM   3337  CA  ASN A  76       8.200  25.368 -69.573  1.00 90.13           C  
ANISOU 3337  CA  ASN A  76    13718  10097  10431   -306    157    184       C  
ATOM   3338  C   ASN A  76       7.677  25.449 -71.009  1.00101.40           C  
ANISOU 3338  C   ASN A  76    15253  11441  11832   -307    135    166       C  
ATOM   3339  O   ASN A  76       7.204  26.505 -71.458  1.00 92.55           O  
ANISOU 3339  O   ASN A  76    14192  10278  10695   -319     76    136       O  
ATOM   3340  CB  ASN A  76       7.549  26.431 -68.699  1.00 90.42           C  
ANISOU 3340  CB  ASN A  76    13725  10153  10478   -307     86    147       C  
ATOM   3341  CG  ASN A  76       6.142  26.065 -68.316  1.00 87.68           C  
ANISOU 3341  CG  ASN A  76    13362   9802  10151   -277     36    109       C  
ATOM   3342  OD1 ASN A  76       5.191  26.433 -68.986  1.00 86.28           O  
ANISOU 3342  OD1 ASN A  76    13250   9569   9964   -271    -18     73       O  
ATOM   3343  ND2 ASN A  76       6.005  25.300 -67.245  1.00102.79           N  
ANISOU 3343  ND2 ASN A  76    15186  11775  12094   -255     56    117       N  
ATOM   3344  N   ILE A  77       7.784  24.329 -71.733  1.00102.63           N  
ANISOU 3344  N   ILE A  77    15434  11576  11985   -294    183    186       N  
ATOM   3345  CA  ILE A  77       7.434  24.213 -73.151  1.00 91.83           C  
ANISOU 3345  CA  ILE A  77    14167  10132  10593   -294    176    176       C  
ATOM   3346  C   ILE A  77       6.993  22.776 -73.424  1.00 94.24           C  
ANISOU 3346  C   ILE A  77    14465  10429  10911   -264    209    183       C  
ATOM   3347  O   ILE A  77       7.665  21.830 -73.002  1.00 94.88           O  
ANISOU 3347  O   ILE A  77    14488  10555  11007   -258    272    218       O  
ATOM   3348  CB  ILE A  77       8.629  24.543 -74.065  1.00 92.33           C  
ANISOU 3348  CB  ILE A  77    14286  10171  10625   -322    220    210       C  
ATOM   3349  CG1 ILE A  77       9.430  25.730 -73.533  1.00 94.23           C  
ANISOU 3349  CG1 ILE A  77    14504  10440  10859   -352    212    218       C  
ATOM   3350  CG2 ILE A  77       8.134  24.839 -75.461  1.00 96.32           C  
ANISOU 3350  CG2 ILE A  77    14901  10594  11101   -325    191    190       C  
ATOM   3351  CD1 ILE A  77      10.736  25.907 -74.205  1.00105.38           C  
ANISOU 3351  CD1 ILE A  77    15950  11844  12247   -380    267    258       C  
ATOM   3352  N   LEU A  78       5.890  22.593 -74.151  1.00 93.04           N  
ANISOU 3352  N   LEU A  78    14374  10221  10755   -247    167    150       N  
ATOM   3353  CA  LEU A  78       5.477  21.261 -74.590  1.00 90.07           C  
ANISOU 3353  CA  LEU A  78    14004   9828  10389   -220    197    155       C  
ATOM   3354  C   LEU A  78       5.843  21.071 -76.058  1.00 89.61           C  
ANISOU 3354  C   LEU A  78    14041   9708  10300   -229    223    168       C  
ATOM   3355  O   LEU A  78       5.707  21.996 -76.862  1.00 91.88           O  
ANISOU 3355  O   LEU A  78    14406   9943  10559   -244    186    150       O  
ATOM   3356  CB  LEU A  78       3.972  21.036 -74.410  1.00 89.26           C  
ANISOU 3356  CB  LEU A  78    13902   9706  10307   -192    136    110       C  
ATOM   3357  CG  LEU A  78       3.498  19.590 -74.670  1.00 85.29           C  
ANISOU 3357  CG  LEU A  78    13391   9194   9822   -162    167    116       C  
ATOM   3358  CD1 LEU A  78       3.857  18.651 -73.515  1.00 85.16           C  
ANISOU 3358  CD1 LEU A  78    13268   9251   9838   -148    216    143       C  
ATOM   3359  CD2 LEU A  78       2.008  19.469 -75.034  1.00 80.89           C  
ANISOU 3359  CD2 LEU A  78    12873   8589   9272   -138    104     69       C  
ATOM   3360  N   TYR A  79       6.292  19.869 -76.416  1.00 91.20           N  
ANISOU 3360  N   TYR A  79    14235   9912  10505   -217    287    198       N  
ATOM   3361  CA  TYR A  79       6.779  19.621 -77.768  1.00 92.82           C  
ANISOU 3361  CA  TYR A  79    14524  10064  10679   -225    321    215       C  
ATOM   3362  C   TYR A  79       5.885  18.641 -78.518  1.00 94.07           C  
ANISOU 3362  C   TYR A  79    14724  10176  10842   -197    315    198       C  
ATOM   3363  O   TYR A  79       5.013  17.979 -77.945  1.00 95.94           O  
ANISOU 3363  O   TYR A  79    14916  10429  11108   -171    297    180       O  
ATOM   3364  CB  TYR A  79       8.218  19.097 -77.743  1.00 99.83           C  
ANISOU 3364  CB  TYR A  79    15380  10988  11562   -239    406    269       C  
ATOM   3365  CG  TYR A  79       9.152  20.087 -77.132  1.00 93.57           C  
ANISOU 3365  CG  TYR A  79    14554  10235  10764   -269    413    286       C  
ATOM   3366  CD1 TYR A  79       9.061  21.427 -77.462  1.00 93.44           C  
ANISOU 3366  CD1 TYR A  79    14591  10186  10724   -291    362    265       C  
ATOM   3367  CD2 TYR A  79      10.123  19.694 -76.237  1.00 99.90           C  
ANISOU 3367  CD2 TYR A  79    15272  11103  11581   -275    469    323       C  
ATOM   3368  CE1 TYR A  79       9.906  22.360 -76.910  1.00106.91           C  
ANISOU 3368  CE1 TYR A  79    16268  11927  12426   -318    366    280       C  
ATOM   3369  CE2 TYR A  79      10.977  20.617 -75.677  1.00 98.80           C  
ANISOU 3369  CE2 TYR A  79    15103  11000  11438   -302    474    338       C  
ATOM   3370  CZ  TYR A  79      10.862  21.955 -76.012  1.00109.80           C  
ANISOU 3370  CZ  TYR A  79    16549  12360  12809   -323    422    316       C  
ATOM   3371  OH  TYR A  79      11.705  22.892 -75.454  1.00107.05           O  
ANISOU 3371  OH  TYR A  79    16171  12046  12457   -350    425    331       O  
ATOM   3372  N   LEU A  80       6.131  18.552 -79.830  1.00 92.98           N  
ANISOU 3372  N   LEU A  80    14674   9981  10674   -203    332    205       N  
ATOM   3373  CA  LEU A  80       5.413  17.609 -80.686  1.00 88.30           C  
ANISOU 3373  CA  LEU A  80    14129   9340  10080   -177    332    192       C  
ATOM   3374  C   LEU A  80       6.314  17.312 -81.886  1.00 88.28           C  
ANISOU 3374  C   LEU A  80    14195   9302  10046   -189    387    223       C  
ATOM   3375  O   LEU A  80       6.294  18.050 -82.870  1.00 91.46           O  
ANISOU 3375  O   LEU A  80    14685   9650  10417   -202    362    211       O  
ATOM   3376  CB  LEU A  80       4.067  18.165 -81.121  1.00 85.36           C  
ANISOU 3376  CB  LEU A  80    13817   8913   9704   -166    250    140       C  
ATOM   3377  CG  LEU A  80       3.157  17.165 -81.829  1.00 87.67           C  
ANISOU 3377  CG  LEU A  80    14146   9160  10002   -136    243    121       C  
ATOM   3378  CD1 LEU A  80       3.191  15.834 -81.100  1.00 84.99           C  
ANISOU 3378  CD1 LEU A  80    13725   8869   9699   -113    290    141       C  
ATOM   3379  CD2 LEU A  80       1.743  17.707 -81.890  1.00 90.54           C  
ANISOU 3379  CD2 LEU A  80    14543   9485  10372   -123    157     67       C  
ATOM   3380  N   GLN A  81       7.100  16.244 -81.776  1.00 93.06           N  
ANISOU 3380  N   GLN A  81    14759   9940  10662   -183    460    262       N  
ATOM   3381  CA  GLN A  81       8.018  15.819 -82.827  1.00 96.35           C  
ANISOU 3381  CA  GLN A  81    15228  10329  11050   -192    520    295       C  
ATOM   3382  C   GLN A  81       7.272  14.881 -83.763  1.00 94.94           C  
ANISOU 3382  C   GLN A  81    15105  10098  10870   -165    517    280       C  
ATOM   3383  O   GLN A  81       6.986  13.726 -83.416  1.00 91.65           O  
ANISOU 3383  O   GLN A  81    14641   9702  10480   -141    542    285       O  
ATOM   3384  CB  GLN A  81       9.245  15.136 -82.231  1.00104.73           C  
ANISOU 3384  CB  GLN A  81    16217  11451  12124   -199    600    345       C  
ATOM   3385  CG  GLN A  81      10.124  14.453 -83.261  1.00100.24           C  
ANISOU 3385  CG  GLN A  81    15695  10858  11532   -203    666    379       C  
ATOM   3386  CD  GLN A  81      11.561  14.921 -83.200  1.00106.69           C  
ANISOU 3386  CD  GLN A  81    16499  11704  12332   -233    719    421       C  
ATOM   3387  OE1 GLN A  81      12.107  15.175 -82.113  1.00106.03           O  
ANISOU 3387  OE1 GLN A  81    16337  11682  12267   -245    733    437       O  
ATOM   3388  NE2 GLN A  81      12.190  15.043 -84.379  1.00104.72           N  
ANISOU 3388  NE2 GLN A  81    16329  11412  12048   -247    747    438       N  
ATOM   3389  N   MET A  82       6.970  15.378 -84.951  1.00 93.83           N  
ANISOU 3389  N   MET A  82    15064   9889  10696   -170    488    261       N  
ATOM   3390  CA  MET A  82       6.207  14.640 -85.943  1.00 92.69           C  
ANISOU 3390  CA  MET A  82    14984   9688  10546   -146    477    242       C  
ATOM   3391  C   MET A  82       7.164  14.078 -86.989  1.00 91.42           C  
ANISOU 3391  C   MET A  82    14874   9504  10359   -151    543    277       C  
ATOM   3392  O   MET A  82       7.869  14.839 -87.658  1.00 96.25           O  
ANISOU 3392  O   MET A  82    15542  10092  10936   -175    553    290       O  
ATOM   3393  CB  MET A  82       5.157  15.563 -86.547  1.00 84.49           C  
ANISOU 3393  CB  MET A  82    14023   8590   9491   -145    396    194       C  
ATOM   3394  CG  MET A  82       4.666  16.532 -85.502  1.00 85.53           C  
ANISOU 3394  CG  MET A  82    14107   8752   9639   -153    339    169       C  
ATOM   3395  SD  MET A  82       3.920  18.015 -86.149  1.00116.23           S  
ANISOU 3395  SD  MET A  82    18085  12580  13499   -166    254    126       S  
ATOM   3396  CE  MET A  82       2.348  17.376 -86.713  1.00 94.03           C  
ANISOU 3396  CE  MET A  82    15318   9712  10698   -130    200     79       C  
ATOM   3397  N   ASN A  83       7.216  12.750 -87.094  1.00 85.98           N  
ANISOU 3397  N   ASN A  83    14161   8823   9685   -129    590    294       N  
ATOM   3398  CA  ASN A  83       8.158  12.061 -87.964  1.00 92.45           C  
ANISOU 3398  CA  ASN A  83    15015   9627  10483   -132    659    330       C  
ATOM   3399  C   ASN A  83       7.399  11.185 -88.954  1.00 98.42           C  
ANISOU 3399  C   ASN A  83    15832  10328  11235   -104    652    311       C  
ATOM   3400  O   ASN A  83       6.456  10.481 -88.562  1.00 98.65           O  
ANISOU 3400  O   ASN A  83    15828  10360  11295    -78    628    289       O  
ATOM   3401  CB  ASN A  83       9.149  11.231 -87.138  1.00 95.65           C  
ANISOU 3401  CB  ASN A  83    15331  10102  10912   -134    733    374       C  
ATOM   3402  CG  ASN A  83      10.132  12.095 -86.384  1.00 96.19           C  
ANISOU 3402  CG  ASN A  83    15352  10220  10977   -164    751    399       C  
ATOM   3403  OD1 ASN A  83      10.564  13.133 -86.895  1.00 93.40           O  
ANISOU 3403  OD1 ASN A  83    15053   9842  10592   -189    739    401       O  
ATOM   3404  ND2 ASN A  83      10.468  11.699 -85.141  1.00100.56           N  
ANISOU 3404  ND2 ASN A  83    15803  10842  11563   -162    778    418       N  
ATOM   3405  N   SER A  84       7.803  11.238 -90.237  1.00 88.78           N  
ANISOU 3405  N   SER A  84    14701   9056   9977   -110    671    320       N  
ATOM   3406  CA  SER A  84       7.149  10.483 -91.302  1.00 90.97           C  
ANISOU 3406  CA  SER A  84    15045   9274  10244    -85    664    302       C  
ATOM   3407  C   SER A  84       5.683  10.916 -91.431  1.00 89.78           C  
ANISOU 3407  C   SER A  84    14932   9081  10101    -69    577    248       C  
ATOM   3408  O   SER A  84       4.746  10.190 -91.103  1.00 91.65           O  
ANISOU 3408  O   SER A  84    15139   9318  10368    -43    555    225       O  
ATOM   3409  CB  SER A  84       7.287   8.973 -91.043  1.00 95.93           C  
ANISOU 3409  CB  SER A  84    15618   9930  10901    -62    719    323       C  
ATOM   3410  OG  SER A  84       6.545   8.198 -91.972  1.00 95.90           O  
ANISOU 3410  OG  SER A  84    15671   9871  10893    -35    707    303       O  
ATOM   3411  N   LEU A  85       5.520  12.132 -91.936  1.00 83.05           N  
ANISOU 3411  N   LEU A  85    14147   8192   9218    -87    530    228       N  
ATOM   3412  CA  LEU A  85       4.237  12.831 -91.927  1.00 88.98           C  
ANISOU 3412  CA  LEU A  85    14928   8907   9973    -79    444    177       C  
ATOM   3413  C   LEU A  85       3.289  12.370 -93.033  1.00 91.80           C  
ANISOU 3413  C   LEU A  85    15367   9195  10319    -53    412    145       C  
ATOM   3414  O   LEU A  85       3.705  12.147 -94.169  1.00 95.36           O  
ANISOU 3414  O   LEU A  85    15890   9604  10737    -54    440    158       O  
ATOM   3415  CB  LEU A  85       4.513  14.325 -92.063  1.00 91.83           C  
ANISOU 3415  CB  LEU A  85    15332   9256  10305   -109    410    171       C  
ATOM   3416  CG  LEU A  85       4.501  15.162 -90.793  1.00 85.03           C  
ANISOU 3416  CG  LEU A  85    14397   8446   9464   -125    381    165       C  
ATOM   3417  CD1 LEU A  85       5.220  16.470 -91.042  1.00 85.55           C  
ANISOU 3417  CD1 LEU A  85    14503   8505   9498   -159    374    175       C  
ATOM   3418  CD2 LEU A  85       3.072  15.420 -90.369  1.00 83.85           C  
ANISOU 3418  CD2 LEU A  85    14239   8282   9337   -107    302    115       C  
ATOM   3419  N   LYS A  86       2.001  12.236 -92.700  1.00 88.23           N  
ANISOU 3419  N   LYS A  86    14901   8729   9892    -31    352    104       N  
ATOM   3420  CA  LYS A  86       0.933  11.894 -93.638  1.00 90.39           C  
ANISOU 3420  CA  LYS A  86    15247   8937  10159     -6    310     67       C  
ATOM   3421  C   LYS A  86       0.141  13.138 -94.009  1.00 95.83           C  
ANISOU 3421  C   LYS A  86    16001   9580  10828    -14    230     25       C  
ATOM   3422  O   LYS A  86      -0.025  14.047 -93.188  1.00 95.16           O  
ANISOU 3422  O   LYS A  86    15880   9522  10753    -29    193     13       O  
ATOM   3423  CB  LYS A  86      -0.035  10.856 -93.065  1.00 99.23           C  
ANISOU 3423  CB  LYS A  86    16311  10069  11324     26    295     46       C  
ATOM   3424  CG  LYS A  86       0.534   9.431 -92.933  1.00107.22           C  
ANISOU 3424  CG  LYS A  86    17272  11111  12355     41    369     81       C  
ATOM   3425  CD  LYS A  86      -0.544   8.347 -93.116  1.00103.66           C  
ANISOU 3425  CD  LYS A  86    16819  10633  11932     76    350     55       C  
ATOM   3426  CE  LYS A  86      -1.715   8.618 -92.193  1.00101.25           C  
ANISOU 3426  CE  LYS A  86    16465  10342  11662     88    285     16       C  
ATOM   3427  NZ  LYS A  86      -2.910   7.784 -92.451  1.00 89.21           N  
ANISOU 3427  NZ  LYS A  86    14951   8783  10163    122    252    -17       N  
ATOM   3428  N   PRO A  87      -0.322  13.215 -95.254  1.00101.15           N  
ANISOU 3428  N   PRO A  87    16774  10184  11473     -5    203      3       N  
ATOM   3429  CA  PRO A  87      -1.190  14.334 -95.647  1.00101.98           C  
ANISOU 3429  CA  PRO A  87    16945  10242  11561     -9    123    -40       C  
ATOM   3430  C   PRO A  87      -2.488  14.399 -94.877  1.00105.19           C  
ANISOU 3430  C   PRO A  87    17310  10653  12004      9     56    -83       C  
ATOM   3431  O   PRO A  87      -3.058  15.483 -94.742  1.00109.24           O  
ANISOU 3431  O   PRO A  87    17846  11151  12511     -1     -7   -113       O  
ATOM   3432  CB  PRO A  87      -1.439  14.077 -97.135  1.00105.52           C  
ANISOU 3432  CB  PRO A  87    17500  10617  11976      4    117    -52       C  
ATOM   3433  CG  PRO A  87      -1.131  12.627 -97.338  1.00100.34           C  
ANISOU 3433  CG  PRO A  87    16821   9970  11334     25    179    -28       C  
ATOM   3434  CD  PRO A  87      -0.027  12.321 -96.382  1.00101.74           C  
ANISOU 3434  CD  PRO A  87    16907  10221  11528      9    246     18       C  
ATOM   3435  N   GLU A  88      -2.986  13.280 -94.373  1.00100.89           N  
ANISOU 3435  N   GLU A  88    16706  10129  11497     35     68    -87       N  
ATOM   3436  CA  GLU A  88      -4.188  13.342 -93.560  1.00 99.31           C  
ANISOU 3436  CA  GLU A  88    16461   9939  11335     51      7   -126       C  
ATOM   3437  C   GLU A  88      -3.930  13.978 -92.209  1.00101.27           C  
ANISOU 3437  C   GLU A  88    16623  10253  11604     33      2   -117       C  
ATOM   3438  O   GLU A  88      -4.893  14.379 -91.542  1.00102.97           O  
ANISOU 3438  O   GLU A  88    16807  10473  11842     40    -58   -152       O  
ATOM   3439  CB  GLU A  88      -4.795  11.944 -93.405  1.00101.67           C  
ANISOU 3439  CB  GLU A  88    16720  10241  11670     84     23   -131       C  
ATOM   3440  CG  GLU A  88      -5.261  11.338 -94.747  1.00128.28           C  
ANISOU 3440  CG  GLU A  88    20178  13541  15021    105     16   -148       C  
ATOM   3441  CD  GLU A  88      -4.096  10.946 -95.673  1.00126.67           C  
ANISOU 3441  CD  GLU A  88    20022  13325  14783     96     85   -108       C  
ATOM   3442  OE1 GLU A  88      -2.947  10.907 -95.159  1.00119.85           O  
ANISOU 3442  OE1 GLU A  88    19108  12513  13918     77    145    -65       O  
ATOM   3443  OE2 GLU A  88      -4.311  10.690 -96.893  1.00119.83           O  
ANISOU 3443  OE2 GLU A  88    19242  12398  13892    108     79   -119       O  
ATOM   3444  N   ASP A  89      -2.656  14.078 -91.814  1.00104.56           N  
ANISOU 3444  N   ASP A  89    16999  10716  12012     10     62    -73       N  
ATOM   3445  CA  ASP A  89      -2.198  14.980 -90.768  1.00 96.34           C  
ANISOU 3445  CA  ASP A  89    15898   9729  10978    -14     56    -62       C  
ATOM   3446  C   ASP A  89      -1.984  16.408 -91.276  1.00 98.83           C  
ANISOU 3446  C   ASP A  89    16283  10014  11256    -41     19    -73       C  
ATOM   3447  O   ASP A  89      -1.141  17.134 -90.738  1.00 94.58           O  
ANISOU 3447  O   ASP A  89    15713   9513  10709    -68     37    -50       O  
ATOM   3448  CB  ASP A  89      -0.914  14.441 -90.121  1.00 94.98           C  
ANISOU 3448  CB  ASP A  89    15653   9622  10815    -27    138    -10       C  
ATOM   3449  CG  ASP A  89      -1.033  12.964 -89.680  1.00104.86           C  
ANISOU 3449  CG  ASP A  89    16838  10903  12102      0    181      4       C  
ATOM   3450  OD1 ASP A  89      -2.172  12.498 -89.446  1.00 99.58           O  
ANISOU 3450  OD1 ASP A  89    16153  10223  11462     25    141    -28       O  
ATOM   3451  OD2 ASP A  89      -0.003  12.262 -89.565  1.00 98.60           O  
ANISOU 3451  OD2 ASP A  89    16009  10145  11311     -5    255     48       O  
ATOM   3452  N   THR A  90      -2.696  16.823 -92.322  1.00 98.06           N  
ANISOU 3452  N   THR A  90    16279   9846  11133    -35    -31   -105       N  
ATOM   3453  CA  THR A  90      -2.743  18.230 -92.706  1.00100.19           C  
ANISOU 3453  CA  THR A  90    16612  10084  11372    -57    -80   -123       C  
ATOM   3454  C   THR A  90      -3.829  18.897 -91.878  1.00 97.51           C  
ANISOU 3454  C   THR A  90    16239   9754  11057    -52   -155   -166       C  
ATOM   3455  O   THR A  90      -5.010  18.558 -92.014  1.00 91.49           O  
ANISOU 3455  O   THR A  90    15491   8960  10311    -27   -203   -204       O  
ATOM   3456  CB  THR A  90      -3.031  18.418 -94.202  1.00101.48           C  
ANISOU 3456  CB  THR A  90    16893  10169  11496    -52   -102   -140       C  
ATOM   3457  OG1 THR A  90      -1.833  18.234 -94.973  1.00 98.56           O  
ANISOU 3457  OG1 THR A  90    16563   9793  11094    -67    -36    -99       O  
ATOM   3458  CG2 THR A  90      -3.553  19.817 -94.470  1.00 96.98           C  
ANISOU 3458  CG2 THR A  90    16382   9562  10904    -67   -174   -174       C  
ATOM   3459  N   ALA A  91      -3.424  19.827 -91.015  1.00 99.55           N  
ANISOU 3459  N   ALA A  91    16452  10054  11319    -75   -166   -159       N  
ATOM   3460  CA  ALA A  91      -4.365  20.511 -90.137  1.00 99.65           C  
ANISOU 3460  CA  ALA A  91    16427  10082  11356    -72   -235   -197       C  
ATOM   3461  C   ALA A  91      -3.684  21.562 -89.269  1.00 95.44           C  
ANISOU 3461  C   ALA A  91    15848   9596  10821   -102   -236   -183       C  
ATOM   3462  O   ALA A  91      -2.456  21.699 -89.285  1.00 91.64           O  
ANISOU 3462  O   ALA A  91    15357   9140  10323   -124   -181   -142       O  
ATOM   3463  CB  ALA A  91      -5.093  19.511 -89.238  1.00100.20           C  
ANISOU 3463  CB  ALA A  91    16413  10186  11471    -45   -236   -208       C  
ATOM   3464  N   MET A  92      -4.481  22.293 -88.494  1.00 98.77           N  
ANISOU 3464  N   MET A  92    16238  10030  11261   -101   -300   -217       N  
ATOM   3465  CA  MET A  92      -4.003  23.379 -87.651  1.00100.59           C  
ANISOU 3465  CA  MET A  92    16427  10301  11491   -127   -314   -211       C  
ATOM   3466  C   MET A  92      -3.992  22.934 -86.199  1.00100.76           C  
ANISOU 3466  C   MET A  92    16332  10397  11553   -120   -298   -202       C  
ATOM   3467  O   MET A  92      -5.039  22.574 -85.650  1.00 94.70           O  
ANISOU 3467  O   MET A  92    15528   9637  10816    -97   -335   -232       O  
ATOM   3468  CB  MET A  92      -4.863  24.629 -87.824  1.00 99.68           C  
ANISOU 3468  CB  MET A  92    16364  10147  11364   -134   -399   -256       C  
ATOM   3469  CG  MET A  92      -4.255  25.854 -87.168  1.00 96.70           C  
ANISOU 3469  CG  MET A  92    15960   9803  10979   -164   -412   -248       C  
ATOM   3470  SD  MET A  92      -4.532  27.390 -88.067  1.00107.45           S  
ANISOU 3470  SD  MET A  92    17425  11099  12301   -185   -479   -277       S  
ATOM   3471  CE  MET A  92      -6.308  27.633 -87.903  1.00124.30           C  
ANISOU 3471  CE  MET A  92    19573  13200  14455   -159   -575   -342       C  
ATOM   3472  N   TYR A  93      -2.822  23.026 -85.568  1.00103.34           N  
ANISOU 3472  N   TYR A  93    16603  10780  11882   -140   -244   -162       N  
ATOM   3473  CA  TYR A  93      -2.555  22.419 -84.270  1.00 92.73           C  
ANISOU 3473  CA  TYR A  93    15148   9510  10574   -134   -210   -142       C  
ATOM   3474  C   TYR A  93      -2.609  23.478 -83.180  1.00 90.72           C  
ANISOU 3474  C   TYR A  93    14840   9298  10331   -149   -250   -155       C  
ATOM   3475  O   TYR A  93      -2.021  24.549 -83.332  1.00 93.50           O  
ANISOU 3475  O   TYR A  93    15221   9645  10659   -176   -260   -149       O  
ATOM   3476  CB  TYR A  93      -1.181  21.743 -84.285  1.00 84.75           C  
ANISOU 3476  CB  TYR A  93    14108   8535   9557   -145   -121    -87       C  
ATOM   3477  CG  TYR A  93      -1.148  20.520 -85.174  1.00 99.63           C  
ANISOU 3477  CG  TYR A  93    16028  10389  11437   -126    -77    -73       C  
ATOM   3478  CD1 TYR A  93      -1.332  20.635 -86.550  1.00108.65           C  
ANISOU 3478  CD1 TYR A  93    17275  11461  12548   -125    -90    -84       C  
ATOM   3479  CD2 TYR A  93      -0.948  19.253 -84.649  1.00 89.50           C  
ANISOU 3479  CD2 TYR A  93    14675   9147  10183   -108    -23    -49       C  
ATOM   3480  CE1 TYR A  93      -1.316  19.528 -87.372  1.00105.48           C  
ANISOU 3480  CE1 TYR A  93    16907  11030  12142   -107    -51    -73       C  
ATOM   3481  CE2 TYR A  93      -0.928  18.137 -85.472  1.00 87.61           C  
ANISOU 3481  CE2 TYR A  93    14469   8878   9939    -90     16    -38       C  
ATOM   3482  CZ  TYR A  93      -1.112  18.287 -86.826  1.00 91.61           C  
ANISOU 3482  CZ  TYR A  93    15079   9315  10413    -90      1    -50       C  
ATOM   3483  OH  TYR A  93      -1.089  17.187 -87.637  1.00 87.84           O  
ANISOU 3483  OH  TYR A  93    14635   8809   9933    -72     39    -38       O  
ATOM   3484  N   TYR A  94      -3.315  23.185 -82.091  1.00 93.43           N  
ANISOU 3484  N   TYR A  94    15106   9682  10711   -131   -273   -173       N  
ATOM   3485  CA  TYR A  94      -3.274  24.012 -80.893  1.00 91.20           C  
ANISOU 3485  CA  TYR A  94    14756   9452  10444   -143   -301   -180       C  
ATOM   3486  C   TYR A  94      -2.767  23.181 -79.726  1.00 84.69           C  
ANISOU 3486  C   TYR A  94    13823   8703   9651   -135   -247   -149       C  
ATOM   3487  O   TYR A  94      -2.898  21.954 -79.728  1.00 83.50           O  
ANISOU 3487  O   TYR A  94    13646   8560   9519   -113   -210   -137       O  
ATOM   3488  CB  TYR A  94      -4.654  24.578 -80.530  1.00 95.16           C  
ANISOU 3488  CB  TYR A  94    15260   9936  10962   -129   -386   -233       C  
ATOM   3489  CG  TYR A  94      -5.594  24.873 -81.688  1.00101.94           C  
ANISOU 3489  CG  TYR A  94    16219  10715  11801   -120   -441   -271       C  
ATOM   3490  CD1 TYR A  94      -5.559  26.103 -82.350  1.00102.87           C  
ANISOU 3490  CD1 TYR A  94    16412  10788  11886   -142   -483   -288       C  
ATOM   3491  CD2 TYR A  94      -6.530  23.928 -82.107  1.00 96.77           C  
ANISOU 3491  CD2 TYR A  94    15582  10028  11160    -91   -452   -292       C  
ATOM   3492  CE1 TYR A  94      -6.431  26.383 -83.377  1.00102.05           C  
ANISOU 3492  CE1 TYR A  94    16397  10612  11764   -133   -535   -323       C  
ATOM   3493  CE2 TYR A  94      -7.401  24.199 -83.138  1.00102.44           C  
ANISOU 3493  CE2 TYR A  94    16389  10673  11861    -82   -504   -327       C  
ATOM   3494  CZ  TYR A  94      -7.349  25.423 -83.768  1.00108.26           C  
ANISOU 3494  CZ  TYR A  94    17200  11369  12565   -103   -545   -343       C  
ATOM   3495  OH  TYR A  94      -8.225  25.671 -84.804  1.00117.90           O  
ANISOU 3495  OH  TYR A  94    18511  12517  13769    -94   -597   -379       O  
ATOM   3496  N   CYS A  95      -2.187  23.849 -78.722  1.00 85.64           N  
ANISOU 3496  N   CYS A  95    13882   8879   9780   -153   -244   -137       N  
ATOM   3497  CA  CYS A  95      -1.920  23.218 -77.432  1.00 82.75           C  
ANISOU 3497  CA  CYS A  95    13406   8588   9446   -143   -209   -117       C  
ATOM   3498  C   CYS A  95      -2.883  23.765 -76.396  1.00 80.47           C  
ANISOU 3498  C   CYS A  95    13067   8326   9183   -133   -274   -155       C  
ATOM   3499  O   CYS A  95      -3.068  24.982 -76.287  1.00 81.12           O  
ANISOU 3499  O   CYS A  95    13171   8398   9253   -149   -327   -178       O  
ATOM   3500  CB  CYS A  95      -0.489  23.430 -76.930  1.00 82.77           C  
ANISOU 3500  CB  CYS A  95    13363   8644   9443   -168   -151    -72       C  
ATOM   3501  SG  CYS A  95       0.014  25.121 -76.581  1.00 96.74           S  
ANISOU 3501  SG  CYS A  95    15139  10424  11193   -202   -190    -79       S  
ATOM   3502  N   ALA A  96      -3.497  22.867 -75.651  1.00 81.78           N  
ANISOU 3502  N   ALA A  96    13166   8524   9383   -107   -269   -160       N  
ATOM   3503  CA  ALA A  96      -4.236  23.272 -74.479  1.00 89.45           C  
ANISOU 3503  CA  ALA A  96    14072   9534  10381    -97   -318   -188       C  
ATOM   3504  C   ALA A  96      -3.402  23.009 -73.242  1.00 85.37           C  
ANISOU 3504  C   ALA A  96    13453   9100   9884   -101   -270   -154       C  
ATOM   3505  O   ALA A  96      -2.233  22.617 -73.305  1.00 89.07           O  
ANISOU 3505  O   ALA A  96    13905   9593  10344   -114   -203   -110       O  
ATOM   3506  CB  ALA A  96      -5.568  22.545 -74.356  1.00 86.13           C  
ANISOU 3506  CB  ALA A  96    13639   9099   9988    -64   -352   -220       C  
ATOM   3507  N   ALA A  97      -4.042  23.212 -72.099  1.00 88.10           N  
ANISOU 3507  N   ALA A  97    13729   9487  10256    -89   -306   -175       N  
ATOM   3508  CA  ALA A  97      -3.456  22.986 -70.795  1.00 86.07           C  
ANISOU 3508  CA  ALA A  97    13370   9310  10021    -89   -271   -150       C  
ATOM   3509  C   ALA A  97      -4.615  22.921 -69.817  1.00 88.16           C  
ANISOU 3509  C   ALA A  97    13577   9601  10318    -64   -320   -184       C  
ATOM   3510  O   ALA A  97      -5.672  23.509 -70.071  1.00 89.45           O  
ANISOU 3510  O   ALA A  97    13782   9724  10480    -58   -389   -227       O  
ATOM   3511  CB  ALA A  97      -2.462  24.089 -70.425  1.00 88.26           C  
ANISOU 3511  CB  ALA A  97    13637   9617  10281   -120   -268   -134       C  
ATOM   3512  N   VAL A  98      -4.421  22.193 -68.714  1.00 94.17           N  
ANISOU 3512  N   VAL A  98    14243  10429  11108    -50   -284   -163       N  
ATOM   3513  CA  VAL A  98      -5.509  21.892 -67.778  1.00 94.75           C  
ANISOU 3513  CA  VAL A  98    14255  10530  11215    -23   -320   -190       C  
ATOM   3514  C   VAL A  98      -5.001  21.760 -66.340  1.00 96.24           C  
ANISOU 3514  C   VAL A  98    14337  10805  11426    -21   -291   -168       C  
ATOM   3515  O   VAL A  98      -3.883  21.267 -66.126  1.00 96.30           O  
ANISOU 3515  O   VAL A  98    14308  10851  11433    -29   -224   -124       O  
ATOM   3516  CB  VAL A  98      -6.243  20.612 -68.203  1.00 91.14           C  
ANISOU 3516  CB  VAL A  98    13805  10047  10777      6   -305   -194       C  
ATOM   3517  CG1 VAL A  98      -7.265  20.905 -69.300  1.00 93.15           C  
ANISOU 3517  CG1 VAL A  98    14152  10222  11020     11   -362   -234       C  
ATOM   3518  CG2 VAL A  98      -5.234  19.573 -68.654  1.00 88.28           C  
ANISOU 3518  CG2 VAL A  98    13441   9692  10410      3   -222   -146       C  
ATOM   3519  N   PRO A  99      -5.788  22.162 -65.362  1.00 95.70           N  
ANISOU 3519  N   PRO A  99    14218  10767  11378     -8   -340   -197       N  
ATOM   3520  CA  PRO A  99      -5.342  22.001 -63.989  1.00 97.52           C  
ANISOU 3520  CA  PRO A  99    14345  11078  11629     -3   -314   -176       C  
ATOM   3521  C   PRO A  99      -5.468  20.567 -63.475  1.00103.69           C  
ANISOU 3521  C   PRO A  99    15061  11896  12442     24   -264   -154       C  
ATOM   3522  O   PRO A  99      -6.333  19.820 -63.899  1.00105.24           O  
ANISOU 3522  O   PRO A  99    15276  12058  12651     45   -273   -169       O  
ATOM   3523  CB  PRO A  99      -6.296  22.900 -63.217  1.00 99.91           C  
ANISOU 3523  CB  PRO A  99    14624  11393  11942      3   -388   -219       C  
ATOM   3524  CG  PRO A  99      -7.348  23.343 -64.176  1.00106.21           C  
ANISOU 3524  CG  PRO A  99    15508  12116  12730      7   -451   -263       C  
ATOM   3525  CD  PRO A  99      -7.182  22.585 -65.437  1.00 96.68           C  
ANISOU 3525  CD  PRO A  99    14369  10854  11510      7   -416   -248       C  
ATOM   3526  N   ARG A 100      -4.621  20.207 -62.522  1.00 99.28           N  
ANISOU 3526  N   ARG A 100    14420  11406  11894     23   -213   -118       N  
ATOM   3527  CA  ARG A 100      -4.634  18.897 -61.885  1.00 93.63           C  
ANISOU 3527  CA  ARG A 100    13632  10734  11208     47   -164    -94       C  
ATOM   3528  C   ARG A 100      -5.470  18.973 -60.623  1.00 98.45           C  
ANISOU 3528  C   ARG A 100    14166  11393  11848     68   -200   -116       C  
ATOM   3529  O   ARG A 100      -6.367  19.790 -60.501  1.00106.47           O  
ANISOU 3529  O   ARG A 100    15199  12389  12863     71   -269   -158       O  
ATOM   3530  CB  ARG A 100      -3.228  18.469 -61.509  1.00 89.66           C  
ANISOU 3530  CB  ARG A 100    13080  10283  10702     34    -88    -42       C  
ATOM   3531  CG  ARG A 100      -2.258  18.457 -62.661  1.00 95.32           C  
ANISOU 3531  CG  ARG A 100    13866  10961  11390     11    -47    -16       C  
ATOM   3532  CD  ARG A 100      -0.825  18.508 -62.194  1.00 90.20           C  
ANISOU 3532  CD  ARG A 100    13173  10366  10734     -8     12     28       C  
ATOM   3533  NE  ARG A 100      -0.084  17.295 -62.486  1.00 84.16           N  
ANISOU 3533  NE  ARG A 100    12393   9610   9973     -3     89     71       N  
ATOM   3534  CZ  ARG A 100       1.203  17.286 -62.801  1.00 89.84           C  
ANISOU 3534  CZ  ARG A 100    13121  10341  10675    -25    143    109       C  
ATOM   3535  NH1 ARG A 100       1.881  18.414 -62.878  1.00 90.96           N  
ANISOU 3535  NH1 ARG A 100    13285  10482  10792    -53    130    110       N  
ATOM   3536  NH2 ARG A 100       1.820  16.154 -63.048  1.00 97.52           N  
ANISOU 3536  NH2 ARG A 100    14079  11322  11653    -19    212    146       N  
ATOM   3537  N   ALA A 101      -5.238  18.072 -59.689  1.00105.49           N  
ANISOU 3537  N   ALA A 101    14971  12345  12765     85   -155    -90       N  
ATOM   3538  CA  ALA A 101      -5.985  18.150 -58.444  1.00 98.58           C  
ANISOU 3538  CA  ALA A 101    14021  11519  11916    106   -187   -109       C  
ATOM   3539  C   ALA A 101      -5.185  17.829 -57.186  1.00100.58           C  
ANISOU 3539  C   ALA A 101    14174  11856  12184    109   -140    -74       C  
ATOM   3540  O   ALA A 101      -4.195  17.121 -57.218  1.00100.54           O  
ANISOU 3540  O   ALA A 101    14147  11875  12178    104    -73    -32       O  
ATOM   3541  CB  ALA A 101      -7.232  17.294 -58.523  1.00105.43           C  
ANISOU 3541  CB  ALA A 101    14885  12363  12812    136   -206   -131       C  
ATOM   3542  N   GLY A 102      -5.611  18.394 -56.071  1.00111.92           N  
ANISOU 3542  N   GLY A 102    15553  13339  13634    117   -178    -94       N  
ATOM   3543  CA  GLY A 102      -4.964  18.104 -54.810  1.00113.21           C  
ANISOU 3543  CA  GLY A 102    15619  13584  13811    123   -139    -64       C  
ATOM   3544  C   GLY A 102      -4.591  16.640 -54.824  1.00108.32           C  
ANISOU 3544  C   GLY A 102    14965  12982  13210    138    -67    -25       C  
ATOM   3545  O   GLY A 102      -5.336  15.804 -55.355  1.00 97.22           O  
ANISOU 3545  O   GLY A 102    13582  11539  11818    157    -66    -33       O  
ATOM   3546  N   ILE A 103      -3.418  16.315 -54.283  1.00104.67           N  
ANISOU 3546  N   ILE A 103    14449  12575  12747    130     -6     17       N  
ATOM   3547  CA  ILE A 103      -2.923  14.956 -54.412  1.00102.27           C  
ANISOU 3547  CA  ILE A 103    14118  12284  12456    141     66     58       C  
ATOM   3548  C   ILE A 103      -3.871  13.964 -53.765  1.00101.36           C  
ANISOU 3548  C   ILE A 103    13946  12190  12376    176     67     52       C  
ATOM   3549  O   ILE A 103      -3.792  12.765 -54.050  1.00103.75           O  
ANISOU 3549  O   ILE A 103    14239  12488  12693    190    115     77       O  
ATOM   3550  CB  ILE A 103      -1.523  14.827 -53.804  1.00100.42           C  
ANISOU 3550  CB  ILE A 103    13828  12110  12216    128    128    103       C  
ATOM   3551  CG1 ILE A 103      -0.706  16.049 -54.168  1.00103.01           C  
ANISOU 3551  CG1 ILE A 103    14200  12427  12512     95    113    102       C  
ATOM   3552  CG2 ILE A 103      -0.829  13.617 -54.355  1.00 94.05           C  
ANISOU 3552  CG2 ILE A 103    13024  11297  11412    130    201    144       C  
ATOM   3553  CD1 ILE A 103      -0.593  16.940 -53.004  1.00102.12           C  
ANISOU 3553  CD1 ILE A 103    14028  12370  12401     91     83     92       C  
ATOM   3554  N   GLU A 104      -4.864  14.482 -53.068  1.00 98.83           N  
ANISOU 3554  N   GLU A 104    13600  11884  12069    190      8     16       N  
ATOM   3555  CA  GLU A 104      -5.848  13.613 -52.474  1.00101.67           C  
ANISOU 3555  CA  GLU A 104    13908  12260  12462    223      4      8       C  
ATOM   3556  C   GLU A 104      -6.650  12.995 -53.601  1.00107.26           C  
ANISOU 3556  C   GLU A 104    14682  12896  13175    233     -7     -9       C  
ATOM   3557  O   GLU A 104      -7.379  12.039 -53.392  1.00110.48           O  
ANISOU 3557  O   GLU A 104    15060  13306  13611    259      1    -10       O  
ATOM   3558  CB  GLU A 104      -6.754  14.343 -51.492  1.00 97.15           C  
ANISOU 3558  CB  GLU A 104    13295  11717  11902    236    -58    -28       C  
ATOM   3559  CG  GLU A 104      -6.344  14.191 -50.030  1.00105.11           C  
ANISOU 3559  CG  GLU A 104    14200  12812  12926    247    -33     -7       C  
ATOM   3560  CD  GLU A 104      -7.037  13.056 -49.305  1.00105.47           C  
ANISOU 3560  CD  GLU A 104    14177  12890  13007    281    -14      0       C  
ATOM   3561  OE1 GLU A 104      -7.611  12.189 -49.971  1.00 98.94           O  
ANISOU 3561  OE1 GLU A 104    13378  12021  12194    294     -4     -1       O  
ATOM   3562  OE2 GLU A 104      -6.991  13.030 -48.070  1.00 89.66           O  
ANISOU 3562  OE2 GLU A 104    12092  10954  11019    294     -8      9       O  
ATOM   3563  N   SER A 105      -6.560  13.575 -54.789  1.00104.52           N  
ANISOU 3563  N   SER A 105    14428  12484  12801    212    -28    -23       N  
ATOM   3564  CA  SER A 105      -7.200  12.988 -55.954  1.00104.35           C  
ANISOU 3564  CA  SER A 105    14475  12392  12781    220    -35    -37       C  
ATOM   3565  C   SER A 105      -6.236  12.161 -56.793  1.00104.54           C  
ANISOU 3565  C   SER A 105    14529  12398  12795    210     34      3       C  
ATOM   3566  O   SER A 105      -6.655  11.190 -57.433  1.00 94.93           O  
ANISOU 3566  O   SER A 105    13335  11144  11590    225     52      6       O  
ATOM   3567  CB  SER A 105      -7.826  14.093 -56.803  1.00102.20           C  
ANISOU 3567  CB  SER A 105    14290  12054  12486    206   -104    -80       C  
ATOM   3568  OG  SER A 105      -8.346  15.127 -55.966  1.00108.38           O  
ANISOU 3568  OG  SER A 105    15046  12864  13271    206   -163   -112       O  
ATOM   3569  N   GLY A 106      -4.952  12.509 -56.777  1.00109.14           N  
ANISOU 3569  N   GLY A 106    15108  13006  13355    186     73     35       N  
ATOM   3570  CA  GLY A 106      -3.936  11.727 -57.447  1.00 99.38           C  
ANISOU 3570  CA  GLY A 106    13889  11760  12109    177    143     76       C  
ATOM   3571  C   GLY A 106      -3.081  12.551 -58.382  1.00 93.70           C  
ANISOU 3571  C   GLY A 106    13245  11005  11352    145    145     81       C  
ATOM   3572  O   GLY A 106      -2.356  11.997 -59.212  1.00 96.71           O  
ANISOU 3572  O   GLY A 106    13663  11362  11721    135    194    109       O  
ATOM   3573  N   ALA A 107      -3.145  13.877 -58.245  1.00 94.01           N  
ANISOU 3573  N   ALA A 107    13305  11040  11373    127     93     56       N  
ATOM   3574  CA  ALA A 107      -2.558  14.806 -59.219  1.00101.90           C  
ANISOU 3574  CA  ALA A 107    14386  11994  12336     97     81     52       C  
ATOM   3575  C   ALA A 107      -3.061  14.502 -60.627  1.00106.90           C  
ANISOU 3575  C   ALA A 107    15112  12547  12958     98     69     37       C  
ATOM   3576  O   ALA A 107      -2.287  14.356 -61.574  1.00102.94           O  
ANISOU 3576  O   ALA A 107    14664  12013  12434     81    106     59       O  
ATOM   3577  CB  ALA A 107      -1.032  14.785 -59.183  1.00 91.33           C  
ANISOU 3577  CB  ALA A 107    13031  10690  10982     74    145     98       C  
ATOM   3578  N   TYR A 108      -4.377  14.393 -60.754  1.00 99.93           N  
ANISOU 3578  N   TYR A 108    14248  11631  12091    118     18     -1       N  
ATOM   3579  CA  TYR A 108      -5.004  13.990 -62.001  1.00 96.40           C  
ANISOU 3579  CA  TYR A 108    13882  11109  11638    125      5    -18       C  
ATOM   3580  C   TYR A 108      -5.306  15.220 -62.826  1.00105.48           C  
ANISOU 3580  C   TYR A 108    15118  12201  12758    105    -55    -53       C  
ATOM   3581  O   TYR A 108      -5.751  16.239 -62.289  1.00112.29           O  
ANISOU 3581  O   TYR A 108    15971  13074  13619    101   -111    -82       O  
ATOM   3582  CB  TYR A 108      -6.295  13.218 -61.764  1.00107.68           C  
ANISOU 3582  CB  TYR A 108    15287  12528  13100    157    -20    -43       C  
ATOM   3583  CG  TYR A 108      -6.052  11.782 -61.446  1.00113.17           C  
ANISOU 3583  CG  TYR A 108    15925  13255  13821    177     44     -8       C  
ATOM   3584  CD1 TYR A 108      -4.756  11.315 -61.277  1.00112.88           C  
ANISOU 3584  CD1 TYR A 108    15855  13257  13778    166    116     40       C  
ATOM   3585  CD2 TYR A 108      -7.107  10.889 -61.304  1.00118.97           C  
ANISOU 3585  CD2 TYR A 108    16638  13980  14587    207     34    -23       C  
ATOM   3586  CE1 TYR A 108      -4.509   9.993 -60.991  1.00110.74           C  
ANISOU 3586  CE1 TYR A 108    15531  13014  13530    184    176     73       C  
ATOM   3587  CE2 TYR A 108      -6.875   9.562 -60.993  1.00121.93           C  
ANISOU 3587  CE2 TYR A 108    16957  14383  14986    225     93     10       C  
ATOM   3588  CZ  TYR A 108      -5.567   9.116 -60.856  1.00112.71           C  
ANISOU 3588  CZ  TYR A 108    15760  13254  13811    214    165     58       C  
ATOM   3589  OH  TYR A 108      -5.307   7.793 -60.578  1.00115.61           O  
ANISOU 3589  OH  TYR A 108    16075  13649  14202    231    225     91       O  
ATOM   3590  N   CYS A 109      -4.919  15.154 -64.094  1.00105.53           N  
ANISOU 3590  N   CYS A 109    15206  12150  12739     92    -39    -45       N  
ATOM   3591  CA  CYS A 109      -5.110  16.215 -65.039  1.00 99.31           C  
ANISOU 3591  CA  CYS A 109    14510  11303  11922     73    -88    -73       C  
ATOM   3592  C   CYS A 109      -6.559  16.251 -65.336  1.00101.74           C  
ANISOU 3592  C   CYS A 109    14851  11563  12241     93   -152   -120       C  
ATOM   3593  O   CYS A 109      -7.140  15.225 -65.562  1.00107.33           O  
ANISOU 3593  O   CYS A 109    15556  12255  12969    116   -139   -122       O  
ATOM   3594  CB  CYS A 109      -4.370  15.867 -66.305  1.00 97.54           C  
ANISOU 3594  CB  CYS A 109    14358  11032  11672     59    -45    -50       C  
ATOM   3595  SG  CYS A 109      -2.606  16.051 -66.160  1.00 83.32           S  
ANISOU 3595  SG  CYS A 109    12535   9274   9850     30     25      2       S  
ATOM   3596  N   LYS A 110      -7.171  17.423 -65.385  1.00 96.35           N  
ANISOU 3596  N   LYS A 110    14205  10857  11547     84   -222   -159       N  
ATOM   3597  CA  LYS A 110      -8.587  17.509 -65.720  1.00106.32           C  
ANISOU 3597  CA  LYS A 110    15504  12071  12820    103   -287   -206       C  
ATOM   3598  C   LYS A 110      -8.800  17.647 -67.225  1.00121.18           C  
ANISOU 3598  C   LYS A 110    17496  13871  14677     96   -304   -222       C  
ATOM   3599  O   LYS A 110      -9.473  18.553 -67.679  1.00110.82           O  
ANISOU 3599  O   LYS A 110    16242  12514  13351     90   -368   -260       O  
ATOM   3600  CB  LYS A 110      -9.192  18.733 -65.064  1.00117.87           C  
ANISOU 3600  CB  LYS A 110    16956  13546  14283     98   -357   -243       C  
ATOM   3601  CG  LYS A 110      -8.885  18.934 -63.593  1.00111.09           C  
ANISOU 3601  CG  LYS A 110    15998  12768  13442    100   -348   -231       C  
ATOM   3602  CD  LYS A 110      -9.930  19.876 -63.004  1.00112.27           C  
ANISOU 3602  CD  LYS A 110    16138  12919  13600    106   -427   -278       C  
ATOM   3603  CE  LYS A 110      -9.674  20.247 -61.554  1.00107.43           C  
ANISOU 3603  CE  LYS A 110    15432  12385  13002    107   -427   -271       C  
ATOM   3604  NZ  LYS A 110     -10.749  21.147 -61.055  1.00111.58           N  
ANISOU 3604  NZ  LYS A 110    15954  12907  13535    115   -506   -319       N  
ATOM   3605  N   TRP A 111      -8.318  16.688 -67.988  1.00120.79           N  
ANISOU 3605  N   TRP A 111    17472  13800  14623     98   -250   -194       N  
ATOM   3606  CA  TRP A 111      -8.361  16.744 -69.410  1.00111.92           C  
ANISOU 3606  CA  TRP A 111    16449  12602  13472     91   -257   -202       C  
ATOM   3607  C   TRP A 111      -9.734  16.779 -69.878  1.00103.97           C  
ANISOU 3607  C   TRP A 111    15488  11542  12476    110   -320   -249       C  
ATOM   3608  O   TRP A 111     -10.035  17.444 -70.830  1.00 98.08           O  
ANISOU 3608  O   TRP A 111    14827  10736  11705    100   -360   -273       O  
ATOM   3609  CB  TRP A 111      -7.672  15.540 -70.002  1.00 86.66           C  
ANISOU 3609  CB  TRP A 111    13257   9397  10273     96   -184   -164       C  
ATOM   3610  CG  TRP A 111      -6.291  15.809 -70.205  1.00 86.55           C  
ANISOU 3610  CG  TRP A 111    13251   9401  10233     69   -133   -125       C  
ATOM   3611  CD1 TRP A 111      -5.245  15.053 -69.831  1.00 85.64           C  
ANISOU 3611  CD1 TRP A 111    13084   9333  10124     67    -59    -78       C  
ATOM   3612  CD2 TRP A 111      -5.761  16.963 -70.815  1.00 87.40           C  
ANISOU 3612  CD2 TRP A 111    13424   9480  10304     41   -153   -129       C  
ATOM   3613  NE1 TRP A 111      -4.076  15.655 -70.183  1.00 85.89           N  
ANISOU 3613  NE1 TRP A 111    13142   9367  10124     38    -30    -52       N  
ATOM   3614  CE2 TRP A 111      -4.375  16.842 -70.796  1.00 86.97           C  
ANISOU 3614  CE2 TRP A 111    13352   9457  10235     21    -87    -83       C  
ATOM   3615  CE3 TRP A 111      -6.327  18.086 -71.391  1.00 88.53           C  
ANISOU 3615  CE3 TRP A 111    13639   9574  10426     30   -220   -167       C  
ATOM   3616  CZ2 TRP A 111      -3.547  17.803 -71.331  1.00 87.65           C  
ANISOU 3616  CZ2 TRP A 111    13489   9526  10286     -9    -86    -74       C  
ATOM   3617  CZ3 TRP A 111      -5.514  19.022 -71.913  1.00 89.18           C  
ANISOU 3617  CZ3 TRP A 111    13772   9639  10474      0   -218   -157       C  
ATOM   3618  CH2 TRP A 111      -4.138  18.883 -71.885  1.00 88.73           C  
ANISOU 3618  CH2 TRP A 111    13697   9615  10404    -19   -152   -111       C  
ATOM   3619  N   ASN A 112     -10.595  15.995 -69.289  1.00117.10           N  
ANISOU 3619  N   ASN A 112    17098  13221  14174    137   -328   -261       N  
ATOM   3620  CA  ASN A 112     -11.910  15.879 -69.875  1.00133.52           C  
ANISOU 3620  CA  ASN A 112    19225  15242  16263    157   -383   -304       C  
ATOM   3621  C   ASN A 112     -12.902  16.829 -69.339  1.00117.08           C  
ANISOU 3621  C   ASN A 112    17137  13159  14189    161   -460   -348       C  
ATOM   3622  O   ASN A 112     -14.095  16.679 -69.560  1.00130.18           O  
ANISOU 3622  O   ASN A 112    18817  14782  15865    180   -508   -385       O  
ATOM   3623  CB  ASN A 112     -12.446  14.449 -69.767  1.00120.31           C  
ANISOU 3623  CB  ASN A 112    17515  13573  14625    187   -354   -297       C  
ATOM   3624  CG  ASN A 112     -12.395  13.694 -71.088  1.00120.78           C  
ANISOU 3624  CG  ASN A 112    17648  13571  14673    192   -329   -290       C  
ATOM   3625  OD1 ASN A 112     -11.886  14.198 -72.088  1.00121.47           O  
ANISOU 3625  OD1 ASN A 112    17813  13615  14724    172   -329   -287       O  
ATOM   3626  ND2 ASN A 112     -12.929  12.475 -71.091  1.00120.46           N  
ANISOU 3626  ND2 ASN A 112    17582  13526  14662    218   -309   -288       N  
ATOM   3627  N   MET A 113     -12.526  17.391 -68.231  1.00127.21           N  
ANISOU 3627  N   MET A 113    18353  14504  15477    152   -460   -340       N  
ATOM   3628  CA  MET A 113     -13.656  17.922 -67.544  1.00126.85           C  
ANISOU 3628  CA  MET A 113    18280  14464  15451    165   -527   -382       C  
ATOM   3629  C   MET A 113     -14.381  18.917 -68.318  1.00130.73           C  
ANISOU 3629  C   MET A 113    18855  14893  15922    158   -598   -425       C  
ATOM   3630  O   MET A 113     -15.575  18.810 -68.547  1.00116.74           O  
ANISOU 3630  O   MET A 113    17107  13085  14166    177   -648   -463       O  
ATOM   3631  CB  MET A 113     -13.257  18.338 -66.150  1.00132.88           C  
ANISOU 3631  CB  MET A 113    18955  15306  16227    161   -521   -369       C  
ATOM   3632  CG  MET A 113     -12.845  17.090 -65.405  1.00131.78           C  
ANISOU 3632  CG  MET A 113    18732  15224  16116    177   -454   -331       C  
ATOM   3633  SD  MET A 113     -13.692  15.701 -66.180  1.00131.98           S  
ANISOU 3633  SD  MET A 113    18784  15200  16164    206   -441   -338       S  
ATOM   3634  CE  MET A 113     -15.392  16.232 -66.040  1.00132.96           C  
ANISOU 3634  CE  MET A 113    18922  15290  16306    225   -534   -400       C  
ATOM   3635  N   LYS A 114     -13.590  19.816 -68.814  1.00122.78           N  
ANISOU 3635  N   LYS A 114    17899  13872  14881    130   -599   -417       N  
ATOM   3636  CA  LYS A 114     -14.001  20.850 -69.685  1.00127.73           C  
ANISOU 3636  CA  LYS A 114    18614  14436  15480    116   -658   -452       C  
ATOM   3637  C   LYS A 114     -12.720  21.121 -70.421  1.00116.18           C  
ANISOU 3637  C   LYS A 114    17200  12962  13982     89   -614   -418       C  
ATOM   3638  O   LYS A 114     -11.607  21.122 -69.861  1.00112.95           O  
ANISOU 3638  O   LYS A 114    16742  12606  13568     74   -563   -379       O  
ATOM   3639  CB  LYS A 114     -14.425  22.087 -68.912  1.00132.37           C  
ANISOU 3639  CB  LYS A 114    19181  15046  16068    109   -721   -483       C  
ATOM   3640  CG  LYS A 114     -15.772  22.001 -68.206  1.00132.07           C  
ANISOU 3640  CG  LYS A 114    19102  15016  16064    135   -774   -522       C  
ATOM   3641  CD  LYS A 114     -16.897  21.668 -69.173  1.00132.65           C  
ANISOU 3641  CD  LYS A 114    19243  15016  16141    153   -815   -557       C  
ATOM   3642  CE  LYS A 114     -18.019  20.902 -68.483  1.00132.91           C  
ANISOU 3642  CE  LYS A 114    19218  15067  16216    185   -833   -577       C  
ATOM   3643  NZ  LYS A 114     -18.906  21.790 -67.686  1.00133.21           N  
ANISOU 3643  NZ  LYS A 114    19228  15120  16267    190   -902   -617       N  
ATOM   3644  N   ASP A 115     -12.858  21.478 -71.673  1.00 98.78           N  
ANISOU 3644  N   ASP A 115    15093  10688  11751     80   -636   -433       N  
ATOM   3645  CA  ASP A 115     -11.673  21.813 -72.394  1.00 99.18           C  
ANISOU 3645  CA  ASP A 115    15193  10725  11766     53   -598   -402       C  
ATOM   3646  C   ASP A 115     -12.002  23.187 -72.819  1.00100.54           C  
ANISOU 3646  C   ASP A 115    15431  10858  11913     36   -664   -436       C  
ATOM   3647  O   ASP A 115     -12.185  23.503 -73.966  1.00101.49           O  
ANISOU 3647  O   ASP A 115    15641  10913  12008     29   -687   -451       O  
ATOM   3648  CB  ASP A 115     -11.447  20.843 -73.513  1.00104.58           C  
ANISOU 3648  CB  ASP A 115    15930  11365  12440     60   -554   -384       C  
ATOM   3649  CG  ASP A 115     -10.700  19.632 -73.042  1.00103.29           C  
ANISOU 3649  CG  ASP A 115    15699  11251  12295     68   -475   -339       C  
ATOM   3650  OD1 ASP A 115      -9.979  19.788 -72.051  1.00102.45           O  
ANISOU 3650  OD1 ASP A 115    15521  11210  12197     58   -446   -314       O  
ATOM   3651  OD2 ASP A 115     -10.826  18.545 -73.637  1.00103.14           O  
ANISOU 3651  OD2 ASP A 115    15696  11207  12283     84   -443   -329       O  
ATOM   3652  N   SER A 116     -12.093  23.984 -71.773  1.00106.53           N  
ANISOU 3652  N   SER A 116    16134  11660  12681     30   -695   -448       N  
ATOM   3653  CA  SER A 116     -12.376  25.351 -71.778  1.00102.73           C  
ANISOU 3653  CA  SER A 116    15688  11161  12183     13   -759   -479       C  
ATOM   3654  C   SER A 116     -11.329  25.700 -70.776  1.00105.32           C  
ANISOU 3654  C   SER A 116    15944  11559  12511     -4   -723   -448       C  
ATOM   3655  O   SER A 116     -11.630  26.195 -69.718  1.00 88.03           O  
ANISOU 3655  O   SER A 116    13695   9414  10339     -1   -754   -463       O  
ATOM   3656  CB  SER A 116     -13.736  25.547 -71.159  1.00100.47           C  
ANISOU 3656  CB  SER A 116    15375  10876  11923     35   -826   -525       C  
ATOM   3657  OG  SER A 116     -13.705  25.080 -69.833  1.00101.35           O  
ANISOU 3657  OG  SER A 116    15382  11061  12066     48   -804   -512       O  
ATOM   3658  N   GLY A 117     -10.099  25.332 -71.065  1.00101.25           N  
ANISOU 3658  N   GLY A 117    15430  11058  11981    -20   -655   -402       N  
ATOM   3659  CA  GLY A 117      -9.027  25.715 -70.169  1.00 90.60           C  
ANISOU 3659  CA  GLY A 117    14017   9775  10631    -38   -621   -371       C  
ATOM   3660  C   GLY A 117      -8.079  26.679 -70.854  1.00 93.83           C  
ANISOU 3660  C   GLY A 117    14488  10160  11003    -72   -615   -357       C  
ATOM   3661  O   GLY A 117      -8.508  27.534 -71.638  1.00103.58           O  
ANISOU 3661  O   GLY A 117    15802  11338  12217    -81   -667   -387       O  
ATOM   3662  N   SER A 118      -6.785  26.557 -70.590  1.00 89.27           N  
ANISOU 3662  N   SER A 118    13876   9624  10419    -89   -553   -313       N  
ATOM   3663  CA  SER A 118      -5.803  27.404 -71.256  1.00 93.47           C  
ANISOU 3663  CA  SER A 118    14464  10134  10915   -121   -541   -296       C  
ATOM   3664  C   SER A 118      -5.543  26.867 -72.652  1.00 92.88           C  
ANISOU 3664  C   SER A 118    14473  10000  10818   -124   -509   -281       C  
ATOM   3665  O   SER A 118      -5.084  25.732 -72.802  1.00 87.07           O  
ANISOU 3665  O   SER A 118    13716   9276  10089   -115   -446   -249       O  
ATOM   3666  CB  SER A 118      -4.514  27.445 -70.452  1.00 96.92           C  
ANISOU 3666  CB  SER A 118    14832  10638  11355   -139   -485   -253       C  
ATOM   3667  OG  SER A 118      -4.810  27.712 -69.093  1.00 98.27           O  
ANISOU 3667  OG  SER A 118    14918  10870  11552   -131   -508   -265       O  
ATOM   3668  N   TRP A 119      -5.836  27.671 -73.668  1.00 91.54           N  
ANISOU 3668  N   TRP A 119    14396   9765  10621   -136   -552   -304       N  
ATOM   3669  CA  TRP A 119      -5.652  27.258 -75.050  1.00 90.32           C  
ANISOU 3669  CA  TRP A 119    14328   9548  10441   -139   -529   -294       C  
ATOM   3670  C   TRP A 119      -4.624  28.164 -75.735  1.00 88.73           C  
ANISOU 3670  C   TRP A 119    14184   9325  10203   -172   -515   -275       C  
ATOM   3671  O   TRP A 119      -3.900  28.935 -75.090  1.00 87.39           O  
ANISOU 3671  O   TRP A 119    13980   9195  10031   -194   -511   -261       O  
ATOM   3672  CB  TRP A 119      -6.980  27.280 -75.805  1.00 94.91           C  
ANISOU 3672  CB  TRP A 119    14976  10063  11020   -120   -591   -340       C  
ATOM   3673  CG  TRP A 119      -7.854  26.057 -75.638  1.00 86.16           C  
ANISOU 3673  CG  TRP A 119    13837   8957   9942    -86   -586   -351       C  
ATOM   3674  CD1 TRP A 119      -9.007  25.979 -74.916  1.00 87.83           C  
ANISOU 3674  CD1 TRP A 119    14007   9181  10183    -64   -635   -386       C  
ATOM   3675  CD2 TRP A 119      -7.638  24.743 -76.188  1.00 85.67           C  
ANISOU 3675  CD2 TRP A 119    13782   8884   9884    -71   -528   -326       C  
ATOM   3676  NE1 TRP A 119      -9.536  24.712 -75.006  1.00 94.26           N  
ANISOU 3676  NE1 TRP A 119    14803   9991  11020    -36   -612   -385       N  
ATOM   3677  CE2 TRP A 119      -8.716  23.935 -75.777  1.00 84.11           C  
ANISOU 3677  CE2 TRP A 119    13547   8692   9720    -40   -547   -348       C  
ATOM   3678  CE3 TRP A 119      -6.647  24.179 -76.986  1.00 91.10           C  
ANISOU 3678  CE3 TRP A 119    14503   9558  10552    -81   -462   -286       C  
ATOM   3679  CZ2 TRP A 119      -8.827  22.602 -76.129  1.00 82.16           C  
ANISOU 3679  CZ2 TRP A 119    13294   8436   9486    -18   -505   -333       C  
ATOM   3680  CZ3 TRP A 119      -6.761  22.852 -77.328  1.00 87.39           C  
ANISOU 3680  CZ3 TRP A 119    14028   9081  10095    -59   -420   -272       C  
ATOM   3681  CH2 TRP A 119      -7.839  22.076 -76.890  1.00 86.42           C  
ANISOU 3681  CH2 TRP A 119    13867   8964  10006    -28   -441   -295       C  
ATOM   3682  N   GLY A 120      -4.580  28.066 -77.066  1.00 92.86           N  
ANISOU 3682  N   GLY A 120    14799   9783  10699   -176   -509   -273       N  
ATOM   3683  CA  GLY A 120      -3.693  28.866 -77.889  1.00 94.97           C  
ANISOU 3683  CA  GLY A 120    15134  10020  10929   -206   -497   -256       C  
ATOM   3684  C   GLY A 120      -4.241  29.034 -79.292  1.00 90.72           C  
ANISOU 3684  C   GLY A 120    14707   9400  10365   -204   -528   -278       C  
ATOM   3685  O   GLY A 120      -5.166  28.333 -79.711  1.00 89.17           O  
ANISOU 3685  O   GLY A 120    14534   9170  10177   -179   -545   -300       O  
ATOM   3686  N   GLN A 121      -3.580  29.874 -80.078  1.00 89.22           N  
ANISOU 3686  N   GLN A 121    14585   9176  10141   -230   -527   -268       N  
ATOM   3687  CA  GLN A 121      -4.039  30.205 -81.421  1.00 95.26           C  
ANISOU 3687  CA  GLN A 121    15458   9861  10875   -231   -559   -289       C  
ATOM   3688  C   GLN A 121      -4.132  28.960 -82.258  1.00102.16           C  
ANISOU 3688  C   GLN A 121    16365  10705  11746   -211   -518   -276       C  
ATOM   3689  O   GLN A 121      -5.186  28.679 -82.858  1.00102.67           O  
ANISOU 3689  O   GLN A 121    16479  10721  11812   -190   -558   -309       O  
ATOM   3690  CB  GLN A 121      -3.171  31.294 -81.992  1.00 97.90           C  
ANISOU 3690  CB  GLN A 121    15849  10174  11176   -265   -557   -274       C  
ATOM   3691  CG  GLN A 121      -3.168  32.453 -81.026  1.00 99.52           C  
ANISOU 3691  CG  GLN A 121    16010  10414  11390   -281   -600   -289       C  
ATOM   3692  CD  GLN A 121      -4.463  32.528 -80.247  1.00 98.02           C  
ANISOU 3692  CD  GLN A 121    15781  10234  11228   -259   -665   -334       C  
ATOM   3693  OE1 GLN A 121      -5.543  32.356 -80.797  1.00 97.17           O  
ANISOU 3693  OE1 GLN A 121    15721  10079  11120   -239   -710   -368       O  
ATOM   3694  NE2 GLN A 121      -4.358  32.782 -78.966  1.00 87.48           N  
ANISOU 3694  NE2 GLN A 121    14358   8962   9918   -261   -671   -333       N  
ATOM   3695  N   GLY A 122      -3.114  28.133 -82.104  1.00 98.77           N  
ANISOU 3695  N   GLY A 122    15894  10313  11320   -215   -440   -231       N  
ATOM   3696  CA  GLY A 122      -2.960  26.907 -82.850  1.00 90.48           C  
ANISOU 3696  CA  GLY A 122    14868   9242  10267   -199   -388   -210       C  
ATOM   3697  C   GLY A 122      -1.862  27.396 -83.857  1.00 92.70           C  
ANISOU 3697  C   GLY A 122    15222   9493  10508   -226   -352   -180       C  
ATOM   3698  O   GLY A 122      -1.436  28.565 -84.088  1.00103.52           O  
ANISOU 3698  O   GLY A 122    16630  10849  11854   -253   -373   -180       O  
ATOM   3699  N   THR A 123      -1.255  26.406 -84.414  1.00 97.78           N  
ANISOU 3699  N   THR A 123    15875  10132  11144   -221   -288   -148       N  
ATOM   3700  CA  THR A 123      -0.323  26.616 -85.464  1.00 99.43           C  
ANISOU 3700  CA  THR A 123    16155  10308  11317   -241   -249   -120       C  
ATOM   3701  C   THR A 123      -0.904  25.549 -86.425  1.00101.68           C  
ANISOU 3701  C   THR A 123    16491  10545  11596   -214   -239   -128       C  
ATOM   3702  O   THR A 123      -1.551  24.436 -86.073  1.00 98.71           O  
ANISOU 3702  O   THR A 123    16072  10183  11250   -185   -232   -136       O  
ATOM   3703  CB  THR A 123       1.077  26.179 -85.122  1.00 89.04           C  
ANISOU 3703  CB  THR A 123    14787   9043  10001   -256   -167    -66       C  
ATOM   3704  OG1 THR A 123       1.911  26.345 -86.263  1.00 89.98           O  
ANISOU 3704  OG1 THR A 123    14982   9123  10082   -274   -130    -40       O  
ATOM   3705  CG2 THR A 123       1.045  24.750 -84.818  1.00 96.20           C  
ANISOU 3705  CG2 THR A 123    15639   9978  10933   -232   -118    -50       C  
ATOM   3706  N   GLN A 124      -0.647  25.880 -87.669  1.00 94.48           N  
ANISOU 3706  N   GLN A 124    15675   9575  10648   -224   -237   -124       N  
ATOM   3707  CA  GLN A 124      -1.101  25.088 -88.756  1.00 95.12           C  
ANISOU 3707  CA  GLN A 124    15822   9602  10716   -203   -231   -132       C  
ATOM   3708  C   GLN A 124       0.080  24.484 -89.481  1.00 95.23           C  
ANISOU 3708  C   GLN A 124    15862   9614  10708   -213   -151    -85       C  
ATOM   3709  O   GLN A 124       1.126  25.158 -89.659  1.00 90.22           O  
ANISOU 3709  O   GLN A 124    15243   8987  10050   -241   -122    -57       O  
ATOM   3710  CB  GLN A 124      -1.974  25.941 -89.636  1.00 92.62           C  
ANISOU 3710  CB  GLN A 124    15600   9216  10375   -203   -302   -174       C  
ATOM   3711  CG  GLN A 124      -2.279  25.328 -90.953  1.00 91.98           C  
ANISOU 3711  CG  GLN A 124    15605   9072  10272   -187   -296   -179       C  
ATOM   3712  CD  GLN A 124      -1.324  25.827 -91.962  1.00 94.53           C  
ANISOU 3712  CD  GLN A 124    16002   9362  10551   -210   -264   -153       C  
ATOM   3713  OE1 GLN A 124      -0.155  26.012 -91.683  1.00 92.17           O  
ANISOU 3713  OE1 GLN A 124    15674   9101  10247   -233   -213   -113       O  
ATOM   3714  NE2 GLN A 124      -1.820  26.078 -93.144  1.00107.37           N  
ANISOU 3714  NE2 GLN A 124    17727  10919  12148   -204   -297   -174       N  
ATOM   3715  N   VAL A 125      -0.146  23.197 -89.810  1.00 92.91           N  
ANISOU 3715  N   VAL A 125    15564   9312  10424   -187   -118    -80       N  
ATOM   3716  CA  VAL A 125       0.712  22.230 -90.478  1.00 88.19           C  
ANISOU 3716  CA  VAL A 125    14983   8711   9814   -184    -42    -40       C  
ATOM   3717  C   VAL A 125       0.057  21.801 -91.781  1.00 93.61           C  
ANISOU 3717  C   VAL A 125    15763   9326  10479   -165    -59    -61       C  
ATOM   3718  O   VAL A 125      -1.147  21.523 -91.817  1.00 93.42           O  
ANISOU 3718  O   VAL A 125    15749   9275  10471   -140   -110   -100       O  
ATOM   3719  CB  VAL A 125       0.982  21.009 -89.577  1.00 93.91           C  
ANISOU 3719  CB  VAL A 125    15610   9496  10575   -169     12    -16       C  
ATOM   3720  CG1 VAL A 125       1.910  20.052 -90.266  1.00100.10           C  
ANISOU 3720  CG1 VAL A 125    16412  10277  11345   -167     90     25       C  
ATOM   3721  CG2 VAL A 125       1.592  21.440 -88.273  1.00 94.87           C  
ANISOU 3721  CG2 VAL A 125    15639   9689  10717   -187     26      3       C  
ATOM   3722  N   THR A 126       0.872  21.720 -92.839  1.00 96.93           N  
ANISOU 3722  N   THR A 126    16250   9715  10865   -175    -15    -34       N  
ATOM   3723  CA  THR A 126       0.446  21.418 -94.209  1.00 98.45           C  
ANISOU 3723  CA  THR A 126    16541   9836  11029   -161    -26    -48       C  
ATOM   3724  C   THR A 126       1.277  20.262 -94.749  1.00 96.36           C  
ANISOU 3724  C   THR A 126    16280   9577  10757   -153     55     -9       C  
ATOM   3725  O   THR A 126       2.506  20.362 -94.805  1.00 94.27           O  
ANISOU 3725  O   THR A 126    16007   9336  10476   -175    114     34       O  
ATOM   3726  CB  THR A 126       0.636  22.632 -95.130  1.00 92.65           C  
ANISOU 3726  CB  THR A 126    15901   9051  10251   -183    -56    -55       C  
ATOM   3727  OG1 THR A 126      -0.434  23.569 -94.971  1.00 89.53           O  
ANISOU 3727  OG1 THR A 126    15528   8629   9858   -181   -141   -102       O  
ATOM   3728  CG2 THR A 126       0.670  22.188 -96.549  1.00100.05           C  
ANISOU 3728  CG2 THR A 126    16933   9927  11155   -172    -38    -52       C  
ATOM   3729  N   VAL A 127       0.627  19.185 -95.177  1.00 92.34           N  
ANISOU 3729  N   VAL A 127    15785   9043  10258   -123     57    -22       N  
ATOM   3730  CA  VAL A 127       1.344  18.020 -95.688  1.00 97.89           C  
ANISOU 3730  CA  VAL A 127    16490   9749  10956   -113    132     13       C  
ATOM   3731  C   VAL A 127       0.867  17.779 -97.111  1.00106.07           C  
ANISOU 3731  C   VAL A 127    17631  10710  11962    -97    116     -5       C  
ATOM   3732  O   VAL A 127      -0.303  17.434 -97.325  1.00103.95           O  
ANISOU 3732  O   VAL A 127    17383  10407  11706    -71     67    -44       O  
ATOM   3733  CB  VAL A 127       1.142  16.770 -94.816  1.00100.55           C  
ANISOU 3733  CB  VAL A 127    16734  10133  11337    -91    162     21       C  
ATOM   3734  CG1 VAL A 127       2.001  15.619 -95.336  1.00100.11           C  
ANISOU 3734  CG1 VAL A 127    16680  10083  11274    -83    243     61       C  
ATOM   3735  CG2 VAL A 127       1.455  17.060 -93.339  1.00 92.91           C  
ANISOU 3735  CG2 VAL A 127    15661   9238  10401   -104    168     33       C  
ATOM   3736  N   SER A 128       1.779  17.948 -98.082  1.00101.89           N  
ANISOU 3736  N   SER A 128    17166  10154  11392   -112    157     23       N  
ATOM   3737  CA  SER A 128       1.514  17.817 -99.508  1.00108.18           C  
ANISOU 3737  CA  SER A 128    18070  10881  12154   -100    148     11       C  
ATOM   3738  C   SER A 128       1.981  16.460-100.032  1.00114.53           C  
ANISOU 3738  C   SER A 128    18875  11684  12957    -82    216     38       C  
ATOM   3739  O   SER A 128       2.555  15.648 -99.309  1.00110.14           O  
ANISOU 3739  O   SER A 128    18239  11182  12428    -80    271     68       O  
ATOM   3740  CB  SER A 128       2.200  18.937-100.288  1.00120.63           C  
ANISOU 3740  CB  SER A 128    19723  12427  13684   -128    148     24       C  
ATOM   3741  OG  SER A 128       2.219  18.626-101.681  1.00113.94           O  
ANISOU 3741  OG  SER A 128    18972  11519  12800   -117    160     24       O  
ATOM   3742  N   SER A 129       1.762  16.234-101.325  1.00111.06           N  
ANISOU 3742  N   SER A 129    18529  11182  12486    -69    212     28       N  
ATOM   3743  CA  SER A 129       2.102  14.969-101.971  1.00114.93           C  
ANISOU 3743  CA  SER A 129    19034  11662  12973    -49    269     49       C  
ATOM   3744  C   SER A 129       3.421  15.015-102.738  1.00109.60           C  
ANISOU 3744  C   SER A 129    18401  10982  12259    -68    337     94       C  
ATOM   3745  O   SER A 129       4.193  14.055-102.718  1.00103.91           O  
ANISOU 3745  O   SER A 129    17647  10289  11545    -64    407    129       O  
ATOM   3746  CB  SER A 129       0.973  14.566-102.908  1.00123.95           C  
ANISOU 3746  CB  SER A 129    20249  12738  14107    -19    223      9       C  
ATOM   3747  OG  SER A 129      -0.251  14.543-102.193  1.00104.34           O  
ANISOU 3747  OG  SER A 129    17726  10258  11660     -2    160    -33       O  
TER    3748      SER A 129                                                      
HETATM 3749 ZN    ZN B1101      14.452  10.306   8.629  1.00 90.84          ZN  
ANISOU 3749 ZN    ZN B1101     8611  14705  11197   1156    786    793      ZN  
CONECT   15 2409                                                                
CONECT  690 1295                                                                
CONECT 1295  690                                                                
CONECT 1719 3749                                                                
CONECT 1739 3749                                                                
CONECT 1973 3749                                                                
CONECT 1994 3749                                                                
CONECT 2409   15                                                                
CONECT 2932 3501                                                                
CONECT 3501 2932                                                                
CONECT 3749 1719 1739 1973 1994                                                 
MASTER      386    0    1   17   20    0    1    6 3747    2   11   42          
END