HEADER    MEMBRANE PROTEIN                        11-SEP-18   6HLL              
TITLE     CRYSTAL STRUCTURE OF THE NEUROKININ 1 RECEPTOR IN COMPLEX WITH THE    
TITLE    2 SMALL MOLECULE ANTAGONIST CP-99,994                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUBSTANCE-P RECEPTOR,GLGA GLYCOGEN SYNTHASE,SUBSTANCE-P    
COMPND   3 RECEPTOR;                                                            
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: SPR,NK-1 RECEPTOR,NK-1R,TACHYKININ RECEPTOR 1,GLYCOGEN      
COMPND   6 SYNTHASE,SPR,NK-1 RECEPTOR,NK-1R,TACHYKININ RECEPTOR 1;              
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI GE5;            
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 272844;                                        
SOURCE   5 GENE: TACR1, NK1R, TAC1R, PAB2292;                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    7-TM; GPCR; SIGNALLING PROTEIN, MEMBRANE PROTEIN                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SCHOPPE,J.EHRENMANN,C.KLENK,P.RUCKTOOA,M.SCHUTZ,A.S.DORE,           
AUTHOR   2 A.PLUCKTHUN                                                          
REVDAT   2   03-APR-19 6HLL    1       SOURCE                                   
REVDAT   1   16-JAN-19 6HLL    0                                                
JRNL        AUTH   J.SCHOPPE,J.EHRENMANN,C.KLENK,P.RUCKTOOA,M.SCHUTZ,A.S.DORE,  
JRNL        AUTH 2 A.PLUCKTHUN                                                  
JRNL        TITL   CRYSTAL STRUCTURES OF THE HUMAN NEUROKININ 1 RECEPTOR IN     
JRNL        TITL 2 COMPLEX WITH CLINICALLY USED ANTAGONISTS.                    
JRNL        REF    NAT COMMUN                    V.  10    17 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30604743                                                     
JRNL        DOI    10.1038/S41467-018-07939-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.92                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 17325                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 874                             
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 24.9165 -  5.9201    1.00     2886   147  0.1909 0.2556        
REMARK   3     2  5.9201 -  4.7094    1.00     2744   158  0.1958 0.2438        
REMARK   3     3  4.7094 -  4.1171    1.00     2722   143  0.2108 0.2654        
REMARK   3     4  4.1171 -  3.7420    1.00     2730   142  0.2508 0.2852        
REMARK   3     5  3.7420 -  3.4746    1.00     2694   142  0.2875 0.3151        
REMARK   3     6  3.4746 -  3.2702    1.00     2675   142  0.3339 0.3754        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.500            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.630           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.004           3877                                  
REMARK   3   ANGLE     :  0.911           5254                                  
REMARK   3   CHIRALITY :  0.057            597                                  
REMARK   3   PLANARITY :  0.006            640                                  
REMARK   3   DIHEDRAL  : 12.421           2266                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 27 THROUGH 1232 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.0675  17.5616 -41.2069              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5760 T22:   0.6306                                     
REMARK   3      T33:   0.3361 T12:   0.1002                                     
REMARK   3      T13:  -0.1063 T23:  -0.0725                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7224 L22:   0.4662                                     
REMARK   3      L33:   0.8941 L12:   0.5216                                     
REMARK   3      L13:   0.6342 L23:   0.7243                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0580 S12:   0.1178 S13:   0.0655                       
REMARK   3      S21:  -0.0949 S22:  -0.0215 S23:   0.0777                       
REMARK   3      S31:  -0.0036 S32:   0.0499 S33:   0.0014                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1233 THROUGH 1413 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.8622  41.0303   3.7033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2879 T22:   0.2489                                     
REMARK   3      T33:   0.4677 T12:   0.0606                                     
REMARK   3      T13:  -0.0076 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4320 L22:   0.8037                                     
REMARK   3      L33:   0.9895 L12:  -0.3758                                     
REMARK   3      L13:  -0.3402 L23:  -0.0713                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1030 S12:  -0.1831 S13:  -0.0743                       
REMARK   3      S21:  -0.0244 S22:  -0.0013 S23:   0.1479                       
REMARK   3      S31:  -0.1653 S32:   0.0642 S33:   0.0000                       
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 6HLL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200011861.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-FEB-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00003                            
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17430                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.880                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 32.20                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 29.60                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
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: 4ZJC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NEEDLE-LIKE                                                  
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 76.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.0, 31% (V/V) PEG400,     
REMARK 280  190-210 MM POTASSIUM ACETATE, 2.4% (V/V) 2,5-HEXANEDIOL AND 50      
REMARK 280  UM CP-99,994, LIPIDIC CUBIC PHASE, TEMPERATURE 293K                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      143.24700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      143.24700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       30.99800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       61.36650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       30.99800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       61.36650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      143.24700            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       30.99800            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       61.36650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      143.24700            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       30.99800            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       61.36650            
REMARK 290   SMTRY3   8  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 22720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     ASN A    14                                                      
REMARK 465     ILE A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     ASN A    18                                                      
REMARK 465     THR A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     PRO A    22                                                      
REMARK 465     ASN A    23                                                      
REMARK 465     GLN A    24                                                      
REMARK 465     PHE A    25                                                      
REMARK 465     VAL A    26                                                      
REMARK 465     ILE A   273                                                      
REMARK 465     ASN A   274                                                      
REMARK 465     PRO A   275                                                      
REMARK 465     ASP A   276                                                      
REMARK 465     LEU A   277                                                      
REMARK 465     TYR A   278                                                      
REMARK 465     LEU A   279                                                      
REMARK 465     LYS A   280                                                      
REMARK 465     LYS A   281                                                      
REMARK 465     PHE A   282                                                      
REMARK 465     ARG A   321                                                      
REMARK 465     CYS A   322                                                      
REMARK 465     CYS A   323                                                      
REMARK 465     PRO A   324                                                      
REMARK 465     PHE A   325                                                      
REMARK 465     ILE A   326                                                      
REMARK 465     SER A   327                                                      
REMARK 465     ALA A   328                                                      
REMARK 465     GLY A   329                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     TYR A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     GLY A   333                                                      
REMARK 465     LEU A   334                                                      
REMARK 465     GLU A   335                                                      
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   O    LEU A   144     OG1  THR A   147              2.11            
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    ASN A  85      -33.05   -135.25                                   
REMARK 500    GLU A 186       45.22    -82.21                                   
REMARK 500    TYR A 205      -70.53   -139.68                                   
REMARK 500    GLN A1262      -81.78   -131.05                                   
REMARK 500    PRO A1335       42.90    -90.90                                   
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    PRO A1294         10.63                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GBK A 1501                
DBREF  6HLL A    1  1219  UNP    P25103   NK1R_HUMAN       1    228             
DBREF  6HLL A 1220  1413  UNP    Q9V2J8   Q9V2J8_PYRAB   220    413             
DBREF  6HLL A  238   335  UNP    P25103   NK1R_HUMAN     238    335             
SEQADV 6HLL ALA A   74  UNP  P25103    LEU    74 ENGINEERED MUTATION            
SEQADV 6HLL ILE A  116  UNP  P25103    VAL   116 ENGINEERED MUTATION            
SEQADV 6HLL LEU A  144  UNP  P25103    ALA   144 ENGINEERED MUTATION            
SEQADV 6HLL LYS A  181  UNP  P25103    MET   181 ENGINEERED MUTATION            
SEQADV 6HLL LEU A  215  UNP  P25103    ALA   215 ENGINEERED MUTATION            
SEQADV 6HLL ARG A  224  UNP  P25103    TRP   224 ENGINEERED MUTATION            
SEQADV 6HLL GLY A 1218  UNP  P25103    GLU   227 CONFLICT                       
SEQADV 6HLL ALA A  243  UNP  P25103    LYS   243 ENGINEERED MUTATION            
SEQRES   1 A  520  MET ASP ASN VAL LEU PRO VAL ASP SER ASP LEU SER PRO          
SEQRES   2 A  520  ASN ILE SER THR ASN THR SER GLU PRO ASN GLN PHE VAL          
SEQRES   3 A  520  GLN PRO ALA TRP GLN ILE VAL LEU TRP ALA ALA ALA TYR          
SEQRES   4 A  520  THR VAL ILE VAL VAL THR SER VAL VAL GLY ASN VAL VAL          
SEQRES   5 A  520  VAL MET TRP ILE ILE LEU ALA HIS LYS ARG MET ARG THR          
SEQRES   6 A  520  VAL THR ASN TYR PHE LEU VAL ASN ALA ALA PHE ALA GLU          
SEQRES   7 A  520  ALA SER MET ALA ALA PHE ASN THR VAL VAL ASN PHE THR          
SEQRES   8 A  520  TYR ALA VAL HIS ASN GLU TRP TYR TYR GLY LEU PHE TYR          
SEQRES   9 A  520  CYS LYS PHE HIS ASN PHE PHE PRO ILE ALA ALA ILE PHE          
SEQRES  10 A  520  ALA SER ILE TYR SER MET THR ALA VAL ALA PHE ASP ARG          
SEQRES  11 A  520  TYR MET ALA ILE ILE HIS PRO LEU GLN PRO ARG LEU SER          
SEQRES  12 A  520  LEU THR ALA THR LYS VAL VAL ILE CYS VAL ILE TRP VAL          
SEQRES  13 A  520  LEU ALA LEU LEU LEU ALA PHE PRO GLN GLY TYR TYR SER          
SEQRES  14 A  520  THR THR GLU THR MET PRO SER ARG VAL VAL CYS LYS ILE          
SEQRES  15 A  520  GLU TRP PRO GLU HIS PRO ASN LYS ILE TYR GLU LYS VAL          
SEQRES  16 A  520  TYR HIS ILE CYS VAL THR VAL LEU ILE TYR PHE LEU PRO          
SEQRES  17 A  520  LEU LEU VAL ILE GLY TYR LEU TYR THR VAL VAL GLY ILE          
SEQRES  18 A  520  THR LEU ARG ALA SER GLY ILE ASP CYS SER PHE TRP ASN          
SEQRES  19 A  520  GLU SER TYR LEU THR GLY SER ARG ASP GLU ARG LYS LYS          
SEQRES  20 A  520  SER LEU LEU SER LYS PHE GLY MET ASP GLU GLY VAL THR          
SEQRES  21 A  520  PHE MET PHE ILE GLY ARG PHE ASP ARG GLY GLN LYS GLY          
SEQRES  22 A  520  VAL ASP VAL LEU LEU LYS ALA ILE GLU ILE LEU SER SER          
SEQRES  23 A  520  LYS LYS GLU PHE GLN GLU MET ARG PHE ILE ILE ILE GLY          
SEQRES  24 A  520  LYS GLY ASP PRO GLU LEU GLU GLY TRP ALA ARG SER LEU          
SEQRES  25 A  520  GLU GLU LYS HIS GLY ASN VAL LYS VAL ILE THR GLU MET          
SEQRES  26 A  520  LEU SER ARG GLU PHE VAL ARG GLU LEU TYR GLY SER VAL          
SEQRES  27 A  520  ASP PHE VAL ILE ILE PRO SER TYR PHE GLU PRO PHE GLY          
SEQRES  28 A  520  LEU VAL ALA LEU GLU ALA MET CYS LEU GLY ALA ILE PRO          
SEQRES  29 A  520  ILE ALA SER ALA VAL GLY GLY LEU ARG ASP ILE ILE THR          
SEQRES  30 A  520  ASN GLU THR GLY ILE LEU VAL LYS ALA GLY ASP PRO GLY          
SEQRES  31 A  520  GLU LEU ALA ASN ALA ILE LEU LYS ALA LEU GLU LEU SER          
SEQRES  32 A  520  ARG SER ASP LEU SER LYS PHE ARG GLU ASN CYS LYS LYS          
SEQRES  33 A  520  ARG ALA MET SER PHE SER GLU GLN VAL SER ALA ALA ARG          
SEQRES  34 A  520  LYS VAL VAL LYS MET MET ILE VAL VAL VAL CYS THR PHE          
SEQRES  35 A  520  ALA ILE CYS TRP LEU PRO PHE HIS ILE PHE PHE LEU LEU          
SEQRES  36 A  520  PRO TYR ILE ASN PRO ASP LEU TYR LEU LYS LYS PHE ILE          
SEQRES  37 A  520  GLN GLN VAL TYR LEU ALA ILE MET TRP LEU ALA MET SER          
SEQRES  38 A  520  SER THR MET TYR ASN PRO ILE ILE TYR CYS CYS LEU ASN          
SEQRES  39 A  520  ASP ARG PHE ARG LEU GLY PHE LYS HIS ALA PHE ARG CYS          
SEQRES  40 A  520  CYS PRO PHE ILE SER ALA GLY ASP TYR GLU GLY LEU GLU          
HET    GBK  A1501      22                                                       
HETNAM     GBK (2~{S},3~{S})-~{N}-[(2-METHOXYPHENYL)METHYL]-2-PHENYL-           
HETNAM   2 GBK  PIPERIDIN-3-AMINE                                               
FORMUL   2  GBK    C19 H24 N2 O                                                 
HELIX    1 AA1 PRO A   28  HIS A   60  1                                  33    
HELIX    2 AA2 LYS A   61  ARG A   64  5                                   4    
HELIX    3 AA3 THR A   65  ASN A   96  1                                  32    
HELIX    4 AA4 TYR A  100  HIS A  136  1                                  37    
HELIX    5 AA5 SER A  143  TYR A  168  1                                  26    
HELIX    6 AA6 LYS A  190  TYR A  205  1                                  16    
HELIX    7 AA7 TYR A  205  SER A  226  1                                  22    
HELIX    8 AA8 ASN A 1225  LEU A 1229  5                                   5    
HELIX    9 AA9 SER A 1232  PHE A 1244  1                                  13    
HELIX   10 AB1 GLY A 1264  SER A 1277  1                                  14    
HELIX   11 AB2 LYS A 1278  GLN A 1282  5                                   5    
HELIX   12 AB3 ASP A 1293  HIS A 1307  1                                  15    
HELIX   13 AB4 SER A 1318  GLY A 1327  1                                  10    
HELIX   14 AB5 GLY A 1342  LEU A 1351  1                                  10    
HELIX   15 AB6 VAL A 1360  ILE A 1367  1                                   8    
HELIX   16 AB7 ASP A 1379  SER A 1396  1                                  18    
HELIX   17 AB8 LEU A 1398  LEU A  270  1                                  49    
HELIX   18 AB9 GLN A  284  SER A  296  1                                  13    
HELIX   19 AC1 SER A  296  ASN A  309  1                                  14    
HELIX   20 AC2 ASN A  309  PHE A  320  1                                  12    
SHEET    1 AA1 2 SER A 169  THR A 173  0                                        
SHEET    2 AA1 2 VAL A 178  ILE A 182 -1  O  LYS A 181   N  THR A 170           
SHEET    1 AA2 6 VAL A1310  ILE A1313  0                                        
SHEET    2 AA2 6 MET A1284  ILE A1289  1  N  ILE A1288   O  LYS A1311           
SHEET    3 AA2 6 VAL A1250  ILE A1255  1  N  PHE A1252   O  ARG A1285           
SHEET    4 AA2 6 PHE A1331  ILE A1334  1  O  ILE A1333   N  MET A1253           
SHEET    5 AA2 6 ILE A1354  SER A1358  1  O  ILE A1356   N  ILE A1334           
SHEET    6 AA2 6 ILE A1373  VAL A1375  1  O  ILE A1373   N  PRO A1355           
SSBOND   1 CYS A  105    CYS A  180                          1555   1555  2.03  
SITE     1 AC1  8 PRO A 112  ILE A 113  GLN A 165  ILE A 182                    
SITE     2 AC1  8 HIS A 197  VAL A 200  PHE A 264  PHE A 268                    
CRYST1   61.996  122.733  286.494  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016130  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008148  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003490        0.00000                         
ATOM      1  N   GLN A  27      24.863  16.555 -62.987  1.00157.34           N  
ANISOU    1  N   GLN A  27    19784  23791  16205   -292   -430  -2046       N  
ATOM      2  CA  GLN A  27      25.287  15.537 -63.983  1.00159.38           C  
ANISOU    2  CA  GLN A  27    19962  24137  16459   -304   -430  -2137       C  
ATOM      3  C   GLN A  27      26.603  14.910 -63.518  1.00171.76           C  
ANISOU    3  C   GLN A  27    21356  25812  18092   -273   -392  -2344       C  
ATOM      4  O   GLN A  27      26.750  13.683 -63.629  1.00170.21           O  
ANISOU    4  O   GLN A  27    21077  25641  17953   -193   -424  -2443       O  
ATOM      5  CB  GLN A  27      25.501  16.195 -65.346  1.00149.35           C  
ANISOU    5  CB  GLN A  27    18756  22946  15045   -498   -397  -2045       C  
ATOM      6  CG  GLN A  27      24.640  17.427 -65.579  1.00139.59           C  
ANISOU    6  CG  GLN A  27    17619  21715  13705   -660   -354  -1927       C  
ATOM      7  CD  GLN A  27      25.136  18.599 -64.773  1.00137.18           C  
ANISOU    7  CD  GLN A  27    17396  21464  13262   -846   -343  -1821       C  
ATOM      8  OE1 GLN A  27      25.877  18.438 -63.809  1.00138.11           O  
ANISOU    8  OE1 GLN A  27    17446  21681  13346   -901   -324  -1892       O  
ATOM      9  NE2 GLN A  27      24.728  19.791 -65.170  1.00135.87           N  
ANISOU    9  NE2 GLN A  27    17380  21227  13018   -944   -362  -1650       N  
ATOM     10  N   PRO A  28      27.542  15.675 -62.933  1.00182.60           N  
ANISOU   10  N   PRO A  28    22668  27251  19461   -334   -329  -2414       N  
ATOM     11  CA  PRO A  28      28.802  15.083 -62.530  1.00191.49           C  
ANISOU   11  CA  PRO A  28    23623  28462  20675   -271   -311  -2616       C  
ATOM     12  C   PRO A  28      28.361  13.917 -61.643  1.00204.15           C  
ANISOU   12  C   PRO A  28    25192  29947  22428    -52   -392  -2683       C  
ATOM     13  O   PRO A  28      27.504  14.117 -60.807  1.00231.37           O  
ANISOU   13  O   PRO A  28    28738  33258  25912     34   -438  -2583       O  
ATOM     14  CB  PRO A  28      29.457  16.181 -61.681  1.00187.57           C  
ANISOU   14  CB  PRO A  28    23093  28037  20137   -382   -233  -2646       C  
ATOM     15  CG  PRO A  28      28.340  17.166 -61.398  1.00184.36           C  
ANISOU   15  CG  PRO A  28    22845  27527  19677   -423   -235  -2466       C  
ATOM     16  CD  PRO A  28      27.426  17.087 -62.602  1.00182.89           C  
ANISOU   16  CD  PRO A  28    22779  27295  19415   -466   -273  -2322       C  
ATOM     17  N   ALA A  29      28.995  12.753 -61.799  1.00184.82           N  
ANISOU   17  N   ALA A  29    22601  27553  20068     34   -414  -2856       N  
ATOM     18  CA  ALA A  29      28.594  11.558 -61.021  1.00165.72           C  
ANISOU   18  CA  ALA A  29    20155  25018  17794    238   -508  -2921       C  
ATOM     19  C   ALA A  29      28.741  11.856 -59.527  1.00179.33           C  
ANISOU   19  C   ALA A  29    21911  26638  19589    325   -529  -2906       C  
ATOM     20  O   ALA A  29      27.827  11.489 -58.764  1.00173.43           O  
ANISOU   20  O   ALA A  29    21217  25749  18929    471   -612  -2873       O  
ATOM     21  CB  ALA A  29      29.427  10.374 -61.436  1.00146.86           C  
ANISOU   21  CB  ALA A  29    17597  22715  15489    304   -528  -3121       C  
ATOM     22  N   TRP A  30      29.818  12.534 -59.123  1.00193.24           N  
ANISOU   22  N   TRP A  30    23643  28467  21313    234   -457  -2926       N  
ATOM     23  CA  TRP A  30      29.929  12.875 -57.687  1.00189.21           C  
ANISOU   23  CA  TRP A  30    23164  27860  20867    313   -474  -2909       C  
ATOM     24  C   TRP A  30      28.733  13.750 -57.310  1.00183.59           C  
ANISOU   24  C   TRP A  30    22619  27018  20120    323   -497  -2720       C  
ATOM     25  O   TRP A  30      28.072  13.386 -56.324  1.00182.95           O  
ANISOU   25  O   TRP A  30    22581  26807  20125    455   -561  -2695       O  
ATOM     26  CB  TRP A  30      31.258  13.570 -57.381  1.00187.94           C  
ANISOU   26  CB  TRP A  30    22934  27805  20671    206   -387  -2971       C  
ATOM     27  CG  TRP A  30      31.621  14.652 -58.348  1.00187.51           C  
ANISOU   27  CG  TRP A  30    22943  27837  20466      0   -294  -2866       C  
ATOM     28  CD1 TRP A  30      32.218  14.496 -59.563  1.00187.84           C  
ANISOU   28  CD1 TRP A  30    22946  28015  20409   -151   -236  -2885       C  
ATOM     29  CD2 TRP A  30      31.426  16.066 -58.174  1.00184.60           C  
ANISOU   29  CD2 TRP A  30    22687  27422  20031    -81   -253  -2730       C  
ATOM     30  NE1 TRP A  30      32.402  15.712 -60.159  1.00186.73           N  
ANISOU   30  NE1 TRP A  30    22897  27908  20143   -324   -169  -2762       N  
ATOM     31  CE2 TRP A  30      31.927  16.694 -59.331  1.00184.90           C  
ANISOU   31  CE2 TRP A  30    22759  27564  19931   -282   -179  -2666       C  
ATOM     32  CE3 TRP A  30      30.880  16.860 -57.163  1.00178.26           C  
ANISOU   32  CE3 TRP A  30    21961  26497  19272     -5   -276  -2656       C  
ATOM     33  CZ2 TRP A  30      31.895  18.076 -59.499  1.00180.88           C  
ANISOU   33  CZ2 TRP A  30    22362  27034  19331   -405   -134  -2529       C  
ATOM     34  CZ3 TRP A  30      30.851  18.225 -57.327  1.00172.47           C  
ANISOU   34  CZ3 TRP A  30    21329  25754  18449   -124   -224  -2526       C  
ATOM     35  CH2 TRP A  30      31.351  18.823 -58.481  1.00173.18           C  
ANISOU   35  CH2 TRP A  30    21455  25941  18405   -321   -157  -2463       C  
ATOM     36  N   GLN A  31      28.365  14.777 -58.091  1.00181.02           N  
ANISOU   36  N   GLN A  31    22387  26721  19670    187   -454  -2585       N  
ATOM     37  CA  GLN A  31      27.190  15.446 -57.539  1.00171.20           C  
ANISOU   37  CA  GLN A  31    21293  25358  18397    203   -486  -2409       C  
ATOM     38  C   GLN A  31      26.030  14.479 -57.364  1.00157.92           C  
ANISOU   38  C   GLN A  31    19650  23565  16786    348   -581  -2379       C  
ATOM     39  O   GLN A  31      25.259  14.599 -56.405  1.00161.78           O  
ANISOU   39  O   GLN A  31    20224  23898  17346    432   -626  -2268       O  
ATOM     40  CB  GLN A  31      26.759  16.604 -58.439  1.00173.85           C  
ANISOU   40  CB  GLN A  31    21721  25747  18588     28   -436  -2274       C  
ATOM     41  CG  GLN A  31      27.714  17.783 -58.470  1.00180.76           C  
ANISOU   41  CG  GLN A  31    22597  26703  19381   -128   -349  -2260       C  
ATOM     42  CD  GLN A  31      27.091  19.005 -59.111  1.00183.04           C  
ANISOU   42  CD  GLN A  31    23015  26998  19536   -287   -327  -2093       C  
ATOM     43  OE1 GLN A  31      25.919  19.308 -58.884  1.00181.12           O  
ANISOU   43  OE1 GLN A  31    22884  26640  19293   -249   -380  -1949       O  
ATOM     44  NE2 GLN A  31      27.871  19.712 -59.922  1.00188.25           N  
ANISOU   44  NE2 GLN A  31    23658  27772  20096   -466   -254  -2102       N  
ATOM     45  N   ILE A  32      25.897  13.507 -58.266  1.00147.88           N  
ANISOU   45  N   ILE A  32    18315  22339  15534    373   -607  -2457       N  
ATOM     46  CA  ILE A  32      24.792  12.562 -58.169  1.00144.61           C  
ANISOU   46  CA  ILE A  32    17939  21820  15187    502   -698  -2430       C  
ATOM     47  C   ILE A  32      24.979  11.638 -56.973  1.00162.20           C  
ANISOU   47  C   ILE A  32    20136  23939  17553    670   -772  -2506       C  
ATOM     48  O   ILE A  32      24.012  11.300 -56.280  1.00164.93           O  
ANISOU   48  O   ILE A  32    20561  24132  17974    768   -839  -2414       O  
ATOM     49  CB  ILE A  32      24.643  11.782 -59.487  1.00127.37           C  
ANISOU   49  CB  ILE A  32    15692  19719  12985    478   -704  -2497       C  
ATOM     50  CG1 ILE A  32      24.367  12.756 -60.636  1.00115.22           C  
ANISOU   50  CG1 ILE A  32    14204  18273  11301    302   -639  -2400       C  
ATOM     51  CG2 ILE A  32      23.535  10.745 -59.379  1.00118.62           C  
ANISOU   51  CG2 ILE A  32    14618  18499  11952    613   -799  -2475       C  
ATOM     52  CD1 ILE A  32      23.262  13.751 -60.342  1.00101.98           C  
ANISOU   52  CD1 ILE A  32    12679  16509   9560    269   -654  -2208       C  
ATOM     53  N   VAL A  33      26.218  11.217 -56.700  1.00171.49           N  
ANISOU   53  N   VAL A  33    21200  25166  18791    698   -760  -2654       N  
ATOM     54  CA  VAL A  33      26.451  10.444 -55.481  1.00165.91           C  
ANISOU   54  CA  VAL A  33    20478  24346  18212    849   -839  -2715       C  
ATOM     55  C   VAL A  33      26.236  11.307 -54.242  1.00160.14           C  
ANISOU   55  C   VAL A  33    19843  23524  17479    860   -834  -2607       C  
ATOM     56  O   VAL A  33      25.731  10.822 -53.219  1.00167.42           O  
ANISOU   56  O   VAL A  33    20820  24298  18495    973   -909  -2565       O  
ATOM     57  CB  VAL A  33      27.855   9.811 -55.496  1.00166.51           C  
ANISOU   57  CB  VAL A  33    20408  24500  18359    880   -835  -2902       C  
ATOM     58  CG1 VAL A  33      28.043   8.922 -54.281  1.00167.85           C  
ANISOU   58  CG1 VAL A  33    20571  24539  18663   1040   -936  -2962       C  
ATOM     59  CG2 VAL A  33      28.060   9.007 -56.770  1.00169.54           C  
ANISOU   59  CG2 VAL A  33    20688  24986  18742    864   -835  -3013       C  
ATOM     60  N   LEU A  34      26.570  12.600 -54.321  1.00150.20           N  
ANISOU   60  N   LEU A  34    18610  22333  16125    733   -743  -2542       N  
ATOM     61  CA  LEU A  34      26.312  13.506 -53.205  1.00131.60           C  
ANISOU   61  CA  LEU A  34    16344  19857  13801    728   -724  -2402       C  
ATOM     62  C   LEU A  34      24.827  13.539 -52.870  1.00127.42           C  
ANISOU   62  C   LEU A  34    15933  19144  13338    769   -766  -2211       C  
ATOM     63  O   LEU A  34      24.419  13.270 -51.731  1.00119.09           O  
ANISOU   63  O   LEU A  34    14923  17938  12387    862   -814  -2154       O  
ATOM     64  CB  LEU A  34      26.792  14.917 -53.554  1.00118.64           C  
ANISOU   64  CB  LEU A  34    14721  18313  12044    568   -622  -2346       C  
ATOM     65  CG  LEU A  34      28.099  15.516 -53.047  1.00110.50           C  
ANISOU   65  CG  LEU A  34    13630  17377  10979    521   -563  -2441       C  
ATOM     66  CD1 LEU A  34      28.258  16.900 -53.651  1.00108.86           C  
ANISOU   66  CD1 LEU A  34    13467  17252  10641    341   -471  -2351       C  
ATOM     67  CD2 LEU A  34      28.107  15.592 -51.532  1.00109.75           C  
ANISOU   67  CD2 LEU A  34    13571  17130  10998    617   -592  -2390       C  
ATOM     68  N   TRP A  35      24.001  13.861 -53.868  1.00130.34           N  
ANISOU   68  N   TRP A  35    16351  19530  13644    696   -749  -2117       N  
ATOM     69  CA  TRP A  35      22.569  13.990 -53.634  1.00131.42           C  
ANISOU   69  CA  TRP A  35    16593  19504  13835    726   -784  -1943       C  
ATOM     70  C   TRP A  35      21.927  12.652 -53.292  1.00128.42           C  
ANISOU   70  C   TRP A  35    16212  19025  13558    861   -875  -1974       C  
ATOM     71  O   TRP A  35      20.968  12.609 -52.511  1.00136.11           O  
ANISOU   71  O   TRP A  35    17261  19843  14612    915   -912  -1859       O  
ATOM     72  CB  TRP A  35      21.902  14.627 -54.852  1.00130.37           C  
ANISOU   72  CB  TRP A  35    16509  19419  13606    616   -754  -1848       C  
ATOM     73  CG  TRP A  35      22.255  16.071 -55.014  1.00130.96           C  
ANISOU   73  CG  TRP A  35    16627  19539  13592    479   -682  -1767       C  
ATOM     74  CD1 TRP A  35      23.137  16.606 -55.903  1.00127.94           C  
ANISOU   74  CD1 TRP A  35    16204  19326  13081    348   -620  -1831       C  
ATOM     75  CD2 TRP A  35      21.744  17.168 -54.248  1.00138.08           C  
ANISOU   75  CD2 TRP A  35    17622  20315  14527    454   -668  -1611       C  
ATOM     76  NE1 TRP A  35      23.204  17.968 -55.744  1.00131.92           N  
ANISOU   76  NE1 TRP A  35    16780  19810  13534    240   -573  -1716       N  
ATOM     77  CE2 TRP A  35      22.357  18.339 -54.734  1.00135.70           C  
ANISOU   77  CE2 TRP A  35    17339  20106  14116    309   -604  -1582       C  
ATOM     78  CE3 TRP A  35      20.823  17.273 -53.199  1.00143.37           C  
ANISOU   78  CE3 TRP A  35    18359  20809  15308    535   -706  -1500       C  
ATOM     79  CZ2 TRP A  35      22.080  19.600 -54.210  1.00137.63           C  
ANISOU   79  CZ2 TRP A  35    17669  20259  14364    252   -584  -1444       C  
ATOM     80  CZ3 TRP A  35      20.550  18.527 -52.679  1.00145.94           C  
ANISOU   80  CZ3 TRP A  35    18759  21055  15638    480   -681  -1373       C  
ATOM     81  CH2 TRP A  35      21.176  19.673 -53.186  1.00140.12           C  
ANISOU   81  CH2 TRP A  35    18041  20400  14797    345   -624  -1345       C  
ATOM     82  N   ALA A  36      22.445  11.551 -53.846  1.00114.71           N  
ANISOU   82  N   ALA A  36    14387  17377  11819    912   -914  -2134       N  
ATOM     83  CA  ALA A  36      21.930  10.240 -53.469  1.00107.69           C  
ANISOU   83  CA  ALA A  36    13500  16387  11030   1040  -1011  -2172       C  
ATOM     84  C   ALA A  36      22.188   9.963 -51.996  1.00111.63           C  
ANISOU   84  C   ALA A  36    14019  16766  11631   1128  -1058  -2175       C  
ATOM     85  O   ALA A  36      21.306   9.461 -51.281  1.00119.60           O  
ANISOU   85  O   ALA A  36    15095  17625  12722   1196  -1120  -2095       O  
ATOM     86  CB  ALA A  36      22.563   9.158 -54.345  1.00106.25           C  
ANISOU   86  CB  ALA A  36    13212  16329  10829   1079  -1049  -2362       C  
ATOM     87  N   ALA A  37      23.374  10.339 -51.509  1.00101.43           N  
ANISOU   87  N   ALA A  37    12673  15539  10327   1116  -1026  -2263       N  
ATOM     88  CA  ALA A  37      23.669  10.136 -50.098  1.00 87.30           C  
ANISOU   88  CA  ALA A  37    10905  13639   8627   1192  -1070  -2264       C  
ATOM     89  C   ALA A  37      22.803  11.024 -49.215  1.00 90.37           C  
ANISOU   89  C   ALA A  37    11398  13895   9045   1161  -1040  -2074       C  
ATOM     90  O   ALA A  37      22.298  10.574 -48.179  1.00103.42           O  
ANISOU   90  O   ALA A  37    13105  15408  10782   1229  -1100  -2021       O  
ATOM     91  CB  ALA A  37      25.149  10.397 -49.827  1.00 91.48           C  
ANISOU   91  CB  ALA A  37    11347  14278   9133   1183  -1039  -2406       C  
ATOM     92  N   ALA A  38      22.605  12.285 -49.608  1.00 81.52           N  
ANISOU   92  N   ALA A  38    10307  12814   7852   1054   -952  -1973       N  
ATOM     93  CA  ALA A  38      21.782  13.174 -48.794  1.00 82.60           C  
ANISOU   93  CA  ALA A  38    10535  12828   8022   1028   -928  -1806       C  
ATOM     94  C   ALA A  38      20.332  12.700 -48.711  1.00 88.60           C  
ANISOU   94  C   ALA A  38    11366  13461   8835   1070   -981  -1699       C  
ATOM     95  O   ALA A  38      19.751  12.619 -47.616  1.00 94.90           O  
ANISOU   95  O   ALA A  38    12218  14132   9707   1111  -1012  -1628       O  
ATOM     96  CB  ALA A  38      21.859  14.590 -49.363  1.00 75.48           C  
ANISOU   96  CB  ALA A  38     9654  11993   7033    906   -839  -1727       C  
ATOM     97  N   TYR A  39      19.738  12.338 -49.853  1.00 95.01           N  
ANISOU   97  N   TYR A  39    12177  14313   9609   1056   -994  -1696       N  
ATOM     98  CA  TYR A  39      18.348  11.887 -49.824  1.00105.13           C  
ANISOU   98  CA  TYR A  39    13523  15484  10939   1092  -1042  -1603       C  
ATOM     99  C   TYR A  39      18.200  10.577 -49.060  1.00108.20           C  
ANISOU   99  C   TYR A  39    13913  15785  11413   1194  -1131  -1656       C  
ATOM    100  O   TYR A  39      17.236  10.400 -48.298  1.00113.31           O  
ANISOU  100  O   TYR A  39    14624  16308  12119   1221  -1164  -1568       O  
ATOM    101  CB  TYR A  39      17.803  11.765 -51.249  1.00106.67           C  
ANISOU  101  CB  TYR A  39    13712  15747  11072   1055  -1038  -1595       C  
ATOM    102  CG  TYR A  39      17.327  13.091 -51.809  1.00109.35           C  
ANISOU  102  CG  TYR A  39    14099  16102  11347    956   -978  -1477       C  
ATOM    103  CD1 TYR A  39      18.237  14.074 -52.182  1.00115.37           C  
ANISOU  103  CD1 TYR A  39    14840  16967  12029    865   -910  -1492       C  
ATOM    104  CD2 TYR A  39      15.972  13.366 -51.951  1.00105.28           C  
ANISOU  104  CD2 TYR A  39    13653  15497  10852    951   -995  -1354       C  
ATOM    105  CE1 TYR A  39      17.814  15.294 -52.687  1.00118.69           C  
ANISOU  105  CE1 TYR A  39    15316  17390  12390    770   -870  -1379       C  
ATOM    106  CE2 TYR A  39      15.538  14.586 -52.457  1.00105.82           C  
ANISOU  106  CE2 TYR A  39    13770  15568  10869    866   -957  -1248       C  
ATOM    107  CZ  TYR A  39      16.465  15.546 -52.823  1.00111.96           C  
ANISOU  107  CZ  TYR A  39    14536  16438  11567    775   -899  -1257       C  
ATOM    108  OH  TYR A  39      16.047  16.759 -53.327  1.00110.71           O  
ANISOU  108  OH  TYR A  39    14438  16271  11356    686   -875  -1148       O  
ATOM    109  N   THR A  40      19.178   9.675 -49.190  1.00103.54           N  
ANISOU  109  N   THR A  40    13255  15256  10830   1248  -1174  -1805       N  
ATOM    110  CA  THR A  40      19.111   8.441 -48.414  1.00102.23           C  
ANISOU  110  CA  THR A  40    13102  14993  10747   1343  -1274  -1856       C  
ATOM    111  C   THR A  40      19.234   8.718 -46.923  1.00 97.91           C  
ANISOU  111  C   THR A  40    12600  14344  10256   1358  -1284  -1804       C  
ATOM    112  O   THR A  40      18.584   8.045 -46.111  1.00100.69           O  
ANISOU  112  O   THR A  40    13011  14575  10670   1401  -1354  -1760       O  
ATOM    113  CB  THR A  40      20.194   7.467 -48.875  1.00110.30           C  
ANISOU  113  CB  THR A  40    14037  16101  11771   1403  -1330  -2040       C  
ATOM    114  OG1 THR A  40      21.418   8.178 -49.091  1.00108.45           O  
ANISOU  114  OG1 THR A  40    13729  15995  11482   1361  -1262  -2125       O  
ATOM    115  CG2 THR A  40      19.772   6.782 -50.170  1.00115.42           C  
ANISOU  115  CG2 THR A  40    14654  16811  12389   1411  -1353  -2089       C  
ATOM    116  N   VAL A  41      20.027   9.728 -46.550  1.00101.18           N  
ANISOU  116  N   VAL A  41    12992  14809  10644   1314  -1215  -1804       N  
ATOM    117  CA  VAL A  41      20.111  10.131 -45.149  1.00103.56           C  
ANISOU  117  CA  VAL A  41    13336  15021  10993   1318  -1213  -1747       C  
ATOM    118  C   VAL A  41      18.750  10.599 -44.652  1.00 98.73           C  
ANISOU  118  C   VAL A  41    12806  14301  10404   1285  -1197  -1590       C  
ATOM    119  O   VAL A  41      18.327  10.259 -43.536  1.00 85.74           O  
ANISOU  119  O   VAL A  41    11212  12549   8816   1310  -1242  -1545       O  
ATOM    120  CB  VAL A  41      21.181  11.226 -44.972  1.00101.84           C  
ANISOU  120  CB  VAL A  41    13074  14887  10735   1267  -1131  -1774       C  
ATOM    121  CG1 VAL A  41      20.987  11.965 -43.659  1.00103.18           C  
ANISOU  121  CG1 VAL A  41    13296  14966  10942   1249  -1105  -1678       C  
ATOM    122  CG2 VAL A  41      22.580  10.627 -45.043  1.00 98.44           C  
ANISOU  122  CG2 VAL A  41    12560  14542  10302   1315  -1163  -1947       C  
ATOM    123  N   ILE A  42      18.022  11.344 -45.492  1.00102.22           N  
ANISOU  123  N   ILE A  42    13263  14774  10802   1227  -1141  -1511       N  
ATOM    124  CA  ILE A  42      16.686  11.787 -45.097  1.00 99.44           C  
ANISOU  124  CA  ILE A  42    12979  14328  10477   1202  -1132  -1379       C  
ATOM    125  C   ILE A  42      15.778  10.589 -44.860  1.00 98.28           C  
ANISOU  125  C   ILE A  42    12871  14095  10378   1252  -1213  -1371       C  
ATOM    126  O   ILE A  42      15.083  10.504 -43.837  1.00105.53           O  
ANISOU  126  O   ILE A  42    13839  14915  11342   1253  -1235  -1307       O  
ATOM    127  CB  ILE A  42      16.084  12.725 -46.156  1.00 98.88           C  
ANISOU  127  CB  ILE A  42    12916  14301  10351   1138  -1075  -1307       C  
ATOM    128  CG1 ILE A  42      16.769  14.087 -46.129  1.00103.12           C  
ANISOU  128  CG1 ILE A  42    13443  14893  10847   1072   -998  -1281       C  
ATOM    129  CG2 ILE A  42      14.586  12.880 -45.929  1.00 96.48           C  
ANISOU  129  CG2 ILE A  42    12672  13903  10082   1132  -1089  -1199       C  
ATOM    130  CD1 ILE A  42      16.220  15.029 -47.164  1.00108.08           C  
ANISOU  130  CD1 ILE A  42    14092  15555  11418   1003   -958  -1207       C  
ATOM    131  N   VAL A  43      15.790   9.629 -45.789  1.00 94.59           N  
ANISOU  131  N   VAL A  43    12378  13665   9897   1288  -1261  -1440       N  
ATOM    132  CA  VAL A  43      14.848   8.515 -45.689  1.00 94.64           C  
ANISOU  132  CA  VAL A  43    12426  13591   9943   1328  -1338  -1427       C  
ATOM    133  C   VAL A  43      15.141   7.675 -44.451  1.00 97.34           C  
ANISOU  133  C   VAL A  43    12798  13844  10341   1371  -1415  -1457       C  
ATOM    134  O   VAL A  43      14.232   7.342 -43.676  1.00 97.88           O  
ANISOU  134  O   VAL A  43    12930  13816  10445   1364  -1450  -1389       O  
ATOM    135  CB  VAL A  43      14.877   7.657 -46.966  1.00 83.15           C  
ANISOU  135  CB  VAL A  43    10933  12199   8462   1360  -1376  -1504       C  
ATOM    136  CG1 VAL A  43      13.790   6.596 -46.908  1.00 73.73           C  
ANISOU  136  CG1 VAL A  43     9789  10919   7306   1391  -1451  -1478       C  
ATOM    137  CG2 VAL A  43      14.700   8.522 -48.199  1.00 78.12           C  
ANISOU  137  CG2 VAL A  43    10268  11656   7757   1305  -1302  -1476       C  
ATOM    138  N   VAL A  44      16.417   7.339 -44.229  1.00 95.08           N  
ANISOU  138  N   VAL A  44    12471  13593  10064   1412  -1445  -1562       N  
ATOM    139  CA  VAL A  44      16.741   6.454 -43.113  1.00 96.53           C  
ANISOU  139  CA  VAL A  44    12690  13686  10301   1457  -1538  -1596       C  
ATOM    140  C   VAL A  44      16.521   7.159 -41.778  1.00100.88           C  
ANISOU  140  C   VAL A  44    13291  14168  10872   1415  -1506  -1506       C  
ATOM    141  O   VAL A  44      15.954   6.575 -40.844  1.00102.91           O  
ANISOU  141  O   VAL A  44    13615  14322  11163   1413  -1569  -1462       O  
ATOM    142  CB  VAL A  44      18.174   5.901 -43.242  1.00 89.31           C  
ANISOU  142  CB  VAL A  44    11712  12825   9396   1521  -1591  -1745       C  
ATOM    143  CG1 VAL A  44      18.309   5.060 -44.504  1.00 93.23           C  
ANISOU  143  CG1 VAL A  44    12157  13386   9879   1565  -1635  -1846       C  
ATOM    144  CG2 VAL A  44      19.207   7.021 -43.221  1.00 87.47           C  
ANISOU  144  CG2 VAL A  44    11418  12688   9129   1491  -1500  -1777       C  
ATOM    145  N   THR A  45      16.949   8.423 -41.657  1.00 92.17           N  
ANISOU  145  N   THR A  45    12157  13120   9743   1372  -1410  -1478       N  
ATOM    146  CA  THR A  45      16.785   9.102 -40.377  1.00 83.70           C  
ANISOU  146  CA  THR A  45    11123  11987   8691   1334  -1380  -1403       C  
ATOM    147  C   THR A  45      15.311   9.308 -40.058  1.00 93.72           C  
ANISOU  147  C   THR A  45    12449  13188   9971   1288  -1364  -1291       C  
ATOM    148  O   THR A  45      14.886   9.138 -38.907  1.00119.13           O  
ANISOU  148  O   THR A  45    15719  16328  13218   1267  -1391  -1245       O  
ATOM    149  CB  THR A  45      17.513  10.446 -40.380  1.00 85.32           C  
ANISOU  149  CB  THR A  45    11283  12266   8868   1296  -1281  -1397       C  
ATOM    150  OG1 THR A  45      18.852  10.268 -40.851  1.00 95.59           O  
ANISOU  150  OG1 THR A  45    12518  13652  10149   1332  -1286  -1516       O  
ATOM    151  CG2 THR A  45      17.550  11.037 -38.971  1.00 85.16           C  
ANISOU  151  CG2 THR A  45    11294  12187   8876   1268  -1259  -1343       C  
ATOM    152  N   SER A  46      14.508   9.628 -41.076  1.00 87.65           N  
ANISOU  152  N   SER A  46    11672  12453   9177   1268  -1327  -1252       N  
ATOM    153  CA  SER A  46      13.093   9.878 -40.834  1.00 90.33           C  
ANISOU  153  CA  SER A  46    12055  12738   9529   1228  -1311  -1159       C  
ATOM    154  C   SER A  46      12.347   8.599 -40.484  1.00 96.08           C  
ANISOU  154  C   SER A  46    12835  13390  10281   1242  -1398  -1157       C  
ATOM    155  O   SER A  46      11.541   8.586 -39.544  1.00103.66           O  
ANISOU  155  O   SER A  46    13840  14286  11259   1202  -1405  -1101       O  
ATOM    156  CB  SER A  46      12.458  10.540 -42.051  1.00 94.69           C  
ANISOU  156  CB  SER A  46    12587  13342  10050   1208  -1260  -1123       C  
ATOM    157  OG  SER A  46      11.055  10.602 -41.882  1.00102.18           O  
ANISOU  157  OG  SER A  46    13571  14238  11016   1181  -1261  -1053       O  
ATOM    158  N   VAL A  47      12.592   7.513 -41.226  1.00 92.13           N  
ANISOU  158  N   VAL A  47    12329  12899   9777   1291  -1466  -1223       N  
ATOM    159  CA  VAL A  47      11.854   6.281 -40.961  1.00 92.07           C  
ANISOU  159  CA  VAL A  47    12378  12814   9789   1300  -1555  -1219       C  
ATOM    160  C   VAL A  47      12.302   5.654 -39.645  1.00 96.17           C  
ANISOU  160  C   VAL A  47    12949  13256  10337   1300  -1628  -1230       C  
ATOM    161  O   VAL A  47      11.471   5.210 -38.841  1.00 93.12           O  
ANISOU  161  O   VAL A  47    12627  12794   9959   1257  -1666  -1178       O  
ATOM    162  CB  VAL A  47      11.994   5.297 -42.137  1.00 85.02           C  
ANISOU  162  CB  VAL A  47    11464  11950   8890   1356  -1614  -1290       C  
ATOM    163  CG1 VAL A  47      11.343   3.968 -41.792  1.00 82.46           C  
ANISOU  163  CG1 VAL A  47    11206  11536   8589   1364  -1719  -1290       C  
ATOM    164  CG2 VAL A  47      11.358   5.873 -43.394  1.00 88.47           C  
ANISOU  164  CG2 VAL A  47    11864  12456   9294   1342  -1548  -1265       C  
ATOM    165  N   VAL A  48      13.614   5.625 -39.390  1.00 93.02           N  
ANISOU  165  N   VAL A  48    12522  12875   9947   1341  -1651  -1300       N  
ATOM    166  CA  VAL A  48      14.091   5.072 -38.126  1.00 89.88           C  
ANISOU  166  CA  VAL A  48    12178  12399   9575   1342  -1729  -1310       C  
ATOM    167  C   VAL A  48      13.546   5.887 -36.962  1.00 75.24           C  
ANISOU  167  C   VAL A  48    10357  10512   7718   1264  -1670  -1220       C  
ATOM    168  O   VAL A  48      12.944   5.342 -36.030  1.00 78.16           O  
ANISOU  168  O   VAL A  48    10800  10803   8094   1219  -1724  -1175       O  
ATOM    169  CB  VAL A  48      15.632   5.006 -38.104  1.00101.61           C  
ANISOU  169  CB  VAL A  48    13615  13919  11073   1405  -1759  -1411       C  
ATOM    170  CG1 VAL A  48      16.146   4.656 -36.707  1.00100.14           C  
ANISOU  170  CG1 VAL A  48    13485  13652  10913   1400  -1832  -1411       C  
ATOM    171  CG2 VAL A  48      16.136   3.975 -39.102  1.00 99.81           C  
ANISOU  171  CG2 VAL A  48    13355  13712  10856   1483  -1843  -1519       C  
ATOM    172  N   GLY A  49      13.700   7.212 -37.020  1.00 66.48           N  
ANISOU  172  N   GLY A  49     9197   9466   6597   1241  -1559  -1193       N  
ATOM    173  CA  GLY A  49      13.284   8.023 -35.888  1.00 67.24           C  
ANISOU  173  CA  GLY A  49     9314   9538   6696   1173  -1504  -1123       C  
ATOM    174  C   GLY A  49      11.784   8.028 -35.665  1.00 70.29           C  
ANISOU  174  C   GLY A  49     9738   9890   7078   1110  -1488  -1050       C  
ATOM    175  O   GLY A  49      11.318   7.992 -34.521  1.00 68.84           O  
ANISOU  175  O   GLY A  49     9599   9660   6897   1050  -1497  -1010       O  
ATOM    176  N   ASN A  50      11.006   8.054 -36.747  1.00 67.47           N  
ANISOU  176  N   ASN A  50     9362   9563   6711   1118  -1466  -1039       N  
ATOM    177  CA  ASN A  50       9.556   8.102 -36.594  1.00 72.29           C  
ANISOU  177  CA  ASN A  50     9997  10151   7319   1061  -1448   -982       C  
ATOM    178  C   ASN A  50       8.989   6.753 -36.176  1.00 81.79           C  
ANISOU  178  C   ASN A  50    11271  11286   8519   1038  -1542   -980       C  
ATOM    179  O   ASN A  50       8.038   6.694 -35.387  1.00 83.71           O  
ANISOU  179  O   ASN A  50    11551  11499   8756    965  -1539   -938       O  
ATOM    180  CB  ASN A  50       8.909   8.607 -37.880  1.00 71.68           C  
ANISOU  180  CB  ASN A  50     9877  10124   7232   1079  -1399   -971       C  
ATOM    181  CG  ASN A  50       8.918  10.128 -37.976  1.00 70.70           C  
ANISOU  181  CG  ASN A  50     9706  10046   7112   1062  -1304   -941       C  
ATOM    182  OD1 ASN A  50       8.430  10.821 -37.085  1.00 69.52           O  
ANISOU  182  OD1 ASN A  50     9557   9881   6975   1013  -1265   -906       O  
ATOM    183  ND2 ASN A  50       9.487  10.650 -39.057  1.00 70.88           N  
ANISOU  183  ND2 ASN A  50     9688  10126   7119   1098  -1272   -958       N  
ATOM    184  N   VAL A  51       9.555   5.660 -36.694  1.00 86.20           N  
ANISOU  184  N   VAL A  51    11849  11822   9080   1095  -1630  -1031       N  
ATOM    185  CA  VAL A  51       9.132   4.340 -36.241  1.00 85.32           C  
ANISOU  185  CA  VAL A  51    11819  11633   8967   1071  -1736  -1028       C  
ATOM    186  C   VAL A  51       9.472   4.171 -34.767  1.00 86.09           C  
ANISOU  186  C   VAL A  51    11976  11671   9064   1018  -1778  -1008       C  
ATOM    187  O   VAL A  51       8.667   3.653 -33.979  1.00 88.82           O  
ANISOU  187  O   VAL A  51    12392  11965   9393    938  -1816   -966       O  
ATOM    188  CB  VAL A  51       9.778   3.242 -37.109  1.00 80.26           C  
ANISOU  188  CB  VAL A  51    11182  10976   8337   1154  -1832  -1099       C  
ATOM    189  CG1 VAL A  51       9.744   1.898 -36.391  1.00 76.97           C  
ANISOU  189  CG1 VAL A  51    10861  10458   7926   1136  -1967  -1103       C  
ATOM    190  CG2 VAL A  51       9.080   3.145 -38.459  1.00 78.68           C  
ANISOU  190  CG2 VAL A  51    10944  10822   8129   1181  -1805  -1106       C  
ATOM    191  N   VAL A  52      10.645   4.667 -34.360  1.00 84.86           N  
ANISOU  191  N   VAL A  52    11793  11528   8920   1051  -1765  -1036       N  
ATOM    192  CA  VAL A  52      11.018   4.610 -32.950  1.00 87.13           C  
ANISOU  192  CA  VAL A  52    12135  11765   9207   1000  -1800  -1015       C  
ATOM    193  C   VAL A  52      10.050   5.432 -32.115  1.00 88.25           C  
ANISOU  193  C   VAL A  52    12278  11922   9329    899  -1715   -949       C  
ATOM    194  O   VAL A  52       9.684   5.038 -31.002  1.00 83.21           O  
ANISOU  194  O   VAL A  52    11708  11234   8672    816  -1756   -914       O  
ATOM    195  CB  VAL A  52      12.473   5.082 -32.749  1.00 85.81           C  
ANISOU  195  CB  VAL A  52    11924  11620   9058   1061  -1794  -1066       C  
ATOM    196  CG1 VAL A  52      12.770   5.268 -31.275  1.00 80.42           C  
ANISOU  196  CG1 VAL A  52    11289  10897   8372   1001  -1808  -1036       C  
ATOM    197  CG2 VAL A  52      13.451   4.086 -33.333  1.00 93.40           C  
ANISOU  197  CG2 VAL A  52    12890  12557  10041   1155  -1903  -1149       C  
ATOM    198  N   VAL A  53       9.591   6.568 -32.649  1.00 85.28           N  
ANISOU  198  N   VAL A  53    11829  11617   8958    899  -1602   -934       N  
ATOM    199  CA  VAL A  53       8.664   7.401 -31.889  1.00 78.34           C  
ANISOU  199  CA  VAL A  53    10938  10759   8070    812  -1523   -888       C  
ATOM    200  C   VAL A  53       7.328   6.685 -31.720  1.00 86.54           C  
ANISOU  200  C   VAL A  53    12025  11771   9084    736  -1554   -861       C  
ATOM    201  O   VAL A  53       6.734   6.688 -30.632  1.00 95.05           O  
ANISOU  201  O   VAL A  53    13136  12837  10141    638  -1548   -834       O  
ATOM    202  CB  VAL A  53       8.499   8.777 -32.563  1.00 64.11           C  
ANISOU  202  CB  VAL A  53     9049   9027   6284    839  -1413   -884       C  
ATOM    203  CG1 VAL A  53       7.221   9.459 -32.097  1.00 59.71           C  
ANISOU  203  CG1 VAL A  53     8472   8489   5725    762  -1348   -852       C  
ATOM    204  CG2 VAL A  53       9.708   9.654 -32.295  1.00 58.82           C  
ANISOU  204  CG2 VAL A  53     8338   8383   5629    874  -1369   -900       C  
ATOM    205  N   MET A  54       6.837   6.051 -32.788  1.00 87.19           N  
ANISOU  205  N   MET A  54    12111  11852   9166    773  -1586   -872       N  
ATOM    206  CA  MET A  54       5.578   5.321 -32.686  1.00 85.00           C  
ANISOU  206  CA  MET A  54    11879  11553   8863    700  -1617   -852       C  
ATOM    207  C   MET A  54       5.686   4.165 -31.699  1.00 82.13           C  
ANISOU  207  C   MET A  54    11619  11114   8471    633  -1721   -838       C  
ATOM    208  O   MET A  54       4.745   3.902 -30.936  1.00 81.64           O  
ANISOU  208  O   MET A  54    11601  11044   8375    521  -1724   -811       O  
ATOM    209  CB  MET A  54       5.155   4.816 -34.068  1.00 87.28           C  
ANISOU  209  CB  MET A  54    12152  11852   9157    762  -1637   -870       C  
ATOM    210  CG  MET A  54       4.759   5.929 -35.032  1.00 88.37           C  
ANISOU  210  CG  MET A  54    12203  12060   9313    805  -1542   -873       C  
ATOM    211  SD  MET A  54       4.212   5.340 -36.646  1.00 89.35           S  
ANISOU  211  SD  MET A  54    12311  12201   9437    868  -1566   -892       S  
ATOM    212  CE  MET A  54       5.756   4.765 -37.347  1.00 90.26           C  
ANISOU  212  CE  MET A  54    12425  12307   9563    971  -1629   -940       C  
ATOM    213  N   TRP A  55       6.835   3.479 -31.674  1.00 86.14           N  
ANISOU  213  N   TRP A  55    12169  11568   8992    693  -1813   -861       N  
ATOM    214  CA  TRP A  55       7.028   2.418 -30.687  1.00100.88           C  
ANISOU  214  CA  TRP A  55    14145  13349  10834    630  -1929   -845       C  
ATOM    215  C   TRP A  55       7.110   2.983 -29.272  1.00 95.73           C  
ANISOU  215  C   TRP A  55    13514  12700  10160    535  -1896   -812       C  
ATOM    216  O   TRP A  55       6.608   2.370 -28.320  1.00 81.51           O  
ANISOU  216  O   TRP A  55    11800  10855   8315    421  -1951   -777       O  
ATOM    217  CB  TRP A  55       8.286   1.612 -31.017  1.00114.46           C  
ANISOU  217  CB  TRP A  55    15896  15009  12583    731  -2045   -891       C  
ATOM    218  CG  TRP A  55       8.678   0.606 -29.952  1.00126.29           C  
ANISOU  218  CG  TRP A  55    17514  16406  14065    678  -2182   -875       C  
ATOM    219  CD1 TRP A  55       8.111  -0.617 -29.729  1.00130.52           C  
ANISOU  219  CD1 TRP A  55    18159  16861  14573    615  -2299   -851       C  
ATOM    220  CD2 TRP A  55       9.725   0.742 -28.979  1.00134.64           C  
ANISOU  220  CD2 TRP A  55    18600  17428  15129    681  -2225   -879       C  
ATOM    221  NE1 TRP A  55       8.734  -1.244 -28.676  1.00136.27           N  
ANISOU  221  NE1 TRP A  55    18987  17499  15288    575  -2418   -836       N  
ATOM    222  CE2 TRP A  55       9.729  -0.432 -28.200  1.00138.87           C  
ANISOU  222  CE2 TRP A  55    19268  17856  15640    617  -2375   -855       C  
ATOM    223  CE3 TRP A  55      10.657   1.744 -28.690  1.00134.86           C  
ANISOU  223  CE3 TRP A  55    18558  17503  15179    727  -2154   -901       C  
ATOM    224  CZ2 TRP A  55      10.627  -0.631 -27.153  1.00140.00           C  
ANISOU  224  CZ2 TRP A  55    19476  17936  15783    603  -2461   -852       C  
ATOM    225  CZ3 TRP A  55      11.545   1.544 -27.649  1.00132.02           C  
ANISOU  225  CZ3 TRP A  55    18255  17086  14819    715  -2231   -902       C  
ATOM    226  CH2 TRP A  55      11.525   0.366 -26.895  1.00135.15           C  
ANISOU  226  CH2 TRP A  55    18784  17374  15193    655  -2385   -878       C  
ATOM    227  N   ILE A  56       7.722   4.160 -29.121  1.00 91.04           N  
ANISOU  227  N   ILE A  56    12842  12159   9589    573  -1805   -823       N  
ATOM    228  CA  ILE A  56       7.880   4.761 -27.802  1.00 84.73           C  
ANISOU  228  CA  ILE A  56    12052  11368   8772    490  -1768   -799       C  
ATOM    229  C   ILE A  56       6.525   5.129 -27.224  1.00 85.80           C  
ANISOU  229  C   ILE A  56    12181  11548   8873    364  -1699   -769       C  
ATOM    230  O   ILE A  56       6.252   4.898 -26.041  1.00 99.96           O  
ANISOU  230  O   ILE A  56    14033  13324  10623    246  -1721   -743       O  
ATOM    231  CB  ILE A  56       8.807   5.991 -27.886  1.00 84.35           C  
ANISOU  231  CB  ILE A  56    11915  11373   8761    564  -1682   -822       C  
ATOM    232  CG1 ILE A  56      10.273   5.568 -27.912  1.00 94.05           C  
ANISOU  232  CG1 ILE A  56    13164  12558  10013    653  -1762   -857       C  
ATOM    233  CG2 ILE A  56       8.548   6.959 -26.736  1.00 72.24           C  
ANISOU  233  CG2 ILE A  56    10356   9878   7214    474  -1598   -798       C  
ATOM    234  CD1 ILE A  56      11.217   6.722 -28.150  1.00 96.00           C  
ANISOU  234  CD1 ILE A  56    13320  12863  10290    726  -1676   -887       C  
ATOM    235  N   ILE A  57       5.647   5.691 -28.052  1.00 80.38           N  
ANISOU  235  N   ILE A  57    11421  10920   8200    382  -1618   -780       N  
ATOM    236  CA  ILE A  57       4.363   6.147 -27.536  1.00 86.73           C  
ANISOU  236  CA  ILE A  57    12198  11777   8978    271  -1546   -772       C  
ATOM    237  C   ILE A  57       3.395   4.984 -27.367  1.00 87.62           C  
ANISOU  237  C   ILE A  57    12391  11860   9039    172  -1614   -757       C  
ATOM    238  O   ILE A  57       2.650   4.922 -26.383  1.00101.62           O  
ANISOU  238  O   ILE A  57    14190  13655  10764     35  -1599   -747       O  
ATOM    239  CB  ILE A  57       3.790   7.239 -28.453  1.00 96.10           C  
ANISOU  239  CB  ILE A  57    13276  13033  10204    332  -1445   -794       C  
ATOM    240  CG1 ILE A  57       4.673   8.483 -28.386  1.00 98.75           C  
ANISOU  240  CG1 ILE A  57    13541  13399  10580    397  -1375   -803       C  
ATOM    241  CG2 ILE A  57       2.348   7.560 -28.076  1.00 94.74           C  
ANISOU  241  CG2 ILE A  57    13070  12916  10011    229  -1387   -805       C  
ATOM    242  CD1 ILE A  57       4.312   9.532 -29.397  1.00100.79           C  
ANISOU  242  CD1 ILE A  57    13709  13708  10879    468  -1298   -819       C  
ATOM    243  N   LEU A  58       3.383   4.044 -28.310  1.00 81.45           N  
ANISOU  243  N   LEU A  58    11650  11034   8262    231  -1688   -759       N  
ATOM    244  CA  LEU A  58       2.361   3.005 -28.255  1.00 85.16           C  
ANISOU  244  CA  LEU A  58    12191  11481   8684    136  -1745   -746       C  
ATOM    245  C   LEU A  58       2.747   1.861 -27.321  1.00 97.47           C  
ANISOU  245  C   LEU A  58    13884  12954  10196     50  -1869   -714       C  
ATOM    246  O   LEU A  58       1.891   1.334 -26.602  1.00 99.42           O  
ANISOU  246  O   LEU A  58    14195  13200  10380    -96  -1891   -692       O  
ATOM    247  CB  LEU A  58       2.080   2.494 -29.666  1.00 83.13           C  
ANISOU  247  CB  LEU A  58    11919  11215   8452    229  -1772   -764       C  
ATOM    248  CG  LEU A  58       1.577   3.601 -30.600  1.00 82.58           C  
ANISOU  248  CG  LEU A  58    11729  11226   8422    300  -1659   -790       C  
ATOM    249  CD1 LEU A  58       1.789   3.232 -32.056  1.00 80.07           C  
ANISOU  249  CD1 LEU A  58    11391  10897   8135    422  -1689   -808       C  
ATOM    250  CD2 LEU A  58       0.110   3.927 -30.335  1.00 84.69           C  
ANISOU  250  CD2 LEU A  58    11960  11556   8662    196  -1592   -800       C  
ATOM    251  N   ALA A  59       4.024   1.466 -27.312  1.00102.94           N  
ANISOU  251  N   ALA A  59    14622  13576  10916    134  -1956   -713       N  
ATOM    252  CA  ALA A  59       4.443   0.299 -26.541  1.00109.01           C  
ANISOU  252  CA  ALA A  59    15528  14243  11647     69  -2101   -684       C  
ATOM    253  C   ALA A  59       4.542   0.562 -25.043  1.00113.04           C  
ANISOU  253  C   ALA A  59    16088  14754  12109    -62  -2097   -650       C  
ATOM    254  O   ALA A  59       4.565  -0.396 -24.262  1.00120.14           O  
ANISOU  254  O   ALA A  59    17115  15576  12956   -163  -2213   -614       O  
ATOM    255  CB  ALA A  59       5.789  -0.215 -27.055  1.00112.53           C  
ANISOU  255  CB  ALA A  59    15997  14612  12145    214  -2206   -711       C  
ATOM    256  N   HIS A  60       4.603   1.823 -24.625  1.00113.49           N  
ANISOU  256  N   HIS A  60    16049  14893  12178    -68  -1972   -662       N  
ATOM    257  CA  HIS A  60       4.739   2.181 -23.220  1.00113.02           C  
ANISOU  257  CA  HIS A  60    16021  14847  12075   -188  -1956   -637       C  
ATOM    258  C   HIS A  60       3.424   2.763 -22.718  1.00115.07           C  
ANISOU  258  C   HIS A  60    16229  15205  12287   -329  -1845   -642       C  
ATOM    259  O   HIS A  60       2.868   3.676 -23.334  1.00106.58           O  
ANISOU  259  O   HIS A  60    15036  14212  11249   -280  -1730   -677       O  
ATOM    260  CB  HIS A  60       5.896   3.163 -23.023  1.00110.74           C  
ANISOU  260  CB  HIS A  60    15662  14577  11838    -90  -1905   -656       C  
ATOM    261  CG  HIS A  60       7.235   2.590 -23.376  1.00120.48           C  
ANISOU  261  CG  HIS A  60    16940  15723  13113     37  -2016   -667       C  
ATOM    262  ND1 HIS A  60       7.566   2.203 -24.656  1.00132.60           N  
ANISOU  262  ND1 HIS A  60    18450  17233  14697    175  -2054   -700       N  
ATOM    263  CD2 HIS A  60       8.323   2.329 -22.613  1.00126.52           C  
ANISOU  263  CD2 HIS A  60    17769  16424  13879     47  -2102   -659       C  
ATOM    264  CE1 HIS A  60       8.800   1.733 -24.669  1.00138.05           C  
ANISOU  264  CE1 HIS A  60    19181  17854  15419    265  -2157   -720       C  
ATOM    265  NE2 HIS A  60       9.282   1.798 -23.441  1.00134.54           N  
ANISOU  265  NE2 HIS A  60    18790  17380  14947    194  -2191   -696       N  
ATOM    266  N   LYS A  61       2.941   2.237 -21.590  1.00124.93           N  
ANISOU  266  N   LYS A  61    17569  16447  13453   -508  -1886   -611       N  
ATOM    267  CA  LYS A  61       1.580   2.527 -21.147  1.00131.40           C  
ANISOU  267  CA  LYS A  61    18349  17363  14214   -662  -1798   -628       C  
ATOM    268  C   LYS A  61       1.396   3.989 -20.749  1.00125.64           C  
ANISOU  268  C   LYS A  61    17482  16743  13512   -664  -1651   -670       C  
ATOM    269  O   LYS A  61       0.363   4.593 -21.064  1.00122.20           O  
ANISOU  269  O   LYS A  61    16948  16399  13084   -686  -1553   -717       O  
ATOM    270  CB  LYS A  61       1.213   1.612 -19.978  1.00145.40           C  
ANISOU  270  CB  LYS A  61    20257  19107  15880   -869  -1880   -585       C  
ATOM    271  CG  LYS A  61       1.164   0.134 -20.332  1.00156.18           C  
ANISOU  271  CG  LYS A  61    21767  20363  17211   -893  -2032   -543       C  
ATOM    272  CD  LYS A  61       0.830  -0.707 -19.112  1.00165.85           C  
ANISOU  272  CD  LYS A  61    23138  21557  18321  -1115  -2118   -493       C  
ATOM    273  CE  LYS A  61       0.685  -2.173 -19.477  1.00169.41           C  
ANISOU  273  CE  LYS A  61    23737  21893  18737  -1149  -2275   -451       C  
ATOM    274  NZ  LYS A  61       0.360  -3.003 -18.286  1.00170.92           N  
ANISOU  274  NZ  LYS A  61    24087  22048  18807  -1380  -2369   -394       N  
ATOM    275  N   ARG A  62       2.381   4.577 -20.063  1.00121.68           N  
ANISOU  275  N   ARG A  62    16970  16233  13029   -637  -1640   -662       N  
ATOM    276  CA  ARG A  62       2.205   5.926 -19.537  1.00112.25           C  
ANISOU  276  CA  ARG A  62    15655  15139  11856   -656  -1510   -702       C  
ATOM    277  C   ARG A  62       2.119   6.979 -20.633  1.00115.54           C  
ANISOU  277  C   ARG A  62    15936  15602  12363   -501  -1415   -747       C  
ATOM    278  O   ARG A  62       1.524   8.037 -20.405  1.00119.79           O  
ANISOU  278  O   ARG A  62    16365  16230  12920   -526  -1308   -793       O  
ATOM    279  CB  ARG A  62       3.333   6.272 -18.561  1.00107.37           C  
ANISOU  279  CB  ARG A  62    15063  14497  11237   -661  -1525   -680       C  
ATOM    280  CG  ARG A  62       2.879   6.305 -17.104  1.00116.95           C  
ANISOU  280  CG  ARG A  62    16308  15764  12363   -863  -1505   -676       C  
ATOM    281  CD  ARG A  62       3.921   6.899 -16.168  1.00122.92           C  
ANISOU  281  CD  ARG A  62    17061  16515  13127   -860  -1495   -665       C  
ATOM    282  NE  ARG A  62       4.716   5.874 -15.498  1.00134.78           N  
ANISOU  282  NE  ARG A  62    18716  17918  14577   -914  -1633   -604       N  
ATOM    283  CZ  ARG A  62       5.962   5.550 -15.831  1.00148.29           C  
ANISOU  283  CZ  ARG A  62    20477  19529  16335   -778  -1722   -580       C  
ATOM    284  NH1 ARG A  62       6.571   6.173 -16.832  1.00154.02           N  
ANISOU  284  NH1 ARG A  62    21113  20254  17156   -590  -1677   -611       N  
ATOM    285  NH2 ARG A  62       6.602   4.602 -15.159  1.00149.42           N  
ANISOU  285  NH2 ARG A  62    20763  19578  16431   -835  -1860   -531       N  
ATOM    286  N   MET A  63       2.667   6.708 -21.818  1.00119.64           N  
ANISOU  286  N   MET A  63    16460  16062  12935   -348  -1458   -737       N  
ATOM    287  CA  MET A  63       2.754   7.708 -22.876  1.00113.80           C  
ANISOU  287  CA  MET A  63    15607  15357  12276   -203  -1380   -769       C  
ATOM    288  C   MET A  63       1.473   7.843 -23.691  1.00107.08           C  
ANISOU  288  C   MET A  63    14694  14558  11433   -204  -1332   -802       C  
ATOM    289  O   MET A  63       1.426   8.692 -24.585  1.00101.24           O  
ANISOU  289  O   MET A  63    13865  13846  10756    -94  -1274   -827       O  
ATOM    290  CB  MET A  63       3.926   7.387 -23.813  1.00109.04           C  
ANISOU  290  CB  MET A  63    15029  14682  11718    -47  -1442   -753       C  
ATOM    291  CG  MET A  63       5.303   7.474 -23.162  1.00106.17           C  
ANISOU  291  CG  MET A  63    14700  14276  11364    -13  -1478   -737       C  
ATOM    292  SD  MET A  63       5.844   9.159 -22.801  1.00109.77           S  
ANISOU  292  SD  MET A  63    15040  14799  11870     32  -1357   -761       S  
ATOM    293  CE  MET A  63       6.417   9.720 -24.403  1.00108.35           C  
ANISOU  293  CE  MET A  63    14788  14621  11761    212  -1326   -781       C  
ATOM    294  N   ARG A  64       0.442   7.040 -23.423  1.00110.46           N  
ANISOU  294  N   ARG A  64    15169  15001  11801   -328  -1359   -805       N  
ATOM    295  CA  ARG A  64      -0.767   7.044 -24.251  1.00111.77           C  
ANISOU  295  CA  ARG A  64    15280  15213  11974   -324  -1325   -841       C  
ATOM    296  C   ARG A  64      -1.677   8.211 -23.856  1.00105.63           C  
ANISOU  296  C   ARG A  64    14382  14540  11213   -374  -1215   -906       C  
ATOM    297  O   ARG A  64      -2.771   8.046 -23.309  1.00120.44           O  
ANISOU  297  O   ARG A  64    16242  16481  13040   -509  -1189   -945       O  
ATOM    298  CB  ARG A  64      -1.488   5.706 -24.142  1.00125.97           C  
ANISOU  298  CB  ARG A  64    17176  16987  13698   -439  -1399   -824       C  
ATOM    299  CG  ARG A  64      -0.608   4.496 -24.436  1.00135.11           C  
ANISOU  299  CG  ARG A  64    18461  18033  14843   -395  -1525   -768       C  
ATOM    300  CD  ARG A  64      -1.432   3.270 -24.799  1.00141.45           C  
ANISOU  300  CD  ARG A  64    19341  18807  15595   -466  -1595   -757       C  
ATOM    301  NE  ARG A  64      -0.617   2.058 -24.835  1.00149.71           N  
ANISOU  301  NE  ARG A  64    20521  19739  16623   -448  -1732   -707       N  
ATOM    302  CZ  ARG A  64      -0.530   1.183 -23.836  1.00162.21           C  
ANISOU  302  CZ  ARG A  64    22229  21269  18133   -586  -1821   -666       C  
ATOM    303  NH1 ARG A  64      -1.213   1.375 -22.716  1.00168.11           N  
ANISOU  303  NH1 ARG A  64    22984  22082  18808   -764  -1776   -670       N  
ATOM    304  NH2 ARG A  64       0.238   0.109 -23.960  1.00164.64           N  
ANISOU  304  NH2 ARG A  64    22656  21461  18438   -549  -1960   -627       N  
ATOM    305  N   THR A  65      -1.204   9.416 -24.159  1.00 87.33           N  
ANISOU  305  N   THR A  65    11975  12239   8968   -264  -1155   -924       N  
ATOM    306  CA  THR A  65      -1.968  10.643 -23.986  1.00 83.93           C  
ANISOU  306  CA  THR A  65    11421  11893   8577   -273  -1063   -991       C  
ATOM    307  C   THR A  65      -2.628  11.057 -25.301  1.00 77.81           C  
ANISOU  307  C   THR A  65    10577  11129   7860   -165  -1044  -1021       C  
ATOM    308  O   THR A  65      -2.339  10.520 -26.371  1.00 79.14           O  
ANISOU  308  O   THR A  65    10787  11243   8041    -73  -1092   -985       O  
ATOM    309  CB  THR A  65      -1.068  11.770 -23.470  1.00 94.00           C  
ANISOU  309  CB  THR A  65    12644  13172   9897   -224  -1015   -992       C  
ATOM    310  OG1 THR A  65      -0.172  12.180 -24.511  1.00106.10           O  
ANISOU  310  OG1 THR A  65    14170  14652  11491    -65  -1025   -960       O  
ATOM    311  CG2 THR A  65      -0.257  11.303 -22.273  1.00 86.60           C  
ANISOU  311  CG2 THR A  65    11786  12212   8905   -314  -1045   -954       C  
ATOM    312  N   VAL A  66      -3.538  12.029 -25.203  1.00 78.51           N  
ANISOU  312  N   VAL A  66    10556  11290   7984   -177   -979  -1095       N  
ATOM    313  CA  VAL A  66      -4.167  12.604 -26.394  1.00 76.68           C  
ANISOU  313  CA  VAL A  66    10253  11067   7815    -71   -966  -1128       C  
ATOM    314  C   VAL A  66      -3.111  13.217 -27.310  1.00 82.22           C  
ANISOU  314  C   VAL A  66    10956  11707   8577     82   -975  -1079       C  
ATOM    315  O   VAL A  66      -3.022  12.900 -28.513  1.00 81.65           O  
ANISOU  315  O   VAL A  66    10908  11597   8520    173  -1009  -1050       O  
ATOM    316  CB  VAL A  66      -5.215  13.652 -25.970  1.00 77.19           C  
ANISOU  316  CB  VAL A  66    10196  11216   7918   -107   -905  -1226       C  
ATOM    317  CG1 VAL A  66      -5.568  14.583 -27.119  1.00 61.00           C  
ANISOU  317  CG1 VAL A  66     8071   9155   5951     27   -899  -1254       C  
ATOM    318  CG2 VAL A  66      -6.458  12.983 -25.387  1.00 89.43           C  
ANISOU  318  CG2 VAL A  66    11732  12841   9406   -253   -896  -1291       C  
ATOM    319  N   THR A  67      -2.270  14.081 -26.738  1.00 98.72           N  
ANISOU  319  N   THR A  67    13022  13793  10695    103   -943  -1070       N  
ATOM    320  CA  THR A  67      -1.244  14.750 -27.524  1.00 94.19           C  
ANISOU  320  CA  THR A  67    12445  13172  10170    231   -943  -1029       C  
ATOM    321  C   THR A  67      -0.334  13.731 -28.188  1.00 90.39           C  
ANISOU  321  C   THR A  67    12055  12631   9659    282  -1002   -965       C  
ATOM    322  O   THR A  67      -0.012  13.853 -29.376  1.00 95.39           O  
ANISOU  322  O   THR A  67    12689  13237  10317    383  -1018   -943       O  
ATOM    323  CB  THR A  67      -0.440  15.697 -26.626  1.00 94.67           C  
ANISOU  323  CB  THR A  67    12476  13240  10255    225   -901  -1031       C  
ATOM    324  OG1 THR A  67      -1.115  16.958 -26.522  1.00 96.10           O  
ANISOU  324  OG1 THR A  67    12557  13461  10496    238   -854  -1091       O  
ATOM    325  CG2 THR A  67       0.956  15.919 -27.182  1.00 93.96           C  
ANISOU  325  CG2 THR A  67    12420  13097  10182    322   -914   -974       C  
ATOM    326  N   ASN A  68       0.071  12.701 -27.444  1.00 88.71           N  
ANISOU  326  N   ASN A  68    11920  12397   9389    209  -1040   -940       N  
ATOM    327  CA  ASN A  68       1.007  11.740 -28.008  1.00 93.62           C  
ANISOU  327  CA  ASN A  68    12624  12957   9990    265  -1107   -892       C  
ATOM    328  C   ASN A  68       0.355  10.900 -29.099  1.00 86.35           C  
ANISOU  328  C   ASN A  68    11729  12022   9059    295  -1151   -890       C  
ATOM    329  O   ASN A  68       1.052  10.400 -29.989  1.00 81.84           O  
ANISOU  329  O   ASN A  68    11194  11411   8492    379  -1195   -865       O  
ATOM    330  CB  ASN A  68       1.569  10.859 -26.900  1.00 96.84           C  
ANISOU  330  CB  ASN A  68    13115  13335  10346    180  -1154   -868       C  
ATOM    331  CG  ASN A  68       2.660  11.552 -26.112  1.00 95.73           C  
ANISOU  331  CG  ASN A  68    12964  13190  10220    190  -1128   -858       C  
ATOM    332  OD1 ASN A  68       3.300  12.484 -26.602  1.00 93.49           O  
ANISOU  332  OD1 ASN A  68    12628  12910   9984    282  -1090   -859       O  
ATOM    333  ND2 ASN A  68       2.869  11.113 -24.879  1.00100.94           N  
ANISOU  333  ND2 ASN A  68    13676  13843  10835     89  -1150   -847       N  
ATOM    334  N   TYR A  69      -0.971  10.732 -29.053  1.00 88.97           N  
ANISOU  334  N   TYR A  69    12035  12392   9376    228  -1138   -924       N  
ATOM    335  CA  TYR A  69      -1.647  10.049 -30.150  1.00 92.86           C  
ANISOU  335  CA  TYR A  69    12542  12876   9863    263  -1173   -926       C  
ATOM    336  C   TYR A  69      -1.580  10.884 -31.421  1.00 93.46           C  
ANISOU  336  C   TYR A  69    12560  12956   9995    386  -1151   -928       C  
ATOM    337  O   TYR A  69      -1.281  10.359 -32.507  1.00103.99           O  
ANISOU  337  O   TYR A  69    13922  14261  11328    461  -1190   -907       O  
ATOM    338  CB  TYR A  69      -3.103   9.734 -29.792  1.00 93.42           C  
ANISOU  338  CB  TYR A  69    12593  12997   9905    158  -1160   -971       C  
ATOM    339  CG  TYR A  69      -3.325   8.443 -29.025  1.00 98.71           C  
ANISOU  339  CG  TYR A  69    13352  13652  10500     34  -1211   -956       C  
ATOM    340  CD1 TYR A  69      -2.273   7.772 -28.415  1.00102.41           C  
ANISOU  340  CD1 TYR A  69    13912  14063  10938     10  -1265   -907       C  
ATOM    341  CD2 TYR A  69      -4.593   7.878 -28.943  1.00108.16           C  
ANISOU  341  CD2 TYR A  69    14549  14890  11658    -62  -1212   -991       C  
ATOM    342  CE1 TYR A  69      -2.485   6.585 -27.725  1.00115.79           C  
ANISOU  342  CE1 TYR A  69    15703  15732  12561   -109  -1327   -887       C  
ATOM    343  CE2 TYR A  69      -4.814   6.692 -28.257  1.00118.50           C  
ANISOU  343  CE2 TYR A  69    15951  16183  12891   -189  -1264   -972       C  
ATOM    344  CZ  TYR A  69      -3.756   6.050 -27.649  1.00121.78           C  
ANISOU  344  CZ  TYR A  69    16465  16531  13275   -214  -1326   -916       C  
ATOM    345  OH  TYR A  69      -3.966   4.871 -26.965  1.00123.42           O  
ANISOU  345  OH  TYR A  69    16779  16710  13404   -346  -1392   -891       O  
ATOM    346  N   PHE A  70      -1.805  12.199 -31.297  1.00 83.45           N  
ANISOU  346  N   PHE A  70    11212  11721   8773    407  -1093   -955       N  
ATOM    347  CA  PHE A  70      -1.640  13.056 -32.472  1.00 81.48           C  
ANISOU  347  CA  PHE A  70    10921  11465   8571    516  -1082   -948       C  
ATOM    348  C   PHE A  70      -0.198  13.049 -32.970  1.00 84.92           C  
ANISOU  348  C   PHE A  70    11394  11864   9006    591  -1098   -901       C  
ATOM    349  O   PHE A  70       0.046  13.061 -34.187  1.00 83.00           O  
ANISOU  349  O   PHE A  70    11154  11611   8771    669  -1115   -883       O  
ATOM    350  CB  PHE A  70      -2.129  14.470 -32.173  1.00 83.14           C  
ANISOU  350  CB  PHE A  70    11048  11707   8836    521  -1033   -986       C  
ATOM    351  CG  PHE A  70      -3.623  14.574 -32.090  1.00 90.50           C  
ANISOU  351  CG  PHE A  70    11924  12682   9780    477  -1024  -1051       C  
ATOM    352  CD1 PHE A  70      -4.403  14.328 -33.207  1.00 92.85           C  
ANISOU  352  CD1 PHE A  70    12214  12979  10087    523  -1051  -1061       C  
ATOM    353  CD2 PHE A  70      -4.250  14.889 -30.898  1.00 92.36           C  
ANISOU  353  CD2 PHE A  70    12111  12965  10016    387   -988  -1109       C  
ATOM    354  CE1 PHE A  70      -5.779  14.413 -33.139  1.00 94.98           C  
ANISOU  354  CE1 PHE A  70    12426  13292  10369    486  -1046  -1131       C  
ATOM    355  CE2 PHE A  70      -5.626  14.973 -30.823  1.00 86.12           C  
ANISOU  355  CE2 PHE A  70    11258  12226   9237    344   -979  -1185       C  
ATOM    356  CZ  PHE A  70      -6.391  14.736 -31.944  1.00 89.81           C  
ANISOU  356  CZ  PHE A  70    11717  12690   9717    397  -1009  -1197       C  
ATOM    357  N   LEU A  71       0.773  12.999 -32.051  1.00 87.43           N  
ANISOU  357  N   LEU A  71    11739  12169   9311    564  -1093   -886       N  
ATOM    358  CA  LEU A  71       2.171  12.908 -32.465  1.00 83.82           C  
ANISOU  358  CA  LEU A  71    11312  11685   8851    631  -1110   -857       C  
ATOM    359  C   LEU A  71       2.445  11.599 -33.192  1.00 74.62           C  
ANISOU  359  C   LEU A  71    10206  10491   7654    662  -1177   -846       C  
ATOM    360  O   LEU A  71       3.292  11.558 -34.092  1.00 63.73           O  
ANISOU  360  O   LEU A  71     8831   9106   6278    737  -1191   -838       O  
ATOM    361  CB  LEU A  71       3.111  13.062 -31.273  1.00 79.11           C  
ANISOU  361  CB  LEU A  71    10731  11079   8247    595  -1099   -850       C  
ATOM    362  CG  LEU A  71       3.085  14.402 -30.546  1.00 70.21           C  
ANISOU  362  CG  LEU A  71     9543   9978   7153    574  -1033   -863       C  
ATOM    363  CD1 LEU A  71       4.089  14.376 -29.412  1.00 75.51           C  
ANISOU  363  CD1 LEU A  71    10239  10640   7812    540  -1028   -855       C  
ATOM    364  CD2 LEU A  71       3.377  15.532 -31.510  1.00 65.20           C  
ANISOU  364  CD2 LEU A  71     8863   9351   6558    654  -1002   -856       C  
ATOM    365  N   VAL A  72       1.771  10.515 -32.798  1.00 77.75           N  
ANISOU  365  N   VAL A  72    10649  10874   8020    598  -1220   -850       N  
ATOM    366  CA  VAL A  72       1.940   9.260 -33.520  1.00 80.36           C  
ANISOU  366  CA  VAL A  72    11035  11172   8326    629  -1291   -845       C  
ATOM    367  C   VAL A  72       1.383   9.404 -34.926  1.00 83.39           C  
ANISOU  367  C   VAL A  72    11384  11576   8724    694  -1285   -851       C  
ATOM    368  O   VAL A  72       1.941   8.862 -35.886  1.00 91.15           O  
ANISOU  368  O   VAL A  72    12385  12547   9702    761  -1323   -850       O  
ATOM    369  CB  VAL A  72       1.288   8.092 -32.761  1.00 86.73           C  
ANISOU  369  CB  VAL A  72    11908  11953   9093    534  -1344   -844       C  
ATOM    370  CG1 VAL A  72       0.872   6.991 -33.726  1.00 89.73           C  
ANISOU  370  CG1 VAL A  72    12326  12311   9458    562  -1405   -846       C  
ATOM    371  CG2 VAL A  72       2.260   7.540 -31.744  1.00 97.11           C  
ANISOU  371  CG2 VAL A  72    13288  13223  10385    500  -1392   -829       C  
ATOM    372  N   ASN A  73       0.272  10.130 -35.076  1.00 76.82           N  
ANISOU  372  N   ASN A  73    10500  10777   7910    675  -1241   -864       N  
ATOM    373  CA  ASN A  73      -0.257  10.333 -36.419  1.00 79.20           C  
ANISOU  373  CA  ASN A  73    10773  11095   8226    738  -1241   -867       C  
ATOM    374  C   ASN A  73       0.723  11.121 -37.281  1.00 89.24           C  
ANISOU  374  C   ASN A  73    12021  12372   9513    820  -1223   -850       C  
ATOM    375  O   ASN A  73       0.954  10.774 -38.446  1.00 94.70           O  
ANISOU  375  O   ASN A  73    12719  13067  10194    876  -1247   -846       O  
ATOM    376  CB  ASN A  73      -1.603  11.049 -36.367  1.00 86.89           C  
ANISOU  376  CB  ASN A  73    11691  12099   9223    709  -1206   -893       C  
ATOM    377  CG  ASN A  73      -2.338  10.985 -37.692  1.00 94.47           C  
ANISOU  377  CG  ASN A  73    12634  13070  10191    761  -1223   -899       C  
ATOM    378  OD1 ASN A  73      -2.388   9.937 -38.337  1.00 93.76           O  
ANISOU  378  OD1 ASN A  73    12580  12968  10074    776  -1265   -894       O  
ATOM    379  ND2 ASN A  73      -2.901  12.114 -38.113  1.00 95.12           N  
ANISOU  379  ND2 ASN A  73    12660  13170  10311    792  -1197   -910       N  
ATOM    380  N   ALA A  74       1.314  12.186 -36.727  1.00 95.99           N  
ANISOU  380  N   ALA A  74    12849  13234  10390    819  -1179   -843       N  
ATOM    381  CA  ALA A  74       2.292  12.961 -37.491  1.00 91.01           C  
ANISOU  381  CA  ALA A  74    12201  12613   9766    880  -1160   -826       C  
ATOM    382  C   ALA A  74       3.548  12.152 -37.817  1.00 80.37           C  
ANISOU  382  C   ALA A  74    10887  11261   8390    916  -1192   -828       C  
ATOM    383  O   ALA A  74       4.096  12.275 -38.919  1.00 71.19           O  
ANISOU  383  O   ALA A  74     9716  10118   7214    967  -1194   -827       O  
ATOM    384  CB  ALA A  74       2.655  14.238 -36.732  1.00 91.97           C  
ANISOU  384  CB  ALA A  74    12290  12739   9916    865  -1110   -820       C  
ATOM    385  N   ALA A  75       4.031  11.334 -36.877  1.00 84.95           N  
ANISOU  385  N   ALA A  75    11505  11816   8958    888  -1222   -838       N  
ATOM    386  CA  ALA A  75       5.194  10.492 -37.160  1.00 85.16           C  
ANISOU  386  CA  ALA A  75    11559  11832   8966    930  -1268   -855       C  
ATOM    387  C   ALA A  75       4.871   9.427 -38.199  1.00 84.06           C  
ANISOU  387  C   ALA A  75    11440  11690   8810    964  -1322   -871       C  
ATOM    388  O   ALA A  75       5.734   9.056 -39.009  1.00 78.87           O  
ANISOU  388  O   ALA A  75    10778  11048   8141   1020  -1347   -896       O  
ATOM    389  CB  ALA A  75       5.694   9.839 -35.870  1.00 84.80           C  
ANISOU  389  CB  ALA A  75    11557  11747   8914    891  -1304   -861       C  
ATOM    390  N   PHE A  76       3.630   8.944 -38.193  1.00 85.21           N  
ANISOU  390  N   PHE A  76    11601  11821   8953    929  -1340   -864       N  
ATOM    391  CA  PHE A  76       3.181   7.977 -39.182  1.00 88.03           C  
ANISOU  391  CA  PHE A  76    11975  12176   9296    957  -1388   -877       C  
ATOM    392  C   PHE A  76       3.132   8.602 -40.568  1.00 86.35           C  
ANISOU  392  C   PHE A  76    11718  12008   9082   1011  -1359   -876       C  
ATOM    393  O   PHE A  76       3.619   8.012 -41.541  1.00 91.13           O  
ANISOU  393  O   PHE A  76    12324  12629   9672   1061  -1391   -898       O  
ATOM    394  CB  PHE A  76       1.812   7.441 -38.759  1.00 95.10           C  
ANISOU  394  CB  PHE A  76    12895  13053  10186    894  -1404   -871       C  
ATOM    395  CG  PHE A  76       1.111   6.639 -39.809  1.00 95.34           C  
ANISOU  395  CG  PHE A  76    12933  13086  10204    918  -1442   -882       C  
ATOM    396  CD1 PHE A  76       1.494   5.337 -40.074  1.00 89.15           C  
ANISOU  396  CD1 PHE A  76    12197  12270   9407    939  -1518   -900       C  
ATOM    397  CD2 PHE A  76       0.046   7.177 -40.511  1.00 91.05           C  
ANISOU  397  CD2 PHE A  76    12352  12575   9670    922  -1408   -878       C  
ATOM    398  CE1 PHE A  76       0.843   4.592 -41.030  1.00 79.09           C  
ANISOU  398  CE1 PHE A  76    10929  10999   8124    960  -1552   -913       C  
ATOM    399  CE2 PHE A  76      -0.610   6.435 -41.468  1.00 89.44           C  
ANISOU  399  CE2 PHE A  76    12155  12375   9454    943  -1442   -889       C  
ATOM    400  CZ  PHE A  76      -0.210   5.140 -41.727  1.00 81.71           C  
ANISOU  400  CZ  PHE A  76    11221  11368   8458    961  -1510   -906       C  
ATOM    401  N   ALA A  77       2.596   9.822 -40.665  1.00 76.15           N  
ANISOU  401  N   ALA A  77    10389  10738   7806   1000  -1303   -854       N  
ATOM    402  CA  ALA A  77       2.531  10.509 -41.951  1.00 76.67           C  
ANISOU  402  CA  ALA A  77    10425  10840   7867   1040  -1283   -843       C  
ATOM    403  C   ALA A  77       3.921  10.854 -42.478  1.00 86.43           C  
ANISOU  403  C   ALA A  77    11649  12107   9083   1075  -1269   -850       C  
ATOM    404  O   ALA A  77       4.206  10.664 -43.667  1.00 93.91           O  
ANISOU  404  O   ALA A  77    12587  13090  10005   1109  -1280   -861       O  
ATOM    405  CB  ALA A  77       1.682  11.773 -41.823  1.00 70.67           C  
ANISOU  405  CB  ALA A  77     9636  10082   7135   1021  -1242   -820       C  
ATOM    406  N   GLU A  78       4.798  11.362 -41.610  1.00 88.06           N  
ANISOU  406  N   GLU A  78    11852  12310   9298   1062  -1242   -850       N  
ATOM    407  CA  GLU A  78       6.131  11.758 -42.053  1.00 87.72           C  
ANISOU  407  CA  GLU A  78    11791  12306   9234   1087  -1223   -865       C  
ATOM    408  C   GLU A  78       6.968  10.551 -42.464  1.00 89.03           C  
ANISOU  408  C   GLU A  78    11963  12485   9378   1125  -1272   -917       C  
ATOM    409  O   GLU A  78       7.644  10.581 -43.503  1.00 95.60           O  
ANISOU  409  O   GLU A  78    12771  13372  10180   1152  -1267   -944       O  
ATOM    410  CB  GLU A  78       6.820  12.566 -40.949  1.00 94.38           C  
ANISOU  410  CB  GLU A  78    12627  13140  10094   1063  -1184   -856       C  
ATOM    411  CG  GLU A  78       6.219  13.960 -40.765  1.00 99.99           C  
ANISOU  411  CG  GLU A  78    13319  13846  10827   1036  -1135   -814       C  
ATOM    412  CD  GLU A  78       6.625  14.637 -39.467  1.00107.53           C  
ANISOU  412  CD  GLU A  78    14267  14783  11808   1007  -1101   -808       C  
ATOM    413  OE1 GLU A  78       7.570  14.162 -38.800  1.00115.38           O  
ANISOU  413  OE1 GLU A  78    15269  15774  12794   1009  -1108   -832       O  
ATOM    414  OE2 GLU A  78       5.988  15.653 -39.115  1.00109.88           O  
ANISOU  414  OE2 GLU A  78    14549  15067  12135    984  -1071   -784       O  
ATOM    415  N   ALA A  79       6.915   9.467 -41.684  1.00 89.60           N  
ANISOU  415  N   ALA A  79    12068  12511   9463   1124  -1325   -938       N  
ATOM    416  CA  ALA A  79       7.640   8.264 -42.077  1.00 96.48           C  
ANISOU  416  CA  ALA A  79    12948  13384  10324   1168  -1390   -996       C  
ATOM    417  C   ALA A  79       7.100   7.702 -43.385  1.00 96.55           C  
ANISOU  417  C   ALA A  79    12949  13421  10316   1196  -1414  -1011       C  
ATOM    418  O   ALA A  79       7.876   7.308 -44.271  1.00105.21           O  
ANISOU  418  O   ALA A  79    14018  14564  11393   1238  -1432  -1064       O  
ATOM    419  CB  ALA A  79       7.553   7.214 -40.969  1.00103.58           C  
ANISOU  419  CB  ALA A  79    13901  14213  11243   1154  -1458  -1004       C  
ATOM    420  N   SER A  80       5.773   7.713 -43.546  1.00 88.81           N  
ANISOU  420  N   SER A  80    11982  12420   9340   1171  -1410   -971       N  
ATOM    421  CA  SER A  80       5.176   7.161 -44.756  1.00 83.64           C  
ANISOU  421  CA  SER A  80    11321  11789   8669   1196  -1434   -983       C  
ATOM    422  C   SER A  80       5.594   7.959 -45.983  1.00 81.47           C  
ANISOU  422  C   SER A  80    11004  11589   8364   1212  -1391   -985       C  
ATOM    423  O   SER A  80       6.047   7.391 -46.987  1.00 83.20           O  
ANISOU  423  O   SER A  80    11203  11853   8557   1246  -1414  -1031       O  
ATOM    424  CB  SER A  80       3.653   7.146 -44.630  1.00 87.12           C  
ANISOU  424  CB  SER A  80    11781  12200   9122   1162  -1432   -943       C  
ATOM    425  OG  SER A  80       3.243   6.644 -43.370  1.00 96.52           O  
ANISOU  425  OG  SER A  80    13010  13332  10330   1121  -1458   -935       O  
ATOM    426  N   MET A  81       5.468   9.288 -45.910  1.00 80.67           N  
ANISOU  426  N   MET A  81    10890  11501   8261   1184  -1332   -938       N  
ATOM    427  CA  MET A  81       5.838  10.109 -47.055  1.00 77.71           C  
ANISOU  427  CA  MET A  81    10488  11190   7848   1183  -1297   -929       C  
ATOM    428  C   MET A  81       7.323   9.999 -47.358  1.00 73.65           C  
ANISOU  428  C   MET A  81     9946  10736   7302   1198  -1289   -985       C  
ATOM    429  O   MET A  81       7.715  10.021 -48.531  1.00 79.42           O  
ANISOU  429  O   MET A  81    10652  11537   7988   1201  -1282  -1010       O  
ATOM    430  CB  MET A  81       5.450  11.568 -46.814  1.00 76.13           C  
ANISOU  430  CB  MET A  81    10290  10979   7659   1149  -1250   -868       C  
ATOM    431  CG  MET A  81       5.569  12.427 -48.054  1.00 79.30           C  
ANISOU  431  CG  MET A  81    10682  11431   8015   1135  -1229   -842       C  
ATOM    432  SD  MET A  81       5.559  14.189 -47.698  1.00 85.37           S  
ANISOU  432  SD  MET A  81    11459  12181   8796   1094  -1185   -779       S  
ATOM    433  CE  MET A  81       7.177  14.394 -46.970  1.00 92.12           C  
ANISOU  433  CE  MET A  81    12296  13067   9637   1082  -1147   -812       C  
ATOM    434  N   ALA A  82       8.160   9.825 -46.334  1.00 75.96           N  
ANISOU  434  N   ALA A  82    10238  11008   7615   1204  -1292  -1014       N  
ATOM    435  CA  ALA A  82       9.580   9.648 -46.602  1.00 87.94           C  
ANISOU  435  CA  ALA A  82    11720  12587   9106   1223  -1290  -1085       C  
ATOM    436  C   ALA A  82       9.821   8.377 -47.405  1.00 93.17           C  
ANISOU  436  C   ALA A  82    12364  13280   9756   1268  -1347  -1162       C  
ATOM    437  O   ALA A  82      10.361   8.424 -48.520  1.00 98.57           O  
ANISOU  437  O   ALA A  82    13007  14050  10394   1270  -1333  -1208       O  
ATOM    438  CB  ALA A  82      10.362   9.624 -45.289  1.00 89.82           C  
ANISOU  438  CB  ALA A  82    11963  12788   9374   1228  -1294  -1105       C  
ATOM    439  N   ALA A  83       9.351   7.234 -46.883  1.00 89.87           N  
ANISOU  439  N   ALA A  83    11978  12794   9375   1297  -1416  -1178       N  
ATOM    440  CA  ALA A  83       9.668   5.963 -47.527  1.00 92.90           C  
ANISOU  440  CA  ALA A  83    12345  13194   9758   1347  -1484  -1261       C  
ATOM    441  C   ALA A  83       9.017   5.830 -48.898  1.00103.02           C  
ANISOU  441  C   ALA A  83    13608  14528  11006   1348  -1477  -1260       C  
ATOM    442  O   ALA A  83       9.594   5.201 -49.794  1.00 99.03           O  
ANISOU  442  O   ALA A  83    13062  14086  10480   1381  -1504  -1342       O  
ATOM    443  CB  ALA A  83       9.244   4.802 -46.632  1.00 88.53           C  
ANISOU  443  CB  ALA A  83    11844  12542   9250   1368  -1568  -1266       C  
ATOM    444  N   PHE A  84       7.839   6.421 -49.095  1.00111.10           N  
ANISOU  444  N   PHE A  84    14657  15531  12024   1314  -1446  -1176       N  
ATOM    445  CA  PHE A  84       7.071   6.186 -50.312  1.00108.69           C  
ANISOU  445  CA  PHE A  84    14344  15262  11693   1317  -1451  -1170       C  
ATOM    446  C   PHE A  84       7.193   7.313 -51.327  1.00 98.95           C  
ANISOU  446  C   PHE A  84    13085  14108  10405   1280  -1390  -1141       C  
ATOM    447  O   PHE A  84       6.648   7.194 -52.427  1.00 96.53           O  
ANISOU  447  O   PHE A  84    12770  13840  10067   1277  -1394  -1136       O  
ATOM    448  CB  PHE A  84       5.588   5.961 -49.984  1.00109.54           C  
ANISOU  448  CB  PHE A  84    14494  15295  11829   1305  -1470  -1109       C  
ATOM    449  CG  PHE A  84       5.325   4.754 -49.123  1.00108.77           C  
ANISOU  449  CG  PHE A  84    14434  15121  11773   1324  -1538  -1132       C  
ATOM    450  CD1 PHE A  84       6.279   3.758 -48.976  1.00108.65           C  
ANISOU  450  CD1 PHE A  84    14413  15101  11769   1366  -1598  -1210       C  
ATOM    451  CD2 PHE A  84       4.114   4.616 -48.463  1.00109.27           C  
ANISOU  451  CD2 PHE A  84    14539  15117  11861   1296  -1548  -1080       C  
ATOM    452  CE1 PHE A  84       6.032   2.651 -48.180  1.00107.90           C  
ANISOU  452  CE1 PHE A  84    14366  14922  11708   1376  -1674  -1224       C  
ATOM    453  CE2 PHE A  84       3.858   3.513 -47.666  1.00111.25           C  
ANISOU  453  CE2 PHE A  84    14835  15298  12138   1295  -1614  -1095       C  
ATOM    454  CZ  PHE A  84       4.819   2.528 -47.524  1.00110.16           C  
ANISOU  454  CZ  PHE A  84    14704  15143  12010   1334  -1681  -1161       C  
ATOM    455  N   ASN A  85       7.883   8.405 -50.991  1.00 97.12           N  
ANISOU  455  N   ASN A  85    12845  13899  10157   1246  -1338  -1117       N  
ATOM    456  CA  ASN A  85       7.986   9.519 -51.927  1.00 89.83           C  
ANISOU  456  CA  ASN A  85    11912  13042   9176   1198  -1288  -1080       C  
ATOM    457  C   ASN A  85       9.383  10.107 -52.065  1.00102.89           C  
ANISOU  457  C   ASN A  85    13531  14778  10784   1168  -1245  -1122       C  
ATOM    458  O   ASN A  85       9.722  10.554 -53.166  1.00114.28           O  
ANISOU  458  O   ASN A  85    14956  16308  12159   1127  -1219  -1129       O  
ATOM    459  CB  ASN A  85       7.008  10.636 -51.539  1.00 78.49           C  
ANISOU  459  CB  ASN A  85    10517  11544   7761   1166  -1266   -978       C  
ATOM    460  CG  ASN A  85       5.567  10.278 -51.855  1.00 73.59           C  
ANISOU  460  CG  ASN A  85     9920  10876   7164   1181  -1299   -942       C  
ATOM    461  OD1 ASN A  85       4.850   9.725 -51.023  1.00 79.35           O  
ANISOU  461  OD1 ASN A  85    10667  11537   7945   1202  -1325   -936       O  
ATOM    462  ND2 ASN A  85       5.143  10.573 -53.073  1.00 71.14           N  
ANISOU  462  ND2 ASN A  85     9611  10608   6809   1164  -1301   -919       N  
ATOM    463  N   THR A  86      10.210  10.128 -51.012  1.00110.57           N  
ANISOU  463  N   THR A  86    14494  15730  11786   1181  -1238  -1152       N  
ATOM    464  CA  THR A  86      11.520  10.760 -51.148  1.00112.58           C  
ANISOU  464  CA  THR A  86    14712  16069  11995   1147  -1191  -1196       C  
ATOM    465  C   THR A  86      12.373  10.036 -52.183  1.00 97.23           C  
ANISOU  465  C   THR A  86    12708  14237   9999   1156  -1201  -1307       C  
ATOM    466  O   THR A  86      13.028  10.671 -53.027  1.00 88.14           O  
ANISOU  466  O   THR A  86    11527  13190   8773   1098  -1155  -1327       O  
ATOM    467  CB  THR A  86      12.232  10.786 -49.792  1.00121.52           C  
ANISOU  467  CB  THR A  86    15843  17157  13174   1168  -1189  -1218       C  
ATOM    468  OG1 THR A  86      11.357  11.336 -48.800  1.00117.39           O  
ANISOU  468  OG1 THR A  86    15369  16533  12701   1159  -1183  -1126       O  
ATOM    469  CG2 THR A  86      13.500  11.631 -49.859  1.00126.44           C  
ANISOU  469  CG2 THR A  86    16429  17863  13749   1124  -1132  -1253       C  
ATOM    470  N   VAL A  87      12.307   8.701 -52.180  1.00 99.20           N  
ANISOU  470  N   VAL A  87    12939  14469  10285   1223  -1264  -1381       N  
ATOM    471  CA  VAL A  87      13.136   7.894 -53.070  1.00107.61           C  
ANISOU  471  CA  VAL A  87    13936  15638  11314   1245  -1285  -1509       C  
ATOM    472  C   VAL A  87      12.791   8.188 -54.523  1.00113.15           C  
ANISOU  472  C   VAL A  87    14622  16430  11938   1193  -1256  -1496       C  
ATOM    473  O   VAL A  87      13.664   8.502 -55.347  1.00119.60           O  
ANISOU  473  O   VAL A  87    15386  17374  12681   1146  -1217  -1561       O  
ATOM    474  CB  VAL A  87      12.948   6.400 -52.746  1.00109.26           C  
ANISOU  474  CB  VAL A  87    14142  15785  11588   1331  -1374  -1579       C  
ATOM    475  CG1 VAL A  87      13.889   5.535 -53.573  1.00106.99           C  
ANISOU  475  CG1 VAL A  87    13774  15602  11277   1366  -1406  -1732       C  
ATOM    476  CG2 VAL A  87      13.126   6.145 -51.259  1.00112.65           C  
ANISOU  476  CG2 VAL A  87    14607  16107  12089   1369  -1412  -1569       C  
ATOM    477  N   VAL A  88      11.500   8.112 -54.852  1.00107.63           N  
ANISOU  477  N   VAL A  88    13970  15672  11251   1195  -1275  -1413       N  
ATOM    478  CA  VAL A  88      11.071   8.283 -56.234  1.00 95.31           C  
ANISOU  478  CA  VAL A  88    12403  14189   9621   1151  -1260  -1398       C  
ATOM    479  C   VAL A  88      11.234   9.730 -56.689  1.00 93.28           C  
ANISOU  479  C   VAL A  88    12169  13983   9291   1056  -1197  -1321       C  
ATOM    480  O   VAL A  88      11.566   9.989 -57.849  1.00 93.77           O  
ANISOU  480  O   VAL A  88    12206  14156   9265    994  -1172  -1345       O  
ATOM    481  CB  VAL A  88       9.628   7.783 -56.388  1.00 83.94           C  
ANISOU  481  CB  VAL A  88    11008  12665   8220   1184  -1304  -1334       C  
ATOM    482  CG1 VAL A  88       9.215   7.815 -57.843  1.00 89.22           C  
ANISOU  482  CG1 VAL A  88    11666  13415   8819   1147  -1298  -1329       C  
ATOM    483  CG2 VAL A  88       9.536   6.383 -55.822  1.00 78.61           C  
ANISOU  483  CG2 VAL A  88    10322  11931   7616   1268  -1371  -1404       C  
ATOM    484  N   ASN A  89      11.020  10.696 -55.794  1.00105.34           N  
ANISOU  484  N   ASN A  89    13745  15431  10849   1036  -1175  -1231       N  
ATOM    485  CA  ASN A  89      11.264  12.082 -56.180  1.00116.44           C  
ANISOU  485  CA  ASN A  89    15178  16876  12187    944  -1125  -1162       C  
ATOM    486  C   ASN A  89      12.721  12.289 -56.565  1.00117.29           C  
ANISOU  486  C   ASN A  89    15228  17116  12219    889  -1079  -1251       C  
ATOM    487  O   ASN A  89      13.016  12.962 -57.563  1.00122.23           O  
ANISOU  487  O   ASN A  89    15858  17836  12750    797  -1047  -1236       O  
ATOM    488  CB  ASN A  89      10.866  13.032 -55.046  1.00134.92           C  
ANISOU  488  CB  ASN A  89    17573  19107  14585    941  -1114  -1066       C  
ATOM    489  CG  ASN A  89       9.402  13.408 -55.093  1.00147.03           C  
ANISOU  489  CG  ASN A  89    19165  20544  16155    950  -1144   -962       C  
ATOM    490  OD1 ASN A  89       9.043  14.474 -55.590  1.00145.12           O  
ANISOU  490  OD1 ASN A  89    18967  20297  15877    891  -1137   -882       O  
ATOM    491  ND2 ASN A  89       8.544  12.527 -54.585  1.00161.00           N  
ANISOU  491  ND2 ASN A  89    20939  22238  17996   1020  -1185   -968       N  
ATOM    492  N   PHE A  90      13.649  11.659 -55.837  1.00118.68           N  
ANISOU  492  N   PHE A  90    15351  17310  12432    939  -1081  -1352       N  
ATOM    493  CA  PHE A  90      15.052  11.828 -56.201  1.00119.25           C  
ANISOU  493  CA  PHE A  90    15357  17519  12434    888  -1037  -1456       C  
ATOM    494  C   PHE A  90      15.376  11.131 -57.520  1.00125.69           C  
ANISOU  494  C   PHE A  90    16110  18471  13177    867  -1041  -1559       C  
ATOM    495  O   PHE A  90      15.949  11.746 -58.433  1.00126.86           O  
ANISOU  495  O   PHE A  90    16237  18745  13219    766   -992  -1579       O  
ATOM    496  CB  PHE A  90      15.970  11.314 -55.094  1.00121.56           C  
ANISOU  496  CB  PHE A  90    15604  17794  12789    955  -1047  -1549       C  
ATOM    497  CG  PHE A  90      17.423  11.346 -55.472  1.00130.78           C  
ANISOU  497  CG  PHE A  90    16688  19112  13890    915  -1008  -1683       C  
ATOM    498  CD1 PHE A  90      18.075  12.558 -55.649  1.00134.81           C  
ANISOU  498  CD1 PHE A  90    17203  19697  14322    809   -937  -1654       C  
ATOM    499  CD2 PHE A  90      18.130  10.173 -55.676  1.00135.23           C  
ANISOU  499  CD2 PHE A  90    17167  19746  14470    979  -1045  -1845       C  
ATOM    500  CE1 PHE A  90      19.410  12.599 -56.008  1.00132.50           C  
ANISOU  500  CE1 PHE A  90    16827  19556  13961    761   -895  -1786       C  
ATOM    501  CE2 PHE A  90      19.467  10.207 -56.035  1.00134.90           C  
ANISOU  501  CE2 PHE A  90    17035  19854  14368    942  -1009  -1986       C  
ATOM    502  CZ  PHE A  90      20.108  11.425 -56.202  1.00131.65           C  
ANISOU  502  CZ  PHE A  90    16625  19527  13871    829   -929  -1958       C  
ATOM    503  N   THR A  91      15.000   9.851 -57.652  1.00123.24           N  
ANISOU  503  N   THR A  91    15770  18138  12919    955  -1100  -1626       N  
ATOM    504  CA  THR A  91      15.397   9.106 -58.845  1.00110.66           C  
ANISOU  504  CA  THR A  91    14102  16680  11264    944  -1106  -1747       C  
ATOM    505  C   THR A  91      14.775   9.706 -60.097  1.00106.76           C  
ANISOU  505  C   THR A  91    13641  16247  10676    849  -1080  -1670       C  
ATOM    506  O   THR A  91      15.452   9.892 -61.112  1.00111.72           O  
ANISOU  506  O   THR A  91    14219  17029  11200    765  -1041  -1739       O  
ATOM    507  CB  THR A  91      15.006   7.629 -58.729  1.00106.92           C  
ANISOU  507  CB  THR A  91    13600  16152  10872   1059  -1185  -1824       C  
ATOM    508  OG1 THR A  91      13.579   7.503 -58.683  1.00102.24           O  
ANISOU  508  OG1 THR A  91    13084  15441  10322   1086  -1219  -1703       O  
ATOM    509  CG2 THR A  91      15.623   6.997 -57.493  1.00112.23           C  
ANISOU  509  CG2 THR A  91    14252  16755  11636   1149  -1228  -1897       C  
ATOM    510  N   TYR A  92      13.478  10.009 -60.046  1.00105.36           N  
ANISOU  510  N   TYR A  92    13548  15954  10531    858  -1103  -1531       N  
ATOM    511  CA  TYR A  92      12.823  10.593 -61.208  1.00109.45           C  
ANISOU  511  CA  TYR A  92    14108  16515  10964    774  -1092  -1451       C  
ATOM    512  C   TYR A  92      13.318  12.006 -61.490  1.00112.70           C  
ANISOU  512  C   TYR A  92    14557  16982  11282    646  -1038  -1382       C  
ATOM    513  O   TYR A  92      13.367  12.418 -62.655  1.00118.85           O  
ANISOU  513  O   TYR A  92    15345  17862  11953    545  -1019  -1368       O  
ATOM    514  CB  TYR A  92      11.308  10.574 -61.010  1.00112.21           C  
ANISOU  514  CB  TYR A  92    14533  16721  11380    824  -1139  -1330       C  
ATOM    515  CG  TYR A  92      10.506  11.095 -62.181  1.00115.98           C  
ANISOU  515  CG  TYR A  92    15058  17224  11784    753  -1145  -1246       C  
ATOM    516  CD1 TYR A  92      10.633  10.532 -63.444  1.00122.57           C  
ANISOU  516  CD1 TYR A  92    15848  18181  12540    718  -1146  -1315       C  
ATOM    517  CD2 TYR A  92       9.602  12.135 -62.016  1.00119.39           C  
ANISOU  517  CD2 TYR A  92    15580  17554  12227    724  -1158  -1103       C  
ATOM    518  CE1 TYR A  92       9.892  11.003 -64.515  1.00125.59           C  
ANISOU  518  CE1 TYR A  92    16282  18585  12853    650  -1158  -1234       C  
ATOM    519  CE2 TYR A  92       8.858  12.611 -63.077  1.00124.37           C  
ANISOU  519  CE2 TYR A  92    16261  18198  12794    664  -1178  -1025       C  
ATOM    520  CZ  TYR A  92       9.005  12.043 -64.322  1.00125.00           C  
ANISOU  520  CZ  TYR A  92    16303  18399  12792    624  -1178  -1087       C  
ATOM    521  OH  TYR A  92       8.259  12.524 -65.372  1.00123.78           O  
ANISOU  521  OH  TYR A  92    16205  18256  12571    560  -1203  -1005       O  
ATOM    522  N   ALA A  93      13.694  12.762 -60.453  1.00110.32           N  
ANISOU  522  N   ALA A  93    14283  16617  11016    642  -1014  -1338       N  
ATOM    523  CA  ALA A  93      14.188  14.114 -60.695  1.00113.89           C  
ANISOU  523  CA  ALA A  93    14777  17115  11380    517   -967  -1272       C  
ATOM    524  C   ALA A  93      15.546  14.092 -61.383  1.00125.92           C  
ANISOU  524  C   ALA A  93    16224  18827  12794    427   -913  -1396       C  
ATOM    525  O   ALA A  93      15.785  14.860 -62.322  1.00126.38           O  
ANISOU  525  O   ALA A  93    16308  18979  12731    293   -883  -1362       O  
ATOM    526  CB  ALA A  93      14.261  14.894 -59.383  1.00108.76           C  
ANISOU  526  CB  ALA A  93    14171  16353  10802    539   -955  -1203       C  
ATOM    527  N   VAL A  94      16.441  13.203 -60.953  1.00134.31           N  
ANISOU  527  N   VAL A  94    17190  19949  13892    493   -905  -1547       N  
ATOM    528  CA  VAL A  94      17.776  13.183 -61.541  1.00147.82           C  
ANISOU  528  CA  VAL A  94    18813  21849  15503    411   -852  -1687       C  
ATOM    529  C   VAL A  94      17.775  12.461 -62.884  1.00148.92           C  
ANISOU  529  C   VAL A  94    18892  22126  15563    375   -857  -1778       C  
ATOM    530  O   VAL A  94      18.398  12.920 -63.846  1.00149.67           O  
ANISOU  530  O   VAL A  94    18961  22381  15524    240   -809  -1820       O  
ATOM    531  CB  VAL A  94      18.779  12.556 -60.555  1.00155.36           C  
ANISOU  531  CB  VAL A  94    19682  22816  16530    499   -851  -1825       C  
ATOM    532  CG1 VAL A  94      20.076  12.180 -61.267  1.00160.77           C  
ANISOU  532  CG1 VAL A  94    20248  23710  17128    443   -811  -2015       C  
ATOM    533  CG2 VAL A  94      19.060  13.517 -59.408  1.00154.14           C  
ANISOU  533  CG2 VAL A  94    19578  22574  16414    489   -823  -1745       C  
ATOM    534  N   HIS A  95      17.077  11.328 -62.976  1.00152.65           N  
ANISOU  534  N   HIS A  95    19343  22545  16111    487   -916  -1813       N  
ATOM    535  CA  HIS A  95      17.150  10.481 -64.162  1.00162.94           C  
ANISOU  535  CA  HIS A  95    20573  23982  17355    472   -925  -1926       C  
ATOM    536  C   HIS A  95      16.188  10.893 -65.272  1.00170.69           C  
ANISOU  536  C   HIS A  95    21624  24974  18257    389   -930  -1811       C  
ATOM    537  O   HIS A  95      16.364  10.450 -66.412  1.00183.81           O  
ANISOU  537  O   HIS A  95    23228  26777  19834    334   -921  -1897       O  
ATOM    538  CB  HIS A  95      16.890   9.024 -63.776  1.00163.87           C  
ANISOU  538  CB  HIS A  95    20634  24038  17591    631   -993  -2025       C  
ATOM    539  CG  HIS A  95      17.416   8.034 -64.766  1.00171.20           C  
ANISOU  539  CG  HIS A  95    21449  25125  18476    634  -1000  -2204       C  
ATOM    540  ND1 HIS A  95      18.576   7.320 -64.559  1.00173.59           N  
ANISOU  540  ND1 HIS A  95    21633  25475  18846    675   -990  -2368       N  
ATOM    541  CD2 HIS A  95      16.943   7.643 -65.973  1.00176.16           C  
ANISOU  541  CD2 HIS A  95    22058  25813  19061    593  -1001  -2210       C  
ATOM    542  CE1 HIS A  95      18.794   6.530 -65.595  1.00177.36           C  
ANISOU  542  CE1 HIS A  95    22020  26042  19326    662   -984  -2472       C  
ATOM    543  NE2 HIS A  95      17.819   6.708 -66.468  1.00178.45           N  
ANISOU  543  NE2 HIS A  95    22217  26191  19395    610   -988  -2378       N  
ATOM    544  N   ASN A  96      15.187  11.719 -64.972  1.00156.84           N  
ANISOU  544  N   ASN A  96    19988  23075  16527    378   -949  -1628       N  
ATOM    545  CA  ASN A  96      14.236  12.206 -65.976  1.00141.62           C  
ANISOU  545  CA  ASN A  96    18139  21141  14530    301   -966  -1510       C  
ATOM    546  C   ASN A  96      13.525  11.070 -66.712  1.00137.69           C  
ANISOU  546  C   ASN A  96    17603  20660  14051    367  -1009  -1561       C  
ATOM    547  O   ASN A  96      13.250  11.170 -67.908  1.00134.48           O  
ANISOU  547  O   ASN A  96    17209  20343  13546    280  -1008  -1545       O  
ATOM    548  CB  ASN A  96      14.919  13.127 -66.991  1.00137.11           C  
ANISOU  548  CB  ASN A  96    17579  20724  13791    115   -915  -1502       C  
ATOM    549  CG  ASN A  96      15.311  14.458 -66.402  1.00138.43           C  
ANISOU  549  CG  ASN A  96    17821  20847  13931     32   -885  -1403       C  
ATOM    550  OD1 ASN A  96      14.882  14.819 -65.306  1.00140.88           O  
ANISOU  550  OD1 ASN A  96    18184  20997  14347    111   -906  -1318       O  
ATOM    551  ND2 ASN A  96      16.123  15.208 -67.137  1.00135.89           N  
ANISOU  551  ND2 ASN A  96    17502  20669  13461   -137   -835  -1416       N  
ATOM    552  N   GLU A  97      13.214   9.984 -66.006  1.00143.83           N  
ANISOU  552  N   GLU A  97    18343  21352  14955    515  -1051  -1619       N  
ATOM    553  CA  GLU A  97      12.509   8.866 -66.627  1.00145.60           C  
ANISOU  553  CA  GLU A  97    18535  21580  15208    585  -1097  -1667       C  
ATOM    554  C   GLU A  97      11.607   8.192 -65.603  1.00130.28           C  
ANISOU  554  C   GLU A  97    16627  19460  13414    729  -1156  -1626       C  
ATOM    555  O   GLU A  97      12.065   7.843 -64.511  1.00128.47           O  
ANISOU  555  O   GLU A  97    16374  19169  13268    806  -1165  -1674       O  
ATOM    556  CB  GLU A  97      13.492   7.839 -67.210  1.00164.51           C  
ANISOU  556  CB  GLU A  97    20799  24137  17568    596  -1087  -1870       C  
ATOM    557  CG  GLU A  97      14.249   8.295 -68.454  1.00177.24           C  
ANISOU  557  CG  GLU A  97    22365  25956  19020    443  -1031  -1932       C  
ATOM    558  CD  GLU A  97      15.220   7.250 -68.972  1.00186.02           C  
ANISOU  558  CD  GLU A  97    23334  27184  20159    456  -1008  -2124       C  
ATOM    559  OE1 GLU A  97      14.777   6.126 -69.297  1.00182.57           O  
ANISOU  559  OE1 GLU A  97    22852  26728  19789    544  -1052  -2188       O  
ATOM    560  OE2 GLU A  97      16.431   7.553 -69.046  1.00198.54           O  
ANISOU  560  OE2 GLU A  97    24851  28870  21714    379   -945  -2207       O  
ATOM    561  N   TRP A  98      10.338   7.994 -65.960  1.00118.02           N  
ANISOU  561  N   TRP A  98    15128  17829  11886    759  -1196  -1540       N  
ATOM    562  CA  TRP A  98       9.398   7.316 -65.077  1.00105.64           C  
ANISOU  562  CA  TRP A  98    13591  16104  10445    880  -1250  -1504       C  
ATOM    563  C   TRP A  98       9.457   5.809 -65.293  1.00108.28           C  
ANISOU  563  C   TRP A  98    13851  16467  10826    968  -1292  -1636       C  
ATOM    564  O   TRP A  98       9.320   5.334 -66.424  1.00125.29           O  
ANISOU  564  O   TRP A  98    15966  18716  12923    946  -1298  -1689       O  
ATOM    565  CB  TRP A  98       7.970   7.811 -65.298  1.00 95.49           C  
ANISOU  565  CB  TRP A  98    12393  14717   9171    874  -1276  -1359       C  
ATOM    566  CG  TRP A  98       7.077   7.289 -64.239  1.00 96.84           C  
ANISOU  566  CG  TRP A  98    12596  14734   9464    978  -1320  -1322       C  
ATOM    567  CD1 TRP A  98       6.163   6.281 -64.349  1.00 88.53           C  
ANISOU  567  CD1 TRP A  98    11540  13629   8468   1052  -1367  -1337       C  
ATOM    568  CD2 TRP A  98       7.056   7.709 -62.874  1.00107.96           C  
ANISOU  568  CD2 TRP A  98    14042  16029  10951   1012  -1317  -1270       C  
ATOM    569  NE1 TRP A  98       5.552   6.067 -63.137  1.00 93.72           N  
ANISOU  569  NE1 TRP A  98    12235  14148   9227   1121  -1394  -1295       N  
ATOM    570  CE2 TRP A  98       6.085   6.931 -62.214  1.00106.64           C  
ANISOU  570  CE2 TRP A  98    13894  15746  10878   1098  -1364  -1255       C  
ATOM    571  CE3 TRP A  98       7.756   8.678 -62.145  1.00105.14           C  
ANISOU  571  CE3 TRP A  98    13702  15658  10588    972  -1279  -1237       C  
ATOM    572  CZ2 TRP A  98       5.801   7.088 -60.858  1.00103.24           C  
ANISOU  572  CZ2 TRP A  98    13499  15196  10531   1139  -1372  -1210       C  
ATOM    573  CZ3 TRP A  98       7.469   8.836 -60.805  1.00 98.23           C  
ANISOU  573  CZ3 TRP A  98    12860  14660   9803   1022  -1288  -1191       C  
ATOM    574  CH2 TRP A  98       6.497   8.047 -60.175  1.00 98.14           C  
ANISOU  574  CH2 TRP A  98    12867  14542   9880   1102  -1334  -1179       C  
ATOM    575  N   TYR A  99       9.626   5.058 -64.202  1.00 93.69           N  
ANISOU  575  N   TYR A  99    11988  14530   9081   1066  -1328  -1687       N  
ATOM    576  CA  TYR A  99       9.814   3.615 -64.278  1.00 99.51           C  
ANISOU  576  CA  TYR A  99    12660  15280   9871   1155  -1383  -1821       C  
ATOM    577  C   TYR A  99       8.749   2.794 -63.562  1.00112.32           C  
ANISOU  577  C   TYR A  99    14331  16746  11598   1249  -1449  -1775       C  
ATOM    578  O   TYR A  99       8.805   1.559 -63.623  1.00115.85           O  
ANISOU  578  O   TYR A  99    14737  17186  12094   1323  -1507  -1877       O  
ATOM    579  CB  TYR A  99      11.190   3.243 -63.709  1.00105.58           C  
ANISOU  579  CB  TYR A  99    13355  16098  10663   1188  -1385  -1959       C  
ATOM    580  CG  TYR A  99      12.328   3.748 -64.551  1.00123.08           C  
ANISOU  580  CG  TYR A  99    15495  18498  12771   1098  -1324  -2051       C  
ATOM    581  CD1 TYR A  99      12.286   3.630 -65.932  1.00141.11           C  
ANISOU  581  CD1 TYR A  99    17734  20920  14963   1036  -1305  -2099       C  
ATOM    582  CD2 TYR A  99      13.438   4.353 -63.973  1.00127.47           C  
ANISOU  582  CD2 TYR A  99    16025  19098  13310   1066  -1284  -2091       C  
ATOM    583  CE1 TYR A  99      13.315   4.089 -66.720  1.00151.38           C  
ANISOU  583  CE1 TYR A  99    18963  22402  16152    936  -1246  -2188       C  
ATOM    584  CE2 TYR A  99      14.478   4.819 -64.754  1.00140.64           C  
ANISOU  584  CE2 TYR A  99    17620  20946  14870    970  -1224  -2182       C  
ATOM    585  CZ  TYR A  99      14.409   4.683 -66.128  1.00154.44           C  
ANISOU  585  CZ  TYR A  99    19323  22833  16522    901  -1204  -2231       C  
ATOM    586  OH  TYR A  99      15.436   5.140 -66.920  1.00163.49           O  
ANISOU  586  OH  TYR A  99    20397  24132  17590    782  -1127  -2299       O  
ATOM    587  N   TYR A 100       7.779   3.427 -62.899  1.00117.87           N  
ANISOU  587  N   TYR A 100    15121  17328  12337   1244  -1446  -1634       N  
ATOM    588  CA  TYR A 100       6.993   2.758 -61.865  1.00109.09           C  
ANISOU  588  CA  TYR A 100    14056  16069  11326   1319  -1500  -1598       C  
ATOM    589  C   TYR A 100       5.509   2.630 -62.197  1.00100.07           C  
ANISOU  589  C   TYR A 100    12965  14860  10198   1326  -1521  -1511       C  
ATOM    590  O   TYR A 100       4.729   2.215 -61.329  1.00101.57           O  
ANISOU  590  O   TYR A 100    13200  14931  10461   1369  -1558  -1469       O  
ATOM    591  CB  TYR A 100       7.185   3.488 -60.530  1.00 97.08           C  
ANISOU  591  CB  TYR A 100    12580  14457   9848   1315  -1481  -1530       C  
ATOM    592  CG  TYR A 100       8.618   3.934 -60.304  1.00 98.13           C  
ANISOU  592  CG  TYR A 100    12668  14668   9951   1289  -1444  -1598       C  
ATOM    593  CD1 TYR A 100       9.564   3.065 -59.772  1.00100.81           C  
ANISOU  593  CD1 TYR A 100    12959  15011  10334   1349  -1483  -1718       C  
ATOM    594  CD2 TYR A 100       9.026   5.224 -60.643  1.00107.29           C  
ANISOU  594  CD2 TYR A 100    13832  15896  11036   1203  -1377  -1546       C  
ATOM    595  CE1 TYR A 100      10.875   3.469 -59.574  1.00103.76           C  
ANISOU  595  CE1 TYR A 100    13282  15461  10680   1328  -1450  -1792       C  
ATOM    596  CE2 TYR A 100      10.334   5.637 -60.451  1.00111.29           C  
ANISOU  596  CE2 TYR A 100    14295  16482  11510   1172  -1339  -1613       C  
ATOM    597  CZ  TYR A 100      11.254   4.758 -59.915  1.00106.93           C  
ANISOU  597  CZ  TYR A 100    13686  15940  11003   1236  -1372  -1740       C  
ATOM    598  OH  TYR A 100      12.553   5.170 -59.723  1.00102.71           O  
ANISOU  598  OH  TYR A 100    13100  15489  10437   1208  -1335  -1816       O  
ATOM    599  N   GLY A 101       5.091   2.977 -63.413  1.00 83.67           N  
ANISOU  599  N   GLY A 101    10882  12860   8051   1279  -1501  -1486       N  
ATOM    600  CA  GLY A 101       3.734   2.728 -63.852  1.00 82.94           C  
ANISOU  600  CA  GLY A 101    10825  12719   7971   1293  -1528  -1425       C  
ATOM    601  C   GLY A 101       2.761   3.853 -63.530  1.00 90.27           C  
ANISOU  601  C   GLY A 101    11825  13569   8905   1260  -1511  -1288       C  
ATOM    602  O   GLY A 101       3.041   4.781 -62.765  1.00 97.98           O  
ANISOU  602  O   GLY A 101    12831  14506   9891   1234  -1483  -1232       O  
ATOM    603  N   LEU A 102       1.571   3.742 -64.131  1.00 93.73           N  
ANISOU  603  N   LEU A 102    12287  13984   9341   1265  -1533  -1242       N  
ATOM    604  CA  LEU A 102       0.557   4.782 -63.987  1.00100.96           C  
ANISOU  604  CA  LEU A 102    13263  14831  10264   1240  -1530  -1127       C  
ATOM    605  C   LEU A 102       0.072   4.892 -62.546  1.00119.80           C  
ANISOU  605  C   LEU A 102    15684  17097  12737   1273  -1537  -1087       C  
ATOM    606  O   LEU A 102      -0.049   6.000 -62.001  1.00131.32           O  
ANISOU  606  O   LEU A 102    17179  18510  14206   1246  -1518  -1015       O  
ATOM    607  CB  LEU A 102      -0.620   4.492 -64.919  1.00 95.88           C  
ANISOU  607  CB  LEU A 102    12631  14191   9608   1249  -1560  -1104       C  
ATOM    608  CG  LEU A 102      -1.892   5.281 -64.597  1.00101.11           C  
ANISOU  608  CG  LEU A 102    13348  14761  10307   1250  -1576  -1007       C  
ATOM    609  CD1 LEU A 102      -1.790   6.699 -65.135  1.00104.30           C  
ANISOU  609  CD1 LEU A 102    13790  15188  10653   1185  -1564   -928       C  
ATOM    610  CD2 LEU A 102      -3.140   4.580 -65.116  1.00107.30           C  
ANISOU  610  CD2 LEU A 102    14133  15525  11111   1286  -1614  -1011       C  
ATOM    611  N   PHE A 103      -0.189   3.747 -61.906  1.00117.35           N  
ANISOU  611  N   PHE A 103    15366  16734  12488   1327  -1568  -1136       N  
ATOM    612  CA  PHE A 103      -0.721   3.762 -60.548  1.00110.53           C  
ANISOU  612  CA  PHE A 103    14537  15764  11697   1345  -1576  -1102       C  
ATOM    613  C   PHE A 103       0.216   4.507 -59.610  1.00106.30           C  
ANISOU  613  C   PHE A 103    14007  15211  11171   1325  -1543  -1087       C  
ATOM    614  O   PHE A 103      -0.205   5.406 -58.869  1.00101.03           O  
ANISOU  614  O   PHE A 103    13371  14485  10530   1306  -1526  -1022       O  
ATOM    615  CB  PHE A 103      -0.946   2.328 -60.060  1.00113.56           C  
ANISOU  615  CB  PHE A 103    14918  16101  12130   1391  -1621  -1162       C  
ATOM    616  CG  PHE A 103      -1.344   2.235 -58.611  1.00114.51           C  
ANISOU  616  CG  PHE A 103    15074  16121  12312   1394  -1630  -1135       C  
ATOM    617  CD1 PHE A 103      -2.660   2.435 -58.227  1.00110.39           C  
ANISOU  617  CD1 PHE A 103    14581  15541  11820   1384  -1634  -1085       C  
ATOM    618  CD2 PHE A 103      -0.404   1.943 -57.633  1.00111.85           C  
ANISOU  618  CD2 PHE A 103    14741  15754  12001   1402  -1637  -1167       C  
ATOM    619  CE1 PHE A 103      -3.032   2.352 -56.900  1.00103.15           C  
ANISOU  619  CE1 PHE A 103    13695  14547  10952   1372  -1638  -1067       C  
ATOM    620  CE2 PHE A 103      -0.771   1.859 -56.302  1.00105.53           C  
ANISOU  620  CE2 PHE A 103    13979  14868  11250   1393  -1646  -1140       C  
ATOM    621  CZ  PHE A 103      -2.088   2.063 -55.937  1.00104.82           C  
ANISOU  621  CZ  PHE A 103    13916  14729  11183   1373  -1644  -1090       C  
ATOM    622  N   TYR A 104       1.503   4.170 -59.653  1.00110.12           N  
ANISOU  622  N   TYR A 104    14455  15751  11633   1329  -1536  -1155       N  
ATOM    623  CA  TYR A 104       2.449   4.856 -58.792  1.00117.22           C  
ANISOU  623  CA  TYR A 104    15357  16642  12539   1310  -1504  -1148       C  
ATOM    624  C   TYR A 104       2.756   6.277 -59.254  1.00113.26           C  
ANISOU  624  C   TYR A 104    14865  16188  11982   1249  -1457  -1088       C  
ATOM    625  O   TYR A 104       3.262   7.069 -58.456  1.00121.43           O  
ANISOU  625  O   TYR A 104    15913  17198  13028   1228  -1428  -1059       O  
ATOM    626  CB  TYR A 104       3.745   4.057 -58.661  1.00132.86           C  
ANISOU  626  CB  TYR A 104    17293  18669  14518   1336  -1516  -1251       C  
ATOM    627  CG  TYR A 104       4.563   4.547 -57.496  1.00149.40           C  
ANISOU  627  CG  TYR A 104    19395  20729  16639   1330  -1495  -1247       C  
ATOM    628  CD1 TYR A 104       4.219   4.210 -56.192  1.00150.48           C  
ANISOU  628  CD1 TYR A 104    19570  20762  16845   1354  -1520  -1226       C  
ATOM    629  CD2 TYR A 104       5.646   5.387 -57.693  1.00158.31           C  
ANISOU  629  CD2 TYR A 104    20498  21932  17719   1291  -1448  -1260       C  
ATOM    630  CE1 TYR A 104       4.948   4.679 -55.121  1.00156.91           C  
ANISOU  630  CE1 TYR A 104    20392  21546  17682   1346  -1501  -1220       C  
ATOM    631  CE2 TYR A 104       6.375   5.862 -56.632  1.00158.33           C  
ANISOU  631  CE2 TYR A 104    20507  21905  17747   1285  -1427  -1256       C  
ATOM    632  CZ  TYR A 104       6.028   5.503 -55.348  1.00162.51           C  
ANISOU  632  CZ  TYR A 104    21070  22328  18347   1316  -1454  -1235       C  
ATOM    633  OH  TYR A 104       6.762   5.975 -54.286  1.00171.56           O  
ANISOU  633  OH  TYR A 104    22222  23447  19516   1309  -1434  -1232       O  
ATOM    634  N   CYS A 105       2.487   6.629 -60.514  1.00105.88           N  
ANISOU  634  N   CYS A 105    13927  15318  10982   1215  -1452  -1068       N  
ATOM    635  CA  CYS A 105       2.583   8.043 -60.870  1.00105.19           C  
ANISOU  635  CA  CYS A 105    13871  15251  10846   1150  -1423   -992       C  
ATOM    636  C   CYS A 105       1.493   8.848 -60.172  1.00102.98           C  
ANISOU  636  C   CYS A 105    13643  14864  10622   1156  -1435   -902       C  
ATOM    637  O   CYS A 105       1.758   9.925 -59.609  1.00107.65           O  
ANISOU  637  O   CYS A 105    14259  15423  11219   1125  -1414   -851       O  
ATOM    638  CB  CYS A 105       2.517   8.208 -62.392  1.00105.74           C  
ANISOU  638  CB  CYS A 105    13936  15414  10828   1103  -1426   -987       C  
ATOM    639  SG  CYS A 105       2.213   9.893 -63.012  1.00112.97           S  
ANISOU  639  SG  CYS A 105    14916  16326  11681   1019  -1421   -871       S  
ATOM    640  N   LYS A 106       0.279   8.295 -60.117  1.00 96.75           N  
ANISOU  640  N   LYS A 106    12863  14019   9879   1198  -1470   -894       N  
ATOM    641  CA  LYS A 106      -0.802   8.970 -59.408  1.00 97.00           C  
ANISOU  641  CA  LYS A 106    12929  13957   9970   1207  -1484   -832       C  
ATOM    642  C   LYS A 106      -0.536   9.025 -57.910  1.00107.79           C  
ANISOU  642  C   LYS A 106    14296  15260  11399   1220  -1465   -837       C  
ATOM    643  O   LYS A 106      -0.701  10.079 -57.284  1.00117.19           O  
ANISOU  643  O   LYS A 106    15508  16404  12617   1203  -1454   -788       O  
ATOM    644  CB  LYS A 106      -2.138   8.288 -59.692  1.00 98.21           C  
ANISOU  644  CB  LYS A 106    13083  14078  10154   1244  -1522   -837       C  
ATOM    645  CG  LYS A 106      -2.612   8.399 -61.134  1.00 97.39           C  
ANISOU  645  CG  LYS A 106    12985  14024   9995   1231  -1546   -819       C  
ATOM    646  CD  LYS A 106      -3.996   7.782 -61.300  1.00 93.22           C  
ANISOU  646  CD  LYS A 106    12456  13458   9505   1270  -1583   -826       C  
ATOM    647  CE  LYS A 106      -4.527   7.974 -62.707  1.00 95.07           C  
ANISOU  647  CE  LYS A 106    12701  13737   9686   1258  -1612   -803       C  
ATOM    648  NZ  LYS A 106      -4.727   9.425 -62.998  1.00 93.28           N  
ANISOU  648  NZ  LYS A 106    12516  13485   9442   1223  -1629   -727       N  
ATOM    649  N   PHE A 107      -0.142   7.900 -57.308  1.00104.67           N  
ANISOU  649  N   PHE A 107    13880  14860  11029   1250  -1469   -898       N  
ATOM    650  CA  PHE A 107       0.151   7.922 -55.877  1.00 91.76           C  
ANISOU  650  CA  PHE A 107    12252  13167   9446   1254  -1455   -901       C  
ATOM    651  C   PHE A 107       1.322   8.847 -55.570  1.00 85.65           C  
ANISOU  651  C   PHE A 107    11475  12418   8650   1224  -1416   -888       C  
ATOM    652  O   PHE A 107       1.313   9.556 -54.559  1.00 94.46           O  
ANISOU  652  O   PHE A 107    12605  13483   9802   1212  -1398   -856       O  
ATOM    653  CB  PHE A 107       0.440   6.504 -55.379  1.00 85.09           C  
ANISOU  653  CB  PHE A 107    11396  12309   8625   1287  -1482   -968       C  
ATOM    654  CG  PHE A 107       0.726   6.418 -53.903  1.00 85.75           C  
ANISOU  654  CG  PHE A 107    11494  12330   8755   1285  -1478   -970       C  
ATOM    655  CD1 PHE A 107      -0.308   6.314 -52.988  1.00 81.76           C  
ANISOU  655  CD1 PHE A 107    11013  11756   8298   1278  -1488   -946       C  
ATOM    656  CD2 PHE A 107       2.033   6.421 -53.433  1.00 87.78           C  
ANISOU  656  CD2 PHE A 107    11739  12605   9007   1286  -1465  -1003       C  
ATOM    657  CE1 PHE A 107      -0.046   6.224 -51.636  1.00 81.23           C  
ANISOU  657  CE1 PHE A 107    10962  11638   8264   1264  -1485   -947       C  
ATOM    658  CE2 PHE A 107       2.299   6.334 -52.080  1.00 77.05           C  
ANISOU  658  CE2 PHE A 107    10398  11188   7688   1282  -1466  -1002       C  
ATOM    659  CZ  PHE A 107       1.259   6.233 -51.184  1.00 76.43           C  
ANISOU  659  CZ  PHE A 107    10349  11041   7652   1268  -1476   -971       C  
ATOM    660  N   HIS A 108       2.323   8.881 -56.450  1.00 80.47           N  
ANISOU  660  N   HIS A 108    10798  11847   7931   1205  -1401   -918       N  
ATOM    661  CA  HIS A 108       3.476   9.747 -56.234  1.00 90.56           C  
ANISOU  661  CA  HIS A 108    12070  13161   9178   1167  -1360   -912       C  
ATOM    662  C   HIS A 108       3.095  11.220 -56.273  1.00 93.52           C  
ANISOU  662  C   HIS A 108    12482  13507   9545   1123  -1346   -826       C  
ATOM    663  O   HIS A 108       3.718  12.035 -55.584  1.00 81.00           O  
ANISOU  663  O   HIS A 108    10903  11906   7966   1098  -1316   -805       O  
ATOM    664  CB  HIS A 108       4.561   9.447 -57.272  1.00101.12           C  
ANISOU  664  CB  HIS A 108    13369  14611  10439   1145  -1346   -974       C  
ATOM    665  CG  HIS A 108       5.512  10.581 -57.499  1.00111.12           C  
ANISOU  665  CG  HIS A 108    14639  15936  11647   1079  -1302   -952       C  
ATOM    666  ND1 HIS A 108       5.472  11.368 -58.630  1.00117.25           N  
ANISOU  666  ND1 HIS A 108    15434  16769  12346   1015  -1293   -909       N  
ATOM    667  CD2 HIS A 108       6.523  11.065 -56.739  1.00119.23           C  
ANISOU  667  CD2 HIS A 108    15656  16971  12677   1061  -1267   -966       C  
ATOM    668  CE1 HIS A 108       6.419  12.286 -58.558  1.00128.25           C  
ANISOU  668  CE1 HIS A 108    16831  18204  13694    954  -1254   -896       C  
ATOM    669  NE2 HIS A 108       7.070  12.125 -57.420  1.00130.40           N  
ANISOU  669  NE2 HIS A 108    17082  18449  14015    984  -1235   -933       N  
ATOM    670  N   ASN A 109       2.095  11.590 -57.069  1.00103.99           N  
ANISOU  670  N   ASN A 109    13833  14820  10859   1115  -1372   -778       N  
ATOM    671  CA  ASN A 109       1.620  12.968 -57.028  1.00101.71           C  
ANISOU  671  CA  ASN A 109    13585  14483  10577   1084  -1379   -699       C  
ATOM    672  C   ASN A 109       0.456  13.179 -56.062  1.00 91.22           C  
ANISOU  672  C   ASN A 109    12266  13056   9336   1121  -1400   -676       C  
ATOM    673  O   ASN A 109      -0.016  14.311 -55.922  1.00 90.50           O  
ANISOU  673  O   ASN A 109    12204  12915   9268   1106  -1415   -622       O  
ATOM    674  CB  ASN A 109       1.234  13.440 -58.434  1.00105.66           C  
ANISOU  674  CB  ASN A 109    14114  15019  11013   1048  -1407   -656       C  
ATOM    675  CG  ASN A 109       2.446  13.691 -59.317  1.00102.14           C  
ANISOU  675  CG  ASN A 109    13665  14675  10468    980  -1379   -666       C  
ATOM    676  OD1 ASN A 109       3.444  14.260 -58.874  1.00104.14           O  
ANISOU  676  OD1 ASN A 109    13918  14949  10702    943  -1342   -665       O  
ATOM    677  ND2 ASN A 109       2.365  13.264 -60.570  1.00102.72           N  
ANISOU  677  ND2 ASN A 109    13735  14821  10474    959  -1394   -679       N  
ATOM    678  N   PHE A 110      -0.017  12.131 -55.390  1.00 93.42           N  
ANISOU  678  N   PHE A 110    12524  13309   9663   1163  -1406   -720       N  
ATOM    679  CA  PHE A 110      -1.187  12.224 -54.524  1.00 95.71           C  
ANISOU  679  CA  PHE A 110    12815  13524  10026   1186  -1422   -712       C  
ATOM    680  C   PHE A 110      -0.845  12.197 -53.043  1.00 95.56           C  
ANISOU  680  C   PHE A 110    12786  13466  10055   1185  -1394   -729       C  
ATOM    681  O   PHE A 110      -1.298  13.063 -52.289  1.00 95.44           O  
ANISOU  681  O   PHE A 110    12775  13402  10086   1178  -1390   -706       O  
ATOM    682  CB  PHE A 110      -2.160  11.079 -54.844  1.00 91.42           C  
ANISOU  682  CB  PHE A 110    12260  12979   9495   1218  -1452   -747       C  
ATOM    683  CG  PHE A 110      -3.238  10.894 -53.814  1.00 82.97           C  
ANISOU  683  CG  PHE A 110    11183  11850   8492   1231  -1461   -760       C  
ATOM    684  CD1 PHE A 110      -4.280  11.799 -53.711  1.00 80.49           C  
ANISOU  684  CD1 PHE A 110    10869  11495   8217   1234  -1480   -738       C  
ATOM    685  CD2 PHE A 110      -3.215   9.810 -52.957  1.00 80.38           C  
ANISOU  685  CD2 PHE A 110    10847  11509   8184   1234  -1456   -802       C  
ATOM    686  CE1 PHE A 110      -5.276  11.630 -52.770  1.00 78.23           C  
ANISOU  686  CE1 PHE A 110    10565  11171   7987   1238  -1483   -766       C  
ATOM    687  CE2 PHE A 110      -4.208   9.639 -52.015  1.00 84.82           C  
ANISOU  687  CE2 PHE A 110    11404  12030   8796   1228  -1460   -817       C  
ATOM    688  CZ  PHE A 110      -5.241  10.554 -51.924  1.00 83.07           C  
ANISOU  688  CZ  PHE A 110    11171  11782   8610   1228  -1468   -805       C  
ATOM    689  N   PHE A 111      -0.066  11.205 -52.610  1.00 91.77           N  
ANISOU  689  N   PHE A 111    12295  13007   9568   1193  -1382   -774       N  
ATOM    690  CA  PHE A 111       0.186  10.995 -51.183  1.00 91.11           C  
ANISOU  690  CA  PHE A 111    12208  12882   9526   1190  -1366   -791       C  
ATOM    691  C   PHE A 111       0.788  12.203 -50.467  1.00 84.05           C  
ANISOU  691  C   PHE A 111    11316  11972   8646   1165  -1331   -761       C  
ATOM    692  O   PHE A 111       0.305  12.539 -49.372  1.00 80.94           O  
ANISOU  692  O   PHE A 111    10921  11532   8302   1156  -1322   -755       O  
ATOM    693  CB  PHE A 111       1.061   9.750 -51.003  1.00 92.98           C  
ANISOU  693  CB  PHE A 111    12439  13141   9748   1205  -1374   -845       C  
ATOM    694  CG  PHE A 111       1.063   9.202 -49.601  1.00 93.67           C  
ANISOU  694  CG  PHE A 111    12537  13178   9877   1201  -1379   -863       C  
ATOM    695  CD1 PHE A 111      -0.124   8.879 -48.967  1.00 94.48           C  
ANISOU  695  CD1 PHE A 111    12650  13234  10014   1189  -1394   -858       C  
ATOM    696  CD2 PHE A 111       2.251   8.996 -48.924  1.00 90.26           C  
ANISOU  696  CD2 PHE A 111    12103  12748   9443   1201  -1370   -888       C  
ATOM    697  CE1 PHE A 111      -0.123   8.374 -47.683  1.00 92.13           C  
ANISOU  697  CE1 PHE A 111    12368  12896   9743   1168  -1400   -871       C  
ATOM    698  CE2 PHE A 111       2.256   8.489 -47.641  1.00 93.14           C  
ANISOU  698  CE2 PHE A 111    12486  13062   9840   1190  -1383   -899       C  
ATOM    699  CZ  PHE A 111       1.069   8.178 -47.021  1.00 94.38           C  
ANISOU  699  CZ  PHE A 111    12660  13176  10025   1168  -1397   -887       C  
ATOM    700  N   PRO A 112       1.821  12.881 -50.989  1.00 76.60           N  
ANISOU  700  N   PRO A 112    10374  11070   7659   1146  -1308   -746       N  
ATOM    701  CA  PRO A 112       2.497  13.911 -50.179  1.00 70.75           C  
ANISOU  701  CA  PRO A 112     9635  10312   6933   1121  -1274   -723       C  
ATOM    702  C   PRO A 112       1.589  15.022 -49.673  1.00 72.93           C  
ANISOU  702  C   PRO A 112     9921  10529   7260   1113  -1278   -682       C  
ATOM    703  O   PRO A 112       1.785  15.488 -48.544  1.00 79.74           O  
ANISOU  703  O   PRO A 112    10777  11360   8162   1103  -1255   -681       O  
ATOM    704  CB  PRO A 112       3.561  14.459 -51.133  1.00 67.62           C  
ANISOU  704  CB  PRO A 112     9243   9980   6468   1091  -1255   -712       C  
ATOM    705  CG  PRO A 112       3.869  13.323 -52.014  1.00 73.17           C  
ANISOU  705  CG  PRO A 112     9930  10745   7127   1108  -1269   -760       C  
ATOM    706  CD  PRO A 112       2.563  12.624 -52.239  1.00 79.00           C  
ANISOU  706  CD  PRO A 112    10673  11449   7895   1139  -1308   -760       C  
ATOM    707  N   ILE A 113       0.579  15.434 -50.447  1.00 70.75           N  
ANISOU  707  N   ILE A 113     9657  10237   6989   1120  -1314   -655       N  
ATOM    708  CA  ILE A 113      -0.338  16.461 -49.958  1.00 80.75           C  
ANISOU  708  CA  ILE A 113    10924  11443   8314   1122  -1331   -633       C  
ATOM    709  C   ILE A 113      -1.086  15.957 -48.730  1.00 88.02           C  
ANISOU  709  C   ILE A 113    11817  12332   9295   1133  -1324   -674       C  
ATOM    710  O   ILE A 113      -1.136  16.625 -47.688  1.00 89.21           O  
ANISOU  710  O   ILE A 113    11954  12451   9491   1122  -1306   -678       O  
ATOM    711  CB  ILE A 113      -1.314  16.889 -51.069  1.00 84.07           C  
ANISOU  711  CB  ILE A 113    11363  11849   8732   1134  -1384   -606       C  
ATOM    712  CG1 ILE A 113      -0.603  17.737 -52.123  1.00 86.38           C  
ANISOU  712  CG1 ILE A 113    11695  12162   8963   1102  -1396   -552       C  
ATOM    713  CG2 ILE A 113      -2.493  17.649 -50.470  1.00 90.43           C  
ANISOU  713  CG2 ILE A 113    12155  12591   9614   1153  -1415   -612       C  
ATOM    714  CD1 ILE A 113      -1.418  17.961 -53.385  1.00 96.74           C  
ANISOU  714  CD1 ILE A 113    13036  13468  10254   1108  -1455   -523       C  
ATOM    715  N   ALA A 114      -1.650  14.750 -48.825  1.00 84.55           N  
ANISOU  715  N   ALA A 114    11368  11905   8851   1147  -1337   -707       N  
ATOM    716  CA  ALA A 114      -2.402  14.198 -47.706  1.00 79.59           C  
ANISOU  716  CA  ALA A 114    10720  11254   8265   1140  -1331   -746       C  
ATOM    717  C   ALA A 114      -1.509  13.988 -46.489  1.00 81.15           C  
ANISOU  717  C   ALA A 114    10917  11449   8469   1116  -1295   -758       C  
ATOM    718  O   ALA A 114      -1.946  14.188 -45.350  1.00 81.78           O  
ANISOU  718  O   ALA A 114    10979  11506   8587   1093  -1280   -776       O  
ATOM    719  CB  ALA A 114      -3.062  12.884 -48.121  1.00 78.18           C  
ANISOU  719  CB  ALA A 114    10543  11091   8071   1151  -1356   -775       C  
ATOM    720  N   ALA A 115      -0.246  13.618 -46.709  1.00 85.04           N  
ANISOU  720  N   ALA A 115    11424  11967   8920   1118  -1282   -753       N  
ATOM    721  CA  ALA A 115       0.653  13.399 -45.581  1.00 77.76           C  
ANISOU  721  CA  ALA A 115    10503  11038   8003   1099  -1256   -766       C  
ATOM    722  C   ALA A 115       0.976  14.711 -44.877  1.00 76.82           C  
ANISOU  722  C   ALA A 115    10374  10903   7912   1081  -1223   -745       C  
ATOM    723  O   ALA A 115       0.920  14.799 -43.640  1.00 83.07           O  
ANISOU  723  O   ALA A 115    11155  11673   8734   1057  -1204   -758       O  
ATOM    724  CB  ALA A 115       1.931  12.706 -46.054  1.00 68.64           C  
ANISOU  724  CB  ALA A 115     9357   9919   6802   1114  -1257   -782       C  
ATOM    725  N   ILE A 116       1.285  15.755 -45.653  1.00 74.25           N  
ANISOU  725  N   ILE A 116    10052  10586   7574   1085  -1219   -711       N  
ATOM    726  CA  ILE A 116       1.571  17.050 -45.043  1.00 78.55           C  
ANISOU  726  CA  ILE A 116    10590  11107   8147   1067  -1194   -689       C  
ATOM    727  C   ILE A 116       0.350  17.558 -44.291  1.00 91.51           C  
ANISOU  727  C   ILE A 116    12208  12708   9853   1065  -1204   -704       C  
ATOM    728  O   ILE A 116       0.466  18.115 -43.191  1.00 96.57           O  
ANISOU  728  O   ILE A 116    12830  13331  10530   1047  -1178   -714       O  
ATOM    729  CB  ILE A 116       2.029  18.060 -46.111  1.00 70.46           C  
ANISOU  729  CB  ILE A 116     9587  10093   7092   1062  -1201   -645       C  
ATOM    730  CG1 ILE A 116       3.285  17.563 -46.820  1.00 70.50           C  
ANISOU  730  CG1 ILE A 116     9603  10157   7026   1053  -1183   -648       C  
ATOM    731  CG2 ILE A 116       2.273  19.419 -45.483  1.00 68.82           C  
ANISOU  731  CG2 ILE A 116     9379   9852   6919   1043  -1185   -622       C  
ATOM    732  CD1 ILE A 116       4.326  17.035 -45.881  1.00 87.75           C  
ANISOU  732  CD1 ILE A 116    11773  12359   9208   1049  -1149   -681       C  
ATOM    733  N   PHE A 117      -0.842  17.321 -44.845  1.00 92.16           N  
ANISOU  733  N   PHE A 117    12284  12783   9950   1083  -1241   -715       N  
ATOM    734  CA  PHE A 117      -2.065  17.754 -44.179  1.00 87.32           C  
ANISOU  734  CA  PHE A 117    11637  12143   9399   1082  -1253   -749       C  
ATOM    735  C   PHE A 117      -2.258  17.014 -42.861  1.00 90.40           C  
ANISOU  735  C   PHE A 117    12005  12541   9801   1048  -1224   -792       C  
ATOM    736  O   PHE A 117      -2.574  17.627 -41.831  1.00 94.51           O  
ANISOU  736  O   PHE A 117    12493  13051  10366   1027  -1205   -819       O  
ATOM    737  CB  PHE A 117      -3.253  17.527 -45.114  1.00 80.64           C  
ANISOU  737  CB  PHE A 117    10787  11294   8560   1109  -1300   -760       C  
ATOM    738  CG  PHE A 117      -4.542  18.124 -44.632  1.00 73.40           C  
ANISOU  738  CG  PHE A 117     9826  10355   7709   1116  -1322   -807       C  
ATOM    739  CD1 PHE A 117      -5.375  17.415 -43.782  1.00 75.61           C  
ANISOU  739  CD1 PHE A 117    10069  10653   8007   1091  -1308   -867       C  
ATOM    740  CD2 PHE A 117      -4.931  19.386 -45.046  1.00 68.78           C  
ANISOU  740  CD2 PHE A 117     9236   9731   7166   1144  -1363   -797       C  
ATOM    741  CE1 PHE A 117      -6.565  17.956 -43.345  1.00 81.71           C  
ANISOU  741  CE1 PHE A 117    10788  11420   8839   1094  -1326   -928       C  
ATOM    742  CE2 PHE A 117      -6.122  19.936 -44.615  1.00 75.91           C  
ANISOU  742  CE2 PHE A 117    10088  10615   8138   1158  -1392   -857       C  
ATOM    743  CZ  PHE A 117      -6.941  19.220 -43.762  1.00 82.54           C  
ANISOU  743  CZ  PHE A 117    10879  11487   8996   1134  -1369   -929       C  
ATOM    744  N   ALA A 118      -2.032  15.698 -42.864  1.00 86.81           N  
ANISOU  744  N   ALA A 118    11571  12107   9307   1038  -1224   -800       N  
ATOM    745  CA  ALA A 118      -2.244  14.916 -41.652  1.00 82.27           C  
ANISOU  745  CA  ALA A 118    10991  11535   8734    993  -1208   -834       C  
ATOM    746  C   ALA A 118      -1.258  15.303 -40.560  1.00 84.01           C  
ANISOU  746  C   ALA A 118    11212  11750   8959    966  -1172   -827       C  
ATOM    747  O   ALA A 118      -1.633  15.392 -39.382  1.00 96.19           O  
ANISOU  747  O   ALA A 118    12734  13293  10523    921  -1151   -855       O  
ATOM    748  CB  ALA A 118      -2.138  13.425 -41.967  1.00 82.40           C  
ANISOU  748  CB  ALA A 118    11041  11561   8706    990  -1231   -838       C  
ATOM    749  N   SER A 119      -0.002  15.576 -40.928  1.00 76.15           N  
ANISOU  749  N   SER A 119    10236  10756   7941    987  -1161   -794       N  
ATOM    750  CA  SER A 119       0.983  15.903 -39.900  1.00 81.74           C  
ANISOU  750  CA  SER A 119    10944  11461   8652    964  -1127   -791       C  
ATOM    751  C   SER A 119       0.774  17.316 -39.367  1.00 88.89           C  
ANISOU  751  C   SER A 119    11815  12353   9605    955  -1101   -790       C  
ATOM    752  O   SER A 119       0.760  17.529 -38.149  1.00 94.74           O  
ANISOU  752  O   SER A 119    12537  13091  10367    919  -1075   -811       O  
ATOM    753  CB  SER A 119       2.406  15.731 -40.435  1.00 78.78           C  
ANISOU  753  CB  SER A 119    10594  11101   8239    988  -1122   -771       C  
ATOM    754  OG  SER A 119       2.900  16.943 -40.972  1.00 86.15           O  
ANISOU  754  OG  SER A 119    11519  12039   9175   1001  -1104   -743       O  
ATOM    755  N   ILE A 120       0.601  18.299 -40.259  1.00 83.11           N  
ANISOU  755  N   ILE A 120    11079  11611   8889    985  -1114   -768       N  
ATOM    756  CA  ILE A 120       0.462  19.673 -39.782  1.00 69.16           C  
ANISOU  756  CA  ILE A 120     9284   9821   7172    982  -1102   -769       C  
ATOM    757  C   ILE A 120      -0.835  19.854 -39.006  1.00 69.07           C  
ANISOU  757  C   ILE A 120     9225   9804   7213    966  -1107   -823       C  
ATOM    758  O   ILE A 120      -0.888  20.641 -38.053  1.00 77.38           O  
ANISOU  758  O   ILE A 120    10242  10849   8308    947  -1085   -847       O  
ATOM    759  CB  ILE A 120       0.576  20.685 -40.939  1.00 60.14           C  
ANISOU  759  CB  ILE A 120     8160   8658   6031   1011  -1129   -728       C  
ATOM    760  CG1 ILE A 120       0.744  22.098 -40.384  1.00 53.71           C  
ANISOU  760  CG1 ILE A 120     7329   7813   5266   1006  -1121   -723       C  
ATOM    761  CG2 ILE A 120      -0.641  20.639 -41.835  1.00 52.88           C  
ANISOU  761  CG2 ILE A 120     7238   7726   5127   1039  -1181   -736       C  
ATOM    762  CD1 ILE A 120       1.894  22.240 -39.419  1.00 53.15           C  
ANISOU  762  CD1 ILE A 120     7256   7755   5186    978  -1068   -720       C  
ATOM    763  N   TYR A 121      -1.898  19.137 -39.377  1.00 73.15           N  
ANISOU  763  N   TYR A 121     9734  10332   7729    970  -1134   -851       N  
ATOM    764  CA  TYR A 121      -3.127  19.290 -38.611  1.00 81.86           C  
ANISOU  764  CA  TYR A 121    10782  11444   8878    946  -1135   -917       C  
ATOM    765  C   TYR A 121      -3.139  18.427 -37.360  1.00 79.11           C  
ANISOU  765  C   TYR A 121    10425  11125   8506    879  -1100   -950       C  
ATOM    766  O   TYR A 121      -3.879  18.734 -36.417  1.00 79.79           O  
ANISOU  766  O   TYR A 121    10459  11231   8625    840  -1083  -1010       O  
ATOM    767  CB  TYR A 121      -4.337  19.027 -39.506  1.00 84.75           C  
ANISOU  767  CB  TYR A 121    11135  11811   9254    974  -1180   -943       C  
ATOM    768  CG  TYR A 121      -4.635  20.252 -40.339  1.00 84.13           C  
ANISOU  768  CG  TYR A 121    11049  11696   9222   1029  -1224   -931       C  
ATOM    769  CD1 TYR A 121      -5.449  21.264 -39.852  1.00 87.04           C  
ANISOU  769  CD1 TYR A 121    11360  12049   9664   1039  -1242   -990       C  
ATOM    770  CD2 TYR A 121      -4.045  20.433 -41.577  1.00 87.63           C  
ANISOU  770  CD2 TYR A 121    11544  12116   9634   1065  -1252   -864       C  
ATOM    771  CE1 TYR A 121      -5.696  22.403 -40.596  1.00 91.16           C  
ANISOU  771  CE1 TYR A 121    11884  12522  10232   1091  -1300   -978       C  
ATOM    772  CE2 TYR A 121      -4.286  21.567 -42.324  1.00 91.44           C  
ANISOU  772  CE2 TYR A 121    12035  12557  10152   1103  -1303   -845       C  
ATOM    773  CZ  TYR A 121      -5.112  22.547 -41.830  1.00 95.15           C  
ANISOU  773  CZ  TYR A 121    12454  12998  10700   1120  -1332   -899       C  
ATOM    774  OH  TYR A 121      -5.354  23.676 -42.577  1.00102.22           O  
ANISOU  774  OH  TYR A 121    13367  13837  11635   1161  -1400   -878       O  
ATOM    775  N   SER A 122      -2.306  17.384 -37.312  1.00 78.48           N  
ANISOU  775  N   SER A 122    10397  11051   8372    862  -1093   -916       N  
ATOM    776  CA  SER A 122      -2.022  16.750 -36.031  1.00 76.31           C  
ANISOU  776  CA  SER A 122    10129  10790   8073    795  -1067   -931       C  
ATOM    777  C   SER A 122      -1.299  17.717 -35.097  1.00 73.51           C  
ANISOU  777  C   SER A 122     9754  10433   7745    780  -1029   -931       C  
ATOM    778  O   SER A 122      -1.599  17.779 -33.896  1.00 68.89           O  
ANISOU  778  O   SER A 122     9139   9868   7167    718  -1003   -969       O  
ATOM    779  CB  SER A 122      -1.189  15.486 -36.246  1.00 73.60           C  
ANISOU  779  CB  SER A 122     9851  10439   7673    793  -1086   -896       C  
ATOM    780  OG  SER A 122      -1.824  14.601 -37.152  1.00 69.37           O  
ANISOU  780  OG  SER A 122     9335   9905   7115    810  -1123   -898       O  
ATOM    781  N   MET A 123      -0.358  18.499 -35.642  1.00 77.12           N  
ANISOU  781  N   MET A 123    10222  10869   8212    829  -1024   -890       N  
ATOM    782  CA  MET A 123       0.311  19.522 -34.844  1.00 79.96           C  
ANISOU  782  CA  MET A 123    10559  11223   8600    819   -989   -889       C  
ATOM    783  C   MET A 123      -0.667  20.602 -34.399  1.00 81.74           C  
ANISOU  783  C   MET A 123    10719  11449   8890    813   -984   -939       C  
ATOM    784  O   MET A 123      -0.565  21.122 -33.276  1.00 91.35           O  
ANISOU  784  O   MET A 123    11900  12677  10131    776   -951   -970       O  
ATOM    785  CB  MET A 123       1.460  20.141 -35.641  1.00 78.52           C  
ANISOU  785  CB  MET A 123    10404  11022   8407    865   -987   -837       C  
ATOM    786  CG  MET A 123       2.537  19.154 -36.059  1.00 80.87           C  
ANISOU  786  CG  MET A 123    10753  11329   8647    875   -992   -806       C  
ATOM    787  SD  MET A 123       3.272  18.278 -34.665  1.00 85.78           S  
ANISOU  787  SD  MET A 123    11391  11959   9241    825   -972   -819       S  
ATOM    788  CE  MET A 123       4.457  17.236 -35.509  1.00 94.11           C  
ANISOU  788  CE  MET A 123    12497  13018  10241    863  -1000   -798       C  
ATOM    789  N   THR A 124      -1.636  20.937 -35.256  1.00 69.36           N  
ANISOU  789  N   THR A 124     9131   9870   7352    851  -1021   -957       N  
ATOM    790  CA  THR A 124      -2.680  21.864 -34.842  1.00 69.70           C  
ANISOU  790  CA  THR A 124     9105   9915   7465    852  -1030  -1025       C  
ATOM    791  C   THR A 124      -3.505  21.271 -33.712  1.00 65.45           C  
ANISOU  791  C   THR A 124     8518   9427   6921    781  -1004  -1099       C  
ATOM    792  O   THR A 124      -3.907  21.983 -32.784  1.00 64.32           O  
ANISOU  792  O   THR A 124     8310   9304   6823    753   -984  -1164       O  
ATOM    793  CB  THR A 124      -3.571  22.221 -36.035  1.00 77.98           C  
ANISOU  793  CB  THR A 124    10146  10937   8544    911  -1089  -1032       C  
ATOM    794  OG1 THR A 124      -2.821  22.989 -36.986  1.00 81.10           O  
ANISOU  794  OG1 THR A 124    10586  11287   8943    961  -1115   -965       O  
ATOM    795  CG2 THR A 124      -4.790  23.024 -35.590  1.00 75.79           C  
ANISOU  795  CG2 THR A 124     9787  10666   8343    917  -1110  -1125       C  
ATOM    796  N   ALA A 125      -3.736  19.956 -33.750  1.00 70.09           N  
ANISOU  796  N   ALA A 125     9139  10040   7451    742  -1005  -1094       N  
ATOM    797  CA  ALA A 125      -4.448  19.314 -32.649  1.00 70.84           C  
ANISOU  797  CA  ALA A 125     9202  10187   7525    653   -979  -1157       C  
ATOM    798  C   ALA A 125      -3.645  19.389 -31.357  1.00 63.56           C  
ANISOU  798  C   ALA A 125     8284   9281   6585    590   -935  -1152       C  
ATOM    799  O   ALA A 125      -4.214  19.568 -30.274  1.00 58.92           O  
ANISOU  799  O   ALA A 125     7641   8741   6006    519   -906  -1220       O  
ATOM    800  CB  ALA A 125      -4.769  17.862 -33.002  1.00 67.77           C  
ANISOU  800  CB  ALA A 125     8865   9812   7074    620   -998  -1140       C  
ATOM    801  N   VAL A 126      -2.317  19.300 -31.452  1.00 73.07           N  
ANISOU  801  N   VAL A 126     9546  10451   7765    614   -930  -1079       N  
ATOM    802  CA  VAL A 126      -1.490  19.380 -30.251  1.00 78.24           C  
ANISOU  802  CA  VAL A 126    10207  11116   8403    561   -893  -1072       C  
ATOM    803  C   VAL A 126      -1.536  20.786 -29.660  1.00 86.83           C  
ANISOU  803  C   VAL A 126    11224  12211   9555    568   -863  -1114       C  
ATOM    804  O   VAL A 126      -1.757  20.964 -28.451  1.00 99.60           O  
ANISOU  804  O   VAL A 126    12799  13870  11176    497   -828  -1165       O  
ATOM    805  CB  VAL A 126      -0.048  18.940 -30.563  1.00 80.90           C  
ANISOU  805  CB  VAL A 126    10618  11417   8703    594   -900   -995       C  
ATOM    806  CG1 VAL A 126       0.900  19.417 -29.481  1.00 89.18           C  
ANISOU  806  CG1 VAL A 126    11662  12469   9753    563   -863   -989       C  
ATOM    807  CG2 VAL A 126       0.022  17.428 -30.695  1.00 76.93           C  
ANISOU  807  CG2 VAL A 126    10182  10910   8136    564   -932   -971       C  
ATOM    808  N   ALA A 127      -1.359  21.809 -30.504  1.00 83.53           N  
ANISOU  808  N   ALA A 127    10794  11755   9189    650   -880  -1097       N  
ATOM    809  CA  ALA A 127      -1.411  23.178 -29.996  1.00 79.62           C  
ANISOU  809  CA  ALA A 127    10235  11256   8762    663   -864  -1138       C  
ATOM    810  C   ALA A 127      -2.787  23.499 -29.427  1.00 77.74           C  
ANISOU  810  C   ALA A 127     9908  11061   8569    630   -864  -1244       C  
ATOM    811  O   ALA A 127      -2.902  24.195 -28.409  1.00 78.72           O  
ANISOU  811  O   ALA A 127     9968  11214   8730    595   -834  -1306       O  
ATOM    812  CB  ALA A 127      -1.040  24.170 -31.099  1.00 72.99           C  
ANISOU  812  CB  ALA A 127     9411  10357   7964    749   -898  -1094       C  
ATOM    813  N   PHE A 128      -3.843  22.983 -30.060  1.00 78.72           N  
ANISOU  813  N   PHE A 128    10020  11198   8691    638   -897  -1277       N  
ATOM    814  CA  PHE A 128      -5.190  23.211 -29.552  1.00 85.48           C  
ANISOU  814  CA  PHE A 128    10784  12109   9586    604   -897  -1395       C  
ATOM    815  C   PHE A 128      -5.385  22.529 -28.205  1.00 97.20           C  
ANISOU  815  C   PHE A 128    12244  13669  11018    483   -845  -1444       C  
ATOM    816  O   PHE A 128      -6.043  23.075 -27.310  1.00101.63           O  
ANISOU  816  O   PHE A 128    12714  14286  11613    436   -821  -1546       O  
ATOM    817  CB  PHE A 128      -6.214  22.702 -30.566  1.00 83.04           C  
ANISOU  817  CB  PHE A 128    10474  11800   9276    636   -943  -1416       C  
ATOM    818  CG  PHE A 128      -7.610  23.207 -30.336  1.00 91.20           C  
ANISOU  818  CG  PHE A 128    11401  12879  10370    632   -959  -1547       C  
ATOM    819  CD1 PHE A 128      -8.402  22.680 -29.327  1.00 93.13           C  
ANISOU  819  CD1 PHE A 128    11586  13215  10587    530   -920  -1642       C  
ATOM    820  CD2 PHE A 128      -8.137  24.198 -31.146  1.00103.17           C  
ANISOU  820  CD2 PHE A 128    12880  14349  11970    727  -1020  -1581       C  
ATOM    821  CE1 PHE A 128      -9.688  23.144 -29.120  1.00 97.49           C  
ANISOU  821  CE1 PHE A 128    12027  13821  11194    525   -933  -1781       C  
ATOM    822  CE2 PHE A 128      -9.423  24.664 -30.946  1.00108.72           C  
ANISOU  822  CE2 PHE A 128    13478  15093  12737    733  -1045  -1717       C  
ATOM    823  CZ  PHE A 128     -10.200  24.137 -29.932  1.00104.26           C  
ANISOU  823  CZ  PHE A 128    12840  14630  12145    633   -998  -1824       C  
ATOM    824  N   ASP A 129      -4.801  21.342 -28.038  1.00 96.18           N  
ANISOU  824  N   ASP A 129    12196  13543  10806    429   -832  -1375       N  
ATOM    825  CA  ASP A 129      -4.983  20.615 -26.789  1.00 89.15           C  
ANISOU  825  CA  ASP A 129    11301  12718   9853    301   -794  -1410       C  
ATOM    826  C   ASP A 129      -4.265  21.323 -25.646  1.00 94.47           C  
ANISOU  826  C   ASP A 129    11947  13408  10540    263   -751  -1421       C  
ATOM    827  O   ASP A 129      -4.807  21.431 -24.539  1.00100.67           O  
ANISOU  827  O   ASP A 129    12669  14267  11316    168   -714  -1503       O  
ATOM    828  CB  ASP A 129      -4.503  19.170 -26.950  1.00 85.73           C  
ANISOU  828  CB  ASP A 129    10974  12266   9332    259   -811  -1329       C  
ATOM    829  CG  ASP A 129      -4.767  18.323 -25.720  1.00 99.43           C  
ANISOU  829  CG  ASP A 129    12724  14063  10993    113   -786  -1357       C  
ATOM    830  OD1 ASP A 129      -5.940  17.935 -25.512  1.00107.38           O  
ANISOU  830  OD1 ASP A 129    13689  15132  11977     39   -781  -1431       O  
ATOM    831  OD2 ASP A 129      -3.809  18.026 -24.974  1.00108.30           O  
ANISOU  831  OD2 ASP A 129    13902  15172  12075     68   -776  -1305       O  
ATOM    832  N   ARG A 130      -3.050  21.828 -25.895  1.00 97.26           N  
ANISOU  832  N   ARG A 130    12342  13700  10912    332   -751  -1345       N  
ATOM    833  CA  ARG A 130      -2.367  22.586 -24.848  1.00105.97           C  
ANISOU  833  CA  ARG A 130    13414  14816  12033    304   -710  -1358       C  
ATOM    834  C   ARG A 130      -3.089  23.892 -24.545  1.00104.98           C  
ANISOU  834  C   ARG A 130    13175  14717  11995    325   -699  -1459       C  
ATOM    835  O   ARG A 130      -3.186  24.299 -23.377  1.00105.66           O  
ANISOU  835  O   ARG A 130    13199  14859  12088    256   -658  -1525       O  
ATOM    836  CB  ARG A 130      -0.910  22.845 -25.243  1.00110.47           C  
ANISOU  836  CB  ARG A 130    14051  15320  12604    372   -713  -1261       C  
ATOM    837  CG  ARG A 130      -0.071  21.597 -25.503  1.00113.68           C  
ANISOU  837  CG  ARG A 130    14561  15698  12933    362   -731  -1174       C  
ATOM    838  CD  ARG A 130       0.041  20.729 -24.242  1.00119.14           C  
ANISOU  838  CD  ARG A 130    15280  16431  13557    245   -713  -1181       C  
ATOM    839  NE  ARG A 130      -1.102  19.849 -24.010  1.00125.16           N  
ANISOU  839  NE  ARG A 130    16039  17241  14276    158   -723  -1225       N  
ATOM    840  CZ  ARG A 130      -1.350  19.241 -22.853  1.00128.78           C  
ANISOU  840  CZ  ARG A 130    16507  17750  14675     31   -706  -1250       C  
ATOM    841  NH1 ARG A 130      -0.537  19.416 -21.820  1.00127.60           N  
ANISOU  841  NH1 ARG A 130    16369  17607  14505    -18   -681  -1235       N  
ATOM    842  NH2 ARG A 130      -2.413  18.459 -22.726  1.00134.85           N  
ANISOU  842  NH2 ARG A 130    17274  18564  15398    -54   -716  -1291       N  
ATOM    843  N   TYR A 131      -3.630  24.548 -25.577  1.00 92.97           N  
ANISOU  843  N   TYR A 131    11627  13158  10542    419   -742  -1478       N  
ATOM    844  CA  TYR A 131      -4.368  25.782 -25.340  1.00 92.44           C  
ANISOU  844  CA  TYR A 131    11451  13104  10567    450   -751  -1584       C  
ATOM    845  C   TYR A 131      -5.604  25.519 -24.493  1.00101.42           C  
ANISOU  845  C   TYR A 131    12495  14342  11699    359   -727  -1716       C  
ATOM    846  O   TYR A 131      -5.980  26.355 -23.664  1.00 97.11           O  
ANISOU  846  O   TYR A 131    11849  13842  11205    336   -707  -1820       O  
ATOM    847  CB  TYR A 131      -4.759  26.429 -26.673  1.00 92.41           C  
ANISOU  847  CB  TYR A 131    11449  13031  10631    565   -819  -1575       C  
ATOM    848  CG  TYR A 131      -5.668  27.637 -26.548  1.00 95.17           C  
ANISOU  848  CG  TYR A 131    11690  13384  11086    610   -853  -1696       C  
ATOM    849  CD1 TYR A 131      -7.047  27.488 -26.404  1.00 88.56           C  
ANISOU  849  CD1 TYR A 131    10764  12611  10274    586   -867  -1823       C  
ATOM    850  CD2 TYR A 131      -5.149  28.927 -26.591  1.00103.51           C  
ANISOU  850  CD2 TYR A 131    12732  14377  12219    676   -877  -1689       C  
ATOM    851  CE1 TYR A 131      -7.877  28.585 -26.289  1.00 94.11           C  
ANISOU  851  CE1 TYR A 131    11359  13317  11080    634   -908  -1949       C  
ATOM    852  CE2 TYR A 131      -5.977  30.036 -26.482  1.00103.65           C  
ANISOU  852  CE2 TYR A 131    12652  14388  12342    723   -923  -1806       C  
ATOM    853  CZ  TYR A 131      -7.339  29.858 -26.331  1.00101.72           C  
ANISOU  853  CZ  TYR A 131    12313  14209  12126    707   -940  -1940       C  
ATOM    854  OH  TYR A 131      -8.166  30.953 -26.222  1.00113.61           O  
ANISOU  854  OH  TYR A 131    13714  15708  13744    763   -996  -2072       O  
ATOM    855  N   MET A 132      -6.240  24.360 -24.680  1.00111.10           N  
ANISOU  855  N   MET A 132    13746  15607  12858    301   -729  -1720       N  
ATOM    856  CA  MET A 132      -7.400  24.015 -23.866  1.00109.11           C  
ANISOU  856  CA  MET A 132    13409  15464  12583    194   -702  -1846       C  
ATOM    857  C   MET A 132      -6.997  23.678 -22.438  1.00100.97           C  
ANISOU  857  C   MET A 132    12375  14504  11485     60   -639  -1859       C  
ATOM    858  O   MET A 132      -7.645  24.124 -21.483  1.00 94.14           O  
ANISOU  858  O   MET A 132    11405  13729  10636    -14   -604  -1983       O  
ATOM    859  CB  MET A 132      -8.150  22.840 -24.496  1.00109.15           C  
ANISOU  859  CB  MET A 132    13454  15490  12529    163   -723  -1838       C  
ATOM    860  CG  MET A 132      -9.004  23.225 -25.681  1.00112.62           C  
ANISOU  860  CG  MET A 132    13856  15897  13038    269   -780  -1881       C  
ATOM    861  SD  MET A 132     -10.376  24.276 -25.180  1.00115.68           S  
ANISOU  861  SD  MET A 132    14068  16367  13519    268   -785  -2087       S  
ATOM    862  CE  MET A 132     -11.265  23.165 -24.091  1.00118.54           C  
ANISOU  862  CE  MET A 132    14385  16875  13778     79   -723  -2183       C  
ATOM    863  N   ALA A 133      -5.927  22.896 -22.273  1.00101.91           N  
ANISOU  863  N   ALA A 133    12608  14585  11529     26   -629  -1736       N  
ATOM    864  CA  ALA A 133      -5.478  22.509 -20.944  1.00101.98           C  
ANISOU  864  CA  ALA A 133    12631  14649  11466   -103   -581  -1734       C  
ATOM    865  C   ALA A 133      -4.996  23.693 -20.122  1.00103.33           C  
ANISOU  865  C   ALA A 133    12730  14835  11694    -94   -545  -1778       C  
ATOM    866  O   ALA A 133      -5.038  23.626 -18.889  1.00103.10           O  
ANISOU  866  O   ALA A 133    12666  14885  11622   -214   -499  -1829       O  
ATOM    867  CB  ALA A 133      -4.370  21.461 -21.056  1.00104.75           C  
ANISOU  867  CB  ALA A 133    13123  14938  11738   -118   -598  -1593       C  
ATOM    868  N   ILE A 134      -4.534  24.761 -20.763  1.00 99.60           N  
ANISOU  868  N   ILE A 134    12240  14289  11313     38   -567  -1759       N  
ATOM    869  CA  ILE A 134      -4.001  25.918 -20.053  1.00 93.00           C  
ANISOU  869  CA  ILE A 134    11343  13455  10537     56   -538  -1793       C  
ATOM    870  C   ILE A 134      -5.044  27.017 -19.888  1.00 98.14           C  
ANISOU  870  C   ILE A 134    11853  14152  11284     83   -543  -1945       C  
ATOM    871  O   ILE A 134      -5.243  27.526 -18.785  1.00108.45           O  
ANISOU  871  O   ILE A 134    13068  15533  12604     14   -501  -2042       O  
ATOM    872  CB  ILE A 134      -2.734  26.441 -20.765  1.00 85.41           C  
ANISOU  872  CB  ILE A 134    10456  12386   9611    170   -559  -1677       C  
ATOM    873  CG1 ILE A 134      -1.535  25.569 -20.384  1.00 92.23           C  
ANISOU  873  CG1 ILE A 134    11427  13230  10386    122   -539  -1565       C  
ATOM    874  CG2 ILE A 134      -2.482  27.905 -20.418  1.00 72.33           C  
ANISOU  874  CG2 ILE A 134     8722  10713   8048    224   -550  -1730       C  
ATOM    875  CD1 ILE A 134      -0.243  25.975 -21.037  1.00 93.82           C  
ANISOU  875  CD1 ILE A 134    11697  13342  10607    220   -553  -1461       C  
ATOM    876  N   ILE A 135      -5.727  27.397 -20.970  1.00 96.63           N  
ANISOU  876  N   ILE A 135    11637  13916  11162    184   -600  -1973       N  
ATOM    877  CA  ILE A 135      -6.547  28.607 -20.930  1.00 93.79           C  
ANISOU  877  CA  ILE A 135    11150  13571  10916    242   -627  -2112       C  
ATOM    878  C   ILE A 135      -7.915  28.346 -20.302  1.00 95.52           C  
ANISOU  878  C   ILE A 135    11251  13917  11127    151   -607  -2278       C  
ATOM    879  O   ILE A 135      -8.434  29.189 -19.562  1.00 98.32           O  
ANISOU  879  O   ILE A 135    11477  14334  11545    134   -594  -2422       O  
ATOM    880  CB  ILE A 135      -6.665  29.211 -22.340  1.00 97.41           C  
ANISOU  880  CB  ILE A 135    11636  13920  11455    390   -710  -2074       C  
ATOM    881  CG1 ILE A 135      -5.283  29.630 -22.846  1.00 90.76           C  
ANISOU  881  CG1 ILE A 135    10897  12970  10619    463   -722  -1927       C  
ATOM    882  CG2 ILE A 135      -7.600  30.407 -22.333  1.00100.12           C  
ANISOU  882  CG2 ILE A 135    11851  14268  11921    455   -758  -2226       C  
ATOM    883  CD1 ILE A 135      -4.571  30.602 -21.932  1.00 80.30           C  
ANISOU  883  CD1 ILE A 135     9531  11644   9337    455   -689  -1948       C  
ATOM    884  N   HIS A 136      -8.518  27.186 -20.563  1.00101.09           N  
ANISOU  884  N   HIS A 136    11991  14666  11752     85   -603  -2270       N  
ATOM    885  CA  HIS A 136      -9.784  26.794 -19.940  1.00110.46           C  
ANISOU  885  CA  HIS A 136    13073  15987  12909    -26   -575  -2425       C  
ATOM    886  C   HIS A 136      -9.626  25.392 -19.366  1.00111.58           C  
ANISOU  886  C   HIS A 136    13298  16191  12907   -182   -526  -2360       C  
ATOM    887  O   HIS A 136     -10.175  24.423 -19.905  1.00118.60           O  
ANISOU  887  O   HIS A 136    14232  17091  13739   -213   -542  -2340       O  
ATOM    888  CB  HIS A 136     -10.946  26.825 -20.937  1.00114.33           C  
ANISOU  888  CB  HIS A 136    13512  16473  13454     49   -635  -2506       C  
ATOM    889  CG  HIS A 136     -10.934  28.002 -21.864  1.00114.26           C  
ANISOU  889  CG  HIS A 136    13479  16358  13578    221   -713  -2514       C  
ATOM    890  ND1 HIS A 136     -11.744  29.102 -21.683  1.00119.00           N  
ANISOU  890  ND1 HIS A 136    13938  16987  14292    276   -748  -2683       N  
ATOM    891  CD2 HIS A 136     -10.232  28.236 -22.999  1.00106.08           C  
ANISOU  891  CD2 HIS A 136    12546  15186  12574    346   -770  -2376       C  
ATOM    892  CE1 HIS A 136     -11.530  29.970 -22.655  1.00113.51           C  
ANISOU  892  CE1 HIS A 136    13269  16166  13695    427   -831  -2640       C  
ATOM    893  NE2 HIS A 136     -10.617  29.469 -23.467  1.00106.83           N  
ANISOU  893  NE2 HIS A 136    12571  15223  12796    466   -841  -2453       N  
ATOM    894  N   PRO A 137      -8.880  25.247 -18.269  1.00107.92           N  
ANISOU  894  N   PRO A 137    12860  15763  12382   -283   -473  -2325       N  
ATOM    895  CA  PRO A 137      -8.647  23.901 -17.718  1.00103.36           C  
ANISOU  895  CA  PRO A 137    12381  15227  11665   -433   -443  -2250       C  
ATOM    896  C   PRO A 137      -9.922  23.162 -17.334  1.00116.43           C  
ANISOU  896  C   PRO A 137    13979  17010  13249   -576   -421  -2364       C  
ATOM    897  O   PRO A 137      -9.964  21.931 -17.443  1.00115.21           O  
ANISOU  897  O   PRO A 137    13926  16857  12992   -661   -428  -2289       O  
ATOM    898  CB  PRO A 137      -7.751  24.169 -16.497  1.00 96.33           C  
ANISOU  898  CB  PRO A 137    11498  14363  10741   -512   -394  -2227       C  
ATOM    899  CG  PRO A 137      -7.960  25.610 -16.167  1.00 98.48           C  
ANISOU  899  CG  PRO A 137    11629  14662  11126   -448   -380  -2351       C  
ATOM    900  CD  PRO A 137      -8.246  26.302 -17.457  1.00103.02           C  
ANISOU  900  CD  PRO A 137    12182  15147  11816   -270   -443  -2357       C  
ATOM    901  N   LEU A 138     -10.955  23.874 -16.874  1.00134.05           N  
ANISOU  901  N   LEU A 138    16051  19352  15531   -609   -397  -2551       N  
ATOM    902  CA  LEU A 138     -12.173  23.202 -16.432  1.00136.51           C  
ANISOU  902  CA  LEU A 138    16296  19805  15766   -762   -367  -2677       C  
ATOM    903  C   LEU A 138     -12.936  22.564 -17.591  1.00141.57           C  
ANISOU  903  C   LEU A 138    16966  20416  16408   -708   -414  -2670       C  
ATOM    904  O   LEU A 138     -13.616  21.552 -17.394  1.00147.35           O  
ANISOU  904  O   LEU A 138    17718  21231  17039   -847   -397  -2697       O  
ATOM    905  CB  LEU A 138     -13.067  24.190 -15.675  1.00135.50           C  
ANISOU  905  CB  LEU A 138    15973  19811  15702   -801   -332  -2899       C  
ATOM    906  CG  LEU A 138     -13.914  23.632 -14.524  1.00136.41           C  
ANISOU  906  CG  LEU A 138    16012  20114  15704  -1030   -265  -3034       C  
ATOM    907  CD1 LEU A 138     -13.055  22.858 -13.537  1.00136.69           C  
ANISOU  907  CD1 LEU A 138    16165  20166  15604  -1194   -222  -2914       C  
ATOM    908  CD2 LEU A 138     -14.651  24.748 -13.807  1.00135.28           C  
ANISOU  908  CD2 LEU A 138    15664  20098  15640  -1046   -232  -3262       C  
ATOM    909  N   GLN A 139     -12.826  23.119 -18.799  1.00139.23           N  
ANISOU  909  N   GLN A 139    16679  20005  16218   -516   -476  -2630       N  
ATOM    910  CA  GLN A 139     -13.569  22.586 -19.931  1.00136.24           C  
ANISOU  910  CA  GLN A 139    16319  19598  15846   -457   -523  -2629       C  
ATOM    911  C   GLN A 139     -12.973  21.252 -20.384  1.00133.98           C  
ANISOU  911  C   GLN A 139    16206  19244  15455   -495   -537  -2453       C  
ATOM    912  O   GLN A 139     -11.758  21.046 -20.301  1.00128.72           O  
ANISOU  912  O   GLN A 139    15653  18494  14761   -477   -539  -2306       O  
ATOM    913  CB  GLN A 139     -13.576  23.586 -21.084  1.00136.39           C  
ANISOU  913  CB  GLN A 139    16309  19509  16003   -248   -592  -2629       C  
ATOM    914  CG  GLN A 139     -14.312  24.882 -20.774  1.00144.68           C  
ANISOU  914  CG  GLN A 139    17187  20615  17172   -194   -603  -2819       C  
ATOM    915  CD  GLN A 139     -14.449  25.788 -21.982  1.00157.90           C  
ANISOU  915  CD  GLN A 139    18844  22174  18977      4   -691  -2819       C  
ATOM    916  OE1 GLN A 139     -14.254  25.359 -23.120  1.00159.16           O  
ANISOU  916  OE1 GLN A 139    19105  22238  19132     88   -739  -2701       O  
ATOM    917  NE2 GLN A 139     -14.784  27.051 -21.739  1.00165.52           N  
ANISOU  917  NE2 GLN A 139    19683  23148  20060     78   -719  -2955       N  
ATOM    918  N   PRO A 140     -13.810  20.324 -20.859  1.00134.10           N  
ANISOU  918  N   PRO A 140    16241  19297  15416   -546   -550  -2473       N  
ATOM    919  CA  PRO A 140     -13.327  18.963 -21.146  1.00133.77           C  
ANISOU  919  CA  PRO A 140    16358  19201  15267   -605   -565  -2322       C  
ATOM    920  C   PRO A 140     -12.650  18.856 -22.507  1.00143.91           C  
ANISOU  920  C   PRO A 140    17742  20338  16599   -434   -627  -2183       C  
ATOM    921  O   PRO A 140     -13.213  19.250 -23.532  1.00153.33           O  
ANISOU  921  O   PRO A 140    18890  21500  17868   -313   -666  -2221       O  
ATOM    922  CB  PRO A 140     -14.607  18.124 -21.097  1.00122.16           C  
ANISOU  922  CB  PRO A 140    14852  17841  13725   -732   -552  -2421       C  
ATOM    923  CG  PRO A 140     -15.671  19.075 -21.551  1.00117.95           C  
ANISOU  923  CG  PRO A 140    14159  17357  13298   -640   -563  -2587       C  
ATOM    924  CD  PRO A 140     -15.266  20.451 -21.072  1.00125.37           C  
ANISOU  924  CD  PRO A 140    15006  18291  14338   -564   -551  -2647       C  
ATOM    925  N   ARG A 141     -11.428  18.328 -22.507  1.00145.03           N  
ANISOU  925  N   ARG A 141    18017  20393  16695   -427   -639  -2026       N  
ATOM    926  CA  ARG A 141     -10.783  17.888 -23.735  1.00134.15           C  
ANISOU  926  CA  ARG A 141    16747  18894  15329   -304   -693  -1894       C  
ATOM    927  C   ARG A 141     -11.321  16.524 -24.156  1.00136.48           C  
ANISOU  927  C   ARG A 141    17117  19199  15541   -374   -717  -1863       C  
ATOM    928  O   ARG A 141     -11.794  15.738 -23.330  1.00141.15           O  
ANISOU  928  O   ARG A 141    17722  19869  16040   -538   -693  -1898       O  
ATOM    929  CB  ARG A 141      -9.268  17.822 -23.558  1.00120.84           C  
ANISOU  929  CB  ARG A 141    15166  17121  13628   -270   -699  -1757       C  
ATOM    930  CG  ARG A 141      -8.587  19.172 -23.636  1.00114.18           C  
ANISOU  930  CG  ARG A 141    14273  16231  12881   -152   -693  -1754       C  
ATOM    931  CD  ARG A 141      -7.328  19.173 -22.799  1.00113.15           C  
ANISOU  931  CD  ARG A 141    14203  16072  12715   -189   -670  -1675       C  
ATOM    932  NE  ARG A 141      -7.642  19.037 -21.380  1.00115.45           N  
ANISOU  932  NE  ARG A 141    14455  16462  12948   -350   -622  -1746       N  
ATOM    933  CZ  ARG A 141      -6.765  18.677 -20.451  1.00112.20           C  
ANISOU  933  CZ  ARG A 141    14110  16047  12474   -433   -606  -1684       C  
ATOM    934  NH1 ARG A 141      -7.143  18.581 -19.183  1.00108.78           N  
ANISOU  934  NH1 ARG A 141    13638  15713  11982   -591   -562  -1754       N  
ATOM    935  NH2 ARG A 141      -5.512  18.404 -20.789  1.00110.92           N  
ANISOU  935  NH2 ARG A 141    14052  15787  12305   -363   -635  -1559       N  
ATOM    936  N   LEU A 142     -11.238  16.246 -25.455  1.00133.00           N  
ANISOU  936  N   LEU A 142    16727  18678  15128   -254   -766  -1797       N  
ATOM    937  CA  LEU A 142     -11.808  15.020 -25.998  1.00127.77           C  
ANISOU  937  CA  LEU A 142    16127  18020  14400   -301   -793  -1775       C  
ATOM    938  C   LEU A 142     -10.975  13.798 -25.607  1.00115.99           C  
ANISOU  938  C   LEU A 142    14778  16484  12811   -388   -812  -1658       C  
ATOM    939  O   LEU A 142      -9.765  13.886 -25.376  1.00118.52           O  
ANISOU  939  O   LEU A 142    15163  16737  13131   -353   -820  -1568       O  
ATOM    940  CB  LEU A 142     -11.945  15.129 -27.522  1.00131.44           C  
ANISOU  940  CB  LEU A 142    16601  18414  14927   -144   -842  -1742       C  
ATOM    941  CG  LEU A 142     -10.744  15.521 -28.391  1.00123.73           C  
ANISOU  941  CG  LEU A 142    15688  17323  14000      6   -876  -1626       C  
ATOM    942  CD1 LEU A 142     -10.006  14.294 -28.816  1.00125.70           C  
ANISOU  942  CD1 LEU A 142    16069  17509  14182      0   -910  -1508       C  
ATOM    943  CD2 LEU A 142     -11.163  16.310 -29.619  1.00113.53           C  
ANISOU  943  CD2 LEU A 142    14344  15996  12796    151   -910  -1650       C  
ATOM    944  N   SER A 143     -11.646  12.647 -25.538  1.00105.96           N  
ANISOU  944  N   SER A 143    13555  15249  11456   -502   -825  -1666       N  
ATOM    945  CA  SER A 143     -11.077  11.410 -25.019  1.00108.27           C  
ANISOU  945  CA  SER A 143    13982  15506  11648   -614   -854  -1574       C  
ATOM    946  C   SER A 143     -10.201  10.721 -26.064  1.00118.11           C  
ANISOU  946  C   SER A 143    15342  16632  12903   -497   -920  -1451       C  
ATOM    947  O   SER A 143     -10.123  11.138 -27.220  1.00125.84           O  
ANISOU  947  O   SER A 143    16294  17565  13954   -345   -937  -1438       O  
ATOM    948  CB  SER A 143     -12.182  10.461 -24.558  1.00106.78           C  
ANISOU  948  CB  SER A 143    13805  15403  11364   -792   -848  -1632       C  
ATOM    949  OG  SER A 143     -12.800   9.825 -25.662  1.00 98.37           O  
ANISOU  949  OG  SER A 143    12758  14316  10301   -740   -883  -1629       O  
ATOM    950  N   LEU A 144      -9.534   9.644 -25.633  1.00127.18           N  
ANISOU  950  N   LEU A 144    16619  17729  13974   -576   -964  -1365       N  
ATOM    951  CA  LEU A 144      -8.590   8.940 -26.500  1.00134.44           C  
ANISOU  951  CA  LEU A 144    17644  18536  14902   -470  -1032  -1259       C  
ATOM    952  C   LEU A 144      -9.274   8.390 -27.749  1.00151.67           C  
ANISOU  952  C   LEU A 144    19829  20702  17095   -406  -1064  -1265       C  
ATOM    953  O   LEU A 144      -8.813   8.613 -28.876  1.00174.85           O  
ANISOU  953  O   LEU A 144    22764  23581  20091   -252  -1087  -1228       O  
ATOM    954  CB  LEU A 144      -7.906   7.810 -25.725  1.00128.20           C  
ANISOU  954  CB  LEU A 144    16990  17695  14026   -579  -1088  -1183       C  
ATOM    955  CG  LEU A 144      -6.511   8.080 -25.151  1.00126.43           C  
ANISOU  955  CG  LEU A 144    16814  17409  13813   -543  -1103  -1117       C  
ATOM    956  CD1 LEU A 144      -6.537   9.212 -24.137  1.00132.99           C  
ANISOU  956  CD1 LEU A 144    17555  18314  14660   -594  -1028  -1173       C  
ATOM    957  CD2 LEU A 144      -5.926   6.816 -24.535  1.00126.47           C  
ANISOU  957  CD2 LEU A 144    16966  17349  13736   -642  -1184  -1043       C  
ATOM    958  N   THR A 145     -10.378   7.663 -27.573  1.00139.81           N  
ANISOU  958  N   THR A 145    18331  19257  15531   -528  -1065  -1313       N  
ATOM    959  CA  THR A 145     -11.108   7.183 -28.741  1.00126.17           C  
ANISOU  959  CA  THR A 145    16598  17524  13817   -469  -1090  -1327       C  
ATOM    960  C   THR A 145     -11.646   8.344 -29.567  1.00123.02           C  
ANISOU  960  C   THR A 145    16073  17159  13511   -339  -1053  -1396       C  
ATOM    961  O   THR A 145     -11.686   8.265 -30.805  1.00129.82           O  
ANISOU  961  O   THR A 145    16935  17977  14412   -218  -1083  -1374       O  
ATOM    962  CB  THR A 145     -12.236   6.250 -28.307  1.00124.20           C  
ANISOU  962  CB  THR A 145    16370  17340  13479   -639  -1092  -1376       C  
ATOM    963  OG1 THR A 145     -12.951   6.844 -27.217  1.00128.66           O  
ANISOU  963  OG1 THR A 145    16849  18018  14018   -770  -1025  -1472       O  
ATOM    964  CG2 THR A 145     -11.669   4.910 -27.865  1.00122.26           C  
ANISOU  964  CG2 THR A 145    16280  17027  13147   -740  -1162  -1286       C  
ATOM    965  N   ALA A 146     -12.013   9.447 -28.909  1.00116.82           N  
ANISOU  965  N   ALA A 146    15181  16445  12761   -361   -995  -1478       N  
ATOM    966  CA  ALA A 146     -12.366  10.655 -29.645  1.00109.03           C  
ANISOU  966  CA  ALA A 146    14084  15470  11873   -226   -976  -1536       C  
ATOM    967  C   ALA A 146     -11.176  11.202 -30.425  1.00116.50           C  
ANISOU  967  C   ALA A 146    15062  16320  12881    -66  -1002  -1447       C  
ATOM    968  O   ALA A 146     -11.354  11.728 -31.531  1.00104.44           O  
ANISOU  968  O   ALA A 146    13497  14766  11417     60  -1019  -1451       O  
ATOM    969  CB  ALA A 146     -12.911  11.713 -28.690  1.00101.57           C  
ANISOU  969  CB  ALA A 146    13019  14615  10958   -282   -919  -1648       C  
ATOM    970  N   THR A 147      -9.954  11.063 -29.890  1.00135.42           N  
ANISOU  970  N   THR A 147    17532  18665  15256    -75  -1008  -1366       N  
ATOM    971  CA  THR A 147      -8.778  11.430 -30.675  1.00136.98           C  
ANISOU  971  CA  THR A 147    17767  18779  15500     65  -1032  -1284       C  
ATOM    972  C   THR A 147      -8.665  10.558 -31.911  1.00129.66           C  
ANISOU  972  C   THR A 147    16904  17799  14561    136  -1085  -1229       C  
ATOM    973  O   THR A 147      -8.301  11.041 -32.988  1.00138.29           O  
ANISOU  973  O   THR A 147    17987  18854  15704    263  -1100  -1201       O  
ATOM    974  CB  THR A 147      -7.483  11.288 -29.866  1.00140.66           C  
ANISOU  974  CB  THR A 147    18302  19204  15940     38  -1034  -1216       C  
ATOM    975  OG1 THR A 147      -7.277   9.913 -29.526  1.00147.94           O  
ANISOU  975  OG1 THR A 147    19328  20100  16783    -50  -1078  -1170       O  
ATOM    976  CG2 THR A 147      -7.511  12.097 -28.615  1.00142.62           C  
ANISOU  976  CG2 THR A 147    18491  19505  16194    -38   -982  -1265       C  
ATOM    977  N   LYS A 148      -8.972   9.266 -31.774  1.00114.98           N  
ANISOU  977  N   LYS A 148    15116  15937  12633     51  -1117  -1215       N  
ATOM    978  CA  LYS A 148      -8.886   8.388 -32.935  1.00103.31           C  
ANISOU  978  CA  LYS A 148    13697  14410  11146    118  -1170  -1171       C  
ATOM    979  C   LYS A 148      -9.908   8.780 -33.997  1.00112.29           C  
ANISOU  979  C   LYS A 148    14762  15579  12325    187  -1165  -1222       C  
ATOM    980  O   LYS A 148      -9.603   8.762 -35.201  1.00120.21           O  
ANISOU  980  O   LYS A 148    15777  16541  13356    300  -1194  -1186       O  
ATOM    981  CB  LYS A 148      -9.049   6.932 -32.496  1.00 91.26           C  
ANISOU  981  CB  LYS A 148    12266  12870   9539      4  -1214  -1148       C  
ATOM    982  CG  LYS A 148      -7.826   6.399 -31.751  1.00 91.55           C  
ANISOU  982  CG  LYS A 148    12398  12846   9542    -30  -1251  -1079       C  
ATOM    983  CD  LYS A 148      -8.031   4.998 -31.198  1.00 96.20           C  
ANISOU  983  CD  LYS A 148    13092  13412  10049   -158  -1307  -1056       C  
ATOM    984  CE  LYS A 148      -6.739   4.469 -30.587  1.00 99.24           C  
ANISOU  984  CE  LYS A 148    13576  13720  10410   -169  -1364   -987       C  
ATOM    985  NZ  LYS A 148      -6.947   3.298 -29.689  1.00100.54           N  
ANISOU  985  NZ  LYS A 148    13849  13863  10490   -326  -1421   -964       N  
ATOM    986  N   VAL A 149     -11.102   9.208 -33.573  1.00105.44           N  
ANISOU  986  N   VAL A 149    13811  14788  11465    124  -1128  -1314       N  
ATOM    987  CA  VAL A 149     -12.078   9.692 -34.548  1.00105.56           C  
ANISOU  987  CA  VAL A 149    13750  14830  11528    198  -1130  -1372       C  
ATOM    988  C   VAL A 149     -11.570  10.959 -35.225  1.00108.37           C  
ANISOU  988  C   VAL A 149    14060  15150  11964    336  -1130  -1356       C  
ATOM    989  O   VAL A 149     -11.690  11.121 -36.449  1.00105.18           O  
ANISOU  989  O   VAL A 149    13652  14718  11593    438  -1160  -1338       O  
ATOM    990  CB  VAL A 149     -13.446   9.921 -33.879  1.00102.76           C  
ANISOU  990  CB  VAL A 149    13304  14572  11168    101  -1094  -1493       C  
ATOM    991  CG1 VAL A 149     -14.370  10.693 -34.813  1.00 99.70           C  
ANISOU  991  CG1 VAL A 149    12824  14207  10851    198  -1102  -1565       C  
ATOM    992  CG2 VAL A 149     -14.079   8.595 -33.488  1.00106.08           C  
ANISOU  992  CG2 VAL A 149    13776  15029  11501    -36  -1100  -1507       C  
ATOM    993  N   VAL A 150     -10.972  11.868 -34.447  1.00109.06           N  
ANISOU  993  N   VAL A 150    14121  15237  12081    334  -1100  -1356       N  
ATOM    994  CA  VAL A 150     -10.481  13.115 -35.029  1.00100.62           C  
ANISOU  994  CA  VAL A 150    13015  14130  11084    451  -1103  -1339       C  
ATOM    995  C   VAL A 150      -9.352  12.839 -36.014  1.00103.66           C  
ANISOU  995  C   VAL A 150    13479  14445  11462    540  -1135  -1236       C  
ATOM    996  O   VAL A 150      -9.224  13.518 -37.040  1.00101.40           O  
ANISOU  996  O   VAL A 150    13180  14130  11218    640  -1157  -1215       O  
ATOM    997  CB  VAL A 150     -10.046  14.092 -33.919  1.00 73.84           C  
ANISOU  997  CB  VAL A 150     9580  10753   7722    422  -1063  -1362       C  
ATOM    998  CG1 VAL A 150      -9.470  15.357 -34.523  1.00 72.60           C  
ANISOU  998  CG1 VAL A 150     9400  10550   7637    537  -1074  -1335       C  
ATOM    999  CG2 VAL A 150     -11.227  14.436 -33.042  1.00 62.73           C  
ANISOU  999  CG2 VAL A 150     8078   9429   6327    339  -1032  -1483       C  
ATOM   1000  N   ILE A 151      -8.528  11.829 -35.732  1.00103.70           N  
ANISOU 1000  N   ILE A 151    13566  14424  11410    500  -1145  -1177       N  
ATOM   1001  CA  ILE A 151      -7.458  11.475 -36.656  1.00106.79           C  
ANISOU 1001  CA  ILE A 151    14023  14762  11792    580  -1176  -1098       C  
ATOM   1002  C   ILE A 151      -8.031  10.903 -37.947  1.00115.76           C  
ANISOU 1002  C   ILE A 151    15169  15893  12922    633  -1213  -1095       C  
ATOM   1003  O   ILE A 151      -7.548  11.212 -39.046  1.00119.15           O  
ANISOU 1003  O   ILE A 151    15607  16296  13369    723  -1232  -1057       O  
ATOM   1004  CB  ILE A 151      -6.465  10.511 -35.981  1.00 97.63           C  
ANISOU 1004  CB  ILE A 151    12942  13573  10580    530  -1189  -1051       C  
ATOM   1005  CG1 ILE A 151      -5.689  11.251 -34.886  1.00 99.27           C  
ANISOU 1005  CG1 ILE A 151    13139  13780  10800    501  -1154  -1044       C  
ATOM   1006  CG2 ILE A 151      -5.523   9.900 -37.006  1.00 95.21           C  
ANISOU 1006  CG2 ILE A 151    12694  13221  10260    608  -1231   -994       C  
ATOM   1007  CD1 ILE A 151      -4.777  10.372 -34.068  1.00 97.36           C  
ANISOU 1007  CD1 ILE A 151    12974  13508  10510    444  -1174  -1005       C  
ATOM   1008  N   CYS A 152      -9.075  10.075 -37.847  1.00113.86           N  
ANISOU 1008  N   CYS A 152    14927  15682  12652    570  -1223  -1137       N  
ATOM   1009  CA  CYS A 152      -9.682   9.562 -39.072  1.00106.52           C  
ANISOU 1009  CA  CYS A 152    14002  14751  11720    621  -1256  -1140       C  
ATOM   1010  C   CYS A 152     -10.295  10.691 -39.894  1.00104.91           C  
ANISOU 1010  C   CYS A 152    13728  14558  11574    702  -1257  -1170       C  
ATOM   1011  O   CYS A 152     -10.206  10.689 -41.129  1.00111.69           O  
ANISOU 1011  O   CYS A 152    14600  15396  12440    781  -1287  -1140       O  
ATOM   1012  CB  CYS A 152     -10.730   8.499 -38.745  1.00106.09           C  
ANISOU 1012  CB  CYS A 152    13956  14731  11621    529  -1264  -1185       C  
ATOM   1013  SG  CYS A 152     -10.043   6.862 -38.406  1.00109.75           S  
ANISOU 1013  SG  CYS A 152    14533  15154  12013    462  -1304  -1130       S  
ATOM   1014  N   VAL A 153     -10.888  11.683 -39.227  1.00 89.51           N  
ANISOU 1014  N   VAL A 153    11705  12638   9666    682  -1231  -1232       N  
ATOM   1015  CA  VAL A 153     -11.409  12.841 -39.949  1.00 86.97           C  
ANISOU 1015  CA  VAL A 153    11324  12312   9410    765  -1249  -1262       C  
ATOM   1016  C   VAL A 153     -10.273  13.625 -40.601  1.00 91.64           C  
ANISOU 1016  C   VAL A 153    11947  12850  10022    848  -1262  -1185       C  
ATOM   1017  O   VAL A 153     -10.406  14.120 -41.732  1.00 96.24           O  
ANISOU 1017  O   VAL A 153    12528  13409  10629    925  -1298  -1166       O  
ATOM   1018  CB  VAL A 153     -12.244  13.713 -38.992  1.00 88.87           C  
ANISOU 1018  CB  VAL A 153    11475  12596   9697    726  -1224  -1359       C  
ATOM   1019  CG1 VAL A 153     -12.537  15.075 -39.602  1.00 79.83           C  
ANISOU 1019  CG1 VAL A 153    10276  11426   8631    820  -1256  -1384       C  
ATOM   1020  CG2 VAL A 153     -13.538  12.996 -38.635  1.00 93.76           C  
ANISOU 1020  CG2 VAL A 153    12050  13281  10292    648  -1216  -1450       C  
ATOM   1021  N   ILE A 154      -9.121  13.702 -39.924  1.00 93.93           N  
ANISOU 1021  N   ILE A 154    12271  13122  10296    826  -1235  -1139       N  
ATOM   1022  CA  ILE A 154      -7.961  14.392 -40.483  1.00 92.36           C  
ANISOU 1022  CA  ILE A 154    12103  12881  10107    890  -1240  -1069       C  
ATOM   1023  C   ILE A 154      -7.519  13.707 -41.765  1.00 94.89           C  
ANISOU 1023  C   ILE A 154    12477  13187  10390    939  -1271  -1015       C  
ATOM   1024  O   ILE A 154      -7.220  14.362 -42.773  1.00 96.79           O  
ANISOU 1024  O   ILE A 154    12726  13407  10642   1001  -1293   -979       O  
ATOM   1025  CB  ILE A 154      -6.801  14.413 -39.465  1.00 93.18           C  
ANISOU 1025  CB  ILE A 154    12233  12976  10193    850  -1204  -1038       C  
ATOM   1026  CG1 ILE A 154      -7.026  15.409 -38.332  1.00 89.11           C  
ANISOU 1026  CG1 ILE A 154    11661  12475   9723    816  -1172  -1085       C  
ATOM   1027  CG2 ILE A 154      -5.495  14.756 -40.160  1.00101.15           C  
ANISOU 1027  CG2 ILE A 154    13285  13955  11192    906  -1209   -967       C  
ATOM   1028  CD1 ILE A 154      -5.968  15.294 -37.225  1.00 83.20           C  
ANISOU 1028  CD1 ILE A 154    10938  11723   8950    766  -1136  -1059       C  
ATOM   1029  N   TRP A 155      -7.498  12.372 -41.753  1.00 93.13           N  
ANISOU 1029  N   TRP A 155    12293  12973  10119    906  -1278  -1011       N  
ATOM   1030  CA  TRP A 155      -7.081  11.639 -42.940  1.00 90.63           C  
ANISOU 1030  CA  TRP A 155    12019  12647   9768    951  -1308   -971       C  
ATOM   1031  C   TRP A 155      -8.105  11.774 -44.057  1.00 95.47           C  
ANISOU 1031  C   TRP A 155    12609  13271  10396    995  -1339   -989       C  
ATOM   1032  O   TRP A 155      -7.740  11.816 -45.238  1.00101.85           O  
ANISOU 1032  O   TRP A 155    13437  14071  11189   1049  -1363   -952       O  
ATOM   1033  CB  TRP A 155      -6.834  10.177 -42.592  1.00 86.74           C  
ANISOU 1033  CB  TRP A 155    11574  12153   9229    907  -1320   -969       C  
ATOM   1034  CG  TRP A 155      -5.425   9.955 -42.164  1.00 89.96           C  
ANISOU 1034  CG  TRP A 155    12024  12540   9617    906  -1314   -932       C  
ATOM   1035  CD1 TRP A 155      -4.996   9.664 -40.904  1.00 98.37           C  
ANISOU 1035  CD1 TRP A 155    13109  13595  10671    845  -1301   -934       C  
ATOM   1036  CD2 TRP A 155      -4.246  10.132 -42.957  1.00 92.60           C  
ANISOU 1036  CD2 TRP A 155    12377  12866   9940    965  -1320   -894       C  
ATOM   1037  NE1 TRP A 155      -3.627   9.577 -40.877  1.00100.75           N  
ANISOU 1037  NE1 TRP A 155    13443  13876  10960    872  -1305   -902       N  
ATOM   1038  CE2 TRP A 155      -3.140   9.866 -42.124  1.00 96.75           C  
ANISOU 1038  CE2 TRP A 155    12932  13376  10453    944  -1313   -882       C  
ATOM   1039  CE3 TRP A 155      -4.018  10.457 -44.297  1.00 98.25           C  
ANISOU 1039  CE3 TRP A 155    13089  13593  10649   1026  -1333   -873       C  
ATOM   1040  CZ2 TRP A 155      -1.826   9.917 -42.586  1.00 96.18           C  
ANISOU 1040  CZ2 TRP A 155    12875  13303  10366    987  -1316   -860       C  
ATOM   1041  CZ3 TRP A 155      -2.713  10.506 -44.755  1.00 99.57           C  
ANISOU 1041  CZ3 TRP A 155    13274  13764  10794   1058  -1331   -848       C  
ATOM   1042  CH2 TRP A 155      -1.634  10.239 -43.901  1.00 95.03           C  
ANISOU 1042  CH2 TRP A 155    12719  13178  10211   1041  -1321   -847       C  
ATOM   1043  N   VAL A 156      -9.392  11.830 -43.708  1.00 91.82           N  
ANISOU 1043  N   VAL A 156    12100  12829   9957    968  -1341  -1052       N  
ATOM   1044  CA  VAL A 156     -10.421  11.995 -44.732  1.00 89.15           C  
ANISOU 1044  CA  VAL A 156    11734  12500   9638   1013  -1376  -1078       C  
ATOM   1045  C   VAL A 156     -10.232  13.325 -45.452  1.00 91.45           C  
ANISOU 1045  C   VAL A 156    12014  12763   9968   1081  -1400  -1051       C  
ATOM   1046  O   VAL A 156     -10.156  13.381 -46.689  1.00 87.51           O  
ANISOU 1046  O   VAL A 156    11539  12254   9457   1132  -1434  -1015       O  
ATOM   1047  CB  VAL A 156     -11.822  11.882 -44.106  1.00 78.41           C  
ANISOU 1047  CB  VAL A 156    10316  11177   8301    968  -1370  -1167       C  
ATOM   1048  CG1 VAL A 156     -12.855  12.575 -44.981  1.00 83.54           C  
ANISOU 1048  CG1 VAL A 156    10919  11829   8995   1029  -1411  -1208       C  
ATOM   1049  CG2 VAL A 156     -12.186  10.421 -43.889  1.00 62.39           C  
ANISOU 1049  CG2 VAL A 156     8313   9172   6218    905  -1365  -1184       C  
ATOM   1050  N   LEU A 157     -10.094  14.410 -44.682  1.00 84.20           N  
ANISOU 1050  N   LEU A 157    11065  11832   9095   1076  -1385  -1066       N  
ATOM   1051  CA  LEU A 157      -9.872  15.713 -45.301  1.00 72.98           C  
ANISOU 1051  CA  LEU A 157     9644  10373   7712   1132  -1417  -1036       C  
ATOM   1052  C   LEU A 157      -8.561  15.753 -46.074  1.00 89.04           C  
ANISOU 1052  C   LEU A 157    11742  12389   9701   1153  -1417   -947       C  
ATOM   1053  O   LEU A 157      -8.469  16.418 -47.114  1.00 91.77           O  
ANISOU 1053  O   LEU A 157    12109  12711  10048   1195  -1458   -908       O  
ATOM   1054  CB  LEU A 157      -9.886  16.799 -44.233  1.00 54.33           C  
ANISOU 1054  CB  LEU A 157     7238   7998   5406   1119  -1401  -1072       C  
ATOM   1055  CG  LEU A 157     -11.208  16.911 -43.485  1.00 69.92           C  
ANISOU 1055  CG  LEU A 157     9134  10003   7429   1098  -1402  -1178       C  
ATOM   1056  CD1 LEU A 157     -10.959  17.261 -42.027  1.00 79.57           C  
ANISOU 1056  CD1 LEU A 157    10319  11243   8671   1042  -1353  -1217       C  
ATOM   1057  CD2 LEU A 157     -12.083  17.958 -44.153  1.00 72.13           C  
ANISOU 1057  CD2 LEU A 157     9377  10254   7776   1165  -1470  -1218       C  
ATOM   1058  N   ALA A 158      -7.547  15.028 -45.599  1.00 98.80           N  
ANISOU 1058  N   ALA A 158    13008  13638  10894   1119  -1377   -920       N  
ATOM   1059  CA  ALA A 158      -6.253  15.051 -46.268  1.00 98.58           C  
ANISOU 1059  CA  ALA A 158    13027  13606  10821   1134  -1372   -854       C  
ATOM   1060  C   ALA A 158      -6.321  14.356 -47.620  1.00 91.06           C  
ANISOU 1060  C   ALA A 158    12102  12671   9826   1162  -1402   -833       C  
ATOM   1061  O   ALA A 158      -5.880  14.907 -48.636  1.00 96.48           O  
ANISOU 1061  O   ALA A 158    12813  13354  10491   1186  -1423   -789       O  
ATOM   1062  CB  ALA A 158      -5.198  14.395 -45.379  1.00105.41           C  
ANISOU 1062  CB  ALA A 158    13911  14481  11659   1098  -1330   -847       C  
ATOM   1063  N   LEU A 159      -6.875  13.142 -47.649  1.00 85.24           N  
ANISOU 1063  N   LEU A 159    11363  11953   9070   1153  -1407   -864       N  
ATOM   1064  CA  LEU A 159      -6.986  12.409 -48.903  1.00 84.75           C  
ANISOU 1064  CA  LEU A 159    11321  11911   8969   1180  -1435   -852       C  
ATOM   1065  C   LEU A 159      -7.922  13.102 -49.882  1.00 88.94           C  
ANISOU 1065  C   LEU A 159    11841  12434   9519   1216  -1479   -850       C  
ATOM   1066  O   LEU A 159      -7.677  13.077 -51.095  1.00 90.22           O  
ANISOU 1066  O   LEU A 159    12027  12608   9645   1239  -1504   -816       O  
ATOM   1067  CB  LEU A 159      -7.462  10.984 -48.630  1.00 77.01           C  
ANISOU 1067  CB  LEU A 159    10342  10946   7971   1158  -1436   -890       C  
ATOM   1068  CG  LEU A 159      -6.525  10.138 -47.768  1.00 69.12           C  
ANISOU 1068  CG  LEU A 159     9368   9944   6948   1124  -1414   -889       C  
ATOM   1069  CD1 LEU A 159      -7.170   8.805 -47.432  1.00 61.78           C  
ANISOU 1069  CD1 LEU A 159     8450   9019   6005   1093  -1428   -924       C  
ATOM   1070  CD2 LEU A 159      -5.189   9.935 -48.470  1.00 72.37           C  
ANISOU 1070  CD2 LEU A 159     9808  10369   7322   1151  -1415   -857       C  
ATOM   1071  N   LEU A 160      -8.985  13.738 -49.384  1.00 87.58           N  
ANISOU 1071  N   LEU A 160    11629  12244   9402   1219  -1493   -892       N  
ATOM   1072  CA  LEU A 160      -9.888  14.414 -50.305  1.00 89.63           C  
ANISOU 1072  CA  LEU A 160    11879  12488   9688   1261  -1549   -896       C  
ATOM   1073  C   LEU A 160      -9.305  15.719 -50.829  1.00 90.38           C  
ANISOU 1073  C   LEU A 160    12004  12548   9790   1281  -1579   -839       C  
ATOM   1074  O   LEU A 160      -9.617  16.113 -51.957  1.00 96.58           O  
ANISOU 1074  O   LEU A 160    12811  13319  10565   1310  -1633   -812       O  
ATOM   1075  CB  LEU A 160     -11.242  14.641 -49.636  1.00 91.90           C  
ANISOU 1075  CB  LEU A 160    12106  12773  10037   1263  -1564   -977       C  
ATOM   1076  CG  LEU A 160     -11.934  13.323 -49.268  1.00 96.05           C  
ANISOU 1076  CG  LEU A 160    12610  13340  10544   1231  -1540  -1032       C  
ATOM   1077  CD1 LEU A 160     -13.415  13.538 -49.011  1.00 97.05           C  
ANISOU 1077  CD1 LEU A 160    12673  13479  10722   1237  -1564  -1120       C  
ATOM   1078  CD2 LEU A 160     -11.711  12.239 -50.329  1.00 99.72           C  
ANISOU 1078  CD2 LEU A 160    13115  13825  10951   1242  -1551   -999       C  
ATOM   1079  N   LEU A 161      -8.459  16.399 -50.049  1.00 88.17           N  
ANISOU 1079  N   LEU A 161    11729  12250   9522   1260  -1548   -819       N  
ATOM   1080  CA  LEU A 161      -7.744  17.548 -50.598  1.00 87.63           C  
ANISOU 1080  CA  LEU A 161    11701  12150   9446   1266  -1573   -756       C  
ATOM   1081  C   LEU A 161      -6.696  17.112 -51.615  1.00 84.36           C  
ANISOU 1081  C   LEU A 161    11336  11769   8948   1251  -1562   -696       C  
ATOM   1082  O   LEU A 161      -6.527  17.751 -52.660  1.00 77.40           O  
ANISOU 1082  O   LEU A 161    10495  10876   8037   1253  -1605   -645       O  
ATOM   1083  CB  LEU A 161      -7.083  18.357 -49.481  1.00 92.89           C  
ANISOU 1083  CB  LEU A 161    12356  12792  10144   1245  -1540   -753       C  
ATOM   1084  CG  LEU A 161      -6.138  19.440 -50.019  1.00 97.43           C  
ANISOU 1084  CG  LEU A 161    12982  13339  10696   1235  -1557   -681       C  
ATOM   1085  CD1 LEU A 161      -6.915  20.521 -50.769  1.00 95.31           C  
ANISOU 1085  CD1 LEU A 161    12734  13015  10465   1266  -1646   -665       C  
ATOM   1086  CD2 LEU A 161      -5.255  20.052 -48.935  1.00 96.36           C  
ANISOU 1086  CD2 LEU A 161    12841  13192  10580   1208  -1511   -674       C  
ATOM   1087  N   ALA A 162      -5.979  16.026 -51.325  1.00 91.50           N  
ANISOU 1087  N   ALA A 162    12238  12716   9812   1231  -1510   -705       N  
ATOM   1088  CA  ALA A 162      -4.940  15.555 -52.232  1.00 97.77           C  
ANISOU 1088  CA  ALA A 162    13064  13554  10530   1217  -1497   -670       C  
ATOM   1089  C   ALA A 162      -5.512  14.896 -53.474  1.00 99.29           C  
ANISOU 1089  C   ALA A 162    13266  13774  10686   1236  -1533   -670       C  
ATOM   1090  O   ALA A 162      -4.787  14.735 -54.461  1.00 99.07           O  
ANISOU 1090  O   ALA A 162    13263  13787  10593   1223  -1533   -642       O  
ATOM   1091  CB  ALA A 162      -4.016  14.574 -51.508  1.00101.32           C  
ANISOU 1091  CB  ALA A 162    13504  14035  10957   1200  -1444   -694       C  
ATOM   1092  N   PHE A 163      -6.791  14.515 -53.437  1.00105.61           N  
ANISOU 1092  N   PHE A 163    14042  14561  11526   1262  -1561   -709       N  
ATOM   1093  CA  PHE A 163      -7.371  13.700 -54.503  1.00106.95           C  
ANISOU 1093  CA  PHE A 163    14214  14760  11663   1281  -1590   -719       C  
ATOM   1094  C   PHE A 163      -7.288  14.324 -55.890  1.00 95.72           C  
ANISOU 1094  C   PHE A 163    12829  13345  10197   1283  -1635   -668       C  
ATOM   1095  O   PHE A 163      -6.911  13.606 -56.832  1.00 92.58           O  
ANISOU 1095  O   PHE A 163    12443  12998   9737   1276  -1632   -660       O  
ATOM   1096  CB  PHE A 163      -8.821  13.343 -54.159  1.00112.99           C  
ANISOU 1096  CB  PHE A 163    14942  15509  12481   1304  -1612   -774       C  
ATOM   1097  CG  PHE A 163      -9.474  12.463 -55.184  1.00112.51           C  
ANISOU 1097  CG  PHE A 163    14880  15477  12390   1324  -1640   -789       C  
ATOM   1098  CD1 PHE A 163      -9.267  11.093 -55.167  1.00110.97           C  
ANISOU 1098  CD1 PHE A 163    14680  15318  12165   1315  -1614   -816       C  
ATOM   1099  CD2 PHE A 163     -10.274  13.004 -56.176  1.00105.45           C  
ANISOU 1099  CD2 PHE A 163    13994  14571  11501   1351  -1699   -777       C  
ATOM   1100  CE1 PHE A 163      -9.856  10.275 -56.110  1.00103.07           C  
ANISOU 1100  CE1 PHE A 163    13677  14346  11138   1333  -1639   -833       C  
ATOM   1101  CE2 PHE A 163     -10.866  12.189 -57.122  1.00103.39           C  
ANISOU 1101  CE2 PHE A 163    13731  14341  11212   1369  -1723   -792       C  
ATOM   1102  CZ  PHE A 163     -10.657  10.821 -57.087  1.00102.35           C  
ANISOU 1102  CZ  PHE A 163    13588  14249  11049   1360  -1689   -821       C  
ATOM   1103  N   PRO A 164      -7.632  15.603 -56.110  1.00 88.75           N  
ANISOU 1103  N   PRO A 164    11968  12414   9340   1287  -1683   -633       N  
ATOM   1104  CA  PRO A 164      -7.639  16.096 -57.502  1.00 92.36           C  
ANISOU 1104  CA  PRO A 164    12473  12876   9744   1279  -1738   -580       C  
ATOM   1105  C   PRO A 164      -6.301  15.935 -58.206  1.00 93.27           C  
ANISOU 1105  C   PRO A 164    12620  13051   9767   1230  -1704   -538       C  
ATOM   1106  O   PRO A 164      -6.258  15.565 -59.396  1.00102.80           O  
ANISOU 1106  O   PRO A 164    13847  14304  10908   1217  -1723   -521       O  
ATOM   1107  CB  PRO A 164      -8.011  17.578 -57.336  1.00 95.42           C  
ANISOU 1107  CB  PRO A 164    12887  13186  10182   1286  -1799   -548       C  
ATOM   1108  CG  PRO A 164      -8.812  17.622 -56.074  1.00 91.00           C  
ANISOU 1108  CG  PRO A 164    12270  12589   9715   1321  -1790   -615       C  
ATOM   1109  CD  PRO A 164      -8.182  16.602 -55.173  1.00 87.20           C  
ANISOU 1109  CD  PRO A 164    11755  12154   9222   1302  -1703   -649       C  
ATOM   1110  N   GLN A 165      -5.198  16.116 -57.480  1.00 82.89           N  
ANISOU 1110  N   GLN A 165    11303  11748   8442   1200  -1649   -532       N  
ATOM   1111  CA  GLN A 165      -3.886  16.012 -58.109  1.00 84.18           C  
ANISOU 1111  CA  GLN A 165    11488  11980   8517   1149  -1614   -508       C  
ATOM   1112  C   GLN A 165      -3.583  14.577 -58.515  1.00 80.42           C  
ANISOU 1112  C   GLN A 165    10979  11578   7999   1158  -1581   -557       C  
ATOM   1113  O   GLN A 165      -3.081  14.328 -59.616  1.00 85.45           O  
ANISOU 1113  O   GLN A 165    11628  12283   8557   1127  -1582   -548       O  
ATOM   1114  CB  GLN A 165      -2.804  16.546 -57.177  1.00 87.22           C  
ANISOU 1114  CB  GLN A 165    11872  12360   8907   1119  -1564   -500       C  
ATOM   1115  CG  GLN A 165      -1.419  16.412 -57.765  1.00 84.19           C  
ANISOU 1115  CG  GLN A 165    11498  12058   8431   1064  -1523   -492       C  
ATOM   1116  CD  GLN A 165      -0.453  17.434 -57.219  1.00 86.90           C  
ANISOU 1116  CD  GLN A 165    11862  12390   8765   1019  -1495   -460       C  
ATOM   1117  OE1 GLN A 165      -0.619  18.636 -57.429  1.00 85.31           O  
ANISOU 1117  OE1 GLN A 165    11709  12141   8564    990  -1534   -401       O  
ATOM   1118  NE2 GLN A 165       0.565  16.965 -56.510  1.00 92.95           N  
ANISOU 1118  NE2 GLN A 165    12595  13196   9526   1013  -1433   -501       N  
ATOM   1119  N   GLY A 166      -3.888  13.613 -57.647  1.00 79.02           N  
ANISOU 1119  N   GLY A 166    10761  11392   7871   1195  -1558   -613       N  
ATOM   1120  CA  GLY A 166      -3.655  12.229 -58.014  1.00 87.27           C  
ANISOU 1120  CA  GLY A 166    11780  12494   8885   1208  -1542   -662       C  
ATOM   1121  C   GLY A 166      -4.596  11.773 -59.104  1.00102.23           C  
ANISOU 1121  C   GLY A 166    13676  14405  10761   1227  -1584   -666       C  
ATOM   1122  O   GLY A 166      -4.256  10.891 -59.897  1.00111.07           O  
ANISOU 1122  O   GLY A 166    14783  15589  11831   1226  -1579   -694       O  
ATOM   1123  N   TYR A 167      -5.782  12.380 -59.166  1.00105.40           N  
ANISOU 1123  N   TYR A 167    14090  14753  11205   1247  -1629   -644       N  
ATOM   1124  CA  TYR A 167      -6.740  12.075 -60.221  1.00107.83           C  
ANISOU 1124  CA  TYR A 167    14401  15073  11498   1267  -1676   -645       C  
ATOM   1125  C   TYR A 167      -6.224  12.506 -61.590  1.00108.57           C  
ANISOU 1125  C   TYR A 167    14530  15216  11504   1227  -1697   -599       C  
ATOM   1126  O   TYR A 167      -6.479  11.830 -62.595  1.00104.40           O  
ANISOU 1126  O   TYR A 167    13998  14738  10933   1231  -1713   -612       O  
ATOM   1127  CB  TYR A 167      -8.071  12.754 -59.892  1.00115.18           C  
ANISOU 1127  CB  TYR A 167    15333  15932  12500   1300  -1725   -643       C  
ATOM   1128  CG  TYR A 167      -9.222  12.478 -60.833  1.00123.09           C  
ANISOU 1128  CG  TYR A 167    16332  16935  13500   1329  -1779   -652       C  
ATOM   1129  CD1 TYR A 167      -9.970  11.309 -60.730  1.00129.61           C  
ANISOU 1129  CD1 TYR A 167    17120  17779  14347   1359  -1771   -711       C  
ATOM   1130  CD2 TYR A 167      -9.594  13.412 -61.794  1.00126.10           C  
ANISOU 1130  CD2 TYR A 167    16755  17295  13861   1325  -1846   -602       C  
ATOM   1131  CE1 TYR A 167     -11.041  11.070 -61.577  1.00134.21           C  
ANISOU 1131  CE1 TYR A 167    17698  18365  14929   1387  -1820   -724       C  
ATOM   1132  CE2 TYR A 167     -10.659  13.183 -62.646  1.00129.11           C  
ANISOU 1132  CE2 TYR A 167    17136  17677  14243   1355  -1902   -613       C  
ATOM   1133  CZ  TYR A 167     -11.380  12.013 -62.533  1.00131.90           C  
ANISOU 1133  CZ  TYR A 167    17443  18055  14619   1388  -1885   -676       C  
ATOM   1134  OH  TYR A 167     -12.438  11.783 -63.385  1.00127.32           O  
ANISOU 1134  OH  TYR A 167    16859  17477  14039   1418  -1938   -691       O  
ATOM   1135  N   TYR A 168      -5.484  13.615 -61.656  1.00111.69           N  
ANISOU 1135  N   TYR A 168    14964  15604  11869   1181  -1697   -545       N  
ATOM   1136  CA  TYR A 168      -5.037  14.125 -62.954  1.00100.18           C  
ANISOU 1136  CA  TYR A 168    13551  14195  10319   1123  -1722   -495       C  
ATOM   1137  C   TYR A 168      -3.608  13.740 -63.347  1.00 86.40           C  
ANISOU 1137  C   TYR A 168    11794  12549   8485   1066  -1664   -511       C  
ATOM   1138  O   TYR A 168      -3.126  14.207 -64.384  1.00 84.20           O  
ANISOU 1138  O   TYR A 168    11551  12324   8116    999  -1676   -472       O  
ATOM   1139  CB  TYR A 168      -5.195  15.644 -62.998  1.00107.43           C  
ANISOU 1139  CB  TYR A 168    14532  15043  11243   1094  -1775   -420       C  
ATOM   1140  CG  TYR A 168      -6.641  16.072 -63.066  1.00118.10           C  
ANISOU 1140  CG  TYR A 168    15897  16311  12663   1147  -1856   -409       C  
ATOM   1141  CD1 TYR A 168      -7.531  15.442 -63.922  1.00117.22           C  
ANISOU 1141  CD1 TYR A 168    15778  16218  12541   1176  -1895   -426       C  
ATOM   1142  CD2 TYR A 168      -7.121  17.092 -62.261  1.00129.83           C  
ANISOU 1142  CD2 TYR A 168    17398  17702  14229   1171  -1895   -393       C  
ATOM   1143  CE1 TYR A 168      -8.858  15.829 -63.986  1.00121.06           C  
ANISOU 1143  CE1 TYR A 168    16271  16632  13093   1228  -1972   -428       C  
ATOM   1144  CE2 TYR A 168      -8.447  17.484 -62.317  1.00132.84           C  
ANISOU 1144  CE2 TYR A 168    17783  18012  14680   1226  -1975   -402       C  
ATOM   1145  CZ  TYR A 168      -9.311  16.848 -63.180  1.00126.91           C  
ANISOU 1145  CZ  TYR A 168    17023  17282  13915   1255  -2013   -420       C  
ATOM   1146  OH  TYR A 168     -10.631  17.237 -63.236  1.00130.20           O  
ANISOU 1146  OH  TYR A 168    17437  17631  14403   1312  -2096   -439       O  
ATOM   1147  N   SER A 169      -2.905  12.942 -62.549  1.00 93.58           N  
ANISOU 1147  N   SER A 169    12655  13486   9416   1085  -1606   -571       N  
ATOM   1148  CA  SER A 169      -1.602  12.433 -62.963  1.00106.06           C  
ANISOU 1148  CA  SER A 169    14208  15169  10920   1043  -1558   -612       C  
ATOM   1149  C   SER A 169      -1.767  11.310 -63.982  1.00112.39           C  
ANISOU 1149  C   SER A 169    14978  16047  11677   1055  -1565   -662       C  
ATOM   1150  O   SER A 169      -2.699  10.504 -63.899  1.00123.33           O  
ANISOU 1150  O   SER A 169    16345  17402  13114   1114  -1587   -690       O  
ATOM   1151  CB  SER A 169      -0.811  11.926 -61.756  1.00113.57           C  
ANISOU 1151  CB  SER A 169    15119  16115  11916   1069  -1508   -666       C  
ATOM   1152  OG  SER A 169      -0.865  12.846 -60.680  1.00109.11           O  
ANISOU 1152  OG  SER A 169    14577  15471  11409   1071  -1503   -626       O  
ATOM   1153  N   THR A 170      -0.835  11.236 -64.931  1.00106.84           N  
ANISOU 1153  N   THR A 170    14265  15452  10877    993  -1543   -681       N  
ATOM   1154  CA  THR A 170      -0.921  10.217 -65.972  1.00104.91           C  
ANISOU 1154  CA  THR A 170    13985  15292  10585    998  -1548   -736       C  
ATOM   1155  C   THR A 170       0.435  10.024 -66.635  1.00111.12           C  
ANISOU 1155  C   THR A 170    14735  16212  11274    931  -1505   -792       C  
ATOM   1156  O   THR A 170       1.302  10.905 -66.603  1.00109.12           O  
ANISOU 1156  O   THR A 170    14503  15992  10968    859  -1477   -765       O  
ATOM   1157  CB  THR A 170      -1.976  10.566 -67.032  1.00 96.31           C  
ANISOU 1157  CB  THR A 170    12939  14193   9463    982  -1603   -678       C  
ATOM   1158  OG1 THR A 170      -2.029   9.521 -68.012  1.00 98.26           O  
ANISOU 1158  OG1 THR A 170    13144  14528   9663    988  -1604   -739       O  
ATOM   1159  CG2 THR A 170      -1.637  11.879 -67.720  1.00 91.26           C  
ANISOU 1159  CG2 THR A 170    12364  13573   8738    886  -1619   -596       C  
ATOM   1160  N   THR A 171       0.600   8.842 -67.231  1.00113.67           N  
ANISOU 1160  N   THR A 171    15000  16614  11576    955  -1500   -879       N  
ATOM   1161  CA  THR A 171       1.803   8.474 -67.965  1.00118.70           C  
ANISOU 1161  CA  THR A 171    15582  17394  12123    899  -1462   -960       C  
ATOM   1162  C   THR A 171       1.606   8.730 -69.452  1.00123.96           C  
ANISOU 1162  C   THR A 171    16265  18153  12680    820  -1475   -936       C  
ATOM   1163  O   THR A 171       0.578   8.352 -70.027  1.00122.11           O  
ANISOU 1163  O   THR A 171    16044  17896  12458    851  -1515   -917       O  
ATOM   1164  CB  THR A 171       2.162   7.003 -67.749  1.00120.28           C  
ANISOU 1164  CB  THR A 171    15703  17631  12368    973  -1458  -1085       C  
ATOM   1165  OG1 THR A 171       1.013   6.186 -68.008  1.00129.93           O  
ANISOU 1165  OG1 THR A 171    16924  18806  13637   1037  -1500  -1088       O  
ATOM   1166  CG2 THR A 171       2.649   6.773 -66.334  1.00116.00           C  
ANISOU 1166  CG2 THR A 171    15146  17017  11912   1030  -1445  -1116       C  
ATOM   1167  N   GLU A 172       2.596   9.361 -70.065  1.00129.76           N  
ANISOU 1167  N   GLU A 172    17000  18996  13307    712  -1441   -940       N  
ATOM   1168  CA  GLU A 172       2.674   9.536 -71.507  1.00126.24           C  
ANISOU 1168  CA  GLU A 172    16563  18669  12735    613  -1445   -933       C  
ATOM   1169  C   GLU A 172       3.843   8.684 -71.979  1.00123.27           C  
ANISOU 1169  C   GLU A 172    16086  18455  12296    584  -1395  -1077       C  
ATOM   1170  O   GLU A 172       5.012   9.024 -71.746  1.00129.64           O  
ANISOU 1170  O   GLU A 172    16864  19336  13057    525  -1347  -1122       O  
ATOM   1171  CB  GLU A 172       2.850  11.005 -71.879  1.00124.39           C  
ANISOU 1171  CB  GLU A 172    16418  18433  12411    490  -1452   -821       C  
ATOM   1172  CG  GLU A 172       1.767  11.912 -71.320  1.00127.57           C  
ANISOU 1172  CG  GLU A 172    16914  18667  12888    528  -1511   -693       C  
ATOM   1173  CD  GLU A 172       2.086  13.383 -71.490  1.00135.91           C  
ANISOU 1173  CD  GLU A 172    18062  19705  13871    413  -1526   -588       C  
ATOM   1174  OE1 GLU A 172       3.165  13.700 -72.031  1.00142.22           O  
ANISOU 1174  OE1 GLU A 172    18855  20628  14554    294  -1483   -610       O  
ATOM   1175  OE2 GLU A 172       1.255  14.221 -71.077  1.00141.73           O  
ANISOU 1175  OE2 GLU A 172    18878  20306  14668    440  -1583   -489       O  
ATOM   1176  N   THR A 173       3.512   7.536 -72.569  1.00115.59           N  
ANISOU 1176  N   THR A 173    15052  17533  11332    635  -1409  -1159       N  
ATOM   1177  CA  THR A 173       4.499   6.760 -73.303  1.00109.23           C  
ANISOU 1177  CA  THR A 173    14148  16900  10455    598  -1373  -1302       C  
ATOM   1178  C   THR A 173       4.911   7.557 -74.527  1.00120.43           C  
ANISOU 1178  C   THR A 173    15589  18457  11712    438  -1349  -1274       C  
ATOM   1179  O   THR A 173       4.071   8.128 -75.225  1.00135.19           O  
ANISOU 1179  O   THR A 173    17535  20302  13529    384  -1384  -1167       O  
ATOM   1180  CB  THR A 173       3.914   5.419 -73.746  1.00 98.71           C  
ANISOU 1180  CB  THR A 173    12755  15583   9168    686  -1404  -1386       C  
ATOM   1181  OG1 THR A 173       3.271   4.789 -72.633  1.00105.45           O  
ANISOU 1181  OG1 THR A 173    13616  16285  10164    819  -1437  -1380       O  
ATOM   1182  CG2 THR A 173       5.019   4.500 -74.268  1.00 92.35           C  
ANISOU 1182  CG2 THR A 173    11829  14942   8317    674  -1372  -1562       C  
ATOM   1183  N   MET A 174       6.200   7.589 -74.796  1.00119.24           N  
ANISOU 1183  N   MET A 174    15372  18455  11479    357  -1294  -1373       N  
ATOM   1184  CA  MET A 174       6.669   8.575 -75.751  1.00127.05           C  
ANISOU 1184  CA  MET A 174    16402  19563  12307    180  -1267  -1325       C  
ATOM   1185  C   MET A 174       7.935   8.059 -76.434  1.00143.19           C  
ANISOU 1185  C   MET A 174    18330  21808  14268     98  -1203  -1486       C  
ATOM   1186  O   MET A 174       8.227   6.862 -76.318  1.00154.75           O  
ANISOU 1186  O   MET A 174    19686  23295  15819    191  -1192  -1622       O  
ATOM   1187  CB  MET A 174       6.806   9.936 -75.065  1.00118.62           C  
ANISOU 1187  CB  MET A 174    15426  18403  11240    128  -1260  -1207       C  
ATOM   1188  CG  MET A 174       7.202  11.049 -76.018  1.00115.40           C  
ANISOU 1188  CG  MET A 174    15153  17846  10849    119  -1325  -1026       C  
ATOM   1189  SD  MET A 174       7.243  12.651 -75.207  1.00116.53           S  
ANISOU 1189  SD  MET A 174    15412  18001  10863    -64  -1322   -896       S  
ATOM   1190  CE  MET A 174       5.494  13.054 -75.135  1.00117.15           C  
ANISOU 1190  CE  MET A 174    15398  18213  10900   -120  -1229  -1025       C  
ATOM   1191  N   PRO A 175       8.678   8.874 -77.215  1.00143.05           N  
ANISOU 1191  N   PRO A 175    18329  21896  14127    -81  -1152  -1465       N  
ATOM   1192  CA  PRO A 175       9.796   8.294 -77.968  1.00140.80           C  
ANISOU 1192  CA  PRO A 175    17922  21764  13812   -159  -1078  -1613       C  
ATOM   1193  C   PRO A 175      10.909   7.702 -77.123  1.00136.86           C  
ANISOU 1193  C   PRO A 175    17306  21295  13399    -87  -1033  -1764       C  
ATOM   1194  O   PRO A 175      11.102   6.483 -77.106  1.00148.94           O  
ANISOU 1194  O   PRO A 175    18724  22848  15020     16  -1033  -1902       O  
ATOM   1195  CB  PRO A 175      10.300   9.478 -78.798  1.00142.55           C  
ANISOU 1195  CB  PRO A 175    18209  22069  13882   -371  -1039  -1534       C  
ATOM   1196  CG  PRO A 175       9.173  10.449 -78.798  1.00139.39           C  
ANISOU 1196  CG  PRO A 175    17970  21556  13434   -395  -1114  -1341       C  
ATOM   1197  CD  PRO A 175       8.590  10.326 -77.462  1.00140.92           C  
ANISOU 1197  CD  PRO A 175    18188  21613  13740   -226  -1164  -1311       C  
ATOM   1198  N   SER A 176      11.661   8.555 -76.431  1.00123.25           N  
ANISOU 1198  N   SER A 176    15610  19570  11651   -140  -1000  -1740       N  
ATOM   1199  CA  SER A 176      12.795   8.060 -75.662  1.00119.59           C  
ANISOU 1199  CA  SER A 176    15035  19140  11264    -80   -958  -1885       C  
ATOM   1200  C   SER A 176      12.394   7.551 -74.281  1.00123.71           C  
ANISOU 1200  C   SER A 176    15563  19520  11920    107  -1012  -1892       C  
ATOM   1201  O   SER A 176      13.054   6.654 -73.745  1.00126.68           O  
ANISOU 1201  O   SER A 176    15835  19902  12395    204  -1006  -2032       O  
ATOM   1202  CB  SER A 176      13.855   9.156 -75.537  1.00110.96           C  
ANISOU 1202  CB  SER A 176    13958  18114  10087   -223   -893  -1868       C  
ATOM   1203  OG  SER A 176      13.270  10.371 -75.104  1.00100.43           O  
ANISOU 1203  OG  SER A 176    12773  16687   8698   -269   -925  -1691       O  
ATOM   1204  N   ARG A 177      11.321   8.080 -73.698  1.00119.86           N  
ANISOU 1204  N   ARG A 177    15195  18904  11444    160  -1071  -1746       N  
ATOM   1205  CA  ARG A 177      11.053   7.838 -72.290  1.00107.21           C  
ANISOU 1205  CA  ARG A 177    13610  17167   9958    311  -1113  -1738       C  
ATOM   1206  C   ARG A 177       9.556   7.848 -72.018  1.00107.43           C  
ANISOU 1206  C   ARG A 177    13734  17010  10074    395  -1174  -1592       C  
ATOM   1207  O   ARG A 177       8.754   8.316 -72.829  1.00111.35           O  
ANISOU 1207  O   ARG A 177    14301  17500  10508    331  -1194  -1488       O  
ATOM   1208  CB  ARG A 177      11.745   8.884 -71.413  1.00105.32           C  
ANISOU 1208  CB  ARG A 177    13412  16891   9713    262  -1076  -1684       C  
ATOM   1209  CG  ARG A 177      11.456  10.324 -71.826  1.00 99.52           C  
ANISOU 1209  CG  ARG A 177    12796  16140   8877    119  -1066  -1519       C  
ATOM   1210  CD  ARG A 177      12.005  11.301 -70.804  1.00113.51           C  
ANISOU 1210  CD  ARG A 177    14615  17844  10672     94  -1039  -1458       C  
ATOM   1211  NE  ARG A 177      11.912  12.693 -71.235  1.00121.39           N  
ANISOU 1211  NE  ARG A 177    15722  18839  11563    -56  -1033  -1316       N  
ATOM   1212  CZ  ARG A 177      12.957  13.453 -71.547  1.00129.49           C  
ANISOU 1212  CZ  ARG A 177    16745  19992  12464   -208   -978  -1339       C  
ATOM   1213  NH1 ARG A 177      14.186  12.960 -71.476  1.00126.64           N  
ANISOU 1213  NH1 ARG A 177    16265  19781  12071   -225   -919  -1508       N  
ATOM   1214  NH2 ARG A 177      12.776  14.712 -71.925  1.00136.81           N  
ANISOU 1214  NH2 ARG A 177    17788  20894  13298   -344   -988  -1196       N  
ATOM   1215  N   VAL A 178       9.196   7.289 -70.867  1.00106.68           N  
ANISOU 1215  N   VAL A 178    13640  16771  10124    537  -1206  -1593       N  
ATOM   1216  CA  VAL A 178       7.858   7.414 -70.300  1.00101.13           C  
ANISOU 1216  CA  VAL A 178    13026  15883   9516    616  -1256  -1459       C  
ATOM   1217  C   VAL A 178       7.873   8.583 -69.325  1.00103.03           C  
ANISOU 1217  C   VAL A 178    13346  16014   9787    595  -1245  -1343       C  
ATOM   1218  O   VAL A 178       8.813   8.722 -68.533  1.00108.61           O  
ANISOU 1218  O   VAL A 178    14022  16731  10515    600  -1213  -1394       O  
ATOM   1219  CB  VAL A 178       7.443   6.112 -69.596  1.00 93.52           C  
ANISOU 1219  CB  VAL A 178    12020  14830   8685    767  -1299  -1530       C  
ATOM   1220  CG1 VAL A 178       6.018   6.214 -69.075  1.00 85.19           C  
ANISOU 1220  CG1 VAL A 178    11048  13603   7716    835  -1345  -1404       C  
ATOM   1221  CG2 VAL A 178       7.610   4.923 -70.541  1.00102.82           C  
ANISOU 1221  CG2 VAL A 178    13107  16125   9836    790  -1312  -1667       C  
ATOM   1222  N   VAL A 179       6.841   9.428 -69.364  1.00103.80           N  
ANISOU 1222  N   VAL A 179    13544  16007   9890    574  -1275  -1194       N  
ATOM   1223  CA  VAL A 179       6.838  10.559 -68.441  1.00112.01           C  
ANISOU 1223  CA  VAL A 179    14656  16941  10963    557  -1270  -1090       C  
ATOM   1224  C   VAL A 179       5.558  10.578 -67.617  1.00120.97           C  
ANISOU 1224  C   VAL A 179    15847  17897  12219    658  -1319  -1002       C  
ATOM   1225  O   VAL A 179       4.487  10.159 -68.065  1.00117.27           O  
ANISOU 1225  O   VAL A 179    15396  17387  11775    700  -1362   -974       O  
ATOM   1226  CB  VAL A 179       7.045  11.913 -69.152  1.00111.45           C  
ANISOU 1226  CB  VAL A 179    14660  16914  10772    410  -1260   -993       C  
ATOM   1227  CG1 VAL A 179       8.402  11.945 -69.843  1.00114.51           C  
ANISOU 1227  CG1 VAL A 179    14987  17490  11032    294  -1200  -1089       C  
ATOM   1228  CG2 VAL A 179       5.919  12.194 -70.127  1.00113.48           C  
ANISOU 1228  CG2 VAL A 179    14987  17141  10989    379  -1314   -899       C  
ATOM   1229  N   CYS A 180       5.692  11.068 -66.388  1.00127.63           N  
ANISOU 1229  N   CYS A 180    16714  18643  13136    692  -1310   -966       N  
ATOM   1230  CA  CYS A 180       4.600  11.187 -65.428  1.00132.55           C  
ANISOU 1230  CA  CYS A 180    17382  19106  13874    777  -1347   -895       C  
ATOM   1231  C   CYS A 180       4.277  12.670 -65.282  1.00131.94           C  
ANISOU 1231  C   CYS A 180    17391  18957  13784    717  -1361   -772       C  
ATOM   1232  O   CYS A 180       5.104  13.443 -64.786  1.00132.24           O  
ANISOU 1232  O   CYS A 180    17442  19002  13803    668  -1328   -756       O  
ATOM   1233  CB  CYS A 180       5.003  10.555 -64.094  1.00135.79           C  
ANISOU 1233  CB  CYS A 180    17750  19463  14380    860  -1332   -957       C  
ATOM   1234  SG  CYS A 180       3.944  10.904 -62.666  1.00137.88           S  
ANISOU 1234  SG  CYS A 180    18064  19550  14773    936  -1359   -879       S  
ATOM   1235  N   LYS A 181       3.083  13.071 -65.721  1.00126.82           N  
ANISOU 1235  N   LYS A 181    16801  18236  13147    724  -1416   -689       N  
ATOM   1236  CA  LYS A 181       2.730  14.483 -65.749  1.00122.06           C  
ANISOU 1236  CA  LYS A 181    16286  17562  12529    667  -1450   -575       C  
ATOM   1237  C   LYS A 181       1.307  14.671 -65.244  1.00115.75           C  
ANISOU 1237  C   LYS A 181    15523  16623  11835    749  -1509   -520       C  
ATOM   1238  O   LYS A 181       0.475  13.767 -65.340  1.00127.46           O  
ANISOU 1238  O   LYS A 181    16976  18088  13365    822  -1531   -554       O  
ATOM   1239  CB  LYS A 181       2.866  15.075 -67.164  1.00125.83           C  
ANISOU 1239  CB  LYS A 181    16815  18119  12877    551  -1471   -526       C  
ATOM   1240  CG  LYS A 181       2.800  16.599 -67.202  1.00131.48           C  
ANISOU 1240  CG  LYS A 181    17629  18766  13561    471  -1510   -411       C  
ATOM   1241  CD  LYS A 181       2.705  17.148 -68.618  1.00127.37           C  
ANISOU 1241  CD  LYS A 181    17178  18303  12914    356  -1553   -347       C  
ATOM   1242  CE  LYS A 181       2.472  18.654 -68.594  1.00123.10           C  
ANISOU 1242  CE  LYS A 181    16751  17662  12360    289  -1617   -225       C  
ATOM   1243  NZ  LYS A 181       2.501  19.266 -69.950  1.00114.38           N  
ANISOU 1243  NZ  LYS A 181    15730  16612  11118    155  -1665   -153       N  
ATOM   1244  N   ILE A 182       1.038  15.851 -64.696  1.00 98.30           N  
ANISOU 1244  N   ILE A 182    13373  14316   9662    737  -1538   -442       N  
ATOM   1245  CA  ILE A 182      -0.294  16.216 -64.234  1.00 98.06           C  
ANISOU 1245  CA  ILE A 182    13373  14158   9728    807  -1600   -397       C  
ATOM   1246  C   ILE A 182      -0.970  17.016 -65.337  1.00102.30           C  
ANISOU 1246  C   ILE A 182    13987  14669  10214    758  -1679   -317       C  
ATOM   1247  O   ILE A 182      -0.587  18.158 -65.618  1.00 94.47           O  
ANISOU 1247  O   ILE A 182    13065  13660   9169    678  -1706   -245       O  
ATOM   1248  CB  ILE A 182      -0.247  17.015 -62.930  1.00 98.00           C  
ANISOU 1248  CB  ILE A 182    13377  14055   9804    832  -1594   -374       C  
ATOM   1249  CG1 ILE A 182       0.623  16.300 -61.905  1.00 94.45           C  
ANISOU 1249  CG1 ILE A 182    12861  13639   9386    861  -1518   -447       C  
ATOM   1250  CG2 ILE A 182      -1.654  17.205 -62.394  1.00 88.96           C  
ANISOU 1250  CG2 ILE A 182    12239  12794   8766    913  -1653   -358       C  
ATOM   1251  CD1 ILE A 182       0.565  16.931 -60.568  1.00 85.27           C  
ANISOU 1251  CD1 ILE A 182    11701  12387   8310    892  -1510   -433       C  
ATOM   1252  N   GLU A 183      -1.978  16.416 -65.962  1.00106.57           N  
ANISOU 1252  N   GLU A 183    14521  15204  10768    804  -1722   -327       N  
ATOM   1253  CA  GLU A 183      -2.742  17.073 -67.018  1.00106.87           C  
ANISOU 1253  CA  GLU A 183    14631  15210  10763    770  -1809   -255       C  
ATOM   1254  C   GLU A 183      -3.918  17.801 -66.385  1.00105.52           C  
ANISOU 1254  C   GLU A 183    14493  14897  10704    841  -1885   -219       C  
ATOM   1255  O   GLU A 183      -5.030  17.278 -66.295  1.00 96.00           O  
ANISOU 1255  O   GLU A 183    13258  13650   9569    924  -1918   -251       O  
ATOM   1256  CB  GLU A 183      -3.187  16.059 -68.062  1.00108.70           C  
ANISOU 1256  CB  GLU A 183    14836  15518  10949    780  -1817   -291       C  
ATOM   1257  CG  GLU A 183      -2.150  15.835 -69.146  1.00110.58           C  
ANISOU 1257  CG  GLU A 183    15074  15895  11045    673  -1778   -299       C  
ATOM   1258  CD  GLU A 183      -1.811  17.118 -69.879  1.00110.82           C  
ANISOU 1258  CD  GLU A 183    15204  15923  10979    553  -1827   -202       C  
ATOM   1259  OE1 GLU A 183      -2.737  17.911 -70.148  1.00112.33           O  
ANISOU 1259  OE1 GLU A 183    15472  16015  11195    561  -1922   -126       O  
ATOM   1260  OE2 GLU A 183      -0.618  17.339 -70.174  1.00109.30           O  
ANISOU 1260  OE2 GLU A 183    15016  15829  10686    449  -1775   -205       O  
ATOM   1261  N   TRP A 184      -3.668  19.028 -65.940  1.00118.64           N  
ANISOU 1261  N   TRP A 184    16211  16485  12381    808  -1916   -160       N  
ATOM   1262  CA  TRP A 184      -4.734  19.842 -65.386  1.00133.55           C  
ANISOU 1262  CA  TRP A 184    18129  18239  14376    872  -2000   -134       C  
ATOM   1263  C   TRP A 184      -5.701  20.239 -66.499  1.00132.37           C  
ANISOU 1263  C   TRP A 184    18045  18046  14204    869  -2112    -83       C  
ATOM   1264  O   TRP A 184      -5.315  20.294 -67.670  1.00138.51           O  
ANISOU 1264  O   TRP A 184    18875  18887  14866    783  -2131    -37       O  
ATOM   1265  CB  TRP A 184      -4.168  21.088 -64.709  1.00149.80           C  
ANISOU 1265  CB  TRP A 184    20236  20229  16453    833  -2013    -84       C  
ATOM   1266  CG  TRP A 184      -3.307  20.810 -63.503  1.00150.93           C  
ANISOU 1266  CG  TRP A 184    20316  20399  16631    845  -1912   -133       C  
ATOM   1267  CD1 TRP A 184      -1.960  21.007 -63.391  1.00152.51           C  
ANISOU 1267  CD1 TRP A 184    20523  20665  16759    765  -1843   -123       C  
ATOM   1268  CD2 TRP A 184      -3.741  20.293 -62.240  1.00148.23           C  
ANISOU 1268  CD2 TRP A 184    19898  20021  16401    936  -1871   -203       C  
ATOM   1269  NE1 TRP A 184      -1.530  20.644 -62.138  1.00146.33           N  
ANISOU 1269  NE1 TRP A 184    19673  19884  16042    809  -1768   -180       N  
ATOM   1270  CE2 TRP A 184      -2.605  20.204 -61.411  1.00147.57           C  
ANISOU 1270  CE2 TRP A 184    19783  19978  16309    910  -1784   -225       C  
ATOM   1271  CE3 TRP A 184      -4.981  19.896 -61.729  1.00149.37           C  
ANISOU 1271  CE3 TRP A 184    19998  20110  16648   1030  -1901   -252       C  
ATOM   1272  CZ2 TRP A 184      -2.671  19.729 -60.100  1.00152.66           C  
ANISOU 1272  CZ2 TRP A 184    20360  20602  17040    972  -1731   -287       C  
ATOM   1273  CZ3 TRP A 184      -5.046  19.427 -60.428  1.00151.98           C  
ANISOU 1273  CZ3 TRP A 184    20259  20428  17059   1083  -1842   -315       C  
ATOM   1274  CH2 TRP A 184      -3.898  19.348 -59.628  1.00153.98           C  
ANISOU 1274  CH2 TRP A 184    20490  20716  17299   1053  -1761   -328       C  
ATOM   1275  N   PRO A 185      -6.959  20.526 -66.162  1.00128.30           N  
ANISOU 1275  N   PRO A 185    17526  17428  13794    957  -2192    -96       N  
ATOM   1276  CA  PRO A 185      -7.946  20.815 -67.207  1.00136.48           C  
ANISOU 1276  CA  PRO A 185    18618  18420  14818    967  -2307    -59       C  
ATOM   1277  C   PRO A 185      -7.529  22.015 -68.046  1.00155.30           C  
ANISOU 1277  C   PRO A 185    21124  20765  17117    867  -2395     48       C  
ATOM   1278  O   PRO A 185      -6.966  22.988 -67.543  1.00156.49           O  
ANISOU 1278  O   PRO A 185    21321  20861  17276    827  -2408     91       O  
ATOM   1279  CB  PRO A 185      -9.223  21.098 -66.408  1.00124.63           C  
ANISOU 1279  CB  PRO A 185    17083  16810  13462   1081  -2372   -107       C  
ATOM   1280  CG  PRO A 185      -9.072  20.261 -65.191  1.00112.07           C  
ANISOU 1280  CG  PRO A 185    15390  15255  11937   1133  -2261   -192       C  
ATOM   1281  CD  PRO A 185      -7.601  20.273 -64.859  1.00115.58           C  
ANISOU 1281  CD  PRO A 185    15839  15762  12315   1057  -2167   -169       C  
ATOM   1282  N   GLU A 186      -7.823  21.929 -69.344  1.00170.17           N  
ANISOU 1282  N   GLU A 186    23064  22679  18915    821  -2458     91       N  
ATOM   1283  CA  GLU A 186      -7.206  22.784 -70.356  1.00182.53           C  
ANISOU 1283  CA  GLU A 186    24748  24251  20355    689  -2520    194       C  
ATOM   1284  C   GLU A 186      -7.857  24.156 -70.478  1.00184.26           C  
ANISOU 1284  C   GLU A 186    25077  24314  20618    692  -2682    271       C  
ATOM   1285  O   GLU A 186      -8.099  24.629 -71.590  1.00197.51           O  
ANISOU 1285  O   GLU A 186    26857  25971  22219    625  -2788    347       O  
ATOM   1286  CB  GLU A 186      -7.235  22.062 -71.700  1.00193.45           C  
ANISOU 1286  CB  GLU A 186    26142  25739  21619    630  -2518    205       C  
ATOM   1287  CG  GLU A 186      -6.662  20.656 -71.657  1.00199.99           C  
ANISOU 1287  CG  GLU A 186    26859  26717  22410    637  -2375    118       C  
ATOM   1288  CD  GLU A 186      -5.145  20.637 -71.629  1.00201.86           C  
ANISOU 1288  CD  GLU A 186    27090  27064  22543    524  -2272    121       C  
ATOM   1289  OE1 GLU A 186      -4.532  21.718 -71.752  1.00204.07           O  
ANISOU 1289  OE1 GLU A 186    27459  27315  22762    424  -2308    199       O  
ATOM   1290  OE2 GLU A 186      -4.563  19.540 -71.489  1.00202.72           O  
ANISOU 1290  OE2 GLU A 186    27105  27289  22631    534  -2160     40       O  
ATOM   1291  N   HIS A 187      -8.139  24.824 -69.368  1.00175.69           N  
ANISOU 1291  N   HIS A 187    23977  23119  19656    765  -2711    251       N  
ATOM   1292  CA  HIS A 187      -8.540  26.220 -69.455  1.00167.40           C  
ANISOU 1292  CA  HIS A 187    23038  21920  18645    756  -2868    324       C  
ATOM   1293  C   HIS A 187      -7.315  27.051 -69.822  1.00166.04           C  
ANISOU 1293  C   HIS A 187    22973  21764  18350    601  -2868    424       C  
ATOM   1294  O   HIS A 187      -6.280  26.943 -69.150  1.00145.59           O  
ANISOU 1294  O   HIS A 187    20341  19239  15736    558  -2747    407       O  
ATOM   1295  CB  HIS A 187      -9.165  26.688 -68.138  1.00165.00           C  
ANISOU 1295  CB  HIS A 187    22677  21504  18512    878  -2896    259       C  
ATOM   1296  CG  HIS A 187     -10.431  25.966 -67.781  1.00171.02           C  
ANISOU 1296  CG  HIS A 187    23338  22251  19390   1017  -2906    156       C  
ATOM   1297  ND1 HIS A 187     -11.543  26.608 -67.277  1.00172.83           N  
ANISOU 1297  ND1 HIS A 187    23555  22354  19760   1125  -3022    110       N  
ATOM   1298  CD2 HIS A 187     -10.759  24.654 -67.857  1.00173.95           C  
ANISOU 1298  CD2 HIS A 187    23613  22722  19757   1063  -2814     83       C  
ATOM   1299  CE1 HIS A 187     -12.499  25.722 -67.057  1.00172.75           C  
ANISOU 1299  CE1 HIS A 187    23443  22374  19819   1224  -2995     12       C  
ATOM   1300  NE2 HIS A 187     -12.048  24.529 -67.401  1.00174.10           N  
ANISOU 1300  NE2 HIS A 187    23566  22678  19905   1187  -2871     -1       N  
ATOM   1301  N   PRO A 188      -7.385  27.871 -70.878  1.00186.47           N  
ANISOU 1301  N   PRO A 188    25702  24297  20853    507  -3001    528       N  
ATOM   1302  CA  PRO A 188      -6.154  28.458 -71.437  1.00192.10           C  
ANISOU 1302  CA  PRO A 188    26517  25063  21410    327  -2984    623       C  
ATOM   1303  C   PRO A 188      -5.371  29.295 -70.448  1.00187.95           C  
ANISOU 1303  C   PRO A 188    26007  24486  20920    298  -2954    640       C  
ATOM   1304  O   PRO A 188      -4.136  29.338 -70.523  1.00194.91           O  
ANISOU 1304  O   PRO A 188    26904  25466  21686    170  -2858    668       O  
ATOM   1305  CB  PRO A 188      -6.671  29.302 -72.611  1.00196.18           C  
ANISOU 1305  CB  PRO A 188    27192  25488  21859    252  -3170    732       C  
ATOM   1306  CG  PRO A 188      -8.082  29.623 -72.253  1.00193.55           C  
ANISOU 1306  CG  PRO A 188    26851  24997  21693    414  -3309    697       C  
ATOM   1307  CD  PRO A 188      -8.596  28.407 -71.524  1.00192.63           C  
ANISOU 1307  CD  PRO A 188    26561  24951  21681    559  -3187    563       C  
ATOM   1308  N   ASN A 189      -6.048  29.944 -69.510  1.00177.69           N  
ANISOU 1308  N   ASN A 189    24696  23040  19777    413  -3031    614       N  
ATOM   1309  CA  ASN A 189      -5.378  30.758 -68.508  1.00165.44           C  
ANISOU 1309  CA  ASN A 189    23155  21433  18273    397  -3007    624       C  
ATOM   1310  C   ASN A 189      -4.780  29.933 -67.376  1.00151.85           C  
ANISOU 1310  C   ASN A 189    21286  19811  16598    451  -2822    526       C  
ATOM   1311  O   ASN A 189      -4.241  30.518 -66.430  1.00146.77           O  
ANISOU 1311  O   ASN A 189    20633  19128  16004    449  -2789    522       O  
ATOM   1312  CB  ASN A 189      -6.351  31.798 -67.946  1.00163.24           C  
ANISOU 1312  CB  ASN A 189    22916  20960  18149    501  -3169    624       C  
ATOM   1313  CG  ASN A 189      -7.758  31.254 -67.792  1.00157.91           C  
ANISOU 1313  CG  ASN A 189    22157  20239  17604    664  -3223    534       C  
ATOM   1314  OD1 ASN A 189      -7.970  30.041 -67.789  1.00151.47           O  
ANISOU 1314  OD1 ASN A 189    21232  19535  16785    715  -3113    460       O  
ATOM   1315  ND2 ASN A 189      -8.727  32.151 -67.651  1.00158.10           N  
ANISOU 1315  ND2 ASN A 189    22228  20098  17745    747  -3396    533       N  
ATOM   1316  N   LYS A 190      -4.870  28.601 -67.446  1.00143.43           N  
ANISOU 1316  N   LYS A 190    20110  18867  15520    497  -2710    449       N  
ATOM   1317  CA  LYS A 190      -4.347  27.712 -66.406  1.00132.90           C  
ANISOU 1317  CA  LYS A 190    18643  17624  14229    550  -2547    356       C  
ATOM   1318  C   LYS A 190      -4.970  28.039 -65.052  1.00140.74           C  
ANISOU 1318  C   LYS A 190    19572  18512  15392    677  -2561    293       C  
ATOM   1319  O   LYS A 190      -4.284  28.134 -64.033  1.00138.31           O  
ANISOU 1319  O   LYS A 190    19215  18218  15117    679  -2474    264       O  
ATOM   1320  CB  LYS A 190      -2.819  27.787 -66.325  1.00121.98           C  
ANISOU 1320  CB  LYS A 190    17270  16344  12734    425  -2435    379       C  
ATOM   1321  CG  LYS A 190      -2.056  26.988 -67.363  1.00118.40           C  
ANISOU 1321  CG  LYS A 190    16812  16053  12123    318  -2357    383       C  
ATOM   1322  CD  LYS A 190      -0.572  27.293 -67.225  1.00119.62           C  
ANISOU 1322  CD  LYS A 190    16980  16296  12174    191  -2264    401       C  
ATOM   1323  CE  LYS A 190       0.298  26.081 -67.491  1.00119.30           C  
ANISOU 1323  CE  LYS A 190    16846  16439  12044    153  -2122    326       C  
ATOM   1324  NZ  LYS A 190       1.721  26.376 -67.154  1.00119.57           N  
ANISOU 1324  NZ  LYS A 190    16874  16557  12000     48  -2027    321       N  
ATOM   1325  N   ILE A 191      -6.286  28.247 -65.050  1.00153.78           N  
ANISOU 1325  N   ILE A 191    21222  20060  17149    779  -2676    268       N  
ATOM   1326  CA  ILE A 191      -6.933  28.681 -63.818  1.00159.19           C  
ANISOU 1326  CA  ILE A 191    21846  20646  17992    891  -2704    202       C  
ATOM   1327  C   ILE A 191      -7.128  27.521 -62.850  1.00157.89           C  
ANISOU 1327  C   ILE A 191    21536  20559  17895    976  -2572     90       C  
ATOM   1328  O   ILE A 191      -6.864  27.662 -61.653  1.00163.89           O  
ANISOU 1328  O   ILE A 191    22235  21306  18728   1009  -2509     42       O  
ATOM   1329  CB  ILE A 191      -8.263  29.392 -64.121  1.00163.16           C  
ANISOU 1329  CB  ILE A 191    22393  21011  18591    971  -2883    200       C  
ATOM   1330  CG1 ILE A 191      -7.997  30.819 -64.600  1.00165.66           C  
ANISOU 1330  CG1 ILE A 191    22856  21208  18878    897  -3027    306       C  
ATOM   1331  CG2 ILE A 191      -9.147  29.418 -62.884  1.00164.78           C  
ANISOU 1331  CG2 ILE A 191    22491  21157  18963   1104  -2887     87       C  
ATOM   1332  CD1 ILE A 191      -7.178  31.645 -63.639  1.00163.60           C  
ANISOU 1332  CD1 ILE A 191    22606  20906  18649    864  -2994    320       C  
ATOM   1333  N   TYR A 192      -7.592  26.362 -63.327  1.00149.57           N  
ANISOU 1333  N   TYR A 192    20428  19586  16818   1008  -2530     46       N  
ATOM   1334  CA  TYR A 192      -7.897  25.285 -62.387  1.00144.67           C  
ANISOU 1334  CA  TYR A 192    19681  19023  16266   1087  -2424    -59       C  
ATOM   1335  C   TYR A 192      -6.645  24.814 -61.657  1.00143.36           C  
ANISOU 1335  C   TYR A 192    19471  18943  16058   1039  -2280    -72       C  
ATOM   1336  O   TYR A 192      -6.675  24.576 -60.441  1.00152.47           O  
ANISOU 1336  O   TYR A 192    20546  20094  17291   1090  -2215   -138       O  
ATOM   1337  CB  TYR A 192      -8.563  24.113 -63.105  1.00144.67           C  
ANISOU 1337  CB  TYR A 192    19639  19091  16237   1120  -2410    -97       C  
ATOM   1338  CG  TYR A 192      -8.910  22.980 -62.163  1.00145.42           C  
ANISOU 1338  CG  TYR A 192    19615  19240  16396   1190  -2310   -200       C  
ATOM   1339  CD1 TYR A 192     -10.127  22.952 -61.498  1.00145.16           C  
ANISOU 1339  CD1 TYR A 192    19520  19153  16483   1284  -2350   -280       C  
ATOM   1340  CD2 TYR A 192      -8.010  21.947 -61.922  1.00146.61           C  
ANISOU 1340  CD2 TYR A 192    19719  19498  16488   1156  -2181   -222       C  
ATOM   1341  CE1 TYR A 192     -10.444  21.919 -60.627  1.00145.05           C  
ANISOU 1341  CE1 TYR A 192    19406  19191  16516   1330  -2260   -370       C  
ATOM   1342  CE2 TYR A 192      -8.318  20.912 -61.054  1.00143.28           C  
ANISOU 1342  CE2 TYR A 192    19203  19115  16120   1211  -2103   -308       C  
ATOM   1343  CZ  TYR A 192      -9.535  20.902 -60.410  1.00140.07           C  
ANISOU 1343  CZ  TYR A 192    18743  18655  15821   1290  -2140   -377       C  
ATOM   1344  OH  TYR A 192      -9.840  19.870 -59.549  1.00131.80           O  
ANISOU 1344  OH  TYR A 192    17611  17650  14816   1327  -2063   -458       O  
ATOM   1345  N   GLU A 193      -5.522  24.726 -62.372  1.00140.94           N  
ANISOU 1345  N   GLU A 193    19213  18715  15623    937  -2233    -13       N  
ATOM   1346  CA  GLU A 193      -4.275  24.308 -61.742  1.00139.49           C  
ANISOU 1346  CA  GLU A 193    18987  18616  15397    892  -2105    -32       C  
ATOM   1347  C   GLU A 193      -3.849  25.304 -60.672  1.00139.70           C  
ANISOU 1347  C   GLU A 193    19022  18572  15485    888  -2101    -22       C  
ATOM   1348  O   GLU A 193      -3.506  24.921 -59.545  1.00157.89           O  
ANISOU 1348  O   GLU A 193    21252  20898  17841    922  -2014    -79       O  
ATOM   1349  CB  GLU A 193      -3.179  24.158 -62.801  1.00137.30           C  
ANISOU 1349  CB  GLU A 193    18760  18440  14968    775  -2067     20       C  
ATOM   1350  CG  GLU A 193      -1.765  24.291 -62.248  1.00134.39           C  
ANISOU 1350  CG  GLU A 193    18379  18134  14549    705  -1969     19       C  
ATOM   1351  CD  GLU A 193      -0.732  24.542 -63.330  1.00132.43           C  
ANISOU 1351  CD  GLU A 193    18197  17973  14148    569  -1955     77       C  
ATOM   1352  OE1 GLU A 193      -1.027  24.277 -64.517  1.00124.50           O  
ANISOU 1352  OE1 GLU A 193    17230  17010  13066    530  -1998    104       O  
ATOM   1353  OE2 GLU A 193       0.374  25.014 -62.989  1.00136.95           O  
ANISOU 1353  OE2 GLU A 193    18783  18579  14674    496  -1901     92       O  
ATOM   1354  N   LYS A 194      -3.871  26.595 -61.008  1.00129.85           N  
ANISOU 1354  N   LYS A 194    17870  17234  14234    846  -2202     53       N  
ATOM   1355  CA  LYS A 194      -3.437  27.609 -60.054  1.00118.55           C  
ANISOU 1355  CA  LYS A 194    16452  15732  12858    838  -2206     65       C  
ATOM   1356  C   LYS A 194      -4.367  27.680 -58.851  1.00116.51           C  
ANISOU 1356  C   LYS A 194    16116  15401  12753    953  -2221    -14       C  
ATOM   1357  O   LYS A 194      -3.913  27.888 -57.717  1.00113.88           O  
ANISOU 1357  O   LYS A 194    15737  15062  12472    964  -2158    -47       O  
ATOM   1358  CB  LYS A 194      -3.334  28.964 -60.748  1.00112.81           C  
ANISOU 1358  CB  LYS A 194    15855  14915  12094    765  -2329    165       C  
ATOM   1359  CG  LYS A 194      -2.040  29.105 -61.518  1.00112.18           C  
ANISOU 1359  CG  LYS A 194    15845  14919  11858    621  -2282    238       C  
ATOM   1360  CD  LYS A 194      -0.920  28.442 -60.723  1.00112.64           C  
ANISOU 1360  CD  LYS A 194    15820  15087  11890    602  -2124    185       C  
ATOM   1361  CE  LYS A 194       0.353  28.283 -61.525  1.00117.58           C  
ANISOU 1361  CE  LYS A 194    16484  15835  12356    466  -2056    224       C  
ATOM   1362  NZ  LYS A 194       1.212  27.223 -60.930  1.00111.31           N  
ANISOU 1362  NZ  LYS A 194    15585  15164  11543    477  -1909    144       N  
ATOM   1363  N   VAL A 195      -5.664  27.467 -59.073  1.00113.89           N  
ANISOU 1363  N   VAL A 195    15761  15023  12491   1034  -2298    -55       N  
ATOM   1364  CA  VAL A 195      -6.608  27.440 -57.964  1.00110.22           C  
ANISOU 1364  CA  VAL A 195    15207  14509  12163   1136  -2305   -149       C  
ATOM   1365  C   VAL A 195      -6.270  26.295 -57.026  1.00108.42           C  
ANISOU 1365  C   VAL A 195    14877  14376  11943   1154  -2162   -221       C  
ATOM   1366  O   VAL A 195      -6.215  26.467 -55.802  1.00108.16           O  
ANISOU 1366  O   VAL A 195    14786  14327  11984   1182  -2117   -273       O  
ATOM   1367  CB  VAL A 195      -8.052  27.327 -58.485  1.00106.80           C  
ANISOU 1367  CB  VAL A 195    14762  14027  11791   1214  -2411   -189       C  
ATOM   1368  CG1 VAL A 195      -8.945  26.676 -57.435  1.00107.25           C  
ANISOU 1368  CG1 VAL A 195    14698  14100  11953   1302  -2365   -309       C  
ATOM   1369  CG2 VAL A 195      -8.586  28.697 -58.859  1.00107.32           C  
ANISOU 1369  CG2 VAL A 195    14909  13959  11910   1230  -2575   -148       C  
ATOM   1370  N   TYR A 196      -6.002  25.112 -57.588  1.00102.35           N  
ANISOU 1370  N   TYR A 196    14089  13705  11094   1133  -2093   -225       N  
ATOM   1371  CA  TYR A 196      -5.686  23.983 -56.724  1.00 92.89           C  
ANISOU 1371  CA  TYR A 196    12806  12586   9904   1150  -1973   -292       C  
ATOM   1372  C   TYR A 196      -4.410  24.232 -55.937  1.00 88.63           C  
ANISOU 1372  C   TYR A 196    12262  12072   9340   1100  -1890   -277       C  
ATOM   1373  O   TYR A 196      -4.334  23.911 -54.745  1.00 89.86           O  
ANISOU 1373  O   TYR A 196    12353  12238   9553   1127  -1825   -334       O  
ATOM   1374  CB  TYR A 196      -5.547  22.701 -57.534  1.00 89.84           C  
ANISOU 1374  CB  TYR A 196    12406  12294   9436   1136  -1927   -299       C  
ATOM   1375  CG  TYR A 196      -5.269  21.508 -56.656  1.00 86.81           C  
ANISOU 1375  CG  TYR A 196    11944  11977   9064   1155  -1823   -367       C  
ATOM   1376  CD1 TYR A 196      -6.299  20.875 -55.978  1.00 86.33           C  
ANISOU 1376  CD1 TYR A 196    11816  11905   9080   1217  -1818   -442       C  
ATOM   1377  CD2 TYR A 196      -3.978  21.027 -56.488  1.00 91.34           C  
ANISOU 1377  CD2 TYR A 196    12511  12622   9571   1107  -1736   -361       C  
ATOM   1378  CE1 TYR A 196      -6.058  19.788 -55.167  1.00 96.08           C  
ANISOU 1378  CE1 TYR A 196    12993  13192  10320   1224  -1734   -497       C  
ATOM   1379  CE2 TYR A 196      -3.724  19.939 -55.678  1.00 96.04           C  
ANISOU 1379  CE2 TYR A 196    13044  13265  10180   1126  -1658   -421       C  
ATOM   1380  CZ  TYR A 196      -4.768  19.321 -55.018  1.00101.19           C  
ANISOU 1380  CZ  TYR A 196    13644  13899  10906   1182  -1660   -483       C  
ATOM   1381  OH  TYR A 196      -4.526  18.234 -54.206  1.00106.51           O  
ANISOU 1381  OH  TYR A 196    14269  14612  11587   1190  -1594   -536       O  
ATOM   1382  N   HIS A 197      -3.405  24.833 -56.575  1.00 94.32           N  
ANISOU 1382  N   HIS A 197    13056  12807   9976   1021  -1893   -203       N  
ATOM   1383  CA  HIS A 197      -2.138  25.012 -55.877  1.00101.46           C  
ANISOU 1383  CA  HIS A 197    13952  13748  10851    972  -1808   -195       C  
ATOM   1384  C   HIS A 197      -2.252  26.047 -54.764  1.00105.69           C  
ANISOU 1384  C   HIS A 197    14480  14198  11481    995  -1828   -204       C  
ATOM   1385  O   HIS A 197      -1.716  25.842 -53.666  1.00106.39           O  
ANISOU 1385  O   HIS A 197    14515  14309  11598   1001  -1748   -244       O  
ATOM   1386  CB  HIS A 197      -1.038  25.376 -56.872  1.00107.75           C  
ANISOU 1386  CB  HIS A 197    14822  14594  11523    870  -1802   -123       C  
ATOM   1387  CG  HIS A 197      -0.578  24.216 -57.702  1.00111.74           C  
ANISOU 1387  CG  HIS A 197    15310  15215  11932    840  -1746   -139       C  
ATOM   1388  ND1 HIS A 197       0.643  24.191 -58.340  1.00116.38           N  
ANISOU 1388  ND1 HIS A 197    15925  15891  12402    746  -1697   -111       N  
ATOM   1389  CD2 HIS A 197      -1.175  23.034 -57.990  1.00107.59           C  
ANISOU 1389  CD2 HIS A 197    14735  14733  11410    891  -1732   -188       C  
ATOM   1390  CE1 HIS A 197       0.778  23.047 -58.987  1.00113.09           C  
ANISOU 1390  CE1 HIS A 197    15473  15569  11926    746  -1658   -149       C  
ATOM   1391  NE2 HIS A 197      -0.312  22.326 -58.791  1.00108.60           N  
ANISOU 1391  NE2 HIS A 197    14862  14971  11431    833  -1680   -191       N  
ATOM   1392  N   ILE A 198      -2.961  27.155 -55.012  1.00110.51           N  
ANISOU 1392  N   ILE A 198    15140  14705  12142   1011  -1941   -173       N  
ATOM   1393  CA  ILE A 198      -3.156  28.133 -53.942  1.00110.93           C  
ANISOU 1393  CA  ILE A 198    15176  14675  12296   1042  -1968   -196       C  
ATOM   1394  C   ILE A 198      -3.991  27.535 -52.815  1.00107.49           C  
ANISOU 1394  C   ILE A 198    14635  14243  11962   1123  -1931   -298       C  
ATOM   1395  O   ILE A 198      -3.724  27.774 -51.629  1.00 92.69           O  
ANISOU 1395  O   ILE A 198    12712  12362  10143   1132  -1881   -337       O  
ATOM   1396  CB  ILE A 198      -3.792  29.424 -54.492  1.00105.79           C  
ANISOU 1396  CB  ILE A 198    14604  13905  11687   1050  -2116   -149       C  
ATOM   1397  CG1 ILE A 198      -2.711  30.365 -55.030  1.00101.33           C  
ANISOU 1397  CG1 ILE A 198    14144  13319  11039    950  -2139    -49       C  
ATOM   1398  CG2 ILE A 198      -4.617  30.122 -53.412  1.00 99.87           C  
ANISOU 1398  CG2 ILE A 198    13799  13067  11079   1128  -2167   -219       C  
ATOM   1399  CD1 ILE A 198      -3.258  31.667 -55.587  1.00 93.88           C  
ANISOU 1399  CD1 ILE A 198    13297  12245  10131    948  -2299      8       C  
ATOM   1400  N   CYS A 199      -4.988  26.716 -53.163  1.00113.73           N  
ANISOU 1400  N   CYS A 199    15388  15054  12770   1172  -1951   -343       N  
ATOM   1401  CA  CYS A 199      -5.831  26.105 -52.139  1.00113.18           C  
ANISOU 1401  CA  CYS A 199    15221  14999  12785   1233  -1915   -443       C  
ATOM   1402  C   CYS A 199      -5.021  25.172 -51.250  1.00107.39           C  
ANISOU 1402  C   CYS A 199    14437  14347  12021   1207  -1788   -471       C  
ATOM   1403  O   CYS A 199      -5.150  25.193 -50.017  1.00101.14           O  
ANISOU 1403  O   CYS A 199    13583  13553  11293   1222  -1745   -531       O  
ATOM   1404  CB  CYS A 199      -6.985  25.345 -52.796  1.00118.42           C  
ANISOU 1404  CB  CYS A 199    15861  15677  13457   1279  -1958   -483       C  
ATOM   1405  SG  CYS A 199      -8.576  26.204 -52.781  1.00128.54           S  
ANISOU 1405  SG  CYS A 199    17117  16863  14860   1360  -2091   -547       S  
ATOM   1406  N   VAL A 200      -4.157  24.358 -51.859  1.00109.40           N  
ANISOU 1406  N   VAL A 200    14717  14674  12178   1164  -1731   -433       N  
ATOM   1407  CA  VAL A 200      -3.335  23.446 -51.072  1.00105.48           C  
ANISOU 1407  CA  VAL A 200    14178  14247  11653   1144  -1625   -461       C  
ATOM   1408  C   VAL A 200      -2.369  24.231 -50.195  1.00109.20           C  
ANISOU 1408  C   VAL A 200    14652  14702  12135   1112  -1584   -446       C  
ATOM   1409  O   VAL A 200      -2.233  23.957 -48.998  1.00124.53           O  
ANISOU 1409  O   VAL A 200    16542  16656  14117   1119  -1526   -494       O  
ATOM   1410  CB  VAL A 200      -2.591  22.459 -51.988  1.00 97.87           C  
ANISOU 1410  CB  VAL A 200    13237  13362  10587   1112  -1586   -436       C  
ATOM   1411  CG1 VAL A 200      -1.334  21.965 -51.306  1.00 96.83           C  
ANISOU 1411  CG1 VAL A 200    13086  13288  10418   1080  -1496   -447       C  
ATOM   1412  CG2 VAL A 200      -3.489  21.288 -52.328  1.00 96.15           C  
ANISOU 1412  CG2 VAL A 200    12987  13175  10372   1150  -1593   -480       C  
ATOM   1413  N   THR A 201      -1.710  25.244 -50.767  1.00102.72           N  
ANISOU 1413  N   THR A 201    13898  13853  11278   1070  -1616   -378       N  
ATOM   1414  CA  THR A 201      -0.730  25.995 -49.988  1.00 95.22           C  
ANISOU 1414  CA  THR A 201    12953  12892  10333   1034  -1575   -361       C  
ATOM   1415  C   THR A 201      -1.382  26.679 -48.797  1.00 95.86           C  
ANISOU 1415  C   THR A 201    12989  12908  10525   1075  -1593   -410       C  
ATOM   1416  O   THR A 201      -0.841  26.656 -47.684  1.00 96.56           O  
ANISOU 1416  O   THR A 201    13036  13014  10637   1067  -1525   -439       O  
ATOM   1417  CB  THR A 201      -0.027  27.026 -50.873  1.00 95.92           C  
ANISOU 1417  CB  THR A 201    13129  12957  10360    972  -1618   -278       C  
ATOM   1418  OG1 THR A 201       1.059  26.406 -51.571  1.00 98.14           O  
ANISOU 1418  OG1 THR A 201    13432  13329  10528    912  -1558   -251       O  
ATOM   1419  CG2 THR A 201       0.507  28.177 -50.041  1.00 95.71           C  
ANISOU 1419  CG2 THR A 201    13114  12878  10375    951  -1614   -263       C  
ATOM   1420  N   VAL A 202      -2.569  27.252 -48.997  1.00 99.90           N  
ANISOU 1420  N   VAL A 202    13499  13349  11108   1121  -1685   -428       N  
ATOM   1421  CA  VAL A 202      -3.269  27.877 -47.880  1.00102.45           C  
ANISOU 1421  CA  VAL A 202    13763  13620  11542   1164  -1705   -495       C  
ATOM   1422  C   VAL A 202      -3.645  26.833 -46.841  1.00100.15           C  
ANISOU 1422  C   VAL A 202    13385  13389  11280   1182  -1628   -578       C  
ATOM   1423  O   VAL A 202      -3.513  27.062 -45.632  1.00101.11           O  
ANISOU 1423  O   VAL A 202    13455  13512  11450   1180  -1584   -624       O  
ATOM   1424  CB  VAL A 202      -4.508  28.639 -48.385  1.00104.18           C  
ANISOU 1424  CB  VAL A 202    13993  13755  11835   1217  -1832   -514       C  
ATOM   1425  CG1 VAL A 202      -5.481  28.915 -47.244  1.00 92.34           C  
ANISOU 1425  CG1 VAL A 202    12403  12230  10452   1270  -1845   -620       C  
ATOM   1426  CG2 VAL A 202      -4.093  29.939 -49.060  1.00111.49           C  
ANISOU 1426  CG2 VAL A 202    15013  14598  12752   1191  -1920   -433       C  
ATOM   1427  N   LEU A 203      -4.090  25.659 -47.294  1.00 97.80           N  
ANISOU 1427  N   LEU A 203    13073  13143  10946   1193  -1612   -597       N  
ATOM   1428  CA  LEU A 203      -4.595  24.663 -46.355  1.00 94.47           C  
ANISOU 1428  CA  LEU A 203    12577  12770  10548   1202  -1554   -674       C  
ATOM   1429  C   LEU A 203      -3.483  24.038 -45.518  1.00101.13           C  
ANISOU 1429  C   LEU A 203    13410  13667  11348   1160  -1457   -669       C  
ATOM   1430  O   LEU A 203      -3.686  23.753 -44.333  1.00110.08           O  
ANISOU 1430  O   LEU A 203    14488  14819  12519   1152  -1412   -727       O  
ATOM   1431  CB  LEU A 203      -5.373  23.588 -47.108  1.00 83.87           C  
ANISOU 1431  CB  LEU A 203    11229  11462   9177   1222  -1570   -693       C  
ATOM   1432  CG  LEU A 203      -6.870  23.871 -47.181  1.00 78.85           C  
ANISOU 1432  CG  LEU A 203    10550  10793   8617   1271  -1642   -760       C  
ATOM   1433  CD1 LEU A 203      -7.610  22.717 -47.837  1.00 83.16           C  
ANISOU 1433  CD1 LEU A 203    11086  11381   9131   1285  -1648   -782       C  
ATOM   1434  CD2 LEU A 203      -7.414  24.143 -45.787  1.00 75.25           C  
ANISOU 1434  CD2 LEU A 203    10013  10338   8240   1275  -1618   -850       C  
ATOM   1435  N   ILE A 204      -2.309  23.810 -46.104  1.00 94.34           N  
ANISOU 1435  N   ILE A 204    12601  12836  10410   1129  -1426   -606       N  
ATOM   1436  CA  ILE A 204      -1.257  23.055 -45.432  1.00 87.97           C  
ANISOU 1436  CA  ILE A 204    11784  12081   9559   1098  -1345   -609       C  
ATOM   1437  C   ILE A 204      -0.060  23.926 -45.084  1.00 94.16           C  
ANISOU 1437  C   ILE A 204    12589  12856  10329   1065  -1313   -572       C  
ATOM   1438  O   ILE A 204       1.001  23.395 -44.738  1.00102.22           O  
ANISOU 1438  O   ILE A 204    13612  13923  11304   1040  -1254   -569       O  
ATOM   1439  CB  ILE A 204      -0.813  21.836 -46.257  1.00 82.43           C  
ANISOU 1439  CB  ILE A 204    11104  11436   8778   1091  -1326   -595       C  
ATOM   1440  CG1 ILE A 204      -0.093  22.282 -47.532  1.00 88.50           C  
ANISOU 1440  CG1 ILE A 204    11931  12216   9479   1069  -1347   -531       C  
ATOM   1441  CG2 ILE A 204      -1.999  20.939 -46.566  1.00 75.52           C  
ANISOU 1441  CG2 ILE A 204    10208  10570   7916   1120  -1355   -632       C  
ATOM   1442  CD1 ILE A 204       0.545  21.152 -48.298  1.00 96.37           C  
ANISOU 1442  CD1 ILE A 204    12939  13282  10396   1058  -1322   -528       C  
ATOM   1443  N   TYR A 205      -0.186  25.246 -45.170  1.00 95.94           N  
ANISOU 1443  N   TYR A 205    12834  13023  10595   1066  -1358   -548       N  
ATOM   1444  CA  TYR A 205       0.912  26.076 -44.695  1.00101.10           C  
ANISOU 1444  CA  TYR A 205    13505  13669  11240   1031  -1324   -519       C  
ATOM   1445  C   TYR A 205       0.382  27.294 -43.949  1.00112.75           C  
ANISOU 1445  C   TYR A 205    14960  15074  12807   1048  -1361   -540       C  
ATOM   1446  O   TYR A 205       0.507  27.374 -42.723  1.00120.17           O  
ANISOU 1446  O   TYR A 205    15849  16019  13790   1046  -1316   -584       O  
ATOM   1447  CB  TYR A 205       1.799  26.496 -45.866  1.00 91.03           C  
ANISOU 1447  CB  TYR A 205    12300  12404   9883    989  -1337   -446       C  
ATOM   1448  CG  TYR A 205       2.921  27.440 -45.498  1.00 88.56           C  
ANISOU 1448  CG  TYR A 205    12005  12100   9543    942  -1290   -418       C  
ATOM   1449  CD1 TYR A 205       4.072  26.985 -44.866  1.00 92.09           C  
ANISOU 1449  CD1 TYR A 205    12481  12480  10029    927  -1329   -388       C  
ATOM   1450  CD2 TYR A 205       2.816  28.796 -45.776  1.00 94.75           C  
ANISOU 1450  CD2 TYR A 205    12777  12960  10264    914  -1213   -428       C  
ATOM   1451  CE1 TYR A 205       5.092  27.860 -44.527  1.00103.46           C  
ANISOU 1451  CE1 TYR A 205    13937  13932  11440    878  -1284   -363       C  
ATOM   1452  CE2 TYR A 205       3.826  29.676 -45.445  1.00104.84           C  
ANISOU 1452  CE2 TYR A 205    14065  14254  11515    871  -1168   -411       C  
ATOM   1453  CZ  TYR A 205       4.962  29.206 -44.820  1.00109.38           C  
ANISOU 1453  CZ  TYR A 205    14669  14766  12124    850  -1199   -376       C  
ATOM   1454  OH  TYR A 205       5.966  30.086 -44.493  1.00115.51           O  
ANISOU 1454  OH  TYR A 205    15456  15561  12870    802  -1152   -361       O  
ATOM   1455  N   PHE A 206      -0.223  28.239 -44.668  1.00109.65           N  
ANISOU 1455  N   PHE A 206    14604  14614  12445   1065  -1451   -514       N  
ATOM   1456  CA  PHE A 206      -0.503  29.536 -44.062  1.00103.82           C  
ANISOU 1456  CA  PHE A 206    13855  13800  11790   1079  -1498   -529       C  
ATOM   1457  C   PHE A 206      -1.569  29.436 -42.981  1.00 94.81           C  
ANISOU 1457  C   PHE A 206    12624  12653  10745   1123  -1498   -628       C  
ATOM   1458  O   PHE A 206      -1.394  29.969 -41.879  1.00 94.50           O  
ANISOU 1458  O   PHE A 206    12541  12605  10759   1119  -1469   -667       O  
ATOM   1459  CB  PHE A 206      -0.914  30.535 -45.140  1.00108.01           C  
ANISOU 1459  CB  PHE A 206    14457  14249  12333   1088  -1613   -477       C  
ATOM   1460  CG  PHE A 206       0.227  30.996 -45.992  1.00114.15           C  
ANISOU 1460  CG  PHE A 206    15327  15026  13020   1023  -1614   -381       C  
ATOM   1461  CD1 PHE A 206       1.176  31.872 -45.491  1.00115.99           C  
ANISOU 1461  CD1 PHE A 206    15581  15238  13250    981  -1590   -352       C  
ATOM   1462  CD2 PHE A 206       0.352  30.551 -47.294  1.00112.93           C  
ANISOU 1462  CD2 PHE A 206    15233  14899  12777    995  -1637   -324       C  
ATOM   1463  CE1 PHE A 206       2.225  32.294 -46.278  1.00114.83           C  
ANISOU 1463  CE1 PHE A 206    15517  15101  13010    907  -1587   -269       C  
ATOM   1464  CE2 PHE A 206       1.398  30.969 -48.084  1.00111.20           C  
ANISOU 1464  CE2 PHE A 206    15094  14693  12464    920  -1635   -243       C  
ATOM   1465  CZ  PHE A 206       2.335  31.840 -47.578  1.00113.72           C  
ANISOU 1465  CZ  PHE A 206    15436  14995  12777    873  -1609   -216       C  
ATOM   1466  N   LEU A 207      -2.689  28.779 -43.276  1.00 88.83           N  
ANISOU 1466  N   LEU A 207    11835  11908  10008   1159  -1530   -675       N  
ATOM   1467  CA  LEU A 207      -3.720  28.635 -42.249  1.00 82.61           C  
ANISOU 1467  CA  LEU A 207    10954  11132   9301   1187  -1523   -781       C  
ATOM   1468  C   LEU A 207      -3.230  27.878 -41.023  1.00 97.70           C  
ANISOU 1468  C   LEU A 207    12815  13114  11193   1149  -1418   -817       C  
ATOM   1469  O   LEU A 207      -3.390  28.395 -39.903  1.00102.44           O  
ANISOU 1469  O   LEU A 207    13356  13712  11855   1145  -1398   -879       O  
ATOM   1470  CB  LEU A 207      -4.968  27.976 -42.839  1.00 67.09           C  
ANISOU 1470  CB  LEU A 207     8964   9177   7348   1224  -1570   -827       C  
ATOM   1471  CG  LEU A 207      -5.968  27.560 -41.758  1.00 76.45           C  
ANISOU 1471  CG  LEU A 207    10048  10405   8593   1233  -1543   -945       C  
ATOM   1472  CD1 LEU A 207      -6.678  28.773 -41.164  1.00 83.42           C  
ANISOU 1472  CD1 LEU A 207    10873  11237   9587   1270  -1604  -1025       C  
ATOM   1473  CD2 LEU A 207      -6.965  26.535 -42.270  1.00 77.32           C  
ANISOU 1473  CD2 LEU A 207    10137  10555   8686   1249  -1556   -984       C  
ATOM   1474  N   PRO A 208      -2.645  26.674 -41.136  1.00101.75           N  
ANISOU 1474  N   PRO A 208    13348  13688  11624   1118  -1354   -788       N  
ATOM   1475  CA  PRO A 208      -2.148  26.013 -39.919  1.00100.11           C  
ANISOU 1475  CA  PRO A 208    13103  13534  11401   1080  -1268   -819       C  
ATOM   1476  C   PRO A 208      -1.074  26.792 -39.184  1.00 91.57           C  
ANISOU 1476  C   PRO A 208    12025  12440  10325   1054  -1228   -796       C  
ATOM   1477  O   PRO A 208      -1.032  26.745 -37.949  1.00 92.69           O  
ANISOU 1477  O   PRO A 208    12117  12607  10493   1031  -1180   -846       O  
ATOM   1478  CB  PRO A 208      -1.630  24.664 -40.437  1.00104.86           C  
ANISOU 1478  CB  PRO A 208    13741  14184  11915   1062  -1233   -782       C  
ATOM   1479  CG  PRO A 208      -1.342  24.883 -41.859  1.00111.03           C  
ANISOU 1479  CG  PRO A 208    14586  14945  12656   1079  -1278   -715       C  
ATOM   1480  CD  PRO A 208      -2.362  25.869 -42.338  1.00105.83           C  
ANISOU 1480  CD  PRO A 208    13923  14227  12062   1117  -1361   -729       C  
ATOM   1481  N   LEU A 209      -0.196  27.501 -39.897  1.00 85.44           N  
ANISOU 1481  N   LEU A 209    11310  11633   9521   1051  -1245   -724       N  
ATOM   1482  CA  LEU A 209       0.812  28.300 -39.208  1.00 76.71           C  
ANISOU 1482  CA  LEU A 209    10208  10515   8422   1025  -1207   -705       C  
ATOM   1483  C   LEU A 209       0.185  29.472 -38.464  1.00 85.61           C  
ANISOU 1483  C   LEU A 209    11289  11593   9648   1044  -1242   -757       C  
ATOM   1484  O   LEU A 209       0.667  29.853 -37.392  1.00 92.73           O  
ANISOU 1484  O   LEU A 209    12155  12503  10574   1023  -1195   -782       O  
ATOM   1485  CB  LEU A 209       1.884  28.773 -40.182  1.00 65.88           C  
ANISOU 1485  CB  LEU A 209     8913   9131   6988   1003  -1216   -620       C  
ATOM   1486  CG  LEU A 209       2.803  27.635 -40.649  1.00 63.60           C  
ANISOU 1486  CG  LEU A 209     8654   8910   6603    978  -1163   -589       C  
ATOM   1487  CD1 LEU A 209       3.920  28.139 -41.548  1.00 71.69           C  
ANISOU 1487  CD1 LEU A 209     9742   9938   7557    943  -1162   -519       C  
ATOM   1488  CD2 LEU A 209       3.359  26.861 -39.478  1.00 56.82           C  
ANISOU 1488  CD2 LEU A 209     7753   8101   5735    962  -1087   -627       C  
ATOM   1489  N   LEU A 210      -0.883  30.061 -39.012  1.00 86.73           N  
ANISOU 1489  N   LEU A 210    11425  11680   9849   1086  -1330   -781       N  
ATOM   1490  CA  LEU A 210      -1.550  31.147 -38.300  1.00 89.38           C  
ANISOU 1490  CA  LEU A 210    11705  11966  10289   1113  -1374   -850       C  
ATOM   1491  C   LEU A 210      -2.323  30.629 -37.094  1.00 91.35           C  
ANISOU 1491  C   LEU A 210    11854  12273  10582   1109  -1329   -958       C  
ATOM   1492  O   LEU A 210      -2.285  31.237 -36.017  1.00110.71           O  
ANISOU 1492  O   LEU A 210    14248  14726  13089   1100  -1306  -1015       O  
ATOM   1493  CB  LEU A 210      -2.476  31.918 -39.242  1.00 91.90           C  
ANISOU 1493  CB  LEU A 210    12047  12206  10664   1166  -1496   -853       C  
ATOM   1494  CG  LEU A 210      -1.805  32.793 -40.305  1.00 98.10           C  
ANISOU 1494  CG  LEU A 210    12936  12917  11420   1158  -1562   -751       C  
ATOM   1495  CD1 LEU A 210      -2.682  33.988 -40.663  1.00100.40           C  
ANISOU 1495  CD1 LEU A 210    13236  13106  11807   1211  -1695   -778       C  
ATOM   1496  CD2 LEU A 210      -0.419  33.249 -39.866  1.00 95.17           C  
ANISOU 1496  CD2 LEU A 210    12599  12553  11010   1107  -1499   -695       C  
ATOM   1497  N   VAL A 211      -3.013  29.497 -37.247  1.00 83.51           N  
ANISOU 1497  N   VAL A 211    10839  11331   9559   1107  -1314   -989       N  
ATOM   1498  CA  VAL A 211      -3.772  28.926 -36.135  1.00 95.52           C  
ANISOU 1498  CA  VAL A 211    12271  12917  11106   1084  -1270  -1091       C  
ATOM   1499  C   VAL A 211      -2.836  28.518 -35.002  1.00105.57           C  
ANISOU 1499  C   VAL A 211    13534  14241  12338   1024  -1175  -1083       C  
ATOM   1500  O   VAL A 211      -3.019  28.911 -33.839  1.00106.50           O  
ANISOU 1500  O   VAL A 211    13582  14383  12501   1000  -1144  -1155       O  
ATOM   1501  CB  VAL A 211      -4.609  27.732 -36.628  1.00 91.99           C  
ANISOU 1501  CB  VAL A 211    11818  12512  10621   1083  -1274  -1113       C  
ATOM   1502  CG1 VAL A 211      -5.263  27.015 -35.463  1.00 81.99           C  
ANISOU 1502  CG1 VAL A 211    10473  11322   9356   1035  -1218  -1207       C  
ATOM   1503  CG2 VAL A 211      -5.646  28.193 -37.642  1.00 94.99           C  
ANISOU 1503  CG2 VAL A 211    12196  12843  11051   1146  -1372  -1137       C  
ATOM   1504  N   ILE A 212      -1.805  27.735 -35.332  1.00106.86           N  
ANISOU 1504  N   ILE A 212    13764  14423  12415    999  -1132  -1000       N  
ATOM   1505  CA  ILE A 212      -0.832  27.318 -34.328  1.00 99.01           C  
ANISOU 1505  CA  ILE A 212    12769  13470  11380    948  -1054   -988       C  
ATOM   1506  C   ILE A 212      -0.103  28.525 -33.756  1.00 97.91           C  
ANISOU 1506  C   ILE A 212    12620  13301  11282    946  -1040   -981       C  
ATOM   1507  O   ILE A 212       0.256  28.539 -32.567  1.00 94.61           O  
ANISOU 1507  O   ILE A 212    12164  12915  10869    907   -985  -1014       O  
ATOM   1508  CB  ILE A 212       0.146  26.292 -34.939  1.00 88.27           C  
ANISOU 1508  CB  ILE A 212    11480  12129   9928    935  -1027   -911       C  
ATOM   1509  CG1 ILE A 212      -0.594  24.993 -35.286  1.00 88.15           C  
ANISOU 1509  CG1 ILE A 212    11469  12147   9875    929  -1036   -928       C  
ATOM   1510  CG2 ILE A 212       1.301  26.021 -33.996  1.00 73.29           C  
ANISOU 1510  CG2 ILE A 212     9591  10261   7995    893   -962   -894       C  
ATOM   1511  CD1 ILE A 212       0.254  23.971 -36.036  1.00 82.31           C  
ANISOU 1511  CD1 ILE A 212    10797  11423   9056    929  -1027   -863       C  
ATOM   1512  N   GLY A 213       0.089  29.572 -34.567  1.00 99.81           N  
ANISOU 1512  N   GLY A 213    12896  13476  11551    983  -1095   -940       N  
ATOM   1513  CA  GLY A 213       0.755  30.760 -34.062  1.00101.68           C  
ANISOU 1513  CA  GLY A 213    13128  13676  11828    979  -1089   -932       C  
ATOM   1514  C   GLY A 213      -0.070  31.502 -33.027  1.00103.83           C  
ANISOU 1514  C   GLY A 213    13312  13945  12196    987  -1100  -1033       C  
ATOM   1515  O   GLY A 213       0.463  31.955 -32.008  1.00113.45           O  
ANISOU 1515  O   GLY A 213    14495  15177  13433    961  -1054  -1056       O  
ATOM   1516  N   TYR A 214      -1.388  31.585 -33.233  1.00 91.91           N  
ANISOU 1516  N   TYR A 214    11753  12424  10743   1022  -1160  -1106       N  
ATOM   1517  CA  TYR A 214      -2.225  32.182 -32.197  1.00 90.63           C  
ANISOU 1517  CA  TYR A 214    11488  12277  10669   1026  -1167  -1226       C  
ATOM   1518  C   TYR A 214      -2.256  31.306 -30.955  1.00 94.27           C  
ANISOU 1518  C   TYR A 214    11889  12833  11095    959  -1076  -1283       C  
ATOM   1519  O   TYR A 214      -2.139  31.810 -29.829  1.00105.49           O  
ANISOU 1519  O   TYR A 214    13247  14280  12553    931  -1038  -1344       O  
ATOM   1520  CB  TYR A 214      -3.644  32.426 -32.716  1.00 96.06           C  
ANISOU 1520  CB  TYR A 214    12130  12941  11427   1080  -1254  -1307       C  
ATOM   1521  CG  TYR A 214      -4.646  32.796 -31.632  1.00105.54           C  
ANISOU 1521  CG  TYR A 214    13204  14184  12711   1077  -1254  -1459       C  
ATOM   1522  CD1 TYR A 214      -4.815  34.117 -31.227  1.00104.24           C  
ANISOU 1522  CD1 TYR A 214    12989  13969  12649   1115  -1307  -1525       C  
ATOM   1523  CD2 TYR A 214      -5.426  31.820 -31.017  1.00117.36           C  
ANISOU 1523  CD2 TYR A 214    14632  15777  14182   1031  -1204  -1543       C  
ATOM   1524  CE1 TYR A 214      -5.731  34.452 -30.237  1.00111.54           C  
ANISOU 1524  CE1 TYR A 214    13786  14944  13651   1112  -1306  -1681       C  
ATOM   1525  CE2 TYR A 214      -6.339  32.143 -30.028  1.00122.94           C  
ANISOU 1525  CE2 TYR A 214    15216  16540  14955   1016  -1198  -1693       C  
ATOM   1526  CZ  TYR A 214      -6.490  33.459 -29.642  1.00124.27           C  
ANISOU 1526  CZ  TYR A 214    15324  16663  15228   1059  -1247  -1767       C  
ATOM   1527  OH  TYR A 214      -7.401  33.775 -28.660  1.00133.47           O  
ANISOU 1527  OH  TYR A 214    16356  17896  16460   1043  -1241  -1933       O  
ATOM   1528  N   LEU A 215      -2.376  29.989 -31.137  1.00 87.85           N  
ANISOU 1528  N   LEU A 215    11101  12072  10206    927  -1042  -1261       N  
ATOM   1529  CA  LEU A 215      -2.515  29.112 -29.979  1.00 87.51           C  
ANISOU 1529  CA  LEU A 215    11012  12113  10123    852   -970  -1313       C  
ATOM   1530  C   LEU A 215      -1.266  29.146 -29.103  1.00 95.11           C  
ANISOU 1530  C   LEU A 215    11995  13092  11050    807   -903  -1270       C  
ATOM   1531  O   LEU A 215      -1.346  29.409 -27.892  1.00 90.26           O  
ANISOU 1531  O   LEU A 215    11315  12522  10458    760   -861  -1338       O  
ATOM   1532  CB  LEU A 215      -2.817  27.687 -30.440  1.00 76.42           C  
ANISOU 1532  CB  LEU A 215     9647  10746   8642    827   -961  -1286       C  
ATOM   1533  CG  LEU A 215      -4.211  27.476 -31.026  1.00 62.07           C  
ANISOU 1533  CG  LEU A 215     7790   8938   6856    853  -1014  -1353       C  
ATOM   1534  CD1 LEU A 215      -4.384  26.035 -31.453  1.00 61.16           C  
ANISOU 1534  CD1 LEU A 215     7722   8857   6658    823  -1001  -1318       C  
ATOM   1535  CD2 LEU A 215      -5.282  27.867 -30.025  1.00 53.22           C  
ANISOU 1535  CD2 LEU A 215     6554   7873   5796    823  -1006  -1494       C  
ATOM   1536  N   TYR A 216      -0.095  28.910 -29.701  1.00 99.63           N  
ANISOU 1536  N   TYR A 216    12654  13634  11566    818   -892  -1164       N  
ATOM   1537  CA  TYR A 216       1.129  28.912 -28.911  1.00 96.40           C  
ANISOU 1537  CA  TYR A 216    12265  13241  11123    780   -832  -1127       C  
ATOM   1538  C   TYR A 216       1.580  30.307 -28.500  1.00 93.95           C  
ANISOU 1538  C   TYR A 216    11926  12896  10877    797   -830  -1139       C  
ATOM   1539  O   TYR A 216       2.352  30.424 -27.542  1.00 99.69           O  
ANISOU 1539  O   TYR A 216    12641  13647  11591    759   -776  -1140       O  
ATOM   1540  CB  TYR A 216       2.267  28.198 -29.646  1.00 89.67           C  
ANISOU 1540  CB  TYR A 216    11502  12378  10191    786   -821  -1028       C  
ATOM   1541  CG  TYR A 216       2.175  26.688 -29.580  1.00 92.23           C  
ANISOU 1541  CG  TYR A 216    11854  12744  10444    752   -806  -1019       C  
ATOM   1542  CD1 TYR A 216       1.584  26.054 -28.496  1.00 90.38           C  
ANISOU 1542  CD1 TYR A 216    11579  12562  10200    689   -779  -1079       C  
ATOM   1543  CD2 TYR A 216       2.703  25.895 -30.590  1.00 96.47           C  
ANISOU 1543  CD2 TYR A 216    12460  13271  10922    774   -823   -954       C  
ATOM   1544  CE1 TYR A 216       1.502  24.677 -28.432  1.00 92.19           C  
ANISOU 1544  CE1 TYR A 216    11846  12819  10362    651   -777  -1065       C  
ATOM   1545  CE2 TYR A 216       2.626  24.517 -30.534  1.00 91.09           C  
ANISOU 1545  CE2 TYR A 216    11808  12619  10182    747   -820   -949       C  
ATOM   1546  CZ  TYR A 216       2.025  23.914 -29.452  1.00 92.73           C  
ANISOU 1546  CZ  TYR A 216    11985  12866  10382    685   -801  -1000       C  
ATOM   1547  OH  TYR A 216       1.937  22.544 -29.387  1.00 97.17           O  
ANISOU 1547  OH  TYR A 216    12588  13449  10885    650   -809   -990       O  
ATOM   1548  N   THR A 217       1.137  31.366 -29.186  1.00 83.32           N  
ANISOU 1548  N   THR A 217    10573  11487   9599    853   -895  -1148       N  
ATOM   1549  CA  THR A 217       1.421  32.703 -28.666  1.00 82.06           C  
ANISOU 1549  CA  THR A 217    10378  11290   9510    865   -902  -1174       C  
ATOM   1550  C   THR A 217       0.625  32.987 -27.396  1.00 81.71           C  
ANISOU 1550  C   THR A 217    10224  11294   9527    839   -881  -1297       C  
ATOM   1551  O   THR A 217       1.177  33.501 -26.411  1.00 73.76           O  
ANISOU 1551  O   THR A 217     9183  10305   8539    811   -836  -1320       O  
ATOM   1552  CB  THR A 217       1.140  33.760 -29.731  1.00 75.33           C  
ANISOU 1552  CB  THR A 217     9559  10348   8716    928   -994  -1151       C  
ATOM   1553  OG1 THR A 217       2.020  33.550 -30.839  1.00 71.59           O  
ANISOU 1553  OG1 THR A 217     9186   9842   8172    934  -1003  -1037       O  
ATOM   1554  CG2 THR A 217       1.383  35.153 -29.170  1.00 71.02           C  
ANISOU 1554  CG2 THR A 217     8979   9755   8250    942  -1013  -1183       C  
ATOM   1555  N   VAL A 218      -0.665  32.636 -27.387  1.00 87.82           N  
ANISOU 1555  N   VAL A 218    10938  12100  10329    843   -909  -1382       N  
ATOM   1556  CA  VAL A 218      -1.461  32.790 -26.170  1.00 87.67           C  
ANISOU 1556  CA  VAL A 218    10805  12148  10355    803   -881  -1513       C  
ATOM   1557  C   VAL A 218      -0.854  31.969 -25.039  1.00 97.38           C  
ANISOU 1557  C   VAL A 218    12033  13459  11510    712   -788  -1505       C  
ATOM   1558  O   VAL A 218      -0.604  32.475 -23.932  1.00 98.72           O  
ANISOU 1558  O   VAL A 218    12143  13663  11703    674   -745  -1558       O  
ATOM   1559  CB  VAL A 218      -2.925  32.385 -26.429  1.00 75.00           C  
ANISOU 1559  CB  VAL A 218     9141  10579   8777    812   -921  -1608       C  
ATOM   1560  CG1 VAL A 218      -3.685  32.267 -25.113  1.00 77.31           C  
ANISOU 1560  CG1 VAL A 218     9316  10972   9086    742   -873  -1746       C  
ATOM   1561  CG2 VAL A 218      -3.606  33.378 -27.363  1.00 60.30           C  
ANISOU 1561  CG2 VAL A 218     7267   8634   7010    905  -1026  -1639       C  
ATOM   1562  N   VAL A 219      -0.564  30.695 -25.321  1.00 98.50           N  
ANISOU 1562  N   VAL A 219    12242  13626  11558    678   -763  -1436       N  
ATOM   1563  CA  VAL A 219      -0.031  29.806 -24.294  1.00 93.81           C  
ANISOU 1563  CA  VAL A 219    11659  13098  10887    590   -692  -1424       C  
ATOM   1564  C   VAL A 219       1.315  30.312 -23.786  1.00 84.83           C  
ANISOU 1564  C   VAL A 219    10550  11940   9742    585   -653  -1369       C  
ATOM   1565  O   VAL A 219       1.592  30.290 -22.578  1.00 78.96           O  
ANISOU 1565  O   VAL A 219     9770  11249   8984    520   -600  -1404       O  
ATOM   1566  CB  VAL A 219       0.077  28.375 -24.855  1.00 92.41           C  
ANISOU 1566  CB  VAL A 219    11562  12930  10620    568   -694  -1355       C  
ATOM   1567  CG1 VAL A 219       0.957  27.509 -23.973  1.00 98.35           C  
ANISOU 1567  CG1 VAL A 219    12357  13719  11292    494   -642  -1313       C  
ATOM   1568  CG2 VAL A 219      -1.309  27.759 -25.025  1.00 81.61           C  
ANISOU 1568  CG2 VAL A 219    10153  11604   9249    546   -717  -1426       C  
ATOM   1569  N   GLY A 220       2.152  30.820 -24.691  1.00 84.18           N  
ANISOU 1569  N   GLY A 220    10531  11787   9667    649   -678  -1286       N  
ATOM   1570  CA  GLY A 220       3.485  31.237 -24.292  1.00 90.57           C  
ANISOU 1570  CA  GLY A 220    11371  12581  10460    642   -638  -1232       C  
ATOM   1571  C   GLY A 220       3.500  32.518 -23.480  1.00 86.38           C  
ANISOU 1571  C   GLY A 220    10768  12045  10006    643   -626  -1295       C  
ATOM   1572  O   GLY A 220       4.276  32.649 -22.526  1.00 83.14           O  
ANISOU 1572  O   GLY A 220    10345  11663   9580    603   -572  -1295       O  
ATOM   1573  N   ILE A 221       2.634  33.474 -23.827  1.00 89.44           N  
ANISOU 1573  N   ILE A 221    11106  12396  10482    691   -681  -1354       N  
ATOM   1574  CA  ILE A 221       2.537  34.692 -23.026  1.00 92.36           C  
ANISOU 1574  CA  ILE A 221    11396  12759  10936    696   -679  -1431       C  
ATOM   1575  C   ILE A 221       1.979  34.388 -21.638  1.00 95.59           C  
ANISOU 1575  C   ILE A 221    11710  13264  11346    622   -624  -1537       C  
ATOM   1576  O   ILE A 221       2.536  34.830 -20.622  1.00 91.88           O  
ANISOU 1576  O   ILE A 221    11202  12823  10886    586   -575  -1563       O  
ATOM   1577  CB  ILE A 221       1.705  35.758 -23.762  1.00 89.69           C  
ANISOU 1577  CB  ILE A 221    11030  12349  10699    771   -770  -1477       C  
ATOM   1578  CG1 ILE A 221       2.577  36.475 -24.802  1.00 80.74           C  
ANISOU 1578  CG1 ILE A 221     9990  11117   9569    822   -814  -1370       C  
ATOM   1579  CG2 ILE A 221       1.093  36.745 -22.772  1.00 90.34           C  
ANISOU 1579  CG2 ILE A 221    10995  12450  10879    772   -776  -1608       C  
ATOM   1580  CD1 ILE A 221       1.875  37.588 -25.555  1.00 74.50           C  
ANISOU 1580  CD1 ILE A 221     9194  10237   8876    893   -921  -1399       C  
ATOM   1581  N   THR A 222       0.885  33.617 -21.563  1.00 98.34           N  
ANISOU 1581  N   THR A 222    12019  13670  11678    591   -630  -1602       N  
ATOM   1582  CA  THR A 222       0.333  33.340 -20.237  1.00 89.04           C  
ANISOU 1582  CA  THR A 222    10749  12594  10488    502   -576  -1708       C  
ATOM   1583  C   THR A 222       1.276  32.485 -19.398  1.00 75.75           C  
ANISOU 1583  C   THR A 222     9114  10959   8707    417   -505  -1647       C  
ATOM   1584  O   THR A 222       1.269  32.594 -18.168  1.00 72.24           O  
ANISOU 1584  O   THR A 222     8606  10586   8256    343   -454  -1713       O  
ATOM   1585  CB  THR A 222      -1.041  32.668 -20.326  1.00 91.54           C  
ANISOU 1585  CB  THR A 222    11014  12972  10798    472   -594  -1795       C  
ATOM   1586  OG1 THR A 222      -0.896  31.310 -20.759  1.00100.72           O  
ANISOU 1586  OG1 THR A 222    12264  14144  11859    436   -584  -1710       O  
ATOM   1587  CG2 THR A 222      -1.955  33.425 -21.280  1.00 86.30           C  
ANISOU 1587  CG2 THR A 222    10312  12250  10229    567   -679  -1851       C  
ATOM   1588  N   LEU A 223       2.093  31.637 -20.029  1.00 82.63           N  
ANISOU 1588  N   LEU A 223    10096  11796   9504    426   -505  -1527       N  
ATOM   1589  CA  LEU A 223       3.038  30.835 -19.257  1.00 85.03           C  
ANISOU 1589  CA  LEU A 223    10452  12135   9722    356   -454  -1471       C  
ATOM   1590  C   LEU A 223       4.218  31.664 -18.765  1.00 80.24           C  
ANISOU 1590  C   LEU A 223     9847  11504   9135    371   -421  -1441       C  
ATOM   1591  O   LEU A 223       4.626  31.536 -17.604  1.00 76.60           O  
ANISOU 1591  O   LEU A 223     9365  11096   8644    300   -372  -1461       O  
ATOM   1592  CB  LEU A 223       3.536  29.652 -20.087  1.00 90.21           C  
ANISOU 1592  CB  LEU A 223    11217  12759  10299    369   -475  -1368       C  
ATOM   1593  CG  LEU A 223       2.645  28.412 -20.134  1.00 92.58           C  
ANISOU 1593  CG  LEU A 223    11533  13103  10541    312   -489  -1385       C  
ATOM   1594  CD1 LEU A 223       3.415  27.261 -20.748  1.00102.30           C  
ANISOU 1594  CD1 LEU A 223    12875  14300  11695    323   -507  -1283       C  
ATOM   1595  CD2 LEU A 223       2.133  28.047 -18.746  1.00 89.09           C  
ANISOU 1595  CD2 LEU A 223    11037  12750  10063    193   -447  -1460       C  
ATOM   1596  N   ARG A 224       4.788  32.505 -19.633  1.00 79.76           N  
ANISOU 1596  N   ARG A 224     9817  11367   9121    455   -449  -1391       N  
ATOM   1597  CA  ARG A 224       5.916  33.327 -19.212  1.00 82.02           C  
ANISOU 1597  CA  ARG A 224    10107  11632   9426    466   -417  -1364       C  
ATOM   1598  C   ARG A 224       5.496  34.325 -18.142  1.00 87.30           C  
ANISOU 1598  C   ARG A 224    10670  12335  10166    440   -394  -1467       C  
ATOM   1599  O   ARG A 224       6.259  34.609 -17.211  1.00 93.79           O  
ANISOU 1599  O   ARG A 224    11475  13184  10979    404   -345  -1471       O  
ATOM   1600  CB  ARG A 224       6.520  34.035 -20.423  1.00 90.68           C  
ANISOU 1600  CB  ARG A 224    11262  12644  10550    547   -456  -1292       C  
ATOM   1601  CG  ARG A 224       7.765  34.872 -20.147  1.00102.39           C  
ANISOU 1601  CG  ARG A 224    12760  14101  12043    556   -425  -1255       C  
ATOM   1602  CD  ARG A 224       8.444  35.221 -21.462  1.00118.27           C  
ANISOU 1602  CD  ARG A 224    14851  16042  14045    612   -460  -1168       C  
ATOM   1603  NE  ARG A 224       7.456  35.466 -22.512  1.00136.84           N  
ANISOU 1603  NE  ARG A 224    17210  18344  16437    659   -532  -1173       N  
ATOM   1604  CZ  ARG A 224       7.733  35.536 -23.811  1.00142.65           C  
ANISOU 1604  CZ  ARG A 224    18020  19027  17152    698   -575  -1099       C  
ATOM   1605  NH1 ARG A 224       8.970  35.329 -24.242  1.00146.54           N  
ANISOU 1605  NH1 ARG A 224    18581  19517  17580    692   -548  -1022       N  
ATOM   1606  NH2 ARG A 224       6.763  35.767 -24.686  1.00140.99           N  
ANISOU 1606  NH2 ARG A 224    17815  18772  16982    739   -645  -1109       N  
ATOM   1607  N   ALA A 225       4.268  34.836 -18.232  1.00 80.41           N  
ANISOU 1607  N   ALA A 225     9719  11468   9366    459   -431  -1561       N  
ATOM   1608  CA  ALA A 225       3.805  35.794 -17.238  1.00 82.90           C  
ANISOU 1608  CA  ALA A 225     9919  11821   9756    440   -414  -1679       C  
ATOM   1609  C   ALA A 225       3.356  35.142 -15.934  1.00 76.21           C  
ANISOU 1609  C   ALA A 225     9006  11090   8862    330   -355  -1759       C  
ATOM   1610  O   ALA A 225       3.255  35.840 -14.919  1.00 80.66           O  
ANISOU 1610  O   ALA A 225     9478  11702   9468    295   -323  -1850       O  
ATOM   1611  CB  ALA A 225       2.667  36.633 -17.819  1.00 96.50           C  
ANISOU 1611  CB  ALA A 225    11576  13506  11583    507   -487  -1766       C  
ATOM   1612  N   SER A 226       3.115  33.831 -15.930  1.00 72.96           N  
ANISOU 1612  N   SER A 226     8641  10723   8358    268   -343  -1728       N  
ATOM   1613  CA  SER A 226       2.537  33.136 -14.776  1.00 62.72           C  
ANISOU 1613  CA  SER A 226     7290   9537   7003    147   -297  -1803       C  
ATOM   1614  C   SER A 226       3.393  33.261 -13.528  1.00 74.76           C  
ANISOU 1614  C   SER A 226     8803  11109   8493     75   -235  -1801       C  
ATOM   1615  O   SER A 226       3.850  32.260 -12.979  1.00101.85           O  
ANISOU 1615  O   SER A 226    12295  14576  11827     -8   -207  -1748       O  
ATOM   1616  CB  SER A 226       2.318  31.655 -15.095  1.00 72.63           C  
ANISOU 1616  CB  SER A 226     8627  10811   8158     94   -305  -1742       C  
ATOM   1617  OG  SER A 226       1.228  31.466 -15.985  1.00 93.43           O  
ANISOU 1617  OG  SER A 226    11245  13436  10819    133   -352  -1779       O  
ATOM   1618  N   GLY A1218       5.495  31.286 -13.403  1.00124.77           N  
ANISOU 1618  N   GLY A1218    15363  17405  14638     16   -215  -1572       N  
ATOM   1619  CA  GLY A1218       6.341  32.418 -13.729  1.00117.36           C  
ANISOU 1619  CA  GLY A1218    14417  16405  13770    106   -211  -1547       C  
ATOM   1620  C   GLY A1218       6.886  33.179 -12.535  1.00 99.15           C  
ANISOU 1620  C   GLY A1218    12049  14138  11483     64   -158  -1592       C  
ATOM   1621  O   GLY A1218       6.743  34.397 -12.457  1.00101.32           O  
ANISOU 1621  O   GLY A1218    12248  14402  11847    107   -153  -1653       O  
ATOM   1622  N   ILE A1219       7.523  32.464 -11.608  1.00 86.40           N  
ANISOU 1622  N   ILE A1219    10474  12567   9788    -18   -126  -1562       N  
ATOM   1623  CA  ILE A1219       8.177  33.085 -10.463  1.00 83.63           C  
ANISOU 1623  CA  ILE A1219    10077  12255   9445    -61    -76  -1592       C  
ATOM   1624  C   ILE A1219       9.573  32.491 -10.345  1.00 85.06           C  
ANISOU 1624  C   ILE A1219    10357  12402   9559    -58    -72  -1491       C  
ATOM   1625  O   ILE A1219       9.804  31.322 -10.676  1.00 94.91           O  
ANISOU 1625  O   ILE A1219    11697  13631  10733    -71   -104  -1422       O  
ATOM   1626  CB  ILE A1219       7.397  32.881  -9.147  1.00 83.77           C  
ANISOU 1626  CB  ILE A1219    10018  12385   9428   -194    -38  -1688       C  
ATOM   1627  CG1 ILE A1219       8.061  33.662  -8.016  1.00 79.46           C  
ANISOU 1627  CG1 ILE A1219     9414  11878   8898   -230     15  -1726       C  
ATOM   1628  CG2 ILE A1219       7.325  31.414  -8.781  1.00 98.72           C  
ANISOU 1628  CG2 ILE A1219    11994  14312  11203   -296    -50  -1640       C  
ATOM   1629  CD1 ILE A1219       7.369  33.501  -6.706  1.00 85.80           C  
ANISOU 1629  CD1 ILE A1219    10141  12801   9660   -370     56  -1823       C  
ATOM   1630  N   ASP A1220      10.509  33.311  -9.868  1.00 70.20           N  
ANISOU 1630  N   ASP A1220     8453  10513   7708    -37    -37  -1489       N  
ATOM   1631  CA  ASP A1220      11.878  32.866  -9.628  1.00 70.11           C  
ANISOU 1631  CA  ASP A1220     8519  10480   7641    -33    -30  -1412       C  
ATOM   1632  C   ASP A1220      11.958  32.225  -8.244  1.00 73.59           C  
ANISOU 1632  C   ASP A1220     8962  10992   8008   -153     -8  -1431       C  
ATOM   1633  O   ASP A1220      12.200  32.899  -7.241  1.00 72.13           O  
ANISOU 1633  O   ASP A1220     8713  10853   7839   -197     39  -1479       O  
ATOM   1634  CB  ASP A1220      12.805  34.068  -9.780  1.00 71.40           C  
ANISOU 1634  CB  ASP A1220     8657  10606   7868     40     -3  -1406       C  
ATOM   1635  CG  ASP A1220      14.268  33.725  -9.623  1.00 82.77           C  
ANISOU 1635  CG  ASP A1220    10165  12025   9259     55      5  -1339       C  
ATOM   1636  OD1 ASP A1220      14.620  32.528  -9.636  1.00 98.05           O  
ANISOU 1636  OD1 ASP A1220    12180  13956  11118     34    -25  -1289       O  
ATOM   1637  OD2 ASP A1220      15.075  34.672  -9.522  1.00 79.33           O  
ANISOU 1637  OD2 ASP A1220     9704  11574   8864     93     37  -1341       O  
ATOM   1638  N   CYS A1221      11.768  30.896  -8.188  1.00 71.84           N  
ANISOU 1638  N   CYS A1221     8818  10776   7700   -213    -46  -1390       N  
ATOM   1639  CA  CYS A1221      11.825  30.185  -6.909  1.00 78.35           C  
ANISOU 1639  CA  CYS A1221     9665  11661   8442   -341    -39  -1396       C  
ATOM   1640  C   CYS A1221      13.224  30.157  -6.312  1.00 77.19           C  
ANISOU 1640  C   CYS A1221     9564  11496   8267   -334    -33  -1350       C  
ATOM   1641  O   CYS A1221      13.368  29.894  -5.112  1.00 74.92           O  
ANISOU 1641  O   CYS A1221     9280  11262   7925   -438    -19  -1364       O  
ATOM   1642  CB  CYS A1221      11.281  28.758  -7.027  1.00 84.22           C  
ANISOU 1642  CB  CYS A1221    10495  12405   9099   -411    -95  -1358       C  
ATOM   1643  SG  CYS A1221       9.513  28.645  -7.377  1.00 88.50           S  
ANISOU 1643  SG  CYS A1221    10975  12999   9652   -462    -95  -1430       S  
ATOM   1644  N   SER A1222      14.254  30.391  -7.125  1.00 79.68           N  
ANISOU 1644  N   SER A1222     9918  11742   8614   -219    -46  -1299       N  
ATOM   1645  CA  SER A1222      15.607  30.483  -6.594  1.00 88.38           C  
ANISOU 1645  CA  SER A1222    11049  12832   9700   -202    -36  -1270       C  
ATOM   1646  C   SER A1222      15.808  31.743  -5.767  1.00 80.25           C  
ANISOU 1646  C   SER A1222     9922  11847   8721   -219     34  -1329       C  
ATOM   1647  O   SER A1222      16.758  31.806  -4.981  1.00 76.17           O  
ANISOU 1647  O   SER A1222     9417  11343   8180   -239     50  -1320       O  
ATOM   1648  CB  SER A1222      16.625  30.445  -7.733  1.00 88.83           C  
ANISOU 1648  CB  SER A1222    11159  12816   9775    -80    -62  -1215       C  
ATOM   1649  OG  SER A1222      16.695  31.702  -8.384  1.00 86.24           O  
ANISOU 1649  OG  SER A1222    10767  12472   9528     -4    -21  -1236       O  
ATOM   1650  N   PHE A1223      14.930  32.735  -5.913  1.00 71.42           N  
ANISOU 1650  N   PHE A1223     8709  10753   7676   -209     71  -1394       N  
ATOM   1651  CA  PHE A1223      14.984  33.944  -5.103  1.00 67.62           C  
ANISOU 1651  CA  PHE A1223     8127  10316   7250   -228    132  -1463       C  
ATOM   1652  C   PHE A1223      13.906  33.969  -4.025  1.00 70.54           C  
ANISOU 1652  C   PHE A1223     8418  10780   7603   -349    160  -1549       C  
ATOM   1653  O   PHE A1223      14.221  34.122  -2.840  1.00 61.09           O  
ANISOU 1653  O   PHE A1223     7191   9644   6379   -429    197  -1580       O  
ATOM   1654  CB  PHE A1223      14.873  35.197  -5.977  1.00 70.30           C  
ANISOU 1654  CB  PHE A1223     8408  10610   7694   -126    145  -1488       C  
ATOM   1655  CG  PHE A1223      14.873  36.470  -5.186  1.00 74.12           C  
ANISOU 1655  CG  PHE A1223     8786  11131   8245   -139    198  -1566       C  
ATOM   1656  CD1 PHE A1223      16.069  37.000  -4.731  1.00 73.32           C  
ANISOU 1656  CD1 PHE A1223     8685  11023   8149   -121    232  -1548       C  
ATOM   1657  CD2 PHE A1223      13.699  37.131  -4.884  1.00 87.43           C  
ANISOU 1657  CD2 PHE A1223    10367  12862   9991   -168    212  -1665       C  
ATOM   1658  CE1 PHE A1223      16.100  38.168  -3.991  1.00 67.85           C  
ANISOU 1658  CE1 PHE A1223     7896  10363   7520   -132    280  -1621       C  
ATOM   1659  CE2 PHE A1223      13.724  38.306  -4.144  1.00 84.60           C  
ANISOU 1659  CE2 PHE A1223     9907  12537   9701   -176    255  -1746       C  
ATOM   1660  CZ  PHE A1223      14.931  38.820  -3.695  1.00 70.23           C  
ANISOU 1660  CZ  PHE A1223     8094  10706   7885   -159    290  -1720       C  
ATOM   1661  N   TRP A1224      12.638  33.813  -4.405  1.00 74.07           N  
ANISOU 1661  N   TRP A1224     8830  11248   8063   -371    145  -1594       N  
ATOM   1662  CA  TRP A1224      11.541  33.877  -3.438  1.00 65.90           C  
ANISOU 1662  CA  TRP A1224     7706  10318   7013   -492    175  -1695       C  
ATOM   1663  C   TRP A1224      11.510  32.556  -2.685  1.00 62.14           C  
ANISOU 1663  C   TRP A1224     7310   9889   6412   -624    157  -1656       C  
ATOM   1664  O   TRP A1224      10.805  31.610  -3.042  1.00 65.03           O  
ANISOU 1664  O   TRP A1224     7727  10258   6724   -667    118  -1637       O  
ATOM   1665  CB  TRP A1224      10.223  34.163  -4.140  1.00 67.61           C  
ANISOU 1665  CB  TRP A1224     7856  10544   7289   -465    161  -1765       C  
ATOM   1666  CG  TRP A1224      10.289  35.425  -4.913  1.00 71.68           C  
ANISOU 1666  CG  TRP A1224     8313  10998   7925   -336    160  -1792       C  
ATOM   1667  CD1 TRP A1224      10.497  35.554  -6.251  1.00 79.27           C  
ANISOU 1667  CD1 TRP A1224     9328  11860   8930   -216    117  -1728       C  
ATOM   1668  CD2 TRP A1224      10.240  36.754  -4.383  1.00 63.72           C  
ANISOU 1668  CD2 TRP A1224     7188  10015   7006   -318    198  -1885       C  
ATOM   1669  NE1 TRP A1224      10.529  36.883  -6.598  1.00 81.66           N  
ANISOU 1669  NE1 TRP A1224     9564  12123   9342   -131    120  -1771       N  
ATOM   1670  CE2 TRP A1224      10.377  37.641  -5.467  1.00 67.68           C  
ANISOU 1670  CE2 TRP A1224     7688  10423   7605   -186    167  -1869       C  
ATOM   1671  CE3 TRP A1224      10.071  37.279  -3.099  1.00 58.74           C  
ANISOU 1671  CE3 TRP A1224     6456   9480   6381   -404    251  -1984       C  
ATOM   1672  CZ2 TRP A1224      10.355  39.024  -5.306  1.00 64.71           C  
ANISOU 1672  CZ2 TRP A1224     7217  10034   7335   -135    180  -1945       C  
ATOM   1673  CZ3 TRP A1224      10.046  38.651  -2.941  1.00 60.78           C  
ANISOU 1673  CZ3 TRP A1224     6610   9734   6750   -348    270  -2067       C  
ATOM   1674  CH2 TRP A1224      10.187  39.509  -4.039  1.00 61.31           C  
ANISOU 1674  CH2 TRP A1224     6683   9695   6916   -212    230  -2046       C  
ATOM   1675  N   ASN A1225      12.317  32.510  -1.629  1.00 62.60           N  
ANISOU 1675  N   ASN A1225     7384   9979   6422   -689    180  -1642       N  
ATOM   1676  CA  ASN A1225      12.669  31.299  -0.905  1.00 66.09           C  
ANISOU 1676  CA  ASN A1225     7930  10438   6744   -800    146  -1581       C  
ATOM   1677  C   ASN A1225      13.042  31.705   0.513  1.00 62.11           C  
ANISOU 1677  C   ASN A1225     7376  10014   6207   -903    195  -1625       C  
ATOM   1678  O   ASN A1225      13.883  32.591   0.697  1.00 51.78           O  
ANISOU 1678  O   ASN A1225     6027   8690   4957   -834    230  -1633       O  
ATOM   1679  CB  ASN A1225      13.820  30.552  -1.585  1.00 70.77           C  
ANISOU 1679  CB  ASN A1225     8655  10924   7312   -710     83  -1465       C  
ATOM   1680  CG  ASN A1225      13.969  29.123  -1.083  1.00 70.27           C  
ANISOU 1680  CG  ASN A1225     8715  10855   7129   -814     17  -1399       C  
ATOM   1681  OD1 ASN A1225      13.893  28.857   0.121  1.00 65.72           O  
ANISOU 1681  OD1 ASN A1225     8144  10346   6480   -953     26  -1416       O  
ATOM   1682  ND2 ASN A1225      14.191  28.195  -2.007  1.00 70.27           N  
ANISOU 1682  ND2 ASN A1225     8819  10771   7108   -751    -56  -1324       N  
ATOM   1683  N   GLU A1226      12.428  31.062   1.509  1.00 68.86           N  
ANISOU 1683  N   GLU A1226     8239  10958   6965  -1074    197  -1652       N  
ATOM   1684  CA  GLU A1226      12.640  31.468   2.895  1.00 74.69           C  
ANISOU 1684  CA  GLU A1226     8921  11790   7667  -1190    248  -1705       C  
ATOM   1685  C   GLU A1226      14.070  31.233   3.356  1.00 66.38           C  
ANISOU 1685  C   GLU A1226     7957  10685   6580  -1168    224  -1622       C  
ATOM   1686  O   GLU A1226      14.490  31.821   4.358  1.00 57.81           O  
ANISOU 1686  O   GLU A1226     6816   9659   5489  -1222    272  -1662       O  
ATOM   1687  CB  GLU A1226      11.707  30.700   3.832  1.00 83.70           C  
ANISOU 1687  CB  GLU A1226    10069  13041   8691  -1398    248  -1743       C  
ATOM   1688  CG  GLU A1226      11.520  31.370   5.186  1.00 96.93           C  
ANISOU 1688  CG  GLU A1226    11636  14849  10343  -1529    321  -1842       C  
ATOM   1689  CD  GLU A1226      10.590  30.603   6.105  1.00108.45           C  
ANISOU 1689  CD  GLU A1226    13103  16430  11672  -1755    324  -1883       C  
ATOM   1690  OE1 GLU A1226       9.809  29.763   5.605  1.00116.27           O  
ANISOU 1690  OE1 GLU A1226    14148  17415  12613  -1802    283  -1864       O  
ATOM   1691  OE2 GLU A1226      10.665  30.826   7.335  1.00101.91           O  
ANISOU 1691  OE2 GLU A1226    12231  15705  10785  -1892    367  -1933       O  
ATOM   1692  N   SER A1227      14.829  30.411   2.634  1.00 72.29           N  
ANISOU 1692  N   SER A1227     8835  11326   7308  -1086    149  -1515       N  
ATOM   1693  CA  SER A1227      16.177  30.042   3.051  1.00 80.97           C  
ANISOU 1693  CA  SER A1227    10025  12372   8369  -1065    111  -1443       C  
ATOM   1694  C   SER A1227      17.127  31.235   3.168  1.00 86.76           C  
ANISOU 1694  C   SER A1227    10682  13098   9186   -964    170  -1470       C  
ATOM   1695  O   SER A1227      18.131  31.137   3.885  1.00 82.67           O  
ANISOU 1695  O   SER A1227    10204  12574   8633   -980    159  -1441       O  
ATOM   1696  CB  SER A1227      16.746  29.016   2.072  1.00 82.05           C  
ANISOU 1696  CB  SER A1227    10295  12393   8487   -972     17  -1346       C  
ATOM   1697  OG  SER A1227      15.883  27.898   1.964  1.00 85.38           O  
ANISOU 1697  OG  SER A1227    10794  12816   8832  -1066    -43  -1317       O  
ATOM   1698  N   TYR A1228      16.848  32.352   2.491  1.00 84.20           N  
ANISOU 1698  N   TYR A1228    10252  12769   8969   -864    226  -1526       N  
ATOM   1699  CA  TYR A1228      17.728  33.511   2.571  1.00 65.32           C  
ANISOU 1699  CA  TYR A1228     7794  10368   6658   -775    279  -1551       C  
ATOM   1700  C   TYR A1228      17.403  34.437   3.738  1.00 65.02           C  
ANISOU 1700  C   TYR A1228     7634  10433   6637   -863    355  -1646       C  
ATOM   1701  O   TYR A1228      18.141  35.400   3.972  1.00 74.50           O  
ANISOU 1701  O   TYR A1228     8777  11632   7898   -806    401  -1671       O  
ATOM   1702  CB  TYR A1228      17.648  34.291   1.255  1.00 46.15           C  
ANISOU 1702  CB  TYR A1228     5324   7874   4335   -627    290  -1557       C  
ATOM   1703  CG  TYR A1228      18.082  33.458   0.075  1.00 39.76           C  
ANISOU 1703  CG  TYR A1228     4626   6970   3511   -535    222  -1469       C  
ATOM   1704  CD1 TYR A1228      19.416  33.134  -0.121  1.00 53.81           C  
ANISOU 1704  CD1 TYR A1228     6482   8692   5272   -466    192  -1406       C  
ATOM   1705  CD2 TYR A1228      17.153  32.967  -0.823  1.00 43.76           C  
ANISOU 1705  CD2 TYR A1228     5155   7451   4019   -519    186  -1458       C  
ATOM   1706  CE1 TYR A1228      19.817  32.355  -1.191  1.00 48.21           C  
ANISOU 1706  CE1 TYR A1228     5864   7905   4549   -383    128  -1341       C  
ATOM   1707  CE2 TYR A1228      17.542  32.190  -1.896  1.00 52.75           C  
ANISOU 1707  CE2 TYR A1228     6390   8510   5143   -437    124  -1384       C  
ATOM   1708  CZ  TYR A1228      18.876  31.887  -2.077  1.00 54.62           C  
ANISOU 1708  CZ  TYR A1228     6697   8693   5363   -370     95  -1328       C  
ATOM   1709  OH  TYR A1228      19.262  31.108  -3.147  1.00 63.32           O  
ANISOU 1709  OH  TYR A1228     7885   9723   6451   -289     33  -1268       O  
ATOM   1710  N   LEU A1229      16.330  34.160   4.469  1.00 66.38           N  
ANISOU 1710  N   LEU A1229     7764  10700   6756  -1007    370  -1706       N  
ATOM   1711  CA  LEU A1229      15.951  34.833   5.704  1.00 78.38           C  
ANISOU 1711  CA  LEU A1229     9173  12340   8270  -1122    438  -1805       C  
ATOM   1712  C   LEU A1229      16.712  34.249   6.898  1.00 94.76           C  
ANISOU 1712  C   LEU A1229    11315  14451  10239  -1236    427  -1763       C  
ATOM   1713  O   LEU A1229      17.198  33.117   6.858  1.00106.31           O  
ANISOU 1713  O   LEU A1229    12916  15859  11617  -1261    354  -1666       O  
ATOM   1714  CB  LEU A1229      14.441  34.760   5.896  1.00 74.24           C  
ANISOU 1714  CB  LEU A1229     8568  11912   7728  -1231    458  -1898       C  
ATOM   1715  CG  LEU A1229      13.776  35.470   4.713  1.00 74.00           C  
ANISOU 1715  CG  LEU A1229     8465  11834   7816  -1100    462  -1945       C  
ATOM   1716  CD1 LEU A1229      12.272  35.484   4.841  1.00 79.54           C  
ANISOU 1716  CD1 LEU A1229     9072  12633   8515  -1191    480  -2056       C  
ATOM   1717  CD2 LEU A1229      14.326  36.882   4.537  1.00 74.26           C  
ANISOU 1717  CD2 LEU A1229     8406  11835   7974   -976    505  -1991       C  
ATOM   1718  N   THR A1230      16.845  35.051   7.956  1.00 88.52           N  
ANISOU 1718  N   THR A1230    10426  13749   9458  -1302    494  -1839       N  
ATOM   1719  CA  THR A1230      17.614  34.669   9.135  1.00 86.35           C  
ANISOU 1719  CA  THR A1230    10204  13513   9091  -1406    488  -1806       C  
ATOM   1720  C   THR A1230      16.720  34.467  10.354  1.00 94.15           C  
ANISOU 1720  C   THR A1230    11141  14646   9987  -1618    522  -1880       C  
ATOM   1721  O   THR A1230      15.760  35.213  10.561  1.00 97.38           O  
ANISOU 1721  O   THR A1230    11408  15151  10441  -1661    587  -2001       O  
ATOM   1722  CB  THR A1230      18.642  35.753   9.472  1.00 87.37           C  
ANISOU 1722  CB  THR A1230    10267  13635   9296  -1322    542  -1831       C  
ATOM   1723  OG1 THR A1230      19.205  36.274   8.264  1.00 87.27           O  
ANISOU 1723  OG1 THR A1230    10258  13513   9387  -1133    535  -1799       O  
ATOM   1724  CG2 THR A1230      19.750  35.190  10.347  1.00 99.88           C  
ANISOU 1724  CG2 THR A1230    11946  15212  10793  -1377    509  -1764       C  
ATOM   1725  N   GLY A1231      17.028  33.442  11.150  1.00 93.46           N  
ANISOU 1725  N   GLY A1231    11169  14575   9766  -1754    470  -1812       N  
ATOM   1726  CA  GLY A1231      16.338  33.258  12.411  1.00 93.00           C  
ANISOU 1726  CA  GLY A1231    11071  14661   9602  -1975    502  -1875       C  
ATOM   1727  C   GLY A1231      14.974  32.604  12.293  1.00 94.55           C  
ANISOU 1727  C   GLY A1231    11267  14926   9730  -2106    492  -1911       C  
ATOM   1728  O   GLY A1231      14.521  32.188  11.224  1.00 89.60           O  
ANISOU 1728  O   GLY A1231    10682  14229   9134  -2027    451  -1879       O  
ATOM   1729  N   SER A1232      14.312  32.503  13.443  1.00 92.56           N  
ANISOU 1729  N   SER A1232    10967  14824   9377  -2321    530  -1983       N  
ATOM   1730  CA  SER A1232      12.960  31.978  13.475  1.00 89.13           C  
ANISOU 1730  CA  SER A1232    10510  14485   8870  -2472    536  -2041       C  
ATOM   1731  C   SER A1232      12.006  33.060  12.967  1.00 86.45           C  
ANISOU 1731  C   SER A1232     9979  14211   8658  -2393    615  -2193       C  
ATOM   1732  O   SER A1232      12.313  34.254  12.999  1.00 75.76           O  
ANISOU 1732  O   SER A1232     8498  12866   7422  -2282    675  -2270       O  
ATOM   1733  CB  SER A1232      12.587  31.522  14.889  1.00101.20           C  
ANISOU 1733  CB  SER A1232    12050  16164  10238  -2744    552  -2074       C  
ATOM   1734  OG  SER A1232      12.107  32.593  15.686  1.00105.70           O  
ANISOU 1734  OG  SER A1232    12428  16893  10840  -2817    659  -2236       O  
ATOM   1735  N   ARG A1233      10.841  32.624  12.482  1.00 75.72           N  
ANISOU 1735  N   ARG A1233     8503   9969  10297    637   -187    -29       N  
ATOM   1736  CA  ARG A1233       9.841  33.563  11.983  1.00 70.60           C  
ANISOU 1736  CA  ARG A1233     7912   9210   9701    587   -168    -72       C  
ATOM   1737  C   ARG A1233       9.332  34.484  13.082  1.00 77.45           C  
ANISOU 1737  C   ARG A1233     8797  10109  10523    549   -146   -105       C  
ATOM   1738  O   ARG A1233       8.969  35.635  12.809  1.00 92.27           O  
ANISOU 1738  O   ARG A1233    10716  11937  12406    489   -129   -165       O  
ATOM   1739  CB  ARG A1233       8.673  32.802  11.354  1.00 66.91           C  
ANISOU 1739  CB  ARG A1233     7479   8613   9329    632   -163    -22       C  
ATOM   1740  CG  ARG A1233       7.758  33.672  10.517  1.00 62.67           C  
ANISOU 1740  CG  ARG A1233     6998   7963   8853    592   -153    -65       C  
ATOM   1741  CD  ARG A1233       6.570  32.889   9.995  1.00 57.38           C  
ANISOU 1741  CD  ARG A1233     6349   7176   8276    634   -156    -17       C  
ATOM   1742  NE  ARG A1233       5.826  33.666   9.017  1.00 56.82           N  
ANISOU 1742  NE  ARG A1233     6327   7004   8260    605   -155    -58       N  
ATOM   1743  CZ  ARG A1233       6.097  33.642   7.713  1.00 65.54           C  
ANISOU 1743  CZ  ARG A1233     7456   8049   9397    606   -177    -78       C  
ATOM   1744  NH1 ARG A1233       7.077  32.870   7.263  1.00 68.45           N  
ANISOU 1744  NH1 ARG A1233     7806   8450   9753    633   -197    -59       N  
ATOM   1745  NH2 ARG A1233       5.395  34.375   6.856  1.00 61.49           N  
ANISOU 1745  NH2 ARG A1233     6991   7447   8926    588   -177   -115       N  
ATOM   1746  N   ASP A1234       9.297  33.996  14.324  1.00 81.48           N  
ANISOU 1746  N   ASP A1234     9283  10695  10981    587   -141    -66       N  
ATOM   1747  CA  ASP A1234       8.840  34.811  15.442  1.00 89.36           C  
ANISOU 1747  CA  ASP A1234    10302  11726  11924    561   -119    -94       C  
ATOM   1748  C   ASP A1234       9.801  35.966  15.712  1.00 84.58           C  
ANISOU 1748  C   ASP A1234     9689  11209  11239    484   -131   -180       C  
ATOM   1749  O   ASP A1234       9.373  37.114  15.915  1.00 81.73           O  
ANISOU 1749  O   ASP A1234     9374  10817  10861    427   -108   -238       O  
ATOM   1750  CB  ASP A1234       8.722  33.915  16.676  1.00116.95           C  
ANISOU 1750  CB  ASP A1234    13773  15290  15374    630   -111    -27       C  
ATOM   1751  CG  ASP A1234       7.441  33.120  16.688  1.00140.79           C  
ANISOU 1751  CG  ASP A1234    16814  18206  18473    685    -81     46       C  
ATOM   1752  OD1 ASP A1234       6.884  32.886  15.593  1.00145.90           O  
ANISOU 1752  OD1 ASP A1234    17478  18744  19215    683    -82     56       O  
ATOM   1753  OD2 ASP A1234       7.003  32.696  17.779  1.00154.28           O  
ANISOU 1753  OD2 ASP A1234    18523  19945  20151    732    -55     95       O  
ATOM   1754  N   GLU A1235      11.106  35.684  15.690  1.00 83.14           N  
ANISOU 1754  N   GLU A1235     9448  11134  11007    480   -164   -190       N  
ATOM   1755  CA  GLU A1235      12.108  36.726  15.879  1.00 77.03           C  
ANISOU 1755  CA  GLU A1235     8655  10449  10164    398   -180   -274       C  
ATOM   1756  C   GLU A1235      12.042  37.753  14.756  1.00 74.28           C  
ANISOU 1756  C   GLU A1235     8350  10008   9866    322   -162   -338       C  
ATOM   1757  O   GLU A1235      12.203  38.959  14.989  1.00 85.90           O  
ANISOU 1757  O   GLU A1235     9849  11490  11299    242   -149   -416       O  
ATOM   1758  CB  GLU A1235      13.481  36.058  15.943  1.00 84.41           C  
ANISOU 1758  CB  GLU A1235     9505  11514  11051    421   -220   -260       C  
ATOM   1759  CG  GLU A1235      13.553  34.990  17.037  1.00102.00           C  
ANISOU 1759  CG  GLU A1235    11697  13833  13224    510   -234   -189       C  
ATOM   1760  CD  GLU A1235      14.870  34.237  17.064  1.00115.15           C  
ANISOU 1760  CD  GLU A1235    13278  15629  14844    549   -273   -165       C  
ATOM   1761  OE1 GLU A1235      15.208  33.607  16.038  1.00113.44           O  
ANISOU 1761  OE1 GLU A1235    13044  15375  14684    578   -276   -132       O  
ATOM   1762  OE2 GLU A1235      15.550  34.247  18.117  1.00125.64           O  
ANISOU 1762  OE2 GLU A1235    14560  17099  16077    559   -301   -176       O  
ATOM   1763  N   ARG A1236      11.774  37.289  13.530  1.00 70.48           N  
ANISOU 1763  N   ARG A1236     7883   9429   9468    349   -158   -308       N  
ATOM   1764  CA  ARG A1236      11.675  38.198  12.392  1.00 65.32           C  
ANISOU 1764  CA  ARG A1236     7277   8681   8860    291   -138   -361       C  
ATOM   1765  C   ARG A1236      10.437  39.078  12.489  1.00 62.83           C  
ANISOU 1765  C   ARG A1236     7040   8264   8569    269   -102   -386       C  
ATOM   1766  O   ARG A1236      10.492  40.268  12.165  1.00 74.84           O  
ANISOU 1766  O   ARG A1236     8607   9748  10082    199    -78   -455       O  
ATOM   1767  CB  ARG A1236      11.682  37.430  11.069  1.00 66.75           C  
ANISOU 1767  CB  ARG A1236     7459   8785   9116    337   -146   -320       C  
ATOM   1768  CG  ARG A1236      12.974  36.689  10.780  1.00 66.24           C  
ANISOU 1768  CG  ARG A1236     7325   8812   9031    359   -173   -299       C  
ATOM   1769  CD  ARG A1236      13.090  36.327   9.304  1.00 61.48           C  
ANISOU 1769  CD  ARG A1236     6744   8123   8494    383   -172   -283       C  
ATOM   1770  NE  ARG A1236      12.000  35.488   8.816  1.00 63.16           N  
ANISOU 1770  NE  ARG A1236     6997   8225   8778    451   -175   -226       N  
ATOM   1771  CZ  ARG A1236      12.019  34.158   8.840  1.00 64.69           C  
ANISOU 1771  CZ  ARG A1236     7164   8426   8988    528   -194   -155       C  
ATOM   1772  NH1 ARG A1236      13.071  33.517   9.334  1.00 60.58           N  
ANISOU 1772  NH1 ARG A1236     6579   8024   8416    557   -210   -128       N  
ATOM   1773  NH2 ARG A1236      10.989  33.467   8.369  1.00 61.70           N  
ANISOU 1773  NH2 ARG A1236     6825   7939   8679    577   -197   -112       N  
ATOM   1774  N   LYS A1237       9.306  38.513  12.924  1.00 57.37           N  
ANISOU 1774  N   LYS A1237     6366   7524   7909    328    -93   -331       N  
ATOM   1775  CA  LYS A1237       8.108  39.336  13.055  1.00 63.60           C  
ANISOU 1775  CA  LYS A1237     7222   8223   8719    315    -56   -350       C  
ATOM   1776  C   LYS A1237       8.269  40.373  14.156  1.00 67.60           C  
ANISOU 1776  C   LYS A1237     7752   8791   9142    261    -36   -408       C  
ATOM   1777  O   LYS A1237       7.870  41.533  13.984  1.00 59.72           O  
ANISOU 1777  O   LYS A1237     6818   7732   8141    212     -2   -463       O  
ATOM   1778  CB  LYS A1237       6.891  38.457  13.350  1.00 61.73           C  
ANISOU 1778  CB  LYS A1237     6986   7931   8537    389    -48   -274       C  
ATOM   1779  CG  LYS A1237       5.555  39.189  13.269  1.00 50.11           C  
ANISOU 1779  CG  LYS A1237     5576   6358   7108    388    -10   -283       C  
ATOM   1780  CD  LYS A1237       4.386  38.245  13.496  1.00 51.39           C  
ANISOU 1780  CD  LYS A1237     5723   6467   7334    456     -2   -205       C  
ATOM   1781  CE  LYS A1237       4.147  38.001  14.989  1.00 61.56           C  
ANISOU 1781  CE  LYS A1237     6996   7826   8568    483     20   -172       C  
ATOM   1782  NZ  LYS A1237       3.004  37.074  15.270  1.00 61.21           N  
ANISOU 1782  NZ  LYS A1237     6935   7730   8591    546     37    -92       N  
ATOM   1783  N   LYS A1238       8.875  39.989  15.284  1.00 66.53           N  
ANISOU 1783  N   LYS A1238     7570   8775   8931    270    -55   -398       N  
ATOM   1784  CA  LYS A1238       9.045  40.965  16.355  1.00 61.43           C  
ANISOU 1784  CA  LYS A1238     6952   8191   8199    219    -42   -459       C  
ATOM   1785  C   LYS A1238      10.026  42.063  15.952  1.00 59.60           C  
ANISOU 1785  C   LYS A1238     6730   7984   7932    119    -44   -552       C  
ATOM   1786  O   LYS A1238       9.803  43.242  16.248  1.00 59.49           O  
ANISOU 1786  O   LYS A1238     6780   7941   7884     59    -14   -617       O  
ATOM   1787  CB  LYS A1238       9.465  40.279  17.656  1.00 65.14           C  
ANISOU 1787  CB  LYS A1238     7373   8788   8589    259    -66   -428       C  
ATOM   1788  CG  LYS A1238       9.769  41.247  18.796  1.00 76.69           C  
ANISOU 1788  CG  LYS A1238     8863  10327   9949    205    -63   -497       C  
ATOM   1789  CD  LYS A1238      10.380  40.532  19.994  1.00 89.23           C  
ANISOU 1789  CD  LYS A1238    10396  12057  11449    250    -98   -470       C  
ATOM   1790  CE  LYS A1238      10.885  41.510  21.042  1.00 93.52           C  
ANISOU 1790  CE  LYS A1238    10962  12690  11882    187   -108   -553       C  
ATOM   1791  NZ  LYS A1238      11.610  40.789  22.125  1.00 94.44           N  
ANISOU 1791  NZ  LYS A1238    11018  12958  11906    234   -153   -529       N  
ATOM   1792  N   SER A1239      11.124  41.701  15.283  1.00 65.93           N  
ANISOU 1792  N   SER A1239     7472   8837   8742    100    -76   -557       N  
ATOM   1793  CA  SER A1239      12.053  42.726  14.815  1.00 70.84           C  
ANISOU 1793  CA  SER A1239     8098   9475   9343      1    -71   -642       C  
ATOM   1794  C   SER A1239      11.420  43.631  13.764  1.00 72.04           C  
ANISOU 1794  C   SER A1239     8335   9484   9555    -33    -24   -674       C  
ATOM   1795  O   SER A1239      11.663  44.848  13.752  1.00 75.55           O  
ANISOU 1795  O   SER A1239     8828   9907   9971   -119      5   -752       O  
ATOM   1796  CB  SER A1239      13.302  42.043  14.249  1.00 71.81           C  
ANISOU 1796  CB  SER A1239     8133   9680   9473      1   -109   -628       C  
ATOM   1797  OG  SER A1239      14.280  42.968  13.826  1.00 80.25           O  
ANISOU 1797  OG  SER A1239     9192  10774  10525    -98   -102   -706       O  
ATOM   1798  N   LEU A1240      10.573  43.067  12.899  1.00 65.92           N  
ANISOU 1798  N   LEU A1240     7581   8605   8859     34    -15   -616       N  
ATOM   1799  CA  LEU A1240       9.955  43.875  11.853  1.00 67.31           C  
ANISOU 1799  CA  LEU A1240     7837   8649   9089     15     25   -641       C  
ATOM   1800  C   LEU A1240       8.950  44.857  12.434  1.00 69.77           C  
ANISOU 1800  C   LEU A1240     8231   8899   9380      0     69   -672       C  
ATOM   1801  O   LEU A1240       8.973  46.053  12.111  1.00 69.64           O  
ANISOU 1801  O   LEU A1240     8283   8824   9351    -62    110   -736       O  
ATOM   1802  CB  LEU A1240       9.281  42.988  10.806  1.00 65.00           C  
ANISOU 1802  CB  LEU A1240     7545   8270   8882     94     15   -574       C  
ATOM   1803  CG  LEU A1240       8.357  43.805   9.896  1.00 53.34           C  
ANISOU 1803  CG  LEU A1240     6156   6656   7454     95     54   -593       C  
ATOM   1804  CD1 LEU A1240       9.188  44.690   8.985  1.00 43.22           C  
ANISOU 1804  CD1 LEU A1240     4908   5346   6166     28     79   -654       C  
ATOM   1805  CD2 LEU A1240       7.398  42.926   9.100  1.00 51.35           C  
ANISOU 1805  CD2 LEU A1240     5907   6320   7283    179     37   -527       C  
ATOM   1806  N   LEU A1241       8.054  44.365  13.296  1.00 62.32           N  
ANISOU 1806  N   LEU A1241     7284   7961   8432     60     68   -624       N  
ATOM   1807  CA  LEU A1241       7.088  45.247  13.937  1.00 55.19           C  
ANISOU 1807  CA  LEU A1241     6458   7007   7505     56    114   -646       C  
ATOM   1808  C   LEU A1241       7.771  46.267  14.836  1.00 71.10           C  
ANISOU 1808  C   LEU A1241     8502   9086   9427    -27    128   -727       C  
ATOM   1809  O   LEU A1241       7.309  47.408  14.938  1.00 79.84           O  
ANISOU 1809  O   LEU A1241     9696  10128  10513    -63    176   -777       O  
ATOM   1810  CB  LEU A1241       6.101  44.402  14.736  1.00 51.14           C  
ANISOU 1810  CB  LEU A1241     5924   6502   7006    139    112   -572       C  
ATOM   1811  CG  LEU A1241       5.163  43.535  13.898  1.00 51.81           C  
ANISOU 1811  CG  LEU A1241     5992   6503   7189    214    105   -498       C  
ATOM   1812  CD1 LEU A1241       4.392  42.563  14.778  1.00 48.53           C  
ANISOU 1812  CD1 LEU A1241     5540   6113   6788    286    103   -422       C  
ATOM   1813  CD2 LEU A1241       4.220  44.412  13.090  1.00 46.55           C  
ANISOU 1813  CD2 LEU A1241     5401   5714   6571    216    145   -517       C  
ATOM   1814  N   SER A1242       8.866  45.882  15.496  1.00 76.28           N  
ANISOU 1814  N   SER A1242     9089   9870  10023    -57     86   -743       N  
ATOM   1815  CA  SER A1242       9.590  46.846  16.313  1.00 76.90           C  
ANISOU 1815  CA  SER A1242     9190  10016  10013   -145     90   -829       C  
ATOM   1816  C   SER A1242      10.205  47.946  15.459  1.00 77.82           C  
ANISOU 1816  C   SER A1242     9349  10079  10138   -242    117   -908       C  
ATOM   1817  O   SER A1242      10.268  49.100  15.893  1.00 85.51           O  
ANISOU 1817  O   SER A1242    10394  11036  11062   -315    151   -984       O  
ATOM   1818  CB  SER A1242      10.658  46.136  17.142  1.00 95.29           C  
ANISOU 1818  CB  SER A1242    11425  12503  12278   -150     30   -827       C  
ATOM   1819  OG  SER A1242      11.666  47.033  17.570  1.00114.53           O  
ANISOU 1819  OG  SER A1242    13862  15011  14643   -255     20   -922       O  
ATOM   1820  N   LYS A1243      10.652  47.613  14.240  1.00 83.00           N  
ANISOU 1820  N   LYS A1243     9972  10705  10860   -242    110   -890       N  
ATOM   1821  CA  LYS A1243      11.193  48.638  13.347  1.00 79.38           C  
ANISOU 1821  CA  LYS A1243     9560  10185  10417   -327    147   -957       C  
ATOM   1822  C   LYS A1243      10.125  49.624  12.892  1.00 73.08           C  
ANISOU 1822  C   LYS A1243     8883   9241   9643   -323    214   -975       C  
ATOM   1823  O   LYS A1243      10.447  50.764  12.546  1.00 79.34           O  
ANISOU 1823  O   LYS A1243     9744   9980  10423   -403    260  -1045       O  
ATOM   1824  CB  LYS A1243      11.916  47.994  12.166  1.00 83.08           C  
ANISOU 1824  CB  LYS A1243     9966  10657  10943   -317    127   -927       C  
ATOM   1825  CG  LYS A1243      13.418  47.909  12.416  1.00 93.07           C  
ANISOU 1825  CG  LYS A1243    11141  12053  12169   -391     92   -968       C  
ATOM   1826  CD  LYS A1243      14.047  46.599  11.984  1.00100.17           C  
ANISOU 1826  CD  LYS A1243    11935  13025  13099   -331     42   -902       C  
ATOM   1827  CE  LYS A1243      15.506  46.565  12.434  1.00109.45           C  
ANISOU 1827  CE  LYS A1243    13013  14349  14225   -401      6   -943       C  
ATOM   1828  NZ  LYS A1243      16.209  45.296  12.106  1.00111.73           N  
ANISOU 1828  NZ  LYS A1243    13196  14723  14533   -337    -40   -878       N  
ATOM   1829  N   PHE A1244       8.867  49.205  12.854  1.00 66.38           N  
ANISOU 1829  N   PHE A1244     8062   8326   8832   -229    223   -911       N  
ATOM   1830  CA  PHE A1244       7.768  50.089  12.491  1.00 71.18           C  
ANISOU 1830  CA  PHE A1244     8779   8804   9460   -208    284   -920       C  
ATOM   1831  C   PHE A1244       7.165  50.817  13.690  1.00 73.29           C  
ANISOU 1831  C   PHE A1244     9112   9071   9663   -218    318   -951       C  
ATOM   1832  O   PHE A1244       6.179  51.542  13.521  1.00 84.56           O  
ANISOU 1832  O   PHE A1244    10631  10398  11102   -191    372   -953       O  
ATOM   1833  CB  PHE A1244       6.690  49.344  11.695  1.00 78.60           C  
ANISOU 1833  CB  PHE A1244     9714   9668  10483   -104    277   -839       C  
ATOM   1834  CG  PHE A1244       7.143  48.917  10.322  1.00 80.69           C  
ANISOU 1834  CG  PHE A1244     9953   9898  10809    -93    259   -821       C  
ATOM   1835  CD1 PHE A1244       7.975  49.741   9.578  1.00 87.48           C  
ANISOU 1835  CD1 PHE A1244    10852  10727  11661   -166    289   -880       C  
ATOM   1836  CD2 PHE A1244       6.701  47.734   9.752  1.00 79.47           C  
ANISOU 1836  CD2 PHE A1244     9744   9732  10718    -10    217   -746       C  
ATOM   1837  CE1 PHE A1244       8.384  49.378   8.304  1.00 90.06           C  
ANISOU 1837  CE1 PHE A1244    11162  11017  12038   -150    279   -861       C  
ATOM   1838  CE2 PHE A1244       7.106  47.365   8.474  1.00 76.02           C  
ANISOU 1838  CE2 PHE A1244     9295   9258  10331      4    202   -732       C  
ATOM   1839  CZ  PHE A1244       7.949  48.185   7.752  1.00 80.76           C  
ANISOU 1839  CZ  PHE A1244     9935   9833  10919    -62    234   -787       C  
ATOM   1840  N   GLY A1245       7.709  50.627  14.894  1.00 60.90           N  
ANISOU 1840  N   GLY A1245     7501   7615   8023   -249    287   -972       N  
ATOM   1841  CA  GLY A1245       7.141  51.228  16.086  1.00 49.40           C  
ANISOU 1841  CA  GLY A1245     6110   6164   6497   -249    317   -998       C  
ATOM   1842  C   GLY A1245       5.974  50.495  16.699  1.00 62.07           C  
ANISOU 1842  C   GLY A1245     7702   7765   8116   -142    318   -917       C  
ATOM   1843  O   GLY A1245       5.291  51.059  17.562  1.00 69.97           O  
ANISOU 1843  O   GLY A1245     8771   8746   9068   -127    358   -930       O  
ATOM   1844  N   MET A1246       5.722  49.261  16.286  1.00 65.74           N  
ANISOU 1844  N   MET A1246     8085   8245   8647    -69    280   -834       N  
ATOM   1845  CA  MET A1246       4.651  48.438  16.818  1.00 66.73           C  
ANISOU 1845  CA  MET A1246     8188   8369   8799     29    281   -751       C  
ATOM   1846  C   MET A1246       5.217  47.324  17.690  1.00 70.62           C  
ANISOU 1846  C   MET A1246     8590   8986   9256     54    229   -712       C  
ATOM   1847  O   MET A1246       6.383  46.941  17.569  1.00 73.21           O  
ANISOU 1847  O   MET A1246     8855   9397   9564     13    180   -732       O  
ATOM   1848  CB  MET A1246       3.849  47.843  15.665  1.00 65.96           C  
ANISOU 1848  CB  MET A1246     8069   8183   8809     95    280   -685       C  
ATOM   1849  CG  MET A1246       3.297  48.910  14.755  1.00 68.41           C  
ANISOU 1849  CG  MET A1246     8468   8375   9150     83    329   -719       C  
ATOM   1850  SD  MET A1246       2.518  48.257  13.284  1.00 69.29           S  
ANISOU 1850  SD  MET A1246     8554   8393   9379    153    314   -655       S  
ATOM   1851  CE  MET A1246       2.207  49.795  12.430  1.00 80.74           C  
ANISOU 1851  CE  MET A1246    10125   9725  10826    125    377   -717       C  
ATOM   1852  N   ASP A1247       4.371  46.790  18.563  1.00 79.45           N  
ANISOU 1852  N   ASP A1247     9703  10119  10367    127    242   -652       N  
ATOM   1853  CA  ASP A1247       4.724  45.607  19.326  1.00 89.28           C  
ANISOU 1853  CA  ASP A1247    10868  11467  11587    173    201   -597       C  
ATOM   1854  C   ASP A1247       4.022  44.417  18.690  1.00 87.70           C  
ANISOU 1854  C   ASP A1247    10612  11221  11490    251    191   -502       C  
ATOM   1855  O   ASP A1247       3.277  44.549  17.717  1.00 84.56           O  
ANISOU 1855  O   ASP A1247    10234  10720  11175    267    210   -485       O  
ATOM   1856  CB  ASP A1247       4.349  45.718  20.808  1.00 97.44           C  
ANISOU 1856  CB  ASP A1247    11932  12554  12536    204    224   -590       C  
ATOM   1857  CG  ASP A1247       2.897  46.092  21.027  1.00114.85           C  
ANISOU 1857  CG  ASP A1247    14201  14665  14772    259    292   -554       C  
ATOM   1858  OD1 ASP A1247       2.290  46.715  20.134  1.00119.93           O  
ANISOU 1858  OD1 ASP A1247    14888  15203  15476    250    324   -567       O  
ATOM   1859  OD2 ASP A1247       2.349  45.718  22.088  1.00121.42           O  
ANISOU 1859  OD2 ASP A1247    15036  15529  15568    319    315   -508       O  
ATOM   1860  N   GLU A1248       4.276  43.240  19.243  1.00 86.05           N  
ANISOU 1860  N   GLU A1248    10335  11089  11272    301    160   -441       N  
ATOM   1861  CA  GLU A1248       3.932  42.002  18.564  1.00 80.52           C  
ANISOU 1861  CA  GLU A1248     9574  10355  10665    360    140   -360       C  
ATOM   1862  C   GLU A1248       2.421  41.898  18.361  1.00 60.63           C  
ANISOU 1862  C   GLU A1248     7078   7731   8228    414    184   -305       C  
ATOM   1863  O   GLU A1248       1.627  42.349  19.191  1.00 54.82           O  
ANISOU 1863  O   GLU A1248     6384   6981   7465    437    231   -297       O  
ATOM   1864  CB  GLU A1248       4.449  40.835  19.400  1.00 87.25           C  
ANISOU 1864  CB  GLU A1248    10362  11310  11477    408    111   -304       C  
ATOM   1865  CG  GLU A1248       5.964  40.837  19.530  1.00 93.83           C  
ANISOU 1865  CG  GLU A1248    11157  12259  12236    362     60   -352       C  
ATOM   1866  CD  GLU A1248       6.511  39.543  20.078  1.00114.94           C  
ANISOU 1866  CD  GLU A1248    13761  15027  14884    424     27   -287       C  
ATOM   1867  OE1 GLU A1248       7.128  38.778  19.308  1.00121.14           O  
ANISOU 1867  OE1 GLU A1248    14494  15824  15711    434     -8   -263       O  
ATOM   1868  OE2 GLU A1248       6.332  39.302  21.291  1.00128.37           O  
ANISOU 1868  OE2 GLU A1248    15467  16790  16519    466     40   -260       O  
ATOM   1869  N   GLY A1249       2.032  41.312  17.236  1.00 50.52           N  
ANISOU 1869  N   GLY A1249     5770   6377   7048    436    167   -269       N  
ATOM   1870  CA  GLY A1249       0.636  41.049  16.943  1.00 47.62           C  
ANISOU 1870  CA  GLY A1249     5405   5918   6771    486    196   -213       C  
ATOM   1871  C   GLY A1249       0.539  40.273  15.650  1.00 58.16           C  
ANISOU 1871  C   GLY A1249     6702   7193   8205    500    157   -185       C  
ATOM   1872  O   GLY A1249       1.533  40.061  14.948  1.00 59.94           O  
ANISOU 1872  O   GLY A1249     6910   7439   8424    472    115   -210       O  
ATOM   1873  N   VAL A1250      -0.684  39.860  15.330  1.00 59.42           N  
ANISOU 1873  N   VAL A1250     6847   7275   8454    544    172   -132       N  
ATOM   1874  CA  VAL A1250      -0.920  39.157  14.076  1.00 54.13           C  
ANISOU 1874  CA  VAL A1250     6148   6538   7880    558    132   -110       C  
ATOM   1875  C   VAL A1250      -0.786  40.147  12.931  1.00 56.87           C  
ANISOU 1875  C   VAL A1250     6546   6828   8235    524    122   -174       C  
ATOM   1876  O   VAL A1250      -1.558  41.105  12.831  1.00 58.78           O  
ANISOU 1876  O   VAL A1250     6832   7018   8482    525    156   -197       O  
ATOM   1877  CB  VAL A1250      -2.297  38.487  14.091  1.00 55.69           C  
ANISOU 1877  CB  VAL A1250     6312   6673   8173    607    148    -41       C  
ATOM   1878  CG1 VAL A1250      -2.456  37.545  12.915  1.00 56.87           C  
ANISOU 1878  CG1 VAL A1250     6427   6764   8417    620     97    -16       C  
ATOM   1879  CG2 VAL A1250      -2.445  37.723  15.379  1.00 74.53           C  
ANISOU 1879  CG2 VAL A1250     8665   9115  10539    640    177     20       C  
ATOM   1880  N   THR A1251       0.163  39.887  12.035  1.00 58.59           N  
ANISOU 1880  N   THR A1251     6757   7051   8454    502     79   -198       N  
ATOM   1881  CA  THR A1251       0.626  40.863  11.055  1.00 48.59           C  
ANISOU 1881  CA  THR A1251     5543   5747   7172    463     76   -264       C  
ATOM   1882  C   THR A1251       0.108  40.545   9.655  1.00 49.41           C  
ANISOU 1882  C   THR A1251     5651   5762   7361    491     44   -254       C  
ATOM   1883  O   THR A1251       0.357  39.458   9.117  1.00 51.11           O  
ANISOU 1883  O   THR A1251     5827   5973   7620    512      1   -220       O  
ATOM   1884  CB  THR A1251       2.148  40.927  11.070  1.00 59.88           C  
ANISOU 1884  CB  THR A1251     6965   7253   8533    416     57   -304       C  
ATOM   1885  OG1 THR A1251       2.579  41.253  12.396  1.00 70.01           O  
ANISOU 1885  OG1 THR A1251     8244   8623   9733    391     79   -320       O  
ATOM   1886  CG2 THR A1251       2.643  41.988  10.109  1.00 67.07           C  
ANISOU 1886  CG2 THR A1251     7934   8123   9429    370     65   -372       C  
ATOM   1887  N   PHE A1252      -0.620  41.497   9.083  1.00 54.83           N  
ANISOU 1887  N   PHE A1252     6392   6377   8065    495     66   -282       N  
ATOM   1888  CA  PHE A1252      -1.133  41.452   7.722  1.00 44.30           C  
ANISOU 1888  CA  PHE A1252     5077   4959   6798    523     37   -284       C  
ATOM   1889  C   PHE A1252      -0.360  42.409   6.832  1.00 40.72           C  
ANISOU 1889  C   PHE A1252     4690   4479   6304    490     46   -346       C  
ATOM   1890  O   PHE A1252       0.064  43.478   7.276  1.00 53.42           O  
ANISOU 1890  O   PHE A1252     6346   6106   7845    448     91   -393       O  
ATOM   1891  CB  PHE A1252      -2.613  41.824   7.682  1.00 43.09           C  
ANISOU 1891  CB  PHE A1252     4933   4744   6697    564     57   -265       C  
ATOM   1892  CG  PHE A1252      -3.448  41.007   8.597  1.00 46.93           C  
ANISOU 1892  CG  PHE A1252     5356   5251   7227    592     62   -202       C  
ATOM   1893  CD1 PHE A1252      -3.624  41.381   9.918  1.00 45.92           C  
ANISOU 1893  CD1 PHE A1252     5228   5170   7051    586    114   -193       C  
ATOM   1894  CD2 PHE A1252      -4.055  39.854   8.139  1.00 54.60           C  
ANISOU 1894  CD2 PHE A1252     6270   6190   8287    624     18   -154       C  
ATOM   1895  CE1 PHE A1252      -4.385  40.611  10.774  1.00 49.93           C  
ANISOU 1895  CE1 PHE A1252     5678   5695   7598    616    128   -130       C  
ATOM   1896  CE2 PHE A1252      -4.822  39.084   8.982  1.00 56.26           C  
ANISOU 1896  CE2 PHE A1252     6420   6414   8543    646     31    -94       C  
ATOM   1897  CZ  PHE A1252      -4.989  39.460  10.305  1.00 51.49           C  
ANISOU 1897  CZ  PHE A1252     5815   5858   7891    644     89    -79       C  
ATOM   1898  N   MET A1253      -0.167  42.019   5.583  1.00 45.31           N  
ANISOU 1898  N   MET A1253     5279   5014   6923    509      6   -348       N  
ATOM   1899  CA  MET A1253       0.558  42.839   4.627  1.00 41.39           C  
ANISOU 1899  CA  MET A1253     4847   4485   6393    485     18   -400       C  
ATOM   1900  C   MET A1253      -0.239  42.908   3.337  1.00 44.83           C  
ANISOU 1900  C   MET A1253     5321   4829   6882    537     -6   -398       C  
ATOM   1901  O   MET A1253      -0.775  41.901   2.880  1.00 42.53           O  
ANISOU 1901  O   MET A1253     4990   4514   6654    579    -58   -360       O  
ATOM   1902  CB  MET A1253       1.969  42.309   4.344  1.00 37.12           C  
ANISOU 1902  CB  MET A1253     4283   3996   5825    454     -3   -409       C  
ATOM   1903  CG  MET A1253       2.677  43.055   3.218  1.00 50.75           C  
ANISOU 1903  CG  MET A1253     6074   5680   7529    436     12   -456       C  
ATOM   1904  SD  MET A1253       4.272  42.365   2.765  1.00 69.87           S  
ANISOU 1904  SD  MET A1253     8460   8159   9928    410    -10   -458       S  
ATOM   1905  CE  MET A1253       3.974  40.657   3.124  1.00 67.58           C  
ANISOU 1905  CE  MET A1253     8087   7902   9687    460    -70   -389       C  
ATOM   1906  N   PHE A1254      -0.255  44.084   2.725  1.00 57.02           N  
ANISOU 1906  N   PHE A1254     6946   6322   8398    533     31   -441       N  
ATOM   1907  CA  PHE A1254      -0.757  44.272   1.376  1.00 62.45           C  
ANISOU 1907  CA  PHE A1254     7684   6928   9118    584     10   -448       C  
ATOM   1908  C   PHE A1254       0.394  44.851   0.586  1.00 63.13           C  
ANISOU 1908  C   PHE A1254     7832   6998   9156    554     34   -490       C  
ATOM   1909  O   PHE A1254       1.145  45.683   1.095  1.00 70.73           O  
ANISOU 1909  O   PHE A1254     8825   7988  10062    495     89   -527       O  
ATOM   1910  CB  PHE A1254      -1.956  45.227   1.341  1.00 59.18           C  
ANISOU 1910  CB  PHE A1254     7317   6458   8709    623     42   -454       C  
ATOM   1911  CG  PHE A1254      -2.340  45.674  -0.044  1.00 56.35           C  
ANISOU 1911  CG  PHE A1254     7029   6020   8363    677     30   -469       C  
ATOM   1912  CD1 PHE A1254      -3.219  44.934  -0.819  1.00 61.85           C  
ANISOU 1912  CD1 PHE A1254     7696   6680   9124    740    -37   -441       C  
ATOM   1913  CD2 PHE A1254      -1.809  46.842  -0.575  1.00 48.21           C  
ANISOU 1913  CD2 PHE A1254     6093   4948   7276    663     86   -513       C  
ATOM   1914  CE1 PHE A1254      -3.562  45.353  -2.102  1.00 57.71           C  
ANISOU 1914  CE1 PHE A1254     7239   6087   8600    797    -53   -458       C  
ATOM   1915  CE2 PHE A1254      -2.143  47.264  -1.852  1.00 44.26           C  
ANISOU 1915  CE2 PHE A1254     5665   4374   6778    722     79   -525       C  
ATOM   1916  CZ  PHE A1254      -3.022  46.522  -2.617  1.00 48.26           C  
ANISOU 1916  CZ  PHE A1254     6143   4851   7342    793      7   -497       C  
ATOM   1917  N   ILE A1255       0.575  44.369  -0.634  1.00 49.58           N  
ANISOU 1917  N   ILE A1255     6134   5239   7464    592     -6   -486       N  
ATOM   1918  CA  ILE A1255       1.550  44.961  -1.533  1.00 41.12           C  
ANISOU 1918  CA  ILE A1255     5131   4141   6354    575     25   -521       C  
ATOM   1919  C   ILE A1255       0.963  44.997  -2.938  1.00 55.41           C  
ANISOU 1919  C   ILE A1255     7002   5865   8188    649     -3   -520       C  
ATOM   1920  O   ILE A1255       0.497  43.973  -3.447  1.00 73.27           O  
ANISOU 1920  O   ILE A1255     9230   8112  10498    699    -72   -491       O  
ATOM   1921  CB  ILE A1255       2.879  44.185  -1.438  1.00 30.77           C  
ANISOU 1921  CB  ILE A1255     3769   2895   5029    535     10   -516       C  
ATOM   1922  CG1 ILE A1255       3.895  44.641  -2.465  1.00 32.81           C  
ANISOU 1922  CG1 ILE A1255     4086   3124   5255    524     40   -545       C  
ATOM   1923  CG2 ILE A1255       2.634  42.686  -1.551  1.00 31.85           C  
ANISOU 1923  CG2 ILE A1255     3837   3048   5218    577    -64   -469       C  
ATOM   1924  CD1 ILE A1255       5.273  44.076  -2.174  1.00 29.51           C  
ANISOU 1924  CD1 ILE A1255     3609   2786   4816    475     40   -542       C  
ATOM   1925  N   GLY A1256       0.969  46.169  -3.554  1.00 62.19           N  
ANISOU 1925  N   GLY A1256     7954   6665   9010    659     50   -553       N  
ATOM   1926  CA  GLY A1256       0.436  46.317  -4.895  1.00 61.93           C  
ANISOU 1926  CA  GLY A1256     7991   6552   8987    737     28   -554       C  
ATOM   1927  C   GLY A1256       0.106  47.762  -5.194  1.00 60.99           C  
ANISOU 1927  C   GLY A1256     7974   6371   8827    753     99   -583       C  
ATOM   1928  O   GLY A1256       0.159  48.635  -4.325  1.00 60.82           O  
ANISOU 1928  O   GLY A1256     7971   6364   8776    703    164   -603       O  
ATOM   1929  N   ARG A1257      -0.247  48.013  -6.457  1.00 49.59           N  
ANISOU 1929  N   ARG A1257     6607   4856   7379    828     88   -586       N  
ATOM   1930  CA  ARG A1257      -0.557  49.376  -6.860  1.00 49.43           C  
ANISOU 1930  CA  ARG A1257     6697   4769   7316    857    160   -610       C  
ATOM   1931  C   ARG A1257      -1.802  49.837  -6.119  1.00 53.69           C  
ANISOU 1931  C   ARG A1257     7222   5308   7868    883    166   -600       C  
ATOM   1932  O   ARG A1257      -2.718  49.049  -5.862  1.00 49.89           O  
ANISOU 1932  O   ARG A1257     6663   4854   7439    918     96   -570       O  
ATOM   1933  CB  ARG A1257      -0.796  49.483  -8.377  1.00 69.87           C  
ANISOU 1933  CB  ARG A1257     9371   7284   9894    949    139   -609       C  
ATOM   1934  CG  ARG A1257      -0.970  50.942  -8.822  1.00 93.42           C  
ANISOU 1934  CG  ARG A1257    12482  10192  12823    981    228   -632       C  
ATOM   1935  CD  ARG A1257      -1.284  51.241 -10.293  1.00107.51           C  
ANISOU 1935  CD  ARG A1257    14368  11898  14582   1086    220   -631       C  
ATOM   1936  NE  ARG A1257      -2.469  50.570 -10.820  1.00123.64           N  
ANISOU 1936  NE  ARG A1257    16378  13938  16662   1182    120   -608       N  
ATOM   1937  CZ  ARG A1257      -2.753  50.463 -12.116  1.00136.33           C  
ANISOU 1937  CZ  ARG A1257    18027  15527  18246   1246     93   -590       C  
ATOM   1938  NH1 ARG A1257      -1.935  50.983 -13.023  1.00141.71           N  
ANISOU 1938  NH1 ARG A1257    18783  16181  18881   1237    151   -596       N  
ATOM   1939  NH2 ARG A1257      -3.862  49.852 -12.507  1.00140.07           N  
ANISOU 1939  NH2 ARG A1257    18446  16036  18740   1295     13   -558       N  
ATOM   1940  N   PHE A1258      -1.816  51.113  -5.741  1.00 63.54           N  
ANISOU 1940  N   PHE A1258     8547   6526   9071    863    256   -624       N  
ATOM   1941  CA  PHE A1258      -2.991  51.741  -5.146  1.00 60.44           C  
ANISOU 1941  CA  PHE A1258     8164   6121   8679    902    279   -615       C  
ATOM   1942  C   PHE A1258      -3.884  52.240  -6.273  1.00 68.92           C  
ANISOU 1942  C   PHE A1258     9317   7124   9746   1014    272   -608       C  
ATOM   1943  O   PHE A1258      -3.530  53.193  -6.974  1.00 70.51           O  
ANISOU 1943  O   PHE A1258     9634   7259   9896   1035    339   -630       O  
ATOM   1944  CB  PHE A1258      -2.601  52.881  -4.206  1.00 46.13           C  
ANISOU 1944  CB  PHE A1258     6408   4305   6815    833    381   -646       C  
ATOM   1945  CG  PHE A1258      -1.896  52.433  -2.948  1.00 46.23           C  
ANISOU 1945  CG  PHE A1258     6338   4399   6830    731    381   -654       C  
ATOM   1946  CD1 PHE A1258      -1.550  51.103  -2.744  1.00 51.39           C  
ANISOU 1946  CD1 PHE A1258     6880   5121   7526    708    303   -630       C  
ATOM   1947  CD2 PHE A1258      -1.589  53.353  -1.961  1.00 48.95           C  
ANISOU 1947  CD2 PHE A1258     6721   4749   7127    663    460   -686       C  
ATOM   1948  CE1 PHE A1258      -0.905  50.703  -1.583  1.00 47.81           C  
ANISOU 1948  CE1 PHE A1258     6354   4746   7067    625    303   -635       C  
ATOM   1949  CE2 PHE A1258      -0.942  52.962  -0.799  1.00 51.07           C  
ANISOU 1949  CE2 PHE A1258     6916   5098   7389    575    455   -695       C  
ATOM   1950  CZ  PHE A1258      -0.599  51.638  -0.609  1.00 47.48           C  
ANISOU 1950  CZ  PHE A1258     6349   4716   6975    559    377   -668       C  
ATOM   1951  N   ASP A1259      -5.032  51.593  -6.454  1.00 70.70           N  
ANISOU 1951  N   ASP A1259     9478   7363  10022   1088    193   -576       N  
ATOM   1952  CA  ASP A1259      -5.932  51.948  -7.541  1.00 76.36           C  
ANISOU 1952  CA  ASP A1259    10255   8025  10734   1202    168   -569       C  
ATOM   1953  C   ASP A1259      -7.341  51.486  -7.197  1.00 78.47           C  
ANISOU 1953  C   ASP A1259    10430   8325  11059   1259    103   -536       C  
ATOM   1954  O   ASP A1259      -7.561  50.764  -6.221  1.00 78.20           O  
ANISOU 1954  O   ASP A1259    10289   8351  11074   1210     74   -517       O  
ATOM   1955  CB  ASP A1259      -5.439  51.369  -8.875  1.00 86.19           C  
ANISOU 1955  CB  ASP A1259    11531   9241  11976   1240    111   -574       C  
ATOM   1956  CG  ASP A1259      -5.249  49.860  -8.838  1.00 91.47           C  
ANISOU 1956  CG  ASP A1259    12087   9961  12705   1209     12   -559       C  
ATOM   1957  OD1 ASP A1259      -5.967  49.162  -8.095  1.00101.16           O  
ANISOU 1957  OD1 ASP A1259    13208  11238  13990   1197    -40   -536       O  
ATOM   1958  OD2 ASP A1259      -4.366  49.372  -9.572  1.00 93.10           O  
ANISOU 1958  OD2 ASP A1259    12318  10156  12900   1199     -9   -568       O  
ATOM   1959  N   ARG A1260      -8.289  51.896  -8.032  1.00 82.19           N  
ANISOU 1959  N   ARG A1260    10945   8758  11525   1367     81   -528       N  
ATOM   1960  CA  ARG A1260      -9.700  51.586  -7.855  1.00 82.29           C  
ANISOU 1960  CA  ARG A1260    10874   8801  11593   1434     21   -498       C  
ATOM   1961  C   ARG A1260     -10.156  50.582  -8.902  1.00 80.69           C  
ANISOU 1961  C   ARG A1260    10618   8614  11425   1479    -94   -484       C  
ATOM   1962  O   ARG A1260      -9.838  50.725 -10.087  1.00 81.48           O  
ANISOU 1962  O   ARG A1260    10791   8702  11466   1497    -94   -483       O  
ATOM   1963  CB  ARG A1260     -10.547  52.859  -7.950  1.00 92.03           C  
ANISOU 1963  CB  ARG A1260    12186   9997  12783   1522     86   -493       C  
ATOM   1964  CG  ARG A1260     -10.117  53.993  -7.022  1.00 97.94           C  
ANISOU 1964  CG  ARG A1260    13012  10725  13476   1473    215   -505       C  
ATOM   1965  CD  ARG A1260     -11.082  55.171  -7.119  1.00103.30           C  
ANISOU 1965  CD  ARG A1260    13764  11369  14116   1570    276   -493       C  
ATOM   1966  NE  ARG A1260     -10.908  56.144  -6.041  1.00112.91           N  
ANISOU 1966  NE  ARG A1260    15042  12569  15291   1530    393   -502       N  
ATOM   1967  CZ  ARG A1260     -11.447  56.027  -4.829  1.00116.93           C  
ANISOU 1967  CZ  ARG A1260    15472  13126  15829   1501    409   -482       C  
ATOM   1968  NH1 ARG A1260     -12.194  54.972  -4.529  1.00114.99           N  
ANISOU 1968  NH1 ARG A1260    15082  12945  15662   1510    322   -449       N  
ATOM   1969  NH2 ARG A1260     -11.236  56.962  -3.911  1.00118.97           N  
ANISOU 1969  NH2 ARG A1260    15800  13365  16038   1464    516   -496       N  
ATOM   1970  N   GLY A1261     -10.878  49.559  -8.450  1.00 92.87           N  
ANISOU 1970  N   GLY A1261    12029  10202  13054   1472   -178   -465       N  
ATOM   1971  CA  GLY A1261     -11.457  48.542  -9.305  1.00 98.20           C  
ANISOU 1971  CA  GLY A1261    12642  10913  13756   1489   -284   -447       C  
ATOM   1972  C   GLY A1261     -10.510  47.486  -9.825  1.00104.10           C  
ANISOU 1972  C   GLY A1261    13384  11664  14506   1434   -338   -458       C  
ATOM   1973  O   GLY A1261     -10.900  46.715 -10.708  1.00118.37           O  
ANISOU 1973  O   GLY A1261    15165  13492  16320   1450   -423   -451       O  
ATOM   1974  N   GLN A1262      -9.281  47.428  -9.322  1.00 96.90           N  
ANISOU 1974  N   GLN A1262    12496  10734  13589   1372   -293   -478       N  
ATOM   1975  CA  GLN A1262      -8.286  46.481  -9.813  1.00 86.68           C  
ANISOU 1975  CA  GLN A1262    11201   9442  12289   1327   -333   -485       C  
ATOM   1976  C   GLN A1262      -7.608  45.724  -8.677  1.00 74.93           C  
ANISOU 1976  C   GLN A1262     9632   7978  10860   1246   -331   -484       C  
ATOM   1977  O   GLN A1262      -7.983  44.586  -8.384  1.00 61.93           O  
ANISOU 1977  O   GLN A1262     7887   6361   9282   1224   -401   -465       O  
ATOM   1978  CB  GLN A1262      -7.270  47.144 -10.742  1.00 91.34           C  
ANISOU 1978  CB  GLN A1262    11918   9998  12787   1332   -273   -502       C  
ATOM   1979  CG  GLN A1262      -7.929  47.730 -11.979  1.00 98.47           C  
ANISOU 1979  CG  GLN A1262    12894  10893  13628   1402   -273   -490       C  
ATOM   1980  CD  GLN A1262      -6.931  48.164 -13.031  1.00112.12           C  
ANISOU 1980  CD  GLN A1262    14730  12590  15279   1403   -220   -498       C  
ATOM   1981  OE1 GLN A1262      -6.511  49.320 -13.070  1.00126.99           O  
ANISOU 1981  OE1 GLN A1262    16697  14436  17116   1405   -123   -508       O  
ATOM   1982  NE2 GLN A1262      -6.536  47.225 -13.889  1.00103.80           N  
ANISOU 1982  NE2 GLN A1262    13673  11550  14217   1397   -279   -494       N  
ATOM   1983  N   LYS A1263      -6.605  46.331  -8.040  1.00 77.29           N  
ANISOU 1983  N   LYS A1263     9970   8287  11109   1184   -240   -493       N  
ATOM   1984  CA  LYS A1263      -5.837  45.621  -7.025  1.00 74.89           C  
ANISOU 1984  CA  LYS A1263     9594   8037  10823   1093   -228   -482       C  
ATOM   1985  C   LYS A1263      -6.488  45.650  -5.645  1.00 66.52           C  
ANISOU 1985  C   LYS A1263     8453   7025   9795   1058   -201   -458       C  
ATOM   1986  O   LYS A1263      -6.001  44.964  -4.738  1.00 64.41           O  
ANISOU 1986  O   LYS A1263     8118   6808   9547    993   -199   -442       O  
ATOM   1987  CB  LYS A1263      -4.431  46.221  -6.931  1.00 76.12           C  
ANISOU 1987  CB  LYS A1263     9819   8193  10912   1037   -149   -506       C  
ATOM   1988  CG  LYS A1263      -3.479  45.791  -8.041  1.00 74.58           C  
ANISOU 1988  CG  LYS A1263     9674   7970  10694   1048   -173   -520       C  
ATOM   1989  CD  LYS A1263      -3.691  44.352  -8.467  1.00 77.54           C  
ANISOU 1989  CD  LYS A1263     9983   8352  11125   1068   -274   -501       C  
ATOM   1990  CE  LYS A1263      -3.041  44.097  -9.812  1.00 80.12           C  
ANISOU 1990  CE  LYS A1263    10385   8633  11422   1111   -301   -516       C  
ATOM   1991  NZ  LYS A1263      -3.677  42.968 -10.540  1.00 86.70           N  
ANISOU 1991  NZ  LYS A1263    11188   9458  12297   1156   -405   -504       N  
ATOM   1992  N   GLY A1264      -7.578  46.396  -5.472  1.00 60.73           N  
ANISOU 1992  N   GLY A1264     7726   6281   9069   1107   -181   -451       N  
ATOM   1993  CA  GLY A1264      -8.401  46.252  -4.288  1.00 61.74           C  
ANISOU 1993  CA  GLY A1264     7766   6451   9239   1090   -168   -420       C  
ATOM   1994  C   GLY A1264      -7.931  46.916  -3.016  1.00 62.21           C  
ANISOU 1994  C   GLY A1264     7838   6543   9256   1029    -76   -422       C  
ATOM   1995  O   GLY A1264      -8.412  46.547  -1.941  1.00 64.18           O  
ANISOU 1995  O   GLY A1264     8009   6837   9542   1006    -68   -393       O  
ATOM   1996  N   VAL A1265      -6.996  47.867  -3.081  1.00 63.57           N  
ANISOU 1996  N   VAL A1265     8106   6694   9352   1000     -5   -457       N  
ATOM   1997  CA  VAL A1265      -6.568  48.507  -1.840  1.00 54.78           C  
ANISOU 1997  CA  VAL A1265     7005   5613   8195    938     77   -466       C  
ATOM   1998  C   VAL A1265      -7.723  49.273  -1.215  1.00 59.62           C  
ANISOU 1998  C   VAL A1265     7624   6220   8809    982    124   -451       C  
ATOM   1999  O   VAL A1265      -7.778  49.431   0.010  1.00 67.37           O  
ANISOU 1999  O   VAL A1265     8578   7240   9780    943    170   -442       O  
ATOM   2000  CB  VAL A1265      -5.341  49.414  -2.078  1.00 51.89           C  
ANISOU 2000  CB  VAL A1265     6742   5222   7752    890    145   -512       C  
ATOM   2001  CG1 VAL A1265      -5.752  50.749  -2.662  1.00 56.22           C  
ANISOU 2001  CG1 VAL A1265     7405   5700   8255    945    207   -533       C  
ATOM   2002  CG2 VAL A1265      -4.577  49.631  -0.777  1.00 49.21           C  
ANISOU 2002  CG2 VAL A1265     6387   4934   7374    800    200   -527       C  
ATOM   2003  N   ASP A1266      -8.667  49.751  -2.034  1.00 64.06           N  
ANISOU 2003  N   ASP A1266     8222   6736   9382   1069    112   -445       N  
ATOM   2004  CA  ASP A1266      -9.851  50.409  -1.488  1.00 70.98           C  
ANISOU 2004  CA  ASP A1266     9094   7612  10266   1124    153   -423       C  
ATOM   2005  C   ASP A1266     -10.703  49.453  -0.660  1.00 55.75           C  
ANISOU 2005  C   ASP A1266     7032   5738   8414   1122    112   -376       C  
ATOM   2006  O   ASP A1266     -11.213  49.829   0.403  1.00 62.54           O  
ANISOU 2006  O   ASP A1266     7872   6620   9269   1121    169   -357       O  
ATOM   2007  CB  ASP A1266     -10.687  51.009  -2.625  1.00 89.86           C  
ANISOU 2007  CB  ASP A1266    11539   9950  12654   1229    138   -423       C  
ATOM   2008  CG  ASP A1266     -10.839  50.064  -3.811  1.00103.52           C  
ANISOU 2008  CG  ASP A1266    13226  11672  14433   1266     30   -419       C  
ATOM   2009  OD1 ASP A1266     -10.043  49.109  -3.926  1.00113.38           O  
ANISOU 2009  OD1 ASP A1266    14437  12940  15702   1207    -19   -425       O  
ATOM   2010  OD2 ASP A1266     -11.754  50.280  -4.635  1.00 99.56           O  
ANISOU 2010  OD2 ASP A1266    12734  11148  13946   1357     -8   -411       O  
ATOM   2011  N   VAL A1267     -10.827  48.199  -1.102  1.00 49.26           N  
ANISOU 2011  N   VAL A1267     6121   4934   7662   1119     19   -358       N  
ATOM   2012  CA  VAL A1267     -11.574  47.215  -0.323  1.00 56.37           C  
ANISOU 2012  CA  VAL A1267     6894   5881   8642   1107    -15   -313       C  
ATOM   2013  C   VAL A1267     -10.867  46.930   0.991  1.00 53.13           C  
ANISOU 2013  C   VAL A1267     6458   5518   8211   1029     33   -304       C  
ATOM   2014  O   VAL A1267     -11.508  46.765   2.039  1.00 62.30           O  
ANISOU 2014  O   VAL A1267     7556   6715   9401   1027     63   -268       O  
ATOM   2015  CB  VAL A1267     -11.788  45.923  -1.134  1.00 60.79           C  
ANISOU 2015  CB  VAL A1267     7377   6441   9280   1113   -123   -301       C  
ATOM   2016  CG1 VAL A1267     -12.562  44.908  -0.310  1.00 67.50           C  
ANISOU 2016  CG1 VAL A1267     8098   7332  10217   1095   -149   -253       C  
ATOM   2017  CG2 VAL A1267     -12.514  46.213  -2.429  1.00 62.90           C  
ANISOU 2017  CG2 VAL A1267     7671   6667   9561   1195   -178   -314       C  
ATOM   2018  N   LEU A1268      -9.533  46.909   0.968  1.00 37.42           N  
ANISOU 2018  N   LEU A1268     4517   3533   6167    968     44   -336       N  
ATOM   2019  CA  LEU A1268      -8.802  46.655   2.199  1.00 37.65           C  
ANISOU 2019  CA  LEU A1268     4521   3615   6167    898     82   -332       C  
ATOM   2020  C   LEU A1268      -8.941  47.820   3.165  1.00 42.63           C  
ANISOU 2020  C   LEU A1268     5210   4252   6736    892    176   -343       C  
ATOM   2021  O   LEU A1268      -9.105  47.612   4.367  1.00 40.82           O  
ANISOU 2021  O   LEU A1268     4937   4068   6506    870    208   -318       O  
ATOM   2022  CB  LEU A1268      -7.330  46.385   1.903  1.00 42.41           C  
ANISOU 2022  CB  LEU A1268     5157   4230   6728    837     69   -364       C  
ATOM   2023  CG  LEU A1268      -6.470  46.293   3.167  1.00 49.69           C  
ANISOU 2023  CG  LEU A1268     6062   5214   7603    766    110   -368       C  
ATOM   2024  CD1 LEU A1268      -6.955  45.167   4.082  1.00 54.33           C  
ANISOU 2024  CD1 LEU A1268     6544   5851   8248    763     85   -314       C  
ATOM   2025  CD2 LEU A1268      -4.996  46.148   2.842  1.00 46.58           C  
ANISOU 2025  CD2 LEU A1268     5696   4836   7164    708    101   -402       C  
ATOM   2026  N   LEU A1269      -8.890  49.052   2.663  1.00 48.15           N  
ANISOU 2026  N   LEU A1269     6014   4901   7378    916    225   -379       N  
ATOM   2027  CA  LEU A1269      -9.034  50.196   3.555  1.00 53.88           C  
ANISOU 2027  CA  LEU A1269     6808   5623   8042    913    318   -393       C  
ATOM   2028  C   LEU A1269     -10.437  50.267   4.148  1.00 63.91           C  
ANISOU 2028  C   LEU A1269     8029   6901   9353    978    339   -346       C  
ATOM   2029  O   LEU A1269     -10.596  50.594   5.334  1.00 65.19           O  
ANISOU 2029  O   LEU A1269     8194   7090   9484    963    401   -336       O  
ATOM   2030  CB  LEU A1269      -8.668  51.486   2.825  1.00 54.23           C  
ANISOU 2030  CB  LEU A1269     6985   5601   8019    925    371   -441       C  
ATOM   2031  CG  LEU A1269      -7.194  51.520   2.397  1.00 57.55           C  
ANISOU 2031  CG  LEU A1269     7454   6017   8395    850    367   -488       C  
ATOM   2032  CD1 LEU A1269      -6.860  52.812   1.665  1.00 63.62           C  
ANISOU 2032  CD1 LEU A1269     8358   6713   9102    861    430   -533       C  
ATOM   2033  CD2 LEU A1269      -6.239  51.283   3.572  1.00 54.74           C  
ANISOU 2033  CD2 LEU A1269     7072   5726   8003    757    387   -505       C  
ATOM   2034  N   LYS A1270     -11.467  49.942   3.349  1.00 66.36           N  
ANISOU 2034  N   LYS A1270     8290   7192   9731   1051    289   -316       N  
ATOM   2035  CA  LYS A1270     -12.818  49.881   3.905  1.00 68.90           C  
ANISOU 2035  CA  LYS A1270     8543   7532  10106   1111    305   -265       C  
ATOM   2036  C   LYS A1270     -12.903  48.796   4.973  1.00 69.54           C  
ANISOU 2036  C   LYS A1270     8514   7671  10235   1068    292   -224       C  
ATOM   2037  O   LYS A1270     -13.529  48.990   6.027  1.00 73.92           O  
ANISOU 2037  O   LYS A1270     9044   8251  10790   1084    350   -191       O  
ATOM   2038  CB  LYS A1270     -13.834  49.580   2.802  1.00 74.75           C  
ANISOU 2038  CB  LYS A1270     9232   8252  10919   1187    236   -244       C  
ATOM   2039  CG  LYS A1270     -13.941  50.601   1.677  1.00 92.77           C  
ANISOU 2039  CG  LYS A1270    11617  10476  13156   1252    245   -275       C  
ATOM   2040  CD  LYS A1270     -14.497  49.928   0.413  1.00 96.15           C  
ANISOU 2040  CD  LYS A1270    11988  10892  13651   1304    142   -267       C  
ATOM   2041  CE  LYS A1270     -14.601  50.871  -0.780  1.00 80.39           C  
ANISOU 2041  CE  LYS A1270    10096   8841  11606   1379    144   -296       C  
ATOM   2042  NZ  LYS A1270     -14.917  50.115  -2.025  1.00 71.77           N  
ANISOU 2042  NZ  LYS A1270     8958   7742  10569   1418     33   -297       N  
ATOM   2043  N   ALA A1271     -12.244  47.655   4.727  1.00 47.86           N  
ANISOU 2043  N   ALA A1271     5711   4947   7526   1017    222   -223       N  
ATOM   2044  CA  ALA A1271     -12.229  46.575   5.708  1.00 35.88           C  
ANISOU 2044  CA  ALA A1271     4100   3482   6051    978    212   -181       C  
ATOM   2045  C   ALA A1271     -11.494  46.979   6.981  1.00 41.68           C  
ANISOU 2045  C   ALA A1271     4878   4254   6705    930    285   -193       C  
ATOM   2046  O   ALA A1271     -11.876  46.559   8.081  1.00 55.85           O  
ANISOU 2046  O   ALA A1271     6617   6088   8516    927    315   -151       O  
ATOM   2047  CB  ALA A1271     -11.598  45.325   5.103  1.00 39.14           C  
ANISOU 2047  CB  ALA A1271     4460   3903   6511    939    127   -181       C  
ATOM   2048  N   ILE A1272     -10.433  47.785   6.851  1.00 41.80           N  
ANISOU 2048  N   ILE A1272     4993   4257   6632    890    312   -250       N  
ATOM   2049  CA  ILE A1272      -9.688  48.250   8.017  1.00 45.73           C  
ANISOU 2049  CA  ILE A1272     5538   4792   7046    839    374   -272       C  
ATOM   2050  C   ILE A1272     -10.553  49.178   8.848  1.00 50.34           C  
ANISOU 2050  C   ILE A1272     6162   5367   7599    882    457   -259       C  
ATOM   2051  O   ILE A1272     -10.548  49.117  10.086  1.00 44.49           O  
ANISOU 2051  O   ILE A1272     5410   4668   6825    867    501   -243       O  
ATOM   2052  CB  ILE A1272      -8.379  48.938   7.580  1.00 52.15           C  
ANISOU 2052  CB  ILE A1272     6445   5590   7781    781    382   -341       C  
ATOM   2053  CG1 ILE A1272      -7.409  47.926   6.963  1.00 64.42           C  
ANISOU 2053  CG1 ILE A1272     7952   7166   9359    738    307   -347       C  
ATOM   2054  CG2 ILE A1272      -7.725  49.658   8.756  1.00 39.19           C  
ANISOU 2054  CG2 ILE A1272     4863   3980   6046    730    449   -375       C  
ATOM   2055  CD1 ILE A1272      -6.107  48.539   6.485  1.00 62.54           C  
ANISOU 2055  CD1 ILE A1272     7792   6918   9052    680    317   -410       C  
ATOM   2056  N   GLU A1273     -11.324  50.042   8.180  1.00 60.31           N  
ANISOU 2056  N   GLU A1273     7475   6574   8865    944    482   -265       N  
ATOM   2057  CA  GLU A1273     -12.239  50.899   8.920  1.00 57.03           C  
ANISOU 2057  CA  GLU A1273     7097   6149   8424    998    564   -246       C  
ATOM   2058  C   GLU A1273     -13.314  50.069   9.607  1.00 54.76           C  
ANISOU 2058  C   GLU A1273     6694   5900   8214   1039    562   -173       C  
ATOM   2059  O   GLU A1273     -13.722  50.387  10.732  1.00 45.71           O  
ANISOU 2059  O   GLU A1273     5558   4774   7038   1057    633   -150       O  
ATOM   2060  CB  GLU A1273     -12.840  51.961   8.002  1.00 53.94           C  
ANISOU 2060  CB  GLU A1273     6782   5691   8021   1067    591   -262       C  
ATOM   2061  CG  GLU A1273     -11.777  52.899   7.453  1.00 67.82           C  
ANISOU 2061  CG  GLU A1273     8668   7403   9696   1024    614   -334       C  
ATOM   2062  CD  GLU A1273     -12.343  54.171   6.870  1.00 88.84           C  
ANISOU 2062  CD  GLU A1273    11437   9996  12321   1095    673   -349       C  
ATOM   2063  OE1 GLU A1273     -13.492  54.149   6.377  1.00101.55           O  
ANISOU 2063  OE1 GLU A1273    13005  11592  13986   1185    660   -308       O  
ATOM   2064  OE2 GLU A1273     -11.630  55.197   6.906  1.00 92.11           O  
ANISOU 2064  OE2 GLU A1273    11977  10369  12653   1060    734   -404       O  
ATOM   2065  N   ILE A1274     -13.743  48.971   8.979  1.00 58.51           N  
ANISOU 2065  N   ILE A1274     7060   6383   8788   1051    485   -136       N  
ATOM   2066  CA  ILE A1274     -14.733  48.113   9.624  1.00 53.69           C  
ANISOU 2066  CA  ILE A1274     6332   5806   8260   1079    486    -65       C  
ATOM   2067  C   ILE A1274     -14.150  47.458  10.868  1.00 52.77           C  
ANISOU 2067  C   ILE A1274     6189   5742   8118   1027    509    -46       C  
ATOM   2068  O   ILE A1274     -14.807  47.396  11.915  1.00 49.79           O  
ANISOU 2068  O   ILE A1274     5780   5391   7749   1054    569      1       O  
ATOM   2069  CB  ILE A1274     -15.238  47.045   8.639  1.00 45.08           C  
ANISOU 2069  CB  ILE A1274     5136   4710   7283   1089    392    -39       C  
ATOM   2070  CG1 ILE A1274     -16.067  47.675   7.525  1.00 49.14           C  
ANISOU 2070  CG1 ILE A1274     5662   5182   7826   1159    370    -47       C  
ATOM   2071  CG2 ILE A1274     -16.017  45.969   9.379  1.00 50.70           C  
ANISOU 2071  CG2 ILE A1274     5722   5457   8084   1092    392     31       C  
ATOM   2072  CD1 ILE A1274     -16.429  46.682   6.449  1.00 57.12           C  
ANISOU 2072  CD1 ILE A1274     6583   6185   8936   1163    266    -37       C  
ATOM   2073  N   LEU A1275     -12.915  46.960  10.783  1.00 57.24           N  
ANISOU 2073  N   LEU A1275     6770   6329   8652    958    466    -79       N  
ATOM   2074  CA  LEU A1275     -12.321  46.313  11.944  1.00 53.08           C  
ANISOU 2074  CA  LEU A1275     6218   5858   8094    917    483    -60       C  
ATOM   2075  C   LEU A1275     -11.964  47.306  13.040  1.00 59.94           C  
ANISOU 2075  C   LEU A1275     7178   6745   8851    908    565    -88       C  
ATOM   2076  O   LEU A1275     -11.863  46.908  14.206  1.00 54.94           O  
ANISOU 2076  O   LEU A1275     6524   6159   8191    900    598    -59       O  
ATOM   2077  CB  LEU A1275     -11.079  45.528  11.529  1.00 50.21           C  
ANISOU 2077  CB  LEU A1275     5842   5514   7720    854    414    -87       C  
ATOM   2078  CG  LEU A1275     -11.331  44.393  10.538  1.00 52.37           C  
ANISOU 2078  CG  LEU A1275     6030   5769   8097    857    331    -61       C  
ATOM   2079  CD1 LEU A1275     -10.026  43.940   9.912  1.00 67.53           C  
ANISOU 2079  CD1 LEU A1275     7970   7698   9991    804    271   -100       C  
ATOM   2080  CD2 LEU A1275     -12.034  43.248  11.232  1.00 49.65           C  
ANISOU 2080  CD2 LEU A1275     5583   5450   7833    870    333     13       C  
ATOM   2081  N   SER A1276     -11.765  48.582  12.692  1.00 64.67           N  
ANISOU 2081  N   SER A1276     7884   7306   9383    911    599   -144       N  
ATOM   2082  CA  SER A1276     -11.203  49.532  13.647  1.00 63.60           C  
ANISOU 2082  CA  SER A1276     7848   7183   9132    885    668   -187       C  
ATOM   2083  C   SER A1276     -12.101  49.749  14.859  1.00 77.82           C  
ANISOU 2083  C   SER A1276     9649   9002  10918    937    747   -140       C  
ATOM   2084  O   SER A1276     -11.603  50.108  15.933  1.00 91.33           O  
ANISOU 2084  O   SER A1276    11418  10745  12539    912    792   -162       O  
ATOM   2085  CB  SER A1276     -10.931  50.870  12.963  1.00 63.59           C  
ANISOU 2085  CB  SER A1276     7967   7123   9073    880    697   -253       C  
ATOM   2086  OG  SER A1276     -12.127  51.434  12.452  1.00 66.61           O  
ANISOU 2086  OG  SER A1276     8360   7453   9496    961    729   -226       O  
ATOM   2087  N   SER A1277     -13.415  49.536  14.723  1.00 74.61           N  
ANISOU 2087  N   SER A1277     9176   8577  10594   1010    764    -77       N  
ATOM   2088  CA  SER A1277     -14.281  49.721  15.881  1.00 64.41           C  
ANISOU 2088  CA  SER A1277     7880   7303   9290   1064    847    -27       C  
ATOM   2089  C   SER A1277     -14.330  48.507  16.794  1.00 59.56           C  
ANISOU 2089  C   SER A1277     7172   6745   8711   1055    842     34       C  
ATOM   2090  O   SER A1277     -14.889  48.611  17.890  1.00 68.80           O  
ANISOU 2090  O   SER A1277     8347   7936   9857   1096    916     75       O  
ATOM   2091  CB  SER A1277     -15.697  50.075  15.425  1.00 66.12           C  
ANISOU 2091  CB  SER A1277     8062   7482   9578   1151    879     19       C  
ATOM   2092  OG  SER A1277     -16.203  49.093  14.538  1.00 73.39           O  
ANISOU 2092  OG  SER A1277     8862   8402  10622   1159    804     58       O  
ATOM   2093  N   LYS A1278     -13.781  47.371  16.373  1.00 53.83           N  
ANISOU 2093  N   LYS A1278     6370   6042   8040   1010    763     43       N  
ATOM   2094  CA  LYS A1278     -13.838  46.149  17.161  1.00 63.04           C  
ANISOU 2094  CA  LYS A1278     7450   7255   9246   1005    760    105       C  
ATOM   2095  C   LYS A1278     -12.630  46.058  18.088  1.00 73.34           C  
ANISOU 2095  C   LYS A1278     8807   8615  10442    958    764     74       C  
ATOM   2096  O   LYS A1278     -11.562  46.613  17.810  1.00 82.53           O  
ANISOU 2096  O   LYS A1278    10044   9784  11529    906    735      0       O  
ATOM   2097  CB  LYS A1278     -13.964  44.905  16.279  1.00 59.78           C  
ANISOU 2097  CB  LYS A1278     6928   6834   8951    988    678    138       C  
ATOM   2098  CG  LYS A1278     -15.078  45.009  15.244  1.00 58.12           C  
ANISOU 2098  CG  LYS A1278     6663   6575   8843   1030    657    157       C  
ATOM   2099  CD  LYS A1278     -15.525  43.627  14.792  1.00 57.40           C  
ANISOU 2099  CD  LYS A1278     6447   6481   8879   1020    598    209       C  
ATOM   2100  CE  LYS A1278     -16.981  43.645  14.330  1.00 68.51           C  
ANISOU 2100  CE  LYS A1278     7775   7861  10395   1074    605    253       C  
ATOM   2101  NZ  LYS A1278     -17.166  44.020  12.897  1.00 80.88           N  
ANISOU 2101  NZ  LYS A1278     9346   9386  11997   1084    535    211       N  
ATOM   2102  N   LYS A1279     -12.816  45.356  19.208  1.00 74.66           N  
ANISOU 2102  N   LYS A1279     8936   8826  10605    977    801    132       N  
ATOM   2103  CA  LYS A1279     -11.724  45.159  20.155  1.00 76.04           C  
ANISOU 2103  CA  LYS A1279     9151   9064  10677    943    800    110       C  
ATOM   2104  C   LYS A1279     -10.614  44.289  19.579  1.00 86.33           C  
ANISOU 2104  C   LYS A1279    10415  10395  11993    884    711     88       C  
ATOM   2105  O   LYS A1279      -9.429  44.528  19.862  1.00 95.13           O  
ANISOU 2105  O   LYS A1279    11582  11553  13010    838    687     32       O  
ATOM   2106  CB  LYS A1279     -12.267  44.527  21.442  1.00 76.81           C  
ANISOU 2106  CB  LYS A1279     9214   9198  10772    990    864    188       C  
ATOM   2107  CG  LYS A1279     -12.854  43.123  21.255  1.00 86.72           C  
ANISOU 2107  CG  LYS A1279    10347  10448  12153   1006    845    272       C  
ATOM   2108  CD  LYS A1279     -13.302  42.497  22.572  1.00 91.89           C  
ANISOU 2108  CD  LYS A1279    10977  11139  12799   1053    918    351       C  
ATOM   2109  CE  LYS A1279     -13.893  41.103  22.379  1.00 94.11           C  
ANISOU 2109  CE  LYS A1279    11141  11406  13212   1062    907    435       C  
ATOM   2110  NZ  LYS A1279     -15.175  41.116  21.624  1.00 97.12           N  
ANISOU 2110  NZ  LYS A1279    11448  11728  13723   1085    916    470       N  
ATOM   2111  N   GLU A1280     -10.955  43.394  18.645  1.00 87.38           N  
ANISOU 2111  N   GLU A1280    10462  10497  12241    884    658    123       N  
ATOM   2112  CA  GLU A1280      -9.947  42.530  18.046  1.00 81.71           C  
ANISOU 2112  CA  GLU A1280     9709   9798  11537    837    578    107       C  
ATOM   2113  C   GLU A1280      -8.929  43.326  17.255  1.00 76.98           C  
ANISOU 2113  C   GLU A1280     9178   9194  10878    786    534     19       C  
ATOM   2114  O   GLU A1280      -7.811  42.846  17.031  1.00 67.82           O  
ANISOU 2114  O   GLU A1280     8010   8069   9688    743    480     -7       O  
ATOM   2115  CB  GLU A1280     -10.626  41.492  17.147  1.00 74.17           C  
ANISOU 2115  CB  GLU A1280     8661   8801  10721    848    533    157       C  
ATOM   2116  CG  GLU A1280     -11.539  40.517  17.895  1.00 79.20           C  
ANISOU 2116  CG  GLU A1280     9219   9442  11431    886    575    248       C  
ATOM   2117  CD  GLU A1280     -12.950  41.056  18.071  1.00 85.59           C  
ANISOU 2117  CD  GLU A1280    10009  10217  12295    936    639    285       C  
ATOM   2118  OE1 GLU A1280     -13.888  40.243  18.225  1.00 89.97           O  
ANISOU 2118  OE1 GLU A1280    10479  10756  12951    961    659    357       O  
ATOM   2119  OE2 GLU A1280     -13.127  42.291  18.021  1.00 93.95           O  
ANISOU 2119  OE2 GLU A1280    11137  11262  13299    950    670    242       O  
ATOM   2120  N   PHE A1281      -9.292  44.539  16.848  1.00 75.03           N  
ANISOU 2120  N   PHE A1281     8997   8901  10608    792    562    -25       N  
ATOM   2121  CA  PHE A1281      -8.395  45.360  16.053  1.00 66.10           C  
ANISOU 2121  CA  PHE A1281     7936   7753   9425    744    532   -107       C  
ATOM   2122  C   PHE A1281      -7.113  45.662  16.815  1.00 77.95           C  
ANISOU 2122  C   PHE A1281     9489   9319  10810    689    532   -160       C  
ATOM   2123  O   PHE A1281      -6.072  45.912  16.195  1.00 79.20           O  
ANISOU 2123  O   PHE A1281     9674   9483  10935    635    491   -219       O  
ATOM   2124  CB  PHE A1281      -9.110  46.646  15.645  1.00 65.46           C  
ANISOU 2124  CB  PHE A1281     7927   7609   9335    770    579   -137       C  
ATOM   2125  CG  PHE A1281      -8.333  47.504  14.699  1.00 66.99           C  
ANISOU 2125  CG  PHE A1281     8195   7768   9488    727    557   -215       C  
ATOM   2126  CD1 PHE A1281      -8.194  47.146  13.369  1.00 73.52           C  
ANISOU 2126  CD1 PHE A1281     8993   8559  10381    720    495   -222       C  
ATOM   2127  CD2 PHE A1281      -7.768  48.690  15.134  1.00 63.63           C  
ANISOU 2127  CD2 PHE A1281     7875   7341   8959    693    604   -280       C  
ATOM   2128  CE1 PHE A1281      -7.486  47.950  12.497  1.00 72.99           C  
ANISOU 2128  CE1 PHE A1281     9000   8456  10275    685    484   -289       C  
ATOM   2129  CE2 PHE A1281      -7.063  49.499  14.272  1.00 60.01           C  
ANISOU 2129  CE2 PHE A1281     7488   6845   8467    649    593   -350       C  
ATOM   2130  CZ  PHE A1281      -6.920  49.130  12.950  1.00 68.25           C  
ANISOU 2130  CZ  PHE A1281     8502   7854   9578    647    536   -351       C  
ATOM   2131  N   GLN A1282      -7.160  45.637  18.157  1.00 87.79           N  
ANISOU 2131  N   GLN A1282    10747  10616  11993    705    578   -139       N  
ATOM   2132  CA  GLN A1282      -5.932  45.863  18.923  1.00 91.41           C  
ANISOU 2132  CA  GLN A1282    11247  11147  12338    654    568   -192       C  
ATOM   2133  C   GLN A1282      -4.885  44.791  18.634  1.00 77.81           C  
ANISOU 2133  C   GLN A1282     9458   9479  10627    621    495   -186       C  
ATOM   2134  O   GLN A1282      -3.682  45.070  18.682  1.00 65.05           O  
ANISOU 2134  O   GLN A1282     7868   7913   8937    563    464   -247       O  
ATOM   2135  CB  GLN A1282      -6.232  45.966  20.416  1.00109.04           C  
ANISOU 2135  CB  GLN A1282    13507  13426  14497    688    628   -167       C  
ATOM   2136  CG  GLN A1282      -7.074  47.183  20.765  1.00125.77           C  
ANISOU 2136  CG  GLN A1282    15713  15495  16581    718    706   -185       C  
ATOM   2137  CD  GLN A1282      -7.513  47.199  22.213  1.00138.50           C  
ANISOU 2137  CD  GLN A1282    17351  17146  18128    765    771   -149       C  
ATOM   2138  OE1 GLN A1282      -7.956  46.183  22.747  1.00142.86           O  
ANISOU 2138  OE1 GLN A1282    17833  17727  18720    811    780    -70       O  
ATOM   2139  NE2 GLN A1282      -7.389  48.354  22.859  1.00146.00           N  
ANISOU 2139  NE2 GLN A1282    18407  18093  18973    755    820   -208       N  
ATOM   2140  N   GLU A1283      -5.319  43.564  18.350  1.00 77.64           N  
ANISOU 2140  N   GLU A1283     9351   9451  10698    656    468   -114       N  
ATOM   2141  CA  GLU A1283      -4.426  42.420  18.196  1.00 69.25           C  
ANISOU 2141  CA  GLU A1283     8226   8439   9645    639    408    -94       C  
ATOM   2142  C   GLU A1283      -3.851  42.308  16.785  1.00 58.43           C  
ANISOU 2142  C   GLU A1283     6843   7034   8323    603    346   -129       C  
ATOM   2143  O   GLU A1283      -3.007  41.440  16.541  1.00 38.73           O  
ANISOU 2143  O   GLU A1283     4304   4579   5833    589    296   -120       O  
ATOM   2144  CB  GLU A1283      -5.180  41.142  18.557  1.00 72.86           C  
ANISOU 2144  CB  GLU A1283     8609   8895  10181    693    417      0       C  
ATOM   2145  CG  GLU A1283      -5.848  41.193  19.922  1.00 82.55           C  
ANISOU 2145  CG  GLU A1283     9848  10150  11369    739    487     46       C  
ATOM   2146  CD  GLU A1283      -6.651  39.945  20.227  1.00 92.79           C  
ANISOU 2146  CD  GLU A1283    11071  11433  12753    789    506    143       C  
ATOM   2147  OE1 GLU A1283      -7.900  39.984  20.074  1.00 94.94           O  
ANISOU 2147  OE1 GLU A1283    11319  11645  13109    821    545    185       O  
ATOM   2148  OE2 GLU A1283      -6.046  38.927  20.604  1.00 96.60           O  
ANISOU 2148  OE2 GLU A1283    11517  11964  13223    796    484    178       O  
ATOM   2149  N   MET A1284      -4.301  43.148  15.861  1.00 59.69           N  
ANISOU 2149  N   MET A1284     7043   7122   8516    596    352   -164       N  
ATOM   2150  CA  MET A1284      -3.887  43.120  14.469  1.00 47.66           C  
ANISOU 2150  CA  MET A1284     5518   5555   7037    572    301   -195       C  
ATOM   2151  C   MET A1284      -2.845  44.192  14.175  1.00 42.78           C  
ANISOU 2151  C   MET A1284     4969   4947   6338    512    302   -280       C  
ATOM   2152  O   MET A1284      -2.813  45.252  14.804  1.00 32.52           O  
ANISOU 2152  O   MET A1284     3737   3654   4966    491    349   -323       O  
ATOM   2153  CB  MET A1284      -5.071  43.281  13.525  1.00 50.81           C  
ANISOU 2153  CB  MET A1284     5913   5865   7527    611    303   -176       C  
ATOM   2154  CG  MET A1284      -6.199  42.311  13.778  1.00 51.75           C  
ANISOU 2154  CG  MET A1284     5958   5968   7735    663    307    -95       C  
ATOM   2155  SD  MET A1284      -7.687  42.757  12.879  1.00 62.72           S  
ANISOU 2155  SD  MET A1284     7343   7268   9218    710    316    -80       S  
ATOM   2156  CE  MET A1284      -8.753  41.403  13.342  1.00 64.16           C  
ANISOU 2156  CE  MET A1284     7420   7451   9506    750    316     14       C  
ATOM   2157  N   ARG A1285      -1.997  43.894  13.197  1.00 48.18           N  
ANISOU 2157  N   ARG A1285     5639   5628   7038    482    252   -304       N  
ATOM   2158  CA  ARG A1285      -1.053  44.829  12.609  1.00 50.29           C  
ANISOU 2158  CA  ARG A1285     5965   5888   7254    423    251   -380       C  
ATOM   2159  C   ARG A1285      -1.245  44.841  11.101  1.00 56.44           C  
ANISOU 2159  C   ARG A1285     6755   6588   8101    437    225   -385       C  
ATOM   2160  O   ARG A1285      -1.573  43.809  10.510  1.00 71.68           O  
ANISOU 2160  O   ARG A1285     8630   8500  10106    474    182   -337       O  
ATOM   2161  CB  ARG A1285       0.388  44.402  12.912  1.00 56.13           C  
ANISOU 2161  CB  ARG A1285     6670   6718   7938    374    216   -403       C  
ATOM   2162  CG  ARG A1285       0.667  44.133  14.376  1.00 58.58           C  
ANISOU 2162  CG  ARG A1285     6957   7121   8180    371    226   -390       C  
ATOM   2163  CD  ARG A1285       0.690  45.407  15.189  1.00 57.88           C  
ANISOU 2163  CD  ARG A1285     6944   7042   8006    334    276   -449       C  
ATOM   2164  NE  ARG A1285       0.897  45.136  16.608  1.00 56.67           N  
ANISOU 2164  NE  ARG A1285     6773   6978   7781    340    283   -437       N  
ATOM   2165  CZ  ARG A1285      -0.088  44.888  17.467  1.00 61.53           C  
ANISOU 2165  CZ  ARG A1285     7388   7590   8400    397    318   -384       C  
ATOM   2166  NH1 ARG A1285      -1.345  44.880  17.050  1.00 58.90           N  
ANISOU 2166  NH1 ARG A1285     7060   7173   8145    449    348   -340       N  
ATOM   2167  NH2 ARG A1285       0.180  44.652  18.743  1.00 72.71           N  
ANISOU 2167  NH2 ARG A1285     8796   9089   9741    407    325   -374       N  
ATOM   2168  N   PHE A1286      -1.081  46.007  10.479  1.00 58.23           N  
ANISOU 2168  N   PHE A1286     7060   6763   8301    409    254   -443       N  
ATOM   2169  CA  PHE A1286      -1.277  46.141   9.039  1.00 49.26           C  
ANISOU 2169  CA  PHE A1286     5950   5550   7218    430    235   -451       C  
ATOM   2170  C   PHE A1286      -0.089  46.871   8.439  1.00 47.21           C  
ANISOU 2170  C   PHE A1286     5743   5285   6908    368    244   -516       C  
ATOM   2171  O   PHE A1286       0.354  47.892   8.974  1.00 58.63           O  
ANISOU 2171  O   PHE A1286     7248   6744   8286    316    290   -569       O  
ATOM   2172  CB  PHE A1286      -2.568  46.888   8.702  1.00 46.17           C  
ANISOU 2172  CB  PHE A1286     5609   5077   6856    482    271   -444       C  
ATOM   2173  CG  PHE A1286      -3.817  46.139   9.059  1.00 61.85           C  
ANISOU 2173  CG  PHE A1286     7531   7058   8909    545    260   -376       C  
ATOM   2174  CD1 PHE A1286      -4.288  46.123  10.363  1.00 63.30           C  
ANISOU 2174  CD1 PHE A1286     7697   7283   9070    554    298   -350       C  
ATOM   2175  CD2 PHE A1286      -4.530  45.461   8.082  1.00 61.17           C  
ANISOU 2175  CD2 PHE A1286     7406   6926   8910    594    214   -340       C  
ATOM   2176  CE1 PHE A1286      -5.446  45.440  10.689  1.00 58.24           C  
ANISOU 2176  CE1 PHE A1286     6995   6636   8498    610    297   -284       C  
ATOM   2177  CE2 PHE A1286      -5.685  44.778   8.395  1.00 59.54           C  
ANISOU 2177  CE2 PHE A1286     7134   6714   8774    643    205   -280       C  
ATOM   2178  CZ  PHE A1286      -6.148  44.765   9.702  1.00 61.63           C  
ANISOU 2178  CZ  PHE A1286     7376   7019   9021    651    250   -250       C  
ATOM   2179  N   ILE A1287       0.419  46.350   7.330  1.00 38.68           N  
ANISOU 2179  N   ILE A1287     4646   4187   5864    372    202   -513       N  
ATOM   2180  CA  ILE A1287       1.498  46.975   6.578  1.00 38.26           C  
ANISOU 2180  CA  ILE A1287     4639   4121   5777    320    214   -567       C  
ATOM   2181  C   ILE A1287       1.022  47.056   5.144  1.00 34.47           C  
ANISOU 2181  C   ILE A1287     4200   3550   5347    370    203   -561       C  
ATOM   2182  O   ILE A1287       0.982  46.035   4.449  1.00 38.45           O  
ANISOU 2182  O   ILE A1287     4658   4048   5904    408    148   -524       O  
ATOM   2183  CB  ILE A1287       2.821  46.201   6.672  1.00 42.21           C  
ANISOU 2183  CB  ILE A1287     5075   4704   6259    277    177   -569       C  
ATOM   2184  CG1 ILE A1287       3.252  46.033   8.129  1.00 40.10           C  
ANISOU 2184  CG1 ILE A1287     4762   4538   5938    240    179   -572       C  
ATOM   2185  CG2 ILE A1287       3.899  46.893   5.870  1.00 43.75           C  
ANISOU 2185  CG2 ILE A1287     5313   4883   6425    223    197   -623       C  
ATOM   2186  CD1 ILE A1287       4.350  45.014   8.335  1.00 37.83           C  
ANISOU 2186  CD1 ILE A1287     4392   4343   5639    223    132   -554       C  
ATOM   2187  N   ILE A1288       0.662  48.255   4.695  1.00 41.15           N  
ANISOU 2187  N   ILE A1288     5139   4324   6174    373    255   -596       N  
ATOM   2188  CA  ILE A1288       0.199  48.462   3.332  1.00 48.47           C  
ANISOU 2188  CA  ILE A1288     6117   5163   7136    427    248   -593       C  
ATOM   2189  C   ILE A1288       1.353  49.058   2.548  1.00 51.97           C  
ANISOU 2189  C   ILE A1288     6618   5585   7544    379    276   -640       C  
ATOM   2190  O   ILE A1288       1.921  50.080   2.944  1.00 59.86           O  
ANISOU 2190  O   ILE A1288     7673   6584   8488    315    336   -689       O  
ATOM   2191  CB  ILE A1288      -1.036  49.377   3.291  1.00 27.85           C  
ANISOU 2191  CB  ILE A1288     3573   2483   4527    480    291   -593       C  
ATOM   2192  CG1 ILE A1288      -2.148  48.809   4.162  1.00 27.86           C  
ANISOU 2192  CG1 ILE A1288     3508   2512   4564    522    272   -544       C  
ATOM   2193  CG2 ILE A1288      -1.524  49.530   1.866  1.00 48.10           C  
ANISOU 2193  CG2 ILE A1288     6186   4965   7123    546    276   -587       C  
ATOM   2194  CD1 ILE A1288      -2.290  49.507   5.473  1.00 47.44           C  
ANISOU 2194  CD1 ILE A1288     6010   5022   6992    491    331   -559       C  
ATOM   2195  N   ILE A1289       1.687  48.427   1.430  1.00 48.83           N  
ANISOU 2195  N   ILE A1289     6209   5165   7178    408    235   -625       N  
ATOM   2196  CA  ILE A1289       2.851  48.769   0.631  1.00 45.01           C  
ANISOU 2196  CA  ILE A1289     5764   4667   6669    368    258   -659       C  
ATOM   2197  C   ILE A1289       2.400  48.980  -0.802  1.00 45.92           C  
ANISOU 2197  C   ILE A1289     5952   4690   6807    439    256   -653       C  
ATOM   2198  O   ILE A1289       1.725  48.119  -1.377  1.00 44.75           O  
ANISOU 2198  O   ILE A1289     5773   4522   6706    510    194   -614       O  
ATOM   2199  CB  ILE A1289       3.903  47.656   0.703  1.00 47.31           C  
ANISOU 2199  CB  ILE A1289     5968   5038   6969    340    210   -642       C  
ATOM   2200  CG1 ILE A1289       4.324  47.455   2.153  1.00 46.64           C  
ANISOU 2200  CG1 ILE A1289     5814   5053   6855    279    209   -647       C  
ATOM   2201  CG2 ILE A1289       5.111  48.026  -0.134  1.00 49.11           C  
ANISOU 2201  CG2 ILE A1289     6231   5255   7175    300    241   -673       C  
ATOM   2202  CD1 ILE A1289       4.956  46.135   2.402  1.00 47.87           C  
ANISOU 2202  CD1 ILE A1289     5871   5289   7027    282    151   -610       C  
ATOM   2203  N   GLY A1290       2.849  50.081  -1.398  1.00 51.19           N  
ANISOU 2203  N   GLY A1290     6716   5296   7438    420    324   -692       N  
ATOM   2204  CA  GLY A1290       2.540  50.381  -2.805  1.00 59.65           C  
ANISOU 2204  CA  GLY A1290     7866   6281   8519    490    328   -688       C  
ATOM   2205  C   GLY A1290       2.464  51.868  -3.057  1.00 64.68           C  
ANISOU 2205  C   GLY A1290     8623   6839   9112    484    419   -725       C  
ATOM   2206  O   GLY A1290       2.681  52.623  -2.125  1.00 63.89           O  
ANISOU 2206  O   GLY A1290     8548   6752   8977    416    478   -759       O  
ATOM   2207  N   LYS A1291       2.192  52.255  -4.298  1.00 69.87           N  
ANISOU 2207  N   LYS A1291     9362   7414   9771    561    427   -719       N  
ATOM   2208  CA  LYS A1291       2.019  53.673  -4.696  1.00 72.85           C  
ANISOU 2208  CA  LYS A1291     9868   7706  10107    572    518   -747       C  
ATOM   2209  C   LYS A1291       0.952  53.717  -5.787  1.00 69.88           C  
ANISOU 2209  C   LYS A1291     9555   7255   9741    695    494   -722       C  
ATOM   2210  O   LYS A1291       0.796  52.722  -6.471  1.00 76.14           O  
ANISOU 2210  O   LYS A1291    10302   8059  10569    753    414   -693       O  
ATOM   2211  CB  LYS A1291       3.340  54.251  -5.200  1.00 88.80           C  
ANISOU 2211  CB  LYS A1291    11941   9707  12090    488    594   -788       C  
ATOM   2212  CG  LYS A1291       4.026  53.430  -6.284  1.00105.34           C  
ANISOU 2212  CG  LYS A1291    14027  11797  14200    508    567   -774       C  
ATOM   2213  CD  LYS A1291       5.370  53.973  -6.709  1.00115.42           C  
ANISOU 2213  CD  LYS A1291    15372  13038  15444    437    660   -810       C  
ATOM   2214  CE  LYS A1291       6.433  53.805  -5.646  1.00119.42           C  
ANISOU 2214  CE  LYS A1291    15775  13640  15958    333    645   -823       C  
ATOM   2215  NZ  LYS A1291       7.786  54.078  -6.182  1.00125.08           N  
ANISOU 2215  NZ  LYS A1291    16538  14332  16656    265    728   -853       N  
ATOM   2216  N   GLY A1292       0.223  54.817  -5.931  1.00 76.35           N  
ANISOU 2216  N   GLY A1292    10486   7998  10526    735    565   -735       N  
ATOM   2217  CA  GLY A1292      -0.838  54.825  -6.954  1.00 76.80           C  
ANISOU 2217  CA  GLY A1292    10611   7986  10582    859    548   -713       C  
ATOM   2218  C   GLY A1292      -1.721  56.049  -6.857  1.00 79.90           C  
ANISOU 2218  C   GLY A1292    11092   8323  10943    906    616   -718       C  
ATOM   2219  O   GLY A1292      -1.215  57.150  -7.041  1.00 95.20           O  
ANISOU 2219  O   GLY A1292    13141  10200  12832    875    720   -748       O  
ATOM   2220  N   ASP A1293      -3.012  55.834  -6.610  1.00 64.49           N  
ANISOU 2220  N   ASP A1293     9094   6389   9019    985    562   -687       N  
ATOM   2221  CA  ASP A1293      -3.995  56.936  -6.495  1.00 62.86           C  
ANISOU 2221  CA  ASP A1293     8969   6131   8784   1053    622   -684       C  
ATOM   2222  C   ASP A1293      -3.662  57.771  -5.259  1.00 76.00           C  
ANISOU 2222  C   ASP A1293    10667   7796  10412    966    714   -713       C  
ATOM   2223  O   ASP A1293      -3.555  57.210  -4.175  1.00 82.97           O  
ANISOU 2223  O   ASP A1293    11454   8753  11318    897    687   -713       O  
ATOM   2224  CB  ASP A1293      -5.394  56.335  -6.396  1.00 66.14           C  
ANISOU 2224  CB  ASP A1293     9297   6584   9249   1145    534   -641       C  
ATOM   2225  CG  ASP A1293      -6.511  57.335  -6.571  1.00 72.60           C  
ANISOU 2225  CG  ASP A1293    10188   7356  10040   1240    585   -628       C  
ATOM   2226  OD1 ASP A1293      -6.325  58.472  -6.159  1.00 94.17           O  
ANISOU 2226  OD1 ASP A1293    12981  10066  12734   1206    678   -645       O  
ATOM   2227  OD2 ASP A1293      -7.549  56.958  -7.113  1.00 64.84           O  
ANISOU 2227  OD2 ASP A1293     9175   6391   9070   1330    512   -598       O  
ATOM   2228  N   PRO A1294      -3.507  59.099  -5.397  1.00 72.13           N  
ANISOU 2228  N   PRO A1294    10319   7223   9866    968    824   -740       N  
ATOM   2229  CA  PRO A1294      -3.221  60.014  -4.262  1.00 77.85           C  
ANISOU 2229  CA  PRO A1294    11093   7936  10549    883    917   -776       C  
ATOM   2230  C   PRO A1294      -4.276  60.018  -3.155  1.00 80.23           C  
ANISOU 2230  C   PRO A1294    11345   8278  10860    911    907   -756       C  
ATOM   2231  O   PRO A1294      -3.989  60.543  -2.045  1.00 98.55           O  
ANISOU 2231  O   PRO A1294    13686  10609  13150    830    966   -787       O  
ATOM   2232  CB  PRO A1294      -3.084  61.374  -4.952  1.00 81.62           C  
ANISOU 2232  CB  PRO A1294    11701   8355  10955    889    994   -782       C  
ATOM   2233  CG  PRO A1294      -2.701  61.042  -6.361  1.00 73.46           C  
ANISOU 2233  CG  PRO A1294    10665   7325   9923    923    944   -760       C  
ATOM   2234  CD  PRO A1294      -3.432  59.786  -6.695  1.00 67.27           C  
ANISOU 2234  CD  PRO A1294     9779   6582   9200   1010    831   -725       C  
ATOM   2235  N   GLU A1295      -5.547  59.835  -3.551  1.00 71.25           N  
ANISOU 2235  N   GLU A1295    10189   7137   9747   1039    865   -711       N  
ATOM   2236  CA  GLU A1295      -6.638  59.731  -2.588  1.00 74.51           C  
ANISOU 2236  CA  GLU A1295    10540   7592  10178   1079    852   -681       C  
ATOM   2237  C   GLU A1295      -6.528  58.439  -1.795  1.00 76.92           C  
ANISOU 2237  C   GLU A1295    10685   8001  10541   1019    763   -664       C  
ATOM   2238  O   GLU A1295      -6.832  58.411  -0.599  1.00 94.61           O  
ANISOU 2238  O   GLU A1295    12881  10285  12782    988    778   -659       O  
ATOM   2239  CB  GLU A1295      -8.002  59.827  -3.267  1.00 85.50           C  
ANISOU 2239  CB  GLU A1295    11938   8961  11588   1230    826   -636       C  
ATOM   2240  CG  GLU A1295      -8.272  61.158  -3.920  1.00108.78           C  
ANISOU 2240  CG  GLU A1295    14996  11877  14459   1264    878   -632       C  
ATOM   2241  CD  GLU A1295      -9.698  61.267  -4.416  1.00128.12           C  
ANISOU 2241  CD  GLU A1295    17412  14351  16918   1389    831   -582       C  
ATOM   2242  OE1 GLU A1295     -10.524  60.394  -4.049  1.00127.60           O  
ANISOU 2242  OE1 GLU A1295    17241  14323  16920   1446    771   -553       O  
ATOM   2243  OE2 GLU A1295      -9.994  62.256  -5.128  1.00138.12           O  
ANISOU 2243  OE2 GLU A1295    18754  15599  18126   1428    861   -570       O  
ATOM   2244  N   LEU A1296      -6.169  57.338  -2.462  1.00 54.08           N  
ANISOU 2244  N   LEU A1296     7708   5144   7695   1014    670   -651       N  
ATOM   2245  CA  LEU A1296      -5.962  56.106  -1.714  1.00 55.37           C  
ANISOU 2245  CA  LEU A1296     7729   5399   7909    954    594   -634       C  
ATOM   2246  C   LEU A1296      -4.708  56.231  -0.861  1.00 64.29           C  
ANISOU 2246  C   LEU A1296     8862   6562   9004    824    634   -676       C  
ATOM   2247  O   LEU A1296      -4.629  55.617   0.205  1.00 70.53           O  
ANISOU 2247  O   LEU A1296     9562   7426   9811    773    607   -667       O  
ATOM   2248  CB  LEU A1296      -5.939  54.892  -2.644  1.00 57.32           C  
ANISOU 2248  CB  LEU A1296     7894   5671   8214    986    487   -609       C  
ATOM   2249  CG  LEU A1296      -7.244  54.703  -3.429  1.00 45.13           C  
ANISOU 2249  CG  LEU A1296     6333   4105   6707   1111    433   -572       C  
ATOM   2250  CD1 LEU A1296      -7.211  53.508  -4.364  1.00 45.60           C  
ANISOU 2250  CD1 LEU A1296     6322   4185   6821   1138    324   -555       C  
ATOM   2251  CD2 LEU A1296      -8.388  54.543  -2.447  1.00 42.45           C  
ANISOU 2251  CD2 LEU A1296     5916   3810   6404   1142    426   -537       C  
ATOM   2252  N   GLU A1297      -3.686  56.948  -1.354  1.00 67.63           N  
ANISOU 2252  N   GLU A1297     9380   6936   9382    771    693   -720       N  
ATOM   2253  CA  GLU A1297      -2.503  57.198  -0.532  1.00 64.57           C  
ANISOU 2253  CA  GLU A1297     8996   6581   8958    643    735   -766       C  
ATOM   2254  C   GLU A1297      -2.863  58.039   0.698  1.00 69.74           C  
ANISOU 2254  C   GLU A1297     9696   7234   9570    613    805   -787       C  
ATOM   2255  O   GLU A1297      -2.453  57.706   1.812  1.00 76.21           O  
ANISOU 2255  O   GLU A1297    10451   8124  10380    537    792   -800       O  
ATOM   2256  CB  GLU A1297      -1.381  57.835  -1.355  1.00 70.66           C  
ANISOU 2256  CB  GLU A1297     9858   7295   9696    590    790   -809       C  
ATOM   2257  CG  GLU A1297      -0.806  56.906  -2.419  1.00 75.52           C  
ANISOU 2257  CG  GLU A1297    10421   7926  10348    604    723   -791       C  
ATOM   2258  CD  GLU A1297       0.476  57.435  -3.037  1.00 86.18           C  
ANISOU 2258  CD  GLU A1297    11840   9237  11668    532    782   -832       C  
ATOM   2259  OE1 GLU A1297       1.114  58.315  -2.421  1.00 93.02           O  
ANISOU 2259  OE1 GLU A1297    12761  10090  12494    440    861   -879       O  
ATOM   2260  OE2 GLU A1297       0.857  56.958  -4.129  1.00 89.88           O  
ANISOU 2260  OE2 GLU A1297    12306   9690  12155    565    751   -817       O  
ATOM   2261  N   GLY A1298      -3.640  59.129   0.533  1.00 72.67           N  
ANISOU 2261  N   GLY A1298    10181   7525   9908    679    880   -789       N  
ATOM   2262  CA  GLY A1298      -4.003  59.904   1.691  1.00 84.87           C  
ANISOU 2262  CA  GLY A1298    11775   9063  11408    658    948   -808       C  
ATOM   2263  C   GLY A1298      -4.943  59.135   2.597  1.00 83.94           C  
ANISOU 2263  C   GLY A1298    11548   9019  11326    702    896   -760       C  
ATOM   2264  O   GLY A1298      -4.956  59.358   3.806  1.00 95.87           O  
ANISOU 2264  O   GLY A1298    13057  10563  12805    657    927   -775       O  
ATOM   2265  N   TRP A1299      -5.800  58.284   2.030  1.00 70.16           N  
ANISOU 2265  N   TRP A1299     9718   7296   9644    794    821   -704       N  
ATOM   2266  CA  TRP A1299      -6.643  57.456   2.887  1.00 68.86           C  
ANISOU 2266  CA  TRP A1299     9438   7203   9524    826    772   -656       C  
ATOM   2267  C   TRP A1299      -5.823  56.441   3.690  1.00 73.61           C  
ANISOU 2267  C   TRP A1299     9932   7895  10141    732    717   -660       C  
ATOM   2268  O   TRP A1299      -6.066  56.248   4.888  1.00 79.02           O  
ANISOU 2268  O   TRP A1299    10574   8633  10818    712    726   -649       O  
ATOM   2269  CB  TRP A1299      -7.705  56.758   2.038  1.00 59.84           C  
ANISOU 2269  CB  TRP A1299     8223   6061   8451    934    701   -600       C  
ATOM   2270  CG  TRP A1299      -8.702  55.959   2.829  1.00 52.98           C  
ANISOU 2270  CG  TRP A1299     7236   5255   7637    973    659   -546       C  
ATOM   2271  CD1 TRP A1299      -8.869  55.969   4.182  1.00 57.88           C  
ANISOU 2271  CD1 TRP A1299     7829   5920   8242    941    694   -539       C  
ATOM   2272  CD2 TRP A1299      -9.719  55.095   2.309  1.00 47.04           C  
ANISOU 2272  CD2 TRP A1299     6383   4524   6965   1054    582   -493       C  
ATOM   2273  NE1 TRP A1299      -9.899  55.139   4.542  1.00 56.28           N  
ANISOU 2273  NE1 TRP A1299     7512   5764   8106    997    650   -479       N  
ATOM   2274  CE2 TRP A1299     -10.444  54.594   3.409  1.00 50.12           C  
ANISOU 2274  CE2 TRP A1299     6682   4971   7389   1062    579   -452       C  
ATOM   2275  CE3 TRP A1299     -10.077  54.685   1.022  1.00 49.31           C  
ANISOU 2275  CE3 TRP A1299     6650   4789   7297   1119    513   -477       C  
ATOM   2276  CZ2 TRP A1299     -11.504  53.703   3.262  1.00 55.10           C  
ANISOU 2276  CZ2 TRP A1299     7196   5635   8106   1124    513   -396       C  
ATOM   2277  CZ3 TRP A1299     -11.127  53.802   0.877  1.00 54.80           C  
ANISOU 2277  CZ3 TRP A1299     7230   5519   8072   1180    440   -428       C  
ATOM   2278  CH2 TRP A1299     -11.828  53.319   1.990  1.00 60.00           C  
ANISOU 2278  CH2 TRP A1299     7793   6232   8771   1178    442   -388       C  
ATOM   2279  N   ALA A1300      -4.840  55.788   3.056  1.00 74.67           N  
ANISOU 2279  N   ALA A1300    10028   8051  10294    681    663   -674       N  
ATOM   2280  CA  ALA A1300      -4.009  54.822   3.777  1.00 67.19           C  
ANISOU 2280  CA  ALA A1300     8981   7193   9357    601    612   -676       C  
ATOM   2281  C   ALA A1300      -3.141  55.511   4.819  1.00 78.69           C  
ANISOU 2281  C   ALA A1300    10484   8673  10742    501    671   -730       C  
ATOM   2282  O   ALA A1300      -2.970  55.003   5.933  1.00 82.97           O  
ANISOU 2282  O   ALA A1300    10959   9291  11275    462    652   -724       O  
ATOM   2283  CB  ALA A1300      -3.144  54.030   2.799  1.00 64.01           C  
ANISOU 2283  CB  ALA A1300     8533   6802   8985    577    549   -677       C  
ATOM   2284  N   ARG A1301      -2.585  56.671   4.466  1.00 80.03           N  
ANISOU 2284  N   ARG A1301    10772   8776  10859    461    743   -784       N  
ATOM   2285  CA  ARG A1301      -1.788  57.462   5.396  1.00 76.40           C  
ANISOU 2285  CA  ARG A1301    10371   8329  10330    360    803   -846       C  
ATOM   2286  C   ARG A1301      -2.663  57.997   6.525  1.00 75.97           C  
ANISOU 2286  C   ARG A1301    10354   8272  10240    389    852   -842       C  
ATOM   2287  O   ARG A1301      -2.197  58.144   7.661  1.00 82.52           O  
ANISOU 2287  O   ARG A1301    11182   9151  11021    318    867   -875       O  
ATOM   2288  CB  ARG A1301      -1.120  58.608   4.638  1.00 73.35           C  
ANISOU 2288  CB  ARG A1301    10110   7855   9905    315    876   -902       C  
ATOM   2289  CG  ARG A1301       0.019  58.271   3.664  1.00 67.98           C  
ANISOU 2289  CG  ARG A1301     9408   7178   9245    263    849   -920       C  
ATOM   2290  CD  ARG A1301       1.330  57.973   4.363  1.00 70.79           C  
ANISOU 2290  CD  ARG A1301     9701   7617   9578    138    828   -964       C  
ATOM   2291  NE  ARG A1301       2.376  57.536   3.441  1.00 79.66           N  
ANISOU 2291  NE  ARG A1301    10788   8754  10727     98    800   -971       N  
ATOM   2292  CZ  ARG A1301       3.498  56.929   3.818  1.00 97.25           C  
ANISOU 2292  CZ  ARG A1301    12925  11072  12953     13    758   -990       C  
ATOM   2293  NH1 ARG A1301       3.722  56.686   5.102  1.00105.17           N  
ANISOU 2293  NH1 ARG A1301    13869  12162  13927    -41    734  -1005       N  
ATOM   2294  NH2 ARG A1301       4.406  56.572   2.916  1.00102.69           N  
ANISOU 2294  NH2 ARG A1301    13584  11766  13665    -13    741   -991       N  
ATOM   2295  N   SER A1302      -3.926  58.315   6.204  1.00 68.37           N  
ANISOU 2295  N   SER A1302     9428   7252   9296    498    878   -801       N  
ATOM   2296  CA  SER A1302      -4.898  58.790   7.182  1.00 70.28           C  
ANISOU 2296  CA  SER A1302     9705   7489   9511    546    929   -784       C  
ATOM   2297  C   SER A1302      -5.210  57.698   8.192  1.00 75.32           C  
ANISOU 2297  C   SER A1302    10216   8224  10177    551    872   -741       C  
ATOM   2298  O   SER A1302      -5.284  57.949   9.405  1.00 85.87           O  
ANISOU 2298  O   SER A1302    11569   9593  11465    528    908   -753       O  
ATOM   2299  CB  SER A1302      -6.168  59.226   6.446  1.00 79.88           C  
ANISOU 2299  CB  SER A1302    10967   8633  10752    672    959   -741       C  
ATOM   2300  OG  SER A1302      -7.189  59.611   7.343  1.00 95.47           O  
ANISOU 2300  OG  SER A1302    12963  10606  12707    733   1009   -715       O  
ATOM   2301  N   LEU A1303      -5.335  56.466   7.706  1.00 65.57           N  
ANISOU 2301  N   LEU A1303     8860   7036   9017    580    786   -692       N  
ATOM   2302  CA  LEU A1303      -5.479  55.331   8.599  1.00 44.71           C  
ANISOU 2302  CA  LEU A1303     6097   4485   6405    576    732   -649       C  
ATOM   2303  C   LEU A1303      -4.197  55.124   9.388  1.00 51.98           C  
ANISOU 2303  C   LEU A1303     7000   5476   7276    468    718   -695       C  
ATOM   2304  O   LEU A1303      -4.242  54.642  10.527  1.00 47.31           O  
ANISOU 2304  O   LEU A1303     6355   4953   6667    457    709   -677       O  
ATOM   2305  CB  LEU A1303      -5.842  54.084   7.801  1.00 38.99           C  
ANISOU 2305  CB  LEU A1303     5260   3783   5773    624    646   -593       C  
ATOM   2306  CG  LEU A1303      -7.308  54.014   7.372  1.00 39.60           C  
ANISOU 2306  CG  LEU A1303     5314   3823   5910    735    644   -536       C  
ATOM   2307  CD1 LEU A1303      -7.610  52.729   6.632  1.00 53.77           C  
ANISOU 2307  CD1 LEU A1303     6994   5640   7794    768    552   -488       C  
ATOM   2308  CD2 LEU A1303      -8.186  54.127   8.598  1.00 38.53           C  
ANISOU 2308  CD2 LEU A1303     5163   3715   5764    770    690   -503       C  
ATOM   2309  N   GLU A1304      -3.047  55.455   8.782  1.00 66.42           N  
ANISOU 2309  N   GLU A1304     8867   7290   9079    393    716   -750       N  
ATOM   2310  CA  GLU A1304      -1.780  55.308   9.481  1.00 68.64           C  
ANISOU 2310  CA  GLU A1304     9124   7644   9312    288    699   -797       C  
ATOM   2311  C   GLU A1304      -1.670  56.278  10.656  1.00 67.43           C  
ANISOU 2311  C   GLU A1304     9054   7493   9073    240    765   -848       C  
ATOM   2312  O   GLU A1304      -1.143  55.899  11.705  1.00 71.06           O  
ANISOU 2312  O   GLU A1304     9467   8039   9495    190    742   -862       O  
ATOM   2313  CB  GLU A1304      -0.621  55.495   8.499  1.00 70.50           C  
ANISOU 2313  CB  GLU A1304     9379   7861   9548    220    689   -842       C  
ATOM   2314  CG  GLU A1304       0.763  55.357   9.109  1.00 75.68           C  
ANISOU 2314  CG  GLU A1304     9999   8598  10159    108    668   -893       C  
ATOM   2315  CD  GLU A1304       1.862  55.755   8.145  1.00 81.97           C  
ANISOU 2315  CD  GLU A1304    10827   9364  10953     39    678   -941       C  
ATOM   2316  OE1 GLU A1304       1.565  56.434   7.144  1.00 85.42           O  
ANISOU 2316  OE1 GLU A1304    11348   9704  11405     69    723   -947       O  
ATOM   2317  OE2 GLU A1304       3.026  55.371   8.379  1.00 86.18           O  
ANISOU 2317  OE2 GLU A1304    11298   9975  11471    -41    643   -969       O  
ATOM   2318  N   GLU A1305      -2.131  57.542  10.519  1.00 72.27           N  
ANISOU 2318  N   GLU A1305     9796   8014   9649    255    848   -880       N  
ATOM   2319  CA  GLU A1305      -2.061  58.391  11.709  1.00 82.55           C  
ANISOU 2319  CA  GLU A1305    11179   9319  10867    212    908   -929       C  
ATOM   2320  C   GLU A1305      -3.213  58.141  12.678  1.00 82.44           C  
ANISOU 2320  C   GLU A1305    11145   9328  10849    296    924   -874       C  
ATOM   2321  O   GLU A1305      -3.069  58.430  13.868  1.00 82.39           O  
ANISOU 2321  O   GLU A1305    11171   9359  10774    262    949   -903       O  
ATOM   2322  CB  GLU A1305      -2.169  59.905  11.479  1.00101.18           C  
ANISOU 2322  CB  GLU A1305    13702  11569  13173    197   1006   -985       C  
ATOM   2323  CG  GLU A1305      -3.538  60.362  10.979  1.00118.86           C  
ANISOU 2323  CG  GLU A1305    16001  13721  15438    321   1059   -935       C  
ATOM   2324  CD  GLU A1305      -3.631  61.850  10.717  1.00123.35           C  
ANISOU 2324  CD  GLU A1305    16741  14176  15952    315   1162   -986       C  
ATOM   2325  OE1 GLU A1305      -2.742  62.583  11.198  1.00122.93           O  
ANISOU 2325  OE1 GLU A1305    16766  14111  15833    209   1201  -1065       O  
ATOM   2326  OE2 GLU A1305      -4.633  62.313  10.108  1.00121.10           O  
ANISOU 2326  OE2 GLU A1305    16514  13813  15684    419   1208   -949       O  
ATOM   2327  N   LYS A1306      -4.343  57.592  12.214  1.00 85.97           N  
ANISOU 2327  N   LYS A1306    11538   9759  11368    403    909   -797       N  
ATOM   2328  CA  LYS A1306      -5.460  57.389  13.129  1.00 83.38           C  
ANISOU 2328  CA  LYS A1306    11188   9451  11042    482    933   -742       C  
ATOM   2329  C   LYS A1306      -5.226  56.205  14.060  1.00 85.76           C  
ANISOU 2329  C   LYS A1306    11373   9861  11353    466    874   -707       C  
ATOM   2330  O   LYS A1306      -5.625  56.248  15.231  1.00 91.49           O  
ANISOU 2330  O   LYS A1306    12109  10620  12035    487    907   -693       O  
ATOM   2331  CB  LYS A1306      -6.745  57.222  12.307  1.00 86.06           C  
ANISOU 2331  CB  LYS A1306    11500   9740  11459    597    936   -672       C  
ATOM   2332  CG  LYS A1306      -7.957  56.746  13.058  1.00 98.41           C  
ANISOU 2332  CG  LYS A1306    13003  11334  13055    685    949   -599       C  
ATOM   2333  CD  LYS A1306      -8.441  57.723  14.113  1.00112.61           C  
ANISOU 2333  CD  LYS A1306    14903  13108  14774    710   1043   -614       C  
ATOM   2334  CE  LYS A1306      -9.420  57.034  15.064  1.00107.70           C  
ANISOU 2334  CE  LYS A1306    14202  12539  14181    781   1051   -539       C  
ATOM   2335  NZ  LYS A1306      -9.816  57.886  16.222  1.00 97.26           N  
ANISOU 2335  NZ  LYS A1306    12978  11203  12774    806   1141   -552       N  
ATOM   2336  N   HIS A1307      -4.560  55.168  13.583  1.00 87.80           N  
ANISOU 2336  N   HIS A1307    11528  10171  11659    434    794   -692       N  
ATOM   2337  CA  HIS A1307      -4.371  53.937  14.336  1.00 79.18           C  
ANISOU 2337  CA  HIS A1307    10324   9177  10584    431    737   -650       C  
ATOM   2338  C   HIS A1307      -2.890  53.597  14.372  1.00 62.18           C  
ANISOU 2338  C   HIS A1307     8138   7090   8397    334    684   -699       C  
ATOM   2339  O   HIS A1307      -2.198  53.663  13.352  1.00 67.42           O  
ANISOU 2339  O   HIS A1307     8803   7731   9083    293    658   -729       O  
ATOM   2340  CB  HIS A1307      -5.184  52.774  13.769  1.00 77.57           C  
ANISOU 2340  CB  HIS A1307    10008   8978  10486    506    687   -565       C  
ATOM   2341  CG  HIS A1307      -6.637  53.086  13.587  1.00 69.50           C  
ANISOU 2341  CG  HIS A1307     9002   7896   9508    601    732   -515       C  
ATOM   2342  ND1 HIS A1307      -7.200  53.339  12.356  1.00 63.97           N  
ANISOU 2342  ND1 HIS A1307     8315   7124   8865    648    727   -504       N  
ATOM   2343  CD2 HIS A1307      -7.643  53.184  14.488  1.00 69.85           C  
ANISOU 2343  CD2 HIS A1307     9047   7945   9547    663    783   -472       C  
ATOM   2344  CE1 HIS A1307      -8.493  53.570  12.505  1.00 69.62           C  
ANISOU 2344  CE1 HIS A1307     9032   7810   9611    735    769   -457       C  
ATOM   2345  NE2 HIS A1307      -8.786  53.488  13.790  1.00 71.89           N  
ANISOU 2345  NE2 HIS A1307     9312   8141   9864    744    807   -435       N  
ATOM   2346  N   GLY A1308      -2.413  53.223  15.548  1.00 53.25           N  
ANISOU 2346  N   GLY A1308     6976   6046   7210    303    669   -706       N  
ATOM   2347  CA  GLY A1308      -1.008  52.946  15.723  1.00 59.56           C  
ANISOU 2347  CA  GLY A1308     7740   6923   7968    213    620   -754       C  
ATOM   2348  C   GLY A1308      -0.572  51.596  15.226  1.00 59.93           C  
ANISOU 2348  C   GLY A1308     7665   7026   8079    223    542   -706       C  
ATOM   2349  O   GLY A1308       0.631  51.335  15.154  1.00 72.42           O  
ANISOU 2349  O   GLY A1308     9210   8669   9636    155    498   -742       O  
ATOM   2350  N   ASN A1309      -1.520  50.726  14.885  1.00 60.28           N  
ANISOU 2350  N   ASN A1309     7646   7051   8206    304    524   -625       N  
ATOM   2351  CA  ASN A1309      -1.211  49.409  14.349  1.00 67.41           C  
ANISOU 2351  CA  ASN A1309     8444   7994   9176    319    454   -576       C  
ATOM   2352  C   ASN A1309      -1.241  49.359  12.824  1.00 71.62           C  
ANISOU 2352  C   ASN A1309     8975   8456   9781    329    430   -574       C  
ATOM   2353  O   ASN A1309      -1.121  48.271  12.251  1.00 63.62           O  
ANISOU 2353  O   ASN A1309     7884   7460   8830    350    374   -532       O  
ATOM   2354  CB  ASN A1309      -2.164  48.363  14.939  1.00 52.48           C  
ANISOU 2354  CB  ASN A1309     6479   6126   7335    395    445   -489       C  
ATOM   2355  CG  ASN A1309      -3.626  48.670  14.661  1.00 45.78           C  
ANISOU 2355  CG  ASN A1309     5653   5198   6544    468    487   -448       C  
ATOM   2356  OD1 ASN A1309      -3.972  49.766  14.225  1.00 44.32           O  
ANISOU 2356  OD1 ASN A1309     5550   4944   6345    470    531   -485       O  
ATOM   2357  ND2 ASN A1309      -4.489  47.692  14.902  1.00 47.34           N  
ANISOU 2357  ND2 ASN A1309     5775   5405   6809    529    477   -370       N  
ATOM   2358  N   VAL A1310      -1.394  50.500  12.153  1.00 73.73           N  
ANISOU 2358  N   VAL A1310     9334   8643  10036    318    473   -619       N  
ATOM   2359  CA  VAL A1310      -1.380  50.559  10.696  1.00 63.89           C  
ANISOU 2359  CA  VAL A1310     8101   7329   8845    331    456   -622       C  
ATOM   2360  C   VAL A1310      -0.127  51.306  10.258  1.00 58.67           C  
ANISOU 2360  C   VAL A1310     7494   6662   8134    245    469   -697       C  
ATOM   2361  O   VAL A1310       0.216  52.352  10.826  1.00 63.62           O  
ANISOU 2361  O   VAL A1310     8199   7283   8691    190    521   -756       O  
ATOM   2362  CB  VAL A1310      -2.646  51.248  10.146  1.00 54.36           C  
ANISOU 2362  CB  VAL A1310     6957   6028   7671    402    499   -606       C  
ATOM   2363  CG1 VAL A1310      -2.553  51.427   8.633  1.00 49.84           C  
ANISOU 2363  CG1 VAL A1310     6413   5384   7139    417    483   -616       C  
ATOM   2364  CG2 VAL A1310      -3.889  50.455  10.520  1.00 50.05           C  
ANISOU 2364  CG2 VAL A1310     6340   5490   7186    482    485   -529       C  
ATOM   2365  N   LYS A1311       0.549  50.771   9.237  1.00 44.85           N  
ANISOU 2365  N   LYS A1311     5707   4911   6421    232    424   -695       N  
ATOM   2366  CA  LYS A1311       1.749  51.372   8.671  1.00 47.05           C  
ANISOU 2366  CA  LYS A1311     6026   5184   6668    154    437   -757       C  
ATOM   2367  C   LYS A1311       1.638  51.338   7.159  1.00 60.18           C  
ANISOU 2367  C   LYS A1311     7712   6769   8384    192    429   -745       C  
ATOM   2368  O   LYS A1311       1.194  50.339   6.590  1.00 68.66           O  
ANISOU 2368  O   LYS A1311     8725   7840   9520    255    376   -690       O  
ATOM   2369  CB  LYS A1311       3.033  50.655   9.118  1.00 59.25           C  
ANISOU 2369  CB  LYS A1311     7487   6836   8188     91    390   -770       C  
ATOM   2370  CG  LYS A1311       4.250  50.966   8.247  1.00 74.74           C  
ANISOU 2370  CG  LYS A1311     9461   8794  10144     24    392   -816       C  
ATOM   2371  CD  LYS A1311       4.790  52.381   8.454  1.00 85.32           C  
ANISOU 2371  CD  LYS A1311    10892  10102  11422    -64    459   -897       C  
ATOM   2372  CE  LYS A1311       6.131  52.557   7.744  1.00 92.47           C  
ANISOU 2372  CE  LYS A1311    11787  11024  12324   -141    460   -940       C  
ATOM   2373  NZ  LYS A1311       6.747  53.885   8.014  1.00101.90           N  
ANISOU 2373  NZ  LYS A1311    13062  12193  13461   -242    524  -1024       N  
ATOM   2374  N   VAL A1312       2.041  52.424   6.511  1.00 63.12           N  
ANISOU 2374  N   VAL A1312     8178   7076   8731    154    482   -797       N  
ATOM   2375  CA  VAL A1312       1.952  52.545   5.063  1.00 53.00           C  
ANISOU 2375  CA  VAL A1312     6937   5713   7486    195    484   -790       C  
ATOM   2376  C   VAL A1312       3.331  52.887   4.527  1.00 52.91           C  
ANISOU 2376  C   VAL A1312     6944   5708   7451    113    502   -839       C  
ATOM   2377  O   VAL A1312       4.049  53.710   5.108  1.00 61.97           O  
ANISOU 2377  O   VAL A1312     8129   6870   8545     24    548   -897       O  
ATOM   2378  CB  VAL A1312       0.917  53.602   4.625  1.00 43.38           C  
ANISOU 2378  CB  VAL A1312     5829   4389   6263    252    546   -795       C  
ATOM   2379  CG1 VAL A1312       0.875  53.704   3.109  1.00 32.16           C  
ANISOU 2379  CG1 VAL A1312     4455   2891   4875    300    545   -787       C  
ATOM   2380  CG2 VAL A1312      -0.453  53.246   5.159  1.00 51.51           C  
ANISOU 2380  CG2 VAL A1312     6828   5421   7322    334    530   -743       C  
ATOM   2381  N   ILE A1313       3.701  52.257   3.417  1.00 49.57           N  
ANISOU 2381  N   ILE A1313     6493   5271   7069    141    466   -816       N  
ATOM   2382  CA  ILE A1313       4.987  52.482   2.785  1.00 51.06           C  
ANISOU 2382  CA  ILE A1313     6691   5464   7244     74    485   -852       C  
ATOM   2383  C   ILE A1313       4.659  52.738   1.326  1.00 53.30           C  
ANISOU 2383  C   ILE A1313     7050   5647   7556    139    504   -839       C  
ATOM   2384  O   ILE A1313       4.193  51.832   0.625  1.00 50.61           O  
ANISOU 2384  O   ILE A1313     6672   5296   7260    219    447   -790       O  
ATOM   2385  CB  ILE A1313       5.912  51.263   2.915  1.00 40.21           C  
ANISOU 2385  CB  ILE A1313     5198   4192   5887     52    418   -829       C  
ATOM   2386  CG1 ILE A1313       6.118  50.882   4.379  1.00 35.24           C  
ANISOU 2386  CG1 ILE A1313     4493   3670   5228      9    390   -832       C  
ATOM   2387  CG2 ILE A1313       7.254  51.535   2.255  1.00 51.21           C  
ANISOU 2387  CG2 ILE A1313     6595   5593   7268    -16    444   -864       C  
ATOM   2388  CD1 ILE A1313       6.901  49.595   4.568  1.00 33.48           C  
ANISOU 2388  CD1 ILE A1313     4152   3550   5019      7    323   -799       C  
ATOM   2389  N   THR A1314       4.891  53.967   0.865  1.00 61.21           N  
ANISOU 2389  N   THR A1314     8160   6570   8527    106    585   -883       N  
ATOM   2390  CA  THR A1314       4.636  54.308  -0.525  1.00 64.09           C  
ANISOU 2390  CA  THR A1314     8608   6835   8906    172    613   -872       C  
ATOM   2391  C   THR A1314       5.904  54.386  -1.350  1.00 76.98           C  
ANISOU 2391  C   THR A1314    10250   8461  10536    120    640   -893       C  
ATOM   2392  O   THR A1314       5.829  54.331  -2.581  1.00 86.14           O  
ANISOU 2392  O   THR A1314    11460   9557  11713    184    645   -873       O  
ATOM   2393  CB  THR A1314       3.883  55.637  -0.635  1.00 65.49           C  
ANISOU 2393  CB  THR A1314     8919   6912   9053    196    695   -895       C  
ATOM   2394  OG1 THR A1314       4.587  56.649   0.094  1.00 91.05           O  
ANISOU 2394  OG1 THR A1314    12204  10148  12243     86    769   -957       O  
ATOM   2395  CG2 THR A1314       2.468  55.494  -0.090  1.00 50.34           C  
ANISOU 2395  CG2 THR A1314     6992   4989   7147    277    668   -861       C  
ATOM   2396  N   GLU A1315       7.058  54.488  -0.706  1.00 91.15           N  
ANISOU 2396  N   GLU A1315    11995  10326  12310      9    655   -931       N  
ATOM   2397  CA  GLU A1315       8.298  54.529  -1.451  1.00106.44           C  
ANISOU 2397  CA  GLU A1315    13927  12266  14250    -44    684   -948       C  
ATOM   2398  C   GLU A1315       8.623  53.131  -1.957  1.00100.21           C  
ANISOU 2398  C   GLU A1315    13040  11538  13498      9    603   -897       C  
ATOM   2399  O   GLU A1315       8.231  52.124  -1.361  1.00 95.22           O  
ANISOU 2399  O   GLU A1315    12320  10976  12885     44    526   -862       O  
ATOM   2400  CB  GLU A1315       9.400  55.136  -0.579  1.00122.95           C  
ANISOU 2400  CB  GLU A1315    15991  14418  16309   -183    725  -1010       C  
ATOM   2401  CG  GLU A1315       9.925  54.275   0.553  1.00137.89           C  
ANISOU 2401  CG  GLU A1315    17747  16449  18195   -233    653  -1009       C  
ATOM   2402  CD  GLU A1315      10.231  55.115   1.787  1.00151.62           C  
ANISOU 2402  CD  GLU A1315    19494  18227  19888   -342    686  -1073       C  
ATOM   2403  OE1 GLU A1315      11.423  55.276   2.131  1.00154.86           O  
ANISOU 2403  OE1 GLU A1315    19851  18707  20283   -448    695  -1117       O  
ATOM   2404  OE2 GLU A1315       9.267  55.612   2.412  1.00157.38           O  
ANISOU 2404  OE2 GLU A1315    20284  18918  20595   -319    701  -1082       O  
ATOM   2405  N   MET A1316       9.341  53.080  -3.075  1.00103.37           N  
ANISOU 2405  N   MET A1316    13462  11904  13909     18    628   -891       N  
ATOM   2406  CA  MET A1316       9.753  51.807  -3.649  1.00103.49           C  
ANISOU 2406  CA  MET A1316    13398  11968  13954     70    562   -846       C  
ATOM   2407  C   MET A1316      10.738  51.074  -2.741  1.00 96.55           C  
ANISOU 2407  C   MET A1316    12388  11221  13074     -2    520   -848       C  
ATOM   2408  O   MET A1316      11.605  51.682  -2.106  1.00110.96           O  
ANISOU 2408  O   MET A1316    14188  13096  14875   -108    561   -894       O  
ATOM   2409  CB  MET A1316      10.312  52.029  -5.051  1.00111.74           C  
ANISOU 2409  CB  MET A1316    14510  12941  15003     98    611   -840       C  
ATOM   2410  CG  MET A1316      10.817  50.785  -5.726  1.00123.40           C  
ANISOU 2410  CG  MET A1316    15921  14459  16505    153    553   -795       C  
ATOM   2411  SD  MET A1316      10.342  50.950  -7.451  1.00133.45           S  
ANISOU 2411  SD  MET A1316    17321  15602  17782    268    578   -771       S  
ATOM   2412  CE  MET A1316       8.577  50.647  -7.293  1.00134.98           C  
ANISOU 2412  CE  MET A1316    17541  15754  17991    368    505   -747       C  
ATOM   2413  N   LEU A1317      10.607  49.753  -2.706  1.00 76.53           N  
ANISOU 2413  N   LEU A1317     9770   8744  10564     60    439   -798       N  
ATOM   2414  CA  LEU A1317      11.427  48.872  -1.892  1.00 66.66           C  
ANISOU 2414  CA  LEU A1317     8395   7622   9312     20    390   -787       C  
ATOM   2415  C   LEU A1317      12.220  47.920  -2.775  1.00 65.46           C  
ANISOU 2415  C   LEU A1317     8198   7494   9181     62    366   -749       C  
ATOM   2416  O   LEU A1317      11.812  47.606  -3.897  1.00 56.11           O  
ANISOU 2416  O   LEU A1317     7070   6231   8017    146    358   -720       O  
ATOM   2417  CB  LEU A1317      10.561  48.055  -0.926  1.00 67.40           C  
ANISOU 2417  CB  LEU A1317     8429   7764   9414     61    319   -754       C  
ATOM   2418  CG  LEU A1317       9.642  48.817   0.027  1.00 74.63           C  
ANISOU 2418  CG  LEU A1317     9383   8662  10310     38    336   -780       C  
ATOM   2419  CD1 LEU A1317       8.713  47.853   0.742  1.00 83.17           C  
ANISOU 2419  CD1 LEU A1317    10409   9779  11413     99    269   -734       C  
ATOM   2420  CD2 LEU A1317      10.450  49.627   1.029  1.00 79.68           C  
ANISOU 2420  CD2 LEU A1317    10003   9368  10904    -76    375   -838       C  
ATOM   2421  N   SER A1318      13.363  47.468  -2.260  1.00 68.24           N  
ANISOU 2421  N   SER A1318     8448   7958   9522      8    353   -751       N  
ATOM   2422  CA  SER A1318      14.096  46.416  -2.946  1.00 62.69           C  
ANISOU 2422  CA  SER A1318     7691   7293   8837     58    325   -707       C  
ATOM   2423  C   SER A1318      13.330  45.106  -2.808  1.00 63.94           C  
ANISOU 2423  C   SER A1318     7814   7462   9018    152    243   -651       C  
ATOM   2424  O   SER A1318      12.585  44.898  -1.845  1.00 73.21           O  
ANISOU 2424  O   SER A1318     8962   8664  10191    154    205   -645       O  
ATOM   2425  CB  SER A1318      15.491  46.273  -2.342  1.00 54.84           C  
ANISOU 2425  CB  SER A1318     6588   6427   7823    -20    331   -721       C  
ATOM   2426  OG  SER A1318      15.411  45.700  -1.046  1.00 41.00           O  
ANISOU 2426  OG  SER A1318     4746   4777   6053    -34    274   -713       O  
ATOM   2427  N   ARG A1319      13.533  44.199  -3.770  1.00 58.06           N  
ANISOU 2427  N   ARG A1319     7070   6695   8293    229    219   -608       N  
ATOM   2428  CA  ARG A1319      12.897  42.892  -3.648  1.00 66.93           C  
ANISOU 2428  CA  ARG A1319     8161   7828   9443    310    143   -556       C  
ATOM   2429  C   ARG A1319      13.483  42.058  -2.517  1.00 67.20           C  
ANISOU 2429  C   ARG A1319     8078   7990   9464    289    105   -534       C  
ATOM   2430  O   ARG A1319      12.810  41.143  -2.029  1.00 71.20           O  
ANISOU 2430  O   ARG A1319     8555   8510   9987    338     49   -497       O  
ATOM   2431  CB  ARG A1319      12.925  42.112  -4.962  1.00 76.03           C  
ANISOU 2431  CB  ARG A1319     9356   8917  10616    401    125   -520       C  
ATOM   2432  CG  ARG A1319      14.242  41.590  -5.483  1.00 79.47           C  
ANISOU 2432  CG  ARG A1319     9749   9404  11042    409    142   -500       C  
ATOM   2433  CD  ARG A1319      14.033  41.203  -6.941  1.00 79.20           C  
ANISOU 2433  CD  ARG A1319     9800   9269  11021    500    139   -478       C  
ATOM   2434  NE  ARG A1319      15.078  40.339  -7.476  1.00 80.88           N  
ANISOU 2434  NE  ARG A1319     9978   9524  11229    540    141   -443       N  
ATOM   2435  CZ  ARG A1319      14.828  39.143  -8.005  1.00 88.54           C  
ANISOU 2435  CZ  ARG A1319    10961  10466  12214    630     90   -400       C  
ATOM   2436  NH1 ARG A1319      13.577  38.698  -8.077  1.00 94.30           N  
ANISOU 2436  NH1 ARG A1319    11733  11127  12969    680     30   -392       N  
ATOM   2437  NH2 ARG A1319      15.816  38.396  -8.474  1.00 89.39           N  
ANISOU 2437  NH2 ARG A1319    11041  10611  12313    671     99   -367       N  
ATOM   2438  N   GLU A1320      14.712  42.348  -2.088  1.00 71.60           N  
ANISOU 2438  N   GLU A1320     8568   8644   9992    220    133   -555       N  
ATOM   2439  CA  GLU A1320      15.249  41.646  -0.929  1.00 62.50           C  
ANISOU 2439  CA  GLU A1320     7306   7623   8819    203     95   -536       C  
ATOM   2440  C   GLU A1320      14.465  42.015   0.324  1.00 52.43           C  
ANISOU 2440  C   GLU A1320     6021   6371   7527    166     78   -557       C  
ATOM   2441  O   GLU A1320      14.141  41.143   1.145  1.00 52.98           O  
ANISOU 2441  O   GLU A1320     6039   6496   7595    201     31   -520       O  
ATOM   2442  CB  GLU A1320      16.736  41.986  -0.759  1.00 61.18           C  
ANISOU 2442  CB  GLU A1320     7064   7560   8623    132    128   -561       C  
ATOM   2443  CG  GLU A1320      17.658  41.395  -1.836  1.00 64.71           C  
ANISOU 2443  CG  GLU A1320     7494   8010   9082    179    143   -528       C  
ATOM   2444  CD  GLU A1320      17.675  42.209  -3.130  1.00 74.59           C  
ANISOU 2444  CD  GLU A1320     8842   9148  10349    175    206   -550       C  
ATOM   2445  OE1 GLU A1320      17.104  43.321  -3.155  1.00 83.99           O  
ANISOU 2445  OE1 GLU A1320    10107  10266  11539    126    242   -596       O  
ATOM   2446  OE2 GLU A1320      18.253  41.735  -4.131  1.00 72.65           O  
ANISOU 2446  OE2 GLU A1320     8606   8883  10114    228    223   -520       O  
ATOM   2447  N   PHE A1321      14.130  43.302   0.470  1.00 51.06           N  
ANISOU 2447  N   PHE A1321     5908   6151   7341    100    123   -612       N  
ATOM   2448  CA  PHE A1321      13.311  43.738   1.595  1.00 52.79           C  
ANISOU 2448  CA  PHE A1321     6136   6381   7543     71    115   -632       C  
ATOM   2449  C   PHE A1321      11.888  43.196   1.498  1.00 55.32           C  
ANISOU 2449  C   PHE A1321     6499   6622   7900    153     82   -591       C  
ATOM   2450  O   PHE A1321      11.287  42.834   2.517  1.00 63.41           O  
ANISOU 2450  O   PHE A1321     7491   7684   8919    164     53   -574       O  
ATOM   2451  CB  PHE A1321      13.291  45.263   1.700  1.00 55.34           C  
ANISOU 2451  CB  PHE A1321     6525   6660   7842    -15    177   -701       C  
ATOM   2452  CG  PHE A1321      12.529  45.763   2.894  1.00 64.84           C  
ANISOU 2452  CG  PHE A1321     7741   7876   9019    -45    175   -725       C  
ATOM   2453  CD1 PHE A1321      12.922  45.411   4.178  1.00 73.72           C  
ANISOU 2453  CD1 PHE A1321     8784   9122  10106    -77    142   -727       C  
ATOM   2454  CD2 PHE A1321      11.398  46.544   2.734  1.00 66.04           C  
ANISOU 2454  CD2 PHE A1321     7989   7922   9180    -31    206   -741       C  
ATOM   2455  CE1 PHE A1321      12.213  45.848   5.288  1.00 73.73           C  
ANISOU 2455  CE1 PHE A1321     8804   9134  10077    -97    143   -747       C  
ATOM   2456  CE2 PHE A1321      10.686  46.986   3.832  1.00 70.06           C  
ANISOU 2456  CE2 PHE A1321     8514   8442   9663    -51    210   -759       C  
ATOM   2457  CZ  PHE A1321      11.093  46.639   5.113  1.00 74.59           C  
ANISOU 2457  CZ  PHE A1321     9010   9132  10197    -85    179   -762       C  
ATOM   2458  N   VAL A1322      11.331  43.126   0.284  1.00 46.88           N  
ANISOU 2458  N   VAL A1322     5499   5445   6868    212     84   -576       N  
ATOM   2459  CA  VAL A1322       9.985  42.579   0.136  1.00 39.08           C  
ANISOU 2459  CA  VAL A1322     4542   4387   5921    286     46   -540       C  
ATOM   2460  C   VAL A1322       9.970  41.101   0.503  1.00 47.94           C  
ANISOU 2460  C   VAL A1322     5590   5562   7064    340    -12   -482       C  
ATOM   2461  O   VAL A1322       9.022  40.609   1.136  1.00 51.00           O  
ANISOU 2461  O   VAL A1322     5960   5944   7472    370    -42   -453       O  
ATOM   2462  CB  VAL A1322       9.487  42.808  -1.300  1.00 36.77           C  
ANISOU 2462  CB  VAL A1322     4339   3975   5658    339     55   -541       C  
ATOM   2463  CG1 VAL A1322       8.231  41.992  -1.572  1.00 38.06           C  
ANISOU 2463  CG1 VAL A1322     4514   4078   5870    420      1   -500       C  
ATOM   2464  CG2 VAL A1322       9.252  44.290  -1.536  1.00 39.85           C  
ANISOU 2464  CG2 VAL A1322     4813   4301   6028    297    118   -592       C  
ATOM   2465  N   ARG A1323      11.045  40.384   0.166  1.00 52.06           N  
ANISOU 2465  N   ARG A1323     6066   6138   7578    353    -24   -461       N  
ATOM   2466  CA  ARG A1323      11.172  39.002   0.603  1.00 54.56           C  
ANISOU 2466  CA  ARG A1323     6314   6512   7905    402    -71   -405       C  
ATOM   2467  C   ARG A1323      11.287  38.934   2.122  1.00 65.60           C  
ANISOU 2467  C   ARG A1323     7643   8015   9269    366    -78   -402       C  
ATOM   2468  O   ARG A1323      10.790  37.989   2.748  1.00 73.63           O  
ANISOU 2468  O   ARG A1323     8624   9051  10299    409   -111   -356       O  
ATOM   2469  CB  ARG A1323      12.388  38.355  -0.040  1.00 48.40           C  
ANISOU 2469  CB  ARG A1323     5501   5774   7114    426    -72   -385       C  
ATOM   2470  CG  ARG A1323      12.668  36.942   0.428  1.00 54.32           C  
ANISOU 2470  CG  ARG A1323     6184   6588   7867    480   -113   -326       C  
ATOM   2471  CD  ARG A1323      13.820  36.408  -0.360  1.00 61.88           C  
ANISOU 2471  CD  ARG A1323     7123   7575   8814    511   -106   -307       C  
ATOM   2472  NE  ARG A1323      14.982  37.214  -0.004  1.00 70.95           N  
ANISOU 2472  NE  ARG A1323     8220   8820   9919    439    -70   -344       N  
ATOM   2473  CZ  ARG A1323      16.179  37.113  -0.563  1.00 78.24           C  
ANISOU 2473  CZ  ARG A1323     9111   9790  10826    441    -48   -340       C  
ATOM   2474  NH1 ARG A1323      16.397  36.228  -1.526  1.00 71.14           N  
ANISOU 2474  NH1 ARG A1323     8235   8849   9946    519    -56   -299       N  
ATOM   2475  NH2 ARG A1323      17.157  37.909  -0.149  1.00 90.95           N  
ANISOU 2475  NH2 ARG A1323    10665  11490  12401    362    -17   -379       N  
ATOM   2476  N   GLU A1324      11.942  39.932   2.730  1.00 61.28           N  
ANISOU 2476  N   GLU A1324     7078   7532   8674    287    -45   -452       N  
ATOM   2477  CA  GLU A1324      12.004  39.986   4.187  1.00 54.94           C  
ANISOU 2477  CA  GLU A1324     6220   6827   7829    252    -53   -457       C  
ATOM   2478  C   GLU A1324      10.611  40.153   4.782  1.00 60.13           C  
ANISOU 2478  C   GLU A1324     6915   7428   8504    269    -55   -449       C  
ATOM   2479  O   GLU A1324      10.310  39.595   5.847  1.00 66.33           O  
ANISOU 2479  O   GLU A1324     7657   8269   9275    288    -74   -419       O  
ATOM   2480  CB  GLU A1324      12.895  41.159   4.607  1.00 69.13           C  
ANISOU 2480  CB  GLU A1324     8005   8687   9573    155    -18   -525       C  
ATOM   2481  CG  GLU A1324      13.517  41.098   5.991  1.00 87.95           C  
ANISOU 2481  CG  GLU A1324    10311  11208  11897    115    -35   -536       C  
ATOM   2482  CD  GLU A1324      14.576  40.023   6.099  1.00108.65           C  
ANISOU 2482  CD  GLU A1324    12840  13939  14503    150    -69   -495       C  
ATOM   2483  OE1 GLU A1324      15.329  39.841   5.116  1.00119.32           O  
ANISOU 2483  OE1 GLU A1324    14180  15282  15872    158    -60   -489       O  
ATOM   2484  OE2 GLU A1324      14.671  39.377   7.165  1.00111.04           O  
ANISOU 2484  OE2 GLU A1324    13084  14334  14771    175   -100   -466       O  
ATOM   2485  N   LEU A1325       9.756  40.946   4.123  1.00 54.05           N  
ANISOU 2485  N   LEU A1325     6226   6549   7763    267    -30   -475       N  
ATOM   2486  CA  LEU A1325       8.389  41.137   4.605  1.00 47.63           C  
ANISOU 2486  CA  LEU A1325     5446   5680   6971    289    -28   -464       C  
ATOM   2487  C   LEU A1325       7.555  39.872   4.462  1.00 45.92           C  
ANISOU 2487  C   LEU A1325     5207   5428   6811    367    -70   -399       C  
ATOM   2488  O   LEU A1325       6.803  39.510   5.375  1.00 52.54           O  
ANISOU 2488  O   LEU A1325     6022   6283   7658    385    -77   -369       O  
ATOM   2489  CB  LEU A1325       7.731  42.309   3.884  1.00 42.36           C  
ANISOU 2489  CB  LEU A1325     4869   4909   6316    274     10   -506       C  
ATOM   2490  CG  LEU A1325       8.502  43.591   4.165  1.00 45.93           C  
ANISOU 2490  CG  LEU A1325     5348   5390   6713    188     60   -573       C  
ATOM   2491  CD1 LEU A1325       7.876  44.776   3.491  1.00 58.51           C  
ANISOU 2491  CD1 LEU A1325     7041   6878   8313    179    107   -611       C  
ATOM   2492  CD2 LEU A1325       8.498  43.793   5.652  1.00 36.62           C  
ANISOU 2492  CD2 LEU A1325     4133   4293   5486    149     64   -585       C  
ATOM   2493  N   TYR A1326       7.674  39.190   3.322  1.00 39.06           N  
ANISOU 2493  N   TYR A1326     4350   4508   5982    412    -95   -376       N  
ATOM   2494  CA  TYR A1326       6.875  37.991   3.097  1.00 39.24           C  
ANISOU 2494  CA  TYR A1326     4359   4487   6064    479   -136   -320       C  
ATOM   2495  C   TYR A1326       7.200  36.909   4.114  1.00 46.13           C  
ANISOU 2495  C   TYR A1326     5159   5445   6925    497   -155   -271       C  
ATOM   2496  O   TYR A1326       6.316  36.144   4.514  1.00 67.65           O  
ANISOU 2496  O   TYR A1326     7868   8146   9691    534   -173   -227       O  
ATOM   2497  CB  TYR A1326       7.131  37.449   1.694  1.00 41.27           C  
ANISOU 2497  CB  TYR A1326     4647   4680   6353    522   -161   -311       C  
ATOM   2498  CG  TYR A1326       6.475  38.195   0.553  1.00 41.71           C  
ANISOU 2498  CG  TYR A1326     4782   4631   6435    534   -155   -342       C  
ATOM   2499  CD1 TYR A1326       5.281  38.866   0.720  1.00 30.31           C  
ANISOU 2499  CD1 TYR A1326     3371   3133   5012    534   -146   -356       C  
ATOM   2500  CD2 TYR A1326       7.073  38.224  -0.703  1.00 44.85           C  
ANISOU 2500  CD2 TYR A1326     5225   4986   6831    554   -156   -356       C  
ATOM   2501  CE1 TYR A1326       4.697  39.548  -0.330  1.00 35.74           C  
ANISOU 2501  CE1 TYR A1326     4132   3730   5718    555   -142   -382       C  
ATOM   2502  CE2 TYR A1326       6.500  38.904  -1.754  1.00 34.85           C  
ANISOU 2502  CE2 TYR A1326     4036   3626   5579    574   -150   -383       C  
ATOM   2503  CZ  TYR A1326       5.315  39.563  -1.564  1.00 35.36           C  
ANISOU 2503  CZ  TYR A1326     4131   3641   5664    575   -145   -396       C  
ATOM   2504  OH  TYR A1326       4.750  40.235  -2.619  1.00 45.36           O  
ANISOU 2504  OH  TYR A1326     5476   4819   6940    605   -141   -420       O  
ATOM   2505  N   GLY A1327       8.448  36.850   4.564  1.00 45.35           N  
ANISOU 2505  N   GLY A1327     5014   5446   6769    473   -149   -278       N  
ATOM   2506  CA  GLY A1327       8.908  35.895   5.545  1.00 60.39           C  
ANISOU 2506  CA  GLY A1327     6852   7445   8648    496   -164   -232       C  
ATOM   2507  C   GLY A1327       8.730  36.279   6.989  1.00 64.05           C  
ANISOU 2507  C   GLY A1327     7287   7984   9065    467   -148   -238       C  
ATOM   2508  O   GLY A1327       9.126  35.512   7.869  1.00 65.25           O  
ANISOU 2508  O   GLY A1327     7386   8220   9186    492   -159   -199       O  
ATOM   2509  N   SER A1328       8.148  37.433   7.271  1.00 64.63           N  
ANISOU 2509  N   SER A1328     7399   8028   9127    422   -121   -283       N  
ATOM   2510  CA  SER A1328       7.966  37.869   8.647  1.00 66.09           C  
ANISOU 2510  CA  SER A1328     7569   8281   9262    396   -103   -293       C  
ATOM   2511  C   SER A1328       6.503  38.014   9.020  1.00 72.80           C  
ANISOU 2511  C   SER A1328     8452   9059  10151    418    -86   -274       C  
ATOM   2512  O   SER A1328       6.116  37.677  10.141  1.00 84.90           O  
ANISOU 2512  O   SER A1328     9960  10636  11665    436    -79   -242       O  
ATOM   2513  CB  SER A1328       8.673  39.216   8.862  1.00 63.20           C  
ANISOU 2513  CB  SER A1328     7222   7958   8833    315    -77   -370       C  
ATOM   2514  OG  SER A1328      10.013  39.178   8.404  1.00 69.10           O  
ANISOU 2514  OG  SER A1328     7934   8767   9553    288    -88   -391       O  
ATOM   2515  N   VAL A1329       5.674  38.485   8.091  1.00 55.38           N  
ANISOU 2515  N   VAL A1329     6298   6745   7999    422    -78   -289       N  
ATOM   2516  CA  VAL A1329       4.273  38.714   8.378  1.00 30.46           C  
ANISOU 2516  CA  VAL A1329     3166   3523   4883    443    -61   -272       C  
ATOM   2517  C   VAL A1329       3.541  37.384   8.528  1.00 32.87           C  
ANISOU 2517  C   VAL A1329     3431   3806   5251    502    -84   -199       C  
ATOM   2518  O   VAL A1329       3.993  36.330   8.070  1.00 43.94           O  
ANISOU 2518  O   VAL A1329     4806   5212   6678    531   -116   -166       O  
ATOM   2519  CB  VAL A1329       3.654  39.568   7.264  1.00 31.54           C  
ANISOU 2519  CB  VAL A1329     3368   3558   5058    439    -51   -308       C  
ATOM   2520  CG1 VAL A1329       4.444  40.845   7.092  1.00 31.73           C  
ANISOU 2520  CG1 VAL A1329     3438   3597   5022    378    -19   -378       C  
ATOM   2521  CG2 VAL A1329       3.606  38.781   5.970  1.00 32.90           C  
ANISOU 2521  CG2 VAL A1329     3543   3667   5292    478    -91   -287       C  
ATOM   2522  N   ASP A1330       2.391  37.434   9.193  1.00 49.35           N  
ANISOU 2522  N   ASP A1330     5518   5867   7366    520    -62   -173       N  
ATOM   2523  CA  ASP A1330       1.579  36.229   9.317  1.00 61.29           C  
ANISOU 2523  CA  ASP A1330     6992   7346   8948    568    -76   -105       C  
ATOM   2524  C   ASP A1330       0.747  35.976   8.057  1.00 57.21           C  
ANISOU 2524  C   ASP A1330     6493   6724   8522    590   -106   -101       C  
ATOM   2525  O   ASP A1330       0.649  34.830   7.600  1.00 52.43           O  
ANISOU 2525  O   ASP A1330     5863   6086   7971    620   -139    -61       O  
ATOM   2526  CB  ASP A1330       0.709  36.303  10.571  1.00 62.25           C  
ANISOU 2526  CB  ASP A1330     7099   7487   9067    581    -36    -72       C  
ATOM   2527  CG  ASP A1330       1.530  36.363  11.839  1.00 62.02           C  
ANISOU 2527  CG  ASP A1330     7054   7567   8946    570    -16    -71       C  
ATOM   2528  OD1 ASP A1330       2.227  35.363  12.124  1.00 62.45           O  
ANISOU 2528  OD1 ASP A1330     7070   7674   8983    592    -35    -34       O  
ATOM   2529  OD2 ASP A1330       1.470  37.395  12.546  1.00 64.56           O  
ANISOU 2529  OD2 ASP A1330     7403   7919   9208    543     18   -108       O  
ATOM   2530  N   PHE A1331       0.157  37.024   7.473  1.00 43.53           N  
ANISOU 2530  N   PHE A1331     4804   4934   6801    579    -96   -142       N  
ATOM   2531  CA  PHE A1331      -0.756  36.875   6.347  1.00 32.92           C  
ANISOU 2531  CA  PHE A1331     3476   3497   5537    606   -127   -140       C  
ATOM   2532  C   PHE A1331      -0.529  37.971   5.321  1.00 41.62           C  
ANISOU 2532  C   PHE A1331     4642   4556   6615    593   -126   -200       C  
ATOM   2533  O   PHE A1331      -0.103  39.082   5.651  1.00 52.68           O  
ANISOU 2533  O   PHE A1331     6079   5985   7952    560    -87   -242       O  
ATOM   2534  CB  PHE A1331      -2.230  36.934   6.748  1.00 37.03           C  
ANISOU 2534  CB  PHE A1331     3974   3976   6118    627   -111   -111       C  
ATOM   2535  CG  PHE A1331      -2.648  35.881   7.712  1.00 49.89           C  
ANISOU 2535  CG  PHE A1331     5544   5630   7783    642   -101    -47       C  
ATOM   2536  CD1 PHE A1331      -2.458  36.044   9.071  1.00 43.65           C  
ANISOU 2536  CD1 PHE A1331     4738   4910   6936    634    -54    -29       C  
ATOM   2537  CD2 PHE A1331      -3.268  34.731   7.254  1.00 61.35           C  
ANISOU 2537  CD2 PHE A1331     6959   7030   9323    665   -138     -6       C  
ATOM   2538  CE1 PHE A1331      -2.867  35.067   9.955  1.00 44.23           C  
ANISOU 2538  CE1 PHE A1331     4762   5001   7040    655    -38     36       C  
ATOM   2539  CE2 PHE A1331      -3.678  33.752   8.128  1.00 55.72           C  
ANISOU 2539  CE2 PHE A1331     6194   6330   8647    678   -121     56       C  
ATOM   2540  CZ  PHE A1331      -3.477  33.914   9.482  1.00 47.79           C  
ANISOU 2540  CZ  PHE A1331     5177   5396   7586    676    -68     80       C  
ATOM   2541  N   VAL A1332      -0.796  37.629   4.064  1.00 40.62           N  
ANISOU 2541  N   VAL A1332     4534   4361   6540    619   -170   -204       N  
ATOM   2542  CA  VAL A1332      -0.737  38.576   2.960  1.00 39.06           C  
ANISOU 2542  CA  VAL A1332     4404   4110   6328    622   -171   -253       C  
ATOM   2543  C   VAL A1332      -2.129  38.689   2.368  1.00 38.56           C  
ANISOU 2543  C   VAL A1332     4348   3972   6331    661   -194   -247       C  
ATOM   2544  O   VAL A1332      -2.718  37.681   1.970  1.00 38.35           O  
ANISOU 2544  O   VAL A1332     4287   3911   6374    689   -243   -217       O  
ATOM   2545  CB  VAL A1332       0.272  38.138   1.889  1.00 50.88           C  
ANISOU 2545  CB  VAL A1332     5926   5594   7813    628   -203   -268       C  
ATOM   2546  CG1 VAL A1332       0.147  39.006   0.639  1.00 43.74           C  
ANISOU 2546  CG1 VAL A1332     5096   4620   6901    645   -205   -310       C  
ATOM   2547  CG2 VAL A1332       1.665  38.217   2.447  1.00 69.86           C  
ANISOU 2547  CG2 VAL A1332     8317   8079  10146    588   -176   -279       C  
ATOM   2548  N   ILE A1333      -2.628  39.912   2.268  1.00 43.38           N  
ANISOU 2548  N   ILE A1333     5006   4557   6921    665   -159   -278       N  
ATOM   2549  CA  ILE A1333      -3.963  40.199   1.773  1.00 48.31           C  
ANISOU 2549  CA  ILE A1333     5635   5122   7599    708   -176   -273       C  
ATOM   2550  C   ILE A1333      -3.841  40.627   0.318  1.00 52.50           C  
ANISOU 2550  C   ILE A1333     6234   5590   8122    737   -204   -310       C  
ATOM   2551  O   ILE A1333      -3.088  41.556  -0.007  1.00 45.93           O  
ANISOU 2551  O   ILE A1333     5472   4754   7227    722   -166   -349       O  
ATOM   2552  CB  ILE A1333      -4.631  41.293   2.621  1.00 45.33           C  
ANISOU 2552  CB  ILE A1333     5272   4755   7196    706   -113   -279       C  
ATOM   2553  CG1 ILE A1333      -4.656  40.869   4.094  1.00 43.10           C  
ANISOU 2553  CG1 ILE A1333     4930   4536   6909    681    -81   -242       C  
ATOM   2554  CG2 ILE A1333      -6.044  41.550   2.130  1.00 42.71           C  
ANISOU 2554  CG2 ILE A1333     4934   4370   6923    759   -130   -268       C  
ATOM   2555  CD1 ILE A1333      -5.159  41.924   5.038  1.00 33.85           C  
ANISOU 2555  CD1 ILE A1333     3781   3381   5699    678    -12   -249       C  
ATOM   2556  N   ILE A1334      -4.580  39.947  -0.554  1.00 56.60           N  
ANISOU 2556  N   ILE A1334     6737   6061   8707    779   -269   -298       N  
ATOM   2557  CA  ILE A1334      -4.556  40.181  -1.996  1.00 60.04           C  
ANISOU 2557  CA  ILE A1334     7238   6437   9138    819   -307   -328       C  
ATOM   2558  C   ILE A1334      -5.996  40.367  -2.453  1.00 61.59           C  
ANISOU 2558  C   ILE A1334     7422   6591   9390    870   -343   -324       C  
ATOM   2559  O   ILE A1334      -6.616  39.413  -2.952  1.00 51.76           O  
ANISOU 2559  O   ILE A1334     6135   5321   8212    892   -414   -309       O  
ATOM   2560  CB  ILE A1334      -3.890  39.008  -2.734  1.00 53.20           C  
ANISOU 2560  CB  ILE A1334     6367   5557   8290    823   -366   -323       C  
ATOM   2561  CG1 ILE A1334      -2.597  38.606  -2.020  1.00 48.79           C  
ANISOU 2561  CG1 ILE A1334     5790   5059   7689    776   -334   -313       C  
ATOM   2562  CG2 ILE A1334      -3.584  39.388  -4.166  1.00 42.20           C  
ANISOU 2562  CG2 ILE A1334     5059   4109   6868    864   -391   -358       C  
ATOM   2563  CD1 ILE A1334      -1.984  37.351  -2.532  1.00 30.68           C  
ANISOU 2563  CD1 ILE A1334     3483   2758   5415    784   -383   -297       C  
ATOM   2564  N   PRO A1335      -6.592  41.550  -2.245  1.00 72.18           N  
ANISOU 2564  N   PRO A1335     8794   7924  10706    890   -295   -336       N  
ATOM   2565  CA  PRO A1335      -8.027  41.703  -2.509  1.00 69.02           C  
ANISOU 2565  CA  PRO A1335     8364   7498  10361    942   -326   -324       C  
ATOM   2566  C   PRO A1335      -8.325  42.161  -3.931  1.00 59.45           C  
ANISOU 2566  C   PRO A1335     7221   6231   9138   1006   -368   -354       C  
ATOM   2567  O   PRO A1335      -9.181  43.026  -4.143  1.00 56.73           O  
ANISOU 2567  O   PRO A1335     6899   5868   8788   1056   -353   -360       O  
ATOM   2568  CB  PRO A1335      -8.438  42.755  -1.477  1.00 62.86           C  
ANISOU 2568  CB  PRO A1335     7589   6743   9551    938   -243   -317       C  
ATOM   2569  CG  PRO A1335      -7.228  43.655  -1.413  1.00 59.55           C  
ANISOU 2569  CG  PRO A1335     7260   6327   9040    905   -178   -353       C  
ATOM   2570  CD  PRO A1335      -6.015  42.774  -1.657  1.00 64.00           C  
ANISOU 2570  CD  PRO A1335     7818   6907   9593    864   -208   -358       C  
ATOM   2571  N   SER A1336      -7.628  41.583  -4.908  1.00 50.26           N  
ANISOU 2571  N   SER A1336     6094   5039   7964   1012   -418   -372       N  
ATOM   2572  CA  SER A1336      -7.732  42.051  -6.285  1.00 52.95           C  
ANISOU 2572  CA  SER A1336     6516   5326   8276   1076   -452   -403       C  
ATOM   2573  C   SER A1336      -9.139  41.841  -6.838  1.00 59.09           C  
ANISOU 2573  C   SER A1336     7252   6083   9115   1136   -526   -398       C  
ATOM   2574  O   SER A1336      -9.747  40.788  -6.641  1.00 49.40           O  
ANISOU 2574  O   SER A1336     5936   4869   7967   1121   -588   -377       O  
ATOM   2575  CB  SER A1336      -6.705  41.326  -7.151  1.00 47.66           C  
ANISOU 2575  CB  SER A1336     5888   4634   7586   1071   -490   -419       C  
ATOM   2576  OG  SER A1336      -5.469  41.211  -6.469  1.00 42.80           O  
ANISOU 2576  OG  SER A1336     5274   4055   6934   1008   -435   -415       O  
ATOM   2577  N   TYR A1337      -9.645  42.840  -7.570  1.00 67.55           N  
ANISOU 2577  N   TYR A1337     8390   7124  10150   1206   -520   -417       N  
ATOM   2578  CA  TYR A1337     -10.806  42.620  -8.432  1.00 67.64           C  
ANISOU 2578  CA  TYR A1337     8380   7133  10187   1261   -600   -416       C  
ATOM   2579  C   TYR A1337     -10.462  41.783  -9.663  1.00 72.06           C  
ANISOU 2579  C   TYR A1337     8978   7686  10715   1259   -673   -430       C  
ATOM   2580  O   TYR A1337     -11.324  41.076 -10.196  1.00 81.16           O  
ANISOU 2580  O   TYR A1337    10082   8848  11908   1272   -758   -429       O  
ATOM   2581  CB  TYR A1337     -11.368  43.962  -8.904  1.00 67.16           C  
ANISOU 2581  CB  TYR A1337     8393   7063  10061   1331   -558   -424       C  
ATOM   2582  CG  TYR A1337     -12.083  44.798  -7.864  1.00 63.54           C  
ANISOU 2582  CG  TYR A1337     7896   6611   9635   1353   -497   -408       C  
ATOM   2583  CD1 TYR A1337     -11.368  45.674  -7.055  1.00 63.31           C  
ANISOU 2583  CD1 TYR A1337     7922   6582   9553   1319   -389   -411       C  
ATOM   2584  CD2 TYR A1337     -13.459  44.734  -7.702  1.00 64.38           C  
ANISOU 2584  CD2 TYR A1337     7918   6746   9800   1391   -534   -385       C  
ATOM   2585  CE1 TYR A1337     -11.999  46.460  -6.112  1.00 67.64           C  
ANISOU 2585  CE1 TYR A1337     8451   7151  10098   1326   -318   -392       C  
ATOM   2586  CE2 TYR A1337     -14.101  45.514  -6.755  1.00 67.68           C  
ANISOU 2586  CE2 TYR A1337     8306   7179  10232   1411   -465   -364       C  
ATOM   2587  CZ  TYR A1337     -13.363  46.376  -5.964  1.00 77.82           C  
ANISOU 2587  CZ  TYR A1337     9658   8462  11448   1376   -353   -366       C  
ATOM   2588  OH  TYR A1337     -13.991  47.162  -5.023  1.00 91.67           O  
ANISOU 2588  OH  TYR A1337    11397  10236  13197   1390   -276   -342       O  
ATOM   2589  N   PHE A1338      -9.214  41.858 -10.120  1.00 78.55           N  
ANISOU 2589  N   PHE A1338     9886   8491  11468   1244   -639   -445       N  
ATOM   2590  CA  PHE A1338      -8.771  41.311 -11.402  1.00 83.14           C  
ANISOU 2590  CA  PHE A1338    10532   9063  11996   1255   -686   -458       C  
ATOM   2591  C   PHE A1338      -7.313  40.925 -11.217  1.00 87.52           C  
ANISOU 2591  C   PHE A1338    11117   9609  12527   1211   -648   -460       C  
ATOM   2592  O   PHE A1338      -6.475  41.792 -10.945  1.00 89.20           O  
ANISOU 2592  O   PHE A1338    11386   9811  12696   1205   -567   -469       O  
ATOM   2593  CB  PHE A1338      -8.947  42.333 -12.532  1.00101.36           C  
ANISOU 2593  CB  PHE A1338    12943  11358  14213   1318   -664   -469       C  
ATOM   2594  CG  PHE A1338      -8.262  41.962 -13.826  1.00118.41           C  
ANISOU 2594  CG  PHE A1338    15184  13504  16303   1331   -685   -481       C  
ATOM   2595  CD1 PHE A1338      -8.719  40.907 -14.605  1.00121.32           C  
ANISOU 2595  CD1 PHE A1338    15530  13876  16690   1338   -785   -489       C  
ATOM   2596  CD2 PHE A1338      -7.165  42.687 -14.268  1.00123.61           C  
ANISOU 2596  CD2 PHE A1338    15943  14142  16880   1336   -603   -484       C  
ATOM   2597  CE1 PHE A1338      -8.090  40.583 -15.801  1.00118.82           C  
ANISOU 2597  CE1 PHE A1338    15294  13546  16306   1354   -801   -500       C  
ATOM   2598  CE2 PHE A1338      -6.530  42.366 -15.458  1.00123.34           C  
ANISOU 2598  CE2 PHE A1338    15982  14097  16786   1350   -613   -489       C  
ATOM   2599  CZ  PHE A1338      -6.993  41.313 -16.226  1.00120.25           C  
ANISOU 2599  CZ  PHE A1338    15571  13713  16406   1362   -711   -496       C  
ATOM   2600  N   GLU A1339      -7.013  39.639 -11.367  1.00 89.01           N  
ANISOU 2600  N   GLU A1339    11270   9802  12748   1181   -705   -455       N  
ATOM   2601  CA  GLU A1339      -5.668  39.112 -11.123  1.00 85.75           C  
ANISOU 2601  CA  GLU A1339    10871   9387  12323   1144   -676   -451       C  
ATOM   2602  C   GLU A1339      -5.383  37.947 -12.053  1.00 82.85           C  
ANISOU 2602  C   GLU A1339    10526   9014  11941   1144   -738   -452       C  
ATOM   2603  O   GLU A1339      -5.575  36.779 -11.696  1.00 88.11           O  
ANISOU 2603  O   GLU A1339    11125   9682  12670   1115   -789   -439       O  
ATOM   2604  CB  GLU A1339      -5.478  38.704  -9.661  1.00 86.09           C  
ANISOU 2604  CB  GLU A1339    10819   9445  12445   1098   -657   -433       C  
ATOM   2605  CG  GLU A1339      -4.011  38.579  -9.244  1.00 88.59           C  
ANISOU 2605  CG  GLU A1339    11150   9766  12743   1069   -606   -434       C  
ATOM   2606  CD  GLU A1339      -3.243  39.888  -9.299  1.00 94.90           C  
ANISOU 2606  CD  GLU A1339    12024  10569  13464   1065   -518   -453       C  
ATOM   2607  OE1 GLU A1339      -2.408  40.051 -10.217  1.00104.92           O  
ANISOU 2607  OE1 GLU A1339    13373  11808  14683   1091   -506   -471       O  
ATOM   2608  OE2 GLU A1339      -3.456  40.744  -8.416  1.00 89.63           O  
ANISOU 2608  OE2 GLU A1339    11339   9932  12786   1035   -457   -451       O  
ATOM   2609  N   PRO A1340      -4.934  38.228 -13.278  1.00 71.18           N  
ANISOU 2609  N   PRO A1340     9144   7522  10378   1178   -729   -464       N  
ATOM   2610  CA  PRO A1340      -4.722  37.130 -14.229  1.00 58.45           C  
ANISOU 2610  CA  PRO A1340     7560   5900   8748   1184   -788   -467       C  
ATOM   2611  C   PRO A1340      -3.744  36.103 -13.704  1.00 53.42           C  
ANISOU 2611  C   PRO A1340     6893   5266   8136   1146   -781   -451       C  
ATOM   2612  O   PRO A1340      -3.887  34.914 -14.019  1.00 48.29           O  
ANISOU 2612  O   PRO A1340     6229   4606   7512   1137   -843   -449       O  
ATOM   2613  CB  PRO A1340      -4.170  37.840 -15.473  1.00 63.17           C  
ANISOU 2613  CB  PRO A1340     8272   6485   9245   1227   -749   -477       C  
ATOM   2614  CG  PRO A1340      -3.656  39.152 -14.981  1.00 67.98           C  
ANISOU 2614  CG  PRO A1340     8910   7093   9824   1228   -653   -476       C  
ATOM   2615  CD  PRO A1340      -4.540  39.532 -13.838  1.00 75.06           C  
ANISOU 2615  CD  PRO A1340     9728   8003  10789   1212   -657   -474       C  
ATOM   2616  N   PHE A1341      -2.776  36.499 -12.897  1.00 66.03           N  
ANISOU 2616  N   PHE A1341     8481   6874   9734   1125   -712   -442       N  
ATOM   2617  CA  PHE A1341      -1.768  35.487 -12.621  1.00 71.11           C  
ANISOU 2617  CA  PHE A1341     9108   7523  10390   1105   -709   -425       C  
ATOM   2618  C   PHE A1341      -1.548  35.263 -11.135  1.00 79.42           C  
ANISOU 2618  C   PHE A1341    10067   8595  11516   1066   -689   -408       C  
ATOM   2619  O   PHE A1341      -1.291  34.125 -10.733  1.00 90.67           O  
ANISOU 2619  O   PHE A1341    11446  10024  12981   1049   -714   -386       O  
ATOM   2620  CB  PHE A1341      -0.441  35.892 -13.281  1.00 65.76           C  
ANISOU 2620  CB  PHE A1341     8511   6840   9636   1125   -648   -430       C  
ATOM   2621  CG  PHE A1341      -0.543  36.083 -14.766  1.00 72.06           C  
ANISOU 2621  CG  PHE A1341     9403   7618  10357   1167   -656   -440       C  
ATOM   2622  CD1 PHE A1341      -0.716  34.997 -15.607  1.00 65.84           C  
ANISOU 2622  CD1 PHE A1341     8639   6820   9557   1180   -715   -438       C  
ATOM   2623  CD2 PHE A1341      -0.478  37.352 -15.322  1.00 73.51           C  
ANISOU 2623  CD2 PHE A1341     9655   7791  10483   1193   -601   -452       C  
ATOM   2624  CE1 PHE A1341      -0.820  35.173 -16.972  1.00 58.96           C  
ANISOU 2624  CE1 PHE A1341     7851   5932   8618   1221   -724   -449       C  
ATOM   2625  CE2 PHE A1341      -0.579  37.533 -16.688  1.00 62.99           C  
ANISOU 2625  CE2 PHE A1341     8406   6442   9083   1234   -604   -458       C  
ATOM   2626  CZ  PHE A1341      -0.752  36.444 -17.512  1.00 59.56           C  
ANISOU 2626  CZ  PHE A1341     7989   6002   8637   1249   -668   -457       C  
ATOM   2627  N   GLY A1342      -1.615  36.311 -10.317  1.00 72.83           N  
ANISOU 2627  N   GLY A1342     9206   7768  10698   1057   -641   -416       N  
ATOM   2628  CA  GLY A1342      -1.591  36.125  -8.874  1.00 61.02           C  
ANISOU 2628  CA  GLY A1342     7618   6321   9247   1004   -611   -391       C  
ATOM   2629  C   GLY A1342      -0.209  35.652  -8.502  1.00 58.50           C  
ANISOU 2629  C   GLY A1342     7290   6046   8893    975   -570   -373       C  
ATOM   2630  O   GLY A1342      -0.055  34.859  -7.566  1.00 44.44           O  
ANISOU 2630  O   GLY A1342     5437   4307   7139    940   -567   -341       O  
ATOM   2631  N   LEU A1343       0.807  36.166  -9.186  1.00 81.45           N  
ANISOU 2631  N   LEU A1343    10266   8947  11737    990   -531   -391       N  
ATOM   2632  CA  LEU A1343       2.192  35.898  -8.823  1.00 88.45           C  
ANISOU 2632  CA  LEU A1343    11137   9886  12584    962   -482   -375       C  
ATOM   2633  C   LEU A1343       2.551  36.389  -7.419  1.00 78.51           C  
ANISOU 2633  C   LEU A1343     9809   8710  11312    894   -422   -364       C  
ATOM   2634  O   LEU A1343       3.400  35.783  -6.752  1.00 65.94           O  
ANISOU 2634  O   LEU A1343     8166   7179   9709    867   -404   -339       O  
ATOM   2635  CB  LEU A1343       3.070  36.467  -9.937  1.00 93.04           C  
ANISOU 2635  CB  LEU A1343    11807  10437  13106    994   -450   -398       C  
ATOM   2636  CG  LEU A1343       4.535  36.820  -9.855  1.00112.08           C  
ANISOU 2636  CG  LEU A1343    14225  12897  15463    967   -377   -396       C  
ATOM   2637  CD1 LEU A1343       5.271  35.546  -9.571  1.00126.27           C  
ANISOU 2637  CD1 LEU A1343    15973  14734  17270    968   -396   -362       C  
ATOM   2638  CD2 LEU A1343       4.928  37.331 -11.219  1.00114.63           C  
ANISOU 2638  CD2 LEU A1343    14651  13158  15744   1019   -359   -419       C  
ATOM   2639  N   VAL A1344       1.923  37.465  -6.943  1.00 77.12           N  
ANISOU 2639  N   VAL A1344     9632   8539  11131    871   -390   -381       N  
ATOM   2640  CA  VAL A1344       2.255  37.969  -5.609  1.00 61.27           C  
ANISOU 2640  CA  VAL A1344     7569   6606   9103    807   -334   -376       C  
ATOM   2641  C   VAL A1344       1.862  36.931  -4.563  1.00 63.45           C  
ANISOU 2641  C   VAL A1344     7758   6925   9424    791   -362   -336       C  
ATOM   2642  O   VAL A1344       2.530  36.779  -3.531  1.00 53.19           O  
ANISOU 2642  O   VAL A1344     6406   5701   8103    750   -330   -319       O  
ATOM   2643  CB  VAL A1344       1.587  39.337  -5.344  1.00 40.23           C  
ANISOU 2643  CB  VAL A1344     4934   3928   6423    793   -292   -403       C  
ATOM   2644  CG1 VAL A1344       0.154  39.346  -5.840  1.00 50.31           C  
ANISOU 2644  CG1 VAL A1344     6226   5141   7747    843   -341   -404       C  
ATOM   2645  CG2 VAL A1344       1.660  39.703  -3.873  1.00 28.88           C  
ANISOU 2645  CG2 VAL A1344     3437   2562   4972    733   -247   -397       C  
ATOM   2646  N   ALA A1345       0.788  36.182  -4.829  1.00 66.00           N  
ANISOU 2646  N   ALA A1345     8065   7200   9811    824   -423   -320       N  
ATOM   2647  CA  ALA A1345       0.391  35.107  -3.930  1.00 42.95           C  
ANISOU 2647  CA  ALA A1345     5070   4308   6942    810   -445   -278       C  
ATOM   2648  C   ALA A1345       1.425  33.994  -3.921  1.00 39.17           C  
ANISOU 2648  C   ALA A1345     4575   3855   6451    815   -453   -251       C  
ATOM   2649  O   ALA A1345       1.687  33.405  -2.870  1.00 46.47           O  
ANISOU 2649  O   ALA A1345     5440   4837   7379    793   -437   -216       O  
ATOM   2650  CB  ALA A1345      -0.972  34.556  -4.338  1.00 41.54           C  
ANISOU 2650  CB  ALA A1345     4878   4065   6840    839   -508   -271       C  
ATOM   2651  N   LEU A1346       2.005  33.667  -5.077  1.00 50.90           N  
ANISOU 2651  N   LEU A1346     6118   5300   7920    852   -477   -264       N  
ATOM   2652  CA  LEU A1346       3.056  32.654  -5.080  1.00 62.45           C  
ANISOU 2652  CA  LEU A1346     7571   6791   9366    864   -477   -236       C  
ATOM   2653  C   LEU A1346       4.273  33.145  -4.312  1.00 67.90           C  
ANISOU 2653  C   LEU A1346     8230   7576   9993    828   -415   -232       C  
ATOM   2654  O   LEU A1346       4.926  32.369  -3.599  1.00 74.33           O  
ANISOU 2654  O   LEU A1346     8995   8450  10797    824   -405   -196       O  
ATOM   2655  CB  LEU A1346       3.455  32.292  -6.515  1.00 63.42           C  
ANISOU 2655  CB  LEU A1346     7770   6849   9476    916   -509   -251       C  
ATOM   2656  CG  LEU A1346       2.460  31.580  -7.432  1.00 62.28           C  
ANISOU 2656  CG  LEU A1346     7665   6612   9387    957   -583   -259       C  
ATOM   2657  CD1 LEU A1346       3.020  31.503  -8.839  1.00 69.36           C  
ANISOU 2657  CD1 LEU A1346     8652   7454  10249   1010   -602   -282       C  
ATOM   2658  CD2 LEU A1346       2.163  30.190  -6.910  1.00 59.97           C  
ANISOU 2658  CD2 LEU A1346     7326   6312   9147    955   -615   -220       C  
ATOM   2659  N   GLU A1347       4.561  34.445  -4.407  1.00 70.60           N  
ANISOU 2659  N   GLU A1347     8598   7933  10293    801   -372   -269       N  
ATOM   2660  CA  GLU A1347       5.680  35.008  -3.662  1.00 71.07           C  
ANISOU 2660  CA  GLU A1347     8624   8083  10295    755   -316   -275       C  
ATOM   2661  C   GLU A1347       5.434  34.930  -2.160  1.00 62.74           C  
ANISOU 2661  C   GLU A1347     7495   7101   9242    717   -302   -253       C  
ATOM   2662  O   GLU A1347       6.342  34.588  -1.393  1.00 62.02           O  
ANISOU 2662  O   GLU A1347     7352   7096   9118    699   -283   -234       O  
ATOM   2663  CB  GLU A1347       5.928  36.449  -4.113  1.00 68.78           C  
ANISOU 2663  CB  GLU A1347     8387   7779   9966    729   -270   -323       C  
ATOM   2664  CG  GLU A1347       6.330  36.553  -5.578  1.00 57.11           C  
ANISOU 2664  CG  GLU A1347     6988   6237   8476    772   -273   -340       C  
ATOM   2665  CD  GLU A1347       6.477  37.973  -6.086  1.00 66.14           C  
ANISOU 2665  CD  GLU A1347     8196   7351   9584    751   -221   -384       C  
ATOM   2666  OE1 GLU A1347       5.991  38.918  -5.426  1.00 76.34           O  
ANISOU 2666  OE1 GLU A1347     9484   8653  10869    711   -192   -405       O  
ATOM   2667  OE2 GLU A1347       7.070  38.139  -7.172  1.00 69.74           O  
ANISOU 2667  OE2 GLU A1347     8713   7769  10017    781   -205   -395       O  
ATOM   2668  N   ALA A1348       4.211  35.237  -1.721  1.00 44.07           N  
ANISOU 2668  N   ALA A1348     5124   4706   6914    709   -310   -255       N  
ATOM   2669  CA  ALA A1348       3.907  35.159  -0.298  1.00 28.30           C  
ANISOU 2669  CA  ALA A1348     3064   2773   4917    680   -291   -231       C  
ATOM   2670  C   ALA A1348       3.894  33.719   0.197  1.00 39.70           C  
ANISOU 2670  C   ALA A1348     4457   4236   6392    705   -318   -176       C  
ATOM   2671  O   ALA A1348       4.430  33.425   1.271  1.00 43.12           O  
ANISOU 2671  O   ALA A1348     4839   4752   6794    689   -297   -151       O  
ATOM   2672  CB  ALA A1348       2.566  35.826  -0.017  1.00 30.14           C  
ANISOU 2672  CB  ALA A1348     3304   2964   5184    673   -287   -242       C  
ATOM   2673  N   MET A1349       3.306  32.803  -0.578  1.00 47.11           N  
ANISOU 2673  N   MET A1349     5413   5099   7389    745   -365   -158       N  
ATOM   2674  CA  MET A1349       3.187  31.422  -0.120  1.00 41.99           C  
ANISOU 2674  CA  MET A1349     4726   4453   6777    767   -385   -105       C  
ATOM   2675  C   MET A1349       4.542  30.741  -0.056  1.00 50.83           C  
ANISOU 2675  C   MET A1349     5833   5630   7848    785   -374    -82       C  
ATOM   2676  O   MET A1349       4.783  29.917   0.834  1.00 51.38           O  
ANISOU 2676  O   MET A1349     5858   5749   7913    795   -364    -36       O  
ATOM   2677  CB  MET A1349       2.239  30.646  -1.028  1.00 41.36           C  
ANISOU 2677  CB  MET A1349     4673   4271   6772    798   -439   -100       C  
ATOM   2678  CG  MET A1349       0.812  31.145  -0.987  1.00 50.95           C  
ANISOU 2678  CG  MET A1349     5879   5436   8043    785   -454   -113       C  
ATOM   2679  SD  MET A1349      -0.124  30.582  -2.415  1.00 50.90           S  
ANISOU 2679  SD  MET A1349     5917   5314   8108    818   -529   -132       S  
ATOM   2680  CE  MET A1349      -0.649  28.973  -1.837  1.00 56.35           C  
ANISOU 2680  CE  MET A1349     6558   5979   8874    819   -550    -77       C  
ATOM   2681  N   CYS A1350       5.436  31.054  -1.001  1.00 61.53           N  
ANISOU 2681  N   CYS A1350     7230   6982   9165    797   -373   -109       N  
ATOM   2682  CA  CYS A1350       6.766  30.458  -0.944  1.00 64.18           C  
ANISOU 2682  CA  CYS A1350     7548   7384   9454    818   -359    -86       C  
ATOM   2683  C   CYS A1350       7.505  30.881   0.317  1.00 66.21           C  
ANISOU 2683  C   CYS A1350     7740   7762   9654    782   -320    -79       C  
ATOM   2684  O   CYS A1350       8.326  30.122   0.845  1.00 63.70           O  
ANISOU 2684  O   CYS A1350     7383   7515   9307    805   -312    -41       O  
ATOM   2685  CB  CYS A1350       7.585  30.836  -2.177  1.00 64.24           C  
ANISOU 2685  CB  CYS A1350     7608   7368   9432    835   -355   -116       C  
ATOM   2686  SG  CYS A1350       7.119  29.982  -3.691  1.00 72.17           S  
ANISOU 2686  SG  CYS A1350     8693   8247  10482    897   -406   -115       S  
ATOM   2687  N   LEU A1351       7.227  32.087   0.808  1.00 60.15           N  
ANISOU 2687  N   LEU A1351     6966   7019   8867    731   -296   -117       N  
ATOM   2688  CA  LEU A1351       7.855  32.623   2.003  1.00 50.75           C  
ANISOU 2688  CA  LEU A1351     5722   5940   7618    690   -263   -122       C  
ATOM   2689  C   LEU A1351       7.086  32.313   3.275  1.00 44.56           C  
ANISOU 2689  C   LEU A1351     4900   5185   6848    686   -259    -90       C  
ATOM   2690  O   LEU A1351       7.446  32.825   4.338  1.00 53.32           O  
ANISOU 2690  O   LEU A1351     5972   6383   7906    653   -235    -99       O  
ATOM   2691  CB  LEU A1351       8.027  34.136   1.868  1.00 53.06           C  
ANISOU 2691  CB  LEU A1351     6041   6242   7878    632   -233   -185       C  
ATOM   2692  CG  LEU A1351       9.268  34.654   1.140  1.00 62.57           C  
ANISOU 2692  CG  LEU A1351     7257   7477   9041    614   -213   -217       C  
ATOM   2693  CD1 LEU A1351      10.518  34.156   1.836  1.00 72.27           C  
ANISOU 2693  CD1 LEU A1351     8415   8827  10219    612   -207   -194       C  
ATOM   2694  CD2 LEU A1351       9.277  34.255  -0.325  1.00 66.89           C  
ANISOU 2694  CD2 LEU A1351     7863   7934   9619    662   -232   -214       C  
ATOM   2695  N   GLY A1352       6.034  31.509   3.196  1.00 34.10           N  
ANISOU 2695  N   GLY A1352     3582   3786   5588    717   -281    -55       N  
ATOM   2696  CA  GLY A1352       5.317  31.091   4.380  1.00 46.80           C  
ANISOU 2696  CA  GLY A1352     5152   5416   7214    720   -269    -15       C  
ATOM   2697  C   GLY A1352       4.228  32.021   4.857  1.00 49.09           C  
ANISOU 2697  C   GLY A1352     5448   5683   7523    687   -251    -37       C  
ATOM   2698  O   GLY A1352       3.555  31.701   5.843  1.00 64.89           O  
ANISOU 2698  O   GLY A1352     7418   7697   9541    691   -235     -1       O  
ATOM   2699  N   ALA A1353       4.029  33.157   4.204  1.00 40.78           N  
ANISOU 2699  N   ALA A1353     4435   4593   6466    659   -247    -92       N  
ATOM   2700  CA  ALA A1353       2.879  33.981   4.527  1.00 43.82           C  
ANISOU 2700  CA  ALA A1353     4831   4942   6876    640   -230   -108       C  
ATOM   2701  C   ALA A1353       1.621  33.294   4.014  1.00 41.66           C  
ANISOU 2701  C   ALA A1353     4559   4576   6695    671   -261    -81       C  
ATOM   2702  O   ALA A1353       1.621  32.689   2.940  1.00 44.28           O  
ANISOU 2702  O   ALA A1353     4914   4847   7065    695   -301    -81       O  
ATOM   2703  CB  ALA A1353       3.025  35.370   3.914  1.00 26.16           C  
ANISOU 2703  CB  ALA A1353     2646   2686   4609    609   -213   -172       C  
ATOM   2704  N   ILE A1354       0.537  33.397   4.771  1.00 47.31           N  
ANISOU 2704  N   ILE A1354     5249   5280   7445    668   -243    -60       N  
ATOM   2705  CA  ILE A1354      -0.721  32.748   4.415  1.00 45.78           C  
ANISOU 2705  CA  ILE A1354     5041   5007   7345    688   -270    -33       C  
ATOM   2706  C   ILE A1354      -1.572  33.763   3.660  1.00 47.58           C  
ANISOU 2706  C   ILE A1354     5303   5177   7599    686   -280    -76       C  
ATOM   2707  O   ILE A1354      -1.829  34.857   4.190  1.00 55.52           O  
ANISOU 2707  O   ILE A1354     6318   6207   8570    670   -240    -97       O  
ATOM   2708  CB  ILE A1354      -1.455  32.220   5.653  1.00 50.33           C  
ANISOU 2708  CB  ILE A1354     5565   5605   7954    691   -239     21       C  
ATOM   2709  CG1 ILE A1354      -0.599  31.176   6.371  1.00 52.84           C  
ANISOU 2709  CG1 ILE A1354     5856   5979   8240    704   -228     67       C  
ATOM   2710  CG2 ILE A1354      -2.816  31.655   5.275  1.00 61.70           C  
ANISOU 2710  CG2 ILE A1354     6980   6962   9499    702   -264     45       C  
ATOM   2711  CD1 ILE A1354      -0.938  30.999   7.826  1.00 62.39           C  
ANISOU 2711  CD1 ILE A1354     7026   7241   9437    707   -179    114       C  
ATOM   2712  N   PRO A1355      -1.955  33.483   2.418  1.00 45.65           N  
ANISOU 2712  N   PRO A1355     5085   4858   7404    707   -331    -91       N  
ATOM   2713  CA  PRO A1355      -2.708  34.468   1.645  1.00 49.16           C  
ANISOU 2713  CA  PRO A1355     5564   5251   7862    716   -343   -132       C  
ATOM   2714  C   PRO A1355      -4.177  34.488   2.033  1.00 44.18           C  
ANISOU 2714  C   PRO A1355     4890   4593   7304    722   -343   -109       C  
ATOM   2715  O   PRO A1355      -4.795  33.455   2.308  1.00 43.35           O  
ANISOU 2715  O   PRO A1355     4733   4468   7269    725   -362    -68       O  
ATOM   2716  CB  PRO A1355      -2.511  33.995   0.201  1.00 47.36           C  
ANISOU 2716  CB  PRO A1355     5379   4959   7656    742   -404   -153       C  
ATOM   2717  CG  PRO A1355      -2.359  32.523   0.317  1.00 34.93           C  
ANISOU 2717  CG  PRO A1355     3771   3376   6124    748   -432   -111       C  
ATOM   2718  CD  PRO A1355      -1.670  32.267   1.635  1.00 34.62           C  
ANISOU 2718  CD  PRO A1355     3692   3418   6043    728   -381    -76       C  
ATOM   2719  N   ILE A1356      -4.727  35.693   2.041  1.00 44.84           N  
ANISOU 2719  N   ILE A1356     4996   4671   7370    726   -317   -136       N  
ATOM   2720  CA  ILE A1356      -6.151  35.964   2.142  1.00 45.13           C  
ANISOU 2720  CA  ILE A1356     4998   4678   7470    743   -319   -124       C  
ATOM   2721  C   ILE A1356      -6.463  36.756   0.888  1.00 49.69           C  
ANISOU 2721  C   ILE A1356     5632   5204   8043    773   -351   -170       C  
ATOM   2722  O   ILE A1356      -6.061  37.921   0.783  1.00 38.70           O  
ANISOU 2722  O   ILE A1356     4300   3820   6582    774   -313   -205       O  
ATOM   2723  CB  ILE A1356      -6.497  36.768   3.405  1.00 44.08           C  
ANISOU 2723  CB  ILE A1356     4849   4592   7307    732   -246   -109       C  
ATOM   2724  CG1 ILE A1356      -5.966  36.062   4.663  1.00 34.28           C  
ANISOU 2724  CG1 ILE A1356     3567   3411   6047    708   -209    -68       C  
ATOM   2725  CG2 ILE A1356      -8.004  37.028   3.472  1.00 27.42           C  
ANISOU 2725  CG2 ILE A1356     2698   2453   5267    757   -244    -92       C  
ATOM   2726  CD1 ILE A1356      -6.205  36.821   5.947  1.00 27.31           C  
ANISOU 2726  CD1 ILE A1356     2678   2578   5121    701   -137    -56       C  
ATOM   2727  N   ALA A1357      -7.142  36.137  -0.078  1.00 61.02           N  
ANISOU 2727  N   ALA A1357     7055   6585   9547    797   -421   -172       N  
ATOM   2728  CA  ALA A1357      -7.199  36.711  -1.414  1.00 58.31           C  
ANISOU 2728  CA  ALA A1357     6777   6193   9185    833   -463   -217       C  
ATOM   2729  C   ALA A1357      -8.591  36.586  -2.013  1.00 58.94           C  
ANISOU 2729  C   ALA A1357     6820   6231   9343    867   -520   -217       C  
ATOM   2730  O   ALA A1357      -9.394  35.731  -1.617  1.00 57.09           O  
ANISOU 2730  O   ALA A1357     6506   5993   9192    854   -544   -184       O  
ATOM   2731  CB  ALA A1357      -6.177  36.045  -2.349  1.00 61.95           C  
ANISOU 2731  CB  ALA A1357     7286   6630   9623    837   -506   -235       C  
ATOM   2732  N   SER A1358      -8.886  37.505  -2.931  1.00 66.54           N  
ANISOU 2732  N   SER A1358     7840   7164  10278    911   -536   -253       N  
ATOM   2733  CA  SER A1358     -10.094  37.389  -3.735  1.00 66.80           C  
ANISOU 2733  CA  SER A1358     7846   7160  10375    952   -606   -262       C  
ATOM   2734  C   SER A1358     -10.021  36.162  -4.630  1.00 61.01           C  
ANISOU 2734  C   SER A1358     7107   6386   9688    951   -696   -271       C  
ATOM   2735  O   SER A1358      -8.963  35.833  -5.172  1.00 42.87           O  
ANISOU 2735  O   SER A1358     4872   4072   7345    948   -708   -289       O  
ATOM   2736  CB  SER A1358     -10.293  38.643  -4.579  1.00 66.65           C  
ANISOU 2736  CB  SER A1358     7905   7120  10301   1009   -603   -299       C  
ATOM   2737  OG  SER A1358     -10.172  39.810  -3.789  1.00 69.70           O  
ANISOU 2737  OG  SER A1358     8317   7535  10631   1007   -512   -295       O  
ATOM   2738  N   ALA A1359     -11.166  35.497  -4.805  1.00 69.85           N  
ANISOU 2738  N   ALA A1359     8151   7487  10900    953   -760   -262       N  
ATOM   2739  CA  ALA A1359     -11.256  34.341  -5.694  1.00 68.56           C  
ANISOU 2739  CA  ALA A1359     7985   7277  10788    951   -852   -277       C  
ATOM   2740  C   ALA A1359     -11.492  34.839  -7.120  1.00 60.08           C  
ANISOU 2740  C   ALA A1359     6980   6167   9681   1012   -921   -327       C  
ATOM   2741  O   ALA A1359     -12.587  34.760  -7.677  1.00 60.84           O  
ANISOU 2741  O   ALA A1359     7039   6257   9820   1029   -987   -340       O  
ATOM   2742  CB  ALA A1359     -12.358  33.398  -5.231  1.00 69.74           C  
ANISOU 2742  CB  ALA A1359     8022   7422  11054    916   -888   -248       C  
ATOM   2743  N   VAL A1360     -10.429  35.381  -7.707  1.00 56.31           N  
ANISOU 2743  N   VAL A1360     6611   5689   9097   1030   -893   -350       N  
ATOM   2744  CA  VAL A1360     -10.442  35.833  -9.092  1.00 65.59           C  
ANISOU 2744  CA  VAL A1360     7878   6853  10192   1073   -932   -388       C  
ATOM   2745  C   VAL A1360      -9.183  35.354  -9.800  1.00 67.50           C  
ANISOU 2745  C   VAL A1360     8208   7079  10359   1066   -932   -402       C  
ATOM   2746  O   VAL A1360      -8.119  35.221  -9.188  1.00 59.01           O  
ANISOU 2746  O   VAL A1360     7143   6011   9267   1041   -877   -387       O  
ATOM   2747  CB  VAL A1360     -10.561  37.369  -9.196  1.00 65.87           C  
ANISOU 2747  CB  VAL A1360     7967   6903  10158   1120   -875   -399       C  
ATOM   2748  CG1 VAL A1360     -11.859  37.843  -8.569  1.00 68.21           C  
ANISOU 2748  CG1 VAL A1360     8177   7217  10521   1138   -874   -382       C  
ATOM   2749  CG2 VAL A1360      -9.369  38.033  -8.528  1.00 62.31           C  
ANISOU 2749  CG2 VAL A1360     7563   6458   9655   1106   -781   -394       C  
ATOM   2750  N   GLY A1361      -9.312  35.093 -11.100  1.00 74.57           N  
ANISOU 2750  N   GLY A1361     9166   7957  11212   1092   -996   -431       N  
ATOM   2751  CA  GLY A1361      -8.146  34.930 -11.952  1.00 67.70           C  
ANISOU 2751  CA  GLY A1361     8397   7076  10250   1102   -982   -444       C  
ATOM   2752  C   GLY A1361      -7.247  33.807 -11.482  1.00 60.65           C  
ANISOU 2752  C   GLY A1361     7486   6175   9381   1060   -973   -424       C  
ATOM   2753  O   GLY A1361      -7.701  32.711 -11.137  1.00 65.46           O  
ANISOU 2753  O   GLY A1361     8031   6768  10074   1029  -1022   -414       O  
ATOM   2754  N   GLY A1362      -5.941  34.082 -11.476  1.00 58.94           N  
ANISOU 2754  N   GLY A1362     7331   5969   9095   1062   -907   -418       N  
ATOM   2755  CA  GLY A1362      -4.974  33.086 -11.056  1.00 61.16           C  
ANISOU 2755  CA  GLY A1362     7601   6250   9389   1034   -893   -397       C  
ATOM   2756  C   GLY A1362      -4.969  32.836  -9.562  1.00 61.58           C  
ANISOU 2756  C   GLY A1362     7558   6319   9519    998   -860   -364       C  
ATOM   2757  O   GLY A1362      -4.476  31.796  -9.121  1.00 60.33           O  
ANISOU 2757  O   GLY A1362     7373   6158   9394    977   -862   -340       O  
ATOM   2758  N   LEU A1363      -5.479  33.782  -8.769  1.00 64.55           N  
ANISOU 2758  N   LEU A1363     7889   6714   9923    996   -824   -360       N  
ATOM   2759  CA  LEU A1363      -5.596  33.555  -7.331  1.00 64.68           C  
ANISOU 2759  CA  LEU A1363     7813   6757  10005    959   -787   -324       C  
ATOM   2760  C   LEU A1363      -6.541  32.400  -7.023  1.00 75.11           C  
ANISOU 2760  C   LEU A1363     9057   8058  11424    936   -841   -302       C  
ATOM   2761  O   LEU A1363      -6.311  31.639  -6.075  1.00 80.96           O  
ANISOU 2761  O   LEU A1363     9744   8824  12194    897   -812   -262       O  
ATOM   2762  CB  LEU A1363      -6.082  34.823  -6.629  1.00 60.25           C  
ANISOU 2762  CB  LEU A1363     7230   6235   9426    953   -728   -323       C  
ATOM   2763  CG  LEU A1363      -5.247  36.095  -6.738  1.00 53.96           C  
ANISOU 2763  CG  LEU A1363     6506   5457   8538    963   -660   -345       C  
ATOM   2764  CD1 LEU A1363      -6.041  37.269  -6.203  1.00 57.79           C  
ANISOU 2764  CD1 LEU A1363     6977   5962   9019    967   -616   -348       C  
ATOM   2765  CD2 LEU A1363      -3.965  35.919  -5.951  1.00 54.40           C  
ANISOU 2765  CD2 LEU A1363     6556   5564   8549    919   -598   -327       C  
ATOM   2766  N   ARG A1364      -7.633  32.281  -7.782  1.00 79.77           N  
ANISOU 2766  N   ARG A1364     9639   8618  12050    950   -911   -323       N  
ATOM   2767  CA  ARG A1364      -8.556  31.172  -7.569  1.00 84.52           C  
ANISOU 2767  CA  ARG A1364    10165   9192  12758    922   -967   -308       C  
ATOM   2768  C   ARG A1364      -7.903  29.843  -7.940  1.00 85.23           C  
ANISOU 2768  C   ARG A1364    10287   9248  12849    905   -998   -303       C  
ATOM   2769  O   ARG A1364      -8.228  28.801  -7.355  1.00 83.40           O  
ANISOU 2769  O   ARG A1364     9993   8990  12704    874  -1011   -275       O  
ATOM   2770  CB  ARG A1364      -9.852  31.425  -8.337  1.00 96.00           C  
ANISOU 2770  CB  ARG A1364    11600  10630  14247    940  -1040   -338       C  
ATOM   2771  CG  ARG A1364     -10.987  30.478  -7.986  1.00114.16           C  
ANISOU 2771  CG  ARG A1364    13796  12899  16681    909  -1096   -324       C  
ATOM   2772  CD  ARG A1364     -12.311  31.195  -8.217  1.00123.92           C  
ANISOU 2772  CD  ARG A1364    14977  14147  17961    932  -1135   -340       C  
ATOM   2773  NE  ARG A1364     -13.484  30.374  -7.943  1.00131.03           N  
ANISOU 2773  NE  ARG A1364    15767  15026  18993    897  -1189   -328       N  
ATOM   2774  CZ  ARG A1364     -14.655  30.872  -7.553  1.00134.42           C  
ANISOU 2774  CZ  ARG A1364    16105  15488  19481    898  -1188   -316       C  
ATOM   2775  NH1 ARG A1364     -14.797  32.178  -7.379  1.00133.27           N  
ANISOU 2775  NH1 ARG A1364    15972  15384  19279    943  -1140   -314       N  
ATOM   2776  NH2 ARG A1364     -15.678  30.065  -7.315  1.00138.09           N  
ANISOU 2776  NH2 ARG A1364    16466  15940  20061    852  -1230   -303       N  
ATOM   2777  N   ASP A1365      -6.983  29.864  -8.909  1.00 82.90           N  
ANISOU 2777  N   ASP A1365    10092   8950  12456    928  -1002   -328       N  
ATOM   2778  CA  ASP A1365      -6.308  28.649  -9.350  1.00 82.91           C  
ANISOU 2778  CA  ASP A1365    10137   8920  12444    922  -1024   -324       C  
ATOM   2779  C   ASP A1365      -5.181  28.251  -8.407  1.00 72.38           C  
ANISOU 2779  C   ASP A1365     8792   7609  11100    913   -956   -281       C  
ATOM   2780  O   ASP A1365      -4.939  27.058  -8.203  1.00 79.57           O  
ANISOU 2780  O   ASP A1365     9695   8493  12046    898   -965   -258       O  
ATOM   2781  CB  ASP A1365      -5.722  28.831 -10.753  1.00104.22           C  
ANISOU 2781  CB  ASP A1365    12948  11612  15039    958  -1046   -361       C  
ATOM   2782  CG  ASP A1365      -6.777  28.999 -11.819  1.00113.84           C  
ANISOU 2782  CG  ASP A1365    14187  12805  16263    975  -1128   -404       C  
ATOM   2783  OD1 ASP A1365      -7.873  28.417 -11.682  1.00113.85           O  
ANISOU 2783  OD1 ASP A1365    14121  12773  16364    952  -1193   -411       O  
ATOM   2784  OD2 ASP A1365      -6.498  29.713 -12.805  1.00119.63           O  
ANISOU 2784  OD2 ASP A1365    15000  13548  16904   1014  -1127   -431       O  
ATOM   2785  N   ILE A1366      -4.481  29.224  -7.826  1.00 68.32           N  
ANISOU 2785  N   ILE A1366     8276   7141  10542    924   -890   -272       N  
ATOM   2786  CA  ILE A1366      -3.353  28.904  -6.956  1.00 67.41           C  
ANISOU 2786  CA  ILE A1366     8145   7061  10406    917   -829   -235       C  
ATOM   2787  C   ILE A1366      -3.822  28.476  -5.571  1.00 62.36           C  
ANISOU 2787  C   ILE A1366     7414   6459   9821    872   -792   -187       C  
ATOM   2788  O   ILE A1366      -3.351  27.472  -5.024  1.00 62.77           O  
ANISOU 2788  O   ILE A1366     7448   6517   9884    861   -773   -149       O  
ATOM   2789  CB  ILE A1366      -2.397  30.109  -6.880  1.00 64.36           C  
ANISOU 2789  CB  ILE A1366     7793   6731   9929    926   -765   -247       C  
ATOM   2790  CG1 ILE A1366      -1.751  30.368  -8.241  1.00 55.37           C  
ANISOU 2790  CG1 ILE A1366     6753   5557   8730    973   -787   -284       C  
ATOM   2791  CG2 ILE A1366      -1.346  29.891  -5.808  1.00 76.08           C  
ANISOU 2791  CG2 ILE A1366     9244   8288  11375    902   -696   -208       C  
ATOM   2792  CD1 ILE A1366      -1.056  31.696  -8.323  1.00 46.38           C  
ANISOU 2792  CD1 ILE A1366     5651   4454   7519    981   -729   -304       C  
ATOM   2793  N   ILE A1367      -4.733  29.219  -4.977  1.00 57.08           N  
ANISOU 2793  N   ILE A1367     6690   5815   9182    852   -775   -186       N  
ATOM   2794  CA  ILE A1367      -5.118  28.978  -3.593  1.00 63.13           C  
ANISOU 2794  CA  ILE A1367     7375   6624   9988    814   -725   -138       C  
ATOM   2795  C   ILE A1367      -6.196  27.900  -3.549  1.00 79.95           C  
ANISOU 2795  C   ILE A1367     9453   8700  12224    794   -770   -119       C  
ATOM   2796  O   ILE A1367      -7.108  27.865  -4.385  1.00 87.99           O  
ANISOU 2796  O   ILE A1367    10470   9665  13296    800   -838   -151       O  
ATOM   2797  CB  ILE A1367      -5.567  30.285  -2.918  1.00 61.00           C  
ANISOU 2797  CB  ILE A1367     7074   6406   9697    805   -677   -142       C  
ATOM   2798  CG1 ILE A1367      -4.441  31.320  -3.013  1.00 48.01           C  
ANISOU 2798  CG1 ILE A1367     5487   4806   7948    817   -632   -166       C  
ATOM   2799  CG2 ILE A1367      -5.953  30.039  -1.465  1.00 68.20           C  
ANISOU 2799  CG2 ILE A1367     7908   7362  10642    773   -620    -90       C  
ATOM   2800  CD1 ILE A1367      -4.861  32.723  -2.644  1.00 51.44           C  
ANISOU 2800  CD1 ILE A1367     5919   5272   8353    814   -590   -183       C  
ATOM   2801  N   THR A1368      -6.099  27.031  -2.549  1.00 79.13           N  
ANISOU 2801  N   THR A1368     9304   8610  12152    769   -730    -67       N  
ATOM   2802  CA  THR A1368      -7.047  25.958  -2.283  1.00 76.56           C  
ANISOU 2802  CA  THR A1368     8923   8234  11931    739   -751    -39       C  
ATOM   2803  C   THR A1368      -7.558  26.091  -0.851  1.00 81.20           C  
ANISOU 2803  C   THR A1368     9431   8872  12549    712   -680     14       C  
ATOM   2804  O   THR A1368      -7.146  26.980  -0.100  1.00 81.64           O  
ANISOU 2804  O   THR A1368     9482   9000  12540    719   -620     24       O  
ATOM   2805  CB  THR A1368      -6.405  24.588  -2.515  1.00 78.81           C  
ANISOU 2805  CB  THR A1368     9247   8471  12225    742   -765    -19       C  
ATOM   2806  OG1 THR A1368      -5.453  24.326  -1.478  1.00 99.22           O  
ANISOU 2806  OG1 THR A1368    11828  11115  14756    748   -690     31       O  
ATOM   2807  CG2 THR A1368      -5.694  24.553  -3.864  1.00 64.16           C  
ANISOU 2807  CG2 THR A1368     7483   6577  10317    779   -822    -68       C  
ATOM   2808  N   ASN A1369      -8.493  25.214  -0.482  1.00 88.87           N  
ANISOU 2808  N   ASN A1369    10343   9802  13622    680   -684     45       N  
ATOM   2809  CA  ASN A1369      -9.067  25.271   0.859  1.00103.56           C  
ANISOU 2809  CA  ASN A1369    12128  11702  15518    659   -611    100       C  
ATOM   2810  C   ASN A1369      -8.035  25.044   1.963  1.00105.09           C  
ANISOU 2810  C   ASN A1369    12336  11955  15640    670   -532    150       C  
ATOM   2811  O   ASN A1369      -8.168  25.603   3.060  1.00107.76           O  
ANISOU 2811  O   ASN A1369    12636  12355  15955    669   -466    181       O  
ATOM   2812  CB  ASN A1369     -10.159  24.200   0.952  1.00111.21           C  
ANISOU 2812  CB  ASN A1369    13036  12604  16615    619   -629    127       C  
ATOM   2813  CG  ASN A1369     -11.119  24.418   2.106  1.00109.73           C  
ANISOU 2813  CG  ASN A1369    12759  12448  16487    597   -564    176       C  
ATOM   2814  OD1 ASN A1369     -11.085  25.446   2.778  1.00 95.06           O  
ANISOU 2814  OD1 ASN A1369    10887  10657  14573    615   -512    184       O  
ATOM   2815  ND2 ASN A1369     -11.958  23.415   2.369  1.00118.09           N  
ANISOU 2815  ND2 ASN A1369    13760  13452  17657    558   -559    210       N  
ATOM   2816  N   GLU A1370      -6.997  24.262   1.689  1.00 87.26           N  
ANISOU 2816  N   GLU A1370    10132   9683  13340    687   -540    156       N  
ATOM   2817  CA  GLU A1370      -5.940  23.928   2.638  1.00 81.30           C  
ANISOU 2817  CA  GLU A1370     9390   8987  12513    706   -475    203       C  
ATOM   2818  C   GLU A1370      -4.745  24.867   2.600  1.00 71.41           C  
ANISOU 2818  C   GLU A1370     8179   7812  11141    733   -461    175       C  
ATOM   2819  O   GLU A1370      -3.822  24.688   3.400  1.00 68.47           O  
ANISOU 2819  O   GLU A1370     7811   7504  10702    750   -413    209       O  
ATOM   2820  CB  GLU A1370      -5.472  22.478   2.457  1.00102.48           C  
ANISOU 2820  CB  GLU A1370    12105  11614  15218    716   -481    234       C  
ATOM   2821  CG  GLU A1370      -6.586  21.427   2.461  1.00121.47           C  
ANISOU 2821  CG  GLU A1370    14476  13931  17747    681   -492    259       C  
ATOM   2822  CD  GLU A1370      -7.442  21.425   1.206  1.00131.44           C  
ANISOU 2822  CD  GLU A1370    15742  15114  19084    656   -580    201       C  
ATOM   2823  OE1 GLU A1370      -7.093  22.132   0.236  1.00129.65           O  
ANISOU 2823  OE1 GLU A1370    15560  14894  18808    676   -633    143       O  
ATOM   2824  OE2 GLU A1370      -8.474  20.717   1.197  1.00135.40           O  
ANISOU 2824  OE2 GLU A1370    16202  15548  19695    616   -594    213       O  
ATOM   2825  N   THR A1371      -4.716  25.842   1.684  1.00 74.64           N  
ANISOU 2825  N   THR A1371     8618   8218  11521    737   -502    115       N  
ATOM   2826  CA  THR A1371      -3.535  26.679   1.485  1.00 63.39           C  
ANISOU 2826  CA  THR A1371     7239   6855   9991    755   -490     85       C  
ATOM   2827  C   THR A1371      -3.826  28.179   1.517  1.00 55.27           C  
ANISOU 2827  C   THR A1371     6209   5864   8927    746   -476     46       C  
ATOM   2828  O   THR A1371      -3.021  28.966   1.011  1.00 52.27           O  
ANISOU 2828  O   THR A1371     5876   5511   8476    756   -478      6       O  
ATOM   2829  CB  THR A1371      -2.837  26.317   0.171  1.00 49.08           C  
ANISOU 2829  CB  THR A1371     5495   4997   8158    780   -543     50       C  
ATOM   2830  OG1 THR A1371      -3.765  26.443  -0.909  1.00 59.11           O  
ANISOU 2830  OG1 THR A1371     6781   6191   9488    778   -608      9       O  
ATOM   2831  CG2 THR A1371      -2.332  24.889   0.222  1.00 41.98           C  
ANISOU 2831  CG2 THR A1371     4609   4068   7273    797   -544     91       C  
ATOM   2832  N   GLY A1372      -4.953  28.598   2.075  1.00 60.73           N  
ANISOU 2832  N   GLY A1372     6852   6554   9669    730   -458     56       N  
ATOM   2833  CA  GLY A1372      -5.236  30.016   2.153  1.00 60.37           C  
ANISOU 2833  CA  GLY A1372     6812   6539   9586    727   -438     23       C  
ATOM   2834  C   GLY A1372      -6.681  30.274   2.515  1.00 59.04           C  
ANISOU 2834  C   GLY A1372     6588   6351   9494    718   -431     37       C  
ATOM   2835  O   GLY A1372      -7.471  29.351   2.748  1.00 68.75           O  
ANISOU 2835  O   GLY A1372     7766   7544  10811    707   -440     73       O  
ATOM   2836  N   ILE A1373      -7.013  31.562   2.562  1.00 44.57           N  
ANISOU 2836  N   ILE A1373     4766   4541   7629    724   -410      8       N  
ATOM   2837  CA  ILE A1373      -8.365  32.016   2.858  1.00 45.63           C  
ANISOU 2837  CA  ILE A1373     4850   4663   7825    725   -398     19       C  
ATOM   2838  C   ILE A1373      -8.826  32.835   1.667  1.00 48.17           C  
ANISOU 2838  C   ILE A1373     5206   4947   8150    749   -447    -33       C  
ATOM   2839  O   ILE A1373      -8.175  33.817   1.297  1.00 67.11           O  
ANISOU 2839  O   ILE A1373     7670   7361  10468    761   -435    -73       O  
ATOM   2840  CB  ILE A1373      -8.414  32.858   4.143  1.00 54.86           C  
ANISOU 2840  CB  ILE A1373     6005   5895   8944    722   -315     40       C  
ATOM   2841  CG1 ILE A1373      -7.853  32.076   5.332  1.00 59.04           C  
ANISOU 2841  CG1 ILE A1373     6509   6470   9454    709   -267     91       C  
ATOM   2842  CG2 ILE A1373      -9.835  33.317   4.433  1.00 51.80           C  
ANISOU 2842  CG2 ILE A1373     5564   5496   8622    732   -297     56       C  
ATOM   2843  CD1 ILE A1373      -7.478  32.963   6.515  1.00 65.01           C  
ANISOU 2843  CD1 ILE A1373     7278   7299  10126    707   -193     96       C  
ATOM   2844  N   LEU A1374      -9.944  32.436   1.071  1.00 46.58           N  
ANISOU 2844  N   LEU A1374     4961   4697   8040    754   -501    -34       N  
ATOM   2845  CA  LEU A1374     -10.483  33.076  -0.119  1.00 52.33           C  
ANISOU 2845  CA  LEU A1374     5718   5389   8777    785   -560    -81       C  
ATOM   2846  C   LEU A1374     -11.792  33.790   0.194  1.00 58.15           C  
ANISOU 2846  C   LEU A1374     6398   6136   9561    801   -543    -71       C  
ATOM   2847  O   LEU A1374     -12.580  33.336   1.031  1.00 56.08           O  
ANISOU 2847  O   LEU A1374     6054   5885   9369    783   -515    -25       O  
ATOM   2848  CB  LEU A1374     -10.700  32.037  -1.228  1.00 54.87           C  
ANISOU 2848  CB  LEU A1374     6039   5648   9160    785   -653    -99       C  
ATOM   2849  CG  LEU A1374      -9.420  31.389  -1.766  1.00 50.86           C  
ANISOU 2849  CG  LEU A1374     5601   5123   8602    783   -674   -114       C  
ATOM   2850  CD1 LEU A1374      -9.728  30.185  -2.643  1.00 52.18           C  
ANISOU 2850  CD1 LEU A1374     5764   5224   8839    777   -758   -125       C  
ATOM   2851  CD2 LEU A1374      -8.578  32.405  -2.526  1.00 44.94           C  
ANISOU 2851  CD2 LEU A1374     4942   4379   7753    815   -672   -160       C  
ATOM   2852  N   VAL A1375     -12.024  34.921  -0.486  1.00 68.16           N  
ANISOU 2852  N   VAL A1375     7712   7400  10787    841   -554   -109       N  
ATOM   2853  CA  VAL A1375     -13.231  35.714  -0.274  1.00 78.61           C  
ANISOU 2853  CA  VAL A1375     8989   8734  12144    871   -535   -101       C  
ATOM   2854  C   VAL A1375     -13.721  36.252  -1.611  1.00 82.98           C  
ANISOU 2854  C   VAL A1375     9577   9256  12697    920   -606   -146       C  
ATOM   2855  O   VAL A1375     -12.985  36.281  -2.600  1.00 82.44           O  
ANISOU 2855  O   VAL A1375     9587   9157  12578    935   -649   -187       O  
ATOM   2856  CB  VAL A1375     -13.025  36.892   0.714  1.00 71.12           C  
ANISOU 2856  CB  VAL A1375     8071   7831  11121    880   -436    -90       C  
ATOM   2857  CG1 VAL A1375     -12.690  36.383   2.099  1.00 67.89           C  
ANISOU 2857  CG1 VAL A1375     7623   7460  10711    840   -369    -43       C  
ATOM   2858  CG2 VAL A1375     -11.942  37.826   0.201  1.00 66.61           C  
ANISOU 2858  CG2 VAL A1375     7612   7257  10439    894   -419   -137       C  
ATOM   2859  N   LYS A1376     -14.985  36.681  -1.631  1.00 82.97           N  
ANISOU 2859  N   LYS A1376     9515   9261  12750    952   -615   -137       N  
ATOM   2860  CA  LYS A1376     -15.511  37.335  -2.821  1.00 76.43           C  
ANISOU 2860  CA  LYS A1376     8719   8410  11909   1013   -677   -177       C  
ATOM   2861  C   LYS A1376     -14.790  38.649  -3.063  1.00 69.04           C  
ANISOU 2861  C   LYS A1376     7899   7477  10857   1053   -624   -206       C  
ATOM   2862  O   LYS A1376     -14.570  39.431  -2.133  1.00 68.23           O  
ANISOU 2862  O   LYS A1376     7817   7402  10705   1049   -532   -189       O  
ATOM   2863  CB  LYS A1376     -17.001  37.652  -2.715  1.00 71.82           C  
ANISOU 2863  CB  LYS A1376     8043   7846  11399   1047   -688   -157       C  
ATOM   2864  CG  LYS A1376     -17.496  38.199  -4.063  1.00 73.42           C  
ANISOU 2864  CG  LYS A1376     8281   8029  11586   1117   -768   -201       C  
ATOM   2865  CD  LYS A1376     -18.948  38.661  -4.157  1.00 86.01           C  
ANISOU 2865  CD  LYS A1376     9791   9649  13241   1169   -789   -188       C  
ATOM   2866  CE  LYS A1376     -19.989  37.762  -3.539  1.00 95.42           C  
ANISOU 2866  CE  LYS A1376    10832  10861  14561   1126   -807   -147       C  
ATOM   2867  NZ  LYS A1376     -21.280  38.515  -3.452  1.00100.07           N  
ANISOU 2867  NZ  LYS A1376    11347  11488  15188   1188   -798   -128       N  
ATOM   2868  N   ALA A1377     -14.432  38.900  -4.317  1.00 65.06           N  
ANISOU 2868  N   ALA A1377     7475   6937  10308   1092   -680   -251       N  
ATOM   2869  CA  ALA A1377     -13.787  40.159  -4.641  1.00 63.30           C  
ANISOU 2869  CA  ALA A1377     7366   6706   9978   1131   -626   -279       C  
ATOM   2870  C   ALA A1377     -14.789  41.286  -4.430  1.00 71.26           C  
ANISOU 2870  C   ALA A1377     8365   7729  10980   1189   -586   -269       C  
ATOM   2871  O   ALA A1377     -15.981  41.140  -4.714  1.00 75.52           O  
ANISOU 2871  O   ALA A1377     8830   8275  11588   1227   -639   -259       O  
ATOM   2872  CB  ALA A1377     -13.283  40.152  -6.084  1.00 56.43           C  
ANISOU 2872  CB  ALA A1377     6585   5792   9066   1170   -693   -324       C  
ATOM   2873  N   GLY A1378     -14.302  42.411  -3.922  1.00 78.06           N  
ANISOU 2873  N   GLY A1378     9302   8597  11760   1197   -491   -272       N  
ATOM   2874  CA  GLY A1378     -15.115  43.605  -3.809  1.00 88.20           C  
ANISOU 2874  CA  GLY A1378    10606   9887  13020   1262   -441   -267       C  
ATOM   2875  C   GLY A1378     -16.115  43.653  -2.673  1.00 94.33           C  
ANISOU 2875  C   GLY A1378    11285  10704  13853   1261   -395   -220       C  
ATOM   2876  O   GLY A1378     -17.029  44.482  -2.720  1.00 99.59           O  
ANISOU 2876  O   GLY A1378    11948  11376  14517   1329   -372   -210       O  
ATOM   2877  N   ASP A1379     -16.000  42.786  -1.660  1.00 98.51           N  
ANISOU 2877  N   ASP A1379    11736  11261  14432   1193   -378   -187       N  
ATOM   2878  CA  ASP A1379     -16.949  42.766  -0.544  1.00 92.95           C  
ANISOU 2878  CA  ASP A1379    10938  10595  13784   1193   -327   -137       C  
ATOM   2879  C   ASP A1379     -16.118  43.000   0.711  1.00 83.23           C  
ANISOU 2879  C   ASP A1379     9743   9386  12495   1142   -231   -124       C  
ATOM   2880  O   ASP A1379     -15.571  42.049   1.291  1.00 93.64           O  
ANISOU 2880  O   ASP A1379    11023  10719  13836   1078   -234   -107       O  
ATOM   2881  CB  ASP A1379     -17.738  41.458  -0.470  1.00 97.22           C  
ANISOU 2881  CB  ASP A1379    11342  11147  14448   1163   -394   -105       C  
ATOM   2882  CG  ASP A1379     -18.807  41.476   0.621  1.00102.93           C  
ANISOU 2882  CG  ASP A1379    11964  11908  15236   1170   -336    -49       C  
ATOM   2883  OD1 ASP A1379     -19.030  42.547   1.227  1.00105.15           O  
ANISOU 2883  OD1 ASP A1379    12282  12205  15463   1210   -250    -37       O  
ATOM   2884  OD2 ASP A1379     -19.431  40.422   0.870  1.00108.54           O  
ANISOU 2884  OD2 ASP A1379    12560  12629  16051   1136   -371    -17       O  
ATOM   2885  N   PRO A1380     -15.989  44.255   1.158  1.00 65.62           N  
ANISOU 2885  N   PRO A1380     7593   7157  10183   1170   -144   -132       N  
ATOM   2886  CA  PRO A1380     -15.134  44.541   2.324  1.00 61.52           C  
ANISOU 2886  CA  PRO A1380     7117   6659   9596   1119    -59   -130       C  
ATOM   2887  C   PRO A1380     -15.545  43.825   3.598  1.00 62.20           C  
ANISOU 2887  C   PRO A1380     7109   6788   9737   1087    -24    -76       C  
ATOM   2888  O   PRO A1380     -14.679  43.493   4.415  1.00 59.86           O  
ANISOU 2888  O   PRO A1380     6825   6515   9403   1031     10    -72       O  
ATOM   2889  CB  PRO A1380     -15.241  46.070   2.470  1.00 51.66           C  
ANISOU 2889  CB  PRO A1380     5968   5396   8264   1166     23   -149       C  
ATOM   2890  CG  PRO A1380     -15.741  46.552   1.157  1.00 52.41           C  
ANISOU 2890  CG  PRO A1380     6096   5454   8362   1237    -25   -171       C  
ATOM   2891  CD  PRO A1380     -16.617  45.469   0.622  1.00 63.59           C  
ANISOU 2891  CD  PRO A1380     7393   6880   9888   1251   -121   -146       C  
ATOM   2892  N   GLY A1381     -16.835  43.583   3.811  1.00 62.39           N  
ANISOU 2892  N   GLY A1381     7036   6824   9844   1123    -27    -32       N  
ATOM   2893  CA  GLY A1381     -17.235  42.909   5.033  1.00 64.84           C  
ANISOU 2893  CA  GLY A1381     7260   7170  10207   1096     17     24       C  
ATOM   2894  C   GLY A1381     -16.808  41.456   5.046  1.00 59.77           C  
ANISOU 2894  C   GLY A1381     6554   6531   9627   1033    -39     39       C  
ATOM   2895  O   GLY A1381     -16.399  40.928   6.085  1.00 52.39           O  
ANISOU 2895  O   GLY A1381     5600   5622   8685    993      5     69       O  
ATOM   2896  N   GLU A1382     -16.865  40.801   3.885  1.00 65.58           N  
ANISOU 2896  N   GLU A1382     7264   7238  10417   1029   -137     17       N  
ATOM   2897  CA  GLU A1382     -16.352  39.441   3.785  1.00 72.64           C  
ANISOU 2897  CA  GLU A1382     8118   8124  11360    972   -191     25       C  
ATOM   2898  C   GLU A1382     -14.848  39.407   4.015  1.00 59.58           C  
ANISOU 2898  C   GLU A1382     6548   6476   9612    931   -172      0       C  
ATOM   2899  O   GLU A1382     -14.324  38.453   4.607  1.00 43.98           O  
ANISOU 2899  O   GLU A1382     4545   4515   7651    887   -167     25       O  
ATOM   2900  CB  GLU A1382     -16.692  38.880   2.404  1.00 83.69           C  
ANISOU 2900  CB  GLU A1382     9491   9485  12822    981   -302     -3       C  
ATOM   2901  CG  GLU A1382     -17.812  37.851   2.370  1.00 84.43           C  
ANISOU 2901  CG  GLU A1382     9457   9574  13049    967   -349     32       C  
ATOM   2902  CD  GLU A1382     -17.615  36.818   1.267  1.00 80.30           C  
ANISOU 2902  CD  GLU A1382     8924   9010  12577    940   -458      3       C  
ATOM   2903  OE1 GLU A1382     -16.590  36.102   1.288  1.00 73.74           O  
ANISOU 2903  OE1 GLU A1382     8133   8165  11719    898   -468     -4       O  
ATOM   2904  OE2 GLU A1382     -18.484  36.731   0.368  1.00 82.43           O  
ANISOU 2904  OE2 GLU A1382     9147   9265  12910    965   -535    -15       O  
ATOM   2905  N   LEU A1383     -14.138  40.443   3.551  1.00 58.89           N  
ANISOU 2905  N   LEU A1383     6566   6381   9430    948   -159    -49       N  
ATOM   2906  CA  LEU A1383     -12.692  40.500   3.743  1.00 54.48           C  
ANISOU 2906  CA  LEU A1383     6081   5834   8783    907   -140    -77       C  
ATOM   2907  C   LEU A1383     -12.327  40.741   5.204  1.00 63.15           C  
ANISOU 2907  C   LEU A1383     7184   6981   9829    882    -53    -53       C  
ATOM   2908  O   LEU A1383     -11.401  40.116   5.737  1.00 58.98           O  
ANISOU 2908  O   LEU A1383     6656   6480   9272    839    -48    -46       O  
ATOM   2909  CB  LEU A1383     -12.102  41.599   2.858  1.00 35.11           C  
ANISOU 2909  CB  LEU A1383     3736   3356   6250    928   -140   -134       C  
ATOM   2910  CG  LEU A1383     -10.596  41.857   2.962  1.00 48.28           C  
ANISOU 2910  CG  LEU A1383     5483   5037   7825    884   -115   -170       C  
ATOM   2911  CD1 LEU A1383      -9.778  40.578   2.784  1.00 50.11           C  
ANISOU 2911  CD1 LEU A1383     5683   5278   8079    845   -168   -162       C  
ATOM   2912  CD2 LEU A1383     -10.152  42.957   1.998  1.00 54.74           C  
ANISOU 2912  CD2 LEU A1383     6405   5818   8575    907   -110   -223       C  
ATOM   2913  N   ALA A1384     -13.058  41.635   5.873  1.00 60.71           N  
ANISOU 2913  N   ALA A1384     6881   6683   9504    913     14    -39       N  
ATOM   2914  CA  ALA A1384     -12.840  41.861   7.295  1.00 47.82           C  
ANISOU 2914  CA  ALA A1384     5255   5095   7821    896     96    -15       C  
ATOM   2915  C   ALA A1384     -13.158  40.612   8.101  1.00 52.75           C  
ANISOU 2915  C   ALA A1384     5784   5744   8514    878     98     46       C  
ATOM   2916  O   ALA A1384     -12.460  40.293   9.072  1.00 52.60           O  
ANISOU 2916  O   ALA A1384     5773   5765   8449    849    134     62       O  
ATOM   2917  CB  ALA A1384     -13.675  43.047   7.771  1.00 44.36           C  
ANISOU 2917  CB  ALA A1384     4845   4656   7355    943    169     -9       C  
ATOM   2918  N   ASN A1385     -14.207  39.884   7.702  1.00 60.76           N  
ANISOU 2918  N   ASN A1385     6710   6736   9641    894     58     82       N  
ATOM   2919  CA  ASN A1385     -14.533  38.637   8.378  1.00 57.32           C  
ANISOU 2919  CA  ASN A1385     6185   6312   9281    872     63    141       C  
ATOM   2920  C   ASN A1385     -13.426  37.615   8.184  1.00 56.05           C  
ANISOU 2920  C   ASN A1385     6035   6152   9109    828     17    133       C  
ATOM   2921  O   ASN A1385     -13.101  36.854   9.108  1.00 65.75           O  
ANISOU 2921  O   ASN A1385     7237   7407  10336    808     49    175       O  
ATOM   2922  CB  ASN A1385     -15.863  38.095   7.859  1.00 67.06           C  
ANISOU 2922  CB  ASN A1385     7319   7516  10643    889     24    172       C  
ATOM   2923  CG  ASN A1385     -17.055  38.844   8.419  1.00 76.60           C  
ANISOU 2923  CG  ASN A1385     8488   8738  11877    935     88    205       C  
ATOM   2924  OD1 ASN A1385     -16.966  39.484   9.466  1.00 82.04           O  
ANISOU 2924  OD1 ASN A1385     9213   9458  12500    950    174    221       O  
ATOM   2925  ND2 ASN A1385     -18.186  38.757   7.727  1.00 80.78           N  
ANISOU 2925  ND2 ASN A1385     8944   9248  12502    960     46    213       N  
ATOM   2926  N   ALA A1386     -12.828  37.588   6.990  1.00 38.04           N  
ANISOU 2926  N   ALA A1386     3796   3842   6816    820    -55     84       N  
ATOM   2927  CA  ALA A1386     -11.724  36.666   6.766  1.00 44.08           C  
ANISOU 2927  CA  ALA A1386     4577   4608   7562    785    -95     77       C  
ATOM   2928  C   ALA A1386     -10.519  37.055   7.606  1.00 54.24           C  
ANISOU 2928  C   ALA A1386     5923   5949   8739    767    -44     65       C  
ATOM   2929  O   ALA A1386      -9.777  36.186   8.082  1.00 54.21           O  
ANISOU 2929  O   ALA A1386     5906   5970   8719    745    -44     88       O  
ATOM   2930  CB  ALA A1386     -11.352  36.640   5.288  1.00 52.99           C  
ANISOU 2930  CB  ALA A1386     5746   5694   8695    788   -176     26       C  
ATOM   2931  N   ILE A1387     -10.289  38.359   7.771  1.00 60.14           N  
ANISOU 2931  N   ILE A1387     6735   6713   9404    775     -3     27       N  
ATOM   2932  CA  ILE A1387      -9.195  38.818   8.621  1.00 55.45           C  
ANISOU 2932  CA  ILE A1387     6193   6173   8703    751     43      9       C  
ATOM   2933  C   ILE A1387      -9.444  38.441  10.082  1.00 56.77           C  
ANISOU 2933  C   ILE A1387     6321   6387   8863    753    104     64       C  
ATOM   2934  O   ILE A1387      -8.518  38.040  10.799  1.00 58.32           O  
ANISOU 2934  O   ILE A1387     6525   6633   9002    733    117     71       O  
ATOM   2935  CB  ILE A1387      -9.003  40.334   8.437  1.00 52.50           C  
ANISOU 2935  CB  ILE A1387     5903   5795   8250    755     77    -46       C  
ATOM   2936  CG1 ILE A1387      -8.471  40.627   7.028  1.00 47.60           C  
ANISOU 2936  CG1 ILE A1387     5333   5133   7621    752     23    -99       C  
ATOM   2937  CG2 ILE A1387      -8.078  40.894   9.510  1.00 46.35           C  
ANISOU 2937  CG2 ILE A1387     5172   5075   7366    726    132    -66       C  
ATOM   2938  CD1 ILE A1387      -8.401  42.098   6.692  1.00 31.52           C  
ANISOU 2938  CD1 ILE A1387     3383   3075   5518    761     59   -150       C  
ATOM   2939  N   LEU A1388     -10.700  38.526  10.543  1.00 57.80           N  
ANISOU 2939  N   LEU A1388     6406   6504   9052    783    143    105       N  
ATOM   2940  CA  LEU A1388     -10.997  38.101  11.911  1.00 59.87           C  
ANISOU 2940  CA  LEU A1388     6631   6805   9313    791    207    164       C  
ATOM   2941  C   LEU A1388     -10.798  36.600  12.078  1.00 61.57           C  
ANISOU 2941  C   LEU A1388     6787   7022   9585    777    182    214       C  
ATOM   2942  O   LEU A1388     -10.290  36.148  13.116  1.00 66.79           O  
ANISOU 2942  O   LEU A1388     7447   7730  10200    775    220    246       O  
ATOM   2943  CB  LEU A1388     -12.419  38.505  12.295  1.00 61.59           C  
ANISOU 2943  CB  LEU A1388     6809   7005   9588    829    259    202       C  
ATOM   2944  CG  LEU A1388     -12.661  40.003  12.500  1.00 57.52           C  
ANISOU 2944  CG  LEU A1388     6361   6493   9001    855    310    167       C  
ATOM   2945  CD1 LEU A1388     -14.142  40.350  12.419  1.00 50.79           C  
ANISOU 2945  CD1 LEU A1388     5459   5613   8227    901    340    200       C  
ATOM   2946  CD2 LEU A1388     -12.082  40.444  13.834  1.00 55.53           C  
ANISOU 2946  CD2 LEU A1388     6161   6296   8642    852    381    168       C  
ATOM   2947  N   LYS A1389     -11.163  35.819  11.049  1.00 60.07           N  
ANISOU 2947  N   LYS A1389     6552   6780   9490    770    117    218       N  
ATOM   2948  CA  LYS A1389     -10.912  34.382  11.073  1.00 60.42           C  
ANISOU 2948  CA  LYS A1389     6554   6814   9590    754     91    259       C  
ATOM   2949  C   LYS A1389      -9.416  34.092  11.119  1.00 63.53           C  
ANISOU 2949  C   LYS A1389     6997   7246   9894    738     70    236       C  
ATOM   2950  O   LYS A1389      -8.971  33.187  11.833  1.00 72.66           O  
ANISOU 2950  O   LYS A1389     8137   8430  11041    738     90    280       O  
ATOM   2951  CB  LYS A1389     -11.547  33.715   9.862  1.00 61.36           C  
ANISOU 2951  CB  LYS A1389     6629   6865   9819    745     19    254       C  
ATOM   2952  CG  LYS A1389     -11.169  32.239   9.768  1.00 54.59           C  
ANISOU 2952  CG  LYS A1389     5745   5986   9011    726    -11    287       C  
ATOM   2953  CD  LYS A1389     -11.855  31.316  10.747  1.00 69.95           C  
ANISOU 2953  CD  LYS A1389     7625   7926  11026    726     44    365       C  
ATOM   2954  CE  LYS A1389     -11.476  29.865  10.417  1.00 65.31           C  
ANISOU 2954  CE  LYS A1389     7024   7300  10492    706      8    390       C  
ATOM   2955  NZ  LYS A1389     -12.261  28.852  11.151  1.00 57.12           N  
ANISOU 2955  NZ  LYS A1389     5922   6236   9545    700     57    464       N  
ATOM   2956  N   ALA A1390      -8.619  34.870  10.381  1.00 50.65           N  
ANISOU 2956  N   ALA A1390     5427   5622   8197    727     36    170       N  
ATOM   2957  CA  ALA A1390      -7.176  34.680  10.424  1.00 54.72           C  
ANISOU 2957  CA  ALA A1390     5980   6182   8627    711     19    147       C  
ATOM   2958  C   ALA A1390      -6.624  34.997  11.802  1.00 60.57           C  
ANISOU 2958  C   ALA A1390     6738   7002   9276    712     80    161       C  
ATOM   2959  O   ALA A1390      -5.718  34.306  12.287  1.00 60.32           O  
ANISOU 2959  O   ALA A1390     6703   7018   9199    710     78    180       O  
ATOM   2960  CB  ALA A1390      -6.506  35.535   9.359  1.00 60.45           C  
ANISOU 2960  CB  ALA A1390     6765   6895   9306    697    -20     76       C  
ATOM   2961  N   LEU A1391      -7.184  36.014  12.462  1.00 65.86           N  
ANISOU 2961  N   LEU A1391     7426   7686   9912    720    133    153       N  
ATOM   2962  CA  LEU A1391      -6.756  36.308  13.822  1.00 58.79           C  
ANISOU 2962  CA  LEU A1391     6550   6863   8926    724    190    165       C  
ATOM   2963  C   LEU A1391      -7.096  35.171  14.775  1.00 56.78           C  
ANISOU 2963  C   LEU A1391     6244   6625   8704    749    224    244       C  
ATOM   2964  O   LEU A1391      -6.276  34.799  15.619  1.00 47.69           O  
ANISOU 2964  O   LEU A1391     5101   5540   7479    755    239    261       O  
ATOM   2965  CB  LEU A1391      -7.402  37.610  14.302  1.00 43.73           C  
ANISOU 2965  CB  LEU A1391     4680   4955   6980    733    245    142       C  
ATOM   2966  CG  LEU A1391      -7.215  37.912  15.796  1.00 38.35           C  
ANISOU 2966  CG  LEU A1391     4021   4340   6209    746    310    159       C  
ATOM   2967  CD1 LEU A1391      -5.767  38.114  16.161  1.00 42.10           C  
ANISOU 2967  CD1 LEU A1391     4536   4889   6570    717    292    114       C  
ATOM   2968  CD2 LEU A1391      -8.048  39.093  16.264  1.00 41.85           C  
ANISOU 2968  CD2 LEU A1391     4502   4770   6628    765    372    146       C  
ATOM   2969  N   GLU A1392      -8.279  34.574  14.626  1.00 59.58           N  
ANISOU 2969  N   GLU A1392     6544   6923   9170    765    235    295       N  
ATOM   2970  CA  GLU A1392      -8.636  33.450  15.475  1.00 64.40           C  
ANISOU 2970  CA  GLU A1392     7109   7539   9823    786    274    375       C  
ATOM   2971  C   GLU A1392      -7.752  32.243  15.176  1.00 59.95           C  
ANISOU 2971  C   GLU A1392     6536   6979   9265    780    231    393       C  
ATOM   2972  O   GLU A1392      -7.385  31.493  16.085  1.00 68.94           O  
ANISOU 2972  O   GLU A1392     7668   8156  10371    801    265    444       O  
ATOM   2973  CB  GLU A1392     -10.113  33.182  15.270  1.00 82.74           C  
ANISOU 2973  CB  GLU A1392     9370   9796  12271    795    295    418       C  
ATOM   2974  CG  GLU A1392     -10.897  34.455  15.684  1.00101.44           C  
ANISOU 2974  CG  GLU A1392    11754  12172  14616    813    347    404       C  
ATOM   2975  CD  GLU A1392     -10.807  34.863  17.137  1.00109.37           C  
ANISOU 2975  CD  GLU A1392    12789  13237  15531    841    429    431       C  
ATOM   2976  OE1 GLU A1392     -10.345  34.111  18.010  1.00103.87           O  
ANISOU 2976  OE1 GLU A1392    12090  12578  14798    855    458    475       O  
ATOM   2977  OE2 GLU A1392     -11.046  36.051  17.348  1.00112.26           O  
ANISOU 2977  OE2 GLU A1392    13196  13614  15844    852    460    397       O  
ATOM   2978  N   LEU A1393      -7.388  32.048  13.905  1.00 60.40           N  
ANISOU 2978  N   LEU A1393     6597   6995   9355    758    159    352       N  
ATOM   2979  CA  LEU A1393      -6.497  30.947  13.548  1.00 62.69           C  
ANISOU 2979  CA  LEU A1393     6888   7286   9645    757    119    366       C  
ATOM   2980  C   LEU A1393      -5.088  31.134  14.094  1.00 74.90           C  
ANISOU 2980  C   LEU A1393     8471   8922  11064    762    120    346       C  
ATOM   2981  O   LEU A1393      -4.415  30.144  14.410  1.00 82.91           O  
ANISOU 2981  O   LEU A1393     9480   9963  12060    781    118    385       O  
ATOM   2982  CB  LEU A1393      -6.423  30.743  12.031  1.00 50.86           C  
ANISOU 2982  CB  LEU A1393     5395   5724   8206    737     43    325       C  
ATOM   2983  CG  LEU A1393      -7.631  30.231  11.262  1.00 45.79           C  
ANISOU 2983  CG  LEU A1393     4710   4991   7696    728     17    340       C  
ATOM   2984  CD1 LEU A1393      -7.408  30.397   9.769  1.00 36.41           C  
ANISOU 2984  CD1 LEU A1393     3548   3756   6530    714    -62    281       C  
ATOM   2985  CD2 LEU A1393      -7.880  28.783  11.607  1.00 61.12           C  
ANISOU 2985  CD2 LEU A1393     6615   6900   9708    733     32    409       C  
ATOM   2986  N   SER A1394      -4.631  32.383  14.223  1.00 79.98           N  
ANISOU 2986  N   SER A1394     9153   9614  11622    747    123    287       N  
ATOM   2987  CA  SER A1394      -3.290  32.625  14.736  1.00 76.27           C  
ANISOU 2987  CA  SER A1394     8710   9235  11033    744    118    261       C  
ATOM   2988  C   SER A1394      -3.143  32.133  16.168  1.00 87.87           C  
ANISOU 2988  C   SER A1394    10168  10772  12446    778    169    317       C  
ATOM   2989  O   SER A1394      -2.018  31.883  16.614  1.00 98.38           O  
ANISOU 2989  O   SER A1394    11506  12182  13692    788    157    315       O  
ATOM   2990  CB  SER A1394      -2.948  34.113  14.661  1.00 66.33           C  
ANISOU 2990  CB  SER A1394     7496   8007   9700    712    119    184       C  
ATOM   2991  OG  SER A1394      -3.602  34.817  15.703  1.00 74.71           O  
ANISOU 2991  OG  SER A1394     8570   9088  10727    722    179    192       O  
ATOM   2992  N   ARG A1395      -4.255  31.988  16.892  1.00 85.56           N  
ANISOU 2992  N   ARG A1395     9858  10452  12199    801    226    370       N  
ATOM   2993  CA  ARG A1395      -4.205  31.458  18.252  1.00 81.92           C  
ANISOU 2993  CA  ARG A1395     9392  10047  11687    843    281    432       C  
ATOM   2994  C   ARG A1395      -3.552  30.080  18.287  1.00 76.31           C  
ANISOU 2994  C   ARG A1395     8663   9349  10983    871    266    485       C  
ATOM   2995  O   ARG A1395      -2.694  29.807  19.134  1.00 84.44           O  
ANISOU 2995  O   ARG A1395     9704  10462  11917    902    277    502       O  
ATOM   2996  CB  ARG A1395      -5.620  31.388  18.828  1.00 85.63           C  
ANISOU 2996  CB  ARG A1395     9840  10467  12230    864    349    489       C  
ATOM   2997  CG  ARG A1395      -6.388  32.697  18.768  1.00 84.69           C  
ANISOU 2997  CG  ARG A1395     9738  10328  12113    847    371    446       C  
ATOM   2998  CD  ARG A1395      -5.750  33.734  19.664  1.00 90.24           C  
ANISOU 2998  CD  ARG A1395    10495  11114  12679    850    393    402       C  
ATOM   2999  NE  ARG A1395      -6.421  35.025  19.570  1.00 94.76           N  
ANISOU 2999  NE  ARG A1395    11097  11661  13245    837    418    358       N  
ATOM   3000  CZ  ARG A1395      -7.544  35.331  20.209  1.00 99.54           C  
ANISOU 3000  CZ  ARG A1395    11699  12244  13880    866    487    396       C  
ATOM   3001  NH1 ARG A1395      -8.134  34.436  20.990  1.00113.51           N  
ANISOU 3001  NH1 ARG A1395    13432  14008  15688    906    540    481       N  
ATOM   3002  NH2 ARG A1395      -8.079  36.534  20.064  1.00 94.16           N  
ANISOU 3002  NH2 ARG A1395    11050  11539  13186    859    508    354       N  
ATOM   3003  N   SER A1396      -3.938  29.203  17.369  1.00 72.26           N  
ANISOU 3003  N   SER A1396     8125   8752  10578    864    240    508       N  
ATOM   3004  CA  SER A1396      -3.342  27.884  17.243  1.00 79.44           C  
ANISOU 3004  CA  SER A1396     9027   9657  11501    890    226    555       C  
ATOM   3005  C   SER A1396      -2.069  27.956  16.409  1.00 80.14           C  
ANISOU 3005  C   SER A1396     9133   9782  11536    877    158    501       C  
ATOM   3006  O   SER A1396      -1.816  28.937  15.704  1.00 88.69           O  
ANISOU 3006  O   SER A1396    10229  10868  12600    839    119    428       O  
ATOM   3007  CB  SER A1396      -4.329  26.912  16.605  1.00 97.49           C  
ANISOU 3007  CB  SER A1396    11284  11830  13928    882    228    599       C  
ATOM   3008  OG  SER A1396      -5.645  27.150  17.072  1.00111.86           O  
ANISOU 3008  OG  SER A1396    13077  13608  15816    877    282    630       O  
ATOM   3009  N   ASP A1397      -1.254  26.908  16.506  1.00 76.04           N  
ANISOU 3009  N   ASP A1397     8614   9289  10991    913    150    541       N  
ATOM   3010  CA  ASP A1397      -0.066  26.838  15.666  1.00 79.28           C  
ANISOU 3010  CA  ASP A1397     9034   9729  11359    908     90    499       C  
ATOM   3011  C   ASP A1397      -0.462  26.861  14.196  1.00 83.97           C  
ANISOU 3011  C   ASP A1397     9634  10224  12048    871     42    460       C  
ATOM   3012  O   ASP A1397      -1.415  26.197  13.783  1.00 90.00           O  
ANISOU 3012  O   ASP A1397    10387  10890  12917    867     46    491       O  
ATOM   3013  CB  ASP A1397       0.741  25.576  15.956  1.00 86.71           C  
ANISOU 3013  CB  ASP A1397     9975  10702  12269    964     95    559       C  
ATOM   3014  CG  ASP A1397       1.934  25.432  15.031  1.00 94.19           C  
ANISOU 3014  CG  ASP A1397    10930  11677  13183    965     38    523       C  
ATOM   3015  OD1 ASP A1397       2.776  26.358  15.000  1.00 99.30           O  
ANISOU 3015  OD1 ASP A1397    11575  12406  13748    943     11    463       O  
ATOM   3016  OD2 ASP A1397       2.020  24.405  14.324  1.00 94.21           O  
ANISOU 3016  OD2 ASP A1397    10942  11614  13241    985     23    552       O  
ATOM   3017  N   LEU A1398       0.290  27.626  13.405  1.00 84.32           N  
ANISOU 3017  N   LEU A1398     9693  10294  12050    843     -4    391       N  
ATOM   3018  CA  LEU A1398       0.020  27.812  11.986  1.00 61.87           C  
ANISOU 3018  CA  LEU A1398     6865   7367   9277    813    -52    346       C  
ATOM   3019  C   LEU A1398       1.079  27.164  11.104  1.00 54.98           C  
ANISOU 3019  C   LEU A1398     6007   6494   8388    830    -95    338       C  
ATOM   3020  O   LEU A1398       1.062  27.371   9.886  1.00 55.71           O  
ANISOU 3020  O   LEU A1398     6121   6528   8519    810   -137    295       O  
ATOM   3021  CB  LEU A1398      -0.066  29.307  11.668  1.00 52.28           C  
ANISOU 3021  CB  LEU A1398     5667   6165   8033    771    -62    272       C  
ATOM   3022  CG  LEU A1398      -1.279  30.124  12.125  1.00 53.26           C  
ANISOU 3022  CG  LEU A1398     5786   6262   8189    753    -27    265       C  
ATOM   3023  CD1 LEU A1398      -1.016  31.609  11.893  1.00 53.92           C  
ANISOU 3023  CD1 LEU A1398     5900   6373   8214    718    -32    191       C  
ATOM   3024  CD2 LEU A1398      -2.563  29.686  11.448  1.00 51.35           C  
ANISOU 3024  CD2 LEU A1398     5528   5911   8070    750    -38    285       C  
ATOM   3025  N   SER A1399       1.995  26.377  11.687  1.00 64.04           N  
ANISOU 3025  N   SER A1399     7147   7707   9476    872    -83    381       N  
ATOM   3026  CA  SER A1399       3.134  25.877  10.919  1.00 60.52           C  
ANISOU 3026  CA  SER A1399     6714   7280   9001    894   -118    373       C  
ATOM   3027  C   SER A1399       2.697  24.940   9.793  1.00 61.33           C  
ANISOU 3027  C   SER A1399     6841   7264   9196    903   -145    387       C  
ATOM   3028  O   SER A1399       3.236  25.027   8.681  1.00 50.29           O  
ANISOU 3028  O   SER A1399     5468   5842   7800    899   -185    349       O  
ATOM   3029  CB  SER A1399       4.125  25.195  11.865  1.00 69.28           C  
ANISOU 3029  CB  SER A1399     7807   8490  10028    948    -96    423       C  
ATOM   3030  OG  SER A1399       4.649  26.136  12.798  1.00 78.76           O  
ANISOU 3030  OG  SER A1399     8986   9807  11132    935    -84    396       O  
ATOM   3031  N   LYS A1400       1.750  24.017  10.044  1.00 78.05           N  
ANISOU 3031  N   LYS A1400     8958   9305  11394    916   -123    441       N  
ATOM   3032  CA  LYS A1400       1.339  23.171   8.907  1.00 87.98           C  
ANISOU 3032  CA  LYS A1400    10242  10445  12739    916   -157    443       C  
ATOM   3033  C   LYS A1400       0.608  23.988   7.839  1.00 90.36           C  
ANISOU 3033  C   LYS A1400    10554  10678  13099    868   -201    377       C  
ATOM   3034  O   LYS A1400       0.662  23.621   6.666  1.00101.35           O  
ANISOU 3034  O   LYS A1400    11979  11999  14529    869   -246    353       O  
ATOM   3035  CB  LYS A1400       0.635  21.842   9.202  1.00 97.85           C  
ANISOU 3035  CB  LYS A1400    11495  11616  14068    935   -129    511       C  
ATOM   3036  CG  LYS A1400       1.550  20.886   9.961  1.00111.80           C  
ANISOU 3036  CG  LYS A1400    13270  13439  15771    998    -91    576       C  
ATOM   3037  CD  LYS A1400       0.905  19.542  10.240  1.00122.62           C  
ANISOU 3037  CD  LYS A1400    14654  14721  17217   1018    -54    646       C  
ATOM   3038  CE  LYS A1400       1.935  18.671  10.966  1.00125.23           C  
ANISOU 3038  CE  LYS A1400    15000  15116  17467   1094    -15    711       C  
ATOM   3039  NZ  LYS A1400       1.424  17.302  11.237  1.00130.98           N  
ANISOU 3039  NZ  LYS A1400    15754  15753  18261   1120     30    784       N  
ATOM   3040  N   PHE A1401      -0.127  25.035   8.207  1.00 77.82           N  
ANISOU 3040  N   PHE A1401     8943   9104  11519    833   -189    350       N  
ATOM   3041  CA  PHE A1401      -0.790  25.810   7.169  1.00 62.81           C  
ANISOU 3041  CA  PHE A1401     7057   7142   9667    800   -230    291       C  
ATOM   3042  C   PHE A1401       0.253  26.436   6.246  1.00 61.82           C  
ANISOU 3042  C   PHE A1401     6968   7044   9478    800   -265    234       C  
ATOM   3043  O   PHE A1401       0.148  26.341   5.015  1.00 68.16           O  
ANISOU 3043  O   PHE A1401     7804   7776  10318    800   -312    201       O  
ATOM   3044  CB  PHE A1401      -1.642  26.904   7.816  1.00 65.96           C  
ANISOU 3044  CB  PHE A1401     7428   7563  10070    772   -201    276       C  
ATOM   3045  CG  PHE A1401      -2.835  27.316   7.013  1.00 72.37           C  
ANISOU 3045  CG  PHE A1401     8237   8293  10967    748   -232    244       C  
ATOM   3046  CD1 PHE A1401      -2.909  27.057   5.654  1.00 75.15           C  
ANISOU 3046  CD1 PHE A1401     8619   8571  11363    747   -293    209       C  
ATOM   3047  CD2 PHE A1401      -3.868  28.007   7.613  1.00 62.05           C  
ANISOU 3047  CD2 PHE A1401     6899   6989   9690    732   -201    248       C  
ATOM   3048  CE1 PHE A1401      -4.006  27.461   4.913  1.00 57.14           C  
ANISOU 3048  CE1 PHE A1401     6331   6223   9154    730   -328    178       C  
ATOM   3049  CE2 PHE A1401      -4.965  28.409   6.878  1.00 46.54           C  
ANISOU 3049  CE2 PHE A1401     4924   4958   7801    717   -231    220       C  
ATOM   3050  CZ  PHE A1401      -5.033  28.134   5.526  1.00 45.83           C  
ANISOU 3050  CZ  PHE A1401     4860   4799   7754    715   -298    185       C  
ATOM   3051  N   ARG A1402       1.283  27.055   6.825  1.00 60.39           N  
ANISOU 3051  N   ARG A1402     6782   6965   9200    802   -243    222       N  
ATOM   3052  CA  ARG A1402       2.356  27.624   6.014  1.00 55.20           C  
ANISOU 3052  CA  ARG A1402     6153   6338   8483    799   -267    173       C  
ATOM   3053  C   ARG A1402       3.102  26.551   5.226  1.00 59.39           C  
ANISOU 3053  C   ARG A1402     6708   6841   9018    838   -293    192       C  
ATOM   3054  O   ARG A1402       3.576  26.816   4.116  1.00 60.87           O  
ANISOU 3054  O   ARG A1402     6932   7001   9196    840   -322    152       O  
ATOM   3055  CB  ARG A1402       3.360  28.362   6.898  1.00 50.20           C  
ANISOU 3055  CB  ARG A1402     5498   5827   7749    789   -237    159       C  
ATOM   3056  CG  ARG A1402       2.765  29.316   7.915  1.00 51.15           C  
ANISOU 3056  CG  ARG A1402     5600   5988   7848    758   -203    147       C  
ATOM   3057  CD  ARG A1402       3.861  30.147   8.563  1.00 47.97           C  
ANISOU 3057  CD  ARG A1402     5186   5700   7342    738   -186    116       C  
ATOM   3058  NE  ARG A1402       3.348  30.980   9.647  1.00 64.92           N  
ANISOU 3058  NE  ARG A1402     7323   7888   9458    714   -150    106       N  
ATOM   3059  CZ  ARG A1402       2.764  32.162   9.489  1.00 74.70           C  
ANISOU 3059  CZ  ARG A1402     8585   9097  10701    676   -140     57       C  
ATOM   3060  NH1 ARG A1402       2.607  32.673   8.276  1.00 76.61           N  
ANISOU 3060  NH1 ARG A1402     8862   9271  10977    660   -163     14       N  
ATOM   3061  NH2 ARG A1402       2.331  32.836  10.550  1.00 76.09           N  
ANISOU 3061  NH2 ARG A1402     8757   9312  10843    662   -103     54       N  
ATOM   3062  N   GLU A1403       3.262  25.353   5.802  1.00 49.24           N  
ANISOU 3062  N   GLU A1403     5410   5561   7739    875   -276    254       N  
ATOM   3063  CA  GLU A1403       3.903  24.264   5.073  1.00 49.88           C  
ANISOU 3063  CA  GLU A1403     5522   5606   7825    919   -295    277       C  
ATOM   3064  C   GLU A1403       3.084  23.863   3.856  1.00 59.37           C  
ANISOU 3064  C   GLU A1403     6768   6679   9113    912   -339    256       C  
ATOM   3065  O   GLU A1403       3.638  23.619   2.775  1.00 70.34           O  
ANISOU 3065  O   GLU A1403     8201   8031  10495    934   -369    234       O  
ATOM   3066  CB  GLU A1403       4.122  23.074   6.004  1.00 74.80           C  
ANISOU 3066  CB  GLU A1403     8662   8786  10972    963   -261    353       C  
ATOM   3067  CG  GLU A1403       4.885  21.909   5.387  1.00 94.39           C  
ANISOU 3067  CG  GLU A1403    11181  11237  13447   1018   -270    384       C  
ATOM   3068  CD  GLU A1403       4.964  20.700   6.307  1.00115.99           C  
ANISOU 3068  CD  GLU A1403    13910  13982  16179   1067   -230    463       C  
ATOM   3069  OE1 GLU A1403       4.075  20.548   7.174  1.00119.67           O  
ANISOU 3069  OE1 GLU A1403    14354  14432  16685   1051   -200    495       O  
ATOM   3070  OE2 GLU A1403       5.936  19.916   6.171  1.00128.29           O  
ANISOU 3070  OE2 GLU A1403    15487  15564  17692   1126   -222    496       O  
ATOM   3071  N   ASN A1404       1.756  23.832   4.003  1.00 62.67           N  
ANISOU 3071  N   ASN A1404     7171   7029   9612    882   -343    259       N  
ATOM   3072  CA  ASN A1404       0.904  23.520   2.865  1.00 63.11           C  
ANISOU 3072  CA  ASN A1404     7260   6969   9751    870   -394    231       C  
ATOM   3073  C   ASN A1404       0.977  24.624   1.823  1.00 52.82           C  
ANISOU 3073  C   ASN A1404     5986   5656   8428    856   -431    162       C  
ATOM   3074  O   ASN A1404       0.936  24.349   0.618  1.00 60.93           O  
ANISOU 3074  O   ASN A1404     7062   6608   9479    869   -478    132       O  
ATOM   3075  CB  ASN A1404      -0.545  23.318   3.319  1.00 69.82           C  
ANISOU 3075  CB  ASN A1404     8072   7761  10695    837   -389    250       C  
ATOM   3076  CG  ASN A1404      -0.730  22.081   4.186  1.00 69.06           C  
ANISOU 3076  CG  ASN A1404     7958   7648  10634    852   -349    322       C  
ATOM   3077  OD1 ASN A1404       0.124  21.193   4.222  1.00 74.13           O  
ANISOU 3077  OD1 ASN A1404     8628   8297  11242    891   -337    356       O  
ATOM   3078  ND2 ASN A1404      -1.865  22.010   4.875  1.00 61.39           N  
ANISOU 3078  ND2 ASN A1404     6942   6652   9733    823   -324    348       N  
ATOM   3079  N   CYS A1405       1.103  25.879   2.271  1.00 46.66           N  
ANISOU 3079  N   CYS A1405     5184   4946   7599    833   -408    134       N  
ATOM   3080  CA  CYS A1405       1.242  26.992   1.337  1.00 49.79           C  
ANISOU 3080  CA  CYS A1405     5616   5334   7969    822   -431     71       C  
ATOM   3081  C   CYS A1405       2.549  26.909   0.555  1.00 55.50           C  
ANISOU 3081  C   CYS A1405     6382   6077   8630    851   -439     55       C  
ATOM   3082  O   CYS A1405       2.564  27.113  -0.664  1.00 49.32           O  
ANISOU 3082  O   CYS A1405     5651   5235   7852    863   -475     17       O  
ATOM   3083  CB  CYS A1405       1.194  28.315   2.100  1.00 48.32           C  
ANISOU 3083  CB  CYS A1405     5403   5219   7738    790   -393     49       C  
ATOM   3084  SG  CYS A1405      -0.382  28.708   2.836  1.00 59.37           S  
ANISOU 3084  SG  CYS A1405     6760   6593   9205    763   -380     59       S  
ATOM   3085  N   LYS A1406       3.653  26.584   1.241  1.00 60.13           N  
ANISOU 3085  N   LYS A1406     6945   6747   9153    867   -405     87       N  
ATOM   3086  CA  LYS A1406       4.954  26.487   0.584  1.00 54.71           C  
ANISOU 3086  CA  LYS A1406     6288   6092   8408    897   -406     78       C  
ATOM   3087  C   LYS A1406       4.969  25.344  -0.415  1.00 55.57           C  
ANISOU 3087  C   LYS A1406     6449   6113   8553    942   -440     93       C  
ATOM   3088  O   LYS A1406       5.442  25.493  -1.551  1.00 56.52           O  
ANISOU 3088  O   LYS A1406     6621   6198   8655    963   -460     62       O  
ATOM   3089  CB  LYS A1406       6.048  26.272   1.637  1.00 69.38           C  
ANISOU 3089  CB  LYS A1406     8097   8067  10196    910   -366    115       C  
ATOM   3090  CG  LYS A1406       7.454  26.718   1.240  1.00 82.58           C  
ANISOU 3090  CG  LYS A1406     9772   9813  11794    920   -354     95       C  
ATOM   3091  CD  LYS A1406       8.491  26.358   2.320  1.00 86.07           C  
ANISOU 3091  CD  LYS A1406    10156  10378  12170    939   -323    136       C  
ATOM   3092  CE  LYS A1406       8.219  26.979   3.685  1.00 74.99           C  
ANISOU 3092  CE  LYS A1406     8698   9055  10740    900   -299    137       C  
ATOM   3093  NZ  LYS A1406       8.379  28.452   3.693  1.00 69.23           N  
ANISOU 3093  NZ  LYS A1406     7962   8366   9976    840   -289     75       N  
ATOM   3094  N   LYS A1407       4.401  24.208  -0.016  1.00 61.84           N  
ANISOU 3094  N   LYS A1407     7236   6862   9399    956   -444    138       N  
ATOM   3095  CA  LYS A1407       4.355  23.042  -0.886  1.00 55.70           C  
ANISOU 3095  CA  LYS A1407     6514   5992   8658    994   -475    151       C  
ATOM   3096  C   LYS A1407       3.480  23.316  -2.105  1.00 55.13           C  
ANISOU 3096  C   LYS A1407     6491   5816   8639    980   -531     98       C  
ATOM   3097  O   LYS A1407       3.806  22.897  -3.228  1.00 40.75           O  
ANISOU 3097  O   LYS A1407     4737   3934   6813   1015   -563     79       O  
ATOM   3098  CB  LYS A1407       3.864  21.877  -0.035  1.00 50.69           C  
ANISOU 3098  CB  LYS A1407     5858   5333   8071   1001   -457    210       C  
ATOM   3099  CG  LYS A1407       5.014  21.020   0.503  1.00 58.01           C  
ANISOU 3099  CG  LYS A1407     6782   6319   8939   1055   -418    267       C  
ATOM   3100  CD  LYS A1407       4.597  20.290   1.784  1.00 70.15           C  
ANISOU 3100  CD  LYS A1407     8280   7874  10501   1057   -379    330       C  
ATOM   3101  CE  LYS A1407       3.795  19.035   1.590  1.00 84.01           C  
ANISOU 3101  CE  LYS A1407    10070   9511  12338   1063   -387    361       C  
ATOM   3102  NZ  LYS A1407       3.560  18.418   2.922  1.00 88.90           N  
ANISOU 3102  NZ  LYS A1407    10651  10161  12967   1070   -334    428       N  
ATOM   3103  N   ARG A1408       2.368  24.031  -1.899  1.00 61.79           N  
ANISOU 3103  N   ARG A1408     7305   6642   9529    936   -545     73       N  
ATOM   3104  CA  ARG A1408       1.477  24.376  -3.002  1.00 58.47           C  
ANISOU 3104  CA  ARG A1408     6923   6136   9155    927   -603     21       C  
ATOM   3105  C   ARG A1408       2.126  25.356  -3.978  1.00 61.60           C  
ANISOU 3105  C   ARG A1408     7371   6544   9490    945   -611    -28       C  
ATOM   3106  O   ARG A1408       2.012  25.191  -5.201  1.00 60.20           O  
ANISOU 3106  O   ARG A1408     7260   6293   9322    971   -658    -60       O  
ATOM   3107  CB  ARG A1408       0.179  24.951  -2.438  1.00 46.98           C  
ANISOU 3107  CB  ARG A1408     5414   4675   7760    882   -607     14       C  
ATOM   3108  CG  ARG A1408      -0.749  25.500  -3.483  1.00 48.60           C  
ANISOU 3108  CG  ARG A1408     5648   4812   8006    876   -665    -40       C  
ATOM   3109  CD  ARG A1408      -1.056  24.505  -4.565  1.00 58.63           C  
ANISOU 3109  CD  ARG A1408     6972   5983   9320    897   -730    -56       C  
ATOM   3110  NE  ARG A1408      -2.193  24.944  -5.360  1.00 75.97           N  
ANISOU 3110  NE  ARG A1408     9176   8121  11568    887   -793   -102       N  
ATOM   3111  CZ  ARG A1408      -2.467  24.486  -6.575  1.00 86.25           C  
ANISOU 3111  CZ  ARG A1408    10539   9343  12889    908   -862   -139       C  
ATOM   3112  NH1 ARG A1408      -1.680  23.579  -7.136  1.00 83.92           N  
ANISOU 3112  NH1 ARG A1408    10312   9026  12549    931   -864   -132       N  
ATOM   3113  NH2 ARG A1408      -3.519  24.944  -7.238  1.00 94.95           N  
ANISOU 3113  NH2 ARG A1408    11642  10420  14014    893   -915   -181       N  
ATOM   3114  N   ALA A1409       2.801  26.387  -3.461  1.00 58.92           N  
ANISOU 3114  N   ALA A1409     7006   6293   9089    929   -565    -35       N  
ATOM   3115  CA  ALA A1409       3.450  27.355  -4.340  1.00 46.96           C  
ANISOU 3115  CA  ALA A1409     5539   4787   7518    941   -561    -79       C  
ATOM   3116  C   ALA A1409       4.590  26.720  -5.123  1.00 53.81           C  
ANISOU 3116  C   ALA A1409     6457   5646   8341    990   -560    -71       C  
ATOM   3117  O   ALA A1409       4.803  27.050  -6.298  1.00 45.87           O  
ANISOU 3117  O   ALA A1409     5519   4594   7315   1018   -579   -105       O  
ATOM   3118  CB  ALA A1409       3.955  28.545  -3.533  1.00 42.26           C  
ANISOU 3118  CB  ALA A1409     4903   4286   6868    904   -507    -89       C  
ATOM   3119  N   MET A1410       5.326  25.796  -4.496  1.00 68.48           N  
ANISOU 3119  N   MET A1410     8288   7548  10182   1009   -535    -22       N  
ATOM   3120  CA  MET A1410       6.419  25.138  -5.203  1.00 71.24           C  
ANISOU 3120  CA  MET A1410     8684   7894  10490   1064   -529     -7       C  
ATOM   3121  C   MET A1410       5.881  24.205  -6.280  1.00 70.57           C  
ANISOU 3121  C   MET A1410     8677   7690  10448   1103   -583    -16       C  
ATOM   3122  O   MET A1410       6.352  24.224  -7.423  1.00 76.89           O  
ANISOU 3122  O   MET A1410     9549   8448  11219   1144   -596    -39       O  
ATOM   3123  CB  MET A1410       7.321  24.387  -4.218  1.00 73.00           C  
ANISOU 3123  CB  MET A1410     8856   8199  10680   1084   -488     51       C  
ATOM   3124  CG  MET A1410       8.170  25.300  -3.349  1.00 79.44           C  
ANISOU 3124  CG  MET A1410     9605   9144  11436   1055   -440     52       C  
ATOM   3125  SD  MET A1410       8.996  24.501  -1.956  1.00 93.95           S  
ANISOU 3125  SD  MET A1410    11369  11094  13235   1075   -400    119       S  
ATOM   3126  CE  MET A1410       8.704  22.757  -2.273  1.00 96.50           C  
ANISOU 3126  CE  MET A1410    11743  11323  13602   1139   -420    170       C  
ATOM   3127  N   SER A1411       4.889  23.382  -5.935  1.00 66.70           N  
ANISOU 3127  N   SER A1411     8175   7141  10027   1088   -613      1       N  
ATOM   3128  CA  SER A1411       4.354  22.430  -6.906  1.00 73.13           C  
ANISOU 3128  CA  SER A1411     9062   7840  10885   1116   -668    -12       C  
ATOM   3129  C   SER A1411       3.630  23.114  -8.064  1.00 75.30           C  
ANISOU 3129  C   SER A1411     9391   8055  11165   1107   -720    -74       C  
ATOM   3130  O   SER A1411       3.635  22.593  -9.186  1.00 85.14           O  
ANISOU 3130  O   SER A1411    10723   9256  12370   1123   -742    -94       O  
ATOM   3131  CB  SER A1411       3.423  21.438  -6.211  1.00 73.99           C  
ANISOU 3131  CB  SER A1411     9138   7902  11072   1089   -682     19       C  
ATOM   3132  OG  SER A1411       2.143  22.005  -6.012  1.00 80.93           O  
ANISOU 3132  OG  SER A1411     9976   8759  12014   1035   -713     -8       O  
ATOM   3133  N   PHE A1412       2.985  24.260  -7.819  1.00 63.56           N  
ANISOU 3133  N   PHE A1412     7863   6588   9700   1073   -727   -103       N  
ATOM   3134  CA  PHE A1412       2.370  25.010  -8.915  1.00 49.71           C  
ANISOU 3134  CA  PHE A1412     6164   4805   7917   1064   -761   -157       C  
ATOM   3135  C   PHE A1412       3.403  25.550  -9.903  1.00 54.93           C  
ANISOU 3135  C   PHE A1412     6899   5482   8490   1104   -736   -177       C  
ATOM   3136  O   PHE A1412       3.135  25.614 -11.109  1.00 51.17           O  
ANISOU 3136  O   PHE A1412     6501   4973   7968   1113   -760   -208       O  
ATOM   3137  CB  PHE A1412       1.518  26.148  -8.355  1.00 49.96           C  
ANISOU 3137  CB  PHE A1412     6136   4856   7992   1029   -764   -178       C  
ATOM   3138  CG  PHE A1412       0.798  26.961  -9.407  1.00 46.48           C  
ANISOU 3138  CG  PHE A1412     5748   4393   7521   1025   -796   -227       C  
ATOM   3139  CD1 PHE A1412       1.432  28.002 -10.074  1.00 44.85           C  
ANISOU 3139  CD1 PHE A1412     5593   4205   7242   1049   -768   -254       C  
ATOM   3140  CD2 PHE A1412      -0.530  26.694  -9.706  1.00 42.23           C  
ANISOU 3140  CD2 PHE A1412     5200   3815   7030    999   -854   -246       C  
ATOM   3141  CE1 PHE A1412       0.767  28.739 -11.028  1.00 33.37           C  
ANISOU 3141  CE1 PHE A1412     4192   2734   5755   1052   -792   -292       C  
ATOM   3142  CE2 PHE A1412      -1.202  27.435 -10.653  1.00 38.44           C  
ANISOU 3142  CE2 PHE A1412     4763   3323   6522   1005   -888   -289       C  
ATOM   3143  CZ  PHE A1412      -0.551  28.457 -11.316  1.00 34.40           C  
ANISOU 3143  CZ  PHE A1412     4311   2833   5927   1033   -854   -309       C  
ATOM   3144  N   SER A1413       4.582  25.942  -9.428  1.00 63.25           N  
ANISOU 3144  N   SER A1413     7925   6584   9522   1130   -687   -159       N  
ATOM   3145  CA  SER A1413       5.598  26.507 -10.323  1.00 61.32           C  
ANISOU 3145  CA  SER A1413     7743   6351   9205   1169   -657   -175       C  
ATOM   3146  C   SER A1413       6.256  25.468 -11.226  1.00 69.90           C  
ANISOU 3146  C   SER A1413     8907   7414  10238   1213   -652   -157       C  
ATOM   3147  O   SER A1413       6.645  25.774 -12.354  1.00 79.13           O  
ANISOU 3147  O   SER A1413    10154   8568  11343   1240   -638   -176       O  
ATOM   3148  CB  SER A1413       6.678  27.216  -9.508  1.00 55.80           C  
ANISOU 3148  CB  SER A1413     6982   5758   8460   1146   -583   -156       C  
ATOM   3149  OG  SER A1413       6.157  28.372  -8.888  1.00 62.02           O  
ANISOU 3149  OG  SER A1413     7725   6586   9256   1090   -566   -178       O  
ATOM   3150  N   GLU A 238       6.162  23.594 -10.027  1.00 74.13           N  
ANISOU 3150  N   GLU A 238     9450  11119   7595   -607   -328  -1310       N  
ATOM   3151  CA  GLU A 238       6.858  22.870 -11.076  1.00 75.18           C  
ANISOU 3151  CA  GLU A 238     9685  11152   7726   -503   -394  -1220       C  
ATOM   3152  C   GLU A 238       5.981  22.685 -12.319  1.00 84.52           C  
ANISOU 3152  C   GLU A 238    10857  12314   8942   -438   -415  -1229       C  
ATOM   3153  O   GLU A 238       6.502  22.440 -13.406  1.00103.37           O  
ANISOU 3153  O   GLU A 238    13296  14626  11353   -323   -454  -1173       O  
ATOM   3154  CB  GLU A 238       7.341  21.520 -10.537  1.00 92.72           C  
ANISOU 3154  CB  GLU A 238    12037  13344   9848   -589   -461  -1151       C  
ATOM   3155  CG  GLU A 238       8.572  21.643  -9.639  1.00115.64           C  
ANISOU 3155  CG  GLU A 238    14975  16230  12731   -602   -463  -1119       C  
ATOM   3156  CD  GLU A 238       8.593  20.643  -8.487  1.00134.49           C  
ANISOU 3156  CD  GLU A 238    17453  18637  15012   -762   -509  -1090       C  
ATOM   3157  OE1 GLU A 238       7.556  19.997  -8.223  1.00139.61           O  
ANISOU 3157  OE1 GLU A 238    18120  19329  15595   -886   -522  -1107       O  
ATOM   3158  OE2 GLU A 238       9.656  20.509  -7.841  1.00141.82           O  
ANISOU 3158  OE2 GLU A 238    18435  19535  15916   -767   -535  -1052       O  
ATOM   3159  N   GLN A 239       4.659  22.834 -12.160  1.00 76.80           N  
ANISOU 3159  N   GLN A 239     9807  11411   7965   -511   -388  -1308       N  
ATOM   3160  CA  GLN A 239       3.734  22.647 -13.279  1.00 70.45           C  
ANISOU 3160  CA  GLN A 239     8986  10592   7188   -457   -409  -1325       C  
ATOM   3161  C   GLN A 239       4.048  23.601 -14.423  1.00 74.39           C  
ANISOU 3161  C   GLN A 239     9444  11032   7787   -292   -406  -1318       C  
ATOM   3162  O   GLN A 239       4.245  23.181 -15.572  1.00 82.10           O  
ANISOU 3162  O   GLN A 239    10478  11943   8773   -201   -449  -1262       O  
ATOM   3163  CB  GLN A 239       2.291  22.880 -12.831  1.00 72.69           C  
ANISOU 3163  CB  GLN A 239     9172  10978   7468   -557   -373  -1436       C  
ATOM   3164  CG  GLN A 239       1.725  21.943 -11.794  1.00 83.87           C  
ANISOU 3164  CG  GLN A 239    10622  12470   8775   -744   -373  -1455       C  
ATOM   3165  CD  GLN A 239       0.309  22.342 -11.417  1.00 89.90           C  
ANISOU 3165  CD  GLN A 239    11264  13350   9544   -835   -326  -1588       C  
ATOM   3166  OE1 GLN A 239      -0.398  22.967 -12.210  1.00 91.00           O  
ANISOU 3166  OE1 GLN A 239    11319  13492   9764   -746   -319  -1651       O  
ATOM   3167  NE2 GLN A 239      -0.104  22.005 -10.201  1.00 89.80           N  
ANISOU 3167  NE2 GLN A 239    11238  13437   9446  -1015   -298  -1636       N  
ATOM   3168  N   VAL A 240       4.089  24.901 -14.117  1.00 75.43           N  
ANISOU 3168  N   VAL A 240     9478  11189   7993   -257   -358  -1377       N  
ATOM   3169  CA  VAL A 240       4.258  25.920 -15.148  1.00 75.41           C  
ANISOU 3169  CA  VAL A 240     9435  11131   8084   -117   -360  -1377       C  
ATOM   3170  C   VAL A 240       5.585  25.737 -15.872  1.00 80.31           C  
ANISOU 3170  C   VAL A 240    10144  11669   8701    -23   -386  -1276       C  
ATOM   3171  O   VAL A 240       5.681  25.968 -17.086  1.00 84.28           O  
ANISOU 3171  O   VAL A 240    10663  12115   9243     80   -412  -1243       O  
ATOM   3172  CB  VAL A 240       4.130  27.320 -14.510  1.00 68.44           C  
ANISOU 3172  CB  VAL A 240     8438  10287   7278   -111   -311  -1460       C  
ATOM   3173  CG1 VAL A 240       4.735  28.397 -15.406  1.00 63.97           C  
ANISOU 3173  CG1 VAL A 240     7860   9647   6797     24   -319  -1433       C  
ATOM   3174  CG2 VAL A 240       2.668  27.626 -14.193  1.00 65.13           C  
ANISOU 3174  CG2 VAL A 240     7913   9947   6886   -170   -296  -1582       C  
ATOM   3175  N   SER A 241       6.614  25.278 -15.157  1.00 80.20           N  
ANISOU 3175  N   SER A 241    10189  11649   8636    -60   -384  -1229       N  
ATOM   3176  CA  SER A 241       7.885  24.989 -15.808  1.00 79.69           C  
ANISOU 3176  CA  SER A 241    10202  11515   8561     24   -412  -1149       C  
ATOM   3177  C   SER A 241       7.753  23.837 -16.797  1.00 79.55           C  
ANISOU 3177  C   SER A 241    10266  11455   8504     56   -473  -1099       C  
ATOM   3178  O   SER A 241       8.263  23.916 -17.922  1.00 85.86           O  
ANISOU 3178  O   SER A 241    11091  12204   9326    156   -494  -1060       O  
ATOM   3179  CB  SER A 241       8.947  24.670 -14.760  1.00 81.72           C  
ANISOU 3179  CB  SER A 241    10503  11777   8771    -25   -407  -1122       C  
ATOM   3180  OG  SER A 241      10.139  24.226 -15.384  1.00 89.49           O  
ANISOU 3180  OG  SER A 241    11559  12701   9740     53   -443  -1059       O  
ATOM   3181  N   ALA A 242       7.050  22.769 -16.408  1.00 72.92           N  
ANISOU 3181  N   ALA A 242     9466  10638   7602    -35   -503  -1102       N  
ATOM   3182  CA  ALA A 242       6.891  21.633 -17.309  1.00 78.45           C  
ANISOU 3182  CA  ALA A 242    10244  11296   8266     -9   -565  -1058       C  
ATOM   3183  C   ALA A 242       6.132  22.037 -18.564  1.00 81.12           C  
ANISOU 3183  C   ALA A 242    10543  11623   8657     70   -566  -1073       C  
ATOM   3184  O   ALA A 242       6.530  21.686 -19.690  1.00 87.59           O  
ANISOU 3184  O   ALA A 242    11407  12392   9480    156   -603  -1029       O  
ATOM   3185  CB  ALA A 242       6.169  20.494 -16.589  1.00 77.46           C  
ANISOU 3185  CB  ALA A 242    10168  11199   8063   -137   -596  -1062       C  
ATOM   3186  N   ALA A 243       5.060  22.819 -18.389  1.00 71.26           N  
ANISOU 3186  N   ALA A 243     9204  10421   7450     45   -530  -1142       N  
ATOM   3187  CA  ALA A 243       4.301  23.287 -19.541  1.00 59.38           C  
ANISOU 3187  CA  ALA A 243     7659   8901   6000    122   -540  -1162       C  
ATOM   3188  C   ALA A 243       5.146  24.181 -20.440  1.00 76.60           C  
ANISOU 3188  C   ALA A 243     9838  11028   8237    239   -539  -1126       C  
ATOM   3189  O   ALA A 243       5.057  24.088 -21.672  1.00 89.39           O  
ANISOU 3189  O   ALA A 243    11484  12610   9872    315   -571  -1096       O  
ATOM   3190  CB  ALA A 243       3.049  24.025 -19.075  1.00 43.47           C  
ANISOU 3190  CB  ALA A 243     5540   6948   4029     76   -509  -1260       C  
ATOM   3191  N   ARG A 244       5.990  25.039 -19.851  1.00 74.52           N  
ANISOU 3191  N   ARG A 244     9549  10764   8001    249   -502  -1127       N  
ATOM   3192  CA  ARG A 244       6.849  25.872 -20.688  1.00 76.49           C  
ANISOU 3192  CA  ARG A 244     9804  10966   8292    345   -500  -1089       C  
ATOM   3193  C   ARG A 244       7.871  25.053 -21.458  1.00 78.50           C  
ANISOU 3193  C   ARG A 244    10144  11183   8499    393   -531  -1019       C  
ATOM   3194  O   ARG A 244       8.187  25.371 -22.612  1.00 79.18           O  
ANISOU 3194  O   ARG A 244    10248  11236   8603    467   -547   -987       O  
ATOM   3195  CB  ARG A 244       7.603  26.913 -19.865  1.00 78.58           C  
ANISOU 3195  CB  ARG A 244    10026  11240   8589    340   -454  -1105       C  
ATOM   3196  CG  ARG A 244       6.861  28.148 -19.447  1.00 85.36           C  
ANISOU 3196  CG  ARG A 244    10791  12119   9523    335   -428  -1176       C  
ATOM   3197  CD  ARG A 244       7.619  29.321 -20.068  1.00 92.84           C  
ANISOU 3197  CD  ARG A 244    11734  13018  10524    413   -423  -1150       C  
ATOM   3198  NE  ARG A 244       8.556  29.982 -19.162  1.00 97.08           N  
ANISOU 3198  NE  ARG A 244    12249  13566  11070    395   -379  -1155       N  
ATOM   3199  CZ  ARG A 244       9.474  30.859 -19.560  1.00108.40           C  
ANISOU 3199  CZ  ARG A 244    13693  14964  12532    446   -368  -1123       C  
ATOM   3200  NH1 ARG A 244       9.587  31.166 -20.847  1.00112.44           N  
ANISOU 3200  NH1 ARG A 244    14240  15426  13057    511   -401  -1080       N  
ATOM   3201  NH2 ARG A 244      10.292  31.415 -18.674  1.00114.44           N  
ANISOU 3201  NH2 ARG A 244    14434  15743  13304    425   -325  -1132       N  
ATOM   3202  N   LYS A 245       8.382  23.982 -20.855  1.00 89.65           N  
ANISOU 3202  N   LYS A 245    11612  12601   9850    347   -548   -998       N  
ATOM   3203  CA  LYS A 245       9.351  23.158 -21.565  1.00 94.24           C  
ANISOU 3203  CA  LYS A 245    12266  13148  10393    398   -586   -949       C  
ATOM   3204  C   LYS A 245       8.708  22.457 -22.758  1.00 91.44           C  
ANISOU 3204  C   LYS A 245    11942  12773  10026    435   -631   -932       C  
ATOM   3205  O   LYS A 245       9.221  22.527 -23.891  1.00 91.27           O  
ANISOU 3205  O   LYS A 245    11940  12729  10009    509   -646   -905       O  
ATOM   3206  CB  LYS A 245       9.993  22.166 -20.589  1.00100.36           C  
ANISOU 3206  CB  LYS A 245    13096  13923  11112    344   -611   -937       C  
ATOM   3207  CG  LYS A 245      10.902  22.854 -19.562  1.00107.11           C  
ANISOU 3207  CG  LYS A 245    13927  14793  11976    324   -569   -946       C  
ATOM   3208  CD  LYS A 245      11.489  21.888 -18.539  1.00121.10           C  
ANISOU 3208  CD  LYS A 245    15758  16561  13693    265   -604   -934       C  
ATOM   3209  CE  LYS A 245      10.488  21.550 -17.440  1.00131.34           C  
ANISOU 3209  CE  LYS A 245    17051  17894  14959    146   -601   -956       C  
ATOM   3210  NZ  LYS A 245      11.114  20.830 -16.291  1.00130.18           N  
ANISOU 3210  NZ  LYS A 245    16963  17743  14757     74   -633   -941       N  
ATOM   3211  N   VAL A 246       7.552  21.824 -22.539  1.00 81.53           N  
ANISOU 3211  N   VAL A 246    10689  11535   8755    378   -650   -952       N  
ATOM   3212  CA  VAL A 246       6.900  21.118 -23.640  1.00 71.14           C  
ANISOU 3212  CA  VAL A 246     9402  10202   7427    410   -693   -939       C  
ATOM   3213  C   VAL A 246       6.490  22.097 -24.736  1.00 74.42           C  
ANISOU 3213  C   VAL A 246     9774  10607   7896    481   -682   -943       C  
ATOM   3214  O   VAL A 246       6.714  21.854 -25.933  1.00 80.87           O  
ANISOU 3214  O   VAL A 246    10621  11399   8706    544   -710   -913       O  
ATOM   3215  CB  VAL A 246       5.696  20.311 -23.126  1.00 62.05           C  
ANISOU 3215  CB  VAL A 246     8256   9076   6245    324   -711   -966       C  
ATOM   3216  CG1 VAL A 246       4.866  19.817 -24.291  1.00 60.08           C  
ANISOU 3216  CG1 VAL A 246     8019   8813   5995    361   -746   -962       C  
ATOM   3217  CG2 VAL A 246       6.170  19.141 -22.278  1.00 68.53           C  
ANISOU 3217  CG2 VAL A 246     9149   9888   7000    255   -746   -944       C  
ATOM   3218  N   VAL A 247       5.909  23.234 -24.345  1.00 67.37           N  
ANISOU 3218  N   VAL A 247     8810   9732   7057    470   -647   -984       N  
ATOM   3219  CA  VAL A 247       5.431  24.178 -25.350  1.00 63.17           C  
ANISOU 3219  CA  VAL A 247     8245   9179   6579    534   -654   -989       C  
ATOM   3220  C   VAL A 247       6.593  24.787 -26.130  1.00 61.01           C  
ANISOU 3220  C   VAL A 247     7997   8873   6311    600   -651   -940       C  
ATOM   3221  O   VAL A 247       6.472  25.039 -27.337  1.00 67.73           O  
ANISOU 3221  O   VAL A 247     8863   9698   7172    653   -677   -915       O  
ATOM   3222  CB  VAL A 247       4.538  25.245 -24.689  1.00 63.44           C  
ANISOU 3222  CB  VAL A 247     8194   9235   6677    510   -631  -1057       C  
ATOM   3223  CG1 VAL A 247       4.302  26.422 -25.627  1.00 66.59           C  
ANISOU 3223  CG1 VAL A 247     8566   9594   7141    583   -649  -1056       C  
ATOM   3224  CG2 VAL A 247       3.204  24.622 -24.269  1.00 50.81           C  
ANISOU 3224  CG2 VAL A 247     6561   7677   5067    449   -639  -1115       C  
ATOM   3225  N   LYS A 248       7.749  24.990 -25.488  1.00 62.14           N  
ANISOU 3225  N   LYS A 248     8149   9020   6440    590   -620   -927       N  
ATOM   3226  CA  LYS A 248       8.912  25.430 -26.254  1.00 74.90           C  
ANISOU 3226  CA  LYS A 248     9793  10619   8049    641   -615   -886       C  
ATOM   3227  C   LYS A 248       9.315  24.380 -27.280  1.00 72.92           C  
ANISOU 3227  C   LYS A 248     9598  10362   7746    674   -651   -854       C  
ATOM   3228  O   LYS A 248       9.653  24.714 -28.427  1.00 75.07           O  
ANISOU 3228  O   LYS A 248     9887  10623   8012    717   -661   -828       O  
ATOM   3229  CB  LYS A 248      10.094  25.737 -25.334  1.00 84.45           C  
ANISOU 3229  CB  LYS A 248    10997  11840   9249    623   -576   -887       C  
ATOM   3230  CG  LYS A 248      11.350  26.152 -26.112  1.00 93.16           C  
ANISOU 3230  CG  LYS A 248    12125  12938  10335    665   -565   -855       C  
ATOM   3231  CD  LYS A 248      12.650  25.846 -25.370  1.00 95.39           C  
ANISOU 3231  CD  LYS A 248    12419  13239  10586    655   -543   -859       C  
ATOM   3232  CE  LYS A 248      13.848  25.972 -26.312  1.00 99.81           C  
ANISOU 3232  CE  LYS A 248    13001  13807  11114    694   -538   -841       C  
ATOM   3233  NZ  LYS A 248      15.118  26.279 -25.594  1.00103.36           N  
ANISOU 3233  NZ  LYS A 248    13441  14278  11554    687   -502   -855       N  
ATOM   3234  N   MET A 249       9.247  23.098 -26.898  1.00 68.01           N  
ANISOU 3234  N   MET A 249     9008   9748   7084    650   -676   -859       N  
ATOM   3235  CA  MET A 249       9.579  22.043 -27.853  1.00 56.66           C  
ANISOU 3235  CA  MET A 249     7620   8303   5603    686   -718   -840       C  
ATOM   3236  C   MET A 249       8.652  22.077 -29.061  1.00 73.26           C  
ANISOU 3236  C   MET A 249     9723  10397   7716    716   -743   -829       C  
ATOM   3237  O   MET A 249       9.105  22.015 -30.216  1.00 88.33           O  
ANISOU 3237  O   MET A 249    11653  12304   9605    760   -758   -809       O  
ATOM   3238  CB  MET A 249       9.491  20.675 -27.183  1.00 48.59           C  
ANISOU 3238  CB  MET A 249     6639   7278   4544    649   -756   -847       C  
ATOM   3239  CG  MET A 249       9.805  19.529 -28.125  1.00 53.78           C  
ANISOU 3239  CG  MET A 249     7345   7924   5165    690   -809   -837       C  
ATOM   3240  SD  MET A 249       9.675  17.916 -27.338  1.00 77.27           S  
ANISOU 3240  SD  MET A 249    10381  10878   8098    645   -873   -842       S  
ATOM   3241  CE  MET A 249       7.898  17.674 -27.313  1.00 69.99           C  
ANISOU 3241  CE  MET A 249     9451   9962   7181    589   -879   -847       C  
ATOM   3242  N   MET A 250       7.346  22.202 -28.817  1.00 71.05           N  
ANISOU 3242  N   MET A 250     9416  10116   7464    689   -748   -850       N  
ATOM   3243  CA  MET A 250       6.415  22.243 -29.937  1.00 76.71           C  
ANISOU 3243  CA  MET A 250    10131  10823   8194    721   -777   -845       C  
ATOM   3244  C   MET A 250       6.621  23.476 -30.805  1.00 86.33           C  
ANISOU 3244  C   MET A 250    11336  12023   9441    763   -772   -824       C  
ATOM   3245  O   MET A 250       6.446  23.409 -32.030  1.00 95.35           O  
ANISOU 3245  O   MET A 250    12502  13156  10572    799   -801   -800       O  
ATOM   3246  CB  MET A 250       4.984  22.177 -29.419  1.00 70.74           C  
ANISOU 3246  CB  MET A 250     9338  10077   7465    682   -783   -887       C  
ATOM   3247  CG  MET A 250       4.702  20.918 -28.629  1.00 76.92           C  
ANISOU 3247  CG  MET A 250    10145  10876   8205    622   -795   -902       C  
ATOM   3248  SD  MET A 250       5.421  19.458 -29.410  1.00 89.74           S  
ANISOU 3248  SD  MET A 250    11846  12483   9767    652   -842   -864       S  
ATOM   3249  CE  MET A 250       4.520  19.413 -30.957  1.00 92.75           C  
ANISOU 3249  CE  MET A 250    12226  12857  10158    705   -874   -856       C  
ATOM   3250  N   ILE A 251       7.021  24.597 -30.202  1.00 77.68           N  
ANISOU 3250  N   ILE A 251    10211  10922   8381    755   -739   -830       N  
ATOM   3251  CA  ILE A 251       7.334  25.775 -31.001  1.00 66.34           C  
ANISOU 3251  CA  ILE A 251     8778   9463   6967    785   -741   -802       C  
ATOM   3252  C   ILE A 251       8.524  25.501 -31.909  1.00 66.49           C  
ANISOU 3252  C   ILE A 251     8842   9493   6929    804   -739   -762       C  
ATOM   3253  O   ILE A 251       8.555  25.942 -33.065  1.00 75.09           O  
ANISOU 3253  O   ILE A 251     9954  10570   8006    824   -760   -731       O  
ATOM   3254  CB  ILE A 251       7.578  26.986 -30.084  1.00 62.40           C  
ANISOU 3254  CB  ILE A 251     8238   8953   6517    768   -708   -820       C  
ATOM   3255  CG1 ILE A 251       6.263  27.414 -29.432  1.00 73.53           C  
ANISOU 3255  CG1 ILE A 251     9591  10356   7991    755   -719   -874       C  
ATOM   3256  CG2 ILE A 251       8.206  28.132 -30.864  1.00 48.90           C  
ANISOU 3256  CG2 ILE A 251     6549   7216   4816    788   -712   -781       C  
ATOM   3257  CD1 ILE A 251       6.434  28.285 -28.214  1.00 81.08           C  
ANISOU 3257  CD1 ILE A 251    10495  11317   8992    728   -681   -911       C  
ATOM   3258  N   VAL A 252       9.506  24.738 -31.420  1.00 64.68           N  
ANISOU 3258  N   VAL A 252     8626   9292   6659    794   -718   -769       N  
ATOM   3259  CA  VAL A 252      10.611  24.351 -32.296  1.00 68.80           C  
ANISOU 3259  CA  VAL A 252     9179   9837   7125    813   -719   -752       C  
ATOM   3260  C   VAL A 252      10.127  23.441 -33.421  1.00 81.10           C  
ANISOU 3260  C   VAL A 252    10763  11400   8651    838   -762   -744       C  
ATOM   3261  O   VAL A 252      10.607  23.542 -34.561  1.00 75.29           O  
ANISOU 3261  O   VAL A 252    10047  10682   7879    852   -768   -726       O  
ATOM   3262  CB  VAL A 252      11.738  23.689 -31.483  1.00 64.48           C  
ANISOU 3262  CB  VAL A 252     8634   9315   6551    807   -700   -775       C  
ATOM   3263  CG1 VAL A 252      12.843  23.195 -32.404  1.00 54.69           C  
ANISOU 3263  CG1 VAL A 252     7414   8110   5256    831   -706   -780       C  
ATOM   3264  CG2 VAL A 252      12.292  24.668 -30.467  1.00 69.30           C  
ANISOU 3264  CG2 VAL A 252     9216   9925   7188    783   -654   -782       C  
ATOM   3265  N   VAL A 253       9.143  22.579 -33.145  1.00 84.85           N  
ANISOU 3265  N   VAL A 253    11239  11864   9137    836   -790   -759       N  
ATOM   3266  CA  VAL A 253       8.613  21.713 -34.199  1.00 88.07           C  
ANISOU 3266  CA  VAL A 253    11671  12275   9518    860   -831   -753       C  
ATOM   3267  C   VAL A 253       7.969  22.554 -35.297  1.00 89.16           C  
ANISOU 3267  C   VAL A 253    11809  12398   9668    875   -847   -726       C  
ATOM   3268  O   VAL A 253       8.277  22.404 -36.490  1.00 73.98           O  
ANISOU 3268  O   VAL A 253     9910  10491   7707    893   -863   -707       O  
ATOM   3269  CB  VAL A 253       7.615  20.699 -33.608  1.00 82.27           C  
ANISOU 3269  CB  VAL A 253    10938  11529   8791    843   -858   -775       C  
ATOM   3270  CG1 VAL A 253       6.788  20.060 -34.715  1.00 91.35           C  
ANISOU 3270  CG1 VAL A 253    12104  12677   9927    867   -898   -769       C  
ATOM   3271  CG2 VAL A 253       8.343  19.646 -32.788  1.00 67.99           C  
ANISOU 3271  CG2 VAL A 253     9151   9727   6955    829   -865   -793       C  
ATOM   3272  N   VAL A 254       7.077  23.467 -34.905  1.00 98.30           N  
ANISOU 3272  N   VAL A 254    12941  13526  10882    867   -847   -729       N  
ATOM   3273  CA  VAL A 254       6.353  24.258 -35.894  1.00 92.97           C  
ANISOU 3273  CA  VAL A 254    12272  12824  10228    885   -881   -706       C  
ATOM   3274  C   VAL A 254       7.321  25.155 -36.656  1.00 81.75           C  
ANISOU 3274  C   VAL A 254    10878  11403   8779    882   -873   -665       C  
ATOM   3275  O   VAL A 254       7.182  25.358 -37.869  1.00 83.96           O  
ANISOU 3275  O   VAL A 254    11190  11678   9033    890   -904   -633       O  
ATOM   3276  CB  VAL A 254       5.228  25.059 -35.213  1.00 93.87           C  
ANISOU 3276  CB  VAL A 254    12345  12906  10417    883   -892   -735       C  
ATOM   3277  CG1 VAL A 254       4.415  25.818 -36.238  1.00 88.75           C  
ANISOU 3277  CG1 VAL A 254    11707  12219   9796    910   -945   -718       C  
ATOM   3278  CG2 VAL A 254       4.330  24.125 -34.417  1.00101.89           C  
ANISOU 3278  CG2 VAL A 254    13332  13938  11444    867   -891   -783       C  
ATOM   3279  N   CYS A 255       8.327  25.693 -35.960  1.00 72.17           N  
ANISOU 3279  N   CYS A 255     9657  10200   7565    861   -830   -666       N  
ATOM   3280  CA  CYS A 255       9.313  26.536 -36.627  1.00 75.33           C  
ANISOU 3280  CA  CYS A 255    10084  10608   7930    843   -817   -630       C  
ATOM   3281  C   CYS A 255      10.089  25.749 -37.674  1.00 74.18           C  
ANISOU 3281  C   CYS A 255     9965  10515   7704    842   -815   -622       C  
ATOM   3282  O   CYS A 255      10.301  26.230 -38.796  1.00 76.48           O  
ANISOU 3282  O   CYS A 255    10290  10814   7955    826   -831   -587       O  
ATOM   3283  CB  CYS A 255      10.274  27.132 -35.601  1.00 85.45           C  
ANISOU 3283  CB  CYS A 255    11347  11899   9223    820   -767   -642       C  
ATOM   3284  SG  CYS A 255       9.859  28.792 -35.051  1.00103.11           S  
ANISOU 3284  SG  CYS A 255    13569  14074  11533    808   -772   -630       S  
ATOM   3285  N   THR A 256      10.484  24.516 -37.339  1.00 71.42           N  
ANISOU 3285  N   THR A 256     9604  10202   7331    857   -804   -659       N  
ATOM   3286  CA  THR A 256      11.159  23.681 -38.325  1.00 73.79           C  
ANISOU 3286  CA  THR A 256     9918  10555   7562    863   -810   -669       C  
ATOM   3287  C   THR A 256      10.255  23.429 -39.521  1.00 77.43           C  
ANISOU 3287  C   THR A 256    10402  11009   8008    876   -854   -646       C  
ATOM   3288  O   THR A 256      10.717  23.392 -40.671  1.00 68.91           O  
ANISOU 3288  O   THR A 256     9342   9971   6870    863   -859   -635       O  
ATOM   3289  CB  THR A 256      11.574  22.351 -37.694  1.00 62.02           C  
ANISOU 3289  CB  THR A 256     8414   9087   6065    886   -810   -718       C  
ATOM   3290  OG1 THR A 256      12.403  22.597 -36.552  1.00 54.00           O  
ANISOU 3290  OG1 THR A 256     7380   8075   5063    875   -775   -739       O  
ATOM   3291  CG2 THR A 256      12.332  21.507 -38.693  1.00 53.94           C  
ANISOU 3291  CG2 THR A 256     7395   8121   4978    900   -821   -746       C  
ATOM   3292  N   PHE A 257       8.952  23.297 -39.270  1.00 80.46           N  
ANISOU 3292  N   PHE A 257    10782  11346   8443    895   -886   -643       N  
ATOM   3293  CA  PHE A 257       8.026  23.043 -40.365  1.00 80.87           C  
ANISOU 3293  CA  PHE A 257    10853  11389   8484    910   -931   -624       C  
ATOM   3294  C   PHE A 257       7.963  24.245 -41.300  1.00 80.97           C  
ANISOU 3294  C   PHE A 257    10896  11384   8485    889   -951   -575       C  
ATOM   3295  O   PHE A 257       8.052  24.101 -42.527  1.00 90.61           O  
ANISOU 3295  O   PHE A 257    12145  12631   9651    881   -972   -553       O  
ATOM   3296  CB  PHE A 257       6.654  22.715 -39.776  1.00 87.36           C  
ANISOU 3296  CB  PHE A 257    11656  12171   9366    930   -958   -642       C  
ATOM   3297  CG  PHE A 257       5.603  22.397 -40.790  1.00 87.79           C  
ANISOU 3297  CG  PHE A 257    11724  12214   9417    951  -1006   -632       C  
ATOM   3298  CD1 PHE A 257       4.823  23.397 -41.344  1.00 77.43           C  
ANISOU 3298  CD1 PHE A 257    10423  10862   8135    956  -1043   -604       C  
ATOM   3299  CD2 PHE A 257       5.374  21.083 -41.165  1.00 92.93           C  
ANISOU 3299  CD2 PHE A 257    12378  12891  10039    968  -1021   -653       C  
ATOM   3300  CE1 PHE A 257       3.846  23.093 -42.259  1.00 81.38           C  
ANISOU 3300  CE1 PHE A 257    10935  11351   8634    978  -1092   -598       C  
ATOM   3301  CE2 PHE A 257       4.399  20.774 -42.082  1.00 93.48           C  
ANISOU 3301  CE2 PHE A 257    12458  12954  10106    988  -1063   -646       C  
ATOM   3302  CZ  PHE A 257       3.633  21.779 -42.630  1.00 88.92           C  
ANISOU 3302  CZ  PHE A 257    11889  12340   9557    993  -1097   -619       C  
ATOM   3303  N   ALA A 258       7.844  25.447 -40.729  1.00 80.18           N  
ANISOU 3303  N   ALA A 258    10794  11238   8431    876   -949   -557       N  
ATOM   3304  CA  ALA A 258       7.729  26.656 -41.540  1.00 75.81           C  
ANISOU 3304  CA  ALA A 258    10282  10649   7872    852   -984   -505       C  
ATOM   3305  C   ALA A 258       8.998  26.916 -42.344  1.00 79.74           C  
ANISOU 3305  C   ALA A 258    10814  11201   8284    802   -958   -477       C  
ATOM   3306  O   ALA A 258       8.929  27.255 -43.536  1.00 81.14           O  
ANISOU 3306  O   ALA A 258    11037  11381   8412    774   -993   -435       O  
ATOM   3307  CB  ALA A 258       7.412  27.855 -40.649  1.00 71.43           C  
ANISOU 3307  CB  ALA A 258     9715  10031   7394    851   -992   -502       C  
ATOM   3308  N   ILE A 259      10.164  26.729 -41.712  1.00 81.20           N  
ANISOU 3308  N   ILE A 259    10975  11434   8443    784   -898   -506       N  
ATOM   3309  CA  ILE A 259      11.440  26.917 -42.402  1.00 84.87           C  
ANISOU 3309  CA  ILE A 259    11460  11967   8822    730   -864   -498       C  
ATOM   3310  C   ILE A 259      11.579  25.918 -43.538  1.00 94.38           C  
ANISOU 3310  C   ILE A 259    12669  13238   9954    730   -874   -514       C  
ATOM   3311  O   ILE A 259      11.965  26.271 -44.659  1.00 99.24           O  
ANISOU 3311  O   ILE A 259    13319  13893  10495    677   -880   -486       O  
ATOM   3312  CB  ILE A 259      12.613  26.778 -41.414  1.00 88.24           C  
ANISOU 3312  CB  ILE A 259    11848  12436   9243    724   -801   -543       C  
ATOM   3313  CG1 ILE A 259      12.533  27.814 -40.289  1.00 94.05           C  
ANISOU 3313  CG1 ILE A 259    12576  13113  10048    719   -787   -530       C  
ATOM   3314  CG2 ILE A 259      13.943  26.861 -42.150  1.00 85.46           C  
ANISOU 3314  CG2 ILE A 259    11502  12171   8797    667   -763   -555       C  
ATOM   3315  CD1 ILE A 259      13.486  27.509 -39.128  1.00 93.46           C  
ANISOU 3315  CD1 ILE A 259    12458  13071   9982    725   -730   -579       C  
ATOM   3316  N   CYS A 260      11.276  24.648 -43.263  1.00 96.60           N  
ANISOU 3316  N   CYS A 260    12916  13534  10252    782   -877   -561       N  
ATOM   3317  CA  CYS A 260      11.457  23.625 -44.285  1.00 95.74           C  
ANISOU 3317  CA  CYS A 260    12804  13490  10081    788   -887   -588       C  
ATOM   3318  C   CYS A 260      10.513  23.809 -45.465  1.00 85.37           C  
ANISOU 3318  C   CYS A 260    11530  12158   8748    780   -938   -541       C  
ATOM   3319  O   CYS A 260      10.879  23.487 -46.601  1.00 81.02           O  
ANISOU 3319  O   CYS A 260    10991  11672   8121    751   -941   -545       O  
ATOM   3320  CB  CYS A 260      11.269  22.236 -43.682  1.00100.29           C  
ANISOU 3320  CB  CYS A 260    13346  14072  10689    847   -892   -645       C  
ATOM   3321  SG  CYS A 260      12.648  21.687 -42.667  1.00106.22           S  
ANISOU 3321  SG  CYS A 260    14056  14868  11436    857   -847   -715       S  
ATOM   3322  N   TRP A 261       9.305  24.321 -45.235  1.00 87.99           N  
ANISOU 3322  N   TRP A 261    11880  12406   9146    803   -981   -503       N  
ATOM   3323  CA  TRP A 261       8.339  24.379 -46.322  1.00101.96           C  
ANISOU 3323  CA  TRP A 261    13685  14153  10904    805  -1038   -466       C  
ATOM   3324  C   TRP A 261       8.246  25.723 -47.031  1.00109.72           C  
ANISOU 3324  C   TRP A 261    14727  15098  11864    753  -1076   -396       C  
ATOM   3325  O   TRP A 261       7.631  25.785 -48.101  1.00107.97           O  
ANISOU 3325  O   TRP A 261    14543  14867  11613    743  -1128   -362       O  
ATOM   3326  CB  TRP A 261       6.958  23.968 -45.810  1.00110.79           C  
ANISOU 3326  CB  TRP A 261    14783  15208  12104    866  -1076   -480       C  
ATOM   3327  CG  TRP A 261       6.902  22.502 -45.591  1.00112.40           C  
ANISOU 3327  CG  TRP A 261    14952  15451  12305    904  -1061   -534       C  
ATOM   3328  CD1 TRP A 261       6.774  21.849 -44.400  1.00115.27           C  
ANISOU 3328  CD1 TRP A 261    15279  15801  12717    934  -1041   -576       C  
ATOM   3329  CD2 TRP A 261       7.026  21.490 -46.595  1.00113.48           C  
ANISOU 3329  CD2 TRP A 261    15090  15646  12383    910  -1071   -552       C  
ATOM   3330  NE1 TRP A 261       6.788  20.490 -44.604  1.00117.81           N  
ANISOU 3330  NE1 TRP A 261    15588  16159  13016    959  -1046   -615       N  
ATOM   3331  CE2 TRP A 261       6.942  20.245 -45.945  1.00117.95           C  
ANISOU 3331  CE2 TRP A 261    15623  16221  12971    950  -1063   -605       C  
ATOM   3332  CE3 TRP A 261       7.189  21.517 -47.984  1.00105.93           C  
ANISOU 3332  CE3 TRP A 261    14161  14735  11354    881  -1089   -530       C  
ATOM   3333  CZ2 TRP A 261       7.018  19.037 -46.637  1.00113.20           C  
ANISOU 3333  CZ2 TRP A 261    15012  15667  12331    970  -1076   -640       C  
ATOM   3334  CZ3 TRP A 261       7.258  20.317 -48.668  1.00 99.87           C  
ANISOU 3334  CZ3 TRP A 261    13377  14025  10545    900  -1094   -569       C  
ATOM   3335  CH2 TRP A 261       7.176  19.095 -47.995  1.00102.13           C  
ANISOU 3335  CH2 TRP A 261    13627  14313  10863    948  -1089   -625       C  
ATOM   3336  N   LEU A 262       8.805  26.799 -46.477  1.00112.81           N  
ANISOU 3336  N   LEU A 262    15133  15463  12269    717  -1059   -373       N  
ATOM   3337  CA  LEU A 262       8.723  28.077 -47.186  1.00104.84           C  
ANISOU 3337  CA  LEU A 262    14192  14406  11234    660  -1108   -302       C  
ATOM   3338  C   LEU A 262       9.362  28.060 -48.576  1.00 99.98           C  
ANISOU 3338  C   LEU A 262    13624  13864  10499    582  -1111   -270       C  
ATOM   3339  O   LEU A 262       8.667  28.409 -49.552  1.00100.41           O  
ANISOU 3339  O   LEU A 262    13736  13883  10532    563  -1180   -218       O  
ATOM   3340  CB  LEU A 262       9.337  29.181 -46.320  1.00 99.73           C  
ANISOU 3340  CB  LEU A 262    13552  13723  10618    630  -1085   -288       C  
ATOM   3341  CG  LEU A 262       9.407  30.567 -46.963  1.00 97.01           C  
ANISOU 3341  CG  LEU A 262    13291  13324  10246    560  -1141   -211       C  
ATOM   3342  CD1 LEU A 262       8.026  31.202 -47.031  1.00 97.39           C  
ANISOU 3342  CD1 LEU A 262    13369  13255  10380    607  -1241   -180       C  
ATOM   3343  CD2 LEU A 262      10.391  31.459 -46.218  1.00 98.56           C  
ANISOU 3343  CD2 LEU A 262    13489  13516  10441    513  -1097   -205       C  
ATOM   3344  N   PRO A 263      10.631  27.655 -48.754  1.00 93.17           N  
ANISOU 3344  N   PRO A 263    12740  13107   9553    532  -1042   -305       N  
ATOM   3345  CA  PRO A 263      11.224  27.699 -50.105  1.00 93.59           C  
ANISOU 3345  CA  PRO A 263    12833  13243   9483    443  -1041   -283       C  
ATOM   3346  C   PRO A 263      10.474  26.862 -51.123  1.00 97.64           C  
ANISOU 3346  C   PRO A 263    13351  13779   9968    466  -1082   -285       C  
ATOM   3347  O   PRO A 263      10.419  27.223 -52.307  1.00 97.83           O  
ANISOU 3347  O   PRO A 263    13435  13826   9911    394  -1118   -236       O  
ATOM   3348  CB  PRO A 263      12.649  27.176 -49.886  1.00 89.15           C  
ANISOU 3348  CB  PRO A 263    12216  12800   8858    410   -954   -356       C  
ATOM   3349  CG  PRO A 263      12.888  27.266 -48.422  1.00 86.63           C  
ANISOU 3349  CG  PRO A 263    11852  12439   8625    464   -917   -388       C  
ATOM   3350  CD  PRO A 263      11.560  27.042 -47.789  1.00 86.98           C  
ANISOU 3350  CD  PRO A 263    11887  12380   8780    556   -965   -377       C  
ATOM   3351  N   PHE A 264       9.897  25.743 -50.688  1.00 98.65           N  
ANISOU 3351  N   PHE A 264    13423  13904  10158    558  -1077   -339       N  
ATOM   3352  CA  PHE A 264       9.173  24.859 -51.593  1.00 97.08           C  
ANISOU 3352  CA  PHE A 264    13221  13728   9938    587  -1113   -348       C  
ATOM   3353  C   PHE A 264       7.916  25.533 -52.130  1.00 98.88           C  
ANISOU 3353  C   PHE A 264    13511  13862  10198    594  -1200   -276       C  
ATOM   3354  O   PHE A 264       7.726  25.659 -53.348  1.00107.03           O  
ANISOU 3354  O   PHE A 264    14592  14917  11158    545  -1240   -236       O  
ATOM   3355  CB  PHE A 264       8.831  23.567 -50.849  1.00 95.28           C  
ANISOU 3355  CB  PHE A 264    12925  13503   9776    680  -1093   -420       C  
ATOM   3356  CG  PHE A 264       7.948  22.632 -51.610  1.00 92.38           C  
ANISOU 3356  CG  PHE A 264    12552  13144   9405    721  -1132   -432       C  
ATOM   3357  CD1 PHE A 264       8.497  21.636 -52.395  1.00 88.07           C  
ANISOU 3357  CD1 PHE A 264    11977  12698   8788    710  -1110   -482       C  
ATOM   3358  CD2 PHE A 264       6.568  22.727 -51.519  1.00 87.55           C  
ANISOU 3358  CD2 PHE A 264    11956  12445   8865    772  -1190   -403       C  
ATOM   3359  CE1 PHE A 264       7.687  20.757 -53.084  1.00 78.81           C  
ANISOU 3359  CE1 PHE A 264    10798  11534   7614    749  -1146   -496       C  
ATOM   3360  CE2 PHE A 264       5.752  21.856 -52.210  1.00 79.12           C  
ANISOU 3360  CE2 PHE A 264    10881  11388   7794    809  -1224   -417       C  
ATOM   3361  CZ  PHE A 264       6.312  20.867 -52.993  1.00 77.10           C  
ANISOU 3361  CZ  PHE A 264    10602  11227   7465    797  -1201   -459       C  
ATOM   3362  N   HIS A 265       7.062  26.011 -51.222  1.00101.59           N  
ANISOU 3362  N   HIS A 265    13852  14100  10648    654  -1234   -264       N  
ATOM   3363  CA  HIS A 265       5.812  26.631 -51.643  1.00103.61           C  
ANISOU 3363  CA  HIS A 265    14156  14261  10951    676  -1326   -214       C  
ATOM   3364  C   HIS A 265       6.075  27.877 -52.473  1.00112.68           C  
ANISOU 3364  C   HIS A 265    15396  15379  12039    589  -1381   -132       C  
ATOM   3365  O   HIS A 265       5.376  28.133 -53.463  1.00115.80           O  
ANISOU 3365  O   HIS A 265    15849  15740  12410    574  -1459    -84       O  
ATOM   3366  CB  HIS A 265       4.962  26.975 -50.421  1.00 99.67           C  
ANISOU 3366  CB  HIS A 265    13624  13668  10579    751  -1347   -236       C  
ATOM   3367  CG  HIS A 265       4.288  25.793 -49.796  1.00105.00           C  
ANISOU 3367  CG  HIS A 265    14228  14355  11313    829  -1324   -304       C  
ATOM   3368  ND1 HIS A 265       3.245  25.127 -50.403  1.00113.30           N  
ANISOU 3368  ND1 HIS A 265    15274  15400  12375    871  -1369   -314       N  
ATOM   3369  CD2 HIS A 265       4.493  25.171 -48.611  1.00108.42           C  
ANISOU 3369  CD2 HIS A 265    14598  14805  11792    865  -1265   -361       C  
ATOM   3370  CE1 HIS A 265       2.842  24.140 -49.623  1.00119.45           C  
ANISOU 3370  CE1 HIS A 265    15992  16192  13202    925  -1336   -376       C  
ATOM   3371  NE2 HIS A 265       3.582  24.145 -48.529  1.00117.90           N  
ANISOU 3371  NE2 HIS A 265    15763  16008  13027    920  -1276   -403       N  
ATOM   3372  N   ILE A 266       7.107  28.646 -52.111  1.00116.76           N  
ANISOU 3372  N   ILE A 266    15932  15909  12524    523  -1343   -113       N  
ATOM   3373  CA  ILE A 266       7.463  29.799 -52.931  1.00117.55           C  
ANISOU 3373  CA  ILE A 266    16129  15985  12550    420  -1394    -31       C  
ATOM   3374  C   ILE A 266       7.940  29.357 -54.310  1.00116.24           C  
ANISOU 3374  C   ILE A 266    15997  15923  12247    333  -1385    -13       C  
ATOM   3375  O   ILE A 266       7.641  30.011 -55.319  1.00118.63           O  
ANISOU 3375  O   ILE A 266    16389  16193  12490    265  -1463     61       O  
ATOM   3376  CB  ILE A 266       8.511  30.655 -52.195  1.00117.89           C  
ANISOU 3376  CB  ILE A 266    16181  16029  12585    363  -1346    -22       C  
ATOM   3377  CG1 ILE A 266       7.815  31.553 -51.163  1.00117.69           C  
ANISOU 3377  CG1 ILE A 266    16159  15870  12689    425  -1398    -11       C  
ATOM   3378  CG2 ILE A 266       9.347  31.467 -53.171  1.00118.32           C  
ANISOU 3378  CG2 ILE A 266    16323  16120  12511    221  -1359     45       C  
ATOM   3379  CD1 ILE A 266       8.721  32.570 -50.513  1.00118.67           C  
ANISOU 3379  CD1 ILE A 266    16304  15975  12810    367  -1369     10       C  
ATOM   3380  N   PHE A 267       8.630  28.216 -54.390  1.00116.16           N  
ANISOU 3380  N   PHE A 267    15914  16037  12184    336  -1300    -85       N  
ATOM   3381  CA  PHE A 267       9.124  27.736 -55.679  1.00113.01           C  
ANISOU 3381  CA  PHE A 267    15531  15753  11654    253  -1284    -87       C  
ATOM   3382  C   PHE A 267       7.976  27.347 -56.604  1.00110.09           C  
ANISOU 3382  C   PHE A 267    15191  15354  11285    285  -1361    -59       C  
ATOM   3383  O   PHE A 267       7.956  27.735 -57.777  1.00115.63           O  
ANISOU 3383  O   PHE A 267    15966  16077  11890    194  -1407     -1       O  
ATOM   3384  CB  PHE A 267      10.074  26.554 -55.467  1.00108.52           C  
ANISOU 3384  CB  PHE A 267    14866  15318  11049    268  -1185   -190       C  
ATOM   3385  CG  PHE A 267      10.566  25.919 -56.745  1.00109.75           C  
ANISOU 3385  CG  PHE A 267    15014  15607  11077    193  -1164   -219       C  
ATOM   3386  CD1 PHE A 267       9.852  24.889 -57.347  1.00107.44           C  
ANISOU 3386  CD1 PHE A 267    14694  15338  10790    251  -1187   -248       C  
ATOM   3387  CD2 PHE A 267      11.751  26.340 -57.336  1.00111.28           C  
ANISOU 3387  CD2 PHE A 267    15226  15912  11144     61  -1118   -223       C  
ATOM   3388  CE1 PHE A 267      10.303  24.302 -58.517  1.00108.60           C  
ANISOU 3388  CE1 PHE A 267    14828  15614  10822    183  -1167   -282       C  
ATOM   3389  CE2 PHE A 267      12.209  25.756 -58.506  1.00110.48           C  
ANISOU 3389  CE2 PHE A 267    15109  15948  10921    -15  -1095   -262       C  
ATOM   3390  CZ  PHE A 267      11.484  24.736 -59.097  1.00111.27           C  
ANISOU 3390  CZ  PHE A 267    15178  16068  11032     49  -1120   -292       C  
ATOM   3391  N   PHE A 268       7.016  26.566 -56.106  1.00106.75           N  
ANISOU 3391  N   PHE A 268    14714  14884  10963    406  -1375   -101       N  
ATOM   3392  CA  PHE A 268       5.934  26.147 -56.992  1.00104.42           C  
ANISOU 3392  CA  PHE A 268    14440  14567  10668    438  -1443    -82       C  
ATOM   3393  C   PHE A 268       4.926  27.256 -57.266  1.00109.55           C  
ANISOU 3393  C   PHE A 268    15177  15086  11362    439  -1559      1       C  
ATOM   3394  O   PHE A 268       4.301  27.258 -58.332  1.00119.04           O  
ANISOU 3394  O   PHE A 268    16430  16278  12520    418  -1629     42       O  
ATOM   3395  CB  PHE A 268       5.232  24.915 -56.428  1.00104.65           C  
ANISOU 3395  CB  PHE A 268    14386  14596  10782    556  -1422   -156       C  
ATOM   3396  CG  PHE A 268       5.924  23.630 -56.763  1.00103.18           C  
ANISOU 3396  CG  PHE A 268    14134  14537  10533    554  -1351   -230       C  
ATOM   3397  CD1 PHE A 268       7.105  23.282 -56.132  1.00101.48           C  
ANISOU 3397  CD1 PHE A 268    13865  14395  10299    541  -1268   -290       C  
ATOM   3398  CD2 PHE A 268       5.404  22.774 -57.715  1.00105.40           C  
ANISOU 3398  CD2 PHE A 268    14406  14863  10777    569  -1373   -247       C  
ATOM   3399  CE1 PHE A 268       7.751  22.103 -56.438  1.00 98.56           C  
ANISOU 3399  CE1 PHE A 268    13431  14136   9879    547  -1215   -370       C  
ATOM   3400  CE2 PHE A 268       6.045  21.592 -58.025  1.00106.40           C  
ANISOU 3400  CE2 PHE A 268    14469  15104  10853    573  -1316   -324       C  
ATOM   3401  CZ  PHE A 268       7.220  21.254 -57.382  1.00100.88           C  
ANISOU 3401  CZ  PHE A 268    13715  14473  10141    564  -1240   -389       C  
ATOM   3402  N   LEU A 269       4.743  28.201 -56.346  1.00105.46           N  
ANISOU 3402  N   LEU A 269    14676  14465  10930    465  -1588     22       N  
ATOM   3403  CA  LEU A 269       3.850  29.312 -56.653  1.00116.10           C  
ANISOU 3403  CA  LEU A 269    16109  15682  12321    466  -1713     94       C  
ATOM   3404  C   LEU A 269       4.552  30.435 -57.407  1.00125.86           C  
ANISOU 3404  C   LEU A 269    17457  16908  13455    332  -1757    184       C  
ATOM   3405  O   LEU A 269       3.900  31.421 -57.768  1.00120.01           O  
ANISOU 3405  O   LEU A 269    16805  16052  12739    320  -1878    253       O  
ATOM   3406  CB  LEU A 269       3.193  29.846 -55.376  1.00115.69           C  
ANISOU 3406  CB  LEU A 269    16023  15518  12417    559  -1741     67       C  
ATOM   3407  CG  LEU A 269       2.227  28.875 -54.682  1.00107.81           C  
ANISOU 3407  CG  LEU A 269    14929  14513  11521    682  -1721    -15       C  
ATOM   3408  CD1 LEU A 269       1.325  29.602 -53.692  1.00102.66           C  
ANISOU 3408  CD1 LEU A 269    14256  13742  11008    761  -1781    -38       C  
ATOM   3409  CD2 LEU A 269       1.398  28.085 -55.693  1.00103.79           C  
ANISOU 3409  CD2 LEU A 269    14423  14028  10984    708  -1764    -18       C  
ATOM   3410  N   LEU A 270       5.861  30.311 -57.636  1.00136.73           N  
ANISOU 3410  N   LEU A 270    18832  18402  14719    229  -1669    181       N  
ATOM   3411  CA  LEU A 270       6.585  31.290 -58.447  1.00146.43           C  
ANISOU 3411  CA  LEU A 270    20168  19642  15826     77  -1703    264       C  
ATOM   3412  C   LEU A 270       6.014  31.466 -59.852  1.00159.83           C  
ANISOU 3412  C   LEU A 270    21962  21327  17441     11  -1803    337       C  
ATOM   3413  O   LEU A 270       5.889  32.621 -60.294  1.00176.55           O  
ANISOU 3413  O   LEU A 270    24199  23353  19528    -67  -1906    430       O  
ATOM   3414  CB  LEU A 270       8.071  30.911 -58.488  1.00143.15           C  
ANISOU 3414  CB  LEU A 270    19710  19384  15296    -20  -1576    221       C  
ATOM   3415  CG  LEU A 270       9.082  31.805 -59.214  1.00141.92           C  
ANISOU 3415  CG  LEU A 270    19648  19281  14994   -200  -1577    287       C  
ATOM   3416  CD1 LEU A 270      10.457  31.642 -58.586  1.00137.52           C  
ANISOU 3416  CD1 LEU A 270    19021  18838  14392   -249  -1449    221       C  
ATOM   3417  CD2 LEU A 270       9.157  31.502 -60.712  1.00148.19           C  
ANISOU 3417  CD2 LEU A 270    20494  20171  15640   -312  -1599    318       C  
ATOM   3418  N   PRO A 271       5.678  30.409 -60.611  1.00144.40           N  
ANISOU 3418  N   PRO A 271    19969  19455  15443     32  -1785    303       N  
ATOM   3419  CA  PRO A 271       5.211  30.650 -61.989  1.00133.54           C  
ANISOU 3419  CA  PRO A 271    18692  18071  13975    -47  -1882    378       C  
ATOM   3420  C   PRO A 271       3.995  31.555 -62.088  1.00138.01           C  
ANISOU 3420  C   PRO A 271    19349  18460  14628      4  -2041    451       C  
ATOM   3421  O   PRO A 271       3.906  32.350 -63.032  1.00140.64           O  
ANISOU 3421  O   PRO A 271    19809  18748  14880   -101  -2144    545       O  
ATOM   3422  CB  PRO A 271       4.890  29.235 -62.484  1.00127.43           C  
ANISOU 3422  CB  PRO A 271    17833  17403  13183     11  -1830    307       C  
ATOM   3423  CG  PRO A 271       5.838  28.377 -61.762  1.00125.89           C  
ANISOU 3423  CG  PRO A 271    17521  17324  12986     34  -1689    209       C  
ATOM   3424  CD  PRO A 271       5.990  28.983 -60.396  1.00134.69           C  
ANISOU 3424  CD  PRO A 271    18614  18351  14211     92  -1672    199       C  
ATOM   3425  N   TYR A 272       3.076  31.489 -61.133  1.00142.97           N  
ANISOU 3425  N   TYR A 272    19918  18985  15418    155  -2070    405       N  
ATOM   3426  CA  TYR A 272       1.867  32.308 -61.186  1.00150.58           C  
ANISOU 3426  CA  TYR A 272    20951  19782  16479    219  -2227    450       C  
ATOM   3427  C   TYR A 272       2.146  33.727 -60.701  1.00142.56           C  
ANISOU 3427  C   TYR A 272    20019  18647  15499    175  -2300    511       C  
ATOM   3428  O   TYR A 272       1.860  34.701 -61.397  1.00135.47           O  
ANISOU 3428  O   TYR A 272    19252  17650  14571    112  -2438    601       O  
ATOM   3429  CB  TYR A 272       0.754  31.670 -60.352  1.00165.70           C  
ANISOU 3429  CB  TYR A 272    22759  21648  18551    392  -2227    362       C  
ATOM   3430  CG  TYR A 272      -0.520  32.485 -60.263  1.00184.35           C  
ANISOU 3430  CG  TYR A 272    25167  23844  21033    476  -2386    379       C  
ATOM   3431  CD1 TYR A 272      -1.426  32.521 -61.320  1.00192.49           C  
ANISOU 3431  CD1 TYR A 272    26264  24827  22048    484  -2507    418       C  
ATOM   3432  CD2 TYR A 272      -0.823  33.209 -59.116  1.00190.73           C  
ANISOU 3432  CD2 TYR A 272    25947  24548  21975    551  -2417    346       C  
ATOM   3433  CE1 TYR A 272      -2.596  33.261 -61.238  1.00195.84           C  
ANISOU 3433  CE1 TYR A 272    26724  25097  22588    570  -2662    420       C  
ATOM   3434  CE2 TYR A 272      -1.989  33.952 -59.023  1.00195.01           C  
ANISOU 3434  CE2 TYR A 272    26520  24941  22634    635  -2568    343       C  
ATOM   3435  CZ  TYR A 272      -2.871  33.976 -60.086  1.00197.26           C  
ANISOU 3435  CZ  TYR A 272    26870  25177  22905    647  -2693    378       C  
ATOM   3436  OH  TYR A 272      -4.028  34.715 -59.992  1.00201.04           O  
ANISOU 3436  OH  TYR A 272    27373  25506  23506    738  -2853    362       O  
ATOM   3437  N   ILE A 283      17.405  26.163 -63.584  1.00179.97           N  
ANISOU 3437  N   ILE A 283    23880  25629  18871   -836   -843   -471       N  
ATOM   3438  CA  ILE A 283      17.457  26.307 -62.137  1.00171.09           C  
ANISOU 3438  CA  ILE A 283    22726  24389  17891   -708   -829   -478       C  
ATOM   3439  C   ILE A 283      17.121  24.977 -61.454  1.00177.12           C  
ANISOU 3439  C   ILE A 283    23376  25131  18789   -512   -817   -579       C  
ATOM   3440  O   ILE A 283      16.612  24.957 -60.333  1.00196.74           O  
ANISOU 3440  O   ILE A 283    25858  27477  21418   -378   -838   -554       O  
ATOM   3441  CB  ILE A 283      16.517  27.443 -61.655  1.00159.42           C  
ANISOU 3441  CB  ILE A 283    21376  22702  16493   -687   -916   -317       C  
ATOM   3442  CG1 ILE A 283      15.044  27.029 -61.750  1.00153.26           C  
ANISOU 3442  CG1 ILE A 283    20626  21788  15818   -557  -1003   -257       C  
ATOM   3443  CG2 ILE A 283      16.754  28.709 -62.471  1.00156.57           C  
ANISOU 3443  CG2 ILE A 283    21145  22351  15993   -887   -951   -207       C  
ATOM   3444  CD1 ILE A 283      14.109  27.911 -60.931  1.00148.88           C  
ANISOU 3444  CD1 ILE A 283    20154  21024  15389   -481  -1082   -145       C  
ATOM   3445  N   GLN A 284      17.413  23.854 -62.123  1.00165.41           N  
ANISOU 3445  N   GLN A 284    21803  23788  17259   -501   -786   -696       N  
ATOM   3446  CA  GLN A 284      17.108  22.563 -61.512  1.00156.01           C  
ANISOU 3446  CA  GLN A 284    20514  22570  16192   -322   -787   -791       C  
ATOM   3447  C   GLN A 284      17.990  22.255 -60.308  1.00168.73           C  
ANISOU 3447  C   GLN A 284    22039  24194  17877   -244   -732   -891       C  
ATOM   3448  O   GLN A 284      17.593  21.448 -59.460  1.00177.94           O  
ANISOU 3448  O   GLN A 284    23158  25279  19173    -90   -749   -929       O  
ATOM   3449  CB  GLN A 284      17.218  21.420 -62.521  1.00139.60           C  
ANISOU 3449  CB  GLN A 284    18357  20633  14051   -323   -776   -900       C  
ATOM   3450  CG  GLN A 284      16.408  20.208 -62.066  1.00132.13           C  
ANISOU 3450  CG  GLN A 284    17358  19606  13240   -140   -814   -943       C  
ATOM   3451  CD  GLN A 284      16.772  18.914 -62.763  1.00132.43           C  
ANISOU 3451  CD  GLN A 284    17288  19785  13242   -112   -796  -1091       C  
ATOM   3452  OE1 GLN A 284      15.926  18.294 -63.408  1.00137.91           O  
ANISOU 3452  OE1 GLN A 284    17989  20465  13947    -71   -840  -1077       O  
ATOM   3453  NE2 GLN A 284      18.021  18.481 -62.613  1.00127.32           N  
ANISOU 3453  NE2 GLN A 284    16538  19276  12561   -127   -737  -1241       N  
ATOM   3454  N   GLN A 285      19.179  22.856 -60.212  1.00175.30           N  
ANISOU 3454  N   GLN A 285    22851  25128  18628   -353   -668   -936       N  
ATOM   3455  CA  GLN A 285      19.961  22.705 -58.989  1.00168.59           C  
ANISOU 3455  CA  GLN A 285    21931  24271  17856   -277   -624  -1017       C  
ATOM   3456  C   GLN A 285      19.205  23.285 -57.798  1.00157.74           C  
ANISOU 3456  C   GLN A 285    20622  22697  16614   -185   -662   -904       C  
ATOM   3457  O   GLN A 285      19.190  22.697 -56.704  1.00162.18           O  
ANISOU 3457  O   GLN A 285    21132  23194  17295    -52   -662   -953       O  
ATOM   3458  CB  GLN A 285      21.324  23.388 -59.142  1.00169.61           C  
ANISOU 3458  CB  GLN A 285    22035  24544  17866   -424   -550  -1077       C  
ATOM   3459  CG  GLN A 285      21.880  23.426 -60.568  1.00168.27           C  
ANISOU 3459  CG  GLN A 285    21852  24563  17520   -592   -518  -1128       C  
ATOM   3460  CD  GLN A 285      21.438  24.660 -61.344  1.00164.27           C  
ANISOU 3460  CD  GLN A 285    21486  24021  16909   -755   -548   -969       C  
ATOM   3461  OE1 GLN A 285      20.256  24.998 -61.373  1.00160.41           O  
ANISOU 3461  OE1 GLN A 285    21095  23374  16478   -712   -624   -830       O  
ATOM   3462  NE2 GLN A 285      22.394  25.343 -61.967  1.00164.01           N  
ANISOU 3462  NE2 GLN A 285    21464  24133  16717   -946   -495   -992       N  
ATOM   3463  N   VAL A 286      18.522  24.412 -58.017  1.00146.01           N  
ANISOU 3463  N   VAL A 286    19254  21111  15112   -254   -705   -755       N  
ATOM   3464  CA  VAL A 286      17.673  24.998 -56.985  1.00130.65           C  
ANISOU 3464  CA  VAL A 286    17369  18978  13294   -168   -750   -653       C  
ATOM   3465  C   VAL A 286      16.537  24.048 -56.635  1.00130.95           C  
ANISOU 3465  C   VAL A 286    17385  18917  13453    -12   -801   -653       C  
ATOM   3466  O   VAL A 286      16.139  23.935 -55.468  1.00124.41           O  
ANISOU 3466  O   VAL A 286    16544  17979  12749     98   -811   -646       O  
ATOM   3467  CB  VAL A 286      17.141  26.365 -57.457  1.00118.19           C  
ANISOU 3467  CB  VAL A 286    15921  17315  11669   -275   -803   -504       C  
ATOM   3468  CG1 VAL A 286      16.124  26.919 -56.477  1.00113.29           C  
ANISOU 3468  CG1 VAL A 286    15355  16501  11190   -175   -861   -411       C  
ATOM   3469  CG2 VAL A 286      18.288  27.345 -57.658  1.00114.43           C  
ANISOU 3469  CG2 VAL A 286    15475  16927  11077   -436   -753   -498       C  
ATOM   3470  N   TYR A 287      16.016  23.330 -57.633  1.00135.40           N  
ANISOU 3470  N   TYR A 287    17943  19526  13978     -8   -830   -668       N  
ATOM   3471  CA  TYR A 287      14.956  22.366 -57.359  1.00133.59           C  
ANISOU 3471  CA  TYR A 287    17690  19213  13855    132   -876   -675       C  
ATOM   3472  C   TYR A 287      15.471  21.208 -56.516  1.00135.59           C  
ANISOU 3472  C   TYR A 287    17842  19497  14180    241   -843   -799       C  
ATOM   3473  O   TYR A 287      14.775  20.738 -55.609  1.00131.96           O  
ANISOU 3473  O   TYR A 287    17373  18929  13837    358   -871   -791       O  
ATOM   3474  CB  TYR A 287      14.355  21.851 -58.667  1.00123.01           C  
ANISOU 3474  CB  TYR A 287    16363  17923  12450    106   -912   -668       C  
ATOM   3475  CG  TYR A 287      13.357  20.727 -58.476  1.00108.76           C  
ANISOU 3475  CG  TYR A 287    14526  16054  10743    242   -953   -693       C  
ATOM   3476  CD1 TYR A 287      12.011  20.995 -58.250  1.00104.53           C  
ANISOU 3476  CD1 TYR A 287    14052  15375  10290    304  -1018   -598       C  
ATOM   3477  CD2 TYR A 287      13.763  19.395 -58.515  1.00103.82           C  
ANISOU 3477  CD2 TYR A 287    13807  15512  10128    308   -932   -818       C  
ATOM   3478  CE1 TYR A 287      11.096  19.970 -58.070  1.00103.35           C  
ANISOU 3478  CE1 TYR A 287    13873  15174  10223    417  -1052   -623       C  
ATOM   3479  CE2 TYR A 287      12.859  18.365 -58.333  1.00100.09           C  
ANISOU 3479  CE2 TYR A 287    13312  14976   9740    424   -973   -837       C  
ATOM   3480  CZ  TYR A 287      11.526  18.656 -58.110  1.00100.17           C  
ANISOU 3480  CZ  TYR A 287    13385  14850   9824    473  -1029   -738       C  
ATOM   3481  OH  TYR A 287      10.620  17.633 -57.929  1.00 92.54           O  
ANISOU 3481  OH  TYR A 287    12397  13829   8936    578  -1066   -760       O  
ATOM   3482  N   LEU A 288      16.693  20.744 -56.791  1.00138.54           N  
ANISOU 3482  N   LEU A 288    18139  20019  14483    201   -789   -918       N  
ATOM   3483  CA  LEU A 288      17.262  19.662 -55.996  1.00130.36           C  
ANISOU 3483  CA  LEU A 288    17010  19007  13516    306   -773  -1042       C  
ATOM   3484  C   LEU A 288      17.433  20.096 -54.548  1.00133.16           C  
ANISOU 3484  C   LEU A 288    17372  19262  13963    360   -761  -1018       C  
ATOM   3485  O   LEU A 288      17.054  19.371 -53.616  1.00127.66           O  
ANISOU 3485  O   LEU A 288    16652  18482  13372    476   -786  -1040       O  
ATOM   3486  CB  LEU A 288      18.604  19.226 -56.587  1.00119.51           C  
ANISOU 3486  CB  LEU A 288    15547  17817  12046    247   -721  -1186       C  
ATOM   3487  CG  LEU A 288      18.577  18.263 -57.773  1.00114.76           C  
ANISOU 3487  CG  LEU A 288    14892  17328  11382    239   -733  -1272       C  
ATOM   3488  CD1 LEU A 288      19.926  18.248 -58.473  1.00117.57           C  
ANISOU 3488  CD1 LEU A 288    15171  17884  11617    136   -673  -1402       C  
ATOM   3489  CD2 LEU A 288      18.193  16.864 -57.312  1.00108.46           C  
ANISOU 3489  CD2 LEU A 288    14039  16479  10691    392   -779  -1349       C  
ATOM   3490  N   ALA A 289      17.959  21.307 -54.341  1.00135.72           N  
ANISOU 3490  N   ALA A 289    17733  19590  14244    270   -725   -966       N  
ATOM   3491  CA  ALA A 289      18.185  21.778 -52.979  1.00124.83           C  
ANISOU 3491  CA  ALA A 289    16357  18125  12947    313   -708   -948       C  
ATOM   3492  C   ALA A 289      16.867  21.982 -52.241  1.00122.67           C  
ANISOU 3492  C   ALA A 289    16141  17683  12786    392   -760   -845       C  
ATOM   3493  O   ALA A 289      16.690  21.491 -51.119  1.00125.22           O  
ANISOU 3493  O   ALA A 289    16436  17934  13206    488   -768   -869       O  
ATOM   3494  CB  ALA A 289      19.001  23.069 -53.001  1.00118.15           C  
ANISOU 3494  CB  ALA A 289    15544  17322  12027    191   -661   -912       C  
ATOM   3495  N   ILE A 290      15.918  22.683 -52.867  1.00120.53           N  
ANISOU 3495  N   ILE A 290    15948  17350  12500    351   -801   -737       N  
ATOM   3496  CA  ILE A 290      14.641  22.958 -52.217  1.00112.04           C  
ANISOU 3496  CA  ILE A 290    14918  16122  11528    421   -852   -653       C  
ATOM   3497  C   ILE A 290      13.885  21.669 -51.935  1.00111.48           C  
ANISOU 3497  C   ILE A 290    14809  16015  11533    534   -884   -697       C  
ATOM   3498  O   ILE A 290      13.213  21.545 -50.903  1.00 97.95           O  
ANISOU 3498  O   ILE A 290    13095  14201   9919    610   -903   -678       O  
ATOM   3499  CB  ILE A 290      13.811  23.923 -53.087  1.00104.37           C  
ANISOU 3499  CB  ILE A 290    14036  15097  10521    355   -903   -542       C  
ATOM   3500  CG1 ILE A 290      14.353  25.350 -52.985  1.00102.51           C  
ANISOU 3500  CG1 ILE A 290    13858  14846  10245    256   -889   -478       C  
ATOM   3501  CG2 ILE A 290      12.350  23.881 -52.699  1.00101.36           C  
ANISOU 3501  CG2 ILE A 290    13685  14583  10245    442   -967   -485       C  
ATOM   3502  CD1 ILE A 290      13.593  26.344 -53.841  1.00107.45           C  
ANISOU 3502  CD1 ILE A 290    14584  15407  10834    186   -956   -366       C  
ATOM   3503  N   MET A 291      14.004  20.679 -52.821  1.00121.88           N  
ANISOU 3503  N   MET A 291    16090  17418  12800    542   -889   -760       N  
ATOM   3504  CA  MET A 291      13.329  19.411 -52.584  1.00121.77           C  
ANISOU 3504  CA  MET A 291    16043  17369  12854    644   -923   -803       C  
ATOM   3505  C   MET A 291      13.957  18.669 -51.415  1.00109.57           C  
ANISOU 3505  C   MET A 291    14443  15818  11372    714   -906   -884       C  
ATOM   3506  O   MET A 291      13.245  18.096 -50.578  1.00106.06           O  
ANISOU 3506  O   MET A 291    13999  15285  11014    792   -936   -879       O  
ATOM   3507  CB  MET A 291      13.364  18.555 -53.850  1.00124.34           C  
ANISOU 3507  CB  MET A 291    16342  17791  13109    632   -936   -857       C  
ATOM   3508  CG  MET A 291      12.345  17.429 -53.862  1.00119.62           C  
ANISOU 3508  CG  MET A 291    15735  17141  12575    723   -985   -872       C  
ATOM   3509  SD  MET A 291      10.683  18.039 -53.519  1.00110.01           S  
ANISOU 3509  SD  MET A 291    14589  15775  11435    753  -1035   -751       S  
ATOM   3510  CE  MET A 291      10.535  19.355 -54.725  1.00107.94           C  
ANISOU 3510  CE  MET A 291    14395  15535  11082    644  -1045   -660       C  
ATOM   3511  N   TRP A 292      15.288  18.687 -51.327  1.00110.77           N  
ANISOU 3511  N   TRP A 292    14549  16062  11477    682   -861   -961       N  
ATOM   3512  CA  TRP A 292      15.935  18.054 -50.186  1.00114.42           C  
ANISOU 3512  CA  TRP A 292    14964  16511  12000    749   -854  -1037       C  
ATOM   3513  C   TRP A 292      15.556  18.737 -48.877  1.00114.13           C  
ANISOU 3513  C   TRP A 292    14961  16362  12042    770   -850   -968       C  
ATOM   3514  O   TRP A 292      15.291  18.064 -47.872  1.00115.30           O  
ANISOU 3514  O   TRP A 292    15099  16443  12268    843   -874   -987       O  
ATOM   3515  CB  TRP A 292      17.450  18.054 -50.388  1.00117.18           C  
ANISOU 3515  CB  TRP A 292    15252  16988  12283    707   -808  -1140       C  
ATOM   3516  CG  TRP A 292      18.174  17.330 -49.319  1.00112.75           C  
ANISOU 3516  CG  TRP A 292    14641  16418  11782    781   -813  -1230       C  
ATOM   3517  CD1 TRP A 292      18.623  16.044 -49.347  1.00106.79           C  
ANISOU 3517  CD1 TRP A 292    13828  15703  11045    851   -848  -1347       C  
ATOM   3518  CD2 TRP A 292      18.572  17.871 -48.056  1.00115.33           C  
ANISOU 3518  CD2 TRP A 292    14973  16689  12158    792   -791  -1213       C  
ATOM   3519  NE1 TRP A 292      19.250  15.740 -48.162  1.00109.28           N  
ANISOU 3519  NE1 TRP A 292    14119  15983  11419    906   -856  -1399       N  
ATOM   3520  CE2 TRP A 292      19.238  16.849 -47.356  1.00115.85           C  
ANISOU 3520  CE2 TRP A 292    14988  16762  12269    869   -817  -1318       C  
ATOM   3521  CE3 TRP A 292      18.421  19.121 -47.445  1.00111.71           C  
ANISOU 3521  CE3 TRP A 292    14559  16174  11713    746   -757  -1121       C  
ATOM   3522  CZ2 TRP A 292      19.752  17.037 -46.074  1.00115.95           C  
ANISOU 3522  CZ2 TRP A 292    14995  16728  12334    896   -807  -1329       C  
ATOM   3523  CZ3 TRP A 292      18.930  19.306 -46.175  1.00107.72           C  
ANISOU 3523  CZ3 TRP A 292    14040  15627  11260    774   -741  -1137       C  
ATOM   3524  CH2 TRP A 292      19.589  18.271 -45.503  1.00112.70           C  
ANISOU 3524  CH2 TRP A 292    14623  16270  11930    846   -764  -1238       C  
ATOM   3525  N   LEU A 293      15.516  20.072 -48.867  1.00109.52           N  
ANISOU 3525  N   LEU A 293    14419  15755  11437    702   -824   -889       N  
ATOM   3526  CA  LEU A 293      15.161  20.775 -47.637  1.00 97.70           C  
ANISOU 3526  CA  LEU A 293    12947  14157  10017    720   -820   -832       C  
ATOM   3527  C   LEU A 293      13.715  20.514 -47.247  1.00 90.50           C  
ANISOU 3527  C   LEU A 293    12065  13137   9185    778   -868   -778       C  
ATOM   3528  O   LEU A 293      13.407  20.315 -46.067  1.00102.39           O  
ANISOU 3528  O   LEU A 293    13563  14574  10766    825   -874   -779       O  
ATOM   3529  CB  LEU A 293      15.397  22.277 -47.786  1.00 99.17           C  
ANISOU 3529  CB  LEU A 293    13176  14337  10168    635   -792   -762       C  
ATOM   3530  CG  LEU A 293      14.931  23.101 -46.578  1.00104.35           C  
ANISOU 3530  CG  LEU A 293    13855  14886  10907    653   -792   -704       C  
ATOM   3531  CD1 LEU A 293      15.667  22.702 -45.307  1.00 98.22           C  
ANISOU 3531  CD1 LEU A 293    13033  14111  10177    696   -761   -766       C  
ATOM   3532  CD2 LEU A 293      15.058  24.598 -46.832  1.00110.33           C  
ANISOU 3532  CD2 LEU A 293    14664  15624  11633    571   -782   -629       C  
ATOM   3533  N   ALA A 294      12.819  20.498 -48.231  1.00 83.62           N  
ANISOU 3533  N   ALA A 294    11224  12255   8294    769   -904   -735       N  
ATOM   3534  CA  ALA A 294      11.411  20.275 -47.942  1.00 84.08           C  
ANISOU 3534  CA  ALA A 294    11304  12220   8423    820   -950   -693       C  
ATOM   3535  C   ALA A 294      11.166  18.869 -47.420  1.00 86.32           C  
ANISOU 3535  C   ALA A 294    11555  12492   8749    891   -970   -753       C  
ATOM   3536  O   ALA A 294      10.386  18.679 -46.479  1.00 88.13           O  
ANISOU 3536  O   ALA A 294    11790  12646   9051    929   -987   -739       O  
ATOM   3537  CB  ALA A 294      10.584  20.530 -49.199  1.00 84.46           C  
ANISOU 3537  CB  ALA A 294    11391  12268   8434    795   -987   -641       C  
ATOM   3538  N   MET A 295      11.826  17.870 -48.005  1.00 86.73           N  
ANISOU 3538  N   MET A 295    11576  12621   8758    905   -972   -824       N  
ATOM   3539  CA  MET A 295      11.592  16.501 -47.570  1.00 89.23           C  
ANISOU 3539  CA  MET A 295    11871  12917   9116    972  -1007   -880       C  
ATOM   3540  C   MET A 295      12.444  16.107 -46.370  1.00 94.89           C  
ANISOU 3540  C   MET A 295    12563  13624   9868    999   -997   -934       C  
ATOM   3541  O   MET A 295      12.232  15.025 -45.811  1.00102.00           O  
ANISOU 3541  O   MET A 295    13460  14488  10808   1049  -1036   -970       O  
ATOM   3542  CB  MET A 295      11.818  15.536 -48.734  1.00 86.75           C  
ANISOU 3542  CB  MET A 295    11532  12679   8750    985  -1029   -940       C  
ATOM   3543  CG  MET A 295      10.985  15.895 -49.957  1.00105.66           C  
ANISOU 3543  CG  MET A 295    13954  15087  11104    954  -1042   -886       C  
ATOM   3544  SD  MET A 295      10.425  14.481 -50.920  1.00128.51           S  
ANISOU 3544  SD  MET A 295    16831  18011  13985    999  -1091   -936       S  
ATOM   3545  CE  MET A 295       9.342  13.675 -49.746  1.00120.41           C  
ANISOU 3545  CE  MET A 295    15824  16870  13056   1065  -1134   -922       C  
ATOM   3546  N   SER A 296      13.389  16.954 -45.954  1.00 88.69           N  
ANISOU 3546  N   SER A 296    11767  12866   9067    965   -951   -937       N  
ATOM   3547  CA  SER A 296      14.160  16.698 -44.745  1.00 83.13           C  
ANISOU 3547  CA  SER A 296    11042  12146   8398    990   -943   -982       C  
ATOM   3548  C   SER A 296      13.364  16.943 -43.468  1.00 86.22           C  
ANISOU 3548  C   SER A 296    11460  12438   8860   1001   -950   -929       C  
ATOM   3549  O   SER A 296      13.788  16.489 -42.401  1.00 86.51           O  
ANISOU 3549  O   SER A 296    11489  12448   8932   1025   -959   -962       O  
ATOM   3550  CB  SER A 296      15.423  17.564 -44.736  1.00 83.09           C  
ANISOU 3550  CB  SER A 296    11012  12209   8350    944   -888  -1007       C  
ATOM   3551  OG  SER A 296      15.098  18.934 -44.593  1.00 83.36           O  
ANISOU 3551  OG  SER A 296    11077  12211   8385    891   -853   -924       O  
ATOM   3552  N   SER A 297      12.218  17.627 -43.549  1.00 91.00           N  
ANISOU 3552  N   SER A 297    12095  12991   9489    983   -951   -854       N  
ATOM   3553  CA  SER A 297      11.433  17.915 -42.355  1.00 93.04           C  
ANISOU 3553  CA  SER A 297    12368  13171   9813    986   -953   -818       C  
ATOM   3554  C   SER A 297      10.931  16.647 -41.680  1.00101.01           C  
ANISOU 3554  C   SER A 297    13383  14139  10857   1022   -997   -846       C  
ATOM   3555  O   SER A 297      10.659  16.661 -40.473  1.00106.40           O  
ANISOU 3555  O   SER A 297    14071  14773  11581   1017   -995   -838       O  
ATOM   3556  CB  SER A 297      10.249  18.811 -42.717  1.00 86.41           C  
ANISOU 3556  CB  SER A 297    11550  12289   8993    967   -958   -751       C  
ATOM   3557  OG  SER A 297       9.347  18.124 -43.564  1.00 84.01           O  
ANISOU 3557  OG  SER A 297    11257  11982   8681    987   -998   -747       O  
ATOM   3558  N   THR A 298      10.790  15.558 -42.437  1.00 95.10           N  
ANISOU 3558  N   THR A 298    12636  13411  10087   1051  -1038   -879       N  
ATOM   3559  CA  THR A 298      10.286  14.312 -41.876  1.00 85.05           C  
ANISOU 3559  CA  THR A 298    11379  12093   8842   1079  -1089   -901       C  
ATOM   3560  C   THR A 298      11.254  13.696 -40.868  1.00 81.54           C  
ANISOU 3560  C   THR A 298    10933  11639   8411   1095  -1107   -950       C  
ATOM   3561  O   THR A 298      10.818  12.998 -39.947  1.00 94.90           O  
ANISOU 3561  O   THR A 298    12652  13274  10132   1095  -1144   -948       O  
ATOM   3562  CB  THR A 298       9.968  13.337 -43.010  1.00 78.30           C  
ANISOU 3562  CB  THR A 298    10526  11263   7962   1108  -1132   -928       C  
ATOM   3563  OG1 THR A 298      11.060  13.298 -43.939  1.00 80.95           O  
ANISOU 3563  OG1 THR A 298    10830  11676   8250   1118  -1121   -978       O  
ATOM   3564  CG2 THR A 298       8.718  13.776 -43.747  1.00 73.65           C  
ANISOU 3564  CG2 THR A 298     9947  10662   7372   1094  -1130   -876       C  
ATOM   3565  N   MET A 299      12.562  13.933 -41.022  1.00 70.02           N  
ANISOU 3565  N   MET A 299     9445  10233   6927   1102  -1085   -995       N  
ATOM   3566  CA  MET A 299      13.547  13.375 -40.099  1.00 77.43           C  
ANISOU 3566  CA  MET A 299    10379  11161   7880   1125  -1110  -1049       C  
ATOM   3567  C   MET A 299      13.717  14.191 -38.818  1.00 77.04           C  
ANISOU 3567  C   MET A 299    10336  11079   7858   1094  -1072  -1016       C  
ATOM   3568  O   MET A 299      14.319  13.683 -37.863  1.00 64.71           O  
ANISOU 3568  O   MET A 299     8782   9491   6314   1107  -1102  -1048       O  
ATOM   3569  CB  MET A 299      14.908  13.240 -40.793  1.00 75.56           C  
ANISOU 3569  CB  MET A 299    10097  11006   7607   1149  -1105  -1130       C  
ATOM   3570  CG  MET A 299      15.678  14.543 -40.861  1.00 82.44           C  
ANISOU 3570  CG  MET A 299    10940  11934   8451   1110  -1028  -1122       C  
ATOM   3571  SD  MET A 299      17.074  14.534 -42.000  1.00 96.21           S  
ANISOU 3571  SD  MET A 299    12622  13802  10131   1114  -1006  -1219       S  
ATOM   3572  CE  MET A 299      18.384  13.913 -40.952  1.00113.78           C  
ANISOU 3572  CE  MET A 299    14818  16028  12383   1160  -1039  -1316       C  
ATOM   3573  N   TYR A 300      13.191  15.423 -38.764  1.00 70.34           N  
ANISOU 3573  N   TYR A 300     9485  10227   7016   1054  -1015   -955       N  
ATOM   3574  CA  TYR A 300      13.551  16.357 -37.697  1.00 64.36           C  
ANISOU 3574  CA  TYR A 300     8720   9455   6279   1025   -970   -935       C  
ATOM   3575  C   TYR A 300      12.749  16.145 -36.416  1.00 79.83           C  
ANISOU 3575  C   TYR A 300    10705  11348   8280   1005   -986   -907       C  
ATOM   3576  O   TYR A 300      13.296  16.285 -35.317  1.00 73.03           O  
ANISOU 3576  O   TYR A 300     9842  10472   7434    993   -976   -917       O  
ATOM   3577  CB  TYR A 300      13.379  17.795 -38.182  1.00 54.85           C  
ANISOU 3577  CB  TYR A 300     7503   8270   5066    990   -911   -887       C  
ATOM   3578  CG  TYR A 300      14.402  18.227 -39.206  1.00 71.71           C  
ANISOU 3578  CG  TYR A 300     9617  10481   7150    984   -882   -913       C  
ATOM   3579  CD1 TYR A 300      15.697  17.728 -39.180  1.00 81.97           C  
ANISOU 3579  CD1 TYR A 300    10889  11832   8423   1003   -883   -986       C  
ATOM   3580  CD2 TYR A 300      14.070  19.131 -40.206  1.00 79.58           C  
ANISOU 3580  CD2 TYR A 300    10620  11499   8118    952   -859   -869       C  
ATOM   3581  CE1 TYR A 300      16.633  18.126 -40.123  1.00 80.10           C  
ANISOU 3581  CE1 TYR A 300    10624  11680   8130    984   -851  -1021       C  
ATOM   3582  CE2 TYR A 300      14.995  19.537 -41.148  1.00 82.94           C  
ANISOU 3582  CE2 TYR A 300    11030  12001   8483    926   -831   -891       C  
ATOM   3583  CZ  TYR A 300      16.273  19.032 -41.103  1.00 79.42           C  
ANISOU 3583  CZ  TYR A 300    10550  11620   8008    939   -822   -970       C  
ATOM   3584  OH  TYR A 300      17.192  19.435 -42.043  1.00 80.16           O  
ANISOU 3584  OH  TYR A 300    10621  11805   8033    902   -788  -1002       O  
ATOM   3585  N   ASN A 301      11.455  15.833 -36.526  1.00 92.38           N  
ANISOU 3585  N   ASN A 301    12313  12904   9884    994  -1008   -877       N  
ATOM   3586  CA  ASN A 301      10.631  15.693 -35.323  1.00 89.58           C  
ANISOU 3586  CA  ASN A 301    11977  12501   9559    958  -1016   -858       C  
ATOM   3587  C   ASN A 301      11.194  14.688 -34.328  1.00 87.32           C  
ANISOU 3587  C   ASN A 301    11720  12187   9271    956  -1062   -886       C  
ATOM   3588  O   ASN A 301      11.251  15.014 -33.128  1.00 91.67           O  
ANISOU 3588  O   ASN A 301    12274  12719   9837    918  -1045   -877       O  
ATOM   3589  CB  ASN A 301       9.184  15.366 -35.707  1.00 88.71           C  
ANISOU 3589  CB  ASN A 301    11879  12370   9457    946  -1038   -837       C  
ATOM   3590  CG  ASN A 301       8.475  16.541 -36.344  1.00 88.96           C  
ANISOU 3590  CG  ASN A 301    11884  12413   9503    941   -999   -806       C  
ATOM   3591  OD1 ASN A 301       8.939  17.678 -36.262  1.00 80.36           O  
ANISOU 3591  OD1 ASN A 301    10774  11335   8424    934   -956   -793       O  
ATOM   3592  ND2 ASN A 301       7.336  16.277 -36.970  1.00101.60           N  
ANISOU 3592  ND2 ASN A 301    13490  14005  11108    944  -1022   -796       N  
ATOM   3593  N   PRO A 302      11.605  13.478 -34.717  1.00 88.09           N  
ANISOU 3593  N   PRO A 302    11841  12276   9351    992  -1128   -921       N  
ATOM   3594  CA  PRO A 302      12.213  12.582 -33.722  1.00 88.89           C  
ANISOU 3594  CA  PRO A 302    11979  12340   9456    991  -1187   -947       C  
ATOM   3595  C   PRO A 302      13.451  13.168 -33.061  1.00 93.00           C  
ANISOU 3595  C   PRO A 302    12477  12878   9980    999  -1159   -970       C  
ATOM   3596  O   PRO A 302      13.669  12.952 -31.859  1.00100.63           O  
ANISOU 3596  O   PRO A 302    13472  13809  10955    971  -1182   -967       O  
ATOM   3597  CB  PRO A 302      12.559  11.335 -34.547  1.00 94.99           C  
ANISOU 3597  CB  PRO A 302    12770  13107  10216   1046  -1266   -993       C  
ATOM   3598  CG  PRO A 302      11.619  11.375 -35.698  1.00100.65           C  
ANISOU 3598  CG  PRO A 302    13474  13844  10923   1052  -1251   -973       C  
ATOM   3599  CD  PRO A 302      11.500  12.824 -36.035  1.00 96.21           C  
ANISOU 3599  CD  PRO A 302    12868  13326  10361   1034  -1162   -942       C  
ATOM   3600  N   ILE A 303      14.246  13.949 -33.800  1.00 81.78           N  
ANISOU 3600  N   ILE A 303    11008  11514   8549   1027  -1108   -992       N  
ATOM   3601  CA  ILE A 303      15.409  14.602 -33.205  1.00 76.24           C  
ANISOU 3601  CA  ILE A 303    10280  10838   7851   1029  -1072  -1016       C  
ATOM   3602  C   ILE A 303      14.988  15.653 -32.189  1.00 80.67           C  
ANISOU 3602  C   ILE A 303    10836  11384   8432    974  -1012   -968       C  
ATOM   3603  O   ILE A 303      15.558  15.742 -31.092  1.00 88.51           O  
ANISOU 3603  O   ILE A 303    11834  12363   9435    959  -1011   -977       O  
ATOM   3604  CB  ILE A 303      16.277  15.234 -34.308  1.00 67.38           C  
ANISOU 3604  CB  ILE A 303     9107   9790   6703   1055  -1026  -1051       C  
ATOM   3605  CG1 ILE A 303      16.640  14.211 -35.385  1.00 68.73           C  
ANISOU 3605  CG1 ILE A 303     9272   9991   6853   1106  -1082  -1112       C  
ATOM   3606  CG2 ILE A 303      17.530  15.856 -33.709  1.00 61.88           C  
ANISOU 3606  CG2 ILE A 303     8380   9126   6005   1055   -989  -1086       C  
ATOM   3607  CD1 ILE A 303      17.375  14.822 -36.558  1.00 71.59           C  
ANISOU 3607  CD1 ILE A 303     9584  10442   7177   1113  -1032  -1148       C  
ATOM   3608  N   ILE A 304      13.975  16.455 -32.527  1.00 72.88           N  
ANISOU 3608  N   ILE A 304     9837  10400   7455    945   -966   -921       N  
ATOM   3609  CA  ILE A 304      13.501  17.479 -31.599  1.00 71.26           C  
ANISOU 3609  CA  ILE A 304     9618  10183   7276    897   -913   -887       C  
ATOM   3610  C   ILE A 304      12.957  16.848 -30.324  1.00 70.26           C  
ANISOU 3610  C   ILE A 304     9523  10014   7158    854   -945   -880       C  
ATOM   3611  O   ILE A 304      13.252  17.307 -29.210  1.00 73.43           O  
ANISOU 3611  O   ILE A 304     9916  10411   7571    821   -919   -878       O  
ATOM   3612  CB  ILE A 304      12.457  18.373 -32.288  1.00 69.75           C  
ANISOU 3612  CB  ILE A 304     9408   9996   7099    884   -877   -850       C  
ATOM   3613  CG1 ILE A 304      13.094  19.106 -33.466  1.00 71.26           C  
ANISOU 3613  CG1 ILE A 304     9579  10228   7270    908   -847   -849       C  
ATOM   3614  CG2 ILE A 304      11.880  19.373 -31.307  1.00 63.50           C  
ANISOU 3614  CG2 ILE A 304     8595   9190   6343    839   -833   -830       C  
ATOM   3615  CD1 ILE A 304      12.100  19.806 -34.349  1.00 82.66           C  
ANISOU 3615  CD1 ILE A 304    11018  11667   8722    902   -836   -812       C  
ATOM   3616  N   TYR A 305      12.175  15.772 -30.459  1.00 64.07           N  
ANISOU 3616  N   TYR A 305     8777   9201   6364    847  -1003   -876       N  
ATOM   3617  CA  TYR A 305      11.658  15.109 -29.268  1.00 62.72           C  
ANISOU 3617  CA  TYR A 305     8646   8994   6190    789  -1039   -867       C  
ATOM   3618  C   TYR A 305      12.787  14.538 -28.424  1.00 80.58           C  
ANISOU 3618  C   TYR A 305    10940  11234   8441    794  -1083   -889       C  
ATOM   3619  O   TYR A 305      12.756  14.629 -27.191  1.00 85.70           O  
ANISOU 3619  O   TYR A 305    11605  11869   9089    736  -1079   -878       O  
ATOM   3620  CB  TYR A 305      10.695  13.980 -29.639  1.00 64.31           C  
ANISOU 3620  CB  TYR A 305     8891   9168   6375    776  -1100   -860       C  
ATOM   3621  CG  TYR A 305       9.539  14.332 -30.548  1.00 69.76           C  
ANISOU 3621  CG  TYR A 305     9555   9876   7074    777  -1073   -846       C  
ATOM   3622  CD1 TYR A 305       9.009  15.612 -30.591  1.00 70.88           C  
ANISOU 3622  CD1 TYR A 305     9646  10044   7243    764  -1003   -834       C  
ATOM   3623  CD2 TYR A 305       8.941  13.350 -31.325  1.00 69.43           C  
ANISOU 3623  CD2 TYR A 305     9544   9820   7018    793  -1126   -847       C  
ATOM   3624  CE1 TYR A 305       7.938  15.910 -31.415  1.00 66.82           C  
ANISOU 3624  CE1 TYR A 305     9110   9540   6740    771   -992   -826       C  
ATOM   3625  CE2 TYR A 305       7.874  13.636 -32.141  1.00 73.02           C  
ANISOU 3625  CE2 TYR A 305     9975  10290   7480    796  -1106   -837       C  
ATOM   3626  CZ  TYR A 305       7.374  14.914 -32.185  1.00 74.84           C  
ANISOU 3626  CZ  TYR A 305    10154  10544   7737    786  -1041   -827       C  
ATOM   3627  OH  TYR A 305       6.308  15.191 -33.010  1.00 89.37           O  
ANISOU 3627  OH  TYR A 305    11973  12394   9588    795  -1034   -821       O  
ATOM   3628  N   CYS A 306      13.802  13.952 -29.066  1.00 90.73           N  
ANISOU 3628  N   CYS A 306    12232  12521   9719    861  -1129   -926       N  
ATOM   3629  CA  CYS A 306      14.901  13.372 -28.298  1.00 99.71           C  
ANISOU 3629  CA  CYS A 306    13398  13633  10853    877  -1186   -957       C  
ATOM   3630  C   CYS A 306      15.717  14.433 -27.566  1.00104.23           C  
ANISOU 3630  C   CYS A 306    13931  14235  11437    867  -1120   -964       C  
ATOM   3631  O   CYS A 306      16.173  14.200 -26.440  1.00113.40           O  
ANISOU 3631  O   CYS A 306    15121  15369  12597    841  -1151   -967       O  
ATOM   3632  CB  CYS A 306      15.800  12.539 -29.211  1.00106.72           C  
ANISOU 3632  CB  CYS A 306    14288  14524  11738    959  -1252  -1015       C  
ATOM   3633  SG  CYS A 306      17.236  11.851 -28.370  1.00115.61           S  
ANISOU 3633  SG  CYS A 306    15440  15618  12869    997  -1337  -1073       S  
ATOM   3634  N   CYS A 307      15.902  15.607 -28.171  1.00 96.91           N  
ANISOU 3634  N   CYS A 307    12943  13359  10518    882  -1035   -963       N  
ATOM   3635  CA  CYS A 307      16.770  16.588 -27.531  1.00 92.24           C  
ANISOU 3635  CA  CYS A 307    12315  12796   9937    875   -976   -973       C  
ATOM   3636  C   CYS A 307      16.051  17.428 -26.480  1.00 89.52           C  
ANISOU 3636  C   CYS A 307    11961  12444   9608    805   -920   -933       C  
ATOM   3637  O   CYS A 307      16.643  17.747 -25.441  1.00 94.30           O  
ANISOU 3637  O   CYS A 307    12562  13050  10219    782   -905   -940       O  
ATOM   3638  CB  CYS A 307      17.405  17.503 -28.582  1.00100.25           C  
ANISOU 3638  CB  CYS A 307    13275  13868  10947    911   -913   -991       C  
ATOM   3639  SG  CYS A 307      18.651  18.640 -27.920  1.00123.59           S  
ANISOU 3639  SG  CYS A 307    16186  16863  13909    906   -844  -1014       S  
ATOM   3640  N   LEU A 308      14.785  17.781 -26.709  1.00 77.07           N  
ANISOU 3640  N   LEU A 308    10376  10865   8041    771   -893   -900       N  
ATOM   3641  CA  LEU A 308      14.091  18.723 -25.838  1.00 65.74           C  
ANISOU 3641  CA  LEU A 308     8913   9437   6629    710   -835   -879       C  
ATOM   3642  C   LEU A 308      13.078  18.076 -24.900  1.00 74.04           C  
ANISOU 3642  C   LEU A 308     9998  10465   7670    637   -865   -867       C  
ATOM   3643  O   LEU A 308      12.317  18.799 -24.248  1.00 89.28           O  
ANISOU 3643  O   LEU A 308    11895  12411   9618    582   -818   -862       O  
ATOM   3644  CB  LEU A 308      13.422  19.826 -26.655  1.00 63.34           C  
ANISOU 3644  CB  LEU A 308     8564   9153   6350    720   -779   -864       C  
ATOM   3645  CG  LEU A 308      14.380  20.666 -27.503  1.00 69.60           C  
ANISOU 3645  CG  LEU A 308     9327   9972   7144    766   -741   -869       C  
ATOM   3646  CD1 LEU A 308      13.618  21.729 -28.285  1.00 74.64           C  
ANISOU 3646  CD1 LEU A 308     9937  10616   7806    767   -704   -845       C  
ATOM   3647  CD2 LEU A 308      15.465  21.296 -26.636  1.00 64.71           C  
ANISOU 3647  CD2 LEU A 308     8687   9370   6531    758   -702   -885       C  
ATOM   3648  N   ASN A 309      12.998  16.746 -24.851  1.00 70.53           N  
ANISOU 3648  N   ASN A 309     9616   9988   7197    631   -945   -866       N  
ATOM   3649  CA  ASN A 309      12.016  16.082 -23.996  1.00 74.14           C  
ANISOU 3649  CA  ASN A 309    10113  10426   7631    544   -977   -851       C  
ATOM   3650  C   ASN A 309      12.667  14.883 -23.320  1.00 88.00           C  
ANISOU 3650  C   ASN A 309    11947  12136   9354    527  -1067   -850       C  
ATOM   3651  O   ASN A 309      13.114  13.954 -24.000  1.00101.83           O  
ANISOU 3651  O   ASN A 309    13739  13855  11097    584  -1141   -860       O  
ATOM   3652  CB  ASN A 309      10.782  15.648 -24.785  1.00 63.91           C  
ANISOU 3652  CB  ASN A 309     8824   9128   6330    535   -992   -842       C  
ATOM   3653  CG  ASN A 309       9.584  15.412 -23.896  1.00 58.99           C  
ANISOU 3653  CG  ASN A 309     8214   8513   5687    429   -990   -837       C  
ATOM   3654  OD1 ASN A 309       9.361  14.300 -23.417  1.00 49.82           O  
ANISOU 3654  OD1 ASN A 309     7122   7321   4485    373  -1057   -826       O  
ATOM   3655  ND2 ASN A 309       8.805  16.462 -23.664  1.00 65.35           N  
ANISOU 3655  ND2 ASN A 309     8951   9360   6519    396   -917   -851       N  
ATOM   3656  N   ASP A 310      12.709  14.908 -21.981  1.00 83.97           N  
ANISOU 3656  N   ASP A 310    11459  11622   8826    448  -1068   -842       N  
ATOM   3657  CA  ASP A 310      13.398  13.866 -21.220  1.00 87.92           C  
ANISOU 3657  CA  ASP A 310    12041  12071   9295    426  -1164   -837       C  
ATOM   3658  C   ASP A 310      12.732  12.500 -21.361  1.00 90.87           C  
ANISOU 3658  C   ASP A 310    12501  12394   9633    388  -1262   -818       C  
ATOM   3659  O   ASP A 310      13.421  11.472 -21.328  1.00 87.49           O  
ANISOU 3659  O   ASP A 310    12145  11906   9192    418  -1368   -822       O  
ATOM   3660  CB  ASP A 310      13.471  14.264 -19.743  1.00 98.97           C  
ANISOU 3660  CB  ASP A 310    13445  13483  10674    333  -1139   -828       C  
ATOM   3661  CG  ASP A 310      14.358  15.476 -19.502  1.00 98.78           C  
ANISOU 3661  CG  ASP A 310    13349  13497  10685    376  -1059   -849       C  
ATOM   3662  OD1 ASP A 310      15.412  15.586 -20.165  1.00103.68           O  
ANISOU 3662  OD1 ASP A 310    13952  14113  11329    473  -1067   -872       O  
ATOM   3663  OD2 ASP A 310      13.999  16.319 -18.651  1.00 92.12           O  
ANISOU 3663  OD2 ASP A 310    12463  12693   9844    307   -988   -848       O  
ATOM   3664  N   ARG A 311      11.405  12.462 -21.514  1.00100.98           N  
ANISOU 3664  N   ARG A 311    13774  13695  10898    323  -1234   -804       N  
ATOM   3665  CA  ARG A 311      10.719  11.181 -21.660  1.00106.87           C  
ANISOU 3665  CA  ARG A 311    14604  14396  11607    277  -1323   -785       C  
ATOM   3666  C   ARG A 311      11.079  10.522 -22.987  1.00104.44           C  
ANISOU 3666  C   ARG A 311    14308  14055  11320    389  -1381   -799       C  
ATOM   3667  O   ARG A 311      11.434   9.334 -23.032  1.00112.25           O  
ANISOU 3667  O   ARG A 311    15380  14978  12292    402  -1496   -797       O  
ATOM   3668  CB  ARG A 311       9.204  11.377 -21.537  1.00109.29           C  
ANISOU 3668  CB  ARG A 311    14886  14747  11892    180  -1269   -778       C  
ATOM   3669  CG  ARG A 311       8.788  12.213 -20.330  1.00110.80           C  
ANISOU 3669  CG  ARG A 311    15036  14993  12069     75  -1194   -784       C  
ATOM   3670  CD  ARG A 311       7.536  11.663 -19.661  1.00115.22           C  
ANISOU 3670  CD  ARG A 311    15633  15575  12570    -73  -1205   -777       C  
ATOM   3671  NE  ARG A 311       7.417  12.128 -18.281  1.00126.89           N  
ANISOU 3671  NE  ARG A 311    17100  17097  14017   -192  -1163   -782       N  
ATOM   3672  CZ  ARG A 311       6.816  11.447 -17.309  1.00130.99           C  
ANISOU 3672  CZ  ARG A 311    17685  17623  14461   -345  -1199   -768       C  
ATOM   3673  NH1 ARG A 311       6.282  10.258 -17.562  1.00132.54           N  
ANISOU 3673  NH1 ARG A 311    17970  17778  14610   -397  -1281   -744       N  
ATOM   3674  NH2 ARG A 311       6.758  11.949 -16.079  1.00124.28           N  
ANISOU 3674  NH2 ARG A 311    16816  16825  13581   -454  -1154   -779       N  
ATOM   3675  N   PHE A 312      11.025  11.293 -24.077  1.00 98.67           N  
ANISOU 3675  N   PHE A 312    13496  13367  10626    469  -1310   -818       N  
ATOM   3676  CA  PHE A 312      11.449  10.772 -25.371  1.00102.07           C  
ANISOU 3676  CA  PHE A 312    13926  13781  11073    573  -1354   -839       C  
ATOM   3677  C   PHE A 312      12.927  10.408 -25.373  1.00108.19           C  
ANISOU 3677  C   PHE A 312    14719  14528  11861    651  -1416   -872       C  
ATOM   3678  O   PHE A 312      13.323   9.439 -26.028  1.00111.73           O  
ANISOU 3678  O   PHE A 312    15203  14938  12311    712  -1504   -897       O  
ATOM   3679  CB  PHE A 312      11.137  11.780 -26.478  1.00 97.84           C  
ANISOU 3679  CB  PHE A 312    13304  13303  10566    628  -1263   -848       C  
ATOM   3680  CG  PHE A 312       9.681  11.824 -26.855  1.00 91.55           C  
ANISOU 3680  CG  PHE A 312    12495  12524   9764    582  -1234   -831       C  
ATOM   3681  CD1 PHE A 312       9.144  10.854 -27.677  1.00 83.84           C  
ANISOU 3681  CD1 PHE A 312    11555  11524   8775    601  -1293   -831       C  
ATOM   3682  CD2 PHE A 312       8.852  12.833 -26.397  1.00 94.16           C  
ANISOU 3682  CD2 PHE A 312    12774  12896  10106    524  -1152   -825       C  
ATOM   3683  CE1 PHE A 312       7.814  10.881 -28.027  1.00 81.04           C  
ANISOU 3683  CE1 PHE A 312    11186  11189   8416    560  -1268   -821       C  
ATOM   3684  CE2 PHE A 312       7.513  12.864 -26.750  1.00 87.83           C  
ANISOU 3684  CE2 PHE A 312    11954  12115   9303    487  -1131   -823       C  
ATOM   3685  CZ  PHE A 312       6.998  11.885 -27.564  1.00 78.64           C  
ANISOU 3685  CZ  PHE A 312    10828  10929   8123    504  -1187   -820       C  
ATOM   3686  N   ARG A 313      13.755  11.164 -24.650  1.00109.92           N  
ANISOU 3686  N   ARG A 313    14908  14765  12090    652  -1375   -881       N  
ATOM   3687  CA  ARG A 313      15.171  10.825 -24.566  1.00112.52           C  
ANISOU 3687  CA  ARG A 313    15249  15072  12431    724  -1436   -924       C  
ATOM   3688  C   ARG A 313      15.374   9.479 -23.878  1.00118.58           C  
ANISOU 3688  C   ARG A 313    16121  15755  13179    699  -1577   -920       C  
ATOM   3689  O   ARG A 313      16.167   8.648 -24.345  1.00124.32           O  
ANISOU 3689  O   ARG A 313    16872  16442  13919    780  -1674   -965       O  
ATOM   3690  CB  ARG A 313      15.923  11.938 -23.830  1.00114.69           C  
ANISOU 3690  CB  ARG A 313    15472  15386  12718    718  -1360   -931       C  
ATOM   3691  CG  ARG A 313      17.241  11.518 -23.194  1.00125.29           C  
ANISOU 3691  CG  ARG A 313    16844  16695  14065    756  -1435   -969       C  
ATOM   3692  CD  ARG A 313      18.439  12.019 -23.992  1.00133.74           C  
ANISOU 3692  CD  ARG A 313    17841  17813  15162    858  -1401  -1033       C  
ATOM   3693  NE  ARG A 313      18.589  13.474 -23.950  1.00140.17           N  
ANISOU 3693  NE  ARG A 313    18577  18697  15987    846  -1271  -1026       N  
ATOM   3694  CZ  ARG A 313      19.630  14.128 -24.460  1.00141.71           C  
ANISOU 3694  CZ  ARG A 313    18705  18943  16194    908  -1223  -1076       C  
ATOM   3695  NH1 ARG A 313      20.615  13.457 -25.046  1.00142.73           N  
ANISOU 3695  NH1 ARG A 313    18828  19073  16328    989  -1290  -1147       N  
ATOM   3696  NH2 ARG A 313      19.694  15.452 -24.382  1.00136.35           N  
ANISOU 3696  NH2 ARG A 313    17965  18318  15522    887  -1111  -1062       N  
ATOM   3697  N   LEU A 314      14.624   9.221 -22.797  1.00117.64           N  
ANISOU 3697  N   LEU A 314    16065  15607  13025    584  -1597   -870       N  
ATOM   3698  CA  LEU A 314      14.687   7.907 -22.161  1.00108.95           C  
ANISOU 3698  CA  LEU A 314    15082  14417  11896    542  -1743   -855       C  
ATOM   3699  C   LEU A 314      14.189   6.803 -23.086  1.00 98.54           C  
ANISOU 3699  C   LEU A 314    13811  13053  10576    573  -1829   -859       C  
ATOM   3700  O   LEU A 314      14.719   5.685 -23.057  1.00102.59           O  
ANISOU 3700  O   LEU A 314    14404  13486  11092    607  -1970   -877       O  
ATOM   3701  CB  LEU A 314      13.886   7.902 -20.856  1.00104.87           C  
ANISOU 3701  CB  LEU A 314    14625  13893  11329    389  -1736   -798       C  
ATOM   3702  CG  LEU A 314      14.366   8.746 -19.673  1.00 98.51           C  
ANISOU 3702  CG  LEU A 314    13797  13118  10515    336  -1680   -790       C  
ATOM   3703  CD1 LEU A 314      13.656   8.304 -18.400  1.00101.69           C  
ANISOU 3703  CD1 LEU A 314    14288  13497  10854    176  -1719   -739       C  
ATOM   3704  CD2 LEU A 314      15.880   8.677 -19.504  1.00 97.84           C  
ANISOU 3704  CD2 LEU A 314    13715  13000  10460    431  -1741   -831       C  
ATOM   3705  N   GLY A 315      13.186   7.092 -23.919  1.00 88.05           N  
ANISOU 3705  N   GLY A 315    12436  11771   9247    565  -1754   -848       N  
ATOM   3706  CA  GLY A 315      12.702   6.065 -24.830  1.00 90.48           C  
ANISOU 3706  CA  GLY A 315    12784  12040   9553    596  -1830   -854       C  
ATOM   3707  C   GLY A 315      13.666   5.757 -25.964  1.00 92.93           C  
ANISOU 3707  C   GLY A 315    13057  12348   9905    737  -1874   -920       C  
ATOM   3708  O   GLY A 315      13.834   4.592 -26.351  1.00 94.82           O  
ANISOU 3708  O   GLY A 315    13355  12521  10150    778  -1998   -943       O  
ATOM   3709  N   PHE A 316      14.350   6.784 -26.480  1.00 96.04           N  
ANISOU 3709  N   PHE A 316    13351  12813  10327    809  -1779   -957       N  
ATOM   3710  CA  PHE A 316      15.361   6.550 -27.506  1.00100.99           C  
ANISOU 3710  CA  PHE A 316    13932  13455  10985    932  -1813  -1032       C  
ATOM   3711  C   PHE A 316      16.574   5.820 -26.951  1.00109.49           C  
ANISOU 3711  C   PHE A 316    15053  14471  12079    983  -1937  -1084       C  
ATOM   3712  O   PHE A 316      17.160   4.979 -27.643  1.00118.34           O  
ANISOU 3712  O   PHE A 316    16177  15564  13222   1070  -2033  -1151       O  
ATOM   3713  CB  PHE A 316      15.806   7.871 -28.139  1.00100.11           C  
ANISOU 3713  CB  PHE A 316    13710  13441  10888    976  -1680  -1056       C  
ATOM   3714  CG  PHE A 316      14.927   8.348 -29.256  1.00100.94           C  
ANISOU 3714  CG  PHE A 316    13764  13601  10988    978  -1597  -1038       C  
ATOM   3715  CD1 PHE A 316      15.134   7.895 -30.552  1.00103.95           C  
ANISOU 3715  CD1 PHE A 316    14116  14005  11377   1055  -1623  -1087       C  
ATOM   3716  CD2 PHE A 316      13.913   9.257 -29.022  1.00101.46           C  
ANISOU 3716  CD2 PHE A 316    13807  13698  11044    907  -1498   -979       C  
ATOM   3717  CE1 PHE A 316      14.340   8.335 -31.596  1.00105.14           C  
ANISOU 3717  CE1 PHE A 316    14224  14205  11520   1055  -1553  -1068       C  
ATOM   3718  CE2 PHE A 316      13.111   9.700 -30.057  1.00104.46           C  
ANISOU 3718  CE2 PHE A 316    14144  14122  11424    914  -1434   -965       C  
ATOM   3719  CZ  PHE A 316      13.325   9.236 -31.350  1.00105.78           C  
ANISOU 3719  CZ  PHE A 316    14290  14307  11593    987  -1462  -1004       C  
ATOM   3720  N   LYS A 317      16.966   6.110 -25.708  1.00111.67           N  
ANISOU 3720  N   LYS A 317    15360  14723  12345    933  -1943  -1061       N  
ATOM   3721  CA  LYS A 317      18.047   5.322 -25.126  1.00114.19           C  
ANISOU 3721  CA  LYS A 317    15734  14970  12682    980  -2082  -1109       C  
ATOM   3722  C   LYS A 317      17.596   3.900 -24.791  1.00124.12           C  
ANISOU 3722  C   LYS A 317    17120  16115  13927    944  -2245  -1084       C  
ATOM   3723  O   LYS A 317      18.421   2.979 -24.793  1.00119.43           O  
ANISOU 3723  O   LYS A 317    16570  15449  13360   1017  -2392  -1143       O  
ATOM   3724  CB  LYS A 317      18.624   6.038 -23.905  1.00115.76           C  
ANISOU 3724  CB  LYS A 317    15933  15177  12874    936  -2046  -1092       C  
ATOM   3725  CG  LYS A 317      19.069   7.483 -24.178  1.00116.91           C  
ANISOU 3725  CG  LYS A 317    15959  15430  13031    963  -1886  -1113       C  
ATOM   3726  CD  LYS A 317      20.335   7.583 -25.032  1.00119.88           C  
ANISOU 3726  CD  LYS A 317    16255  15851  13442   1088  -1892  -1217       C  
ATOM   3727  CE  LYS A 317      20.308   8.851 -25.894  1.00118.95           C  
ANISOU 3727  CE  LYS A 317    16026  15844  13324   1103  -1730  -1224       C  
ATOM   3728  NZ  LYS A 317      21.646   9.481 -26.111  1.00119.06           N  
ANISOU 3728  NZ  LYS A 317    15958  15925  13355   1172  -1688  -1307       N  
ATOM   3729  N   HIS A 318      16.300   3.690 -24.522  1.00143.16           N  
ANISOU 3729  N   HIS A 318    19591  18507  16298    833  -2229  -1003       N  
ATOM   3730  CA  HIS A 318      15.820   2.327 -24.292  1.00150.81           C  
ANISOU 3730  CA  HIS A 318    20685  19368  17246    789  -2385   -976       C  
ATOM   3731  C   HIS A 318      15.851   1.506 -25.577  1.00144.41           C  
ANISOU 3731  C   HIS A 318    19862  18538  16468    889  -2456  -1034       C  
ATOM   3732  O   HIS A 318      16.249   0.334 -25.556  1.00150.77           O  
ANISOU 3732  O   HIS A 318    20751  19245  17292    929  -2626  -1065       O  
ATOM   3733  CB  HIS A 318      14.407   2.350 -23.698  1.00164.15           C  
ANISOU 3733  CB  HIS A 318    22433  21060  18876    632  -2338   -884       C  
ATOM   3734  CG  HIS A 318      13.912   1.010 -23.227  1.00177.19           C  
ANISOU 3734  CG  HIS A 318    24232  22600  20492    553  -2497   -842       C  
ATOM   3735  ND1 HIS A 318      14.221  -0.174 -23.863  1.00180.37           N  
ANISOU 3735  ND1 HIS A 318    24693  22917  20923    631  -2649   -882       N  
ATOM   3736  CD2 HIS A 318      13.119   0.673 -22.180  1.00183.73           C  
ANISOU 3736  CD2 HIS A 318    25163  23390  21254    393  -2530   -766       C  
ATOM   3737  CE1 HIS A 318      13.645  -1.180 -23.229  1.00182.63           C  
ANISOU 3737  CE1 HIS A 318    25120  23108  21165    525  -2774   -825       C  
ATOM   3738  NE2 HIS A 318      12.969  -0.693 -22.205  1.00186.76           N  
ANISOU 3738  NE2 HIS A 318    25674  23662  21625    373  -2702   -753       N  
ATOM   3739  N   ALA A 319      15.445   2.098 -26.705  1.00129.75           N  
ANISOU 3739  N   ALA A 319    17906  16771  14622    931  -2336  -1051       N  
ATOM   3740  CA  ALA A 319      15.431   1.330 -27.949  1.00114.96           C  
ANISOU 3740  CA  ALA A 319    16016  14888  12775   1020  -2397  -1108       C  
ATOM   3741  C   ALA A 319      16.842   0.982 -28.410  1.00118.99           C  
ANISOU 3741  C   ALA A 319    16483  15391  13336   1156  -2481  -1220       C  
ATOM   3742  O   ALA A 319      17.109  -0.158 -28.813  1.00112.79           O  
ANISOU 3742  O   ALA A 319    15743  14535  12578   1219  -2627  -1275       O  
ATOM   3743  CB  ALA A 319      14.699   2.105 -29.041  1.00107.36           C  
ANISOU 3743  CB  ALA A 319    14958  14029  11807   1028  -2249  -1100       C  
ATOM   3744  N   PHE A 320      17.758   1.939 -28.328  1.00129.03           N  
ANISOU 3744  N   PHE A 320    17668  16735  14622   1200  -2397  -1263       N  
ATOM   3745  CA  PHE A 320      19.109   1.770 -28.845  1.00131.79           C  
ANISOU 3745  CA  PHE A 320    17951  17107  15015   1327  -2452  -1386       C  
ATOM   3746  C   PHE A 320      20.005   1.131 -27.784  1.00136.29           C  
ANISOU 3746  C   PHE A 320    18596  17580  15608   1348  -2603  -1418       C  
ATOM   3747  O   PHE A 320      21.175   1.485 -27.640  1.00140.19           O  
ANISOU 3747  O   PHE A 320    19030  18107  16129   1418  -2605  -1499       O  
ATOM   3748  CB  PHE A 320      19.683   3.121 -29.299  1.00129.79           C  
ANISOU 3748  CB  PHE A 320    17569  16985  14761   1355  -2287  -1421       C  
ATOM   3749  CG  PHE A 320      19.085   3.650 -30.586  1.00132.31           C  
ANISOU 3749  CG  PHE A 320    17807  17398  15065   1362  -2167  -1418       C  
ATOM   3750  CD1 PHE A 320      17.721   3.563 -30.835  1.00131.66           C  
ANISOU 3750  CD1 PHE A 320    17764  17303  14958   1293  -2131  -1332       C  
ATOM   3751  CD2 PHE A 320      19.891   4.258 -31.538  1.00132.45           C  
ANISOU 3751  CD2 PHE A 320    17712  17523  15090   1431  -2091  -1503       C  
ATOM   3752  CE1 PHE A 320      17.178   4.053 -32.015  1.00127.67           C  
ANISOU 3752  CE1 PHE A 320    17189  16879  14439   1302  -2030  -1330       C  
ATOM   3753  CE2 PHE A 320      19.353   4.754 -32.721  1.00126.83           C  
ANISOU 3753  CE2 PHE A 320    16936  16896  14358   1429  -1989  -1495       C  
ATOM   3754  CZ  PHE A 320      17.996   4.649 -32.959  1.00125.05           C  
ANISOU 3754  CZ  PHE A 320    16754  16647  14113   1368  -1962  -1407       C  
TER    3755      PHE A 320                                                      
HETATM 3756  C10 GBK A1501       4.628  18.565 -57.102  1.00 77.01           C  
HETATM 3757  C13 GBK A1501       2.999  20.442 -56.777  1.00 84.25           C  
HETATM 3758  C17 GBK A1501       2.350  21.295 -55.683  1.00 90.87           C  
HETATM 3759  C20 GBK A1501       1.196  22.845 -53.697  1.00 86.33           C  
HETATM 3760  C21 GBK A1501       0.494  21.779 -54.237  1.00 88.10           C  
HETATM 3761  C22 GBK A1501       1.071  21.002 -55.229  1.00 93.75           C  
HETATM 3762  C01 GBK A1501       6.742  16.805 -51.986  1.00 89.59           C  
HETATM 3763  C02 GBK A1501       4.629  17.730 -52.444  1.00 90.76           C  
HETATM 3764  C03 GBK A1501       4.626  18.251 -51.162  1.00 98.60           C  
HETATM 3765  C04 GBK A1501       3.570  19.041 -50.735  1.00100.74           C  
HETATM 3766  C05 GBK A1501       2.509  19.311 -51.584  1.00 98.55           C  
HETATM 3767  C06 GBK A1501       2.516  18.788 -52.864  1.00 98.02           C  
HETATM 3768  C07 GBK A1501       3.570  17.997 -53.289  1.00 92.26           C  
HETATM 3769  C08 GBK A1501       3.550  17.436 -54.700  1.00 87.66           C  
HETATM 3770  C09 GBK A1501       3.782  19.332 -56.097  1.00 85.89           C  
HETATM 3771  C11 GBK A1501       4.062  18.686 -58.518  1.00 75.89           C  
HETATM 3772  C12 GBK A1501       2.518  18.828 -58.536  1.00 72.21           C  
HETATM 3773  N14 GBK A1501       2.833  18.409 -55.487  1.00 88.24           N  
HETATM 3774  N15 GBK A1501       1.981  19.864 -57.643  1.00 68.88           N  
HETATM 3775  O16 GBK A1501       5.686  16.932 -52.892  1.00 86.66           O  
HETATM 3776  C18 GBK A1501       3.052  22.360 -55.140  1.00 89.56           C  
HETATM 3777  C19 GBK A1501       2.475  23.135 -54.148  1.00 89.79           C  
CONECT  639 1234                                                                
CONECT 1234  639                                                                
CONECT 3756 3770 3771                                                           
CONECT 3757 3758 3770 3774                                                      
CONECT 3758 3757 3761 3776                                                      
CONECT 3759 3760 3777                                                           
CONECT 3760 3759 3761                                                           
CONECT 3761 3758 3760                                                           
CONECT 3762 3775                                                                
CONECT 3763 3764 3768 3775                                                      
CONECT 3764 3763 3765                                                           
CONECT 3765 3764 3766                                                           
CONECT 3766 3765 3767                                                           
CONECT 3767 3766 3768                                                           
CONECT 3768 3763 3767 3769                                                      
CONECT 3769 3768 3773                                                           
CONECT 3770 3756 3757 3773                                                      
CONECT 3771 3756 3772                                                           
CONECT 3772 3771 3774                                                           
CONECT 3773 3769 3770                                                           
CONECT 3774 3757 3772                                                           
CONECT 3775 3762 3763                                                           
CONECT 3776 3758 3777                                                           
CONECT 3777 3759 3776                                                           
MASTER      353    0    1   20    8    0    2    6 3776    1   24   40          
END