HEADER    SIGNALING PROTEIN                       24-JUN-13   4BV0              
TITLE     HIGH RESOLUTION STRUCTURE OF EVOLVED AGONIST-BOUND NEUROTENSIN        
TITLE    2 RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROTENSIN RECEPTOR TYPE 1;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 50-390;                                           
COMPND   5 SYNONYM: NEUROTENSIN RECEPTOR 1 TM86VDIC3B, NT-R-1, NTR1, HIGH-      
COMPND   6 AFFINITY LEVOCABASTINE-INSENSITIVE NEUROTENSIN RECEPTOR, NTRH;       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: THERMOSTABLE MUTANT WITH INTRACELLULAR LOOP 3 DELETION
COMPND  10 B (T279-I295);                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: NEUROTENSIN/NEUROMEDIN N;                                  
COMPND  13 CHAIN: C, D;                                                         
COMPND  14 FRAGMENT: C-TERMINUS, RESIDUES 157-162;                              
COMPND  15 SYNONYM: LARGE NEUROMEDIN N, NMN-125, NEUROMEDIN N, NN, NMN,         
COMPND  16 NEUROTENSIN, NT, TAIL PEPTIDE;                                       
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 OTHER_DETAILS: THE SEQUENCE RRPYIL CORRESPONDS TO RESIDUES 8-13 OF   
COMPND  19 THE NEUROTENSIN C-TERMINUS. THE FULL CRYSTALLIZED CONSTRUCT WAS      
COMPND  20 GPGGRRPYIL (THE N-TERMINAL GPGG IS AN ARTIFICIAL LINKER).            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: TUNER;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PEP-TM86VDIC3III;                         
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  13 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  14 ORGANISM_TAXID: 10116;                                               
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    SIGNALING PROTEIN, G PROTEIN COUPLED RECEPTOR, MEMBRANE PROTEIN       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.EGLOFF,M.HILLENBRAND,D.J.SCOTT,K.M.SCHLINKMANN,P.HEINE,S.BALADA,    
AUTHOR   2 A.BATYUK,P.MITTL,M.SCHUETZ,A.PLUECKTHUN                              
REVDAT   4   20-JUN-18 4BV0    1       JRNL   REMARK                            
REVDAT   3   26-FEB-14 4BV0    1       JRNL                                     
REVDAT   2   05-FEB-14 4BV0    1       JRNL                                     
REVDAT   1   29-JAN-14 4BV0    0                                                
JRNL        AUTH   P.EGLOFF,M.HILLENBRAND,C.KLENK,A.BATYUK,P.HEINE,S.BALADA,    
JRNL        AUTH 2 K.M.SCHLINKMANN,D.J.SCOTT,M.SCHUETZ,A.PLUECKTHUN             
JRNL        TITL   STRUCTURE OF SIGNALING-COMPETENT NEUROTENSIN RECEPTOR 1      
JRNL        TITL 2 OBTAINED BY DIRECTED EVOLUTION IN ESCHERICHIA COLI           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111  E655 2014              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24453215                                                     
JRNL        DOI    10.1073/PNAS.1317903111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 20680                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.284                           
REMARK   3   FREE R VALUE                     : 0.311                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1036                            
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 19.8765 -  5.8862    1.00     3108   164  0.2375 0.2655        
REMARK   3     2  5.8862 -  4.6923    1.00     2967   156  0.2628 0.2864        
REMARK   3     3  4.6923 -  4.1051    1.00     2934   155  0.2395 0.2904        
REMARK   3     4  4.1051 -  3.7325    0.99     2899   151  0.3379 0.3458        
REMARK   3     5  3.7325 -  3.4665    0.86     2512   133  0.4268 0.4762        
REMARK   3     6  3.4665 -  3.2630    0.92     2635   140  0.4534 0.4471        
REMARK   3     7  3.2630 -  3.1002    0.89     2589   137  0.4485 0.4484        
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)     : 0.770            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 45.010           
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      :  0.003           4985                                  
REMARK   3   ANGLE     :  0.651           6794                                  
REMARK   3   CHIRALITY :  0.046            821                                  
REMARK   3   PLANARITY :  0.003            818                                  
REMARK   3   DIHEDRAL  : 10.105           1725                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: PHENIX AND REFMAC WERE USED               
REMARK   4                                                                      
REMARK   4 4BV0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290057425.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21665                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.510                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3ZEV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% (V/V) PEG600, 0.5 M NACL, 50 MM    
REMARK 280  GLYCINE PH 9.4                                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       30.29000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      104.29000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.78000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      104.29000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.29000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.78000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.1 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.1 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    46                                                      
REMARK 465     PRO A    47                                                      
REMARK 465     GLY A    48                                                      
REMARK 465     SER A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     PRO A    51                                                      
REMARK 465     LYS A    93                                                      
REMARK 465     SER A    94                                                      
REMARK 465     LEU A    95                                                      
REMARK 465     GLN A    96                                                      
REMARK 465     SER A    97                                                      
REMARK 465     LEU A    98                                                      
REMARK 465     GLN A    99                                                      
REMARK 465     PHE A   175                                                      
REMARK 465     LYS A   176                                                      
REMARK 465     HIS A   177                                                      
REMARK 465     LYS A   178                                                      
REMARK 465     THR A   179                                                      
REMARK 465     GLN A   270                                                      
REMARK 465     ALA A   271                                                      
REMARK 465     ALA A   272                                                      
REMARK 465     GLU A   273                                                      
REMARK 465     GLN A   274                                                      
REMARK 465     GLY A   275                                                      
REMARK 465     ARG A   276                                                      
REMARK 465     VAL A   277                                                      
REMARK 465     CYS A   278                                                      
REMARK 465     THR A   279                                                      
REMARK 465     GLU A   280                                                      
REMARK 465     CYS A   388                                                      
REMARK 465     PRO A   389                                                      
REMARK 465     GLY A   390                                                      
REMARK 465     THR A   391                                                      
REMARK 465     ARG A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     LEU A   394                                                      
REMARK 465     GLU A   395                                                      
REMARK 465     VAL A   396                                                      
REMARK 465     LEU A   397                                                      
REMARK 465     PHE A   398                                                      
REMARK 465     GLN A   399                                                      
REMARK 465     GLY B    46                                                      
REMARK 465     PRO B    47                                                      
REMARK 465     GLY B    48                                                      
REMARK 465     SER B    49                                                      
REMARK 465     GLY B    50                                                      
REMARK 465     LYS B    92                                                      
REMARK 465     LYS B    93                                                      
REMARK 465     SER B    94                                                      
REMARK 465     LEU B    95                                                      
REMARK 465     GLN B    96                                                      
REMARK 465     SER B    97                                                      
REMARK 465     LEU B   180                                                      
REMARK 465     HIS B   269                                                      
REMARK 465     GLN B   270                                                      
REMARK 465     ALA B   271                                                      
REMARK 465     ALA B   272                                                      
REMARK 465     GLU B   273                                                      
REMARK 465     GLN B   274                                                      
REMARK 465     GLY B   275                                                      
REMARK 465     ARG B   276                                                      
REMARK 465     VAL B   277                                                      
REMARK 465     CYS B   278                                                      
REMARK 465     THR B   279                                                      
REMARK 465     GLU B   280                                                      
REMARK 465     PRO B   281                                                      
REMARK 465     GLY B   282                                                      
REMARK 465     GLY B   390                                                      
REMARK 465     THR B   391                                                      
REMARK 465     ARG B   392                                                      
REMARK 465     GLU B   393                                                      
REMARK 465     LEU B   394                                                      
REMARK 465     GLU B   395                                                      
REMARK 465     VAL B   396                                                      
REMARK 465     LEU B   397                                                      
REMARK 465     PHE B   398                                                      
REMARK 465     GLN B   399                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     GLY D     4                                                      
REMARK 465     PRO D     5                                                      
REMARK 465     GLY D     6                                                      
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  58       53.99   -116.94                                   
REMARK 500    ALA A 136       52.81   -118.26                                   
REMARK 500    PHE A 137       -3.81   -143.68                                   
REMARK 500    MET A 181       75.43     53.93                                   
REMARK 500    PHE A 246      -78.91   -131.63                                   
REMARK 500    SER B  53     -172.77    -65.32                                   
REMARK 500    ILE B 129      -49.67   -137.14                                   
REMARK 500    LEU B 213       48.68   -103.05                                   
REMARK 500    PHE B 246      -77.25   -130.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ZEV   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THERMOSTABLE AGONIST-BOUND NEUROTENSIN RECEPTOR 1       
REMARK 900 MUTANT WITHOUT LYSOZYME FUSION                                       
REMARK 900 RELATED ID: 4BV0   RELATED DB: PDB                                   
REMARK 900 HIGH RESOLUTION STRUCTURE OF EVOLVED AGONIST-BOUND NEUROTENSIN       
REMARK 900 RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION                            
REMARK 900 RELATED ID: 4BWB   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF EVOLVED AGONIST-BOUND NEUROTENSIN RECEPTOR 1 MUTANT     
REMARK 900 WITHOUT LYSOZYME FUSION                                              
DBREF  4BV0 A   50   390  UNP    P20789   NTR1_RAT        50    390             
DBREF  4BV0 B   50   390  UNP    P20789   NTR1_RAT        50    390             
DBREF  4BV0 C    8    13  UNP    P20068   NEUT_RAT       157    162             
DBREF  4BV0 D    8    13  UNP    P20068   NEUT_RAT       157    162             
SEQADV 4BV0 GLY A   46  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 PRO A   47  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 GLY A   48  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 SER A   49  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 GLY A   83  UNP  P20789    SER    83 ENGINEERED MUTATION            
SEQADV 4BV0 LEU A   86  UNP  P20789    ALA    86 ENGINEERED MUTATION            
SEQADV 4BV0 ARG A  101  UNP  P20789    THR   101 ENGINEERED MUTATION            
SEQADV 4BV0 ASP A  103  UNP  P20789    HIS   103 ENGINEERED MUTATION            
SEQADV 4BV0 TYR A  105  UNP  P20789    HIS   105 ENGINEERED MUTATION            
SEQADV 4BV0 PHE A  119  UNP  P20789    LEU   119 ENGINEERED MUTATION            
SEQADV 4BV0 LEU A  121  UNP  P20789    MET   121 ENGINEERED MUTATION            
SEQADV 4BV0 ASP A  124  UNP  P20789    GLU   124 ENGINEERED MUTATION            
SEQADV 4BV0 VAL A  125  UNP  P20789    LEU   125 ENGINEERED MUTATION            
SEQADV 4BV0 LYS A  143  UNP  P20789    ARG   143 ENGINEERED MUTATION            
SEQADV 4BV0 GLU A  150  UNP  P20789    ASP   150 ENGINEERED MUTATION            
SEQADV 4BV0 VAL A  161  UNP  P20789    ALA   161 ENGINEERED MUTATION            
SEQADV 4BV0 LEU A  167  UNP  P20789    ARG   167 ENGINEERED MUTATION            
SEQADV 4BV0 ARG A  172  UNP  P20789    CYS   172 ENGINEERED MUTATION            
SEQADV 4BV0 HIS A  177  UNP  P20789    ALA   177 ENGINEERED MUTATION            
SEQADV 4BV0 VAL A  208  UNP  P20789    MET   208 ENGINEERED MUTATION            
SEQADV 4BV0 LEU A  213  UNP  P20789    ARG   213 ENGINEERED MUTATION            
SEQADV 4BV0 LEU A  234  UNP  P20789    VAL   234 ENGINEERED MUTATION            
SEQADV 4BV0 LEU A  240  UNP  P20789    VAL   240 ENGINEERED MUTATION            
SEQADV 4BV0 ALA A  253  UNP  P20789    ILE   253 ENGINEERED MUTATION            
SEQADV 4BV0 ARG A  262  UNP  P20789    ASN   262 ENGINEERED MUTATION            
SEQADV 4BV0 ARG A  263  UNP  P20789    LYS   263 ENGINEERED MUTATION            
SEQADV 4BV0     A       UNP  P20789    VAL   280 DELETION                       
SEQADV 4BV0     A       UNP  P20789    GLY   281 DELETION                       
SEQADV 4BV0     A       UNP  P20789    THR   282 DELETION                       
SEQADV 4BV0     A       UNP  P20789    HIS   283 DELETION                       
SEQADV 4BV0     A       UNP  P20789    ASN   284 DELETION                       
SEQADV 4BV0     A       UNP  P20789    GLY   285 DELETION                       
SEQADV 4BV0     A       UNP  P20789    LEU   286 DELETION                       
SEQADV 4BV0     A       UNP  P20789    GLU   287 DELETION                       
SEQADV 4BV0     A       UNP  P20789    HIS   288 DELETION                       
SEQADV 4BV0     A       UNP  P20789    SER   289 DELETION                       
SEQADV 4BV0     A       UNP  P20789    THR   290 DELETION                       
SEQADV 4BV0     A       UNP  P20789    PHE   291 DELETION                       
SEQADV 4BV0     A       UNP  P20789    ASN   292 DELETION                       
SEQADV 4BV0     A       UNP  P20789    MET   293 DELETION                       
SEQADV 4BV0     A       UNP  P20789    THR   294 DELETION                       
SEQADV 4BV0     A       UNP  P20789    ILE   295 DELETION                       
SEQADV 4BV0 ARG A  305  UNP  P20789    HIS   305 ENGINEERED MUTATION            
SEQADV 4BV0 MET A  313  UNP  P20789    VAL   313 ENGINEERED MUTATION            
SEQADV 4BV0 VAL A  332  UNP  P20789    CYS   332 ENGINEERED MUTATION            
SEQADV 4BV0 ALA A  342  UNP  P20789    PHE   342 ENGINEERED MUTATION            
SEQADV 4BV0 SER A  354  UNP  P20789    THR   354 ENGINEERED MUTATION            
SEQADV 4BV0 VAL A  358  UNP  P20789    PHE   358 ENGINEERED MUTATION            
SEQADV 4BV0 ALA A  362  UNP  P20789    SER   362 ENGINEERED MUTATION            
SEQADV 4BV0 THR A  391  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 ARG A  392  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 GLU A  393  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 LEU A  394  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 GLU A  395  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 VAL A  396  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 LEU A  397  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 PHE A  398  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 GLN A  399  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 GLY B   46  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 PRO B   47  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 GLY B   48  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 SER B   49  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 GLY B   83  UNP  P20789    SER    83 ENGINEERED MUTATION            
SEQADV 4BV0 LEU B   86  UNP  P20789    ALA    86 ENGINEERED MUTATION            
SEQADV 4BV0 ARG B  101  UNP  P20789    THR   101 ENGINEERED MUTATION            
SEQADV 4BV0 ASP B  103  UNP  P20789    HIS   103 ENGINEERED MUTATION            
SEQADV 4BV0 TYR B  105  UNP  P20789    HIS   105 ENGINEERED MUTATION            
SEQADV 4BV0 PHE B  119  UNP  P20789    LEU   119 ENGINEERED MUTATION            
SEQADV 4BV0 LEU B  121  UNP  P20789    MET   121 ENGINEERED MUTATION            
SEQADV 4BV0 ASP B  124  UNP  P20789    GLU   124 ENGINEERED MUTATION            
SEQADV 4BV0 VAL B  125  UNP  P20789    LEU   125 ENGINEERED MUTATION            
SEQADV 4BV0 LYS B  143  UNP  P20789    ARG   143 ENGINEERED MUTATION            
SEQADV 4BV0 GLU B  150  UNP  P20789    ASP   150 ENGINEERED MUTATION            
SEQADV 4BV0 VAL B  161  UNP  P20789    ALA   161 ENGINEERED MUTATION            
SEQADV 4BV0 LEU B  167  UNP  P20789    ARG   167 ENGINEERED MUTATION            
SEQADV 4BV0 ARG B  172  UNP  P20789    CYS   172 ENGINEERED MUTATION            
SEQADV 4BV0 HIS B  177  UNP  P20789    ALA   177 ENGINEERED MUTATION            
SEQADV 4BV0 VAL B  208  UNP  P20789    MET   208 ENGINEERED MUTATION            
SEQADV 4BV0 LEU B  213  UNP  P20789    ARG   213 ENGINEERED MUTATION            
SEQADV 4BV0 LEU B  234  UNP  P20789    VAL   234 ENGINEERED MUTATION            
SEQADV 4BV0 LEU B  240  UNP  P20789    VAL   240 ENGINEERED MUTATION            
SEQADV 4BV0 ALA B  253  UNP  P20789    ILE   253 ENGINEERED MUTATION            
SEQADV 4BV0 ARG B  262  UNP  P20789    ASN   262 ENGINEERED MUTATION            
SEQADV 4BV0 ARG B  263  UNP  P20789    LYS   263 ENGINEERED MUTATION            
SEQADV 4BV0     B       UNP  P20789    VAL   280 DELETION                       
SEQADV 4BV0     B       UNP  P20789    GLY   281 DELETION                       
SEQADV 4BV0     B       UNP  P20789    THR   282 DELETION                       
SEQADV 4BV0     B       UNP  P20789    HIS   283 DELETION                       
SEQADV 4BV0     B       UNP  P20789    ASN   284 DELETION                       
SEQADV 4BV0     B       UNP  P20789    GLY   285 DELETION                       
SEQADV 4BV0     B       UNP  P20789    LEU   286 DELETION                       
SEQADV 4BV0     B       UNP  P20789    GLU   287 DELETION                       
SEQADV 4BV0     B       UNP  P20789    HIS   288 DELETION                       
SEQADV 4BV0     B       UNP  P20789    SER   289 DELETION                       
SEQADV 4BV0     B       UNP  P20789    THR   290 DELETION                       
SEQADV 4BV0     B       UNP  P20789    PHE   291 DELETION                       
SEQADV 4BV0     B       UNP  P20789    ASN   292 DELETION                       
SEQADV 4BV0     B       UNP  P20789    MET   293 DELETION                       
SEQADV 4BV0     B       UNP  P20789    THR   294 DELETION                       
SEQADV 4BV0     B       UNP  P20789    ILE   295 DELETION                       
SEQADV 4BV0 ARG B  305  UNP  P20789    HIS   305 ENGINEERED MUTATION            
SEQADV 4BV0 MET B  313  UNP  P20789    VAL   313 ENGINEERED MUTATION            
SEQADV 4BV0 VAL B  332  UNP  P20789    CYS   332 ENGINEERED MUTATION            
SEQADV 4BV0 ALA B  342  UNP  P20789    PHE   342 ENGINEERED MUTATION            
SEQADV 4BV0 SER B  354  UNP  P20789    THR   354 ENGINEERED MUTATION            
SEQADV 4BV0 VAL B  358  UNP  P20789    PHE   358 ENGINEERED MUTATION            
SEQADV 4BV0 ALA B  362  UNP  P20789    SER   362 ENGINEERED MUTATION            
SEQADV 4BV0 THR B  391  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 ARG B  392  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 GLU B  393  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 LEU B  394  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 GLU B  395  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 VAL B  396  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 LEU B  397  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 PHE B  398  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 GLN B  399  UNP  P20789              EXPRESSION TAG                 
SEQADV 4BV0 GLY C    4  UNP  P20068              EXPRESSION TAG                 
SEQADV 4BV0 PRO C    5  UNP  P20068              EXPRESSION TAG                 
SEQADV 4BV0 GLY C    6  UNP  P20068              EXPRESSION TAG                 
SEQADV 4BV0 GLY C    7  UNP  P20068              EXPRESSION TAG                 
SEQADV 4BV0 GLY D    4  UNP  P20068              EXPRESSION TAG                 
SEQADV 4BV0 PRO D    5  UNP  P20068              EXPRESSION TAG                 
SEQADV 4BV0 GLY D    6  UNP  P20068              EXPRESSION TAG                 
SEQADV 4BV0 GLY D    7  UNP  P20068              EXPRESSION TAG                 
SEQRES   1 A  338  GLY PRO GLY SER GLY PRO ASN SER ASP LEU ASP VAL ASN          
SEQRES   2 A  338  THR ASP ILE TYR SER LYS VAL LEU VAL THR ALA ILE TYR          
SEQRES   3 A  338  LEU ALA LEU PHE VAL VAL GLY THR VAL GLY ASN GLY VAL          
SEQRES   4 A  338  THR LEU PHE THR LEU ALA ARG LYS LYS SER LEU GLN SER          
SEQRES   5 A  338  LEU GLN SER ARG VAL ASP TYR TYR LEU GLY SER LEU ALA          
SEQRES   6 A  338  LEU SER ASP LEU LEU ILE LEU LEU PHE ALA LEU PRO VAL          
SEQRES   7 A  338  ASP VAL TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA          
SEQRES   8 A  338  PHE GLY ASP ALA GLY CYS LYS GLY TYR TYR PHE LEU ARG          
SEQRES   9 A  338  GLU ALA CYS THR TYR ALA THR ALA LEU ASN VAL VAL SER          
SEQRES  10 A  338  LEU SER VAL GLU LEU TYR LEU ALA ILE ARG HIS PRO PHE          
SEQRES  11 A  338  LYS HIS LYS THR LEU MET SER ARG SER ARG THR LYS LYS          
SEQRES  12 A  338  PHE ILE SER ALA ILE TRP LEU ALA SER ALA LEU LEU ALA          
SEQRES  13 A  338  ILE PRO MET LEU PHE THR VAL GLY LEU GLN ASN LEU SER          
SEQRES  14 A  338  GLY ASP GLY THR HIS PRO GLY GLY LEU VAL CYS THR PRO          
SEQRES  15 A  338  ILE VAL ASP THR ALA THR LEU LYS VAL VAL ILE GLN LEU          
SEQRES  16 A  338  ASN THR PHE MET SER PHE LEU PHE PRO MET LEU VAL ALA          
SEQRES  17 A  338  SER ILE LEU ASN THR VAL ILE ALA ARG ARG LEU THR VAL          
SEQRES  18 A  338  MET VAL HIS GLN ALA ALA GLU GLN GLY ARG VAL CYS THR          
SEQRES  19 A  338  GLU PRO GLY ARG VAL GLN ALA LEU ARG ARG GLY VAL LEU          
SEQRES  20 A  338  VAL LEU ARG ALA MET VAL ILE ALA PHE VAL VAL CYS TRP          
SEQRES  21 A  338  LEU PRO TYR HIS VAL ARG ARG LEU MET PHE VAL TYR ILE          
SEQRES  22 A  338  SER ASP GLU GLN TRP THR THR ALA LEU PHE ASP PHE TYR          
SEQRES  23 A  338  HIS TYR PHE TYR MET LEU SER ASN ALA LEU VAL TYR VAL          
SEQRES  24 A  338  SER ALA ALA ILE ASN PRO ILE LEU TYR ASN LEU VAL SER          
SEQRES  25 A  338  ALA ASN PHE ARG GLN VAL PHE LEU SER THR LEU ALA CYS          
SEQRES  26 A  338  LEU CYS PRO GLY THR ARG GLU LEU GLU VAL LEU PHE GLN          
SEQRES   1 B  338  GLY PRO GLY SER GLY PRO ASN SER ASP LEU ASP VAL ASN          
SEQRES   2 B  338  THR ASP ILE TYR SER LYS VAL LEU VAL THR ALA ILE TYR          
SEQRES   3 B  338  LEU ALA LEU PHE VAL VAL GLY THR VAL GLY ASN GLY VAL          
SEQRES   4 B  338  THR LEU PHE THR LEU ALA ARG LYS LYS SER LEU GLN SER          
SEQRES   5 B  338  LEU GLN SER ARG VAL ASP TYR TYR LEU GLY SER LEU ALA          
SEQRES   6 B  338  LEU SER ASP LEU LEU ILE LEU LEU PHE ALA LEU PRO VAL          
SEQRES   7 B  338  ASP VAL TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA          
SEQRES   8 B  338  PHE GLY ASP ALA GLY CYS LYS GLY TYR TYR PHE LEU ARG          
SEQRES   9 B  338  GLU ALA CYS THR TYR ALA THR ALA LEU ASN VAL VAL SER          
SEQRES  10 B  338  LEU SER VAL GLU LEU TYR LEU ALA ILE ARG HIS PRO PHE          
SEQRES  11 B  338  LYS HIS LYS THR LEU MET SER ARG SER ARG THR LYS LYS          
SEQRES  12 B  338  PHE ILE SER ALA ILE TRP LEU ALA SER ALA LEU LEU ALA          
SEQRES  13 B  338  ILE PRO MET LEU PHE THR VAL GLY LEU GLN ASN LEU SER          
SEQRES  14 B  338  GLY ASP GLY THR HIS PRO GLY GLY LEU VAL CYS THR PRO          
SEQRES  15 B  338  ILE VAL ASP THR ALA THR LEU LYS VAL VAL ILE GLN LEU          
SEQRES  16 B  338  ASN THR PHE MET SER PHE LEU PHE PRO MET LEU VAL ALA          
SEQRES  17 B  338  SER ILE LEU ASN THR VAL ILE ALA ARG ARG LEU THR VAL          
SEQRES  18 B  338  MET VAL HIS GLN ALA ALA GLU GLN GLY ARG VAL CYS THR          
SEQRES  19 B  338  GLU PRO GLY ARG VAL GLN ALA LEU ARG ARG GLY VAL LEU          
SEQRES  20 B  338  VAL LEU ARG ALA MET VAL ILE ALA PHE VAL VAL CYS TRP          
SEQRES  21 B  338  LEU PRO TYR HIS VAL ARG ARG LEU MET PHE VAL TYR ILE          
SEQRES  22 B  338  SER ASP GLU GLN TRP THR THR ALA LEU PHE ASP PHE TYR          
SEQRES  23 B  338  HIS TYR PHE TYR MET LEU SER ASN ALA LEU VAL TYR VAL          
SEQRES  24 B  338  SER ALA ALA ILE ASN PRO ILE LEU TYR ASN LEU VAL SER          
SEQRES  25 B  338  ALA ASN PHE ARG GLN VAL PHE LEU SER THR LEU ALA CYS          
SEQRES  26 B  338  LEU CYS PRO GLY THR ARG GLU LEU GLU VAL LEU PHE GLN          
SEQRES   1 C   10  GLY PRO GLY GLY ARG ARG PRO TYR ILE LEU                      
SEQRES   1 D   10  GLY PRO GLY GLY ARG ARG PRO TYR ILE LEU                      
HELIX    1   1 ASP A   60  LYS A   92  1                                  33    
HELIX    2   2 ARG A  101  ALA A  120  1                                  20    
HELIX    3   3 ALA A  120  PHE A  128  1                                   9    
HELIX    4   4 PHE A  137  HIS A  173  1                                  37    
HELIX    5   5 SER A  182  ALA A  201  1                                  20    
HELIX    6   6 ILE A  202  PHE A  206  5                                   5    
HELIX    7   7 HIS A  219  GLY A  221  5                                   3    
HELIX    8   8 ASP A  230  PHE A  246  1                                  17    
HELIX    9   9 PHE A  246  HIS A  269  1                                  24    
HELIX   10  10 GLY A  298  ILE A  334  1                                  37    
HELIX   11  11 THR A  340  VAL A  372  1                                  33    
HELIX   12  12 ALA A  374  CYS A  386  1                                  13    
HELIX   13  13 ASP B   60  ALA B   90  1                                  31    
HELIX   14  14 LEU B   98  ASN B  127  1                                  30    
HELIX   15  15 GLY B  138  HIS B  173  1                                  36    
HELIX   16  16 SER B  182  ILE B  202  1                                  21    
HELIX   17  17 PRO B  203  THR B  207  1                                   5    
HELIX   18  18 HIS B  219  GLY B  221  5                                   3    
HELIX   19  19 ASP B  230  PHE B  246  1                                  17    
HELIX   20  20 PHE B  246  VAL B  266  1                                  21    
HELIX   21  21 ARG B  299  ILE B  334  1                                  36    
HELIX   22  22 THR B  340  VAL B  372  1                                  33    
HELIX   23  23 ALA B  374  LEU B  387  1                                  14    
SHEET    1  AA 2 VAL A 208  ASN A 212  0                                        
SHEET    2  AA 2 LEU A 223  PRO A 227 -1  O  VAL A 224   N  GLN A 211           
SHEET    1  BA 2 VAL B 208  ASN B 212  0                                        
SHEET    2  BA 2 LEU B 223  PRO B 227 -1  O  VAL B 224   N  GLN B 211           
SSBOND   1 CYS A  142    CYS A  225                          1555   1555  2.03  
SSBOND   2 CYS B  142    CYS B  225                          1555   1555  2.03  
CISPEP   1 HIS A  133    PRO A  134          0        -0.35                     
CISPEP   2 HIS B  133    PRO B  134          0         1.36                     
CRYST1   60.580   91.560  208.580  90.00  90.00  90.00 P 21 21 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      0.016507  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010922  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004794        0.00000                         
MTRIX1   1 -0.488000 -0.155000 -0.859000       -4.46500    1                    
MTRIX2   1 -0.146400 -0.955600  0.255600      -30.54000    1                    
MTRIX3   1 -0.860400  0.250500  0.443700        2.75000    1                    
ATOM      1  N   ASN A  52     -36.736 -41.270  49.553  1.00 93.50           N  
ANISOU    1  N   ASN A  52    12288   7698  15538  -1202   2582   1338       N  
ATOM      2  CA  ASN A  52     -36.547 -40.605  48.269  1.00 92.56           C  
ANISOU    2  CA  ASN A  52    11964   7807  15396  -1219   2332   1059       C  
ATOM      3  C   ASN A  52     -35.724 -41.438  47.290  1.00 93.28           C  
ANISOU    3  C   ASN A  52    12261   7678  15504  -1176   2172    838       C  
ATOM      4  O   ASN A  52     -34.623 -41.049  46.900  1.00 92.60           O  
ANISOU    4  O   ASN A  52    12226   7724  15235   -921   2030    705       O  
ATOM      5  CB  ASN A  52     -35.910 -39.227  48.468  1.00 88.62           C  
ANISOU    5  CB  ASN A  52    11331   7694  14645   -947   2253   1047       C  
ATOM      6  CG  ASN A  52     -34.710 -39.265  49.396  1.00 88.44           C  
ANISOU    6  CG  ASN A  52    11565   7648  14389   -589   2297   1166       C  
ATOM      7  OD1 ASN A  52     -34.095 -40.312  49.595  1.00 90.27           O  
ANISOU    7  OD1 ASN A  52    12081   7588  14628   -491   2323   1201       O  
ATOM      8  ND2 ASN A  52     -34.373 -38.118  49.972  1.00 87.17           N  
ANISOU    8  ND2 ASN A  52    11305   7793  14022   -389   2297   1226       N  
ATOM      9  N   SER A  53     -36.270 -42.583  46.892  1.00117.02           N  
ANISOU    9  N   SER A  53    15383  10345  18736  -1435   2208    792       N  
ATOM     10  CA  SER A  53     -35.583 -43.478  45.968  1.00117.58           C  
ANISOU   10  CA  SER A  53    15672  10159  18842  -1417   2082    573       C  
ATOM     11  C   SER A  53     -35.751 -43.031  44.518  1.00116.89           C  
ANISOU   11  C   SER A  53    15383  10256  18775  -1571   1851    269       C  
ATOM     12  O   SER A  53     -35.250 -43.677  43.598  1.00117.33           O  
ANISOU   12  O   SER A  53    15596  10135  18850  -1581   1735     47       O  
ATOM     13  CB  SER A  53     -36.084 -44.914  46.138  1.00119.80           C  
ANISOU   13  CB  SER A  53    16194   9968  19355  -1641   2218    638       C  
ATOM     14  OG  SER A  53     -37.478 -45.000  45.902  1.00121.93           O  
ANISOU   14  OG  SER A  53    16244  10225  19860  -2055   2260    638       O  
ATOM     15  N   ASP A  54     -36.458 -41.923  44.323  1.00140.30           N  
ANISOU   15  N   ASP A  54    18011  13572  21726  -1680   1787    264       N  
ATOM     16  CA  ASP A  54     -36.666 -41.368  42.992  1.00140.06           C  
ANISOU   16  CA  ASP A  54    17779  13756  21684  -1810   1557      6       C  
ATOM     17  C   ASP A  54     -35.469 -40.515  42.584  1.00138.77           C  
ANISOU   17  C   ASP A  54    17626  13847  21253  -1495   1425   -114       C  
ATOM     18  O   ASP A  54     -35.307 -40.168  41.414  1.00139.31           O  
ANISOU   18  O   ASP A  54    17618  14054  21259  -1541   1236   -345       O  
ATOM     19  CB  ASP A  54     -37.950 -40.535  42.958  1.00142.99           C  
ANISOU   19  CB  ASP A  54    17779  14390  22163  -2043   1540     65       C  
ATOM     20  CG  ASP A  54     -38.322 -40.090  41.557  1.00142.97           C  
ANISOU   20  CG  ASP A  54    17578  14579  22167  -2213   1287   -186       C  
ATOM     21  OD1 ASP A  54     -38.043 -40.841  40.599  1.00144.10           O  
ANISOU   21  OD1 ASP A  54    17877  14541  22334  -2312   1161   -408       O  
ATOM     22  OD2 ASP A  54     -38.895 -38.990  41.414  1.00141.20           O  
ANISOU   22  OD2 ASP A  54    17054  14680  21915  -2238   1214   -161       O  
ATOM     23  N   LEU A  55     -34.630 -40.185  43.560  1.00 57.81           N  
ANISOU   23  N   LEU A  55     7471   3655  10837  -1184   1526     45       N  
ATOM     24  CA  LEU A  55     -33.450 -39.362  43.316  1.00 54.29           C  
ANISOU   24  CA  LEU A  55     7025   3454  10148   -887   1422    -50       C  
ATOM     25  C   LEU A  55     -32.207 -40.216  43.091  1.00 55.01           C  
ANISOU   25  C   LEU A  55     7403   3327  10171   -670   1402   -161       C  
ATOM     26  O   LEU A  55     -31.145 -39.701  42.740  1.00 52.97           O  
ANISOU   26  O   LEU A  55     7151   3242   9732   -439   1313   -277       O  
ATOM     27  CB  LEU A  55     -33.218 -38.391  44.478  1.00 52.14           C  
ANISOU   27  CB  LEU A  55     6670   3416   9725   -672   1518    161       C  
ATOM     28  CG  LEU A  55     -33.877 -37.011  44.397  1.00 49.92           C  
ANISOU   28  CG  LEU A  55     6083   3492   9394   -737   1472    182       C  
ATOM     29  CD1 LEU A  55     -35.378 -37.118  44.175  1.00 51.69           C  
ANISOU   29  CD1 LEU A  55     6106   3695   9841  -1072   1492    213       C  
ATOM     30  CD2 LEU A  55     -33.575 -36.204  45.649  1.00 48.34           C  
ANISOU   30  CD2 LEU A  55     5864   3461   9042   -517   1592    385       C  
ATOM     31  N   ASP A  56     -32.344 -41.522  43.296  1.00 75.00           N  
ANISOU   31  N   ASP A  56    10167   5471  12858   -744   1495   -122       N  
ATOM     32  CA  ASP A  56     -31.231 -42.444  43.114  1.00 75.33           C  
ANISOU   32  CA  ASP A  56    10496   5260  12868   -528   1492   -219       C  
ATOM     33  C   ASP A  56     -30.885 -42.600  41.639  1.00 75.35           C  
ANISOU   33  C   ASP A  56    10508   5270  12852   -591   1332   -546       C  
ATOM     34  O   ASP A  56     -31.724 -42.375  40.766  1.00 75.60           O  
ANISOU   34  O   ASP A  56    10385   5390  12950   -875   1232   -685       O  
ATOM     35  CB  ASP A  56     -31.562 -43.819  43.701  1.00 78.41           C  
ANISOU   35  CB  ASP A  56    11153   5194  13445   -614   1640    -90       C  
ATOM     36  CG  ASP A  56     -32.009 -43.748  45.147  1.00 78.98           C  
ANISOU   36  CG  ASP A  56    11246   5237  13526   -573   1820    246       C  
ATOM     37  OD1 ASP A  56     -31.797 -42.700  45.790  1.00 76.82           O  
ANISOU   37  OD1 ASP A  56    10832   5277  13080   -396   1827    369       O  
ATOM     38  OD2 ASP A  56     -32.571 -44.747  45.642  1.00 81.48           O  
ANISOU   38  OD2 ASP A  56    11736   5209  14013   -726   1962    384       O  
ATOM     39  N   VAL A  57     -29.641 -42.982  41.368  1.00103.56           N  
ANISOU   39  N   VAL A  57    14260   8760  16327   -317   1309   -669       N  
ATOM     40  CA  VAL A  57     -29.220 -43.322  40.016  1.00104.25           C  
ANISOU   40  CA  VAL A  57    14421   8793  16395   -355   1197   -984       C  
ATOM     41  C   VAL A  57     -28.625 -44.725  40.028  1.00105.60           C  
ANISOU   41  C   VAL A  57    14925   8534  16666   -226   1274  -1041       C  
ATOM     42  O   VAL A  57     -28.255 -45.239  41.085  1.00106.39           O  
ANISOU   42  O   VAL A  57    15181   8451  16793    -18   1390   -834       O  
ATOM     43  CB  VAL A  57     -28.179 -42.325  39.465  1.00100.31           C  
ANISOU   43  CB  VAL A  57    13795   8652  15667   -129   1099  -1128       C  
ATOM     44  CG1 VAL A  57     -28.623 -40.892  39.720  1.00 98.84           C  
ANISOU   44  CG1 VAL A  57    13315   8868  15372   -182   1051  -1015       C  
ATOM     45  CG2 VAL A  57     -26.812 -42.588  40.073  1.00 99.91           C  
ANISOU   45  CG2 VAL A  57    13885   8554  15523    269   1161  -1081       C  
ATOM     46  N   ASN A  58     -28.538 -45.348  38.858  1.00119.23           N  
ANISOU   46  N   ASN A  58    16777  10089  18438   -341   1208  -1322       N  
ATOM     47  CA  ASN A  58     -27.988 -46.695  38.771  1.00120.15           C  
ANISOU   47  CA  ASN A  58    17225   9772  18654   -211   1284  -1406       C  
ATOM     48  C   ASN A  58     -26.714 -46.754  37.935  1.00119.16           C  
ANISOU   48  C   ASN A  58    17178   9709  18389     60   1236  -1664       C  
ATOM     49  O   ASN A  58     -26.618 -47.530  36.984  1.00120.77           O  
ANISOU   49  O   ASN A  58    17560   9686  18643    -21   1214  -1924       O  
ATOM     50  CB  ASN A  58     -29.029 -47.679  38.233  1.00123.29           C  
ANISOU   50  CB  ASN A  58    17778   9800  19269   -583   1291  -1514       C  
ATOM     51  CG  ASN A  58     -28.722 -49.120  38.608  1.00127.19           C  
ANISOU   51  CG  ASN A  58    18642   9771  19914   -468   1418  -1487       C  
ATOM     52  OD1 ASN A  58     -27.568 -49.486  38.829  1.00127.40           O  
ANISOU   52  OD1 ASN A  58    18816   9749  19843    -89   1445  -1488       O  
ATOM     53  ND2 ASN A  58     -29.761 -49.944  38.685  1.00130.32           N  
ANISOU   53  ND2 ASN A  58    19143   9915  20459   -779   1431  -1425       N  
ATOM     54  N   THR A  59     -25.741 -45.922  38.291  1.00 89.04           N  
ANISOU   54  N   THR A  59    13225   6209  14398    373   1226  -1601       N  
ATOM     55  CA  THR A  59     -24.422 -45.993  37.679  1.00 88.62           C  
ANISOU   55  CA  THR A  59    13230   6218  14226    676   1215  -1810       C  
ATOM     56  C   THR A  59     -23.613 -47.060  38.405  1.00 90.13           C  
ANISOU   56  C   THR A  59    13676   6064  14505   1002   1322  -1714       C  
ATOM     57  O   THR A  59     -23.491 -47.026  39.629  1.00 89.80           O  
ANISOU   57  O   THR A  59    13637   6009  14473   1171   1375  -1432       O  
ATOM     58  CB  THR A  59     -23.687 -44.644  37.754  1.00 84.90           C  
ANISOU   58  CB  THR A  59    12485   6235  13540    859   1158  -1790       C  
ATOM     59  OG1 THR A  59     -23.577 -44.231  39.121  1.00 84.05           O  
ANISOU   59  OG1 THR A  59    12293   6232  13409   1025   1199  -1486       O  
ATOM     60  CG2 THR A  59     -24.444 -43.582  36.971  1.00 84.58           C  
ANISOU   60  CG2 THR A  59    12217   6514  13405    560   1050  -1884       C  
ATOM     61  N   ASP A  60     -23.073 -48.012  37.649  1.00152.25           N  
ANISOU   61  N   ASP A  60    21769  13651  22427   1098   1352  -1948       N  
ATOM     62  CA  ASP A  60     -22.358 -49.142  38.237  1.00154.87           C  
ANISOU   62  CA  ASP A  60    22326  13734  22785   1393   1378  -1838       C  
ATOM     63  C   ASP A  60     -21.125 -48.704  39.025  1.00153.17           C  
ANISOU   63  C   ASP A  60    21997  13750  22452   1827   1379  -1699       C  
ATOM     64  O   ASP A  60     -20.537 -47.658  38.750  1.00150.18           O  
ANISOU   64  O   ASP A  60    21388  13731  21943   1936   1355  -1787       O  
ATOM     65  CB  ASP A  60     -21.976 -50.163  37.162  1.00159.07           C  
ANISOU   65  CB  ASP A  60    23059  14065  23314   1411   1339  -2114       C  
ATOM     66  CG  ASP A  60     -21.079 -49.577  36.092  1.00157.67           C  
ANISOU   66  CG  ASP A  60    22754  14188  22965   1545   1298  -2398       C  
ATOM     67  OD1 ASP A  60     -21.609 -48.977  35.133  1.00156.42           O  
ANISOU   67  OD1 ASP A  60    22506  14179  22748   1268   1259  -2595       O  
ATOM     68  OD2 ASP A  60     -19.844 -49.721  36.207  1.00158.11           O  
ANISOU   68  OD2 ASP A  60    22788  14345  22942   1922   1299  -2421       O  
ATOM     69  N   ILE A  61     -20.749 -49.516  40.008  1.00 89.59           N  
ANISOU   69  N   ILE A  61    14095   5500  14445   2059   1393  -1482       N  
ATOM     70  CA  ILE A  61     -19.646 -49.194  40.909  1.00 89.12           C  
ANISOU   70  CA  ILE A  61    13922   5657  14282   2454   1362  -1319       C  
ATOM     71  C   ILE A  61     -18.310 -49.107  40.174  1.00 88.84           C  
ANISOU   71  C   ILE A  61    13767   5838  14150   2741   1301  -1560       C  
ATOM     72  O   ILE A  61     -17.500 -48.220  40.444  1.00 86.19           O  
ANISOU   72  O   ILE A  61    13195   5860  13692   2950   1262  -1538       O  
ATOM     73  CB  ILE A  61     -19.533 -50.223  42.060  1.00 93.30           C  
ANISOU   73  CB  ILE A  61    14654   5908  14886   2627   1373  -1047       C  
ATOM     74  CG1 ILE A  61     -20.856 -50.333  42.825  1.00 93.89           C  
ANISOU   74  CG1 ILE A  61    14846   5778  15049   2331   1455   -794       C  
ATOM     75  CG2 ILE A  61     -18.404 -49.848  43.009  1.00 92.23           C  
ANISOU   75  CG2 ILE A  61    14376   6032  14636   3014   1312   -883       C  
ATOM     76  CD1 ILE A  61     -21.756 -51.460  42.355  1.00 96.94           C  
ANISOU   76  CD1 ILE A  61    15481   5747  15605   2039   1498   -860       C  
ATOM     77  N   TYR A  62     -18.090 -50.028  39.240  1.00137.87           N  
ANISOU   77  N   TYR A  62    20131  11838  20417   2739   1296  -1794       N  
ATOM     78  CA  TYR A  62     -16.849 -50.063  38.473  1.00139.32           C  
ANISOU   78  CA  TYR A  62    20205  12201  20528   2999   1260  -2038       C  
ATOM     79  C   TYR A  62     -16.639 -48.784  37.667  1.00134.88           C  
ANISOU   79  C   TYR A  62    19403  12051  19796   2922   1254  -2221       C  
ATOM     80  O   TYR A  62     -15.511 -48.313  37.517  1.00133.86           O  
ANISOU   80  O   TYR A  62    19064  12225  19572   3170   1226  -2309       O  
ATOM     81  CB  TYR A  62     -16.820 -51.286  37.554  1.00148.75           C  
ANISOU   81  CB  TYR A  62    21635  13069  21813   2972   1269  -2265       C  
ATOM     82  CG  TYR A  62     -16.701 -52.598  38.297  1.00153.98           C  
ANISOU   82  CG  TYR A  62    22513  13349  22645   3129   1276  -2108       C  
ATOM     83  CD1 TYR A  62     -16.078 -52.659  39.537  1.00154.40           C  
ANISOU   83  CD1 TYR A  62    22489  13451  22724   3416   1257  -1845       C  
ATOM     84  CD2 TYR A  62     -17.213 -53.772  37.762  1.00158.24           C  
ANISOU   84  CD2 TYR A  62    23335  13479  23309   2982   1297  -2218       C  
ATOM     85  CE1 TYR A  62     -15.967 -53.853  40.223  1.00158.42           C  
ANISOU   85  CE1 TYR A  62    23209  13610  23374   3561   1266  -1685       C  
ATOM     86  CE2 TYR A  62     -17.106 -54.972  38.441  1.00162.11           C  
ANISOU   86  CE2 TYR A  62    24033  13607  23955   3122   1311  -2067       C  
ATOM     87  CZ  TYR A  62     -16.482 -55.006  39.671  1.00162.20           C  
ANISOU   87  CZ  TYR A  62    23972  13672  23984   3416   1299  -1795       C  
ATOM     88  OH  TYR A  62     -16.373 -56.197  40.352  1.00165.58           O  
ANISOU   88  OH  TYR A  62    24622  13738  24554   3559   1314  -1630       O  
ATOM     89  N   SER A  63     -17.731 -48.223  37.155  1.00 97.75           N  
ANISOU   89  N   SER A  63    14705   7361  15074   2557   1280  -2276       N  
ATOM     90  CA  SER A  63     -17.668 -46.959  36.433  1.00 94.66           C  
ANISOU   90  CA  SER A  63    14083   7351  14534   2440   1278  -2423       C  
ATOM     91  C   SER A  63     -17.292 -45.833  37.388  1.00 91.84           C  
ANISOU   91  C   SER A  63    13465   7322  14110   2583   1267  -2222       C  
ATOM     92  O   SER A  63     -16.505 -44.953  37.042  1.00 90.21           O  
ANISOU   92  O   SER A  63    13037   7480  13758   2696   1252  -2318       O  
ATOM     93  CB  SER A  63     -19.005 -46.652  35.758  1.00 95.56           C  
ANISOU   93  CB  SER A  63    14223   7395  14692   1994   1279  -2520       C  
ATOM     94  OG  SER A  63     -20.034 -46.482  36.716  1.00 94.63           O  
ANISOU   94  OG  SER A  63    14100   7150  14707   1814   1296  -2273       O  
ATOM     95  N   LYS A  64     -17.861 -45.871  38.590  1.00 87.88           N  
ANISOU   95  N   LYS A  64    12999   6693  13697   2568   1277  -1936       N  
ATOM     96  CA  LYS A  64     -17.556 -44.882  39.617  1.00 85.60           C  
ANISOU   96  CA  LYS A  64    12500   6691  13331   2708   1259  -1721       C  
ATOM     97  C   LYS A  64     -16.072 -44.901  39.962  1.00 86.24           C  
ANISOU   97  C   LYS A  64    12452   6994  13319   3096   1191  -1722       C  
ATOM     98  O   LYS A  64     -15.427 -43.857  40.007  1.00 84.59           O  
ANISOU   98  O   LYS A  64    11987   7167  12987   3185   1157  -1749       O  
ATOM     99  CB  LYS A  64     -18.378 -45.138  40.882  1.00 85.10           C  
ANISOU   99  CB  LYS A  64    12553   6431  13348   2648   1280  -1397       C  
ATOM    100  CG  LYS A  64     -19.881 -45.020  40.703  1.00 84.74           C  
ANISOU  100  CG  LYS A  64    12538   6290  13367   2212   1285  -1348       C  
ATOM    101  CD  LYS A  64     -20.596 -45.232  42.029  1.00 85.37           C  
ANISOU  101  CD  LYS A  64    12713   6216  13507   2175   1327  -1012       C  
ATOM    102  CE  LYS A  64     -22.105 -45.183  41.869  1.00 85.73           C  
ANISOU  102  CE  LYS A  64    12771   6151  13650   1744   1350   -962       C  
ATOM    103  NZ  LYS A  64     -22.569 -43.875  41.333  1.00 85.02           N  
ANISOU  103  NZ  LYS A  64    12398   6457  13450   1505   1272  -1050       N  
ATOM    104  N   VAL A  65     -15.540 -46.096  40.200  1.00 84.92           N  
ANISOU  104  N   VAL A  65    12433   6586  13246   3299   1170  -1702       N  
ATOM    105  CA  VAL A  65     -14.139 -46.258  40.576  1.00 85.74           C  
ANISOU  105  CA  VAL A  65    12364   6860  13353   3631   1118  -1701       C  
ATOM    106  C   VAL A  65     -13.199 -45.873  39.435  1.00 84.94           C  
ANISOU  106  C   VAL A  65    12042   7017  13214   3676   1145  -2002       C  
ATOM    107  O   VAL A  65     -12.178 -45.220  39.655  1.00 84.16           O  
ANISOU  107  O   VAL A  65    11662   7238  13077   3808   1169  -1979       O  
ATOM    108  CB  VAL A  65     -13.842 -47.704  41.025  1.00 89.29           C  
ANISOU  108  CB  VAL A  65    13025   6949  13952   3816   1116  -1614       C  
ATOM    109  CG1 VAL A  65     -12.378 -47.857  41.406  1.00 91.01           C  
ANISOU  109  CG1 VAL A  65    13038   7344  14198   4143   1087  -1598       C  
ATOM    110  CG2 VAL A  65     -14.741 -48.090  42.189  1.00 89.91           C  
ANISOU  110  CG2 VAL A  65    13321   6777  14064   3754   1115  -1296       C  
ATOM    111  N   LEU A  66     -13.552 -46.278  38.219  1.00 75.70           N  
ANISOU  111  N   LEU A  66    11026   5706  12030   3543   1169  -2256       N  
ATOM    112  CA  LEU A  66     -12.764 -45.942  37.037  1.00 75.72           C  
ANISOU  112  CA  LEU A  66    10866   5971  11934   3538   1208  -2520       C  
ATOM    113  C   LEU A  66     -12.686 -44.431  36.843  1.00 71.92           C  
ANISOU  113  C   LEU A  66    10313   5874  11140   3442   1402  -2371       C  
ATOM    114  O   LEU A  66     -11.596 -43.853  36.796  1.00 71.49           O  
ANISOU  114  O   LEU A  66     9961   6107  11095   3537   1471  -2395       O  
ATOM    115  CB  LEU A  66     -13.369 -46.596  35.793  1.00 77.34           C  
ANISOU  115  CB  LEU A  66    11442   5944  11999   3424   1234  -2719       C  
ATOM    116  CG  LEU A  66     -12.711 -46.271  34.451  1.00 77.53           C  
ANISOU  116  CG  LEU A  66    11503   6181  11775   3417   1399  -2893       C  
ATOM    117  CD1 LEU A  66     -11.292 -46.815  34.399  1.00 80.35           C  
ANISOU  117  CD1 LEU A  66    11814   6554  12160   3664   1659  -2829       C  
ATOM    118  CD2 LEU A  66     -13.543 -46.813  33.299  1.00 78.84           C  
ANISOU  118  CD2 LEU A  66    11902   6098  11957   3166   1392  -3146       C  
ATOM    119  N   VAL A  67     -13.853 -43.802  36.737  1.00 69.41           N  
ANISOU  119  N   VAL A  67    10013   5569  10793   3203   1270  -2427       N  
ATOM    120  CA  VAL A  67     -13.950 -42.358  36.550  1.00 65.88           C  
ANISOU  120  CA  VAL A  67     9288   5500  10242   3017   1259  -2438       C  
ATOM    121  C   VAL A  67     -13.272 -41.595  37.690  1.00 64.32           C  
ANISOU  121  C   VAL A  67     8852   5573  10014   3188   1236  -2222       C  
ATOM    122  O   VAL A  67     -12.643 -40.560  37.468  1.00 62.54           O  
ANISOU  122  O   VAL A  67     8377   5723   9661   3156   1227  -2253       O  
ATOM    123  CB  VAL A  67     -15.425 -41.918  36.399  1.00 63.87           C  
ANISOU  123  CB  VAL A  67     9052   5148  10069   2655   1213  -2458       C  
ATOM    124  CG1 VAL A  67     -15.553 -40.407  36.446  1.00 60.11           C  
ANISOU  124  CG1 VAL A  67     8304   5071   9465   2505   1160  -2421       C  
ATOM    125  CG2 VAL A  67     -16.007 -42.462  35.103  1.00 65.32           C  
ANISOU  125  CG2 VAL A  67     9416   5145  10256   2423   1239  -2695       C  
ATOM    126  N   THR A  68     -13.388 -42.121  38.906  1.00 65.26           N  
ANISOU  126  N   THR A  68     9017   5491  10287   3324   1218  -2013       N  
ATOM    127  CA  THR A  68     -12.734 -41.521  40.065  1.00 64.32           C  
ANISOU  127  CA  THR A  68     8667   5630  10141   3471   1126  -1826       C  
ATOM    128  C   THR A  68     -11.217 -41.563  39.917  1.00 65.87           C  
ANISOU  128  C   THR A  68     8670   6046  10311   3662   1159  -1870       C  
ATOM    129  O   THR A  68     -10.537 -40.558  40.126  1.00 64.28           O  
ANISOU  129  O   THR A  68     8228   6211   9984   3670   1116  -1835       O  
ATOM    130  CB  THR A  68     -13.125 -42.236  41.372  1.00 65.69           C  
ANISOU  130  CB  THR A  68     8994   5562  10405   3600   1038  -1584       C  
ATOM    131  OG1 THR A  68     -14.550 -42.213  41.522  1.00 64.56           O  
ANISOU  131  OG1 THR A  68     9062   5197  10272   3400   1058  -1490       O  
ATOM    132  CG2 THR A  68     -12.479 -41.557  42.570  1.00 64.76           C  
ANISOU  132  CG2 THR A  68     8687   5735  10185   3743    949  -1377       C  
ATOM    133  N   ALA A  69     -10.696 -42.732  39.554  1.00 69.20           N  
ANISOU  133  N   ALA A  69     9195   6230  10868   3806   1226  -1955       N  
ATOM    134  CA  ALA A  69      -9.263 -42.914  39.351  1.00 71.27           C  
ANISOU  134  CA  ALA A  69     9286   6657  11135   4006   1271  -2006       C  
ATOM    135  C   ALA A  69      -8.744 -41.970  38.273  1.00 69.74           C  
ANISOU  135  C   ALA A  69     8936   6796  10765   3885   1353  -2163       C  
ATOM    136  O   ALA A  69      -7.678 -41.367  38.420  1.00 69.65           O  
ANISOU  136  O   ALA A  69     8676   7097  10691   3966   1329  -2144       O  
ATOM    137  CB  ALA A  69      -8.961 -44.359  38.983  1.00 75.25           C  
ANISOU  137  CB  ALA A  69     9955   6813  11825   4160   1348  -2103       C  
ATOM    138  N   ILE A  70      -9.508 -41.846  37.191  1.00 84.02           N  
ANISOU  138  N   ILE A  70    10903   8539  12484   3682   1421  -2321       N  
ATOM    139  CA  ILE A  70      -9.168 -40.921  36.117  1.00 82.81           C  
ANISOU  139  CA  ILE A  70    10626   8696  12144   3534   1459  -2476       C  
ATOM    140  C   ILE A  70      -9.133 -39.485  36.636  1.00 79.80           C  
ANISOU  140  C   ILE A  70     9993   8680  11649   3413   1354  -2375       C  
ATOM    141  O   ILE A  70      -8.213 -38.725  36.327  1.00 79.14           O  
ANISOU  141  O   ILE A  70     9690   8905  11474   3401   1371  -2413       O  
ATOM    142  CB  ILE A  70     -10.168 -41.020  34.947  1.00 82.26           C  
ANISOU  142  CB  ILE A  70    10778   8492  11988   3308   1482  -2663       C  
ATOM    143  CG1 ILE A  70     -10.142 -42.423  34.339  1.00 85.55           C  
ANISOU  143  CG1 ILE A  70    11473   8551  12484   3415   1587  -2787       C  
ATOM    144  CG2 ILE A  70      -9.855 -39.981  33.882  1.00 80.61           C  
ANISOU  144  CG2 ILE A  70    10419   8614  11597   3128   1503  -2808       C  
ATOM    145  CD1 ILE A  70     -11.140 -42.622  33.219  1.00 85.51           C  
ANISOU  145  CD1 ILE A  70    11698   8398  12397   3179   1565  -2989       C  
ATOM    146  N   TYR A  71     -10.132 -39.128  37.437  1.00 75.04           N  
ANISOU  146  N   TYR A  71     9428   8024  11058   3321   1255  -2245       N  
ATOM    147  CA  TYR A  71     -10.227 -37.786  38.004  1.00 71.67           C  
ANISOU  147  CA  TYR A  71     8795   7909  10528   3202   1161  -2146       C  
ATOM    148  C   TYR A  71      -9.046 -37.471  38.913  1.00 71.59           C  
ANISOU  148  C   TYR A  71     8564   8118  10519   3373   1108  -2022       C  
ATOM    149  O   TYR A  71      -8.573 -36.338  38.952  1.00 68.88           O  
ANISOU  149  O   TYR A  71     8012   8093  10065   3276   1069  -2017       O  
ATOM    150  CB  TYR A  71     -11.534 -37.609  38.782  1.00 68.22           C  
ANISOU  150  CB  TYR A  71     8457   7335  10126   3110   1080  -2021       C  
ATOM    151  CG  TYR A  71     -12.761 -37.416  37.920  1.00 68.33           C  
ANISOU  151  CG  TYR A  71     8589   7243  10130   2856   1084  -2155       C  
ATOM    152  CD1 TYR A  71     -12.694 -37.534  36.538  1.00 68.88           C  
ANISOU  152  CD1 TYR A  71     8714   7310  10146   2733   1149  -2372       C  
ATOM    153  CD2 TYR A  71     -13.988 -37.098  38.490  1.00 69.05           C  
ANISOU  153  CD2 TYR A  71     8718   7237  10282   2722   1020  -2069       C  
ATOM    154  CE1 TYR A  71     -13.815 -37.356  35.751  1.00 69.10           C  
ANISOU  154  CE1 TYR A  71     8831   7245  10178   2472   1135  -2503       C  
ATOM    155  CE2 TYR A  71     -15.114 -36.915  37.710  1.00 68.97           C  
ANISOU  155  CE2 TYR A  71     8791   7152  10261   2402   1019  -2125       C  
ATOM    156  CZ  TYR A  71     -15.021 -37.043  36.341  1.00 68.94           C  
ANISOU  156  CZ  TYR A  71     8832   7142  10221   2297   1067  -2372       C  
ATOM    157  OH  TYR A  71     -16.140 -36.864  35.560  1.00 69.22           O  
ANISOU  157  OH  TYR A  71     8949   7119  10231   1981   1039  -2424       O  
ATOM    158  N   LEU A  72      -8.577 -38.476  39.646  1.00 63.43           N  
ANISOU  158  N   LEU A  72     7580   6904   9615   3615   1093  -1928       N  
ATOM    159  CA  LEU A  72      -7.449 -38.297  40.552  1.00 64.53           C  
ANISOU  159  CA  LEU A  72     7516   7242   9761   3794   1007  -1820       C  
ATOM    160  C   LEU A  72      -6.137 -38.199  39.781  1.00 66.18           C  
ANISOU  160  C   LEU A  72     7542   7649   9953   3854   1080  -1956       C  
ATOM    161  O   LEU A  72      -5.243 -37.435  40.152  1.00 65.99           O  
ANISOU  161  O   LEU A  72     7282   7921   9869   3872   1013  -1928       O  
ATOM    162  CB  LEU A  72      -7.385 -39.436  41.571  1.00 67.11           C  
ANISOU  162  CB  LEU A  72     7965   7311  10225   4042    945  -1674       C  
ATOM    163  CG  LEU A  72      -8.584 -39.563  42.513  1.00 65.94           C  
ANISOU  163  CG  LEU A  72     8001   6966  10087   4007    867  -1503       C  
ATOM    164  CD1 LEU A  72      -8.356 -40.668  43.534  1.00 68.92           C  
ANISOU  164  CD1 LEU A  72     8504   7115  10567   4263    793  -1338       C  
ATOM    165  CD2 LEU A  72      -8.872 -38.238  43.204  1.00 62.88           C  
ANISOU  165  CD2 LEU A  72     7480   6865   9548   3875    771  -1404       C  
ATOM    166  N   ALA A  73      -6.027 -38.977  38.708  1.00 66.69           N  
ANISOU  166  N   ALA A  73     7725   7545  10071   3882   1221  -2109       N  
ATOM    167  CA  ALA A  73      -4.855 -38.918  37.841  1.00 68.49           C  
ANISOU  167  CA  ALA A  73     7803   7943  10280   3935   1323  -2250       C  
ATOM    168  C   ALA A  73      -4.742 -37.535  37.209  1.00 65.95           C  
ANISOU  168  C   ALA A  73     7320   7951   9788   3693   1327  -2322       C  
ATOM    169  O   ALA A  73      -3.682 -36.907  37.240  1.00 66.44           O  
ANISOU  169  O   ALA A  73     7140   8287   9817   3713   1314  -2333       O  
ATOM    170  CB  ALA A  73      -4.936 -39.989  36.767  1.00 70.86           C  
ANISOU  170  CB  ALA A  73     8308   7977  10639   3989   1484  -2409       C  
ATOM    171  N   LEU A  74      -5.849 -37.064  36.644  1.00 63.46           N  
ANISOU  171  N   LEU A  74     7138   7599   9374   3458   1337  -2372       N  
ATOM    172  CA  LEU A  74      -5.906 -35.731  36.056  1.00 60.99           C  
ANISOU  172  CA  LEU A  74     6701   7565   8906   3207   1331  -2427       C  
ATOM    173  C   LEU A  74      -5.707 -34.664  37.127  1.00 59.08           C  
ANISOU  173  C   LEU A  74     6262   7559   8627   3158   1199  -2284       C  
ATOM    174  O   LEU A  74      -5.223 -33.568  36.843  1.00 58.02           O  
ANISOU  174  O   LEU A  74     5956   7693   8396   3013   1194  -2316       O  
ATOM    175  CB  LEU A  74      -7.242 -35.521  35.343  1.00 58.92           C  
ANISOU  175  CB  LEU A  74     6629   7192   8567   2981   1338  -2496       C  
ATOM    176  CG  LEU A  74      -7.507 -36.428  34.140  1.00 60.78           C  
ANISOU  176  CG  LEU A  74     7079   7215   8801   2979   1453  -2673       C  
ATOM    177  CD1 LEU A  74      -8.956 -36.325  33.697  1.00 59.00           C  
ANISOU  177  CD1 LEU A  74     7040   6846   8530   2765   1411  -2731       C  
ATOM    178  CD2 LEU A  74      -6.568 -36.083  32.996  1.00 61.98           C  
ANISOU  178  CD2 LEU A  74     7134   7564   8851   2935   1567  -2817       C  
ATOM    179  N   PHE A  75      -6.081 -34.996  38.359  1.00 62.89           N  
ANISOU  179  N   PHE A  75     6786   7931   9180   3275   1094  -2129       N  
ATOM    180  CA  PHE A  75      -5.904 -34.089  39.486  1.00 61.43           C  
ANISOU  180  CA  PHE A  75     6446   7950   8946   3251    959  -1997       C  
ATOM    181  C   PHE A  75      -4.427 -33.875  39.780  1.00 63.37           C  
ANISOU  181  C   PHE A  75     6451   8426   9203   3375    924  -2008       C  
ATOM    182  O   PHE A  75      -3.955 -32.742  39.802  1.00 62.26           O  
ANISOU  182  O   PHE A  75     6132   8552   8973   3237    885  -2027       O  
ATOM    183  CB  PHE A  75      -6.617 -34.618  40.733  1.00 61.30           C  
ANISOU  183  CB  PHE A  75     6553   7747   8990   3374    861  -1827       C  
ATOM    184  CG  PHE A  75      -6.325 -33.830  41.979  1.00 60.45           C  
ANISOU  184  CG  PHE A  75     6306   7845   8816   3394    716  -1695       C  
ATOM    185  CD1 PHE A  75      -6.979 -32.636  42.229  1.00 57.52           C  
ANISOU  185  CD1 PHE A  75     5903   7619   8333   3184    670  -1658       C  
ATOM    186  CD2 PHE A  75      -5.401 -34.288  42.905  1.00 62.82           C  
ANISOU  186  CD2 PHE A  75     6517   8193   9160   3630    620  -1614       C  
ATOM    187  CE1 PHE A  75      -6.713 -31.910  43.375  1.00 56.94           C  
ANISOU  187  CE1 PHE A  75     5724   7729   8184   3202    541  -1554       C  
ATOM    188  CE2 PHE A  75      -5.131 -33.566  44.052  1.00 62.28           C  
ANISOU  188  CE2 PHE A  75     6338   8323   9005   3650    473  -1509       C  
ATOM    189  CZ  PHE A  75      -5.788 -32.376  44.288  1.00 59.33           C  
ANISOU  189  CZ  PHE A  75     5946   8086   8511   3434    439  -1485       C  
ATOM    190  N   VAL A  76      -3.698 -34.964  40.006  1.00 62.50           N  
ANISOU  190  N   VAL A  76     6335   8202   9212   3635    937  -2001       N  
ATOM    191  CA  VAL A  76      -2.275 -34.852  40.317  1.00 64.83           C  
ANISOU  191  CA  VAL A  76     6384   8713   9537   3781    893  -2014       C  
ATOM    192  C   VAL A  76      -1.465 -34.320  39.133  1.00 65.41           C  
ANISOU  192  C   VAL A  76     6302   8980   9570   3667   1018  -2176       C  
ATOM    193  O   VAL A  76      -0.617 -33.442  39.304  1.00 65.54           O  
ANISOU  193  O   VAL A  76     6087   9274   9541   3608    969  -2197       O  
ATOM    194  CB  VAL A  76      -1.678 -36.181  40.844  1.00 68.45           C  
ANISOU  194  CB  VAL A  76     6866   8996  10145   4109    872  -1961       C  
ATOM    195  CG1 VAL A  76      -2.173 -36.461  42.255  1.00 68.24           C  
ANISOU  195  CG1 VAL A  76     6932   8870  10127   4230    707  -1772       C  
ATOM    196  CG2 VAL A  76      -2.012 -37.339  39.918  1.00 70.02           C  
ANISOU  196  CG2 VAL A  76     7270   8891  10442   4185   1034  -2050       C  
ATOM    197  N   VAL A  77      -1.740 -34.835  37.938  1.00 65.92           N  
ANISOU  197  N   VAL A  77     6506   8898   9643   3629   1179  -2297       N  
ATOM    198  CA  VAL A  77      -1.037 -34.388  36.737  1.00 66.69           C  
ANISOU  198  CA  VAL A  77     6493   9162   9686   3524   1317  -2449       C  
ATOM    199  C   VAL A  77      -1.280 -32.903  36.475  1.00 63.78           C  
ANISOU  199  C   VAL A  77     6037   9026   9171   3224   1287  -2463       C  
ATOM    200  O   VAL A  77      -0.345 -32.147  36.200  1.00 64.47           O  
ANISOU  200  O   VAL A  77     5914   9357   9224   3153   1314  -2520       O  
ATOM    201  CB  VAL A  77      -1.446 -35.213  35.497  1.00 67.73           C  
ANISOU  201  CB  VAL A  77     6841   9077   9818   3528   1488  -2580       C  
ATOM    202  CG1 VAL A  77      -0.924 -34.563  34.223  1.00 68.05           C  
ANISOU  202  CG1 VAL A  77     6801   9301   9753   3371   1626  -2728       C  
ATOM    203  CG2 VAL A  77      -0.937 -36.641  35.617  1.00 71.34           C  
ANISOU  203  CG2 VAL A  77     7358   9315  10432   3833   1551  -2595       C  
ATOM    204  N   GLY A  78      -2.538 -32.490  36.579  1.00113.37           N  
ANISOU  204  N   GLY A  78    12478  15219  15376   3051   1235  -2409       N  
ATOM    205  CA  GLY A  78      -2.908 -31.107  36.345  1.00110.49           C  
ANISOU  205  CA  GLY A  78    12063  15035  14882   2771   1207  -2411       C  
ATOM    206  C   GLY A  78      -2.373 -30.147  37.390  1.00109.47           C  
ANISOU  206  C   GLY A  78    11733  15127  14733   2735   1076  -2327       C  
ATOM    207  O   GLY A  78      -1.859 -29.080  37.055  1.00108.96           O  
ANISOU  207  O   GLY A  78    11525  15277  14598   2567   1092  -2377       O  
ATOM    208  N   THR A  79      -2.497 -30.521  38.660  1.00 75.16           N  
ANISOU  208  N   THR A  79     7391  10724  10443   2892    946  -2205       N  
ATOM    209  CA  THR A  79      -2.052 -29.666  39.756  1.00 74.84           C  
ANISOU  209  CA  THR A  79     7184  10887  10365   2872    802  -2134       C  
ATOM    210  C   THR A  79      -0.533 -29.530  39.799  1.00 76.96           C  
ANISOU  210  C   THR A  79     7192  11374  10674   2964    795  -2205       C  
ATOM    211  O   THR A  79      -0.010 -28.435  40.004  1.00 75.85           O  
ANISOU  211  O   THR A  79     6884  11463  10472   2821    746  -2234       O  
ATOM    212  CB  THR A  79      -2.559 -30.167  41.122  1.00 72.98           C  
ANISOU  212  CB  THR A  79     7034  10537  10159   3037    662  -1984       C  
ATOM    213  OG1 THR A  79      -2.316 -31.574  41.238  1.00 75.83           O  
ANISOU  213  OG1 THR A  79     7464  10707  10640   3305    682  -1960       O  
ATOM    214  CG2 THR A  79      -4.049 -29.902  41.266  1.00 69.58           C  
ANISOU  214  CG2 THR A  79     6806   9958   9672   2895    655  -1907       C  
ATOM    215  N   VAL A  80       0.172 -30.641  39.609  1.00 75.89           N  
ANISOU  215  N   VAL A  80     7020  11164  10652   3202    847  -2237       N  
ATOM    216  CA  VAL A  80       1.629 -30.602  39.567  1.00 78.95           C  
ANISOU  216  CA  VAL A  80     7141  11757  11099   3308    855  -2310       C  
ATOM    217  C   VAL A  80       2.106 -29.832  38.338  1.00 78.97           C  
ANISOU  217  C   VAL A  80     7042  11913  11051   3099   1006  -2447       C  
ATOM    218  O   VAL A  80       2.977 -28.967  38.437  1.00 79.77           O  
ANISOU  218  O   VAL A  80     6914  12261  11133   3007    980  -2496       O  
ATOM    219  CB  VAL A  80       2.245 -32.017  39.575  1.00 82.47           C  
ANISOU  219  CB  VAL A  80     7578  12066  11691   3627    897  -2314       C  
ATOM    220  CG1 VAL A  80       3.729 -31.958  39.245  1.00 85.82           C  
ANISOU  220  CG1 VAL A  80     7715  12707  12186   3718    949  -2413       C  
ATOM    221  CG2 VAL A  80       2.022 -32.685  40.923  1.00 83.11           C  
ANISOU  221  CG2 VAL A  80     7722  12036  11820   3849    725  -2166       C  
ATOM    222  N   GLY A  81       1.516 -30.142  37.187  1.00107.14           N  
ANISOU  222  N   GLY A  81    10786  15331  14589   3021   1162  -2511       N  
ATOM    223  CA  GLY A  81       1.871 -29.487  35.941  1.00107.29           C  
ANISOU  223  CA  GLY A  81    10752  15472  14540   2830   1317  -2633       C  
ATOM    224  C   GLY A  81       1.690 -27.981  35.979  1.00105.53           C  
ANISOU  224  C   GLY A  81    10465  15428  14204   2537   1269  -2626       C  
ATOM    225  O   GLY A  81       2.634 -27.230  35.732  1.00106.83           O  
ANISOU  225  O   GLY A  81    10422  15808  14358   2441   1310  -2694       O  
ATOM    226  N   ASN A  82       0.477 -27.539  36.297  1.00 94.36           N  
ANISOU  226  N   ASN A  82     9225  13915  12711   2398   1190  -2545       N  
ATOM    227  CA  ASN A  82       0.167 -26.113  36.350  1.00 91.72           C  
ANISOU  227  CA  ASN A  82     8865  13713  12272   2126   1149  -2531       C  
ATOM    228  C   ASN A  82       0.841 -25.399  37.519  1.00 91.91           C  
ANISOU  228  C   ASN A  82     8687  13928  12307   2124   1007  -2498       C  
ATOM    229  O   ASN A  82       1.155 -24.212  37.432  1.00 92.28           O  
ANISOU  229  O   ASN A  82     8627  14141  12293   1918   1011  -2538       O  
ATOM    230  CB  ASN A  82      -1.346 -25.891  36.400  1.00 86.72           C  
ANISOU  230  CB  ASN A  82     8468  12917  11566   2002   1108  -2452       C  
ATOM    231  CG  ASN A  82      -2.052 -26.405  35.161  1.00 86.45           C  
ANISOU  231  CG  ASN A  82     8627  12725  11495   1956   1237  -2509       C  
ATOM    232  OD1 ASN A  82      -2.141 -25.710  34.149  1.00 85.00           O  
ANISOU  232  OD1 ASN A  82     8471  12603  11221   1761   1331  -2573       O  
ATOM    233  ND2 ASN A  82      -2.563 -27.629  35.236  1.00 86.96           N  
ANISOU  233  ND2 ASN A  82     8835  12582  11623   2133   1240  -2492       N  
ATOM    234  N   GLY A  83       1.056 -26.125  38.611  1.00 62.55           N  
ANISOU  234  N   GLY A  83     4926  10181   8660   2353    881  -2429       N  
ATOM    235  CA  GLY A  83       1.724 -25.568  39.774  1.00 63.35           C  
ANISOU  235  CA  GLY A  83     4838  10472   8761   2383    727  -2408       C  
ATOM    236  C   GLY A  83       3.179 -25.260  39.482  1.00 66.36           C  
ANISOU  236  C   GLY A  83     4937  11083   9194   2384    769  -2519       C  
ATOM    237  O   GLY A  83       3.657 -24.150  39.736  1.00 66.39           O  
ANISOU  237  O   GLY A  83     4789  11284   9153   2216    725  -2566       O  
ATOM    238  N   VAL A  84       3.885 -26.249  38.943  1.00 65.34           N  
ANISOU  238  N   VAL A  84     4736  10925   9166   2576    865  -2567       N  
ATOM    239  CA  VAL A  84       5.275 -26.069  38.544  1.00 68.60           C  
ANISOU  239  CA  VAL A  84     4868  11549   9646   2593    936  -2676       C  
ATOM    240  C   VAL A  84       5.366 -25.038  37.421  1.00 67.87           C  
ANISOU  240  C   VAL A  84     4758  11551   9481   2301   1095  -2769       C  
ATOM    241  O   VAL A  84       6.309 -24.247  37.369  1.00 69.55           O  
ANISOU  241  O   VAL A  84     4738  11983   9706   2187   1116  -2846       O  
ATOM    242  CB  VAL A  84       5.917 -27.405  38.108  1.00 71.84           C  
ANISOU  242  CB  VAL A  84     5227  11884  10187   2876   1032  -2707       C  
ATOM    243  CG1 VAL A  84       7.303 -27.177  37.527  1.00 75.30           C  
ANISOU  243  CG1 VAL A  84     5371  12544  10697   2875   1144  -2826       C  
ATOM    244  CG2 VAL A  84       5.989 -28.365  39.286  1.00 73.16           C  
ANISOU  244  CG2 VAL A  84     5387  11975  10435   3174    865  -2608       C  
ATOM    245  N   THR A  85       4.370 -25.039  36.538  1.00 94.42           N  
ANISOU  245  N   THR A  85     8366  14744  12765   2179   1203  -2759       N  
ATOM    246  CA  THR A  85       4.294 -24.055  35.461  1.00 94.46           C  
ANISOU  246  CA  THR A  85     8398  14813  12678   1901   1346  -2827       C  
ATOM    247  C   THR A  85       4.272 -22.635  36.019  1.00 93.06           C  
ANISOU  247  C   THR A  85     8146  14781  12433   1660   1255  -2817       C  
ATOM    248  O   THR A  85       5.080 -21.795  35.624  1.00 94.57           O  
ANISOU  248  O   THR A  85     8166  15148  12617   1499   1333  -2897       O  
ATOM    249  CB  THR A  85       3.050 -24.268  34.577  1.00 90.16           C  
ANISOU  249  CB  THR A  85     8151  14059  12045   1815   1433  -2803       C  
ATOM    250  OG1 THR A  85       3.096 -25.575  33.989  1.00 91.78           O  
ANISOU  250  OG1 THR A  85     8436  14128  12308   2026   1535  -2839       O  
ATOM    251  CG2 THR A  85       2.995 -23.225  33.472  1.00 89.68           C  
ANISOU  251  CG2 THR A  85     8125  14072  11878   1536   1571  -2861       C  
ATOM    252  N   LEU A  86       3.350 -22.377  36.942  1.00100.36           N  
ANISOU  252  N   LEU A  86     9199  15624  13309   1636   1102  -2723       N  
ATOM    253  CA  LEU A  86       3.269 -21.076  37.602  1.00 99.37           C  
ANISOU  253  CA  LEU A  86     9022  15616  13119   1431   1009  -2716       C  
ATOM    254  C   LEU A  86       4.561 -20.750  38.338  1.00102.60           C  
ANISOU  254  C   LEU A  86     9133  16260  13588   1469    929  -2784       C  
ATOM    255  O   LEU A  86       5.007 -19.602  38.347  1.00103.19           O  
ANISOU  255  O   LEU A  86     9090  16487  13630   1252    942  -2848       O  
ATOM    256  CB  LEU A  86       2.094 -21.034  38.581  1.00 92.78           C  
ANISOU  256  CB  LEU A  86     8367  14654  12232   1457    861  -2602       C  
ATOM    257  CG  LEU A  86       0.723 -20.684  38.005  1.00 89.67           C  
ANISOU  257  CG  LEU A  86     8236  14081  11753   1305    916  -2540       C  
ATOM    258  CD1 LEU A  86      -0.319 -20.627  39.108  1.00 87.61           C  
ANISOU  258  CD1 LEU A  86     8111  13721  11457   1346    774  -2429       C  
ATOM    259  CD2 LEU A  86       0.783 -19.363  37.257  1.00 89.34           C  
ANISOU  259  CD2 LEU A  86     8189  14121  11636   1012   1014  -2595       C  
ATOM    260  N   PHE A  87       5.156 -21.769  38.952  1.00104.72           N  
ANISOU  260  N   PHE A  87     9284  16555  13951   1744    845  -2770       N  
ATOM    261  CA  PHE A  87       6.397 -21.603  39.698  1.00108.39           C  
ANISOU  261  CA  PHE A  87     9450  17251  14485   1818    746  -2829       C  
ATOM    262  C   PHE A  87       7.508 -21.059  38.801  1.00110.91           C  
ANISOU  262  C   PHE A  87     9545  17747  14850   1674    903  -2954       C  
ATOM    263  O   PHE A  87       8.046 -19.973  39.045  1.00111.53           O  
ANISOU  263  O   PHE A  87     9465  18003  14908   1474    879  -3020       O  
ATOM    264  CB  PHE A  87       6.822 -22.937  40.315  1.00110.27           C  
ANISOU  264  CB  PHE A  87     9616  17458  14825   2168    652  -2782       C  
ATOM    265  CG  PHE A  87       7.605 -22.798  41.589  1.00113.33           C  
ANISOU  265  CG  PHE A  87     9784  18037  15240   2279    447  -2784       C  
ATOM    266  CD1 PHE A  87       6.954 -22.668  42.805  1.00112.09           C  
ANISOU  266  CD1 PHE A  87     9738  17851  15001   2319    254  -2698       C  
ATOM    267  CD2 PHE A  87       8.990 -22.805  41.574  1.00117.90           C  
ANISOU  267  CD2 PHE A  87    10042  18833  15922   2349    445  -2871       C  
ATOM    268  CE1 PHE A  87       7.668 -22.542  43.981  1.00114.15           C  
ANISOU  268  CE1 PHE A  87     9808  18298  15266   2426     54  -2703       C  
ATOM    269  CE2 PHE A  87       9.711 -22.679  42.747  1.00120.02           C  
ANISOU  269  CE2 PHE A  87    10102  19289  16211   2452    238  -2874       C  
ATOM    270  CZ  PHE A  87       9.049 -22.548  43.952  1.00118.09           C  
ANISOU  270  CZ  PHE A  87     9987  19016  15868   2491     36  -2791       C  
ATOM    271  N   THR A  88       7.837 -21.810  37.754  1.00130.60           N  
ANISOU  271  N   THR A  88    12031  20187  17403   1769   1076  -2988       N  
ATOM    272  CA  THR A  88       8.904 -21.414  36.842  1.00132.60           C  
ANISOU  272  CA  THR A  88    12072  20605  17703   1657   1252  -3101       C  
ATOM    273  C   THR A  88       8.585 -20.123  36.087  1.00131.04           C  
ANISOU  273  C   THR A  88    11958  20430  17399   1306   1373  -3138       C  
ATOM    274  O   THR A  88       9.468 -19.294  35.883  1.00133.31           O  
ANISOU  274  O   THR A  88    12035  20905  17709   1134   1439  -3222       O  
ATOM    275  CB  THR A  88       9.277 -22.542  35.848  1.00132.04           C  
ANISOU  275  CB  THR A  88    11997  20464  17709   1851   1432  -3134       C  
ATOM    276  OG1 THR A  88      10.292 -22.076  34.951  1.00134.93           O  
ANISOU  276  OG1 THR A  88    12159  21000  18109   1725   1622  -3241       O  
ATOM    277  CG2 THR A  88       8.066 -22.987  35.045  1.00129.56           C  
ANISOU  277  CG2 THR A  88    12022  19899  17306   1839   1526  -3085       C  
ATOM    278  N   LEU A  89       7.326 -19.948  35.687  1.00126.70           N  
ANISOU  278  N   LEU A  89    11712  19689  16739   1199   1400  -3073       N  
ATOM    279  CA  LEU A  89       6.918 -18.738  34.977  1.00125.51           C  
ANISOU  279  CA  LEU A  89    11671  19534  16481    881   1507  -3089       C  
ATOM    280  C   LEU A  89       7.089 -17.500  35.850  1.00125.13           C  
ANISOU  280  C   LEU A  89    11524  19612  16407    683   1393  -3106       C  
ATOM    281  O   LEU A  89       7.491 -16.441  35.368  1.00125.81           O  
ANISOU  281  O   LEU A  89    11545  19795  16463    430   1500  -3166       O  
ATOM    282  CB  LEU A  89       5.472 -18.841  34.488  1.00120.98           C  
ANISOU  282  CB  LEU A  89    11434  18730  15801    832   1526  -3004       C  
ATOM    283  CG  LEU A  89       5.219 -19.693  33.242  1.00121.85           C  
ANISOU  283  CG  LEU A  89    11685  18720  15892    915   1692  -3016       C  
ATOM    284  CD1 LEU A  89       3.751 -19.637  32.846  1.00117.88           C  
ANISOU  284  CD1 LEU A  89    11498  18012  15279    833   1684  -2936       C  
ATOM    285  CD2 LEU A  89       6.108 -19.246  32.091  1.00124.98           C  
ANISOU  285  CD2 LEU A  89    11967  19245  16276    777   1910  -3111       C  
ATOM    286  N   ALA A  90       6.782 -17.640  37.135  1.00138.75           N  
ANISOU  286  N   ALA A  90    13250  21331  18139    796   1184  -3056       N  
ATOM    287  CA  ALA A  90       6.974 -16.548  38.080  1.00138.68           C  
ANISOU  287  CA  ALA A  90    13144  21448  18101    634   1064  -3088       C  
ATOM    288  C   ALA A  90       8.459 -16.321  38.332  1.00142.66           C  
ANISOU  288  C   ALA A  90    13301  22203  18701    623   1058  -3197       C  
ATOM    289  O   ALA A  90       8.894 -15.191  38.556  1.00143.56           O  
ANISOU  289  O   ALA A  90    13302  22445  18799    389   1060  -3267       O  
ATOM    290  CB  ALA A  90       6.249 -16.834  39.385  1.00145.23           C  
ANISOU  290  CB  ALA A  90    14072  22213  18897    779    848  -3007       C  
ATOM    291  N   ARG A  91       9.236 -17.400  38.288  1.00163.77           N  
ANISOU  291  N   ARG A  91    15802  24939  21483    875   1055  -3212       N  
ATOM    292  CA  ARG A  91      10.675 -17.304  38.518  1.00167.96           C  
ANISOU  292  CA  ARG A  91    15974  25717  22127    896   1046  -3310       C  
ATOM    293  C   ARG A  91      11.446 -16.803  37.295  1.00170.28           C  
ANISOU  293  C   ARG A  91    16134  26106  22457    705   1289  -3398       C  
ATOM    294  O   ARG A  91      12.614 -16.428  37.405  1.00173.78           O  
ANISOU  294  O   ARG A  91    16273  26766  22990    639   1306  -3488       O  
ATOM    295  CB  ARG A  91      11.241 -18.646  38.992  1.00160.27           C  
ANISOU  295  CB  ARG A  91    14850  24778  21266   1257    949  -3285       C  
ATOM    296  CG  ARG A  91      10.805 -19.039  40.394  1.00159.15           C  
ANISOU  296  CG  ARG A  91    14766  24607  21096   1443    688  -3207       C  
ATOM    297  CD  ARG A  91      11.195 -17.979  41.412  1.00159.92           C  
ANISOU  297  CD  ARG A  91    14710  24891  21159   1282    526  -3262       C  
ATOM    298  NE  ARG A  91      10.726 -18.310  42.754  1.00158.93           N  
ANISOU  298  NE  ARG A  91    14659  24745  20981   1456    280  -3186       N  
ATOM    299  CZ  ARG A  91      11.432 -18.999  43.645  1.00161.75           C  
ANISOU  299  CZ  ARG A  91    14824  25226  21406   1709    103  -3173       C  
ATOM    300  NH1 ARG A  91      12.647 -19.433  43.338  1.00165.75           N  
ANISOU  300  NH1 ARG A  91    15036  25888  22054   1821    144  -3233       N  
ATOM    301  NH2 ARG A  91      10.924 -19.255  44.843  1.00160.78           N  
ANISOU  301  NH2 ARG A  91    14805  25076  21209   1857   -114  -3093       N  
ATOM    302  N   LYS A  92      10.796 -16.797  36.134  1.00134.07           N  
ANISOU  302  N   LYS A  92    11774  21366  17801    616   1475  -3372       N  
ATOM    303  CA  LYS A  92      11.429 -16.302  34.913  1.00136.22           C  
ANISOU  303  CA  LYS A  92    11961  21716  18082    430   1723  -3444       C  
ATOM    304  C   LYS A  92      11.634 -14.792  34.967  1.00136.47           C  
ANISOU  304  C   LYS A  92    11942  21843  18068     79   1758  -3494       C  
ATOM    305  O   LYS A  92      12.218 -14.202  34.057  1.00138.58           O  
ANISOU  305  O   LYS A  92    12124  22190  18341   -114   1962  -3552       O  
ATOM    306  CB  LYS A  92      10.608 -16.675  33.675  1.00126.79           C  
ANISOU  306  CB  LYS A  92    11049  20329  16797    424   1899  -3398       C  
ATOM    307  CG  LYS A  92      10.678 -18.144  33.292  1.00127.78           C  
ANISOU  307  CG  LYS A  92    11188  20378  16984    739   1947  -3385       C  
ATOM    308  CD  LYS A  92      12.109 -18.590  33.044  1.00132.49           C  
ANISOU  308  CD  LYS A  92    11449  21171  17722    864   2056  -3475       C  
ATOM    309  CE  LYS A  92      12.186 -20.091  32.811  1.00133.67           C  
ANISOU  309  CE  LYS A  92    11615  21230  17945   1208   2090  -3462       C  
ATOM    310  NZ  LYS A  92      11.343 -20.524  31.662  1.00131.98           N  
ANISOU  310  NZ  LYS A  92    11703  20820  17625   1207   2255  -3441       N  
ATOM    311  N   SER A 100       8.297 -13.163  27.129  1.00118.63           N  
ANISOU  311  N   SER A 100    11109  18901  15064   -764   2934  -3301       N  
ATOM    312  CA  SER A 100       7.814 -13.046  28.500  1.00116.64           C  
ANISOU  312  CA  SER A 100    10841  18607  14871   -716   2679  -3264       C  
ATOM    313  C   SER A 100       6.418 -12.436  28.544  1.00113.10           C  
ANISOU  313  C   SER A 100    10702  17973  14299   -838   2594  -3159       C  
ATOM    314  O   SER A 100       5.743 -12.480  29.572  1.00112.15           O  
ANISOU  314  O   SER A 100    10634  17777  14201   -763   2392  -3111       O  
ATOM    315  CB  SER A 100       8.781 -12.209  29.340  1.00116.13           C  
ANISOU  315  CB  SER A 100    10506  18712  14907   -857   2637  -3328       C  
ATOM    316  OG  SER A 100      10.057 -12.822  29.411  1.00120.90           O  
ANISOU  316  OG  SER A 100    10794  19498  15644   -721   2692  -3420       O  
ATOM    317  N   ARG A 101       5.994 -11.866  27.422  1.00129.03           N  
ANISOU  317  N   ARG A 101    12922  19923  16181  -1019   2754  -3119       N  
ATOM    318  CA  ARG A 101       4.675 -11.255  27.323  1.00125.56           C  
ANISOU  318  CA  ARG A 101    12777  19311  15620  -1133   2693  -3012       C  
ATOM    319  C   ARG A 101       3.582 -12.316  27.373  1.00121.53           C  
ANISOU  319  C   ARG A 101    12442  18655  15079   -911   2572  -2955       C  
ATOM    320  O   ARG A 101       2.517 -12.100  27.950  1.00119.32           O  
ANISOU  320  O   ARG A 101    12313  18252  14773   -910   2425  -2874       O  
ATOM    321  CB  ARG A 101       4.560 -10.443  26.032  1.00122.85           C  
ANISOU  321  CB  ARG A 101    12610  18940  15129  -1364   2902  -2976       C  
ATOM    322  CG  ARG A 101       3.232  -9.727  25.860  1.00120.46           C  
ANISOU  322  CG  ARG A 101    12611  18464  14694  -1483   2851  -2856       C  
ATOM    323  CD  ARG A 101       3.163  -9.031  24.514  1.00122.25           C  
ANISOU  323  CD  ARG A 101    13025  18667  14759  -1688   3063  -2810       C  
ATOM    324  NE  ARG A 101       4.248  -8.071  24.343  1.00125.89           N  
ANISOU  324  NE  ARG A 101    13348  19238  15248  -1915   3217  -2853       N  
ATOM    325  CZ  ARG A 101       4.493  -7.413  23.214  1.00128.63           C  
ANISOU  325  CZ  ARG A 101    13808  19594  15472  -2108   3434  -2825       C  
ATOM    326  NH1 ARG A 101       3.728  -7.613  22.150  1.00128.13           N  
ANISOU  326  NH1 ARG A 101    14004  19446  15234  -2094   3513  -2754       N  
ATOM    327  NH2 ARG A 101       5.502  -6.556  23.148  1.00131.45           N  
ANISOU  327  NH2 ARG A 101    14024  20047  15874  -2319   3571  -2866       N  
ATOM    328  N   VAL A 102       3.857 -13.467  26.766  1.00108.14           N  
ANISOU  328  N   VAL A 102    10725  16972  13391   -725   2644  -3003       N  
ATOM    329  CA  VAL A 102       2.896 -14.563  26.733  1.00105.25           C  
ANISOU  329  CA  VAL A 102    10523  16464  13003   -519   2549  -2966       C  
ATOM    330  C   VAL A 102       2.882 -15.342  28.046  1.00104.13           C  
ANISOU  330  C   VAL A 102    10256  16307  13002   -296   2351  -2965       C  
ATOM    331  O   VAL A 102       1.968 -16.127  28.301  1.00102.58           O  
ANISOU  331  O   VAL A 102    10197  15974  12804   -143   2240  -2918       O  
ATOM    332  CB  VAL A 102       3.180 -15.530  25.568  1.00104.86           C  
ANISOU  332  CB  VAL A 102    10525  16419  12900   -402   2713  -3030       C  
ATOM    333  CG1 VAL A 102       2.986 -14.823  24.235  1.00106.16           C  
ANISOU  333  CG1 VAL A 102    10874  16577  12885   -608   2895  -3013       C  
ATOM    334  CG2 VAL A 102       4.586 -16.096  25.678  1.00108.09           C  
ANISOU  334  CG2 VAL A 102    10652  16984  13434   -277   2806  -3134       C  
ATOM    335  N   ASP A 103       3.895 -15.116  28.878  1.00111.19           N  
ANISOU  335  N   ASP A 103    10892  17343  14012   -285   2307  -3015       N  
ATOM    336  CA  ASP A 103       3.991 -15.792  30.168  1.00111.36           C  
ANISOU  336  CA  ASP A 103    10786  17370  14153    -74   2118  -3010       C  
ATOM    337  C   ASP A 103       2.857 -15.383  31.105  1.00107.37           C  
ANISOU  337  C   ASP A 103    10425  16748  13620   -104   1932  -2915       C  
ATOM    338  O   ASP A 103       2.481 -16.136  32.002  1.00106.62           O  
ANISOU  338  O   ASP A 103    10334  16591  13585     91   1778  -2876       O  
ATOM    339  CB  ASP A 103       5.345 -15.519  30.826  1.00123.13           C  
ANISOU  339  CB  ASP A 103    11961  19063  15758    -76   2108  -3090       C  
ATOM    340  CG  ASP A 103       6.499 -16.149  30.070  1.00127.19           C  
ANISOU  340  CG  ASP A 103    12293  19699  16334     22   2278  -3182       C  
ATOM    341  OD1 ASP A 103       6.249 -17.058  29.250  1.00127.90           O  
ANISOU  341  OD1 ASP A 103    12502  19701  16391    156   2373  -3186       O  
ATOM    342  OD2 ASP A 103       7.657 -15.741  30.302  1.00130.12           O  
ANISOU  342  OD2 ASP A 103    12398  20254  16788    -34   2320  -3255       O  
ATOM    343  N   TYR A 104       2.319 -14.187  30.892  1.00124.08           N  
ANISOU  343  N   TYR A 104    12668  18831  15648   -343   1960  -2872       N  
ATOM    344  CA  TYR A 104       1.193 -13.706  31.684  1.00121.61           C  
ANISOU  344  CA  TYR A 104    12503  18403  15302   -382   1813  -2782       C  
ATOM    345  C   TYR A 104      -0.095 -14.417  31.281  1.00118.38           C  
ANISOU  345  C   TYR A 104    12330  17813  14836   -278   1780  -2700       C  
ATOM    346  O   TYR A 104      -0.924 -14.749  32.130  1.00115.89           O  
ANISOU  346  O   TYR A 104    12087  17402  14546   -168   1633  -2631       O  
ATOM    347  CB  TYR A 104       1.040 -12.191  31.537  1.00121.63           C  
ANISOU  347  CB  TYR A 104    12569  18414  15232   -666   1872  -2764       C  
ATOM    348  CG  TYR A 104       2.146 -11.403  32.203  1.00124.59           C  
ANISOU  348  CG  TYR A 104    12719  18950  15670   -785   1870  -2848       C  
ATOM    349  CD1 TYR A 104       2.789 -11.892  33.333  1.00126.40           C  
ANISOU  349  CD1 TYR A 104    12744  19282  16000   -632   1731  -2898       C  
ATOM    350  CD2 TYR A 104       2.550 -10.173  31.700  1.00126.49           C  
ANISOU  350  CD2 TYR A 104    12956  19241  15865  -1055   2008  -2876       C  
ATOM    351  CE1 TYR A 104       3.801 -11.177  33.946  1.00128.51           C  
ANISOU  351  CE1 TYR A 104    12794  19713  16321   -746   1719  -2986       C  
ATOM    352  CE2 TYR A 104       3.562  -9.450  32.306  1.00128.98           C  
ANISOU  352  CE2 TYR A 104    13061  19703  16243  -1182   2010  -2964       C  
ATOM    353  CZ  TYR A 104       4.183  -9.957  33.428  1.00129.73           C  
ANISOU  353  CZ  TYR A 104    12941  19914  16439  -1027   1859  -3024       C  
ATOM    354  OH  TYR A 104       5.190  -9.242  34.035  1.00131.98           O  
ANISOU  354  OH  TYR A 104    13005  20358  16783  -1158   1849  -3121       O  
ATOM    355  N   TYR A 105      -0.254 -14.651  29.982  1.00 57.14           N  
ANISOU  355  N   TYR A 105     4693  10020   6999   -317   1921  -2712       N  
ATOM    356  CA  TYR A 105      -1.406 -15.386  29.475  1.00 55.50           C  
ANISOU  356  CA  TYR A 105     4699   9659   6730   -228   1899  -2660       C  
ATOM    357  C   TYR A 105      -1.334 -16.843  29.919  1.00 55.71           C  
ANISOU  357  C   TYR A 105     4677   9639   6852     40   1826  -2685       C  
ATOM    358  O   TYR A 105      -2.337 -17.429  30.332  1.00 53.79           O  
ANISOU  358  O   TYR A 105     4557   9261   6619    148   1719  -2626       O  
ATOM    359  CB  TYR A 105      -1.467 -15.311  27.950  1.00 56.75           C  
ANISOU  359  CB  TYR A 105     4993   9811   6758   -333   2072  -2687       C  
ATOM    360  CG  TYR A 105      -1.527 -13.906  27.396  1.00 56.93           C  
ANISOU  360  CG  TYR A 105     5093   9865   6673   -596   2166  -2649       C  
ATOM    361  CD1 TYR A 105      -2.726 -13.210  27.341  1.00 54.76           C  
ANISOU  361  CD1 TYR A 105     5015   9482   6309   -706   2112  -2549       C  
ATOM    362  CD2 TYR A 105      -0.384 -13.279  26.917  1.00 59.53           C  
ANISOU  362  CD2 TYR A 105     5302  10326   6991   -734   2320  -2709       C  
ATOM    363  CE1 TYR A 105      -2.784 -11.926  26.834  1.00 55.16           C  
ANISOU  363  CE1 TYR A 105     5157   9543   6257   -938   2205  -2503       C  
ATOM    364  CE2 TYR A 105      -0.433 -11.995  26.405  1.00 59.95           C  
ANISOU  364  CE2 TYR A 105     5446  10388   6944   -982   2419  -2667       C  
ATOM    365  CZ  TYR A 105      -1.636 -11.324  26.366  1.00 57.75           C  
ANISOU  365  CZ  TYR A 105     5381   9988   6573  -1079   2360  -2560       C  
ATOM    366  OH  TYR A 105      -1.690 -10.046  25.859  1.00 58.39           O  
ANISOU  366  OH  TYR A 105     5573  10060   6552  -1317   2465  -2505       O  
ATOM    367  N   LEU A 106      -0.139 -17.420  29.831  1.00 67.97           N  
ANISOU  367  N   LEU A 106     6047  11298   8478    149   1894  -2772       N  
ATOM    368  CA  LEU A 106       0.083 -18.801  30.247  1.00 68.92           C  
ANISOU  368  CA  LEU A 106     6112  11374   8698    417   1842  -2797       C  
ATOM    369  C   LEU A 106      -0.138 -18.965  31.748  1.00 66.80           C  
ANISOU  369  C   LEU A 106     5779  11080   8520    536   1648  -2731       C  
ATOM    370  O   LEU A 106      -0.689 -19.971  32.196  1.00 65.58           O  
ANISOU  370  O   LEU A 106     5703  10801   8413    721   1564  -2691       O  
ATOM    371  CB  LEU A 106       1.492 -19.261  29.866  1.00 71.82           C  
ANISOU  371  CB  LEU A 106     6276  11878   9132    511   1967  -2902       C  
ATOM    372  CG  LEU A 106       1.661 -19.979  28.524  1.00 73.87           C  
ANISOU  372  CG  LEU A 106     6623  12109   9335    563   2149  -2978       C  
ATOM    373  CD1 LEU A 106       1.178 -19.122  27.363  1.00 72.66           C  
ANISOU  373  CD1 LEU A 106     6639  11949   9019    326   2270  -2974       C  
ATOM    374  CD2 LEU A 106       3.112 -20.388  28.322  1.00 77.51           C  
ANISOU  374  CD2 LEU A 106     6847  12720   9884    672   2272  -3076       C  
ATOM    375  N   GLY A 107       0.296 -17.972  32.516  1.00 52.99           N  
ANISOU  375  N   GLY A 107     3898   9449   6789    424   1585  -2724       N  
ATOM    376  CA  GLY A 107       0.093 -17.975  33.952  1.00 51.80           C  
ANISOU  376  CA  GLY A 107     3695   9292   6693    516   1405  -2667       C  
ATOM    377  C   GLY A 107      -1.378 -17.851  34.297  1.00 48.68           C  
ANISOU  377  C   GLY A 107     3517   8732   6246    492   1315  -2560       C  
ATOM    378  O   GLY A 107      -1.868 -18.498  35.226  1.00 47.66           O  
ANISOU  378  O   GLY A 107     3424   8522   6164    655   1193  -2496       O  
ATOM    379  N   SER A 108      -2.083 -17.014  33.541  1.00 56.54           N  
ANISOU  379  N   SER A 108     4657   9679   7147    292   1384  -2534       N  
ATOM    380  CA  SER A 108      -3.520 -16.845  33.712  1.00 53.66           C  
ANISOU  380  CA  SER A 108     4491   9163   6734    259   1319  -2434       C  
ATOM    381  C   SER A 108      -4.241 -18.163  33.448  1.00 52.95           C  
ANISOU  381  C   SER A 108     4524   8928   6668    433   1303  -2412       C  
ATOM    382  O   SER A 108      -5.152 -18.548  34.186  1.00 51.18           O  
ANISOU  382  O   SER A 108     4386   8591   6472    523   1201  -2333       O  
ATOM    383  CB  SER A 108      -4.043 -15.758  32.771  1.00 52.11           C  
ANISOU  383  CB  SER A 108     4419   8952   6429     25   1413  -2418       C  
ATOM    384  OG  SER A 108      -5.436 -15.559  32.940  1.00 50.20           O  
ANISOU  384  OG  SER A 108     4351   8578   6146     -1   1351  -2322       O  
ATOM    385  N   LEU A 109      -3.819 -18.852  32.391  1.00 59.91           N  
ANISOU  385  N   LEU A 109     5415   9812   7538    477   1417  -2490       N  
ATOM    386  CA  LEU A 109      -4.368 -20.159  32.049  1.00 60.65           C  
ANISOU  386  CA  LEU A 109     5623   9767   7655    638   1421  -2502       C  
ATOM    387  C   LEU A 109      -4.097 -21.176  33.151  1.00 61.61           C  
ANISOU  387  C   LEU A 109     5669   9844   7898    876   1323  -2477       C  
ATOM    388  O   LEU A 109      -4.969 -21.973  33.502  1.00 60.24           O  
ANISOU  388  O   LEU A 109     5613   9519   7759    989   1261  -2429       O  
ATOM    389  CB  LEU A 109      -3.779 -20.655  30.727  1.00 62.26           C  
ANISOU  389  CB  LEU A 109     5844   9997   7815    644   1577  -2611       C  
ATOM    390  CG  LEU A 109      -4.289 -19.979  29.454  1.00 62.28           C  
ANISOU  390  CG  LEU A 109     5992  10001   7671    443   1679  -2631       C  
ATOM    391  CD1 LEU A 109      -3.473 -20.417  28.250  1.00 64.95           C  
ANISOU  391  CD1 LEU A 109     6324  10397   7957    456   1848  -2745       C  
ATOM    392  CD2 LEU A 109      -5.761 -20.295  29.249  1.00 60.21           C  
ANISOU  392  CD2 LEU A 109     5937   9584   7357    431   1615  -2590       C  
ATOM    393  N   ALA A 110      -2.884 -21.141  33.693  1.00118.78           N  
ANISOU  393  N   ALA A 110    12710  17220  15202    949   1312  -2512       N  
ATOM    394  CA  ALA A 110      -2.487 -22.063  34.751  1.00120.49           C  
ANISOU  394  CA  ALA A 110    12840  17416  15525   1186   1217  -2485       C  
ATOM    395  C   ALA A 110      -3.311 -21.848  36.016  1.00118.21           C  
ANISOU  395  C   ALA A 110    12607  17063  15243   1211   1066  -2371       C  
ATOM    396  O   ALA A 110      -3.708 -22.808  36.678  1.00117.89           O  
ANISOU  396  O   ALA A 110    12626  16903  15264   1396    998  -2313       O  
ATOM    397  CB  ALA A 110      -1.003 -21.923  35.047  1.00118.52           C  
ANISOU  397  CB  ALA A 110    12343  17356  15332   1240   1227  -2552       C  
ATOM    398  N   LEU A 111      -3.563 -20.585  36.349  1.00 62.13           N  
ANISOU  398  N   LEU A 111     5494  10036   8078   1026   1026  -2339       N  
ATOM    399  CA  LEU A 111      -4.414 -20.253  37.485  1.00 59.65           C  
ANISOU  399  CA  LEU A 111     5246   9666   7753   1033    905  -2236       C  
ATOM    400  C   LEU A 111      -5.834 -20.749  37.232  1.00 57.35           C  
ANISOU  400  C   LEU A 111     5161   9177   7452   1047    909  -2162       C  
ATOM    401  O   LEU A 111      -6.459 -21.361  38.105  1.00 55.53           O  
ANISOU  401  O   LEU A 111     4995   8842   7263   1180    831  -2079       O  
ATOM    402  CB  LEU A 111      -4.424 -18.743  37.728  1.00 57.13           C  
ANISOU  402  CB  LEU A 111     4891   9451   7363    818    891  -2236       C  
ATOM    403  CG  LEU A 111      -5.295 -18.250  38.886  1.00 55.39           C  
ANISOU  403  CG  LEU A 111     4739   9186   7119    815    784  -2141       C  
ATOM    404  CD1 LEU A 111      -4.744 -18.732  40.219  1.00 56.53           C  
ANISOU  404  CD1 LEU A 111     4770   9404   7303    998    663  -2129       C  
ATOM    405  CD2 LEU A 111      -5.417 -16.733  38.865  1.00 55.04           C  
ANISOU  405  CD2 LEU A 111     4700   9210   7004    585    805  -2153       C  
ATOM    406  N   SER A 112      -6.328 -20.482  36.026  1.00 59.24           N  
ANISOU  406  N   SER A 112     5500   9374   7634    907   1003  -2198       N  
ATOM    407  CA  SER A 112      -7.665 -20.902  35.619  1.00 57.71           C  
ANISOU  407  CA  SER A 112     5484   9017   7427    897   1009  -2157       C  
ATOM    408  C   SER A 112      -7.853 -22.409  35.764  1.00 59.02           C  
ANISOU  408  C   SER A 112     5705   9043   7677   1107    998  -2163       C  
ATOM    409  O   SER A 112      -8.903 -22.873  36.208  1.00 57.60           O  
ANISOU  409  O   SER A 112     5630   8722   7531   1163    950  -2097       O  
ATOM    410  CB  SER A 112      -7.939 -20.478  34.174  1.00 57.36           C  
ANISOU  410  CB  SER A 112     5521   8980   7292    729   1112  -2223       C  
ATOM    411  OG  SER A 112      -9.222 -20.906  33.750  1.00 56.13           O  
ANISOU  411  OG  SER A 112     5521   8685   7120    717   1106  -2209       O  
ATOM    412  N   ASP A 113      -6.828 -23.168  35.392  1.00 91.71           N  
ANISOU  412  N   ASP A 113     9773  13215  11859   1226   1053  -2246       N  
ATOM    413  CA  ASP A 113      -6.876 -24.621  35.504  1.00 93.14           C  
ANISOU  413  CA  ASP A 113    10013  13248  12127   1440   1058  -2261       C  
ATOM    414  C   ASP A 113      -6.776 -25.069  36.960  1.00 92.73           C  
ANISOU  414  C   ASP A 113     9916  13161  12156   1620    949  -2159       C  
ATOM    415  O   ASP A 113      -7.496 -25.971  37.391  1.00 91.81           O  
ANISOU  415  O   ASP A 113     9913  12870  12101   1745    919  -2106       O  
ATOM    416  CB  ASP A 113      -5.760 -25.263  34.678  1.00 97.41           C  
ANISOU  416  CB  ASP A 113    10489  13835  12690   1528   1163  -2379       C  
ATOM    417  CG  ASP A 113      -5.863 -24.931  33.202  1.00 98.17           C  
ANISOU  417  CG  ASP A 113    10656  13958  12686   1365   1282  -2481       C  
ATOM    418  OD1 ASP A 113      -6.988 -24.670  32.726  1.00 97.10           O  
ANISOU  418  OD1 ASP A 113    10664  13745  12484   1233   1276  -2473       O  
ATOM    419  OD2 ASP A 113      -4.818 -24.932  32.518  1.00100.74           O  
ANISOU  419  OD2 ASP A 113    10891  14390  12996   1371   1384  -2571       O  
ATOM    420  N   LEU A 114      -5.882 -24.431  37.711  1.00 46.55           N  
ANISOU  420  N   LEU A 114     3904   7479   6303   1630    890  -2140       N  
ATOM    421  CA  LEU A 114      -5.669 -24.778  39.114  1.00 46.97           C  
ANISOU  421  CA  LEU A 114     3904   7535   6406   1803    774  -2051       C  
ATOM    422  C   LEU A 114      -6.918 -24.574  39.966  1.00 44.85           C  
ANISOU  422  C   LEU A 114     3760   7162   6118   1780    703  -1930       C  
ATOM    423  O   LEU A 114      -7.183 -25.356  40.880  1.00 45.25           O  
ANISOU  423  O   LEU A 114     3860   7112   6221   1958    640  -1845       O  
ATOM    424  CB  LEU A 114      -4.495 -23.991  39.701  1.00 48.01           C  
ANISOU  424  CB  LEU A 114     3830   7896   6517   1785    713  -2081       C  
ATOM    425  CG  LEU A 114      -3.099 -24.561  39.441  1.00 50.97           C  
ANISOU  425  CG  LEU A 114     4036   8372   6956   1924    744  -2168       C  
ATOM    426  CD1 LEU A 114      -2.037 -23.689  40.085  1.00 52.03           C  
ANISOU  426  CD1 LEU A 114     3954   8746   7069   1882    668  -2207       C  
ATOM    427  CD2 LEU A 114      -3.003 -25.990  39.954  1.00 52.60           C  
ANISOU  427  CD2 LEU A 114     4283   8441   7260   2207    708  -2119       C  
ATOM    428  N   LEU A 115      -7.679 -23.524  39.669  1.00 43.89           N  
ANISOU  428  N   LEU A 115     3691   7063   5923   1569    719  -1916       N  
ATOM    429  CA  LEU A 115      -8.919 -23.263  40.395  1.00 42.09           C  
ANISOU  429  CA  LEU A 115     3572   6740   5681   1540    672  -1805       C  
ATOM    430  C   LEU A 115      -9.900 -24.427  40.261  1.00 42.03           C  
ANISOU  430  C   LEU A 115     3711   6512   5747   1645    699  -1768       C  
ATOM    431  O   LEU A 115     -10.491 -24.871  41.247  1.00 42.11           O  
ANISOU  431  O   LEU A 115     3782   6422   5795   1760    651  -1666       O  
ATOM    432  CB  LEU A 115      -9.567 -21.962  39.916  1.00 40.53           C  
ANISOU  432  CB  LEU A 115     3405   6591   5403   1302    701  -1804       C  
ATOM    433  CG  LEU A 115      -8.819 -20.671  40.252  1.00 40.45           C  
ANISOU  433  CG  LEU A 115     3279   6768   5324   1181    672  -1830       C  
ATOM    434  CD1 LEU A 115      -9.578 -19.458  39.735  1.00 38.98           C  
ANISOU  434  CD1 LEU A 115     3156   6584   5069    962    713  -1818       C  
ATOM    435  CD2 LEU A 115      -8.582 -20.563  41.752  1.00 40.97           C  
ANISOU  435  CD2 LEU A 115     3287   6896   5383   1295    568  -1770       C  
ATOM    436  N   ILE A 116     -10.058 -24.921  39.037  1.00 68.51           N  
ANISOU  436  N   ILE A 116     7124   9790   9117   1603    779  -1863       N  
ATOM    437  CA  ILE A 116     -10.947 -26.045  38.767  1.00 69.71           C  
ANISOU  437  CA  ILE A 116     7417   9725   9345   1683    808  -1872       C  
ATOM    438  C   ILE A 116     -10.411 -27.337  39.377  1.00 71.40           C  
ANISOU  438  C   ILE A 116     7649   9822   9656   1935    793  -1848       C  
ATOM    439  O   ILE A 116     -11.155 -28.103  39.989  1.00 72.14           O  
ANISOU  439  O   ILE A 116     7848   9734   9825   2047    772  -1774       O  
ATOM    440  CB  ILE A 116     -11.145 -26.254  37.252  1.00 69.07           C  
ANISOU  440  CB  ILE A 116     7401   9605   9238   1573    891  -2014       C  
ATOM    441  CG1 ILE A 116     -11.735 -24.998  36.610  1.00 68.01           C  
ANISOU  441  CG1 ILE A 116     7265   9570   9003   1334    902  -2026       C  
ATOM    442  CG2 ILE A 116     -12.040 -27.455  36.988  1.00 70.64           C  
ANISOU  442  CG2 ILE A 116     7749   9563   9526   1650    911  -2057       C  
ATOM    443  CD1 ILE A 116     -12.002 -25.144  35.127  1.00 68.77           C  
ANISOU  443  CD1 ILE A 116     7441   9641   9046   1218    974  -2166       C  
ATOM    444  N   LEU A 117      -9.115 -27.571  39.208  1.00 56.67           N  
ANISOU  444  N   LEU A 117     5678   8055   7797   2030    808  -1906       N  
ATOM    445  CA  LEU A 117      -8.486 -28.790  39.705  1.00 58.43           C  
ANISOU  445  CA  LEU A 117     5908   8174   8117   2284    796  -1886       C  
ATOM    446  C   LEU A 117      -8.524 -28.894  41.228  1.00 58.76           C  
ANISOU  446  C   LEU A 117     5937   8209   8181   2430    687  -1737       C  
ATOM    447  O   LEU A 117      -8.605 -29.991  41.778  1.00 60.45           O  
ANISOU  447  O   LEU A 117     6239   8247   8481   2633    669  -1673       O  
ATOM    448  CB  LEU A 117      -7.042 -28.880  39.210  1.00 59.48           C  
ANISOU  448  CB  LEU A 117     5894   8450   8256   2351    836  -1983       C  
ATOM    449  CG  LEU A 117      -6.866 -29.107  37.709  1.00 60.29           C  
ANISOU  449  CG  LEU A 117     6035   8531   8341   2274    963  -2134       C  
ATOM    450  CD1 LEU A 117      -5.477 -28.683  37.268  1.00 61.87           C  
ANISOU  450  CD1 LEU A 117     6046   8944   8518   2268   1008  -2217       C  
ATOM    451  CD2 LEU A 117      -7.122 -30.564  37.354  1.00 62.08           C  
ANISOU  451  CD2 LEU A 117     6418   8506   8662   2444   1025  -2179       C  
ATOM    452  N   LEU A 118      -8.473 -27.752  41.905  1.00 44.38           N  
ANISOU  452  N   LEU A 118     4023   6567   6274   2329    615  -1683       N  
ATOM    453  CA  LEU A 118      -8.391 -27.741  43.364  1.00 44.70           C  
ANISOU  453  CA  LEU A 118     4046   6641   6297   2467    503  -1558       C  
ATOM    454  C   LEU A 118      -9.733 -27.545  44.066  1.00 42.94           C  
ANISOU  454  C   LEU A 118     3957   6307   6051   2429    487  -1437       C  
ATOM    455  O   LEU A 118      -9.966 -28.116  45.131  1.00 43.70           O  
ANISOU  455  O   LEU A 118     4126   6319   6158   2601    427  -1316       O  
ATOM    456  CB  LEU A 118      -7.395 -26.679  43.838  1.00 44.87           C  
ANISOU  456  CB  LEU A 118     3883   6935   6232   2414    422  -1589       C  
ATOM    457  CG  LEU A 118      -5.919 -26.974  43.568  1.00 47.32           C  
ANISOU  457  CG  LEU A 118     4025   7377   6578   2516    411  -1682       C  
ATOM    458  CD1 LEU A 118      -5.043 -25.831  44.053  1.00 47.50           C  
ANISOU  458  CD1 LEU A 118     3860   7671   6519   2431    328  -1729       C  
ATOM    459  CD2 LEU A 118      -5.511 -28.281  44.227  1.00 49.77           C  
ANISOU  459  CD2 LEU A 118     4363   7576   6972   2809    356  -1616       C  
ATOM    460  N   PHE A 119     -10.614 -26.743  43.477  1.00 47.30           N  
ANISOU  460  N   PHE A 119     4545   6860   6568   2213    542  -1462       N  
ATOM    461  CA  PHE A 119     -11.855 -26.379  44.157  1.00 46.85           C  
ANISOU  461  CA  PHE A 119     4580   6733   6489   2166    536  -1351       C  
ATOM    462  C   PHE A 119     -13.120 -26.902  43.477  1.00 46.56           C  
ANISOU  462  C   PHE A 119     4670   6487   6533   2107    613  -1359       C  
ATOM    463  O   PHE A 119     -14.209 -26.828  44.044  1.00 47.55           O  
ANISOU  463  O   PHE A 119     4872   6521   6673   2104    620  -1262       O  
ATOM    464  CB  PHE A 119     -11.935 -24.861  44.340  1.00 45.46           C  
ANISOU  464  CB  PHE A 119     4327   6744   6203   1978    517  -1353       C  
ATOM    465  CG  PHE A 119     -10.775 -24.283  45.102  1.00 46.76           C  
ANISOU  465  CG  PHE A 119     4364   7114   6288   2027    427  -1367       C  
ATOM    466  CD1 PHE A 119     -10.793 -24.235  46.486  1.00 48.37           C  
ANISOU  466  CD1 PHE A 119     4584   7362   6433   2165    343  -1268       C  
ATOM    467  CD2 PHE A 119      -9.665 -23.793  44.434  1.00 46.28           C  
ANISOU  467  CD2 PHE A 119     4167   7212   6205   1943    425  -1488       C  
ATOM    468  CE1 PHE A 119      -9.726 -23.707  47.190  1.00 48.75           C  
ANISOU  468  CE1 PHE A 119     4505   7620   6398   2217    241  -1305       C  
ATOM    469  CE2 PHE A 119      -8.595 -23.265  45.132  1.00 47.06           C  
ANISOU  469  CE2 PHE A 119     4127   7512   6243   1984    334  -1522       C  
ATOM    470  CZ  PHE A 119      -8.626 -23.221  46.511  1.00 48.29           C  
ANISOU  470  CZ  PHE A 119     4290   7720   6338   2121    233  -1439       C  
ATOM    471  N   ALA A 120     -12.977 -27.431  42.267  1.00 51.44           N  
ANISOU  471  N   ALA A 120     5307   7036   7202   2064    669  -1486       N  
ATOM    472  CA  ALA A 120     -14.121 -27.979  41.546  1.00 51.76           C  
ANISOU  472  CA  ALA A 120     5459   6881   7326   1999    723  -1539       C  
ATOM    473  C   ALA A 120     -14.045 -29.499  41.443  1.00 53.81           C  
ANISOU  473  C   ALA A 120     5840   6898   7708   2180    745  -1568       C  
ATOM    474  O   ALA A 120     -15.062 -30.184  41.540  1.00 54.51           O  
ANISOU  474  O   ALA A 120     6092   6744   7875   2121    756  -1472       O  
ATOM    475  CB  ALA A 120     -14.236 -27.353  40.163  1.00 49.24           C  
ANISOU  475  CB  ALA A 120     5107   6647   6956   1786    768  -1681       C  
ATOM    476  N   LEU A 121     -12.836 -30.018  41.253  1.00 42.60           N  
ANISOU  476  N   LEU A 121     4386   5516   6286   2306    751  -1615       N  
ATOM    477  CA  LEU A 121     -12.629 -31.461  41.117  1.00 44.93           C  
ANISOU  477  CA  LEU A 121     4807   5571   6696   2491    782  -1644       C  
ATOM    478  C   LEU A 121     -13.046 -32.285  42.347  1.00 45.94           C  
ANISOU  478  C   LEU A 121     5061   5491   6905   2687    742  -1477       C  
ATOM    479  O   LEU A 121     -13.738 -33.289  42.194  1.00 46.80           O  
ANISOU  479  O   LEU A 121     5351   5307   7125   2720    776  -1471       O  
ATOM    480  CB  LEU A 121     -11.185 -31.777  40.688  1.00 46.84           C  
ANISOU  480  CB  LEU A 121     4957   5914   6925   2599    805  -1723       C  
ATOM    481  CG  LEU A 121     -10.834 -33.217  40.295  1.00 49.54           C  
ANISOU  481  CG  LEU A 121     5425   6019   7382   2779    863  -1785       C  
ATOM    482  CD1 LEU A 121      -9.772 -33.221  39.207  1.00 50.80           C  
ANISOU  482  CD1 LEU A 121     5493   6304   7504   2768    936  -1940       C  
ATOM    483  CD2 LEU A 121     -10.356 -34.028  41.494  1.00 51.49           C  
ANISOU  483  CD2 LEU A 121     5702   6156   7708   3038    807  -1638       C  
ATOM    484  N   PRO A 122     -12.622 -31.881  43.564  1.00 45.89           N  
ANISOU  484  N   PRO A 122     4986   5619   6832   2789    667  -1327       N  
ATOM    485  CA  PRO A 122     -13.049 -32.672  44.727  1.00 47.08           C  
ANISOU  485  CA  PRO A 122     5294   5569   7026   2976    635  -1141       C  
ATOM    486  C   PRO A 122     -14.562 -32.650  44.943  1.00 44.94           C  
ANISOU  486  C   PRO A 122     5180   5116   6780   2782    679  -1007       C  
ATOM    487  O   PRO A 122     -15.160 -33.692  45.222  1.00 45.87           O  
ANISOU  487  O   PRO A 122     5496   4940   6994   2818    716   -896       O  
ATOM    488  CB  PRO A 122     -12.344 -31.980  45.897  1.00 47.02           C  
ANISOU  488  CB  PRO A 122     5169   5800   6895   3054    534  -1026       C  
ATOM    489  CG  PRO A 122     -11.169 -31.310  45.285  1.00 46.94           C  
ANISOU  489  CG  PRO A 122     4948   6050   6837   2983    513  -1172       C  
ATOM    490  CD  PRO A 122     -11.650 -30.842  43.949  1.00 45.32           C  
ANISOU  490  CD  PRO A 122     4719   5858   6643   2755    603  -1322       C  
ATOM    491  N   VAL A 123     -15.165 -31.472  44.812  1.00 43.49           N  
ANISOU  491  N   VAL A 123     4908   5098   6519   2548    682  -1004       N  
ATOM    492  CA  VAL A 123     -16.607 -31.322  44.977  1.00 42.40           C  
ANISOU  492  CA  VAL A 123     4874   4824   6411   2325    727   -873       C  
ATOM    493  C   VAL A 123     -17.352 -32.156  43.938  1.00 43.06           C  
ANISOU  493  C   VAL A 123     5073   4659   6629   2182    781   -950       C  
ATOM    494  O   VAL A 123     -18.412 -32.719  44.218  1.00 43.57           O  
ANISOU  494  O   VAL A 123     5274   4499   6781   2080    822   -824       O  
ATOM    495  CB  VAL A 123     -17.032 -29.847  44.848  1.00 39.93           C  
ANISOU  495  CB  VAL A 123     4429   4741   6000   2117    719   -887       C  
ATOM    496  CG1 VAL A 123     -18.496 -29.680  45.216  1.00 39.13           C  
ANISOU  496  CG1 VAL A 123     4411   4517   5939   1931    766   -730       C  
ATOM    497  CG2 VAL A 123     -16.158 -28.966  45.727  1.00 39.46           C  
ANISOU  497  CG2 VAL A 123     4250   4939   5804   2236    658   -863       C  
ATOM    498  N   ASP A 124     -16.780 -32.237  42.741  1.00 49.37           N  
ANISOU  498  N   ASP A 124     5817   5503   7439   2168    785  -1166       N  
ATOM    499  CA  ASP A 124     -17.369 -33.004  41.651  1.00 50.22           C  
ANISOU  499  CA  ASP A 124     6038   5397   7647   2030    823  -1280       C  
ATOM    500  C   ASP A 124     -17.286 -34.498  41.939  1.00 52.85           C  
ANISOU  500  C   ASP A 124     6563   5408   8109   2191    856  -1239       C  
ATOM    501  O   ASP A 124     -18.304 -35.189  41.961  1.00 53.65           O  
ANISOU  501  O   ASP A 124     6816   5250   8317   2059    887  -1162       O  
ATOM    502  CB  ASP A 124     -16.654 -32.683  40.337  1.00 50.09           C  
ANISOU  502  CB  ASP A 124     5928   5528   7575   1999    832  -1527       C  
ATOM    503  CG  ASP A 124     -17.434 -33.136  39.112  1.00 50.58           C  
ANISOU  503  CG  ASP A 124     6097   5431   7689   1791    852  -1659       C  
ATOM    504  OD1 ASP A 124     -18.089 -34.198  39.164  1.00 52.09           O  
ANISOU  504  OD1 ASP A 124     6458   5329   8004   1759    869  -1620       O  
ATOM    505  OD2 ASP A 124     -17.386 -32.422  38.089  1.00 49.64           O  
ANISOU  505  OD2 ASP A 124     5901   5480   7480   1650    849  -1803       O  
ATOM    506  N   VAL A 125     -16.071 -34.991  42.157  1.00 46.07           N  
ANISOU  506  N   VAL A 125     5693   4564   7249   2478    850  -1291       N  
ATOM    507  CA  VAL A 125     -15.853 -36.415  42.391  1.00 49.08           C  
ANISOU  507  CA  VAL A 125     6267   4628   7753   2676    881  -1262       C  
ATOM    508  C   VAL A 125     -16.616 -36.898  43.624  1.00 49.44           C  
ANISOU  508  C   VAL A 125     6472   4466   7846   2687    889   -992       C  
ATOM    509  O   VAL A 125     -17.030 -38.053  43.690  1.00 51.50           O  
ANISOU  509  O   VAL A 125     6945   4386   8235   2692    939   -940       O  
ATOM    510  CB  VAL A 125     -14.344 -36.766  42.498  1.00 52.24           C  
ANISOU  510  CB  VAL A 125     6592   5114   8142   3024    862  -1348       C  
ATOM    511  CG1 VAL A 125     -13.729 -36.166  43.750  1.00 52.29           C  
ANISOU  511  CG1 VAL A 125     6471   5352   8046   3204    783  -1191       C  
ATOM    512  CG2 VAL A 125     -14.140 -38.272  42.473  1.00 55.83           C  
ANISOU  512  CG2 VAL A 125     7267   5208   8739   3230    905  -1348       C  
ATOM    513  N   TYR A 126     -16.830 -36.008  44.588  1.00 47.77           N  
ANISOU  513  N   TYR A 126     6171   4451   7528   2676    853   -826       N  
ATOM    514  CA  TYR A 126     -17.609 -36.371  45.765  1.00 48.18           C  
ANISOU  514  CA  TYR A 126     6375   4335   7599   2671    882   -564       C  
ATOM    515  C   TYR A 126     -19.112 -36.336  45.500  1.00 46.44           C  
ANISOU  515  C   TYR A 126     6215   3969   7460   2342    948   -507       C  
ATOM    516  O   TYR A 126     -19.774 -37.372  45.505  1.00 48.16           O  
ANISOU  516  O   TYR A 126     6621   3864   7814   2278   1012   -439       O  
ATOM    517  CB  TYR A 126     -17.271 -35.470  46.956  1.00 47.35           C  
ANISOU  517  CB  TYR A 126     6171   4489   7332   2778    827   -414       C  
ATOM    518  CG  TYR A 126     -18.226 -35.634  48.119  1.00 47.37           C  
ANISOU  518  CG  TYR A 126     6322   4355   7321   2723    882   -149       C  
ATOM    519  CD1 TYR A 126     -18.164 -36.751  48.942  1.00 50.44           C  
ANISOU  519  CD1 TYR A 126     6932   4483   7750   2909    910     31       C  
ATOM    520  CD2 TYR A 126     -19.193 -34.673  48.392  1.00 44.63           C  
ANISOU  520  CD2 TYR A 126     5903   4134   6922   2490    919    -74       C  
ATOM    521  CE1 TYR A 126     -19.037 -36.907  50.003  1.00 50.74           C  
ANISOU  521  CE1 TYR A 126     7118   4396   7764   2848    984    281       C  
ATOM    522  CE2 TYR A 126     -20.070 -34.821  49.449  1.00 44.89           C  
ANISOU  522  CE2 TYR A 126     6064   4051   6941   2438    997    162       C  
ATOM    523  CZ  TYR A 126     -19.988 -35.939  50.251  1.00 47.92           C  
ANISOU  523  CZ  TYR A 126     6670   4184   7353   2609   1035    341       C  
ATOM    524  OH  TYR A 126     -20.859 -36.088  51.306  1.00 48.42           O  
ANISOU  524  OH  TYR A 126     6872   4136   7391   2547   1134    584       O  
ATOM    525  N   ASN A 127     -19.639 -35.140  45.254  1.00 49.31           N  
ANISOU  525  N   ASN A 127     6414   4570   7752   2134    932   -537       N  
ATOM    526  CA  ASN A 127     -21.083 -34.921  45.277  1.00 48.58           C  
ANISOU  526  CA  ASN A 127     6333   4400   7726   1852    985   -441       C  
ATOM    527  C   ASN A 127     -21.797 -35.065  43.934  1.00 48.43           C  
ANISOU  527  C   ASN A 127     6295   4296   7810   1596    981   -611       C  
ATOM    528  O   ASN A 127     -22.982 -34.748  43.824  1.00 48.20           O  
ANISOU  528  O   ASN A 127     6226   4250   7839   1353   1002   -552       O  
ATOM    529  CB  ASN A 127     -21.390 -33.546  45.877  1.00 46.65           C  
ANISOU  529  CB  ASN A 127     5936   4437   7354   1782    973   -351       C  
ATOM    530  CG  ASN A 127     -22.642 -33.549  46.732  1.00 47.30           C  
ANISOU  530  CG  ASN A 127     6075   4414   7484   1644   1060   -135       C  
ATOM    531  OD1 ASN A 127     -23.571 -34.321  46.496  1.00 48.60           O  
ANISOU  531  OD1 ASN A 127     6330   4337   7801   1486   1120    -93       O  
ATOM    532  ND2 ASN A 127     -22.670 -32.683  47.737  1.00 46.55           N  
ANISOU  532  ND2 ASN A 127     5924   4502   7260   1696   1074     -5       N  
ATOM    533  N   PHE A 128     -21.092 -35.545  42.916  1.00 52.87           N  
ANISOU  533  N   PHE A 128     6884   4815   8392   1653    952   -823       N  
ATOM    534  CA  PHE A 128     -21.700 -35.669  41.595  1.00 53.27           C  
ANISOU  534  CA  PHE A 128     6932   4806   8504   1414    932  -1002       C  
ATOM    535  C   PHE A 128     -21.635 -37.073  41.000  1.00 55.28           C  
ANISOU  535  C   PHE A 128     7385   4731   8890   1425    961  -1120       C  
ATOM    536  O   PHE A 128     -22.530 -37.474  40.256  1.00 56.79           O  
ANISOU  536  O   PHE A 128     7639   4759   9182   1182    958  -1182       O  
ATOM    537  CB  PHE A 128     -21.113 -34.640  40.624  1.00 52.55           C  
ANISOU  537  CB  PHE A 128     6677   5015   8277   1383    875  -1189       C  
ATOM    538  CG  PHE A 128     -21.657 -33.252  40.815  1.00 51.20           C  
ANISOU  538  CG  PHE A 128     6336   5104   8015   1243    844  -1106       C  
ATOM    539  CD1 PHE A 128     -22.976 -33.058  41.191  1.00 53.19           C  
ANISOU  539  CD1 PHE A 128     6573   5296   8341   1049    855   -958       C  
ATOM    540  CD2 PHE A 128     -20.850 -32.143  40.624  1.00 48.78           C  
ANISOU  540  CD2 PHE A 128     5882   5093   7559   1305    812  -1179       C  
ATOM    541  CE1 PHE A 128     -23.481 -31.784  41.370  1.00 52.53           C  
ANISOU  541  CE1 PHE A 128     6338   5438   8183    946    834   -884       C  
ATOM    542  CE2 PHE A 128     -21.350 -30.867  40.802  1.00 48.08           C  
ANISOU  542  CE2 PHE A 128     5663   5213   7394   1183    789  -1104       C  
ATOM    543  CZ  PHE A 128     -22.667 -30.688  41.176  1.00 49.88           C  
ANISOU  543  CZ  PHE A 128     5884   5373   7696   1017    799   -957       C  
ATOM    544  N   ILE A 129     -20.587 -37.823  41.320  1.00 76.53           N  
ANISOU  544  N   ILE A 129    10172   7320  11585   1705    984  -1159       N  
ATOM    545  CA  ILE A 129     -20.470 -39.177  40.789  1.00 77.71           C  
ANISOU  545  CA  ILE A 129    10534   7128  11864   1745   1024  -1277       C  
ATOM    546  C   ILE A 129     -20.552 -40.250  41.874  1.00 79.06           C  
ANISOU  546  C   ILE A 129    10914   6969  12158   1867   1087  -1070       C  
ATOM    547  O   ILE A 129     -20.980 -41.372  41.606  1.00 79.73           O  
ANISOU  547  O   ILE A 129    11198   6707  12391   1763   1132  -1099       O  
ATOM    548  CB  ILE A 129     -19.189 -39.367  39.939  1.00 74.59           C  
ANISOU  548  CB  ILE A 129    10131   6796  11416   1970   1024  -1510       C  
ATOM    549  CG1 ILE A 129     -17.929 -39.247  40.799  1.00 74.33           C  
ANISOU  549  CG1 ILE A 129    10029   6893  11320   2326   1019  -1414       C  
ATOM    550  CG2 ILE A 129     -19.159 -38.362  38.799  1.00 72.98           C  
ANISOU  550  CG2 ILE A 129     9759   6884  11086   1815    983  -1716       C  
ATOM    551  CD1 ILE A 129     -16.657 -39.587  40.059  1.00 74.81           C  
ANISOU  551  CD1 ILE A 129    10071   6988  11365   2577   1038  -1630       C  
ATOM    552  N   TRP A 130     -20.146 -39.903  43.093  1.00 53.19           N  
ANISOU  552  N   TRP A 130     7606   3792   8811   2079   1088   -862       N  
ATOM    553  CA  TRP A 130     -20.166 -40.853  44.202  1.00 55.89           C  
ANISOU  553  CA  TRP A 130     8161   3839   9237   2205   1149   -630       C  
ATOM    554  C   TRP A 130     -21.451 -40.763  45.026  1.00 54.67           C  
ANISOU  554  C   TRP A 130     8022   3626   9125   1944   1204   -416       C  
ATOM    555  O   TRP A 130     -22.154 -41.762  45.195  1.00 55.94           O  
ANISOU  555  O   TRP A 130     8302   3515   9437   1707   1260   -416       O  
ATOM    556  CB  TRP A 130     -18.919 -40.696  45.086  1.00 56.99           C  
ANISOU  556  CB  TRP A 130     8285   4103   9266   2578   1114   -503       C  
ATOM    557  CG  TRP A 130     -17.718 -41.448  44.568  1.00 59.85           C  
ANISOU  557  CG  TRP A 130     8691   4396   9652   2884   1090   -664       C  
ATOM    558  CD1 TRP A 130     -16.592 -40.916  44.011  1.00 59.17           C  
ANISOU  558  CD1 TRP A 130     8402   4608   9470   3047   1030   -845       C  
ATOM    559  CD2 TRP A 130     -17.534 -42.870  44.560  1.00 64.19           C  
ANISOU  559  CD2 TRP A 130     9500   4549  10341   3066   1142   -660       C  
ATOM    560  NE1 TRP A 130     -15.715 -41.916  43.662  1.00 62.79           N  
ANISOU  560  NE1 TRP A 130     8957   4899  10001   3330   1043   -957       N  
ATOM    561  CE2 TRP A 130     -16.270 -43.125  43.988  1.00 65.74           C  
ANISOU  561  CE2 TRP A 130     9613   4852  10513   3342   1096   -848       C  
ATOM    562  CE3 TRP A 130     -18.313 -43.951  44.983  1.00 67.10           C  
ANISOU  562  CE3 TRP A 130    10157   4483  10855   3009   1223   -515       C  
ATOM    563  CZ2 TRP A 130     -15.770 -44.414  43.829  1.00 69.20           C  
ANISOU  563  CZ2 TRP A 130    10194   5052  11047   3506   1074   -901       C  
ATOM    564  CZ3 TRP A 130     -17.814 -45.231  44.823  1.00 70.86           C  
ANISOU  564  CZ3 TRP A 130    10819   4686  11419   3196   1213   -565       C  
ATOM    565  CH2 TRP A 130     -16.555 -45.451  44.251  1.00 71.70           C  
ANISOU  565  CH2 TRP A 130    10799   4959  11486   3440   1128   -758       C  
ATOM    566  N   VAL A 131     -21.766 -39.569  45.518  1.00 52.52           N  
ANISOU  566  N   VAL A 131     7622   3609   8722   1981   1193   -246       N  
ATOM    567  CA  VAL A 131     -23.027 -39.344  46.221  1.00 51.37           C  
ANISOU  567  CA  VAL A 131     7464   3447   8606   1749   1265    -48       C  
ATOM    568  C   VAL A 131     -23.846 -38.233  45.560  1.00 47.84           C  
ANISOU  568  C   VAL A 131     6786   3253   8141   1471   1227   -157       C  
ATOM    569  O   VAL A 131     -23.455 -37.068  45.549  1.00 45.28           O  
ANISOU  569  O   VAL A 131     6277   3257   7672   1523   1161   -219       O  
ATOM    570  CB  VAL A 131     -22.809 -39.076  47.727  1.00 51.49           C  
ANISOU  570  CB  VAL A 131     7510   3567   8488   1933   1296    212       C  
ATOM    571  CG1 VAL A 131     -21.677 -38.088  47.931  1.00 49.90           C  
ANISOU  571  CG1 VAL A 131     7148   3719   8094   2165   1189    144       C  
ATOM    572  CG2 VAL A 131     -24.090 -38.584  48.381  1.00 49.85           C  
ANISOU  572  CG2 VAL A 131     7236   3421   8285   1689   1383    380       C  
ATOM    573  N   HIS A 132     -24.984 -38.614  44.992  1.00 77.41           N  
ANISOU  573  N   HIS A 132    10542   6833  12037   1172   1265   -180       N  
ATOM    574  CA  HIS A 132     -25.788 -37.695  44.200  1.00 77.43           C  
ANISOU  574  CA  HIS A 132    10334   7045  12041    911   1210   -289       C  
ATOM    575  C   HIS A 132     -26.735 -36.883  45.074  1.00 76.84           C  
ANISOU  575  C   HIS A 132    10128   7122  11946    793   1269    -89       C  
ATOM    576  O   HIS A 132     -27.229 -35.835  44.660  1.00 76.55           O  
ANISOU  576  O   HIS A 132     9890   7328  11866    659   1218   -143       O  
ATOM    577  CB  HIS A 132     -26.560 -38.466  43.130  1.00 81.46           C  
ANISOU  577  CB  HIS A 132    10899   7329  12721    645   1193   -437       C  
ATOM    578  CG  HIS A 132     -25.686 -39.316  42.261  1.00 81.99           C  
ANISOU  578  CG  HIS A 132    11115   7229  12807    752   1151   -655       C  
ATOM    579  ND1 HIS A 132     -25.357 -38.967  40.969  1.00 81.12           N  
ANISOU  579  ND1 HIS A 132    10926   7260  12636    689   1055   -913       N  
ATOM    580  CD2 HIS A 132     -25.061 -40.493  42.504  1.00 83.34           C  
ANISOU  580  CD2 HIS A 132    11520   7100  13045    932   1203   -654       C  
ATOM    581  CE1 HIS A 132     -24.574 -39.896  40.451  1.00 82.06           C  
ANISOU  581  CE1 HIS A 132    11217   7179  12783    821   1060  -1073       C  
ATOM    582  NE2 HIS A 132     -24.377 -40.832  41.362  1.00 83.30           N  
ANISOU  582  NE2 HIS A 132    11562   7061  13027    978   1146   -922       N  
ATOM    583  N   HIS A 133     -26.979 -37.372  46.286  1.00 65.58           N  
ANISOU  583  N   HIS A 133     8828   5544  10548    853   1386    146       N  
ATOM    584  CA  HIS A 133     -27.860 -36.690  47.227  1.00 65.74           C  
ANISOU  584  CA  HIS A 133     8749   5689  10542    764   1478    347       C  
ATOM    585  C   HIS A 133     -27.616 -37.194  48.647  1.00 65.69           C  
ANISOU  585  C   HIS A 133     8933   5553  10474    948   1594    594       C  
ATOM    586  O   HIS A 133     -27.347 -38.379  48.848  1.00 67.36           O  
ANISOU  586  O   HIS A 133     9368   5467  10759   1026   1638    652       O  
ATOM    587  CB  HIS A 133     -29.326 -36.896  46.835  1.00 65.84           C  
ANISOU  587  CB  HIS A 133     8671   5595  10750    426   1535    366       C  
ATOM    588  CG  HIS A 133     -29.780 -38.320  46.914  1.00 67.89           C  
ANISOU  588  CG  HIS A 133     9129   5467  11198    307   1626    430       C  
ATOM    589  ND1 HIS A 133     -29.443 -39.262  45.966  1.00 68.65           N  
ANISOU  589  ND1 HIS A 133     9350   5336  11399    260   1559    248       N  
ATOM    590  CD2 HIS A 133     -30.547 -38.962  47.826  1.00 69.23           C  
ANISOU  590  CD2 HIS A 133     9411   5425  11470    219   1792    655       C  
ATOM    591  CE1 HIS A 133     -29.981 -40.424  46.293  1.00 70.20           C  
ANISOU  591  CE1 HIS A 133     9729   5181  11762    144   1671    354       C  
ATOM    592  NE2 HIS A 133     -30.657 -40.268  47.417  1.00 70.66           N  
ANISOU  592  NE2 HIS A 133     9781   5243  11824    111   1817    609       N  
ATOM    593  N   PRO A 134     -27.709 -36.296  49.640  1.00 61.45           N  
ANISOU  593  N   PRO A 134     8327   5231   9790   1024   1645    743       N  
ATOM    594  CA  PRO A 134     -28.019 -34.875  49.455  1.00 61.00           C  
ANISOU  594  CA  PRO A 134     8028   5500   9648    948   1605    680       C  
ATOM    595  C   PRO A 134     -26.771 -34.030  49.217  1.00 59.31           C  
ANISOU  595  C   PRO A 134     7740   5547   9249   1155   1465    536       C  
ATOM    596  O   PRO A 134     -25.658 -34.477  49.491  1.00 58.47           O  
ANISOU  596  O   PRO A 134     7757   5402   9056   1390   1414    527       O  
ATOM    597  CB  PRO A 134     -28.646 -34.496  50.793  1.00 62.46           C  
ANISOU  597  CB  PRO A 134     8234   5738   9759    958   1756    920       C  
ATOM    598  CG  PRO A 134     -27.925 -35.350  51.774  1.00 62.88           C  
ANISOU  598  CG  PRO A 134     8543   5626   9722   1184   1801   1075       C  
ATOM    599  CD  PRO A 134     -27.642 -36.657  51.067  1.00 63.19           C  
ANISOU  599  CD  PRO A 134     8730   5362   9916   1177   1764    998       C  
ATOM    600  N   TRP A 135     -26.966 -32.818  48.707  1.00 55.03           N  
ANISOU  600  N   TRP A 135     6993   5261   8655   1066   1406    428       N  
ATOM    601  CA  TRP A 135     -25.869 -31.878  48.514  1.00 52.89           C  
ANISOU  601  CA  TRP A 135     6635   5249   8211   1221   1293    299       C  
ATOM    602  C   TRP A 135     -25.376 -31.378  49.867  1.00 52.39           C  
ANISOU  602  C   TRP A 135     6626   5316   7964   1416   1327    442       C  
ATOM    603  O   TRP A 135     -26.162 -30.899  50.686  1.00 53.02           O  
ANISOU  603  O   TRP A 135     6697   5436   8012   1361   1431    592       O  
ATOM    604  CB  TRP A 135     -26.322 -30.706  47.641  1.00 51.76           C  
ANISOU  604  CB  TRP A 135     6286   5315   8065   1057   1238    175       C  
ATOM    605  CG  TRP A 135     -25.283 -29.642  47.452  1.00 49.29           C  
ANISOU  605  CG  TRP A 135     5882   5265   7583   1177   1144     53       C  
ATOM    606  CD1 TRP A 135     -25.173 -28.473  48.146  1.00 48.52           C  
ANISOU  606  CD1 TRP A 135     5715   5377   7344   1230   1155    101       C  
ATOM    607  CD2 TRP A 135     -24.208 -29.648  46.504  1.00 47.79           C  
ANISOU  607  CD2 TRP A 135     5664   5147   7349   1245   1038   -145       C  
ATOM    608  NE1 TRP A 135     -24.098 -27.751  47.690  1.00 46.26           N  
ANISOU  608  NE1 TRP A 135     5355   5283   6939   1310   1056    -52       N  
ATOM    609  CE2 TRP A 135     -23.488 -28.450  46.682  1.00 45.67           C  
ANISOU  609  CE2 TRP A 135     5295   5137   6921   1322    990   -200       C  
ATOM    610  CE3 TRP A 135     -23.785 -30.549  45.522  1.00 48.29           C  
ANISOU  610  CE3 TRP A 135     5780   5077   7492   1244    992   -289       C  
ATOM    611  CZ2 TRP A 135     -22.369 -28.130  45.916  1.00 44.01           C  
ANISOU  611  CZ2 TRP A 135     5020   5066   6638   1386    906   -382       C  
ATOM    612  CZ3 TRP A 135     -22.673 -30.230  44.763  1.00 46.67           C  
ANISOU  612  CZ3 TRP A 135     5515   5016   7203   1328    915   -473       C  
ATOM    613  CH2 TRP A 135     -21.979 -29.031  44.964  1.00 44.62           C  
ANISOU  613  CH2 TRP A 135     5138   5023   6792   1393    876   -513       C  
ATOM    614  N   ALA A 136     -24.073 -31.493  50.100  1.00 48.25           N  
ANISOU  614  N   ALA A 136     6153   4864   7315   1646   1238    389       N  
ATOM    615  CA  ALA A 136     -23.498 -31.155  51.398  1.00 48.04           C  
ANISOU  615  CA  ALA A 136     6198   4954   7099   1846   1239    517       C  
ATOM    616  C   ALA A 136     -22.489 -30.013  51.318  1.00 45.74           C  
ANISOU  616  C   ALA A 136     5769   4966   6644   1941   1122    377       C  
ATOM    617  O   ALA A 136     -21.358 -30.142  51.788  1.00 45.64           O  
ANISOU  617  O   ALA A 136     5792   5036   6511   2158   1035    366       O  
ATOM    618  CB  ALA A 136     -22.857 -32.385  52.027  1.00 47.99           C  
ANISOU  618  CB  ALA A 136     6394   4757   7083   2061   1230    624       C  
ATOM    619  N   PHE A 137     -22.900 -28.897  50.723  1.00 42.19           N  
ANISOU  619  N   PHE A 137     5159   4678   6196   1778   1116    274       N  
ATOM    620  CA  PHE A 137     -22.040 -27.720  50.630  1.00 40.62           C  
ANISOU  620  CA  PHE A 137     4834   4749   5852   1827   1024    143       C  
ATOM    621  C   PHE A 137     -22.843 -26.430  50.772  1.00 39.06           C  
ANISOU  621  C   PHE A 137     4546   4686   5611   1681   1079    158       C  
ATOM    622  O   PHE A 137     -22.281 -25.335  50.788  1.00 37.85           O  
ANISOU  622  O   PHE A 137     4305   4738   5338   1693   1022     62       O  
ATOM    623  CB  PHE A 137     -21.256 -27.719  49.315  1.00 39.89           C  
ANISOU  623  CB  PHE A 137     4632   4715   5809   1811    929    -72       C  
ATOM    624  CG  PHE A 137     -20.340 -28.898  49.155  1.00 41.56           C  
ANISOU  624  CG  PHE A 137     4918   4810   6063   1986    879   -111       C  
ATOM    625  CD1 PHE A 137     -19.081 -28.897  49.733  1.00 42.33           C  
ANISOU  625  CD1 PHE A 137     5006   5036   6042   2211    793   -133       C  
ATOM    626  CD2 PHE A 137     -20.738 -30.009  48.431  1.00 42.61           C  
ANISOU  626  CD2 PHE A 137     5128   4704   6360   1930    912   -133       C  
ATOM    627  CE1 PHE A 137     -18.237 -29.981  49.590  1.00 44.12           C  
ANISOU  627  CE1 PHE A 137     5291   5155   6320   2401    747   -166       C  
ATOM    628  CE2 PHE A 137     -19.898 -31.097  48.285  1.00 44.38           C  
ANISOU  628  CE2 PHE A 137     5435   4798   6629   2110    877   -174       C  
ATOM    629  CZ  PHE A 137     -18.646 -31.082  48.865  1.00 45.14           C  
ANISOU  629  CZ  PHE A 137     5513   5024   6614   2358    798   -185       C  
ATOM    630  N   GLY A 138     -24.161 -26.567  50.873  1.00 42.48           N  
ANISOU  630  N   GLY A 138     4995   4994   6151   1543   1194    274       N  
ATOM    631  CA  GLY A 138     -25.032 -25.425  51.084  1.00 41.48           C  
ANISOU  631  CA  GLY A 138     4784   4973   6003   1430   1265    308       C  
ATOM    632  C   GLY A 138     -25.319 -24.628  49.826  1.00 38.92           C  
ANISOU  632  C   GLY A 138     4302   4731   5752   1278   1209    165       C  
ATOM    633  O   GLY A 138     -24.829 -24.952  48.744  1.00 38.21           O  
ANISOU  633  O   GLY A 138     4172   4627   5718   1243   1119     31       O  
ATOM    634  N   ASP A 139     -26.118 -23.577  49.979  1.00 52.35           N  
ANISOU  634  N   ASP A 139     5927   6518   7444   1198   1269    197       N  
ATOM    635  CA  ASP A 139     -26.508 -22.724  48.864  1.00 49.66           C  
ANISOU  635  CA  ASP A 139     5451   6254   7163   1064   1218     93       C  
ATOM    636  C   ASP A 139     -25.302 -21.958  48.327  1.00 46.89           C  
ANISOU  636  C   ASP A 139     5069   6058   6686   1105   1108    -70       C  
ATOM    637  O   ASP A 139     -25.122 -21.823  47.113  1.00 45.87           O  
ANISOU  637  O   ASP A 139     4875   5955   6599   1019   1030   -189       O  
ATOM    638  CB  ASP A 139     -27.598 -21.747  49.313  1.00 50.34           C  
ANISOU  638  CB  ASP A 139     5474   6387   7264   1012   1319    183       C  
ATOM    639  CG  ASP A 139     -28.342 -21.125  48.149  1.00 48.80           C  
ANISOU  639  CG  ASP A 139     5139   6222   7181    871   1273    127       C  
ATOM    640  OD1 ASP A 139     -28.433 -21.772  47.086  1.00 49.81           O  
ANISOU  640  OD1 ASP A 139     5226   6285   7414    775   1192     64       O  
ATOM    641  OD2 ASP A 139     -28.844 -19.990  48.302  1.00 46.44           O  
ANISOU  641  OD2 ASP A 139     4782   6005   6858    864   1314    147       O  
ATOM    642  N   ALA A 140     -24.474 -21.468  49.244  1.00 27.58           N  
ANISOU  642  N   ALA A 140     2676   3721   4080   1227   1103    -75       N  
ATOM    643  CA  ALA A 140     -23.285 -20.700  48.891  1.00 27.15           C  
ANISOU  643  CA  ALA A 140     2582   3826   3910   1256   1010   -228       C  
ATOM    644  C   ALA A 140     -22.268 -21.549  48.137  1.00 27.33           C  
ANISOU  644  C   ALA A 140     2589   3838   3957   1299    922   -339       C  
ATOM    645  O   ALA A 140     -21.664 -21.092  47.168  1.00 26.88           O  
ANISOU  645  O   ALA A 140     2457   3870   3884   1241    863   -480       O  
ATOM    646  CB  ALA A 140     -22.655 -20.099  50.138  1.00 27.76           C  
ANISOU  646  CB  ALA A 140     2717   4017   3813   1371   1012   -212       C  
ATOM    647  N   GLY A 141     -22.077 -22.784  48.590  1.00 37.80           N  
ANISOU  647  N   GLY A 141     3995   5048   5320   1406    926   -272       N  
ATOM    648  CA  GLY A 141     -21.190 -23.709  47.910  1.00 38.21           C  
ANISOU  648  CA  GLY A 141     4043   5061   5412   1474    860   -373       C  
ATOM    649  C   GLY A 141     -21.752 -24.080  46.552  1.00 38.05           C  
ANISOU  649  C   GLY A 141     3988   4942   5525   1328    857   -449       C  
ATOM    650  O   GLY A 141     -21.022 -24.133  45.557  1.00 37.36           O  
ANISOU  650  O   GLY A 141     3850   4908   5435   1315    804   -602       O  
ATOM    651  N   CYS A 142     -23.059 -24.325  46.518  1.00 40.81           N  
ANISOU  651  N   CYS A 142     4360   5159   5986   1213    916   -345       N  
ATOM    652  CA  CYS A 142     -23.757 -24.681  45.287  1.00 41.43           C  
ANISOU  652  CA  CYS A 142     4405   5146   6188   1053    897   -408       C  
ATOM    653  C   CYS A 142     -23.570 -23.627  44.202  1.00 39.38           C  
ANISOU  653  C   CYS A 142     4051   5040   5871    951    838   -539       C  
ATOM    654  O   CYS A 142     -23.197 -23.947  43.075  1.00 39.52           O  
ANISOU  654  O   CYS A 142     4061   5054   5899    902    787   -674       O  
ATOM    655  CB  CYS A 142     -25.250 -24.884  45.560  1.00 43.93           C  
ANISOU  655  CB  CYS A 142     4717   5342   6630    935    966   -265       C  
ATOM    656  SG  CYS A 142     -26.234 -25.270  44.095  1.00 46.19           S  
ANISOU  656  SG  CYS A 142     4945   5531   7072    719    914   -335       S  
ATOM    657  N   LYS A 143     -23.824 -22.369  44.548  1.00 26.09           N  
ANISOU  657  N   LYS A 143     2315   3482   4118    923    856   -498       N  
ATOM    658  CA  LYS A 143     -23.722 -21.280  43.579  1.00 25.42           C  
ANISOU  658  CA  LYS A 143     2162   3521   3974    823    811   -593       C  
ATOM    659  C   LYS A 143     -22.270 -20.923  43.253  1.00 25.78           C  
ANISOU  659  C   LYS A 143     2191   3703   3899    877    775   -737       C  
ATOM    660  O   LYS A 143     -21.916 -20.712  42.086  1.00 25.70           O  
ANISOU  660  O   LYS A 143     2156   3747   3861    797    738   -854       O  
ATOM    661  CB  LYS A 143     -24.487 -20.053  44.079  1.00 24.96           C  
ANISOU  661  CB  LYS A 143     2069   3523   3894    786    852   -499       C  
ATOM    662  CG  LYS A 143     -25.968 -20.316  44.315  1.00 25.14           C  
ANISOU  662  CG  LYS A 143     2065   3436   4052    724    898   -363       C  
ATOM    663  CD  LYS A 143     -26.709 -19.060  44.742  1.00 25.11           C  
ANISOU  663  CD  LYS A 143     2013   3494   4032    709    947   -284       C  
ATOM    664  CE  LYS A 143     -28.208 -19.309  44.820  1.00 25.73           C  
ANISOU  664  CE  LYS A 143     2022   3487   4268    641    992   -161       C  
ATOM    665  NZ  LYS A 143     -28.973 -18.055  45.064  1.00 26.02           N  
ANISOU  665  NZ  LYS A 143     1997   3583   4305    643   1038    -96       N  
ATOM    666  N   GLY A 144     -21.434 -20.867  44.285  1.00 39.73           N  
ANISOU  666  N   GLY A 144     3969   5536   5590   1010    786   -727       N  
ATOM    667  CA  GLY A 144     -20.029 -20.538  44.122  1.00 38.52           C  
ANISOU  667  CA  GLY A 144     3767   5530   5338   1065    751   -861       C  
ATOM    668  C   GLY A 144     -19.288 -21.528  43.244  1.00 38.75           C  
ANISOU  668  C   GLY A 144     3786   5531   5406   1103    727   -982       C  
ATOM    669  O   GLY A 144     -18.364 -21.158  42.518  1.00 37.55           O  
ANISOU  669  O   GLY A 144     3569   5502   5196   1080    716  -1120       O  
ATOM    670  N   TYR A 145     -19.700 -22.790  43.312  1.00 44.04           N  
ANISOU  670  N   TYR A 145     4526   6032   6177   1159    733   -932       N  
ATOM    671  CA  TYR A 145     -19.120 -23.844  42.486  1.00 44.72           C  
ANISOU  671  CA  TYR A 145     4630   6049   6313   1207    722  -1050       C  
ATOM    672  C   TYR A 145     -19.287 -23.545  40.994  1.00 43.95           C  
ANISOU  672  C   TYR A 145     4514   5981   6205   1047    716  -1175       C  
ATOM    673  O   TYR A 145     -18.303 -23.356  40.262  1.00 43.64           O  
ANISOU  673  O   TYR A 145     4422   6058   6101   1054    720  -1322       O  
ATOM    674  CB  TYR A 145     -19.775 -25.181  42.839  1.00 46.98           C  
ANISOU  674  CB  TYR A 145     5026   6105   6721   1262    738   -959       C  
ATOM    675  CG  TYR A 145     -19.372 -26.340  41.961  1.00 48.08           C  
ANISOU  675  CG  TYR A 145     5219   6121   6930   1300    736  -1082       C  
ATOM    676  CD1 TYR A 145     -18.153 -26.979  42.138  1.00 48.01           C  
ANISOU  676  CD1 TYR A 145     5205   6127   6911   1497    732  -1158       C  
ATOM    677  CD2 TYR A 145     -20.222 -26.809  40.970  1.00 49.72           C  
ANISOU  677  CD2 TYR A 145     5481   6194   7216   1147    733  -1128       C  
ATOM    678  CE1 TYR A 145     -17.785 -28.046  41.342  1.00 48.90           C  
ANISOU  678  CE1 TYR A 145     5378   6110   7091   1549    745  -1281       C  
ATOM    679  CE2 TYR A 145     -19.864 -27.874  40.169  1.00 50.77           C  
ANISOU  679  CE2 TYR A 145     5687   6200   7404   1177    737  -1259       C  
ATOM    680  CZ  TYR A 145     -18.645 -28.488  40.359  1.00 50.15           C  
ANISOU  680  CZ  TYR A 145     5616   6124   7317   1384    753  -1336       C  
ATOM    681  OH  TYR A 145     -18.284 -29.551  39.562  1.00 51.49           O  
ANISOU  681  OH  TYR A 145     5868   6152   7544   1432    771  -1477       O  
ATOM    682  N   TYR A 146     -20.542 -23.497  40.555  1.00 49.00           N  
ANISOU  682  N   TYR A 146     5190   6524   6903    903    705  -1114       N  
ATOM    683  CA  TYR A 146     -20.865 -23.231  39.158  1.00 49.06           C  
ANISOU  683  CA  TYR A 146     5201   6554   6886    748    677  -1213       C  
ATOM    684  C   TYR A 146     -20.327 -21.879  38.696  1.00 46.83           C  
ANISOU  684  C   TYR A 146     4856   6464   6471    685    681  -1269       C  
ATOM    685  O   TYR A 146     -19.865 -21.743  37.557  1.00 45.86           O  
ANISOU  685  O   TYR A 146     4739   6408   6276    619    681  -1399       O  
ATOM    686  CB  TYR A 146     -22.377 -23.314  38.931  1.00 49.45           C  
ANISOU  686  CB  TYR A 146     5272   6491   7024    610    642  -1116       C  
ATOM    687  CG  TYR A 146     -22.932 -24.718  39.033  1.00 51.84           C  
ANISOU  687  CG  TYR A 146     5646   6585   7464    614    641  -1096       C  
ATOM    688  CD1 TYR A 146     -22.993 -25.543  37.919  1.00 53.98           C  
ANISOU  688  CD1 TYR A 146     5982   6765   7763    539    605  -1227       C  
ATOM    689  CD2 TYR A 146     -23.393 -25.218  40.243  1.00 53.28           C  
ANISOU  689  CD2 TYR A 146     5850   6653   7741    685    685   -948       C  
ATOM    690  CE1 TYR A 146     -23.499 -26.828  38.006  1.00 56.96           C  
ANISOU  690  CE1 TYR A 146     6440   6926   8274    526    608  -1219       C  
ATOM    691  CE2 TYR A 146     -23.900 -26.501  40.341  1.00 56.77           C  
ANISOU  691  CE2 TYR A 146     6373   6881   8316    672    698   -921       C  
ATOM    692  CZ  TYR A 146     -23.951 -27.301  39.218  1.00 58.46           C  
ANISOU  692  CZ  TYR A 146     6648   6992   8571    588    657  -1060       C  
ATOM    693  OH  TYR A 146     -24.455 -28.580  39.309  1.00 61.73           O  
ANISOU  693  OH  TYR A 146     7157   7170   9126    559    672  -1043       O  
ATOM    694  N   PHE A 147     -20.380 -20.885  39.582  1.00 27.69           N  
ANISOU  694  N   PHE A 147     2389   4120   4010    700    694  -1175       N  
ATOM    695  CA  PHE A 147     -19.820 -19.573  39.271  1.00 27.56           C  
ANISOU  695  CA  PHE A 147     2329   4263   3878    634    708  -1223       C  
ATOM    696  C   PHE A 147     -18.331 -19.687  38.957  1.00 28.95           C  
ANISOU  696  C   PHE A 147     2454   4562   3986    690    737  -1375       C  
ATOM    697  O   PHE A 147     -17.850 -19.132  37.965  1.00 29.24           O  
ANISOU  697  O   PHE A 147     2476   4695   3939    594    760  -1473       O  
ATOM    698  CB  PHE A 147     -20.040 -18.593  40.427  1.00 27.06           C  
ANISOU  698  CB  PHE A 147     2246   4244   3793    658    723  -1114       C  
ATOM    699  CG  PHE A 147     -19.479 -17.221  40.172  1.00 27.02           C  
ANISOU  699  CG  PHE A 147     2214   4373   3679    579    743  -1163       C  
ATOM    700  CD1 PHE A 147     -20.219 -16.271  39.487  1.00 26.14           C  
ANISOU  700  CD1 PHE A 147     2136   4256   3540    455    737  -1121       C  
ATOM    701  CD2 PHE A 147     -18.212 -16.880  40.619  1.00 27.99           C  
ANISOU  701  CD2 PHE A 147     2276   4624   3734    626    762  -1250       C  
ATOM    702  CE1 PHE A 147     -19.707 -15.009  39.250  1.00 26.17           C  
ANISOU  702  CE1 PHE A 147     2142   4354   3449    375    766  -1157       C  
ATOM    703  CE2 PHE A 147     -17.693 -15.621  40.384  1.00 28.06           C  
ANISOU  703  CE2 PHE A 147     2265   4742   3656    526    789  -1300       C  
ATOM    704  CZ  PHE A 147     -18.443 -14.684  39.699  1.00 27.14           C  
ANISOU  704  CZ  PHE A 147     2209   4591   3510    398    799  -1250       C  
ATOM    705  N   LEU A 148     -17.611 -20.412  39.810  1.00 39.81           N  
ANISOU  705  N   LEU A 148     3795   5937   5395    849    739  -1388       N  
ATOM    706  CA  LEU A 148     -16.183 -20.634  39.618  1.00 39.55           C  
ANISOU  706  CA  LEU A 148     3684   6023   5322    928    759  -1522       C  
ATOM    707  C   LEU A 148     -15.909 -21.313  38.282  1.00 40.10           C  
ANISOU  707  C   LEU A 148     3774   6070   5393    898    793  -1663       C  
ATOM    708  O   LEU A 148     -15.031 -20.886  37.528  1.00 39.68           O  
ANISOU  708  O   LEU A 148     3696   6122   5258    823    817  -1738       O  
ATOM    709  CB  LEU A 148     -15.607 -21.481  40.754  1.00 39.64           C  
ANISOU  709  CB  LEU A 148     3686   6001   5376   1119    724  -1469       C  
ATOM    710  CG  LEU A 148     -14.140 -21.885  40.582  1.00 40.01           C  
ANISOU  710  CG  LEU A 148     3677   6126   5399   1193    710  -1546       C  
ATOM    711  CD1 LEU A 148     -13.231 -20.666  40.652  1.00 39.38           C  
ANISOU  711  CD1 LEU A 148     3514   6222   5226   1091    694  -1569       C  
ATOM    712  CD2 LEU A 148     -13.733 -22.929  41.610  1.00 41.43           C  
ANISOU  712  CD2 LEU A 148     3860   6243   5639   1413    672  -1495       C  
ATOM    713  N   ARG A 149     -16.667 -22.370  37.994  1.00 66.54           N  
ANISOU  713  N   ARG A 149     7217   9242   8823    917    776  -1648       N  
ATOM    714  CA  ARG A 149     -16.505 -23.094  36.734  1.00 67.41           C  
ANISOU  714  CA  ARG A 149     7382   9306   8926    884    804  -1791       C  
ATOM    715  C   ARG A 149     -16.690 -22.184  35.518  1.00 66.76           C  
ANISOU  715  C   ARG A 149     7321   9320   8726    695    819  -1849       C  
ATOM    716  O   ARG A 149     -15.847 -22.157  34.614  1.00 66.74           O  
ANISOU  716  O   ARG A 149     7300   9417   8642    676    884  -1996       O  
ATOM    717  CB  ARG A 149     -17.475 -24.274  36.660  1.00 72.09           C  
ANISOU  717  CB  ARG A 149     8095   9669   9628    891    767  -1753       C  
ATOM    718  CG  ARG A 149     -17.227 -25.346  37.705  1.00 73.78           C  
ANISOU  718  CG  ARG A 149     8326   9755   9952   1085    767  -1698       C  
ATOM    719  CD  ARG A 149     -18.088 -26.571  37.449  1.00 76.23           C  
ANISOU  719  CD  ARG A 149     8771   9817  10376   1064    751  -1685       C  
ATOM    720  NE  ARG A 149     -17.800 -27.183  36.155  1.00 77.08           N  
ANISOU  720  NE  ARG A 149     8947   9879  10462   1025    774  -1872       N  
ATOM    721  CZ  ARG A 149     -16.875 -28.116  35.959  1.00 77.74           C  
ANISOU  721  CZ  ARG A 149     9057   9904  10577   1186    824  -1999       C  
ATOM    722  NH1 ARG A 149     -16.141 -28.550  36.976  1.00 78.19           N  
ANISOU  722  NH1 ARG A 149     9070   9945  10692   1404    838  -1948       N  
ATOM    723  NH2 ARG A 149     -16.681 -28.617  34.747  1.00 78.16           N  
ANISOU  723  NH2 ARG A 149     9187   9915  10594   1140    858  -2181       N  
ATOM    724  N   GLU A 150     -17.789 -21.436  35.510  1.00 41.38           N  
ANISOU  724  N   GLU A 150     4147   6076   5499    566    766  -1728       N  
ATOM    725  CA  GLU A 150     -18.099 -20.537  34.402  1.00 41.57           C  
ANISOU  725  CA  GLU A 150     4214   6176   5405    397    762  -1749       C  
ATOM    726  C   GLU A 150     -17.041 -19.449  34.216  1.00 39.81           C  
ANISOU  726  C   GLU A 150     3924   6137   5067    358    837  -1805       C  
ATOM    727  O   GLU A 150     -16.563 -19.218  33.100  1.00 40.42           O  
ANISOU  727  O   GLU A 150     4032   6296   5031    276    892  -1913       O  
ATOM    728  CB  GLU A 150     -19.476 -19.907  34.601  1.00 43.82           C  
ANISOU  728  CB  GLU A 150     4531   6398   5721    304    683  -1588       C  
ATOM    729  CG  GLU A 150     -20.620 -20.890  34.447  1.00 46.43           C  
ANISOU  729  CG  GLU A 150     4919   6566   6157    280    608  -1550       C  
ATOM    730  CD  GLU A 150     -21.038 -21.079  33.004  1.00 48.94           C  
ANISOU  730  CD  GLU A 150     5325   6877   6394    149    553  -1634       C  
ATOM    731  OE1 GLU A 150     -21.095 -20.073  32.265  1.00 48.31           O  
ANISOU  731  OE1 GLU A 150     5269   6899   6187     50    537  -1622       O  
ATOM    732  OE2 GLU A 150     -21.312 -22.233  32.609  1.00 51.31           O  
ANISOU  732  OE2 GLU A 150     5687   7061   6749    143    522  -1713       O  
ATOM    733  N   ALA A 151     -16.680 -18.785  35.310  1.00 42.59           N  
ANISOU  733  N   ALA A 151     4190   6550   5439    406    847  -1736       N  
ATOM    734  CA  ALA A 151     -15.642 -17.762  35.266  1.00 42.39           C  
ANISOU  734  CA  ALA A 151     4092   6687   5326    350    913  -1789       C  
ATOM    735  C   ALA A 151     -14.350 -18.344  34.701  1.00 43.09           C  
ANISOU  735  C   ALA A 151     4155   6826   5391    380    948  -1888       C  
ATOM    736  O   ALA A 151     -13.664 -17.704  33.897  1.00 43.42           O  
ANISOU  736  O   ALA A 151     4196   6961   5340    269   1006  -1938       O  
ATOM    737  CB  ALA A 151     -15.407 -17.183  36.650  1.00 49.24           C  
ANISOU  737  CB  ALA A 151     4910   7566   6231    398    871  -1679       C  
ATOM    738  N   CYS A 152     -14.037 -19.569  35.113  1.00 50.57           N  
ANISOU  738  N   CYS A 152     5082   7705   6427    536    925  -1913       N  
ATOM    739  CA  CYS A 152     -12.845 -20.258  34.633  1.00 50.43           C  
ANISOU  739  CA  CYS A 152     5028   7724   6407    601    965  -2007       C  
ATOM    740  C   CYS A 152     -12.876 -20.519  33.128  1.00 51.19           C  
ANISOU  740  C   CYS A 152     5200   7826   6421    517   1039  -2131       C  
ATOM    741  O   CYS A 152     -11.903 -20.227  32.430  1.00 52.11           O  
ANISOU  741  O   CYS A 152     5287   8042   6471    463   1107  -2191       O  
ATOM    742  CB  CYS A 152     -12.626 -21.567  35.395  1.00 50.39           C  
ANISOU  742  CB  CYS A 152     5008   7620   6516    806    930  -2000       C  
ATOM    743  SG  CYS A 152     -11.890 -21.362  37.035  1.00 50.90           S  
ANISOU  743  SG  CYS A 152     4964   7744   6629    929    858  -1893       S  
ATOM    744  N   THR A 153     -13.981 -21.066  32.624  1.00 58.28           N  
ANISOU  744  N   THR A 153     6201   8624   7320    500   1029  -2181       N  
ATOM    745  CA  THR A 153     -14.063 -21.362  31.192  1.00 58.96           C  
ANISOU  745  CA  THR A 153     6392   8713   7299    416   1086  -2315       C  
ATOM    746  C   THR A 153     -14.045 -20.089  30.337  1.00 58.30           C  
ANISOU  746  C   THR A 153     6344   8756   7051    229   1132  -2303       C  
ATOM    747  O   THR A 153     -13.422 -20.060  29.267  1.00 58.15           O  
ANISOU  747  O   THR A 153     6374   8798   6921    165   1208  -2380       O  
ATOM    748  CB  THR A 153     -15.269 -22.275  30.828  1.00 59.60           C  
ANISOU  748  CB  THR A 153     6600   8633   7414    412   1027  -2369       C  
ATOM    749  OG1 THR A 153     -15.211 -22.613  29.436  1.00 62.25           O  
ANISOU  749  OG1 THR A 153     7057   8975   7622    333   1073  -2517       O  
ATOM    750  CG2 THR A 153     -16.596 -21.596  31.122  1.00 59.19           C  
ANISOU  750  CG2 THR A 153     6597   8519   7373    293    906  -2188       C  
ATOM    751  N   TYR A 154     -14.703 -19.036  30.819  1.00 39.17           N  
ANISOU  751  N   TYR A 154     3905   6366   4613    150   1096  -2199       N  
ATOM    752  CA  TYR A 154     -14.670 -17.748  30.130  1.00 39.15           C  
ANISOU  752  CA  TYR A 154     3950   6466   4459    -19   1144  -2165       C  
ATOM    753  C   TYR A 154     -13.249 -17.196  30.071  1.00 40.01           C  
ANISOU  753  C   TYR A 154     3980   6670   4550    -53   1219  -2157       C  
ATOM    754  O   TYR A 154     -12.769 -16.802  29.003  1.00 41.22           O  
ANISOU  754  O   TYR A 154     4193   6892   4576   -162   1303  -2200       O  
ATOM    755  CB  TYR A 154     -15.599 -16.737  30.805  1.00 36.98           C  
ANISOU  755  CB  TYR A 154     3693   6148   4211    -77   1060  -1990       C  
ATOM    756  CG  TYR A 154     -17.040 -16.822  30.355  1.00 35.37           C  
ANISOU  756  CG  TYR A 154     3619   5821   3996   -131    930  -1887       C  
ATOM    757  CD1 TYR A 154     -17.430 -16.326  29.119  1.00 35.66           C  
ANISOU  757  CD1 TYR A 154     3793   5884   3873   -264    914  -1876       C  
ATOM    758  CD2 TYR A 154     -18.012 -17.388  31.168  1.00 33.77           C  
ANISOU  758  CD2 TYR A 154     3398   5490   3943    -53    821  -1794       C  
ATOM    759  CE1 TYR A 154     -18.745 -16.398  28.704  1.00 34.40           C  
ANISOU  759  CE1 TYR A 154     3729   5634   3707   -308    770  -1784       C  
ATOM    760  CE2 TYR A 154     -19.330 -17.465  30.762  1.00 32.43           C  
ANISOU  760  CE2 TYR A 154     3312   5228   3784   -112    699  -1706       C  
ATOM    761  CZ  TYR A 154     -19.691 -16.968  29.529  1.00 32.73           C  
ANISOU  761  CZ  TYR A 154     3465   5304   3666   -236    663  -1704       C  
ATOM    762  OH  TYR A 154     -21.003 -17.041  29.120  1.00 31.65           O  
ANISOU  762  OH  TYR A 154     3388   5094   3542   -289    517  -1618       O  
ATOM    763  N   ALA A 155     -12.581 -17.176  31.222  1.00 34.82           N  
ANISOU  763  N   ALA A 155     3194   6021   4014     37   1185  -2107       N  
ATOM    764  CA  ALA A 155     -11.208 -16.687  31.306  1.00 35.84           C  
ANISOU  764  CA  ALA A 155     3219   6254   4145      4   1241  -2124       C  
ATOM    765  C   ALA A 155     -10.275 -17.471  30.389  1.00 37.83           C  
ANISOU  765  C   ALA A 155     3456   6547   4372     41   1326  -2237       C  
ATOM    766  O   ALA A 155      -9.414 -16.892  29.723  1.00 39.12           O  
ANISOU  766  O   ALA A 155     3590   6808   4467    -61   1422  -2274       O  
ATOM    767  CB  ALA A 155     -10.711 -16.742  32.742  1.00 35.35           C  
ANISOU  767  CB  ALA A 155     3029   6199   4202    114   1165  -2075       C  
ATOM    768  N   THR A 156     -10.457 -18.788  30.355  1.00 40.44           N  
ANISOU  768  N   THR A 156     3811   6795   4761    188   1303  -2295       N  
ATOM    769  CA  THR A 156      -9.646 -19.654  29.507  1.00 42.53           C  
ANISOU  769  CA  THR A 156     4077   7075   5006    250   1391  -2411       C  
ATOM    770  C   THR A 156      -9.854 -19.329  28.030  1.00 43.50           C  
ANISOU  770  C   THR A 156     4338   7231   4960    105   1485  -2472       C  
ATOM    771  O   THR A 156      -8.887 -19.140  27.287  1.00 45.76           O  
ANISOU  771  O   THR A 156     4596   7608   5181     57   1600  -2527       O  
ATOM    772  CB  THR A 156      -9.963 -21.142  29.750  1.00 42.94           C  
ANISOU  772  CB  THR A 156     4168   6995   5152    434   1351  -2465       C  
ATOM    773  OG1 THR A 156      -9.790 -21.450  31.138  1.00 42.23           O  
ANISOU  773  OG1 THR A 156     3973   6871   5202    577   1265  -2389       O  
ATOM    774  CG2 THR A 156      -9.041 -22.024  28.922  1.00 45.37           C  
ANISOU  774  CG2 THR A 156     4479   7313   5446    517   1456  -2588       C  
ATOM    775  N   ALA A 157     -11.117 -19.259  27.613  1.00 47.40           N  
ANISOU  775  N   ALA A 157     4981   7658   5372     33   1435  -2463       N  
ATOM    776  CA  ALA A 157     -11.448 -18.942  26.226  1.00 48.93           C  
ANISOU  776  CA  ALA A 157     5339   7884   5370   -108   1498  -2509       C  
ATOM    777  C   ALA A 157     -10.857 -17.599  25.794  1.00 48.74           C  
ANISOU  777  C   ALA A 157     5305   7978   5238   -266   1588  -2447       C  
ATOM    778  O   ALA A 157     -10.191 -17.500  24.753  1.00 50.12           O  
ANISOU  778  O   ALA A 157     5534   8217   5293   -330   1706  -2502       O  
ATOM    779  CB  ALA A 157     -12.957 -18.948  26.027  1.00 47.35           C  
ANISOU  779  CB  ALA A 157     5284   7611   5098   -168   1396  -2498       C  
ATOM    780  N   LEU A 158     -11.097 -16.571  26.604  1.00 40.37           N  
ANISOU  780  N   LEU A 158     4183   6935   4219   -328   1543  -2335       N  
ATOM    781  CA  LEU A 158     -10.589 -15.234  26.312  1.00 40.83           C  
ANISOU  781  CA  LEU A 158     4244   7078   4192   -489   1628  -2274       C  
ATOM    782  C   LEU A 158      -9.063 -15.202  26.263  1.00 42.53           C  
ANISOU  782  C   LEU A 158     4314   7386   4460   -485   1736  -2330       C  
ATOM    783  O   LEU A 158      -8.479 -14.498  25.440  1.00 44.03           O  
ANISOU  783  O   LEU A 158     4541   7649   4541   -621   1858  -2334       O  
ATOM    784  CB  LEU A 158     -11.110 -14.220  27.332  1.00 38.98           C  
ANISOU  784  CB  LEU A 158     3975   6823   4013   -539   1558  -2158       C  
ATOM    785  CG  LEU A 158     -12.619 -13.967  27.325  1.00 37.57           C  
ANISOU  785  CG  LEU A 158     3931   6578   3767   -565   1472  -2090       C  
ATOM    786  CD1 LEU A 158     -12.986 -12.885  28.330  1.00 36.11           C  
ANISOU  786  CD1 LEU A 158     3705   6374   3640   -605   1435  -1979       C  
ATOM    787  CD2 LEU A 158     -13.096 -13.594  25.929  1.00 38.72           C  
ANISOU  787  CD2 LEU A 158     4282   6745   3684   -697   1518  -2088       C  
ATOM    788  N   ASN A 159      -8.422 -15.966  27.143  1.00 59.65           N  
ANISOU  788  N   ASN A 159     6319   9556   6791   -331   1693  -2372       N  
ATOM    789  CA  ASN A 159      -6.968 -16.080  27.127  1.00 61.48           C  
ANISOU  789  CA  ASN A 159     6392   9891   7079   -305   1785  -2442       C  
ATOM    790  C   ASN A 159      -6.464 -16.724  25.838  1.00 63.74           C  
ANISOU  790  C   ASN A 159     6741  10209   7269   -294   1920  -2543       C  
ATOM    791  O   ASN A 159      -5.446 -16.307  25.282  1.00 65.55           O  
ANISOU  791  O   ASN A 159     6908  10542   7456   -375   2055  -2583       O  
ATOM    792  CB  ASN A 159      -6.467 -16.863  28.342  1.00 61.52           C  
ANISOU  792  CB  ASN A 159     6227   9889   7260   -118   1694  -2459       C  
ATOM    793  CG  ASN A 159      -6.411 -16.017  29.599  1.00 60.38           C  
ANISOU  793  CG  ASN A 159     5978   9771   7194   -153   1601  -2383       C  
ATOM    794  OD1 ASN A 159      -6.053 -14.840  29.553  1.00 60.47           O  
ANISOU  794  OD1 ASN A 159     5959   9854   7164   -317   1650  -2364       O  
ATOM    795  ND2 ASN A 159      -6.766 -16.614  30.731  1.00 60.18           N  
ANISOU  795  ND2 ASN A 159     5911   9681   7274     -2   1472  -2343       N  
ATOM    796  N   VAL A 160      -7.183 -17.739  25.368  1.00 64.93           N  
ANISOU  796  N   VAL A 160     7022  10268   7382   -198   1890  -2591       N  
ATOM    797  CA  VAL A 160      -6.837 -18.402  24.115  1.00 67.11           C  
ANISOU  797  CA  VAL A 160     7398  10557   7545   -181   2014  -2698       C  
ATOM    798  C   VAL A 160      -6.936 -17.438  22.937  1.00 67.84           C  
ANISOU  798  C   VAL A 160     7639  10711   7428   -380   2119  -2673       C  
ATOM    799  O   VAL A 160      -5.994 -17.306  22.149  1.00 70.75           O  
ANISOU  799  O   VAL A 160     7987  11169   7725   -425   2277  -2727       O  
ATOM    800  CB  VAL A 160      -7.736 -19.627  23.850  1.00 66.41           C  
ANISOU  800  CB  VAL A 160     7455  10337   7441    -66   1944  -2765       C  
ATOM    801  CG1 VAL A 160      -7.537 -20.138  22.430  1.00 69.18           C  
ANISOU  801  CG1 VAL A 160     7965  10696   7627    -82   2066  -2877       C  
ATOM    802  CG2 VAL A 160      -7.448 -20.724  24.862  1.00 66.11           C  
ANISOU  802  CG2 VAL A 160     7290  10227   7601    147   1878  -2798       C  
ATOM    803  N   VAL A 161      -8.077 -16.762  22.824  1.00 48.52           N  
ANISOU  803  N   VAL A 161     5342   8216   4876   -493   2038  -2586       N  
ATOM    804  CA  VAL A 161      -8.285 -15.799  21.744  1.00 49.53           C  
ANISOU  804  CA  VAL A 161     5644   8390   4786   -677   2121  -2535       C  
ATOM    805  C   VAL A 161      -7.235 -14.689  21.778  1.00 50.55           C  
ANISOU  805  C   VAL A 161     5663   8618   4925   -804   2249  -2489       C  
ATOM    806  O   VAL A 161      -6.663 -14.320  20.746  1.00 52.81           O  
ANISOU  806  O   VAL A 161     6026   8972   5068   -905   2401  -2507       O  
ATOM    807  CB  VAL A 161      -9.690 -15.171  21.810  1.00 47.69           C  
ANISOU  807  CB  VAL A 161     5569   8093   4457   -765   1993  -2428       C  
ATOM    808  CG1 VAL A 161      -9.884 -14.181  20.673  1.00 49.05           C  
ANISOU  808  CG1 VAL A 161     5943   8307   4386   -943   2073  -2356       C  
ATOM    809  CG2 VAL A 161     -10.753 -16.254  21.762  1.00 46.97           C  
ANISOU  809  CG2 VAL A 161     5581   7911   4354   -666   1861  -2488       C  
ATOM    810  N   SER A 162      -6.980 -14.172  22.976  1.00 49.09           N  
ANISOU  810  N   SER A 162     5305   8440   4907   -803   2188  -2438       N  
ATOM    811  CA  SER A 162      -5.989 -13.121  23.165  1.00 50.08           C  
ANISOU  811  CA  SER A 162     5311   8651   5065   -935   2289  -2412       C  
ATOM    812  C   SER A 162      -4.606 -13.589  22.729  1.00 52.77           C  
ANISOU  812  C   SER A 162     5510   9099   5441   -899   2439  -2524       C  
ATOM    813  O   SER A 162      -3.862 -12.840  22.098  1.00 54.78           O  
ANISOU  813  O   SER A 162     5760   9434   5620  -1047   2594  -2524       O  
ATOM    814  CB  SER A 162      -5.955 -12.668  24.625  1.00 48.18           C  
ANISOU  814  CB  SER A 162     4909   8397   5001   -915   2172  -2366       C  
ATOM    815  OG  SER A 162      -5.064 -11.581  24.796  1.00 49.29           O  
ANISOU  815  OG  SER A 162     4951   8613   5165  -1069   2263  -2355       O  
ATOM    816  N   LEU A 163      -4.269 -14.831  23.064  1.00 53.01           N  
ANISOU  816  N   LEU A 163     5429   9128   5586   -700   2403  -2615       N  
ATOM    817  CA  LEU A 163      -3.001 -15.416  22.639  1.00 55.78           C  
ANISOU  817  CA  LEU A 163     5642   9577   5975   -628   2547  -2726       C  
ATOM    818  C   LEU A 163      -2.931 -15.543  21.122  1.00 58.13           C  
ANISOU  818  C   LEU A 163     6117   9899   6070   -687   2714  -2773       C  
ATOM    819  O   LEU A 163      -1.866 -15.371  20.525  1.00 60.84           O  
ANISOU  819  O   LEU A 163     6381  10352   6384   -735   2893  -2830       O  
ATOM    820  CB  LEU A 163      -2.786 -16.782  23.293  1.00 55.63           C  
ANISOU  820  CB  LEU A 163     5505   9521   6109   -380   2467  -2801       C  
ATOM    821  CG  LEU A 163      -2.090 -16.758  24.653  1.00 55.11           C  
ANISOU  821  CG  LEU A 163     5186   9508   6245   -298   2377  -2795       C  
ATOM    822  CD1 LEU A 163      -2.043 -18.151  25.256  1.00 55.00           C  
ANISOU  822  CD1 LEU A 163     5105   9432   6362    -41   2291  -2845       C  
ATOM    823  CD2 LEU A 163      -0.688 -16.183  24.514  1.00 57.70           C  
ANISOU  823  CD2 LEU A 163     5317   9997   6608   -382   2521  -2848       C  
ATOM    824  N   SER A 164      -4.069 -15.844  20.504  1.00 57.29           N  
ANISOU  824  N   SER A 164     6253   9698   5817   -686   2654  -2754       N  
ATOM    825  CA  SER A 164      -4.143 -15.919  19.049  1.00 59.53           C  
ANISOU  825  CA  SER A 164     6750  10000   5868   -749   2787  -2791       C  
ATOM    826  C   SER A 164      -3.845 -14.558  18.426  1.00 60.78           C  
ANISOU  826  C   SER A 164     6977  10232   5885   -974   2917  -2705       C  
ATOM    827  O   SER A 164      -3.074 -14.457  17.468  1.00 63.70           O  
ANISOU  827  O   SER A 164     7376  10686   6140  -1028   3108  -2752       O  
ATOM    828  CB  SER A 164      -5.516 -16.423  18.600  1.00 58.36           C  
ANISOU  828  CB  SER A 164     6852   9740   5582   -722   2658  -2784       C  
ATOM    829  OG  SER A 164      -5.765 -17.729  19.087  1.00 57.66           O  
ANISOU  829  OG  SER A 164     6722   9569   5619   -526   2561  -2874       O  
ATOM    830  N   VAL A 165      -4.455 -13.514  18.981  1.00 58.78           N  
ANISOU  830  N   VAL A 165     6757   9937   5639  -1100   2823  -2578       N  
ATOM    831  CA  VAL A 165      -4.219 -12.155  18.502  1.00 59.95           C  
ANISOU  831  CA  VAL A 165     6987  10125   5667  -1319   2940  -2482       C  
ATOM    832  C   VAL A 165      -2.756 -11.748  18.676  1.00 62.03           C  
ANISOU  832  C   VAL A 165     7022  10504   6044  -1386   3103  -2533       C  
ATOM    833  O   VAL A 165      -2.131 -11.228  17.748  1.00 64.76           O  
ANISOU  833  O   VAL A 165     7429  10918   6260  -1516   3294  -2529       O  
ATOM    834  CB  VAL A 165      -5.113 -11.133  19.229  1.00 57.45           C  
ANISOU  834  CB  VAL A 165     6734   9726   5368  -1422   2807  -2341       C  
ATOM    835  CG1 VAL A 165      -4.831  -9.731  18.721  1.00 58.98           C  
ANISOU  835  CG1 VAL A 165     7034   9936   5440  -1648   2941  -2238       C  
ATOM    836  CG2 VAL A 165      -6.580 -11.481  19.046  1.00 55.66           C  
ANISOU  836  CG2 VAL A 165     6721   9402   5027  -1364   2647  -2288       C  
ATOM    837  N   GLU A 166      -2.219 -11.992  19.868  1.00 80.30           N  
ANISOU  837  N   GLU A 166     9074  12844   8593  -1299   3025  -2579       N  
ATOM    838  CA  GLU A 166      -0.833 -11.656  20.183  1.00 82.63           C  
ANISOU  838  CA  GLU A 166     9119  13262   9015  -1356   3147  -2640       C  
ATOM    839  C   GLU A 166       0.147 -12.358  19.249  1.00 85.73           C  
ANISOU  839  C   GLU A 166     9453  13759   9360  -1292   3343  -2752       C  
ATOM    840  O   GLU A 166       1.092 -11.743  18.756  1.00 88.70           O  
ANISOU  840  O   GLU A 166     9759  14238   9705  -1429   3532  -2769       O  
ATOM    841  CB  GLU A 166      -0.510 -12.008  21.638  1.00 80.89           C  
ANISOU  841  CB  GLU A 166     8642  13057   9035  -1233   2994  -2680       C  
ATOM    842  CG  GLU A 166      -1.242 -11.161  22.669  1.00 78.32           C  
ANISOU  842  CG  GLU A 166     8339  12651   8769  -1311   2830  -2581       C  
ATOM    843  CD  GLU A 166      -0.724  -9.737  22.737  1.00 79.54           C  
ANISOU  843  CD  GLU A 166     8474  12840   8907  -1558   2924  -2535       C  
ATOM    844  OE1 GLU A 166       0.438  -9.505  22.340  1.00 81.95           O  
ANISOU  844  OE1 GLU A 166     8642  13262   9231  -1648   3087  -2601       O  
ATOM    845  OE2 GLU A 166      -1.479  -8.851  23.188  1.00 78.21           O  
ANISOU  845  OE2 GLU A 166     8428  12578   8710  -1664   2843  -2435       O  
ATOM    846  N   LEU A 167      -0.082 -13.646  19.010  1.00 67.79           N  
ANISOU  846  N   LEU A 167     7216  11457   7084  -1084   3308  -2831       N  
ATOM    847  CA  LEU A 167       0.778 -14.413  18.115  1.00 71.06           C  
ANISOU  847  CA  LEU A 167     7595  11957   7447   -993   3498  -2946       C  
ATOM    848  C   LEU A 167       0.672 -13.907  16.681  1.00 73.35           C  
ANISOU  848  C   LEU A 167     8127  12270   7472  -1142   3679  -2919       C  
ATOM    849  O   LEU A 167       1.683 -13.762  15.990  1.00 76.69           O  
ANISOU  849  O   LEU A 167     8481  12810   7848  -1194   3902  -2973       O  
ATOM    850  CB  LEU A 167       0.443 -15.905  18.173  1.00 70.58           C  
ANISOU  850  CB  LEU A 167     7564  11827   7429   -738   3417  -3037       C  
ATOM    851  CG  LEU A 167       1.292 -16.792  17.257  1.00 74.14           C  
ANISOU  851  CG  LEU A 167     7998  12350   7824   -616   3620  -3168       C  
ATOM    852  CD1 LEU A 167       2.770 -16.655  17.594  1.00 76.63           C  
ANISOU  852  CD1 LEU A 167     7997  12819   8300   -600   3762  -3227       C  
ATOM    853  CD2 LEU A 167       0.855 -18.245  17.342  1.00 73.67           C  
ANISOU  853  CD2 LEU A 167     8005  12184   7800   -371   3532  -3257       C  
ATOM    854  N   TYR A 168      -0.555 -13.639  16.238  1.00 73.50           N  
ANISOU  854  N   TYR A 168     8429  12185   7312  -1207   3583  -2831       N  
ATOM    855  CA  TYR A 168      -0.770 -13.123  14.890  1.00 75.66           C  
ANISOU  855  CA  TYR A 168     8970  12475   7305  -1345   3724  -2784       C  
ATOM    856  C   TYR A 168      -0.052 -11.796  14.682  1.00 77.47           C  
ANISOU  856  C   TYR A 168     9157  12778   7502  -1575   3890  -2704       C  
ATOM    857  O   TYR A 168       0.534 -11.565  13.630  1.00 80.76           O  
ANISOU  857  O   TYR A 168     9657  13272   7756  -1659   4105  -2718       O  
ATOM    858  CB  TYR A 168      -2.260 -12.965  14.580  1.00 74.28           C  
ANISOU  858  CB  TYR A 168     9093  12179   6950  -1378   3556  -2687       C  
ATOM    859  CG  TYR A 168      -2.520 -12.312  13.239  1.00 76.36           C  
ANISOU  859  CG  TYR A 168     9649  12461   6905  -1527   3677  -2613       C  
ATOM    860  CD1 TYR A 168      -2.439 -13.044  12.061  1.00 79.24           C  
ANISOU  860  CD1 TYR A 168    10181  12864   7062  -1460   3786  -2703       C  
ATOM    861  CD2 TYR A 168      -2.839 -10.963  13.150  1.00 76.16           C  
ANISOU  861  CD2 TYR A 168     9747  12407   6785  -1728   3685  -2451       C  
ATOM    862  CE1 TYR A 168      -2.671 -12.450  10.833  1.00 82.15           C  
ANISOU  862  CE1 TYR A 168    10830  13257   7126  -1589   3890  -2628       C  
ATOM    863  CE2 TYR A 168      -3.071 -10.361  11.927  1.00 79.31           C  
ANISOU  863  CE2 TYR A 168    10429  12816   6888  -1855   3791  -2365       C  
ATOM    864  CZ  TYR A 168      -2.987 -11.109  10.772  1.00 82.13           C  
ANISOU  864  CZ  TYR A 168    10946  13227   7033  -1784   3888  -2452       C  
ATOM    865  OH  TYR A 168      -3.220 -10.514   9.554  1.00 84.93           O  
ANISOU  865  OH  TYR A 168    11595  13599   7074  -1903   3985  -2361       O  
ATOM    866  N   LEU A 169      -0.101 -10.926  15.685  1.00 83.51           N  
ANISOU  866  N   LEU A 169     9803  13513   8415  -1681   3796  -2625       N  
ATOM    867  CA  LEU A 169       0.577  -9.637  15.598  1.00 85.85           C  
ANISOU  867  CA  LEU A 169    10059  13858   8702  -1915   3945  -2556       C  
ATOM    868  C   LEU A 169       2.089  -9.793  15.718  1.00 89.18           C  
ANISOU  868  C   LEU A 169    10177  14431   9277  -1915   4121  -2672       C  
ATOM    869  O   LEU A 169       2.849  -8.967  15.212  1.00 92.60           O  
ANISOU  869  O   LEU A 169    10588  14934   9660  -2101   4320  -2649       O  
ATOM    870  CB  LEU A 169       0.056  -8.670  16.664  1.00 83.94           C  
ANISOU  870  CB  LEU A 169     9800  13524   8567  -2028   3790  -2449       C  
ATOM    871  CG  LEU A 169      -1.064  -7.720  16.230  1.00 83.07           C  
ANISOU  871  CG  LEU A 169    10015  13292   8257  -2164   3740  -2282       C  
ATOM    872  CD1 LEU A 169      -2.304  -8.490  15.810  1.00 81.40           C  
ANISOU  872  CD1 LEU A 169    10013  13002   7912  -2014   3582  -2261       C  
ATOM    873  CD2 LEU A 169      -1.393  -6.732  17.339  1.00 80.79           C  
ANISOU  873  CD2 LEU A 169     9682  12919   8095  -2282   3631  -2192       C  
ATOM    874  N   ALA A 170       2.521 -10.858  16.386  1.00 90.97           N  
ANISOU  874  N   ALA A 170    10171  14704   9689  -1705   4048  -2791       N  
ATOM    875  CA  ALA A 170       3.944 -11.127  16.554  1.00 93.88           C  
ANISOU  875  CA  ALA A 170    10230  15226  10213  -1667   4196  -2905       C  
ATOM    876  C   ALA A 170       4.495 -11.930  15.381  1.00 97.00           C  
ANISOU  876  C   ALA A 170    10667  15705  10484  -1567   4412  -2998       C  
ATOM    877  O   ALA A 170       5.682 -12.254  15.344  1.00100.36           O  
ANISOU  877  O   ALA A 170    10845  16267  11017  -1514   4567  -3098       O  
ATOM    878  CB  ALA A 170       4.198 -11.856  17.864  1.00 91.75           C  
ANISOU  878  CB  ALA A 170     9691  14969  10198  -1477   4014  -2977       C  
ATOM    879  N   ILE A 171       3.629 -12.250  14.426  1.00131.08           N  
ANISOU  879  N   ILE A 171    15296  19944  14565  -1538   4420  -2970       N  
ATOM    880  CA  ILE A 171       4.040 -13.015  13.253  1.00134.61           C  
ANISOU  880  CA  ILE A 171    15834  20458  14855  -1440   4620  -3064       C  
ATOM    881  C   ILE A 171       3.719 -12.267  11.957  1.00136.51           C  
ANISOU  881  C   ILE A 171    16384  20697  14787  -1622   4774  -2978       C  
ATOM    882  O   ILE A 171       4.175 -12.646  10.879  1.00139.69           O  
ANISOU  882  O   ILE A 171    16874  21178  15025  -1589   4984  -3045       O  
ATOM    883  CB  ILE A 171       3.385 -14.413  13.239  1.00131.42           C  
ANISOU  883  CB  ILE A 171    15526  19968  14441  -1181   4486  -3151       C  
ATOM    884  CG1 ILE A 171       4.277 -15.421  12.513  1.00134.86           C  
ANISOU  884  CG1 ILE A 171    15892  20498  14850  -1010   4695  -3302       C  
ATOM    885  CG2 ILE A 171       1.990 -14.354  12.628  1.00130.55           C  
ANISOU  885  CG2 ILE A 171    15784  19730  14088  -1220   4362  -3076       C  
ATOM    886  CD1 ILE A 171       3.805 -16.847  12.651  1.00133.72           C  
ANISOU  886  CD1 ILE A 171    15801  20258  14748   -743   4572  -3407       C  
ATOM    887  N   ARG A 172       2.938 -11.197  12.077  1.00114.62           N  
ANISOU  887  N   ARG A 172    13784  17833  11931  -1805   4672  -2827       N  
ATOM    888  CA  ARG A 172       2.569 -10.368  10.934  1.00117.17           C  
ANISOU  888  CA  ARG A 172    14419  18140  11959  -1985   4793  -2713       C  
ATOM    889  C   ARG A 172       3.492  -9.157  10.840  1.00119.98           C  
ANISOU  889  C   ARG A 172    14676  18566  12342  -2228   4994  -2645       C  
ATOM    890  O   ARG A 172       3.782  -8.667   9.748  1.00124.03           O  
ANISOU  890  O   ARG A 172    15362  19126  12638  -2360   5207  -2594       O  
ATOM    891  CB  ARG A 172       1.105  -9.929  11.044  1.00117.00           C  
ANISOU  891  CB  ARG A 172    14676  17966  11813  -2027   4560  -2576       C  
ATOM    892  CG  ARG A 172       0.671  -8.843  10.069  1.00119.09           C  
ANISOU  892  CG  ARG A 172    15256  18193  11799  -2230   4645  -2414       C  
ATOM    893  CD  ARG A 172       0.777  -9.289   8.620  1.00123.15           C  
ANISOU  893  CD  ARG A 172    16004  18775  12011  -2203   4814  -2450       C  
ATOM    894  NE  ARG A 172       0.301  -8.250   7.710  1.00125.03           N  
ANISOU  894  NE  ARG A 172    16567  18972  11965  -2385   4872  -2276       N  
ATOM    895  CZ  ARG A 172       0.367  -8.325   6.385  1.00129.39           C  
ANISOU  895  CZ  ARG A 172    17366  19584  12212  -2410   5030  -2266       C  
ATOM    896  NH1 ARG A 172       0.897  -9.392   5.804  1.00132.11           N  
ANISOU  896  NH1 ARG A 172    17666  20031  12496  -2267   5158  -2432       N  
ATOM    897  NH2 ARG A 172      -0.094  -7.329   5.641  1.00131.28           N  
ANISOU  897  NH2 ARG A 172    17906  19777  12197  -2571   5063  -2087       N  
ATOM    898  N   HIS A 173       3.969  -8.689  11.990  1.00155.79           N  
ANISOU  898  N   HIS A 173    18938  23111  17143  -2289   4928  -2649       N  
ATOM    899  CA  HIS A 173       4.918  -7.580  12.021  1.00158.96           C  
ANISOU  899  CA  HIS A 173    19210  23579  17606  -2526   5111  -2609       C  
ATOM    900  C   HIS A 173       6.225  -7.901  12.757  1.00160.47           C  
ANISOU  900  C   HIS A 173    18981  23919  18071  -2482   5192  -2747       C  
ATOM    901  O   HIS A 173       6.558  -7.233  13.736  1.00160.44           O  
ANISOU  901  O   HIS A 173    18783  23916  18259  -2599   5125  -2736       O  
ATOM    902  CB  HIS A 173       4.270  -6.349  12.662  1.00150.08           C  
ANISOU  902  CB  HIS A 173    18188  22319  16515  -2711   4969  -2464       C  
ATOM    903  CG  HIS A 173       2.994  -5.925  12.006  1.00148.79           C  
ANISOU  903  CG  HIS A 173    18426  22014  16092  -2762   4889  -2308       C  
ATOM    904  ND1 HIS A 173       2.947  -4.960  11.023  1.00151.13           N  
ANISOU  904  ND1 HIS A 173    18979  22276  16166  -2967   5055  -2173       N  
ATOM    905  CD2 HIS A 173       1.716  -6.330  12.196  1.00145.75           C  
ANISOU  905  CD2 HIS A 173    18228  21516  15633  -2630   4657  -2259       C  
ATOM    906  CE1 HIS A 173       1.696  -4.792  10.633  1.00149.50           C  
ANISOU  906  CE1 HIS A 173    19103  21945  15754  -2949   4916  -2044       C  
ATOM    907  NE2 HIS A 173       0.929  -5.611  11.329  1.00146.43           N  
ANISOU  907  NE2 HIS A 173    18671  21513  15453  -2750   4675  -2098       N  
ATOM    908  N   PRO A 174       6.975  -8.919  12.296  1.00146.16           N  
ANISOU  908  N   PRO A 174    17026  22232  16274  -2310   5332  -2880       N  
ATOM    909  CA  PRO A 174       8.268  -9.162  12.931  1.00148.14           C  
ANISOU  909  CA  PRO A 174    16873  22640  16773  -2278   5428  -2998       C  
ATOM    910  C   PRO A 174       9.413  -8.801  11.991  1.00152.97           C  
ANISOU  910  C   PRO A 174    17418  23405  17297  -2397   5777  -3032       C  
ATOM    911  O   PRO A 174      10.426  -8.268  12.444  1.00154.38           O  
ANISOU  911  O   PRO A 174    17335  23693  17630  -2547   5897  -3055       O  
ATOM    912  CB  PRO A 174       8.242 -10.674  13.158  1.00146.27           C  
ANISOU  912  CB  PRO A 174    16516  22420  16640  -1953   5317  -3122       C  
ATOM    913  CG  PRO A 174       7.284 -11.214  12.075  1.00145.38           C  
ANISOU  913  CG  PRO A 174    16770  22208  16259  -1847   5305  -3101       C  
ATOM    914  CD  PRO A 174       6.645 -10.026  11.387  1.00145.68           C  
ANISOU  914  CD  PRO A 174    17129  22169  16051  -2094   5359  -2949       C  
ATOM    915  N   LEU A 180       3.288  -3.495  20.852  1.00138.31           N  
ANISOU  915  N   LEU A 180    15859  20492  16201  -2901   3845  -2459       N  
ATOM    916  CA  LEU A 180       3.126  -2.685  22.054  1.00136.50           C  
ANISOU  916  CA  LEU A 180    15580  20195  16089  -3002   3717  -2451       C  
ATOM    917  C   LEU A 180       2.815  -3.561  23.263  1.00132.95           C  
ANISOU  917  C   LEU A 180    14958  19769  15787  -2771   3473  -2520       C  
ATOM    918  O   LEU A 180       3.508  -4.548  23.513  1.00132.14           O  
ANISOU  918  O   LEU A 180    14608  19806  15795  -2607   3443  -2634       O  
ATOM    919  CB  LEU A 180       2.029  -1.634  21.864  1.00124.37           C  
ANISOU  919  CB  LEU A 180    14382  18456  14419  -3143   3704  -2287       C  
ATOM    920  CG  LEU A 180       2.323  -0.452  20.932  1.00127.47           C  
ANISOU  920  CG  LEU A 180    14970  18785  14680  -3415   3928  -2194       C  
ATOM    921  CD1 LEU A 180       3.707   0.122  21.206  1.00130.71           C  
ANISOU  921  CD1 LEU A 180    15138  19307  15219  -3611   4067  -2301       C  
ATOM    922  CD2 LEU A 180       2.167  -0.830  19.462  1.00129.11           C  
ANISOU  922  CD2 LEU A 180    15368  19009  14680  -3385   4076  -2127       C  
ATOM    923  N   MET A 181       1.772  -3.192  24.003  1.00154.22           N  
ANISOU  923  N   MET A 181    17793  22324  18481  -2752   3310  -2443       N  
ATOM    924  CA  MET A 181       1.352  -3.928  25.195  1.00152.01           C  
ANISOU  924  CA  MET A 181    17386  22048  18323  -2540   3080  -2487       C  
ATOM    925  C   MET A 181       2.486  -4.116  26.199  1.00152.96           C  
ANISOU  925  C   MET A 181    17175  22322  18621  -2517   3026  -2629       C  
ATOM    926  O   MET A 181       3.043  -5.207  26.318  1.00153.14           O  
ANISOU  926  O   MET A 181    16998  22463  18724  -2321   2979  -2714       O  
ATOM    927  CB  MET A 181       0.755  -5.287  24.816  1.00142.41           C  
ANISOU  927  CB  MET A 181    16208  20832  17071  -2279   3002  -2480       C  
ATOM    928  CG  MET A 181      -0.680  -5.228  24.317  1.00140.22           C  
ANISOU  928  CG  MET A 181    16234  20396  16647  -2245   2950  -2343       C  
ATOM    929  SD  MET A 181      -1.852  -4.820  25.625  1.00136.65           S  
ANISOU  929  SD  MET A 181    15851  19809  16259  -2193   2734  -2270       S  
ATOM    930  CE  MET A 181      -3.404  -4.940  24.738  1.00134.95           C  
ANISOU  930  CE  MET A 181    15968  19450  15858  -2139   2706  -2118       C  
ATOM    931  N   SER A 182       2.824  -3.050  26.917  1.00108.00           N  
ANISOU  931  N   SER A 182    11430  16623  12983  -2715   3030  -2655       N  
ATOM    932  CA  SER A 182       3.858  -3.121  27.943  1.00110.46           C  
ANISOU  932  CA  SER A 182    11432  17088  13449  -2710   2960  -2792       C  
ATOM    933  C   SER A 182       3.409  -4.020  29.091  1.00108.04           C  
ANISOU  933  C   SER A 182    11028  16796  13225  -2454   2720  -2820       C  
ATOM    934  O   SER A 182       2.238  -4.391  29.173  1.00106.09           O  
ANISOU  934  O   SER A 182    10967  16418  12923  -2329   2615  -2728       O  
ATOM    935  CB  SER A 182       4.205  -1.724  28.462  1.00110.70           C  
ANISOU  935  CB  SER A 182    11466  17089  13507  -2993   3009  -2815       C  
ATOM    936  OG  SER A 182       3.065  -1.083  29.009  1.00107.91           O  
ANISOU  936  OG  SER A 182    11340  16555  13106  -3035   2914  -2728       O  
ATOM    937  N   ARG A 183       4.348  -4.367  29.968  1.00132.38           N  
ANISOU  937  N   ARG A 183    13820  20042  16435  -2377   2636  -2940       N  
ATOM    938  CA  ARG A 183       4.083  -5.262  31.092  1.00131.23           C  
ANISOU  938  CA  ARG A 183    13566  19930  16365  -2121   2414  -2966       C  
ATOM    939  C   ARG A 183       2.890  -4.798  31.923  1.00128.17           C  
ANISOU  939  C   ARG A 183    13364  19393  15941  -2118   2272  -2893       C  
ATOM    940  O   ARG A 183       1.989  -5.585  32.234  1.00126.35           O  
ANISOU  940  O   ARG A 183    13222  19085  15699  -1905   2145  -2829       O  
ATOM    941  CB  ARG A 183       5.325  -5.375  31.978  1.00134.09           C  
ANISOU  941  CB  ARG A 183    13601  20493  16856  -2099   2346  -3100       C  
ATOM    942  CG  ARG A 183       6.567  -5.852  31.241  1.00138.28           C  
ANISOU  942  CG  ARG A 183    13907  21188  17446  -2089   2490  -3177       C  
ATOM    943  CD  ARG A 183       7.799  -5.784  32.127  1.00141.55           C  
ANISOU  943  CD  ARG A 183    13986  21807  17991  -2102   2424  -3304       C  
ATOM    944  NE  ARG A 183       7.657  -6.600  33.329  1.00140.94           N  
ANISOU  944  NE  ARG A 183    13799  21778  17976  -1847   2187  -3324       N  
ATOM    945  CZ  ARG A 183       8.022  -7.875  33.414  1.00142.57           C  
ANISOU  945  CZ  ARG A 183    13857  22065  18249  -1569   2124  -3342       C  
ATOM    946  NH1 ARG A 183       8.553  -8.486  32.363  1.00144.43           N  
ANISOU  946  NH1 ARG A 183    14028  22349  18502  -1508   2285  -3354       N  
ATOM    947  NH2 ARG A 183       7.855  -8.541  34.549  1.00141.91           N  
ANISOU  947  NH2 ARG A 183    13699  22009  18210  -1349   1908  -3344       N  
ATOM    948  N   SER A 184       2.890  -3.515  32.269  1.00125.63           N  
ANISOU  948  N   SER A 184    13103  19025  15604  -2359   2309  -2902       N  
ATOM    949  CA  SER A 184       1.797  -2.917  33.024  1.00122.72           C  
ANISOU  949  CA  SER A 184    12918  18510  15201  -2384   2210  -2838       C  
ATOM    950  C   SER A 184       0.475  -3.063  32.277  1.00119.95           C  
ANISOU  950  C   SER A 184    12850  17976  14750  -2322   2237  -2686       C  
ATOM    951  O   SER A 184      -0.485  -3.615  32.811  1.00117.65           O  
ANISOU  951  O   SER A 184    12632  17613  14457  -2138   2101  -2627       O  
ATOM    952  CB  SER A 184       2.084  -1.440  33.305  1.00121.27           C  
ANISOU  952  CB  SER A 184    12783  18283  15013  -2686   2291  -2873       C  
ATOM    953  OG  SER A 184       2.302  -0.724  32.102  1.00122.44           O  
ANISOU  953  OG  SER A 184    13059  18366  15097  -2902   2499  -2824       O  
ATOM    954  N   ARG A 185       0.441  -2.579  31.038  1.00 97.81           N  
ANISOU  954  N   ARG A 185    10201  15105  11858  -2473   2412  -2621       N  
ATOM    955  CA  ARG A 185      -0.762  -2.645  30.213  1.00 95.41           C  
ANISOU  955  CA  ARG A 185    10168  14643  11439  -2431   2445  -2474       C  
ATOM    956  C   ARG A 185      -1.246  -4.078  30.000  1.00 94.16           C  
ANISOU  956  C   ARG A 185     9989  14505  11281  -2150   2346  -2452       C  
ATOM    957  O   ARG A 185      -2.450  -4.341  29.997  1.00 92.88           O  
ANISOU  957  O   ARG A 185     9994  14225  11073  -2039   2267  -2352       O  
ATOM    958  CB  ARG A 185      -0.530  -1.957  28.865  1.00 98.28           C  
ANISOU  958  CB  ARG A 185    10687  14963  11693  -2632   2655  -2416       C  
ATOM    959  CG  ARG A 185      -0.451  -0.441  28.950  1.00100.27           C  
ANISOU  959  CG  ARG A 185    11076  15107  11916  -2916   2760  -2381       C  
ATOM    960  CD  ARG A 185      -0.306   0.191  27.574  1.00103.30           C  
ANISOU  960  CD  ARG A 185    11652  15427  12171  -3096   2967  -2292       C  
ATOM    961  NE  ARG A 185       1.017  -0.034  26.999  1.00107.74           N  
ANISOU  961  NE  ARG A 185    12022  16150  12765  -3184   3106  -2393       N  
ATOM    962  CZ  ARG A 185       1.396   0.409  25.804  1.00111.52           C  
ANISOU  962  CZ  ARG A 185    12619  16614  13140  -3342   3308  -2339       C  
ATOM    963  NH1 ARG A 185       0.550   1.100  25.052  1.00111.79           N  
ANISOU  963  NH1 ARG A 185    12978  16477  13022  -3423   3379  -2179       N  
ATOM    964  NH2 ARG A 185       2.621   0.160  25.360  1.00114.94           N  
ANISOU  964  NH2 ARG A 185    12847  17208  13618  -3412   3440  -2438       N  
ATOM    965  N   THR A 186      -0.303  -5.000  29.825  1.00 73.97           N  
ANISOU  965  N   THR A 186     7229  12094   8784  -2038   2357  -2545       N  
ATOM    966  CA  THR A 186      -0.636  -6.409  29.642  1.00 72.76           C  
ANISOU  966  CA  THR A 186     7054  11949   8642  -1776   2276  -2538       C  
ATOM    967  C   THR A 186      -1.298  -6.986  30.890  1.00 70.66           C  
ANISOU  967  C   THR A 186     6750  11646   8452  -1578   2068  -2524       C  
ATOM    968  O   THR A 186      -2.329  -7.657  30.799  1.00 68.63           O  
ANISOU  968  O   THR A 186     6623  11287   8165  -1428   1992  -2446       O  
ATOM    969  CB  THR A 186       0.605  -7.247  29.275  1.00 75.98           C  
ANISOU  969  CB  THR A 186     7243  12516   9111  -1690   2345  -2647       C  
ATOM    970  OG1 THR A 186       1.073  -6.863  27.976  1.00 77.77           O  
ANISOU  970  OG1 THR A 186     7541  12763   9244  -1839   2552  -2642       O  
ATOM    971  CG2 THR A 186       0.266  -8.730  29.262  1.00 75.13           C  
ANISOU  971  CG2 THR A 186     7110  12399   9038  -1406   2245  -2648       C  
ATOM    972  N   LYS A 187      -0.709  -6.719  32.053  1.00108.58           N  
ANISOU  972  N   LYS A 187    11378  16534  13344  -1585   1980  -2600       N  
ATOM    973  CA  LYS A 187      -1.287  -7.182  33.313  1.00106.18           C  
ANISOU  973  CA  LYS A 187    11044  16204  13095  -1408   1791  -2584       C  
ATOM    974  C   LYS A 187      -2.669  -6.573  33.550  1.00103.19           C  
ANISOU  974  C   LYS A 187    10892  15658  12658  -1447   1753  -2470       C  
ATOM    975  O   LYS A 187      -3.581  -7.249  34.040  1.00101.88           O  
ANISOU  975  O   LYS A 187    10788  15416  12506  -1263   1635  -2405       O  
ATOM    976  CB  LYS A 187      -0.350  -6.886  34.487  1.00105.66           C  
ANISOU  976  CB  LYS A 187    10758  16280  13110  -1433   1711  -2695       C  
ATOM    977  CG  LYS A 187       0.903  -7.752  34.502  1.00108.40           C  
ANISOU  977  CG  LYS A 187    10851  16800  13535  -1320   1706  -2797       C  
ATOM    978  CD  LYS A 187       1.646  -7.648  35.825  1.00109.40           C  
ANISOU  978  CD  LYS A 187    10763  17069  13734  -1280   1571  -2891       C  
ATOM    979  CE  LYS A 187       2.922  -6.834  35.690  1.00112.40           C  
ANISOU  979  CE  LYS A 187    10946  17607  14153  -1484   1664  -3010       C  
ATOM    980  NZ  LYS A 187       2.651  -5.419  35.318  1.00112.82           N  
ANISOU  980  NZ  LYS A 187    11136  17582  14148  -1790   1788  -3002       N  
ATOM    981  N   LYS A 188      -2.820  -5.301  33.190  1.00 57.04           N  
ANISOU  981  N   LYS A 188     5172   9749   6753  -1685   1865  -2442       N  
ATOM    982  CA  LYS A 188      -4.113  -4.629  33.263  1.00 56.37           C  
ANISOU  982  CA  LYS A 188     5313   9498   6607  -1731   1859  -2325       C  
ATOM    983  C   LYS A 188      -5.131  -5.346  32.383  1.00 55.34           C  
ANISOU  983  C   LYS A 188     5346   9272   6410  -1601   1857  -2213       C  
ATOM    984  O   LYS A 188      -6.289  -5.521  32.769  1.00 55.03           O  
ANISOU  984  O   LYS A 188     5420   9129   6362  -1492   1774  -2126       O  
ATOM    985  CB  LYS A 188      -3.994  -3.166  32.828  1.00 56.44           C  
ANISOU  985  CB  LYS A 188     5453   9438   6555  -2015   2008  -2304       C  
ATOM    986  CG  LYS A 188      -3.131  -2.303  33.735  1.00 57.84           C  
ANISOU  986  CG  LYS A 188     5501   9684   6792  -2183   2015  -2418       C  
ATOM    987  CD  LYS A 188      -2.986  -0.894  33.176  1.00 59.47           C  
ANISOU  987  CD  LYS A 188     5870   9787   6941  -2477   2180  -2386       C  
ATOM    988  CE  LYS A 188      -1.837  -0.148  33.837  1.00 61.55           C  
ANISOU  988  CE  LYS A 188     5972  10147   7268  -2674   2213  -2527       C  
ATOM    989  NZ  LYS A 188      -1.987  -0.082  35.316  1.00 60.88           N  
ANISOU  989  NZ  LYS A 188     5773  10108   7250  -2615   2066  -2613       N  
ATOM    990  N   PHE A 189      -4.689  -5.766  31.200  1.00 64.87           N  
ANISOU  990  N   PHE A 189     6560  10523   7566  -1617   1954  -2226       N  
ATOM    991  CA  PHE A 189      -5.563  -6.470  30.268  1.00 63.78           C  
ANISOU  991  CA  PHE A 189     6573  10314   7345  -1514   1959  -2148       C  
ATOM    992  C   PHE A 189      -5.964  -7.848  30.790  1.00 62.32           C  
ANISOU  992  C   PHE A 189     6315  10129   7234  -1255   1815  -2159       C  
ATOM    993  O   PHE A 189      -7.100  -8.281  30.600  1.00 61.43           O  
ANISOU  993  O   PHE A 189     6336   9922   7083  -1159   1757  -2081       O  
ATOM    994  CB  PHE A 189      -4.911  -6.595  28.891  1.00 65.20           C  
ANISOU  994  CB  PHE A 189     6783  10552   7436  -1600   2112  -2175       C  
ATOM    995  CG  PHE A 189      -5.771  -7.297  27.880  1.00 64.41           C  
ANISOU  995  CG  PHE A 189     6851  10395   7226  -1512   2119  -2115       C  
ATOM    996  CD1 PHE A 189      -6.920  -6.695  27.395  1.00 63.66           C  
ANISOU  996  CD1 PHE A 189     6993  10188   7005  -1580   2128  -1994       C  
ATOM    997  CD2 PHE A 189      -5.433  -8.557  27.415  1.00 64.80           C  
ANISOU  997  CD2 PHE A 189     6828  10503   7289  -1361   2116  -2186       C  
ATOM    998  CE1 PHE A 189      -7.718  -7.336  26.468  1.00 64.07           C  
ANISOU  998  CE1 PHE A 189     7199  10207   6936  -1507   2119  -1953       C  
ATOM    999  CE2 PHE A 189      -6.226  -9.203  26.486  1.00 64.92           C  
ANISOU  999  CE2 PHE A 189     7007  10468   7191  -1294   2120  -2153       C  
ATOM   1000  CZ  PHE A 189      -7.370  -8.592  26.012  1.00 64.77           C  
ANISOU 1000  CZ  PHE A 189     7216  10357   7038  -1372   2114  -2041       C  
ATOM   1001  N   ILE A 190      -5.027  -8.534  31.439  1.00 50.04           N  
ANISOU 1001  N   ILE A 190     4552   8678   5782  -1146   1759  -2254       N  
ATOM   1002  CA  ILE A 190      -5.319  -9.828  32.049  1.00 48.94           C  
ANISOU 1002  CA  ILE A 190     4351   8523   5719   -900   1626  -2257       C  
ATOM   1003  C   ILE A 190      -6.360  -9.658  33.151  1.00 47.17           C  
ANISOU 1003  C   ILE A 190     4189   8207   5527   -828   1499  -2178       C  
ATOM   1004  O   ILE A 190      -7.323 -10.428  33.240  1.00 45.76           O  
ANISOU 1004  O   ILE A 190     4092   7937   5357   -682   1424  -2116       O  
ATOM   1005  CB  ILE A 190      -4.051 -10.479  32.634  1.00 51.31           C  
ANISOU 1005  CB  ILE A 190     4419   8957   6119   -796   1590  -2363       C  
ATOM   1006  CG1 ILE A 190      -3.042 -10.769  31.523  1.00 54.02           C  
ANISOU 1006  CG1 ILE A 190     4688   9395   6443   -839   1731  -2442       C  
ATOM   1007  CG2 ILE A 190      -4.400 -11.763  33.371  1.00 50.30           C  
ANISOU 1007  CG2 ILE A 190     4256   8789   6066   -542   1452  -2344       C  
ATOM   1008  CD1 ILE A 190      -3.539 -11.759  30.495  1.00 54.13           C  
ANISOU 1008  CD1 ILE A 190     4820   9343   6405   -733   1775  -2425       C  
ATOM   1009  N   SER A 191      -6.162  -8.637  33.981  1.00 44.25           N  
ANISOU 1009  N   SER A 191     3780   7860   5173   -939   1486  -2191       N  
ATOM   1010  CA  SER A 191      -7.118  -8.306  35.031  1.00 44.22           C  
ANISOU 1010  CA  SER A 191     3842   7773   5187   -887   1392  -2123       C  
ATOM   1011  C   SER A 191      -8.494  -8.009  34.437  1.00 43.44           C  
ANISOU 1011  C   SER A 191     3955   7533   5020   -907   1422  -2004       C  
ATOM   1012  O   SER A 191      -9.522  -8.386  35.004  1.00 42.32           O  
ANISOU 1012  O   SER A 191     3872   7306   4902   -774   1337  -1932       O  
ATOM   1013  CB  SER A 191      -6.623  -7.112  35.848  1.00 45.79           C  
ANISOU 1013  CB  SER A 191     3984   8022   5394  -1044   1408  -2180       C  
ATOM   1014  OG  SER A 191      -5.375  -7.396  36.457  1.00 47.19           O  
ANISOU 1014  OG  SER A 191     3947   8355   5629  -1024   1366  -2301       O  
ATOM   1015  N   ALA A 192      -8.502  -7.340  33.287  1.00 46.95           N  
ANISOU 1015  N   ALA A 192     4510   7957   5371  -1073   1547  -1983       N  
ATOM   1016  CA  ALA A 192      -9.743  -7.043  32.579  1.00 46.77           C  
ANISOU 1016  CA  ALA A 192     4692   7824   5257  -1097   1579  -1873       C  
ATOM   1017  C   ALA A 192     -10.431  -8.326  32.117  1.00 45.67           C  
ANISOU 1017  C   ALA A 192     4581   7660   5111   -929   1515  -1854       C  
ATOM   1018  O   ALA A 192     -11.653  -8.460  32.227  1.00 45.81           O  
ANISOU 1018  O   ALA A 192     4696   7596   5115   -856   1461  -1778       O  
ATOM   1019  CB  ALA A 192      -9.473  -6.125  31.396  1.00 46.40           C  
ANISOU 1019  CB  ALA A 192     4771   7772   5087  -1307   1729  -1850       C  
ATOM   1020  N   ILE A 193      -9.639  -9.263  31.601  1.00 37.08           N  
ANISOU 1020  N   ILE A 193     3406   6646   4038   -873   1529  -1934       N  
ATOM   1021  CA  ILE A 193     -10.154 -10.562  31.179  1.00 36.61           C  
ANISOU 1021  CA  ILE A 193     3372   6559   3982   -722   1479  -1945       C  
ATOM   1022  C   ILE A 193     -10.807 -11.286  32.347  1.00 34.97           C  
ANISOU 1022  C   ILE A 193     3115   6290   3885   -544   1345  -1912       C  
ATOM   1023  O   ILE A 193     -11.927 -11.788  32.231  1.00 33.91           O  
ANISOU 1023  O   ILE A 193     3066   6079   3740   -474   1298  -1866       O  
ATOM   1024  CB  ILE A 193      -9.041 -11.463  30.606  1.00 38.27           C  
ANISOU 1024  CB  ILE A 193     3480   6851   4209   -671   1527  -2051       C  
ATOM   1025  CG1 ILE A 193      -8.494 -10.885  29.301  1.00 40.12           C  
ANISOU 1025  CG1 ILE A 193     3783   7141   4318   -838   1678  -2078       C  
ATOM   1026  CG2 ILE A 193      -9.561 -12.873  30.373  1.00 37.86           C  
ANISOU 1026  CG2 ILE A 193     3457   6749   4181   -503   1471  -2077       C  
ATOM   1027  CD1 ILE A 193      -7.470 -11.774  28.627  1.00 41.99           C  
ANISOU 1027  CD1 ILE A 193     3933   7458   4562   -781   1750  -2183       C  
ATOM   1028  N   TRP A 194     -10.101 -11.332  33.473  1.00 50.78           N  
ANISOU 1028  N   TRP A 194     4978   8332   5982   -478   1288  -1939       N  
ATOM   1029  CA  TRP A 194     -10.619 -11.986  34.670  1.00 50.16           C  
ANISOU 1029  CA  TRP A 194     4864   8199   5995   -308   1169  -1896       C  
ATOM   1030  C   TRP A 194     -11.913 -11.344  35.159  1.00 49.73           C  
ANISOU 1030  C   TRP A 194     4914   8051   5931   -320   1139  -1796       C  
ATOM   1031  O   TRP A 194     -12.877 -12.042  35.484  1.00 48.59           O  
ANISOU 1031  O   TRP A 194     4806   7826   5828   -199   1078  -1741       O  
ATOM   1032  CB  TRP A 194      -9.574 -11.985  35.786  1.00 49.97           C  
ANISOU 1032  CB  TRP A 194     4687   8260   6037   -256   1115  -1946       C  
ATOM   1033  CG  TRP A 194      -8.563 -13.081  35.655  1.00 50.53           C  
ANISOU 1033  CG  TRP A 194     4640   8400   6157   -141   1104  -2024       C  
ATOM   1034  CD1 TRP A 194      -7.255 -12.952  35.290  1.00 52.03           C  
ANISOU 1034  CD1 TRP A 194     4704   8717   6349   -199   1163  -2121       C  
ATOM   1035  CD2 TRP A 194      -8.781 -14.478  35.881  1.00 50.14           C  
ANISOU 1035  CD2 TRP A 194     4589   8293   6170     58   1044  -2012       C  
ATOM   1036  NE1 TRP A 194      -6.644 -14.183  35.280  1.00 52.37           N  
ANISOU 1036  NE1 TRP A 194     4660   8787   6450    -34   1140  -2169       N  
ATOM   1037  CE2 TRP A 194      -7.560 -15.137  35.638  1.00 50.93           C  
ANISOU 1037  CE2 TRP A 194     4563   8485   6304    125   1069  -2102       C  
ATOM   1038  CE3 TRP A 194      -9.891 -15.236  36.267  1.00 49.99           C  
ANISOU 1038  CE3 TRP A 194     4658   8148   6186    182    982  -1935       C  
ATOM   1039  CZ2 TRP A 194      -7.417 -16.516  35.769  1.00 51.49           C  
ANISOU 1039  CZ2 TRP A 194     4610   8513   6440    320   1035  -2115       C  
ATOM   1040  CZ3 TRP A 194      -9.747 -16.606  36.396  1.00 49.55           C  
ANISOU 1040  CZ3 TRP A 194     4582   8048   6195    358    950  -1952       C  
ATOM   1041  CH2 TRP A 194      -8.519 -17.232  36.147  1.00 50.22           C  
ANISOU 1041  CH2 TRP A 194     4556   8214   6309    431    977  -2039       C  
ATOM   1042  N   LEU A 195     -11.933 -10.015  35.203  1.00 35.41           N  
ANISOU 1042  N   LEU A 195     3146   6243   4068   -467   1195  -1775       N  
ATOM   1043  CA  LEU A 195     -13.121  -9.293  35.648  1.00 34.51           C  
ANISOU 1043  CA  LEU A 195     3131   6038   3942   -474   1189  -1683       C  
ATOM   1044  C   LEU A 195     -14.318  -9.566  34.742  1.00 34.05           C  
ANISOU 1044  C   LEU A 195     3185   5920   3833   -463   1204  -1626       C  
ATOM   1045  O   LEU A 195     -15.417  -9.839  35.225  1.00 32.76           O  
ANISOU 1045  O   LEU A 195     3069   5648   3728   -360   1116  -1525       O  
ATOM   1046  CB  LEU A 195     -12.853  -7.790  35.731  1.00 35.65           C  
ANISOU 1046  CB  LEU A 195     3327   6187   4034   -650   1273  -1684       C  
ATOM   1047  CG  LEU A 195     -14.056  -6.942  36.153  1.00 36.05           C  
ANISOU 1047  CG  LEU A 195     3514   6104   4078   -647   1263  -1569       C  
ATOM   1048  CD1 LEU A 195     -14.590  -7.392  37.505  1.00 35.67           C  
ANISOU 1048  CD1 LEU A 195     3420   6014   4120   -477   1167  -1534       C  
ATOM   1049  CD2 LEU A 195     -13.697  -5.466  36.181  1.00 37.93           C  
ANISOU 1049  CD2 LEU A 195     3840   6300   4272   -825   1342  -1564       C  
ATOM   1050  N   ALA A 196     -14.098  -9.494  33.431  1.00 34.12           N  
ANISOU 1050  N   ALA A 196     3260   5966   3738   -569   1276  -1657       N  
ATOM   1051  CA  ALA A 196     -15.157  -9.763  32.463  1.00 34.34           C  
ANISOU 1051  CA  ALA A 196     3432   5909   3705   -567   1223  -1573       C  
ATOM   1052  C   ALA A 196     -15.672 -11.193  32.600  1.00 33.74           C  
ANISOU 1052  C   ALA A 196     3308   5802   3708   -415   1132  -1596       C  
ATOM   1053  O   ALA A 196     -16.877 -11.444  32.513  1.00 34.30           O  
ANISOU 1053  O   ALA A 196     3456   5766   3810   -368   1028  -1492       O  
ATOM   1054  CB  ALA A 196     -14.659  -9.512  31.050  1.00 35.39           C  
ANISOU 1054  CB  ALA A 196     3654   6111   3683   -708   1325  -1620       C  
ATOM   1055  N   SER A 197     -14.747 -12.122  32.823  1.00 34.02           N  
ANISOU 1055  N   SER A 197     3211   5928   3787   -338   1173  -1732       N  
ATOM   1056  CA  SER A 197     -15.089 -13.524  33.018  1.00 33.58           C  
ANISOU 1056  CA  SER A 197     3119   5823   3818   -190   1103  -1764       C  
ATOM   1057  C   SER A 197     -15.992 -13.681  34.233  1.00 32.10           C  
ANISOU 1057  C   SER A 197     2919   5525   3751    -83   1000  -1644       C  
ATOM   1058  O   SER A 197     -16.996 -14.393  34.186  1.00 31.93           O  
ANISOU 1058  O   SER A 197     2950   5396   3787    -27    919  -1582       O  
ATOM   1059  CB  SER A 197     -13.820 -14.356  33.205  1.00 34.34           C  
ANISOU 1059  CB  SER A 197     3116   5957   3973   -108   1104  -1841       C  
ATOM   1060  OG  SER A 197     -12.872 -14.067  32.194  1.00 35.74           O  
ANISOU 1060  OG  SER A 197     3301   6216   4062   -212   1191  -1911       O  
ATOM   1061  N   ALA A 198     -15.628 -13.005  35.319  1.00 28.86           N  
ANISOU 1061  N   ALA A 198     2442   5146   3375    -65   1011  -1620       N  
ATOM   1062  CA  ALA A 198     -16.423 -13.033  36.541  1.00 27.62           C  
ANISOU 1062  CA  ALA A 198     2285   4899   3309     35    939  -1510       C  
ATOM   1063  C   ALA A 198     -17.804 -12.425  36.312  1.00 26.05           C  
ANISOU 1063  C   ALA A 198     2202   4580   3115    -10    891  -1364       C  
ATOM   1064  O   ALA A 198     -18.798 -12.889  36.872  1.00 25.09           O  
ANISOU 1064  O   ALA A 198     2090   4363   3082     74    831  -1270       O  
ATOM   1065  CB  ALA A 198     -15.699 -12.303  37.659  1.00 27.90           C  
ANISOU 1065  CB  ALA A 198     2263   4990   3348     41    948  -1517       C  
ATOM   1066  N   LEU A 199     -17.858 -11.388  35.482  1.00 27.67           N  
ANISOU 1066  N   LEU A 199     2492   4791   3229   -140    923  -1339       N  
ATOM   1067  CA  LEU A 199     -19.112 -10.704  35.183  1.00 27.41           C  
ANISOU 1067  CA  LEU A 199     2565   4654   3197   -168    870  -1196       C  
ATOM   1068  C   LEU A 199     -20.056 -11.581  34.371  1.00 27.59           C  
ANISOU 1068  C   LEU A 199     2618   4625   3239   -150    782  -1159       C  
ATOM   1069  O   LEU A 199     -21.267 -11.573  34.591  1.00 27.27           O  
ANISOU 1069  O   LEU A 199     2590   4498   3275   -107    707  -1042       O  
ATOM   1070  CB  LEU A 199     -18.844  -9.395  34.437  1.00 28.09           C  
ANISOU 1070  CB  LEU A 199     2755   4750   3168   -305    925  -1172       C  
ATOM   1071  CG  LEU A 199     -18.189  -8.275  35.245  1.00 28.14           C  
ANISOU 1071  CG  LEU A 199     2760   4766   3166   -355   1001  -1188       C  
ATOM   1072  CD1 LEU A 199     -17.774  -7.136  34.331  1.00 29.20           C  
ANISOU 1072  CD1 LEU A 199     3009   4903   3181   -516   1077  -1180       C  
ATOM   1073  CD2 LEU A 199     -19.130  -7.778  36.332  1.00 27.44           C  
ANISOU 1073  CD2 LEU A 199     2697   4567   3163   -266    964  -1076       C  
ATOM   1074  N   LEU A 200     -19.499 -12.337  33.431  1.00 36.85           N  
ANISOU 1074  N   LEU A 200     3800   5858   4346   -188    794  -1270       N  
ATOM   1075  CA  LEU A 200     -20.305 -13.210  32.584  1.00 38.87           C  
ANISOU 1075  CA  LEU A 200     4100   6068   4602   -193    704  -1267       C  
ATOM   1076  C   LEU A 200     -20.748 -14.474  33.321  1.00 38.95           C  
ANISOU 1076  C   LEU A 200     4034   6006   4760    -85    654  -1273       C  
ATOM   1077  O   LEU A 200     -21.621 -15.203  32.849  1.00 40.86           O  
ANISOU 1077  O   LEU A 200     4299   6182   5044    -94    566  -1255       O  
ATOM   1078  CB  LEU A 200     -19.544 -13.573  31.306  1.00 39.17           C  
ANISOU 1078  CB  LEU A 200     4198   6186   4498   -271    750  -1400       C  
ATOM   1079  CG  LEU A 200     -19.190 -12.400  30.388  1.00 40.18           C  
ANISOU 1079  CG  LEU A 200     4434   6376   4456   -400    808  -1379       C  
ATOM   1080  CD1 LEU A 200     -18.381 -12.869  29.190  1.00 40.94           C  
ANISOU 1080  CD1 LEU A 200     4589   6564   4405   -470    882  -1522       C  
ATOM   1081  CD2 LEU A 200     -20.447 -11.673  29.936  1.00 42.77           C  
ANISOU 1081  CD2 LEU A 200     4868   6634   4750   -436    695  -1220       C  
ATOM   1082  N   ALA A 201     -20.146 -14.726  34.480  1.00 33.16           N  
ANISOU 1082  N   ALA A 201     3216   5281   4102     10    707  -1296       N  
ATOM   1083  CA  ALA A 201     -20.466 -15.910  35.271  1.00 33.03           C  
ANISOU 1083  CA  ALA A 201     3147   5187   4217    121    679  -1288       C  
ATOM   1084  C   ALA A 201     -21.564 -15.628  36.295  1.00 32.80           C  
ANISOU 1084  C   ALA A 201     3096   5073   4293    169    646  -1133       C  
ATOM   1085  O   ALA A 201     -22.057 -16.540  36.958  1.00 33.00           O  
ANISOU 1085  O   ALA A 201     3093   5015   4431    242    628  -1092       O  
ATOM   1086  CB  ALA A 201     -19.218 -16.439  35.961  1.00 31.34           C  
ANISOU 1086  CB  ALA A 201     2861   5033   4014    219    743  -1387       C  
ATOM   1087  N   ILE A 202     -21.940 -14.358  36.411  1.00 26.55           N  
ANISOU 1087  N   ILE A 202     2325   4295   3466    128    652  -1048       N  
ATOM   1088  CA  ILE A 202     -22.984 -13.921  37.344  1.00 26.08           C  
ANISOU 1088  CA  ILE A 202     2245   4165   3499    181    644   -906       C  
ATOM   1089  C   ILE A 202     -24.342 -14.655  37.263  1.00 26.41           C  
ANISOU 1089  C   ILE A 202     2254   4114   3665    188    574   -818       C  
ATOM   1090  O   ILE A 202     -24.900 -15.008  38.303  1.00 26.23           O  
ANISOU 1090  O   ILE A 202     2185   4033   3749    262    601   -740       O  
ATOM   1091  CB  ILE A 202     -23.191 -12.381  37.286  1.00 25.94           C  
ANISOU 1091  CB  ILE A 202     2276   4157   3422    139    664   -838       C  
ATOM   1092  CG1 ILE A 202     -21.934 -11.659  37.772  1.00 25.73           C  
ANISOU 1092  CG1 ILE A 202     2263   4202   3310    128    745   -917       C  
ATOM   1093  CG2 ILE A 202     -24.389 -11.957  38.119  1.00 25.76           C  
ANISOU 1093  CG2 ILE A 202     2228   4056   3502    208    664   -697       C  
ATOM   1094  CD1 ILE A 202     -22.081 -10.155  37.845  1.00 25.79           C  
ANISOU 1094  CD1 ILE A 202     2343   4189   3268     82    780   -860       C  
ATOM   1095  N   PRO A 203     -24.877 -14.889  36.043  1.00 41.08           N  
ANISOU 1095  N   PRO A 203     4136   5968   5506    103    487   -831       N  
ATOM   1096  CA  PRO A 203     -26.184 -15.558  35.944  1.00 42.72           C  
ANISOU 1096  CA  PRO A 203     4288   6099   5844     88    407   -754       C  
ATOM   1097  C   PRO A 203     -26.293 -16.890  36.689  1.00 42.83           C  
ANISOU 1097  C   PRO A 203     4259   6030   5985    136    434   -763       C  
ATOM   1098  O   PRO A 203     -27.395 -17.268  37.086  1.00 44.59           O  
ANISOU 1098  O   PRO A 203     4412   6184   6345    138    418   -664       O  
ATOM   1099  CB  PRO A 203     -26.334 -15.800  34.441  1.00 44.84           C  
ANISOU 1099  CB  PRO A 203     4610   6395   6033    -19    299   -823       C  
ATOM   1100  CG  PRO A 203     -25.583 -14.698  33.823  1.00 45.11           C  
ANISOU 1100  CG  PRO A 203     4728   6514   5899    -53    326   -851       C  
ATOM   1101  CD  PRO A 203     -24.398 -14.461  34.714  1.00 42.16           C  
ANISOU 1101  CD  PRO A 203     4352   6172   5496      9    454   -905       C  
ATOM   1102  N   MET A 204     -25.176 -17.587  36.872  1.00 58.82           N  
ANISOU 1102  N   MET A 204     6321   8058   7970    176    482   -874       N  
ATOM   1103  CA  MET A 204     -25.188 -18.863  37.581  1.00 59.39           C  
ANISOU 1103  CA  MET A 204     6381   8030   8152    238    512   -874       C  
ATOM   1104  C   MET A 204     -25.543 -18.694  39.054  1.00 58.17           C  
ANISOU 1104  C   MET A 204     6185   7839   8076    329    584   -742       C  
ATOM   1105  O   MET A 204     -26.123 -19.589  39.667  1.00 59.79           O  
ANISOU 1105  O   MET A 204     6370   7940   8406    342    602   -668       O  
ATOM   1106  CB  MET A 204     -23.846 -19.576  37.436  1.00 57.73           C  
ANISOU 1106  CB  MET A 204     6216   7838   7878    300    550  -1013       C  
ATOM   1107  CG  MET A 204     -23.592 -20.075  36.034  1.00 59.91           C  
ANISOU 1107  CG  MET A 204     6547   8120   8094    219    501  -1153       C  
ATOM   1108  SD  MET A 204     -24.919 -21.141  35.444  1.00 65.24           S  
ANISOU 1108  SD  MET A 204     7239   8652   8895    114    405  -1139       S  
ATOM   1109  CE  MET A 204     -24.472 -21.311  33.720  1.00 67.14           C  
ANISOU 1109  CE  MET A 204     7573   8949   8988     10    343  -1319       C  
ATOM   1110  N   LEU A 205     -25.197 -17.540  39.615  1.00 23.65           N  
ANISOU 1110  N   LEU A 205     1813   3549   3622    380    635   -716       N  
ATOM   1111  CA  LEU A 205     -25.544 -17.226  40.994  1.00 23.86           C  
ANISOU 1111  CA  LEU A 205     1822   3556   3686    466    710   -604       C  
ATOM   1112  C   LEU A 205     -27.056 -17.112  41.141  1.00 23.98           C  
ANISOU 1112  C   LEU A 205     1776   3508   3829    433    712   -472       C  
ATOM   1113  O   LEU A 205     -27.600 -17.270  42.233  1.00 24.50           O  
ANISOU 1113  O   LEU A 205     1821   3524   3962    495    790   -370       O  
ATOM   1114  CB  LEU A 205     -24.877 -15.920  41.431  1.00 23.74           C  
ANISOU 1114  CB  LEU A 205     1831   3637   3553    496    750   -622       C  
ATOM   1115  CG  LEU A 205     -23.349 -15.878  41.383  1.00 24.06           C  
ANISOU 1115  CG  LEU A 205     1895   3770   3477    520    754   -753       C  
ATOM   1116  CD1 LEU A 205     -22.839 -14.493  41.742  1.00 24.03           C  
ANISOU 1116  CD1 LEU A 205     1912   3846   3374    508    789   -771       C  
ATOM   1117  CD2 LEU A 205     -22.759 -16.926  42.310  1.00 24.67           C  
ANISOU 1117  CD2 LEU A 205     1975   3828   3571    634    775   -761       C  
ATOM   1118  N   PHE A 206     -27.729 -16.839  40.029  1.00 26.37           N  
ANISOU 1118  N   PHE A 206     2043   3819   4158    337    626   -472       N  
ATOM   1119  CA  PHE A 206     -29.176 -16.673  40.024  1.00 26.94           C  
ANISOU 1119  CA  PHE A 206     2018   3854   4362    305    607   -354       C  
ATOM   1120  C   PHE A 206     -29.865 -17.863  39.364  1.00 27.41           C  
ANISOU 1120  C   PHE A 206     2028   3845   4540    206    526   -368       C  
ATOM   1121  O   PHE A 206     -31.093 -17.928  39.313  1.00 28.34           O  
ANISOU 1121  O   PHE A 206     2036   3939   4795    158    496   -281       O  
ATOM   1122  CB  PHE A 206     -29.560 -15.381  39.297  1.00 26.68           C  
ANISOU 1122  CB  PHE A 206     1971   3885   4280    282    547   -324       C  
ATOM   1123  CG  PHE A 206     -29.059 -14.131  39.968  1.00 26.36           C  
ANISOU 1123  CG  PHE A 206     1987   3883   4147    363    632   -304       C  
ATOM   1124  CD1 PHE A 206     -27.737 -13.737  39.836  1.00 25.73           C  
ANISOU 1124  CD1 PHE A 206     2005   3855   3916    362    651   -409       C  
ATOM   1125  CD2 PHE A 206     -29.914 -13.344  40.722  1.00 27.02           C  
ANISOU 1125  CD2 PHE A 206     2021   3947   4300    435    699   -191       C  
ATOM   1126  CE1 PHE A 206     -27.275 -12.588  40.450  1.00 25.61           C  
ANISOU 1126  CE1 PHE A 206     2045   3864   3821    410    723   -404       C  
ATOM   1127  CE2 PHE A 206     -29.458 -12.193  41.336  1.00 26.83           C  
ANISOU 1127  CE2 PHE A 206     2070   3936   4186    502    778   -190       C  
ATOM   1128  CZ  PHE A 206     -28.136 -11.815  41.200  1.00 26.02           C  
ANISOU 1128  CZ  PHE A 206     2074   3878   3934    479    784   -299       C  
ATOM   1129  N   THR A 207     -29.071 -18.805  38.865  1.00 59.21           N  
ANISOU 1129  N   THR A 207     6131   7841   8523    173    493   -488       N  
ATOM   1130  CA  THR A 207     -29.613 -19.955  38.146  1.00 62.01           C  
ANISOU 1130  CA  THR A 207     6470   8114   8975     64    411   -535       C  
ATOM   1131  C   THR A 207     -29.705 -21.207  39.015  1.00 62.95           C  
ANISOU 1131  C   THR A 207     6604   8096   9216     85    491   -504       C  
ATOM   1132  O   THR A 207     -30.774 -21.804  39.139  1.00 64.84           O  
ANISOU 1132  O   THR A 207     6768   8252   9613      3    482   -437       O  
ATOM   1133  CB  THR A 207     -28.789 -20.275  36.883  1.00 63.89           C  
ANISOU 1133  CB  THR A 207     6805   8382   9088      5    326   -701       C  
ATOM   1134  OG1 THR A 207     -28.791 -19.142  36.007  1.00 63.37           O  
ANISOU 1134  OG1 THR A 207     6744   8433   8901    -30    253   -711       O  
ATOM   1135  CG2 THR A 207     -29.377 -21.473  36.154  1.00 67.02           C  
ANISOU 1135  CG2 THR A 207     7206   8680   9578   -116    237   -768       C  
ATOM   1136  N   VAL A 208     -28.584 -21.605  39.609  1.00 30.57           N  
ANISOU 1136  N   VAL A 208     2598   3971   5045    193    566   -547       N  
ATOM   1137  CA  VAL A 208     -28.546 -22.806  40.438  1.00 32.18           C  
ANISOU 1137  CA  VAL A 208     2850   4031   5344    238    642   -505       C  
ATOM   1138  C   VAL A 208     -28.872 -22.495  41.896  1.00 31.20           C  
ANISOU 1138  C   VAL A 208     2703   3901   5250    332    765   -347       C  
ATOM   1139  O   VAL A 208     -28.877 -21.335  42.308  1.00 29.66           O  
ANISOU 1139  O   VAL A 208     2469   3817   4982    386    796   -299       O  
ATOM   1140  CB  VAL A 208     -27.172 -23.503  40.371  1.00 32.11           C  
ANISOU 1140  CB  VAL A 208     2957   3993   5250    335    651   -624       C  
ATOM   1141  CG1 VAL A 208     -26.856 -23.916  38.943  1.00 33.69           C  
ANISOU 1141  CG1 VAL A 208     3198   4186   5417    246    557   -791       C  
ATOM   1142  CG2 VAL A 208     -26.086 -22.593  40.924  1.00 29.55           C  
ANISOU 1142  CG2 VAL A 208     2642   3809   4775    466    690   -641       C  
ATOM   1143  N   GLY A 209     -29.146 -23.539  42.673  1.00 59.49           N  
ANISOU 1143  N   GLY A 209     6329   7342   8933    349    842   -267       N  
ATOM   1144  CA  GLY A 209     -29.428 -23.379  44.087  1.00 59.10           C  
ANISOU 1144  CA  GLY A 209     6287   7279   8889    440    974   -114       C  
ATOM   1145  C   GLY A 209     -29.761 -24.693  44.763  1.00 62.47           C  
ANISOU 1145  C   GLY A 209     6786   7521   9430    433   1058    -23       C  
ATOM   1146  O   GLY A 209     -29.466 -25.763  44.233  1.00 65.14           O  
ANISOU 1146  O   GLY A 209     7199   7731   9821    397   1013    -95       O  
ATOM   1147  N   LEU A 210     -30.376 -24.613  45.938  1.00 42.15           N  
ANISOU 1147  N   LEU A 210     4206   4924   6888    468   1193    138       N  
ATOM   1148  CA  LEU A 210     -30.769 -25.806  46.678  1.00 46.15           C  
ANISOU 1148  CA  LEU A 210     4793   5245   7497    452   1301    256       C  
ATOM   1149  C   LEU A 210     -32.265 -26.062  46.562  1.00 47.81           C  
ANISOU 1149  C   LEU A 210     4869   5386   7912    271   1361    345       C  
ATOM   1150  O   LEU A 210     -33.068 -25.132  46.633  1.00 45.78           O  
ANISOU 1150  O   LEU A 210     4460   5246   7688    235   1391    391       O  
ATOM   1151  CB  LEU A 210     -30.393 -25.672  48.155  1.00 45.39           C  
ANISOU 1151  CB  LEU A 210     4807   5164   7276    616   1430    388       C  
ATOM   1152  CG  LEU A 210     -28.909 -25.679  48.517  1.00 43.79           C  
ANISOU 1152  CG  LEU A 210     4741   5015   6885    805   1373    326       C  
ATOM   1153  CD1 LEU A 210     -28.737 -25.610  50.025  1.00 44.49           C  
ANISOU 1153  CD1 LEU A 210     4942   5115   6848    949   1492    473       C  
ATOM   1154  CD2 LEU A 210     -28.232 -26.916  47.955  1.00 45.39           C  
ANISOU 1154  CD2 LEU A 210     5045   5067   7135    824   1301    249       C  
ATOM   1155  N   GLN A 211     -32.635 -27.327  46.385  1.00 64.38           N  
ANISOU 1155  N   GLN A 211     7016   7287  10158    157   1381    364       N  
ATOM   1156  CA  GLN A 211     -34.042 -27.720  46.400  1.00 63.95           C  
ANISOU 1156  CA  GLN A 211     6826   7153  10319    -35   1454    456       C  
ATOM   1157  C   GLN A 211     -34.235 -29.096  47.029  1.00 66.08           C  
ANISOU 1157  C   GLN A 211     7233   7177  10698    -91   1577    561       C  
ATOM   1158  O   GLN A 211     -33.475 -30.027  46.758  1.00 67.57           O  
ANISOU 1158  O   GLN A 211     7593   7210  10868    -59   1526    492       O  
ATOM   1159  CB  GLN A 211     -34.647 -27.690  44.992  1.00 64.70           C  
ANISOU 1159  CB  GLN A 211     6770   7278  10535   -221   1288    323       C  
ATOM   1160  CG  GLN A 211     -35.133 -26.317  44.549  1.00 61.51           C  
ANISOU 1160  CG  GLN A 211     6171   7096  10104   -219   1216    304       C  
ATOM   1161  CD  GLN A 211     -35.981 -26.374  43.293  1.00 61.68           C  
ANISOU 1161  CD  GLN A 211     6025   7145  10265   -416   1057    215       C  
ATOM   1162  OE1 GLN A 211     -36.041 -27.400  42.616  1.00 63.01           O  
ANISOU 1162  OE1 GLN A 211     6241   7176  10522   -559    977    127       O  
ATOM   1163  NE2 GLN A 211     -36.648 -25.269  42.980  1.00 60.43           N  
ANISOU 1163  NE2 GLN A 211     5677   7160  10122   -418   1002    236       N  
ATOM   1164  N   ASN A 212     -35.254 -29.215  47.875  1.00 69.97           N  
ANISOU 1164  N   ASN A 212     7653   7627  11305   -170   1753    730       N  
ATOM   1165  CA  ASN A 212     -35.574 -30.485  48.514  1.00 71.47           C  
ANISOU 1165  CA  ASN A 212     7976   7572  11608   -248   1899    857       C  
ATOM   1166  C   ASN A 212     -36.488 -31.318  47.622  1.00 71.88           C  
ANISOU 1166  C   ASN A 212     7921   7477  11913   -525   1847    798       C  
ATOM   1167  O   ASN A 212     -37.711 -31.194  47.682  1.00 72.01           O  
ANISOU 1167  O   ASN A 212     7728   7529  12105   -700   1922    868       O  
ATOM   1168  CB  ASN A 212     -36.228 -30.246  49.876  1.00 70.76           C  
ANISOU 1168  CB  ASN A 212     7871   7506  11509   -214   2140   1073       C  
ATOM   1169  CG  ASN A 212     -36.174 -31.467  50.776  1.00 72.15           C  
ANISOU 1169  CG  ASN A 212     8270   7433  11711   -220   2307   1233       C  
ATOM   1170  OD1 ASN A 212     -36.353 -32.597  50.324  1.00 72.79           O  
ANISOU 1170  OD1 ASN A 212     8417   7286  11954   -375   2293   1215       O  
ATOM   1171  ND2 ASN A 212     -35.922 -31.242  52.060  1.00 72.09           N  
ANISOU 1171  ND2 ASN A 212     8401   7458  11534    -50   2466   1391       N  
ATOM   1172  N   LEU A 213     -35.886 -32.168  46.796  1.00 97.68           N  
ANISOU 1172  N   LEU A 213    11327  10584  15201   -565   1719    659       N  
ATOM   1173  CA  LEU A 213     -36.639 -32.947  45.818  1.00 98.54           C  
ANISOU 1173  CA  LEU A 213    11359  10555  15527   -835   1634    558       C  
ATOM   1174  C   LEU A 213     -37.169 -34.266  46.372  1.00100.31           C  
ANISOU 1174  C   LEU A 213    11702  10478  15932   -991   1794    678       C  
ATOM   1175  O   LEU A 213     -37.499 -35.175  45.611  1.00101.81           O  
ANISOU 1175  O   LEU A 213    11917  10481  16285  -1200   1722    574       O  
ATOM   1176  CB  LEU A 213     -35.796 -33.205  44.566  1.00 96.43           C  
ANISOU 1176  CB  LEU A 213    11187  10259  15191   -821   1421    323       C  
ATOM   1177  CG  LEU A 213     -35.431 -31.977  43.731  1.00 94.93           C  
ANISOU 1177  CG  LEU A 213    10868  10349  14851   -737   1249    187       C  
ATOM   1178  CD1 LEU A 213     -34.790 -32.396  42.417  1.00 95.72           C  
ANISOU 1178  CD1 LEU A 213    11057  10402  14911   -783   1062    -47       C  
ATOM   1179  CD2 LEU A 213     -36.655 -31.110  43.483  1.00 93.60           C  
ANISOU 1179  CD2 LEU A 213    10406  10374  14784   -872   1221    230       C  
ATOM   1180  N   SER A 214     -37.254 -34.370  47.694  1.00 56.59           N  
ANISOU 1180  N   SER A 214     6256   4886  10360   -899   2013    895       N  
ATOM   1181  CA  SER A 214     -37.847 -35.549  48.316  1.00 59.83           C  
ANISOU 1181  CA  SER A 214     6777   5012  10942  -1062   2199   1045       C  
ATOM   1182  C   SER A 214     -39.356 -35.547  48.091  1.00 61.80           C  
ANISOU 1182  C   SER A 214     6734   5298  11449  -1370   2258   1077       C  
ATOM   1183  O   SER A 214     -39.910 -34.578  47.569  1.00 60.57           O  
ANISOU 1183  O   SER A 214     6297   5402  11314  -1407   2164   1010       O  
ATOM   1184  CB  SER A 214     -37.525 -35.600  49.810  1.00 60.26           C  
ANISOU 1184  CB  SER A 214     7019   5020  10857   -872   2423   1282       C  
ATOM   1185  OG  SER A 214     -38.006 -34.448  50.479  1.00 59.09           O  
ANISOU 1185  OG  SER A 214     6688   5138  10625   -798   2525   1382       O  
ATOM   1186  N   GLY A 215     -40.014 -36.633  48.483  1.00 76.99           N  
ANISOU 1186  N   GLY A 215     8719   6959  13574  -1591   2412   1181       N  
ATOM   1187  CA  GLY A 215     -41.443 -36.786  48.271  1.00 77.02           C  
ANISOU 1187  CA  GLY A 215     8431   6977  13853  -1916   2471   1204       C  
ATOM   1188  C   GLY A 215     -42.280 -35.671  48.870  1.00 75.71           C  
ANISOU 1188  C   GLY A 215     7970   7098  13698  -1888   2601   1330       C  
ATOM   1189  O   GLY A 215     -43.205 -35.168  48.231  1.00 75.50           O  
ANISOU 1189  O   GLY A 215     7606   7250  13829  -2050   2511   1257       O  
ATOM   1190  N   ASP A 216     -41.953 -35.281  50.097  1.00 98.36           N  
ANISOU 1190  N   ASP A 216    10968  10014  16392  -1669   2808   1515       N  
ATOM   1191  CA  ASP A 216     -42.698 -34.237  50.792  1.00 97.62           C  
ANISOU 1191  CA  ASP A 216    10634  10171  16288  -1615   2972   1639       C  
ATOM   1192  C   ASP A 216     -41.918 -32.927  50.846  1.00 95.28           C  
ANISOU 1192  C   ASP A 216    10343  10138  15723  -1304   2867   1580       C  
ATOM   1193  O   ASP A 216     -42.439 -31.904  51.289  1.00 94.02           O  
ANISOU 1193  O   ASP A 216     9991  10200  15534  -1225   2969   1644       O  
ATOM   1194  CB  ASP A 216     -43.062 -34.692  52.208  1.00101.77           C  
ANISOU 1194  CB  ASP A 216    11301  10581  16787  -1611   3299   1885       C  
ATOM   1195  CG  ASP A 216     -43.989 -35.894  52.216  1.00106.61           C  
ANISOU 1195  CG  ASP A 216    11911  11012  17586  -1895   3354   1910       C  
ATOM   1196  OD1 ASP A 216     -43.975 -36.667  51.235  1.00109.17           O  
ANISOU 1196  OD1 ASP A 216    12226  11178  18075  -2095   3184   1769       O  
ATOM   1197  OD2 ASP A 216     -44.733 -36.066  53.205  1.00109.53           O  
ANISOU 1197  OD2 ASP A 216    12295  11395  17926  -1925   3568   2062       O  
ATOM   1198  N   GLY A 217     -40.669 -32.965  50.393  1.00 79.29           N  
ANISOU 1198  N   GLY A 217     8537   8081  13510  -1132   2672   1451       N  
ATOM   1199  CA  GLY A 217     -39.819 -31.788  50.408  1.00 77.68           C  
ANISOU 1199  CA  GLY A 217     8358   8105  13053   -860   2565   1382       C  
ATOM   1200  C   GLY A 217     -39.364 -31.434  51.810  1.00 77.19           C  
ANISOU 1200  C   GLY A 217     8475   8084  12772   -634   2766   1550       C  
ATOM   1201  O   GLY A 217     -39.044 -30.281  52.098  1.00 76.92           O  
ANISOU 1201  O   GLY A 217     8396   8268  12564   -448   2751   1532       O  
ATOM   1202  N   THR A 218     -39.336 -32.434  52.686  1.00 61.62           N  
ANISOU 1202  N   THR A 218     6722   5891  10799   -654   2951   1715       N  
ATOM   1203  CA  THR A 218     -38.942 -32.229  54.075  1.00 61.49           C  
ANISOU 1203  CA  THR A 218     6909   5896  10556   -450   3147   1893       C  
ATOM   1204  C   THR A 218     -37.726 -33.073  54.442  1.00 62.86           C  
ANISOU 1204  C   THR A 218     7444   5880  10558   -285   3097   1929       C  
ATOM   1205  O   THR A 218     -36.964 -32.720  55.343  1.00 62.98           O  
ANISOU 1205  O   THR A 218     7647   5970  10313    -44   3134   2004       O  
ATOM   1206  CB  THR A 218     -40.093 -32.566  55.043  1.00 62.21           C  
ANISOU 1206  CB  THR A 218     6950   5919  10767   -598   3469   2112       C  
ATOM   1207  OG1 THR A 218     -40.480 -33.936  54.872  1.00 65.02           O  
ANISOU 1207  OG1 THR A 218     7390   5980  11333   -825   3534   2177       O  
ATOM   1208  CG2 THR A 218     -41.293 -31.668  54.782  1.00 62.48           C  
ANISOU 1208  CG2 THR A 218     6601   6166  10972   -723   3533   2085       C  
ATOM   1209  N   HIS A 219     -37.550 -34.188  53.741  1.00 55.36           N  
ANISOU 1209  N   HIS A 219     6592   4686   9758   -408   3005   1870       N  
ATOM   1210  CA  HIS A 219     -36.445 -35.099  54.015  1.00 55.42           C  
ANISOU 1210  CA  HIS A 219     6934   4480   9640   -244   2958   1905       C  
ATOM   1211  C   HIS A 219     -35.112 -34.479  53.605  1.00 51.04           C  
ANISOU 1211  C   HIS A 219     6432   4086   8873     12   2721   1736       C  
ATOM   1212  O   HIS A 219     -34.917 -34.127  52.442  1.00 48.56           O  
ANISOU 1212  O   HIS A 219     5969   3860   8622    -38   2524   1523       O  
ATOM   1213  CB  HIS A 219     -36.658 -36.430  53.291  1.00 58.05           C  
ANISOU 1213  CB  HIS A 219     7354   4493  10211   -450   2927   1862       C  
ATOM   1214  CG  HIS A 219     -35.834 -37.554  53.837  1.00 60.05           C  
ANISOU 1214  CG  HIS A 219     7975   4459  10383   -306   2966   1975       C  
ATOM   1215  ND1 HIS A 219     -34.482 -37.669  53.601  1.00 57.84           N  
ANISOU 1215  ND1 HIS A 219     7869   4170   9939    -45   2782   1871       N  
ATOM   1216  CD2 HIS A 219     -36.173 -38.615  54.607  1.00 64.49           C  
ANISOU 1216  CD2 HIS A 219     8763   4729  11012   -379   3170   2190       C  
ATOM   1217  CE1 HIS A 219     -34.021 -38.751  54.203  1.00 60.91           C  
ANISOU 1217  CE1 HIS A 219     8572   4274  10297     57   2858   2018       C  
ATOM   1218  NE2 HIS A 219     -35.028 -39.343  54.820  1.00 64.91           N  
ANISOU 1218  NE2 HIS A 219     9132   4594  10936   -144   3094   2218       N  
ATOM   1219  N   PRO A 220     -34.187 -34.344  54.569  1.00 50.43           N  
ANISOU 1219  N   PRO A 220     6568   4056   8540    280   2740   1832       N  
ATOM   1220  CA  PRO A 220     -32.876 -33.711  54.380  1.00 46.83           C  
ANISOU 1220  CA  PRO A 220     6152   3776   7868    531   2536   1690       C  
ATOM   1221  C   PRO A 220     -31.991 -34.447  53.376  1.00 46.25           C  
ANISOU 1221  C   PRO A 220     6159   3559   7855    574   2343   1524       C  
ATOM   1222  O   PRO A 220     -31.000 -33.885  52.910  1.00 43.54           O  
ANISOU 1222  O   PRO A 220     5785   3377   7384    733   2166   1366       O  
ATOM   1223  CB  PRO A 220     -32.249 -33.782  55.777  1.00 48.17           C  
ANISOU 1223  CB  PRO A 220     6566   3953   7782    772   2626   1875       C  
ATOM   1224  CG  PRO A 220     -33.402 -33.933  56.710  1.00 51.48           C  
ANISOU 1224  CG  PRO A 220     7011   4304   8244    644   2900   2099       C  
ATOM   1225  CD  PRO A 220     -34.396 -34.762  55.965  1.00 53.72           C  
ANISOU 1225  CD  PRO A 220     7196   4371   8845    349   2969   2094       C  
ATOM   1226  N   GLY A 221     -32.343 -35.688  53.056  1.00 64.94           N  
ANISOU 1226  N   GLY A 221     8635   5623  10418    430   2391   1556       N  
ATOM   1227  CA  GLY A 221     -31.593 -36.467  52.089  1.00 64.96           C  
ANISOU 1227  CA  GLY A 221     8732   5456  10492    464   2233   1391       C  
ATOM   1228  C   GLY A 221     -31.951 -36.100  50.662  1.00 65.25           C  
ANISOU 1228  C   GLY A 221     8541   5581  10670    271   2090   1150       C  
ATOM   1229  O   GLY A 221     -31.245 -36.463  49.721  1.00 64.69           O  
ANISOU 1229  O   GLY A 221     8513   5448  10619    313   1940    963       O  
ATOM   1230  N   GLY A 222     -33.055 -35.377  50.503  1.00 56.00           N  
ANISOU 1230  N   GLY A 222     7129   4560   9590     69   2138   1156       N  
ATOM   1231  CA  GLY A 222     -33.508 -34.949  49.192  1.00 54.84           C  
ANISOU 1231  CA  GLY A 222     6754   4522   9560   -115   1992    950       C  
ATOM   1232  C   GLY A 222     -33.058 -33.540  48.861  1.00 53.22           C  
ANISOU 1232  C   GLY A 222     6383   4652   9187      9   1869    838       C  
ATOM   1233  O   GLY A 222     -33.490 -32.957  47.866  1.00 52.93           O  
ANISOU 1233  O   GLY A 222     6146   4750   9214   -124   1755    698       O  
ATOM   1234  N   LEU A 223     -32.189 -32.989  49.702  1.00 57.12           N  
ANISOU 1234  N   LEU A 223     6968   5273   9461    260   1888    902       N  
ATOM   1235  CA  LEU A 223     -31.651 -31.652  49.485  1.00 56.27           C  
ANISOU 1235  CA  LEU A 223     6732   5461   9185    380   1783    798       C  
ATOM   1236  C   LEU A 223     -30.558 -31.687  48.424  1.00 55.20           C  
ANISOU 1236  C   LEU A 223     6622   5362   8989    460   1593    581       C  
ATOM   1237  O   LEU A 223     -29.419 -32.057  48.708  1.00 54.11           O  
ANISOU 1237  O   LEU A 223     6639   5186   8733    661   1555    562       O  
ATOM   1238  CB  LEU A 223     -31.094 -31.083  50.790  1.00 54.84           C  
ANISOU 1238  CB  LEU A 223     6647   5402   8786    602   1865    929       C  
ATOM   1239  CG  LEU A 223     -30.482 -29.683  50.710  1.00 53.41           C  
ANISOU 1239  CG  LEU A 223     6359   5509   8424    723   1769    825       C  
ATOM   1240  CD1 LEU A 223     -31.533 -28.661  50.308  1.00 53.75           C  
ANISOU 1240  CD1 LEU A 223     6172   5702   8547    573   1790    802       C  
ATOM   1241  CD2 LEU A 223     -29.832 -29.303  52.031  1.00 53.10           C  
ANISOU 1241  CD2 LEU A 223     6452   5562   8160    939   1831    938       C  
ATOM   1242  N   VAL A 224     -30.905 -31.297  47.203  1.00 42.99           N  
ANISOU 1242  N   VAL A 224     4918   3897   7518    309   1476    420       N  
ATOM   1243  CA  VAL A 224     -29.965 -31.372  46.091  1.00 42.09           C  
ANISOU 1243  CA  VAL A 224     4829   3812   7349    354   1318    206       C  
ATOM   1244  C   VAL A 224     -29.628 -30.003  45.506  1.00 39.64           C  
ANISOU 1244  C   VAL A 224     4369   3784   6908    385   1213     89       C  
ATOM   1245  O   VAL A 224     -30.381 -29.038  45.664  1.00 39.19           O  
ANISOU 1245  O   VAL A 224     4162   3874   6853    318   1237    149       O  
ATOM   1246  CB  VAL A 224     -30.496 -32.280  44.965  1.00 43.61           C  
ANISOU 1246  CB  VAL A 224     5027   3822   7718    145   1253     83       C  
ATOM   1247  CG1 VAL A 224     -30.714 -33.694  45.483  1.00 46.27           C  
ANISOU 1247  CG1 VAL A 224     5546   3842   8191    111   1357    183       C  
ATOM   1248  CG2 VAL A 224     -31.783 -31.713  44.390  1.00 43.56           C  
ANISOU 1248  CG2 VAL A 224     4805   3913   7830    -91   1219     75       C  
ATOM   1249  N   CYS A 225     -28.483 -29.934  44.833  1.00 59.50           N  
ANISOU 1249  N   CYS A 225     6930   6362   9314    492   1109    -74       N  
ATOM   1250  CA  CYS A 225     -28.048 -28.722  44.152  1.00 57.09           C  
ANISOU 1250  CA  CYS A 225     6509   6299   8882    508   1014   -195       C  
ATOM   1251  C   CYS A 225     -28.506 -28.750  42.699  1.00 57.87           C  
ANISOU 1251  C   CYS A 225     6538   6400   9047    325    905   -348       C  
ATOM   1252  O   CYS A 225     -27.910 -29.426  41.861  1.00 58.01           O  
ANISOU 1252  O   CYS A 225     6640   6337   9063    323    843   -498       O  
ATOM   1253  CB  CYS A 225     -26.527 -28.585  44.223  1.00 54.34           C  
ANISOU 1253  CB  CYS A 225     6229   6041   8375    714    975   -289       C  
ATOM   1254  SG  CYS A 225     -25.862 -27.133  43.378  1.00 51.54           S  
ANISOU 1254  SG  CYS A 225     5751   5967   7862    715    882   -439       S  
ATOM   1255  N   THR A 226     -29.568 -28.007  42.410  1.00 45.86           N  
ANISOU 1255  N   THR A 226     4869   4978   7578    181    878   -309       N  
ATOM   1256  CA  THR A 226     -30.190 -28.018  41.093  1.00 47.66           C  
ANISOU 1256  CA  THR A 226     5023   5216   7870     -6    757   -428       C  
ATOM   1257  C   THR A 226     -30.536 -26.592  40.665  1.00 45.45           C  
ANISOU 1257  C   THR A 226     4595   5162   7512    -34    689   -427       C  
ATOM   1258  O   THR A 226     -30.712 -25.715  41.515  1.00 42.54           O  
ANISOU 1258  O   THR A 226     4160   4895   7106     48    764   -306       O  
ATOM   1259  CB  THR A 226     -31.465 -28.899  41.107  1.00 49.93           C  
ANISOU 1259  CB  THR A 226     5267   5329   8373   -199    778   -361       C  
ATOM   1260  OG1 THR A 226     -32.079 -28.904  39.813  1.00 49.10           O  
ANISOU 1260  OG1 THR A 226     5084   5252   8320   -389    631   -487       O  
ATOM   1261  CG2 THR A 226     -32.460 -28.384  42.135  1.00 49.45           C  
ANISOU 1261  CG2 THR A 226     5076   5313   8399   -218    892   -162       C  
ATOM   1262  N   PRO A 227     -30.599 -26.343  39.344  1.00 44.72           N  
ANISOU 1262  N   PRO A 227     4472   5141   7378   -140    551   -563       N  
ATOM   1263  CA  PRO A 227     -31.068 -25.047  38.841  1.00 41.61           C  
ANISOU 1263  CA  PRO A 227     3951   4935   6924   -176    473   -546       C  
ATOM   1264  C   PRO A 227     -32.460 -24.699  39.364  1.00 40.40           C  
ANISOU 1264  C   PRO A 227     3627   4797   6925   -250    503   -389       C  
ATOM   1265  O   PRO A 227     -33.396 -25.485  39.212  1.00 41.81           O  
ANISOU 1265  O   PRO A 227     3740   4871   7274   -397    482   -367       O  
ATOM   1266  CB  PRO A 227     -31.096 -25.244  37.316  1.00 42.33           C  
ANISOU 1266  CB  PRO A 227     4067   5049   6968   -307    312   -710       C  
ATOM   1267  CG  PRO A 227     -30.903 -26.724  37.091  1.00 44.78           C  
ANISOU 1267  CG  PRO A 227     4498   5160   7356   -367    316   -811       C  
ATOM   1268  CD  PRO A 227     -30.097 -27.192  38.253  1.00 45.84           C  
ANISOU 1268  CD  PRO A 227     4726   5198   7492   -202    465   -748       C  
ATOM   1269  N   ILE A 228     -32.583 -23.525  39.977  1.00 80.17           N  
ANISOU 1269  N   ILE A 228     8589   9962  11909   -151    559   -287       N  
ATOM   1270  CA  ILE A 228     -33.825 -23.116  40.626  1.00 78.94           C  
ANISOU 1270  CA  ILE A 228     8268   9831  11896   -177    626   -133       C  
ATOM   1271  C   ILE A 228     -34.695 -22.237  39.733  1.00 77.98           C  
ANISOU 1271  C   ILE A 228     7986   9835  11807   -251    492   -130       C  
ATOM   1272  O   ILE A 228     -35.748 -21.761  40.158  1.00 77.29           O  
ANISOU 1272  O   ILE A 228     7730   9793  11846   -258    535    -10       O  
ATOM   1273  CB  ILE A 228     -33.542 -22.358  41.936  1.00 75.71           C  
ANISOU 1273  CB  ILE A 228     7882   9471  11414     -9    787    -21       C  
ATOM   1274  CG1 ILE A 228     -32.659 -21.138  41.661  1.00 73.40           C  
ANISOU 1274  CG1 ILE A 228     7647   9315  10929     99    741    -84       C  
ATOM   1275  CG2 ILE A 228     -32.884 -23.277  42.951  1.00 76.85           C  
ANISOU 1275  CG2 ILE A 228     8170   9492  11539     68    913     12       C  
ATOM   1276  CD1 ILE A 228     -32.241 -20.388  42.907  1.00 71.95           C  
ANISOU 1276  CD1 ILE A 228     7508   9178  10652    253    880     -7       C  
ATOM   1277  N   VAL A 229     -34.254 -22.023  38.498  1.00 59.78           N  
ANISOU 1277  N   VAL A 229     5736   7592   9385   -295    332   -258       N  
ATOM   1278  CA  VAL A 229     -34.995 -21.181  37.567  1.00 59.12           C  
ANISOU 1278  CA  VAL A 229     5531   7632   9299   -348    178   -251       C  
ATOM   1279  C   VAL A 229     -35.657 -22.035  36.483  1.00 61.43           C  
ANISOU 1279  C   VAL A 229     5772   7894   9673   -538      4   -340       C  
ATOM   1280  O   VAL A 229     -35.260 -23.179  36.257  1.00 63.57           O  
ANISOU 1280  O   VAL A 229     6154   8046   9954   -621     -4   -448       O  
ATOM   1281  CB  VAL A 229     -34.086 -20.098  36.944  1.00 56.63           C  
ANISOU 1281  CB  VAL A 229     5327   7428   8760   -260    124   -309       C  
ATOM   1282  CG1 VAL A 229     -33.323 -20.654  35.751  1.00 58.72           C  
ANISOU 1282  CG1 VAL A 229     5734   7686   8888   -340      9   -479       C  
ATOM   1283  CG2 VAL A 229     -34.902 -18.874  36.554  1.00 56.57           C  
ANISOU 1283  CG2 VAL A 229     5195   7539   8759   -235     35   -220       C  
ATOM   1284  N   ASP A 230     -36.671 -21.480  35.823  1.00 87.66           N  
ANISOU 1284  N   ASP A 230     8929  11321  13056   -602   -143   -299       N  
ATOM   1285  CA  ASP A 230     -37.469 -22.230  34.854  1.00 89.89           C  
ANISOU 1285  CA  ASP A 230     9127  11595  13431   -797   -332   -377       C  
ATOM   1286  C   ASP A 230     -36.676 -22.681  33.628  1.00 91.23           C  
ANISOU 1286  C   ASP A 230     9493  11755  13414   -873   -472   -565       C  
ATOM   1287  O   ASP A 230     -35.510 -22.324  33.457  1.00 91.22           O  
ANISOU 1287  O   ASP A 230     9674  11774  13212   -770   -423   -628       O  
ATOM   1288  CB  ASP A 230     -38.696 -21.421  34.423  1.00 91.82           C  
ANISOU 1288  CB  ASP A 230     9137  11984  13767   -820   -480   -284       C  
ATOM   1289  CG  ASP A 230     -38.326 -20.119  33.741  1.00 92.08           C  
ANISOU 1289  CG  ASP A 230     9234  12155  13597   -697   -578   -267       C  
ATOM   1290  OD1 ASP A 230     -37.254 -19.564  34.059  1.00 91.82           O  
ANISOU 1290  OD1 ASP A 230     9373  12114  13399   -566   -459   -275       O  
ATOM   1291  OD2 ASP A 230     -39.110 -19.649  32.889  1.00 93.83           O  
ANISOU 1291  OD2 ASP A 230     9334  12492  13826   -736   -779   -242       O  
ATOM   1292  N   THR A 231     -37.329 -23.469  32.779  1.00 72.30           N  
ANISOU 1292  N   THR A 231     7053   9332  11087  -1062   -641   -662       N  
ATOM   1293  CA  THR A 231     -36.697 -24.046  31.597  1.00 73.20           C  
ANISOU 1293  CA  THR A 231     7361   9423  11029  -1154   -770   -860       C  
ATOM   1294  C   THR A 231     -36.228 -22.978  30.612  1.00 72.89           C  
ANISOU 1294  C   THR A 231     7414   9549  10734  -1082   -888   -889       C  
ATOM   1295  O   THR A 231     -35.157 -23.100  30.017  1.00 73.50           O  
ANISOU 1295  O   THR A 231     7703   9618  10605  -1054   -870  -1020       O  
ATOM   1296  CB  THR A 231     -37.655 -25.017  30.873  1.00 75.50           C  
ANISOU 1296  CB  THR A 231     7573   9667  11446  -1391   -954   -961       C  
ATOM   1297  OG1 THR A 231     -38.124 -26.007  31.797  1.00 76.29           O  
ANISOU 1297  OG1 THR A 231     7592   9597  11798  -1479   -827   -920       O  
ATOM   1298  CG2 THR A 231     -36.953 -25.707  29.713  1.00 76.70           C  
ANISOU 1298  CG2 THR A 231     7962   9772  11410  -1482  -1061  -1188       C  
ATOM   1299  N   ALA A 232     -37.031 -21.931  30.451  1.00 47.74           N  
ANISOU 1299  N   ALA A 232     4068   6508   7564  -1044   -997   -760       N  
ATOM   1300  CA  ALA A 232     -36.717 -20.855  29.514  1.00 47.95           C  
ANISOU 1300  CA  ALA A 232     4185   6681   7353   -978  -1117   -755       C  
ATOM   1301  C   ALA A 232     -35.426 -20.131  29.886  1.00 45.99           C  
ANISOU 1301  C   ALA A 232     4110   6435   6932   -818   -935   -743       C  
ATOM   1302  O   ALA A 232     -34.514 -20.004  29.066  1.00 46.40           O  
ANISOU 1302  O   ALA A 232     4358   6523   6752   -820   -956   -852       O  
ATOM   1303  CB  ALA A 232     -37.874 -19.872  29.431  1.00 46.92           C  
ANISOU 1303  CB  ALA A 232     3839   6681   7310   -935  -1251   -591       C  
ATOM   1304  N   THR A 233     -35.355 -19.659  31.127  1.00 33.05           N  
ANISOU 1304  N   THR A 233     2393   4762   5402   -688   -752   -616       N  
ATOM   1305  CA  THR A 233     -34.183 -18.935  31.608  1.00 30.36           C  
ANISOU 1305  CA  THR A 233     2187   4427   4921   -546   -584   -602       C  
ATOM   1306  C   THR A 233     -32.946 -19.828  31.594  1.00 29.16           C  
ANISOU 1306  C   THR A 233     2209   4194   4676   -558   -479   -759       C  
ATOM   1307  O   THR A 233     -31.845 -19.374  31.277  1.00 27.65           O  
ANISOU 1307  O   THR A 233     2162   4046   4298   -501   -416   -821       O  
ATOM   1308  CB  THR A 233     -34.403 -18.395  33.031  1.00 29.59           C  
ANISOU 1308  CB  THR A 233     1977   4301   4967   -417   -412   -453       C  
ATOM   1309  OG1 THR A 233     -35.647 -17.685  33.089  1.00 31.19           O  
ANISOU 1309  OG1 THR A 233     1990   4566   5293   -394   -494   -312       O  
ATOM   1310  CG2 THR A 233     -33.269 -17.465  33.436  1.00 27.33           C  
ANISOU 1310  CG2 THR A 233     1822   4039   4525   -287   -273   -443       C  
ATOM   1311  N   LEU A 234     -33.140 -21.099  31.937  1.00 35.48           N  
ANISOU 1311  N   LEU A 234     2989   4872   5620   -632   -454   -821       N  
ATOM   1312  CA  LEU A 234     -32.064 -22.081  31.897  1.00 35.21           C  
ANISOU 1312  CA  LEU A 234     3114   4738   5526   -630   -366   -971       C  
ATOM   1313  C   LEU A 234     -31.524 -22.194  30.476  1.00 36.07           C  
ANISOU 1313  C   LEU A 234     3377   4904   5425   -703   -477  -1139       C  
ATOM   1314  O   LEU A 234     -30.309 -22.221  30.260  1.00 35.31           O  
ANISOU 1314  O   LEU A 234     3422   4817   5177   -639   -384  -1244       O  
ATOM   1315  CB  LEU A 234     -32.563 -23.441  32.389  1.00 36.42           C  
ANISOU 1315  CB  LEU A 234     3231   4724   5885   -711   -338   -994       C  
ATOM   1316  CG  LEU A 234     -31.511 -24.535  32.582  1.00 36.35           C  
ANISOU 1316  CG  LEU A 234     3384   4574   5856   -672   -227  -1124       C  
ATOM   1317  CD1 LEU A 234     -30.434 -24.079  33.552  1.00 34.34           C  
ANISOU 1317  CD1 LEU A 234     3170   4338   5539   -484    -54  -1069       C  
ATOM   1318  CD2 LEU A 234     -32.164 -25.819  33.067  1.00 37.91           C  
ANISOU 1318  CD2 LEU A 234     3556   4578   6270   -768   -204  -1122       C  
ATOM   1319  N   LYS A 235     -32.437 -22.247  29.509  1.00 32.30           N  
ANISOU 1319  N   LYS A 235     2865   4477   4933   -837   -675  -1165       N  
ATOM   1320  CA  LYS A 235     -32.063 -22.239  28.101  1.00 33.59           C  
ANISOU 1320  CA  LYS A 235     3184   4714   4862   -912   -798  -1311       C  
ATOM   1321  C   LYS A 235     -31.248 -20.995  27.775  1.00 31.95           C  
ANISOU 1321  C   LYS A 235     3067   4640   4434   -812   -743  -1269       C  
ATOM   1322  O   LYS A 235     -30.211 -21.083  27.126  1.00 31.90           O  
ANISOU 1322  O   LYS A 235     3228   4659   4234   -805   -683  -1401       O  
ATOM   1323  CB  LYS A 235     -33.301 -22.298  27.202  1.00 36.47           C  
ANISOU 1323  CB  LYS A 235     3475   5142   5240  -1062  -1050  -1313       C  
ATOM   1324  CG  LYS A 235     -33.943 -23.670  27.102  1.00 38.95           C  
ANISOU 1324  CG  LYS A 235     3759   5325   5715  -1222  -1130  -1428       C  
ATOM   1325  CD  LYS A 235     -35.166 -23.642  26.199  1.00 42.11           C  
ANISOU 1325  CD  LYS A 235     4060   5818   6123  -1378  -1406  -1434       C  
ATOM   1326  CE  LYS A 235     -35.828 -25.008  26.125  1.00 44.94           C  
ANISOU 1326  CE  LYS A 235     4380   6037   6660  -1569  -1487  -1558       C  
ATOM   1327  NZ  LYS A 235     -37.051 -24.988  25.277  1.00 48.42           N  
ANISOU 1327  NZ  LYS A 235     4688   6585   7123  -1735  -1778  -1569       N  
ATOM   1328  N   VAL A 236     -31.716 -19.841  28.240  1.00 30.92           N  
ANISOU 1328  N   VAL A 236     2825   4582   4340   -737   -749  -1087       N  
ATOM   1329  CA  VAL A 236     -31.038 -18.577  27.962  1.00 29.53           C  
ANISOU 1329  CA  VAL A 236     2741   4509   3972   -657   -697  -1030       C  
ATOM   1330  C   VAL A 236     -29.602 -18.544  28.491  1.00 27.50           C  
ANISOU 1330  C   VAL A 236     2576   4228   3644   -571   -479  -1098       C  
ATOM   1331  O   VAL A 236     -28.679 -18.161  27.771  1.00 27.44           O  
ANISOU 1331  O   VAL A 236     2712   4291   3426   -577   -435  -1175       O  
ATOM   1332  CB  VAL A 236     -31.823 -17.374  28.523  1.00 28.87           C  
ANISOU 1332  CB  VAL A 236     2524   4469   3974   -572   -720   -821       C  
ATOM   1333  CG1 VAL A 236     -31.072 -16.078  28.262  1.00 27.47           C  
ANISOU 1333  CG1 VAL A 236     2470   4364   3604   -503   -651   -767       C  
ATOM   1334  CG2 VAL A 236     -33.211 -17.315  27.905  1.00 31.22           C  
ANISOU 1334  CG2 VAL A 236     2707   4820   4336   -640   -952   -750       C  
ATOM   1335  N   VAL A 237     -29.413 -18.955  29.743  1.00 37.46           N  
ANISOU 1335  N   VAL A 237     3753   5402   5077   -494   -346  -1069       N  
ATOM   1336  CA  VAL A 237     -28.084 -18.921  30.353  1.00 36.46           C  
ANISOU 1336  CA  VAL A 237     3684   5269   4899   -399   -162  -1125       C  
ATOM   1337  C   VAL A 237     -27.143 -19.989  29.784  1.00 36.43           C  
ANISOU 1337  C   VAL A 237     3795   5230   4815   -423   -115  -1323       C  
ATOM   1338  O   VAL A 237     -25.952 -19.731  29.581  1.00 35.42           O  
ANISOU 1338  O   VAL A 237     3741   5162   4556   -377     -4  -1406       O  
ATOM   1339  CB  VAL A 237     -28.146 -19.005  31.901  1.00 35.69           C  
ANISOU 1339  CB  VAL A 237     3477   5099   4983   -294    -44  -1026       C  
ATOM   1340  CG1 VAL A 237     -28.843 -17.779  32.469  1.00 34.78           C  
ANISOU 1340  CG1 VAL A 237     3271   5026   4916   -244    -46   -851       C  
ATOM   1341  CG2 VAL A 237     -28.847 -20.274  32.355  1.00 36.37           C  
ANISOU 1341  CG2 VAL A 237     3503   5056   5261   -328    -66  -1032       C  
ATOM   1342  N   ILE A 238     -27.676 -21.179  29.516  1.00 45.02           N  
ANISOU 1342  N   ILE A 238     4894   6219   5992   -496   -194  -1404       N  
ATOM   1343  CA  ILE A 238     -26.875 -22.246  28.921  1.00 45.29           C  
ANISOU 1343  CA  ILE A 238     5053   6195   5958   -511   -151  -1604       C  
ATOM   1344  C   ILE A 238     -26.439 -21.870  27.505  1.00 45.18           C  
ANISOU 1344  C   ILE A 238     5178   6297   5690   -582   -197  -1721       C  
ATOM   1345  O   ILE A 238     -25.295 -22.109  27.114  1.00 44.57           O  
ANISOU 1345  O   ILE A 238     5198   6248   5487   -541    -82  -1860       O  
ATOM   1346  CB  ILE A 238     -27.625 -23.595  28.922  1.00 45.51           C  
ANISOU 1346  CB  ILE A 238     5083   6062   6146   -592   -226  -1670       C  
ATOM   1347  CG1 ILE A 238     -27.789 -24.105  30.355  1.00 45.90           C  
ANISOU 1347  CG1 ILE A 238     5033   5981   6423   -508   -130  -1563       C  
ATOM   1348  CG2 ILE A 238     -26.880 -24.629  28.094  1.00 45.55           C  
ANISOU 1348  CG2 ILE A 238     5250   5999   6055   -615   -198  -1897       C  
ATOM   1349  CD1 ILE A 238     -28.560 -25.399  30.459  1.00 47.65           C  
ANISOU 1349  CD1 ILE A 238     5261   6020   6824   -601   -180  -1606       C  
ATOM   1350  N   GLN A 239     -27.352 -21.267  26.747  1.00 48.46           N  
ANISOU 1350  N   GLN A 239     5598   6788   6026   -681   -362  -1656       N  
ATOM   1351  CA  GLN A 239     -27.034 -20.760  25.415  1.00 48.71           C  
ANISOU 1351  CA  GLN A 239     5779   6942   5787   -749   -417  -1728       C  
ATOM   1352  C   GLN A 239     -25.998 -19.648  25.504  1.00 48.17           C  
ANISOU 1352  C   GLN A 239     5745   6979   5579   -675   -265  -1679       C  
ATOM   1353  O   GLN A 239     -25.097 -19.563  24.672  1.00 48.59           O  
ANISOU 1353  O   GLN A 239     5933   7104   5425   -697   -185  -1799       O  
ATOM   1354  CB  GLN A 239     -28.291 -20.240  24.714  1.00 50.01           C  
ANISOU 1354  CB  GLN A 239     5925   7171   5903   -845   -645  -1628       C  
ATOM   1355  CG  GLN A 239     -29.229 -21.325  24.214  1.00 51.18           C  
ANISOU 1355  CG  GLN A 239     6072   7251   6121   -969   -825  -1728       C  
ATOM   1356  CD  GLN A 239     -30.590 -20.778  23.831  1.00 52.44           C  
ANISOU 1356  CD  GLN A 239     6137   7486   6300  -1042  -1066  -1597       C  
ATOM   1357  OE1 GLN A 239     -31.544 -21.533  23.641  1.00 54.05           O  
ANISOU 1357  OE1 GLN A 239     6273   7643   6618  -1152  -1229  -1642       O  
ATOM   1358  NE2 GLN A 239     -30.688 -19.458  23.717  1.00 52.59           N  
ANISOU 1358  NE2 GLN A 239     6146   7617   6217   -982  -1091  -1436       N  
ATOM   1359  N   LEU A 240     -26.139 -18.795  26.515  1.00 28.81           N  
ANISOU 1359  N   LEU A 240     3173   4532   3240   -598   -216  -1510       N  
ATOM   1360  CA  LEU A 240     -25.178 -17.728  26.764  1.00 27.65           C  
ANISOU 1360  CA  LEU A 240     3046   4464   2995   -543    -69  -1464       C  
ATOM   1361  C   LEU A 240     -23.777 -18.302  26.933  1.00 28.20           C  
ANISOU 1361  C   LEU A 240     3140   4541   3034   -491    111  -1624       C  
ATOM   1362  O   LEU A 240     -22.833 -17.868  26.270  1.00 29.47           O  
ANISOU 1362  O   LEU A 240     3389   4796   3012   -516    211  -1699       O  
ATOM   1363  CB  LEU A 240     -25.568 -16.939  28.015  1.00 25.15           C  
ANISOU 1363  CB  LEU A 240     2596   4120   2841   -460    -38  -1287       C  
ATOM   1364  CG  LEU A 240     -24.505 -15.998  28.588  1.00 23.98           C  
ANISOU 1364  CG  LEU A 240     2444   4023   2646   -402    127  -1259       C  
ATOM   1365  CD1 LEU A 240     -24.304 -14.787  27.689  1.00 24.76           C  
ANISOU 1365  CD1 LEU A 240     2661   4207   2541   -466    130  -1207       C  
ATOM   1366  CD2 LEU A 240     -24.869 -15.573  30.001  1.00 21.69           C  
ANISOU 1366  CD2 LEU A 240     2027   3677   2537   -309    164  -1128       C  
ATOM   1367  N   ASN A 241     -23.655 -19.287  27.818  1.00 72.51           N  
ANISOU 1367  N   ASN A 241     8670  10053   8828   -413    155  -1669       N  
ATOM   1368  CA  ASN A 241     -22.373 -19.938  28.061  1.00 70.85           C  
ANISOU 1368  CA  ASN A 241     8460   9842   8616   -331    310  -1813       C  
ATOM   1369  C   ASN A 241     -21.819 -20.625  26.815  1.00 71.02           C  
ANISOU 1369  C   ASN A 241     8618   9889   8477   -381    338  -2013       C  
ATOM   1370  O   ASN A 241     -20.637 -20.496  26.499  1.00 69.60           O  
ANISOU 1370  O   ASN A 241     8461   9797   8184   -349    482  -2120       O  
ATOM   1371  CB  ASN A 241     -22.493 -20.948  29.205  1.00 73.09           C  
ANISOU 1371  CB  ASN A 241     8657   9991   9121   -228    329  -1805       C  
ATOM   1372  CG  ASN A 241     -21.170 -21.607  29.542  1.00 71.02           C  
ANISOU 1372  CG  ASN A 241     8382   9730   8872   -107    473  -1938       C  
ATOM   1373  OD1 ASN A 241     -20.104 -21.018  29.362  1.00 69.22           O  
ANISOU 1373  OD1 ASN A 241     8139   9628   8531    -83    581  -1993       O  
ATOM   1374  ND2 ASN A 241     -21.231 -22.839  30.034  1.00 71.53           N  
ANISOU 1374  ND2 ASN A 241     8446   9649   9081    -31    476  -1986       N  
ATOM   1375  N   THR A 242     -22.683 -21.347  26.107  1.00 44.04           N  
ANISOU 1375  N   THR A 242     5285   6400   5048   -466    203  -2070       N  
ATOM   1376  CA  THR A 242     -22.270 -22.109  24.932  1.00 44.30           C  
ANISOU 1376  CA  THR A 242     5472   6436   4925   -517    219  -2278       C  
ATOM   1377  C   THR A 242     -21.772 -21.211  23.800  1.00 44.22           C  
ANISOU 1377  C   THR A 242     5581   6589   4632   -592    262  -2311       C  
ATOM   1378  O   THR A 242     -20.760 -21.503  23.165  1.00 42.74           O  
ANISOU 1378  O   THR A 242     5477   6457   4304   -577    403  -2476       O  
ATOM   1379  CB  THR A 242     -23.412 -23.003  24.410  1.00 47.10           C  
ANISOU 1379  CB  THR A 242     5897   6676   5322   -619     38  -2333       C  
ATOM   1380  OG1 THR A 242     -23.877 -23.854  25.465  1.00 46.94           O  
ANISOU 1380  OG1 THR A 242     5777   6490   5569   -565     21  -2294       O  
ATOM   1381  CG2 THR A 242     -22.933 -23.861  23.250  1.00 47.72           C  
ANISOU 1381  CG2 THR A 242     6158   6740   5234   -666     65  -2575       C  
ATOM   1382  N   PHE A 243     -22.485 -20.118  23.552  1.00 48.17           N  
ANISOU 1382  N   PHE A 243     6091   7160   5050   -667    151  -2148       N  
ATOM   1383  CA  PHE A 243     -22.101 -19.186  22.499  1.00 48.34           C  
ANISOU 1383  CA  PHE A 243     6249   7323   4797   -744    187  -2140       C  
ATOM   1384  C   PHE A 243     -20.880 -18.351  22.880  1.00 46.63           C  
ANISOU 1384  C   PHE A 243     5980   7195   4541   -696    403  -2118       C  
ATOM   1385  O   PHE A 243     -19.945 -18.213  22.092  1.00 46.03           O  
ANISOU 1385  O   PHE A 243     6002   7216   4270   -731    547  -2229       O  
ATOM   1386  CB  PHE A 243     -23.265 -18.258  22.136  1.00 51.64           C  
ANISOU 1386  CB  PHE A 243     6700   7774   5148   -817     -8  -1953       C  
ATOM   1387  CG  PHE A 243     -24.307 -18.897  21.261  1.00 53.64           C  
ANISOU 1387  CG  PHE A 243     7047   8007   5326   -909   -229  -2007       C  
ATOM   1388  CD1 PHE A 243     -23.986 -19.339  19.988  1.00 54.47           C  
ANISOU 1388  CD1 PHE A 243     7354   8171   5173   -989   -233  -2175       C  
ATOM   1389  CD2 PHE A 243     -25.612 -19.035  21.702  1.00 55.20           C  
ANISOU 1389  CD2 PHE A 243     7128   8137   5707   -922   -432  -1895       C  
ATOM   1390  CE1 PHE A 243     -24.943 -19.920  19.177  1.00 56.37           C  
ANISOU 1390  CE1 PHE A 243     7688   8400   5329  -1087   -456  -2240       C  
ATOM   1391  CE2 PHE A 243     -26.575 -19.616  20.897  1.00 56.45           C  
ANISOU 1391  CE2 PHE A 243     7353   8291   5806  -1025   -653  -1954       C  
ATOM   1392  CZ  PHE A 243     -26.240 -20.058  19.633  1.00 57.06           C  
ANISOU 1392  CZ  PHE A 243     7642   8424   5615  -1110   -676  -2130       C  
ATOM   1393  N   MET A 244     -20.891 -17.800  24.090  1.00 58.14           N  
ANISOU 1393  N   MET A 244     7282   8626   6182   -625    430  -1981       N  
ATOM   1394  CA  MET A 244     -19.861 -16.846  24.495  1.00 56.29           C  
ANISOU 1394  CA  MET A 244     6992   8478   5917   -608    603  -1944       C  
ATOM   1395  C   MET A 244     -18.540 -17.482  24.929  1.00 54.34           C  
ANISOU 1395  C   MET A 244     6647   8264   5735   -523    787  -2102       C  
ATOM   1396  O   MET A 244     -17.477 -16.889  24.748  1.00 53.58           O  
ANISOU 1396  O   MET A 244     6534   8279   5544   -548    951  -2144       O  
ATOM   1397  CB  MET A 244     -20.386 -15.924  25.600  1.00 54.35           C  
ANISOU 1397  CB  MET A 244     6637   8193   5822   -572    555  -1748       C  
ATOM   1398  CG  MET A 244     -21.578 -15.066  25.195  1.00 56.59           C  
ANISOU 1398  CG  MET A 244     6997   8458   6045   -632    395  -1573       C  
ATOM   1399  SD  MET A 244     -21.219 -13.923  23.846  1.00 58.29           S  
ANISOU 1399  SD  MET A 244     7415   8779   5952   -755    444  -1532       S  
ATOM   1400  CE  MET A 244     -21.986 -14.765  22.463  1.00 60.05           C  
ANISOU 1400  CE  MET A 244     7800   9019   5998   -825    272  -1614       C  
ATOM   1401  N   SER A 245     -18.601 -18.681  25.501  1.00 74.40           N  
ANISOU 1401  N   SER A 245     9119  10708   8442   -421    762  -2185       N  
ATOM   1402  CA  SER A 245     -17.399 -19.316  26.035  1.00 72.73           C  
ANISOU 1402  CA  SER A 245     8797  10519   8318   -301    914  -2316       C  
ATOM   1403  C   SER A 245     -16.857 -20.430  25.145  1.00 73.34           C  
ANISOU 1403  C   SER A 245     8962  10589   8312   -274    990  -2534       C  
ATOM   1404  O   SER A 245     -15.789 -20.980  25.414  1.00 72.31           O  
ANISOU 1404  O   SER A 245     8744  10490   8239   -161   1129  -2661       O  
ATOM   1405  CB  SER A 245     -17.654 -19.856  27.445  1.00 75.53           C  
ANISOU 1405  CB  SER A 245     9016  10761   8918   -169    861  -2248       C  
ATOM   1406  OG  SER A 245     -18.608 -20.903  27.425  1.00 75.67           O  
ANISOU 1406  OG  SER A 245     9094  10625   9030   -157    739  -2261       O  
ATOM   1407  N   PHE A 246     -17.588 -20.762  24.085  1.00 42.61           N  
ANISOU 1407  N   PHE A 246     5244   6659   4286   -372    896  -2585       N  
ATOM   1408  CA  PHE A 246     -17.180 -21.860  23.214  1.00 44.61           C  
ANISOU 1408  CA  PHE A 246     5615   6884   4451   -352    960  -2808       C  
ATOM   1409  C   PHE A 246     -17.213 -21.495  21.733  1.00 46.92           C  
ANISOU 1409  C   PHE A 246     6106   7278   4444   -492    976  -2881       C  
ATOM   1410  O   PHE A 246     -16.175 -21.211  21.140  1.00 48.47           O  
ANISOU 1410  O   PHE A 246     6324   7574   4518   -490   1141  -2919       O  
ATOM   1411  CB  PHE A 246     -18.039 -23.098  23.474  1.00 44.35           C  
ANISOU 1411  CB  PHE A 246     5624   6655   4574   -317    820  -2853       C  
ATOM   1412  CG  PHE A 246     -17.583 -24.320  22.732  1.00 47.41           C  
ANISOU 1412  CG  PHE A 246     6134   6970   4907   -272    896  -3098       C  
ATOM   1413  CD1 PHE A 246     -16.390 -24.941  23.063  1.00 48.60           C  
ANISOU 1413  CD1 PHE A 246     6206   7109   5150   -105   1069  -3204       C  
ATOM   1414  CD2 PHE A 246     -18.350 -24.855  21.712  1.00 49.18           C  
ANISOU 1414  CD2 PHE A 246     6554   7130   5001   -389    780  -3203       C  
ATOM   1415  CE1 PHE A 246     -15.967 -26.068  22.385  1.00 50.91           C  
ANISOU 1415  CE1 PHE A 246     6622   7296   5428    -39   1124  -3348       C  
ATOM   1416  CE2 PHE A 246     -17.933 -25.983  21.030  1.00 52.13           C  
ANISOU 1416  CE2 PHE A 246     7064   7416   5327   -346    854  -3431       C  
ATOM   1417  CZ  PHE A 246     -16.740 -26.590  21.367  1.00 52.67           C  
ANISOU 1417  CZ  PHE A 246     7059   7441   5513   -159   1027  -3468       C  
ATOM   1418  N   LEU A 247     -18.408 -21.504  21.148  1.00 50.84           N  
ANISOU 1418  N   LEU A 247     6736   7724   4857   -603    776  -2828       N  
ATOM   1419  CA  LEU A 247     -18.578 -21.310  19.707  1.00 52.22           C  
ANISOU 1419  CA  LEU A 247     7133   7983   4724   -731    750  -2904       C  
ATOM   1420  C   LEU A 247     -17.888 -20.063  19.151  1.00 52.50           C  
ANISOU 1420  C   LEU A 247     7216   8193   4538   -800    892  -2832       C  
ATOM   1421  O   LEU A 247     -16.931 -20.174  18.392  1.00 54.29           O  
ANISOU 1421  O   LEU A 247     7511   8461   4655   -780   1051  -2885       O  
ATOM   1422  CB  LEU A 247     -20.063 -21.306  19.337  1.00 52.69           C  
ANISOU 1422  CB  LEU A 247     7287   7984   4751   -837    470  -2815       C  
ATOM   1423  CG  LEU A 247     -20.757 -22.665  19.430  1.00 53.93           C  
ANISOU 1423  CG  LEU A 247     7463   7972   5057   -827    342  -2945       C  
ATOM   1424  CD1 LEU A 247     -22.229 -22.549  19.070  1.00 55.71           C  
ANISOU 1424  CD1 LEU A 247     7735   8163   5269   -948     55  -2848       C  
ATOM   1425  CD2 LEU A 247     -20.059 -23.678  18.534  1.00 55.84           C  
ANISOU 1425  CD2 LEU A 247     7875   8196   5146   -819    463  -3224       C  
ATOM   1426  N   PHE A 248     -18.379 -18.889  19.533  1.00 59.28           N  
ANISOU 1426  N   PHE A 248     8026   9080   5415   -846    808  -2603       N  
ATOM   1427  CA  PHE A 248     -17.828 -17.614  19.062  1.00 59.36           C  
ANISOU 1427  CA  PHE A 248     8099   9222   5230   -928    934  -2504       C  
ATOM   1428  C   PHE A 248     -16.305 -17.446  19.265  1.00 57.62           C  
ANISOU 1428  C   PHE A 248     7765   9067   5061   -876   1203  -2554       C  
ATOM   1429  O   PHE A 248     -15.572 -17.222  18.289  1.00 58.91           O  
ANISOU 1429  O   PHE A 248     8035   9287   5061   -918   1331  -2561       O  
ATOM   1430  CB  PHE A 248     -18.621 -16.442  19.669  1.00 60.62           C  
ANISOU 1430  CB  PHE A 248     8205   9353   5475   -951    798  -2243       C  
ATOM   1431  CG  PHE A 248     -18.086 -15.083  19.316  1.00 60.42           C  
ANISOU 1431  CG  PHE A 248     8250   9422   5282  -1037    927  -2121       C  
ATOM   1432  CD1 PHE A 248     -18.358 -14.514  18.083  1.00 62.23           C  
ANISOU 1432  CD1 PHE A 248     8718   9717   5210  -1147    891  -2063       C  
ATOM   1433  CD2 PHE A 248     -17.336 -14.361  20.231  1.00 58.74           C  
ANISOU 1433  CD2 PHE A 248     7880   9226   5211  -1015   1076  -2060       C  
ATOM   1434  CE1 PHE A 248     -17.875 -13.259  17.761  1.00 62.12           C  
ANISOU 1434  CE1 PHE A 248     8793   9765   5044  -1234   1021  -1935       C  
ATOM   1435  CE2 PHE A 248     -16.851 -13.106  19.915  1.00 58.99           C  
ANISOU 1435  CE2 PHE A 248     7987   9323   5103  -1116   1202  -1951       C  
ATOM   1436  CZ  PHE A 248     -17.121 -12.554  18.679  1.00 60.49           C  
ANISOU 1436  CZ  PHE A 248     8425   9559   4999  -1226   1183  -1882       C  
ATOM   1437  N   PRO A 249     -15.816 -17.578  20.517  1.00 62.31           N  
ANISOU 1437  N   PRO A 249     8130   9631   5916   -769   1262  -2550       N  
ATOM   1438  CA  PRO A 249     -14.386 -17.316  20.726  1.00 62.09           C  
ANISOU 1438  CA  PRO A 249     7964   9653   5974   -723   1458  -2539       C  
ATOM   1439  C   PRO A 249     -13.473 -18.351  20.070  1.00 63.37           C  
ANISOU 1439  C   PRO A 249     8143   9805   6132   -641   1569  -2683       C  
ATOM   1440  O   PRO A 249     -12.420 -17.978  19.558  1.00 65.03           O  
ANISOU 1440  O   PRO A 249     8335  10092   6282   -665   1730  -2682       O  
ATOM   1441  CB  PRO A 249     -14.242 -17.372  22.249  1.00 59.67           C  
ANISOU 1441  CB  PRO A 249     7425   9310   5938   -616   1438  -2501       C  
ATOM   1442  CG  PRO A 249     -15.326 -18.275  22.691  1.00 59.81           C  
ANISOU 1442  CG  PRO A 249     7456   9227   6043   -551   1284  -2564       C  
ATOM   1443  CD  PRO A 249     -16.475 -18.002  21.768  1.00 61.05           C  
ANISOU 1443  CD  PRO A 249     7822   9373   6004   -676   1137  -2521       C  
ATOM   1444  N   MET A 250     -13.863 -19.622  20.084  1.00 69.68           N  
ANISOU 1444  N   MET A 250     8977  10502   6995   -549   1493  -2810       N  
ATOM   1445  CA  MET A 250     -13.052 -20.660  19.453  1.00 71.75           C  
ANISOU 1445  CA  MET A 250     9278  10737   7247   -457   1601  -2954       C  
ATOM   1446  C   MET A 250     -13.135 -20.582  17.936  1.00 74.68           C  
ANISOU 1446  C   MET A 250     9889  11153   7330   -557   1637  -3004       C  
ATOM   1447  O   MET A 250     -12.246 -21.059  17.235  1.00 76.68           O  
ANISOU 1447  O   MET A 250    10181  11432   7522   -506   1783  -3098       O  
ATOM   1448  CB  MET A 250     -13.456 -22.054  19.935  1.00 70.03           C  
ANISOU 1448  CB  MET A 250     9051  10368   7189   -330   1515  -3075       C  
ATOM   1449  CG  MET A 250     -13.082 -22.339  21.376  1.00 68.47           C  
ANISOU 1449  CG  MET A 250     8620  10123   7270   -187   1516  -3034       C  
ATOM   1450  SD  MET A 250     -11.325 -22.082  21.699  1.00 69.44           S  
ANISOU 1450  SD  MET A 250     8537  10355   7489    -88   1707  -3007       S  
ATOM   1451  CE  MET A 250     -11.364 -20.556  22.638  1.00 67.41           C  
ANISOU 1451  CE  MET A 250     8120  10199   7294   -180   1673  -2821       C  
ATOM   1452  N   LEU A 251     -14.211 -19.986  17.435  1.00 53.05           N  
ANISOU 1452  N   LEU A 251     7317   8431   4408   -692   1497  -2937       N  
ATOM   1453  CA  LEU A 251     -14.343 -19.746  16.007  1.00 55.53           C  
ANISOU 1453  CA  LEU A 251     7878   8802   4419   -792   1505  -2952       C  
ATOM   1454  C   LEU A 251     -13.332 -18.680  15.616  1.00 56.41           C  
ANISOU 1454  C   LEU A 251     7965   9034   4434   -848   1703  -2856       C  
ATOM   1455  O   LEU A 251     -12.541 -18.870  14.686  1.00 58.94           O  
ANISOU 1455  O   LEU A 251     8370   9404   4622   -840   1855  -2927       O  
ATOM   1456  CB  LEU A 251     -15.763 -19.293  15.665  1.00 55.16           C  
ANISOU 1456  CB  LEU A 251     7997   8755   4209   -916   1273  -2872       C  
ATOM   1457  CG  LEU A 251     -16.167 -19.271  14.192  1.00 57.98           C  
ANISOU 1457  CG  LEU A 251     8638   9151   4242  -1005   1204  -2898       C  
ATOM   1458  CD1 LEU A 251     -15.793 -20.578  13.516  1.00 60.32           C  
ANISOU 1458  CD1 LEU A 251     9028   9383   4507   -927   1257  -3102       C  
ATOM   1459  CD2 LEU A 251     -17.659 -19.015  14.067  1.00 57.58           C  
ANISOU 1459  CD2 LEU A 251     8702   9088   4088  -1104    914  -2829       C  
ATOM   1460  N   VAL A 252     -13.351 -17.568  16.349  1.00 54.48           N  
ANISOU 1460  N   VAL A 252     7605   8831   4266   -907   1707  -2701       N  
ATOM   1461  CA  VAL A 252     -12.386 -16.493  16.130  1.00 55.25           C  
ANISOU 1461  CA  VAL A 252     7659   9023   4312   -981   1891  -2606       C  
ATOM   1462  C   VAL A 252     -10.947 -17.005  16.225  1.00 56.47           C  
ANISOU 1462  C   VAL A 252     7640   9213   4602   -887   2092  -2708       C  
ATOM   1463  O   VAL A 252     -10.111 -16.711  15.367  1.00 58.84           O  
ANISOU 1463  O   VAL A 252     7996   9593   4769   -935   2264  -2722       O  
ATOM   1464  CB  VAL A 252     -12.587 -15.342  17.136  1.00 52.88           C  
ANISOU 1464  CB  VAL A 252     7234   8730   4128  -1043   1859  -2445       C  
ATOM   1465  CG1 VAL A 252     -11.482 -14.307  16.993  1.00 53.88           C  
ANISOU 1465  CG1 VAL A 252     7298   8933   4241  -1129   2056  -2368       C  
ATOM   1466  CG2 VAL A 252     -13.953 -14.701  16.945  1.00 52.15           C  
ANISOU 1466  CG2 VAL A 252     7326   8619   3871  -1136   1677  -2326       C  
ATOM   1467  N   ALA A 253     -10.674 -17.787  17.264  1.00 62.06           N  
ANISOU 1467  N   ALA A 253     8143   9868   5570   -749   2066  -2775       N  
ATOM   1468  CA  ALA A 253      -9.342 -18.335  17.494  1.00 62.82           C  
ANISOU 1468  CA  ALA A 253     8054  10000   5815   -636   2224  -2864       C  
ATOM   1469  C   ALA A 253      -8.935 -19.328  16.408  1.00 65.88           C  
ANISOU 1469  C   ALA A 253     8574  10383   6073   -565   2324  -3019       C  
ATOM   1470  O   ALA A 253      -7.756 -19.446  16.080  1.00 68.38           O  
ANISOU 1470  O   ALA A 253     8804  10774   6403   -521   2508  -3079       O  
ATOM   1471  CB  ALA A 253      -9.266 -18.987  18.868  1.00 61.76           C  
ANISOU 1471  CB  ALA A 253     7699   9799   5968   -489   2142  -2882       C  
ATOM   1472  N   SER A 254      -9.911 -20.042  15.857  1.00 86.89           N  
ANISOU 1472  N   SER A 254    11445  12959   8610   -556   2201  -3092       N  
ATOM   1473  CA  SER A 254      -9.639 -20.999  14.790  1.00 89.83           C  
ANISOU 1473  CA  SER A 254    11982  13311   8840   -492   2280  -3251       C  
ATOM   1474  C   SER A 254      -9.292 -20.278  13.492  1.00 92.67           C  
ANISOU 1474  C   SER A 254    12516  13783   8910   -610   2411  -3228       C  
ATOM   1475  O   SER A 254      -8.375 -20.684  12.775  1.00 96.48           O  
ANISOU 1475  O   SER A 254    13023  14318   9319   -553   2594  -3330       O  
ATOM   1476  CB  SER A 254     -10.830 -21.934  14.574  1.00 88.67           C  
ANISOU 1476  CB  SER A 254    12018  13029   8644   -469   2088  -3345       C  
ATOM   1477  OG  SER A 254     -12.002 -21.203  14.261  1.00 88.28           O  
ANISOU 1477  OG  SER A 254    12121  12988   8435   -619   1913  -3245       O  
ATOM   1478  N   ILE A 255     -10.029 -19.212  13.192  1.00 64.46           N  
ANISOU 1478  N   ILE A 255     9072  10249   5171   -767   2323  -3088       N  
ATOM   1479  CA  ILE A 255      -9.727 -18.392  12.023  1.00 66.93           C  
ANISOU 1479  CA  ILE A 255     9559  10667   5206   -887   2446  -3030       C  
ATOM   1480  C   ILE A 255      -8.334 -17.786  12.160  1.00 67.88           C  
ANISOU 1480  C   ILE A 255     9487  10889   5414   -902   2692  -2997       C  
ATOM   1481  O   ILE A 255      -7.504 -17.869  11.244  1.00 70.94           O  
ANISOU 1481  O   ILE A 255     9937  11355   5663   -901   2887  -3064       O  
ATOM   1482  CB  ILE A 255     -10.751 -17.251  11.847  1.00 65.89           C  
ANISOU 1482  CB  ILE A 255     9579  10548   4907  -1041   2300  -2850       C  
ATOM   1483  CG1 ILE A 255     -12.176 -17.806  11.785  1.00 65.03           C  
ANISOU 1483  CG1 ILE A 255     9628  10353   4727  -1037   2027  -2878       C  
ATOM   1484  CG2 ILE A 255     -10.431 -16.430  10.609  1.00 68.76           C  
ANISOU 1484  CG2 ILE A 255    10144  11009   4972  -1157   2431  -2777       C  
ATOM   1485  CD1 ILE A 255     -12.361 -18.930  10.792  1.00 67.61           C  
ANISOU 1485  CD1 ILE A 255    10146  10646   4897   -978   1993  -3057       C  
ATOM   1486  N   LEU A 256      -8.085 -17.189  13.322  1.00 65.43           N  
ANISOU 1486  N   LEU A 256     8941  10581   5338   -918   2680  -2901       N  
ATOM   1487  CA  LEU A 256      -6.800 -16.565  13.612  1.00 66.20           C  
ANISOU 1487  CA  LEU A 256     8827  10773   5553   -952   2878  -2871       C  
ATOM   1488  C   LEU A 256      -5.644 -17.552  13.488  1.00 68.35           C  
ANISOU 1488  C   LEU A 256     8958  11086   5924   -805   3042  -3032       C  
ATOM   1489  O   LEU A 256      -4.625 -17.237  12.882  1.00 70.97           O  
ANISOU 1489  O   LEU A 256     9253  11524   6189   -846   3255  -3054       O  
ATOM   1490  CB  LEU A 256      -6.810 -15.924  15.001  1.00 63.18           C  
ANISOU 1490  CB  LEU A 256     8215  10371   5421   -975   2794  -2768       C  
ATOM   1491  CG  LEU A 256      -7.118 -14.425  15.049  1.00 62.42           C  
ANISOU 1491  CG  LEU A 256     8180  10294   5242  -1163   2788  -2591       C  
ATOM   1492  CD1 LEU A 256      -8.417 -14.099  14.329  1.00 62.25           C  
ANISOU 1492  CD1 LEU A 256     8460  10225   4970  -1241   2653  -2505       C  
ATOM   1493  CD2 LEU A 256      -7.170 -13.944  16.487  1.00 59.51           C  
ANISOU 1493  CD2 LEU A 256     7591   9893   5126  -1161   2692  -2518       C  
ATOM   1494  N   ASN A 257      -5.808 -18.743  14.056  1.00 85.19           N  
ANISOU 1494  N   ASN A 257    11017  13133   8219   -631   2949  -3140       N  
ATOM   1495  CA  ASN A 257      -4.803 -19.796  13.931  1.00 87.73           C  
ANISOU 1495  CA  ASN A 257    11228  13471   8632   -460   3092  -3293       C  
ATOM   1496  C   ASN A 257      -4.588 -20.205  12.479  1.00 91.26           C  
ANISOU 1496  C   ASN A 257    11903  13956   8815   -455   3239  -3403       C  
ATOM   1497  O   ASN A 257      -3.454 -20.438  12.048  1.00 94.17           O  
ANISOU 1497  O   ASN A 257    12185  14413   9182   -392   3455  -3486       O  
ATOM   1498  CB  ASN A 257      -5.194 -21.017  14.765  1.00 86.03           C  
ANISOU 1498  CB  ASN A 257    10949  13122   8615   -275   2949  -3376       C  
ATOM   1499  CG  ASN A 257      -4.848 -20.858  16.231  1.00 83.69           C  
ANISOU 1499  CG  ASN A 257    10362  12823   8612   -213   2878  -3306       C  
ATOM   1500  OD1 ASN A 257      -3.822 -21.357  16.693  1.00 84.22           O  
ANISOU 1500  OD1 ASN A 257    10225  12925   8849    -74   2969  -3365       O  
ATOM   1501  ND2 ASN A 257      -5.701 -20.160  16.970  1.00 80.88           N  
ANISOU 1501  ND2 ASN A 257     9991  12430   8309   -307   2711  -3179       N  
ATOM   1502  N   THR A 258      -5.686 -20.289  11.732  1.00 77.54           N  
ANISOU 1502  N   THR A 258    10454  12158   6848   -518   3116  -3407       N  
ATOM   1503  CA  THR A 258      -5.637 -20.634  10.316  1.00 81.34           C  
ANISOU 1503  CA  THR A 258    11195  12675   7037   -526   3221  -3507       C  
ATOM   1504  C   THR A 258      -4.769 -19.648   9.542  1.00 83.92           C  
ANISOU 1504  C   THR A 258    11529  13156   7202   -647   3451  -3441       C  
ATOM   1505  O   THR A 258      -3.927 -20.051   8.738  1.00 87.64           O  
ANISOU 1505  O   THR A 258    12029  13700   7572   -585   3661  -3552       O  
ATOM   1506  CB  THR A 258      -7.046 -20.670   9.692  1.00 79.97           C  
ANISOU 1506  CB  THR A 258    11326  12428   6630   -608   3005  -3492       C  
ATOM   1507  OG1 THR A 258      -7.837 -21.670  10.346  1.00 77.88           O  
ANISOU 1507  OG1 THR A 258    11067  12013   6510   -500   2813  -3583       O  
ATOM   1508  CG2 THR A 258      -6.967 -20.986   8.205  1.00 84.24           C  
ANISOU 1508  CG2 THR A 258    12147  13024   6836   -628   3104  -3586       C  
ATOM   1509  N   VAL A 259      -4.970 -18.357   9.792  1.00 80.67           N  
ANISOU 1509  N   VAL A 259    11096  12787   6767   -818   3420  -3261       N  
ATOM   1510  CA  VAL A 259      -4.164 -17.330   9.134  1.00 83.04           C  
ANISOU 1510  CA  VAL A 259    11404  13218   6931   -958   3640  -3181       C  
ATOM   1511  C   VAL A 259      -2.712 -17.364   9.618  1.00 84.16           C  
ANISOU 1511  C   VAL A 259    11231  13450   7298   -904   3856  -3233       C  
ATOM   1512  O   VAL A 259      -1.771 -17.203   8.832  1.00 87.59           O  
ANISOU 1512  O   VAL A 259    11664  13997   7619   -932   4101  -3275       O  
ATOM   1513  CB  VAL A 259      -4.746 -15.925   9.370  1.00 81.21           C  
ANISOU 1513  CB  VAL A 259    11230  12983   6646  -1152   3551  -2970       C  
ATOM   1514  CG1 VAL A 259      -3.988 -14.891   8.553  1.00 84.13           C  
ANISOU 1514  CG1 VAL A 259    11659  13464   6843  -1309   3784  -2884       C  
ATOM   1515  CG2 VAL A 259      -6.222 -15.904   9.019  1.00 80.08           C  
ANISOU 1515  CG2 VAL A 259    11368  12757   6303  -1187   3310  -2912       C  
ATOM   1516  N   ILE A 260      -2.545 -17.580  10.919  1.00103.85           N  
ANISOU 1516  N   ILE A 260    13455  15901  10102   -825   3759  -3230       N  
ATOM   1517  CA  ILE A 260      -1.230 -17.633  11.549  1.00104.74           C  
ANISOU 1517  CA  ILE A 260    13242  16101  10454   -763   3910  -3275       C  
ATOM   1518  C   ILE A 260      -0.351 -18.723  10.940  1.00107.94           C  
ANISOU 1518  C   ILE A 260    13613  16556  10843   -588   4098  -3451       C  
ATOM   1519  O   ILE A 260       0.845 -18.519  10.731  1.00111.46           O  
ANISOU 1519  O   ILE A 260    13884  17130  11333   -594   4322  -3486       O  
ATOM   1520  CB  ILE A 260      -1.352 -17.840  13.078  1.00 98.03           C  
ANISOU 1520  CB  ILE A 260    12143  15184   9920   -677   3726  -3248       C  
ATOM   1521  CG1 ILE A 260      -1.740 -16.528  13.762  1.00 95.47           C  
ANISOU 1521  CG1 ILE A 260    11771  14854   9647   -862   3620  -3078       C  
ATOM   1522  CG2 ILE A 260      -0.051 -18.346  13.669  1.00 99.35           C  
ANISOU 1522  CG2 ILE A 260    11994  15432  10323   -542   3848  -3336       C  
ATOM   1523  CD1 ILE A 260      -1.952 -16.660  15.253  1.00 92.03           C  
ANISOU 1523  CD1 ILE A 260    11121  14357   9490   -785   3430  -3046       C  
ATOM   1524  N   ALA A 261      -0.951 -19.872  10.642  1.00 83.11           N  
ANISOU 1524  N   ALA A 261    10636  13308   7633   -435   4011  -3567       N  
ATOM   1525  CA  ALA A 261      -0.218 -20.983  10.038  1.00 86.48           C  
ANISOU 1525  CA  ALA A 261    11070  13756   8031   -248   4183  -3745       C  
ATOM   1526  C   ALA A 261       0.420 -20.600   8.701  1.00 90.63           C  
ANISOU 1526  C   ALA A 261    11726  14418   8293   -328   4446  -3780       C  
ATOM   1527  O   ALA A 261       1.638 -20.711   8.527  1.00 93.51           O  
ANISOU 1527  O   ALA A 261    11906  14899   8723   -264   4683  -3846       O  
ATOM   1528  CB  ALA A 261      -1.129 -22.190   9.868  1.00 86.04           C  
ANISOU 1528  CB  ALA A 261    11231  13541   7919   -104   4029  -3862       C  
ATOM   1529  N   ARG A 262      -0.405 -20.144   7.763  1.00144.20           N  
ANISOU 1529  N   ARG A 262    18823  21193  14774   -465   4402  -3731       N  
ATOM   1530  CA  ARG A 262       0.084 -19.769   6.439  1.00148.48           C  
ANISOU 1530  CA  ARG A 262    19533  21859  15023   -548   4638  -3751       C  
ATOM   1531  C   ARG A 262       1.027 -18.568   6.499  1.00149.42           C  
ANISOU 1531  C   ARG A 262    19462  22120  15189   -715   4836  -3631       C  
ATOM   1532  O   ARG A 262       1.971 -18.472   5.709  1.00154.55           O  
ANISOU 1532  O   ARG A 262    20093  22900  15727   -727   5112  -3683       O  
ATOM   1533  CB  ARG A 262      -1.077 -19.507   5.474  1.00137.41           C  
ANISOU 1533  CB  ARG A 262    18518  20414  13275   -658   4511  -3708       C  
ATOM   1534  CG  ARG A 262      -2.008 -18.382   5.890  1.00134.62           C  
ANISOU 1534  CG  ARG A 262    18229  20018  12903   -847   4310  -3503       C  
ATOM   1535  CD  ARG A 262      -3.121 -18.187   4.874  1.00136.16           C  
ANISOU 1535  CD  ARG A 262    18805  20185  12742   -934   4177  -3462       C  
ATOM   1536  NE  ARG A 262      -4.004 -17.081   5.234  1.00134.33           N  
ANISOU 1536  NE  ARG A 262    18641  19915  12482  -1100   3995  -3255       N  
ATOM   1537  CZ  ARG A 262      -3.823 -15.824   4.844  1.00135.78           C  
ANISOU 1537  CZ  ARG A 262    18889  20171  12530  -1278   4100  -3088       C  
ATOM   1538  NH1 ARG A 262      -2.787 -15.508   4.078  1.00139.48           N  
ANISOU 1538  NH1 ARG A 262    19354  20761  12878  -1328   4390  -3104       N  
ATOM   1539  NH2 ARG A 262      -4.677 -14.882   5.219  1.00133.76           N  
ANISOU 1539  NH2 ARG A 262    18707  19859  12257  -1405   3924  -2903       N  
ATOM   1540  N   ARG A 263       0.775 -17.660   7.439  1.00104.51           N  
ANISOU 1540  N   ARG A 263    13636  16405   9669   -848   4702  -3478       N  
ATOM   1541  CA  ARG A 263       1.663 -16.520   7.638  1.00105.42           C  
ANISOU 1541  CA  ARG A 263    13557  16634   9864  -1018   4869  -3373       C  
ATOM   1542  C   ARG A 263       3.038 -17.007   8.088  1.00107.29           C  
ANISOU 1542  C   ARG A 263    13444  16974  10346   -896   5053  -3484       C  
ATOM   1543  O   ARG A 263       4.070 -16.460   7.691  1.00110.37           O  
ANISOU 1543  O   ARG A 263    13710  17503  10721   -990   5303  -3478       O  
ATOM   1544  CB  ARG A 263       1.080 -15.554   8.670  1.00101.49           C  
ANISOU 1544  CB  ARG A 263    12980  16065   9515  -1161   4666  -3208       C  
ATOM   1545  CG  ARG A 263       1.743 -14.186   8.679  1.00102.68           C  
ANISOU 1545  CG  ARG A 263    13029  16303   9682  -1388   4819  -3083       C  
ATOM   1546  CD  ARG A 263       1.470 -13.442   7.382  1.00105.47           C  
ANISOU 1546  CD  ARG A 263    13699  16687   9686  -1555   4949  -2990       C  
ATOM   1547  NE  ARG A 263       0.045 -13.181   7.198  1.00103.98           N  
ANISOU 1547  NE  ARG A 263    13814  16379   9316  -1603   4716  -2879       N  
ATOM   1548  CZ  ARG A 263      -0.482 -12.641   6.104  1.00107.60           C  
ANISOU 1548  CZ  ARG A 263    14600  16841   9443  -1716   4751  -2785       C  
ATOM   1549  NH1 ARG A 263       0.299 -12.304   5.086  1.00112.57           N  
ANISOU 1549  NH1 ARG A 263    15310  17582   9879  -1798   5023  -2788       N  
ATOM   1550  NH2 ARG A 263      -1.790 -12.440   6.027  1.00106.48           N  
ANISOU 1550  NH2 ARG A 263    14704  16595   9157  -1742   4512  -2683       N  
ATOM   1551  N   LEU A 264       3.040 -18.046   8.917  1.00145.05           N  
ANISOU 1551  N   LEU A 264    18069  21689  15356   -682   4928  -3582       N  
ATOM   1552  CA  LEU A 264       4.277 -18.662   9.375  1.00147.16           C  
ANISOU 1552  CA  LEU A 264    18012  22045  15856   -521   5074  -3692       C  
ATOM   1553  C   LEU A 264       4.995 -19.328   8.212  1.00152.01           C  
ANISOU 1553  C   LEU A 264    18708  22751  16300   -409   5349  -3833       C  
ATOM   1554  O   LEU A 264       6.217 -19.234   8.093  1.00155.50           O  
ANISOU 1554  O   LEU A 264    18918  23340  16825   -393   5589  -3879       O  
ATOM   1555  CB  LEU A 264       3.999 -19.693  10.469  1.00139.42           C  
ANISOU 1555  CB  LEU A 264    16897  20949  15127   -299   4866  -3752       C  
ATOM   1556  CG  LEU A 264       5.220 -20.457  10.986  1.00141.23           C  
ANISOU 1556  CG  LEU A 264    16805  21257  15600    -89   4990  -3862       C  
ATOM   1557  CD1 LEU A 264       6.218 -19.506  11.631  1.00141.62           C  
ANISOU 1557  CD1 LEU A 264    16517  21457  15836   -217   5075  -3794       C  
ATOM   1558  CD2 LEU A 264       4.806 -21.551  11.959  1.00138.81           C  
ANISOU 1558  CD2 LEU A 264    16436  20806  15499    140   4777  -3910       C  
ATOM   1559  N   THR A 265       4.233 -20.000   7.354  1.00118.96           N  
ANISOU 1559  N   THR A 265    14847  18480  11871   -331   5314  -3909       N  
ATOM   1560  CA  THR A 265       4.821 -20.680   6.203  1.00123.39           C  
ANISOU 1560  CA  THR A 265    15529  19117  12236   -214   5567  -4058       C  
ATOM   1561  C   THR A 265       5.430 -19.698   5.203  1.00125.89           C  
ANISOU 1561  C   THR A 265    15898  19599  12334   -408   5837  -4000       C  
ATOM   1562  O   THR A 265       6.441 -20.001   4.568  1.00129.00           O  
ANISOU 1562  O   THR A 265    16209  20122  12681   -328   6122  -4102       O  
ATOM   1563  CB  THR A 265       3.804 -21.581   5.474  1.00112.96           C  
ANISOU 1563  CB  THR A 265    14578  17665  10676   -111   5448  -4161       C  
ATOM   1564  OG1 THR A 265       2.738 -20.780   4.948  1.00112.75           O  
ANISOU 1564  OG1 THR A 265    14842  17603  10392   -319   5311  -4041       O  
ATOM   1565  CG2 THR A 265       3.237 -22.627   6.422  1.00109.41           C  
ANISOU 1565  CG2 THR A 265    14084  17040  10445     80   5206  -4227       C  
ATOM   1566  N   VAL A 266       4.820 -18.523   5.063  1.00127.43           N  
ANISOU 1566  N   VAL A 266    16236  19788  12394   -657   5758  -3832       N  
ATOM   1567  CA  VAL A 266       5.339 -17.525   4.130  1.00130.51           C  
ANISOU 1567  CA  VAL A 266    16697  20316  12573   -860   6010  -3753       C  
ATOM   1568  C   VAL A 266       6.494 -16.723   4.738  1.00131.88           C  
ANISOU 1568  C   VAL A 266    16501  20613  12993   -975   6174  -3692       C  
ATOM   1569  O   VAL A 266       7.376 -16.252   4.019  1.00136.04           O  
ANISOU 1569  O   VAL A 266    16976  21288  13422  -1067   6469  -3695       O  
ATOM   1570  CB  VAL A 266       4.228 -16.584   3.591  1.00125.20           C  
ANISOU 1570  CB  VAL A 266    16366  19583  11621  -1076   5881  -3589       C  
ATOM   1571  CG1 VAL A 266       3.755 -15.622   4.667  1.00120.90           C  
ANISOU 1571  CG1 VAL A 266    15708  18956  11271  -1230   5664  -3419       C  
ATOM   1572  CG2 VAL A 266       4.719 -15.820   2.370  1.00129.62           C  
ANISOU 1572  CG2 VAL A 266    17075  20276  11896  -1245   6167  -3530       C  
ATOM   1573  N   MET A 267       6.499 -16.584   6.061  1.00161.80           N  
ANISOU 1573  N   MET A 267    20031  24348  17097   -973   5982  -3644       N  
ATOM   1574  CA  MET A 267       7.582 -15.874   6.736  1.00162.97           C  
ANISOU 1574  CA  MET A 267    19813  24613  17494  -1079   6102  -3606       C  
ATOM   1575  C   MET A 267       8.845 -16.728   6.833  1.00166.41           C  
ANISOU 1575  C   MET A 267    19942  25177  18110   -874   6303  -3763       C  
ATOM   1576  O   MET A 267       9.959 -16.225   6.681  1.00170.84           O  
ANISOU 1576  O   MET A 267    20273  25899  18740   -965   6547  -3769       O  
ATOM   1577  CB  MET A 267       7.155 -15.424   8.135  1.00162.18           C  
ANISOU 1577  CB  MET A 267    19543  24422  17657  -1137   5821  -3513       C  
ATOM   1578  CG  MET A 267       8.277 -14.772   8.930  1.00164.34           C  
ANISOU 1578  CG  MET A 267    19428  24816  18197  -1240   5911  -3495       C  
ATOM   1579  SD  MET A 267       7.879 -14.492  10.665  1.00160.70           S  
ANISOU 1579  SD  MET A 267    18740  24261  18056  -1244   5574  -3431       S  
ATOM   1580  CE  MET A 267       9.476 -13.970  11.288  1.00162.88           C  
ANISOU 1580  CE  MET A 267    18558  24731  18599  -1335   5746  -3467       C  
ATOM   1581  N   VAL A 268       8.663 -18.021   7.082  1.00136.83           N  
ANISOU 1581  N   VAL A 268    16194  21355  14440   -596   6204  -3889       N  
ATOM   1582  CA  VAL A 268       9.783 -18.926   7.324  1.00140.30           C  
ANISOU 1582  CA  VAL A 268    16339  21890  15078   -357   6358  -4032       C  
ATOM   1583  C   VAL A 268      10.603 -19.198   6.059  1.00146.83           C  
ANISOU 1583  C   VAL A 268    17220  22860  15706   -306   6719  -4137       C  
ATOM   1584  O   VAL A 268      11.751 -19.639   6.141  1.00150.35           O  
ANISOU 1584  O   VAL A 268    17379  23434  16311   -158   6919  -4234       O  
ATOM   1585  CB  VAL A 268       9.301 -20.263   7.940  1.00133.53           C  
ANISOU 1585  CB  VAL A 268    15501  20881  14351    -64   6151  -4129       C  
ATOM   1586  CG1 VAL A 268       8.664 -21.150   6.878  1.00135.09           C  
ANISOU 1586  CG1 VAL A 268    16067  20991  14270     70   6194  -4239       C  
ATOM   1587  CG2 VAL A 268      10.443 -20.980   8.650  1.00135.01           C  
ANISOU 1587  CG2 VAL A 268    15303  21150  14842    164   6230  -4222       C  
ATOM   1588  N   HIS A 269      10.011 -18.919   4.899  1.00132.36           N  
ANISOU 1588  N   HIS A 269    15755  21014  13523   -422   6800  -4113       N  
ATOM   1589  CA  HIS A 269      10.655 -19.160   3.607  1.00137.78           C  
ANISOU 1589  CA  HIS A 269    16552  21833  13965   -382   7139  -4210       C  
ATOM   1590  C   HIS A 269      11.113 -20.609   3.447  1.00140.25           C  
ANISOU 1590  C   HIS A 269    16817  22145  14327    -41   7239  -4410       C  
ATOM   1591  O   HIS A 269      10.295 -21.527   3.391  1.00138.64           O  
ANISOU 1591  O   HIS A 269    16848  21785  14045    126   7064  -4492       O  
ATOM   1592  CB  HIS A 269      11.833 -18.203   3.389  1.00142.84           C  
ANISOU 1592  CB  HIS A 269    16936  22678  14659   -566   7437  -4154       C  
ATOM   1593  CG  HIS A 269      11.421 -16.791   3.107  1.00143.17           C  
ANISOU 1593  CG  HIS A 269    17135  22723  14542   -907   7431  -3972       C  
ATOM   1594  ND1 HIS A 269      11.190 -16.325   1.830  1.00147.18           N  
ANISOU 1594  ND1 HIS A 269    17964  23277  14681  -1047   7616  -3929       N  
ATOM   1595  CD2 HIS A 269      11.204 -15.742   3.935  1.00139.78           C  
ANISOU 1595  CD2 HIS A 269    16598  22248  14263  -1129   7267  -3820       C  
ATOM   1596  CE1 HIS A 269      10.846 -15.051   1.884  1.00145.71           C  
ANISOU 1596  CE1 HIS A 269    17865  23065  14433  -1337   7567  -3747       C  
ATOM   1597  NE2 HIS A 269      10.846 -14.673   3.150  1.00141.54           N  
ANISOU 1597  NE2 HIS A 269    17082  22478  14220  -1392   7359  -3684       N  
ATOM   1598  N   PRO A 297      16.341 -15.722  12.694  1.00161.38           N  
ANISOU 1598  N   PRO A 297    16358  25468  19490   -783   6539  -3982       N  
ATOM   1599  CA  PRO A 297      17.289 -16.842  12.738  1.00164.97           C  
ANISOU 1599  CA  PRO A 297    16531  26044  20105   -475   6666  -4107       C  
ATOM   1600  C   PRO A 297      16.943 -17.846  13.835  1.00162.13           C  
ANISOU 1600  C   PRO A 297    16092  25577  19933   -182   6371  -4135       C  
ATOM   1601  O   PRO A 297      16.906 -19.049  13.578  1.00162.47           O  
ANISOU 1601  O   PRO A 297    16199  25565  19967    120   6410  -4214       O  
ATOM   1602  CB  PRO A 297      18.628 -16.159  13.038  1.00166.78           C  
ANISOU 1602  CB  PRO A 297    16323  26509  20536   -621   6822  -4129       C  
ATOM   1603  CG  PRO A 297      18.265 -14.851  13.661  1.00163.85           C  
ANISOU 1603  CG  PRO A 297    15971  26098  20186   -952   6649  -4023       C  
ATOM   1604  CD  PRO A 297      16.988 -14.436  13.003  1.00160.83           C  
ANISOU 1604  CD  PRO A 297    16072  25521  19514  -1096   6599  -3929       C  
ATOM   1605  N   GLY A 298      16.694 -17.351  15.043  1.00173.44           N  
ANISOU 1605  N   GLY A 298    17401  26974  21526   -270   6085  -4071       N  
ATOM   1606  CA  GLY A 298      16.329 -18.206  16.157  1.00170.84           C  
ANISOU 1606  CA  GLY A 298    17007  26541  21364    -15   5793  -4078       C  
ATOM   1607  C   GLY A 298      14.940 -17.889  16.676  1.00164.99           C  
ANISOU 1607  C   GLY A 298    16568  25589  20531   -111   5495  -3978       C  
ATOM   1608  O   GLY A 298      14.408 -18.594  17.533  1.00161.51           O  
ANISOU 1608  O   GLY A 298    16154  25027  20186     88   5248  -3968       O  
ATOM   1609  N   ARG A 299      14.353 -16.820  16.149  1.00140.45           N  
ANISOU 1609  N   ARG A 299    13691  22436  17239   -412   5528  -3898       N  
ATOM   1610  CA  ARG A 299      13.019 -16.395  16.556  1.00134.83           C  
ANISOU 1610  CA  ARG A 299    13266  21533  16431   -523   5270  -3795       C  
ATOM   1611  C   ARG A 299      11.943 -17.208  15.842  1.00133.07           C  
ANISOU 1611  C   ARG A 299    13420  21132  16008   -382   5244  -3795       C  
ATOM   1612  O   ARG A 299      10.876 -17.465  16.398  1.00128.99           O  
ANISOU 1612  O   ARG A 299    13080  20448  15483   -323   4992  -3743       O  
ATOM   1613  CB  ARG A 299      12.828 -14.902  16.275  1.00132.95           C  
ANISOU 1613  CB  ARG A 299    13131  21307  16077   -892   5320  -3702       C  
ATOM   1614  CG  ARG A 299      11.475 -14.353  16.702  1.00127.78           C  
ANISOU 1614  CG  ARG A 299    12759  20463  15331  -1012   5069  -3589       C  
ATOM   1615  CD  ARG A 299      11.343 -12.875  16.369  1.00128.12           C  
ANISOU 1615  CD  ARG A 299    12916  20506  15260  -1364   5144  -3494       C  
ATOM   1616  NE  ARG A 299      10.027 -12.353  16.727  1.00123.81           N  
ANISOU 1616  NE  ARG A 299    12648  19774  14620  -1461   4918  -3381       N  
ATOM   1617  CZ  ARG A 299       9.651 -11.090  16.552  1.00123.11           C  
ANISOU 1617  CZ  ARG A 299    12717  19633  14429  -1742   4934  -3278       C  
ATOM   1618  NH1 ARG A 299      10.492 -10.212  16.024  1.00127.16           N  
ANISOU 1618  NH1 ARG A 299    13144  20256  14916  -1971   5165  -3272       N  
ATOM   1619  NH2 ARG A 299       8.433 -10.704  16.907  1.00118.89           N  
ANISOU 1619  NH2 ARG A 299    12424  18930  13820  -1794   4727  -3177       N  
ATOM   1620  N   VAL A 300      12.234 -17.617  14.611  1.00152.67           N  
ANISOU 1620  N   VAL A 300    16023  23657  18326   -331   5509  -3860       N  
ATOM   1621  CA  VAL A 300      11.271 -18.353  13.796  1.00151.30           C  
ANISOU 1621  CA  VAL A 300    16222  23330  17933   -217   5506  -3880       C  
ATOM   1622  C   VAL A 300      10.953 -19.737  14.363  1.00150.03           C  
ANISOU 1622  C   VAL A 300    16067  23049  17890    111   5348  -3947       C  
ATOM   1623  O   VAL A 300       9.851 -20.252  14.176  1.00148.57           O  
ANISOU 1623  O   VAL A 300    16184  22687  17577    179   5215  -3939       O  
ATOM   1624  CB  VAL A 300      11.751 -18.491  12.336  1.00153.38           C  
ANISOU 1624  CB  VAL A 300    16614  23684  17980   -227   5842  -3950       C  
ATOM   1625  CG1 VAL A 300      11.718 -17.139  11.638  1.00154.31           C  
ANISOU 1625  CG1 VAL A 300    16849  23865  17917   -565   5979  -3857       C  
ATOM   1626  CG2 VAL A 300      13.148 -19.091  12.284  1.00158.20           C  
ANISOU 1626  CG2 VAL A 300    16889  24468  18750    -43   6070  -4067       C  
ATOM   1627  N   GLN A 301      11.919 -20.332  15.057  1.00167.07           N  
ANISOU 1627  N   GLN A 301    17892  25298  20290    312   5362  -4012       N  
ATOM   1628  CA  GLN A 301      11.723 -21.645  15.660  1.00167.16           C  
ANISOU 1628  CA  GLN A 301    17892  25189  20433    635   5224  -4065       C  
ATOM   1629  C   GLN A 301      10.804 -21.552  16.873  1.00161.69           C  
ANISOU 1629  C   GLN A 301    17237  24355  19844    624   4878  -3970       C  
ATOM   1630  O   GLN A 301       9.908 -22.380  17.050  1.00159.02           O  
ANISOU 1630  O   GLN A 301    17109  23831  19481    777   4728  -3972       O  
ATOM   1631  CB  GLN A 301      13.065 -22.264  16.055  1.00173.34           C  
ANISOU 1631  CB  GLN A 301    18298  26119  21447    862   5345  -4148       C  
ATOM   1632  CG  GLN A 301      13.997 -22.517  14.880  1.00179.27           C  
ANISOU 1632  CG  GLN A 301    18999  27008  22110    923   5706  -4254       C  
ATOM   1633  CD  GLN A 301      15.285 -23.201  15.293  1.00183.89           C  
ANISOU 1633  CD  GLN A 301    19200  27732  22939   1180   5820  -4334       C  
ATOM   1634  OE1 GLN A 301      15.500 -23.486  16.471  1.00183.63           O  
ANISOU 1634  OE1 GLN A 301    18938  27695  23140   1311   5618  -4307       O  
ATOM   1635  NE2 GLN A 301      16.150 -23.468  14.322  1.00189.00           N  
ANISOU 1635  NE2 GLN A 301    19775  28509  23530   1260   6148  -4430       N  
ATOM   1636  N   ALA A 302      11.030 -20.539  17.703  1.00138.88           N  
ANISOU 1636  N   ALA A 302    14149  21554  17067    437   4760  -3892       N  
ATOM   1637  CA  ALA A 302      10.179 -20.293  18.860  1.00133.53           C  
ANISOU 1637  CA  ALA A 302    13506  20761  16469    400   4447  -3797       C  
ATOM   1638  C   ALA A 302       8.784 -19.879  18.405  1.00129.51           C  
ANISOU 1638  C   ALA A 302    13373  20090  15747    237   4353  -3720       C  
ATOM   1639  O   ALA A 302       7.789 -20.168  19.071  1.00126.59           O  
ANISOU 1639  O   ALA A 302    13136  19564  15397    293   4118  -3664       O  
ATOM   1640  CB  ALA A 302      10.790 -19.225  19.751  1.00128.22           C  
ANISOU 1640  CB  ALA A 302    12550  20229  15938    221   4367  -3749       C  
ATOM   1641  N   LEU A 303       8.723 -19.201  17.263  1.00 96.21           N  
ANISOU 1641  N   LEU A 303     9321  15914  11322     38   4541  -3714       N  
ATOM   1642  CA  LEU A 303       7.451 -18.798  16.676  1.00 93.65           C  
ANISOU 1642  CA  LEU A 303     9358  15452  10774   -112   4472  -3641       C  
ATOM   1643  C   LEU A 303       6.673 -20.016  16.193  1.00 93.16           C  
ANISOU 1643  C   LEU A 303     9554  15236  10607     92   4436  -3702       C  
ATOM   1644  O   LEU A 303       5.471 -20.121  16.428  1.00 89.83           O  
ANISOU 1644  O   LEU A 303     9350  14659  10125     78   4238  -3645       O  
ATOM   1645  CB  LEU A 303       7.673 -17.815  15.525  1.00 95.87           C  
ANISOU 1645  CB  LEU A 303     9756  15824  10848   -362   4697  -3615       C  
ATOM   1646  CG  LEU A 303       7.368 -16.345  15.824  1.00 94.03           C  
ANISOU 1646  CG  LEU A 303     9540  15600  10587   -662   4626  -3489       C  
ATOM   1647  CD1 LEU A 303       8.108 -15.876  17.067  1.00 93.63           C  
ANISOU 1647  CD1 LEU A 303     9145  15641  10791   -696   4531  -3479       C  
ATOM   1648  CD2 LEU A 303       7.718 -15.473  14.628  1.00 96.96           C  
ANISOU 1648  CD2 LEU A 303    10030  16058  10754   -888   4882  -3462       C  
ATOM   1649  N   ARG A 304       7.366 -20.929  15.517  1.00126.31           N  
ANISOU 1649  N   ARG A 304    13727  19478  14788    280   4632  -3825       N  
ATOM   1650  CA  ARG A 304       6.772 -22.187  15.077  1.00126.48           C  
ANISOU 1650  CA  ARG A 304    13983  19348  14726    495   4614  -3911       C  
ATOM   1651  C   ARG A 304       6.256 -22.963  16.282  1.00123.78           C  
ANISOU 1651  C   ARG A 304    13591  18860  14579    679   4359  -3891       C  
ATOM   1652  O   ARG A 304       5.144 -23.500  16.268  1.00122.18           O  
ANISOU 1652  O   ARG A 304    13639  18479  14303    727   4211  -3888       O  
ATOM   1653  CB  ARG A 304       7.808 -23.027  14.329  1.00136.28           C  
ANISOU 1653  CB  ARG A 304    15151  20673  15957    691   4883  -4053       C  
ATOM   1654  CG  ARG A 304       7.302 -24.387  13.876  1.00137.98           C  
ANISOU 1654  CG  ARG A 304    15609  20723  16094    930   4883  -4166       C  
ATOM   1655  CD  ARG A 304       8.457 -25.338  13.596  1.00143.26           C  
ANISOU 1655  CD  ARG A 304    16116  21460  16854   1194   5110  -4300       C  
ATOM   1656  NE  ARG A 304       9.390 -24.801  12.610  1.00147.83           N  
ANISOU 1656  NE  ARG A 304    16618  22238  17313   1099   5411  -4345       N  
ATOM   1657  CZ  ARG A 304       9.380 -25.120  11.319  1.00151.80           C  
ANISOU 1657  CZ  ARG A 304    17360  22749  17569   1123   5621  -4446       C  
ATOM   1658  NH1 ARG A 304       8.484 -25.979  10.853  1.00151.83           N  
ANISOU 1658  NH1 ARG A 304    17697  22570  17422   1236   5549  -4523       N  
ATOM   1659  NH2 ARG A 304      10.269 -24.582  10.495  1.00155.33           N  
ANISOU 1659  NH2 ARG A 304    17716  23388  17915   1031   5903  -4475       N  
ATOM   1660  N   ARG A 305       7.084 -23.009  17.321  1.00 89.37           N  
ANISOU 1660  N   ARG A 305     8906  14585  10468    777   4310  -3876       N  
ATOM   1661  CA  ARG A 305       6.739 -23.644  18.587  1.00 86.91           C  
ANISOU 1661  CA  ARG A 305     8511  14159  10352    948   4072  -3838       C  
ATOM   1662  C   ARG A 305       5.435 -23.069  19.134  1.00 82.31           C  
ANISOU 1662  C   ARG A 305     8097  13454   9722    788   3825  -3720       C  
ATOM   1663  O   ARG A 305       4.527 -23.809  19.519  1.00 80.15           O  
ANISOU 1663  O   ARG A 305     7982  13004   9468    903   3664  -3708       O  
ATOM   1664  CB  ARG A 305       7.874 -23.427  19.589  1.00 88.13           C  
ANISOU 1664  CB  ARG A 305     8274  14467  10743   1012   4052  -3823       C  
ATOM   1665  CG  ARG A 305       7.745 -24.192  20.892  1.00 86.52           C  
ANISOU 1665  CG  ARG A 305     7958  14170  10745   1229   3833  -3788       C  
ATOM   1666  CD  ARG A 305       8.935 -23.900  21.795  1.00 88.23           C  
ANISOU 1666  CD  ARG A 305     7783  14570  11169   1275   3814  -3779       C  
ATOM   1667  NE  ARG A 305      10.204 -24.215  21.142  1.00 92.99           N  
ANISOU 1667  NE  ARG A 305     8186  15325  11821   1389   4070  -3883       N  
ATOM   1668  CZ  ARG A 305      11.390 -23.786  21.561  1.00 95.52           C  
ANISOU 1668  CZ  ARG A 305     8151  15854  12288   1377   4125  -3899       C  
ATOM   1669  NH1 ARG A 305      11.477 -23.013  22.636  1.00 93.72           N  
ANISOU 1669  NH1 ARG A 305     7743  15706  12162   1249   3934  -3826       N  
ATOM   1670  NH2 ARG A 305      12.491 -24.124  20.903  1.00100.07           N  
ANISOU 1670  NH2 ARG A 305     8549  16564  12908   1491   4375  -3995       N  
ATOM   1671  N   GLY A 306       5.347 -21.742  19.147  1.00 81.06           N  
ANISOU 1671  N   GLY A 306     7909  13387   9505    521   3808  -3635       N  
ATOM   1672  CA  GLY A 306       4.162 -21.054  19.623  1.00 77.05           C  
ANISOU 1672  CA  GLY A 306     7552  12778   8945    360   3600  -3520       C  
ATOM   1673  C   GLY A 306       2.930 -21.336  18.785  1.00 75.81           C  
ANISOU 1673  C   GLY A 306     7749  12473   8583    322   3573  -3521       C  
ATOM   1674  O   GLY A 306       1.825 -21.450  19.314  1.00 72.67           O  
ANISOU 1674  O   GLY A 306     7481  11938   8194    324   3372  -3459       O  
ATOM   1675  N   VAL A 307       3.119 -21.445  17.473  1.00 85.65           N  
ANISOU 1675  N   VAL A 307     9150  13755   9637    286   3774  -3594       N  
ATOM   1676  CA  VAL A 307       2.020 -21.739  16.560  1.00 85.46           C  
ANISOU 1676  CA  VAL A 307     9472  13608   9389    247   3750  -3613       C  
ATOM   1677  C   VAL A 307       1.460 -23.135  16.817  1.00 85.38           C  
ANISOU 1677  C   VAL A 307     9575  13427   9438    477   3642  -3692       C  
ATOM   1678  O   VAL A 307       0.247 -23.310  16.966  1.00 82.42           O  
ANISOU 1678  O   VAL A 307     9398  12910   9008    446   3466  -3658       O  
ATOM   1679  CB  VAL A 307       2.458 -21.626  15.086  1.00 89.43           C  
ANISOU 1679  CB  VAL A 307    10123  14199   9658    180   3999  -3689       C  
ATOM   1680  CG1 VAL A 307       1.361 -22.130  14.161  1.00 89.72           C  
ANISOU 1680  CG1 VAL A 307    10522  14108   9460    180   3954  -3736       C  
ATOM   1681  CG2 VAL A 307       2.823 -20.190  14.750  1.00 89.93           C  
ANISOU 1681  CG2 VAL A 307    10139  14400   9630    -80   4103  -3594       C  
ATOM   1682  N   LEU A 308       2.351 -24.122  16.873  1.00 87.28           N  
ANISOU 1682  N   LEU A 308     9690  13677   9796    706   3752  -3798       N  
ATOM   1683  CA  LEU A 308       1.948 -25.499  17.148  1.00 87.52           C  
ANISOU 1683  CA  LEU A 308     9824  13527   9900    941   3672  -3877       C  
ATOM   1684  C   LEU A 308       1.264 -25.623  18.508  1.00 84.32           C  
ANISOU 1684  C   LEU A 308     9347  13009   9682    986   3419  -3779       C  
ATOM   1685  O   LEU A 308       0.219 -26.269  18.628  1.00 83.00           O  
ANISOU 1685  O   LEU A 308     9377  12662   9496   1033   3280  -3790       O  
ATOM   1686  CB  LEU A 308       3.147 -26.449  17.063  1.00 90.77           C  
ANISOU 1686  CB  LEU A 308    10091  13974  10423   1194   3852  -3995       C  
ATOM   1687  CG  LEU A 308       3.456 -27.068  15.695  1.00 94.56           C  
ANISOU 1687  CG  LEU A 308    10766  14453  10710   1265   4078  -4146       C  
ATOM   1688  CD1 LEU A 308       3.896 -26.017  14.686  1.00 96.37           C  
ANISOU 1688  CD1 LEU A 308    10993  14872  10749   1057   4267  -4137       C  
ATOM   1689  CD2 LEU A 308       4.505 -28.164  15.824  1.00 98.21           C  
ANISOU 1689  CD2 LEU A 308    11093  14902  11321   1567   4222  -4257       C  
ATOM   1690  N   VAL A 309       1.853 -24.998  19.525  1.00 90.73           N  
ANISOU 1690  N   VAL A 309     9879  13929  10664    965   3359  -3688       N  
ATOM   1691  CA  VAL A 309       1.270 -24.999  20.865  1.00 87.49           C  
ANISOU 1691  CA  VAL A 309     9393  13435  10414   1000   3124  -3585       C  
ATOM   1692  C   VAL A 309      -0.130 -24.388  20.868  1.00 83.68           C  
ANISOU 1692  C   VAL A 309     9116  12863   9817    810   2966  -3499       C  
ATOM   1693  O   VAL A 309      -1.062 -24.954  21.442  1.00 81.65           O  
ANISOU 1693  O   VAL A 309     8964  12447   9612    881   2805  -3473       O  
ATOM   1694  CB  VAL A 309       2.162 -24.244  21.877  1.00 88.35           C  
ANISOU 1694  CB  VAL A 309     9182  13702  10686    972   3083  -3509       C  
ATOM   1695  CG1 VAL A 309       1.379 -23.897  23.136  1.00 84.30           C  
ANISOU 1695  CG1 VAL A 309     8642  13120  10269    934   2838  -3385       C  
ATOM   1696  CG2 VAL A 309       3.387 -25.070  22.221  1.00 91.60           C  
ANISOU 1696  CG2 VAL A 309     9367  14172  11265   1216   3172  -3579       C  
ATOM   1697  N   LEU A 310      -0.272 -23.240  20.213  1.00 68.40           N  
ANISOU 1697  N   LEU A 310     7237  11025   7725    574   3021  -3454       N  
ATOM   1698  CA  LEU A 310      -1.548 -22.535  20.168  1.00 65.53           C  
ANISOU 1698  CA  LEU A 310     7056  10596   7247    391   2883  -3362       C  
ATOM   1699  C   LEU A 310      -2.626 -23.351  19.461  1.00 65.43           C  
ANISOU 1699  C   LEU A 310     7334  10428   7099    424   2837  -3429       C  
ATOM   1700  O   LEU A 310      -3.737 -23.498  19.975  1.00 62.91           O  
ANISOU 1700  O   LEU A 310     7111   9987   6806    411   2659  -3379       O  
ATOM   1701  CB  LEU A 310      -1.391 -21.174  19.488  1.00 65.88           C  
ANISOU 1701  CB  LEU A 310     7126  10770   7138    145   2980  -3301       C  
ATOM   1702  CG  LEU A 310      -2.636 -20.286  19.491  1.00 63.12           C  
ANISOU 1702  CG  LEU A 310     6945  10364   6675    -42   2844  -3187       C  
ATOM   1703  CD1 LEU A 310      -2.994 -19.855  20.905  1.00 60.06           C  
ANISOU 1703  CD1 LEU A 310     6411   9946   6464    -45   2660  -3079       C  
ATOM   1704  CD2 LEU A 310      -2.436 -19.080  18.592  1.00 64.26           C  
ANISOU 1704  CD2 LEU A 310     7170  10614   6632   -266   2973  -3136       C  
ATOM   1705  N   ARG A 311      -2.297 -23.876  18.283  1.00109.37           N  
ANISOU 1705  N   ARG A 311    13038  16001  12516    462   2997  -3550       N  
ATOM   1706  CA  ARG A 311      -3.232 -24.717  17.539  1.00109.88           C  
ANISOU 1706  CA  ARG A 311    13390  15918  12439    494   2954  -3644       C  
ATOM   1707  C   ARG A 311      -3.639 -25.937  18.359  1.00108.23           C  
ANISOU 1707  C   ARG A 311    13185  15530  12408    689   2827  -3688       C  
ATOM   1708  O   ARG A 311      -4.811 -26.329  18.372  1.00107.07           O  
ANISOU 1708  O   ARG A 311    13220  15238  12223    657   2679  -3697       O  
ATOM   1709  CB  ARG A 311      -2.633 -25.150  16.198  1.00113.08           C  
ANISOU 1709  CB  ARG A 311    13934  16368  12662    534   3162  -3783       C  
ATOM   1710  CG  ARG A 311      -2.647 -24.064  15.132  1.00114.89           C  
ANISOU 1710  CG  ARG A 311    14301  16719  12633    317   3255  -3747       C  
ATOM   1711  CD  ARG A 311      -2.200 -24.604  13.782  1.00119.73           C  
ANISOU 1711  CD  ARG A 311    15091  17361  13040    371   3450  -3895       C  
ATOM   1712  NE  ARG A 311      -0.768 -24.889  13.747  1.00123.12           N  
ANISOU 1712  NE  ARG A 311    15308  17908  13564    495   3675  -3956       N  
ATOM   1713  CZ  ARG A 311      -0.147 -25.468  12.725  1.00127.01           C  
ANISOU 1713  CZ  ARG A 311    15895  18436  13926    593   3879  -4095       C  
ATOM   1714  NH1 ARG A 311      -0.833 -25.834  11.651  1.00129.26           N  
ANISOU 1714  NH1 ARG A 311    16500  18643  13968    579   3876  -4195       N  
ATOM   1715  NH2 ARG A 311       1.160 -25.687  12.778  1.00129.08           N  
ANISOU 1715  NH2 ARG A 311    15932  18816  14296    709   4084  -4142       N  
ATOM   1716  N   ALA A 312      -2.664 -26.524  19.050  1.00 70.18           N  
ANISOU 1716  N   ALA A 312     8162  10719   7784    887   2885  -3710       N  
ATOM   1717  CA  ALA A 312      -2.924 -27.656  19.932  1.00 69.61           C  
ANISOU 1717  CA  ALA A 312     8082  10472   7895   1090   2778  -3731       C  
ATOM   1718  C   ALA A 312      -3.911 -27.276  21.032  1.00 65.89           C  
ANISOU 1718  C   ALA A 312     7576   9932   7525   1019   2558  -3599       C  
ATOM   1719  O   ALA A 312      -4.824 -28.038  21.346  1.00 64.90           O  
ANISOU 1719  O   ALA A 312     7588   9626   7446   1074   2438  -3618       O  
ATOM   1720  CB  ALA A 312      -1.626 -28.169  20.535  1.00 71.55           C  
ANISOU 1720  CB  ALA A 312     8091  10768   8328   1312   2874  -3749       C  
ATOM   1721  N   MET A 313      -3.725 -26.092  21.608  1.00 77.15           N  
ANISOU 1721  N   MET A 313     8826  11502   8987    893   2513  -3470       N  
ATOM   1722  CA  MET A 313      -4.607 -25.610  22.664  1.00 73.85           C  
ANISOU 1722  CA  MET A 313     8369  11038   8652    824   2321  -3341       C  
ATOM   1723  C   MET A 313      -6.022 -25.368  22.149  1.00 72.36           C  
ANISOU 1723  C   MET A 313     8412  10765   8318    662   2224  -3333       C  
ATOM   1724  O   MET A 313      -7.000 -25.634  22.850  1.00 70.94           O  
ANISOU 1724  O   MET A 313     8277  10464   8215    675   2072  -3287       O  
ATOM   1725  CB  MET A 313      -4.051 -24.332  23.299  1.00 75.86           C  
ANISOU 1725  CB  MET A 313     8408  11462   8952    711   2307  -3223       C  
ATOM   1726  CG  MET A 313      -2.815 -24.551  24.159  1.00 77.22           C  
ANISOU 1726  CG  MET A 313     8322  11717   9302    869   2336  -3214       C  
ATOM   1727  SD  MET A 313      -2.352 -23.092  25.114  1.00 75.52           S  
ANISOU 1727  SD  MET A 313     7876  11667   9150    722   2264  -3085       S  
ATOM   1728  CE  MET A 313      -2.006 -21.919  23.806  1.00 76.27           C  
ANISOU 1728  CE  MET A 313     8018  11907   9053    475   2435  -3109       C  
ATOM   1729  N   VAL A 314      -6.126 -24.866  20.923  1.00 59.13           N  
ANISOU 1729  N   VAL A 314     6882   9158   6428    512   2311  -3375       N  
ATOM   1730  CA  VAL A 314      -7.428 -24.604  20.320  1.00 58.06           C  
ANISOU 1730  CA  VAL A 314     6972   8962   6128    355   2211  -3369       C  
ATOM   1731  C   VAL A 314      -8.183 -25.901  20.041  1.00 58.87           C  
ANISOU 1731  C   VAL A 314     7269   8875   6224    441   2143  -3494       C  
ATOM   1732  O   VAL A 314      -9.340 -26.053  20.448  1.00 57.09           O  
ANISOU 1732  O   VAL A 314     7126   8540   6026    390   1983  -3470       O  
ATOM   1733  CB  VAL A 314      -7.303 -23.783  19.022  1.00 59.55           C  
ANISOU 1733  CB  VAL A 314     7294   9270   6063    183   2318  -3377       C  
ATOM   1734  CG1 VAL A 314      -8.659 -23.649  18.346  1.00 58.90           C  
ANISOU 1734  CG1 VAL A 314     7461   9123   5796     42   2191  -3378       C  
ATOM   1735  CG2 VAL A 314      -6.715 -22.413  19.318  1.00 58.72           C  
ANISOU 1735  CG2 VAL A 314     7021   9324   5965     62   2375  -3248       C  
ATOM   1736  N   ILE A 315      -7.528 -26.837  19.357  1.00 63.73           N  
ANISOU 1736  N   ILE A 315     7961   9445   6808    569   2269  -3635       N  
ATOM   1737  CA  ILE A 315      -8.165 -28.116  19.051  1.00 64.95           C  
ANISOU 1737  CA  ILE A 315     8323   9399   6957    649   2215  -3772       C  
ATOM   1738  C   ILE A 315      -8.504 -28.896  20.324  1.00 63.48           C  
ANISOU 1738  C   ILE A 315     8053   9047   7019    791   2101  -3742       C  
ATOM   1739  O   ILE A 315      -9.540 -29.562  20.396  1.00 63.06           O  
ANISOU 1739  O   ILE A 315     8153   8817   6988    768   1977  -3794       O  
ATOM   1740  CB  ILE A 315      -7.326 -28.980  18.068  1.00 68.71           C  
ANISOU 1740  CB  ILE A 315     8915   9852   7342    773   2390  -3938       C  
ATOM   1741  CG1 ILE A 315      -5.955 -29.327  18.655  1.00 69.97           C  
ANISOU 1741  CG1 ILE A 315     8849  10061   7678    986   2532  -3934       C  
ATOM   1742  CG2 ILE A 315      -7.167 -28.265  16.734  1.00 70.38           C  
ANISOU 1742  CG2 ILE A 315     9256  10210   7278    623   2493  -3971       C  
ATOM   1743  CD1 ILE A 315      -5.858 -30.734  19.216  1.00 71.10           C  
ANISOU 1743  CD1 ILE A 315     9022   9995   7998   1219   2520  -4014       C  
ATOM   1744  N   ALA A 316      -7.638 -28.794  21.329  1.00 60.92           N  
ANISOU 1744  N   ALA A 316     7489   8781   6877    928   2138  -3655       N  
ATOM   1745  CA  ALA A 316      -7.890 -29.437  22.613  1.00 59.60           C  
ANISOU 1745  CA  ALA A 316     7239   8473   6934   1072   2031  -3597       C  
ATOM   1746  C   ALA A 316      -9.108 -28.818  23.283  1.00 56.45           C  
ANISOU 1746  C   ALA A 316     6836   8049   6562    929   1858  -3487       C  
ATOM   1747  O   ALA A 316      -9.946 -29.526  23.836  1.00 55.73           O  
ANISOU 1747  O   ALA A 316     6824   7776   6577    970   1750  -3496       O  
ATOM   1748  CB  ALA A 316      -6.675 -29.330  23.518  1.00 59.82           C  
ANISOU 1748  CB  ALA A 316     7009   8600   7119   1236   2088  -3514       C  
ATOM   1749  N   PHE A 317      -9.202 -27.493  23.226  1.00 58.01           N  
ANISOU 1749  N   PHE A 317     6951   8422   6670    761   1841  -3385       N  
ATOM   1750  CA  PHE A 317     -10.330 -26.783  23.817  1.00 55.21           C  
ANISOU 1750  CA  PHE A 317     6588   8063   6328    629   1693  -3278       C  
ATOM   1751  C   PHE A 317     -11.633 -27.213  23.156  1.00 55.34           C  
ANISOU 1751  C   PHE A 317     6832   7945   6249    516   1597  -3368       C  
ATOM   1752  O   PHE A 317     -12.604 -27.540  23.839  1.00 53.96           O  
ANISOU 1752  O   PHE A 317     6675   7643   6184    511   1472  -3346       O  
ATOM   1753  CB  PHE A 317     -10.146 -25.269  23.686  1.00 53.97           C  
ANISOU 1753  CB  PHE A 317     6341   8102   6063    465   1713  -3167       C  
ATOM   1754  CG  PHE A 317     -11.062 -24.465  24.570  1.00 51.12           C  
ANISOU 1754  CG  PHE A 317     5920   7750   5755    377   1580  -3035       C  
ATOM   1755  CD1 PHE A 317     -12.370 -24.212  24.192  1.00 50.20           C  
ANISOU 1755  CD1 PHE A 317     5948   7588   5538    235   1479  -3038       C  
ATOM   1756  CD2 PHE A 317     -10.612 -23.964  25.780  1.00 49.63           C  
ANISOU 1756  CD2 PHE A 317     5532   7617   5708    440   1551  -2912       C  
ATOM   1757  CE1 PHE A 317     -13.212 -23.472  25.001  1.00 47.82           C  
ANISOU 1757  CE1 PHE A 317     5586   7297   5288    170   1372  -2923       C  
ATOM   1758  CE2 PHE A 317     -11.449 -23.224  26.595  1.00 47.22           C  
ANISOU 1758  CE2 PHE A 317     5184   7315   5444    371   1443  -2794       C  
ATOM   1759  CZ  PHE A 317     -12.751 -22.979  26.204  1.00 46.32           C  
ANISOU 1759  CZ  PHE A 317     5206   7155   5240    243   1365  -2800       C  
ATOM   1760  N   VAL A 318     -11.647 -27.221  21.826  1.00 54.01           N  
ANISOU 1760  N   VAL A 318     6838   7809   5875    419   1653  -3471       N  
ATOM   1761  CA  VAL A 318     -12.837 -27.623  21.082  1.00 54.59           C  
ANISOU 1761  CA  VAL A 318     7141   7771   5830    291   1539  -3565       C  
ATOM   1762  C   VAL A 318     -13.246 -29.061  21.401  1.00 55.58           C  
ANISOU 1762  C   VAL A 318     7362   7650   6105    400   1484  -3680       C  
ATOM   1763  O   VAL A 318     -14.381 -29.313  21.812  1.00 54.52           O  
ANISOU 1763  O   VAL A 318     7278   7389   6049    325   1335  -3682       O  
ATOM   1764  CB  VAL A 318     -12.635 -27.476  19.561  1.00 56.98           C  
ANISOU 1764  CB  VAL A 318     7633   8152   5863    191   1610  -3657       C  
ATOM   1765  CG1 VAL A 318     -13.844 -28.015  18.812  1.00 57.99           C  
ANISOU 1765  CG1 VAL A 318     8007   8157   5870     64   1461  -3764       C  
ATOM   1766  CG2 VAL A 318     -12.384 -26.021  19.199  1.00 56.16           C  
ANISOU 1766  CG2 VAL A 318     7473   8263   5604     58   1656  -3533       C  
ATOM   1767  N   VAL A 319     -12.312 -29.993  21.223  1.00 57.80           N  
ANISOU 1767  N   VAL A 319     7670   7857   6436    575   1609  -3775       N  
ATOM   1768  CA  VAL A 319     -12.582 -31.412  21.449  1.00 59.29           C  
ANISOU 1768  CA  VAL A 319     7983   7785   6759    692   1581  -3889       C  
ATOM   1769  C   VAL A 319     -13.045 -31.713  22.876  1.00 57.35           C  
ANISOU 1769  C   VAL A 319     7620   7404   6767    778   1488  -3792       C  
ATOM   1770  O   VAL A 319     -14.018 -32.439  23.080  1.00 57.51           O  
ANISOU 1770  O   VAL A 319     7764   7209   6881    734   1382  -3848       O  
ATOM   1771  CB  VAL A 319     -11.351 -32.283  21.109  1.00 62.15           C  
ANISOU 1771  CB  VAL A 319     8374   8105   7137    903   1752  -3988       C  
ATOM   1772  CG1 VAL A 319     -11.548 -33.712  21.594  1.00 63.56           C  
ANISOU 1772  CG1 VAL A 319     8662   7993   7494   1059   1730  -4070       C  
ATOM   1773  CG2 VAL A 319     -11.081 -32.256  19.612  1.00 64.68           C  
ANISOU 1773  CG2 VAL A 319     8874   8500   7202    824   1841  -4121       C  
ATOM   1774  N   CYS A 320     -12.353 -31.144  23.859  1.00 55.72           N  
ANISOU 1774  N   CYS A 320     7181   7320   6670    887   1525  -3644       N  
ATOM   1775  CA  CYS A 320     -12.670 -31.403  25.262  1.00 54.09           C  
ANISOU 1775  CA  CYS A 320     6863   7002   6686    994   1447  -3533       C  
ATOM   1776  C   CYS A 320     -13.971 -30.741  25.713  1.00 51.60           C  
ANISOU 1776  C   CYS A 320     6529   6683   6395    822   1304  -3459       C  
ATOM   1777  O   CYS A 320     -14.746 -31.334  26.464  1.00 51.09           O  
ANISOU 1777  O   CYS A 320     6494   6423   6496    849   1222  -3443       O  
ATOM   1778  CB  CYS A 320     -11.518 -30.963  26.170  1.00 53.38           C  
ANISOU 1778  CB  CYS A 320     6538   7061   6682   1156   1509  -3394       C  
ATOM   1779  SG  CYS A 320      -9.983 -31.886  25.930  1.00 56.54           S  
ANISOU 1779  SG  CYS A 320     6917   7448   7119   1404   1670  -3467       S  
ATOM   1780  N   TRP A 321     -14.211 -29.516  25.256  1.00 64.30           N  
ANISOU 1780  N   TRP A 321     8093   8493   7843    649   1282  -3411       N  
ATOM   1781  CA  TRP A 321     -15.387 -28.770  25.694  1.00 63.35           C  
ANISOU 1781  CA  TRP A 321     7936   8393   7739    500   1155  -3334       C  
ATOM   1782  C   TRP A 321     -16.624 -29.012  24.831  1.00 64.07           C  
ANISOU 1782  C   TRP A 321     8217   8387   7740    301   1036  -3444       C  
ATOM   1783  O   TRP A 321     -17.697 -28.477  25.116  1.00 63.80           O  
ANISOU 1783  O   TRP A 321     8161   8343   7735    164    880  -3272       O  
ATOM   1784  CB  TRP A 321     -15.082 -27.272  25.785  1.00 62.82           C  
ANISOU 1784  CB  TRP A 321     7728   8577   7562    421   1177  -3200       C  
ATOM   1785  CG  TRP A 321     -14.128 -26.930  26.888  1.00 61.15           C  
ANISOU 1785  CG  TRP A 321     7312   8448   7472    575   1231  -3064       C  
ATOM   1786  CD1 TRP A 321     -12.774 -26.789  26.790  1.00 61.41           C  
ANISOU 1786  CD1 TRP A 321     7249   8599   7484    667   1341  -3045       C  
ATOM   1787  CD2 TRP A 321     -14.456 -26.695  28.263  1.00 59.86           C  
ANISOU 1787  CD2 TRP A 321     7018   8258   7468    646   1166  -2930       C  
ATOM   1788  NE1 TRP A 321     -12.239 -26.477  28.016  1.00 60.42           N  
ANISOU 1788  NE1 TRP A 321     6943   8524   7487    778   1325  -2910       N  
ATOM   1789  CE2 TRP A 321     -13.251 -26.413  28.938  1.00 59.35           C  
ANISOU 1789  CE2 TRP A 321     6794   8302   7452    772   1220  -2831       C  
ATOM   1790  CE3 TRP A 321     -15.652 -26.694  28.988  1.00 59.82           C  
ANISOU 1790  CE3 TRP A 321     7025   8135   7567    599   1045  -2827       C  
ATOM   1791  CZ2 TRP A 321     -13.208 -26.133  30.301  1.00 59.24           C  
ANISOU 1791  CZ2 TRP A 321     6647   8298   7561    863   1165  -2684       C  
ATOM   1792  CZ3 TRP A 321     -15.607 -26.416  30.342  1.00 59.53           C  
ANISOU 1792  CZ3 TRP A 321     6856   8102   7660    697   1013  -2661       C  
ATOM   1793  CH2 TRP A 321     -14.393 -26.139  30.984  1.00 59.32           C  
ANISOU 1793  CH2 TRP A 321     6678   8203   7655    839   1082  -2630       C  
ATOM   1794  N   LEU A 322     -16.481 -29.817  23.782  1.00 51.26           N  
ANISOU 1794  N   LEU A 322     6780   6680   6015    278   1062  -3598       N  
ATOM   1795  CA  LEU A 322     -17.628 -30.146  22.934  1.00 52.40           C  
ANISOU 1795  CA  LEU A 322     7116   6728   6068     78    920  -3708       C  
ATOM   1796  C   LEU A 322     -18.700 -31.007  23.626  1.00 51.74           C  
ANISOU 1796  C   LEU A 322     7066   6382   6212     38    777  -3661       C  
ATOM   1797  O   LEU A 322     -19.868 -30.621  23.645  1.00 50.13           O  
ANISOU 1797  O   LEU A 322     6853   6174   6020   -138    599  -3533       O  
ATOM   1798  CB  LEU A 322     -17.191 -30.764  21.597  1.00 55.37           C  
ANISOU 1798  CB  LEU A 322     7701   7082   6255     60    977  -3859       C  
ATOM   1799  CG  LEU A 322     -18.324 -31.145  20.642  1.00 57.01           C  
ANISOU 1799  CG  LEU A 322     8119   7198   6343   -153    806  -3972       C  
ATOM   1800  CD1 LEU A 322     -19.190 -29.936  20.322  1.00 55.60           C  
ANISOU 1800  CD1 LEU A 322     7906   7205   6013   -355    657  -3874       C  
ATOM   1801  CD2 LEU A 322     -17.768 -31.761  19.368  1.00 60.15           C  
ANISOU 1801  CD2 LEU A 322     8734   7577   6543   -137    880  -4123       C  
ATOM   1802  N   PRO A 323     -18.318 -32.168  24.201  1.00 53.09           N  
ANISOU 1802  N   PRO A 323     7271   6328   6573    203    852  -3736       N  
ATOM   1803  CA  PRO A 323     -19.365 -32.982  24.833  1.00 52.55           C  
ANISOU 1803  CA  PRO A 323     7250   5996   6722    139    726  -3655       C  
ATOM   1804  C   PRO A 323     -19.942 -32.319  26.082  1.00 48.79           C  
ANISOU 1804  C   PRO A 323     6582   5558   6400    134    648  -3363       C  
ATOM   1805  O   PRO A 323     -21.053 -32.647  26.499  1.00 47.93           O  
ANISOU 1805  O   PRO A 323     6480   5299   6431     10    524  -3257       O  
ATOM   1806  CB  PRO A 323     -18.625 -34.268  25.224  1.00 55.00           C  
ANISOU 1806  CB  PRO A 323     7644   6064   7189    358    856  -3779       C  
ATOM   1807  CG  PRO A 323     -17.379 -34.272  24.402  1.00 56.96           C  
ANISOU 1807  CG  PRO A 323     7934   6449   7259    488   1007  -3913       C  
ATOM   1808  CD  PRO A 323     -17.006 -32.835  24.272  1.00 54.90           C  
ANISOU 1808  CD  PRO A 323     7507   6519   6833    445   1029  -3813       C  
ATOM   1809  N   TYR A 324     -19.183 -31.398  26.666  1.00 66.50           N  
ANISOU 1809  N   TYR A 324     8653   8001   8613    260    729  -3245       N  
ATOM   1810  CA  TYR A 324     -19.612 -30.679  27.858  1.00 65.85           C  
ANISOU 1810  CA  TYR A 324     8400   7974   8646    269    675  -2985       C  
ATOM   1811  C   TYR A 324     -20.842 -29.818  27.580  1.00 66.12           C  
ANISOU 1811  C   TYR A 324     8404   8098   8622     43    519  -2860       C  
ATOM   1812  O   TYR A 324     -21.844 -29.902  28.291  1.00 66.53           O  
ANISOU 1812  O   TYR A 324     8405   8047   8827    -26    425  -2704       O  
ATOM   1813  CB  TYR A 324     -18.466 -29.812  28.384  1.00 64.31           C  
ANISOU 1813  CB  TYR A 324     8042   7994   8399    427    788  -2924       C  
ATOM   1814  CG  TYR A 324     -18.847 -28.885  29.516  1.00 63.44           C  
ANISOU 1814  CG  TYR A 324     7771   7971   8361    426    736  -2677       C  
ATOM   1815  CD1 TYR A 324     -18.985 -29.361  30.813  1.00 64.61           C  
ANISOU 1815  CD1 TYR A 324     7868   7985   8696    548    733  -2537       C  
ATOM   1816  CD2 TYR A 324     -19.053 -27.530  29.290  1.00 62.45           C  
ANISOU 1816  CD2 TYR A 324     7567   8056   8107    310    700  -2586       C  
ATOM   1817  CE1 TYR A 324     -19.328 -28.514  31.852  1.00 64.34           C  
ANISOU 1817  CE1 TYR A 324     7705   8034   8707    550    699  -2326       C  
ATOM   1818  CE2 TYR A 324     -19.394 -26.676  30.322  1.00 62.05           C  
ANISOU 1818  CE2 TYR A 324     7387   8072   8119    317    665  -2378       C  
ATOM   1819  CZ  TYR A 324     -19.531 -27.174  31.601  1.00 62.99           C  
ANISOU 1819  CZ  TYR A 324     7454   8066   8414    435    666  -2256       C  
ATOM   1820  OH  TYR A 324     -19.872 -26.328  32.632  1.00 62.59           O  
ANISOU 1820  OH  TYR A 324     7292   8083   8408    444    642  -2063       O  
ATOM   1821  N   HIS A 325     -20.760 -28.996  26.539  1.00 50.57           N  
ANISOU 1821  N   HIS A 325     6464   6319   6431    -65    497  -2924       N  
ATOM   1822  CA  HIS A 325     -21.845 -28.081  26.197  1.00 50.57           C  
ANISOU 1822  CA  HIS A 325     6432   6426   6357   -250    342  -2798       C  
ATOM   1823  C   HIS A 325     -23.051 -28.794  25.590  1.00 52.15           C  
ANISOU 1823  C   HIS A 325     6738   6487   6591   -431    176  -2859       C  
ATOM   1824  O   HIS A 325     -24.177 -28.305  25.684  1.00 52.80           O  
ANISOU 1824  O   HIS A 325     6747   6601   6715   -561     25  -2718       O  
ATOM   1825  CB  HIS A 325     -21.349 -26.975  25.262  1.00 49.83           C  
ANISOU 1825  CB  HIS A 325     6362   6570   6001   -300    373  -2832       C  
ATOM   1826  CG  HIS A 325     -20.470 -25.968  25.935  1.00 48.17           C  
ANISOU 1826  CG  HIS A 325     6009   6519   5775   -189    494  -2719       C  
ATOM   1827  ND1 HIS A 325     -19.161 -25.751  25.562  1.00 48.10           N  
ANISOU 1827  ND1 HIS A 325     6002   6643   5632   -109    659  -2835       N  
ATOM   1828  CD2 HIS A 325     -20.710 -25.126  26.968  1.00 47.39           C  
ANISOU 1828  CD2 HIS A 325     5760   6468   5780   -154    476  -2512       C  
ATOM   1829  CE1 HIS A 325     -18.635 -24.815  26.331  1.00 46.35           C  
ANISOU 1829  CE1 HIS A 325     5630   6543   5438    -44    725  -2705       C  
ATOM   1830  NE2 HIS A 325     -19.555 -24.419  27.193  1.00 45.44           N  
ANISOU 1830  NE2 HIS A 325     5434   6373   5457    -67    614  -2512       N  
ATOM   1831  N   VAL A 326     -22.813 -29.943  24.966  1.00 49.73           N  
ANISOU 1831  N   VAL A 326     6597   6027   6271   -438    202  -3077       N  
ATOM   1832  CA  VAL A 326     -23.900 -30.744  24.412  1.00 51.76           C  
ANISOU 1832  CA  VAL A 326     6965   6129   6575   -624     43  -3166       C  
ATOM   1833  C   VAL A 326     -24.757 -31.314  25.539  1.00 51.36           C  
ANISOU 1833  C   VAL A 326     6820   5880   6817   -647     -5  -3017       C  
ATOM   1834  O   VAL A 326     -25.985 -31.353  25.443  1.00 52.58           O  
ANISOU 1834  O   VAL A 326     6936   5993   7049   -832   -170  -2958       O  
ATOM   1835  CB  VAL A 326     -23.369 -31.891  23.525  1.00 54.57           C  
ANISOU 1835  CB  VAL A 326     7546   6338   6851   -617    105  -3458       C  
ATOM   1836  CG1 VAL A 326     -24.499 -32.820  23.109  1.00 56.88           C  
ANISOU 1836  CG1 VAL A 326     7953   6435   7225   -822    -62  -3558       C  
ATOM   1837  CG2 VAL A 326     -22.665 -31.330  22.300  1.00 55.37           C  
ANISOU 1837  CG2 VAL A 326     7755   6645   6638   -623    158  -3610       C  
ATOM   1838  N   ARG A 327     -24.098 -31.737  26.613  1.00 49.83           N  
ANISOU 1838  N   ARG A 327     6581   5574   6779   -457    141  -2949       N  
ATOM   1839  CA  ARG A 327     -24.781 -32.311  27.768  1.00 49.61           C  
ANISOU 1839  CA  ARG A 327     6488   5349   7015   -457    133  -2794       C  
ATOM   1840  C   ARG A 327     -25.707 -31.310  28.455  1.00 47.65           C  
ANISOU 1840  C   ARG A 327     6042   5229   6834   -532     50  -2544       C  
ATOM   1841  O   ARG A 327     -26.836 -31.642  28.817  1.00 48.25           O  
ANISOU 1841  O   ARG A 327     6066   5191   7077   -671    -36  -2452       O  
ATOM   1842  CB  ARG A 327     -23.761 -32.842  28.776  1.00 49.19           C  
ANISOU 1842  CB  ARG A 327     6440   5180   7073   -206    303  -2758       C  
ATOM   1843  CG  ARG A 327     -24.381 -33.284  30.087  1.00 48.84           C  
ANISOU 1843  CG  ARG A 327     6335   4955   7268   -187    316  -2558       C  
ATOM   1844  CD  ARG A 327     -23.333 -33.746  31.077  1.00 48.60           C  
ANISOU 1844  CD  ARG A 327     6319   4830   7317     80    462  -2507       C  
ATOM   1845  NE  ARG A 327     -22.331 -32.719  31.346  1.00 46.60           N  
ANISOU 1845  NE  ARG A 327     5940   4834   6933    247    528  -2459       N  
ATOM   1846  CZ  ARG A 327     -22.505 -31.709  32.191  1.00 44.37           C  
ANISOU 1846  CZ  ARG A 327     5497   4713   6649    269    519  -2257       C  
ATOM   1847  NH1 ARG A 327     -23.649 -31.581  32.849  1.00 43.82           N  
ANISOU 1847  NH1 ARG A 327     5366   4586   6700    151    460  -2080       N  
ATOM   1848  NH2 ARG A 327     -21.537 -30.824  32.375  1.00 42.91           N  
ANISOU 1848  NH2 ARG A 327     5211   4747   6346    403    577  -2242       N  
ATOM   1849  N   ARG A 328     -25.219 -30.088  28.637  1.00 52.99           N  
ANISOU 1849  N   ARG A 328     6607   6137   7389   -443     87  -2442       N  
ATOM   1850  CA  ARG A 328     -25.989 -29.046  29.306  1.00 52.81           C  
ANISOU 1850  CA  ARG A 328     6409   6237   7419   -483     29  -2214       C  
ATOM   1851  C   ARG A 328     -27.208 -28.649  28.480  1.00 53.49           C  
ANISOU 1851  C   ARG A 328     6461   6395   7466   -697   -160  -2204       C  
ATOM   1852  O   ARG A 328     -28.257 -28.308  29.026  1.00 53.79           O  
ANISOU 1852  O   ARG A 328     6359   6437   7641   -772   -233  -2039       O  
ATOM   1853  CB  ARG A 328     -25.100 -27.835  29.592  1.00 50.43           C  
ANISOU 1853  CB  ARG A 328     6027   6148   6984   -346    114  -2136       C  
ATOM   1854  CG  ARG A 328     -23.868 -28.184  30.411  1.00 49.38           C  
ANISOU 1854  CG  ARG A 328     5898   5973   6888   -132    276  -2150       C  
ATOM   1855  CD  ARG A 328     -22.845 -27.062  30.426  1.00 47.18           C  
ANISOU 1855  CD  ARG A 328     5556   5916   6454    -31    356  -2140       C  
ATOM   1856  NE  ARG A 328     -23.266 -25.929  31.243  1.00 46.63           N  
ANISOU 1856  NE  ARG A 328     5350   5959   6406    -27    341  -1938       N  
ATOM   1857  CZ  ARG A 328     -23.700 -24.774  30.752  1.00 46.84           C  
ANISOU 1857  CZ  ARG A 328     5338   6138   6320   -125    275  -1875       C  
ATOM   1858  NH1 ARG A 328     -23.769 -24.592  29.440  1.00 47.33           N  
ANISOU 1858  NH1 ARG A 328     5488   6271   6222   -239    211  -1987       N  
ATOM   1859  NH2 ARG A 328     -24.061 -23.797  31.573  1.00 46.68           N  
ANISOU 1859  NH2 ARG A 328     5208   6191   6337   -102    277  -1699       N  
ATOM   1860  N   LEU A 329     -27.064 -28.701  27.160  1.00 39.00           N  
ANISOU 1860  N   LEU A 329     4752   4626   5439   -788   -239  -2382       N  
ATOM   1861  CA  LEU A 329     -28.184 -28.473  26.257  1.00 40.73           C  
ANISOU 1861  CA  LEU A 329     4961   4913   5599   -990   -449  -2399       C  
ATOM   1862  C   LEU A 329     -29.110 -29.685  26.266  1.00 43.19           C  
ANISOU 1862  C   LEU A 329     5296   5012   6102  -1147   -542  -2468       C  
ATOM   1863  O   LEU A 329     -30.327 -29.553  26.138  1.00 44.17           O  
ANISOU 1863  O   LEU A 329     5307   5162   6314  -1308   -709  -2396       O  
ATOM   1864  CB  LEU A 329     -27.683 -28.198  24.838  1.00 42.67           C  
ANISOU 1864  CB  LEU A 329     5369   5293   5550  -1037   -500  -2575       C  
ATOM   1865  CG  LEU A 329     -27.004 -26.846  24.610  1.00 40.87           C  
ANISOU 1865  CG  LEU A 329     5119   5294   5116   -945   -440  -2491       C  
ATOM   1866  CD1 LEU A 329     -26.309 -26.811  23.260  1.00 43.25           C  
ANISOU 1866  CD1 LEU A 329     5615   5693   5123   -976   -427  -2687       C  
ATOM   1867  CD2 LEU A 329     -28.020 -25.720  24.717  1.00 39.63           C  
ANISOU 1867  CD2 LEU A 329     4817   5274   4968  -1009   -590  -2284       C  
ATOM   1868  N   MET A 330     -28.519 -30.865  26.420  1.00 73.30           N  
ANISOU 1868  N   MET A 330     9251   8611   9990  -1098   -431  -2610       N  
ATOM   1869  CA  MET A 330     -29.274 -32.109  26.514  1.00 75.21           C  
ANISOU 1869  CA  MET A 330     9544   8602  10431  -1246   -485  -2682       C  
ATOM   1870  C   MET A 330     -30.102 -32.129  27.794  1.00 75.55           C  
ANISOU 1870  C   MET A 330     9402   8562  10743  -1263   -458  -2449       C  
ATOM   1871  O   MET A 330     -31.213 -32.660  27.824  1.00 76.78           O  
ANISOU 1871  O   MET A 330     9497   8609  11069  -1459   -563  -2433       O  
ATOM   1872  CB  MET A 330     -28.317 -33.304  26.490  1.00 76.33           C  
ANISOU 1872  CB  MET A 330     9896   8512  10594  -1142   -340  -2868       C  
ATOM   1873  CG  MET A 330     -28.975 -34.654  26.715  1.00 78.16           C  
ANISOU 1873  CG  MET A 330    10213   8432  11054  -1278   -358  -2933       C  
ATOM   1874  SD  MET A 330     -27.767 -35.986  26.857  1.00 79.27           S  
ANISOU 1874  SD  MET A 330    10607   8276  11237  -1091   -162  -3116       S  
ATOM   1875  CE  MET A 330     -28.842 -37.402  27.062  1.00 82.08           C  
ANISOU 1875  CE  MET A 330    11061   8260  11868  -1324   -218  -3167       C  
ATOM   1876  N   PHE A 331     -29.550 -31.536  28.847  1.00 75.76           N  
ANISOU 1876  N   PHE A 331     9337   8647  10800  -1066   -312  -2274       N  
ATOM   1877  CA  PHE A 331     -30.194 -31.501  30.155  1.00 75.95           C  
ANISOU 1877  CA  PHE A 331     9207   8604  11046  -1049   -249  -2046       C  
ATOM   1878  C   PHE A 331     -31.494 -30.703  30.143  1.00 75.86           C  
ANISOU 1878  C   PHE A 331     8984   8739  11100  -1200   -390  -1905       C  
ATOM   1879  O   PHE A 331     -32.445 -31.041  30.849  1.00 75.91           O  
ANISOU 1879  O   PHE A 331     8872   8644  11326  -1301   -387  -1785       O  
ATOM   1880  CB  PHE A 331     -29.232 -30.915  31.194  1.00 74.91           C  
ANISOU 1880  CB  PHE A 331     9038   8543  10880   -799    -82  -1910       C  
ATOM   1881  CG  PHE A 331     -29.867 -30.644  32.530  1.00 75.22           C  
ANISOU 1881  CG  PHE A 331     8925   8562  11093   -767    -12  -1667       C  
ATOM   1882  CD1 PHE A 331     -30.045 -31.666  33.447  1.00 76.63           C  
ANISOU 1882  CD1 PHE A 331     9153   8503  11462   -753     92  -1597       C  
ATOM   1883  CD2 PHE A 331     -30.273 -29.364  32.875  1.00 74.21           C  
ANISOU 1883  CD2 PHE A 331     8624   8643  10929   -746    -36  -1508       C  
ATOM   1884  CE1 PHE A 331     -30.624 -31.420  34.677  1.00 77.10           C  
ANISOU 1884  CE1 PHE A 331     9087   8550  11658   -726    175  -1372       C  
ATOM   1885  CE2 PHE A 331     -30.854 -29.113  34.104  1.00 74.66           C  
ANISOU 1885  CE2 PHE A 331     8552   8683  11132   -710     47  -1298       C  
ATOM   1886  CZ  PHE A 331     -31.028 -30.142  35.006  1.00 76.00           C  
ANISOU 1886  CZ  PHE A 331     8769   8633  11476   -703    156  -1230       C  
ATOM   1887  N   VAL A 332     -31.534 -29.647  29.336  1.00 49.76           N  
ANISOU 1887  N   VAL A 332     5630   5669   7607  -1209   -505  -1915       N  
ATOM   1888  CA  VAL A 332     -32.649 -28.707  29.374  1.00 49.60           C  
ANISOU 1888  CA  VAL A 332     5397   5812   7636  -1291   -631  -1758       C  
ATOM   1889  C   VAL A 332     -33.631 -28.853  28.205  1.00 51.60           C  
ANISOU 1889  C   VAL A 332     5622   6123   7863  -1515   -875  -1863       C  
ATOM   1890  O   VAL A 332     -34.846 -28.779  28.396  1.00 52.67           O  
ANISOU 1890  O   VAL A 332     5561   6284   8167  -1643   -983  -1761       O  
ATOM   1891  CB  VAL A 332     -32.144 -27.244  29.480  1.00 47.06           C  
ANISOU 1891  CB  VAL A 332     5020   5714   7147  -1131   -597  -1642       C  
ATOM   1892  CG1 VAL A 332     -31.175 -26.918  28.350  1.00 46.66           C  
ANISOU 1892  CG1 VAL A 332     5145   5770   6816  -1093   -625  -1802       C  
ATOM   1893  CG2 VAL A 332     -33.309 -26.269  29.503  1.00 46.95           C  
ANISOU 1893  CG2 VAL A 332     4797   5854   7190  -1190   -729  -1482       C  
ATOM   1894  N   TYR A 333     -33.109 -29.080  27.003  1.00 62.55           N  
ANISOU 1894  N   TYR A 333     7196   7536   9033  -1562   -962  -2070       N  
ATOM   1895  CA  TYR A 333     -33.940 -29.079  25.800  1.00 63.46           C  
ANISOU 1895  CA  TYR A 333     7308   7748   9056  -1758  -1218  -2176       C  
ATOM   1896  C   TYR A 333     -34.854 -30.294  25.654  1.00 64.94           C  
ANISOU 1896  C   TYR A 333     7477   7758   9439  -1993  -1330  -2286       C  
ATOM   1897  O   TYR A 333     -35.874 -30.225  24.969  1.00 65.54           O  
ANISOU 1897  O   TYR A 333     7451   7928   9522  -2176  -1566  -2316       O  
ATOM   1898  CB  TYR A 333     -33.082 -28.900  24.545  1.00 62.53           C  
ANISOU 1898  CB  TYR A 333     7421   7728   8610  -1735  -1264  -2364       C  
ATOM   1899  CG  TYR A 333     -32.914 -27.455  24.137  1.00 61.47           C  
ANISOU 1899  CG  TYR A 333     7247   7847   8260  -1639  -1318  -2246       C  
ATOM   1900  CD1 TYR A 333     -33.838 -26.840  23.303  1.00 62.66           C  
ANISOU 1900  CD1 TYR A 333     7328   8169   8312  -1753  -1571  -2211       C  
ATOM   1901  CD2 TYR A 333     -31.839 -26.703  24.592  1.00 60.28           C  
ANISOU 1901  CD2 TYR A 333     7132   7762   8009  -1438  -1124  -2165       C  
ATOM   1902  CE1 TYR A 333     -33.695 -25.519  22.928  1.00 62.15           C  
ANISOU 1902  CE1 TYR A 333     7253   8311   8051  -1657  -1618  -2088       C  
ATOM   1903  CE2 TYR A 333     -31.687 -25.379  24.222  1.00 59.52           C  
ANISOU 1903  CE2 TYR A 333     7020   7871   7724  -1367  -1162  -2054       C  
ATOM   1904  CZ  TYR A 333     -32.619 -24.793  23.390  1.00 60.60           C  
ANISOU 1904  CZ  TYR A 333     7110   8152   7762  -1471  -1404  -2010       C  
ATOM   1905  OH  TYR A 333     -32.475 -23.477  23.017  1.00 60.89           O  
ANISOU 1905  OH  TYR A 333     7156   8369   7612  -1391  -1439  -1884       O  
ATOM   1906  N   ILE A 334     -34.493 -31.402  26.291  1.00 58.25           N  
ANISOU 1906  N   ILE A 334     6729   6651   8752  -1991  -1169  -2345       N  
ATOM   1907  CA  ILE A 334     -35.325 -32.601  26.236  1.00 60.46           C  
ANISOU 1907  CA  ILE A 334     7009   6721   9242  -2228  -1246  -2446       C  
ATOM   1908  C   ILE A 334     -36.551 -32.446  27.132  1.00 60.73           C  
ANISOU 1908  C   ILE A 334     6748   6762   9563  -2330  -1263  -2232       C  
ATOM   1909  O   ILE A 334     -36.430 -32.127  28.315  1.00 59.41           O  
ANISOU 1909  O   ILE A 334     6478   6574   9522  -2183  -1077  -2030       O  
ATOM   1910  CB  ILE A 334     -34.539 -33.863  26.642  1.00 61.07           C  
ANISOU 1910  CB  ILE A 334     7313   6484   9405  -2183  -1055  -2567       C  
ATOM   1911  CG1 ILE A 334     -33.333 -34.057  25.722  1.00 61.06           C  
ANISOU 1911  CG1 ILE A 334     7587   6480   9131  -2071  -1019  -2794       C  
ATOM   1912  CG2 ILE A 334     -35.440 -35.089  26.601  1.00 64.28           C  
ANISOU 1912  CG2 ILE A 334     7736   6646  10040  -2452  -1128  -2669       C  
ATOM   1913  CD1 ILE A 334     -32.541 -35.312  26.011  1.00 62.11           C  
ANISOU 1913  CD1 ILE A 334     7953   6301   9346  -2004   -844  -2933       C  
ATOM   1914  N   SER A 335     -37.730 -32.667  26.557  1.00142.30           N  
ANISOU 1914  N   SER A 335    16939  17135  19991  -2583  -1487  -2285       N  
ATOM   1915  CA  SER A 335     -38.985 -32.527  27.289  1.00143.21           C  
ANISOU 1915  CA  SER A 335    16738  17285  20389  -2703  -1515  -2098       C  
ATOM   1916  C   SER A 335     -39.080 -33.530  28.434  1.00144.25           C  
ANISOU 1916  C   SER A 335    16876  17131  20800  -2752  -1292  -2027       C  
ATOM   1917  O   SER A 335     -38.431 -34.576  28.410  1.00145.92           O  
ANISOU 1917  O   SER A 335    17340  17084  21018  -2774  -1193  -2171       O  
ATOM   1918  CB  SER A 335     -40.179 -32.690  26.346  1.00142.56           C  
ANISOU 1918  CB  SER A 335    16502  17305  20357  -2984  -1821  -2203       C  
ATOM   1919  OG  SER A 335     -41.403 -32.536  27.043  1.00143.61           O  
ANISOU 1919  OG  SER A 335    16291  17493  20779  -3097  -1842  -2024       O  
ATOM   1920  N   ASP A 336     -39.895 -33.205  29.432  1.00138.91           N  
ANISOU 1920  N   ASP A 336    15933  16497  20352  -2759  -1204  -1800       N  
ATOM   1921  CA  ASP A 336     -40.039 -34.047  30.615  1.00139.11           C  
ANISOU 1921  CA  ASP A 336    15959  16266  20630  -2799   -971  -1689       C  
ATOM   1922  C   ASP A 336     -40.683 -35.393  30.292  1.00140.70           C  
ANISOU 1922  C   ASP A 336    16211  16219  21030  -3117  -1036  -1842       C  
ATOM   1923  O   ASP A 336     -40.470 -36.377  31.001  1.00141.18           O  
ANISOU 1923  O   ASP A 336    16425  15984  21234  -3148   -845  -1829       O  
ATOM   1924  CB  ASP A 336     -40.848 -33.323  31.694  1.00138.66           C  
ANISOU 1924  CB  ASP A 336    15591  16336  20757  -2752   -861  -1419       C  
ATOM   1925  CG  ASP A 336     -40.220 -32.007  32.108  1.00137.28           C  
ANISOU 1925  CG  ASP A 336    15385  16376  20401  -2445   -781  -1271       C  
ATOM   1926  OD1 ASP A 336     -39.039 -31.779  31.772  1.00136.09           O  
ANISOU 1926  OD1 ASP A 336    15463  16240  20007  -2263   -763  -1358       O  
ATOM   1927  OD2 ASP A 336     -40.904 -31.202  32.773  1.00137.13           O  
ANISOU 1927  OD2 ASP A 336    15110  16504  20488  -2388   -727  -1076       O  
ATOM   1928  N   GLU A 337     -41.469 -35.432  29.222  1.00143.15           N  
ANISOU 1928  N   GLU A 337    16402  16645  21345  -3356  -1312  -1986       N  
ATOM   1929  CA  GLU A 337     -42.136 -36.663  28.814  1.00146.48           C  
ANISOU 1929  CA  GLU A 337    16877  16859  21920  -3679  -1401  -2141       C  
ATOM   1930  C   GLU A 337     -41.205 -37.567  28.011  1.00146.74           C  
ANISOU 1930  C   GLU A 337    17303  16666  21785  -3696  -1424  -2417       C  
ATOM   1931  O   GLU A 337     -41.371 -38.787  27.997  1.00148.85           O  
ANISOU 1931  O   GLU A 337    17751  16658  22150  -3862  -1369  -2498       O  
ATOM   1932  CB  GLU A 337     -43.400 -36.354  28.007  1.00153.06           C  
ANISOU 1932  CB  GLU A 337    17482  17967  22707  -3875  -1678  -2133       C  
ATOM   1933  CG  GLU A 337     -43.156 -35.534  26.751  1.00152.77           C  
ANISOU 1933  CG  GLU A 337    17482  18199  22365  -3803  -1943  -2260       C  
ATOM   1934  CD  GLU A 337     -44.401 -35.399  25.896  1.00155.94           C  
ANISOU 1934  CD  GLU A 337    17713  18832  22705  -4022  -2228  -2281       C  
ATOM   1935  OE1 GLU A 337     -45.425 -36.032  26.232  1.00157.82           O  
ANISOU 1935  OE1 GLU A 337    17806  19018  23142  -4249  -2220  -2228       O  
ATOM   1936  OE2 GLU A 337     -44.357 -34.662  24.889  1.00156.61           O  
ANISOU 1936  OE2 GLU A 337    17811  19159  22535  -3971  -2456  -2350       O  
ATOM   1937  N   GLN A 338     -40.223 -36.966  27.346  1.00118.04           N  
ANISOU 1937  N   GLN A 338    13828  13166  17855  -3495  -1483  -2529       N  
ATOM   1938  CA  GLN A 338     -39.276 -37.721  26.533  1.00118.92           C  
ANISOU 1938  CA  GLN A 338    14309  13101  17775  -3477  -1490  -2801       C  
ATOM   1939  C   GLN A 338     -38.217 -38.418  27.381  1.00117.74           C  
ANISOU 1939  C   GLN A 338    14410  12653  17672  -3277  -1192  -2772       C  
ATOM   1940  O   GLN A 338     -37.610 -39.397  26.948  1.00119.47           O  
ANISOU 1940  O   GLN A 338    14929  12620  17846  -3303  -1154  -2990       O  
ATOM   1941  CB  GLN A 338     -38.601 -36.813  25.502  1.00118.49           C  
ANISOU 1941  CB  GLN A 338    14347  13319  17355  -3315  -1625  -2902       C  
ATOM   1942  CG  GLN A 338     -39.504 -36.384  24.360  1.00121.00           C  
ANISOU 1942  CG  GLN A 338    14556  13880  17538  -3516  -1958  -3002       C  
ATOM   1943  CD  GLN A 338     -38.756 -35.608  23.293  1.00120.44           C  
ANISOU 1943  CD  GLN A 338    14634  14032  17097  -3373  -2072  -3130       C  
ATOM   1944  OE1 GLN A 338     -38.411 -34.442  23.483  1.00118.35           O  
ANISOU 1944  OE1 GLN A 338    14265  14003  16702  -3156  -2038  -2953       O  
ATOM   1945  NE2 GLN A 338     -38.496 -36.257  22.163  1.00122.24           N  
ANISOU 1945  NE2 GLN A 338    15159  14196  17090  -3452  -2170  -3356       N  
ATOM   1946  N   TRP A 339     -37.996 -37.908  28.588  1.00 73.18           N  
ANISOU 1946  N   TRP A 339     8652   7041  12112  -3067   -986  -2506       N  
ATOM   1947  CA  TRP A 339     -36.986 -38.467  29.481  1.00 72.58           C  
ANISOU 1947  CA  TRP A 339     8793   6719  12065  -2843   -720  -2444       C  
ATOM   1948  C   TRP A 339     -37.341 -39.870  29.965  1.00 74.98           C  
ANISOU 1948  C   TRP A 339     9231   6625  12633  -3025   -610  -2472       C  
ATOM   1949  O   TRP A 339     -38.359 -40.071  30.628  1.00 76.33           O  
ANISOU 1949  O   TRP A 339     9213   6733  13055  -3218   -578  -2324       O  
ATOM   1950  CB  TRP A 339     -36.751 -37.545  30.680  1.00 70.88           C  
ANISOU 1950  CB  TRP A 339     8416   6652  11862  -2593   -548  -2151       C  
ATOM   1951  CG  TRP A 339     -35.752 -36.459  30.421  1.00 69.01           C  
ANISOU 1951  CG  TRP A 339     8202   6674  11345  -2316   -549  -2145       C  
ATOM   1952  CD1 TRP A 339     -36.015 -35.143  30.180  1.00 67.68           C  
ANISOU 1952  CD1 TRP A 339     7826   6839  11050  -2263   -659  -2055       C  
ATOM   1953  CD2 TRP A 339     -34.327 -36.598  30.378  1.00 68.36           C  
ANISOU 1953  CD2 TRP A 339     8356   6532  11084  -2057   -427  -2231       C  
ATOM   1954  NE1 TRP A 339     -34.842 -34.453  29.990  1.00 66.43           N  
ANISOU 1954  NE1 TRP A 339     7774   6822  10645  -2009   -606  -2079       N  
ATOM   1955  CE2 TRP A 339     -33.791 -35.324  30.106  1.00 66.82           C  
ANISOU 1955  CE2 TRP A 339     8078   6648  10661  -1881   -465  -2191       C  
ATOM   1956  CE3 TRP A 339     -33.453 -37.677  30.542  1.00 69.05           C  
ANISOU 1956  CE3 TRP A 339     8712   6329  11193  -1950   -287  -2337       C  
ATOM   1957  CZ2 TRP A 339     -32.420 -35.099  29.995  1.00 65.94           C  
ANISOU 1957  CZ2 TRP A 339     8121   6583  10349  -1628   -364  -2258       C  
ATOM   1958  CZ3 TRP A 339     -32.093 -37.451  30.432  1.00 68.12           C  
ANISOU 1958  CZ3 TRP A 339     8736   6267  10878  -1670   -195  -2403       C  
ATOM   1959  CH2 TRP A 339     -31.590 -36.173  30.161  1.00 66.55           C  
ANISOU 1959  CH2 TRP A 339     8429   6398  10460  -1523   -232  -2366       C  
ATOM   1960  N   THR A 340     -36.493 -40.835  29.625  1.00 95.05           N  
ANISOU 1960  N   THR A 340    12102   8892  15121  -2960   -539  -2663       N  
ATOM   1961  CA  THR A 340     -36.655 -42.204  30.098  1.00 97.56           C  
ANISOU 1961  CA  THR A 340    12611   8783  15675  -3095   -411  -2691       C  
ATOM   1962  C   THR A 340     -35.497 -42.573  31.018  1.00 97.13           C  
ANISOU 1962  C   THR A 340    12773   8525  15606  -2763   -160  -2583       C  
ATOM   1963  O   THR A 340     -34.564 -41.789  31.195  1.00 96.83           O  
ANISOU 1963  O   THR A 340    12734   8690  15369  -2453   -107  -2528       O  
ATOM   1964  CB  THR A 340     -36.716 -43.207  28.930  1.00100.78           C  
ANISOU 1964  CB  THR A 340    13258   8989  16044  -3312   -551  -3016       C  
ATOM   1965  OG1 THR A 340     -35.488 -43.164  28.193  1.00 99.80           O  
ANISOU 1965  OG1 THR A 340    13373   8880  15668  -3085   -545  -3234       O  
ATOM   1966  CG2 THR A 340     -37.873 -42.875  28.001  1.00102.16           C  
ANISOU 1966  CG2 THR A 340    13233   9432  16152  -3598   -834  -3068       C  
ATOM   1967  N   THR A 341     -35.562 -43.764  31.604  1.00 86.78           N  
ANISOU 1967  N   THR A 341    11648   6814  14510  -2832    -12  -2547       N  
ATOM   1968  CA  THR A 341     -34.511 -44.235  32.501  1.00 86.03           C  
ANISOU 1968  CA  THR A 341    11773   6495  14420  -2516    213  -2430       C  
ATOM   1969  C   THR A 341     -33.197 -44.431  31.751  1.00 85.66           C  
ANISOU 1969  C   THR A 341    11975   6414  14158  -2259    213  -2663       C  
ATOM   1970  O   THR A 341     -32.116 -44.150  32.279  1.00 84.17           O  
ANISOU 1970  O   THR A 341    11846   6276  13859  -1908    337  -2569       O  
ATOM   1971  CB  THR A 341     -34.908 -45.553  33.190  1.00 91.60           C  
ANISOU 1971  CB  THR A 341    12668   6736  15399  -2665    360  -2359       C  
ATOM   1972  OG1 THR A 341     -35.233 -46.535  32.198  1.00 95.75           O  
ANISOU 1972  OG1 THR A 341    13385   7055  15942  -2905    241  -2614       O  
ATOM   1973  CG2 THR A 341     -36.113 -45.338  34.093  1.00 92.20           C  
ANISOU 1973  CG2 THR A 341    12489   6856  15689  -2887    415  -2095       C  
ATOM   1974  N   ALA A 342     -33.302 -44.911  30.515  1.00 77.92           N  
ANISOU 1974  N   ALA A 342    11131   5358  13116  -2439     74  -2973       N  
ATOM   1975  CA  ALA A 342     -32.139 -45.099  29.658  1.00 78.22           C  
ANISOU 1975  CA  ALA A 342    11402   5375  12941  -2224     79  -3228       C  
ATOM   1976  C   ALA A 342     -31.429 -43.771  29.420  1.00 73.53           C  
ANISOU 1976  C   ALA A 342    10640   5219  12078  -1984     41  -3192       C  
ATOM   1977  O   ALA A 342     -30.214 -43.671  29.584  1.00 71.82           O  
ANISOU 1977  O   ALA A 342    10521   5028  11739  -1654    162  -3201       O  
ATOM   1978  CB  ALA A 342     -32.549 -45.728  28.336  1.00 82.02           C  
ANISOU 1978  CB  ALA A 342    12044   5790  13328  -2469    -95  -3513       C  
ATOM   1979  N   LEU A 343     -32.199 -42.753  29.046  1.00 71.82           N  
ANISOU 1979  N   LEU A 343    10163   5342  11781  -2153   -127  -3147       N  
ATOM   1980  CA  LEU A 343     -31.658 -41.416  28.822  1.00 67.58           C  
ANISOU 1980  CA  LEU A 343     9460   5215  11001  -1962   -167  -3089       C  
ATOM   1981  C   LEU A 343     -31.093 -40.813  30.105  1.00 63.47           C  
ANISOU 1981  C   LEU A 343     8819   4789  10507  -1678     -2  -2803       C  
ATOM   1982  O   LEU A 343     -30.192 -39.982  30.061  1.00 60.39           O  
ANISOU 1982  O   LEU A 343     8387   4636   9925  -1436     36  -2784       O  
ATOM   1983  CB  LEU A 343     -32.731 -40.492  28.241  1.00 67.11           C  
ANISOU 1983  CB  LEU A 343     9150   5463  10885  -2203   -385  -3065       C  
ATOM   1984  CG  LEU A 343     -33.080 -40.675  26.763  1.00 70.40           C  
ANISOU 1984  CG  LEU A 343     9664   5934  11150  -2425   -595  -3361       C  
ATOM   1985  CD1 LEU A 343     -34.235 -39.768  26.370  1.00 70.23           C  
ANISOU 1985  CD1 LEU A 343     9366   6212  11106  -2647   -823  -3288       C  
ATOM   1986  CD2 LEU A 343     -31.863 -40.403  25.893  1.00 69.54           C  
ANISOU 1986  CD2 LEU A 343     9729   5952  10739  -2206   -564  -3549       C  
ATOM   1987  N   PHE A 344     -31.634 -41.241  31.241  1.00 69.18           N  
ANISOU 1987  N   PHE A 344     9496   5329  11463  -1723     98  -2585       N  
ATOM   1988  CA  PHE A 344     -31.202 -40.762  32.550  1.00 66.72           C  
ANISOU 1988  CA  PHE A 344     9091   5084  11176  -1473    252  -2308       C  
ATOM   1989  C   PHE A 344     -29.807 -41.292  32.876  1.00 66.62           C  
ANISOU 1989  C   PHE A 344     9298   4915  11102  -1141    400  -2346       C  
ATOM   1990  O   PHE A 344     -28.847 -40.521  33.055  1.00 64.11           O  
ANISOU 1990  O   PHE A 344     8919   4825  10615   -874    440  -2306       O  
ATOM   1991  CB  PHE A 344     -32.206 -41.230  33.607  1.00 67.93           C  
ANISOU 1991  CB  PHE A 344     9174   5049  11587  -1633    333  -2080       C  
ATOM   1992  CG  PHE A 344     -32.036 -40.580  34.948  1.00 66.49           C  
ANISOU 1992  CG  PHE A 344     8863   4988  11412  -1428    467  -1780       C  
ATOM   1993  CD1 PHE A 344     -32.590 -39.338  35.204  1.00 65.50           C  
ANISOU 1993  CD1 PHE A 344     8457   5197  11235  -1456    417  -1633       C  
ATOM   1994  CD2 PHE A 344     -31.346 -41.223  35.963  1.00 67.07           C  
ANISOU 1994  CD2 PHE A 344     9110   4835  11541  -1205    641  -1646       C  
ATOM   1995  CE1 PHE A 344     -32.446 -38.741  36.441  1.00 65.10           C  
ANISOU 1995  CE1 PHE A 344     8308   5252  11178  -1274    545  -1375       C  
ATOM   1996  CE2 PHE A 344     -31.200 -40.631  37.203  1.00 66.43           C  
ANISOU 1996  CE2 PHE A 344     8928   4873  11441  -1023    753  -1378       C  
ATOM   1997  CZ  PHE A 344     -31.749 -39.387  37.441  1.00 65.54           C  
ANISOU 1997  CZ  PHE A 344     8542   5093  11268  -1064    710  -1251       C  
ATOM   1998  N   ASP A 345     -29.705 -42.617  32.949  1.00 84.00           N  
ANISOU 1998  N   ASP A 345    11749   6719  13447  -1159    477  -2428       N  
ATOM   1999  CA  ASP A 345     -28.433 -43.278  33.211  1.00 84.22           C  
ANISOU 1999  CA  ASP A 345    11997   6556  13446   -834    611  -2471       C  
ATOM   2000  C   ASP A 345     -27.382 -42.843  32.193  1.00 82.75           C  
ANISOU 2000  C   ASP A 345    11842   6574  13025   -661    574  -2710       C  
ATOM   2001  O   ASP A 345     -26.253 -42.500  32.558  1.00 81.88           O  
ANISOU 2001  O   ASP A 345    11719   6582  12811   -340    658  -2669       O  
ATOM   2002  CB  ASP A 345     -28.607 -44.798  33.186  1.00 87.82           C  
ANISOU 2002  CB  ASP A 345    12745   6526  14098   -919    681  -2563       C  
ATOM   2003  CG  ASP A 345     -29.625 -45.284  34.201  1.00 89.46           C  
ANISOU 2003  CG  ASP A 345    12939   6509  14544  -1108    746  -2321       C  
ATOM   2004  OD1 ASP A 345     -30.503 -44.487  34.596  1.00 88.79           O  
ANISOU 2004  OD1 ASP A 345    12598   6654  14485  -1276    698  -2152       O  
ATOM   2005  OD2 ASP A 345     -29.547 -46.463  34.607  1.00 91.66           O  
ANISOU 2005  OD2 ASP A 345    13467   6373  14986  -1084    858  -2297       O  
ATOM   2006  N   PHE A 346     -27.768 -42.839  30.919  1.00 77.10           N  
ANISOU 2006  N   PHE A 346    11159   5914  12220   -882    445  -2958       N  
ATOM   2007  CA  PHE A 346     -26.879 -42.387  29.853  1.00 76.07           C  
ANISOU 2007  CA  PHE A 346    11061   5997  11844   -760    416  -3189       C  
ATOM   2008  C   PHE A 346     -26.451 -40.938  30.050  1.00 74.31           C  
ANISOU 2008  C   PHE A 346    10590   6202  11443   -620    400  -3052       C  
ATOM   2009  O   PHE A 346     -25.329 -40.572  29.713  1.00 73.68           O  
ANISOU 2009  O   PHE A 346    10521   6280  11195   -392    461  -3148       O  
ATOM   2010  CB  PHE A 346     -27.530 -42.554  28.478  1.00 76.75           C  
ANISOU 2010  CB  PHE A 346    11225   6094  11841  -1056    260  -3457       C  
ATOM   2011  CG  PHE A 346     -26.799 -41.844  27.373  1.00 75.62           C  
ANISOU 2011  CG  PHE A 346    11081   6242  11408   -973    219  -3653       C  
ATOM   2012  CD1 PHE A 346     -25.621 -42.361  26.860  1.00 76.03           C  
ANISOU 2012  CD1 PHE A 346    11330   6204  11354   -747    340  -3868       C  
ATOM   2013  CD2 PHE A 346     -27.288 -40.658  26.850  1.00 74.66           C  
ANISOU 2013  CD2 PHE A 346    10764   6483  11120  -1112     73  -3614       C  
ATOM   2014  CE1 PHE A 346     -24.944 -41.709  25.846  1.00 75.32           C  
ANISOU 2014  CE1 PHE A 346    11240   6388  10991   -680    330  -4043       C  
ATOM   2015  CE2 PHE A 346     -26.616 -40.001  25.837  1.00 73.64           C  
ANISOU 2015  CE2 PHE A 346    10656   6613  10712  -1044     51  -3777       C  
ATOM   2016  CZ  PHE A 346     -25.443 -40.528  25.334  1.00 73.73           C  
ANISOU 2016  CZ  PHE A 346    10862   6540  10614   -837    187  -3993       C  
ATOM   2017  N   TYR A 347     -27.348 -40.116  30.586  1.00 58.26           N  
ANISOU 2017  N   TYR A 347     8332   4350   9454   -759    327  -2835       N  
ATOM   2018  CA  TYR A 347     -27.015 -38.727  30.875  1.00 54.07           C  
ANISOU 2018  CA  TYR A 347     7579   4192   8773   -637    317  -2691       C  
ATOM   2019  C   TYR A 347     -25.943 -38.659  31.951  1.00 52.38           C  
ANISOU 2019  C   TYR A 347     7354   3982   8566   -307    469  -2547       C  
ATOM   2020  O   TYR A 347     -25.056 -37.806  31.902  1.00 50.29           O  
ANISOU 2020  O   TYR A 347     6996   3974   8135   -127    497  -2551       O  
ATOM   2021  CB  TYR A 347     -28.249 -37.939  31.317  1.00 51.99           C  
ANISOU 2021  CB  TYR A 347     7087   4084   8583   -835    224  -2483       C  
ATOM   2022  CG  TYR A 347     -27.938 -36.542  31.804  1.00 47.80           C  
ANISOU 2022  CG  TYR A 347     6349   3887   7927   -693    236  -2311       C  
ATOM   2023  CD1 TYR A 347     -27.741 -35.501  30.907  1.00 46.43           C  
ANISOU 2023  CD1 TYR A 347     6095   4008   7540   -713    144  -2398       C  
ATOM   2024  CD2 TYR A 347     -27.834 -36.264  33.162  1.00 45.56           C  
ANISOU 2024  CD2 TYR A 347     5971   3612   7728   -543    342  -2065       C  
ATOM   2025  CE1 TYR A 347     -27.455 -34.224  31.347  1.00 42.92           C  
ANISOU 2025  CE1 TYR A 347     5480   3840   6988   -595    162  -2246       C  
ATOM   2026  CE2 TYR A 347     -27.546 -34.990  33.611  1.00 42.04           C  
ANISOU 2026  CE2 TYR A 347     5353   3455   7166   -423    352  -1928       C  
ATOM   2027  CZ  TYR A 347     -27.357 -33.973  32.700  1.00 40.73           C  
ANISOU 2027  CZ  TYR A 347     5108   3559   6806   -454    264  -2021       C  
ATOM   2028  OH  TYR A 347     -27.070 -32.702  33.141  1.00 37.54           O  
ANISOU 2028  OH  TYR A 347     4552   3417   6296   -348    280  -1890       O  
ATOM   2029  N   HIS A 348     -26.024 -39.559  32.925  1.00 58.44           N  
ANISOU 2029  N   HIS A 348     8219   4464   9523   -234    563  -2418       N  
ATOM   2030  CA  HIS A 348     -25.024 -39.577  33.992  1.00 57.49           C  
ANISOU 2030  CA  HIS A 348     8101   4337   9406     89    685  -2270       C  
ATOM   2031  C   HIS A 348     -23.657 -40.097  33.525  1.00 58.62           C  
ANISOU 2031  C   HIS A 348     8386   4418   9471    354    759  -2465       C  
ATOM   2032  O   HIS A 348     -22.612 -39.549  33.899  1.00 57.13           O  
ANISOU 2032  O   HIS A 348     8105   4420   9183    614    811  -2421       O  
ATOM   2033  CB  HIS A 348     -25.543 -40.344  35.210  1.00 58.68           C  
ANISOU 2033  CB  HIS A 348     8328   4206   9762     94    764  -2047       C  
ATOM   2034  CG  HIS A 348     -26.695 -39.672  35.891  1.00 57.31           C  
ANISOU 2034  CG  HIS A 348     7972   4149   9654    -98    734  -1822       C  
ATOM   2035  ND1 HIS A 348     -27.881 -39.395  35.246  1.00 57.60           N  
ANISOU 2035  ND1 HIS A 348     7908   4242   9734   -420    627  -1868       N  
ATOM   2036  CD2 HIS A 348     -26.837 -39.205  37.154  1.00 55.83           C  
ANISOU 2036  CD2 HIS A 348     7679   4044   9490     -4    798  -1555       C  
ATOM   2037  CE1 HIS A 348     -28.706 -38.793  36.083  1.00 56.37           C  
ANISOU 2037  CE1 HIS A 348     7579   4196   9645   -507    639  -1638       C  
ATOM   2038  NE2 HIS A 348     -28.098 -38.667  37.248  1.00 55.27           N  
ANISOU 2038  NE2 HIS A 348     7444   4069   9486   -262    750  -1448       N  
ATOM   2039  N   TYR A 349     -23.660 -41.139  32.697  1.00 58.40           N  
ANISOU 2039  N   TYR A 349     8571   4126   9491    287    766  -2689       N  
ATOM   2040  CA  TYR A 349     -22.412 -41.635  32.118  1.00 60.75           C  
ANISOU 2040  CA  TYR A 349     9001   4367   9713    533    847  -2905       C  
ATOM   2041  C   TYR A 349     -21.778 -40.577  31.212  1.00 59.07           C  
ANISOU 2041  C   TYR A 349     8651   4533   9262    561    820  -3053       C  
ATOM   2042  O   TYR A 349     -20.558 -40.376  31.223  1.00 59.20           O  
ANISOU 2042  O   TYR A 349     8620   4683   9190    832    904  -3109       O  
ATOM   2043  CB  TYR A 349     -22.642 -42.936  31.343  1.00 65.24           C  
ANISOU 2043  CB  TYR A 349     9849   4566  10374    429    862  -3138       C  
ATOM   2044  CG  TYR A 349     -23.009 -44.117  32.215  1.00 67.83           C  
ANISOU 2044  CG  TYR A 349    10362   4469  10943    451    926  -3011       C  
ATOM   2045  CD1 TYR A 349     -22.111 -44.621  33.148  1.00 68.82           C  
ANISOU 2045  CD1 TYR A 349    10558   4445  11146    795   1040  -2885       C  
ATOM   2046  CD2 TYR A 349     -24.246 -44.737  32.096  1.00 69.74           C  
ANISOU 2046  CD2 TYR A 349    10709   4454  11333    124    871  -3014       C  
ATOM   2047  CE1 TYR A 349     -22.440 -45.702  33.945  1.00 71.55           C  
ANISOU 2047  CE1 TYR A 349    11102   4385  11700    820   1106  -2750       C  
ATOM   2048  CE2 TYR A 349     -24.584 -45.818  32.888  1.00 72.50           C  
ANISOU 2048  CE2 TYR A 349    11245   4397  11906    123    948  -2889       C  
ATOM   2049  CZ  TYR A 349     -23.677 -46.297  33.810  1.00 73.38           C  
ANISOU 2049  CZ  TYR A 349    11452   4352  12078    476   1070  -2751       C  
ATOM   2050  OH  TYR A 349     -24.010 -47.374  34.600  1.00 76.48           O  
ANISOU 2050  OH  TYR A 349    12056   4322  12681    480   1152  -2608       O  
ATOM   2051  N   PHE A 350     -22.620 -39.901  30.437  1.00 71.39           N  
ANISOU 2051  N   PHE A 350    10139   6266  10721    278    700  -3108       N  
ATOM   2052  CA  PHE A 350     -22.187 -38.814  29.569  1.00 69.94           C  
ANISOU 2052  CA  PHE A 350     9840   6434  10298    261    667  -3216       C  
ATOM   2053  C   PHE A 350     -21.620 -37.677  30.409  1.00 68.12           C  
ANISOU 2053  C   PHE A 350     9379   6497  10007    428    702  -3012       C  
ATOM   2054  O   PHE A 350     -20.696 -36.980  29.989  1.00 66.31           O  
ANISOU 2054  O   PHE A 350     9068   6514   9611    549    750  -3093       O  
ATOM   2055  CB  PHE A 350     -23.364 -38.305  28.734  1.00 69.47           C  
ANISOU 2055  CB  PHE A 350     9748   6487  10159    -75    506  -3259       C  
ATOM   2056  CG  PHE A 350     -22.976 -37.322  27.666  1.00 68.16           C  
ANISOU 2056  CG  PHE A 350     9526   6643   9729   -112    469  -3386       C  
ATOM   2057  CD1 PHE A 350     -21.732 -37.387  27.059  1.00 67.06           C  
ANISOU 2057  CD1 PHE A 350     9459   6578   9441     77    589  -3576       C  
ATOM   2058  CD2 PHE A 350     -23.857 -36.328  27.272  1.00 68.01           C  
ANISOU 2058  CD2 PHE A 350     9380   6851   9611   -328    323  -3306       C  
ATOM   2059  CE1 PHE A 350     -21.377 -36.482  26.078  1.00 66.32           C  
ANISOU 2059  CE1 PHE A 350     9327   6776   9094     30    576  -3680       C  
ATOM   2060  CE2 PHE A 350     -23.508 -35.421  26.292  1.00 66.67           C  
ANISOU 2060  CE2 PHE A 350     9184   6961   9185   -360    293  -3402       C  
ATOM   2061  CZ  PHE A 350     -22.266 -35.497  25.694  1.00 66.27           C  
ANISOU 2061  CZ  PHE A 350     9221   6979   8978   -191    426  -3587       C  
ATOM   2062  N   TYR A 351     -22.187 -37.494  31.597  1.00 62.64           N  
ANISOU 2062  N   TYR A 351     8586   5770   9445    422    684  -2752       N  
ATOM   2063  CA  TYR A 351     -21.691 -36.504  32.543  1.00 60.97           C  
ANISOU 2063  CA  TYR A 351     8179   5798   9188    580    715  -2555       C  
ATOM   2064  C   TYR A 351     -20.268 -36.862  32.948  1.00 60.12           C  
ANISOU 2064  C   TYR A 351     8086   5684   9073    910    828  -2596       C  
ATOM   2065  O   TYR A 351     -19.361 -36.020  32.891  1.00 58.79           O  
ANISOU 2065  O   TYR A 351     7777   5787   8771   1037    860  -2621       O  
ATOM   2066  CB  TYR A 351     -22.601 -36.440  33.771  1.00 63.12           C  
ANISOU 2066  CB  TYR A 351     8386   5989   9607    519    694  -2284       C  
ATOM   2067  CG  TYR A 351     -22.239 -35.361  34.764  1.00 61.95           C  
ANISOU 2067  CG  TYR A 351     8052   6087   9398    651    713  -2086       C  
ATOM   2068  CD1 TYR A 351     -22.768 -34.084  34.651  1.00 61.43           C  
ANISOU 2068  CD1 TYR A 351     7822   6281   9238    510    646  -2007       C  
ATOM   2069  CD2 TYR A 351     -21.376 -35.621  35.821  1.00 61.53           C  
ANISOU 2069  CD2 TYR A 351     7999   5999   9379    921    789  -1979       C  
ATOM   2070  CE1 TYR A 351     -22.445 -33.093  35.556  1.00 60.10           C  
ANISOU 2070  CE1 TYR A 351     7504   6319   9013    620    667  -1844       C  
ATOM   2071  CE2 TYR A 351     -21.047 -34.637  36.733  1.00 59.98           C  
ANISOU 2071  CE2 TYR A 351     7644   6030   9115   1027    793  -1816       C  
ATOM   2072  CZ  TYR A 351     -21.584 -33.374  36.595  1.00 58.99           C  
ANISOU 2072  CZ  TYR A 351     7368   6148   8898    869    738  -1756       C  
ATOM   2073  OH  TYR A 351     -21.261 -32.387  37.499  1.00 56.02           O  
ANISOU 2073  OH  TYR A 351     6852   5981   8451    963    746  -1611       O  
ATOM   2074  N   MET A 352     -20.083 -38.119  33.347  1.00 64.62           N  
ANISOU 2074  N   MET A 352     8822   5937   9793   1047    887  -2604       N  
ATOM   2075  CA  MET A 352     -18.761 -38.624  33.707  1.00 64.09           C  
ANISOU 2075  CA  MET A 352     8779   5830   9742   1387    984  -2650       C  
ATOM   2076  C   MET A 352     -17.743 -38.383  32.592  1.00 63.10           C  
ANISOU 2076  C   MET A 352     8623   5885   9467   1473   1040  -2909       C  
ATOM   2077  O   MET A 352     -16.666 -37.833  32.832  1.00 61.75           O  
ANISOU 2077  O   MET A 352     8295   5944   9221   1680   1089  -2909       O  
ATOM   2078  CB  MET A 352     -18.824 -40.117  34.035  1.00 66.35           C  
ANISOU 2078  CB  MET A 352     9301   5696  10211   1496   1037  -2657       C  
ATOM   2079  CG  MET A 352     -19.688 -40.461  35.237  1.00 67.35           C  
ANISOU 2079  CG  MET A 352     9477   5622  10489   1438   1017  -2387       C  
ATOM   2080  SD  MET A 352     -19.667 -42.226  35.608  1.00 69.97           S  
ANISOU 2080  SD  MET A 352    10121   5432  11033   1577   1096  -2387       S  
ATOM   2081  CE  MET A 352     -20.754 -42.290  37.029  1.00 71.74           C  
ANISOU 2081  CE  MET A 352    10357   5512  11387   1459   1086  -2033       C  
ATOM   2082  N   LEU A 353     -18.100 -38.788  31.376  1.00 90.64           N  
ANISOU 2082  N   LEU A 353    12259   9275  12905   1301   1033  -3132       N  
ATOM   2083  CA  LEU A 353     -17.229 -38.630  30.212  1.00 90.94           C  
ANISOU 2083  CA  LEU A 353    12305   9466  12782   1357   1106  -3394       C  
ATOM   2084  C   LEU A 353     -16.855 -37.169  29.954  1.00 88.86           C  
ANISOU 2084  C   LEU A 353    11817   9617  12329   1308   1096  -3363       C  
ATOM   2085  O   LEU A 353     -15.669 -36.814  29.893  1.00 87.57           O  
ANISOU 2085  O   LEU A 353    11536   9664  12072   1495   1180  -3375       O  
ATOM   2086  CB  LEU A 353     -17.906 -39.215  28.971  1.00 92.82           C  
ANISOU 2086  CB  LEU A 353    12758   9541  12967   1125   1072  -3622       C  
ATOM   2087  CG  LEU A 353     -17.207 -38.996  27.628  1.00 94.32           C  
ANISOU 2087  CG  LEU A 353    12999   9929  12910   1111   1121  -3816       C  
ATOM   2088  CD1 LEU A 353     -15.884 -39.745  27.577  1.00 96.63           C  
ANISOU 2088  CD1 LEU A 353    13362  10170  13182   1411   1252  -3850       C  
ATOM   2089  CD2 LEU A 353     -18.112 -39.413  26.478  1.00 95.89           C  
ANISOU 2089  CD2 LEU A 353    13399  10006  13027    826   1035  -3998       C  
ATOM   2090  N   SER A 354     -17.877 -36.333  29.799  1.00 63.67           N  
ANISOU 2090  N   SER A 354     8570   6553   9068   1038    981  -3262       N  
ATOM   2091  CA  SER A 354     -17.690 -34.916  29.505  1.00 61.77           C  
ANISOU 2091  CA  SER A 354     8153   6669   8649    956    963  -3221       C  
ATOM   2092  C   SER A 354     -16.812 -34.227  30.543  1.00 59.40           C  
ANISOU 2092  C   SER A 354     7644   6560   8367   1161   1014  -3069       C  
ATOM   2093  O   SER A 354     -15.853 -33.537  30.189  1.00 57.98           O  
ANISOU 2093  O   SER A 354     7344   6624   8061   1239   1091  -3148       O  
ATOM   2094  CB  SER A 354     -19.043 -34.208  29.400  1.00 60.76           C  
ANISOU 2094  CB  SER A 354     7997   6602   8487    669    817  -3092       C  
ATOM   2095  OG  SER A 354     -19.823 -34.425  30.562  1.00 61.75           O  
ANISOU 2095  OG  SER A 354     8090   6580   8795    650    759  -2873       O  
ATOM   2096  N   ASN A 355     -17.131 -34.420  31.820  1.00 71.32           N  
ANISOU 2096  N   ASN A 355     9112   7961  10026   1240    975  -2856       N  
ATOM   2097  CA  ASN A 355     -16.327 -33.828  32.886  1.00 69.93           C  
ANISOU 2097  CA  ASN A 355     8752   7957   9860   1435   1001  -2714       C  
ATOM   2098  C   ASN A 355     -14.895 -34.362  32.898  1.00 70.47           C  
ANISOU 2098  C   ASN A 355     8780   8049   9946   1729   1107  -2842       C  
ATOM   2099  O   ASN A 355     -13.944 -33.621  33.180  1.00 69.61           O  
ANISOU 2099  O   ASN A 355     8502   8203   9745   1814   1125  -2759       O  
ATOM   2100  CB  ASN A 355     -16.993 -34.026  34.248  1.00 68.81           C  
ANISOU 2100  CB  ASN A 355     8612   7677   9856   1466    944  -2464       C  
ATOM   2101  CG  ASN A 355     -18.254 -33.199  34.402  1.00 69.48           C  
ANISOU 2101  CG  ASN A 355     8656   7824   9921   1211    856  -2313       C  
ATOM   2102  OD1 ASN A 355     -18.906 -32.848  33.418  1.00 69.51           O  
ANISOU 2102  OD1 ASN A 355     8687   7875   9847    991    810  -2397       O  
ATOM   2103  ND2 ASN A 355     -18.599 -32.875  35.642  1.00 69.80           N  
ANISOU 2103  ND2 ASN A 355     8629   7871  10022   1249    830  -2089       N  
ATOM   2104  N   ALA A 356     -14.749 -35.647  32.582  1.00 52.96           N  
ANISOU 2104  N   ALA A 356     6745   5570   7808   1830   1151  -2936       N  
ATOM   2105  CA  ALA A 356     -13.430 -36.257  32.465  1.00 55.11           C  
ANISOU 2105  CA  ALA A 356     7022   5870   8049   2065   1234  -2952       C  
ATOM   2106  C   ALA A 356     -12.596 -35.520  31.426  1.00 55.09           C  
ANISOU 2106  C   ALA A 356     6918   6159   7856   1998   1300  -3051       C  
ATOM   2107  O   ALA A 356     -11.434 -35.199  31.672  1.00 55.34           O  
ANISOU 2107  O   ALA A 356     6790   6388   7847   2134   1348  -2984       O  
ATOM   2108  CB  ALA A 356     -13.546 -37.731  32.111  1.00 58.13           C  
ANISOU 2108  CB  ALA A 356     7654   5904   8529   2154   1279  -3060       C  
ATOM   2109  N   LEU A 357     -13.195 -35.241  30.271  1.00 55.00           N  
ANISOU 2109  N   LEU A 357     6999   6169   7730   1774   1300  -3204       N  
ATOM   2110  CA  LEU A 357     -12.506 -34.476  29.232  1.00 55.08           C  
ANISOU 2110  CA  LEU A 357     6939   6444   7545   1687   1368  -3285       C  
ATOM   2111  C   LEU A 357     -12.216 -33.042  29.682  1.00 52.53           C  
ANISOU 2111  C   LEU A 357     6384   6427   7149   1616   1341  -3147       C  
ATOM   2112  O   LEU A 357     -11.161 -32.478  29.362  1.00 52.88           O  
ANISOU 2112  O   LEU A 357     6304   6690   7099   1644   1415  -3139       O  
ATOM   2113  CB  LEU A 357     -13.312 -34.477  27.932  1.00 55.67           C  
ANISOU 2113  CB  LEU A 357     7190   6473   7490   1455   1354  -3461       C  
ATOM   2114  CG  LEU A 357     -13.470 -35.841  27.255  1.00 58.67           C  
ANISOU 2114  CG  LEU A 357     7823   6569   7898   1492   1388  -3628       C  
ATOM   2115  CD1 LEU A 357     -14.222 -35.710  25.940  1.00 59.31           C  
ANISOU 2115  CD1 LEU A 357     8069   6656   7811   1239   1349  -3792       C  
ATOM   2116  CD2 LEU A 357     -12.112 -36.491  27.041  1.00 61.22           C  
ANISOU 2116  CD2 LEU A 357     8152   6896   8212   1739   1528  -3670       C  
ATOM   2117  N   VAL A 358     -13.156 -32.461  30.425  1.00 57.18           N  
ANISOU 2117  N   VAL A 358     6919   7014   7791   1517   1241  -3042       N  
ATOM   2118  CA  VAL A 358     -12.984 -31.118  30.973  1.00 54.43           C  
ANISOU 2118  CA  VAL A 358     6376   6920   7385   1451   1207  -2901       C  
ATOM   2119  C   VAL A 358     -11.718 -31.036  31.821  1.00 54.03           C  
ANISOU 2119  C   VAL A 358     6164   6989   7375   1645   1233  -2781       C  
ATOM   2120  O   VAL A 358     -10.935 -30.093  31.695  1.00 52.75           O  
ANISOU 2120  O   VAL A 358     5857   7063   7121   1595   1259  -2743       O  
ATOM   2121  CB  VAL A 358     -14.203 -30.681  31.815  1.00 52.43           C  
ANISOU 2121  CB  VAL A 358     6101   6605   7213   1364   1108  -2799       C  
ATOM   2122  CG1 VAL A 358     -13.886 -29.420  32.607  1.00 50.50           C  
ANISOU 2122  CG1 VAL A 358     5668   6594   6924   1346   1077  -2634       C  
ATOM   2123  CG2 VAL A 358     -15.414 -30.463  30.924  1.00 52.99           C  
ANISOU 2123  CG2 VAL A 358     6294   6622   7217   1115   1054  -2870       C  
ATOM   2124  N   TYR A 359     -11.513 -32.036  32.673  1.00 59.99           N  
ANISOU 2124  N   TYR A 359     6953   7571   8271   1859   1222  -2724       N  
ATOM   2125  CA  TYR A 359     -10.297 -32.099  33.479  1.00 61.15           C  
ANISOU 2125  CA  TYR A 359     6954   7821   8461   2057   1234  -2622       C  
ATOM   2126  C   TYR A 359      -9.078 -32.433  32.619  1.00 63.82           C  
ANISOU 2126  C   TYR A 359     7256   8239   8754   2138   1349  -2737       C  
ATOM   2127  O   TYR A 359      -7.962 -31.971  32.892  1.00 64.16           O  
ANISOU 2127  O   TYR A 359     7115   8480   8785   2198   1369  -2691       O  
ATOM   2128  CB  TYR A 359     -10.458 -33.114  34.611  1.00 62.45           C  
ANISOU 2128  CB  TYR A 359     7185   7765   8779   2272   1191  -2517       C  
ATOM   2129  CG  TYR A 359     -11.537 -32.731  35.595  1.00 61.25           C  
ANISOU 2129  CG  TYR A 359     7044   7555   8674   2211   1093  -2383       C  
ATOM   2130  CD1 TYR A 359     -11.776 -31.399  35.902  1.00 59.81           C  
ANISOU 2130  CD1 TYR A 359     6728   7592   8405   2055   1040  -2304       C  
ATOM   2131  CD2 TYR A 359     -12.319 -33.698  36.213  1.00 63.31           C  
ANISOU 2131  CD2 TYR A 359     7458   7527   9072   2308   1064  -2332       C  
ATOM   2132  CE1 TYR A 359     -12.760 -31.037  36.797  1.00 59.46           C  
ANISOU 2132  CE1 TYR A 359     6691   7499   8403   2010    969  -2182       C  
ATOM   2133  CE2 TYR A 359     -13.309 -33.345  37.112  1.00 63.25           C  
ANISOU 2133  CE2 TYR A 359     7454   7463   9118   2254    992  -2207       C  
ATOM   2134  CZ  TYR A 359     -13.524 -32.012  37.399  1.00 60.80           C  
ANISOU 2134  CZ  TYR A 359     6997   7394   8713   2112    949  -2135       C  
ATOM   2135  OH  TYR A 359     -14.504 -31.648  38.290  1.00 60.38           O  
ANISOU 2135  OH  TYR A 359     6960   7289   8695   2041    891  -1974       O  
ATOM   2136  N   VAL A 360      -9.304 -33.231  31.577  1.00 56.42           N  
ANISOU 2136  N   VAL A 360     6495   7146   7796   2132   1424  -2895       N  
ATOM   2137  CA  VAL A 360      -8.252 -33.582  30.627  1.00 58.93           C  
ANISOU 2137  CA  VAL A 360     6807   7526   8058   2203   1556  -3021       C  
ATOM   2138  C   VAL A 360      -7.636 -32.330  30.007  1.00 58.14           C  
ANISOU 2138  C   VAL A 360     6549   7724   7819   2044   1600  -3035       C  
ATOM   2139  O   VAL A 360      -6.427 -32.269  29.814  1.00 59.84           O  
ANISOU 2139  O   VAL A 360     6633   8075   8031   2136   1690  -3059       O  
ATOM   2140  CB  VAL A 360      -8.767 -34.541  29.520  1.00 60.82           C  
ANISOU 2140  CB  VAL A 360     7302   7548   8261   2178   1621  -3204       C  
ATOM   2141  CG1 VAL A 360      -7.882 -34.481  28.280  1.00 62.97           C  
ANISOU 2141  CG1 VAL A 360     7573   7943   8410   2175   1766  -3344       C  
ATOM   2142  CG2 VAL A 360      -8.851 -35.964  30.045  1.00 62.79           C  
ANISOU 2142  CG2 VAL A 360     7703   7487   8668   2393   1624  -3205       C  
ATOM   2143  N   SER A 361      -8.464 -31.330  29.718  1.00 62.35           N  
ANISOU 2143  N   SER A 361     7092   8349   8249   1807   1542  -3016       N  
ATOM   2144  CA  SER A 361      -7.960 -30.055  29.200  1.00 61.27           C  
ANISOU 2144  CA  SER A 361     6826   8472   7984   1641   1581  -3005       C  
ATOM   2145  C   SER A 361      -7.030 -29.355  30.197  1.00 60.53           C  
ANISOU 2145  C   SER A 361     6493   8558   7950   1699   1549  -2878       C  
ATOM   2146  O   SER A 361      -5.884 -28.999  29.871  1.00 61.29           O  
ANISOU 2146  O   SER A 361     6449   8820   8018   1712   1634  -2909       O  
ATOM   2147  CB  SER A 361      -9.125 -29.130  28.839  1.00 59.21           C  
ANISOU 2147  CB  SER A 361     6637   8249   7614   1393   1514  -2989       C  
ATOM   2148  OG  SER A 361      -8.657 -27.859  28.421  1.00 58.51           O  
ANISOU 2148  OG  SER A 361     6440   8385   7406   1237   1553  -2959       O  
ATOM   2149  N   ALA A 362      -7.535 -29.169  31.414  1.00 71.49           N  
ANISOU 2149  N   ALA A 362     7836   9908   9417   1729   1426  -2743       N  
ATOM   2150  CA  ALA A 362      -6.791 -28.506  32.481  1.00 71.12           C  
ANISOU 2150  CA  ALA A 362     7589  10015   9416   1774   1363  -2624       C  
ATOM   2151  C   ALA A 362      -5.467 -29.206  32.765  1.00 73.90           C  
ANISOU 2151  C   ALA A 362     7815  10403   9858   1995   1413  -2648       C  
ATOM   2152  O   ALA A 362      -4.496 -28.571  33.179  1.00 73.45           O  
ANISOU 2152  O   ALA A 362     7561  10535   9809   1998   1400  -2617       O  
ATOM   2153  CB  ALA A 362      -7.634 -28.430  33.745  1.00 66.38           C  
ANISOU 2153  CB  ALA A 362     7010   9330   8882   1806   1232  -2484       C  
ATOM   2154  N   ALA A 363      -5.431 -30.515  32.539  1.00 67.13           N  
ANISOU 2154  N   ALA A 363     7073   9358   9074   2178   1468  -2712       N  
ATOM   2155  CA  ALA A 363      -4.198 -31.275  32.708  1.00 69.92           C  
ANISOU 2155  CA  ALA A 363     7317   9726   9523   2410   1531  -2742       C  
ATOM   2156  C   ALA A 363      -3.332 -31.249  31.448  1.00 72.08           C  
ANISOU 2156  C   ALA A 363     7548  10108   9731   2383   1693  -2887       C  
ATOM   2157  O   ALA A 363      -2.130 -31.507  31.509  1.00 74.50           O  
ANISOU 2157  O   ALA A 363     7688  10514  10103   2530   1756  -2915       O  
ATOM   2158  CB  ALA A 363      -4.509 -32.709  33.112  1.00 71.44           C  
ANISOU 2158  CB  ALA A 363     7662   9644   9837   2639   1528  -2733       C  
ATOM   2159  N   ILE A 364      -3.944 -30.932  30.310  1.00 76.83           N  
ANISOU 2159  N   ILE A 364     8294  10697  10202   2199   1760  -2980       N  
ATOM   2160  CA  ILE A 364      -3.241 -30.973  29.030  1.00 79.01           C  
ANISOU 2160  CA  ILE A 364     8575  11052  10391   2173   1929  -3122       C  
ATOM   2161  C   ILE A 364      -2.547 -29.652  28.725  1.00 78.76           C  
ANISOU 2161  C   ILE A 364     8356  11290  10277   1999   1970  -3111       C  
ATOM   2162  O   ILE A 364      -1.645 -29.602  27.890  1.00 82.05           O  
ANISOU 2162  O   ILE A 364     8705  11817  10652   2010   2120  -3206       O  
ATOM   2163  CB  ILE A 364      -4.170 -31.364  27.849  1.00 78.33           C  
ANISOU 2163  CB  ILE A 364     8758  10824  10179   2062   1987  -3243       C  
ATOM   2164  CG1 ILE A 364      -3.414 -32.214  26.825  1.00 81.64           C  
ANISOU 2164  CG1 ILE A 364     9248  11207  10564   2185   2168  -3400       C  
ATOM   2165  CG2 ILE A 364      -4.772 -30.132  27.184  1.00 76.80           C  
ANISOU 2165  CG2 ILE A 364     8593  10765   9823   1773   1966  -3235       C  
ATOM   2166  CD1 ILE A 364      -3.098 -33.613  27.305  1.00 84.59           C  
ANISOU 2166  CD1 ILE A 364     9678  11374  11089   2473   2200  -3429       C  
ATOM   2167  N   ASN A 365      -2.968 -28.584  29.397  1.00 89.96           N  
ANISOU 2167  N   ASN A 365     9700  12807  11674   1839   1849  -3000       N  
ATOM   2168  CA  ASN A 365      -2.285 -27.297  29.233  1.00 89.99           C  
ANISOU 2168  CA  ASN A 365     9530  13046  11615   1669   1883  -2986       C  
ATOM   2169  C   ASN A 365      -0.759 -27.299  29.459  1.00 92.48           C  
ANISOU 2169  C   ASN A 365     9594  13527  12018   1790   1953  -3018       C  
ATOM   2170  O   ASN A 365      -0.016 -26.820  28.603  1.00 94.09           O  
ANISOU 2170  O   ASN A 365     9718  13873  12158   1701   2091  -3094       O  
ATOM   2171  CB  ASN A 365      -2.962 -26.189  30.052  1.00 88.21           C  
ANISOU 2171  CB  ASN A 365     9272  12876  11366   1499   1739  -2862       C  
ATOM   2172  CG  ASN A 365      -4.068 -25.493  29.285  1.00 86.34           C  
ANISOU 2172  CG  ASN A 365     9211  12607  10989   1272   1741  -2860       C  
ATOM   2173  OD1 ASN A 365      -4.149 -25.597  28.061  1.00 86.54           O  
ANISOU 2173  OD1 ASN A 365     9360  12613  10908   1207   1853  -2956       O  
ATOM   2174  ND2 ASN A 365      -4.922 -24.770  30.001  1.00 84.41           N  
ANISOU 2174  ND2 ASN A 365     8979  12359  10733   1156   1618  -2752       N  
ATOM   2175  N   PRO A 366      -0.281 -27.842  30.598  1.00 78.19           N  
ANISOU 2175  N   PRO A 366     7654  11704  10351   1993   1859  -2960       N  
ATOM   2176  CA  PRO A 366       1.166 -27.753  30.834  1.00 80.14           C  
ANISOU 2176  CA  PRO A 366     7633  12134  10683   2095   1909  -2994       C  
ATOM   2177  C   PRO A 366       1.997 -28.802  30.091  1.00 82.95           C  
ANISOU 2177  C   PRO A 366     7968  12453  11094   2300   2079  -3107       C  
ATOM   2178  O   PRO A 366       3.157 -28.534  29.778  1.00 85.64           O  
ANISOU 2178  O   PRO A 366     8103  12973  11464   2316   2186  -3171       O  
ATOM   2179  CB  PRO A 366       1.281 -27.973  32.343  1.00 80.37           C  
ANISOU 2179  CB  PRO A 366     7549  12158  10830   2245   1729  -2887       C  
ATOM   2180  CG  PRO A 366       0.140 -28.862  32.664  1.00 79.65           C  
ANISOU 2180  CG  PRO A 366     7692  11814  10758   2346   1659  -2828       C  
ATOM   2181  CD  PRO A 366      -0.982 -28.447  31.748  1.00 77.85           C  
ANISOU 2181  CD  PRO A 366     7681  11503  10393   2127   1703  -2855       C  
ATOM   2182  N   ILE A 367       1.422 -29.970  29.819  1.00 68.30           N  
ANISOU 2182  N   ILE A 367     6322  10367   9260   2454   2110  -3137       N  
ATOM   2183  CA  ILE A 367       2.163 -31.048  29.165  1.00 71.94           C  
ANISOU 2183  CA  ILE A 367     6792  10762   9779   2674   2276  -3247       C  
ATOM   2184  C   ILE A 367       2.553 -30.676  27.732  1.00 73.48           C  
ANISOU 2184  C   ILE A 367     7017  11060   9843   2546   2480  -3376       C  
ATOM   2185  O   ILE A 367       3.592 -31.108  27.230  1.00 76.93           O  
ANISOU 2185  O   ILE A 367     7343  11562  10324   2689   2643  -3467       O  
ATOM   2186  CB  ILE A 367       1.379 -32.386  29.192  1.00 72.26           C  
ANISOU 2186  CB  ILE A 367     7090  10498   9866   2853   2267  -3261       C  
ATOM   2187  CG1 ILE A 367       2.227 -33.530  28.628  1.00 76.36           C  
ANISOU 2187  CG1 ILE A 367     7626  10934  10453   3098   2451  -3380       C  
ATOM   2188  CG2 ILE A 367       0.074 -32.266  28.433  1.00 69.88           C  
ANISOU 2188  CG2 ILE A 367     7071  10063   9418   2656   2255  -3291       C  
ATOM   2189  CD1 ILE A 367       1.477 -34.841  28.502  1.00 77.09           C  
ANISOU 2189  CD1 ILE A 367     8005  10704  10582   3255   2468  -3419       C  
ATOM   2190  N   LEU A 368       1.727 -29.858  27.086  1.00 71.14           N  
ANISOU 2190  N   LEU A 368     6866  10781   9382   2282   2474  -3379       N  
ATOM   2191  CA  LEU A 368       2.014 -29.395  25.733  1.00 72.50           C  
ANISOU 2191  CA  LEU A 368     7086  11058   9401   2135   2657  -3483       C  
ATOM   2192  C   LEU A 368       3.218 -28.459  25.727  1.00 73.95           C  
ANISOU 2192  C   LEU A 368     6980  11508   9610   2056   2736  -3483       C  
ATOM   2193  O   LEU A 368       3.922 -28.342  24.724  1.00 76.59           O  
ANISOU 2193  O   LEU A 368     7274  11948   9878   2034   2935  -3580       O  
ATOM   2194  CB  LEU A 368       0.796 -28.688  25.134  1.00 69.66           C  
ANISOU 2194  CB  LEU A 368     6948  10657   8864   1871   2606  -3464       C  
ATOM   2195  CG  LEU A 368      -0.443 -29.553  24.897  1.00 68.61           C  
ANISOU 2195  CG  LEU A 368     7112  10274   8681   1905   2545  -3496       C  
ATOM   2196  CD1 LEU A 368      -1.591 -28.711  24.362  1.00 65.93           C  
ANISOU 2196  CD1 LEU A 368     6943   9933   8176   1634   2477  -3467       C  
ATOM   2197  CD2 LEU A 368      -0.126 -30.699  23.951  1.00 71.92           C  
ANISOU 2197  CD2 LEU A 368     7684  10581   9060   2064   2714  -3650       C  
ATOM   2198  N   TYR A 369       3.449 -27.797  26.856  1.00 87.89           N  
ANISOU 2198  N   TYR A 369     8547  13380  11467   2009   2583  -3380       N  
ATOM   2199  CA  TYR A 369       4.575 -26.882  26.991  1.00 90.02           C  
ANISOU 2199  CA  TYR A 369     8529  13899  11775   1919   2632  -3385       C  
ATOM   2200  C   TYR A 369       5.872 -27.665  27.177  1.00 94.20           C  
ANISOU 2200  C   TYR A 369     8825  14507  12460   2180   2724  -3447       C  
ATOM   2201  O   TYR A 369       6.962 -27.145  26.942  1.00 97.33           O  
ANISOU 2201  O   TYR A 369     8985  15109  12886   2137   2839  -3498       O  
ATOM   2202  CB  TYR A 369       4.362 -25.932  28.173  1.00 82.88           C  
ANISOU 2202  CB  TYR A 369     7506  13074  10911   1791   2426  -3272       C  
ATOM   2203  CG  TYR A 369       3.059 -25.160  28.140  1.00 78.85           C  
ANISOU 2203  CG  TYR A 369     7208  12480  10270   1559   2326  -3197       C  
ATOM   2204  CD1 TYR A 369       2.429 -24.864  26.938  1.00 78.40           C  
ANISOU 2204  CD1 TYR A 369     7363  12373  10051   1396   2439  -3237       C  
ATOM   2205  CD2 TYR A 369       2.461 -24.726  29.316  1.00 76.39           C  
ANISOU 2205  CD2 TYR A 369     6886  12144   9994   1514   2121  -3086       C  
ATOM   2206  CE1 TYR A 369       1.239 -24.160  26.909  1.00 75.34           C  
ANISOU 2206  CE1 TYR A 369     7155  11915   9554   1199   2344  -3164       C  
ATOM   2207  CE2 TYR A 369       1.273 -24.020  29.297  1.00 73.21           C  
ANISOU 2207  CE2 TYR A 369     6665  11666   9485   1318   2041  -3016       C  
ATOM   2208  CZ  TYR A 369       0.666 -23.741  28.091  1.00 72.60           C  
ANISOU 2208  CZ  TYR A 369     6781  11541   9262   1164   2150  -3054       C  
ATOM   2209  OH  TYR A 369      -0.517 -23.039  28.067  1.00 70.24           O  
ANISOU 2209  OH  TYR A 369     6650  11172   8865    983   2067  -2980       O  
ATOM   2210  N   ASN A 370       5.742 -28.917  27.606  1.00122.94           N  
ANISOU 2210  N   ASN A 370    12530  17975  16205   2451   2677  -3441       N  
ATOM   2211  CA  ASN A 370       6.895 -29.790  27.796  1.00126.31           C  
ANISOU 2211  CA  ASN A 370    12756  18442  16792   2737   2762  -3492       C  
ATOM   2212  C   ASN A 370       7.247 -30.565  26.530  1.00128.88           C  
ANISOU 2212  C   ASN A 370    13186  18711  17071   2850   3018  -3627       C  
ATOM   2213  O   ASN A 370       8.419 -30.817  26.252  1.00132.67           O  
ANISOU 2213  O   ASN A 370    13449  19324  17635   2984   3172  -3698       O  
ATOM   2214  CB  ASN A 370       6.645 -30.771  28.945  1.00125.51           C  
ANISOU 2214  CB  ASN A 370    12684  18168  16834   2995   2599  -3413       C  
ATOM   2215  CG  ASN A 370       6.617 -30.090  30.300  1.00123.97           C  
ANISOU 2215  CG  ASN A 370    12323  18076  16705   2948   2360  -3291       C  
ATOM   2216  OD1 ASN A 370       7.349 -29.132  30.542  1.00125.11           O  
ANISOU 2216  OD1 ASN A 370    12216  18457  16861   2825   2334  -3292       O  
ATOM   2217  ND2 ASN A 370       5.770 -30.588  31.194  1.00121.77           N  
ANISOU 2217  ND2 ASN A 370    12189  17615  16463   3044   2189  -3191       N  
ATOM   2218  N   LEU A 371       6.224 -30.933  25.764  1.00138.65           N  
ANISOU 2218  N   LEU A 371    14754  19754  18170   2796   3063  -3668       N  
ATOM   2219  CA  LEU A 371       6.403 -31.769  24.579  1.00141.92           C  
ANISOU 2219  CA  LEU A 371    15332  20075  18515   2918   3291  -3806       C  
ATOM   2220  C   LEU A 371       7.177 -31.083  23.454  1.00144.50           C  
ANISOU 2220  C   LEU A 371    15561  20613  18728   2784   3516  -3899       C  
ATOM   2221  O   LEU A 371       7.664 -31.745  22.538  1.00149.21           O  
ANISOU 2221  O   LEU A 371    16212  21189  19292   2927   3735  -4020       O  
ATOM   2222  CB  LEU A 371       5.050 -32.261  24.058  1.00136.40           C  
ANISOU 2222  CB  LEU A 371    15023  19126  17676   2859   3257  -3837       C  
ATOM   2223  CG  LEU A 371       4.324 -33.289  24.927  1.00135.08           C  
ANISOU 2223  CG  LEU A 371    15004  18694  17626   3048   3110  -3785       C  
ATOM   2224  CD1 LEU A 371       3.002 -33.691  24.293  1.00133.40           C  
ANISOU 2224  CD1 LEU A 371    15166  18254  17266   2952   3084  -3838       C  
ATOM   2225  CD2 LEU A 371       5.204 -34.508  25.160  1.00139.18           C  
ANISOU 2225  CD2 LEU A 371    15441  19122  18317   3396   3217  -3836       C  
ATOM   2226  N   VAL A 372       7.292 -29.761  23.525  1.00110.63           N  
ANISOU 2226  N   VAL A 372    11139  16519  14376   2514   3474  -3843       N  
ATOM   2227  CA  VAL A 372       8.023 -29.009  22.510  1.00113.42           C  
ANISOU 2227  CA  VAL A 372    11394  17076  14624   2362   3690  -3914       C  
ATOM   2228  C   VAL A 372       9.532 -29.107  22.715  1.00117.80           C  
ANISOU 2228  C   VAL A 372    11587  17826  15348   2521   3820  -3956       C  
ATOM   2229  O   VAL A 372      10.309 -28.545  21.942  1.00120.73           O  
ANISOU 2229  O   VAL A 372    11832  18380  15662   2424   4025  -4020       O  
ATOM   2230  CB  VAL A 372       7.608 -27.528  22.491  1.00108.19           C  
ANISOU 2230  CB  VAL A 372    10724  16538  13845   2011   3613  -3837       C  
ATOM   2231  CG1 VAL A 372       6.141 -27.398  22.126  1.00104.76           C  
ANISOU 2231  CG1 VAL A 372    10641  15930  13236   1855   3513  -3803       C  
ATOM   2232  CG2 VAL A 372       7.888 -26.883  23.838  1.00106.48           C  
ANISOU 2232  CG2 VAL A 372    10250  16427  13783   1964   3409  -3731       C  
ATOM   2233  N   SER A 373       9.931 -29.819  23.767  1.00193.06           N  
ANISOU 2233  N   SER A 373    20949  27320  25087   2765   3697  -3916       N  
ATOM   2234  CA  SER A 373      11.339 -30.049  24.089  1.00197.87           C  
ANISOU 2234  CA  SER A 373    21194  28103  25885   2958   3787  -3950       C  
ATOM   2235  C   SER A 373      12.119 -28.757  24.318  1.00198.86           C  
ANISOU 2235  C   SER A 373    21004  28516  26039   2733   3783  -3927       C  
ATOM   2236  O   SER A 373      13.340 -28.724  24.161  1.00203.10           O  
ANISOU 2236  O   SER A 373    21235  29244  26690   2822   3924  -3983       O  
ATOM   2237  CB  SER A 373      12.016 -30.899  23.008  1.00198.18           C  
ANISOU 2237  CB  SER A 373    21259  28124  25916   3166   4081  -4084       C  
ATOM   2238  OG  SER A 373      13.374 -31.142  23.329  1.00201.26           O  
ANISOU 2238  OG  SER A 373    21278  28684  26509   3372   4169  -4113       O  
ATOM   2239  N   ALA A 374      11.411 -27.697  24.693  1.00152.70           N  
ANISOU 2239  N   ALA A 374    15231  22693  20093   2442   3627  -3848       N  
ATOM   2240  CA  ALA A 374      12.049 -26.424  25.000  1.00152.40           C  
ANISOU 2240  CA  ALA A 374    14926  22897  20080   2207   3600  -3825       C  
ATOM   2241  C   ALA A 374      12.745 -26.505  26.352  1.00153.50           C  
ANISOU 2241  C   ALA A 374    14755  23139  20428   2350   3405  -3778       C  
ATOM   2242  O   ALA A 374      12.665 -27.523  27.040  1.00153.21           O  
ANISOU 2242  O   ALA A 374    14741  22972  20499   2618   3280  -3743       O  
ATOM   2243  CB  ALA A 374      11.025 -25.302  24.996  1.00151.05           C  
ANISOU 2243  CB  ALA A 374    14954  22689  19748   1878   3485  -3752       C  
ATOM   2244  N   ASN A 375      13.423 -25.428  26.733  1.00131.09           N  
ANISOU 2244  N   ASN A 375    11636  20532  17640   2168   3375  -3777       N  
ATOM   2245  CA  ASN A 375      14.098 -25.375  28.025  1.00132.08           C  
ANISOU 2245  CA  ASN A 375    11456  20786  17943   2277   3174  -3742       C  
ATOM   2246  C   ASN A 375      13.102 -25.324  29.180  1.00128.03           C  
ANISOU 2246  C   ASN A 375    11100  20137  17410   2267   2871  -3631       C  
ATOM   2247  O   ASN A 375      13.469 -25.506  30.345  1.00127.81           O  
ANISOU 2247  O   ASN A 375    10883  20174  17507   2402   2672  -3590       O  
ATOM   2248  CB  ASN A 375      15.055 -24.183  28.084  1.00133.69           C  
ANISOU 2248  CB  ASN A 375    11336  21269  18191   2049   3220  -3783       C  
ATOM   2249  CG  ASN A 375      16.105 -24.228  26.991  1.00137.71           C  
ANISOU 2249  CG  ASN A 375    11667  21929  18730   2058   3535  -3886       C  
ATOM   2250  OD1 ASN A 375      17.153 -24.855  27.147  1.00142.35           O  
ANISOU 2250  OD1 ASN A 375    11973  22630  19485   2299   3606  -3936       O  
ATOM   2251  ND2 ASN A 375      15.828 -23.564  25.875  1.00136.47           N  
ANISOU 2251  ND2 ASN A 375    11672  21775  18407   1802   3730  -3914       N  
ATOM   2252  N   PHE A 376      11.838 -25.078  28.845  1.00160.84           N  
ANISOU 2252  N   PHE A 376    15599  24111  21401   2111   2841  -3583       N  
ATOM   2253  CA  PHE A 376      10.762 -25.109  29.826  1.00157.46           C  
ANISOU 2253  CA  PHE A 376    15356  23529  20943   2114   2587  -3477       C  
ATOM   2254  C   PHE A 376      10.639 -26.496  30.438  1.00157.69           C  
ANISOU 2254  C   PHE A 376    15430  23400  21085   2463   2493  -3440       C  
ATOM   2255  O   PHE A 376      10.282 -26.633  31.603  1.00156.88           O  
ANISOU 2255  O   PHE A 376    15330  23248  21028   2545   2266  -3353       O  
ATOM   2256  CB  PHE A 376       9.429 -24.700  29.194  1.00153.65           C  
ANISOU 2256  CB  PHE A 376    15229  22877  20276   1903   2600  -3438       C  
ATOM   2257  CG  PHE A 376       8.252 -24.842  30.121  1.00150.03           C  
ANISOU 2257  CG  PHE A 376    14973  22241  19793   1931   2369  -3329       C  
ATOM   2258  CD1 PHE A 376       7.935 -23.837  31.019  1.00147.26           C  
ANISOU 2258  CD1 PHE A 376    14582  21952  19419   1762   2184  -3260       C  
ATOM   2259  CD2 PHE A 376       7.463 -25.983  30.096  1.00149.39           C  
ANISOU 2259  CD2 PHE A 376    15124  21927  19712   2125   2349  -3302       C  
ATOM   2260  CE1 PHE A 376       6.856 -23.966  31.874  1.00143.99           C  
ANISOU 2260  CE1 PHE A 376    14350  21381  18980   1795   1989  -3158       C  
ATOM   2261  CE2 PHE A 376       6.386 -26.117  30.951  1.00146.39           C  
ANISOU 2261  CE2 PHE A 376    14919  21387  19316   2147   2152  -3198       C  
ATOM   2262  CZ  PHE A 376       6.080 -25.107  31.838  1.00143.98           C  
ANISOU 2262  CZ  PHE A 376    14566  21155  18985   1985   1975  -3122       C  
ATOM   2263  N   ARG A 377      10.921 -27.523  29.643  1.00124.82           N  
ANISOU 2263  N   ARG A 377    11319  19150  16959   2669   2679  -3507       N  
ATOM   2264  CA  ARG A 377      10.889 -28.896  30.131  1.00125.53           C  
ANISOU 2264  CA  ARG A 377    11459  19069  17170   3013   2623  -3480       C  
ATOM   2265  C   ARG A 377      12.086 -29.149  31.040  1.00128.35           C  
ANISOU 2265  C   ARG A 377    11455  19595  17719   3227   2535  -3473       C  
ATOM   2266  O   ARG A 377      11.990 -29.886  32.023  1.00126.95           O  
ANISOU 2266  O   ARG A 377    11274  19320  17643   3458   2364  -3398       O  
ATOM   2267  CB  ARG A 377      10.887 -29.884  28.963  1.00127.77           C  
ANISOU 2267  CB  ARG A 377    11913  19204  17432   3167   2867  -3571       C  
ATOM   2268  CG  ARG A 377      10.723 -31.338  29.378  1.00128.98           C  
ANISOU 2268  CG  ARG A 377    12183  19124  17701   3509   2829  -3547       C  
ATOM   2269  CD  ARG A 377      10.637 -32.256  28.168  1.00130.84           C  
ANISOU 2269  CD  ARG A 377    12628  19196  17892   3636   3079  -3656       C  
ATOM   2270  NE  ARG A 377      11.853 -32.216  27.361  1.00135.17           N  
ANISOU 2270  NE  ARG A 377    12945  19928  18488   3706   3319  -3767       N  
ATOM   2271  CZ  ARG A 377      12.031 -32.913  26.243  1.00138.46           C  
ANISOU 2271  CZ  ARG A 377    13497  20257  18857   3818   3575  -3882       C  
ATOM   2272  NH1 ARG A 377      11.069 -33.708  25.794  1.00137.99           N  
ANISOU 2272  NH1 ARG A 377    13810  19923  18697   3864   3610  -3910       N  
ATOM   2273  NH2 ARG A 377      13.171 -32.816  25.573  1.00142.93           N  
ANISOU 2273  NH2 ARG A 377    13827  21010  19470   3883   3799  -3976       N  
ATOM   2274  N   GLN A 378      13.211 -28.526  30.703  1.00130.59           N  
ANISOU 2274  N   GLN A 378    11432  20135  18050   3145   2650  -3549       N  
ATOM   2275  CA  GLN A 378      14.425 -28.635  31.501  1.00134.85           C  
ANISOU 2275  CA  GLN A 378    11584  20879  18772   3315   2565  -3555       C  
ATOM   2276  C   GLN A 378      14.195 -28.055  32.893  1.00132.80           C  
ANISOU 2276  C   GLN A 378    11251  20689  18518   3244   2255  -3462       C  
ATOM   2277  O   GLN A 378      14.495 -28.696  33.903  1.00133.75           O  
ANISOU 2277  O   GLN A 378    11256  20804  18757   3494   2078  -3403       O  
ATOM   2278  CB  GLN A 378      15.582 -27.907  30.814  1.00131.43           C  
ANISOU 2278  CB  GLN A 378    10842  20719  18375   3177   2759  -3658       C  
ATOM   2279  CG  GLN A 378      16.938 -28.154  31.451  1.00136.37           C  
ANISOU 2279  CG  GLN A 378    11038  21566  19211   3384   2715  -3684       C  
ATOM   2280  CD  GLN A 378      17.428 -29.572  31.241  1.00139.63           C  
ANISOU 2280  CD  GLN A 378    11408  21873  19772   3782   2830  -3707       C  
ATOM   2281  OE1 GLN A 378      17.668 -29.996  30.111  1.00141.60           O  
ANISOU 2281  OE1 GLN A 378    11707  22081  20011   3844   3110  -3791       O  
ATOM   2282  NE2 GLN A 378      17.574 -30.315  32.331  1.00140.02           N  
ANISOU 2282  NE2 GLN A 378    11378  21869  19953   4061   2618  -3632       N  
ATOM   2283  N   VAL A 379      13.651 -26.842  32.941  1.00171.07           N  
ANISOU 2283  N   VAL A 379    16179  25594  23228   2909   2193  -3447       N  
ATOM   2284  CA  VAL A 379      13.357 -26.202  34.219  1.00167.95           C  
ANISOU 2284  CA  VAL A 379    15747  25259  22810   2819   1916  -3370       C  
ATOM   2285  C   VAL A 379      12.149 -26.848  34.900  1.00163.89           C  
ANISOU 2285  C   VAL A 379    15538  24489  22243   2943   1746  -3255       C  
ATOM   2286  O   VAL A 379      11.956 -26.701  36.107  1.00162.31           O  
ANISOU 2286  O   VAL A 379    15311  24314  22047   2982   1507  -3179       O  
ATOM   2287  CB  VAL A 379      13.131 -24.682  34.068  1.00161.96           C  
ANISOU 2287  CB  VAL A 379    14994  24619  21924   2426   1915  -3394       C  
ATOM   2288  CG1 VAL A 379      14.352 -24.025  33.443  1.00164.65           C  
ANISOU 2288  CG1 VAL A 379    15028  25209  22324   2288   2092  -3503       C  
ATOM   2289  CG2 VAL A 379      11.890 -24.403  33.241  1.00158.74           C  
ANISOU 2289  CG2 VAL A 379    14957  24010  21349   2234   2008  -3366       C  
ATOM   2290  N   PHE A 380      11.344 -27.565  34.120  1.00138.85           N  
ANISOU 2290  N   PHE A 380    12659  21078  19019   3000   1875  -3247       N  
ATOM   2291  CA  PHE A 380      10.207 -28.299  34.663  1.00136.39           C  
ANISOU 2291  CA  PHE A 380    12637  20507  18677   3125   1746  -3143       C  
ATOM   2292  C   PHE A 380      10.712 -29.482  35.471  1.00139.20           C  
ANISOU 2292  C   PHE A 380    12893  20806  19190   3494   1646  -3096       C  
ATOM   2293  O   PHE A 380      10.254 -29.722  36.585  1.00135.95           O  
ANISOU 2293  O   PHE A 380    12551  20320  18786   3594   1434  -2990       O  
ATOM   2294  CB  PHE A 380       9.283 -28.788  33.545  1.00134.46           C  
ANISOU 2294  CB  PHE A 380    12718  20029  18344   3085   1919  -3167       C  
ATOM   2295  CG  PHE A 380       8.042 -29.479  34.039  1.00132.06           C  
ANISOU 2295  CG  PHE A 380    12715  19453  18010   3176   1801  -3067       C  
ATOM   2296  CD1 PHE A 380       6.919 -28.748  34.386  1.00128.31           C  
ANISOU 2296  CD1 PHE A 380    12425  18917  17412   2957   1679  -2992       C  
ATOM   2297  CD2 PHE A 380       7.997 -30.860  34.151  1.00133.49           C  
ANISOU 2297  CD2 PHE A 380    12995  19432  18295   3478   1824  -3049       C  
ATOM   2298  CE1 PHE A 380       5.776 -29.378  34.840  1.00126.00           C  
ANISOU 2298  CE1 PHE A 380    12393  18381  17101   3035   1584  -2899       C  
ATOM   2299  CE2 PHE A 380       6.857 -31.496  34.604  1.00130.92           C  
ANISOU 2299  CE2 PHE A 380    12946  18848  17950   3548   1727  -2958       C  
ATOM   2300  CZ  PHE A 380       5.745 -30.754  34.949  1.00127.15           C  
ANISOU 2300  CZ  PHE A 380    12634  18326  17350   3323   1608  -2882       C  
ATOM   2301  N   LEU A 381      11.656 -30.222  34.897  1.00155.11           N  
ANISOU 2301  N   LEU A 381    14751  22853  21329   3703   1807  -3171       N  
ATOM   2302  CA  LEU A 381      12.289 -31.327  35.605  1.00158.28           C  
ANISOU 2302  CA  LEU A 381    15023  23215  21902   4070   1725  -3130       C  
ATOM   2303  C   LEU A 381      13.130 -30.797  36.760  1.00159.80           C  
ANISOU 2303  C   LEU A 381    14891  23665  22161   4103   1503  -3095       C  
ATOM   2304  O   LEU A 381      13.238 -31.436  37.808  1.00160.22           O  
ANISOU 2304  O   LEU A 381    14908  23675  22292   4346   1311  -3005       O  
ATOM   2305  CB  LEU A 381      13.154 -32.160  34.656  1.00160.25           C  
ANISOU 2305  CB  LEU A 381    15162  23452  22275   4283   1971  -3231       C  
ATOM   2306  CG  LEU A 381      12.492 -33.353  33.959  1.00159.91           C  
ANISOU 2306  CG  LEU A 381    15436  23085  22238   4455   2128  -3244       C  
ATOM   2307  CD1 LEU A 381      11.351 -32.911  33.054  1.00156.21           C  
ANISOU 2307  CD1 LEU A 381    15292  22484  21577   4175   2238  -3276       C  
ATOM   2308  CD2 LEU A 381      13.522 -34.155  33.175  1.00164.72           C  
ANISOU 2308  CD2 LEU A 381    15891  23708  22986   4701   2364  -3348       C  
ATOM   2309  N   SER A 382      13.719 -29.620  36.562  1.00167.77           N  
ANISOU 2309  N   SER A 382    15674  24939  23132   3851   1529  -3169       N  
ATOM   2310  CA  SER A 382      14.532 -28.985  37.594  1.00168.74           C  
ANISOU 2310  CA  SER A 382    15483  25327  23304   3834   1322  -3160       C  
ATOM   2311  C   SER A 382      13.700 -28.613  38.819  1.00164.78           C  
ANISOU 2311  C   SER A 382    15135  24777  22695   3774   1048  -3050       C  
ATOM   2312  O   SER A 382      14.150 -28.765  39.955  1.00164.71           O  
ANISOU 2312  O   SER A 382    14968  24872  22740   3937    824  -2995       O  
ATOM   2313  CB  SER A 382      15.228 -27.741  37.037  1.00175.63           C  
ANISOU 2313  CB  SER A 382    16120  26463  24148   3530   1430  -3271       C  
ATOM   2314  OG  SER A 382      16.060 -28.071  35.938  1.00178.96           O  
ANISOU 2314  OG  SER A 382    16380  26950  24665   3593   1695  -3370       O  
ATOM   2315  N   THR A 383      12.486 -28.126  38.582  1.00156.39           N  
ANISOU 2315  N   THR A 383    14381  23562  21478   3545   1066  -3017       N  
ATOM   2316  CA  THR A 383      11.595 -27.722  39.666  1.00153.04           C  
ANISOU 2316  CA  THR A 383    14123  23082  20940   3472    838  -2915       C  
ATOM   2317  C   THR A 383      10.879 -28.932  40.266  1.00151.70           C  
ANISOU 2317  C   THR A 383    14187  22655  20794   3750    741  -2790       C  
ATOM   2318  O   THR A 383      10.554 -28.951  41.454  1.00149.37           O  
ANISOU 2318  O   THR A 383    13939  22353  20459   3831    518  -2691       O  
ATOM   2319  CB  THR A 383      10.555 -26.691  39.181  1.00144.68           C  
ANISOU 2319  CB  THR A 383    13292  21961  19718   3121    901  -2924       C  
ATOM   2320  OG1 THR A 383      11.220 -25.626  38.490  1.00145.74           O  
ANISOU 2320  OG1 THR A 383    13235  22304  19836   2861   1022  -3037       O  
ATOM   2321  CG2 THR A 383       9.773 -26.116  40.355  1.00141.70           C  
ANISOU 2321  CG2 THR A 383    13039  21569  19230   3036    675  -2833       C  
ATOM   2322  N   LEU A 384      10.641 -29.943  39.439  1.00159.10           N  
ANISOU 2322  N   LEU A 384    15280  23376  21794   3895    916  -2798       N  
ATOM   2323  CA  LEU A 384       9.971 -31.158  39.888  1.00158.62           C  
ANISOU 2323  CA  LEU A 384    15455  23039  21774   4153    858  -2690       C  
ATOM   2324  C   LEU A 384      10.904 -32.003  40.749  1.00162.25           C  
ANISOU 2324  C   LEU A 384    15716  23552  22379   4501    721  -2638       C  
ATOM   2325  O   LEU A 384      10.455 -32.736  41.631  1.00160.44           O  
ANISOU 2325  O   LEU A 384    15636  23162  22163   4702    572  -2514       O  
ATOM   2326  CB  LEU A 384       9.474 -31.970  38.689  1.00152.56           C  
ANISOU 2326  CB  LEU A 384    14910  22023  21034   4194   1098  -2737       C  
ATOM   2327  CG  LEU A 384       8.621 -33.205  38.987  1.00151.80           C  
ANISOU 2327  CG  LEU A 384    15104  21594  20979   4412   1076  -2641       C  
ATOM   2328  CD1 LEU A 384       7.372 -32.819  39.763  1.00147.55           C  
ANISOU 2328  CD1 LEU A 384    14799  20947  20316   4275    915  -2522       C  
ATOM   2329  CD2 LEU A 384       8.254 -33.924  37.698  1.00151.86           C  
ANISOU 2329  CD2 LEU A 384    15313  21383  21005   4425   1327  -2726       C  
ATOM   2330  N   ALA A 385      12.203 -31.893  40.488  1.00155.42           N  
ANISOU 2330  N   ALA A 385    14513  22916  21624   4574    772  -2729       N  
ATOM   2331  CA  ALA A 385      13.204 -32.639  41.244  1.00159.33           C  
ANISOU 2331  CA  ALA A 385    14775  23494  22270   4910    640  -2687       C  
ATOM   2332  C   ALA A 385      13.228 -32.222  42.712  1.00158.37           C  
ANISOU 2332  C   ALA A 385    14579  23513  22079   4933    327  -2589       C  
ATOM   2333  O   ALA A 385      13.261 -33.069  43.605  1.00158.31           O  
ANISOU 2333  O   ALA A 385    14615  23413  22121   5219    160  -2473       O  
ATOM   2334  CB  ALA A 385      14.581 -32.466  40.619  1.00157.01           C  
ANISOU 2334  CB  ALA A 385    14105  23443  22109   4950    770  -2813       C  
ATOM   2335  N   CYS A 386      13.208 -30.916  42.958  1.00161.61           N  
ANISOU 2335  N   CYS A 386    14893  24141  22369   4633    250  -2636       N  
ATOM   2336  CA  CYS A 386      13.220 -30.398  44.322  1.00161.82           C  
ANISOU 2336  CA  CYS A 386    14858  24321  22306   4623    -38  -2565       C  
ATOM   2337  C   CYS A 386      11.844 -30.503  44.977  1.00158.18           C  
ANISOU 2337  C   CYS A 386    14766  23637  21697   4593   -144  -2435       C  
ATOM   2338  O   CYS A 386      11.219 -29.494  45.306  1.00153.96           O  
ANISOU 2338  O   CYS A 386    14324  23163  21012   4333   -209  -2438       O  
ATOM   2339  CB  CYS A 386      13.729 -28.953  44.355  1.00160.29           C  
ANISOU 2339  CB  CYS A 386    14428  24429  22044   4307    -70  -2678       C  
ATOM   2340  SG  CYS A 386      12.882 -27.813  43.234  1.00155.55           S  
ANISOU 2340  SG  CYS A 386    14016  23770  21314   3870    153  -2766       S  
ATOM   2341  N   LEU A 387      11.382 -31.735  45.167  1.00131.56           N  
ANISOU 2341  N   LEU A 387    11605  20001  18379   4864   -152  -2321       N  
ATOM   2342  CA  LEU A 387      10.083 -31.987  45.779  1.00128.25           C  
ANISOU 2342  CA  LEU A 387    11537  19349  17842   4865   -236  -2185       C  
ATOM   2343  C   LEU A 387      10.078 -33.349  46.465  1.00130.10           C  
ANISOU 2343  C   LEU A 387    11886  19388  18159   5241   -340  -2042       C  
ATOM   2344  O   LEU A 387      10.703 -34.297  45.989  1.00132.15           O  
ANISOU 2344  O   LEU A 387    12076  19551  18583   5471   -238  -2062       O  
ATOM   2345  CB  LEU A 387       8.972 -31.906  44.725  1.00123.05           C  
ANISOU 2345  CB  LEU A 387    11152  18462  17141   4653    -15  -2215       C  
ATOM   2346  CG  LEU A 387       7.507 -31.923  45.179  1.00119.21           C  
ANISOU 2346  CG  LEU A 387    11016  17746  16531   4579    -64  -2094       C  
ATOM   2347  CD1 LEU A 387       6.950 -33.341  45.278  1.00120.13           C  
ANISOU 2347  CD1 LEU A 387    11375  17534  16735   4845    -33  -1983       C  
ATOM   2348  CD2 LEU A 387       7.324 -31.164  46.490  1.00118.23           C  
ANISOU 2348  CD2 LEU A 387    10880  17778  16264   4530   -306  -2015       C  
TER    2349      LEU A 387                                                      
ATOM   2350  N   PRO B  51     -24.319  23.598  44.619  1.00111.89           N  
ANISOU 2350  N   PRO B  51    19121   8985  14405   -325   3107   -902       N  
ATOM   2351  CA  PRO B  51     -25.396  24.579  44.453  1.00114.15           C  
ANISOU 2351  CA  PRO B  51    19547   9032  14791     36   3128   -679       C  
ATOM   2352  C   PRO B  51     -24.903  25.788  43.671  1.00117.96           C  
ANISOU 2352  C   PRO B  51    20347   9197  15275   -124   3187   -608       C  
ATOM   2353  O   PRO B  51     -25.006  25.837  42.446  1.00118.64           O  
ANISOU 2353  O   PRO B  51    20526   9189  15363   -142   3161   -373       O  
ATOM   2354  CB  PRO B  51     -25.709  25.004  45.895  1.00112.74           C  
ANISOU 2354  CB  PRO B  51    19327   8862  14647    282   3173   -833       C  
ATOM   2355  CG  PRO B  51     -24.924  24.072  46.788  1.00110.26           C  
ANISOU 2355  CG  PRO B  51    18821   8835  14236     89   3150  -1100       C  
ATOM   2356  CD  PRO B  51     -23.759  23.633  45.977  1.00109.70           C  
ANISOU 2356  CD  PRO B  51    18778   8820  14084   -353   3126  -1185       C  
ATOM   2357  N   ASN B  52     -24.373  26.762  44.401  1.00107.58           N  
ANISOU 2357  N   ASN B  52    19201   7723  13952   -242   3265   -809       N  
ATOM   2358  CA  ASN B  52     -23.708  27.912  43.810  1.00111.45           C  
ANISOU 2358  CA  ASN B  52    19990   7918  14439   -458   3334   -793       C  
ATOM   2359  C   ASN B  52     -22.215  27.648  43.736  1.00111.51           C  
ANISOU 2359  C   ASN B  52    19975   8044  14352   -956   3341   -963       C  
ATOM   2360  O   ASN B  52     -21.460  28.428  43.156  1.00113.70           O  
ANISOU 2360  O   ASN B  52    20456   8131  14614  -1216   3398   -951       O  
ATOM   2361  CB  ASN B  52     -23.957  29.143  44.671  1.00113.16           C  
ANISOU 2361  CB  ASN B  52    20399   7899  14700   -343   3415   -938       C  
ATOM   2362  CG  ASN B  52     -23.626  28.900  46.135  1.00111.80           C  
ANISOU 2362  CG  ASN B  52    20144   7882  14455   -542   3424  -1273       C  
ATOM   2363  OD1 ASN B  52     -24.099  27.932  46.735  1.00108.10           O  
ANISOU 2363  OD1 ASN B  52    19414   7728  13934   -551   3360  -1375       O  
ATOM   2364  ND2 ASN B  52     -22.803  29.772  46.713  1.00114.70           N  
ANISOU 2364  ND2 ASN B  52    20737   8031  14814   -703   3493  -1443       N  
ATOM   2365  N   SER B  53     -21.807  26.517  44.306  1.00151.21           N  
ANISOU 2365  N   SER B  53    24732  13401  19321  -1081   3280  -1119       N  
ATOM   2366  CA  SER B  53     -20.395  26.194  44.503  1.00150.95           C  
ANISOU 2366  CA  SER B  53    24603  13546  19206  -1533   3268  -1333       C  
ATOM   2367  C   SER B  53     -19.596  25.997  43.213  1.00150.57           C  
ANISOU 2367  C   SER B  53    24526  13562  19121  -1813   3268  -1195       C  
ATOM   2368  O   SER B  53     -20.103  26.208  42.111  1.00153.53           O  
ANISOU 2368  O   SER B  53    25062  13754  19519  -1719   3296   -935       O  
ATOM   2369  CB  SER B  53     -20.251  24.966  45.409  1.00147.05           C  
ANISOU 2369  CB  SER B  53    23812  13402  18656  -1542   3187  -1545       C  
ATOM   2370  OG  SER B  53     -20.850  25.201  46.671  1.00148.58           O  
ANISOU 2370  OG  SER B  53    24031  13562  18858  -1299   3195  -1676       O  
ATOM   2371  N   ASP B  54     -18.350  25.557  43.368  1.00167.96           N  
ANISOU 2371  N   ASP B  54    26508  16052  21258  -2149   3229  -1368       N  
ATOM   2372  CA  ASP B  54     -17.405  25.440  42.260  1.00167.36           C  
ANISOU 2372  CA  ASP B  54    26370  16083  21137  -2470   3247  -1285       C  
ATOM   2373  C   ASP B  54     -17.855  24.461  41.175  1.00163.79           C  
ANISOU 2373  C   ASP B  54    25758  15810  20667  -2341   3194  -1082       C  
ATOM   2374  O   ASP B  54     -17.239  24.385  40.115  1.00163.54           O  
ANISOU 2374  O   ASP B  54    25622  15937  20580  -2593   3202  -1023       O  
ATOM   2375  CB  ASP B  54     -16.038  25.007  42.789  1.00168.85           C  
ANISOU 2375  CB  ASP B  54    26342  16537  21275  -2872   3221  -1563       C  
ATOM   2376  CG  ASP B  54     -15.566  25.854  43.950  1.00172.04           C  
ANISOU 2376  CG  ASP B  54    26857  16821  21689  -2974   3235  -1800       C  
ATOM   2377  OD1 ASP B  54     -16.409  26.507  44.602  1.00176.21           O  
ANISOU 2377  OD1 ASP B  54    27690  17002  22260  -2896   3315  -1734       O  
ATOM   2378  OD2 ASP B  54     -14.346  25.861  44.210  1.00171.35           O  
ANISOU 2378  OD2 ASP B  54    26552  16992  21562  -3125   3157  -2050       O  
ATOM   2379  N   LEU B  55     -18.924  23.717  41.446  1.00 74.48           N  
ANISOU 2379  N   LEU B  55    14416   4482   9400  -1946   3143   -975       N  
ATOM   2380  CA  LEU B  55     -19.432  22.699  40.529  1.00 71.16           C  
ANISOU 2380  CA  LEU B  55    13810   4266   8961  -1780   3061   -770       C  
ATOM   2381  C   LEU B  55     -19.740  23.233  39.134  1.00 73.05           C  
ANISOU 2381  C   LEU B  55    14266   4307   9183  -1754   3095   -454       C  
ATOM   2382  O   LEU B  55     -19.506  22.547  38.141  1.00 70.63           O  
ANISOU 2382  O   LEU B  55    13770   4266   8799  -1784   3019   -307       O  
ATOM   2383  CB  LEU B  55     -20.683  22.034  41.111  1.00 68.23           C  
ANISOU 2383  CB  LEU B  55    13260   4024   8638  -1330   2963   -724       C  
ATOM   2384  CG  LEU B  55     -20.549  20.934  42.172  1.00 64.11           C  
ANISOU 2384  CG  LEU B  55    12355   3925   8080  -1306   2857   -921       C  
ATOM   2385  CD1 LEU B  55     -19.769  21.389  43.392  1.00 65.79           C  
ANISOU 2385  CD1 LEU B  55    12594   4140   8260  -1594   2906  -1251       C  
ATOM   2386  CD2 LEU B  55     -21.931  20.435  42.578  1.00 62.33           C  
ANISOU 2386  CD2 LEU B  55    12012   3754   7916   -866   2803   -854       C  
ATOM   2387  N   ASP B  56     -20.252  24.459  39.067  1.00 99.74           N  
ANISOU 2387  N   ASP B  56    17938   7361  12599  -1650   3152   -347       N  
ATOM   2388  CA  ASP B  56     -20.604  25.084  37.793  1.00101.70           C  
ANISOU 2388  CA  ASP B  56    18387   7445  12809  -1594   3158    -43       C  
ATOM   2389  C   ASP B  56     -19.395  25.250  36.875  1.00102.88           C  
ANISOU 2389  C   ASP B  56    18542   7696  12852  -2014   3218    -35       C  
ATOM   2390  O   ASP B  56     -18.417  25.911  37.224  1.00102.74           O  
ANISOU 2390  O   ASP B  56    18525   7686  12825  -2350   3296   -248       O  
ATOM   2391  CB  ASP B  56     -21.292  26.436  38.018  1.00108.85           C  
ANISOU 2391  CB  ASP B  56    19592   7982  13785  -1389   3204     45       C  
ATOM   2392  CG  ASP B  56     -20.682  27.223  39.163  1.00111.20           C  
ANISOU 2392  CG  ASP B  56    19984   8144  14122  -1575   3294   -235       C  
ATOM   2393  OD1 ASP B  56     -19.497  26.992  39.483  1.00111.03           O  
ANISOU 2393  OD1 ASP B  56    19847   8287  14052  -1951   3328   -455       O  
ATOM   2394  OD2 ASP B  56     -21.391  28.071  39.747  1.00113.92           O  
ANISOU 2394  OD2 ASP B  56    20506   8233  14544  -1341   3323   -236       O  
ATOM   2395  N   VAL B  57     -19.470  24.636  35.700  1.00 87.82           N  
ANISOU 2395  N   VAL B  57    16621   5890  10857  -1988   3175    210       N  
ATOM   2396  CA  VAL B  57     -18.389  24.704  34.727  1.00 89.29           C  
ANISOU 2396  CA  VAL B  57    16797   6202  10925  -2352   3241    239       C  
ATOM   2397  C   VAL B  57     -18.775  25.629  33.573  1.00 92.74           C  
ANISOU 2397  C   VAL B  57    17524   6413  11297  -2265   3257    536       C  
ATOM   2398  O   VAL B  57     -19.938  25.688  33.173  1.00 92.41           O  
ANISOU 2398  O   VAL B  57    17595   6243  11271  -1899   3166    769       O  
ATOM   2399  CB  VAL B  57     -18.014  23.297  34.210  1.00 86.77           C  
ANISOU 2399  CB  VAL B  57    16175   6273  10521  -2462   3188    231       C  
ATOM   2400  CG1 VAL B  57     -19.210  22.632  33.560  1.00 85.66           C  
ANISOU 2400  CG1 VAL B  57    16023   6178  10344  -2111   3066    498       C  
ATOM   2401  CG2 VAL B  57     -16.833  23.362  33.246  1.00 87.77           C  
ANISOU 2401  CG2 VAL B  57    16256   6564  10527  -2837   3275    229       C  
ATOM   2402  N   ASN B  58     -17.795  26.361  33.054  1.00113.37           N  
ANISOU 2402  N   ASN B  58    20247   8984  13843  -2594   3369    526       N  
ATOM   2403  CA  ASN B  58     -18.045  27.375  32.039  1.00117.14           C  
ANISOU 2403  CA  ASN B  58    21036   9207  14264  -2546   3405    782       C  
ATOM   2404  C   ASN B  58     -18.171  26.817  30.626  1.00116.26           C  
ANISOU 2404  C   ASN B  58    20919   9262  13991  -2509   3349   1045       C  
ATOM   2405  O   ASN B  58     -17.222  26.254  30.080  1.00114.87           O  
ANISOU 2405  O   ASN B  58    20584   9353  13708  -2790   3400    990       O  
ATOM   2406  CB  ASN B  58     -16.945  28.436  32.079  1.00119.36           C  
ANISOU 2406  CB  ASN B  58    21467   9331  14553  -2912   3564    659       C  
ATOM   2407  CG  ASN B  58     -16.643  28.904  33.486  1.00119.83           C  
ANISOU 2407  CG  ASN B  58    21509   9276  14745  -3002   3610    366       C  
ATOM   2408  OD1 ASN B  58     -15.517  28.775  33.966  1.00119.63           O  
ANISOU 2408  OD1 ASN B  58    21313   9416  14726  -3343   3674    116       O  
ATOM   2409  ND2 ASN B  58     -17.651  29.447  34.159  1.00120.64           N  
ANISOU 2409  ND2 ASN B  58    21772   9115  14949  -2685   3570    392       N  
ATOM   2410  N   THR B  59     -19.353  26.977  30.043  1.00106.99           N  
ANISOU 2410  N   THR B  59    19907   7946  12798  -2147   3237   1324       N  
ATOM   2411  CA  THR B  59     -19.567  26.642  28.644  1.00107.79           C  
ANISOU 2411  CA  THR B  59    20066   8163  12727  -2089   3168   1598       C  
ATOM   2412  C   THR B  59     -19.876  27.911  27.868  1.00112.36           C  
ANISOU 2412  C   THR B  59    21003   8415  13276  -2023   3202   1826       C  
ATOM   2413  O   THR B  59     -20.886  28.569  28.123  1.00113.32           O  
ANISOU 2413  O   THR B  59    21286   8274  13498  -1702   3132   1943       O  
ATOM   2414  CB  THR B  59     -20.733  25.654  28.458  1.00101.67           C  
ANISOU 2414  CB  THR B  59    19163   7538  11929  -1707   2968   1767       C  
ATOM   2415  OG1 THR B  59     -21.940  26.232  28.970  1.00102.21           O  
ANISOU 2415  OG1 THR B  59    19347   7348  12140  -1318   2879   1862       O  
ATOM   2416  CG2 THR B  59     -20.449  24.349  29.182  1.00 97.33           C  
ANISOU 2416  CG2 THR B  59    18270   7307  11405  -1766   2936   1562       C  
ATOM   2417  N   ASP B  60     -18.994  28.262  26.938  1.00118.74           N  
ANISOU 2417  N   ASP B  60    21925   9239  13951  -2321   3317   1883       N  
ATOM   2418  CA  ASP B  60     -19.232  29.391  26.053  1.00122.67           C  
ANISOU 2418  CA  ASP B  60    22769   9451  14391  -2269   3347   2133       C  
ATOM   2419  C   ASP B  60     -20.547  29.150  25.328  1.00122.09           C  
ANISOU 2419  C   ASP B  60    22755   9387  14246  -1850   3139   2436       C  
ATOM   2420  O   ASP B  60     -20.744  28.089  24.737  1.00119.92           O  
ANISOU 2420  O   ASP B  60    22314   9415  13834  -1800   3031   2516       O  
ATOM   2421  CB  ASP B  60     -18.084  29.536  25.052  1.00123.81           C  
ANISOU 2421  CB  ASP B  60    22978   9690  14373  -2645   3495   2163       C  
ATOM   2422  CG  ASP B  60     -18.246  30.741  24.146  1.00129.13           C  
ANISOU 2422  CG  ASP B  60    24028  10060  14976  -2610   3541   2431       C  
ATOM   2423  OD1 ASP B  60     -18.914  31.713  24.557  1.00131.35           O  
ANISOU 2423  OD1 ASP B  60    24532   9997  15379  -2396   3517   2512       O  
ATOM   2424  OD2 ASP B  60     -17.701  30.716  23.022  1.00130.45           O  
ANISOU 2424  OD2 ASP B  60    24270  10331  14964  -2793   3607   2559       O  
ATOM   2425  N   ILE B  61     -21.451  30.124  25.403  1.00107.07           N  
ANISOU 2425  N   ILE B  61    21073   7164  12442  -1546   3076   2593       N  
ATOM   2426  CA  ILE B  61     -22.788  30.002  24.820  1.00107.43           C  
ANISOU 2426  CA  ILE B  61    21151   7209  12458  -1109   2854   2874       C  
ATOM   2427  C   ILE B  61     -22.707  29.576  23.355  1.00108.32           C  
ANISOU 2427  C   ILE B  61    21310   7526  12321  -1149   2775   3112       C  
ATOM   2428  O   ILE B  61     -23.531  28.793  22.876  1.00106.68           O  
ANISOU 2428  O   ILE B  61    20974   7526  12035   -888   2570   3262       O  
ATOM   2429  CB  ILE B  61     -23.597  31.317  24.961  1.00111.65           C  
ANISOU 2429  CB  ILE B  61    21956   7341  13122   -825   2828   3027       C  
ATOM   2430  CG1 ILE B  61     -23.879  31.625  26.435  1.00110.61           C  
ANISOU 2430  CG1 ILE B  61    21751   7045  13229   -703   2873   2795       C  
ATOM   2431  CG2 ILE B  61     -24.910  31.232  24.200  1.00112.75           C  
ANISOU 2431  CG2 ILE B  61    22120   7506  13215   -397   2587   3341       C  
ATOM   2432  CD1 ILE B  61     -22.809  32.451  27.123  1.00112.33           C  
ANISOU 2432  CD1 ILE B  61    22103   7052  13524  -1055   3102   2553       C  
ATOM   2433  N   TYR B  62     -21.689  30.080  22.665  1.00139.75           N  
ANISOU 2433  N   TYR B  62    25466  11459  16176  -1487   2942   3134       N  
ATOM   2434  CA  TYR B  62     -21.376  29.656  21.307  1.00140.63           C  
ANISOU 2434  CA  TYR B  62    25618  11786  16029  -1599   2917   3311       C  
ATOM   2435  C   TYR B  62     -21.212  28.139  21.256  1.00135.83           C  
ANISOU 2435  C   TYR B  62    24678  11609  15325  -1648   2837   3193       C  
ATOM   2436  O   TYR B  62     -21.850  27.461  20.449  1.00135.11           O  
ANISOU 2436  O   TYR B  62    24538  11721  15079  -1451   2654   3373       O  
ATOM   2437  CB  TYR B  62     -20.082  30.328  20.844  1.00146.66           C  
ANISOU 2437  CB  TYR B  62    26550  12466  16711  -2023   3165   3260       C  
ATOM   2438  CG  TYR B  62     -19.847  30.276  19.353  1.00151.09           C  
ANISOU 2438  CG  TYR B  62    27262  13141  17006  -2105   3167   3496       C  
ATOM   2439  CD1 TYR B  62     -20.890  30.023  18.472  1.00152.98           C  
ANISOU 2439  CD1 TYR B  62    27595  13428  17105  -1771   2946   3791       C  
ATOM   2440  CD2 TYR B  62     -18.578  30.478  18.826  1.00153.40           C  
ANISOU 2440  CD2 TYR B  62    27594  13508  17185  -2513   3388   3419       C  
ATOM   2441  CE1 TYR B  62     -20.677  29.976  17.108  1.00155.98           C  
ANISOU 2441  CE1 TYR B  62    28127  13920  17220  -1845   2945   4003       C  
ATOM   2442  CE2 TYR B  62     -18.355  30.432  17.464  1.00156.25           C  
ANISOU 2442  CE2 TYR B  62    28101  13976  17292  -2586   3407   3630       C  
ATOM   2443  CZ  TYR B  62     -19.407  30.181  16.610  1.00157.76           C  
ANISOU 2443  CZ  TYR B  62    28406  14208  17329  -2252   3185   3921       C  
ATOM   2444  OH  TYR B  62     -19.189  30.134  15.252  1.00161.22           O  
ANISOU 2444  OH  TYR B  62    29003  14761  17495  -2324   3200   4127       O  
ATOM   2445  N   SER B  63     -20.362  27.616  22.136  1.00112.55           N  
ANISOU 2445  N   SER B  63    21498   8798  12467  -1909   2967   2885       N  
ATOM   2446  CA  SER B  63     -20.085  26.183  22.194  1.00107.48           C  
ANISOU 2446  CA  SER B  63    20530   8555  11752  -1986   2917   2742       C  
ATOM   2447  C   SER B  63     -21.327  25.374  22.551  1.00103.77           C  
ANISOU 2447  C   SER B  63    19898   8195  11336  -1600   2680   2807       C  
ATOM   2448  O   SER B  63     -21.606  24.351  21.928  1.00102.17           O  
ANISOU 2448  O   SER B  63    19561   8281  10979  -1519   2546   2885       O  
ATOM   2449  CB  SER B  63     -18.969  25.893  23.200  1.00103.97           C  
ANISOU 2449  CB  SER B  63    19864   8208  11431  -2316   3092   2394       C  
ATOM   2450  OG  SER B  63     -17.785  26.599  22.871  1.00107.04           O  
ANISOU 2450  OG  SER B  63    20369   8519  11784  -2681   3305   2322       O  
ATOM   2451  N   LYS B  64     -22.067  25.835  23.556  1.00 94.87           N  
ANISOU 2451  N   LYS B  64    18779   6841  10427  -1362   2633   2767       N  
ATOM   2452  CA  LYS B  64     -23.275  25.145  23.997  1.00 92.28           C  
ANISOU 2452  CA  LYS B  64    18280   6599  10185   -978   2421   2822       C  
ATOM   2453  C   LYS B  64     -24.298  25.035  22.873  1.00 93.93           C  
ANISOU 2453  C   LYS B  64    18571   6870  10248   -674   2192   3140       C  
ATOM   2454  O   LYS B  64     -24.787  23.946  22.576  1.00 91.42           O  
ANISOU 2454  O   LYS B  64    18060   6831   9843   -536   2021   3187       O  
ATOM   2455  CB  LYS B  64     -23.905  25.856  25.197  1.00 92.69           C  
ANISOU 2455  CB  LYS B  64    18359   6365  10494   -751   2429   2742       C  
ATOM   2456  CG  LYS B  64     -25.215  25.231  25.656  1.00 90.48           C  
ANISOU 2456  CG  LYS B  64    17885   6169  10326   -329   2219   2805       C  
ATOM   2457  CD  LYS B  64     -25.949  26.121  26.647  1.00 92.06           C  
ANISOU 2457  CD  LYS B  64    18150   6065  10762    -50   2224   2777       C  
ATOM   2458  CE  LYS B  64     -25.145  26.323  27.919  1.00 90.98           C  
ANISOU 2458  CE  LYS B  64    17988   5812  10768   -282   2429   2461       C  
ATOM   2459  NZ  LYS B  64     -25.871  27.178  28.899  1.00 92.77           N  
ANISOU 2459  NZ  LYS B  64    18291   5750  11208     -9   2444   2418       N  
ATOM   2460  N   VAL B  65     -24.612  26.167  22.250  1.00 98.38           N  
ANISOU 2460  N   VAL B  65    19422   7177  10783   -576   2181   3355       N  
ATOM   2461  CA  VAL B  65     -25.590  26.203  21.166  1.00100.65           C  
ANISOU 2461  CA  VAL B  65    19802   7505  10936   -280   1949   3668       C  
ATOM   2462  C   VAL B  65     -25.131  25.382  19.961  1.00100.25           C  
ANISOU 2462  C   VAL B  65    19730   7773  10587   -454   1902   3749       C  
ATOM   2463  O   VAL B  65     -25.913  24.622  19.386  1.00 99.42           O  
ANISOU 2463  O   VAL B  65    19513   7894  10367   -232   1665   3887       O  
ATOM   2464  CB  VAL B  65     -25.897  27.652  20.730  1.00105.96           C  
ANISOU 2464  CB  VAL B  65    20807   7821  11634   -165   1968   3882       C  
ATOM   2465  CG1 VAL B  65     -26.794  27.664  19.502  1.00108.63           C  
ANISOU 2465  CG1 VAL B  65    21236   8235  11803    107   1721   4209       C  
ATOM   2466  CG2 VAL B  65     -26.545  28.421  21.872  1.00106.65           C  
ANISOU 2466  CG2 VAL B  65    20908   7605  12010     71   1984   3813       C  
ATOM   2467  N   LEU B  66     -23.861  25.531  19.591  1.00101.04           N  
ANISOU 2467  N   LEU B  66    19923   7902  10566   -852   2127   3651       N  
ATOM   2468  CA  LEU B  66     -23.298  24.780  18.471  1.00100.92           C  
ANISOU 2468  CA  LEU B  66    19888   8191  10267  -1045   2127   3694       C  
ATOM   2469  C   LEU B  66     -23.399  23.273  18.692  1.00 96.24           C  
ANISOU 2469  C   LEU B  66    18972   7971   9625  -1030   2017   3550       C  
ATOM   2470  O   LEU B  66     -23.994  22.558  17.884  1.00 95.99           O  
ANISOU 2470  O   LEU B  66    18893   8169   9408   -875   1812   3688       O  
ATOM   2471  CB  LEU B  66     -21.838  25.173  18.235  1.00102.38           C  
ANISOU 2471  CB  LEU B  66    20167   8349  10383  -1485   2421   3560       C  
ATOM   2472  CG  LEU B  66     -21.064  24.334  17.215  1.00101.95           C  
ANISOU 2472  CG  LEU B  66    20040   8634  10061  -1726   2477   3533       C  
ATOM   2473  CD1 LEU B  66     -21.707  24.422  15.839  1.00105.04           C  
ANISOU 2473  CD1 LEU B  66    20632   9084  10195  -1546   2307   3838       C  
ATOM   2474  CD2 LEU B  66     -19.606  24.764  17.158  1.00103.48           C  
ANISOU 2474  CD2 LEU B  66    20279   8794  10246  -2151   2782   3373       C  
ATOM   2475  N   VAL B  67     -22.819  22.803  19.792  1.00 92.78           N  
ANISOU 2475  N   VAL B  67    18315   7589   9348  -1195   2149   3269       N  
ATOM   2476  CA  VAL B  67     -22.819  21.381  20.122  1.00 88.38           C  
ANISOU 2476  CA  VAL B  67    17449   7367   8763  -1209   2076   3111       C  
ATOM   2477  C   VAL B  67     -24.241  20.836  20.276  1.00 86.90           C  
ANISOU 2477  C   VAL B  67    17151   7241   8625   -796   1786   3242       C  
ATOM   2478  O   VAL B  67     -24.525  19.707  19.875  1.00 84.82           O  
ANISOU 2478  O   VAL B  67    16725   7280   8223   -739   1636   3245       O  
ATOM   2479  CB  VAL B  67     -21.988  21.100  21.396  1.00 85.35           C  
ANISOU 2479  CB  VAL B  67    16857   7002   8571  -1444   2268   2792       C  
ATOM   2480  CG1 VAL B  67     -22.118  19.646  21.823  1.00 80.95           C  
ANISOU 2480  CG1 VAL B  67    15984   6770   8003  -1423   2184   2644       C  
ATOM   2481  CG2 VAL B  67     -20.528  21.454  21.159  1.00 86.84           C  
ANISOU 2481  CG2 VAL B  67    17089   7205   8703  -1863   2528   2645       C  
ATOM   2482  N   THR B  68     -25.133  21.646  20.838  1.00 88.25           N  
ANISOU 2482  N   THR B  68    17401   7134   8997   -505   1706   3344       N  
ATOM   2483  CA  THR B  68     -26.533  21.254  20.977  1.00 87.49           C  
ANISOU 2483  CA  THR B  68    17175   7089   8980    -85   1427   3478       C  
ATOM   2484  C   THR B  68     -27.177  21.045  19.610  1.00 89.76           C  
ANISOU 2484  C   THR B  68    17541   7538   9025     74   1184   3736       C  
ATOM   2485  O   THR B  68     -27.843  20.037  19.379  1.00 87.98           O  
ANISOU 2485  O   THR B  68    17126   7574   8728    243    958   3770       O  
ATOM   2486  CB  THR B  68     -27.347  22.297  21.765  1.00 89.25           C  
ANISOU 2486  CB  THR B  68    17462   6978   9472    209   1404   3537       C  
ATOM   2487  OG1 THR B  68     -26.764  22.483  23.061  1.00 87.30           O  
ANISOU 2487  OG1 THR B  68    17147   6589   9434     62   1620   3279       O  
ATOM   2488  CG2 THR B  68     -28.791  21.842  21.924  1.00 88.58           C  
ANISOU 2488  CG2 THR B  68    17177   6986   9493    648   1118   3658       C  
ATOM   2489  N   ALA B  69     -26.968  22.001  18.709  1.00 93.89           N  
ANISOU 2489  N   ALA B  69    18347   7909   9419     13   1227   3912       N  
ATOM   2490  CA  ALA B  69     -27.500  21.914  17.353  1.00 96.65           C  
ANISOU 2490  CA  ALA B  69    18805   8401   9517    142   1010   4161       C  
ATOM   2491  C   ALA B  69     -26.956  20.687  16.626  1.00 94.64           C  
ANISOU 2491  C   ALA B  69    18442   8528   8990    -68    984   4075       C  
ATOM   2492  O   ALA B  69     -27.694  19.989  15.925  1.00 94.74           O  
ANISOU 2492  O   ALA B  69    18373   8780   8846    110    716   4187       O  
ATOM   2493  CB  ALA B  69     -27.176  23.179  16.575  1.00101.55           C  
ANISOU 2493  CB  ALA B  69    19769   8773  10041     65   1115   4348       C  
ATOM   2494  N   ILE B  70     -25.662  20.434  16.800  1.00 93.04           N  
ANISOU 2494  N   ILE B  70    18222   8390   8741   -447   1258   3860       N  
ATOM   2495  CA  ILE B  70     -25.027  19.250  16.233  1.00 91.02           C  
ANISOU 2495  CA  ILE B  70    17834   8494   8255   -666   1278   3728       C  
ATOM   2496  C   ILE B  70     -25.696  17.987  16.765  1.00 87.08           C  
ANISOU 2496  C   ILE B  70    17042   8238   7807   -501   1077   3625       C  
ATOM   2497  O   ILE B  70     -25.967  17.050  16.012  1.00 86.57           O  
ANISOU 2497  O   ILE B  70    16899   8468   7527   -468    900   3644       O  
ATOM   2498  CB  ILE B  70     -23.520  19.208  16.557  1.00 89.83           C  
ANISOU 2498  CB  ILE B  70    17642   8368   8123  -1083   1619   3478       C  
ATOM   2499  CG1 ILE B  70     -22.797  20.379  15.890  1.00 94.07           C  
ANISOU 2499  CG1 ILE B  70    18466   8698   8579  -1274   1817   3581       C  
ATOM   2500  CG2 ILE B  70     -22.908  17.891  16.106  1.00 87.46           C  
ANISOU 2500  CG2 ILE B  70    17147   8455   7628  -1276   1642   3307       C  
ATOM   2501  CD1 ILE B  70     -21.313  20.426  16.180  1.00 93.48           C  
ANISOU 2501  CD1 ILE B  70    18327   8652   8540  -1681   2140   3338       C  
ATOM   2502  N   TYR B  71     -25.977  17.978  18.064  1.00115.03           N  
ANISOU 2502  N   TYR B  71    20427  11649  11631   -394   1104   3512       N  
ATOM   2503  CA  TYR B  71     -26.617  16.833  18.701  1.00112.51           C  
ANISOU 2503  CA  TYR B  71    19733  11576  11440   -226    917   3367       C  
ATOM   2504  C   TYR B  71     -28.041  16.637  18.198  1.00113.63           C  
ANISOU 2504  C   TYR B  71    19821  11800  11554    154    554   3578       C  
ATOM   2505  O   TYR B  71     -28.530  15.513  18.141  1.00113.27           O  
ANISOU 2505  O   TYR B  71    19445  12076  11518    240    346   3467       O  
ATOM   2506  CB  TYR B  71     -26.615  16.970  20.226  1.00107.88           C  
ANISOU 2506  CB  TYR B  71    18902  10871  11217   -181   1024   3154       C  
ATOM   2507  CG  TYR B  71     -25.279  16.684  20.875  1.00106.40           C  
ANISOU 2507  CG  TYR B  71    18589  10754  11086   -542   1303   2859       C  
ATOM   2508  CD1 TYR B  71     -24.118  16.606  20.118  1.00106.84           C  
ANISOU 2508  CD1 TYR B  71    18809  10881  10906   -890   1499   2829       C  
ATOM   2509  CD2 TYR B  71     -25.183  16.476  22.243  1.00105.09           C  
ANISOU 2509  CD2 TYR B  71    18128  10599  11204   -531   1367   2610       C  
ATOM   2510  CE1 TYR B  71     -22.900  16.345  20.707  1.00105.59           C  
ANISOU 2510  CE1 TYR B  71    18501  10805  10814  -1210   1741   2559       C  
ATOM   2511  CE2 TYR B  71     -23.967  16.208  22.841  1.00104.31           C  
ANISOU 2511  CE2 TYR B  71    17900  10581  11152   -848   1592   2344       C  
ATOM   2512  CZ  TYR B  71     -22.829  16.145  22.067  1.00104.44           C  
ANISOU 2512  CZ  TYR B  71    18058  10672  10952  -1184   1774   2318       C  
ATOM   2513  OH  TYR B  71     -21.614  15.882  22.656  1.00103.15           O  
ANISOU 2513  OH  TYR B  71    17735  10607  10851  -1492   1989   2052       O  
ATOM   2514  N   LEU B  72     -28.702  17.733  17.840  1.00 85.88           N  
ANISOU 2514  N   LEU B  72    16583   8011   8035    376    472   3858       N  
ATOM   2515  CA  LEU B  72     -30.053  17.661  17.295  1.00 87.79           C  
ANISOU 2515  CA  LEU B  72    16757   8339   8260    743    114   4070       C  
ATOM   2516  C   LEU B  72     -30.028  17.102  15.877  1.00 89.50           C  
ANISOU 2516  C   LEU B  72    17048   8835   8121    664    -59   4166       C  
ATOM   2517  O   LEU B  72     -30.880  16.293  15.501  1.00 89.24           O  
ANISOU 2517  O   LEU B  72    16842   9049   8018    853   -369   4212       O  
ATOM   2518  CB  LEU B  72     -30.722  19.038  17.311  1.00 91.60           C  
ANISOU 2518  CB  LEU B  72    17394   8504   8905    991     78   4279       C  
ATOM   2519  CG  LEU B  72     -30.952  19.675  18.684  1.00 90.59           C  
ANISOU 2519  CG  LEU B  72    17193   8089   9138   1128    218   4189       C  
ATOM   2520  CD1 LEU B  72     -31.714  20.986  18.550  1.00 94.88           C  
ANISOU 2520  CD1 LEU B  72    17887   8347   9817   1398    146   4405       C  
ATOM   2521  CD2 LEU B  72     -31.680  18.715  19.615  1.00 87.04           C  
ANISOU 2521  CD2 LEU B  72    16388   7796   8889   1337     88   4063       C  
ATOM   2522  N   ALA B  73     -29.044  17.538  15.095  1.00 91.46           N  
ANISOU 2522  N   ALA B  73    17545   9051   8154    381    145   4183       N  
ATOM   2523  CA  ALA B  73     -28.872  17.043  13.733  1.00 93.30           C  
ANISOU 2523  CA  ALA B  73    17873   9545   8031    274     37   4248       C  
ATOM   2524  C   ALA B  73     -28.572  15.547  13.737  1.00 89.71           C  
ANISOU 2524  C   ALA B  73    17197   9440   7450    130    -12   4023       C  
ATOM   2525  O   ALA B  73     -29.186  14.776  12.997  1.00 90.20           O  
ANISOU 2525  O   ALA B  73    17176   9765   7329    236   -291   4061       O  
ATOM   2526  CB  ALA B  73     -27.762  17.807  13.028  1.00 95.99           C  
ANISOU 2526  CB  ALA B  73    18501   9770   8200    -15    322   4281       C  
ATOM   2527  N   LEU B  74     -27.628  15.143  14.580  1.00 86.32           N  
ANISOU 2527  N   LEU B  74    16662   9012   7124   -116    256   3779       N  
ATOM   2528  CA  LEU B  74     -27.285  13.734  14.724  1.00 82.23           C  
ANISOU 2528  CA  LEU B  74    15840   8834   6571   -258    237   3506       C  
ATOM   2529  C   LEU B  74     -28.459  12.951  15.305  1.00 78.86           C  
ANISOU 2529  C   LEU B  74    15002   8576   6385     23    -72   3423       C  
ATOM   2530  O   LEU B  74     -28.604  11.754  15.054  1.00 76.53           O  
ANISOU 2530  O   LEU B  74    14459   8594   6027     -5   -221   3263       O  
ATOM   2531  CB  LEU B  74     -26.045  13.574  15.605  1.00 78.90           C  
ANISOU 2531  CB  LEU B  74    15269   8397   6313   -553    583   3223       C  
ATOM   2532  CG  LEU B  74     -24.756  14.178  15.044  1.00 81.97           C  
ANISOU 2532  CG  LEU B  74    15972   8683   6488   -888    914   3244       C  
ATOM   2533  CD1 LEU B  74     -23.661  14.193  16.099  1.00 79.28           C  
ANISOU 2533  CD1 LEU B  74    15473   8283   6365  -1144   1229   2988       C  
ATOM   2534  CD2 LEU B  74     -24.302  13.416  13.807  1.00 82.97           C  
ANISOU 2534  CD2 LEU B  74    16117   9117   6290  -1038    896   3188       C  
ATOM   2535  N   PHE B  75     -29.297  13.637  16.077  1.00 83.47           N  
ANISOU 2535  N   PHE B  75    15522   8942   7250    291   -153   3529       N  
ATOM   2536  CA  PHE B  75     -30.489  13.024  16.650  1.00 83.55           C  
ANISOU 2536  CA  PHE B  75    15147   9089   7509    573   -430   3482       C  
ATOM   2537  C   PHE B  75     -31.496  12.679  15.564  1.00 84.90           C  
ANISOU 2537  C   PHE B  75    15341   9443   7472    769   -804   3670       C  
ATOM   2538  O   PHE B  75     -31.975  11.552  15.500  1.00 84.89           O  
ANISOU 2538  O   PHE B  75    15022   9732   7498    803  -1013   3533       O  
ATOM   2539  CB  PHE B  75     -31.138  13.943  17.689  1.00 83.29           C  
ANISOU 2539  CB  PHE B  75    15071   8765   7810    826   -402   3566       C  
ATOM   2540  CG  PHE B  75     -32.428  13.412  18.249  1.00 83.91           C  
ANISOU 2540  CG  PHE B  75    14757   8974   8150   1132   -669   3546       C  
ATOM   2541  CD1 PHE B  75     -32.424  12.502  19.292  1.00 83.41           C  
ANISOU 2541  CD1 PHE B  75    14284   9067   8342   1092   -618   3271       C  
ATOM   2542  CD2 PHE B  75     -33.646  13.830  17.738  1.00 85.44           C  
ANISOU 2542  CD2 PHE B  75    14987   9136   8339   1462   -966   3809       C  
ATOM   2543  CE1 PHE B  75     -33.610  12.014  19.810  1.00 83.55           C  
ANISOU 2543  CE1 PHE B  75    13936   9202   8605   1355   -838   3256       C  
ATOM   2544  CE2 PHE B  75     -34.834  13.345  18.251  1.00 85.51           C  
ANISOU 2544  CE2 PHE B  75    14604   9279   8608   1732  -1199   3786       C  
ATOM   2545  CZ  PHE B  75     -34.815  12.436  19.289  1.00 84.06           C  
ANISOU 2545  CZ  PHE B  75    14016   9246   8678   1668  -1123   3509       C  
ATOM   2546  N   VAL B  76     -31.821  13.648  14.713  1.00 85.20           N  
ANISOU 2546  N   VAL B  76    15762   9307   7302    896   -895   3985       N  
ATOM   2547  CA  VAL B  76     -32.805  13.412  13.659  1.00 88.84           C  
ANISOU 2547  CA  VAL B  76    16263   9942   7550   1102  -1281   4185       C  
ATOM   2548  C   VAL B  76     -32.279  12.471  12.571  1.00 89.15           C  
ANISOU 2548  C   VAL B  76    16377  10287   7210    863  -1343   4089       C  
ATOM   2549  O   VAL B  76     -32.977  11.541  12.160  1.00 88.86           O  
ANISOU 2549  O   VAL B  76    16113  10535   7114    943  -1647   4030       O  
ATOM   2550  CB  VAL B  76     -33.345  14.730  13.044  1.00 93.96           C  
ANISOU 2550  CB  VAL B  76    17153  10373   8172   1307  -1357   4497       C  
ATOM   2551  CG1 VAL B  76     -34.240  15.451  14.040  1.00 94.16           C  
ANISOU 2551  CG1 VAL B  76    17027  10165   8587   1629  -1408   4588       C  
ATOM   2552  CG2 VAL B  76     -32.208  15.634  12.593  1.00 95.80           C  
ANISOU 2552  CG2 VAL B  76    17752  10403   8245   1052  -1024   4549       C  
ATOM   2553  N   VAL B  77     -31.047  12.701  12.123  1.00 89.62           N  
ANISOU 2553  N   VAL B  77    16707  10298   7046    559  -1036   4042       N  
ATOM   2554  CA  VAL B  77     -30.439  11.857  11.097  1.00 90.00           C  
ANISOU 2554  CA  VAL B  77    16815  10630   6750    323  -1029   3920       C  
ATOM   2555  C   VAL B  77     -30.262  10.428  11.605  1.00 85.17           C  
ANISOU 2555  C   VAL B  77    15844  10287   6233    203  -1053   3594       C  
ATOM   2556  O   VAL B  77     -30.521   9.462  10.884  1.00 85.55           O  
ANISOU 2556  O   VAL B  77    15810  10615   6079    175  -1265   3507       O  
ATOM   2557  CB  VAL B  77     -29.080  12.422  10.628  1.00 91.16           C  
ANISOU 2557  CB  VAL B  77    17229  10678   6731     17   -637   3890       C  
ATOM   2558  CG1 VAL B  77     -28.390  11.451   9.681  1.00 91.26           C  
ANISOU 2558  CG1 VAL B  77    17259  10993   6423   -219   -589   3718       C  
ATOM   2559  CG2 VAL B  77     -29.271  13.775   9.958  1.00 95.74           C  
ANISOU 2559  CG2 VAL B  77    18092  11034   7250    119   -618   4176       C  
ATOM   2560  N   GLY B  78     -29.837  10.301  12.858  1.00 81.89           N  
ANISOU 2560  N   GLY B  78    15160   9790   6167    136   -830   3385       N  
ATOM   2561  CA  GLY B  78     -29.625   8.999  13.461  1.00 76.79           C  
ANISOU 2561  CA  GLY B  78    14106   9377   5691     32   -813   3054       C  
ATOM   2562  C   GLY B  78     -30.912   8.244  13.741  1.00 75.53           C  
ANISOU 2562  C   GLY B  78    13586   9382   5731    267  -1165   3017       C  
ATOM   2563  O   GLY B  78     -30.995   7.040  13.502  1.00 74.26           O  
ANISOU 2563  O   GLY B  78    13214   9482   5520    192  -1291   2824       O  
ATOM   2564  N   THR B  79     -31.916   8.951  14.252  1.00 74.96           N  
ANISOU 2564  N   THR B  79    13437   9150   5893    548  -1316   3197       N  
ATOM   2565  CA  THR B  79     -33.201   8.338  14.574  1.00 74.03           C  
ANISOU 2565  CA  THR B  79    12951   9181   5998    780  -1639   3180       C  
ATOM   2566  C   THR B  79     -33.942   7.912  13.313  1.00 77.98           C  
ANISOU 2566  C   THR B  79    13519   9900   6208    854  -2008   3295       C  
ATOM   2567  O   THR B  79     -34.459   6.797  13.237  1.00 76.62           O  
ANISOU 2567  O   THR B  79    13056   9978   6078    842  -2219   3136       O  
ATOM   2568  CB  THR B  79     -34.102   9.284  15.392  1.00 74.87           C  
ANISOU 2568  CB  THR B  79    12964   9061   6422   1087  -1696   3356       C  
ATOM   2569  OG1 THR B  79     -33.454   9.615  16.627  1.00 71.21           O  
ANISOU 2569  OG1 THR B  79    12418   8408   6229   1016  -1369   3217       O  
ATOM   2570  CG2 THR B  79     -35.442   8.628  15.689  1.00 74.51           C  
ANISOU 2570  CG2 THR B  79    12510   9195   6607   1316  -2022   3341       C  
ATOM   2571  N   VAL B  80     -33.995   8.803  12.327  1.00120.92           N  
ANISOU 2571  N   VAL B  80    19356  15240  11347    924  -2091   3573       N  
ATOM   2572  CA  VAL B  80     -34.630   8.476  11.056  1.00122.70           C  
ANISOU 2572  CA  VAL B  80    19701  15677  11242    988  -2451   3697       C  
ATOM   2573  C   VAL B  80     -33.880   7.342  10.363  1.00122.06           C  
ANISOU 2573  C   VAL B  80    19657  15852  10869    695  -2407   3457       C  
ATOM   2574  O   VAL B  80     -34.482   6.347   9.957  1.00122.99           O  
ANISOU 2574  O   VAL B  80    19567  16229  10937    700  -2690   3338       O  
ATOM   2575  CB  VAL B  80     -34.712   9.698  10.120  1.00121.98           C  
ANISOU 2575  CB  VAL B  80    20040  15426  10881   1101  -2494   4034       C  
ATOM   2576  CG1 VAL B  80     -35.116   9.270   8.718  1.00125.68           C  
ANISOU 2576  CG1 VAL B  80    20551  16174  11028   1091  -2763   4069       C  
ATOM   2577  CG2 VAL B  80     -35.693  10.722  10.672  1.00122.79           C  
ANISOU 2577  CG2 VAL B  80    20049  15313  11294   1440  -2601   4266       C  
ATOM   2578  N   GLY B  81     -32.564   7.493  10.248  1.00 85.57           N  
ANISOU 2578  N   GLY B  81    15293  11153   6070    438  -2044   3378       N  
ATOM   2579  CA  GLY B  81     -31.726   6.489   9.618  1.00 84.92           C  
ANISOU 2579  CA  GLY B  81    15262  11288   5713    164  -1939   3143       C  
ATOM   2580  C   GLY B  81     -31.879   5.108  10.228  1.00 80.33           C  
ANISOU 2580  C   GLY B  81    14241  10909   5369    101  -1999   2816       C  
ATOM   2581  O   GLY B  81     -32.244   4.155   9.538  1.00 81.52           O  
ANISOU 2581  O   GLY B  81    14331  11300   5342     58  -2232   2701       O  
ATOM   2582  N   ASN B  82     -31.611   5.003  11.527  1.00 80.22           N  
ANISOU 2582  N   ASN B  82    13938  10791   5752     94  -1794   2669       N  
ATOM   2583  CA  ASN B  82     -31.691   3.724  12.228  1.00 79.09           C  
ANISOU 2583  CA  ASN B  82    13390  10806   5856     33  -1813   2371       C  
ATOM   2584  C   ASN B  82     -33.106   3.153  12.300  1.00 80.01           C  
ANISOU 2584  C   ASN B  82    13202  11061   6138    223  -2211   2384       C  
ATOM   2585  O   ASN B  82     -33.295   1.941  12.213  1.00 79.24           O  
ANISOU 2585  O   ASN B  82    12903  11164   6041    136  -2338   2171       O  
ATOM   2586  CB  ASN B  82     -31.095   3.836  13.634  1.00 75.19           C  
ANISOU 2586  CB  ASN B  82    12681  10160   5729     -4  -1507   2236       C  
ATOM   2587  CG  ASN B  82     -29.607   4.128  13.616  1.00 74.07           C  
ANISOU 2587  CG  ASN B  82    12749   9942   5452   -245  -1115   2140       C  
ATOM   2588  OD1 ASN B  82     -28.787   3.225  13.445  1.00 72.86           O  
ANISOU 2588  OD1 ASN B  82    12543   9936   5204   -438   -979   1904       O  
ATOM   2589  ND2 ASN B  82     -29.250   5.394  13.796  1.00 74.42           N  
ANISOU 2589  ND2 ASN B  82    13026   9751   5499   -234   -928   2320       N  
ATOM   2590  N   GLY B  83     -34.094   4.028  12.462  1.00 97.39           N  
ANISOU 2590  N   GLY B  83    15364  13151   8489    481  -2399   2629       N  
ATOM   2591  CA  GLY B  83     -35.481   3.603  12.535  1.00 97.86           C  
ANISOU 2591  CA  GLY B  83    15112  13347   8725    674  -2778   2666       C  
ATOM   2592  C   GLY B  83     -35.973   3.005  11.231  1.00 98.95           C  
ANISOU 2592  C   GLY B  83    15353  13725   8520    639  -3125   2678       C  
ATOM   2593  O   GLY B  83     -36.500   1.885  11.201  1.00 98.01           O  
ANISOU 2593  O   GLY B  83    14959  13808   8473    585  -3328   2493       O  
ATOM   2594  N   VAL B  84     -35.798   3.753  10.144  1.00 94.65           N  
ANISOU 2594  N   VAL B  84    15222  13152   7589    661  -3193   2896       N  
ATOM   2595  CA  VAL B  84     -36.185   3.268   8.825  1.00 97.98           C  
ANISOU 2595  CA  VAL B  84    15806  13802   7618    620  -3519   2917       C  
ATOM   2596  C   VAL B  84     -35.364   2.035   8.460  1.00 96.35           C  
ANISOU 2596  C   VAL B  84    15617  13768   7224    327  -3391   2594       C  
ATOM   2597  O   VAL B  84     -35.867   1.123   7.809  1.00 97.81           O  
ANISOU 2597  O   VAL B  84    15724  14177   7259    272  -3678   2470       O  
ATOM   2598  CB  VAL B  84     -36.035   4.355   7.739  1.00102.16           C  
ANISOU 2598  CB  VAL B  84    16771  14262   7780    689  -3526   3196       C  
ATOM   2599  CG1 VAL B  84     -36.473   3.818   6.386  1.00105.93           C  
ANISOU 2599  CG1 VAL B  84    17281  15012   7955    666  -3783   3150       C  
ATOM   2600  CG2 VAL B  84     -36.856   5.578   8.101  1.00104.00           C  
ANISOU 2600  CG2 VAL B  84    16973  14306   8235    997  -3619   3504       C  
ATOM   2601  N   THR B  85     -34.106   2.006   8.893  1.00 82.82           N  
ANISOU 2601  N   THR B  85    13995  11945   5527    143  -2965   2450       N  
ATOM   2602  CA  THR B  85     -33.270   0.823   8.711  1.00 80.86           C  
ANISOU 2602  CA  THR B  85    13724  11837   5162   -110  -2801   2128       C  
ATOM   2603  C   THR B  85     -33.935  -0.386   9.361  1.00 77.99           C  
ANISOU 2603  C   THR B  85    12918  11601   5114   -112  -2971   1889       C  
ATOM   2604  O   THR B  85     -34.057  -1.449   8.746  1.00 79.33           O  
ANISOU 2604  O   THR B  85    13067  11960   5117   -232  -3128   1695       O  
ATOM   2605  CB  THR B  85     -31.867   1.014   9.317  1.00 77.32           C  
ANISOU 2605  CB  THR B  85    13353  11245   4778   -276  -2314   2012       C  
ATOM   2606  OG1 THR B  85     -31.249   2.173   8.744  1.00 80.37           O  
ANISOU 2606  OG1 THR B  85    14151  11499   4888   -299  -2139   2240       O  
ATOM   2607  CG2 THR B  85     -30.998  -0.205   9.047  1.00 76.03           C  
ANISOU 2607  CG2 THR B  85    13174  11234   4481   -509  -2150   1688       C  
ATOM   2608  N   LEU B  86     -34.380  -0.205  10.601  1.00103.88           N  
ANISOU 2608  N   LEU B  86    15862  14765   8843     17  -2931   1905       N  
ATOM   2609  CA  LEU B  86     -35.075  -1.253  11.340  1.00103.56           C  
ANISOU 2609  CA  LEU B  86    15391  14818   9138     26  -3073   1715       C  
ATOM   2610  C   LEU B  86     -36.317  -1.734  10.602  1.00104.35           C  
ANISOU 2610  C   LEU B  86    15388  15115   9146     93  -3537   1750       C  
ATOM   2611  O   LEU B  86     -36.521  -2.936  10.436  1.00103.93           O  
ANISOU 2611  O   LEU B  86    15206  15218   9063    -44  -3667   1518       O  
ATOM   2612  CB  LEU B  86     -35.475  -0.761  12.734  1.00 98.98           C  
ANISOU 2612  CB  LEU B  86    14506  14079   9023    191  -2970   1788       C  
ATOM   2613  CG  LEU B  86     -34.735  -1.331  13.948  1.00 97.61           C  
ANISOU 2613  CG  LEU B  86    14127  13814   9144     92  -2631   1575       C  
ATOM   2614  CD1 LEU B  86     -34.089  -2.670  13.619  1.00 96.77           C  
ANISOU 2614  CD1 LEU B  86    13995  13842   8929   -133  -2562   1274       C  
ATOM   2615  CD2 LEU B  86     -33.699  -0.346  14.458  1.00 96.95           C  
ANISOU 2615  CD2 LEU B  86    14251  13529   9058     77  -2270   1652       C  
ATOM   2616  N   PHE B  87     -37.146  -0.794  10.157  1.00130.22           N  
ANISOU 2616  N   PHE B  87    18725  18379  12374    306  -3794   2036       N  
ATOM   2617  CA  PHE B  87     -38.402  -1.164   9.507  1.00131.82           C  
ANISOU 2617  CA  PHE B  87    18782  18782  12523    392  -4268   2084       C  
ATOM   2618  C   PHE B  87     -38.254  -1.548   8.032  1.00133.94           C  
ANISOU 2618  C   PHE B  87    19377  19235  12278    261  -4485   2044       C  
ATOM   2619  O   PHE B  87     -39.239  -1.876   7.370  1.00137.18           O  
ANISOU 2619  O   PHE B  87    19621  19830  12673    323  -4797   2017       O  
ATOM   2620  CB  PHE B  87     -39.463  -0.075   9.694  1.00128.38           C  
ANISOU 2620  CB  PHE B  87    18235  18285  12260    698  -4496   2399       C  
ATOM   2621  CG  PHE B  87     -40.066  -0.053  11.070  1.00127.31           C  
ANISOU 2621  CG  PHE B  87    17661  18053  12658    835  -4412   2387       C  
ATOM   2622  CD1 PHE B  87     -39.804  -1.074  11.970  1.00125.10           C  
ANISOU 2622  CD1 PHE B  87    17099  17778  12657    678  -4214   2113       C  
ATOM   2623  CD2 PHE B  87     -40.900   0.980  11.462  1.00128.61           C  
ANISOU 2623  CD2 PHE B  87    17707  18119  13041   1129  -4522   2651       C  
ATOM   2624  CE1 PHE B  87     -40.355  -1.063  13.236  1.00124.08           C  
ANISOU 2624  CE1 PHE B  87    16587  17565  12993    798  -4121   2106       C  
ATOM   2625  CE2 PHE B  87     -41.457   0.997  12.729  1.00127.48           C  
ANISOU 2625  CE2 PHE B  87    17168  17893  13375   1256  -4421   2631       C  
ATOM   2626  CZ  PHE B  87     -41.183  -0.027  13.617  1.00125.24           C  
ANISOU 2626  CZ  PHE B  87    16616  17624  13345   1083  -4217   2359       C  
ATOM   2627  N   THR B  88     -37.026  -1.508   7.524  1.00103.68           N  
ANISOU 2627  N   THR B  88    15926  15359   8110     98  -4199   1986       N  
ATOM   2628  CA  THR B  88     -36.737  -2.031   6.191  1.00106.82           C  
ANISOU 2628  CA  THR B  88    16543  15925   8119    -28  -4224   1845       C  
ATOM   2629  C   THR B  88     -36.166  -3.435   6.310  1.00104.59           C  
ANISOU 2629  C   THR B  88    16173  15727   7838   -272  -4113   1477       C  
ATOM   2630  O   THR B  88     -36.423  -4.294   5.466  1.00107.47           O  
ANISOU 2630  O   THR B  88    16525  16263   8046   -354  -4265   1286       O  
ATOM   2631  CB  THR B  88     -35.741  -1.150   5.415  1.00111.78           C  
ANISOU 2631  CB  THR B  88    17621  16471   8380    -63  -3944   1982       C  
ATOM   2632  OG1 THR B  88     -34.645  -0.795   6.266  1.00108.52           O  
ANISOU 2632  OG1 THR B  88    17320  15864   8048   -162  -3559   1975       O  
ATOM   2633  CG2 THR B  88     -36.418   0.110   4.913  1.00115.92           C  
ANISOU 2633  CG2 THR B  88    18269  16949   8827    174  -4101   2331       C  
ATOM   2634  N   LEU B  89     -35.389  -3.662   7.365  1.00 99.48           N  
ANISOU 2634  N   LEU B  89    15443  14950   7405   -369  -3811   1364       N  
ATOM   2635  CA  LEU B  89     -34.852  -4.990   7.637  1.00 97.37           C  
ANISOU 2635  CA  LEU B  89    15031  14732   7231   -562  -3662   1012       C  
ATOM   2636  C   LEU B  89     -35.949  -5.918   8.153  1.00 96.15           C  
ANISOU 2636  C   LEU B  89    14454  14654   7422   -540  -3944    886       C  
ATOM   2637  O   LEU B  89     -35.778  -7.136   8.194  1.00 95.11           O  
ANISOU 2637  O   LEU B  89    14215  14587   7336   -697  -3937    600       O  
ATOM   2638  CB  LEU B  89     -33.704  -4.914   8.646  1.00 97.50           C  
ANISOU 2638  CB  LEU B  89    14995  14580   7469   -621  -3188    916       C  
ATOM   2639  CG  LEU B  89     -32.465  -4.133   8.204  1.00 97.52           C  
ANISOU 2639  CG  LEU B  89    15377  14506   7169   -693  -2849    994       C  
ATOM   2640  CD1 LEU B  89     -31.429  -4.096   9.316  1.00 96.05           C  
ANISOU 2640  CD1 LEU B  89    15060  14170   7264   -745  -2425    889       C  
ATOM   2641  CD2 LEU B  89     -31.876  -4.724   6.934  1.00 97.70           C  
ANISOU 2641  CD2 LEU B  89    15723  14679   6718   -864  -2835    837       C  
ATOM   2642  N   ALA B  90     -37.075  -5.330   8.546  1.00122.98           N  
ANISOU 2642  N   ALA B  90    17615  18037  11074   -344  -4181   1102       N  
ATOM   2643  CA  ALA B  90     -38.215  -6.097   9.033  1.00122.83           C  
ANISOU 2643  CA  ALA B  90    17175  18106  11390   -320  -4463   1016       C  
ATOM   2644  C   ALA B  90     -39.053  -6.632   7.876  1.00126.19           C  
ANISOU 2644  C   ALA B  90    17617  18743  11586   -361  -4847    942       C  
ATOM   2645  O   ALA B  90     -39.609  -7.727   7.955  1.00126.36           O  
ANISOU 2645  O   ALA B  90    17383  18853  11774   -470  -4983    715       O  
ATOM   2646  CB  ALA B  90     -39.069  -5.245   9.959  1.00123.35           C  
ANISOU 2646  CB  ALA B  90    16953  18086  11830    -78  -4535   1262       C  
ATOM   2647  N   ARG B  91     -39.139  -5.850   6.803  1.00125.93           N  
ANISOU 2647  N   ARG B  91    17849  18774  11226   -253  -4938   1110       N  
ATOM   2648  CA  ARG B  91     -39.903  -6.241   5.624  1.00130.23           C  
ANISOU 2648  CA  ARG B  91    18392  19523  11566   -251  -5226   1036       C  
ATOM   2649  C   ARG B  91     -39.265  -7.437   4.925  1.00130.52           C  
ANISOU 2649  C   ARG B  91    18588  19636  11368   -485  -5132    700       C  
ATOM   2650  O   ARG B  91     -38.333  -7.282   4.136  1.00131.54           O  
ANISOU 2650  O   ARG B  91    19089  19770  11121   -546  -4952    675       O  
ATOM   2651  CB  ARG B  91     -40.019  -5.068   4.648  1.00137.01           C  
ANISOU 2651  CB  ARG B  91    19534  20425  12099    -80  -5311   1313       C  
ATOM   2652  CG  ARG B  91     -40.737  -3.853   5.213  1.00137.45           C  
ANISOU 2652  CG  ARG B  91    19449  20399  12378    189  -5417   1652       C  
ATOM   2653  CD  ARG B  91     -42.209  -4.141   5.463  1.00139.34           C  
ANISOU 2653  CD  ARG B  91    19233  20778  12933    312  -5764   1657       C  
ATOM   2654  NE  ARG B  91     -42.895  -2.994   6.050  1.00139.74           N  
ANISOU 2654  NE  ARG B  91    19119  20741  13235    593  -5830   1965       N  
ATOM   2655  CZ  ARG B  91     -43.442  -2.008   5.346  1.00143.69           C  
ANISOU 2655  CZ  ARG B  91    19728  21292  13578    815  -5987   2231       C  
ATOM   2656  NH1 ARG B  91     -43.383  -2.024   4.021  1.00147.61           N  
ANISOU 2656  NH1 ARG B  91    20497  21937  13651    781  -6105   2239       N  
ATOM   2657  NH2 ARG B  91     -44.046  -1.004   5.966  1.00143.96           N  
ANISOU 2657  NH2 ARG B  91    19598  21223  13877   1081  -6016   2492       N  
ATOM   2658  N   LEU B  98     -28.624 -16.027   3.593  1.00123.10           N  
ANISOU 2658  N   LEU B  98    18877  18204   9690  -1657  -2234  -2002       N  
ATOM   2659  CA  LEU B  98     -27.485 -15.384   4.236  1.00120.35           C  
ANISOU 2659  CA  LEU B  98    18534  17796   9398  -1635  -1857  -1909       C  
ATOM   2660  C   LEU B  98     -27.792 -13.919   4.525  1.00119.62           C  
ANISOU 2660  C   LEU B  98    18455  17737   9259  -1596  -1919  -1569       C  
ATOM   2661  O   LEU B  98     -27.296 -13.352   5.499  1.00116.59           O  
ANISOU 2661  O   LEU B  98    17966  17283   9051  -1589  -1722  -1460       O  
ATOM   2662  CB  LEU B  98     -26.235 -15.511   3.357  1.00114.63           C  
ANISOU 2662  CB  LEU B  98    18036  17099   8418  -1629  -1526  -2025       C  
ATOM   2663  CG  LEU B  98     -24.859 -15.242   3.977  1.00112.11           C  
ANISOU 2663  CG  LEU B  98    17674  16712   8212  -1617  -1088  -2035       C  
ATOM   2664  CD1 LEU B  98     -23.796 -16.057   3.258  1.00113.96           C  
ANISOU 2664  CD1 LEU B  98    18037  16953   8311  -1607   -821  -2268       C  
ATOM   2665  CD2 LEU B  98     -24.498 -13.763   3.935  1.00111.81           C  
ANISOU 2665  CD2 LEU B  98    17726  16708   8051  -1610   -952  -1746       C  
ATOM   2666  N   GLN B  99     -28.615 -13.314   3.675  1.00137.65           N  
ANISOU 2666  N   GLN B  99    20871  20125  11306  -1563  -2195  -1402       N  
ATOM   2667  CA  GLN B  99     -28.957 -11.901   3.810  1.00137.63           C  
ANISOU 2667  CA  GLN B  99    20920  20138  11236  -1501  -2273  -1059       C  
ATOM   2668  C   GLN B  99     -29.743 -11.610   5.086  1.00134.76           C  
ANISOU 2668  C   GLN B  99    20282  19709  11212  -1470  -2455   -920       C  
ATOM   2669  O   GLN B  99     -29.535 -10.582   5.725  1.00133.04           O  
ANISOU 2669  O   GLN B  99    20059  19433  11057  -1429  -2353   -691       O  
ATOM   2670  CB  GLN B  99     -29.727 -11.413   2.580  1.00135.20           C  
ANISOU 2670  CB  GLN B  99    20802  19961  10609  -1449  -2557   -918       C  
ATOM   2671  CG  GLN B  99     -28.904 -11.416   1.300  1.00138.34           C  
ANISOU 2671  CG  GLN B  99    21504  20433  10626  -1472  -2354   -989       C  
ATOM   2672  CD  GLN B  99     -29.673 -10.882   0.108  1.00142.77           C  
ANISOU 2672  CD  GLN B  99    22257  21134  10855  -1416  -2637   -831       C  
ATOM   2673  OE1 GLN B  99     -30.901 -10.814   0.125  1.00143.90           O  
ANISOU 2673  OE1 GLN B  99    22276  21339  11062  -1364  -3025   -744       O  
ATOM   2674  NE2 GLN B  99     -28.949 -10.495  -0.937  1.00145.63           N  
ANISOU 2674  NE2 GLN B  99    22909  21557  10868  -1423  -2440   -789       N  
ATOM   2675  N   SER B 100     -30.643 -12.517   5.455  1.00188.27           N  
ANISOU 2675  N   SER B 100    26828  26489  18217  -1493  -2715  -1058       N  
ATOM   2676  CA  SER B 100     -31.423 -12.358   6.678  1.00185.56           C  
ANISOU 2676  CA  SER B 100    26188  26092  18225  -1469  -2885   -942       C  
ATOM   2677  C   SER B 100     -30.526 -12.483   7.907  1.00181.04           C  
ANISOU 2677  C   SER B 100    25492  25408  17889  -1511  -2560  -1011       C  
ATOM   2678  O   SER B 100     -30.714 -11.781   8.909  1.00179.51           O  
ANISOU 2678  O   SER B 100    25085  25121  17999  -1404  -2502   -820       O  
ATOM   2679  CB  SER B 100     -32.542 -13.399   6.738  1.00185.98           C  
ANISOU 2679  CB  SER B 100    26006  26175  18483  -1505  -3214  -1092       C  
ATOM   2680  OG  SER B 100     -33.404 -13.286   5.619  1.00189.73           O  
ANISOU 2680  OG  SER B 100    26566  26778  18744  -1465  -3524  -1040       O  
ATOM   2681  N   ARG B 101     -29.549 -13.381   7.813  1.00131.60           N  
ANISOU 2681  N   ARG B 101    19280  19107  11615  -1574  -2283  -1280       N  
ATOM   2682  CA  ARG B 101     -28.604 -13.621   8.896  1.00127.35           C  
ANISOU 2682  CA  ARG B 101    18598  18467  11321  -1583  -1944  -1378       C  
ATOM   2683  C   ARG B 101     -27.883 -12.338   9.293  1.00124.96           C  
ANISOU 2683  C   ARG B 101    18336  18120  11023  -1513  -1684  -1152       C  
ATOM   2684  O   ARG B 101     -27.728 -12.050  10.479  1.00123.73           O  
ANISOU 2684  O   ARG B 101    17937  17854  11220  -1435  -1547  -1074       O  
ATOM   2685  CB  ARG B 101     -27.593 -14.701   8.498  1.00125.98           C  
ANISOU 2685  CB  ARG B 101    18517  18269  11081  -1631  -1686  -1682       C  
ATOM   2686  CG  ARG B 101     -26.602 -15.056   9.595  1.00123.35           C  
ANISOU 2686  CG  ARG B 101    18022  17848  10998  -1630  -1356  -1805       C  
ATOM   2687  CD  ARG B 101     -25.680 -16.194   9.180  1.00123.83           C  
ANISOU 2687  CD  ARG B 101    18138  17857  11054  -1625  -1132  -2090       C  
ATOM   2688  NE  ARG B 101     -26.400 -17.448   8.971  1.00125.56           N  
ANISOU 2688  NE  ARG B 101    18312  18028  11367  -1657  -1357  -2284       N  
ATOM   2689  CZ  ARG B 101     -26.661 -17.972   7.778  1.00128.82           C  
ANISOU 2689  CZ  ARG B 101    18909  18477  11559  -1674  -1493  -2397       C  
ATOM   2690  NH1 ARG B 101     -26.257 -17.353   6.677  1.00131.14           N  
ANISOU 2690  NH1 ARG B 101    19445  18868  11515  -1656  -1423  -2329       N  
ATOM   2691  NH2 ARG B 101     -27.323 -19.117   7.684  1.00129.89           N  
ANISOU 2691  NH2 ARG B 101    18989  18551  11811  -1716  -1694  -2580       N  
ATOM   2692  N   VAL B 102     -27.454 -11.565   8.300  1.00 82.65           N  
ANISOU 2692  N   VAL B 102    13298  12842   5263  -1549  -1618  -1048       N  
ATOM   2693  CA  VAL B 102     -26.801 -10.288   8.566  1.00 81.65           C  
ANISOU 2693  CA  VAL B 102    13246  12661   5115  -1509  -1379   -824       C  
ATOM   2694  C   VAL B 102     -27.822  -9.173   8.796  1.00 83.47           C  
ANISOU 2694  C   VAL B 102    13431  12848   5437  -1391  -1623   -500       C  
ATOM   2695  O   VAL B 102     -27.502  -8.144   9.394  1.00 83.48           O  
ANISOU 2695  O   VAL B 102    13405  12749   5564  -1331  -1456   -308       O  
ATOM   2696  CB  VAL B 102     -25.814  -9.890   7.446  1.00 87.04           C  
ANISOU 2696  CB  VAL B 102    14232  13392   5446  -1553  -1131   -825       C  
ATOM   2697  CG1 VAL B 102     -24.672 -10.892   7.367  1.00 86.49           C  
ANISOU 2697  CG1 VAL B 102    14116  13320   5428  -1595   -820  -1120       C  
ATOM   2698  CG2 VAL B 102     -26.528  -9.782   6.111  1.00 91.14           C  
ANISOU 2698  CG2 VAL B 102    14965  14001   5663  -1521  -1395   -749       C  
ATOM   2699  N   ASP B 103     -29.050  -9.383   8.324  1.00100.92           N  
ANISOU 2699  N   ASP B 103    15626  15130   7589  -1355  -2022   -446       N  
ATOM   2700  CA  ASP B 103     -30.141  -8.457   8.612  1.00102.20           C  
ANISOU 2700  CA  ASP B 103    15683  15256   7891  -1213  -2284   -155       C  
ATOM   2701  C   ASP B 103     -30.384  -8.405  10.114  1.00100.75           C  
ANISOU 2701  C   ASP B 103    15126  14935   8217  -1115  -2202   -119       C  
ATOM   2702  O   ASP B 103     -30.709  -7.353  10.665  1.00100.80           O  
ANISOU 2702  O   ASP B 103    15070  14850   8377   -991  -2199    123       O  
ATOM   2703  CB  ASP B 103     -31.431  -8.870   7.896  1.00105.86           C  
ANISOU 2703  CB  ASP B 103    16125  15845   8250  -1197  -2745   -146       C  
ATOM   2704  CG  ASP B 103     -31.442  -8.477   6.433  1.00109.50           C  
ANISOU 2704  CG  ASP B 103    16936  16420   8246  -1205  -2868    -62       C  
ATOM   2705  OD1 ASP B 103     -30.655  -7.588   6.047  1.00110.82           O  
ANISOU 2705  OD1 ASP B 103    17358  16549   8199  -1193  -2632     82       O  
ATOM   2706  OD2 ASP B 103     -32.242  -9.057   5.669  1.00112.60           O  
ANISOU 2706  OD2 ASP B 103    17296  16923   8563  -1194  -3156   -147       O  
ATOM   2707  N   TYR B 104     -30.225  -9.549  10.772  1.00100.69           N  
ANISOU 2707  N   TYR B 104    14890  14906   8462  -1167  -2128   -362       N  
ATOM   2708  CA  TYR B 104     -30.380  -9.613  12.222  1.00100.04           C  
ANISOU 2708  CA  TYR B 104    14469  14700   8841  -1084  -2029   -348       C  
ATOM   2709  C   TYR B 104     -29.288  -8.832  12.956  1.00 99.33           C  
ANISOU 2709  C   TYR B 104    14401  14501   8840  -1059  -1661   -283       C  
ATOM   2710  O   TYR B 104     -29.570  -8.110  13.916  1.00100.23           O  
ANISOU 2710  O   TYR B 104    14352  14511   9220   -948  -1624   -122       O  
ATOM   2711  CB  TYR B 104     -30.423 -11.068  12.694  1.00 98.83           C  
ANISOU 2711  CB  TYR B 104    14107  14540   8905  -1153  -2030   -617       C  
ATOM   2712  CG  TYR B 104     -31.674 -11.799  12.264  1.00100.22           C  
ANISOU 2712  CG  TYR B 104    14180  14796   9102  -1182  -2409   -668       C  
ATOM   2713  CD1 TYR B 104     -32.852 -11.107  12.014  1.00103.25           C  
ANISOU 2713  CD1 TYR B 104    14501  15233   9496  -1092  -2722   -445       C  
ATOM   2714  CD2 TYR B 104     -31.678 -13.179  12.103  1.00 99.35           C  
ANISOU 2714  CD2 TYR B 104    14034  14706   9009  -1300  -2458   -942       C  
ATOM   2715  CE1 TYR B 104     -34.000 -11.767  11.620  1.00104.56           C  
ANISOU 2715  CE1 TYR B 104    14543  15492   9694  -1131  -3084   -497       C  
ATOM   2716  CE2 TYR B 104     -32.822 -13.848  11.708  1.00101.60           C  
ANISOU 2716  CE2 TYR B 104    14220  15062   9322  -1355  -2811  -1001       C  
ATOM   2717  CZ  TYR B 104     -33.979 -13.137  11.468  1.00103.88           C  
ANISOU 2717  CZ  TYR B 104    14420  15425   9623  -1276  -3127   -779       C  
ATOM   2718  OH  TYR B 104     -35.121 -13.797  11.075  1.00104.51           O  
ANISOU 2718  OH  TYR B 104    14372  15595   9742  -1343  -3493   -843       O  
ATOM   2719  N   TYR B 105     -28.047  -8.973  12.498  1.00 77.06           N  
ANISOU 2719  N   TYR B 105    11776  11708   5797  -1165  -1389   -416       N  
ATOM   2720  CA  TYR B 105     -26.929  -8.239  13.085  1.00 75.47           C  
ANISOU 2720  CA  TYR B 105    11598  11424   5654  -1174  -1041   -374       C  
ATOM   2721  C   TYR B 105     -27.098  -6.735  12.896  1.00 76.74           C  
ANISOU 2721  C   TYR B 105    11929  11524   5706  -1118  -1045    -80       C  
ATOM   2722  O   TYR B 105     -26.927  -5.958  13.837  1.00 76.38           O  
ANISOU 2722  O   TYR B 105    11777  11357   5887  -1055   -907     36       O  
ATOM   2723  CB  TYR B 105     -25.597  -8.691  12.482  1.00 74.51           C  
ANISOU 2723  CB  TYR B 105    11650  11372   5290  -1305   -759   -575       C  
ATOM   2724  CG  TYR B 105     -25.216 -10.117  12.811  1.00 73.55           C  
ANISOU 2724  CG  TYR B 105    11363  11272   5309  -1340   -686   -870       C  
ATOM   2725  CD1 TYR B 105     -24.888 -10.487  14.108  1.00 71.92           C  
ANISOU 2725  CD1 TYR B 105    10878  10978   5470  -1287   -545   -948       C  
ATOM   2726  CD2 TYR B 105     -25.169 -11.089  11.821  1.00 74.57           C  
ANISOU 2726  CD2 TYR B 105    11639  11500   5195  -1420   -757  -1070       C  
ATOM   2727  CE1 TYR B 105     -24.537 -11.789  14.413  1.00 70.21           C  
ANISOU 2727  CE1 TYR B 105    10531  10763   5384  -1302   -480  -1200       C  
ATOM   2728  CE2 TYR B 105     -24.818 -12.393  12.116  1.00 73.25           C  
ANISOU 2728  CE2 TYR B 105    11343  11324   5166  -1440   -684  -1340       C  
ATOM   2729  CZ  TYR B 105     -24.502 -12.738  13.413  1.00 70.59           C  
ANISOU 2729  CZ  TYR B 105    10728  10889   5203  -1376   -545  -1396       C  
ATOM   2730  OH  TYR B 105     -24.152 -14.035  13.710  1.00 68.80           O  
ANISOU 2730  OH  TYR B 105    10393  10636   5113  -1380   -474  -1648       O  
ATOM   2731  N   LEU B 106     -27.432  -6.331  11.673  1.00 62.94           N  
ANISOU 2731  N   LEU B 106    10462   9853   3600  -1139  -1204     38       N  
ATOM   2732  CA  LEU B 106     -27.662  -4.922  11.371  1.00 64.58           C  
ANISOU 2732  CA  LEU B 106    10873   9990   3675  -1074  -1233    337       C  
ATOM   2733  C   LEU B 106     -28.837  -4.372  12.175  1.00 63.77           C  
ANISOU 2733  C   LEU B 106    10556   9791   3884   -893  -1456    531       C  
ATOM   2734  O   LEU B 106     -28.846  -3.201  12.556  1.00 63.70           O  
ANISOU 2734  O   LEU B 106    10607   9648   3947   -811  -1380    747       O  
ATOM   2735  CB  LEU B 106     -27.898  -4.715   9.872  1.00 68.59           C  
ANISOU 2735  CB  LEU B 106    11731  10612   3720  -1115  -1404    429       C  
ATOM   2736  CG  LEU B 106     -26.683  -4.364   9.009  1.00 71.18           C  
ANISOU 2736  CG  LEU B 106    12400  10975   3670  -1264  -1109    413       C  
ATOM   2737  CD1 LEU B 106     -25.656  -5.487   9.006  1.00 70.50           C  
ANISOU 2737  CD1 LEU B 106    12253  10974   3558  -1402   -865     85       C  
ATOM   2738  CD2 LEU B 106     -27.116  -4.026   7.590  1.00 76.60           C  
ANISOU 2738  CD2 LEU B 106    13448  11760   3896  -1272  -1321    563       C  
ATOM   2739  N   GLY B 107     -29.823  -5.226  12.431  1.00 59.66           N  
ANISOU 2739  N   GLY B 107     9786   9332   3551   -835  -1721    447       N  
ATOM   2740  CA  GLY B 107     -30.956  -4.854  13.257  1.00 58.27           C  
ANISOU 2740  CA  GLY B 107     9355   9086   3699   -664  -1918    602       C  
ATOM   2741  C   GLY B 107     -30.531  -4.612  14.692  1.00 54.82           C  
ANISOU 2741  C   GLY B 107     8700   8502   3625   -617  -1663    583       C  
ATOM   2742  O   GLY B 107     -30.971  -3.653  15.329  1.00 54.46           O  
ANISOU 2742  O   GLY B 107     8594   8337   3760   -477  -1667    778       O  
ATOM   2743  N   SER B 108     -29.667  -5.487  15.200  1.00 91.76           N  
ANISOU 2743  N   SER B 108    13271  13189   8403   -724  -1443    344       N  
ATOM   2744  CA  SER B 108     -29.135  -5.345  16.551  1.00 91.68           C  
ANISOU 2744  CA  SER B 108    13067  13060   8705   -694  -1199    301       C  
ATOM   2745  C   SER B 108     -28.321  -4.061  16.688  1.00 91.81           C  
ANISOU 2745  C   SER B 108    13272  12964   8649   -703   -956    437       C  
ATOM   2746  O   SER B 108     -28.442  -3.341  17.681  1.00 91.96           O  
ANISOU 2746  O   SER B 108    13188  12851   8902   -607   -880    543       O  
ATOM   2747  CB  SER B 108     -28.276  -6.557  16.919  1.00 90.87           C  
ANISOU 2747  CB  SER B 108    12847  13004   8676   -803  -1023     21       C  
ATOM   2748  OG  SER B 108     -27.806  -6.464  18.253  1.00 90.80           O  
ANISOU 2748  OG  SER B 108    12644  12895   8960   -763   -820    -18       O  
ATOM   2749  N   LEU B 109     -27.495  -3.781  15.684  1.00 54.02           N  
ANISOU 2749  N   LEU B 109     8770   8222   3531   -828   -827    428       N  
ATOM   2750  CA  LEU B 109     -26.687  -2.565  15.663  1.00 54.52           C  
ANISOU 2750  CA  LEU B 109     9045   8176   3493   -874   -591    560       C  
ATOM   2751  C   LEU B 109     -27.558  -1.314  15.641  1.00 56.08           C  
ANISOU 2751  C   LEU B 109     9355   8245   3707   -729   -738    855       C  
ATOM   2752  O   LEU B 109     -27.376  -0.402  16.451  1.00 55.10           O  
ANISOU 2752  O   LEU B 109     9216   7960   3761   -681   -595    955       O  
ATOM   2753  CB  LEU B 109     -25.751  -2.563  14.453  1.00 56.69           C  
ANISOU 2753  CB  LEU B 109     9619   8542   3379  -1040   -445    514       C  
ATOM   2754  CG  LEU B 109     -24.476  -3.399  14.564  1.00 55.36           C  
ANISOU 2754  CG  LEU B 109     9382   8458   3194  -1191   -170    244       C  
ATOM   2755  CD1 LEU B 109     -23.716  -3.394  13.249  1.00 58.34           C  
ANISOU 2755  CD1 LEU B 109    10064   8941   3161  -1338    -43    212       C  
ATOM   2756  CD2 LEU B 109     -23.604  -2.870  15.688  1.00 53.15           C  
ANISOU 2756  CD2 LEU B 109     8975   8068   3152  -1224    108    218       C  
ATOM   2757  N   ALA B 110     -28.503  -1.279  14.706  1.00 65.57           N  
ANISOU 2757  N   ALA B 110    10674   9516   4721   -654  -1030    988       N  
ATOM   2758  CA  ALA B 110     -29.401  -0.140  14.559  1.00 67.24           C  
ANISOU 2758  CA  ALA B 110    11003   9616   4928   -487  -1202   1282       C  
ATOM   2759  C   ALA B 110     -30.237   0.076  15.817  1.00 67.73           C  
ANISOU 2759  C   ALA B 110    10765   9571   5399   -304  -1276   1338       C  
ATOM   2760  O   ALA B 110     -30.567   1.211  16.164  1.00 68.60           O  
ANISOU 2760  O   ALA B 110    10947   9515   5602   -171  -1264   1546       O  
ATOM   2761  CB  ALA B 110     -30.294  -0.324  13.343  1.00 69.29           C  
ANISOU 2761  CB  ALA B 110    11403  10009   4914   -433  -1541   1390       C  
ATOM   2762  N   LEU B 111     -30.573  -1.015  16.499  1.00 56.55           N  
ANISOU 2762  N   LEU B 111     9024   8239   4224   -296  -1339   1153       N  
ATOM   2763  CA  LEU B 111     -31.277  -0.923  17.773  1.00 54.68           C  
ANISOU 2763  CA  LEU B 111     8489   7913   4375   -143  -1360   1179       C  
ATOM   2764  C   LEU B 111     -30.375  -0.311  18.839  1.00 52.40           C  
ANISOU 2764  C   LEU B 111     8199   7462   4250   -171  -1036   1145       C  
ATOM   2765  O   LEU B 111     -30.793   0.579  19.581  1.00 52.24           O  
ANISOU 2765  O   LEU B 111     8138   7288   4422    -27  -1005   1283       O  
ATOM   2766  CB  LEU B 111     -31.763  -2.298  18.231  1.00 53.08           C  
ANISOU 2766  CB  LEU B 111     7963   7834   4373   -159  -1475    985       C  
ATOM   2767  CG  LEU B 111     -32.398  -2.338  19.623  1.00 51.04           C  
ANISOU 2767  CG  LEU B 111     7389   7495   4511    -24  -1449    988       C  
ATOM   2768  CD1 LEU B 111     -33.631  -1.448  19.683  1.00 52.97           C  
ANISOU 2768  CD1 LEU B 111     7575   7678   4873    195  -1649   1230       C  
ATOM   2769  CD2 LEU B 111     -32.741  -3.766  20.024  1.00 49.60           C  
ANISOU 2769  CD2 LEU B 111     6921   7422   4504    -78  -1523    791       C  
ATOM   2770  N   SER B 112     -29.135  -0.791  18.904  1.00 77.53           N  
ANISOU 2770  N   SER B 112    11421  10683   7353   -354   -798    953       N  
ATOM   2771  CA  SER B 112     -28.169  -0.299  19.881  1.00 76.04           C  
ANISOU 2771  CA  SER B 112    11218  10370   7302   -412   -500    891       C  
ATOM   2772  C   SER B 112     -27.878   1.185  19.679  1.00 76.60           C  
ANISOU 2772  C   SER B 112    11566  10267   7269   -406   -384   1089       C  
ATOM   2773  O   SER B 112     -27.559   1.897  20.630  1.00 75.93           O  
ANISOU 2773  O   SER B 112    11459  10028   7361   -383   -217   1106       O  
ATOM   2774  CB  SER B 112     -26.870  -1.106  19.813  1.00 73.08           C  
ANISOU 2774  CB  SER B 112    10830  10098   6838   -607   -288    652       C  
ATOM   2775  OG  SER B 112     -26.201  -0.896  18.582  1.00 75.31           O  
ANISOU 2775  OG  SER B 112    11392  10436   6784   -748   -213    671       O  
ATOM   2776  N   ASP B 113     -27.986   1.643  18.436  1.00 96.25           N  
ANISOU 2776  N   ASP B 113    14334  12773   9462   -431   -474   1237       N  
ATOM   2777  CA  ASP B 113     -27.835   3.061  18.133  1.00 96.87           C  
ANISOU 2777  CA  ASP B 113    14713  12665   9426   -413   -388   1461       C  
ATOM   2778  C   ASP B 113     -29.093   3.823  18.539  1.00 97.36           C  
ANISOU 2778  C   ASP B 113    14729  12586   9675   -156   -579   1675       C  
ATOM   2779  O   ASP B 113     -29.017   4.906  19.129  1.00 96.72           O  
ANISOU 2779  O   ASP B 113    14745  12289   9716    -93   -450   1787       O  
ATOM   2780  CB  ASP B 113     -27.556   3.266  16.643  1.00102.29           C  
ANISOU 2780  CB  ASP B 113    15733  13420   9713   -512   -429   1569       C  
ATOM   2781  CG  ASP B 113     -26.291   2.566  16.184  1.00101.14           C  
ANISOU 2781  CG  ASP B 113    15642  13416   9371   -758   -213   1358       C  
ATOM   2782  OD1 ASP B 113     -25.404   2.323  17.029  1.00 99.62           O  
ANISOU 2782  OD1 ASP B 113    15287  13216   9346   -865     20   1171       O  
ATOM   2783  OD2 ASP B 113     -26.184   2.263  14.976  1.00101.40           O  
ANISOU 2783  OD2 ASP B 113    15879  13573   9075   -836   -277   1378       O  
ATOM   2784  N   LEU B 114     -30.248   3.244  18.220  1.00 50.90           N  
ANISOU 2784  N   LEU B 114     8689   6827   3821     -9   -885   1719       N  
ATOM   2785  CA  LEU B 114     -31.536   3.853  18.537  1.00 52.08           C  
ANISOU 2785  CA  LEU B 114     8748   6885   4157    256  -1093   1917       C  
ATOM   2786  C   LEU B 114     -31.706   4.105  20.032  1.00 48.87           C  
ANISOU 2786  C   LEU B 114     8112   6339   4118    366   -957   1868       C  
ATOM   2787  O   LEU B 114     -32.223   5.145  20.434  1.00 50.32           O  
ANISOU 2787  O   LEU B 114     8352   6338   4429    550   -964   2043       O  
ATOM   2788  CB  LEU B 114     -32.688   2.988  18.020  1.00 53.30           C  
ANISOU 2788  CB  LEU B 114     8701   7240   4310    358  -1441   1923       C  
ATOM   2789  CG  LEU B 114     -33.435   3.516  16.794  1.00 58.43           C  
ANISOU 2789  CG  LEU B 114     9564   7920   4716    479  -1722   2166       C  
ATOM   2790  CD1 LEU B 114     -34.623   2.626  16.464  1.00 59.69           C  
ANISOU 2790  CD1 LEU B 114     9457   8285   4938    580  -2080   2148       C  
ATOM   2791  CD2 LEU B 114     -33.884   4.951  17.018  1.00 60.69           C  
ANISOU 2791  CD2 LEU B 114    10003   7967   5088    691  -1706   2431       C  
ATOM   2792  N   LEU B 115     -31.269   3.151  20.849  1.00 64.78           N  
ANISOU 2792  N   LEU B 115     9881   8439   6293    263   -834   1630       N  
ATOM   2793  CA  LEU B 115     -31.372   3.282  22.300  1.00 63.85           C  
ANISOU 2793  CA  LEU B 115     9554   8209   6495    353   -696   1564       C  
ATOM   2794  C   LEU B 115     -30.573   4.477  22.812  1.00 63.67           C  
ANISOU 2794  C   LEU B 115     9754   7954   6481    316   -439   1612       C  
ATOM   2795  O   LEU B 115     -31.045   5.235  23.659  1.00 64.23           O  
ANISOU 2795  O   LEU B 115     9809   7849   6745    484   -402   1707       O  
ATOM   2796  CB  LEU B 115     -30.901   2.001  22.993  1.00 61.77           C  
ANISOU 2796  CB  LEU B 115     9033   8083   6353    230   -605   1306       C  
ATOM   2797  CG  LEU B 115     -31.704   0.732  22.704  1.00 62.04           C  
ANISOU 2797  CG  LEU B 115     8829   8319   6422    245   -832   1227       C  
ATOM   2798  CD1 LEU B 115     -31.144  -0.445  23.487  1.00 60.78           C  
ANISOU 2798  CD1 LEU B 115     8457   8248   6387    129   -707    984       C  
ATOM   2799  CD2 LEU B 115     -33.177   0.942  23.019  1.00 62.40           C  
ANISOU 2799  CD2 LEU B 115     8674   8356   6679    476  -1045   1370       C  
ATOM   2800  N   ILE B 116     -29.362   4.638  22.289  1.00 50.59           N  
ANISOU 2800  N   ILE B 116     8305   6298   4618     88   -256   1538       N  
ATOM   2801  CA  ILE B 116     -28.496   5.743  22.682  1.00 50.91           C  
ANISOU 2801  CA  ILE B 116     8566   6128   4650     -5     -4   1563       C  
ATOM   2802  C   ILE B 116     -29.062   7.082  22.222  1.00 53.99           C  
ANISOU 2802  C   ILE B 116     9240   6298   4977    136    -58   1836       C  
ATOM   2803  O   ILE B 116     -29.114   8.043  22.991  1.00 54.29           O  
ANISOU 2803  O   ILE B 116     9353   6106   5171    219     59   1895       O  
ATOM   2804  CB  ILE B 116     -27.075   5.577  22.109  1.00 50.81           C  
ANISOU 2804  CB  ILE B 116     8708   6187   4410   -293    194   1442       C  
ATOM   2805  CG1 ILE B 116     -26.443   4.280  22.617  1.00 47.94           C  
ANISOU 2805  CG1 ILE B 116     8069   6022   4124   -411    263   1171       C  
ATOM   2806  CG2 ILE B 116     -26.204   6.771  22.475  1.00 51.59           C  
ANISOU 2806  CG2 ILE B 116     9035   6062   4505   -415    450   1475       C  
ATOM   2807  CD1 ILE B 116     -25.032   4.054  22.118  1.00 47.92           C  
ANISOU 2807  CD1 ILE B 116     8168   6109   3929   -675    471   1032       C  
ATOM   2808  N   LEU B 117     -29.492   7.138  20.967  1.00 56.15           N  
ANISOU 2808  N   LEU B 117     9684   6634   5014    171   -241   2002       N  
ATOM   2809  CA  LEU B 117     -29.980   8.387  20.391  1.00 59.49           C  
ANISOU 2809  CA  LEU B 117    10411   6849   5342    313   -307   2285       C  
ATOM   2810  C   LEU B 117     -31.317   8.837  20.982  1.00 60.28           C  
ANISOU 2810  C   LEU B 117    10367   6841   5694    639   -482   2426       C  
ATOM   2811  O   LEU B 117     -31.585  10.033  21.080  1.00 62.35           O  
ANISOU 2811  O   LEU B 117    10840   6846   6003    780   -441   2612       O  
ATOM   2812  CB  LEU B 117     -30.073   8.271  18.868  1.00 62.19           C  
ANISOU 2812  CB  LEU B 117    10984   7310   5335    269   -473   2427       C  
ATOM   2813  CG  LEU B 117     -28.730   8.020  18.179  1.00 62.14           C  
ANISOU 2813  CG  LEU B 117    11173   7383   5052    -45   -261   2317       C  
ATOM   2814  CD1 LEU B 117     -28.923   7.724  16.705  1.00 64.78           C  
ANISOU 2814  CD1 LEU B 117    11713   7872   5027    -75   -442   2434       C  
ATOM   2815  CD2 LEU B 117     -27.798   9.207  18.374  1.00 63.10           C  
ANISOU 2815  CD2 LEU B 117    11581   7241   5150   -183     36   2382       C  
ATOM   2816  N   LEU B 118     -32.147   7.879  21.381  1.00 56.50           N  
ANISOU 2816  N   LEU B 118     9529   6551   5385    758   -663   2337       N  
ATOM   2817  CA  LEU B 118     -33.461   8.197  21.933  1.00 57.37           C  
ANISOU 2817  CA  LEU B 118     9448   6597   5751   1068   -822   2458       C  
ATOM   2818  C   LEU B 118     -33.412   8.588  23.407  1.00 55.49           C  
ANISOU 2818  C   LEU B 118     9082   6191   5810   1136   -605   2356       C  
ATOM   2819  O   LEU B 118     -34.146   9.473  23.843  1.00 57.07           O  
ANISOU 2819  O   LEU B 118     9317   6193   6172   1373   -608   2498       O  
ATOM   2820  CB  LEU B 118     -34.428   7.022  21.750  1.00 56.94           C  
ANISOU 2820  CB  LEU B 118     9046   6814   5773   1152  -1096   2405       C  
ATOM   2821  CG  LEU B 118     -35.017   6.794  20.358  1.00 59.78           C  
ANISOU 2821  CG  LEU B 118     9489   7331   5894   1199  -1410   2556       C  
ATOM   2822  CD1 LEU B 118     -35.924   5.575  20.364  1.00 59.16           C  
ANISOU 2822  CD1 LEU B 118     9028   7512   5939   1246  -1658   2458       C  
ATOM   2823  CD2 LEU B 118     -35.775   8.026  19.890  1.00 64.07           C  
ANISOU 2823  CD2 LEU B 118    10235   7699   6410   1459  -1547   2858       C  
ATOM   2824  N   PHE B 119     -32.549   7.929  24.173  1.00 53.97           N  
ANISOU 2824  N   PHE B 119     8747   6078   5682    940   -421   2109       N  
ATOM   2825  CA  PHE B 119     -32.563   8.089  25.624  1.00 52.12           C  
ANISOU 2825  CA  PHE B 119     8356   5732   5716   1004   -244   1989       C  
ATOM   2826  C   PHE B 119     -31.310   8.753  26.200  1.00 51.22           C  
ANISOU 2826  C   PHE B 119     8449   5441   5569    810     50   1877       C  
ATOM   2827  O   PHE B 119     -31.412   9.654  27.029  1.00 51.66           O  
ANISOU 2827  O   PHE B 119     8584   5270   5773    910    186   1895       O  
ATOM   2828  CB  PHE B 119     -32.822   6.741  26.303  1.00 49.42           C  
ANISOU 2828  CB  PHE B 119     7630   5616   5532    989   -290   1802       C  
ATOM   2829  CG  PHE B 119     -34.079   6.062  25.834  1.00 50.45           C  
ANISOU 2829  CG  PHE B 119     7522   5918   5727   1156   -573   1891       C  
ATOM   2830  CD1 PHE B 119     -35.320   6.623  26.089  1.00 52.36           C  
ANISOU 2830  CD1 PHE B 119     7661   6078   6155   1445   -688   2054       C  
ATOM   2831  CD2 PHE B 119     -34.020   4.863  25.143  1.00 49.74           C  
ANISOU 2831  CD2 PHE B 119     7305   6073   5521   1021   -724   1802       C  
ATOM   2832  CE1 PHE B 119     -36.479   6.003  25.659  1.00 53.59           C  
ANISOU 2832  CE1 PHE B 119     7565   6410   6386   1586   -958   2131       C  
ATOM   2833  CE2 PHE B 119     -35.177   4.237  24.711  1.00 50.94           C  
ANISOU 2833  CE2 PHE B 119     7231   6386   5738   1149   -997   1870       C  
ATOM   2834  CZ  PHE B 119     -36.408   4.809  24.971  1.00 52.88           C  
ANISOU 2834  CZ  PHE B 119     7350   6565   6176   1426  -1119   2037       C  
ATOM   2835  N   ALA B 120     -30.135   8.308  25.769  1.00 47.23           N  
ANISOU 2835  N   ALA B 120     8026   5042   4875    531    150   1752       N  
ATOM   2836  CA  ALA B 120     -28.886   8.866  26.277  1.00 46.51           C  
ANISOU 2836  CA  ALA B 120     8089   4822   4759    315    419   1626       C  
ATOM   2837  C   ALA B 120     -28.653  10.288  25.769  1.00 49.40           C  
ANISOU 2837  C   ALA B 120     8844   4913   5012    286    519   1803       C  
ATOM   2838  O   ALA B 120     -28.114  11.132  26.485  1.00 49.48           O  
ANISOU 2838  O   ALA B 120     8993   4728   5079    179    730   1737       O  
ATOM   2839  CB  ALA B 120     -27.713   7.968  25.909  1.00 44.81           C  
ANISOU 2839  CB  ALA B 120     7811   4821   4393     39    500   1437       C  
ATOM   2840  N   LEU B 121     -29.062  10.545  24.531  1.00 56.71           N  
ANISOU 2840  N   LEU B 121     9956   5818   5773    378    360   2029       N  
ATOM   2841  CA  LEU B 121     -28.852  11.850  23.905  1.00 59.84           C  
ANISOU 2841  CA  LEU B 121    10757   5944   6038    355    446   2231       C  
ATOM   2842  C   LEU B 121     -29.585  13.019  24.582  1.00 61.58           C  
ANISOU 2842  C   LEU B 121    11100   5846   6454    600    473   2367       C  
ATOM   2843  O   LEU B 121     -28.960  14.037  24.862  1.00 62.79           O  
ANISOU 2843  O   LEU B 121    11518   5728   6612    495    680   2380       O  
ATOM   2844  CB  LEU B 121     -29.147  11.796  22.398  1.00 62.36           C  
ANISOU 2844  CB  LEU B 121    11272   6348   6075    366    269   2438       C  
ATOM   2845  CG  LEU B 121     -28.730  12.997  21.545  1.00 65.79           C  
ANISOU 2845  CG  LEU B 121    12164   6530   6306    289    374   2655       C  
ATOM   2846  CD1 LEU B 121     -28.255  12.524  20.184  1.00 67.00           C  
ANISOU 2846  CD1 LEU B 121    12477   6867   6114    104    331   2709       C  
ATOM   2847  CD2 LEU B 121     -29.871  13.993  21.387  1.00 68.87           C  
ANISOU 2847  CD2 LEU B 121    12727   6680   6762    615    222   2938       C  
ATOM   2848  N   PRO B 122     -30.904  12.888  24.842  1.00 57.63           N  
ANISOU 2848  N   PRO B 122    10407   5368   6120    925    273   2465       N  
ATOM   2849  CA  PRO B 122     -31.583  14.014  25.496  1.00 60.39           C  
ANISOU 2849  CA  PRO B 122    10876   5407   6661   1180    319   2587       C  
ATOM   2850  C   PRO B 122     -31.015  14.308  26.883  1.00 58.45           C  
ANISOU 2850  C   PRO B 122    10592   5009   6606   1101    571   2376       C  
ATOM   2851  O   PRO B 122     -30.966  15.466  27.297  1.00 61.24           O  
ANISOU 2851  O   PRO B 122    11188   5037   7044   1180    704   2441       O  
ATOM   2852  CB  PRO B 122     -33.029  13.525  25.621  1.00 60.58           C  
ANISOU 2852  CB  PRO B 122    10595   5571   6852   1515     68   2674       C  
ATOM   2853  CG  PRO B 122     -33.177  12.506  24.555  1.00 59.80           C  
ANISOU 2853  CG  PRO B 122    10372   5784   6564   1441   -158   2704       C  
ATOM   2854  CD  PRO B 122     -31.854  11.816  24.494  1.00 56.37           C  
ANISOU 2854  CD  PRO B 122     9939   5496   5983   1077      1   2484       C  
ATOM   2855  N   VAL B 123     -30.592  13.263  27.587  1.00 71.94           N  
ANISOU 2855  N   VAL B 123    12014   6945   8374    949    628   2125       N  
ATOM   2856  CA  VAL B 123     -29.994  13.420  28.906  1.00 71.23           C  
ANISOU 2856  CA  VAL B 123    11874   6756   8434    858    844   1907       C  
ATOM   2857  C   VAL B 123     -28.638  14.114  28.808  1.00 72.09           C  
ANISOU 2857  C   VAL B 123    12277   6696   8417    545   1064   1834       C  
ATOM   2858  O   VAL B 123     -28.343  15.028  29.577  1.00 72.59           O  
ANISOU 2858  O   VAL B 123    12509   6495   8577    525   1235   1777       O  
ATOM   2859  CB  VAL B 123     -29.825  12.062  29.613  1.00 70.27           C  
ANISOU 2859  CB  VAL B 123    11375   6938   8387    780    830   1674       C  
ATOM   2860  CG1 VAL B 123     -29.126  12.239  30.948  1.00 69.36           C  
ANISOU 2860  CG1 VAL B 123    11232   6731   8389    676   1040   1452       C  
ATOM   2861  CG2 VAL B 123     -31.176  11.393  29.799  1.00 70.47           C  
ANISOU 2861  CG2 VAL B 123    11096   7119   8561   1062    635   1737       C  
ATOM   2862  N   ASP B 124     -27.822  13.686  27.849  1.00 70.18           N  
ANISOU 2862  N   ASP B 124    12093   6611   7959    294   1066   1826       N  
ATOM   2863  CA  ASP B 124     -26.507  14.281  27.639  1.00 69.51           C  
ANISOU 2863  CA  ASP B 124    12256   6405   7748    -32   1280   1761       C  
ATOM   2864  C   ASP B 124     -26.628  15.749  27.240  1.00 70.19           C  
ANISOU 2864  C   ASP B 124    12760   6112   7795      7   1360   1975       C  
ATOM   2865  O   ASP B 124     -25.807  16.577  27.634  1.00 70.19           O  
ANISOU 2865  O   ASP B 124    12972   5885   7813   -193   1570   1903       O  
ATOM   2866  CB  ASP B 124     -25.726  13.506  26.576  1.00 69.55           C  
ANISOU 2866  CB  ASP B 124    12234   6670   7521   -271   1263   1736       C  
ATOM   2867  CG  ASP B 124     -24.320  14.039  26.381  1.00 69.62           C  
ANISOU 2867  CG  ASP B 124    12442   6596   7413   -631   1504   1649       C  
ATOM   2868  OD1 ASP B 124     -23.740  14.557  27.357  1.00 68.97           O  
ANISOU 2868  OD1 ASP B 124    12380   6365   7460   -749   1672   1499       O  
ATOM   2869  OD2 ASP B 124     -23.793  13.941  25.252  1.00 70.19           O  
ANISOU 2869  OD2 ASP B 124    12648   6759   7260   -802   1529   1725       O  
ATOM   2870  N   VAL B 125     -27.658  16.064  26.462  1.00 71.87           N  
ANISOU 2870  N   VAL B 125    13092   6255   7959    265   1183   2240       N  
ATOM   2871  CA  VAL B 125     -27.919  17.439  26.053  1.00 72.91           C  
ANISOU 2871  CA  VAL B 125    13629   6010   8062    366   1230   2480       C  
ATOM   2872  C   VAL B 125     -28.375  18.279  27.242  1.00 72.43           C  
ANISOU 2872  C   VAL B 125    13617   5648   8254    554   1328   2434       C  
ATOM   2873  O   VAL B 125     -27.893  19.392  27.448  1.00 73.03           O  
ANISOU 2873  O   VAL B 125    14021   5381   8348    451   1514   2457       O  
ATOM   2874  CB  VAL B 125     -28.988  17.510  24.938  1.00 74.21           C  
ANISOU 2874  CB  VAL B 125    13876   6203   8117    644    976   2782       C  
ATOM   2875  CG1 VAL B 125     -29.479  18.939  24.751  1.00 76.87           C  
ANISOU 2875  CG1 VAL B 125    14573   6128   8509    873    992   3032       C  
ATOM   2876  CG2 VAL B 125     -28.437  16.956  23.634  1.00 73.87           C  
ANISOU 2876  CG2 VAL B 125    13944   6359   7763    427    925   2864       C  
ATOM   2877  N   TYR B 126     -29.294  17.731  28.030  1.00 95.41           N  
ANISOU 2877  N   TYR B 126    16209   8686  11359    818   1215   2360       N  
ATOM   2878  CA  TYR B 126     -29.874  18.467  29.149  1.00 95.12           C  
ANISOU 2878  CA  TYR B 126    16196   8389  11558   1042   1303   2315       C  
ATOM   2879  C   TYR B 126     -28.907  18.674  30.315  1.00 93.81           C  
ANISOU 2879  C   TYR B 126    16040   8135  11469    796   1539   2031       C  
ATOM   2880  O   TYR B 126     -28.651  19.806  30.721  1.00 95.33           O  
ANISOU 2880  O   TYR B 126    16537   7973  11714    752   1708   2023       O  
ATOM   2881  CB  TYR B 126     -31.153  17.786  29.644  1.00 95.62           C  
ANISOU 2881  CB  TYR B 126    15891   8641  11800   1385   1132   2317       C  
ATOM   2882  CG  TYR B 126     -31.738  18.430  30.881  1.00 94.80           C  
ANISOU 2882  CG  TYR B 126    15779   8306  11938   1622   1246   2243       C  
ATOM   2883  CD1 TYR B 126     -32.465  19.610  30.794  1.00 96.09           C  
ANISOU 2883  CD1 TYR B 126    16195   8122  12193   1910   1255   2440       C  
ATOM   2884  CD2 TYR B 126     -31.560  17.861  32.135  1.00 92.88           C  
ANISOU 2884  CD2 TYR B 126    15287   8187  11818   1570   1350   1978       C  
ATOM   2885  CE1 TYR B 126     -32.998  20.204  31.922  1.00 95.72           C  
ANISOU 2885  CE1 TYR B 126    16150   7857  12363   2138   1378   2360       C  
ATOM   2886  CE2 TYR B 126     -32.089  18.448  33.268  1.00 92.39           C  
ANISOU 2886  CE2 TYR B 126    15235   7919  11952   1786   1469   1901       C  
ATOM   2887  CZ  TYR B 126     -32.808  19.619  33.156  1.00 93.52           C  
ANISOU 2887  CZ  TYR B 126    15627   7717  12189   2069   1489   2085       C  
ATOM   2888  OH  TYR B 126     -33.337  20.207  34.282  1.00 93.62           O  
ANISOU 2888  OH  TYR B 126    15658   7520  12395   2296   1625   1995       O  
ATOM   2889  N   ASN B 127     -28.376  17.583  30.856  1.00 69.75           N  
ANISOU 2889  N   ASN B 127    12668   5403   8429    639   1542   1796       N  
ATOM   2890  CA  ASN B 127     -27.550  17.661  32.059  1.00 68.61           C  
ANISOU 2890  CA  ASN B 127    12492   5217   8359    434   1729   1518       C  
ATOM   2891  C   ASN B 127     -26.077  17.959  31.810  1.00 69.12           C  
ANISOU 2891  C   ASN B 127    12742   5236   8283     15   1890   1412       C  
ATOM   2892  O   ASN B 127     -25.511  18.878  32.398  1.00 70.40           O  
ANISOU 2892  O   ASN B 127    13151   5111   8487   -123   2064   1333       O  
ATOM   2893  CB  ASN B 127     -27.679  16.383  32.889  1.00 67.80           C  
ANISOU 2893  CB  ASN B 127    11973   5451   8336    466   1669   1314       C  
ATOM   2894  CG  ASN B 127     -28.502  16.586  34.144  1.00 66.82           C  
ANISOU 2894  CG  ASN B 127    11753   5221   8413    737   1705   1240       C  
ATOM   2895  OD1 ASN B 127     -28.037  17.183  35.115  1.00 65.63           O  
ANISOU 2895  OD1 ASN B 127    11731   4883   8324    660   1868   1078       O  
ATOM   2896  ND2 ASN B 127     -29.729  16.081  34.135  1.00 66.60           N  
ANISOU 2896  ND2 ASN B 127    11497   5321   8485   1048   1557   1351       N  
ATOM   2897  N   PHE B 128     -25.453  17.179  30.940  1.00 89.29           N  
ANISOU 2897  N   PHE B 128    15176   8072  10677   -191   1839   1404       N  
ATOM   2898  CA  PHE B 128     -24.013  17.290  30.747  1.00 89.21           C  
ANISOU 2898  CA  PHE B 128    15247   8096  10553   -598   2001   1263       C  
ATOM   2899  C   PHE B 128     -23.595  18.404  29.789  1.00 90.27           C  
ANISOU 2899  C   PHE B 128    15792   7945  10559   -772   2121   1442       C  
ATOM   2900  O   PHE B 128     -22.433  18.483  29.393  1.00 90.62           O  
ANISOU 2900  O   PHE B 128    15909   8021  10499  -1126   2267   1354       O  
ATOM   2901  CB  PHE B 128     -23.433  15.944  30.314  1.00 92.39           C  
ANISOU 2901  CB  PHE B 128    15343   8916  10845   -746   1929   1156       C  
ATOM   2902  CG  PHE B 128     -23.615  14.855  31.337  1.00 91.41           C  
ANISOU 2902  CG  PHE B 128    14838   9049  10842   -645   1854    952       C  
ATOM   2903  CD1 PHE B 128     -23.463  15.125  32.687  1.00 90.79           C  
ANISOU 2903  CD1 PHE B 128    14711   8877  10908   -650   1945    760       C  
ATOM   2904  CD2 PHE B 128     -23.959  13.567  30.952  1.00 91.40           C  
ANISOU 2904  CD2 PHE B 128    14551   9372  10802   -550   1694    953       C  
ATOM   2905  CE1 PHE B 128     -23.632  14.132  33.631  1.00 89.75           C  
ANISOU 2905  CE1 PHE B 128    14256   8976  10867   -555   1883    590       C  
ATOM   2906  CE2 PHE B 128     -24.131  12.571  31.893  1.00 90.85           C  
ANISOU 2906  CE2 PHE B 128    14156   9515  10845   -462   1636    780       C  
ATOM   2907  CZ  PHE B 128     -23.967  12.856  33.233  1.00 89.63           C  
ANISOU 2907  CZ  PHE B 128    13961   9270  10822   -461   1733    608       C  
ATOM   2908  N   ILE B 129     -24.538  19.264  29.424  1.00 66.46           N  
ANISOU 2908  N   ILE B 129    13044   4651   7558   -520   2065   1698       N  
ATOM   2909  CA  ILE B 129     -24.225  20.410  28.579  1.00 71.58           C  
ANISOU 2909  CA  ILE B 129    14130   4975   8092   -654   2183   1897       C  
ATOM   2910  C   ILE B 129     -24.917  21.676  29.062  1.00 75.47           C  
ANISOU 2910  C   ILE B 129    14934   5008   8733   -453   2251   1997       C  
ATOM   2911  O   ILE B 129     -24.281  22.717  29.218  1.00 78.57           O  
ANISOU 2911  O   ILE B 129    15601   5113   9140   -674   2438   1950       O  
ATOM   2912  CB  ILE B 129     -24.592  20.161  27.106  1.00 73.16           C  
ANISOU 2912  CB  ILE B 129    14439   5277   8081   -570   2042   2180       C  
ATOM   2913  CG1 ILE B 129     -23.691  19.075  26.507  1.00 70.42           C  
ANISOU 2913  CG1 ILE B 129    13871   5329   7559   -834   2036   2069       C  
ATOM   2914  CG2 ILE B 129     -24.474  21.453  26.306  1.00 78.97           C  
ANISOU 2914  CG2 ILE B 129    15665   5634   8708   -644   2155   2425       C  
ATOM   2915  CD1 ILE B 129     -23.888  18.886  25.034  1.00 72.75           C  
ANISOU 2915  CD1 ILE B 129    14341   5705   7596   -835   1947   2320       C  
ATOM   2916  N   TRP B 130     -26.219  21.580  29.304  1.00119.98           N  
ANISOU 2916  N   TRP B 130    20488  10608  14493    -32   2092   2113       N  
ATOM   2917  CA  TRP B 130     -26.995  22.735  29.740  1.00122.57           C  
ANISOU 2917  CA  TRP B 130    21062  10525  14984    221   2148   2189       C  
ATOM   2918  C   TRP B 130     -26.909  22.986  31.248  1.00121.13           C  
ANISOU 2918  C   TRP B 130    20764  10272  14989    197   2276   1892       C  
ATOM   2919  O   TRP B 130     -26.411  24.022  31.690  1.00122.15           O  
ANISOU 2919  O   TRP B 130    21046  10234  15134    -88   2454   1713       O  
ATOM   2920  CB  TRP B 130     -28.463  22.604  29.316  1.00123.47           C  
ANISOU 2920  CB  TRP B 130    21089  10656  15171    699   1926   2422       C  
ATOM   2921  CG  TRP B 130     -28.741  22.859  27.866  1.00126.10           C  
ANISOU 2921  CG  TRP B 130    21550  11033  15332    779   1762   2717       C  
ATOM   2922  CD1 TRP B 130     -27.832  23.089  26.874  1.00128.22           C  
ANISOU 2922  CD1 TRP B 130    22012  11328  15380    479   1809   2799       C  
ATOM   2923  CD2 TRP B 130     -30.031  22.902  27.247  1.00128.24           C  
ANISOU 2923  CD2 TRP B 130    21746  11345  15634   1186   1520   2962       C  
ATOM   2924  NE1 TRP B 130     -28.480  23.272  25.675  1.00130.76           N  
ANISOU 2924  NE1 TRP B 130    22413  11696  15577    678   1610   3083       N  
ATOM   2925  CE2 TRP B 130     -29.831  23.162  25.878  1.00130.90           C  
ANISOU 2925  CE2 TRP B 130    22263  11725  15748   1109   1418   3187       C  
ATOM   2926  CE3 TRP B 130     -31.338  22.745  27.721  1.00127.93           C  
ANISOU 2926  CE3 TRP B 130    21481  11333  15796   1603   1378   3002       C  
ATOM   2927  CZ2 TRP B 130     -30.889  23.269  24.976  1.00133.45           C  
ANISOU 2927  CZ2 TRP B 130    22559  12112  16036   1431   1161   3452       C  
ATOM   2928  CZ3 TRP B 130     -32.388  22.853  26.823  1.00130.49           C  
ANISOU 2928  CZ3 TRP B 130    21748  11730  16104   1916   1126   3260       C  
ATOM   2929  CH2 TRP B 130     -32.156  23.112  25.466  1.00133.56           C  
ANISOU 2929  CH2 TRP B 130    22332  12155  16262   1829   1009   3483       C  
ATOM   2930  N   VAL B 131     -27.401  22.029  32.028  1.00 74.43           N  
ANISOU 2930  N   VAL B 131    14522   4551   9208    489   2160   1817       N  
ATOM   2931  CA  VAL B 131     -27.428  22.139  33.482  1.00 73.15           C  
ANISOU 2931  CA  VAL B 131    14245   4341   9209    532   2263   1555       C  
ATOM   2932  C   VAL B 131     -26.539  21.098  34.145  1.00 68.29           C  
ANISOU 2932  C   VAL B 131    13306   4090   8550    251   2280   1269       C  
ATOM   2933  O   VAL B 131     -26.972  19.979  34.415  1.00 64.36           O  
ANISOU 2933  O   VAL B 131    12441   3938   8075    376   2149   1220       O  
ATOM   2934  CB  VAL B 131     -28.860  22.000  34.001  1.00 72.95           C  
ANISOU 2934  CB  VAL B 131    14024   4342   9354    998   2155   1619       C  
ATOM   2935  CG1 VAL B 131     -28.942  22.357  35.472  1.00 72.89           C  
ANISOU 2935  CG1 VAL B 131    13988   4212   9495   1059   2299   1368       C  
ATOM   2936  CG2 VAL B 131     -29.773  22.898  33.191  1.00 77.64           C  
ANISOU 2936  CG2 VAL B 131    14862   4651   9989   1320   2085   1926       C  
ATOM   2937  N   HIS B 132     -25.296  21.477  34.418  1.00 88.52           N  
ANISOU 2937  N   HIS B 132    16004   6569  11060   -129   2438   1084       N  
ATOM   2938  CA  HIS B 132     -24.325  20.544  34.978  1.00 87.48           C  
ANISOU 2938  CA  HIS B 132    15580   6775  10885   -405   2452    816       C  
ATOM   2939  C   HIS B 132     -24.686  20.134  36.400  1.00 85.60           C  
ANISOU 2939  C   HIS B 132    15114   6640  10770   -250   2448    595       C  
ATOM   2940  O   HIS B 132     -24.258  19.085  36.878  1.00 83.70           O  
ANISOU 2940  O   HIS B 132    14556   6743  10504   -346   2396    423       O  
ATOM   2941  CB  HIS B 132     -22.918  21.136  34.924  1.00 88.70           C  
ANISOU 2941  CB  HIS B 132    15929   6807  10967   -851   2621    674       C  
ATOM   2942  CG  HIS B 132     -22.507  21.574  33.554  1.00 90.53           C  
ANISOU 2942  CG  HIS B 132    16396   6939  11062  -1035   2661    887       C  
ATOM   2943  ND1 HIS B 132     -22.676  22.866  33.106  1.00 93.88           N  
ANISOU 2943  ND1 HIS B 132    17254   6927  11489  -1032   2764   1066       N  
ATOM   2944  CD2 HIS B 132     -21.954  20.888  32.527  1.00 90.05           C  
ANISOU 2944  CD2 HIS B 132    16216   7151  10847  -1221   2621    954       C  
ATOM   2945  CE1 HIS B 132     -22.233  22.960  31.864  1.00 95.51           C  
ANISOU 2945  CE1 HIS B 132    17590   7160  11539  -1215   2783   1241       C  
ATOM   2946  NE2 HIS B 132     -21.789  21.774  31.490  1.00 92.89           N  
ANISOU 2946  NE2 HIS B 132    16937   7250  11106  -1335   2706   1174       N  
ATOM   2947  N   HIS B 133     -25.473  20.970  37.070  1.00 92.39           N  
ANISOU 2947  N   HIS B 133    16153   7195  11757      1   2511    606       N  
ATOM   2948  CA  HIS B 133     -25.967  20.660  38.407  1.00 91.42           C  
ANISOU 2948  CA  HIS B 133    15850   7146  11740    191   2525    423       C  
ATOM   2949  C   HIS B 133     -27.261  21.423  38.677  1.00 93.13           C  
ANISOU 2949  C   HIS B 133    16221   7065  12098    598   2552    556       C  
ATOM   2950  O   HIS B 133     -27.386  22.587  38.297  1.00 97.32           O  
ANISOU 2950  O   HIS B 133    17112   7207  12659    637   2636    672       O  
ATOM   2951  CB  HIS B 133     -24.911  20.986  39.469  1.00 89.24           C  
ANISOU 2951  CB  HIS B 133    15651   6809  11447   -101   2658    112       C  
ATOM   2952  CG  HIS B 133     -24.662  22.451  39.653  1.00 92.87           C  
ANISOU 2952  CG  HIS B 133    16541   6800  11946   -191   2821     77       C  
ATOM   2953  ND1 HIS B 133     -23.671  23.130  38.977  1.00 95.60           N  
ANISOU 2953  ND1 HIS B 133    17134   6968  12220   -549   2907     81       N  
ATOM   2954  CD2 HIS B 133     -25.269  23.365  40.446  1.00 95.31           C  
ANISOU 2954  CD2 HIS B 133    17086   6765  12363     24   2927     32       C  
ATOM   2955  CE1 HIS B 133     -23.683  24.399  39.341  1.00 99.19           C  
ANISOU 2955  CE1 HIS B 133    17886   7079  12724   -551   3013     41       C  
ATOM   2956  NE2 HIS B 133     -24.644  24.568  40.232  1.00 98.86           N  
ANISOU 2956  NE2 HIS B 133    17814   6968  12781   -202   3009      7       N  
ATOM   2957  N   PRO B 134     -28.230  20.770  39.338  1.00 66.14           N  
ANISOU 2957  N   PRO B 134    12530   3824   8776    906   2493    541       N  
ATOM   2958  CA  PRO B 134     -28.131  19.399  39.842  1.00 61.36           C  
ANISOU 2958  CA  PRO B 134    11524   3646   8143    868   2407    409       C  
ATOM   2959  C   PRO B 134     -28.599  18.358  38.830  1.00 60.14           C  
ANISOU 2959  C   PRO B 134    11094   3799   7959    956   2217    604       C  
ATOM   2960  O   PRO B 134     -29.228  18.701  37.828  1.00 61.30           O  
ANISOU 2960  O   PRO B 134    11335   3837   8119   1118   2135    852       O  
ATOM   2961  CB  PRO B 134     -29.090  19.415  41.029  1.00 62.21           C  
ANISOU 2961  CB  PRO B 134    11540   3716   8382   1181   2473    325       C  
ATOM   2962  CG  PRO B 134     -30.166  20.349  40.591  1.00 66.38           C  
ANISOU 2962  CG  PRO B 134    12258   3933   9030   1514   2488    547       C  
ATOM   2963  CD  PRO B 134     -29.491  21.411  39.751  1.00 69.39           C  
ANISOU 2963  CD  PRO B 134    13025   3995   9343   1319   2535    640       C  
ATOM   2964  N   TRP B 135     -28.287  17.094  39.101  1.00 58.24           N  
ANISOU 2964  N   TRP B 135    10528   3929   7671    850   2141    488       N  
ATOM   2965  CA  TRP B 135     -28.783  15.983  38.299  1.00 56.37           C  
ANISOU 2965  CA  TRP B 135    10003   3999   7417    935   1961    631       C  
ATOM   2966  C   TRP B 135     -30.285  15.844  38.523  1.00 56.89           C  
ANISOU 2966  C   TRP B 135     9908   4071   7639   1331   1899    765       C  
ATOM   2967  O   TRP B 135     -30.725  15.352  39.561  1.00 55.78           O  
ANISOU 2967  O   TRP B 135     9573   4038   7585   1459   1942    649       O  
ATOM   2968  CB  TRP B 135     -28.054  14.692  38.683  1.00 53.13           C  
ANISOU 2968  CB  TRP B 135     9305   3946   6938    736   1920    449       C  
ATOM   2969  CG  TRP B 135     -28.524  13.471  37.953  1.00 51.22           C  
ANISOU 2969  CG  TRP B 135     8769   4011   6681    803   1746    560       C  
ATOM   2970  CD1 TRP B 135     -29.389  12.524  38.415  1.00 49.68           C  
ANISOU 2970  CD1 TRP B 135     8276   4020   6581   1001   1671    564       C  
ATOM   2971  CD2 TRP B 135     -28.146  13.058  36.633  1.00 50.88           C  
ANISOU 2971  CD2 TRP B 135     8717   4100   6516    658   1632    672       C  
ATOM   2972  NE1 TRP B 135     -29.577  11.549  37.467  1.00 48.42           N  
ANISOU 2972  NE1 TRP B 135     7922   4101   6377    981   1507    664       N  
ATOM   2973  CE2 TRP B 135     -28.826  11.854  36.362  1.00 49.11           C  
ANISOU 2973  CE2 TRP B 135     8187   4153   6322    780   1478    727       C  
ATOM   2974  CE3 TRP B 135     -27.302  13.591  35.654  1.00 52.10           C  
ANISOU 2974  CE3 TRP B 135     9101   4162   6532    429   1657    728       C  
ATOM   2975  CZ2 TRP B 135     -28.687  11.174  35.154  1.00 48.55           C  
ANISOU 2975  CZ2 TRP B 135     8043   4265   6138    687   1339    822       C  
ATOM   2976  CZ3 TRP B 135     -27.167  12.914  34.455  1.00 51.51           C  
ANISOU 2976  CZ3 TRP B 135     8953   4283   6338    346   1532    833       C  
ATOM   2977  CH2 TRP B 135     -27.855  11.718  34.216  1.00 49.75           C  
ANISOU 2977  CH2 TRP B 135     8432   4332   6139    477   1370    872       C  
ATOM   2978  N   ALA B 136     -31.066  16.286  37.541  1.00 92.67           N  
ANISOU 2978  N   ALA B 136    14516   8492  12200   1525   1798   1014       N  
ATOM   2979  CA  ALA B 136     -32.516  16.395  37.691  1.00 92.83           C  
ANISOU 2979  CA  ALA B 136    14406   8473  12392   1921   1746   1157       C  
ATOM   2980  C   ALA B 136     -33.251  15.056  37.641  1.00 92.01           C  
ANISOU 2980  C   ALA B 136    13882   8732  12346   2033   1593   1191       C  
ATOM   2981  O   ALA B 136     -34.474  15.012  37.771  1.00 91.69           O  
ANISOU 2981  O   ALA B 136    13670   8708  12460   2346   1538   1308       O  
ATOM   2982  CB  ALA B 136     -33.083  17.349  36.647  1.00 98.51           C  
ANISOU 2982  CB  ALA B 136    15361   8941  13126   2106   1675   1419       C  
ATOM   2983  N   PHE B 137     -32.510  13.971  37.452  1.00 82.42           N  
ANISOU 2983  N   PHE B 137    12496   7801  11019   1777   1529   1085       N  
ATOM   2984  CA  PHE B 137     -33.116  12.646  37.400  1.00 81.32           C  
ANISOU 2984  CA  PHE B 137    11979   7990  10930   1843   1390   1101       C  
ATOM   2985  C   PHE B 137     -32.820  11.860  38.673  1.00 79.21           C  
ANISOU 2985  C   PHE B 137    11520   7883  10694   1769   1495    882       C  
ATOM   2986  O   PHE B 137     -32.159  12.361  39.582  1.00 78.91           O  
ANISOU 2986  O   PHE B 137    11639   7718  10626   1672   1658    715       O  
ATOM   2987  CB  PHE B 137     -32.632  11.881  36.166  1.00 81.49           C  
ANISOU 2987  CB  PHE B 137    11944   8217  10800   1644   1219   1166       C  
ATOM   2988  CG  PHE B 137     -32.830  12.629  34.877  1.00 83.25           C  
ANISOU 2988  CG  PHE B 137    12390   8295  10946   1692   1113   1386       C  
ATOM   2989  CD1 PHE B 137     -34.066  12.645  34.251  1.00 83.49           C  
ANISOU 2989  CD1 PHE B 137    12311   8350  11063   1965    942   1597       C  
ATOM   2990  CD2 PHE B 137     -31.780  13.317  34.291  1.00 84.36           C  
ANISOU 2990  CD2 PHE B 137    12848   8281  10924   1461   1183   1388       C  
ATOM   2991  CE1 PHE B 137     -34.251  13.333  33.066  1.00 85.09           C  
ANISOU 2991  CE1 PHE B 137    12735   8421  11173   2024    829   1814       C  
ATOM   2992  CE2 PHE B 137     -31.959  14.006  33.106  1.00 85.76           C  
ANISOU 2992  CE2 PHE B 137    13259   8316  11011   1505   1095   1607       C  
ATOM   2993  CZ  PHE B 137     -33.195  14.015  32.493  1.00 86.68           C  
ANISOU 2993  CZ  PHE B 137    13283   8455  11196   1795    910   1825       C  
ATOM   2994  N   GLY B 138     -33.318  10.630  38.739  1.00 63.69           N  
ANISOU 2994  N   GLY B 138     9225   6191   8782   1812   1396    885       N  
ATOM   2995  CA  GLY B 138     -33.099   9.788  39.901  1.00 61.66           C  
ANISOU 2995  CA  GLY B 138     8787   6094   8547   1757   1485    707       C  
ATOM   2996  C   GLY B 138     -31.708   9.189  39.913  1.00 61.84           C  
ANISOU 2996  C   GLY B 138     8846   6243   8407   1440   1493    542       C  
ATOM   2997  O   GLY B 138     -30.897   9.462  39.028  1.00 64.47           O  
ANISOU 2997  O   GLY B 138     9339   6540   8614   1252   1449    556       O  
ATOM   2998  N   ASP B 139     -31.427   8.375  40.924  1.00 85.09           N  
ANISOU 2998  N   ASP B 139    11640   9340  11352   1388   1554    390       N  
ATOM   2999  CA  ASP B 139     -30.153   7.674  41.002  1.00 84.32           C  
ANISOU 2999  CA  ASP B 139    11523   9396  11118   1121   1544    235       C  
ATOM   3000  C   ASP B 139     -30.183   6.487  40.046  1.00 84.87           C  
ANISOU 3000  C   ASP B 139    11389   9696  11162   1049   1380    300       C  
ATOM   3001  O   ASP B 139     -29.178   6.151  39.411  1.00 85.94           O  
ANISOU 3001  O   ASP B 139    11557   9922  11173    833   1333    242       O  
ATOM   3002  CB  ASP B 139     -29.888   7.203  42.433  1.00 81.34           C  
ANISOU 3002  CB  ASP B 139    11069   9097  10738   1118   1652     65       C  
ATOM   3003  CG  ASP B 139     -28.485   6.663  42.619  1.00 80.47           C  
ANISOU 3003  CG  ASP B 139    10966   9120  10490    859   1646   -105       C  
ATOM   3004  OD1 ASP B 139     -27.589   7.062  41.847  1.00 83.35           O  
ANISOU 3004  OD1 ASP B 139    11448   9459  10763    669   1612   -120       O  
ATOM   3005  OD2 ASP B 139     -28.278   5.843  43.538  1.00 77.38           O  
ANISOU 3005  OD2 ASP B 139    10461   8862  10079    850   1679   -220       O  
ATOM   3006  N   ALA B 140     -31.354   5.865  39.944  1.00 63.70           N  
ANISOU 3006  N   ALA B 140     8493   7107   8605   1227   1300    414       N  
ATOM   3007  CA  ALA B 140     -31.567   4.760  39.020  1.00 64.17           C  
ANISOU 3007  CA  ALA B 140     8364   7362   8654   1173   1132    479       C  
ATOM   3008  C   ALA B 140     -31.559   5.266  37.582  1.00 67.19           C  
ANISOU 3008  C   ALA B 140     8883   7690   8956   1133   1010    609       C  
ATOM   3009  O   ALA B 140     -31.291   4.510  36.649  1.00 68.91           O  
ANISOU 3009  O   ALA B 140     9040   8054   9089   1011    884    623       O  
ATOM   3010  CB  ALA B 140     -32.877   4.057  39.329  1.00 72.58           C  
ANISOU 3010  CB  ALA B 140     9164   8524   9889   1363   1081    564       C  
ATOM   3011  N   GLY B 141     -31.861   6.548  37.411  1.00 64.62           N  
ANISOU 3011  N   GLY B 141     8760   7143   8649   1242   1053    707       N  
ATOM   3012  CA  GLY B 141     -31.783   7.180  36.108  1.00 67.13           C  
ANISOU 3012  CA  GLY B 141     9264   7376   8868   1207    957    846       C  
ATOM   3013  C   GLY B 141     -30.335   7.370  35.705  1.00 68.78           C  
ANISOU 3013  C   GLY B 141     9667   7573   8892    925   1018    743       C  
ATOM   3014  O   GLY B 141     -29.981   7.230  34.536  1.00 70.50           O  
ANISOU 3014  O   GLY B 141     9956   7853   8978    805    924    807       O  
ATOM   3015  N   CYS B 142     -29.496   7.685  36.686  1.00 47.61           N  
ANISOU 3015  N   CYS B 142     7068   4823   6199    817   1180    578       N  
ATOM   3016  CA  CYS B 142     -28.066   7.870  36.469  1.00 48.05           C  
ANISOU 3016  CA  CYS B 142     7270   4879   6108    538   1257    454       C  
ATOM   3017  C   CYS B 142     -27.372   6.547  36.156  1.00 48.12           C  
ANISOU 3017  C   CYS B 142     7087   5161   6036    373   1192    349       C  
ATOM   3018  O   CYS B 142     -26.769   6.374  35.083  1.00 49.54           O  
ANISOU 3018  O   CYS B 142     7328   5413   6085    213   1149    370       O  
ATOM   3019  CB  CYS B 142     -27.434   8.508  37.709  1.00 47.29           C  
ANISOU 3019  CB  CYS B 142     7280   4653   6038    480   1424    291       C  
ATOM   3020  SG  CYS B 142     -25.665   8.202  37.898  1.00 46.50           S  
ANISOU 3020  SG  CYS B 142     7192   4670   5806    143   1504     64       S  
ATOM   3021  N   LYS B 143     -27.458   5.620  37.106  1.00 42.46           N  
ANISOU 3021  N   LYS B 143     6152   4588   5392    420   1195    240       N  
ATOM   3022  CA  LYS B 143     -26.874   4.295  36.948  1.00 40.87           C  
ANISOU 3022  CA  LYS B 143     5763   4626   5139    301   1137    138       C  
ATOM   3023  C   LYS B 143     -27.442   3.608  35.714  1.00 43.21           C  
ANISOU 3023  C   LYS B 143     5977   5034   5405    326    980    257       C  
ATOM   3024  O   LYS B 143     -26.720   2.938  34.982  1.00 42.58           O  
ANISOU 3024  O   LYS B 143     5869   5093   5216    174    940    200       O  
ATOM   3025  CB  LYS B 143     -27.131   3.443  38.191  1.00 38.49           C  
ANISOU 3025  CB  LYS B 143     5262   4428   4936    393   1159     44       C  
ATOM   3026  CG  LYS B 143     -26.492   3.982  39.462  1.00 38.47           C  
ANISOU 3026  CG  LYS B 143     5336   4349   4930    359   1296    -97       C  
ATOM   3027  CD  LYS B 143     -26.933   3.184  40.678  1.00 37.37           C  
ANISOU 3027  CD  LYS B 143     5025   4302   4871    480   1319   -156       C  
ATOM   3028  CE  LYS B 143     -26.229   3.658  41.937  1.00 37.53           C  
ANISOU 3028  CE  LYS B 143     5138   4269   4852    436   1437   -309       C  
ATOM   3029  NZ  LYS B 143     -26.627   2.858  43.127  1.00 36.69           N  
ANISOU 3029  NZ  LYS B 143     4894   4254   4794    557   1467   -354       N  
ATOM   3030  N   GLY B 144     -28.739   3.791  35.485  1.00 36.14           N  
ANISOU 3030  N   GLY B 144     5042   4083   4606    523    890    415       N  
ATOM   3031  CA  GLY B 144     -29.397   3.238  34.316  1.00 36.65           C  
ANISOU 3031  CA  GLY B 144     5034   4249   4641    556    714    534       C  
ATOM   3032  C   GLY B 144     -28.880   3.853  33.030  1.00 38.01           C  
ANISOU 3032  C   GLY B 144     5432   4375   4635    433    680    609       C  
ATOM   3033  O   GLY B 144     -28.765   3.174  32.011  1.00 37.95           O  
ANISOU 3033  O   GLY B 144     5398   4505   4515    345    572    618       O  
ATOM   3034  N   TYR B 145     -28.569   5.144  33.082  1.00 42.39           N  
ANISOU 3034  N   TYR B 145     6225   4725   5157    424    783    661       N  
ATOM   3035  CA  TYR B 145     -28.003   5.854  31.940  1.00 43.99           C  
ANISOU 3035  CA  TYR B 145     6681   4852   5183    293    789    744       C  
ATOM   3036  C   TYR B 145     -26.643   5.275  31.562  1.00 42.91           C  
ANISOU 3036  C   TYR B 145     6550   4857   4897     27    861    591       C  
ATOM   3037  O   TYR B 145     -26.436   4.831  30.424  1.00 43.32           O  
ANISOU 3037  O   TYR B 145     6637   5024   4800    -65    785    626       O  
ATOM   3038  CB  TYR B 145     -27.885   7.348  32.262  1.00 45.81           C  
ANISOU 3038  CB  TYR B 145     7172   4802   5433    319    918    809       C  
ATOM   3039  CG  TYR B 145     -27.057   8.157  31.291  1.00 47.52           C  
ANISOU 3039  CG  TYR B 145     7679   4909   5470    132    985    871       C  
ATOM   3040  CD1 TYR B 145     -27.602   8.620  30.101  1.00 49.69           C  
ANISOU 3040  CD1 TYR B 145     8127   5116   5639    202    875   1085       C  
ATOM   3041  CD2 TYR B 145     -25.737   8.479  31.576  1.00 47.26           C  
ANISOU 3041  CD2 TYR B 145     7745   4841   5370   -117   1160    722       C  
ATOM   3042  CE1 TYR B 145     -26.850   9.369  29.215  1.00 51.51           C  
ANISOU 3042  CE1 TYR B 145     8646   5236   5691     25    956   1158       C  
ATOM   3043  CE2 TYR B 145     -24.978   9.227  30.698  1.00 49.08           C  
ANISOU 3043  CE2 TYR B 145     8237   4968   5444   -308   1247    782       C  
ATOM   3044  CZ  TYR B 145     -25.538   9.670  29.518  1.00 51.19           C  
ANISOU 3044  CZ  TYR B 145     8697   5157   5598   -238   1154   1006       C  
ATOM   3045  OH  TYR B 145     -24.783  10.415  28.641  1.00 53.22           O  
ANISOU 3045  OH  TYR B 145     9235   5304   5685   -435   1258   1081       O  
ATOM   3046  N   TYR B 146     -25.720   5.269  32.521  1.00 40.44           N  
ANISOU 3046  N   TYR B 146     6198   4547   4620    -89   1007    415       N  
ATOM   3047  CA  TYR B 146     -24.377   4.750  32.263  1.00 39.64           C  
ANISOU 3047  CA  TYR B 146     6072   4590   4402   -328   1087    259       C  
ATOM   3048  C   TYR B 146     -24.383   3.271  31.862  1.00 38.14           C  
ANISOU 3048  C   TYR B 146     5669   4642   4183   -335    982    189       C  
ATOM   3049  O   TYR B 146     -23.669   2.860  30.935  1.00 38.36           O  
ANISOU 3049  O   TYR B 146     5724   4787   4066   -487    993    146       O  
ATOM   3050  CB  TYR B 146     -23.461   4.991  33.467  1.00 38.88           C  
ANISOU 3050  CB  TYR B 146     5942   4468   4366   -430   1232     80       C  
ATOM   3051  CG  TYR B 146     -22.985   6.423  33.580  1.00 40.72           C  
ANISOU 3051  CG  TYR B 146     6427   4475   4573   -539   1366     98       C  
ATOM   3052  CD1 TYR B 146     -23.728   7.373  34.271  1.00 41.69           C  
ANISOU 3052  CD1 TYR B 146     6671   4371   4801   -389   1394    170       C  
ATOM   3053  CD2 TYR B 146     -21.796   6.827  32.987  1.00 41.74           C  
ANISOU 3053  CD2 TYR B 146     6674   4607   4579   -796   1478     41       C  
ATOM   3054  CE1 TYR B 146     -23.295   8.684  34.372  1.00 43.61           C  
ANISOU 3054  CE1 TYR B 146     7169   4377   5026   -494   1521    179       C  
ATOM   3055  CE2 TYR B 146     -21.356   8.134  33.083  1.00 43.67           C  
ANISOU 3055  CE2 TYR B 146     7157   4627   4809   -922   1609     56       C  
ATOM   3056  CZ  TYR B 146     -22.109   9.058  33.776  1.00 44.59           C  
ANISOU 3056  CZ  TYR B 146     7413   4501   5031   -772   1626    124       C  
ATOM   3057  OH  TYR B 146     -21.671  10.361  33.871  1.00 46.74           O  
ANISOU 3057  OH  TYR B 146     7946   4520   5294   -903   1760    131       O  
ATOM   3058  N   PHE B 147     -25.202   2.483  32.555  1.00 47.15           N  
ANISOU 3058  N   PHE B 147     6607   5848   5463   -172    894    178       N  
ATOM   3059  CA  PHE B 147     -25.365   1.065  32.244  1.00 46.33           C  
ANISOU 3059  CA  PHE B 147     6309   5937   5357   -164    788    119       C  
ATOM   3060  C   PHE B 147     -25.872   0.867  30.821  1.00 49.03           C  
ANISOU 3060  C   PHE B 147     6720   6330   5580   -167    648    235       C  
ATOM   3061  O   PHE B 147     -25.393  -0.010  30.102  1.00 48.29           O  
ANISOU 3061  O   PHE B 147     6588   6382   5379   -270    616    156       O  
ATOM   3062  CB  PHE B 147     -26.320   0.402  33.238  1.00 44.52           C  
ANISOU 3062  CB  PHE B 147     5875   5730   5311     11    728    120       C  
ATOM   3063  CG  PHE B 147     -26.754  -0.979  32.837  1.00 44.48           C  
ANISOU 3063  CG  PHE B 147     5693   5881   5326     31    600     95       C  
ATOM   3064  CD1 PHE B 147     -25.902  -2.059  32.991  1.00 41.34           C  
ANISOU 3064  CD1 PHE B 147     5191   5617   4901    -66    632    -63       C  
ATOM   3065  CD2 PHE B 147     -28.021  -1.200  32.320  1.00 47.87           C  
ANISOU 3065  CD2 PHE B 147     6056   6318   5816    150    443    225       C  
ATOM   3066  CE1 PHE B 147     -26.299  -3.332  32.626  1.00 41.50           C  
ANISOU 3066  CE1 PHE B 147     5074   5750   4947    -52    522    -94       C  
ATOM   3067  CE2 PHE B 147     -28.425  -2.470  31.954  1.00 48.05           C  
ANISOU 3067  CE2 PHE B 147     5922   6471   5864    145    322    189       C  
ATOM   3068  CZ  PHE B 147     -27.562  -3.538  32.108  1.00 44.71           C  
ANISOU 3068  CZ  PHE B 147     5426   6155   5410     41    368     27       C  
ATOM   3069  N   LEU B 148     -26.845   1.683  30.424  1.00 27.08           N  
ANISOU 3069  N   LEU B 148     4047   3430   2813    -41    563    419       N  
ATOM   3070  CA  LEU B 148     -27.377   1.638  29.067  1.00 28.61           C  
ANISOU 3070  CA  LEU B 148     4332   3667   2873    -30    406    550       C  
ATOM   3071  C   LEU B 148     -26.282   1.932  28.051  1.00 30.46           C  
ANISOU 3071  C   LEU B 148     4775   3925   2873   -232    490    526       C  
ATOM   3072  O   LEU B 148     -26.135   1.213  27.058  1.00 31.01           O  
ANISOU 3072  O   LEU B 148     4849   4137   2796   -310    413    496       O  
ATOM   3073  CB  LEU B 148     -28.522   2.637  28.903  1.00 30.53           C  
ANISOU 3073  CB  LEU B 148     4672   3757   3170    155    312    764       C  
ATOM   3074  CG  LEU B 148     -29.096   2.782  27.493  1.00 32.69           C  
ANISOU 3074  CG  LEU B 148     5072   4065   3284    185    129    927       C  
ATOM   3075  CD1 LEU B 148     -29.635   1.452  26.994  1.00 32.20           C  
ANISOU 3075  CD1 LEU B 148     4811   4209   3214    188    -58    875       C  
ATOM   3076  CD2 LEU B 148     -30.177   3.848  27.465  1.00 35.17           C  
ANISOU 3076  CD2 LEU B 148     5469   4216   3678    400     39   1143       C  
ATOM   3077  N   ARG B 149     -25.513   2.987  28.310  1.00 52.20           N  
ANISOU 3077  N   ARG B 149     7703   6536   5592   -324    659    530       N  
ATOM   3078  CA  ARG B 149     -24.415   3.359  27.422  1.00 52.63           C  
ANISOU 3078  CA  ARG B 149     7955   6603   5438   -538    779    511       C  
ATOM   3079  C   ARG B 149     -23.412   2.222  27.227  1.00 49.81           C  
ANISOU 3079  C   ARG B 149     7461   6456   5006   -694    843    310       C  
ATOM   3080  O   ARG B 149     -23.126   1.817  26.092  1.00 49.15           O  
ANISOU 3080  O   ARG B 149     7459   6483   4733   -789    822    311       O  
ATOM   3081  CB  ARG B 149     -23.699   4.608  27.938  1.00 53.06           C  
ANISOU 3081  CB  ARG B 149     8180   6467   5513   -638    969    514       C  
ATOM   3082  CG  ARG B 149     -24.537   5.873  27.872  1.00 54.77           C  
ANISOU 3082  CG  ARG B 149     8614   6440   5754   -505    935    727       C  
ATOM   3083  CD  ARG B 149     -23.701   7.100  28.190  1.00 54.89           C  
ANISOU 3083  CD  ARG B 149     8843   6251   5762   -652   1139    718       C  
ATOM   3084  NE  ARG B 149     -22.590   7.264  27.257  1.00 54.65           N  
ANISOU 3084  NE  ARG B 149     8967   6266   5531   -910   1269    695       N  
ATOM   3085  CZ  ARG B 149     -22.663   7.951  26.122  1.00 55.88           C  
ANISOU 3085  CZ  ARG B 149     9402   6323   5507   -959   1275    877       C  
ATOM   3086  NH1 ARG B 149     -23.798   8.542  25.773  1.00 55.72           N  
ANISOU 3086  NH1 ARG B 149     9532   6152   5487   -751   1135   1100       N  
ATOM   3087  NH2 ARG B 149     -21.600   8.046  25.335  1.00 57.10           N  
ANISOU 3087  NH2 ARG B 149     9683   6533   5479  -1208   1424    843       N  
ATOM   3088  N   GLU B 150     -22.886   1.699  28.332  1.00 62.08           N  
ANISOU 3088  N   GLU B 150     8817   8067   6704   -708    920    140       N  
ATOM   3089  CA  GLU B 150     -21.884   0.639  28.243  1.00 59.38           C  
ANISOU 3089  CA  GLU B 150     8334   7914   6313   -830    986    -52       C  
ATOM   3090  C   GLU B 150     -22.430  -0.659  27.640  1.00 59.54           C  
ANISOU 3090  C   GLU B 150     8239   8083   6298   -762    833    -82       C  
ATOM   3091  O   GLU B 150     -21.751  -1.316  26.846  1.00 58.26           O  
ANISOU 3091  O   GLU B 150     8086   8053   5996   -871    870   -176       O  
ATOM   3092  CB  GLU B 150     -21.215   0.388  29.598  1.00 58.03           C  
ANISOU 3092  CB  GLU B 150     7983   7770   6296   -843   1082   -216       C  
ATOM   3093  CG  GLU B 150     -20.274   1.506  30.020  1.00 59.01           C  
ANISOU 3093  CG  GLU B 150     8214   7795   6411   -992   1255   -253       C  
ATOM   3094  CD  GLU B 150     -19.069   1.000  30.792  1.00 56.61           C  
ANISOU 3094  CD  GLU B 150     7729   7619   6159  -1097   1362   -464       C  
ATOM   3095  OE1 GLU B 150     -19.086  -0.171  31.225  1.00 54.53           O  
ANISOU 3095  OE1 GLU B 150     7262   7489   5966  -1009   1297   -565       O  
ATOM   3096  OE2 GLU B 150     -18.101   1.772  30.956  1.00 56.34           O  
ANISOU 3096  OE2 GLU B 150     7755   7551   6099  -1269   1505   -527       O  
ATOM   3097  N   ALA B 151     -23.656  -1.021  28.006  1.00 53.68           N  
ANISOU 3097  N   ALA B 151     7393   7317   5688   -588    671     -7       N  
ATOM   3098  CA  ALA B 151     -24.297  -2.197  27.425  1.00 54.67           C  
ANISOU 3098  CA  ALA B 151     7418   7561   5794   -537    509    -29       C  
ATOM   3099  C   ALA B 151     -24.388  -2.044  25.911  1.00 56.51           C  
ANISOU 3099  C   ALA B 151     7846   7838   5790   -607    435     51       C  
ATOM   3100  O   ALA B 151     -24.090  -2.977  25.157  1.00 56.04           O  
ANISOU 3100  O   ALA B 151     7776   7909   5609   -679    406    -52       O  
ATOM   3101  CB  ALA B 151     -25.676  -2.408  28.024  1.00 56.17           C  
ANISOU 3101  CB  ALA B 151     7470   7705   6170   -355    353     65       C  
ATOM   3102  N   CYS B 152     -24.786  -0.852  25.473  1.00 45.74           N  
ANISOU 3102  N   CYS B 152     6676   6354   4349   -580    411    234       N  
ATOM   3103  CA  CYS B 152     -24.881  -0.557  24.049  1.00 47.12           C  
ANISOU 3103  CA  CYS B 152     7075   6557   4270   -640    341    340       C  
ATOM   3104  C   CYS B 152     -23.533  -0.645  23.338  1.00 46.29           C  
ANISOU 3104  C   CYS B 152     7095   6536   3957   -846    527    226       C  
ATOM   3105  O   CYS B 152     -23.447  -1.196  22.238  1.00 47.47           O  
ANISOU 3105  O   CYS B 152     7332   6804   3901   -910    474    198       O  
ATOM   3106  CB  CYS B 152     -25.514   0.817  23.816  1.00 49.25           C  
ANISOU 3106  CB  CYS B 152     7549   6656   4508   -556    295    576       C  
ATOM   3107  SG  CYS B 152     -27.319   0.834  23.930  1.00 52.13           S  
ANISOU 3107  SG  CYS B 152     7805   6986   5015   -303      4    752       S  
ATOM   3108  N   THR B 153     -22.480  -0.112  23.956  1.00 44.12           N  
ANISOU 3108  N   THR B 153     6822   6209   3731   -955    747    152       N  
ATOM   3109  CA  THR B 153     -21.165  -0.154  23.313  1.00 45.00           C  
ANISOU 3109  CA  THR B 153     7020   6412   3665  -1158    947     42       C  
ATOM   3110  C   THR B 153     -20.605  -1.582  23.222  1.00 43.92           C  
ANISOU 3110  C   THR B 153     6700   6468   3520  -1192    966   -177       C  
ATOM   3111  O   THR B 153     -20.020  -1.962  22.198  1.00 45.25           O  
ANISOU 3111  O   THR B 153     6964   6751   3478  -1303   1038   -242       O  
ATOM   3112  CB  THR B 153     -20.144   0.839  23.944  1.00 45.15           C  
ANISOU 3112  CB  THR B 153     7079   6333   3741  -1294   1177     14       C  
ATOM   3113  OG1 THR B 153     -18.992   0.946  23.099  1.00 46.77           O  
ANISOU 3113  OG1 THR B 153     7402   6620   3747  -1502   1369    -44       O  
ATOM   3114  CG2 THR B 153     -19.709   0.401  25.330  1.00 42.87           C  
ANISOU 3114  CG2 THR B 153     6526   6077   3685  -1268   1233   -157       C  
ATOM   3115  N   TYR B 154     -20.809  -2.376  24.273  1.00 40.22           N  
ANISOU 3115  N   TYR B 154     5984   6026   3272  -1087    909   -286       N  
ATOM   3116  CA  TYR B 154     -20.411  -3.782  24.239  1.00 39.31           C  
ANISOU 3116  CA  TYR B 154     5704   6061   3173  -1084    906   -479       C  
ATOM   3117  C   TYR B 154     -21.176  -4.527  23.148  1.00 40.38           C  
ANISOU 3117  C   TYR B 154     5919   6263   3161  -1051    733   -458       C  
ATOM   3118  O   TYR B 154     -20.597  -5.317  22.394  1.00 41.13           O  
ANISOU 3118  O   TYR B 154     6039   6478   3110  -1124    786   -593       O  
ATOM   3119  CB  TYR B 154     -20.641  -4.463  25.592  1.00 37.03           C  
ANISOU 3119  CB  TYR B 154     5165   5760   3145   -962    859   -563       C  
ATOM   3120  CG  TYR B 154     -19.605  -4.136  26.646  1.00 36.07           C  
ANISOU 3120  CG  TYR B 154     4930   5635   3141  -1010   1029   -660       C  
ATOM   3121  CD1 TYR B 154     -18.275  -4.501  26.479  1.00 36.41           C  
ANISOU 3121  CD1 TYR B 154     4910   5800   3126  -1125   1197   -825       C  
ATOM   3122  CD2 TYR B 154     -19.961  -3.484  27.818  1.00 35.06           C  
ANISOU 3122  CD2 TYR B 154     4748   5392   3181   -937   1019   -595       C  
ATOM   3123  CE1 TYR B 154     -17.328  -4.209  27.445  1.00 36.07           C  
ANISOU 3123  CE1 TYR B 154     4741   5773   3193  -1173   1326   -919       C  
ATOM   3124  CE2 TYR B 154     -19.024  -3.186  28.787  1.00 34.43           C  
ANISOU 3124  CE2 TYR B 154     4572   5318   3192   -989   1152   -694       C  
ATOM   3125  CZ  TYR B 154     -17.710  -3.551  28.597  1.00 34.82           C  
ANISOU 3125  CZ  TYR B 154     4546   5499   3186  -1110   1293   -854       C  
ATOM   3126  OH  TYR B 154     -16.777  -3.256  29.564  1.00 35.00           O  
ANISOU 3126  OH  TYR B 154     4452   5545   3302  -1165   1400   -957       O  
ATOM   3127  N   ALA B 155     -22.479  -4.263  23.069  1.00 48.24           N  
ANISOU 3127  N   ALA B 155     6951   7185   4194   -938    525   -298       N  
ATOM   3128  CA  ALA B 155     -23.329  -4.880  22.055  1.00 50.23           C  
ANISOU 3128  CA  ALA B 155     7273   7501   4309   -910    320   -267       C  
ATOM   3129  C   ALA B 155     -22.843  -4.555  20.645  1.00 50.90           C  
ANISOU 3129  C   ALA B 155     7621   7653   4066  -1035    373   -242       C  
ATOM   3130  O   ALA B 155     -22.729  -5.443  19.796  1.00 50.13           O  
ANISOU 3130  O   ALA B 155     7569   7671   3808  -1085    334   -360       O  
ATOM   3131  CB  ALA B 155     -24.773  -4.437  22.235  1.00 53.02           C  
ANISOU 3131  CB  ALA B 155     7609   7770   4767   -768     94    -75       C  
ATOM   3132  N   THR B 156     -22.554  -3.278  20.407  1.00 51.75           N  
ANISOU 3132  N   THR B 156     7917   7676   4068  -1089    475    -92       N  
ATOM   3133  CA  THR B 156     -22.064  -2.827  19.108  1.00 52.10           C  
ANISOU 3133  CA  THR B 156     8241   7767   3787  -1217    556    -38       C  
ATOM   3134  C   THR B 156     -20.740  -3.495  18.744  1.00 50.78           C  
ANISOU 3134  C   THR B 156     8056   7735   3504  -1365    787   -255       C  
ATOM   3135  O   THR B 156     -20.574  -3.989  17.625  1.00 52.53           O  
ANISOU 3135  O   THR B 156     8418   8069   3472  -1429    782   -315       O  
ATOM   3136  CB  THR B 156     -21.896  -1.295  19.069  1.00 53.32           C  
ANISOU 3136  CB  THR B 156     8604   7772   3881  -1261    662    167       C  
ATOM   3137  OG1 THR B 156     -23.173  -0.667  19.235  1.00 55.12           O  
ANISOU 3137  OG1 THR B 156     8874   7880   4190  -1098    438    378       O  
ATOM   3138  CG2 THR B 156     -21.293  -0.855  17.744  1.00 54.79           C  
ANISOU 3138  CG2 THR B 156     9093   8006   3718  -1411    781    227       C  
ATOM   3139  N   ALA B 157     -19.806  -3.513  19.692  1.00 42.82           N  
ANISOU 3139  N   ALA B 157     6870   6722   2679  -1409    984   -379       N  
ATOM   3140  CA  ALA B 157     -18.508  -4.148  19.466  1.00 44.35           C  
ANISOU 3140  CA  ALA B 157     6994   7052   2806  -1526   1210   -592       C  
ATOM   3141  C   ALA B 157     -18.661  -5.625  19.097  1.00 44.30           C  
ANISOU 3141  C   ALA B 157     6896   7167   2771  -1467   1116   -773       C  
ATOM   3142  O   ALA B 157     -18.122  -6.089  18.080  1.00 47.00           O  
ANISOU 3142  O   ALA B 157     7350   7623   2885  -1550   1216   -881       O  
ATOM   3143  CB  ALA B 157     -17.621  -3.993  20.693  1.00 42.96           C  
ANISOU 3143  CB  ALA B 157     6594   6859   2870  -1551   1379   -694       C  
ATOM   3144  N   LEU B 158     -19.408  -6.353  19.924  1.00 46.93           N  
ANISOU 3144  N   LEU B 158     7039   7462   3333  -1327    937   -808       N  
ATOM   3145  CA  LEU B 158     -19.651  -7.774  19.693  1.00 46.40           C  
ANISOU 3145  CA  LEU B 158     6885   7469   3276  -1272    837   -975       C  
ATOM   3146  C   LEU B 158     -20.304  -8.026  18.337  1.00 48.59           C  
ANISOU 3146  C   LEU B 158     7385   7800   3277  -1303    688   -945       C  
ATOM   3147  O   LEU B 158     -19.950  -8.977  17.639  1.00 49.64           O  
ANISOU 3147  O   LEU B 158     7564   8028   3272  -1340    724  -1120       O  
ATOM   3148  CB  LEU B 158     -20.512  -8.367  20.811  1.00 45.73           C  
ANISOU 3148  CB  LEU B 158     6584   7309   3485  -1131    663   -973       C  
ATOM   3149  CG  LEU B 158     -19.851  -8.493  22.185  1.00 43.86           C  
ANISOU 3149  CG  LEU B 158     6116   7044   3507  -1082    791  -1051       C  
ATOM   3150  CD1 LEU B 158     -20.797  -9.156  23.175  1.00 44.16           C  
ANISOU 3150  CD1 LEU B 158     5973   7008   3798   -946    623  -1037       C  
ATOM   3151  CD2 LEU B 158     -18.545  -9.265  22.084  1.00 42.21           C  
ANISOU 3151  CD2 LEU B 158     5829   6941   3268  -1127    990  -1270       C  
ATOM   3152  N   ASN B 159     -21.253  -7.171  17.967  1.00 70.94           N  
ANISOU 3152  N   ASN B 159    10362  10569   6021  -1280    515   -728       N  
ATOM   3153  CA  ASN B 159     -21.911  -7.286  16.669  1.00 72.97           C  
ANISOU 3153  CA  ASN B 159    10845  10887   5991  -1307    342   -676       C  
ATOM   3154  C   ASN B 159     -20.950  -7.055  15.505  1.00 73.02           C  
ANISOU 3154  C   ASN B 159    11102  10990   5652  -1448    542   -723       C  
ATOM   3155  O   ASN B 159     -21.027  -7.738  14.484  1.00 73.69           O  
ANISOU 3155  O   ASN B 159    11326  11174   5498  -1488    482   -827       O  
ATOM   3156  CB  ASN B 159     -23.101  -6.330  16.573  1.00 75.89           C  
ANISOU 3156  CB  ASN B 159    11307  11175   6353  -1229    112   -412       C  
ATOM   3157  CG  ASN B 159     -24.272  -6.769  17.429  1.00 77.25           C  
ANISOU 3157  CG  ASN B 159    11247  11292   6813  -1092   -128   -382       C  
ATOM   3158  OD1 ASN B 159     -24.502  -7.963  17.620  1.00 76.55           O  
ANISOU 3158  OD1 ASN B 159    11006  11246   6832  -1075   -206   -549       O  
ATOM   3159  ND2 ASN B 159     -25.020  -5.803  17.949  1.00 78.68           N  
ANISOU 3159  ND2 ASN B 159    11401  11368   7124   -992   -234   -169       N  
ATOM   3160  N   VAL B 160     -20.046  -6.091  15.664  1.00 51.08           N  
ANISOU 3160  N   VAL B 160     8383   8181   2845  -1533    787   -652       N  
ATOM   3161  CA  VAL B 160     -19.045  -5.813  14.639  1.00 54.82           C  
ANISOU 3161  CA  VAL B 160     9073   8745   3009  -1684   1029   -692       C  
ATOM   3162  C   VAL B 160     -18.112  -7.006  14.439  1.00 55.83           C  
ANISOU 3162  C   VAL B 160     9096   9006   3112  -1724   1204   -981       C  
ATOM   3163  O   VAL B 160     -17.915  -7.472  13.309  1.00 58.66           O  
ANISOU 3163  O   VAL B 160     9619   9451   3220  -1764   1234  -1060       O  
ATOM   3164  CB  VAL B 160     -18.218  -4.554  14.974  1.00 55.33           C  
ANISOU 3164  CB  VAL B 160     9183   8740   3102  -1791   1280   -576       C  
ATOM   3165  CG1 VAL B 160     -16.987  -4.469  14.085  1.00 58.84           C  
ANISOU 3165  CG1 VAL B 160     9752   9285   3320  -1945   1575   -662       C  
ATOM   3166  CG2 VAL B 160     -19.073  -3.304  14.831  1.00 55.61           C  
ANISOU 3166  CG2 VAL B 160     9418   8633   3078  -1761   1138   -280       C  
ATOM   3167  N   VAL B 161     -17.548  -7.506  15.537  1.00 53.39           N  
ANISOU 3167  N   VAL B 161     8495   8688   3105  -1676   1304  -1124       N  
ATOM   3168  CA  VAL B 161     -16.661  -8.666  15.468  1.00 54.07           C  
ANISOU 3168  CA  VAL B 161     8437   8863   3243  -1660   1453  -1381       C  
ATOM   3169  C   VAL B 161     -17.379  -9.874  14.865  1.00 54.71           C  
ANISOU 3169  C   VAL B 161     8581   8980   3228  -1595   1259  -1511       C  
ATOM   3170  O   VAL B 161     -16.837 -10.573  14.000  1.00 56.59           O  
ANISOU 3170  O   VAL B 161     8870   9256   3375  -1581   1336  -1637       O  
ATOM   3171  CB  VAL B 161     -16.110  -9.042  16.855  1.00 51.45           C  
ANISOU 3171  CB  VAL B 161     7783   8513   3254  -1592   1540  -1494       C  
ATOM   3172  CG1 VAL B 161     -15.133 -10.203  16.742  1.00 51.91           C  
ANISOU 3172  CG1 VAL B 161     7679   8609   3435  -1517   1654  -1705       C  
ATOM   3173  CG2 VAL B 161     -15.438  -7.842  17.494  1.00 50.98           C  
ANISOU 3173  CG2 VAL B 161     7655   8413   3304  -1668   1707  -1383       C  
ATOM   3174  N   SER B 162     -18.607 -10.103  15.321  1.00 66.72           N  
ANISOU 3174  N   SER B 162    10052  10429   4871  -1511    974  -1438       N  
ATOM   3175  CA  SER B 162     -19.424 -11.201  14.819  1.00 67.37           C  
ANISOU 3175  CA  SER B 162    10178  10524   4896  -1467    751  -1550       C  
ATOM   3176  C   SER B 162     -19.670 -11.071  13.319  1.00 68.60           C  
ANISOU 3176  C   SER B 162    10656  10768   4643  -1555    687  -1532       C  
ATOM   3177  O   SER B 162     -19.697 -12.068  12.599  1.00 68.39           O  
ANISOU 3177  O   SER B 162    10699  10777   4509  -1548    638  -1702       O  
ATOM   3178  CB  SER B 162     -20.758 -11.265  15.564  1.00 66.12           C  
ANISOU 3178  CB  SER B 162     9883  10261   4981  -1367    451  -1425       C  
ATOM   3179  OG  SER B 162     -21.543 -12.350  15.104  1.00 67.79           O  
ANISOU 3179  OG  SER B 162    10122  10483   5154  -1351    232  -1540       O  
ATOM   3180  N   LEU B 163     -19.848  -9.838  12.853  1.00 58.22           N  
ANISOU 3180  N   LEU B 163     9532   9452   3140  -1609    678  -1305       N  
ATOM   3181  CA  LEU B 163     -20.021  -9.585  11.426  1.00 61.91           C  
ANISOU 3181  CA  LEU B 163    10306   9981   3237  -1664    619  -1240       C  
ATOM   3182  C   LEU B 163     -18.738  -9.858  10.654  1.00 63.86           C  
ANISOU 3182  C   LEU B 163    10593  10264   3408  -1684    908  -1362       C  
ATOM   3183  O   LEU B 163     -18.780 -10.313   9.511  1.00 66.56           O  
ANISOU 3183  O   LEU B 163    11106  10657   3526  -1681    864  -1429       O  
ATOM   3184  CB  LEU B 163     -20.495  -8.153  11.176  1.00 62.93           C  
ANISOU 3184  CB  LEU B 163    10642  10079   3191  -1703    545   -941       C  
ATOM   3185  CG  LEU B 163     -22.007  -7.944  11.239  1.00 62.00           C  
ANISOU 3185  CG  LEU B 163    10526   9907   3125  -1604    151   -762       C  
ATOM   3186  CD1 LEU B 163     -22.362  -6.496  10.950  1.00 63.18           C  
ANISOU 3186  CD1 LEU B 163    10877   9991   3138  -1598    100   -450       C  
ATOM   3187  CD2 LEU B 163     -22.707  -8.877  10.265  1.00 64.66           C  
ANISOU 3187  CD2 LEU B 163    10990  10342   3233  -1612    -98   -882       C  
ATOM   3188  N   SER B 164     -17.598  -9.575  11.278  1.00 67.24           N  
ANISOU 3188  N   SER B 164    10853  10672   4023  -1703   1193  -1393       N  
ATOM   3189  CA  SER B 164     -16.311  -9.888  10.664  1.00 68.87           C  
ANISOU 3189  CA  SER B 164    11040  10923   4204  -1715   1466  -1519       C  
ATOM   3190  C   SER B 164     -16.149 -11.397  10.493  1.00 68.95           C  
ANISOU 3190  C   SER B 164    10960  10956   4282  -1626   1445  -1773       C  
ATOM   3191  O   SER B 164     -15.714 -11.872   9.439  1.00 72.22           O  
ANISOU 3191  O   SER B 164    11504  11421   4517  -1620   1527  -1871       O  
ATOM   3192  CB  SER B 164     -15.160  -9.318  11.494  1.00 66.61           C  
ANISOU 3192  CB  SER B 164    10542  10616   4150  -1753   1734  -1506       C  
ATOM   3193  OG  SER B 164     -15.199  -7.901  11.514  1.00 67.03           O  
ANISOU 3193  OG  SER B 164    10716  10627   4126  -1851   1784  -1278       O  
ATOM   3194  N   VAL B 165     -16.510 -12.144  11.533  1.00 65.27           N  
ANISOU 3194  N   VAL B 165    10285  10442   4071  -1554   1338  -1878       N  
ATOM   3195  CA  VAL B 165     -16.454 -13.602  11.483  1.00 65.52           C  
ANISOU 3195  CA  VAL B 165    10243  10457   4192  -1465   1300  -2108       C  
ATOM   3196  C   VAL B 165     -17.397 -14.153  10.413  1.00 68.34           C  
ANISOU 3196  C   VAL B 165    10841  10830   4294  -1475   1070  -2155       C  
ATOM   3197  O   VAL B 165     -17.009 -15.000   9.601  1.00 70.92           O  
ANISOU 3197  O   VAL B 165    11255  11171   4518  -1440   1128  -2317       O  
ATOM   3198  CB  VAL B 165     -16.818 -14.225  12.842  1.00 62.69           C  
ANISOU 3198  CB  VAL B 165     9635  10029   4153  -1392   1205  -2184       C  
ATOM   3199  CG1 VAL B 165     -16.730 -15.739  12.771  1.00 63.00           C  
ANISOU 3199  CG1 VAL B 165     9623  10021   4291  -1300   1180  -2413       C  
ATOM   3200  CG2 VAL B 165     -15.905 -13.687  13.932  1.00 60.84           C  
ANISOU 3200  CG2 VAL B 165     9160   9788   4169  -1373   1404  -2140       C  
ATOM   3201  N   GLU B 166     -18.633 -13.661  10.421  1.00 73.07           N  
ANISOU 3201  N   GLU B 166    11541  11429   4793  -1518    799  -2013       N  
ATOM   3202  CA  GLU B 166     -19.639 -14.056   9.440  1.00 75.62           C  
ANISOU 3202  CA  GLU B 166    12071  11778   4882  -1534    526  -2033       C  
ATOM   3203  C   GLU B 166     -19.166 -13.794   8.017  1.00 78.92           C  
ANISOU 3203  C   GLU B 166    12745  12269   4970  -1560    627  -2020       C  
ATOM   3204  O   GLU B 166     -19.390 -14.608   7.121  1.00 81.64           O  
ANISOU 3204  O   GLU B 166    13225  12637   5156  -1544    532  -2162       O  
ATOM   3205  CB  GLU B 166     -20.954 -13.314   9.691  1.00 73.80           C  
ANISOU 3205  CB  GLU B 166    11886  11553   4602  -1571    219  -1831       C  
ATOM   3206  CG  GLU B 166     -21.780 -13.860  10.845  1.00 71.75           C  
ANISOU 3206  CG  GLU B 166    11403  11238   4619  -1550     23  -1879       C  
ATOM   3207  CD  GLU B 166     -22.538 -15.121  10.478  1.00 72.96           C  
ANISOU 3207  CD  GLU B 166    11565  11369   4785  -1545   -217  -2057       C  
ATOM   3208  OE1 GLU B 166     -22.488 -15.527   9.298  1.00 76.03           O  
ANISOU 3208  OE1 GLU B 166    12150  11792   4946  -1552   -251  -2141       O  
ATOM   3209  OE2 GLU B 166     -23.188 -15.705  11.370  1.00 72.26           O  
ANISOU 3209  OE2 GLU B 166    11288  11228   4939  -1540   -370  -2116       O  
ATOM   3210  N   LEU B 167     -18.511 -12.656   7.813  1.00 70.77           N  
ANISOU 3210  N   LEU B 167    11782  11270   3836  -1607    823  -1852       N  
ATOM   3211  CA  LEU B 167     -18.012 -12.298   6.493  1.00 74.42           C  
ANISOU 3211  CA  LEU B 167    12485  11807   3983  -1642    949  -1816       C  
ATOM   3212  C   LEU B 167     -16.862 -13.211   6.079  1.00 75.84           C  
ANISOU 3212  C   LEU B 167    12619  12013   4184  -1603   1208  -2043       C  
ATOM   3213  O   LEU B 167     -16.787 -13.635   4.922  1.00 79.11           O  
ANISOU 3213  O   LEU B 167    13228  12487   4342  -1596   1210  -2133       O  
ATOM   3214  CB  LEU B 167     -17.575 -10.833   6.451  1.00 74.78           C  
ANISOU 3214  CB  LEU B 167    12606  11858   3950  -1715   1111  -1572       C  
ATOM   3215  CG  LEU B 167     -17.321 -10.268   5.052  1.00 78.85           C  
ANISOU 3215  CG  LEU B 167    13413  12446   4099  -1762   1183  -1470       C  
ATOM   3216  CD1 LEU B 167     -18.559 -10.419   4.183  1.00 80.96           C  
ANISOU 3216  CD1 LEU B 167    13908  12757   4098  -1737    836  -1414       C  
ATOM   3217  CD2 LEU B 167     -16.896  -8.813   5.128  1.00 79.12           C  
ANISOU 3217  CD2 LEU B 167    13512  12450   4100  -1843   1351  -1223       C  
ATOM   3218  N   TYR B 168     -15.972 -13.515   7.023  1.00 73.62           N  
ANISOU 3218  N   TYR B 168    12077  11691   4204  -1567   1417  -2135       N  
ATOM   3219  CA  TYR B 168     -14.875 -14.438   6.743  1.00 74.95           C  
ANISOU 3219  CA  TYR B 168    12172  11879   4428  -1504   1648  -2347       C  
ATOM   3220  C   TYR B 168     -15.410 -15.794   6.313  1.00 76.06           C  
ANISOU 3220  C   TYR B 168    12389  11989   4521  -1430   1484  -2559       C  
ATOM   3221  O   TYR B 168     -14.950 -16.364   5.326  1.00 79.11           O  
ANISOU 3221  O   TYR B 168    12911  12419   4727  -1401   1588  -2696       O  
ATOM   3222  CB  TYR B 168     -13.950 -14.610   7.952  1.00 72.32           C  
ANISOU 3222  CB  TYR B 168    11518  11505   4455  -1455   1841  -2404       C  
ATOM   3223  CG  TYR B 168     -12.768 -15.520   7.672  1.00 73.97           C  
ANISOU 3223  CG  TYR B 168    11639  11738   4727  -1372   2079  -2603       C  
ATOM   3224  CD1 TYR B 168     -12.862 -16.896   7.850  1.00 73.84           C  
ANISOU 3224  CD1 TYR B 168    11571  11660   4826  -1257   2014  -2813       C  
ATOM   3225  CD2 TYR B 168     -11.562 -15.003   7.219  1.00 75.91           C  
ANISOU 3225  CD2 TYR B 168    11857  12064   4921  -1410   2368  -2579       C  
ATOM   3226  CE1 TYR B 168     -11.791 -17.728   7.585  1.00 75.60           C  
ANISOU 3226  CE1 TYR B 168    11727  11898   5102  -1163   2229  -2986       C  
ATOM   3227  CE2 TYR B 168     -10.484 -15.829   6.956  1.00 77.68           C  
ANISOU 3227  CE2 TYR B 168    11992  12322   5202  -1324   2583  -2756       C  
ATOM   3228  CZ  TYR B 168     -10.603 -17.188   7.142  1.00 77.52           C  
ANISOU 3228  CZ  TYR B 168    11929  12237   5287  -1191   2512  -2957       C  
ATOM   3229  OH  TYR B 168      -9.532 -18.011   6.881  1.00 79.51           O  
ANISOU 3229  OH  TYR B 168    12102  12517   5593  -1087   2727  -3127       O  
ATOM   3230  N   LEU B 169     -16.379 -16.311   7.061  1.00 88.13           N  
ANISOU 3230  N   LEU B 169    13830  13438   6217  -1406   1234  -2593       N  
ATOM   3231  CA  LEU B 169     -16.967 -17.604   6.736  1.00 89.52           C  
ANISOU 3231  CA  LEU B 169    14075  13560   6381  -1356   1059  -2797       C  
ATOM   3232  C   LEU B 169     -17.743 -17.551   5.423  1.00 93.49           C  
ANISOU 3232  C   LEU B 169    14872  14130   6523  -1406    857  -2789       C  
ATOM   3233  O   LEU B 169     -17.835 -18.548   4.709  1.00 96.45           O  
ANISOU 3233  O   LEU B 169    15368  14491   6787  -1373    801  -2982       O  
ATOM   3234  CB  LEU B 169     -17.864 -18.092   7.875  1.00 85.46           C  
ANISOU 3234  CB  LEU B 169    13385  12941   6145  -1340    840  -2822       C  
ATOM   3235  CG  LEU B 169     -17.141 -18.412   9.185  1.00 83.15           C  
ANISOU 3235  CG  LEU B 169    12803  12577   6215  -1264   1016  -2869       C  
ATOM   3236  CD1 LEU B 169     -18.108 -18.982  10.211  1.00 81.58           C  
ANISOU 3236  CD1 LEU B 169    12458  12275   6264  -1251    794  -2903       C  
ATOM   3237  CD2 LEU B 169     -15.985 -19.370   8.938  1.00 84.09           C  
ANISOU 3237  CD2 LEU B 169    12886  12673   6392  -1164   1260  -3063       C  
ATOM   3238  N   ALA B 170     -18.288 -16.381   5.104  1.00 78.63           N  
ANISOU 3238  N   ALA B 170    13108  12316   4452  -1479    744  -2562       N  
ATOM   3239  CA  ALA B 170     -19.047 -16.204   3.870  1.00 82.02           C  
ANISOU 3239  CA  ALA B 170    13810  12826   4526  -1517    531  -2519       C  
ATOM   3240  C   ALA B 170     -18.140 -16.197   2.641  1.00 85.81           C  
ANISOU 3240  C   ALA B 170    14492  13398   4715  -1514    761  -2582       C  
ATOM   3241  O   ALA B 170     -18.518 -16.695   1.581  1.00 89.11           O  
ANISOU 3241  O   ALA B 170    15116  13871   4872  -1512    631  -2685       O  
ATOM   3242  CB  ALA B 170     -19.871 -14.926   3.929  1.00 81.52           C  
ANISOU 3242  CB  ALA B 170    13814  12802   4358  -1574    342  -2234       C  
ATOM   3243  N   ILE B 171     -16.945 -15.633   2.788  1.00 85.56           N  
ANISOU 3243  N   ILE B 171    14390  13388   4729  -1520   1101  -2524       N  
ATOM   3244  CA  ILE B 171     -16.009 -15.540   1.671  1.00 89.25           C  
ANISOU 3244  CA  ILE B 171    15026  13950   4934  -1526   1353  -2567       C  
ATOM   3245  C   ILE B 171     -15.151 -16.796   1.515  1.00 90.36           C  
ANISOU 3245  C   ILE B 171    15102  14073   5159  -1439   1545  -2846       C  
ATOM   3246  O   ILE B 171     -15.084 -17.382   0.434  1.00 93.94           O  
ANISOU 3246  O   ILE B 171    15754  14584   5356  -1416   1555  -2988       O  
ATOM   3247  CB  ILE B 171     -15.087 -14.313   1.808  1.00 89.06           C  
ANISOU 3247  CB  ILE B 171    14957  13964   4916  -1591   1637  -2372       C  
ATOM   3248  CG1 ILE B 171     -15.916 -13.027   1.850  1.00 88.53           C  
ANISOU 3248  CG1 ILE B 171    15002  13899   4735  -1667   1458  -2084       C  
ATOM   3249  CG2 ILE B 171     -14.086 -14.266   0.664  1.00 93.11           C  
ANISOU 3249  CG2 ILE B 171    15627  14580   5170  -1605   1916  -2424       C  
ATOM   3250  CD1 ILE B 171     -15.096 -11.780   2.096  1.00 88.08           C  
ANISOU 3250  CD1 ILE B 171    14897  13841   4729  -1745   1716  -1884       C  
ATOM   3251  N   ARG B 172     -14.500 -17.202   2.600  1.00105.16           N  
ANISOU 3251  N   ARG B 172    16701  15868   7387  -1383   1693  -2920       N  
ATOM   3252  CA  ARG B 172     -13.589 -18.344   2.580  1.00106.57           C  
ANISOU 3252  CA  ARG B 172    16793  16018   7681  -1277   1893  -3161       C  
ATOM   3253  C   ARG B 172     -14.310 -19.666   2.324  1.00107.72           C  
ANISOU 3253  C   ARG B 172    17037  16085   7809  -1213   1678  -3382       C  
ATOM   3254  O   ARG B 172     -13.840 -20.495   1.544  1.00111.76           O  
ANISOU 3254  O   ARG B 172    17664  16611   8188  -1148   1788  -3578       O  
ATOM   3255  CB  ARG B 172     -12.800 -18.414   3.890  1.00105.72           C  
ANISOU 3255  CB  ARG B 172    16354  15845   7969  -1222   2063  -3162       C  
ATOM   3256  CG  ARG B 172     -11.875 -19.616   4.010  1.00106.97           C  
ANISOU 3256  CG  ARG B 172    16398  15961   8284  -1087   2250  -3394       C  
ATOM   3257  CD  ARG B 172     -10.865 -19.665   2.874  1.00111.22           C  
ANISOU 3257  CD  ARG B 172    17063  16611   8585  -1068   2522  -3475       C  
ATOM   3258  NE  ARG B 172      -9.904 -20.750   3.051  1.00113.04           N  
ANISOU 3258  NE  ARG B 172    17160  16806   8986   -921   2720  -3680       N  
ATOM   3259  CZ  ARG B 172      -8.988 -21.091   2.150  1.00116.64           C  
ANISOU 3259  CZ  ARG B 172    17702  17343   9273   -864   2962  -3805       C  
ATOM   3260  NH1 ARG B 172      -8.908 -20.435   1.001  1.00120.09           N  
ANISOU 3260  NH1 ARG B 172    18366  17906   9359   -951   3040  -3748       N  
ATOM   3261  NH2 ARG B 172      -8.153 -22.091   2.397  1.00116.71           N  
ANISOU 3261  NH2 ARG B 172    17577  17310   9459   -712   3128  -3985       N  
ATOM   3262  N   HIS B 173     -15.450 -19.860   2.979  1.00117.47           N  
ANISOU 3262  N   HIS B 173    18222  17232   9178  -1237   1375  -3355       N  
ATOM   3263  CA  HIS B 173     -16.219 -21.092   2.826  1.00118.75           C  
ANISOU 3263  CA  HIS B 173    18461  17300   9358  -1202   1148  -3559       C  
ATOM   3264  C   HIS B 173     -17.643 -20.809   2.353  1.00120.53           C  
ANISOU 3264  C   HIS B 173    18848  17558   9391  -1294    776  -3481       C  
ATOM   3265  O   HIS B 173     -18.565 -20.742   3.163  1.00118.68           O  
ANISOU 3265  O   HIS B 173    18494  17256   9343  -1332    539  -3406       O  
ATOM   3266  CB  HIS B 173     -16.249 -21.869   4.144  1.00114.63           C  
ANISOU 3266  CB  HIS B 173    17694  16622   9239  -1138   1125  -3640       C  
ATOM   3267  CG  HIS B 173     -14.893 -22.176   4.697  1.00114.19           C  
ANISOU 3267  CG  HIS B 173    17451  16540   9397  -1029   1456  -3707       C  
ATOM   3268  ND1 HIS B 173     -14.083 -23.163   4.178  1.00117.18           N  
ANISOU 3268  ND1 HIS B 173    17891  16893   9739   -923   1638  -3920       N  
ATOM   3269  CD2 HIS B 173     -14.205 -21.628   5.726  1.00111.41           C  
ANISOU 3269  CD2 HIS B 173    16842  16190   9298  -1004   1624  -3591       C  
ATOM   3270  CE1 HIS B 173     -12.953 -23.209   4.862  1.00115.13           C  
ANISOU 3270  CE1 HIS B 173    17411  16627   9706   -831   1899  -3922       C  
ATOM   3271  NE2 HIS B 173     -13.002 -22.288   5.807  1.00112.02           N  
ANISOU 3271  NE2 HIS B 173    16817  16252   9492   -883   1891  -3727       N  
ATOM   3272  N   PRO B 174     -17.823 -20.651   1.033  1.00108.40           N  
ANISOU 3272  N   PRO B 174    17574  16135   7478  -1328    720  -3498       N  
ATOM   3273  CA  PRO B 174     -19.115 -20.301   0.429  1.00110.35           C  
ANISOU 3273  CA  PRO B 174    17979  16447   7501  -1406    361  -3408       C  
ATOM   3274  C   PRO B 174     -20.224 -21.312   0.717  1.00110.72           C  
ANISOU 3274  C   PRO B 174    17986  16390   7693  -1422     28  -3559       C  
ATOM   3275  O   PRO B 174     -21.342 -20.913   1.041  1.00107.63           O  
ANISOU 3275  O   PRO B 174    17541  16005   7349  -1482   -273  -3425       O  
ATOM   3276  CB  PRO B 174     -18.804 -20.285  -1.072  1.00117.68           C  
ANISOU 3276  CB  PRO B 174    19193  17509   8009  -1410    430  -3474       C  
ATOM   3277  CG  PRO B 174     -17.340 -20.032  -1.153  1.00117.61           C  
ANISOU 3277  CG  PRO B 174    19154  17534   7996  -1363    857  -3475       C  
ATOM   3278  CD  PRO B 174     -16.755 -20.748   0.024  1.00114.46           C  
ANISOU 3278  CD  PRO B 174    18495  16993   8002  -1288   1006  -3592       C  
ATOM   3279  N   PHE B 175     -19.918 -22.601   0.599  1.00174.54           N  
ANISOU 3279  N   PHE B 175    26090  24374  15852  -1369     81  -3830       N  
ATOM   3280  CA  PHE B 175     -20.937 -23.640   0.730  1.00175.19           C  
ANISOU 3280  CA  PHE B 175    26163  24345  16054  -1402   -225  -3997       C  
ATOM   3281  C   PHE B 175     -21.107 -24.147   2.161  1.00171.13           C  
ANISOU 3281  C   PHE B 175    25393  23652  15976  -1387   -243  -4015       C  
ATOM   3282  O   PHE B 175     -22.224 -24.433   2.594  1.00170.19           O  
ANISOU 3282  O   PHE B 175    25191  23466  16005  -1456   -544  -4011       O  
ATOM   3283  CB  PHE B 175     -20.635 -24.809  -0.212  1.00160.48           C  
ANISOU 3283  CB  PHE B 175    24495  22452  14026  -1364   -187  -4291       C  
ATOM   3284  CG  PHE B 175     -21.617 -25.940  -0.108  1.00160.69           C  
ANISOU 3284  CG  PHE B 175    24520  22343  14192  -1411   -482  -4487       C  
ATOM   3285  CD1 PHE B 175     -22.875 -25.838  -0.678  1.00162.52           C  
ANISOU 3285  CD1 PHE B 175    24826  22650  14275  -1516   -862  -4473       C  
ATOM   3286  CD2 PHE B 175     -21.280 -27.108   0.556  1.00159.53           C  
ANISOU 3286  CD2 PHE B 175    24291  21992  14331  -1352   -381  -4682       C  
ATOM   3287  CE1 PHE B 175     -23.781 -26.878  -0.584  1.00163.43           C  
ANISOU 3287  CE1 PHE B 175    24918  22641  14538  -1580  -1133  -4658       C  
ATOM   3288  CE2 PHE B 175     -22.181 -28.152   0.653  1.00160.74           C  
ANISOU 3288  CE2 PHE B 175    24450  22001  14623  -1412   -643  -4859       C  
ATOM   3289  CZ  PHE B 175     -23.433 -28.037   0.082  1.00162.66           C  
ANISOU 3289  CZ  PHE B 175    24752  22321  14728  -1536  -1018  -4852       C  
ATOM   3290  N   LYS B 176     -20.001 -24.263   2.889  1.00162.02           N  
ANISOU 3290  N   LYS B 176    24104  22429  15028  -1296     76  -4033       N  
ATOM   3291  CA  LYS B 176     -20.036 -24.773   4.256  1.00157.83           C  
ANISOU 3291  CA  LYS B 176    23336  21733  14899  -1264     92  -4051       C  
ATOM   3292  C   LYS B 176     -20.763 -23.812   5.193  1.00154.20           C  
ANISOU 3292  C   LYS B 176    22690  21301  14597  -1332    -55  -3810       C  
ATOM   3293  O   LYS B 176     -21.407 -24.231   6.154  1.00152.04           O  
ANISOU 3293  O   LYS B 176    22253  20909  14604  -1357   -196  -3814       O  
ATOM   3294  CB  LYS B 176     -18.617 -25.021   4.771  1.00153.29           C  
ANISOU 3294  CB  LYS B 176    22646  21110  14487  -1134    468  -4108       C  
ATOM   3295  CG  LYS B 176     -18.561 -25.762   6.098  1.00149.41           C  
ANISOU 3295  CG  LYS B 176    21937  20439  14392  -1075    497  -4163       C  
ATOM   3296  CD  LYS B 176     -17.348 -25.346   6.915  1.00146.30           C  
ANISOU 3296  CD  LYS B 176    21326  20072  14190   -977    802  -4064       C  
ATOM   3297  CE  LYS B 176     -16.058 -25.528   6.134  1.00148.99           C  
ANISOU 3297  CE  LYS B 176    21741  20484  14383   -876   1109  -4154       C  
ATOM   3298  NZ  LYS B 176     -14.880 -25.042   6.904  1.00147.24           N  
ANISOU 3298  NZ  LYS B 176    21279  20309  14355   -796   1384  -4049       N  
ATOM   3299  N   HIS B 177     -20.654 -22.520   4.901  1.00153.75           N  
ANISOU 3299  N   HIS B 177    22667  21398  14355  -1364    -14  -3597       N  
ATOM   3300  CA  HIS B 177     -21.257 -21.482   5.731  1.00150.26           C  
ANISOU 3300  CA  HIS B 177    22071  20991  14030  -1417   -132  -3357       C  
ATOM   3301  C   HIS B 177     -22.665 -21.127   5.253  1.00151.88           C  
ANISOU 3301  C   HIS B 177    22364  21264  14082  -1508   -519  -3257       C  
ATOM   3302  O   HIS B 177     -23.425 -20.468   5.965  1.00149.64           O  
ANISOU 3302  O   HIS B 177    21942  20991  13926  -1550   -690  -3080       O  
ATOM   3303  CB  HIS B 177     -20.356 -20.242   5.748  1.00154.71           C  
ANISOU 3303  CB  HIS B 177    22616  21659  14508  -1400    132  -3168       C  
ATOM   3304  CG  HIS B 177     -21.014 -19.016   6.301  1.00153.32           C  
ANISOU 3304  CG  HIS B 177    22370  21540  14346  -1459     -7  -2905       C  
ATOM   3305  ND1 HIS B 177     -21.495 -18.005   5.497  1.00155.07           N  
ANISOU 3305  ND1 HIS B 177    22772  21879  14271  -1511   -137  -2727       N  
ATOM   3306  CD2 HIS B 177     -21.280 -18.642   7.575  1.00150.54           C  
ANISOU 3306  CD2 HIS B 177    21796  21142  14263  -1465    -37  -2787       C  
ATOM   3307  CE1 HIS B 177     -22.024 -17.059   6.251  1.00152.99           C  
ANISOU 3307  CE1 HIS B 177    22405  21626  14098  -1541   -242  -2506       C  
ATOM   3308  NE2 HIS B 177     -21.906 -17.421   7.516  1.00150.19           N  
ANISOU 3308  NE2 HIS B 177    21805  21179  14081  -1518   -181  -2545       N  
ATOM   3309  N   LYS B 178     -23.008 -21.590   4.053  1.00197.76           N  
ANISOU 3309  N   LYS B 178    28389  27127  19624  -1531   -661  -3376       N  
ATOM   3310  CA  LYS B 178     -24.295 -21.293   3.423  1.00200.05           C  
ANISOU 3310  CA  LYS B 178    28764  27507  19740  -1605  -1043  -3298       C  
ATOM   3311  C   LYS B 178     -25.488 -21.557   4.343  1.00197.78           C  
ANISOU 3311  C   LYS B 178    28261  27142  19745  -1664  -1344  -3258       C  
ATOM   3312  O   LYS B 178     -26.499 -20.858   4.280  1.00198.16           O  
ANISOU 3312  O   LYS B 178    28273  27280  19739  -1707  -1625  -3081       O  
ATOM   3313  CB  LYS B 178     -24.446 -22.096   2.128  1.00205.03           C  
ANISOU 3313  CB  LYS B 178    29620  28177  20108  -1618  -1149  -3514       C  
ATOM   3314  CG  LYS B 178     -25.632 -21.691   1.268  1.00207.85           C  
ANISOU 3314  CG  LYS B 178    30085  28672  20218  -1682  -1522  -3433       C  
ATOM   3315  CD  LYS B 178     -25.482 -20.268   0.756  1.00208.56           C  
ANISOU 3315  CD  LYS B 178    30294  28925  20027  -1666  -1484  -3163       C  
ATOM   3316  CE  LYS B 178     -26.563 -19.931  -0.258  1.00212.53           C  
ANISOU 3316  CE  LYS B 178    30934  29581  20238  -1704  -1843  -3097       C  
ATOM   3317  NZ  LYS B 178     -27.929 -20.089   0.311  1.00212.03           N  
ANISOU 3317  NZ  LYS B 178    30670  29499  20393  -1756  -2236  -3062       N  
ATOM   3318  N   THR B 179     -25.361 -22.567   5.198  1.00136.58           N  
ANISOU 3318  N   THR B 179    20360  19224  12310  -1658  -1279  -3414       N  
ATOM   3319  CA  THR B 179     -26.395 -22.877   6.178  1.00134.32           C  
ANISOU 3319  CA  THR B 179    19847  18850  12340  -1720  -1514  -3379       C  
ATOM   3320  C   THR B 179     -25.829 -22.860   7.593  1.00131.97           C  
ANISOU 3320  C   THR B 179    19332  18444  12368  -1675  -1281  -3337       C  
ATOM   3321  O   THR B 179     -25.462 -23.900   8.139  1.00132.91           O  
ANISOU 3321  O   THR B 179    19385  18405  12709  -1651  -1167  -3510       O  
ATOM   3322  CB  THR B 179     -27.040 -24.248   5.909  1.00132.68           C  
ANISOU 3322  CB  THR B 179    19654  18520  12238  -1783  -1714  -3619       C  
ATOM   3323  OG1 THR B 179     -26.026 -25.261   5.895  1.00132.05           O  
ANISOU 3323  OG1 THR B 179    19664  18302  12206  -1719  -1447  -3844       O  
ATOM   3324  CG2 THR B 179     -27.764 -24.244   4.571  1.00136.23           C  
ANISOU 3324  CG2 THR B 179    20274  19097  12391  -1838  -1999  -3666       C  
ATOM   3325  N   MET B 181     -25.838 -20.820   9.940  1.00134.90           N  
ANISOU 3325  N   MET B 181    19272  18885  13099  -1656  -1196  -2889       N  
ATOM   3326  CA  MET B 181     -26.744 -21.212  11.012  1.00132.01           C  
ANISOU 3326  CA  MET B 181    18659  18440  13059  -1702  -1369  -2877       C  
ATOM   3327  C   MET B 181     -28.163 -20.735  10.724  1.00131.02           C  
ANISOU 3327  C   MET B 181    18484  18403  12896  -1780  -1758  -2724       C  
ATOM   3328  O   MET B 181     -28.362 -19.705  10.078  1.00131.89           O  
ANISOU 3328  O   MET B 181    18696  18647  12772  -1769  -1852  -2538       O  
ATOM   3329  CB  MET B 181     -26.256 -20.651  12.350  1.00133.19           C  
ANISOU 3329  CB  MET B 181    18591  18570  13446  -1635  -1161  -2764       C  
ATOM   3330  CG  MET B 181     -26.219 -19.132  12.410  1.00133.04           C  
ANISOU 3330  CG  MET B 181    18561  18655  13334  -1583  -1136  -2477       C  
ATOM   3331  SD  MET B 181     -25.218 -18.502  13.771  1.00132.94           S  
ANISOU 3331  SD  MET B 181    18353  18583  13577  -1450   -786  -2362       S  
ATOM   3332  CE  MET B 181     -23.579 -18.980  13.230  1.00133.16           C  
ANISOU 3332  CE  MET B 181    18582  18664  13349  -1461   -437  -2606       C  
ATOM   3333  N   SER B 182     -29.148 -21.490  11.202  1.00 92.39           N  
ANISOU 3333  N   SER B 182    13428  13430   8247  -1853  -1981  -2792       N  
ATOM   3334  CA  SER B 182     -30.548 -21.133  11.010  1.00 92.79           C  
ANISOU 3334  CA  SER B 182    13369  13566   8324  -1918  -2362  -2649       C  
ATOM   3335  C   SER B 182     -30.878 -19.832  11.734  1.00 91.67           C  
ANISOU 3335  C   SER B 182    13035  13480   8318  -1817  -2378  -2330       C  
ATOM   3336  O   SER B 182     -30.138 -19.403  12.619  1.00 90.19           O  
ANISOU 3336  O   SER B 182    12734  13215   8321  -1707  -2105  -2242       O  
ATOM   3337  CB  SER B 182     -31.463 -22.258  11.498  1.00 91.40           C  
ANISOU 3337  CB  SER B 182    13004  13268   8459  -2014  -2547  -2776       C  
ATOM   3338  OG  SER B 182     -31.250 -22.530  12.872  1.00 89.61           O  
ANISOU 3338  OG  SER B 182    12539  12898   8611  -1963  -2361  -2747       O  
ATOM   3339  N   ARG B 183     -31.990 -19.208  11.353  1.00132.59           N  
ANISOU 3339  N   ARG B 183    18173  18779  13425  -1827  -2694  -2151       N  
ATOM   3340  CA  ARG B 183     -32.401 -17.938  11.946  1.00132.68           C  
ANISOU 3340  CA  ARG B 183    18019  18822  13573  -1693  -2720  -1832       C  
ATOM   3341  C   ARG B 183     -32.635 -18.066  13.449  1.00131.30           C  
ANISOU 3341  C   ARG B 183    17507  18508  13872  -1614  -2603  -1749       C  
ATOM   3342  O   ARG B 183     -32.459 -17.103  14.198  1.00130.81           O  
ANISOU 3342  O   ARG B 183    17340  18421  13940  -1484  -2464  -1539       O  
ATOM   3343  CB  ARG B 183     -33.657 -17.401  11.255  1.00135.41           C  
ANISOU 3343  CB  ARG B 183    18342  19310  13797  -1704  -3121  -1674       C  
ATOM   3344  CG  ARG B 183     -33.460 -17.076   9.782  1.00137.37           C  
ANISOU 3344  CG  ARG B 183    18947  19710  13536  -1760  -3251  -1703       C  
ATOM   3345  CD  ARG B 183     -34.701 -16.431   9.187  1.00140.44           C  
ANISOU 3345  CD  ARG B 183    19276  20229  13854  -1707  -3635  -1509       C  
ATOM   3346  NE  ARG B 183     -34.524 -16.104   7.775  1.00144.09           N  
ANISOU 3346  NE  ARG B 183    20042  20800  13905  -1675  -3691  -1512       N  
ATOM   3347  CZ  ARG B 183     -35.434 -15.481   7.033  1.00147.36           C  
ANISOU 3347  CZ  ARG B 183    20466  21348  14176  -1605  -3992  -1349       C  
ATOM   3348  NH1 ARG B 183     -36.589 -15.113   7.569  1.00147.24           N  
ANISOU 3348  NH1 ARG B 183    20156  21371  14418  -1547  -4261  -1172       N  
ATOM   3349  NH2 ARG B 183     -35.189 -15.224   5.755  1.00150.71           N  
ANISOU 3349  NH2 ARG B 183    21182  21874  14207  -1581  -4016  -1358       N  
ATOM   3350  N   SER B 184     -33.028 -19.261  13.880  1.00 83.67           N  
ANISOU 3350  N   SER B 184    11326  12379   8086  -1700  -2652  -1918       N  
ATOM   3351  CA  SER B 184     -33.217 -19.548  15.296  1.00 82.22           C  
ANISOU 3351  CA  SER B 184    10853  12055   8332  -1640  -2521  -1860       C  
ATOM   3352  C   SER B 184     -31.915 -19.355  16.065  1.00 79.62           C  
ANISOU 3352  C   SER B 184    10563  11635   8055  -1530  -2141  -1862       C  
ATOM   3353  O   SER B 184     -31.864 -18.596  17.032  1.00 78.76           O  
ANISOU 3353  O   SER B 184    10297  11494   8134  -1409  -2018  -1672       O  
ATOM   3354  CB  SER B 184     -33.734 -20.975  15.487  1.00 82.80           C  
ANISOU 3354  CB  SER B 184    10825  12020   8616  -1777  -2609  -2067       C  
ATOM   3355  OG  SER B 184     -33.864 -21.292  16.861  1.00 80.26           O  
ANISOU 3355  OG  SER B 184    10256  11553   8685  -1719  -2451  -2006       O  
ATOM   3356  N   ARG B 185     -30.864 -20.039  15.622  1.00 74.85           N  
ANISOU 3356  N   ARG B 185    10164  10995   7280  -1571  -1961  -2084       N  
ATOM   3357  CA  ARG B 185     -29.559 -19.948  16.268  1.00 72.54           C  
ANISOU 3357  CA  ARG B 185     9897  10636   7028  -1472  -1612  -2114       C  
ATOM   3358  C   ARG B 185     -28.976 -18.541  16.177  1.00 71.77           C  
ANISOU 3358  C   ARG B 185     9874  10635   6762  -1385  -1485  -1927       C  
ATOM   3359  O   ARG B 185     -28.237 -18.109  17.063  1.00 70.74           O  
ANISOU 3359  O   ARG B 185     9656  10456   6765  -1288  -1248  -1856       O  
ATOM   3360  CB  ARG B 185     -28.583 -20.961  15.662  1.00 72.88           C  
ANISOU 3360  CB  ARG B 185    10147  10641   6903  -1523  -1457  -2400       C  
ATOM   3361  CG  ARG B 185     -28.995 -22.412  15.849  1.00 73.70           C  
ANISOU 3361  CG  ARG B 185    10200  10600   7205  -1599  -1524  -2601       C  
ATOM   3362  CD  ARG B 185     -27.886 -23.359  15.416  1.00 73.73           C  
ANISOU 3362  CD  ARG B 185    10402  10537   7077  -1603  -1316  -2877       C  
ATOM   3363  NE  ARG B 185     -28.256 -24.760  15.601  1.00 74.16           N  
ANISOU 3363  NE  ARG B 185    10438  10418   7322  -1676  -1375  -3072       N  
ATOM   3364  CZ  ARG B 185     -28.790 -25.522  14.652  1.00 75.83           C  
ANISOU 3364  CZ  ARG B 185    10807  10615   7390  -1825  -1566  -3269       C  
ATOM   3365  NH1 ARG B 185     -29.016 -25.020  13.446  1.00 77.50           N  
ANISOU 3365  NH1 ARG B 185    11207  10992   7249  -1903  -1724  -3289       N  
ATOM   3366  NH2 ARG B 185     -29.096 -26.787  14.909  1.00 77.44           N  
ANISOU 3366  NH2 ARG B 185    10996  10629   7798  -1898  -1598  -3442       N  
ATOM   3367  N   THR B 186     -29.310 -17.831  15.104  1.00 60.93           N  
ANISOU 3367  N   THR B 186     8672   9391   5087  -1426  -1649  -1846       N  
ATOM   3368  CA  THR B 186     -28.837 -16.464  14.918  1.00 61.40           C  
ANISOU 3368  CA  THR B 186     8836   9522   4972  -1360  -1541  -1652       C  
ATOM   3369  C   THR B 186     -29.478 -15.527  15.936  1.00 61.86           C  
ANISOU 3369  C   THR B 186     8670   9538   5296  -1250  -1583  -1393       C  
ATOM   3370  O   THR B 186     -28.789 -14.742  16.586  1.00 60.98           O  
ANISOU 3370  O   THR B 186     8529   9389   5251  -1171  -1363  -1288       O  
ATOM   3371  CB  THR B 186     -29.124 -15.947  13.497  1.00 63.62           C  
ANISOU 3371  CB  THR B 186     9381   9943   4849  -1424  -1722  -1607       C  
ATOM   3372  OG1 THR B 186     -28.500 -16.809  12.538  1.00 65.59           O  
ANISOU 3372  OG1 THR B 186     9861  10235   4826  -1525  -1658  -1863       O  
ATOM   3373  CG2 THR B 186     -28.585 -14.535  13.326  1.00 63.29           C  
ANISOU 3373  CG2 THR B 186     9469   9945   4633  -1363  -1583  -1394       C  
ATOM   3374  N   LYS B 187     -30.799 -15.616  16.072  1.00 83.82           N  
ANISOU 3374  N   LYS B 187    11286  12326   8234  -1247  -1863  -1302       N  
ATOM   3375  CA  LYS B 187     -31.522 -14.804  17.047  1.00 84.77           C  
ANISOU 3375  CA  LYS B 187    11178  12406   8624  -1129  -1905  -1068       C  
ATOM   3376  C   LYS B 187     -31.103 -15.158  18.472  1.00 82.83           C  
ANISOU 3376  C   LYS B 187    10730  12032   8708  -1068  -1671  -1097       C  
ATOM   3377  O   LYS B 187     -31.001 -14.281  19.337  1.00 82.68           O  
ANISOU 3377  O   LYS B 187    10616  11968   8830   -959  -1548   -935       O  
ATOM   3378  CB  LYS B 187     -33.034 -14.965  16.869  1.00 87.11           C  
ANISOU 3378  CB  LYS B 187    11305  12754   9039  -1144  -2250   -990       C  
ATOM   3379  CG  LYS B 187     -33.564 -14.382  15.566  1.00 89.79           C  
ANISOU 3379  CG  LYS B 187    11823  13233   9058  -1167  -2519   -904       C  
ATOM   3380  CD  LYS B 187     -35.060 -14.610  15.415  1.00 90.96           C  
ANISOU 3380  CD  LYS B 187    11764  13453   9345  -1183  -2880   -843       C  
ATOM   3381  CE  LYS B 187     -35.390 -16.091  15.328  1.00 90.87           C  
ANISOU 3381  CE  LYS B 187    11668  13424   9436  -1344  -2985  -1091       C  
ATOM   3382  NZ  LYS B 187     -36.847 -16.325  15.121  1.00 91.50           N  
ANISOU 3382  NZ  LYS B 187    11526  13590   9648  -1390  -3350  -1045       N  
ATOM   3383  N   LYS B 188     -30.857 -16.444  18.708  1.00 58.62           N  
ANISOU 3383  N   LYS B 188     7621   8901   5752  -1136  -1614  -1304       N  
ATOM   3384  CA  LYS B 188     -30.337 -16.903  19.991  1.00 56.90           C  
ANISOU 3384  CA  LYS B 188     7252   8563   5806  -1076  -1389  -1346       C  
ATOM   3385  C   LYS B 188     -28.978 -16.269  20.266  1.00 55.32           C  
ANISOU 3385  C   LYS B 188     7153   8362   5506  -1010  -1105  -1343       C  
ATOM   3386  O   LYS B 188     -28.680 -15.874  21.395  1.00 55.06           O  
ANISOU 3386  O   LYS B 188     6989   8267   5664   -918   -949  -1257       O  
ATOM   3387  CB  LYS B 188     -30.211 -18.428  20.012  1.00 54.07           C  
ANISOU 3387  CB  LYS B 188     6888   8121   5535  -1159  -1376  -1578       C  
ATOM   3388  CG  LYS B 188     -31.531 -19.176  20.131  1.00 54.91           C  
ANISOU 3388  CG  LYS B 188     6831   8190   5843  -1238  -1611  -1587       C  
ATOM   3389  CD  LYS B 188     -31.301 -20.681  20.166  1.00 54.38           C  
ANISOU 3389  CD  LYS B 188     6792   8002   5870  -1324  -1564  -1820       C  
ATOM   3390  CE  LYS B 188     -32.603 -21.444  20.365  1.00 55.16           C  
ANISOU 3390  CE  LYS B 188     6713   8043   6202  -1431  -1776  -1828       C  
ATOM   3391  NZ  LYS B 188     -33.552 -21.245  19.236  1.00 57.15           N  
ANISOU 3391  NZ  LYS B 188     7001   8424   6289  -1544  -2091  -1832       N  
ATOM   3392  N   PHE B 189     -28.161 -16.171  19.222  1.00 62.39           N  
ANISOU 3392  N   PHE B 189     8280   9332   6094  -1067  -1037  -1442       N  
ATOM   3393  CA  PHE B 189     -26.829 -15.588  19.338  1.00 61.08           C  
ANISOU 3393  CA  PHE B 189     8205   9186   5818  -1033   -764  -1455       C  
ATOM   3394  C   PHE B 189     -26.904 -14.088  19.605  1.00 62.21           C  
ANISOU 3394  C   PHE B 189     8350   9346   5939   -974   -735  -1219       C  
ATOM   3395  O   PHE B 189     -26.081 -13.541  20.338  1.00 61.60           O  
ANISOU 3395  O   PHE B 189     8230   9241   5935   -926   -522  -1184       O  
ATOM   3396  CB  PHE B 189     -26.010 -15.865  18.076  1.00 60.48           C  
ANISOU 3396  CB  PHE B 189     8377   9195   5409  -1119   -687  -1621       C  
ATOM   3397  CG  PHE B 189     -24.585 -15.402  18.164  1.00 59.18           C  
ANISOU 3397  CG  PHE B 189     8278   9063   5146  -1104   -387  -1660       C  
ATOM   3398  CD1 PHE B 189     -23.670 -16.080  18.952  1.00 57.21           C  
ANISOU 3398  CD1 PHE B 189     7909   8762   5067  -1051   -179  -1798       C  
ATOM   3399  CD2 PHE B 189     -24.156 -14.294  17.452  1.00 60.52           C  
ANISOU 3399  CD2 PHE B 189     8624   9315   5055  -1144   -314  -1555       C  
ATOM   3400  CE1 PHE B 189     -22.357 -15.659  19.034  1.00 56.36           C  
ANISOU 3400  CE1 PHE B 189     7825   8705   4885  -1042     87  -1842       C  
ATOM   3401  CE2 PHE B 189     -22.843 -13.870  17.529  1.00 59.08           C  
ANISOU 3401  CE2 PHE B 189     8481   9170   4798  -1155    -28  -1597       C  
ATOM   3402  CZ  PHE B 189     -21.943 -14.552  18.322  1.00 56.81           C  
ANISOU 3402  CZ  PHE B 189     8041   8850   4695  -1105    168  -1747       C  
ATOM   3403  N   ILE B 190     -27.892 -13.429  19.007  1.00 78.40           N  
ANISOU 3403  N   ILE B 190    10454  11441   7893   -977   -958  -1062       N  
ATOM   3404  CA  ILE B 190     -28.116 -12.005  19.238  1.00 79.81           C  
ANISOU 3404  CA  ILE B 190    10648  11608   8067   -904   -953   -825       C  
ATOM   3405  C   ILE B 190     -28.532 -11.768  20.685  1.00 79.69           C  
ANISOU 3405  C   ILE B 190    10387  11495   8395   -795   -911   -723       C  
ATOM   3406  O   ILE B 190     -28.016 -10.867  21.355  1.00 79.96           O  
ANISOU 3406  O   ILE B 190    10415  11479   8486   -738   -744   -627       O  
ATOM   3407  CB  ILE B 190     -29.197 -11.441  18.295  1.00 83.37           C  
ANISOU 3407  CB  ILE B 190    11196  12124   8355   -900  -1233   -670       C  
ATOM   3408  CG1 ILE B 190     -28.752 -11.564  16.837  1.00 84.70           C  
ANISOU 3408  CG1 ILE B 190    11650  12397   8134  -1007  -1268   -757       C  
ATOM   3409  CG2 ILE B 190     -29.495  -9.988  18.629  1.00 84.83           C  
ANISOU 3409  CG2 ILE B 190    11393  12263   8575   -796  -1226   -416       C  
ATOM   3410  CD1 ILE B 190     -27.485 -10.804  16.520  1.00 84.75           C  
ANISOU 3410  CD1 ILE B 190    11862  12413   7925  -1042   -997   -746       C  
ATOM   3411  N   SER B 191     -29.465 -12.589  21.163  1.00 43.54           N  
ANISOU 3411  N   SER B 191     5615   6889   4041   -778  -1055   -750       N  
ATOM   3412  CA  SER B 191     -29.907 -12.521  22.551  1.00 42.32           C  
ANISOU 3412  CA  SER B 191     5227   6647   4208   -681  -1002   -668       C  
ATOM   3413  C   SER B 191     -28.733 -12.751  23.499  1.00 39.92           C  
ANISOU 3413  C   SER B 191     4891   6284   3993   -659   -731   -765       C  
ATOM   3414  O   SER B 191     -28.616 -12.090  24.534  1.00 39.87           O  
ANISOU 3414  O   SER B 191     4798   6221   4132   -573   -613   -668       O  
ATOM   3415  CB  SER B 191     -31.007 -13.551  22.814  1.00 42.18           C  
ANISOU 3415  CB  SER B 191     5015   6612   4400   -702  -1176   -708       C  
ATOM   3416  OG  SER B 191     -32.131 -13.321  21.982  1.00 44.50           O  
ANISOU 3416  OG  SER B 191     5300   6981   4629   -721  -1451   -618       O  
ATOM   3417  N   ALA B 192     -27.864 -13.688  23.132  1.00 34.78           N  
ANISOU 3417  N   ALA B 192     4315   5650   3251   -729   -640   -963       N  
ATOM   3418  CA  ALA B 192     -26.669 -13.980  23.916  1.00 33.04           C  
ANISOU 3418  CA  ALA B 192     4060   5396   3100   -699   -400  -1069       C  
ATOM   3419  C   ALA B 192     -25.725 -12.781  23.941  1.00 32.50           C  
ANISOU 3419  C   ALA B 192     4088   5359   2904   -691   -229  -1006       C  
ATOM   3420  O   ALA B 192     -25.116 -12.483  24.969  1.00 30.86           O  
ANISOU 3420  O   ALA B 192     3792   5115   2819   -636    -73   -998       O  
ATOM   3421  CB  ALA B 192     -25.958 -15.205  23.364  1.00 33.75           C  
ANISOU 3421  CB  ALA B 192     4219   5499   3106   -759   -345  -1295       C  
ATOM   3422  N   ILE B 193     -25.611 -12.099  22.805  1.00 64.26           N  
ANISOU 3422  N   ILE B 193     8298   9447   6673   -756   -262   -962       N  
ATOM   3423  CA  ILE B 193     -24.784 -10.901  22.707  1.00 63.98           C  
ANISOU 3423  CA  ILE B 193     8377   9427   6506   -778   -101   -888       C  
ATOM   3424  C   ILE B 193     -25.309  -9.802  23.625  1.00 64.85           C  
ANISOU 3424  C   ILE B 193     8412   9455   6773   -692   -109   -695       C  
ATOM   3425  O   ILE B 193     -24.545  -9.192  24.375  1.00 63.90           O  
ANISOU 3425  O   ILE B 193     8267   9301   6711   -681     66   -685       O  
ATOM   3426  CB  ILE B 193     -24.712 -10.374  21.258  1.00 64.36           C  
ANISOU 3426  CB  ILE B 193     8671   9551   6235   -866   -145   -850       C  
ATOM   3427  CG1 ILE B 193     -23.833 -11.287  20.402  1.00 63.19           C  
ANISOU 3427  CG1 ILE B 193     8625   9488   5899   -955    -47  -1064       C  
ATOM   3428  CG2 ILE B 193     -24.165  -8.955  21.226  1.00 64.70           C  
ANISOU 3428  CG2 ILE B 193     8838   9572   6174   -889     -7   -711       C  
ATOM   3429  CD1 ILE B 193     -23.642 -10.792  18.986  1.00 64.89           C  
ANISOU 3429  CD1 ILE B 193     9104   9786   5765  -1049    -55  -1037       C  
ATOM   3430  N   TRP B 194     -26.616  -9.562  23.567  1.00 43.02           N  
ANISOU 3430  N   TRP B 194     5605   6661   4080   -631   -314   -553       N  
ATOM   3431  CA  TRP B 194     -27.243  -8.555  24.418  1.00 42.71           C  
ANISOU 3431  CA  TRP B 194     5492   6536   4200   -526   -325   -374       C  
ATOM   3432  C   TRP B 194     -27.069  -8.872  25.902  1.00 41.35           C  
ANISOU 3432  C   TRP B 194     5128   6301   4283   -456   -204   -420       C  
ATOM   3433  O   TRP B 194     -26.689  -8.002  26.691  1.00 41.19           O  
ANISOU 3433  O   TRP B 194     5108   6219   4323   -415    -70   -363       O  
ATOM   3434  CB  TRP B 194     -28.728  -8.407  24.083  1.00 45.99           C  
ANISOU 3434  CB  TRP B 194     5853   6950   4670   -456   -576   -229       C  
ATOM   3435  CG  TRP B 194     -28.985  -7.572  22.867  1.00 48.37           C  
ANISOU 3435  CG  TRP B 194     6363   7285   4729   -474   -694   -102       C  
ATOM   3436  CD1 TRP B 194     -29.455  -8.001  21.660  1.00 49.35           C  
ANISOU 3436  CD1 TRP B 194     6581   7502   4667   -529   -894   -115       C  
ATOM   3437  CD2 TRP B 194     -28.780  -6.160  22.739  1.00 49.21           C  
ANISOU 3437  CD2 TRP B 194     6633   7325   4741   -437   -622     61       C  
ATOM   3438  NE1 TRP B 194     -29.559  -6.943  20.790  1.00 50.65           N  
ANISOU 3438  NE1 TRP B 194     6958   7671   4614   -518   -957     44       N  
ATOM   3439  CE2 TRP B 194     -29.150  -5.802  21.428  1.00 50.54           C  
ANISOU 3439  CE2 TRP B 194     6994   7549   4659   -461   -786    159       C  
ATOM   3440  CE3 TRP B 194     -28.320  -5.164  23.607  1.00 49.11           C  
ANISOU 3440  CE3 TRP B 194     6636   7200   4823   -391   -439    131       C  
ATOM   3441  CZ2 TRP B 194     -29.074  -4.490  20.964  1.00 51.89           C  
ANISOU 3441  CZ2 TRP B 194     7379   7655   4680   -433   -762    341       C  
ATOM   3442  CZ3 TRP B 194     -28.247  -3.863  23.144  1.00 50.34           C  
ANISOU 3442  CZ3 TRP B 194     7001   7282   4842   -376   -412    295       C  
ATOM   3443  CH2 TRP B 194     -28.621  -3.538  21.835  1.00 51.75           C  
ANISOU 3443  CH2 TRP B 194     7377   7507   4780   -393   -568    407       C  
ATOM   3444  N   LEU B 195     -27.344 -10.120  26.272  1.00 38.36           N  
ANISOU 3444  N   LEU B 195     4604   5931   4040   -449   -251   -524       N  
ATOM   3445  CA  LEU B 195     -27.218 -10.552  27.660  1.00 36.88           C  
ANISOU 3445  CA  LEU B 195     4250   5687   4075   -380   -145   -560       C  
ATOM   3446  C   LEU B 195     -25.786 -10.400  28.167  1.00 34.18           C  
ANISOU 3446  C   LEU B 195     3942   5354   3690   -400     66   -663       C  
ATOM   3447  O   LEU B 195     -25.558  -9.846  29.245  1.00 32.77           O  
ANISOU 3447  O   LEU B 195     3704   5129   3620   -339    170   -623       O  
ATOM   3448  CB  LEU B 195     -27.686 -11.999  27.820  1.00 35.60           C  
ANISOU 3448  CB  LEU B 195     3964   5520   4041   -389   -225   -656       C  
ATOM   3449  CG  LEU B 195     -27.551 -12.606  29.219  1.00 33.89           C  
ANISOU 3449  CG  LEU B 195     3601   5242   4035   -319   -114   -688       C  
ATOM   3450  CD1 LEU B 195     -28.245 -11.737  30.257  1.00 34.21           C  
ANISOU 3450  CD1 LEU B 195     3547   5227   4226   -217    -89   -531       C  
ATOM   3451  CD2 LEU B 195     -28.110 -14.020  29.243  1.00 33.54           C  
ANISOU 3451  CD2 LEU B 195     3464   5166   4113   -344   -196   -767       C  
ATOM   3452  N   ALA B 196     -24.829 -10.890  27.384  1.00 23.62           N  
ANISOU 3452  N   ALA B 196     2696   4087   2192   -486    129   -804       N  
ATOM   3453  CA  ALA B 196     -23.418 -10.774  27.734  1.00 24.23           C  
ANISOU 3453  CA  ALA B 196     2778   4200   2227   -513    323   -913       C  
ATOM   3454  C   ALA B 196     -23.019  -9.312  27.892  1.00 24.36           C  
ANISOU 3454  C   ALA B 196     2878   4199   2180   -540    420   -815       C  
ATOM   3455  O   ALA B 196     -22.275  -8.958  28.806  1.00 24.23           O  
ANISOU 3455  O   ALA B 196     2801   4175   2232   -528    550   -849       O  
ATOM   3456  CB  ALA B 196     -22.552 -11.452  26.687  1.00 26.47           C  
ANISOU 3456  CB  ALA B 196     3148   4571   2339   -597    380  -1074       C  
ATOM   3457  N   SER B 197     -23.528  -8.466  27.000  1.00 51.86           N  
ANISOU 3457  N   SER B 197     6506   7668   5529   -578    347   -692       N  
ATOM   3458  CA  SER B 197     -23.264  -7.033  27.056  1.00 52.73           C  
ANISOU 3458  CA  SER B 197     6730   7725   5578   -608    432   -579       C  
ATOM   3459  C   SER B 197     -23.767  -6.433  28.365  1.00 53.06           C  
ANISOU 3459  C   SER B 197     6676   7664   5819   -502    442   -489       C  
ATOM   3460  O   SER B 197     -23.062  -5.656  29.013  1.00 51.99           O  
ANISOU 3460  O   SER B 197     6558   7490   5704   -528    579   -499       O  
ATOM   3461  CB  SER B 197     -23.917  -6.322  25.870  1.00 54.25           C  
ANISOU 3461  CB  SER B 197     7111   7904   5597   -637    322   -436       C  
ATOM   3462  OG  SER B 197     -23.433  -6.836  24.642  1.00 54.13           O  
ANISOU 3462  OG  SER B 197     7213   7989   5363   -740    325   -524       O  
ATOM   3463  N   ALA B 198     -24.987  -6.799  28.747  1.00 33.49           N  
ANISOU 3463  N   ALA B 198     4094   5146   3485   -392    302   -409       N  
ATOM   3464  CA  ALA B 198     -25.567  -6.332  30.002  1.00 32.57           C  
ANISOU 3464  CA  ALA B 198     3880   4938   3557   -277    321   -328       C  
ATOM   3465  C   ALA B 198     -24.720  -6.780  31.191  1.00 31.04           C  
ANISOU 3465  C   ALA B 198     3576   4757   3459   -267    454   -453       C  
ATOM   3466  O   ALA B 198     -24.450  -5.997  32.106  1.00 30.54           O  
ANISOU 3466  O   ALA B 198     3519   4633   3450   -237    551   -434       O  
ATOM   3467  CB  ALA B 198     -26.996  -6.832  30.146  1.00 18.97           C  
ANISOU 3467  CB  ALA B 198     2032   3197   1980   -173    162   -239       C  
ATOM   3468  N   LEU B 199     -24.300  -8.042  31.163  1.00 28.49           N  
ANISOU 3468  N   LEU B 199     3166   4509   3150   -286    452   -583       N  
ATOM   3469  CA  LEU B 199     -23.451  -8.597  32.213  1.00 27.32           C  
ANISOU 3469  CA  LEU B 199     2915   4386   3079   -261    556   -698       C  
ATOM   3470  C   LEU B 199     -22.140  -7.827  32.324  1.00 27.38           C  
ANISOU 3470  C   LEU B 199     2980   4432   2992   -343    697   -774       C  
ATOM   3471  O   LEU B 199     -21.640  -7.592  33.424  1.00 26.66           O  
ANISOU 3471  O   LEU B 199     2827   4335   2968   -312    774   -814       O  
ATOM   3472  CB  LEU B 199     -23.163 -10.075  31.946  1.00 27.20           C  
ANISOU 3472  CB  LEU B 199     2828   4431   3077   -264    529   -823       C  
ATOM   3473  CG  LEU B 199     -24.348 -11.039  32.000  1.00 27.24           C  
ANISOU 3473  CG  LEU B 199     2754   4392   3203   -207    402   -779       C  
ATOM   3474  CD1 LEU B 199     -23.904 -12.434  31.596  1.00 27.47           C  
ANISOU 3474  CD1 LEU B 199     2759   4457   3222   -230    391   -922       C  
ATOM   3475  CD2 LEU B 199     -24.973 -11.047  33.386  1.00 26.33           C  
ANISOU 3475  CD2 LEU B 199     2529   4209   3264    -99    420   -701       C  
ATOM   3476  N   LEU B 200     -21.589  -7.434  31.180  1.00 28.85           N  
ANISOU 3476  N   LEU B 200     3284   4662   3016   -459    731   -795       N  
ATOM   3477  CA  LEU B 200     -20.346  -6.672  31.153  1.00 29.29           C  
ANISOU 3477  CA  LEU B 200     3387   4760   2984   -570    878   -866       C  
ATOM   3478  C   LEU B 200     -20.572  -5.228  31.592  1.00 29.57           C  
ANISOU 3478  C   LEU B 200     3522   4684   3029   -589    919   -755       C  
ATOM   3479  O   LEU B 200     -19.639  -4.548  32.019  1.00 29.78           O  
ANISOU 3479  O   LEU B 200     3560   4718   3039   -674   1037   -815       O  
ATOM   3480  CB  LEU B 200     -19.723  -6.711  29.755  1.00 30.67           C  
ANISOU 3480  CB  LEU B 200     3668   5014   2972   -697    926   -917       C  
ATOM   3481  CG  LEU B 200     -19.263  -8.082  29.255  1.00 31.29           C  
ANISOU 3481  CG  LEU B 200     3670   5201   3020   -690    924  -1064       C  
ATOM   3482  CD1 LEU B 200     -18.796  -8.004  27.810  1.00 33.22           C  
ANISOU 3482  CD1 LEU B 200     4055   5517   3053   -812    977  -1098       C  
ATOM   3483  CD2 LEU B 200     -18.167  -8.644  30.147  1.00 31.92           C  
ANISOU 3483  CD2 LEU B 200     3584   5357   3188   -665   1023  -1214       C  
ATOM   3484  N   ALA B 201     -21.814  -4.766  31.488  1.00 34.05           N  
ANISOU 3484  N   ALA B 201     4156   5147   3634   -508    819   -599       N  
ATOM   3485  CA  ALA B 201     -22.151  -3.394  31.857  1.00 35.59           C  
ANISOU 3485  CA  ALA B 201     4467   5208   3848   -497    855   -485       C  
ATOM   3486  C   ALA B 201     -22.651  -3.284  33.296  1.00 34.44           C  
ANISOU 3486  C   ALA B 201     4227   4990   3868   -369    858   -469       C  
ATOM   3487  O   ALA B 201     -22.894  -2.183  33.792  1.00 35.43           O  
ANISOU 3487  O   ALA B 201     4443   4992   4025   -344    904   -400       O  
ATOM   3488  CB  ALA B 201     -23.174  -2.821  30.891  1.00 42.55           C  
ANISOU 3488  CB  ALA B 201     5488   6013   4664   -463    752   -313       C  
ATOM   3489  N   ILE B 202     -22.807  -4.429  33.956  1.00 32.66           N  
ANISOU 3489  N   ILE B 202     3836   4831   3741   -287    818   -533       N  
ATOM   3490  CA  ILE B 202     -23.199  -4.473  35.371  1.00 31.09           C  
ANISOU 3490  CA  ILE B 202     3550   4585   3679   -169    839   -528       C  
ATOM   3491  C   ILE B 202     -22.425  -3.540  36.332  1.00 29.98           C  
ANISOU 3491  C   ILE B 202     3460   4401   3530   -207    953   -591       C  
ATOM   3492  O   ILE B 202     -23.051  -2.856  37.145  1.00 30.21           O  
ANISOU 3492  O   ILE B 202     3524   4324   3629   -119    977   -529       O  
ATOM   3493  CB  ILE B 202     -23.227  -5.931  35.918  1.00 28.91           C  
ANISOU 3493  CB  ILE B 202     3109   4391   3483   -101    801   -599       C  
ATOM   3494  CG1 ILE B 202     -24.526  -6.626  35.508  1.00 30.03           C  
ANISOU 3494  CG1 ILE B 202     3189   4511   3708    -21    685   -499       C  
ATOM   3495  CG2 ILE B 202     -23.083  -5.954  37.432  1.00 28.20           C  
ANISOU 3495  CG2 ILE B 202     2957   4286   3471    -20    861   -635       C  
ATOM   3496  CD1 ILE B 202     -24.720  -7.989  36.137  1.00 28.23           C  
ANISOU 3496  CD1 ILE B 202     2823   4321   3581     43    660   -544       C  
ATOM   3497  N   PRO B 203     -21.076  -3.499  36.243  1.00 33.01           N  
ANISOU 3497  N   PRO B 203     3843   4868   3832   -341   1026   -723       N  
ATOM   3498  CA  PRO B 203     -20.322  -2.631  37.160  1.00 32.29           C  
ANISOU 3498  CA  PRO B 203     3788   4745   3734   -401   1117   -800       C  
ATOM   3499  C   PRO B 203     -20.736  -1.156  37.149  1.00 34.56           C  
ANISOU 3499  C   PRO B 203     4259   4860   4013   -428   1166   -710       C  
ATOM   3500  O   PRO B 203     -20.502  -0.464  38.140  1.00 34.10           O  
ANISOU 3500  O   PRO B 203     4243   4735   3978   -433   1224   -760       O  
ATOM   3501  CB  PRO B 203     -18.883  -2.764  36.656  1.00 32.59           C  
ANISOU 3501  CB  PRO B 203     3786   4911   3684   -569   1179   -937       C  
ATOM   3502  CG  PRO B 203     -18.829  -4.112  36.068  1.00 32.00           C  
ANISOU 3502  CG  PRO B 203     3594   4958   3605   -525   1122   -972       C  
ATOM   3503  CD  PRO B 203     -20.167  -4.321  35.421  1.00 31.83           C  
ANISOU 3503  CD  PRO B 203     3630   4858   3605   -434   1032   -827       C  
ATOM   3504  N   MET B 204     -21.333  -0.687  36.057  1.00 30.06           N  
ANISOU 3504  N   MET B 204     3809   4212   3400   -440   1138   -583       N  
ATOM   3505  CA  MET B 204     -21.786   0.700  35.973  1.00 30.71           C  
ANISOU 3505  CA  MET B 204     4085   4105   3479   -440   1180   -475       C  
ATOM   3506  C   MET B 204     -22.846   1.018  37.021  1.00 30.49           C  
ANISOU 3506  C   MET B 204     4053   3960   3572   -255   1169   -410       C  
ATOM   3507  O   MET B 204     -22.966   2.158  37.472  1.00 31.47           O  
ANISOU 3507  O   MET B 204     4320   3923   3714   -248   1240   -389       O  
ATOM   3508  CB  MET B 204     -22.320   1.017  34.575  1.00 31.80           C  
ANISOU 3508  CB  MET B 204     4349   4195   3540   -452   1125   -328       C  
ATOM   3509  CG  MET B 204     -21.241   1.278  33.538  1.00 32.81           C  
ANISOU 3509  CG  MET B 204     4576   4373   3519   -662   1198   -372       C  
ATOM   3510  SD  MET B 204     -20.127   2.620  34.003  1.00 34.08           S  
ANISOU 3510  SD  MET B 204     4879   4416   3654   -851   1368   -453       S  
ATOM   3511  CE  MET B 204     -18.664   1.704  34.485  1.00 34.56           C  
ANISOU 3511  CE  MET B 204     4720   4707   3701   -992   1427   -687       C  
ATOM   3512  N   LEU B 205     -23.611   0.003  37.406  1.00 27.75           N  
ANISOU 3512  N   LEU B 205     3547   3686   3311   -111   1093   -384       N  
ATOM   3513  CA  LEU B 205     -24.646   0.161  38.418  1.00 27.64           C  
ANISOU 3513  CA  LEU B 205     3499   3587   3416     68   1101   -325       C  
ATOM   3514  C   LEU B 205     -24.037   0.401  39.796  1.00 27.89           C  
ANISOU 3514  C   LEU B 205     3538   3609   3450     59   1195   -454       C  
ATOM   3515  O   LEU B 205     -24.685   0.953  40.685  1.00 28.42           O  
ANISOU 3515  O   LEU B 205     3655   3565   3578    176   1250   -426       O  
ATOM   3516  CB  LEU B 205     -25.546  -1.075  38.451  1.00 26.75           C  
ANISOU 3516  CB  LEU B 205     3202   3568   3393    189   1011   -271       C  
ATOM   3517  CG  LEU B 205     -26.262  -1.416  37.143  1.00 27.21           C  
ANISOU 3517  CG  LEU B 205     3237   3653   3448    199    888   -157       C  
ATOM   3518  CD1 LEU B 205     -27.013  -2.732  37.266  1.00 26.45           C  
ANISOU 3518  CD1 LEU B 205     2948   3652   3448    277    803   -139       C  
ATOM   3519  CD2 LEU B 205     -27.206  -0.292  36.746  1.00 28.70           C  
ANISOU 3519  CD2 LEU B 205     3537   3696   3672    297    867     -2       C  
ATOM   3520  N   PHE B 206     -22.786  -0.012  39.967  1.00 48.14           N  
ANISOU 3520  N   PHE B 206     6051   6298   5944    -75   1212   -599       N  
ATOM   3521  CA  PHE B 206     -22.109   0.121  41.251  1.00 46.99           C  
ANISOU 3521  CA  PHE B 206     5897   6177   5781    -92   1269   -733       C  
ATOM   3522  C   PHE B 206     -20.979   1.143  41.196  1.00 48.47           C  
ANISOU 3522  C   PHE B 206     6207   6321   5891   -282   1338   -842       C  
ATOM   3523  O   PHE B 206     -20.340   1.427  42.209  1.00 48.35           O  
ANISOU 3523  O   PHE B 206     6205   6318   5849   -324   1374   -967       O  
ATOM   3524  CB  PHE B 206     -21.565  -1.234  41.711  1.00 45.00           C  
ANISOU 3524  CB  PHE B 206     5464   6110   5523    -73   1219   -821       C  
ATOM   3525  CG  PHE B 206     -22.629  -2.269  41.942  1.00 43.50           C  
ANISOU 3525  CG  PHE B 206     5164   5946   5420     94   1170   -724       C  
ATOM   3526  CD1 PHE B 206     -23.226  -2.403  43.184  1.00 42.55           C  
ANISOU 3526  CD1 PHE B 206     5027   5797   5343    230   1204   -709       C  
ATOM   3527  CD2 PHE B 206     -23.033  -3.109  40.918  1.00 43.55           C  
ANISOU 3527  CD2 PHE B 206     5090   5999   5458    103   1096   -654       C  
ATOM   3528  CE1 PHE B 206     -24.206  -3.355  43.400  1.00 41.25           C  
ANISOU 3528  CE1 PHE B 206     4756   5650   5267    362   1178   -615       C  
ATOM   3529  CE2 PHE B 206     -24.012  -4.062  41.129  1.00 42.96           C  
ANISOU 3529  CE2 PHE B 206     4909   5939   5477    229   1051   -572       C  
ATOM   3530  CZ  PHE B 206     -24.599  -4.184  42.372  1.00 41.41           C  
ANISOU 3530  CZ  PHE B 206     4684   5712   5338    354   1099   -548       C  
ATOM   3531  N   THR B 207     -20.738   1.697  40.012  1.00 36.91           N  
ANISOU 3531  N   THR B 207     4837   4805   4382   -406   1354   -793       N  
ATOM   3532  CA  THR B 207     -19.639   2.639  39.820  1.00 38.54           C  
ANISOU 3532  CA  THR B 207     5154   4970   4521   -623   1435   -889       C  
ATOM   3533  C   THR B 207     -20.068   4.090  40.039  1.00 41.30           C  
ANISOU 3533  C   THR B 207     5737   5069   4885   -630   1511   -836       C  
ATOM   3534  O   THR B 207     -19.376   4.853  40.713  1.00 42.23           O  
ANISOU 3534  O   THR B 207     5938   5123   4983   -753   1578   -958       O  
ATOM   3535  CB  THR B 207     -19.009   2.493  38.420  1.00 38.72           C  
ANISOU 3535  CB  THR B 207     5175   5068   4469   -781   1445   -870       C  
ATOM   3536  OG1 THR B 207     -18.518   1.157  38.250  1.00 36.03           O  
ANISOU 3536  OG1 THR B 207     4625   4948   4117   -773   1390   -945       O  
ATOM   3537  CG2 THR B 207     -17.859   3.473  38.245  1.00 41.16           C  
ANISOU 3537  CG2 THR B 207     5586   5333   4720  -1028   1551   -965       C  
ATOM   3538  N   VAL B 208     -21.210   4.466  39.474  1.00 45.74           N  
ANISOU 3538  N   VAL B 208     6405   5488   5488   -494   1493   -660       N  
ATOM   3539  CA  VAL B 208     -21.695   5.839  39.577  1.00 48.35           C  
ANISOU 3539  CA  VAL B 208     6972   5556   5844   -465   1565   -589       C  
ATOM   3540  C   VAL B 208     -22.876   5.964  40.536  1.00 47.87           C  
ANISOU 3540  C   VAL B 208     6914   5393   5881   -218   1567   -537       C  
ATOM   3541  O   VAL B 208     -23.430   4.962  40.988  1.00 45.91           O  
ANISOU 3541  O   VAL B 208     6484   5279   5682    -73   1509   -527       O  
ATOM   3542  CB  VAL B 208     -22.110   6.394  38.201  1.00 51.32           C  
ANISOU 3542  CB  VAL B 208     7498   5814   6188   -479   1553   -410       C  
ATOM   3543  CG1 VAL B 208     -20.902   6.495  37.285  1.00 51.95           C  
ANISOU 3543  CG1 VAL B 208     7619   5963   6156   -743   1598   -463       C  
ATOM   3544  CG2 VAL B 208     -23.190   5.519  37.581  1.00 51.30           C  
ANISOU 3544  CG2 VAL B 208     7366   5903   6221   -292   1429   -263       C  
ATOM   3545  N   GLY B 209     -23.253   7.202  40.843  1.00 57.95           N  
ANISOU 3545  N   GLY B 209     8405   6423   7189   -172   1649   -506       N  
ATOM   3546  CA  GLY B 209     -24.383   7.458  41.718  1.00 56.44           C  
ANISOU 3546  CA  GLY B 209     8234   6118   7093     72   1680   -460       C  
ATOM   3547  C   GLY B 209     -24.522   8.922  42.092  1.00 57.08           C  
ANISOU 3547  C   GLY B 209     8588   5906   7194     87   1793   -471       C  
ATOM   3548  O   GLY B 209     -23.727   9.758  41.666  1.00 60.06           O  
ANISOU 3548  O   GLY B 209     9149   6157   7515   -111   1844   -508       O  
ATOM   3549  N   LEU B 210     -25.537   9.233  42.892  1.00 47.65           N  
ANISOU 3549  N   LEU B 210     7425   4595   6086    320   1847   -440       N  
ATOM   3550  CA  LEU B 210     -25.777  10.606  43.324  1.00 48.43           C  
ANISOU 3550  CA  LEU B 210     7794   4392   6215    373   1967   -460       C  
ATOM   3551  C   LEU B 210     -24.919  10.991  44.525  1.00 47.28           C  
ANISOU 3551  C   LEU B 210     7753   4211   5999    232   2055   -698       C  
ATOM   3552  O   LEU B 210     -24.799  10.231  45.485  1.00 45.32           O  
ANISOU 3552  O   LEU B 210     7359   4142   5717    261   2045   -813       O  
ATOM   3553  CB  LEU B 210     -27.256  10.820  43.655  1.00 47.77           C  
ANISOU 3553  CB  LEU B 210     7697   4193   6259    702   2003   -332       C  
ATOM   3554  CG  LEU B 210     -28.223  10.923  42.475  1.00 49.42           C  
ANISOU 3554  CG  LEU B 210     7880   4347   6552    864   1920    -88       C  
ATOM   3555  CD1 LEU B 210     -29.627  11.244  42.961  1.00 48.54           C  
ANISOU 3555  CD1 LEU B 210     7744   4114   6585   1194   1975     12       C  
ATOM   3556  CD2 LEU B 210     -27.743  11.971  41.484  1.00 51.95           C  
ANISOU 3556  CD2 LEU B 210     8463   4454   6823    730   1927    -12       C  
ATOM   3557  N   GLN B 211     -24.323  12.177  44.460  1.00 63.00           N  
ANISOU 3557  N   GLN B 211    10009   5967   7962     74   2136   -768       N  
ATOM   3558  CA  GLN B 211     -23.548  12.716  45.572  1.00 62.31           C  
ANISOU 3558  CA  GLN B 211    10054   5813   7809    -73   2213  -1006       C  
ATOM   3559  C   GLN B 211     -23.796  14.212  45.731  1.00 63.56           C  
ANISOU 3559  C   GLN B 211    10553   5589   8006    -53   2342  -1022       C  
ATOM   3560  O   GLN B 211     -23.993  14.926  44.748  1.00 65.33           O  
ANISOU 3560  O   GLN B 211    10938   5609   8275    -62   2363   -872       O  
ATOM   3561  CB  GLN B 211     -22.053  12.454  45.378  1.00 62.10           C  
ANISOU 3561  CB  GLN B 211     9960   5951   7684   -414   2164  -1155       C  
ATOM   3562  CG  GLN B 211     -21.630  11.010  45.594  1.00 60.08           C  
ANISOU 3562  CG  GLN B 211     9390   6059   7377   -431   2053  -1208       C  
ATOM   3563  CD  GLN B 211     -20.125  10.835  45.555  1.00 60.31           C  
ANISOU 3563  CD  GLN B 211     9342   6249   7322   -746   2013  -1381       C  
ATOM   3564  OE1 GLN B 211     -19.384  11.784  45.294  1.00 61.21           O  
ANISOU 3564  OE1 GLN B 211     9625   6212   7419   -981   2074  -1458       O  
ATOM   3565  NE2 GLN B 211     -19.663   9.618  45.819  1.00 59.37           N  
ANISOU 3565  NE2 GLN B 211     8961   6436   7160   -754   1916  -1441       N  
ATOM   3566  N   ASN B 212     -23.785  14.680  46.974  1.00 57.87           N  
ANISOU 3566  N   ASN B 212     9961   4766   7259    -20   2428  -1203       N  
ATOM   3567  CA  ASN B 212     -23.978  16.095  47.258  1.00 59.22           C  
ANISOU 3567  CA  ASN B 212    10478   4555   7465     -4   2562  -1255       C  
ATOM   3568  C   ASN B 212     -22.648  16.776  47.565  1.00 60.44           C  
ANISOU 3568  C   ASN B 212    10807   4623   7532   -366   2591  -1484       C  
ATOM   3569  O   ASN B 212     -22.092  16.614  48.651  1.00 61.29           O  
ANISOU 3569  O   ASN B 212    10894   4842   7551   -466   2585  -1712       O  
ATOM   3570  CB  ASN B 212     -24.956  16.278  48.421  1.00 60.29           C  
ANISOU 3570  CB  ASN B 212    10677   4599   7631    287   2661  -1315       C  
ATOM   3571  CG  ASN B 212     -25.581  17.661  48.449  1.00 63.70           C  
ANISOU 3571  CG  ASN B 212    11447   4608   8148    427   2806  -1287       C  
ATOM   3572  OD1 ASN B 212     -24.980  18.639  48.004  1.00 65.41           O  
ANISOU 3572  OD1 ASN B 212    11920   4568   8363    228   2849  -1319       O  
ATOM   3573  ND2 ASN B 212     -26.797  17.748  48.976  1.00 64.43           N  
ANISOU 3573  ND2 ASN B 212    11540   4619   8321    775   2892  -1224       N  
ATOM   3574  N   LEU B 213     -22.143  17.537  46.599  1.00 66.05           N  
ANISOU 3574  N   LEU B 213    11690   5139   8265   -569   2620  -1418       N  
ATOM   3575  CA  LEU B 213     -20.851  18.198  46.738  1.00 66.99           C  
ANISOU 3575  CA  LEU B 213    11956   5172   8323   -952   2654  -1622       C  
ATOM   3576  C   LEU B 213     -21.031  19.682  47.043  1.00 70.51           C  
ANISOU 3576  C   LEU B 213    12810   5164   8814   -973   2801  -1688       C  
ATOM   3577  O   LEU B 213     -20.407  20.534  46.413  1.00 72.58           O  
ANISOU 3577  O   LEU B 213    13283   5204   9091  -1230   2862  -1686       O  
ATOM   3578  CB  LEU B 213     -20.031  18.025  45.459  1.00 66.49           C  
ANISOU 3578  CB  LEU B 213    11806   5210   8245  -1218   2610  -1521       C  
ATOM   3579  CG  LEU B 213     -19.986  16.610  44.877  1.00 64.74           C  
ANISOU 3579  CG  LEU B 213    11218   5384   7996  -1160   2479  -1408       C  
ATOM   3580  CD1 LEU B 213     -19.165  16.578  43.597  1.00 66.54           C  
ANISOU 3580  CD1 LEU B 213    11409   5675   8199  -1422   2471  -1318       C  
ATOM   3581  CD2 LEU B 213     -19.440  15.621  45.894  1.00 62.76           C  
ANISOU 3581  CD2 LEU B 213    10700   5471   7675  -1196   2388  -1606       C  
ATOM   3582  N   SER B 214     -21.883  19.983  48.016  1.00 91.33           N  
ANISOU 3582  N   SER B 214    15569   7657  11474   -704   2872  -1749       N  
ATOM   3583  CA  SER B 214     -22.217  21.366  48.339  1.00 94.71           C  
ANISOU 3583  CA  SER B 214    16324   7712  11949   -652   2982  -1767       C  
ATOM   3584  C   SER B 214     -21.160  22.042  49.206  1.00 96.88           C  
ANISOU 3584  C   SER B 214    16695   7976  12137   -966   2972  -2023       C  
ATOM   3585  O   SER B 214     -21.176  23.260  49.380  1.00101.37           O  
ANISOU 3585  O   SER B 214    17517   8262  12736  -1024   3040  -2037       O  
ATOM   3586  CB  SER B 214     -23.579  21.434  49.036  1.00 93.35           C  
ANISOU 3586  CB  SER B 214    16147   7492  11828   -229   3027  -1698       C  
ATOM   3587  OG  SER B 214     -24.600  20.891  48.217  1.00 92.08           O  
ANISOU 3587  OG  SER B 214    15876   7342  11769     72   3024  -1448       O  
ATOM   3588  N   GLY B 215     -20.240  21.248  49.744  1.00 96.44           N  
ANISOU 3588  N   GLY B 215    16430   8237  11976  -1161   2876  -2222       N  
ATOM   3589  CA  GLY B 215     -19.267  21.749  50.696  1.00 98.14           C  
ANISOU 3589  CA  GLY B 215    16689   8497  12104  -1427   2832  -2472       C  
ATOM   3590  C   GLY B 215     -19.673  21.324  52.092  1.00 97.62           C  
ANISOU 3590  C   GLY B 215    16537   8607  11945  -1231   2784  -2611       C  
ATOM   3591  O   GLY B 215     -18.841  21.188  52.988  1.00 97.74           O  
ANISOU 3591  O   GLY B 215    16480   8807  11851  -1417   2689  -2826       O  
ATOM   3592  N   ASP B 216     -20.974  21.121  52.267  1.00100.14           N  
ANISOU 3592  N   ASP B 216    16859   8880  12309   -847   2846  -2473       N  
ATOM   3593  CA  ASP B 216     -21.519  20.559  53.494  1.00 99.46           C  
ANISOU 3593  CA  ASP B 216    16663   8991  12137   -622   2818  -2553       C  
ATOM   3594  C   ASP B 216     -22.508  19.459  53.128  1.00 95.46           C  
ANISOU 3594  C   ASP B 216    15944   8642  11682   -316   2829  -2358       C  
ATOM   3595  O   ASP B 216     -22.961  18.702  53.987  1.00 93.52           O  
ANISOU 3595  O   ASP B 216    15546   8616  11369   -131   2804  -2380       O  
ATOM   3596  CB  ASP B 216     -22.200  21.641  54.335  1.00102.56           C  
ANISOU 3596  CB  ASP B 216    17290   9143  12535   -453   2913  -2607       C  
ATOM   3597  CG  ASP B 216     -23.307  22.354  53.584  1.00104.47           C  
ANISOU 3597  CG  ASP B 216    17685   9073  12935   -200   3041  -2390       C  
ATOM   3598  OD1 ASP B 216     -23.187  22.513  52.351  1.00104.92           O  
ANISOU 3598  OD1 ASP B 216    17787   8993  13085   -280   3056  -2240       O  
ATOM   3599  OD2 ASP B 216     -24.299  22.755  54.228  1.00106.16           O  
ANISOU 3599  OD2 ASP B 216    17970   9191  13176     82   3123  -2366       O  
ATOM   3600  N   GLY B 217     -22.834  19.382  51.841  1.00 64.76           N  
ANISOU 3600  N   GLY B 217    12051   4641   7914   -272   2865  -2160       N  
ATOM   3601  CA  GLY B 217     -23.711  18.350  51.318  1.00 61.97           C  
ANISOU 3601  CA  GLY B 217    11487   4431   7627    -10   2863  -1968       C  
ATOM   3602  C   GLY B 217     -25.137  18.434  51.827  1.00 62.54           C  
ANISOU 3602  C   GLY B 217    11536   4451   7774    385   2938  -1839       C  
ATOM   3603  O   GLY B 217     -25.754  17.413  52.129  1.00 60.50           O  
ANISOU 3603  O   GLY B 217    11042   4431   7515    584   2917  -1770       O  
ATOM   3604  N   THR B 218     -25.666  19.651  51.918  1.00 71.15           N  
ANISOU 3604  N   THR B 218    12857   5242   8936    494   3027  -1803       N  
ATOM   3605  CA  THR B 218     -27.002  19.859  52.472  1.00 72.32           C  
ANISOU 3605  CA  THR B 218    12976   5343   9158    855   3105  -1703       C  
ATOM   3606  C   THR B 218     -27.922  20.626  51.526  1.00 73.93           C  
ANISOU 3606  C   THR B 218    13286   5272   9531   1071   3164  -1477       C  
ATOM   3607  O   THR B 218     -29.087  20.864  51.843  1.00 75.19           O  
ANISOU 3607  O   THR B 218    13399   5392   9778   1378   3225  -1378       O  
ATOM   3608  CB  THR B 218     -26.941  20.622  53.809  1.00 75.08           C  
ANISOU 3608  CB  THR B 218    13486   5626   9415    846   3160  -1904       C  
ATOM   3609  OG1 THR B 218     -26.457  21.951  53.583  1.00 78.16           O  
ANISOU 3609  OG1 THR B 218    14179   5694   9823    685   3204  -1976       O  
ATOM   3610  CG2 THR B 218     -26.021  19.913  54.789  1.00 73.89           C  
ANISOU 3610  CG2 THR B 218    13239   5754   9083    644   3074  -2119       C  
ATOM   3611  N   HIS B 219     -27.397  21.011  50.368  1.00 68.52           N  
ANISOU 3611  N   HIS B 219    12735   4412   8888    907   3140  -1391       N  
ATOM   3612  CA  HIS B 219     -28.150  21.819  49.415  1.00 70.44           C  
ANISOU 3612  CA  HIS B 219    13110   4385   9271   1091   3171  -1165       C  
ATOM   3613  C   HIS B 219     -28.398  21.037  48.127  1.00 68.13           C  
ANISOU 3613  C   HIS B 219    12661   4173   9052   1164   3092   -930       C  
ATOM   3614  O   HIS B 219     -27.451  20.599  47.474  1.00 66.47           O  
ANISOU 3614  O   HIS B 219    12456   4015   8783    897   3041   -950       O  
ATOM   3615  CB  HIS B 219     -27.393  23.121  49.127  1.00 73.42           C  
ANISOU 3615  CB  HIS B 219    13822   4446   9628    848   3211  -1227       C  
ATOM   3616  CG  HIS B 219     -28.178  24.132  48.347  1.00 76.18           C  
ANISOU 3616  CG  HIS B 219    14348   4497  10102   1050   3246  -1010       C  
ATOM   3617  ND1 HIS B 219     -27.869  25.477  48.357  1.00 79.56           N  
ANISOU 3617  ND1 HIS B 219    15089   4609  10531    897   3301  -1040       N  
ATOM   3618  CD2 HIS B 219     -29.246  24.001  47.525  1.00 76.33           C  
ANISOU 3618  CD2 HIS B 219    14258   4496  10247   1393   3220   -758       C  
ATOM   3619  CE1 HIS B 219     -28.718  26.128  47.584  1.00 81.65           C  
ANISOU 3619  CE1 HIS B 219    15448   4665  10911   1149   3310   -811       C  
ATOM   3620  NE2 HIS B 219     -29.563  25.255  47.064  1.00 79.77           N  
ANISOU 3620  NE2 HIS B 219    14949   4609  10750   1453   3253   -639       N  
ATOM   3621  N   PRO B 220     -29.681  20.855  47.768  1.00102.26           N  
ANISOU 3621  N   PRO B 220    16831   8521  13504   1519   3075   -711       N  
ATOM   3622  CA  PRO B 220     -30.144  20.143  46.569  1.00100.59           C  
ANISOU 3622  CA  PRO B 220    16456   8387  13375   1647   2978   -460       C  
ATOM   3623  C   PRO B 220     -29.451  20.574  45.275  1.00101.01           C  
ANISOU 3623  C   PRO B 220    16722   8252  13405   1434   2932   -343       C  
ATOM   3624  O   PRO B 220     -29.373  19.783  44.335  1.00 99.22           O  
ANISOU 3624  O   PRO B 220    16283   8265  13152   1364   2784   -194       O  
ATOM   3625  CB  PRO B 220     -31.627  20.509  46.510  1.00103.32           C  
ANISOU 3625  CB  PRO B 220    16713   8678  13868   2035   2975   -270       C  
ATOM   3626  CG  PRO B 220     -32.011  20.676  47.933  1.00104.42           C  
ANISOU 3626  CG  PRO B 220    16793   8891  13992   2136   3072   -446       C  
ATOM   3627  CD  PRO B 220     -30.810  21.273  48.620  1.00104.65           C  
ANISOU 3627  CD  PRO B 220    17066   8822  13874   1820   3141   -712       C  
ATOM   3628  N   GLY B 221     -28.961  21.808  45.230  1.00 76.20           N  
ANISOU 3628  N   GLY B 221    13889   4829  10234   1278   2992   -391       N  
ATOM   3629  CA  GLY B 221     -28.285  22.316  44.051  1.00 77.53           C  
ANISOU 3629  CA  GLY B 221    14273   4816  10367   1050   2965   -271       C  
ATOM   3630  C   GLY B 221     -26.979  21.600  43.761  1.00 75.06           C  
ANISOU 3630  C   GLY B 221    13874   4715   9928    649   2915   -390       C  
ATOM   3631  O   GLY B 221     -26.532  21.547  42.615  1.00 75.85           O  
ANISOU 3631  O   GLY B 221    13989   4850   9978    473   2842   -243       O  
ATOM   3632  N   GLY B 222     -26.365  21.047  44.802  1.00 65.96           N  
ANISOU 3632  N   GLY B 222    12579   3779   8704    502   2926   -648       N  
ATOM   3633  CA  GLY B 222     -25.097  20.355  44.661  1.00 63.05           C  
ANISOU 3633  CA  GLY B 222    12049   3694   8211    125   2849   -781       C  
ATOM   3634  C   GLY B 222     -25.248  18.861  44.448  1.00 58.19           C  
ANISOU 3634  C   GLY B 222    11020   3525   7564    183   2700   -711       C  
ATOM   3635  O   GLY B 222     -24.264  18.123  44.464  1.00 55.66           O  
ANISOU 3635  O   GLY B 222    10520   3477   7148    -80   2631   -828       O  
ATOM   3636  N   LEU B 223     -26.484  18.414  44.248  1.00 58.33           N  
ANISOU 3636  N   LEU B 223    10880   3613   7670    529   2650   -522       N  
ATOM   3637  CA  LEU B 223     -26.759  16.999  44.022  1.00 54.33           C  
ANISOU 3637  CA  LEU B 223     9992   3499   7151    601   2512   -448       C  
ATOM   3638  C   LEU B 223     -26.444  16.603  42.583  1.00 53.40           C  
ANISOU 3638  C   LEU B 223     9795   3503   6990    468   2390   -268       C  
ATOM   3639  O   LEU B 223     -27.244  16.834  41.677  1.00 54.29           O  
ANISOU 3639  O   LEU B 223     9944   3521   7161    651   2338    -34       O  
ATOM   3640  CB  LEU B 223     -28.218  16.679  44.356  1.00 54.45           C  
ANISOU 3640  CB  LEU B 223     9853   3547   7289   1000   2511   -324       C  
ATOM   3641  CG  LEU B 223     -28.663  15.229  44.164  1.00 51.31           C  
ANISOU 3641  CG  LEU B 223     9067   3526   6902   1088   2377   -240       C  
ATOM   3642  CD1 LEU B 223     -27.752  14.285  44.929  1.00 49.01           C  
ANISOU 3642  CD1 LEU B 223     8608   3513   6501    875   2354   -447       C  
ATOM   3643  CD2 LEU B 223     -30.110  15.050  44.597  1.00 51.99           C  
ANISOU 3643  CD2 LEU B 223     9007   3618   7129   1463   2407   -137       C  
ATOM   3644  N   VAL B 224     -25.277  16.001  42.380  1.00 48.74           N  
ANISOU 3644  N   VAL B 224     9095   3132   6292    157   2343   -382       N  
ATOM   3645  CA  VAL B 224     -24.824  15.642  41.040  1.00 47.22           C  
ANISOU 3645  CA  VAL B 224     8852   3057   6033     -4   2256   -245       C  
ATOM   3646  C   VAL B 224     -24.654  14.136  40.864  1.00 42.96           C  
ANISOU 3646  C   VAL B 224     7955   2919   5449    -31   2128   -260       C  
ATOM   3647  O   VAL B 224     -24.613  13.386  41.838  1.00 41.31           O  
ANISOU 3647  O   VAL B 224     7550   2901   5244      7   2113   -403       O  
ATOM   3648  CB  VAL B 224     -23.491  16.333  40.696  1.00 48.93           C  
ANISOU 3648  CB  VAL B 224     9268   3161   6164   -379   2336   -349       C  
ATOM   3649  CG1 VAL B 224     -23.658  17.838  40.728  1.00 53.55           C  
ANISOU 3649  CG1 VAL B 224    10240   3310   6796   -375   2468   -324       C  
ATOM   3650  CG2 VAL B 224     -22.399  15.891  41.659  1.00 47.71           C  
ANISOU 3650  CG2 VAL B 224     8968   3208   5951   -616   2349   -627       C  
ATOM   3651  N   CYS B 225     -24.558  13.706  39.609  1.00 54.49           N  
ANISOU 3651  N   CYS B 225     9353   4495   6856    -94   2039   -110       N  
ATOM   3652  CA  CYS B 225     -24.327  12.303  39.284  1.00 54.01           C  
ANISOU 3652  CA  CYS B 225     8986   4789   6747   -137   1923   -125       C  
ATOM   3653  C   CYS B 225     -22.854  12.082  38.954  1.00 54.00           C  
ANISOU 3653  C   CYS B 225     8957   4928   6633   -482   1949   -261       C  
ATOM   3654  O   CYS B 225     -22.358  12.554  37.931  1.00 55.11           O  
ANISOU 3654  O   CYS B 225     9245   4994   6702   -653   1978   -181       O  
ATOM   3655  CB  CYS B 225     -25.207  11.873  38.110  1.00 55.68           C  
ANISOU 3655  CB  CYS B 225     9126   5067   6963     26   1797    109       C  
ATOM   3656  SG  CYS B 225     -25.067  10.128  37.672  1.00 56.16           S  
ANISOU 3656  SG  CYS B 225     8832   5530   6978     -6   1654     84       S  
ATOM   3657  N   THR B 226     -22.164  11.357  39.827  1.00 57.46           N  
ANISOU 3657  N   THR B 226     9200   5577   7055   -576   1941   -462       N  
ATOM   3658  CA  THR B 226     -20.718  11.194  39.732  1.00 57.96           C  
ANISOU 3658  CA  THR B 226     9209   5778   7036   -892   1975   -625       C  
ATOM   3659  C   THR B 226     -20.319   9.776  40.141  1.00 56.02           C  
ANISOU 3659  C   THR B 226     8643   5872   6770   -886   1886   -740       C  
ATOM   3660  O   THR B 226     -21.055   9.116  40.879  1.00 54.06           O  
ANISOU 3660  O   THR B 226     8260   5706   6573   -668   1828   -739       O  
ATOM   3661  CB  THR B 226     -20.005  12.229  40.638  1.00 57.07           C  
ANISOU 3661  CB  THR B 226     9275   5483   6927  -1067   2086   -807       C  
ATOM   3662  OG1 THR B 226     -18.592  11.997  40.640  1.00 56.51           O  
ANISOU 3662  OG1 THR B 226     9093   5584   6792  -1375   2105   -983       O  
ATOM   3663  CG2 THR B 226     -20.528  12.139  42.062  1.00 55.48           C  
ANISOU 3663  CG2 THR B 226     9037   5268   6774   -882   2081   -919       C  
ATOM   3664  N   PRO B 227     -19.170   9.288  39.638  1.00 61.49           N  
ANISOU 3664  N   PRO B 227     9212   6757   7393  -1118   1884   -831       N  
ATOM   3665  CA  PRO B 227     -18.635   8.002  40.101  1.00 58.23           C  
ANISOU 3665  CA  PRO B 227     8510   6649   6967  -1119   1807   -960       C  
ATOM   3666  C   PRO B 227     -18.447   7.983  41.615  1.00 55.46           C  
ANISOU 3666  C   PRO B 227     8110   6326   6637  -1081   1802  -1132       C  
ATOM   3667  O   PRO B 227     -17.746   8.834  42.163  1.00 55.90           O  
ANISOU 3667  O   PRO B 227     8281   6282   6675  -1253   1867  -1271       O  
ATOM   3668  CB  PRO B 227     -17.278   7.902  39.386  1.00 56.75           C  
ANISOU 3668  CB  PRO B 227     8251   6602   6710  -1406   1850  -1052       C  
ATOM   3669  CG  PRO B 227     -17.022   9.268  38.801  1.00 60.14           C  
ANISOU 3669  CG  PRO B 227     8951   6780   7117  -1593   1969  -1001       C  
ATOM   3670  CD  PRO B 227     -18.374   9.833  38.528  1.00 61.94           C  
ANISOU 3670  CD  PRO B 227     9385   6767   7382  -1369   1958   -797       C  
ATOM   3671  N   ILE B 228     -19.076   7.017  42.278  1.00 31.88           N  
ANISOU 3671  N   ILE B 228     4962   3473   3677   -865   1725  -1122       N  
ATOM   3672  CA  ILE B 228     -19.082   6.958  43.736  1.00 32.60           C  
ANISOU 3672  CA  ILE B 228     5033   3588   3767   -786   1720  -1254       C  
ATOM   3673  C   ILE B 228     -18.015   6.022  44.292  1.00 32.55           C  
ANISOU 3673  C   ILE B 228     4805   3855   3707   -877   1648  -1417       C  
ATOM   3674  O   ILE B 228     -17.930   5.820  45.503  1.00 33.12           O  
ANISOU 3674  O   ILE B 228     4845   3990   3750   -812   1621  -1527       O  
ATOM   3675  CB  ILE B 228     -20.453   6.509  44.271  1.00 31.72           C  
ANISOU 3675  CB  ILE B 228     4895   3442   3716   -486   1701  -1136       C  
ATOM   3676  CG1 ILE B 228     -20.805   5.122  43.729  1.00 29.79           C  
ANISOU 3676  CG1 ILE B 228     4422   3400   3496   -376   1608  -1036       C  
ATOM   3677  CG2 ILE B 228     -21.524   7.523  43.902  1.00 32.25           C  
ANISOU 3677  CG2 ILE B 228     5171   3236   3849   -366   1769   -988       C  
ATOM   3678  CD1 ILE B 228     -22.148   4.604  44.195  1.00 29.11           C  
ANISOU 3678  CD1 ILE B 228     4279   3297   3486   -110   1594   -917       C  
ATOM   3679  N   VAL B 229     -17.206   5.451  43.409  1.00 31.91           N  
ANISOU 3679  N   VAL B 229     4578   3939   3606  -1017   1618  -1432       N  
ATOM   3680  CA  VAL B 229     -16.147   4.543  43.831  1.00 32.05           C  
ANISOU 3680  CA  VAL B 229     4368   4223   3589  -1087   1547  -1580       C  
ATOM   3681  C   VAL B 229     -14.808   5.266  43.907  1.00 33.88           C  
ANISOU 3681  C   VAL B 229     4599   4490   3784  -1374   1584  -1756       C  
ATOM   3682  O   VAL B 229     -14.675   6.395  43.435  1.00 34.98           O  
ANISOU 3682  O   VAL B 229     4920   4443   3927  -1542   1677  -1749       O  
ATOM   3683  CB  VAL B 229     -16.019   3.342  42.878  1.00 30.84           C  
ANISOU 3683  CB  VAL B 229     4019   4255   3444  -1043   1496  -1510       C  
ATOM   3684  CG1 VAL B 229     -17.342   2.598  42.783  1.00 29.25           C  
ANISOU 3684  CG1 VAL B 229     3805   4018   3289   -788   1452  -1344       C  
ATOM   3685  CG2 VAL B 229     -15.554   3.801  41.504  1.00 31.30           C  
ANISOU 3685  CG2 VAL B 229     4122   4286   3486  -1234   1565  -1469       C  
ATOM   3686  N   ASP B 230     -13.818   4.610  44.505  1.00 73.42           N  
ANISOU 3686  N   ASP B 230     9398   9735   8764  -1429   1507  -1911       N  
ATOM   3687  CA  ASP B 230     -12.485   5.190  44.633  1.00 75.59           C  
ANISOU 3687  CA  ASP B 230     9613  10089   9019  -1708   1523  -2097       C  
ATOM   3688  C   ASP B 230     -11.750   5.210  43.296  1.00 76.62           C  
ANISOU 3688  C   ASP B 230     9661  10284   9168  -1906   1600  -2077       C  
ATOM   3689  O   ASP B 230     -12.252   4.698  42.297  1.00 76.12           O  
ANISOU 3689  O   ASP B 230     9589  10220   9114  -1813   1624  -1928       O  
ATOM   3690  CB  ASP B 230     -11.666   4.442  45.689  1.00 75.40           C  
ANISOU 3690  CB  ASP B 230     9369  10323   8959  -1682   1395  -2262       C  
ATOM   3691  CG  ASP B 230     -11.735   2.934  45.526  1.00 74.94           C  
ANISOU 3691  CG  ASP B 230     9090  10476   8911  -1476   1311  -2196       C  
ATOM   3692  OD1 ASP B 230     -11.826   2.456  44.377  1.00 75.75           O  
ANISOU 3692  OD1 ASP B 230     9133  10601   9049  -1463   1355  -2091       O  
ATOM   3693  OD2 ASP B 230     -11.700   2.225  46.554  1.00 75.01           O  
ANISOU 3693  OD2 ASP B 230     8999  10619   8883  -1329   1201  -2249       O  
ATOM   3694  N   THR B 231     -10.560   5.800  43.290  1.00101.81           N  
ANISOU 3694  N   THR B 231    12788  13536  12358  -2188   1640  -2234       N  
ATOM   3695  CA  THR B 231      -9.767   5.934  42.073  1.00104.06           C  
ANISOU 3695  CA  THR B 231    12999  13883  12655  -2412   1748  -2230       C  
ATOM   3696  C   THR B 231      -9.377   4.577  41.489  1.00103.27           C  
ANISOU 3696  C   THR B 231    12624  14054  12558  -2308   1706  -2218       C  
ATOM   3697  O   THR B 231      -9.439   4.372  40.275  1.00104.31           O  
ANISOU 3697  O   THR B 231    12767  14187  12677  -2334   1791  -2113       O  
ATOM   3698  CB  THR B 231      -8.492   6.765  42.329  1.00105.56           C  
ANISOU 3698  CB  THR B 231    13128  14118  12862  -2750   1798  -2425       C  
ATOM   3699  OG1 THR B 231      -8.850   8.031  42.897  1.00106.33           O  
ANISOU 3699  OG1 THR B 231    13506  13937  12957  -2851   1839  -2452       O  
ATOM   3700  CG2 THR B 231      -7.728   6.994  41.036  1.00106.86           C  
ANISOU 3700  CG2 THR B 231    13238  14326  13038  -2997   1948  -2405       C  
ATOM   3701  N   ALA B 232      -8.989   3.652  42.362  1.00 63.54           N  
ANISOU 3701  N   ALA B 232     7366   9244   7534  -2179   1574  -2325       N  
ATOM   3702  CA  ALA B 232      -8.515   2.334  41.946  1.00 62.91           C  
ANISOU 3702  CA  ALA B 232     7019   9416   7469  -2066   1530  -2338       C  
ATOM   3703  C   ALA B 232      -9.558   1.539  41.161  1.00 62.04           C  
ANISOU 3703  C   ALA B 232     6981   9243   7350  -1846   1534  -2153       C  
ATOM   3704  O   ALA B 232      -9.329   1.170  40.007  1.00 62.80           O  
ANISOU 3704  O   ALA B 232     7022   9400   7438  -1890   1611  -2111       O  
ATOM   3705  CB  ALA B 232      -8.041   1.538  43.155  1.00 64.22           C  
ANISOU 3705  CB  ALA B 232     6971   9790   7638  -1931   1371  -2463       C  
ATOM   3706  N   THR B 233     -10.700   1.276  41.789  1.00 34.72           N  
ANISOU 3706  N   THR B 233     3639   5666   3888  -1618   1456  -2052       N  
ATOM   3707  CA  THR B 233     -11.748   0.477  41.161  1.00 33.27           C  
ANISOU 3707  CA  THR B 233     3502   5432   3710  -1413   1439  -1887       C  
ATOM   3708  C   THR B 233     -12.372   1.195  39.965  1.00 33.20           C  
ANISOU 3708  C   THR B 233     3697   5239   3678  -1495   1540  -1745       C  
ATOM   3709  O   THR B 233     -12.886   0.555  39.044  1.00 32.59           O  
ANISOU 3709  O   THR B 233     3622   5173   3589  -1407   1539  -1639       O  
ATOM   3710  CB  THR B 233     -12.849   0.081  42.165  1.00 31.74           C  
ANISOU 3710  CB  THR B 233     3368   5162   3531  -1163   1345  -1809       C  
ATOM   3711  OG1 THR B 233     -13.544   1.252  42.607  1.00 31.57           O  
ANISOU 3711  OG1 THR B 233     3575   4916   3504  -1178   1385  -1756       O  
ATOM   3712  CG2 THR B 233     -12.243  -0.632  43.365  1.00 32.05           C  
ANISOU 3712  CG2 THR B 233     3236   5378   3565  -1077   1241  -1933       C  
ATOM   3713  N   LEU B 234     -12.327   2.524  39.982  1.00 54.63           N  
ANISOU 3713  N   LEU B 234     6596   7780   6380  -1663   1620  -1744       N  
ATOM   3714  CA  LEU B 234     -12.780   3.307  38.839  1.00 56.61           C  
ANISOU 3714  CA  LEU B 234     7058   7852   6597  -1756   1719  -1605       C  
ATOM   3715  C   LEU B 234     -11.851   3.054  37.661  1.00 57.35           C  
ANISOU 3715  C   LEU B 234     7054   8090   6645  -1932   1810  -1638       C  
ATOM   3716  O   LEU B 234     -12.302   2.874  36.528  1.00 56.41           O  
ANISOU 3716  O   LEU B 234     7021   7938   6473  -1906   1843  -1510       O  
ATOM   3717  CB  LEU B 234     -12.819   4.799  39.172  1.00 58.01           C  
ANISOU 3717  CB  LEU B 234     7468   7795   6778  -1908   1797  -1608       C  
ATOM   3718  CG  LEU B 234     -13.324   5.705  38.047  1.00 59.97           C  
ANISOU 3718  CG  LEU B 234     7975   7824   6988  -1984   1896  -1439       C  
ATOM   3719  CD1 LEU B 234     -14.726   5.300  37.624  1.00 58.30           C  
ANISOU 3719  CD1 LEU B 234     7849   7526   6776  -1722   1821  -1244       C  
ATOM   3720  CD2 LEU B 234     -13.290   7.165  38.472  1.00 62.60           C  
ANISOU 3720  CD2 LEU B 234     8549   7898   7338  -2130   1979  -1454       C  
ATOM   3721  N   LYS B 235     -10.550   3.038  37.937  1.00 37.72           N  
ANISOU 3721  N   LYS B 235     4381   5777   4176  -2110   1849  -1815       N  
ATOM   3722  CA  LYS B 235      -9.566   2.668  36.929  1.00 39.80           C  
ANISOU 3722  CA  LYS B 235     4496   6217   4406  -2263   1951  -1873       C  
ATOM   3723  C   LYS B 235      -9.834   1.251  36.440  1.00 38.76           C  
ANISOU 3723  C   LYS B 235     4226   6239   4261  -2052   1888  -1840       C  
ATOM   3724  O   LYS B 235      -9.681   0.957  35.259  1.00 39.73           O  
ANISOU 3724  O   LYS B 235     4360   6414   4320  -2102   1973  -1797       O  
ATOM   3725  CB  LYS B 235      -8.144   2.770  37.487  1.00 42.02           C  
ANISOU 3725  CB  LYS B 235     4538   6690   4736  -2455   1980  -2084       C  
ATOM   3726  CG  LYS B 235      -7.631   4.190  37.639  1.00 44.15           C  
ANISOU 3726  CG  LYS B 235     4938   6823   5016  -2751   2084  -2138       C  
ATOM   3727  CD  LYS B 235      -6.230   4.210  38.229  1.00 46.74           C  
ANISOU 3727  CD  LYS B 235     4984   7371   5404  -2943   2085  -2362       C  
ATOM   3728  CE  LYS B 235      -5.693   5.628  38.327  1.00 49.62           C  
ANISOU 3728  CE  LYS B 235     5476   7590   5786  -3277   2197  -2428       C  
ATOM   3729  NZ  LYS B 235      -4.339   5.672  38.945  1.00 52.47           N  
ANISOU 3729  NZ  LYS B 235     5548   8176   6212  -3461   2167  -2653       N  
ATOM   3730  N   VAL B 236     -10.246   0.380  37.357  1.00 46.50           N  
ANISOU 3730  N   VAL B 236     5097   7280   5293  -1821   1744  -1860       N  
ATOM   3731  CA  VAL B 236     -10.554  -1.005  37.012  1.00 43.80           C  
ANISOU 3731  CA  VAL B 236     4639   7050   4952  -1615   1676  -1833       C  
ATOM   3732  C   VAL B 236     -11.705  -1.108  36.009  1.00 42.54           C  
ANISOU 3732  C   VAL B 236     4673   6751   4738  -1530   1675  -1657       C  
ATOM   3733  O   VAL B 236     -11.569  -1.757  34.969  1.00 41.62           O  
ANISOU 3733  O   VAL B 236     4526   6718   4569  -1527   1714  -1648       O  
ATOM   3734  CB  VAL B 236     -10.876  -1.846  38.265  1.00 41.93           C  
ANISOU 3734  CB  VAL B 236     4287   6866   4780  -1388   1527  -1864       C  
ATOM   3735  CG1 VAL B 236     -11.392  -3.218  37.870  1.00 39.19           C  
ANISOU 3735  CG1 VAL B 236     3875   6572   4444  -1180   1463  -1809       C  
ATOM   3736  CG2 VAL B 236      -9.645  -1.971  39.149  1.00 43.77           C  
ANISOU 3736  CG2 VAL B 236     4293   7289   5050  -1445   1497  -2044       C  
ATOM   3737  N   VAL B 237     -12.828  -0.463  36.310  1.00 34.42           N  
ANISOU 3737  N   VAL B 237     3843   5518   3719  -1458   1630  -1523       N  
ATOM   3738  CA  VAL B 237     -13.990  -0.527  35.423  1.00 33.33           C  
ANISOU 3738  CA  VAL B 237     3870   5257   3537  -1364   1600  -1350       C  
ATOM   3739  C   VAL B 237     -13.770   0.220  34.104  1.00 34.84           C  
ANISOU 3739  C   VAL B 237     4227   5391   3620  -1546   1715  -1280       C  
ATOM   3740  O   VAL B 237     -14.235  -0.220  33.048  1.00 34.70           O  
ANISOU 3740  O   VAL B 237     4277   5381   3525  -1504   1699  -1192       O  
ATOM   3741  CB  VAL B 237     -15.286  -0.036  36.114  1.00 31.57           C  
ANISOU 3741  CB  VAL B 237     3788   4839   3368  -1213   1522  -1220       C  
ATOM   3742  CG1 VAL B 237     -15.691  -0.995  37.222  1.00 30.22           C  
ANISOU 3742  CG1 VAL B 237     3471   4730   3282  -1011   1415  -1254       C  
ATOM   3743  CG2 VAL B 237     -15.114   1.372  36.659  1.00 32.26           C  
ANISOU 3743  CG2 VAL B 237     4025   4769   3465  -1335   1592  -1227       C  
ATOM   3744  N   ILE B 238     -13.054   1.340  34.162  1.00 35.50           N  
ANISOU 3744  N   ILE B 238     4388   5414   3688  -1757   1831  -1320       N  
ATOM   3745  CA  ILE B 238     -12.747   2.102  32.955  1.00 37.49           C  
ANISOU 3745  CA  ILE B 238     4812   5604   3828  -1952   1965  -1247       C  
ATOM   3746  C   ILE B 238     -11.836   1.306  32.024  1.00 39.18           C  
ANISOU 3746  C   ILE B 238     4885   6036   3967  -2043   2053  -1337       C  
ATOM   3747  O   ILE B 238     -12.101   1.205  30.826  1.00 39.90           O  
ANISOU 3747  O   ILE B 238     5106   6121   3934  -2066   2095  -1242       O  
ATOM   3748  CB  ILE B 238     -12.114   3.470  33.280  1.00 39.32           C  
ANISOU 3748  CB  ILE B 238     5159   5705   4074  -2186   2087  -1279       C  
ATOM   3749  CG1 ILE B 238     -13.163   4.407  33.880  1.00 38.02           C  
ANISOU 3749  CG1 ILE B 238     5220   5273   3955  -2091   2029  -1156       C  
ATOM   3750  CG2 ILE B 238     -11.524   4.098  32.029  1.00 42.12           C  
ANISOU 3750  CG2 ILE B 238     5656   6039   4311  -2422   2258  -1226       C  
ATOM   3751  CD1 ILE B 238     -12.642   5.790  34.192  1.00 39.97           C  
ANISOU 3751  CD1 ILE B 238     5626   5344   4219  -2318   2148  -1186       C  
ATOM   3752  N   GLN B 239     -10.772   0.734  32.580  1.00 39.99           N  
ANISOU 3752  N   GLN B 239     4722   6337   4137  -2082   2077  -1523       N  
ATOM   3753  CA  GLN B 239      -9.870  -0.114  31.806  1.00 41.57           C  
ANISOU 3753  CA  GLN B 239     4755   6744   4294  -2124   2150  -1624       C  
ATOM   3754  C   GLN B 239     -10.596  -1.345  31.279  1.00 40.10           C  
ANISOU 3754  C   GLN B 239     4557   6610   4069  -1908   2053  -1581       C  
ATOM   3755  O   GLN B 239     -10.298  -1.826  30.188  1.00 40.95           O  
ANISOU 3755  O   GLN B 239     4684   6778   4097  -1919   2087  -1577       O  
ATOM   3756  CB  GLN B 239      -8.659  -0.535  32.641  1.00 42.00           C  
ANISOU 3756  CB  GLN B 239     4529   6953   4476  -2123   2096  -1801       C  
ATOM   3757  CG  GLN B 239      -7.668   0.584  32.907  1.00 44.14           C  
ANISOU 3757  CG  GLN B 239     4779   7215   4776  -2380   2201  -1881       C  
ATOM   3758  CD  GLN B 239      -6.610   0.190  33.918  1.00 44.58           C  
ANISOU 3758  CD  GLN B 239     4552   7438   4947  -2362   2118  -2060       C  
ATOM   3759  OE1 GLN B 239      -5.938   1.043  34.495  1.00 46.07           O  
ANISOU 3759  OE1 GLN B 239     4696   7631   5177  -2550   2161  -2151       O  
ATOM   3760  NE2 GLN B 239      -6.459  -1.112  34.138  1.00 43.49           N  
ANISOU 3760  NE2 GLN B 239     4235   7433   4858  -2137   1992  -2108       N  
ATOM   3761  N   LEU B 240     -11.545  -1.853  32.061  1.00 37.70           N  
ANISOU 3761  N   LEU B 240     4237   6250   3839  -1698   1898  -1539       N  
ATOM   3762  CA  LEU B 240     -12.388  -2.954  31.614  1.00 36.26           C  
ANISOU 3762  CA  LEU B 240     4066   6077   3633  -1509   1790  -1486       C  
ATOM   3763  C   LEU B 240     -13.140  -2.551  30.353  1.00 36.41           C  
ANISOU 3763  C   LEU B 240     4332   5993   3509  -1553   1803  -1334       C  
ATOM   3764  O   LEU B 240     -13.159  -3.286  29.363  1.00 37.05           O  
ANISOU 3764  O   LEU B 240     4433   6155   3490  -1537   1816  -1348       O  
ATOM   3765  CB  LEU B 240     -13.388  -3.349  32.700  1.00 33.73           C  
ANISOU 3765  CB  LEU B 240     3718   5671   3429  -1299   1623  -1430       C  
ATOM   3766  CG  LEU B 240     -14.483  -4.324  32.258  1.00 32.17           C  
ANISOU 3766  CG  LEU B 240     3559   5439   3223  -1127   1502  -1348       C  
ATOM   3767  CD1 LEU B 240     -13.920  -5.725  32.066  1.00 32.70           C  
ANISOU 3767  CD1 LEU B 240     3454   5662   3308  -1046   1495  -1480       C  
ATOM   3768  CD2 LEU B 240     -15.642  -4.328  33.241  1.00 29.97           C  
ANISOU 3768  CD2 LEU B 240     3306   5031   3050   -965   1372  -1244       C  
ATOM   3769  N   ASN B 241     -13.753  -1.372  30.397  1.00 54.47           N  
ANISOU 3769  N   ASN B 241     6820   8099   5780  -1602   1796  -1191       N  
ATOM   3770  CA  ASN B 241     -14.511  -0.864  29.259  1.00 56.05           C  
ANISOU 3770  CA  ASN B 241     7270   8188   5839  -1627   1787  -1022       C  
ATOM   3771  C   ASN B 241     -13.647  -0.626  28.023  1.00 56.71           C  
ANISOU 3771  C   ASN B 241     7443   8354   5750  -1827   1958  -1044       C  
ATOM   3772  O   ASN B 241     -14.013  -1.022  26.919  1.00 57.14           O  
ANISOU 3772  O   ASN B 241     7611   8442   5658  -1808   1937   -985       O  
ATOM   3773  CB  ASN B 241     -15.258   0.417  29.638  1.00 58.53           C  
ANISOU 3773  CB  ASN B 241     7779   8275   6186  -1623   1758   -865       C  
ATOM   3774  CG  ASN B 241     -16.079   0.971  28.491  1.00 61.74           C  
ANISOU 3774  CG  ASN B 241     8449   8562   6448  -1622   1726   -669       C  
ATOM   3775  OD1 ASN B 241     -15.662   1.906  27.808  1.00 63.73           O  
ANISOU 3775  OD1 ASN B 241     8890   8740   6586  -1792   1853   -600       O  
ATOM   3776  ND2 ASN B 241     -17.253   0.391  28.269  1.00 63.16           N  
ANISOU 3776  ND2 ASN B 241     8644   8724   6631  -1435   1552   -572       N  
ATOM   3777  N   THR B 242     -12.498   0.015  28.210  1.00 41.30           N  
ANISOU 3777  N   THR B 242     5439   6441   3811  -2028   2129  -1133       N  
ATOM   3778  CA  THR B 242     -11.620   0.336  27.089  1.00 44.48           C  
ANISOU 3778  CA  THR B 242     5923   6920   4056  -2243   2330  -1150       C  
ATOM   3779  C   THR B 242     -10.991  -0.913  26.474  1.00 44.87           C  
ANISOU 3779  C   THR B 242     5802   7162   4087  -2176   2326  -1279       C  
ATOM   3780  O   THR B 242     -10.791  -0.983  25.263  1.00 46.50           O  
ANISOU 3780  O   THR B 242     6129   7399   4141  -2236   2395  -1242       O  
ATOM   3781  CB  THR B 242     -10.503   1.315  27.498  1.00 46.37           C  
ANISOU 3781  CB  THR B 242     6118   7131   4371  -2466   2474  -1215       C  
ATOM   3782  OG1 THR B 242      -9.638   0.689  28.454  1.00 45.70           O  
ANISOU 3782  OG1 THR B 242     5717   7184   4463  -2419   2422  -1404       O  
ATOM   3783  CG2 THR B 242     -11.095   2.578  28.103  1.00 46.03           C  
ANISOU 3783  CG2 THR B 242     6269   6853   4367  -2523   2468  -1094       C  
ATOM   3784  N   PHE B 243     -10.681  -1.896  27.312  1.00 43.40           N  
ANISOU 3784  N   PHE B 243     5350   7079   4062  -2032   2230  -1418       N  
ATOM   3785  CA  PHE B 243     -10.079  -3.137  26.836  1.00 43.62           C  
ANISOU 3785  CA  PHE B 243     5221   7245   4107  -1932   2204  -1532       C  
ATOM   3786  C   PHE B 243     -11.091  -4.038  26.135  1.00 42.81           C  
ANISOU 3786  C   PHE B 243     5229   7152   3886  -1796   2122  -1490       C  
ATOM   3787  O   PHE B 243     -10.843  -4.517  25.030  1.00 44.16           O  
ANISOU 3787  O   PHE B 243     5468   7378   3932  -1812   2172  -1507       O  
ATOM   3788  CB  PHE B 243      -9.419  -3.899  27.988  1.00 42.55           C  
ANISOU 3788  CB  PHE B 243     4797   7195   4175  -1809   2115  -1671       C  
ATOM   3789  CG  PHE B 243      -8.022  -3.440  28.300  1.00 44.21           C  
ANISOU 3789  CG  PHE B 243     4846   7479   4473  -1941   2197  -1775       C  
ATOM   3790  CD1 PHE B 243      -7.145  -3.102  27.283  1.00 46.66           C  
ANISOU 3790  CD1 PHE B 243     5184   7841   4705  -2093   2345  -1796       C  
ATOM   3791  CD2 PHE B 243      -7.586  -3.349  29.612  1.00 43.58           C  
ANISOU 3791  CD2 PHE B 243     4586   7429   4542  -1916   2126  -1855       C  
ATOM   3792  CE1 PHE B 243      -5.859  -2.682  27.568  1.00 48.46           C  
ANISOU 3792  CE1 PHE B 243     5247   8150   5017  -2223   2425  -1901       C  
ATOM   3793  CE2 PHE B 243      -6.302  -2.929  29.903  1.00 45.37           C  
ANISOU 3793  CE2 PHE B 243     4655   7745   4839  -2048   2189  -1965       C  
ATOM   3794  CZ  PHE B 243      -5.437  -2.595  28.880  1.00 47.83           C  
ANISOU 3794  CZ  PHE B 243     4980   8108   5086  -2204   2340  -1989       C  
ATOM   3795  N   MET B 244     -12.234  -4.260  26.777  1.00 40.84           N  
ANISOU 3795  N   MET B 244     5000   6851   3668  -1669   2001  -1444       N  
ATOM   3796  CA  MET B 244     -13.208  -5.228  26.283  1.00 39.74           C  
ANISOU 3796  CA  MET B 244     4924   6710   3464  -1524   1870  -1421       C  
ATOM   3797  C   MET B 244     -14.170  -4.678  25.231  1.00 39.84           C  
ANISOU 3797  C   MET B 244     5219   6619   3298  -1557   1804  -1244       C  
ATOM   3798  O   MET B 244     -14.668  -5.429  24.392  1.00 40.01           O  
ANISOU 3798  O   MET B 244     5321   6675   3205  -1500   1728  -1249       O  
ATOM   3799  CB  MET B 244     -13.986  -5.844  27.448  1.00 36.90           C  
ANISOU 3799  CB  MET B 244     4437   6286   3297  -1328   1686  -1412       C  
ATOM   3800  CG  MET B 244     -13.112  -6.649  28.392  1.00 37.04           C  
ANISOU 3800  CG  MET B 244     4190   6418   3464  -1253   1718  -1582       C  
ATOM   3801  SD  MET B 244     -12.272  -7.997  27.539  1.00 38.18           S  
ANISOU 3801  SD  MET B 244     4247   6663   3596  -1188   1733  -1714       S  
ATOM   3802  CE  MET B 244     -10.774  -8.127  28.510  1.00 38.61           C  
ANISOU 3802  CE  MET B 244     4048   6783   3839  -1170   1754  -1814       C  
ATOM   3803  N   SER B 245     -14.431  -3.376  25.269  1.00 63.91           N  
ANISOU 3803  N   SER B 245     8429   9537   6319  -1645   1825  -1091       N  
ATOM   3804  CA  SER B 245     -15.375  -2.777  24.329  1.00 67.58           C  
ANISOU 3804  CA  SER B 245     9168   9894   6618  -1652   1744   -899       C  
ATOM   3805  C   SER B 245     -14.697  -2.064  23.162  1.00 68.99           C  
ANISOU 3805  C   SER B 245     9552  10102   6560  -1851   1928   -856       C  
ATOM   3806  O   SER B 245     -15.360  -1.672  22.202  1.00 71.38           O  
ANISOU 3806  O   SER B 245    10099  10352   6673  -1857   1866   -708       O  
ATOM   3807  CB  SER B 245     -16.326  -1.816  25.047  1.00 70.49           C  
ANISOU 3807  CB  SER B 245     9622  10067   7097  -1581   1630   -726       C  
ATOM   3808  OG  SER B 245     -17.117  -1.099  24.118  1.00 72.65           O  
ANISOU 3808  OG  SER B 245    10165  10233   7206  -1592   1569   -527       O  
ATOM   3809  N   PHE B 246     -13.380  -1.899  23.235  1.00 46.34           N  
ANISOU 3809  N   PHE B 246     6583   7325   3698  -2015   2155   -979       N  
ATOM   3810  CA  PHE B 246     -12.664  -1.174  22.190  1.00 49.59           C  
ANISOU 3810  CA  PHE B 246     7173   7746   3922  -2212   2345   -929       C  
ATOM   3811  C   PHE B 246     -11.436  -1.909  21.655  1.00 50.84           C  
ANISOU 3811  C   PHE B 246     7160   8047   4113  -2233   2440  -1092       C  
ATOM   3812  O   PHE B 246     -11.481  -2.480  20.568  1.00 52.05           O  
ANISOU 3812  O   PHE B 246     7410   8268   4098  -2207   2442  -1102       O  
ATOM   3813  CB  PHE B 246     -12.270   0.223  22.675  1.00 50.50           C  
ANISOU 3813  CB  PHE B 246     7357   7720   4110  -2373   2461   -846       C  
ATOM   3814  CG  PHE B 246     -11.790   1.131  21.580  1.00 53.51           C  
ANISOU 3814  CG  PHE B 246     7971   8034   4328  -2546   2603   -731       C  
ATOM   3815  CD1 PHE B 246     -12.694   1.792  20.765  1.00 54.76           C  
ANISOU 3815  CD1 PHE B 246     8477   8067   4263  -2559   2569   -509       C  
ATOM   3816  CD2 PHE B 246     -10.436   1.326  21.367  1.00 55.34           C  
ANISOU 3816  CD2 PHE B 246     8076   8326   4624  -2688   2762   -837       C  
ATOM   3817  CE1 PHE B 246     -12.255   2.629  19.756  1.00 57.76           C  
ANISOU 3817  CE1 PHE B 246     9083   8374   4490  -2705   2696   -391       C  
ATOM   3818  CE2 PHE B 246      -9.992   2.161  20.361  1.00 58.35           C  
ANISOU 3818  CE2 PHE B 246     8671   8644   4855  -2852   2907   -732       C  
ATOM   3819  CZ  PHE B 246     -10.902   2.813  19.554  1.00 59.55           C  
ANISOU 3819  CZ  PHE B 246     9179   8661   4787  -2858   2876   -506       C  
ATOM   3820  N   LEU B 247     -10.347  -1.881  22.419  1.00 50.14           N  
ANISOU 3820  N   LEU B 247     6821   8002   4229  -2278   2514  -1219       N  
ATOM   3821  CA  LEU B 247      -9.059  -2.411  21.967  1.00 51.73           C  
ANISOU 3821  CA  LEU B 247     6851   8333   4471  -2308   2622  -1362       C  
ATOM   3822  C   LEU B 247      -9.123  -3.847  21.456  1.00 51.23           C  
ANISOU 3822  C   LEU B 247     6705   8380   4382  -2136   2551  -1470       C  
ATOM   3823  O   LEU B 247      -8.856  -4.100  20.288  1.00 53.15           O  
ANISOU 3823  O   LEU B 247     7056   8677   4462  -2159   2629  -1479       O  
ATOM   3824  CB  LEU B 247      -8.002  -2.295  23.069  1.00 51.55           C  
ANISOU 3824  CB  LEU B 247     6547   8356   4684  -2352   2658  -1489       C  
ATOM   3825  CG  LEU B 247      -7.239  -0.971  23.172  1.00 53.49           C  
ANISOU 3825  CG  LEU B 247     6830   8539   4954  -2583   2801  -1455       C  
ATOM   3826  CD1 LEU B 247      -8.114   0.138  23.738  1.00 52.59           C  
ANISOU 3826  CD1 LEU B 247     6899   8247   4836  -2649   2764  -1317       C  
ATOM   3827  CD2 LEU B 247      -5.978  -1.143  24.005  1.00 53.94           C  
ANISOU 3827  CD2 LEU B 247     6574   8708   5214  -2615   2829  -1627       C  
ATOM   3828  N   PHE B 248      -9.476  -4.776  22.337  1.00 79.82           N  
ANISOU 3828  N   PHE B 248    10146  12022   8159  -1966   2410  -1553       N  
ATOM   3829  CA  PHE B 248      -9.562  -6.195  21.990  1.00 79.90           C  
ANISOU 3829  CA  PHE B 248    10076  12108   8175  -1801   2341  -1665       C  
ATOM   3830  C   PHE B 248     -10.486  -6.494  20.789  1.00 80.62           C  
ANISOU 3830  C   PHE B 248    10418  12189   8025  -1775   2294  -1610       C  
ATOM   3831  O   PHE B 248     -10.026  -7.047  19.781  1.00 82.40           O  
ANISOU 3831  O   PHE B 248    10665  12481   8161  -1743   2345  -1693       O  
ATOM   3832  CB  PHE B 248      -9.947  -7.011  23.237  1.00 76.39           C  
ANISOU 3832  CB  PHE B 248     9426  11658   7939  -1626   2191  -1736       C  
ATOM   3833  CG  PHE B 248     -10.014  -8.496  23.014  1.00 76.18           C  
ANISOU 3833  CG  PHE B 248     9328  11678   7939  -1457   2123  -1849       C  
ATOM   3834  CD1 PHE B 248      -8.857  -9.252  22.918  1.00 77.12           C  
ANISOU 3834  CD1 PHE B 248     9281  11878   8141  -1403   2198  -1976       C  
ATOM   3835  CD2 PHE B 248     -11.238  -9.143  22.946  1.00 75.85           C  
ANISOU 3835  CD2 PHE B 248     9387  11592   7841  -1355   1987  -1833       C  
ATOM   3836  CE1 PHE B 248      -8.920 -10.620  22.728  1.00 77.70           C  
ANISOU 3836  CE1 PHE B 248     9313  11968   8242  -1244   2147  -2078       C  
ATOM   3837  CE2 PHE B 248     -11.307 -10.509  22.756  1.00 75.54           C  
ANISOU 3837  CE2 PHE B 248     9299  11570   7831  -1215   1930  -1947       C  
ATOM   3838  CZ  PHE B 248     -10.147 -11.249  22.647  1.00 76.42           C  
ANISOU 3838  CZ  PHE B 248     9266  11742   8026  -1155   2015  -2065       C  
ATOM   3839  N   PRO B 249     -11.779  -6.115  20.871  1.00 52.56           N  
ANISOU 3839  N   PRO B 249     7060   8556   4354  -1787   2190  -1474       N  
ATOM   3840  CA  PRO B 249     -12.685  -6.491  19.779  1.00 53.96           C  
ANISOU 3840  CA  PRO B 249     7474   8745   4284  -1765   2111  -1434       C  
ATOM   3841  C   PRO B 249     -12.354  -5.816  18.450  1.00 56.20           C  
ANISOU 3841  C   PRO B 249     7989   9041   4325  -1898   2237  -1354       C  
ATOM   3842  O   PRO B 249     -12.554  -6.430  17.407  1.00 57.50           O  
ANISOU 3842  O   PRO B 249     8269   9259   4317  -1868   2222  -1402       O  
ATOM   3843  CB  PRO B 249     -14.054  -6.018  20.281  1.00 52.49           C  
ANISOU 3843  CB  PRO B 249     7424   8483   4038  -1745   1954  -1297       C  
ATOM   3844  CG  PRO B 249     -13.744  -4.891  21.184  1.00 52.40           C  
ANISOU 3844  CG  PRO B 249     7354   8392   4164  -1818   2028  -1213       C  
ATOM   3845  CD  PRO B 249     -12.470  -5.289  21.879  1.00 50.69           C  
ANISOU 3845  CD  PRO B 249     6841   8226   4191  -1799   2120  -1365       C  
ATOM   3846  N   MET B 250     -11.862  -4.581  18.482  1.00 53.16           N  
ANISOU 3846  N   MET B 250     7677   8597   3924  -2045   2362  -1237       N  
ATOM   3847  CA  MET B 250     -11.537  -3.874  17.246  1.00 56.19           C  
ANISOU 3847  CA  MET B 250     8300   8976   4075  -2177   2489  -1137       C  
ATOM   3848  C   MET B 250     -10.192  -4.305  16.674  1.00 58.28           C  
ANISOU 3848  C   MET B 250     8439   9346   4358  -2218   2675  -1275       C  
ATOM   3849  O   MET B 250      -9.949  -4.169  15.477  1.00 60.95           O  
ANISOU 3849  O   MET B 250     8965   9717   4477  -2282   2771  -1236       O  
ATOM   3850  CB  MET B 250     -11.580  -2.358  17.444  1.00 56.96           C  
ANISOU 3850  CB  MET B 250     8548   8944   4148  -2325   2562   -953       C  
ATOM   3851  CG  MET B 250     -12.973  -1.815  17.707  1.00 55.78           C  
ANISOU 3851  CG  MET B 250     8608   8679   3908  -2282   2392   -771       C  
ATOM   3852  SD  MET B 250     -14.185  -2.365  16.486  1.00 56.78           S  
ANISOU 3852  SD  MET B 250     9015   8848   3713  -2189   2199   -686       S  
ATOM   3853  CE  MET B 250     -15.104  -3.585  17.427  1.00 53.49           C  
ANISOU 3853  CE  MET B 250     8402   8484   3437  -2014   1975   -812       C  
ATOM   3854  N   LEU B 251      -9.318  -4.818  17.533  1.00 57.28           N  
ANISOU 3854  N   LEU B 251     8001   9277   4485  -2174   2721  -1430       N  
ATOM   3855  CA  LEU B 251      -8.073  -5.408  17.071  1.00 59.26           C  
ANISOU 3855  CA  LEU B 251     8103   9640   4771  -2181   2881  -1572       C  
ATOM   3856  C   LEU B 251      -8.423  -6.687  16.323  1.00 59.75           C  
ANISOU 3856  C   LEU B 251     8231   9765   4705  -2043   2828  -1667       C  
ATOM   3857  O   LEU B 251      -7.953  -6.913  15.201  1.00 62.44           O  
ANISOU 3857  O   LEU B 251     8678  10171   4877  -2078   2958  -1699       O  
ATOM   3858  CB  LEU B 251      -7.138  -5.701  18.246  1.00 58.07           C  
ANISOU 3858  CB  LEU B 251     7605   9539   4920  -2137   2896  -1706       C  
ATOM   3859  CG  LEU B 251      -5.710  -6.145  17.922  1.00 60.38           C  
ANISOU 3859  CG  LEU B 251     7708   9954   5281  -2156   3071  -1843       C  
ATOM   3860  CD1 LEU B 251      -5.101  -5.245  16.861  1.00 63.66           C  
ANISOU 3860  CD1 LEU B 251     8281  10384   5522  -2350   3278  -1769       C  
ATOM   3861  CD2 LEU B 251      -4.852  -6.141  19.180  1.00 59.43           C  
ANISOU 3861  CD2 LEU B 251     7270   9872   5437  -2143   3058  -1935       C  
ATOM   3862  N   VAL B 252      -9.268  -7.510  16.942  1.00 57.31           N  
ANISOU 3862  N   VAL B 252     7870   9431   4474  -1892   2638  -1716       N  
ATOM   3863  CA  VAL B 252      -9.754  -8.724  16.288  1.00 57.64           C  
ANISOU 3863  CA  VAL B 252     7994   9503   4403  -1767   2555  -1813       C  
ATOM   3864  C   VAL B 252     -10.441  -8.398  14.959  1.00 59.60           C  
ANISOU 3864  C   VAL B 252     8583   9745   4319  -1834   2527  -1709       C  
ATOM   3865  O   VAL B 252     -10.151  -9.013  13.931  1.00 61.82           O  
ANISOU 3865  O   VAL B 252     8972  10084   4435  -1811   2587  -1788       O  
ATOM   3866  CB  VAL B 252     -10.722  -9.516  17.194  1.00 54.72           C  
ANISOU 3866  CB  VAL B 252     7530   9085   4175  -1622   2343  -1861       C  
ATOM   3867  CG1 VAL B 252     -11.381 -10.645  16.419  1.00 55.34           C  
ANISOU 3867  CG1 VAL B 252     7746   9171   4110  -1526   2236  -1952       C  
ATOM   3868  CG2 VAL B 252      -9.989 -10.058  18.415  1.00 53.18           C  
ANISOU 3868  CG2 VAL B 252     7014   8904   4288  -1523   2359  -1971       C  
ATOM   3869  N   ALA B 253     -11.333  -7.412  14.988  1.00 59.01           N  
ANISOU 3869  N   ALA B 253     8686   9596   4138  -1907   2429  -1529       N  
ATOM   3870  CA  ALA B 253     -12.095  -7.014  13.808  1.00 60.96           C  
ANISOU 3870  CA  ALA B 253     9270   9832   4060  -1958   2360  -1397       C  
ATOM   3871  C   ALA B 253     -11.206  -6.478  12.690  1.00 64.42           C  
ANISOU 3871  C   ALA B 253     9848  10314   4313  -2073   2575  -1359       C  
ATOM   3872  O   ALA B 253     -11.468  -6.721  11.514  1.00 66.75           O  
ANISOU 3872  O   ALA B 253    10370  10651   4340  -2069   2557  -1348       O  
ATOM   3873  CB  ALA B 253     -13.155  -5.986  14.182  1.00 59.83           C  
ANISOU 3873  CB  ALA B 253     9278   9591   3864  -2003   2221  -1188       C  
ATOM   3874  N   SER B 254     -10.160  -5.746  13.060  1.00 64.96           N  
ANISOU 3874  N   SER B 254     9781  10379   4523  -2179   2773  -1344       N  
ATOM   3875  CA  SER B 254      -9.219  -5.212  12.081  1.00 68.41           C  
ANISOU 3875  CA  SER B 254    10320  10862   4813  -2305   3003  -1313       C  
ATOM   3876  C   SER B 254      -8.424  -6.344  11.442  1.00 70.15           C  
ANISOU 3876  C   SER B 254    10445  11204   5005  -2232   3122  -1507       C  
ATOM   3877  O   SER B 254      -8.237  -6.372  10.221  1.00 73.24           O  
ANISOU 3877  O   SER B 254    11036  11649   5141  -2269   3223  -1494       O  
ATOM   3878  CB  SER B 254      -8.271  -4.204  12.732  1.00 68.64           C  
ANISOU 3878  CB  SER B 254    10199  10854   5028  -2451   3174  -1270       C  
ATOM   3879  OG  SER B 254      -7.494  -4.815  13.747  1.00 66.95           O  
ANISOU 3879  OG  SER B 254     9630  10693   5115  -2391   3203  -1441       O  
ATOM   3880  N   ILE B 255      -7.957  -7.271  12.276  1.00 68.45           N  
ANISOU 3880  N   ILE B 255     9933  11028   5047  -2120   3111  -1682       N  
ATOM   3881  CA  ILE B 255      -7.269  -8.464  11.790  1.00 69.93           C  
ANISOU 3881  CA  ILE B 255    10023  11311   5235  -2014   3205  -1872       C  
ATOM   3882  C   ILE B 255      -8.129  -9.193  10.765  1.00 71.05           C  
ANISOU 3882  C   ILE B 255    10426  11462   5109  -1935   3092  -1902       C  
ATOM   3883  O   ILE B 255      -7.703  -9.432   9.628  1.00 74.21           O  
ANISOU 3883  O   ILE B 255    10970  11933   5295  -1950   3226  -1946       O  
ATOM   3884  CB  ILE B 255      -6.955  -9.443  12.935  1.00 67.47           C  
ANISOU 3884  CB  ILE B 255     9393  11006   5236  -1866   3138  -2028       C  
ATOM   3885  CG1 ILE B 255      -5.863  -8.878  13.842  1.00 67.16           C  
ANISOU 3885  CG1 ILE B 255     9072  10996   5450  -1935   3262  -2040       C  
ATOM   3886  CG2 ILE B 255      -6.528 -10.794  12.379  1.00 68.93           C  
ANISOU 3886  CG2 ILE B 255     9540  11256   5396  -1723   3190  -2214       C  
ATOM   3887  CD1 ILE B 255      -5.614  -9.721  15.072  1.00 64.71           C  
ANISOU 3887  CD1 ILE B 255     8463  10686   5439  -1787   3162  -2158       C  
ATOM   3888  N   LEU B 256      -9.347  -9.532  11.176  1.00 68.58           N  
ANISOU 3888  N   LEU B 256    10173  11081   4802  -1855   2841  -1883       N  
ATOM   3889  CA  LEU B 256     -10.275 -10.249  10.313  1.00 69.51           C  
ANISOU 3889  CA  LEU B 256    10527  11202   4683  -1786   2682  -1922       C  
ATOM   3890  C   LEU B 256     -10.568  -9.478   9.031  1.00 72.53           C  
ANISOU 3890  C   LEU B 256    11240  11609   4709  -1891   2706  -1778       C  
ATOM   3891  O   LEU B 256     -10.694 -10.073   7.968  1.00 74.95           O  
ANISOU 3891  O   LEU B 256    11732  11967   4780  -1855   2694  -1851       O  
ATOM   3892  CB  LEU B 256     -11.576 -10.563  11.056  1.00 66.51           C  
ANISOU 3892  CB  LEU B 256    10142  10745   4384  -1715   2398  -1900       C  
ATOM   3893  CG  LEU B 256     -11.453 -11.539  12.227  1.00 63.77           C  
ANISOU 3893  CG  LEU B 256     9506  10366   4358  -1589   2343  -2048       C  
ATOM   3894  CD1 LEU B 256     -12.817 -11.828  12.832  1.00 61.30           C  
ANISOU 3894  CD1 LEU B 256     9219   9984   4089  -1538   2068  -2019       C  
ATOM   3895  CD2 LEU B 256     -10.775 -12.826  11.785  1.00 65.28           C  
ANISOU 3895  CD2 LEU B 256     9636  10596   4574  -1479   2434  -2258       C  
ATOM   3896  N   ASN B 257     -10.664  -8.156   9.134  1.00 75.73           N  
ANISOU 3896  N   ASN B 257    11730  11970   5073  -2015   2739  -1574       N  
ATOM   3897  CA  ASN B 257     -10.923  -7.319   7.966  1.00 78.79           C  
ANISOU 3897  CA  ASN B 257    12444  12366   5127  -2110   2763  -1405       C  
ATOM   3898  C   ASN B 257      -9.779  -7.329   6.955  1.00 82.52           C  
ANISOU 3898  C   ASN B 257    12970  12929   5452  -2173   3041  -1461       C  
ATOM   3899  O   ASN B 257     -10.012  -7.378   5.746  1.00 85.56           O  
ANISOU 3899  O   ASN B 257    13626  13364   5518  -2183   3040  -1426       O  
ATOM   3900  CB  ASN B 257     -11.267  -5.887   8.379  1.00 78.12           C  
ANISOU 3900  CB  ASN B 257    12448  12180   5052  -2220   2738  -1162       C  
ATOM   3901  CG  ASN B 257     -12.743  -5.708   8.679  1.00 76.30           C  
ANISOU 3901  CG  ASN B 257    12355  11877   4757  -2161   2429  -1035       C  
ATOM   3902  OD1 ASN B 257     -13.524  -5.331   7.804  1.00 78.25           O  
ANISOU 3902  OD1 ASN B 257    12895  12119   4717  -2165   2293   -891       O  
ATOM   3903  ND2 ASN B 257     -13.134  -5.985   9.917  1.00 72.76           N  
ANISOU 3903  ND2 ASN B 257    11692  11381   4573  -2098   2308  -1083       N  
ATOM   3904  N   THR B 258      -8.547  -7.281   7.452  1.00 79.36           N  
ANISOU 3904  N   THR B 258    12310  12563   5280  -2213   3271  -1550       N  
ATOM   3905  CA  THR B 258      -7.383  -7.394   6.580  1.00 82.95           C  
ANISOU 3905  CA  THR B 258    12767  13120   5629  -2262   3550  -1628       C  
ATOM   3906  C   THR B 258      -7.370  -8.761   5.905  1.00 84.28           C  
ANISOU 3906  C   THR B 258    12971  13369   5682  -2119   3536  -1828       C  
ATOM   3907  O   THR B 258      -7.204  -8.869   4.682  1.00 87.82           O  
ANISOU 3907  O   THR B 258    13640  13890   5838  -2135   3638  -1839       O  
ATOM   3908  CB  THR B 258      -6.069  -7.205   7.360  1.00 82.60           C  
ANISOU 3908  CB  THR B 258    12388  13107   5888  -2319   3767  -1704       C  
ATOM   3909  OG1 THR B 258      -6.005  -5.871   7.879  1.00 82.02           O  
ANISOU 3909  OG1 THR B 258    12313  12953   5898  -2476   3803  -1527       O  
ATOM   3910  CG2 THR B 258      -4.870  -7.446   6.454  1.00 86.49           C  
ANISOU 3910  CG2 THR B 258    12858  13724   6282  -2352   4057  -1803       C  
ATOM   3911  N   VAL B 259      -7.564  -9.802   6.711  1.00 81.59           N  
ANISOU 3911  N   VAL B 259    12426  13006   5567  -1978   3410  -1985       N  
ATOM   3912  CA  VAL B 259      -7.552 -11.173   6.213  1.00 82.65           C  
ANISOU 3912  CA  VAL B 259    12581  13184   5637  -1831   3388  -2191       C  
ATOM   3913  C   VAL B 259      -8.615 -11.420   5.139  1.00 84.34           C  
ANISOU 3913  C   VAL B 259    13142  13400   5504  -1812   3210  -2170       C  
ATOM   3914  O   VAL B 259      -8.344 -12.079   4.138  1.00 87.37           O  
ANISOU 3914  O   VAL B 259    13663  13853   5681  -1763   3294  -2292       O  
ATOM   3915  CB  VAL B 259      -7.715 -12.194   7.358  1.00 79.31           C  
ANISOU 3915  CB  VAL B 259    11901  12703   5530  -1686   3253  -2335       C  
ATOM   3916  CG1 VAL B 259      -7.847 -13.599   6.803  1.00 80.56           C  
ANISOU 3916  CG1 VAL B 259    12131  12871   5607  -1538   3207  -2539       C  
ATOM   3917  CG2 VAL B 259      -6.533 -12.111   8.310  1.00 78.37           C  
ANISOU 3917  CG2 VAL B 259    11436  12611   5732  -1681   3429  -2384       C  
ATOM   3918  N   ILE B 260      -9.815 -10.882   5.340  1.00110.06           N  
ANISOU 3918  N   ILE B 260    16540  16588   8690  -1846   2958  -2017       N  
ATOM   3919  CA  ILE B 260     -10.890 -11.057   4.365  1.00111.61           C  
ANISOU 3919  CA  ILE B 260    17053  16796   8558  -1830   2746  -1983       C  
ATOM   3920  C   ILE B 260     -10.703 -10.159   3.149  1.00115.33           C  
ANISOU 3920  C   ILE B 260    17805  17331   8683  -1936   2864  -1830       C  
ATOM   3921  O   ILE B 260     -11.169 -10.483   2.057  1.00118.18           O  
ANISOU 3921  O   ILE B 260    18428  17747   8729  -1914   2771  -1853       O  
ATOM   3922  CB  ILE B 260     -12.293 -10.833   4.980  1.00109.09           C  
ANISOU 3922  CB  ILE B 260    16778  16393   8279  -1816   2409  -1869       C  
ATOM   3923  CG1 ILE B 260     -12.455  -9.399   5.488  1.00107.84           C  
ANISOU 3923  CG1 ILE B 260    16631  16178   8164  -1923   2414  -1614       C  
ATOM   3924  CG2 ILE B 260     -12.543 -11.819   6.099  1.00105.73           C  
ANISOU 3924  CG2 ILE B 260    16100  15905   8167  -1711   2287  -2025       C  
ATOM   3925  CD1 ILE B 260     -13.255  -8.501   4.577  1.00109.77           C  
ANISOU 3925  CD1 ILE B 260    17209  16425   8072  -1983   2278  -1397       C  
ATOM   3926  N   ALA B 261     -10.032  -9.027   3.342  1.00 95.70           N  
ANISOU 3926  N   ALA B 261    15271  14835   6256  -2057   3063  -1676       N  
ATOM   3927  CA  ALA B 261      -9.693  -8.158   2.223  1.00 99.66           C  
ANISOU 3927  CA  ALA B 261    16025  15387   6452  -2168   3225  -1530       C  
ATOM   3928  C   ALA B 261      -8.768  -8.921   1.286  1.00103.18           C  
ANISOU 3928  C   ALA B 261    16501  15954   6747  -2135   3455  -1712       C  
ATOM   3929  O   ALA B 261      -8.976  -8.949   0.071  1.00106.75           O  
ANISOU 3929  O   ALA B 261    17239  16477   6844  -2142   3457  -1690       O  
ATOM   3930  CB  ALA B 261      -9.025  -6.886   2.715  1.00 99.41           C  
ANISOU 3930  CB  ALA B 261    15904  15304   6563  -2314   3418  -1360       C  
ATOM   3931  N   ARG B 262      -7.757  -9.558   1.869  1.00124.53           N  
ANISOU 3931  N   ARG B 262    18908  18686   9721  -2088   3641  -1894       N  
ATOM   3932  CA  ARG B 262      -6.812 -10.363   1.105  1.00128.13           C  
ANISOU 3932  CA  ARG B 262    19352  19254  10079  -2033   3876  -2084       C  
ATOM   3933  C   ARG B 262      -7.477 -11.600   0.500  1.00129.58           C  
ANISOU 3933  C   ARG B 262    19701  19459  10075  -1893   3698  -2256       C  
ATOM   3934  O   ARG B 262      -7.181 -11.986  -0.630  1.00134.78           O  
ANISOU 3934  O   ARG B 262    20582  20208  10421  -1882   3792  -2318       O  
ATOM   3935  CB  ARG B 262      -5.648 -10.784   2.001  1.00124.61           C  
ANISOU 3935  CB  ARG B 262    18522  18822  10001  -1986   4066  -2231       C  
ATOM   3936  CG  ARG B 262      -4.523 -11.507   1.284  1.00128.10           C  
ANISOU 3936  CG  ARG B 262    18910  19383  10378  -1932   4355  -2408       C  
ATOM   3937  CD  ARG B 262      -3.364 -11.797   2.230  1.00126.76           C  
ANISOU 3937  CD  ARG B 262    18343  19234  10586  -1892   4528  -2516       C  
ATOM   3938  NE  ARG B 262      -2.773 -10.575   2.774  1.00126.72           N  
ANISOU 3938  NE  ARG B 262    18186  19225  10735  -2062   4656  -2357       N  
ATOM   3939  CZ  ARG B 262      -3.043 -10.081   3.979  1.00123.24           C  
ANISOU 3939  CZ  ARG B 262    17567  18692  10566  -2103   4513  -2270       C  
ATOM   3940  NH1 ARG B 262      -3.900 -10.703   4.778  1.00119.78           N  
ANISOU 3940  NH1 ARG B 262    17070  18165  10277  -1984   4243  -2315       N  
ATOM   3941  NH2 ARG B 262      -2.457  -8.963   4.386  1.00123.55           N  
ANISOU 3941  NH2 ARG B 262    17491  18726  10726  -2269   4643  -2143       N  
ATOM   3942  N   ARG B 263      -8.378 -12.213   1.262  1.00131.70           N  
ANISOU 3942  N   ARG B 263    19865  19640  10534  -1795   3438  -2335       N  
ATOM   3943  CA  ARG B 263      -9.041 -13.445   0.848  1.00132.26           C  
ANISOU 3943  CA  ARG B 263    20062  19702  10491  -1672   3239  -2515       C  
ATOM   3944  C   ARG B 263      -9.997 -13.206  -0.316  1.00135.87           C  
ANISOU 3944  C   ARG B 263    20887  20200  10537  -1709   3048  -2434       C  
ATOM   3945  O   ARG B 263     -10.161 -14.065  -1.183  1.00139.49           O  
ANISOU 3945  O   ARG B 263    21515  20706  10779  -1640   3004  -2597       O  
ATOM   3946  CB  ARG B 263      -9.801 -14.064   2.024  1.00126.98           C  
ANISOU 3946  CB  ARG B 263    19208  18917  10123  -1592   2986  -2571       C  
ATOM   3947  CG  ARG B 263     -10.401 -15.430   1.732  1.00127.34           C  
ANISOU 3947  CG  ARG B 263    19343  18928  10114  -1472   2794  -2783       C  
ATOM   3948  CD  ARG B 263      -9.324 -16.498   1.639  1.00128.93           C  
ANISOU 3948  CD  ARG B 263    19425  19149  10415  -1354   3019  -3021       C  
ATOM   3949  NE  ARG B 263      -8.674 -16.727   2.927  1.00126.47           N  
ANISOU 3949  NE  ARG B 263    18765  18778  10511  -1291   3112  -3062       N  
ATOM   3950  CZ  ARG B 263      -7.652 -17.556   3.111  1.00128.12           C  
ANISOU 3950  CZ  ARG B 263    18803  18998  10879  -1175   3318  -3235       C  
ATOM   3951  NH1 ARG B 263      -7.155 -18.236   2.087  1.00132.47           N  
ANISOU 3951  NH1 ARG B 263    19503  19615  11217  -1111   3469  -3391       N  
ATOM   3952  NH2 ARG B 263      -7.123 -17.703   4.318  1.00125.57           N  
ANISOU 3952  NH2 ARG B 263    18164  18628  10921  -1115   3368  -3250       N  
ATOM   3953  N   LEU B 264     -10.630 -12.039  -0.328  1.00 98.59           N  
ANISOU 3953  N   LEU B 264    16293  15456   5709  -1811   2924  -2182       N  
ATOM   3954  CA  LEU B 264     -11.571 -11.696  -1.387  1.00101.32           C  
ANISOU 3954  CA  LEU B 264    16984  15849   5665  -1839   2720  -2072       C  
ATOM   3955  C   LEU B 264     -10.852 -11.125  -2.604  1.00106.04           C  
ANISOU 3955  C   LEU B 264    17801  16556   5932  -1914   2975  -2000       C  
ATOM   3956  O   LEU B 264     -11.246 -11.382  -3.742  1.00109.63           O  
ANISOU 3956  O   LEU B 264    18529  17095   6030  -1895   2898  -2038       O  
ATOM   3957  CB  LEU B 264     -12.624 -10.709  -0.878  1.00 99.08           C  
ANISOU 3957  CB  LEU B 264    16756  15489   5401  -1891   2457  -1820       C  
ATOM   3958  CG  LEU B 264     -13.677 -10.262  -1.896  1.00101.87           C  
ANISOU 3958  CG  LEU B 264    17448  15891   5369  -1907   2201  -1670       C  
ATOM   3959  CD1 LEU B 264     -15.081 -10.444  -1.342  1.00 99.28           C  
ANISOU 3959  CD1 LEU B 264    17105  15498   5118  -1856   1790  -1622       C  
ATOM   3960  CD2 LEU B 264     -13.444  -8.816  -2.305  1.00103.88           C  
ANISOU 3960  CD2 LEU B 264    17872  16150   5447  -2016   2336  -1386       C  
ATOM   3961  N   THR B 265      -9.795 -10.354  -2.362  1.00154.22           N  
ANISOU 3961  N   THR B 265    23780  22661  12154  -2006   3278  -1901       N  
ATOM   3962  CA  THR B 265      -9.032  -9.750  -3.451  1.00158.50           C  
ANISOU 3962  CA  THR B 265    24511  23302  12409  -2096   3554  -1821       C  
ATOM   3963  C   THR B 265      -8.327 -10.809  -4.298  1.00161.64           C  
ANISOU 3963  C   THR B 265    24948  23816  12649  -2017   3743  -2072       C  
ATOM   3964  O   THR B 265      -8.207 -10.664  -5.515  1.00166.52           O  
ANISOU 3964  O   THR B 265    25844  24536  12889  -2045   3825  -2050       O  
ATOM   3965  CB  THR B 265      -7.991  -8.741  -2.927  1.00155.65           C  
ANISOU 3965  CB  THR B 265    23977  22913  12248  -2228   3848  -1680       C  
ATOM   3966  OG1 THR B 265      -8.623  -7.817  -2.033  1.00152.79           O  
ANISOU 3966  OG1 THR B 265    23576  22426  12049  -2289   3671  -1467       O  
ATOM   3967  CG2 THR B 265      -7.360  -7.972  -4.080  1.00160.25           C  
ANISOU 3967  CG2 THR B 265    24792  23585  12510  -2342   4111  -1559       C  
ATOM   3968  N   VAL B 266      -7.871 -11.878  -3.651  1.00137.08           N  
ANISOU 3968  N   VAL B 266    21575  20687   9821  -1910   3804  -2307       N  
ATOM   3969  CA  VAL B 266      -7.155 -12.942  -4.347  1.00139.75           C  
ANISOU 3969  CA  VAL B 266    21934  21118  10046  -1812   3991  -2558       C  
ATOM   3970  C   VAL B 266      -8.094 -13.741  -5.253  1.00142.52           C  
ANISOU 3970  C   VAL B 266    22582  21504  10065  -1736   3751  -2678       C  
ATOM   3971  O   VAL B 266      -7.654 -14.403  -6.193  1.00146.56           O  
ANISOU 3971  O   VAL B 266    23244  22116  10326  -1688   3903  -2833       O  
ATOM   3972  CB  VAL B 266      -6.433 -13.889  -3.355  1.00134.65           C  
ANISOU 3972  CB  VAL B 266    20934  20425   9800  -1693   4091  -2771       C  
ATOM   3973  CG1 VAL B 266      -7.426 -14.812  -2.668  1.00130.64           C  
ANISOU 3973  CG1 VAL B 266    20373  19803   9460  -1582   3757  -2886       C  
ATOM   3974  CG2 VAL B 266      -5.356 -14.696  -4.068  1.00138.61           C  
ANISOU 3974  CG2 VAL B 266    21428  21032  10206  -1606   4387  -2990       C  
ATOM   3975  N   MET B 267      -9.391 -13.661  -4.974  1.00115.39           N  
ANISOU 3975  N   MET B 267    19228  17991   6624  -1728   3374  -2608       N  
ATOM   3976  CA  MET B 267     -10.390 -14.368  -5.768  1.00117.50           C  
ANISOU 3976  CA  MET B 267    19759  18292   6595  -1672   3096  -2716       C  
ATOM   3977  C   MET B 267     -10.810 -13.556  -6.989  1.00121.60           C  
ANISOU 3977  C   MET B 267    20629  18917   6657  -1756   3045  -2536       C  
ATOM   3978  O   MET B 267     -10.994 -14.105  -8.076  1.00125.60           O  
ANISOU 3978  O   MET B 267    21379  19521   6824  -1721   3009  -2663       O  
ATOM   3979  CB  MET B 267     -11.610 -14.707  -4.911  1.00113.55           C  
ANISOU 3979  CB  MET B 267    19176  17675   6294  -1631   2702  -2724       C  
ATOM   3980  CG  MET B 267     -11.371 -15.829  -3.915  1.00110.49           C  
ANISOU 3980  CG  MET B 267    18516  17186   6281  -1523   2703  -2953       C  
ATOM   3981  SD  MET B 267     -12.608 -15.869  -2.604  1.00104.93           S  
ANISOU 3981  SD  MET B 267    17617  16329   5922  -1513   2340  -2883       S  
ATOM   3982  CE  MET B 267     -14.122 -15.851  -3.559  1.00106.81           C  
ANISOU 3982  CE  MET B 267    18166  16611   5807  -1557   1921  -2781       C  
ATOM   3983  N   VAL B 268     -10.958 -12.249  -6.805  1.00129.76           N  
ANISOU 3983  N   VAL B 268    21697  19927   7678  -1862   3038  -2242       N  
ATOM   3984  CA  VAL B 268     -11.335 -11.360  -7.898  1.00133.69           C  
ANISOU 3984  CA  VAL B 268    22530  20509   7756  -1938   2994  -2030       C  
ATOM   3985  C   VAL B 268     -10.105 -10.859  -8.648  1.00137.64           C  
ANISOU 3985  C   VAL B 268    23117  21106   8076  -2015   3414  -1984       C  
ATOM   3986  O   VAL B 268      -9.769 -11.365  -9.718  1.00141.98           O  
ANISOU 3986  O   VAL B 268    23849  21777   8319  -1988   3540  -2124       O  
ATOM   3987  CB  VAL B 268     -12.146 -10.152  -7.394  1.00131.44           C  
ANISOU 3987  CB  VAL B 268    22278  20138   7526  -2006   2784  -1712       C  
ATOM   3988  CG1 VAL B 268     -11.355  -9.381  -6.350  1.00128.21           C  
ANISOU 3988  CG1 VAL B 268    21601  19628   7484  -2080   3019  -1596       C  
ATOM   3989  CG2 VAL B 268     -12.526  -9.248  -8.557  1.00135.89           C  
ANISOU 3989  CG2 VAL B 268    23201  20781   7651  -2070   2745  -1477       C  
ATOM   3990  N   ARG B 299     -22.884 -12.420  -6.831  1.00182.78           N  
ANISOU 3990  N   ARG B 299    28921  26649  13877  -1643   -720  -1679       N  
ATOM   3991  CA  ARG B 299     -22.596 -12.609  -5.415  1.00177.32           C  
ANISOU 3991  CA  ARG B 299    27931  25800  13642  -1645   -597  -1720       C  
ATOM   3992  C   ARG B 299     -21.316 -11.882  -5.013  1.00175.85           C  
ANISOU 3992  C   ARG B 299    27717  25548  13552  -1677   -153  -1608       C  
ATOM   3993  O   ARG B 299     -21.190 -11.405  -3.884  1.00173.43           O  
ANISOU 3993  O   ARG B 299    27214  25127  13555  -1684    -76  -1491       O  
ATOM   3994  CB  ARG B 299     -22.482 -14.100  -5.085  1.00176.14           C  
ANISOU 3994  CB  ARG B 299    27627  25599  13701  -1636   -596  -2078       C  
ATOM   3995  CG  ARG B 299     -22.206 -14.392  -3.619  1.00170.98           C  
ANISOU 3995  CG  ARG B 299    26667  24788  13511  -1631   -479  -2131       C  
ATOM   3996  CD  ARG B 299     -22.054 -15.880  -3.357  1.00170.38           C  
ANISOU 3996  CD  ARG B 299    26465  24643  13627  -1613   -470  -2474       C  
ATOM   3997  NE  ARG B 299     -21.724 -16.151  -1.961  1.00165.63           N  
ANISOU 3997  NE  ARG B 299    25579  23895  13459  -1600   -340  -2513       N  
ATOM   3998  CZ  ARG B 299     -21.557 -17.369  -1.455  1.00164.37           C  
ANISOU 3998  CZ  ARG B 299    25274  23636  13544  -1575   -315  -2771       C  
ATOM   3999  NH1 ARG B 299     -21.691 -18.436  -2.230  1.00167.44           N  
ANISOU 3999  NH1 ARG B 299    25780  24043  13795  -1565   -408  -3022       N  
ATOM   4000  NH2 ARG B 299     -21.258 -17.520  -0.172  1.00160.18           N  
ANISOU 4000  NH2 ARG B 299    24489  22980  13391  -1558   -198  -2779       N  
ATOM   4001  N   VAL B 300     -20.373 -11.799  -5.947  1.00140.00           N  
ANISOU 4001  N   VAL B 300    23366  21084   8742  -1702    138  -1649       N  
ATOM   4002  CA  VAL B 300     -19.086 -11.160  -5.695  1.00138.65           C  
ANISOU 4002  CA  VAL B 300    23159  20867   8652  -1748    575  -1565       C  
ATOM   4003  C   VAL B 300     -19.253  -9.688  -5.324  1.00137.81           C  
ANISOU 4003  C   VAL B 300    23087  20703   8571  -1783    581  -1208       C  
ATOM   4004  O   VAL B 300     -18.601  -9.193  -4.402  1.00135.20           O  
ANISOU 4004  O   VAL B 300    22582  20269   8518  -1820    813  -1132       O  
ATOM   4005  CB  VAL B 300     -18.156 -11.273  -6.919  1.00144.71           C  
ANISOU 4005  CB  VAL B 300    24152  21751   9080  -1774    860  -1650       C  
ATOM   4006  CG1 VAL B 300     -16.784 -10.695  -6.603  1.00143.63           C  
ANISOU 4006  CG1 VAL B 300    23925  21571   9076  -1831   1319  -1592       C  
ATOM   4007  CG2 VAL B 300     -18.036 -12.724  -7.360  1.00146.51           C  
ANISOU 4007  CG2 VAL B 300    24385  22031   9251  -1727    838  -2003       C  
ATOM   4008  N   GLN B 301     -20.134  -8.998  -6.041  1.00115.29           N  
ANISOU 4008  N   GLN B 301    20459  17915   5430  -1766    316   -992       N  
ATOM   4009  CA  GLN B 301     -20.399  -7.586  -5.786  1.00114.94           C  
ANISOU 4009  CA  GLN B 301    20488  17802   5383  -1779    290   -636       C  
ATOM   4010  C   GLN B 301     -21.001  -7.364  -4.401  1.00110.04           C  
ANISOU 4010  C   GLN B 301    19611  17047   5152  -1748    124   -553       C  
ATOM   4011  O   GLN B 301     -20.653  -6.405  -3.711  1.00108.01           O  
ANISOU 4011  O   GLN B 301    19297  16676   5067  -1781    285   -358       O  
ATOM   4012  CB  GLN B 301     -21.319  -7.002  -6.864  1.00119.38           C  
ANISOU 4012  CB  GLN B 301    21340  18466   5554  -1736     -2   -425       C  
ATOM   4013  CG  GLN B 301     -20.635  -6.718  -8.197  1.00124.57           C  
ANISOU 4013  CG  GLN B 301    22300  19237   5794  -1781    218   -390       C  
ATOM   4014  CD  GLN B 301     -20.283  -7.979  -8.965  1.00126.93           C  
ANISOU 4014  CD  GLN B 301    22647  19666   5914  -1782    271   -726       C  
ATOM   4015  OE1 GLN B 301     -20.781  -9.064  -8.665  1.00125.34           O  
ANISOU 4015  OE1 GLN B 301    22293  19477   5853  -1741     63   -969       O  
ATOM   4016  NE2 GLN B 301     -19.419  -7.840  -9.964  1.00130.96           N  
ANISOU 4016  NE2 GLN B 301    23376  20266   6116  -1830    555   -741       N  
ATOM   4017  N   ALA B 302     -21.901  -8.255  -3.998  1.00133.51           N  
ANISOU 4017  N   ALA B 302    22432  20032   8266  -1693   -194   -708       N  
ATOM   4018  CA  ALA B 302     -22.526  -8.169  -2.682  1.00129.56           C  
ANISOU 4018  CA  ALA B 302    21678  19418   8132  -1662   -363   -652       C  
ATOM   4019  C   ALA B 302     -21.515  -8.477  -1.581  1.00125.36           C  
ANISOU 4019  C   ALA B 302    20898  18780   7954  -1707    -34   -794       C  
ATOM   4020  O   ALA B 302     -21.540  -7.871  -0.507  1.00121.70           O  
ANISOU 4020  O   ALA B 302    20280  18205   7755  -1712      0   -661       O  
ATOM   4021  CB  ALA B 302     -23.714  -9.114  -2.596  1.00131.75           C  
ANISOU 4021  CB  ALA B 302    21846  19744   8470  -1608   -775   -797       C  
ATOM   4022  N   LEU B 303     -20.624  -9.424  -1.855  1.00158.75           N  
ANISOU 4022  N   LEU B 303    25086  23047  12184  -1730    202  -1066       N  
ATOM   4023  CA  LEU B 303     -19.588  -9.789  -0.899  1.00155.42           C  
ANISOU 4023  CA  LEU B 303    24418  22544  12091  -1755    515  -1213       C  
ATOM   4024  C   LEU B 303     -18.607  -8.642  -0.682  1.00155.14           C  
ANISOU 4024  C   LEU B 303    24393  22460  12095  -1825    854  -1027       C  
ATOM   4025  O   LEU B 303     -18.289  -8.300   0.457  1.00152.51           O  
ANISOU 4025  O   LEU B 303    23847  22028  12073  -1845    970   -984       O  
ATOM   4026  CB  LEU B 303     -18.850 -11.051  -1.351  1.00156.29           C  
ANISOU 4026  CB  LEU B 303    24499  22706  12180  -1739    684  -1534       C  
ATOM   4027  CG  LEU B 303     -19.262 -12.350  -0.652  1.00154.19           C  
ANISOU 4027  CG  LEU B 303    24021  22385  12179  -1687    523  -1786       C  
ATOM   4028  CD1 LEU B 303     -20.762 -12.580  -0.766  1.00154.17           C  
ANISOU 4028  CD1 LEU B 303    24064  22401  12113  -1661     66  -1754       C  
ATOM   4029  CD2 LEU B 303     -18.491 -13.535  -1.215  1.00156.06           C  
ANISOU 4029  CD2 LEU B 303    24272  22657  12369  -1656    704  -2086       C  
ATOM   4030  N   ARG B 304     -18.139  -8.042  -1.773  1.00105.02           N  
ANISOU 4030  N   ARG B 304    18293  16180   5431  -1869   1010   -918       N  
ATOM   4031  CA  ARG B 304     -17.196  -6.933  -1.674  1.00105.38           C  
ANISOU 4031  CA  ARG B 304    18363  16172   5502  -1956   1335   -740       C  
ATOM   4032  C   ARG B 304     -17.858  -5.676  -1.109  1.00104.02           C  
ANISOU 4032  C   ARG B 304    18233  15888   5400  -1966   1193   -428       C  
ATOM   4033  O   ARG B 304     -17.212  -4.888  -0.415  1.00102.35           O  
ANISOU 4033  O   ARG B 304    17922  15577   5388  -2035   1418   -319       O  
ATOM   4034  CB  ARG B 304     -16.532  -6.641  -3.024  1.00110.32           C  
ANISOU 4034  CB  ARG B 304    19253  16898   5763  -2009   1546   -702       C  
ATOM   4035  CG  ARG B 304     -17.475  -6.136  -4.101  1.00114.13           C  
ANISOU 4035  CG  ARG B 304    20062  17445   5855  -1979   1284   -505       C  
ATOM   4036  CD  ARG B 304     -16.718  -5.759  -5.364  1.00119.07           C  
ANISOU 4036  CD  ARG B 304    20950  18165   6127  -2043   1537   -449       C  
ATOM   4037  NE  ARG B 304     -17.607  -5.234  -6.396  1.00123.02           N  
ANISOU 4037  NE  ARG B 304    21768  18732   6240  -2007   1282   -246       N  
ATOM   4038  CZ  ARG B 304     -17.968  -3.959  -6.493  1.00124.17           C  
ANISOU 4038  CZ  ARG B 304    22080  18804   6296  -2022   1220     85       C  
ATOM   4039  NH1 ARG B 304     -17.517  -3.072  -5.616  1.00121.63           N  
ANISOU 4039  NH1 ARG B 304    21643  18328   6243  -2085   1400    240       N  
ATOM   4040  NH2 ARG B 304     -18.781  -3.569  -7.465  1.00128.08           N  
ANISOU 4040  NH2 ARG B 304    22857  19375   6432  -1969    971    261       N  
ATOM   4041  N   ARG B 305     -19.144  -5.491  -1.398  1.00118.34           N  
ANISOU 4041  N   ARG B 305    20185  17717   7063  -1892    814   -288       N  
ATOM   4042  CA  ARG B 305     -19.871  -4.359  -0.835  1.00117.45           C  
ANISOU 4042  CA  ARG B 305    20107  17489   7029  -1867    647      9       C  
ATOM   4043  C   ARG B 305     -20.029  -4.560   0.671  1.00112.40           C  
ANISOU 4043  C   ARG B 305    19162  16745   6800  -1852    612    -54       C  
ATOM   4044  O   ARG B 305     -19.981  -3.601   1.445  1.00110.95           O  
ANISOU 4044  O   ARG B 305    18936  16432   6789  -1874    682    134       O  
ATOM   4045  CB  ARG B 305     -21.226  -4.150  -1.530  1.00121.14           C  
ANISOU 4045  CB  ARG B 305    20769  18014   7247  -1767    226    175       C  
ATOM   4046  CG  ARG B 305     -22.393  -4.928  -0.943  1.00118.90           C  
ANISOU 4046  CG  ARG B 305    20302  17747   7127  -1676   -161     79       C  
ATOM   4047  CD  ARG B 305     -23.711  -4.542  -1.598  1.00121.62           C  
ANISOU 4047  CD  ARG B 305    20807  18151   7253  -1573   -581    281       C  
ATOM   4048  NE  ARG B 305     -23.683  -4.726  -3.046  1.00126.22           N  
ANISOU 4048  NE  ARG B 305    21650  18878   7431  -1575   -616    263       N  
ATOM   4049  CZ  ARG B 305     -24.737  -4.562  -3.839  1.00129.45           C  
ANISOU 4049  CZ  ARG B 305    22206  19385   7594  -1488   -977    392       C  
ATOM   4050  NH1 ARG B 305     -25.909  -4.215  -3.324  1.00128.46           N  
ANISOU 4050  NH1 ARG B 305    21973  19227   7610  -1384  -1339    549       N  
ATOM   4051  NH2 ARG B 305     -24.621  -4.748  -5.146  1.00134.09           N  
ANISOU 4051  NH2 ARG B 305    23037  20113   7799  -1499   -981    361       N  
ATOM   4052  N   GLY B 306     -20.188  -5.817   1.082  1.00 92.17           N  
ANISOU 4052  N   GLY B 306    16397  14231   4393  -1816    517   -323       N  
ATOM   4053  CA  GLY B 306     -20.231  -6.154   2.491  1.00 87.58           C  
ANISOU 4053  CA  GLY B 306    15518  13566   4193  -1806    513   -416       C  
ATOM   4054  C   GLY B 306     -18.885  -5.896   3.138  1.00 85.86           C  
ANISOU 4054  C   GLY B 306    15143  13289   4189  -1888    919   -474       C  
ATOM   4055  O   GLY B 306     -18.808  -5.443   4.282  1.00 82.75           O  
ANISOU 4055  O   GLY B 306    14581  12796   4066  -1904    973   -407       O  
ATOM   4056  N   VAL B 307     -17.820  -6.185   2.394  1.00 88.13           N  
ANISOU 4056  N   VAL B 307    15480  13647   4357  -1939   1199   -601       N  
ATOM   4057  CA  VAL B 307     -16.459  -5.925   2.850  1.00 87.26           C  
ANISOU 4057  CA  VAL B 307    15211  13505   4439  -2022   1584   -659       C  
ATOM   4058  C   VAL B 307     -16.250  -4.438   3.117  1.00 87.44           C  
ANISOU 4058  C   VAL B 307    15315  13421   4487  -2107   1707   -386       C  
ATOM   4059  O   VAL B 307     -15.768  -4.049   4.184  1.00 84.73           O  
ANISOU 4059  O   VAL B 307    14765  12992   4436  -2152   1847   -378       O  
ATOM   4060  CB  VAL B 307     -15.417  -6.403   1.816  1.00 90.56           C  
ANISOU 4060  CB  VAL B 307    15703  14030   4674  -2057   1848   -811       C  
ATOM   4061  CG1 VAL B 307     -14.034  -5.871   2.161  1.00 90.50           C  
ANISOU 4061  CG1 VAL B 307    15553  13997   4834  -2160   2234   -811       C  
ATOM   4062  CG2 VAL B 307     -15.410  -7.920   1.727  1.00 90.09           C  
ANISOU 4062  CG2 VAL B 307    15524  14042   4663  -1972   1788  -1112       C  
ATOM   4063  N   LEU B 308     -16.620  -3.610   2.145  1.00 97.69           N  
ANISOU 4063  N   LEU B 308    16920  14718   5480  -2125   1646   -163       N  
ATOM   4064  CA  LEU B 308     -16.463  -2.165   2.274  1.00 98.48           C  
ANISOU 4064  CA  LEU B 308    17146  14691   5582  -2201   1757    113       C  
ATOM   4065  C   LEU B 308     -17.332  -1.583   3.389  1.00 95.35           C  
ANISOU 4065  C   LEU B 308    16673  14155   5400  -2149   1549    269       C  
ATOM   4066  O   LEU B 308     -16.890  -0.703   4.130  1.00 94.10           O  
ANISOU 4066  O   LEU B 308    16452  13866   5436  -2222   1714    378       O  
ATOM   4067  CB  LEU B 308     -16.747  -1.460   0.944  1.00103.71           C  
ANISOU 4067  CB  LEU B 308    18172  15377   5855  -2210   1714    328       C  
ATOM   4068  CG  LEU B 308     -15.550  -1.238   0.013  1.00107.49           C  
ANISOU 4068  CG  LEU B 308    18765  15919   6158  -2328   2065    300       C  
ATOM   4069  CD1 LEU B 308     -14.488  -0.395   0.705  1.00106.63           C  
ANISOU 4069  CD1 LEU B 308    18520  15695   6299  -2468   2393    348       C  
ATOM   4070  CD2 LEU B 308     -14.958  -2.555  -0.467  1.00108.30           C  
ANISOU 4070  CD2 LEU B 308    18763  16186   6202  -2309   2168     -7       C  
ATOM   4071  N   VAL B 309     -18.564  -2.076   3.505  1.00 87.46           N  
ANISOU 4071  N   VAL B 309    15678  13184   4369  -2026   1187    275       N  
ATOM   4072  CA  VAL B 309     -19.452  -1.646   4.584  1.00 84.55           C  
ANISOU 4072  CA  VAL B 309    15220  12697   4207  -1958    973    410       C  
ATOM   4073  C   VAL B 309     -18.853  -1.972   5.951  1.00 80.42           C  
ANISOU 4073  C   VAL B 309    14376  12126   4055  -2001   1143    244       C  
ATOM   4074  O   VAL B 309     -18.791  -1.113   6.836  1.00 78.75           O  
ANISOU 4074  O   VAL B 309    14114  11776   4032  -2028   1215    378       O  
ATOM   4075  CB  VAL B 309     -20.851  -2.291   4.467  1.00 84.29           C  
ANISOU 4075  CB  VAL B 309    15197  12732   4099  -1822    543    408       C  
ATOM   4076  CG1 VAL B 309     -21.613  -2.167   5.779  1.00 80.66           C  
ANISOU 4076  CG1 VAL B 309    14553  12176   3918  -1757    360    468       C  
ATOM   4077  CG2 VAL B 309     -21.637  -1.657   3.332  1.00 88.27           C  
ANISOU 4077  CG2 VAL B 309    16005  13255   4278  -1754    317    649       C  
ATOM   4078  N   LEU B 310     -18.404  -3.214   6.110  1.00 99.70           N  
ANISOU 4078  N   LEU B 310    16607  14675   6599  -1997   1207    -47       N  
ATOM   4079  CA  LEU B 310     -17.807  -3.665   7.362  1.00 96.24           C  
ANISOU 4079  CA  LEU B 310    15845  14213   6508  -2018   1356   -225       C  
ATOM   4080  C   LEU B 310     -16.569  -2.849   7.720  1.00 97.05           C  
ANISOU 4080  C   LEU B 310    15873  14249   6753  -2138   1705   -193       C  
ATOM   4081  O   LEU B 310     -16.418  -2.402   8.859  1.00 95.84           O  
ANISOU 4081  O   LEU B 310    15551  14004   6859  -2163   1769   -168       O  
ATOM   4082  CB  LEU B 310     -17.444  -5.148   7.279  1.00 94.22           C  
ANISOU 4082  CB  LEU B 310    15409  14073   6315  -1977   1379   -534       C  
ATOM   4083  CG  LEU B 310     -16.852  -5.752   8.554  1.00 91.15           C  
ANISOU 4083  CG  LEU B 310    14674  13670   6289  -1966   1503   -725       C  
ATOM   4084  CD1 LEU B 310     -17.900  -5.813   9.655  1.00 88.49           C  
ANISOU 4084  CD1 LEU B 310    14221  13273   6126  -1902   1256   -678       C  
ATOM   4085  CD2 LEU B 310     -16.270  -7.127   8.281  1.00 91.91           C  
ANISOU 4085  CD2 LEU B 310    14635  13858   6429  -1919   1578  -1009       C  
ATOM   4086  N   ARG B 311     -15.690  -2.660   6.740  1.00 86.50           N  
ANISOU 4086  N   ARG B 311    14658  12963   5245  -2218   1927   -200       N  
ATOM   4087  CA  ARG B 311     -14.479  -1.868   6.927  1.00 86.71           C  
ANISOU 4087  CA  ARG B 311    14620  12938   5390  -2355   2254   -172       C  
ATOM   4088  C   ARG B 311     -14.822  -0.447   7.361  1.00 85.62           C  
ANISOU 4088  C   ARG B 311    14615  12624   5293  -2412   2242     96       C  
ATOM   4089  O   ARG B 311     -14.192   0.110   8.265  1.00 83.84           O  
ANISOU 4089  O   ARG B 311    14227  12311   5319  -2497   2410     91       O  
ATOM   4090  CB  ARG B 311     -13.662  -1.838   5.634  1.00 92.15           C  
ANISOU 4090  CB  ARG B 311    15471  13714   5830  -2430   2464   -189       C  
ATOM   4091  CG  ARG B 311     -12.378  -1.030   5.722  1.00 93.94           C  
ANISOU 4091  CG  ARG B 311    15634  13898   6163  -2591   2801   -159       C  
ATOM   4092  CD  ARG B 311     -11.680  -0.973   4.374  1.00 98.39           C  
ANISOU 4092  CD  ARG B 311    16385  14554   6447  -2663   3000   -154       C  
ATOM   4093  NE  ARG B 311     -11.395  -2.306   3.853  1.00 99.61           N  
ANISOU 4093  NE  ARG B 311    16447  14871   6530  -2582   3021   -399       N  
ATOM   4094  CZ  ARG B 311     -10.880  -2.544   2.651  1.00103.68           C  
ANISOU 4094  CZ  ARG B 311    17118  15496   6782  -2609   3170   -441       C  
ATOM   4095  NH1 ARG B 311     -10.593  -1.535   1.839  1.00108.11           N  
ANISOU 4095  NH1 ARG B 311    17929  16028   7120  -2720   3312   -246       N  
ATOM   4096  NH2 ARG B 311     -10.655  -3.790   2.259  1.00103.80           N  
ANISOU 4096  NH2 ARG B 311    17048  15640   6753  -2521   3184   -676       N  
ATOM   4097  N   ALA B 312     -15.831   0.128   6.713  1.00 93.69           N  
ANISOU 4097  N   ALA B 312    15934  13589   6073  -2353   2031    328       N  
ATOM   4098  CA  ALA B 312     -16.292   1.471   7.040  1.00 94.51           C  
ANISOU 4098  CA  ALA B 312    16206  13501   6202  -2369   1987    607       C  
ATOM   4099  C   ALA B 312     -16.786   1.550   8.481  1.00 90.76           C  
ANISOU 4099  C   ALA B 312    15534  12925   6023  -2315   1878    602       C  
ATOM   4100  O   ALA B 312     -16.463   2.493   9.204  1.00 89.72           O  
ANISOU 4100  O   ALA B 312    15381  12637   6072  -2389   2008    698       O  
ATOM   4101  CB  ALA B 312     -17.386   1.907   6.077  1.00 96.40           C  
ANISOU 4101  CB  ALA B 312    16777  13716   6133  -2268   1728    851       C  
ATOM   4102  N   MET B 313     -17.564   0.554   8.897  1.00 87.15           N  
ANISOU 4102  N   MET B 313    14941  12557   5616  -2194   1641    483       N  
ATOM   4103  CA  MET B 313     -18.091   0.519  10.259  1.00 83.54           C  
ANISOU 4103  CA  MET B 313    14295  12024   5421  -2135   1531    472       C  
ATOM   4104  C   MET B 313     -16.989   0.350  11.303  1.00 81.01           C  
ANISOU 4104  C   MET B 313    13667  11704   5409  -2229   1793    274       C  
ATOM   4105  O   MET B 313     -17.055   0.937  12.384  1.00 79.51           O  
ANISOU 4105  O   MET B 313    13390  11390   5431  -2242   1823    332       O  
ATOM   4106  CB  MET B 313     -19.143  -0.583  10.410  1.00 81.25           C  
ANISOU 4106  CB  MET B 313    13918  11842   5112  -2000   1218    376       C  
ATOM   4107  CG  MET B 313     -20.441  -0.303   9.669  1.00 83.66           C  
ANISOU 4107  CG  MET B 313    14477  12131   5177  -1883    881    598       C  
ATOM   4108  SD  MET B 313     -21.720  -1.528  10.007  1.00 83.25           S  
ANISOU 4108  SD  MET B 313    14255  12187   5188  -1736    479    484       S  
ATOM   4109  CE  MET B 313     -20.921  -3.021   9.428  1.00 82.35           C  
ANISOU 4109  CE  MET B 313    14015  12268   5006  -1803    609    126       C  
ATOM   4110  N   VAL B 314     -15.978  -0.450  10.977  1.00 69.52           N  
ANISOU 4110  N   VAL B 314    12048  10386   3981  -2281   1970     44       N  
ATOM   4111  CA  VAL B 314     -14.851  -0.656  11.883  1.00 67.76           C  
ANISOU 4111  CA  VAL B 314    11512  10182   4051  -2354   2198   -144       C  
ATOM   4112  C   VAL B 314     -14.031   0.622  12.044  1.00 69.15           C  
ANISOU 4112  C   VAL B 314    11737  10231   4305  -2509   2428    -27       C  
ATOM   4113  O   VAL B 314     -13.752   1.055  13.168  1.00 67.23           O  
ANISOU 4113  O   VAL B 314    11324   9905   4316  -2551   2493    -50       O  
ATOM   4114  CB  VAL B 314     -13.934  -1.800  11.404  1.00 68.38           C  
ANISOU 4114  CB  VAL B 314    11417  10427   4137  -2351   2328   -396       C  
ATOM   4115  CG1 VAL B 314     -12.663  -1.852  12.239  1.00 67.26           C  
ANISOU 4115  CG1 VAL B 314    10960  10304   4290  -2424   2555   -556       C  
ATOM   4116  CG2 VAL B 314     -14.670  -3.128  11.465  1.00 66.73           C  
ANISOU 4116  CG2 VAL B 314    11122  10315   3919  -2206   2112   -547       C  
ATOM   4117  N   ILE B 315     -13.654   1.223  10.918  1.00 72.69           N  
ANISOU 4117  N   ILE B 315    12424  10663   4532  -2598   2546     91       N  
ATOM   4118  CA  ILE B 315     -12.908   2.477  10.928  1.00 74.61           C  
ANISOU 4118  CA  ILE B 315    12749  10772   4826  -2763   2763    211       C  
ATOM   4119  C   ILE B 315     -13.672   3.562  11.684  1.00 73.65           C  
ANISOU 4119  C   ILE B 315    12759  10431   4793  -2750   2660    422       C  
ATOM   4120  O   ILE B 315     -13.102   4.271  12.518  1.00 73.12           O  
ANISOU 4120  O   ILE B 315    12592  10246   4943  -2861   2800    417       O  
ATOM   4121  CB  ILE B 315     -12.588   2.958   9.497  1.00 78.94           C  
ANISOU 4121  CB  ILE B 315    13584  11330   5080  -2844   2881    340       C  
ATOM   4122  CG1 ILE B 315     -11.609   1.996   8.820  1.00 80.32           C  
ANISOU 4122  CG1 ILE B 315    13613  11703   5201  -2883   3057    122       C  
ATOM   4123  CG2 ILE B 315     -12.008   4.363   9.517  1.00 81.13           C  
ANISOU 4123  CG2 ILE B 315    14001  11425   5399  -3010   3068    507       C  
ATOM   4124  CD1 ILE B 315     -10.273   1.888   9.525  1.00 79.61           C  
ANISOU 4124  CD1 ILE B 315    13200  11654   5396  -3003   3295    -66       C  
ATOM   4125  N   ALA B 316     -14.968   3.671  11.401  1.00 73.62           N  
ANISOU 4125  N   ALA B 316    12977  10371   4626  -2608   2404    603       N  
ATOM   4126  CA  ALA B 316     -15.827   4.636  12.081  1.00 72.88           C  
ANISOU 4126  CA  ALA B 316    13022  10058   4611  -2551   2280    820       C  
ATOM   4127  C   ALA B 316     -15.854   4.395  13.587  1.00 69.11           C  
ANISOU 4127  C   ALA B 316    12263   9551   4444  -2529   2271    687       C  
ATOM   4128  O   ALA B 316     -15.730   5.335  14.374  1.00 68.72           O  
ANISOU 4128  O   ALA B 316    12224   9317   4571  -2588   2354    763       O  
ATOM   4129  CB  ALA B 316     -17.237   4.591  11.511  1.00 73.60           C  
ANISOU 4129  CB  ALA B 316    13355  10130   4479  -2369   1967   1021       C  
ATOM   4130  N   PHE B 317     -16.012   3.134  13.981  1.00 94.01           N  
ANISOU 4130  N   PHE B 317    15173  12882   7663  -2443   2172    484       N  
ATOM   4131  CA  PHE B 317     -16.053   2.776  15.395  1.00 91.42           C  
ANISOU 4131  CA  PHE B 317    14565  12556   7615  -2406   2156    346       C  
ATOM   4132  C   PHE B 317     -14.762   3.172  16.103  1.00 89.79           C  
ANISOU 4132  C   PHE B 317    14147  12319   7651  -2560   2410    210       C  
ATOM   4133  O   PHE B 317     -14.795   3.803  17.159  1.00 89.20           O  
ANISOU 4133  O   PHE B 317    14017  12105   7770  -2586   2440    240       O  
ATOM   4134  CB  PHE B 317     -16.310   1.276  15.572  1.00 89.49           C  
ANISOU 4134  CB  PHE B 317    14086  12516   7401  -2295   2029    128       C  
ATOM   4135  CG  PHE B 317     -16.568   0.867  16.997  1.00 87.89           C  
ANISOU 4135  CG  PHE B 317    13546  12277   7572  -2159   1913     13       C  
ATOM   4136  CD1 PHE B 317     -15.519   0.545  17.844  1.00 86.22           C  
ANISOU 4136  CD1 PHE B 317    13059  12134   7566  -2243   2101   -193       C  
ATOM   4137  CD2 PHE B 317     -17.861   0.805  17.491  1.00 89.44           C  
ANISOU 4137  CD2 PHE B 317    13696  12378   7907  -1946   1615    115       C  
ATOM   4138  CE1 PHE B 317     -15.753   0.169  19.153  1.00 85.42           C  
ANISOU 4138  CE1 PHE B 317    12674  12003   7778  -2115   1991   -288       C  
ATOM   4139  CE2 PHE B 317     -18.101   0.430  18.800  1.00 88.52           C  
ANISOU 4139  CE2 PHE B 317    13288  12230   8115  -1826   1529     17       C  
ATOM   4140  CZ  PHE B 317     -17.046   0.112  19.631  1.00 86.30           C  
ANISOU 4140  CZ  PHE B 317    12765  12012   8011  -1910   1715   -181       C  
ATOM   4141  N   VAL B 318     -13.627   2.800  15.518  1.00 64.25           N  
ANISOU 4141  N   VAL B 318    10795   9215   4403  -2661   2583     58       N  
ATOM   4142  CA  VAL B 318     -12.332   3.115  16.114  1.00 64.41           C  
ANISOU 4142  CA  VAL B 318    10593   9235   4647  -2811   2799    -81       C  
ATOM   4143  C   VAL B 318     -12.113   4.623  16.228  1.00 66.33           C  
ANISOU 4143  C   VAL B 318    11031   9256   4915  -2962   2917     90       C  
ATOM   4144  O   VAL B 318     -11.849   5.140  17.318  1.00 65.16           O  
ANISOU 4144  O   VAL B 318    10757   9008   4992  -3025   2963     46       O  
ATOM   4145  CB  VAL B 318     -11.171   2.482  15.323  1.00 66.24           C  
ANISOU 4145  CB  VAL B 318    10693   9643   4834  -2884   2964   -245       C  
ATOM   4146  CG1 VAL B 318      -9.833   2.969  15.860  1.00 67.04           C  
ANISOU 4146  CG1 VAL B 318    10585   9739   5147  -3055   3172   -360       C  
ATOM   4147  CG2 VAL B 318     -11.256   0.965  15.384  1.00 64.33           C  
ANISOU 4147  CG2 VAL B 318    10228   9591   4625  -2731   2863   -445       C  
ATOM   4148  N   VAL B 319     -12.240   5.321  15.101  1.00 72.55           N  
ANISOU 4148  N   VAL B 319    12137   9959   5470  -3014   2958    283       N  
ATOM   4149  CA  VAL B 319     -12.024   6.766  15.052  1.00 74.95           C  
ANISOU 4149  CA  VAL B 319    12662  10032   5782  -3157   3078    456       C  
ATOM   4150  C   VAL B 319     -12.930   7.533  16.017  1.00 73.42           C  
ANISOU 4150  C   VAL B 319    12575   9606   5714  -3085   2958    597       C  
ATOM   4151  O   VAL B 319     -12.476   8.437  16.720  1.00 73.80           O  
ANISOU 4151  O   VAL B 319    12609   9489   5940  -3211   3071    593       O  
ATOM   4152  CB  VAL B 319     -12.208   7.314  13.618  1.00 78.74           C  
ANISOU 4152  CB  VAL B 319    13496  10457   5962  -3184   3110    668       C  
ATOM   4153  CG1 VAL B 319     -12.214   8.836  13.617  1.00 81.20           C  
ANISOU 4153  CG1 VAL B 319    14075  10488   6288  -3293   3197    879       C  
ATOM   4154  CG2 VAL B 319     -11.116   6.781  12.703  1.00 80.89           C  
ANISOU 4154  CG2 VAL B 319    13676  10927   6130  -3295   3295    529       C  
ATOM   4155  N   CYS B 320     -14.206   7.161  16.060  1.00 75.18           N  
ANISOU 4155  N   CYS B 320    12901   9816   5850  -2883   2727    711       N  
ATOM   4156  CA  CYS B 320     -15.167   7.859  16.911  1.00 73.72           C  
ANISOU 4156  CA  CYS B 320    12837   9402   5773  -2779   2604    868       C  
ATOM   4157  C   CYS B 320     -15.006   7.536  18.396  1.00 71.74           C  
ANISOU 4157  C   CYS B 320    12286   9166   5805  -2776   2618    682       C  
ATOM   4158  O   CYS B 320     -15.069   8.429  19.240  1.00 71.43           O  
ANISOU 4158  O   CYS B 320    12300   8909   5931  -2809   2659    737       O  
ATOM   4159  CB  CYS B 320     -16.602   7.566  16.464  1.00 73.67           C  
ANISOU 4159  CB  CYS B 320    13026   9386   5580  -2551   2332   1061       C  
ATOM   4160  SG  CYS B 320     -17.024   8.217  14.831  1.00 76.74           S  
ANISOU 4160  SG  CYS B 320    13818   9701   5638  -2513   2261   1339       S  
ATOM   4161  N   TRP B 321     -14.798   6.261  18.712  1.00 64.49           N  
ANISOU 4161  N   TRP B 321    11063   8497   4944  -2727   2581    459       N  
ATOM   4162  CA  TRP B 321     -14.752   5.826  20.106  1.00 61.32           C  
ANISOU 4162  CA  TRP B 321    10330   8126   4846  -2645   2517    278       C  
ATOM   4163  C   TRP B 321     -13.373   5.945  20.756  1.00 61.30           C  
ANISOU 4163  C   TRP B 321    10100   8187   5003  -2860   2745     70       C  
ATOM   4164  O   TRP B 321     -13.237   5.731  21.960  1.00 59.52           O  
ANISOU 4164  O   TRP B 321     9634   7974   5005  -2826   2716    -71       O  
ATOM   4165  CB  TRP B 321     -15.276   4.393  20.247  1.00 59.81           C  
ANISOU 4165  CB  TRP B 321     9890   8134   4700  -2435   2311    145       C  
ATOM   4166  CG  TRP B 321     -16.749   4.261  20.006  1.00 62.17           C  
ANISOU 4166  CG  TRP B 321    10303   8357   4962  -2186   2018    316       C  
ATOM   4167  CD1 TRP B 321     -17.365   4.001  18.816  1.00 65.85           C  
ANISOU 4167  CD1 TRP B 321    10968   8878   5171  -2123   1898    439       C  
ATOM   4168  CD2 TRP B 321     -17.792   4.379  20.981  1.00 61.57           C  
ANISOU 4168  CD2 TRP B 321    10132   8149   5110  -1967   1808    376       C  
ATOM   4169  NE1 TRP B 321     -18.727   3.951  18.990  1.00 66.72           N  
ANISOU 4169  NE1 TRP B 321    11093   8908   5350  -1882   1611    573       N  
ATOM   4170  CE2 TRP B 321     -19.015   4.179  20.309  1.00 64.80           C  
ANISOU 4170  CE2 TRP B 321    10665   8548   5405  -1781   1564    539       C  
ATOM   4171  CE3 TRP B 321     -17.811   4.633  22.355  1.00 59.10           C  
ANISOU 4171  CE3 TRP B 321     9642   7736   5075  -1912   1805    304       C  
ATOM   4172  CZ2 TRP B 321     -20.244   4.227  20.965  1.00 65.56           C  
ANISOU 4172  CZ2 TRP B 321    10688   8542   5680  -1543   1333    633       C  
ATOM   4173  CZ3 TRP B 321     -19.032   4.680  23.005  1.00 59.75           C  
ANISOU 4173  CZ3 TRP B 321     9679   7708   5313  -1672   1590    398       C  
ATOM   4174  CH2 TRP B 321     -20.231   4.478  22.310  1.00 62.86           C  
ANISOU 4174  CH2 TRP B 321    10174   8098   5611  -1491   1364    561       C  
ATOM   4175  N   LEU B 322     -12.356   6.280  19.967  1.00 61.47           N  
ANISOU 4175  N   LEU B 322    10148   8242   4965  -3025   2902     39       N  
ATOM   4176  CA  LEU B 322     -11.010   6.458  20.521  1.00 61.98           C  
ANISOU 4176  CA  LEU B 322     9964   8363   5223  -3199   3059   -158       C  
ATOM   4177  C   LEU B 322     -10.902   7.579  21.570  1.00 62.06           C  
ANISOU 4177  C   LEU B 322    10010   8156   5416  -3308   3109   -144       C  
ATOM   4178  O   LEU B 322     -10.458   7.323  22.690  1.00 60.36           O  
ANISOU 4178  O   LEU B 322     9522   8008   5405  -3321   3099   -327       O  
ATOM   4179  CB  LEU B 322      -9.957   6.623  19.413  1.00 65.16           C  
ANISOU 4179  CB  LEU B 322    10400   8842   5517  -3361   3232   -182       C  
ATOM   4180  CG  LEU B 322      -8.484   6.633  19.839  1.00 66.05           C  
ANISOU 4180  CG  LEU B 322    10222   9065   5812  -3532   3384   -399       C  
ATOM   4181  CD1 LEU B 322      -7.633   5.908  18.808  1.00 67.85           C  
ANISOU 4181  CD1 LEU B 322    10346   9500   5935  -3566   3493   -491       C  
ATOM   4182  CD2 LEU B 322      -7.969   8.053  20.040  1.00 68.50           C  
ANISOU 4182  CD2 LEU B 322    10672   9167   6189  -3755   3523   -338       C  
ATOM   4183  N   PRO B 323     -11.307   8.820  21.225  1.00 74.26           N  
ANISOU 4183  N   PRO B 323    11897   9431   6886  -3377   3153     71       N  
ATOM   4184  CA  PRO B 323     -11.111   9.888  22.214  1.00 74.66           C  
ANISOU 4184  CA  PRO B 323    11991   9258   7118  -3494   3213     58       C  
ATOM   4185  C   PRO B 323     -12.073   9.781  23.393  1.00 73.63           C  
ANISOU 4185  C   PRO B 323    11829   9030   7115  -3333   3079     67       C  
ATOM   4186  O   PRO B 323     -11.781  10.301  24.471  1.00 73.11           O  
ANISOU 4186  O   PRO B 323    11683   8860   7236  -3415   3115    -36       O  
ATOM   4187  CB  PRO B 323     -11.406  11.156  21.412  1.00 76.07           C  
ANISOU 4187  CB  PRO B 323    12576   9158   7168  -3562   3278    306       C  
ATOM   4188  CG  PRO B 323     -12.380  10.718  20.386  1.00 75.99           C  
ANISOU 4188  CG  PRO B 323    12764   9183   6925  -3377   3155    503       C  
ATOM   4189  CD  PRO B 323     -11.964   9.327  20.004  1.00 74.69           C  
ANISOU 4189  CD  PRO B 323    12320   9358   6699  -3336   3134    329       C  
ATOM   4190  N   TYR B 324     -13.205   9.116  23.181  1.00 66.51           N  
ANISOU 4190  N   TYR B 324    10987   8166   6117  -3099   2913    182       N  
ATOM   4191  CA  TYR B 324     -14.191   8.899  24.234  1.00 65.04           C  
ANISOU 4191  CA  TYR B 324    10684   7906   6121  -2823   2679    170       C  
ATOM   4192  C   TYR B 324     -13.581   8.132  25.400  1.00 63.20           C  
ANISOU 4192  C   TYR B 324    10065   7859   6086  -2823   2664   -100       C  
ATOM   4193  O   TYR B 324     -13.907   8.380  26.561  1.00 63.97           O  
ANISOU 4193  O   TYR B 324    10082   7851   6370  -2726   2581   -155       O  
ATOM   4194  CB  TYR B 324     -15.397   8.143  23.671  1.00 67.00           C  
ANISOU 4194  CB  TYR B 324    10958   8223   6274  -2538   2443    294       C  
ATOM   4195  CG  TYR B 324     -16.355   7.610  24.714  1.00 66.75           C  
ANISOU 4195  CG  TYR B 324    10729   8190   6440  -2258   2216    251       C  
ATOM   4196  CD1 TYR B 324     -17.337   8.422  25.265  1.00 68.45           C  
ANISOU 4196  CD1 TYR B 324    11089   8154   6765  -2087   2107    398       C  
ATOM   4197  CD2 TYR B 324     -16.287   6.287  25.135  1.00 65.11           C  
ANISOU 4197  CD2 TYR B 324    10201   8226   6311  -2158   2122     70       C  
ATOM   4198  CE1 TYR B 324     -18.218   7.935  26.213  1.00 68.48           C  
ANISOU 4198  CE1 TYR B 324    10907   8166   6945  -1837   1926    361       C  
ATOM   4199  CE2 TYR B 324     -17.161   5.792  26.083  1.00 64.86           C  
ANISOU 4199  CE2 TYR B 324    10000   8190   6454  -1917   1935     43       C  
ATOM   4200  CZ  TYR B 324     -18.124   6.619  26.618  1.00 66.60           C  
ANISOU 4200  CZ  TYR B 324    10354   8175   6774  -1763   1843    187       C  
ATOM   4201  OH  TYR B 324     -18.997   6.128  27.561  1.00 67.11           O  
ANISOU 4201  OH  TYR B 324    10243   8245   7010  -1530   1683    160       O  
ATOM   4202  N   HIS B 325     -12.687   7.202  25.081  1.00 53.90           N  
ANISOU 4202  N   HIS B 325     8660   6961   4860  -2920   2748   -265       N  
ATOM   4203  CA  HIS B 325     -12.026   6.389  26.092  1.00 52.08           C  
ANISOU 4203  CA  HIS B 325     8058   6928   4799  -2910   2731   -515       C  
ATOM   4204  C   HIS B 325     -10.811   7.099  26.681  1.00 54.36           C  
ANISOU 4204  C   HIS B 325     8258   7205   5191  -3192   2920   -656       C  
ATOM   4205  O   HIS B 325     -10.503   6.940  27.861  1.00 52.86           O  
ANISOU 4205  O   HIS B 325     7847   7058   5177  -3171   2864   -816       O  
ATOM   4206  CB  HIS B 325     -11.628   5.034  25.506  1.00 51.81           C  
ANISOU 4206  CB  HIS B 325     7811   7190   4684  -2861   2731   -635       C  
ATOM   4207  CG  HIS B 325     -12.796   4.163  25.164  1.00 49.25           C  
ANISOU 4207  CG  HIS B 325     7511   6897   4303  -2585   2513   -550       C  
ATOM   4208  ND1 HIS B 325     -12.875   3.447  23.989  1.00 50.20           N  
ANISOU 4208  ND1 HIS B 325     7687   7155   4230  -2560   2515   -525       N  
ATOM   4209  CD2 HIS B 325     -13.935   3.894  25.845  1.00 46.02           C  
ANISOU 4209  CD2 HIS B 325     7076   6402   4006  -2335   2290   -490       C  
ATOM   4210  CE1 HIS B 325     -14.013   2.777  23.960  1.00 47.64           C  
ANISOU 4210  CE1 HIS B 325     7367   6826   3909  -2317   2288   -459       C  
ATOM   4211  NE2 HIS B 325     -14.673   3.029  25.076  1.00 45.08           N  
ANISOU 4211  NE2 HIS B 325     6983   6370   3776  -2179   2154   -431       N  
ATOM   4212  N   VAL B 326     -10.126   7.883  25.853  1.00 67.90           N  
ANISOU 4212  N   VAL B 326    10122   8844   6833  -3383   3052   -604       N  
ATOM   4213  CA  VAL B 326      -8.993   8.679  26.310  1.00 68.60           C  
ANISOU 4213  CA  VAL B 326    10134   8887   7044  -3617   3167   -733       C  
ATOM   4214  C   VAL B 326      -9.463   9.708  27.334  1.00 69.88           C  
ANISOU 4214  C   VAL B 326    10454   8781   7317  -3667   3163   -696       C  
ATOM   4215  O   VAL B 326      -8.768   9.997  28.309  1.00 70.22           O  
ANISOU 4215  O   VAL B 326    10334   8837   7510  -3791   3182   -872       O  
ATOM   4216  CB  VAL B 326      -8.293   9.393  25.133  1.00 71.09           C  
ANISOU 4216  CB  VAL B 326    10623   9143   7243  -3808   3323   -653       C  
ATOM   4217  CG1 VAL B 326      -7.163  10.280  25.634  1.00 73.44           C  
ANISOU 4217  CG1 VAL B 326    10850   9385   7668  -4063   3443   -786       C  
ATOM   4218  CG2 VAL B 326      -7.768   8.375  24.134  1.00 71.39           C  
ANISOU 4218  CG2 VAL B 326    10507   9442   7176  -3764   3347   -708       C  
ATOM   4219  N   ARG B 327     -10.659  10.245  27.109  1.00 59.13           N  
ANISOU 4219  N   ARG B 327     9416   7173   5878  -3558   3128   -468       N  
ATOM   4220  CA  ARG B 327     -11.260  11.211  28.021  1.00 58.89           C  
ANISOU 4220  CA  ARG B 327     9567   6843   5965  -3530   3091   -416       C  
ATOM   4221  C   ARG B 327     -11.528  10.596  29.390  1.00 55.11           C  
ANISOU 4221  C   ARG B 327     8822   6456   5661  -3332   2913   -584       C  
ATOM   4222  O   ARG B 327     -11.160  11.162  30.419  1.00 55.44           O  
ANISOU 4222  O   ARG B 327     8827   6401   5835  -3432   2933   -714       O  
ATOM   4223  CB  ARG B 327     -12.567  11.747  27.441  1.00 58.76           C  
ANISOU 4223  CB  ARG B 327     9902   6567   5859  -3319   2997   -135       C  
ATOM   4224  CG  ARG B 327     -13.282  12.721  28.355  1.00 58.30           C  
ANISOU 4224  CG  ARG B 327    10024   6189   5938  -3209   2931    -82       C  
ATOM   4225  CD  ARG B 327     -14.642  13.096  27.803  1.00 58.14           C  
ANISOU 4225  CD  ARG B 327    10295   5951   5846  -2944   2810    194       C  
ATOM   4226  NE  ARG B 327     -15.495  11.929  27.605  1.00 54.66           N  
ANISOU 4226  NE  ARG B 327     9680   5717   5371  -2647   2602    234       N  
ATOM   4227  CZ  ARG B 327     -16.216  11.361  28.566  1.00 51.00           C  
ANISOU 4227  CZ  ARG B 327     9021   5307   5051  -2395   2431    162       C  
ATOM   4228  NH1 ARG B 327     -16.184  11.850  29.797  1.00 50.47           N  
ANISOU 4228  NH1 ARG B 327     8917   5109   5149  -2389   2443     43       N  
ATOM   4229  NH2 ARG B 327     -16.967  10.302  28.297  1.00 49.22           N  
ANISOU 4229  NH2 ARG B 327     8645   5262   4795  -2159   2254    204       N  
ATOM   4230  N   ARG B 328     -12.178   9.436  29.392  1.00 52.80           N  
ANISOU 4230  N   ARG B 328     8360   6345   5358  -3058   2742   -581       N  
ATOM   4231  CA  ARG B 328     -12.492   8.730  30.628  1.00 49.36           C  
ANISOU 4231  CA  ARG B 328     7677   6012   5067  -2855   2578   -720       C  
ATOM   4232  C   ARG B 328     -11.217   8.282  31.338  1.00 49.90           C  
ANISOU 4232  C   ARG B 328     7430   6311   5219  -3026   2635   -979       C  
ATOM   4233  O   ARG B 328     -11.176   8.194  32.565  1.00 48.34           O  
ANISOU 4233  O   ARG B 328     7091   6132   5145  -2961   2548  -1113       O  
ATOM   4234  CB  ARG B 328     -13.413   7.540  30.344  1.00 46.39           C  
ANISOU 4234  CB  ARG B 328     7192   5780   4656  -2561   2403   -653       C  
ATOM   4235  CG  ARG B 328     -14.775   7.952  29.801  1.00 45.67           C  
ANISOU 4235  CG  ARG B 328     7363   5480   4509  -2358   2300   -408       C  
ATOM   4236  CD  ARG B 328     -15.497   6.809  29.101  1.00 43.85           C  
ANISOU 4236  CD  ARG B 328     7046   5417   4200  -2155   2156   -338       C  
ATOM   4237  NE  ARG B 328     -16.000   5.799  30.028  1.00 40.57           N  
ANISOU 4237  NE  ARG B 328     6384   5120   3913  -1932   1998   -429       N  
ATOM   4238  CZ  ARG B 328     -15.443   4.606  30.209  1.00 39.61           C  
ANISOU 4238  CZ  ARG B 328     5992   5248   3812  -1916   1971   -589       C  
ATOM   4239  NH1 ARG B 328     -14.359   4.265  29.524  1.00 41.56           N  
ANISOU 4239  NH1 ARG B 328     6158   5666   3966  -2099   2094   -688       N  
ATOM   4240  NH2 ARG B 328     -15.973   3.751  31.072  1.00 37.02           N  
ANISOU 4240  NH2 ARG B 328     5477   4990   3598  -1712   1833   -645       N  
ATOM   4241  N   LEU B 329     -10.175   8.009  30.558  1.00 51.37           N  
ANISOU 4241  N   LEU B 329     7505   6682   5332  -3237   2782  -1048       N  
ATOM   4242  CA  LEU B 329      -8.866   7.691  31.115  1.00 52.69           C  
ANISOU 4242  CA  LEU B 329     7359   7077   5585  -3421   2852  -1288       C  
ATOM   4243  C   LEU B 329      -8.206   8.947  31.674  1.00 55.30           C  
ANISOU 4243  C   LEU B 329     7778   7241   5994  -3699   2959  -1364       C  
ATOM   4244  O   LEU B 329      -7.465   8.886  32.653  1.00 55.44           O  
ANISOU 4244  O   LEU B 329     7567   7374   6125  -3773   2916  -1566       O  
ATOM   4245  CB  LEU B 329      -7.967   7.048  30.056  1.00 54.02           C  
ANISOU 4245  CB  LEU B 329     7379   7467   5680  -3472   2912  -1336       C  
ATOM   4246  CG  LEU B 329      -8.248   5.582  29.718  1.00 51.86           C  
ANISOU 4246  CG  LEU B 329     6922   7416   5368  -3229   2804  -1355       C  
ATOM   4247  CD1 LEU B 329      -7.354   5.110  28.583  1.00 53.49           C  
ANISOU 4247  CD1 LEU B 329     7040   7781   5503  -3280   2872  -1391       C  
ATOM   4248  CD2 LEU B 329      -8.062   4.708  30.947  1.00 49.81           C  
ANISOU 4248  CD2 LEU B 329     6352   7329   5245  -3083   2669  -1528       C  
ATOM   4249  N   MET B 330      -8.483  10.084  31.045  1.00 63.81           N  
ANISOU 4249  N   MET B 330     9200   8038   7007  -3820   3063  -1200       N  
ATOM   4250  CA  MET B 330      -7.960  11.366  31.501  1.00 65.32           C  
ANISOU 4250  CA  MET B 330     9532   8016   7270  -4052   3144  -1257       C  
ATOM   4251  C   MET B 330      -8.698  11.822  32.756  1.00 65.62           C  
ANISOU 4251  C   MET B 330     9672   7848   7415  -3974   3057  -1287       C  
ATOM   4252  O   MET B 330      -8.147  12.535  33.594  1.00 66.30           O  
ANISOU 4252  O   MET B 330     9751   7844   7595  -4164   3088  -1437       O  
ATOM   4253  CB  MET B 330      -8.097  12.416  30.397  1.00 67.54           C  
ANISOU 4253  CB  MET B 330    10175   8041   7446  -4160   3270  -1053       C  
ATOM   4254  CG  MET B 330      -7.516  13.778  30.742  1.00 70.20           C  
ANISOU 4254  CG  MET B 330    10678   8144   7850  -4399   3365  -1104       C  
ATOM   4255  SD  MET B 330      -7.788  14.994  29.439  1.00 74.32           S  
ANISOU 4255  SD  MET B 330    11647   8346   8244  -4488   3506   -836       S  
ATOM   4256  CE  MET B 330      -6.997  14.184  28.051  1.00 75.63           C  
ANISOU 4256  CE  MET B 330    11635   8825   8275  -4538   3583   -824       C  
ATOM   4257  N   PHE B 331      -9.951  11.396  32.877  1.00 67.85           N  
ANISOU 4257  N   PHE B 331    10036   8066   7680  -3622   2895  -1156       N  
ATOM   4258  CA  PHE B 331     -10.795  11.772  34.006  1.00 68.57           C  
ANISOU 4258  CA  PHE B 331    10228   7964   7861  -3428   2767  -1166       C  
ATOM   4259  C   PHE B 331     -10.286  11.204  35.329  1.00 67.63           C  
ANISOU 4259  C   PHE B 331     9809   8047   7840  -3405   2661  -1412       C  
ATOM   4260  O   PHE B 331     -10.484  11.804  36.386  1.00 67.88           O  
ANISOU 4260  O   PHE B 331     9926   7923   7943  -3392   2618  -1498       O  
ATOM   4261  CB  PHE B 331     -12.236  11.313  33.757  1.00 68.94           C  
ANISOU 4261  CB  PHE B 331    10374   7946   7874  -3056   2625   -968       C  
ATOM   4262  CG  PHE B 331     -13.149  11.498  34.936  1.00 69.15           C  
ANISOU 4262  CG  PHE B 331    10450   7827   7997  -2817   2502   -985       C  
ATOM   4263  CD1 PHE B 331     -13.718  12.732  35.201  1.00 70.47           C  
ANISOU 4263  CD1 PHE B 331    10935   7640   8201  -2806   2549   -901       C  
ATOM   4264  CD2 PHE B 331     -13.449  10.434  35.772  1.00 68.35           C  
ANISOU 4264  CD2 PHE B 331    10091   7934   7946  -2597   2352  -1083       C  
ATOM   4265  CE1 PHE B 331     -14.562  12.903  36.281  1.00 70.27           C  
ANISOU 4265  CE1 PHE B 331    10956   7484   8259  -2577   2459   -926       C  
ATOM   4266  CE2 PHE B 331     -14.290  10.601  36.855  1.00 69.13           C  
ANISOU 4266  CE2 PHE B 331    10241   7907   8119  -2382   2264  -1096       C  
ATOM   4267  CZ  PHE B 331     -14.848  11.837  37.110  1.00 69.59           C  
ANISOU 4267  CZ  PHE B 331    10604   7625   8211  -2370   2321  -1023       C  
ATOM   4268  N   VAL B 332      -9.625  10.053  35.268  1.00 68.63           N  
ANISOU 4268  N   VAL B 332     9600   8516   7961  -3391   2618  -1526       N  
ATOM   4269  CA  VAL B 332      -9.236   9.341  36.482  1.00 68.54           C  
ANISOU 4269  CA  VAL B 332     9298   8721   8025  -3309   2484  -1729       C  
ATOM   4270  C   VAL B 332      -7.719   9.291  36.709  1.00 68.92           C  
ANISOU 4270  C   VAL B 332     9075   8998   8116  -3602   2550  -1954       C  
ATOM   4271  O   VAL B 332      -7.258   9.295  37.852  1.00 69.34           O  
ANISOU 4271  O   VAL B 332     8980   9136   8233  -3638   2460  -2138       O  
ATOM   4272  CB  VAL B 332      -9.838   7.910  36.506  1.00 67.00           C  
ANISOU 4272  CB  VAL B 332     8911   8733   7815  -2983   2336  -1686       C  
ATOM   4273  CG1 VAL B 332      -9.274   7.063  35.373  1.00 65.93           C  
ANISOU 4273  CG1 VAL B 332     8606   8829   7618  -3031   2402  -1672       C  
ATOM   4274  CG2 VAL B 332      -9.605   7.243  37.853  1.00 66.18           C  
ANISOU 4274  CG2 VAL B 332     8570   8801   7776  -2858   2189  -1858       C  
ATOM   4275  N   TYR B 333      -6.945   9.266  35.628  1.00 76.71           N  
ANISOU 4275  N   TYR B 333     9995  10090   9061  -3814   2706  -1940       N  
ATOM   4276  CA  TYR B 333      -5.495   9.113  35.741  1.00 76.97           C  
ANISOU 4276  CA  TYR B 333     9735  10372   9137  -4003   2732  -2137       C  
ATOM   4277  C   TYR B 333      -4.755  10.406  36.079  1.00 78.19           C  
ANISOU 4277  C   TYR B 333     9996  10380   9331  -4279   2800  -2231       C  
ATOM   4278  O   TYR B 333      -3.683  10.369  36.683  1.00 78.59           O  
ANISOU 4278  O   TYR B 333     9800  10623   9437  -4375   2748  -2420       O  
ATOM   4279  CB  TYR B 333      -4.911   8.475  34.478  1.00 75.27           C  
ANISOU 4279  CB  TYR B 333     9407  10339   8853  -3974   2796  -2086       C  
ATOM   4280  CG  TYR B 333      -4.848   6.967  34.538  1.00 73.55           C  
ANISOU 4280  CG  TYR B 333     8893  10410   8643  -3724   2674  -2143       C  
ATOM   4281  CD1 TYR B 333      -5.913   6.188  34.106  1.00 72.55           C  
ANISOU 4281  CD1 TYR B 333     8837  10273   8456  -3490   2632  -2002       C  
ATOM   4282  CD2 TYR B 333      -3.724   6.322  35.036  1.00 72.71           C  
ANISOU 4282  CD2 TYR B 333     8447  10575   8604  -3707   2592  -2332       C  
ATOM   4283  CE1 TYR B 333      -5.857   4.808  34.164  1.00 71.53           C  
ANISOU 4283  CE1 TYR B 333     8463  10376   8340  -3251   2514  -2054       C  
ATOM   4284  CE2 TYR B 333      -3.658   4.945  35.098  1.00 71.48           C  
ANISOU 4284  CE2 TYR B 333     8052  10646   8462  -3457   2474  -2373       C  
ATOM   4285  CZ  TYR B 333      -4.727   4.193  34.661  1.00 71.30           C  
ANISOU 4285  CZ  TYR B 333     8120  10586   8385  -3233   2436  -2236       C  
ATOM   4286  OH  TYR B 333      -4.663   2.821  34.723  1.00 70.59           O  
ANISOU 4286  OH  TYR B 333     7818  10688   8315  -2981   2314  -2274       O  
ATOM   4287  N   ILE B 334      -5.318  11.543  35.687  1.00 90.88           N  
ANISOU 4287  N   ILE B 334    11974  11645  10909  -4388   2910  -2090       N  
ATOM   4288  CA  ILE B 334      -4.706  12.830  36.001  1.00 92.55           C  
ANISOU 4288  CA  ILE B 334    12327  11679  11158  -4638   2980  -2166       C  
ATOM   4289  C   ILE B 334      -4.855  13.140  37.489  1.00 93.11           C  
ANISOU 4289  C   ILE B 334    12390  11682  11306  -4636   2856  -2329       C  
ATOM   4290  O   ILE B 334      -5.962  13.123  38.026  1.00 93.13           O  
ANISOU 4290  O   ILE B 334    12564  11501  11318  -4484   2794  -2276       O  
ATOM   4291  CB  ILE B 334      -5.314  13.972  35.165  1.00 91.89           C  
ANISOU 4291  CB  ILE B 334    12674  11220  11019  -4721   3126  -1955       C  
ATOM   4292  CG1 ILE B 334      -5.145  13.686  33.672  1.00 92.35           C  
ANISOU 4292  CG1 ILE B 334    12762  11351  10974  -4719   3236  -1792       C  
ATOM   4293  CG2 ILE B 334      -4.669  15.300  35.528  1.00 95.67           C  
ANISOU 4293  CG2 ILE B 334    13297  11509  11544  -4975   3200  -2039       C  
ATOM   4294  CD1 ILE B 334      -3.705  13.531  33.237  1.00 94.64           C  
ANISOU 4294  CD1 ILE B 334    12783  11905  11270  -4890   3302  -1920       C  
ATOM   4295  N   SER B 335      -3.734  13.417  38.147  1.00123.66           N  
ANISOU 4295  N   SER B 335    16061  15700  15223  -4799   2817  -2527       N  
ATOM   4296  CA  SER B 335      -3.720  13.655  39.588  1.00124.15           C  
ANISOU 4296  CA  SER B 335    16088  15750  15335  -4794   2676  -2703       C  
ATOM   4297  C   SER B 335      -4.418  14.957  39.969  1.00125.85           C  
ANISOU 4297  C   SER B 335    16712  15548  15556  -4862   2727  -2658       C  
ATOM   4298  O   SER B 335      -4.525  15.876  39.158  1.00127.65           O  
ANISOU 4298  O   SER B 335    17216  15518  15768  -4985   2882  -2521       O  
ATOM   4299  CB  SER B 335      -2.283  13.660  40.113  1.00118.16           C  
ANISOU 4299  CB  SER B 335    15014  15262  14619  -4957   2617  -2909       C  
ATOM   4300  OG  SER B 335      -1.639  12.425  39.854  1.00117.03           O  
ANISOU 4300  OG  SER B 335    14495  15494  14479  -4849   2556  -2957       O  
ATOM   4301  N   ASP B 336      -4.886  15.025  41.213  1.00105.46           N  
ANISOU 4301  N   ASP B 336    14180  12899  12989  -4758   2594  -2772       N  
ATOM   4302  CA  ASP B 336      -5.557  16.215  41.726  1.00106.71           C  
ANISOU 4302  CA  ASP B 336    14723  12665  13155  -4776   2628  -2755       C  
ATOM   4303  C   ASP B 336      -4.605  17.404  41.769  1.00110.66           C  
ANISOU 4303  C   ASP B 336    15299  13064  13683  -5068   2710  -2836       C  
ATOM   4304  O   ASP B 336      -5.001  18.541  41.514  1.00112.25           O  
ANISOU 4304  O   ASP B 336    15855  12904  13890  -5143   2826  -2743       O  
ATOM   4305  CB  ASP B 336      -6.118  15.950  43.124  1.00101.94           C  
ANISOU 4305  CB  ASP B 336    14124  12065  12543  -4587   2459  -2892       C  
ATOM   4306  CG  ASP B 336      -7.122  14.816  43.144  1.00 98.50           C  
ANISOU 4306  CG  ASP B 336    13637  11702  12084  -4295   2381  -2821       C  
ATOM   4307  OD1 ASP B 336      -7.035  13.929  42.270  1.00 97.65           O  
ANISOU 4307  OD1 ASP B 336    13340  11787  11973  -4249   2404  -2721       O  
ATOM   4308  OD2 ASP B 336      -7.997  14.811  44.036  1.00 97.55           O  
ANISOU 4308  OD2 ASP B 336    13664  11458  11941  -4080   2297  -2856       O  
ATOM   4309  N   GLU B 337      -3.346  17.129  42.092  1.00150.99           N  
ANISOU 4309  N   GLU B 337    20068  18487  18814  -5224   2644  -3008       N  
ATOM   4310  CA  GLU B 337      -2.316  18.160  42.140  1.00154.79           C  
ANISOU 4310  CA  GLU B 337    20563  18914  19336  -5525   2711  -3106       C  
ATOM   4311  C   GLU B 337      -1.914  18.589  40.733  1.00156.37           C  
ANISOU 4311  C   GLU B 337    20845  19033  19535  -5697   2916  -2957       C  
ATOM   4312  O   GLU B 337      -1.187  19.566  40.554  1.00160.28           O  
ANISOU 4312  O   GLU B 337    21421  19413  20065  -5959   3014  -2995       O  
ATOM   4313  CB  GLU B 337      -1.091  17.648  42.900  1.00148.46           C  
ANISOU 4313  CB  GLU B 337    19346  18496  18566  -5617   2565  -3325       C  
ATOM   4314  CG  GLU B 337      -0.516  16.355  42.341  1.00146.69           C  
ANISOU 4314  CG  GLU B 337    18733  18662  18340  -5526   2536  -3317       C  
ATOM   4315  CD  GLU B 337       0.665  15.843  43.142  1.00148.13           C  
ANISOU 4315  CD  GLU B 337    18510  19213  18561  -5576   2375  -3523       C  
ATOM   4316  OE1 GLU B 337       1.103  16.547  44.076  1.00150.78           O  
ANISOU 4316  OE1 GLU B 337    18862  19506  18920  -5719   2290  -3673       O  
ATOM   4317  OE2 GLU B 337       1.154  14.735  42.838  1.00146.83           O  
ANISOU 4317  OE2 GLU B 337    18014  19373  18401  -5462   2328  -3533       O  
ATOM   4318  N   GLN B 338      -2.396  17.852  39.738  1.00133.03           N  
ANISOU 4318  N   GLN B 338    17876  16137  16533  -5550   2976  -2787       N  
ATOM   4319  CA  GLN B 338      -2.063  18.121  38.347  1.00134.49           C  
ANISOU 4319  CA  GLN B 338    18135  16277  16688  -5677   3159  -2634       C  
ATOM   4320  C   GLN B 338      -3.273  18.676  37.598  1.00133.73           C  
ANISOU 4320  C   GLN B 338    18472  15802  16539  -5572   3266  -2385       C  
ATOM   4321  O   GLN B 338      -3.144  19.207  36.495  1.00135.29           O  
ANISOU 4321  O   GLN B 338    18844  15865  16698  -5685   3423  -2234       O  
ATOM   4322  CB  GLN B 338      -1.555  16.844  37.675  1.00126.45           C  
ANISOU 4322  CB  GLN B 338    16766  15636  15643  -5589   3145  -2628       C  
ATOM   4323  CG  GLN B 338      -0.705  17.074  36.438  1.00129.12           C  
ANISOU 4323  CG  GLN B 338    17053  16045  15963  -5779   3315  -2566       C  
ATOM   4324  CD  GLN B 338      -0.003  15.811  35.977  1.00127.96           C  
ANISOU 4324  CD  GLN B 338    16507  16303  15810  -5695   3281  -2626       C  
ATOM   4325  OE1 GLN B 338      -0.210  14.734  36.536  1.00125.03           O  
ANISOU 4325  OE1 GLN B 338    15907  16154  15448  -5483   3127  -2698       O  
ATOM   4326  NE2 GLN B 338       0.837  15.939  34.956  1.00130.47           N  
ANISOU 4326  NE2 GLN B 338    16749  16709  16115  -5853   3428  -2595       N  
ATOM   4327  N   TRP B 339      -4.449  18.553  38.208  1.00103.19           N  
ANISOU 4327  N   TRP B 339    14776  11763  12667  -5342   3178  -2337       N  
ATOM   4328  CA  TRP B 339      -5.682  19.066  37.617  1.00103.14           C  
ANISOU 4328  CA  TRP B 339    15176  11390  12623  -5195   3253  -2096       C  
ATOM   4329  C   TRP B 339      -5.799  20.579  37.766  1.00107.23           C  
ANISOU 4329  C   TRP B 339    16064  11510  13167  -5321   3345  -2064       C  
ATOM   4330  O   TRP B 339      -6.201  21.076  38.817  1.00109.11           O  
ANISOU 4330  O   TRP B 339    16442  11565  13450  -5260   3278  -2160       O  
ATOM   4331  CB  TRP B 339      -6.904  18.398  38.252  1.00 97.86           C  
ANISOU 4331  CB  TRP B 339    14553  10669  11959  -4892   3130  -2064       C  
ATOM   4332  CG  TRP B 339      -7.415  17.205  37.503  1.00 93.95           C  
ANISOU 4332  CG  TRP B 339    13920  10360  11414  -4709   3106  -1925       C  
ATOM   4333  CD1 TRP B 339      -7.277  15.895  37.856  1.00 90.29           C  
ANISOU 4333  CD1 TRP B 339    13103  10245  10957  -4602   2989  -2030       C  
ATOM   4334  CD2 TRP B 339      -8.152  17.214  36.274  1.00 92.87           C  
ANISOU 4334  CD2 TRP B 339    14004  10076  11207  -4602   3191  -1651       C  
ATOM   4335  NE1 TRP B 339      -7.882  15.087  36.923  1.00 88.51           N  
ANISOU 4335  NE1 TRP B 339    12860  10094  10676  -4448   3008  -1845       N  
ATOM   4336  CE2 TRP B 339      -8.425  15.873  35.941  1.00 89.88           C  
ANISOU 4336  CE2 TRP B 339    13382   9974  10792  -4445   3126  -1609       C  
ATOM   4337  CE3 TRP B 339      -8.606  18.226  35.423  1.00 95.14           C  
ANISOU 4337  CE3 TRP B 339    14671  10029  11449  -4611   3306  -1430       C  
ATOM   4338  CZ2 TRP B 339      -9.131  15.517  34.794  1.00 90.12           C  
ANISOU 4338  CZ2 TRP B 339    13537   9970  10732  -4305   3167  -1359       C  
ATOM   4339  CZ3 TRP B 339      -9.307  17.870  34.284  1.00 93.50           C  
ANISOU 4339  CZ3 TRP B 339    14587   9788  11149  -4460   3335  -1175       C  
ATOM   4340  CH2 TRP B 339      -9.563  16.528  33.980  1.00 90.85           C  
ANISOU 4340  CH2 TRP B 339    14004   9744  10768  -4314   3264  -1144       C  
ATOM   4341  N   THR B 340      -5.453  21.308  36.710  1.00148.21           N  
ANISOU 4341  N   THR B 340    21421  16565  18327  -5488   3499  -1932       N  
ATOM   4342  CA  THR B 340      -5.614  22.757  36.702  1.00151.84           C  
ANISOU 4342  CA  THR B 340    22260  16622  18810  -5597   3599  -1869       C  
ATOM   4343  C   THR B 340      -6.959  23.133  36.087  1.00151.64           C  
ANISOU 4343  C   THR B 340    22627  16248  18740  -5349   3637  -1592       C  
ATOM   4344  O   THR B 340      -7.733  22.261  35.692  1.00149.10           O  
ANISOU 4344  O   THR B 340    22269  16011  18369  -5113   3581  -1458       O  
ATOM   4345  CB  THR B 340      -4.479  23.453  35.927  1.00153.81           C  
ANISOU 4345  CB  THR B 340    22503  16881  19057  -5920   3752  -1868       C  
ATOM   4346  OG1 THR B 340      -4.471  22.995  34.569  1.00152.95           O  
ANISOU 4346  OG1 THR B 340    22387  16870  18858  -5893   3842  -1672       O  
ATOM   4347  CG2 THR B 340      -3.132  23.150  36.567  1.00154.37           C  
ANISOU 4347  CG2 THR B 340    22175  17290  19189  -6155   3706  -2139       C  
ATOM   4348  N   THR B 341      -7.235  24.431  36.010  1.00123.39           N  
ANISOU 4348  N   THR B 341    19419  12281  15184  -5394   3724  -1506       N  
ATOM   4349  CA  THR B 341      -8.491  24.916  35.444  1.00123.21           C  
ANISOU 4349  CA  THR B 341    19779  11907  15127  -5137   3749  -1235       C  
ATOM   4350  C   THR B 341      -8.508  24.769  33.924  1.00123.33           C  
ANISOU 4350  C   THR B 341    19872  11951  15036  -5134   3835   -981       C  
ATOM   4351  O   THR B 341      -9.555  24.497  33.320  1.00121.34           O  
ANISOU 4351  O   THR B 341    19773  11606  14725  -4860   3794   -751       O  
ATOM   4352  CB  THR B 341      -8.743  26.388  35.816  1.00123.69           C  
ANISOU 4352  CB  THR B 341    20213  11538  15246  -5174   3817  -1221       C  
ATOM   4353  OG1 THR B 341      -7.616  27.180  35.421  1.00127.60           O  
ANISOU 4353  OG1 THR B 341    20716  12014  15751  -5532   3942  -1289       O  
ATOM   4354  CG2 THR B 341      -8.950  26.528  37.317  1.00122.99           C  
ANISOU 4354  CG2 THR B 341    20106  11384  15239  -5091   3718  -1440       C  
ATOM   4355  N   ALA B 342      -7.341  24.955  33.315  1.00112.71           N  
ANISOU 4355  N   ALA B 342    18419  10744  13664  -5434   3948  -1023       N  
ATOM   4356  CA  ALA B 342      -7.186  24.799  31.875  1.00113.79           C  
ANISOU 4356  CA  ALA B 342    18609  10944  13683  -5464   4041   -811       C  
ATOM   4357  C   ALA B 342      -7.582  23.391  31.452  1.00109.47           C  
ANISOU 4357  C   ALA B 342    17829  10708  13058  -5263   3947   -750       C  
ATOM   4358  O   ALA B 342      -8.418  23.214  30.569  1.00107.25           O  
ANISOU 4358  O   ALA B 342    17728  10347  12678  -5059   3933   -500       O  
ATOM   4359  CB  ALA B 342      -5.756  25.097  31.459  1.00115.07           C  
ANISOU 4359  CB  ALA B 342    18619  11258  13846  -5828   4179   -920       C  
ATOM   4360  N   LEU B 343      -6.988  22.395  32.103  1.00122.47           N  
ANISOU 4360  N   LEU B 343    19074  12710  14748  -5312   3872   -978       N  
ATOM   4361  CA  LEU B 343      -7.293  20.995  31.824  1.00118.28           C  
ANISOU 4361  CA  LEU B 343    18288  12493  14160  -5132   3780   -955       C  
ATOM   4362  C   LEU B 343      -8.740  20.655  32.170  1.00115.44           C  
ANISOU 4362  C   LEU B 343    18079  11981  13802  -4797   3658   -823       C  
ATOM   4363  O   LEU B 343      -9.299  19.694  31.649  1.00113.61           O  
ANISOU 4363  O   LEU B 343    17764  11906  13496  -4612   3597   -705       O  
ATOM   4364  CB  LEU B 343      -6.344  20.068  32.590  1.00114.09           C  
ANISOU 4364  CB  LEU B 343    17299  12353  13696  -5236   3712  -1239       C  
ATOM   4365  CG  LEU B 343      -4.965  19.768  31.991  1.00115.85           C  
ANISOU 4365  CG  LEU B 343    17237  12883  13899  -5472   3802  -1347       C  
ATOM   4366  CD1 LEU B 343      -4.078  21.005  31.958  1.00120.55           C  
ANISOU 4366  CD1 LEU B 343    17953  13315  14536  -5777   3940  -1401       C  
ATOM   4367  CD2 LEU B 343      -4.289  18.642  32.760  1.00113.71           C  
ANISOU 4367  CD2 LEU B 343    16504  13009  13691  -5466   3690  -1593       C  
ATOM   4368  N   PHE B 344      -9.336  21.450  33.053  1.00 91.70           N  
ANISOU 4368  N   PHE B 344    15291   8668  10882  -4716   3627   -848       N  
ATOM   4369  CA  PHE B 344     -10.719  21.258  33.478  1.00 88.90           C  
ANISOU 4369  CA  PHE B 344    15090   8132  10553  -4386   3522   -734       C  
ATOM   4370  C   PHE B 344     -11.680  21.636  32.350  1.00 90.13           C  
ANISOU 4370  C   PHE B 344    15572   8052  10618  -4184   3539   -400       C  
ATOM   4371  O   PHE B 344     -12.435  20.793  31.834  1.00 88.56           O  
ANISOU 4371  O   PHE B 344    15336   7960  10353  -3964   3462   -241       O  
ATOM   4372  CB  PHE B 344     -10.991  22.113  34.719  1.00 90.49           C  
ANISOU 4372  CB  PHE B 344    15446   8064  10870  -4356   3500   -872       C  
ATOM   4373  CG  PHE B 344     -12.266  21.773  35.434  1.00 88.55           C  
ANISOU 4373  CG  PHE B 344    15278   7686  10679  -4019   3391   -831       C  
ATOM   4374  CD1 PHE B 344     -13.459  22.382  35.082  1.00 89.23           C  
ANISOU 4374  CD1 PHE B 344    15702   7433  10765  -3743   3387   -588       C  
ATOM   4375  CD2 PHE B 344     -12.268  20.860  36.475  1.00 85.44           C  
ANISOU 4375  CD2 PHE B 344    14612   7511  10340  -3961   3288  -1037       C  
ATOM   4376  CE1 PHE B 344     -14.631  22.076  35.746  1.00 86.64           C  
ANISOU 4376  CE1 PHE B 344    15425   6989  10502  -3409   3294   -553       C  
ATOM   4377  CE2 PHE B 344     -13.436  20.550  37.142  1.00 83.06           C  
ANISOU 4377  CE2 PHE B 344    14382   7081  10093  -3646   3202  -1007       C  
ATOM   4378  CZ  PHE B 344     -14.619  21.157  36.776  1.00 83.97           C  
ANISOU 4378  CZ  PHE B 344    14823   6861  10219  -3366   3211   -765       C  
ATOM   4379  N   ASP B 345     -11.646  22.908  31.964  1.00110.55           N  
ANISOU 4379  N   ASP B 345    18479  10327  13199  -4255   3632   -290       N  
ATOM   4380  CA  ASP B 345     -12.500  23.384  30.880  1.00112.02           C  
ANISOU 4380  CA  ASP B 345    18985  10284  13293  -4062   3637     33       C  
ATOM   4381  C   ASP B 345     -12.200  22.641  29.580  1.00111.66           C  
ANISOU 4381  C   ASP B 345    18835  10503  13087  -4109   3654    171       C  
ATOM   4382  O   ASP B 345     -13.114  22.296  28.822  1.00111.24           O  
ANISOU 4382  O   ASP B 345    18893  10436  12936  -3862   3574    410       O  
ATOM   4383  CB  ASP B 345     -12.352  24.894  30.693  1.00113.92           C  
ANISOU 4383  CB  ASP B 345    19572  10155  13557  -4162   3744    110       C  
ATOM   4384  CG  ASP B 345     -12.891  25.680  31.874  1.00115.18           C  
ANISOU 4384  CG  ASP B 345    19894  10012  13857  -4037   3716     15       C  
ATOM   4385  OD1 ASP B 345     -14.102  25.984  31.884  1.00116.15           O  
ANISOU 4385  OD1 ASP B 345    20238   9893  14002  -3704   3644    196       O  
ATOM   4386  OD2 ASP B 345     -12.105  25.990  32.793  1.00115.61           O  
ANISOU 4386  OD2 ASP B 345    19846  10084  13997  -4259   3759   -245       O  
ATOM   4387  N   PHE B 346     -10.917  22.382  29.336  1.00112.04           N  
ANISOU 4387  N   PHE B 346    18659  10805  13107  -4415   3752     14       N  
ATOM   4388  CA  PHE B 346     -10.506  21.584  28.187  1.00111.11           C  
ANISOU 4388  CA  PHE B 346    18396  10979  12841  -4467   3780     93       C  
ATOM   4389  C   PHE B 346     -11.123  20.194  28.252  1.00106.47           C  
ANISOU 4389  C   PHE B 346    17577  10661  12215  -4244   3642     98       C  
ATOM   4390  O   PHE B 346     -11.527  19.646  27.230  1.00104.39           O  
ANISOU 4390  O   PHE B 346    17349  10511  11805  -4121   3607    278       O  
ATOM   4391  CB  PHE B 346      -8.982  21.477  28.103  1.00110.98           C  
ANISOU 4391  CB  PHE B 346    18118  11213  12837  -4808   3904   -121       C  
ATOM   4392  CG  PHE B 346      -8.500  20.445  27.124  1.00109.91           C  
ANISOU 4392  CG  PHE B 346    17756  11431  12573  -4836   3925   -104       C  
ATOM   4393  CD1 PHE B 346      -8.514  20.702  25.763  1.00111.68           C  
ANISOU 4393  CD1 PHE B 346    18185  11616  12635  -4852   4006    114       C  
ATOM   4394  CD2 PHE B 346      -8.029  19.218  27.564  1.00106.59           C  
ANISOU 4394  CD2 PHE B 346    16927  11383  12191  -4835   3862   -309       C  
ATOM   4395  CE1 PHE B 346      -8.072  19.754  24.860  1.00110.42           C  
ANISOU 4395  CE1 PHE B 346    17830  11776  12349  -4869   4031    115       C  
ATOM   4396  CE2 PHE B 346      -7.586  18.267  26.667  1.00105.70           C  
ANISOU 4396  CE2 PHE B 346    16612  11585  11966  -4839   3883   -306       C  
ATOM   4397  CZ  PHE B 346      -7.607  18.535  25.313  1.00107.50           C  
ANISOU 4397  CZ  PHE B 346    17052  11766  12028  -4859   3971    -99       C  
ATOM   4398  N   TYR B 347     -11.193  19.629  29.455  1.00 75.88           N  
ANISOU 4398  N   TYR B 347    13473   6890   8467  -4197   3563   -103       N  
ATOM   4399  CA  TYR B 347     -11.831  18.332  29.646  1.00 71.92           C  
ANISOU 4399  CA  TYR B 347    12757   6620   7950  -3985   3436   -102       C  
ATOM   4400  C   TYR B 347     -13.296  18.402  29.247  1.00 71.24           C  
ANISOU 4400  C   TYR B 347    12945   6317   7805  -3663   3340    182       C  
ATOM   4401  O   TYR B 347     -13.818  17.478  28.624  1.00 69.37           O  
ANISOU 4401  O   TYR B 347    12636   6264   7458  -3506   3261    305       O  
ATOM   4402  CB  TYR B 347     -11.709  17.855  31.098  1.00 69.54           C  
ANISOU 4402  CB  TYR B 347    12202   6419   7802  -3985   3371   -357       C  
ATOM   4403  CG  TYR B 347     -12.466  16.577  31.393  1.00 65.10           C  
ANISOU 4403  CG  TYR B 347    11408   6088   7240  -3703   3209   -357       C  
ATOM   4404  CD1 TYR B 347     -11.870  15.337  31.207  1.00 62.92           C  
ANISOU 4404  CD1 TYR B 347    10762   6223   6924  -3728   3169   -482       C  
ATOM   4405  CD2 TYR B 347     -13.776  16.612  31.858  1.00 62.63           C  
ANISOU 4405  CD2 TYR B 347    11197   5624   6976  -3331   3050   -247       C  
ATOM   4406  CE1 TYR B 347     -12.557  14.169  31.473  1.00 58.46           C  
ANISOU 4406  CE1 TYR B 347     9960   5889   6364  -3408   2974   -494       C  
ATOM   4407  CE2 TYR B 347     -14.469  15.450  32.122  1.00 58.13           C  
ANISOU 4407  CE2 TYR B 347    10368   5303   6415  -3022   2860   -258       C  
ATOM   4408  CZ  TYR B 347     -13.856  14.231  31.929  1.00 56.06           C  
ANISOU 4408  CZ  TYR B 347     9764   5427   6110  -3069   2822   -381       C  
ATOM   4409  OH  TYR B 347     -14.544  13.071  32.194  1.00 51.93           O  
ANISOU 4409  OH  TYR B 347     9002   5126   5601  -2774   2640   -390       O  
ATOM   4410  N   HIS B 348     -13.963  19.494  29.609  1.00 81.30           N  
ANISOU 4410  N   HIS B 348    14527   7210   9154  -3550   3336    281       N  
ATOM   4411  CA  HIS B 348     -15.382  19.631  29.269  1.00 81.24           C  
ANISOU 4411  CA  HIS B 348    14765   6990   9114  -3203   3226    555       C  
ATOM   4412  C   HIS B 348     -15.651  19.819  27.767  1.00 83.09           C  
ANISOU 4412  C   HIS B 348    15201   7212   9157  -3140   3214    834       C  
ATOM   4413  O   HIS B 348     -16.564  19.195  27.207  1.00 82.24           O  
ANISOU 4413  O   HIS B 348    15113   7182   8951  -2894   3085   1022       O  
ATOM   4414  CB  HIS B 348     -16.044  20.730  30.102  1.00 84.06           C  
ANISOU 4414  CB  HIS B 348    15373   6950   9616  -3053   3219    572       C  
ATOM   4415  CG  HIS B 348     -16.305  20.329  31.521  1.00 82.27           C  
ANISOU 4415  CG  HIS B 348    14962   6749   9548  -2950   3158    359       C  
ATOM   4416  ND1 HIS B 348     -15.297  20.176  32.449  1.00 81.59           N  
ANISOU 4416  ND1 HIS B 348    14649   6812   9541  -3209   3215     53       N  
ATOM   4417  CD2 HIS B 348     -17.458  20.032  32.166  1.00 81.57           C  
ANISOU 4417  CD2 HIS B 348    14804   6641   9547  -2557   2995    385       C  
ATOM   4418  CE1 HIS B 348     -15.819  19.811  33.607  1.00 80.00           C  
ANISOU 4418  CE1 HIS B 348    14277   6670   9449  -2979   3091    -94       C  
ATOM   4419  NE2 HIS B 348     -17.128  19.717  33.462  1.00 80.23           N  
ANISOU 4419  NE2 HIS B 348    14396   6598   9491  -2588   2970    102       N  
ATOM   4420  N   TYR B 349     -14.862  20.666  27.111  1.00 78.07           N  
ANISOU 4420  N   TYR B 349    14714   6488   8460  -3365   3342    859       N  
ATOM   4421  CA  TYR B 349     -14.999  20.834  25.665  1.00 80.25           C  
ANISOU 4421  CA  TYR B 349    15180   6771   8539  -3336   3344   1106       C  
ATOM   4422  C   TYR B 349     -14.678  19.527  24.939  1.00 78.11           C  
ANISOU 4422  C   TYR B 349    14659   6906   8116  -3374   3312   1079       C  
ATOM   4423  O   TYR B 349     -15.364  19.138  23.986  1.00 78.08           O  
ANISOU 4423  O   TYR B 349    14752   6970   7944  -3194   3210   1292       O  
ATOM   4424  CB  TYR B 349     -14.102  21.963  25.152  1.00 84.48           C  
ANISOU 4424  CB  TYR B 349    15904   7147   9048  -3605   3516   1115       C  
ATOM   4425  CG  TYR B 349     -14.535  23.343  25.594  1.00 87.34           C  
ANISOU 4425  CG  TYR B 349    16582   7081   9524  -3537   3542   1195       C  
ATOM   4426  CD1 TYR B 349     -15.738  23.886  25.161  1.00 88.74           C  
ANISOU 4426  CD1 TYR B 349    17054   7002   9662  -3226   3433   1477       C  
ATOM   4427  CD2 TYR B 349     -13.737  24.108  26.434  1.00 88.94           C  
ANISOU 4427  CD2 TYR B 349    16780   7144   9870  -3776   3666    984       C  
ATOM   4428  CE1 TYR B 349     -16.138  25.148  25.559  1.00 91.61           C  
ANISOU 4428  CE1 TYR B 349    17698   6973  10136  -3142   3460   1545       C  
ATOM   4429  CE2 TYR B 349     -14.128  25.370  26.838  1.00 91.80           C  
ANISOU 4429  CE2 TYR B 349    17438   7110  10330  -3713   3695   1045       C  
ATOM   4430  CZ  TYR B 349     -15.328  25.886  26.397  1.00 93.11           C  
ANISOU 4430  CZ  TYR B 349    17895   7019  10464  -3390   3598   1325       C  
ATOM   4431  OH  TYR B 349     -15.720  27.143  26.796  1.00 96.18           O  
ANISOU 4431  OH  TYR B 349    18571   7013  10959  -3306   3630   1381       O  
ATOM   4432  N   PHE B 350     -13.637  18.849  25.412  1.00 76.53           N  
ANISOU 4432  N   PHE B 350    14126   6980   7973  -3596   3388    808       N  
ATOM   4433  CA  PHE B 350     -13.242  17.553  24.876  1.00 74.47           C  
ANISOU 4433  CA  PHE B 350    13581   7116   7597  -3625   3367    731       C  
ATOM   4434  C   PHE B 350     -14.344  16.526  25.107  1.00 71.02           C  
ANISOU 4434  C   PHE B 350    13052   6795   7136  -3336   3189    800       C  
ATOM   4435  O   PHE B 350     -14.476  15.564  24.352  1.00 69.87           O  
ANISOU 4435  O   PHE B 350    12805   6906   6839  -3264   3127    846       O  
ATOM   4436  CB  PHE B 350     -11.932  17.092  25.519  1.00 73.61           C  
ANISOU 4436  CB  PHE B 350    13110   7261   7599  -3879   3464    412       C  
ATOM   4437  CG  PHE B 350     -11.408  15.795  24.978  1.00 71.93           C  
ANISOU 4437  CG  PHE B 350    12590   7450   7290  -3902   3456    308       C  
ATOM   4438  CD1 PHE B 350     -11.292  15.594  23.613  1.00 73.41           C  
ANISOU 4438  CD1 PHE B 350    12877   7742   7275  -3897   3485    451       C  
ATOM   4439  CD2 PHE B 350     -11.008  14.785  25.836  1.00 69.13           C  
ANISOU 4439  CD2 PHE B 350    11852   7369   7047  -3919   3418     59       C  
ATOM   4440  CE1 PHE B 350     -10.804  14.401  23.114  1.00 72.09           C  
ANISOU 4440  CE1 PHE B 350    12438   7930   7024  -3903   3482    339       C  
ATOM   4441  CE2 PHE B 350     -10.515  13.592  25.343  1.00 67.83           C  
ANISOU 4441  CE2 PHE B 350    11404   7560   6808  -3912   3407    -45       C  
ATOM   4442  CZ  PHE B 350     -10.414  13.400  23.982  1.00 69.29           C  
ANISOU 4442  CZ  PHE B 350    11699   7832   6798  -3903   3442     89       C  
ATOM   4443  N   TYR B 351     -15.133  16.738  26.156  1.00 71.22           N  
ANISOU 4443  N   TYR B 351    13119   6627   7314  -3171   3113    800       N  
ATOM   4444  CA  TYR B 351     -16.296  15.901  26.423  1.00 67.14           C  
ANISOU 4444  CA  TYR B 351    12440   6235   6834  -2788   2860    841       C  
ATOM   4445  C   TYR B 351     -17.355  16.139  25.357  1.00 68.64           C  
ANISOU 4445  C   TYR B 351    12909   6305   6866  -2560   2743   1157       C  
ATOM   4446  O   TYR B 351     -17.910  15.185  24.796  1.00 66.53           O  
ANISOU 4446  O   TYR B 351    12506   6278   6495  -2378   2577   1213       O  
ATOM   4447  CB  TYR B 351     -16.864  16.184  27.816  1.00 64.99           C  
ANISOU 4447  CB  TYR B 351    12096   5807   6791  -2602   2772    735       C  
ATOM   4448  CG  TYR B 351     -18.158  15.461  28.110  1.00 62.16           C  
ANISOU 4448  CG  TYR B 351    11581   5546   6493  -2199   2525    796       C  
ATOM   4449  CD1 TYR B 351     -18.153  14.158  28.587  1.00 58.89           C  
ANISOU 4449  CD1 TYR B 351    10780   5466   6129  -2107   2408    620       C  
ATOM   4450  CD2 TYR B 351     -19.386  16.082  27.915  1.00 63.38           C  
ANISOU 4450  CD2 TYR B 351    11967   5453   6661  -1911   2414   1034       C  
ATOM   4451  CE1 TYR B 351     -19.330  13.491  28.857  1.00 56.88           C  
ANISOU 4451  CE1 TYR B 351    10376   5296   5939  -1767   2198    675       C  
ATOM   4452  CE2 TYR B 351     -20.570  15.423  28.181  1.00 61.41           C  
ANISOU 4452  CE2 TYR B 351    11542   5307   6483  -1558   2196   1085       C  
ATOM   4453  CZ  TYR B 351     -20.535  14.128  28.653  1.00 58.15           C  
ANISOU 4453  CZ  TYR B 351    10747   5227   6122  -1501   2095    903       C  
ATOM   4454  OH  TYR B 351     -21.708  13.463  28.921  1.00 56.94           O  
ANISOU 4454  OH  TYR B 351    10412   5174   6048  -1177   1893    953       O  
ATOM   4455  N   MET B 352     -17.632  17.414  25.088  1.00 70.99           N  
ANISOU 4455  N   MET B 352    13603   6225   7145  -2571   2822   1361       N  
ATOM   4456  CA  MET B 352     -18.552  17.785  24.014  1.00 73.42           C  
ANISOU 4456  CA  MET B 352    14217   6392   7285  -2367   2716   1687       C  
ATOM   4457  C   MET B 352     -18.164  17.106  22.701  1.00 73.99           C  
ANISOU 4457  C   MET B 352    14258   6752   7100  -2463   2707   1746       C  
ATOM   4458  O   MET B 352     -18.991  16.450  22.060  1.00 73.12           O  
ANISOU 4458  O   MET B 352    14149   6782   6852  -2243   2521   1891       O  
ATOM   4459  CB  MET B 352     -18.582  19.303  23.822  1.00 77.38           C  
ANISOU 4459  CB  MET B 352    15047   6524   7828  -2378   2788   1822       C  
ATOM   4460  CG  MET B 352     -19.327  20.067  24.905  1.00 77.54           C  
ANISOU 4460  CG  MET B 352    15180   6214   8068  -2165   2746   1839       C  
ATOM   4461  SD  MET B 352     -19.330  21.844  24.591  1.00 82.59           S  
ANISOU 4461  SD  MET B 352    16206   6432   8743  -2183   2837   1987       S  
ATOM   4462  CE  MET B 352     -20.459  22.417  25.857  1.00 82.24           C  
ANISOU 4462  CE  MET B 352    16238   6069   8942  -1821   2736   2011       C  
ATOM   4463  N   LEU B 353     -16.898  17.254  22.320  1.00 88.09           N  
ANISOU 4463  N   LEU B 353    15987   8644   8839  -2775   2892   1610       N  
ATOM   4464  CA  LEU B 353     -16.385  16.656  21.088  1.00 89.01           C  
ANISOU 4464  CA  LEU B 353    16066   9029   8724  -2882   2921   1632       C  
ATOM   4465  C   LEU B 353     -16.507  15.130  21.081  1.00 86.16           C  
ANISOU 4465  C   LEU B 353    15413   9032   8291  -2813   2822   1512       C  
ATOM   4466  O   LEU B 353     -16.977  14.534  20.103  1.00 85.64           O  
ANISOU 4466  O   LEU B 353    15402   9124   8012  -2694   2702   1636       O  
ATOM   4467  CB  LEU B 353     -14.924  17.058  20.875  1.00 89.79           C  
ANISOU 4467  CB  LEU B 353    16098   9179   8837  -3227   3156   1467       C  
ATOM   4468  CG  LEU B 353     -14.210  16.448  19.668  1.00 90.73           C  
ANISOU 4468  CG  LEU B 353    16153   9577   8743  -3358   3230   1450       C  
ATOM   4469  CD1 LEU B 353     -14.802  16.974  18.368  1.00 94.03           C  
ANISOU 4469  CD1 LEU B 353    16922   9872   8930  -3254   3178   1748       C  
ATOM   4470  CD2 LEU B 353     -12.715  16.720  19.733  1.00 91.96           C  
ANISOU 4470  CD2 LEU B 353    16149   9815   8974  -3687   3461   1236       C  
ATOM   4471  N   SER B 354     -16.079  14.508  22.176  1.00 89.05           N  
ANISOU 4471  N   SER B 354    15472   9534   8830  -2889   2865   1261       N  
ATOM   4472  CA  SER B 354     -16.096  13.054  22.300  1.00 87.00           C  
ANISOU 4472  CA  SER B 354    14861   9634   8561  -2801   2755   1091       C  
ATOM   4473  C   SER B 354     -17.500  12.489  22.125  1.00 86.23           C  
ANISOU 4473  C   SER B 354    14734   9585   8444  -2430   2453   1219       C  
ATOM   4474  O   SER B 354     -17.723  11.612  21.286  1.00 85.71           O  
ANISOU 4474  O   SER B 354    14614   9748   8205  -2362   2351   1242       O  
ATOM   4475  CB  SER B 354     -15.521  12.623  23.650  1.00 85.20           C  
ANISOU 4475  CB  SER B 354    14271   9518   8585  -2857   2780    797       C  
ATOM   4476  OG  SER B 354     -14.190  13.085  23.808  1.00 85.36           O  
ANISOU 4476  OG  SER B 354    14265   9533   8636  -3207   3036    655       O  
ATOM   4477  N   ASN B 355     -18.446  12.993  22.912  1.00 67.14           N  
ANISOU 4477  N   ASN B 355    12350   6954   6207  -2196   2314   1294       N  
ATOM   4478  CA  ASN B 355     -19.827  12.537  22.796  1.00 66.07           C  
ANISOU 4478  CA  ASN B 355    12163   6857   6086  -1843   2029   1421       C  
ATOM   4479  C   ASN B 355     -20.426  12.864  21.430  1.00 68.83           C  
ANISOU 4479  C   ASN B 355    12827   7146   6180  -1756   1934   1708       C  
ATOM   4480  O   ASN B 355     -21.271  12.121  20.917  1.00 68.20           O  
ANISOU 4480  O   ASN B 355    12665   7228   6020  -1546   1700   1779       O  
ATOM   4481  CB  ASN B 355     -20.692  13.097  23.927  1.00 65.33           C  
ANISOU 4481  CB  ASN B 355    12043   6538   6244  -1612   1936   1444       C  
ATOM   4482  CG  ASN B 355     -20.389  12.451  25.264  1.00 64.01           C  
ANISOU 4482  CG  ASN B 355    11521   6500   6301  -1613   1946   1169       C  
ATOM   4483  OD1 ASN B 355     -19.275  11.984  25.503  1.00 63.43           O  
ANISOU 4483  OD1 ASN B 355    11278   6597   6228  -1848   2083    958       O  
ATOM   4484  ND2 ASN B 355     -21.385  12.411  26.141  1.00 65.10           N  
ANISOU 4484  ND2 ASN B 355    11542   6567   6628  -1340   1801   1174       N  
ATOM   4485  N   ALA B 356     -19.974  13.970  20.841  1.00 68.13           N  
ANISOU 4485  N   ALA B 356    13105   6824   5959  -1927   2110   1872       N  
ATOM   4486  CA  ALA B 356     -20.377  14.321  19.484  1.00 71.98           C  
ANISOU 4486  CA  ALA B 356    13931   7259   6160  -1880   2046   2152       C  
ATOM   4487  C   ALA B 356     -20.002  13.210  18.511  1.00 71.66           C  
ANISOU 4487  C   ALA B 356    13787   7569   5871  -1975   2023   2079       C  
ATOM   4488  O   ALA B 356     -20.824  12.789  17.699  1.00 72.09           O  
ANISOU 4488  O   ALA B 356    13903   7735   5752  -1788   1798   2218       O  
ATOM   4489  CB  ALA B 356     -19.753  15.642  19.057  1.00 76.53           C  
ANISOU 4489  CB  ALA B 356    14849   7556   6673  -2073   2260   2285       C  
ATOM   4490  N   LEU B 357     -18.765  12.730  18.605  1.00 71.16           N  
ANISOU 4490  N   LEU B 357    13559   7683   5795  -2261   2249   1849       N  
ATOM   4491  CA  LEU B 357     -18.323  11.616  17.766  1.00 70.98           C  
ANISOU 4491  CA  LEU B 357    13421   7995   5554  -2351   2259   1740       C  
ATOM   4492  C   LEU B 357     -19.088  10.329  18.087  1.00 66.50           C  
ANISOU 4492  C   LEU B 357    12517   7672   5080  -2109   1987   1604       C  
ATOM   4493  O   LEU B 357     -19.430   9.549  17.186  1.00 66.82           O  
ANISOU 4493  O   LEU B 357    12569   7914   4907  -2040   1850   1627       O  
ATOM   4494  CB  LEU B 357     -16.817  11.391  17.919  1.00 70.95           C  
ANISOU 4494  CB  LEU B 357    13201   8136   5619  -2645   2527   1479       C  
ATOM   4495  CG  LEU B 357     -15.923  12.548  17.470  1.00 74.43           C  
ANISOU 4495  CG  LEU B 357    13815   8407   6059  -2855   2738   1528       C  
ATOM   4496  CD1 LEU B 357     -14.454  12.191  17.630  1.00 74.25           C  
ANISOU 4496  CD1 LEU B 357    13515   8572   6123  -3115   2963   1252       C  
ATOM   4497  CD2 LEU B 357     -16.232  12.934  16.033  1.00 77.93           C  
ANISOU 4497  CD2 LEU B 357    14566   8820   6224  -2809   2692   1761       C  
ATOM   4498  N   VAL B 358     -19.351  10.119  19.375  1.00 62.64           N  
ANISOU 4498  N   VAL B 358    11744   7157   4901  -1992   1915   1460       N  
ATOM   4499  CA  VAL B 358     -20.109   8.957  19.832  1.00 58.47           C  
ANISOU 4499  CA  VAL B 358    10896   6819   4500  -1766   1673   1342       C  
ATOM   4500  C   VAL B 358     -21.470   8.879  19.145  1.00 59.02           C  
ANISOU 4500  C   VAL B 358    11086   6877   4460  -1504   1379   1560       C  
ATOM   4501  O   VAL B 358     -21.883   7.814  18.685  1.00 57.75           O  
ANISOU 4501  O   VAL B 358    10787   6943   4211  -1418   1205   1501       O  
ATOM   4502  CB  VAL B 358     -20.298   8.969  21.364  1.00 54.89           C  
ANISOU 4502  CB  VAL B 358    10184   6285   4386  -1664   1650   1206       C  
ATOM   4503  CG1 VAL B 358     -21.317   7.922  21.790  1.00 51.13           C  
ANISOU 4503  CG1 VAL B 358     9431   5956   4040  -1405   1388   1149       C  
ATOM   4504  CG2 VAL B 358     -18.968   8.739  22.062  1.00 54.08           C  
ANISOU 4504  CG2 VAL B 358     9885   6276   4387  -1905   1882    950       C  
ATOM   4505  N   TYR B 359     -22.157  10.014  19.065  1.00 62.65           N  
ANISOU 4505  N   TYR B 359    11804   7071   4929  -1376   1319   1807       N  
ATOM   4506  CA  TYR B 359     -23.430  10.071  18.354  1.00 64.24           C  
ANISOU 4506  CA  TYR B 359    12129   7260   5019  -1120   1030   2038       C  
ATOM   4507  C   TYR B 359     -23.217   9.992  16.843  1.00 67.37           C  
ANISOU 4507  C   TYR B 359    12803   7766   5028  -1223   1017   2167       C  
ATOM   4508  O   TYR B 359     -24.053   9.450  16.109  1.00 67.90           O  
ANISOU 4508  O   TYR B 359    12870   7981   4948  -1068    755   2249       O  
ATOM   4509  CB  TYR B 359     -24.195  11.341  18.727  1.00 66.00           C  
ANISOU 4509  CB  TYR B 359    12551   7154   5370   -929    977   2270       C  
ATOM   4510  CG  TYR B 359     -24.590  11.387  20.184  1.00 63.51           C  
ANISOU 4510  CG  TYR B 359    11972   6741   5417   -786    965   2149       C  
ATOM   4511  CD1 TYR B 359     -24.853  10.218  20.884  1.00 60.26           C  
ANISOU 4511  CD1 TYR B 359    11165   6554   5176   -704    853   1941       C  
ATOM   4512  CD2 TYR B 359     -24.691  12.594  20.863  1.00 64.62           C  
ANISOU 4512  CD2 TYR B 359    12277   6556   5718   -737   1078   2238       C  
ATOM   4513  CE1 TYR B 359     -25.211  10.247  22.214  1.00 58.20           C  
ANISOU 4513  CE1 TYR B 359    10680   6213   5219   -576    856   1836       C  
ATOM   4514  CE2 TYR B 359     -25.049  12.633  22.197  1.00 62.56           C  
ANISOU 4514  CE2 TYR B 359    11793   6212   5763   -605   1078   2116       C  
ATOM   4515  CZ  TYR B 359     -25.307  11.455  22.866  1.00 59.35           C  
ANISOU 4515  CZ  TYR B 359    10994   6050   5504   -525    969   1920       C  
ATOM   4516  OH  TYR B 359     -25.663  11.478  24.193  1.00 57.48           O  
ANISOU 4516  OH  TYR B 359    10551   5739   5549   -396    982   1805       O  
ATOM   4517  N   VAL B 360     -22.085  10.528  16.391  1.00 69.46           N  
ANISOU 4517  N   VAL B 360    13300   7965   5124  -1497   1304   2177       N  
ATOM   4518  CA  VAL B 360     -21.732  10.523  14.974  1.00 73.59           C  
ANISOU 4518  CA  VAL B 360    14121   8585   5254  -1630   1355   2295       C  
ATOM   4519  C   VAL B 360     -21.682   9.110  14.400  1.00 72.13           C  
ANISOU 4519  C   VAL B 360    13743   8748   4912  -1644   1246   2115       C  
ATOM   4520  O   VAL B 360     -22.218   8.867  13.324  1.00 74.61           O  
ANISOU 4520  O   VAL B 360    14239   9168   4941  -1567   1066   2246       O  
ATOM   4521  CB  VAL B 360     -20.395  11.264  14.704  1.00 76.34           C  
ANISOU 4521  CB  VAL B 360    14636   8837   5534  -1940   1718   2269       C  
ATOM   4522  CG1 VAL B 360     -19.699  10.712  13.467  1.00 78.10           C  
ANISOU 4522  CG1 VAL B 360    14873   9305   5496  -2083   1799   2186       C  
ATOM   4523  CG2 VAL B 360     -20.634  12.758  14.561  1.00 79.54           C  
ANISOU 4523  CG2 VAL B 360    15335   8907   5979  -1889   1749   2520       C  
ATOM   4524  N   SER B 361     -21.057   8.180  15.119  1.00103.77           N  
ANISOU 4524  N   SER B 361    17397  12928   9101  -1733   1342   1814       N  
ATOM   4525  CA  SER B 361     -20.987   6.793  14.648  1.00103.12           C  
ANISOU 4525  CA  SER B 361    17133  13152   8896  -1741   1252   1621       C  
ATOM   4526  C   SER B 361     -22.375   6.157  14.524  1.00104.23           C  
ANISOU 4526  C   SER B 361    17164  13378   9061  -1470    864   1677       C  
ATOM   4527  O   SER B 361     -22.716   5.550  13.495  1.00104.48           O  
ANISOU 4527  O   SER B 361    17294  13579   8822  -1445    707   1696       O  
ATOM   4528  CB  SER B 361     -20.109   5.951  15.577  1.00102.10           C  
ANISOU 4528  CB  SER B 361    16635  13160   8996  -1852   1418   1302       C  
ATOM   4529  OG  SER B 361     -20.702   5.820  16.857  1.00102.31           O  
ANISOU 4529  OG  SER B 361    16377  13123   9374  -1679   1279   1233       O  
ATOM   4530  N   ALA B 362     -23.168   6.309  15.582  1.00 75.62           N  
ANISOU 4530  N   ALA B 362    13333   9640   5761  -1276    717   1695       N  
ATOM   4531  CA  ALA B 362     -24.520   5.764  15.636  1.00 77.10           C  
ANISOU 4531  CA  ALA B 362    13364   9896   6036  -1021    363   1748       C  
ATOM   4532  C   ALA B 362     -25.385   6.301  14.502  1.00 78.90           C  
ANISOU 4532  C   ALA B 362    13896  10090   5994   -895    134   2028       C  
ATOM   4533  O   ALA B 362     -26.225   5.582  13.959  1.00 79.80           O  
ANISOU 4533  O   ALA B 362    13942  10369   6010   -777   -151   2036       O  
ATOM   4534  CB  ALA B 362     -25.160   6.070  16.982  1.00 80.86           C  
ANISOU 4534  CB  ALA B 362    13606  10220   6896   -842    303   1752       C  
ATOM   4535  N   ALA B 363     -25.177   7.566  14.148  1.00 68.73           N  
ANISOU 4535  N   ALA B 363    12948   8582   4584   -923    252   2261       N  
ATOM   4536  CA  ALA B 363     -25.892   8.159  13.023  1.00 73.47           C  
ANISOU 4536  CA  ALA B 363    13883   9136   4894   -804     50   2554       C  
ATOM   4537  C   ALA B 363     -25.273   7.738  11.690  1.00 76.81           C  
ANISOU 4537  C   ALA B 363    14551   9749   4884   -989    105   2537       C  
ATOM   4538  O   ALA B 363     -25.919   7.811  10.644  1.00 80.41           O  
ANISOU 4538  O   ALA B 363    15224  10274   5052   -889   -133   2714       O  
ATOM   4539  CB  ALA B 363     -25.914   9.674  13.146  1.00 76.46           C  
ANISOU 4539  CB  ALA B 363    14570   9184   5297   -760    165   2821       C  
ATOM   4540  N   ILE B 364     -24.022   7.291  11.740  1.00 76.51           N  
ANISOU 4540  N   ILE B 364    14469   9803   4797  -1252    419   2317       N  
ATOM   4541  CA  ILE B 364     -23.280   6.914  10.539  1.00 79.61           C  
ANISOU 4541  CA  ILE B 364    15058  10370   4819  -1439    546   2262       C  
ATOM   4542  C   ILE B 364     -23.698   5.544  10.020  1.00 79.05           C  
ANISOU 4542  C   ILE B 364    14861  10588   4586  -1399    317   2095       C  
ATOM   4543  O   ILE B 364     -23.837   5.352   8.811  1.00 81.99           O  
ANISOU 4543  O   ILE B 364    15380  11084   4689  -1379    207   2140       O  
ATOM   4544  CB  ILE B 364     -21.745   6.957  10.776  1.00 78.81           C  
ANISOU 4544  CB  ILE B 364    14864  10280   4799  -1709    968   2053       C  
ATOM   4545  CG1 ILE B 364     -21.184   8.324  10.383  1.00 81.84           C  
ANISOU 4545  CG1 ILE B 364    15487  10441   5168  -1804   1190   2234       C  
ATOM   4546  CG2 ILE B 364     -21.029   5.867   9.991  1.00 79.24           C  
ANISOU 4546  CG2 ILE B 364    14833  10608   4669  -1832   1058   1819       C  
ATOM   4547  CD1 ILE B 364     -19.682   8.434  10.537  1.00 81.62           C  
ANISOU 4547  CD1 ILE B 364    15351  10429   5232  -2071   1578   2039       C  
ATOM   4548  N   ASN B 365     -23.911   4.601  10.936  1.00 92.94           N  
ANISOU 4548  N   ASN B 365    16219  12446   6647  -1343    241   1854       N  
ATOM   4549  CA  ASN B 365     -24.284   3.229  10.559  1.00 93.28           C  
ANISOU 4549  CA  ASN B 365    16095  12740   6605  -1316     40   1652       C  
ATOM   4550  C   ASN B 365     -25.315   3.034   9.424  1.00 95.18           C  
ANISOU 4550  C   ASN B 365    16529  13096   6538  -1196   -320   1796       C  
ATOM   4551  O   ASN B 365     -25.090   2.217   8.532  1.00 95.65           O  
ANISOU 4551  O   ASN B 365    16682  13354   6305  -1290   -350   1662       O  
ATOM   4552  CB  ASN B 365     -24.676   2.406  11.793  1.00 93.36           C  
ANISOU 4552  CB  ASN B 365    15656  12785   7032  -1216    -56   1445       C  
ATOM   4553  CG  ASN B 365     -23.472   1.952  12.593  1.00 91.62           C  
ANISOU 4553  CG  ASN B 365    15224  12585   7000  -1376    272   1190       C  
ATOM   4554  OD1 ASN B 365     -22.380   1.782  12.049  1.00 92.22           O  
ANISOU 4554  OD1 ASN B 365    15427  12740   6870  -1571    536   1086       O  
ATOM   4555  ND2 ASN B 365     -23.665   1.751  13.892  1.00 88.84           N  
ANISOU 4555  ND2 ASN B 365    14544  12173   7039  -1289    259   1089       N  
ATOM   4556  N   PRO B 366     -26.441   3.775   9.447  1.00 79.36           N  
ANISOU 4556  N   PRO B 366    14585  10975   4593   -981   -599   2060       N  
ATOM   4557  CA  PRO B 366     -27.420   3.546   8.375  1.00 82.94           C  
ANISOU 4557  CA  PRO B 366    15197  11567   4752   -866   -970   2185       C  
ATOM   4558  C   PRO B 366     -27.027   4.124   7.012  1.00 87.51           C  
ANISOU 4558  C   PRO B 366    16106  12163   4979   -921   -878   2318       C  
ATOM   4559  O   PRO B 366     -27.369   3.529   5.990  1.00 89.84           O  
ANISOU 4559  O   PRO B 366    16448  12651   5036   -903  -1063   2264       O  
ATOM   4560  CB  PRO B 366     -28.677   4.247   8.898  1.00 82.80           C  
ANISOU 4560  CB  PRO B 366    15068  11409   4983   -591  -1263   2420       C  
ATOM   4561  CG  PRO B 366     -28.163   5.303   9.803  1.00 81.29           C  
ANISOU 4561  CG  PRO B 366    14892  10949   5045   -591   -980   2517       C  
ATOM   4562  CD  PRO B 366     -26.961   4.703  10.468  1.00 77.77           C  
ANISOU 4562  CD  PRO B 366    14264  10540   4744   -812   -629   2221       C  
ATOM   4563  N   ILE B 367     -26.333   5.258   6.992  1.00 87.18           N  
ANISOU 4563  N   ILE B 367    16260  11925   4941   -984   -593   2475       N  
ATOM   4564  CA  ILE B 367     -25.993   5.909   5.727  1.00 91.54           C  
ANISOU 4564  CA  ILE B 367    17102  12477   5202  -1024   -499   2621       C  
ATOM   4565  C   ILE B 367     -24.924   5.141   4.952  1.00 92.17           C  
ANISOU 4565  C   ILE B 367    17205  12743   5074  -1235   -251   2377       C  
ATOM   4566  O   ILE B 367     -24.759   5.337   3.748  1.00 95.97           O  
ANISOU 4566  O   ILE B 367    17905  13300   5261  -1261   -233   2452       O  
ATOM   4567  CB  ILE B 367     -25.553   7.381   5.925  1.00 93.03           C  
ANISOU 4567  CB  ILE B 367    17496  12381   5472  -1043   -263   2861       C  
ATOM   4568  CG1 ILE B 367     -24.123   7.463   6.464  1.00 91.03           C  
ANISOU 4568  CG1 ILE B 367    17187  12051   5350  -1297    185   2684       C  
ATOM   4569  CG2 ILE B 367     -26.530   8.114   6.834  1.00 92.19           C  
ANISOU 4569  CG2 ILE B 367    17346  12062   5620   -819   -469   3073       C  
ATOM   4570  CD1 ILE B 367     -23.112   7.974   5.454  1.00 94.40           C  
ANISOU 4570  CD1 ILE B 367    17832  12478   5556  -1475    477   2712       C  
ATOM   4571  N   LEU B 368     -24.203   4.267   5.647  1.00 88.67           N  
ANISOU 4571  N   LEU B 368    16529  12372   4789  -1373    -59   2089       N  
ATOM   4572  CA  LEU B 368     -23.207   3.419   5.004  1.00 89.10           C  
ANISOU 4572  CA  LEU B 368    16552  12605   4697  -1539    168   1829       C  
ATOM   4573  C   LEU B 368     -23.888   2.343   4.169  1.00 90.45           C  
ANISOU 4573  C   LEU B 368    16711  13003   4652  -1463   -124   1708       C  
ATOM   4574  O   LEU B 368     -23.301   1.804   3.232  1.00 92.52           O  
ANISOU 4574  O   LEU B 368    17054  13409   4691  -1549     -5   1569       O  
ATOM   4575  CB  LEU B 368     -22.294   2.771   6.047  1.00 85.08           C  
ANISOU 4575  CB  LEU B 368    15761  12111   4455  -1673    428   1553       C  
ATOM   4576  CG  LEU B 368     -21.325   3.696   6.786  1.00 84.08           C  
ANISOU 4576  CG  LEU B 368    15615  11798   4533  -1803    779   1597       C  
ATOM   4577  CD1 LEU B 368     -20.525   2.914   7.814  1.00 80.25           C  
ANISOU 4577  CD1 LEU B 368    14809  11371   4313  -1908    982   1305       C  
ATOM   4578  CD2 LEU B 368     -20.400   4.396   5.803  1.00 87.74           C  
ANISOU 4578  CD2 LEU B 368    16295  12235   4806  -1936   1052   1674       C  
ATOM   4579  N   TYR B 369     -25.135   2.038   4.515  1.00 90.29           N  
ANISOU 4579  N   TYR B 369    16583  13012   4713  -1302   -510   1756       N  
ATOM   4580  CA  TYR B 369     -25.901   1.020   3.809  1.00 91.61           C  
ANISOU 4580  CA  TYR B 369    16704  13387   4717  -1233   -830   1632       C  
ATOM   4581  C   TYR B 369     -26.475   1.587   2.514  1.00 96.52           C  
ANISOU 4581  C   TYR B 369    17594  14062   5018  -1136  -1027   1853       C  
ATOM   4582  O   TYR B 369     -26.948   0.844   1.654  1.00 98.71           O  
ANISOU 4582  O   TYR B 369    17894  14525   5085  -1107  -1245   1751       O  
ATOM   4583  CB  TYR B 369     -27.030   0.487   4.695  1.00 89.02           C  
ANISOU 4583  CB  TYR B 369    16122  13075   4627  -1106  -1182   1603       C  
ATOM   4584  CG  TYR B 369     -26.579  -0.004   6.056  1.00 84.30           C  
ANISOU 4584  CG  TYR B 369    15265  12419   4347  -1184  -1016   1418       C  
ATOM   4585  CD1 TYR B 369     -25.308  -0.535   6.242  1.00 82.62           C  
ANISOU 4585  CD1 TYR B 369    14984  12235   4172  -1358   -641   1172       C  
ATOM   4586  CD2 TYR B 369     -27.426   0.067   7.155  1.00 81.78           C  
ANISOU 4586  CD2 TYR B 369    14753  12022   4299  -1071  -1237   1494       C  
ATOM   4587  CE1 TYR B 369     -24.895  -0.981   7.484  1.00 78.57           C  
ANISOU 4587  CE1 TYR B 369    14222  11685   3947  -1419   -494   1004       C  
ATOM   4588  CE2 TYR B 369     -27.021  -0.378   8.400  1.00 76.69           C  
ANISOU 4588  CE2 TYR B 369    13766  11318   4053  -1097  -1057   1304       C  
ATOM   4589  CZ  TYR B 369     -25.755  -0.901   8.559  1.00 75.31           C  
ANISOU 4589  CZ  TYR B 369    13557  11183   3874  -1279   -699   1067       C  
ATOM   4590  OH  TYR B 369     -25.348  -1.344   9.797  1.00 70.50           O  
ANISOU 4590  OH  TYR B 369    12602  10522   3664  -1286   -537    884       O  
ATOM   4591  N   ASN B 370     -26.427   2.909   2.385  1.00135.21           N  
ANISOU 4591  N   ASN B 370    22697  18791   9884  -1088   -947   2153       N  
ATOM   4592  CA  ASN B 370     -26.967   3.591   1.214  1.00140.20           C  
ANISOU 4592  CA  ASN B 370    23595  19454  10221   -984  -1121   2401       C  
ATOM   4593  C   ASN B 370     -25.898   3.889   0.167  1.00143.46           C  
ANISOU 4593  C   ASN B 370    24268  19900  10339  -1136   -802   2398       C  
ATOM   4594  O   ASN B 370     -26.116   3.694  -1.029  1.00147.16           O  
ANISOU 4594  O   ASN B 370    24901  20530  10482  -1116   -926   2409       O  
ATOM   4595  CB  ASN B 370     -27.657   4.891   1.628  1.00139.67           C  
ANISOU 4595  CB  ASN B 370    23613  19168  10288   -817  -1237   2750       C  
ATOM   4596  CG  ASN B 370     -28.754   4.669   2.649  1.00137.79           C  
ANISOU 4596  CG  ASN B 370    23112  18899  10342   -636  -1567   2779       C  
ATOM   4597  OD1 ASN B 370     -29.503   3.695   2.572  1.00137.61           O  
ANISOU 4597  OD1 ASN B 370    22905  19063  10316   -571  -1876   2640       O  
ATOM   4598  ND2 ASN B 370     -28.852   5.572   3.617  1.00136.80           N  
ANISOU 4598  ND2 ASN B 370    22961  18532  10486   -555  -1498   2953       N  
ATOM   4599  N   LEU B 371     -24.746   4.366   0.626  1.00104.42           N  
ANISOU 4599  N   LEU B 371    19350  14809   5516  -1292   -394   2381       N  
ATOM   4600  CA  LEU B 371     -23.657   4.749  -0.266  1.00107.50           C  
ANISOU 4600  CA  LEU B 371    19963  15210   5674  -1449    -57   2393       C  
ATOM   4601  C   LEU B 371     -23.078   3.556  -1.019  1.00108.22           C  
ANISOU 4601  C   LEU B 371    20018  15538   5562  -1549     32   2097       C  
ATOM   4602  O   LEU B 371     -22.633   3.685  -2.159  1.00112.21           O  
ANISOU 4602  O   LEU B 371    20750  16131   5752  -1606    144   2132       O  
ATOM   4603  CB  LEU B 371     -22.544   5.445   0.521  1.00105.62           C  
ANISOU 4603  CB  LEU B 371    19685  14776   5671  -1611    354   2392       C  
ATOM   4604  CG  LEU B 371     -22.908   6.746   1.238  1.00105.33           C  
ANISOU 4604  CG  LEU B 371    19721  14463   5838  -1540    343   2674       C  
ATOM   4605  CD1 LEU B 371     -21.705   7.296   1.987  1.00103.51           C  
ANISOU 4605  CD1 LEU B 371    19420  14065   5844  -1735    758   2608       C  
ATOM   4606  CD2 LEU B 371     -23.444   7.769   0.251  1.00110.34           C  
ANISOU 4606  CD2 LEU B 371    20686  15020   6218  -1438    221   3008       C  
ATOM   4607  N   VAL B 372     -23.089   2.394  -0.375  1.00181.04           N  
ANISOU 4607  N   VAL B 372    28962  24856  14968  -1563    -16   1808       N  
ATOM   4608  CA  VAL B 372     -22.451   1.208  -0.932  1.00182.44           C  
ANISOU 4608  CA  VAL B 372    29077  25224  15018  -1653    108   1496       C  
ATOM   4609  C   VAL B 372     -23.401   0.387  -1.805  1.00185.48           C  
ANISOU 4609  C   VAL B 372    29521  25803  15149  -1547   -257   1424       C  
ATOM   4610  O   VAL B 372     -23.003  -0.134  -2.848  1.00190.16           O  
ANISOU 4610  O   VAL B 372    30244  26544  15464  -1598   -177   1295       O  
ATOM   4611  CB  VAL B 372     -21.856   0.325   0.182  1.00170.38           C  
ANISOU 4611  CB  VAL B 372    27220  23693  13822  -1726    269   1203       C  
ATOM   4612  CG1 VAL B 372     -21.062  -0.817  -0.413  1.00170.82           C  
ANISOU 4612  CG1 VAL B 372    27219  23916  13767  -1804    436    889       C  
ATOM   4613  CG2 VAL B 372     -20.969   1.159   1.092  1.00168.40           C  
ANISOU 4613  CG2 VAL B 372    26892  23263  13828  -1834    608   1268       C  
ATOM   4614  N   SER B 373     -24.657   0.279  -1.382  1.00140.84           N  
ANISOU 4614  N   SER B 373    23766  20152   9595  -1401   -659   1504       N  
ATOM   4615  CA  SER B 373     -25.647  -0.489  -2.133  1.00143.40           C  
ANISOU 4615  CA  SER B 373    24100  20663   9721  -1306  -1042   1425       C  
ATOM   4616  C   SER B 373     -26.758   0.402  -2.683  1.00147.60           C  
ANISOU 4616  C   SER B 373    24795  21195  10092  -1143  -1388   1751       C  
ATOM   4617  O   SER B 373     -27.274   1.270  -1.981  1.00146.61           O  
ANISOU 4617  O   SER B 373    24622  20915  10166  -1042  -1490   1986       O  
ATOM   4618  CB  SER B 373     -26.241  -1.594  -1.260  1.00136.64           C  
ANISOU 4618  CB  SER B 373    22925  19853   9139  -1277  -1255   1183       C  
ATOM   4619  OG  SER B 373     -27.175  -2.372  -1.988  1.00140.02           O  
ANISOU 4619  OG  SER B 373    23343  20460   9397  -1209  -1619   1079       O  
ATOM   4620  N   ALA B 374     -27.124   0.175  -3.941  1.00144.11           N  
ANISOU 4620  N   ALA B 374    24538  20926   9291  -1107  -1568   1763       N  
ATOM   4621  CA  ALA B 374     -28.140   0.985  -4.608  1.00148.18           C  
ANISOU 4621  CA  ALA B 374    25211  21472   9618   -944  -1901   2070       C  
ATOM   4622  C   ALA B 374     -29.545   0.421  -4.413  1.00147.60           C  
ANISOU 4622  C   ALA B 374    24908  21513   9660   -798  -2393   2032       C  
ATOM   4623  O   ALA B 374     -30.524   1.167  -4.393  1.00149.39           O  
ANISOU 4623  O   ALA B 374    25120  21704   9937   -626  -2683   2301       O  
ATOM   4624  CB  ALA B 374     -27.821   1.120  -6.090  1.00153.64           C  
ANISOU 4624  CB  ALA B 374    26224  22306   9847   -978  -1856   2122       C  
ATOM   4625  N   ASN B 375     -29.637  -0.898  -4.281  1.00138.17           N  
ANISOU 4625  N   ASN B 375    23525  20454   8522   -865  -2481   1694       N  
ATOM   4626  CA  ASN B 375     -30.914  -1.561  -4.043  1.00138.02           C  
ANISOU 4626  CA  ASN B 375    23248  20549   8647   -764  -2927   1609       C  
ATOM   4627  C   ASN B 375     -31.495  -1.156  -2.692  1.00134.68           C  
ANISOU 4627  C   ASN B 375    22561  19968   8643   -662  -3039   1740       C  
ATOM   4628  O   ASN B 375     -32.645  -0.712  -2.596  1.00135.74           O  
ANISOU 4628  O   ASN B 375    22592  20122   8862   -489  -3393   1943       O  
ATOM   4629  CB  ASN B 375     -30.736  -3.080  -4.107  1.00137.54           C  
ANISOU 4629  CB  ASN B 375    23038  20609   8614   -888  -2920   1197       C  
ATOM   4630  CG  ASN B 375     -32.035  -3.833  -3.891  1.00137.26           C  
ANISOU 4630  CG  ASN B 375    22731  20696   8726   -816  -3373   1081       C  
ATOM   4631  OD1 ASN B 375     -33.121  -3.305  -4.132  1.00139.94           O  
ANISOU 4631  OD1 ASN B 375    23031  21104   9038   -668  -3730   1293       O  
ATOM   4632  ND2 ASN B 375     -31.928  -5.076  -3.434  1.00134.46           N  
ANISOU 4632  ND2 ASN B 375    22174  20369   8546   -919  -3356    740       N  
ATOM   4633  N   PHE B 376     -30.681  -1.302  -1.652  1.00139.94           N  
ANISOU 4633  N   PHE B 376    23111  20484   9574   -764  -2729   1623       N  
ATOM   4634  CA  PHE B 376     -31.088  -0.964  -0.296  1.00136.82           C  
ANISOU 4634  CA  PHE B 376    22476  19931   9576   -687  -2782   1720       C  
ATOM   4635  C   PHE B 376     -31.286   0.545  -0.174  1.00138.28           C  
ANISOU 4635  C   PHE B 376    22814  19947   9776   -551  -2762   2107       C  
ATOM   4636  O   PHE B 376     -32.054   1.020   0.665  1.00136.85           O  
ANISOU 4636  O   PHE B 376    22461  19663   9872   -404  -2944   2271       O  
ATOM   4637  CB  PHE B 376     -30.050  -1.459   0.715  1.00125.85           C  
ANISOU 4637  CB  PHE B 376    20959  18434   8422   -842  -2423   1498       C  
ATOM   4638  CG  PHE B 376     -29.675  -2.909   0.542  1.00125.63           C  
ANISOU 4638  CG  PHE B 376    20824  18541   8366   -977  -2367   1117       C  
ATOM   4639  CD1 PHE B 376     -30.600  -3.832   0.078  1.00127.63           C  
ANISOU 4639  CD1 PHE B 376    20960  18963   8569   -944  -2722    963       C  
ATOM   4640  CD2 PHE B 376     -28.395  -3.347   0.840  1.00123.66           C  
ANISOU 4640  CD2 PHE B 376    20579  18245   8160  -1130  -1956    907       C  
ATOM   4641  CE1 PHE B 376     -30.254  -5.161  -0.085  1.00127.23           C  
ANISOU 4641  CE1 PHE B 376    20830  19005   8506  -1062  -2661    609       C  
ATOM   4642  CE2 PHE B 376     -28.044  -4.674   0.679  1.00123.28           C  
ANISOU 4642  CE2 PHE B 376    20435  18300   8105  -1227  -1896    561       C  
ATOM   4643  CZ  PHE B 376     -28.975  -5.582   0.217  1.00125.27           C  
ANISOU 4643  CZ  PHE B 376    20601  18693   8301  -1193  -2246    412       C  
ATOM   4644  N   ARG B 377     -30.588   1.291  -1.024  1.00138.71           N  
ANISOU 4644  N   ARG B 377    23192  19967   9544   -598  -2532   2251       N  
ATOM   4645  CA  ARG B 377     -30.762   2.734  -1.108  1.00139.91           C  
ANISOU 4645  CA  ARG B 377    23536  19953   9670   -474  -2513   2624       C  
ATOM   4646  C   ARG B 377     -32.172   3.052  -1.588  1.00142.49           C  
ANISOU 4646  C   ARG B 377    23824  20377   9938   -244  -2980   2838       C  
ATOM   4647  O   ARG B 377     -32.837   3.947  -1.063  1.00141.82           O  
ANISOU 4647  O   ARG B 377    23678  20150  10055    -62  -3117   3096       O  
ATOM   4648  CB  ARG B 377     -29.747   3.334  -2.081  1.00143.66           C  
ANISOU 4648  CB  ARG B 377    24366  20401   9818   -591  -2190   2715       C  
ATOM   4649  CG  ARG B 377     -29.778   4.851  -2.161  1.00145.98           C  
ANISOU 4649  CG  ARG B 377    24885  20486  10095   -493  -2113   3093       C  
ATOM   4650  CD  ARG B 377     -29.257   5.343  -3.503  1.00150.91           C  
ANISOU 4650  CD  ARG B 377    25869  21162  10308   -557  -1970   3224       C  
ATOM   4651  NE  ARG B 377     -28.022   4.672  -3.898  1.00150.72           N  
ANISOU 4651  NE  ARG B 377    25916  21235  10115   -785  -1632   2955       N  
ATOM   4652  CZ  ARG B 377     -27.334   4.963  -4.997  1.00154.58           C  
ANISOU 4652  CZ  ARG B 377    26699  21766  10267   -884  -1414   3016       C  
ATOM   4653  NH1 ARG B 377     -27.757   5.919  -5.813  1.00158.95           N  
ANISOU 4653  NH1 ARG B 377    27523  22267  10605   -786  -1501   3344       N  
ATOM   4654  NH2 ARG B 377     -26.221   4.300  -5.281  1.00154.62           N  
ANISOU 4654  NH2 ARG B 377    26725  21864  10160  -1074  -1105   2753       N  
ATOM   4655  N   GLN B 378     -32.623   2.305  -2.591  1.00165.80           N  
ANISOU 4655  N   GLN B 378    26799  23577  12621   -246  -3223   2719       N  
ATOM   4656  CA  GLN B 378     -33.939   2.530  -3.176  1.00169.74           C  
ANISOU 4656  CA  GLN B 378    27245  24215  13035    -40  -3677   2899       C  
ATOM   4657  C   GLN B 378     -35.072   2.009  -2.299  1.00167.75           C  
ANISOU 4657  C   GLN B 378    26581  24011  13147     84  -4019   2827       C  
ATOM   4658  O   GLN B 378     -36.175   2.556  -2.326  1.00170.67           O  
ANISOU 4658  O   GLN B 378    26836  24404  13606    301  -4340   3054       O  
ATOM   4659  CB  GLN B 378     -34.023   1.939  -4.585  1.00163.60           C  
ANISOU 4659  CB  GLN B 378    26640  23694  11827    -91  -3823   2796       C  
ATOM   4660  CG  GLN B 378     -33.229   2.721  -5.621  1.00167.54           C  
ANISOU 4660  CG  GLN B 378    27557  24162  11940   -138  -3582   2984       C  
ATOM   4661  CD  GLN B 378     -33.674   4.170  -5.725  1.00170.13           C  
ANISOU 4661  CD  GLN B 378    28030  24332  12280     49  -3646   3410       C  
ATOM   4662  OE1 GLN B 378     -34.855   4.482  -5.574  1.00171.44           O  
ANISOU 4662  OE1 GLN B 378    28026  24530  12585    262  -4011   3584       O  
ATOM   4663  NE2 GLN B 378     -32.725   5.063  -5.981  1.00171.08           N  
ANISOU 4663  NE2 GLN B 378    28453  24276  12274    -30  -3283   3576       N  
ATOM   4664  N   VAL B 379     -34.815   0.960  -1.522  1.00131.08           N  
ANISOU 4664  N   VAL B 379    21701  19379   8727    -49  -3946   2518       N  
ATOM   4665  CA  VAL B 379     -35.820   0.526  -0.554  1.00128.64           C  
ANISOU 4665  CA  VAL B 379    20988  19084   8807     54  -4225   2461       C  
ATOM   4666  C   VAL B 379     -35.873   1.526   0.603  1.00125.57           C  
ANISOU 4666  C   VAL B 379    20520  18443   8750    189  -4119   2699       C  
ATOM   4667  O   VAL B 379     -36.926   1.733   1.211  1.00124.70           O  
ANISOU 4667  O   VAL B 379    20134  18323   8924    378  -4391   2817       O  
ATOM   4668  CB  VAL B 379     -35.599  -0.924  -0.044  1.00124.16           C  
ANISOU 4668  CB  VAL B 379    20181  18595   8402   -125  -4196   2067       C  
ATOM   4669  CG1 VAL B 379     -35.345  -1.866  -1.211  1.00127.05           C  
ANISOU 4669  CG1 VAL B 379    20682  19166   8426   -269  -4223   1815       C  
ATOM   4670  CG2 VAL B 379     -34.465  -0.994   0.963  1.00119.02           C  
ANISOU 4670  CG2 VAL B 379    19530  17750   7944   -263  -3792   1958       C  
ATOM   4671  N   PHE B 380     -34.735   2.161   0.878  1.00158.58           N  
ANISOU 4671  N   PHE B 380    24936  22419  12897     92  -3713   2764       N  
ATOM   4672  CA  PHE B 380     -34.666   3.219   1.879  1.00157.08           C  
ANISOU 4672  CA  PHE B 380    24737  21963  12983    205  -3569   2992       C  
ATOM   4673  C   PHE B 380     -35.510   4.408   1.433  1.00161.10           C  
ANISOU 4673  C   PHE B 380    25346  22415  13448    456  -3777   3359       C  
ATOM   4674  O   PHE B 380     -36.316   4.930   2.203  1.00159.72           O  
ANISOU 4674  O   PHE B 380    24970  22132  13582    665  -3935   3523       O  
ATOM   4675  CB  PHE B 380     -33.215   3.657   2.099  1.00148.08           C  
ANISOU 4675  CB  PHE B 380    23848  20635  11781     18  -3077   2970       C  
ATOM   4676  CG  PHE B 380     -33.050   4.727   3.145  1.00145.45           C  
ANISOU 4676  CG  PHE B 380    23524  20009  11729    105  -2897   3173       C  
ATOM   4677  CD1 PHE B 380     -33.890   4.781   4.244  1.00143.43           C  
ANISOU 4677  CD1 PHE B 380    22979  19672  11845    279  -3091   3227       C  
ATOM   4678  CD2 PHE B 380     -32.055   5.683   3.023  1.00145.04           C  
ANISOU 4678  CD2 PHE B 380    23765  19759  11582      9  -2524   3300       C  
ATOM   4679  CE1 PHE B 380     -33.739   5.765   5.204  1.00141.14           C  
ANISOU 4679  CE1 PHE B 380    22713  19101  11813    370  -2915   3400       C  
ATOM   4680  CE2 PHE B 380     -31.899   6.669   3.980  1.00143.04           C  
ANISOU 4680  CE2 PHE B 380    23531  19222  11594     78  -2351   3468       C  
ATOM   4681  CZ  PHE B 380     -32.743   6.710   5.071  1.00141.06           C  
ANISOU 4681  CZ  PHE B 380    23012  18885  11698    265  -2546   3515       C  
ATOM   4682  N   LEU B 381     -35.321   4.828   0.186  1.00192.25           N  
ANISOU 4682  N   LEU B 381    29597  26433  17014    444  -3769   3486       N  
ATOM   4683  CA  LEU B 381     -36.080   5.945  -0.369  1.00196.40           C  
ANISOU 4683  CA  LEU B 381    30246  26918  17457    677  -3967   3842       C  
ATOM   4684  C   LEU B 381     -37.570   5.626  -0.463  1.00197.87           C  
ANISOU 4684  C   LEU B 381    30114  27302  17766    897  -4453   3885       C  
ATOM   4685  O   LEU B 381     -38.415   6.470  -0.158  1.00199.44           O  
ANISOU 4685  O   LEU B 381    30206  27408  18165   1147  -4624   4148       O  
ATOM   4686  CB  LEU B 381     -35.541   6.333  -1.748  1.00206.30           C  
ANISOU 4686  CB  LEU B 381    31894  28241  18247    598  -3868   3950       C  
ATOM   4687  CG  LEU B 381     -34.134   6.931  -1.797  1.00205.04           C  
ANISOU 4687  CG  LEU B 381    32066  27875  17965    408  -3382   3984       C  
ATOM   4688  CD1 LEU B 381     -33.747   7.268  -3.229  1.00209.95           C  
ANISOU 4688  CD1 LEU B 381    33050  28594  18125    350  -3329   4102       C  
ATOM   4689  CD2 LEU B 381     -34.044   8.163  -0.909  1.00203.64           C  
ANISOU 4689  CD2 LEU B 381    31934  27366  18074    516  -3211   4234       C  
ATOM   4690  N   SER B 382     -37.885   4.405  -0.887  1.00186.73           N  
ANISOU 4690  N   SER B 382    28538  26163  16250    801  -4664   3617       N  
ATOM   4691  CA  SER B 382     -39.272   3.982  -1.040  1.00189.00           C  
ANISOU 4691  CA  SER B 382    28495  26671  16646    970  -5122   3615       C  
ATOM   4692  C   SER B 382     -39.993   3.951   0.303  1.00185.49           C  
ANISOU 4692  C   SER B 382    27640  26131  16708   1110  -5223   3615       C  
ATOM   4693  O   SER B 382     -41.122   4.425   0.419  1.00186.46           O  
ANISOU 4693  O   SER B 382    27540  26296  17013   1359  -5504   3809       O  
ATOM   4694  CB  SER B 382     -39.351   2.607  -1.707  1.00187.45           C  
ANISOU 4694  CB  SER B 382    28213  26758  16254    794  -5284   3282       C  
ATOM   4695  OG  SER B 382     -38.864   1.594  -0.846  1.00182.35           O  
ANISOU 4695  OG  SER B 382    27381  26076  15829    607  -5125   2961       O  
ATOM   4696  N   THR B 383     -39.336   3.394   1.316  1.00146.59           N  
ANISOU 4696  N   THR B 383    22605  21082  12010    956  -4985   3399       N  
ATOM   4697  CA  THR B 383     -39.924   3.332   2.650  1.00142.54           C  
ANISOU 4697  CA  THR B 383    21713  20470  11978   1074  -5046   3387       C  
ATOM   4698  C   THR B 383     -39.951   4.703   3.320  1.00141.18           C  
ANISOU 4698  C   THR B 383    21616  20015  12013   1282  -4902   3699       C  
ATOM   4699  O   THR B 383     -40.768   4.952   4.207  1.00138.61           O  
ANISOU 4699  O   THR B 383    20975  19623  12069   1479  -5021   3779       O  
ATOM   4700  CB  THR B 383     -39.185   2.334   3.552  1.00134.79           C  
ANISOU 4700  CB  THR B 383    20604  19441  11170    845  -4835   3072       C  
ATOM   4701  OG1 THR B 383     -37.778   2.600   3.503  1.00133.66           O  
ANISOU 4701  OG1 THR B 383    20819  19138  10828    659  -4426   3041       O  
ATOM   4702  CG2 THR B 383     -39.447   0.908   3.088  1.00134.75           C  
ANISOU 4702  CG2 THR B 383    20423  19699  11078    679  -5029   2753       C  
ATOM   4703  N   LEU B 384     -39.055   5.588   2.895  1.00188.67           N  
ANISOU 4703  N   LEU B 384    28043  25853  17788   1235  -4627   3864       N  
ATOM   4704  CA  LEU B 384     -39.054   6.960   3.390  1.00189.56           C  
ANISOU 4704  CA  LEU B 384    28279  25676  18069   1421  -4482   4167       C  
ATOM   4705  C   LEU B 384     -40.224   7.716   2.774  1.00195.17           C  
ANISOU 4705  C   LEU B 384    28939  26457  18761   1710  -4801   4461       C  
ATOM   4706  O   LEU B 384     -40.774   8.636   3.381  1.00195.01           O  
ANISOU 4706  O   LEU B 384    28826  26250  19018   1950  -4819   4688       O  
ATOM   4707  CB  LEU B 384     -37.733   7.658   3.063  1.00182.68           C  
ANISOU 4707  CB  LEU B 384    27857  24595  16956   1249  -4077   4239       C  
ATOM   4708  CG  LEU B 384     -37.538   9.055   3.654  1.00182.51           C  
ANISOU 4708  CG  LEU B 384    27995  24224  17125   1385  -3859   4507       C  
ATOM   4709  CD1 LEU B 384     -37.706   9.025   5.165  1.00178.32           C  
ANISOU 4709  CD1 LEU B 384    27178  23527  17048   1470  -3793   4434       C  
ATOM   4710  CD2 LEU B 384     -36.176   9.613   3.275  1.00182.19           C  
ANISOU 4710  CD2 LEU B 384    28369  24005  16848   1159  -3443   4529       C  
ATOM   4711  N   ALA B 385     -40.601   7.318   1.563  1.00165.39           N  
ANISOU 4711  N   ALA B 385    25224  22957  14659   1690  -5048   4450       N  
ATOM   4712  CA  ALA B 385     -41.783   7.866   0.911  1.00170.07           C  
ANISOU 4712  CA  ALA B 385    25722  23681  15215   1954  -5400   4704       C  
ATOM   4713  C   ALA B 385     -43.038   7.293   1.560  1.00168.17           C  
ANISOU 4713  C   ALA B 385    24950  23606  15342   2121  -5716   4619       C  
ATOM   4714  O   ALA B 385     -44.120   7.873   1.468  1.00170.58           O  
ANISOU 4714  O   ALA B 385    25065  23962  15788   2394  -5966   4845       O  
ATOM   4715  CB  ALA B 385     -41.763   7.557  -0.576  1.00174.47           C  
ANISOU 4715  CB  ALA B 385    26506  24496  15290   1865  -5567   4696       C  
ATOM   4716  N   CYS B 386     -42.885   6.146   2.214  1.00150.94           N  
ANISOU 4716  N   CYS B 386    22519  21507  13324   1950  -5691   4291       N  
ATOM   4717  CA  CYS B 386     -43.980   5.531   2.952  1.00149.79           C  
ANISOU 4717  CA  CYS B 386    21849  21494  13568   2068  -5931   4175       C  
ATOM   4718  C   CYS B 386     -44.051   6.105   4.362  1.00147.37           C  
ANISOU 4718  C   CYS B 386    21365  20915  13713   2214  -5741   4259       C  
ATOM   4719  O   CYS B 386     -45.049   5.938   5.062  1.00146.44           O  
ANISOU 4719  O   CYS B 386    20812  20860  13969   2385  -5902   4246       O  
ATOM   4720  CB  CYS B 386     -43.804   4.013   3.014  1.00144.78           C  
ANISOU 4720  CB  CYS B 386    21030  21053  12926   1804  -5982   3782       C  
ATOM   4721  SG  CYS B 386     -43.909   3.177   1.414  1.00149.00           S  
ANISOU 4721  SG  CYS B 386    21704  21931  12977   1638  -6236   3623       S  
ATOM   4722  N   LEU B 387     -42.985   6.786   4.771  1.00269.53           N  
ANISOU 4722  N   LEU B 387    37171  36088  29151   2141  -5384   4335       N  
ATOM   4723  CA  LEU B 387     -42.918   7.368   6.106  1.00266.78           C  
ANISOU 4723  CA  LEU B 387    36710  35453  29200   2262  -5170   4402       C  
ATOM   4724  C   LEU B 387     -43.100   8.885   6.061  1.00268.78           C  
ANISOU 4724  C   LEU B 387    37172  35456  29497   2502  -5087   4758       C  
ATOM   4725  O   LEU B 387     -43.082   9.554   7.094  1.00266.41           O  
ANISOU 4725  O   LEU B 387    36832  34880  29510   2624  -4894   4841       O  
ATOM   4726  CB  LEU B 387     -41.597   6.999   6.789  1.00249.20           C  
ANISOU 4726  CB  LEU B 387    34664  33055  26967   1996  -4814   4194       C  
ATOM   4727  CG  LEU B 387     -41.551   7.137   8.314  1.00245.03           C  
ANISOU 4727  CG  LEU B 387    33922  32302  26875   2073  -4635   4151       C  
ATOM   4728  CD1 LEU B 387     -42.715   6.396   8.953  1.00244.74           C  
ANISOU 4728  CD1 LEU B 387    33339  32440  27210   2223  -4899   4055       C  
ATOM   4729  CD2 LEU B 387     -40.229   6.634   8.863  1.00240.22           C  
ANISOU 4729  CD2 LEU B 387    33470  31588  26216   1783  -4325   3921       C  
ATOM   4730  N   CYS B 388     -43.280   9.426   4.860  1.00200.65           N  
ANISOU 4730  N   CYS B 388    28772  26912  20555   2567  -5233   4965       N  
ATOM   4731  CA  CYS B 388     -43.570  10.852   4.718  1.00204.28           C  
ANISOU 4731  CA  CYS B 388    29405  27145  21066   2808  -5206   5321       C  
ATOM   4732  C   CYS B 388     -44.896  11.304   5.363  1.00205.91           C  
ANISOU 4732  C   CYS B 388    29192  27343  21700   3145  -5412   5474       C  
ATOM   4733  O   CYS B 388     -45.010  12.461   5.769  1.00207.23           O  
ANISOU 4733  O   CYS B 388    29452  27222  22063   3337  -5298   5712       O  
ATOM   4734  CB  CYS B 388     -43.457  11.320   3.257  1.00198.03           C  
ANISOU 4734  CB  CYS B 388    28967  26447  19827   2796  -5318   5521       C  
ATOM   4735  SG  CYS B 388     -44.825  10.890   2.156  1.00203.73           S  
ANISOU 4735  SG  CYS B 388    29422  27592  20395   2968  -5839   5602       S  
ATOM   4736  N   PRO B 389     -45.903  10.410   5.462  1.00190.02           N  
ANISOU 4736  N   PRO B 389    26713  25641  19848   3212  -5699   5330       N  
ATOM   4737  CA  PRO B 389     -47.025  10.863   6.289  1.00190.77           C  
ANISOU 4737  CA  PRO B 389    26387  25689  20408   3510  -5794   5447       C  
ATOM   4738  C   PRO B 389     -46.841  10.458   7.749  1.00185.21           C  
ANISOU 4738  C   PRO B 389    25421  24862  20089   3464  -5581   5221       C  
ATOM   4739  O   PRO B 389     -46.157   9.469   8.017  1.00181.30           O  
ANISOU 4739  O   PRO B 389    24923  24454  19509   3208  -5498   4932       O  
ATOM   4740  CB  PRO B 389     -48.215  10.120   5.686  1.00183.58           C  
ANISOU 4740  CB  PRO B 389    25091  25193  19470   3607  -6197   5408       C  
ATOM   4741  CG  PRO B 389     -47.633   8.847   5.205  1.00181.64           C  
ANISOU 4741  CG  PRO B 389    24919  25180  18918   3294  -6248   5098       C  
ATOM   4742  CD  PRO B 389     -46.249   9.184   4.714  1.00180.37           C  
ANISOU 4742  CD  PRO B 389    25324  24813  18396   3073  -5978   5119       C  
TER    4743      PRO B 389                                                      
ATOM   4744  N   GLY C   7     -40.593 -40.029  32.313  1.00105.82           N  
ANISOU 4744  N   GLY C   7    12422  10475  17310  -3548   -441  -1901       N  
ATOM   4745  CA  GLY C   7     -40.859 -40.607  33.617  1.00106.61           C  
ANISOU 4745  CA  GLY C   7    12516  10346  17646  -3577   -183  -1679       C  
ATOM   4746  C   GLY C   7     -40.116 -39.898  34.732  1.00104.58           C  
ANISOU 4746  C   GLY C   7    12273  10180  17282  -3219     31  -1435       C  
ATOM   4747  O   GLY C   7     -40.688 -39.604  35.782  1.00104.55           O  
ANISOU 4747  O   GLY C   7    12085  10221  17416  -3217    189  -1191       O  
ATOM   4748  N   ARG C   8     -38.836 -39.624  34.503  1.00130.99           N  
ANISOU 4748  N   ARG C   8    15834  13561  20376  -2921     40  -1510       N  
ATOM   4749  CA  ARG C   8     -38.006 -38.946  35.493  1.00129.34           C  
ANISOU 4749  CA  ARG C   8    15655  13451  20039  -2576    214  -1312       C  
ATOM   4750  C   ARG C   8     -36.961 -38.057  34.825  1.00128.12           C  
ANISOU 4750  C   ARG C   8    15558  13534  19586  -2322    112  -1427       C  
ATOM   4751  O   ARG C   8     -36.445 -38.384  33.757  1.00128.14           O  
ANISOU 4751  O   ARG C   8    15725  13496  19467  -2342    -14  -1668       O  
ATOM   4752  CB  ARG C   8     -37.334 -39.964  36.416  1.00131.92           C  
ANISOU 4752  CB  ARG C   8    16260  13428  20434  -2452    440  -1222       C  
ATOM   4753  CG  ARG C   8     -36.526 -41.028  35.690  1.00132.21           C  
ANISOU 4753  CG  ARG C   8    16626  13181  20427  -2438    406  -1459       C  
ATOM   4754  CD  ARG C   8     -35.986 -42.060  36.665  1.00132.90           C  
ANISOU 4754  CD  ARG C   8    16982  12905  20609  -2308    627  -1339       C  
ATOM   4755  NE  ARG C   8     -35.176 -41.446  37.712  1.00131.91           N  
ANISOU 4755  NE  ARG C   8    16866  12904  20349  -1961    767  -1131       N  
ATOM   4756  CZ  ARG C   8     -34.640 -42.112  38.730  1.00132.20           C  
ANISOU 4756  CZ  ARG C   8    17109  12696  20426  -1785    954   -971       C  
ATOM   4757  NH1 ARG C   8     -34.829 -43.419  38.842  1.00133.49           N  
ANISOU 4757  NH1 ARG C   8    17499  12453  20769  -1919   1041   -984       N  
ATOM   4758  NH2 ARG C   8     -33.916 -41.470  39.637  1.00131.20           N  
ANISOU 4758  NH2 ARG C   8    16973  12724  20154  -1476   1047   -796       N  
ATOM   4759  N   ARG C   9     -36.651 -36.933  35.464  1.00 88.51           N  
ANISOU 4759  N   ARG C   9    10417   8761  14452  -2091    179  -1257       N  
ATOM   4760  CA  ARG C   9     -35.751 -35.941  34.885  1.00 87.07           C  
ANISOU 4760  CA  ARG C   9    10248   8833  14001  -1878     91  -1339       C  
ATOM   4761  C   ARG C   9     -34.555 -35.661  35.794  1.00 85.97           C  
ANISOU 4761  C   ARG C   9    10229   8701  13732  -1549    261  -1228       C  
ATOM   4762  O   ARG C   9     -34.715 -35.519  37.006  1.00 86.07           O  
ANISOU 4762  O   ARG C   9    10186   8694  13823  -1461    417  -1009       O  
ATOM   4763  CB  ARG C   9     -36.518 -34.646  34.607  1.00 84.89           C  
ANISOU 4763  CB  ARG C   9     9681   8889  13685  -1927    -39  -1266       C  
ATOM   4764  CG  ARG C   9     -35.700 -33.555  33.939  1.00 84.38           C  
ANISOU 4764  CG  ARG C   9     9629   9083  13347  -1745   -135  -1342       C  
ATOM   4765  CD  ARG C   9     -36.522 -32.294  33.748  1.00 83.24           C  
ANISOU 4765  CD  ARG C   9     9213   9232  13182  -1780   -255  -1244       C  
ATOM   4766  NE  ARG C   9     -35.785 -31.268  33.017  1.00 82.19           N  
ANISOU 4766  NE  ARG C   9     9117   9324  12787  -1630   -347  -1313       N  
ATOM   4767  CZ  ARG C   9     -35.785 -31.151  31.693  1.00 82.17           C  
ANISOU 4767  CZ  ARG C   9     9163   9419  12639  -1725   -544  -1491       C  
ATOM   4768  NH1 ARG C   9     -36.485 -31.998  30.950  1.00 83.15           N  
ANISOU 4768  NH1 ARG C   9     9299   9441  12852  -1969   -689  -1635       N  
ATOM   4769  NH2 ARG C   9     -35.085 -30.187  31.111  1.00 81.56           N  
ANISOU 4769  NH2 ARG C   9     9131   9538  12319  -1585   -595  -1528       N  
ATOM   4770  N   PRO C  10     -33.349 -35.588  35.205  1.00 54.79           N  
ANISOU 4770  N   PRO C  10     6445   4792   9583  -1369    231  -1383       N  
ATOM   4771  CA  PRO C  10     -32.113 -35.284  35.937  1.00 52.66           C  
ANISOU 4771  CA  PRO C  10     6267   4563   9179  -1057    361  -1309       C  
ATOM   4772  C   PRO C  10     -32.174 -33.951  36.676  1.00 50.01           C  
ANISOU 4772  C   PRO C  10     5739   4497   8765   -932    399  -1119       C  
ATOM   4773  O   PRO C  10     -32.859 -33.028  36.235  1.00 49.26           O  
ANISOU 4773  O   PRO C  10     5459   4619   8641  -1032    292  -1106       O  
ATOM   4774  CB  PRO C  10     -31.062 -35.215  34.825  1.00 52.20           C  
ANISOU 4774  CB  PRO C  10     6336   4578   8919   -959    280  -1544       C  
ATOM   4775  CG  PRO C  10     -31.593 -36.101  33.761  1.00 54.92           C  
ANISOU 4775  CG  PRO C  10     6780   4759   9330  -1194    169  -1748       C  
ATOM   4776  CD  PRO C  10     -33.083 -35.919  33.794  1.00 55.99           C  
ANISOU 4776  CD  PRO C  10     6716   4931   9629  -1465     81  -1655       C  
ATOM   4777  N   TYR C  11     -31.458 -33.861  37.793  1.00 54.60           N  
ANISOU 4777  N   TYR C  11     6376   5059   9309   -707    544   -978       N  
ATOM   4778  CA  TYR C  11     -31.397 -32.630  38.574  1.00 54.14           C  
ANISOU 4778  CA  TYR C  11     6174   5237   9161   -571    594   -816       C  
ATOM   4779  C   TYR C  11     -29.972 -32.089  38.640  1.00 53.06           C  
ANISOU 4779  C   TYR C  11     6111   5232   8819   -316    611   -872       C  
ATOM   4780  O   TYR C  11     -29.734 -31.000  39.161  1.00 53.09           O  
ANISOU 4780  O   TYR C  11     6016   5439   8716   -201    637   -779       O  
ATOM   4781  CB  TYR C  11     -31.953 -32.852  39.985  1.00 54.26           C  
ANISOU 4781  CB  TYR C  11     6164   5151   9303   -549    753   -580       C  
ATOM   4782  CG  TYR C  11     -31.376 -34.055  40.702  1.00 55.29           C  
ANISOU 4782  CG  TYR C  11     6515   5006   9487   -442    873   -532       C  
ATOM   4783  CD1 TYR C  11     -30.179 -33.964  41.401  1.00 54.73           C  
ANISOU 4783  CD1 TYR C  11     6559   4960   9278   -166    938   -488       C  
ATOM   4784  CD2 TYR C  11     -32.033 -35.279  40.685  1.00 56.30           C  
ANISOU 4784  CD2 TYR C  11     6737   4844   9809   -619    914   -526       C  
ATOM   4785  CE1 TYR C  11     -29.649 -35.060  42.059  1.00 54.83           C  
ANISOU 4785  CE1 TYR C  11     6777   4720   9335    -42   1032   -429       C  
ATOM   4786  CE2 TYR C  11     -31.511 -36.379  41.340  1.00 56.82           C  
ANISOU 4786  CE2 TYR C  11     7030   4633   9926   -509   1026   -466       C  
ATOM   4787  CZ  TYR C  11     -30.320 -36.264  42.025  1.00 55.87           C  
ANISOU 4787  CZ  TYR C  11     7024   4546   9657   -207   1081   -412       C  
ATOM   4788  OH  TYR C  11     -29.797 -37.357  42.678  1.00 56.02           O  
ANISOU 4788  OH  TYR C  11     7273   4289   9723    -73   1179   -339       O  
ATOM   4789  N   ILE C  12     -29.028 -32.858  38.105  1.00 56.84           N  
ANISOU 4789  N   ILE C  12     6757   5592   9248   -234    601  -1033       N  
ATOM   4790  CA  ILE C  12     -27.628 -32.454  38.084  1.00 55.27           C  
ANISOU 4790  CA  ILE C  12     6607   5519   8874      0    620  -1107       C  
ATOM   4791  C   ILE C  12     -27.284 -31.739  36.780  1.00 54.55           C  
ANISOU 4791  C   ILE C  12     6471   5624   8630    -52    512  -1291       C  
ATOM   4792  O   ILE C  12     -27.566 -32.244  35.692  1.00 54.16           O  
ANISOU 4792  O   ILE C  12     6484   5502   8592   -198    432  -1453       O  
ATOM   4793  CB  ILE C  12     -26.688 -33.664  38.256  1.00 53.68           C  
ANISOU 4793  CB  ILE C  12     6602   5091   8703    160    686  -1179       C  
ATOM   4794  CG1 ILE C  12     -26.968 -34.373  39.583  1.00 54.84           C  
ANISOU 4794  CG1 ILE C  12     6824   5035   8975    232    798   -972       C  
ATOM   4795  CG2 ILE C  12     -25.232 -33.230  38.178  1.00 51.51           C  
ANISOU 4795  CG2 ILE C  12     6335   4976   8261    397    698  -1272       C  
ATOM   4796  CD1 ILE C  12     -26.083 -35.576  39.830  1.00 55.11           C  
ANISOU 4796  CD1 ILE C  12     7065   4823   9049    414    859  -1013       C  
ATOM   4797  N   LEU C  13     -26.679 -30.562  36.896  1.00 65.36           N  
ANISOU 4797  N   LEU C  13     7749   7238   9848     59    514  -1266       N  
ATOM   4798  CA  LEU C  13     -26.263 -29.795  35.727  1.00 64.38           C  
ANISOU 4798  CA  LEU C  13     7599   7306   9559     20    436  -1417       C  
ATOM   4799  C   LEU C  13     -24.753 -29.888  35.528  1.00 62.31           C  
ANISOU 4799  C   LEU C  13     7406   7098   9170    210    494  -1548       C  
ATOM   4800  O   LEU C  13     -23.997 -30.032  36.489  1.00 60.83           O  
ANISOU 4800  O   LEU C  13     7225   6894   8993    400    575  -1479       O  
ATOM   4801  CB  LEU C  13     -26.693 -28.333  35.866  1.00 64.76           C  
ANISOU 4801  CB  LEU C  13     7493   7584   9531    -18    399  -1304       C  
ATOM   4802  CG  LEU C  13     -26.368 -27.406  34.693  1.00 63.52           C  
ANISOU 4802  CG  LEU C  13     7317   7625   9195    -71    321  -1422       C  
ATOM   4803  CD1 LEU C  13     -26.982 -27.933  33.405  1.00 64.66           C  
ANISOU 4803  CD1 LEU C  13     7523   7712   9333   -253    204  -1564       C  
ATOM   4804  CD2 LEU C  13     -26.845 -25.990  34.978  1.00 63.18           C  
ANISOU 4804  CD2 LEU C  13     7141   7764   9102    -89    297  -1283       C  
ATOM   4805  OXT LEU C  13     -24.251 -29.824  34.406  1.00 62.89           O  
ANISOU 4805  OXT LEU C  13     7526   7244   9127    182    462  -1727       O  
TER    4806      LEU C  13                                                      
ATOM   4807  N   GLY D   7      -6.749  23.000  41.190  1.00105.43           N  
ANISOU 4807  N   GLY D   7    16410  10573  13077  -5256   3192  -2427       N  
ATOM   4808  CA  GLY D   7      -6.729  21.758  41.940  1.00102.10           C  
ANISOU 4808  CA  GLY D   7    15659  10493  12641  -5117   3028  -2566       C  
ATOM   4809  C   GLY D   7      -8.045  21.011  41.854  1.00 98.47           C  
ANISOU 4809  C   GLY D   7    15282   9974  12160  -4772   2984  -2422       C  
ATOM   4810  O   GLY D   7      -8.175  19.900  42.368  1.00 95.65           O  
ANISOU 4810  O   GLY D   7    14666   9889  11787  -4631   2858  -2506       O  
ATOM   4811  N   ARG D   8      -9.024  21.624  41.197  1.00115.17           N  
ANISOU 4811  N   ARG D   8    17754  11730  14275  -4626   3084  -2200       N  
ATOM   4812  CA  ARG D   8     -10.351  21.033  41.067  1.00112.71           C  
ANISOU 4812  CA  ARG D   8    17548  11320  13958  -4285   3049  -2042       C  
ATOM   4813  C   ARG D   8     -10.378  19.911  40.033  1.00110.77           C  
ANISOU 4813  C   ARG D   8    17098  11316  13675  -4249   3049  -1899       C  
ATOM   4814  O   ARG D   8      -9.631  19.932  39.055  1.00112.87           O  
ANISOU 4814  O   ARG D   8    17284  11696  13906  -4448   3131  -1828       O  
ATOM   4815  CB  ARG D   8     -11.382  22.106  40.711  1.00114.87           C  
ANISOU 4815  CB  ARG D   8    18259  11135  14252  -4113   3141  -1836       C  
ATOM   4816  CG  ARG D   8     -11.063  22.871  39.437  1.00117.51           C  
ANISOU 4816  CG  ARG D   8    18781  11308  14562  -4273   3278  -1636       C  
ATOM   4817  CD  ARG D   8     -12.103  23.943  39.163  1.00119.60           C  
ANISOU 4817  CD  ARG D   8    19471  11124  14848  -4066   3345  -1432       C  
ATOM   4818  NE  ARG D   8     -13.444  23.383  39.028  1.00117.39           N  
ANISOU 4818  NE  ARG D   8    19268  10761  14575  -3685   3287  -1253       N  
ATOM   4819  CZ  ARG D   8     -14.526  24.098  38.739  1.00118.11           C  
ANISOU 4819  CZ  ARG D   8    19679  10506  14691  -3416   3316  -1045       C  
ATOM   4820  NH1 ARG D   8     -14.428  25.407  38.553  1.00121.88           N  
ANISOU 4820  NH1 ARG D   8    20446  10678  15185  -3492   3407   -991       N  
ATOM   4821  NH2 ARG D   8     -15.708  23.505  38.636  1.00115.50           N  
ANISOU 4821  NH2 ARG D   8    19367  10141  14377  -3062   3251   -888       N  
ATOM   4822  N   ARG D   9     -11.248  18.932  40.261  1.00 84.61           N  
ANISOU 4822  N   ARG D   9    13697   8088  10362  -3979   2957  -1860       N  
ATOM   4823  CA  ARG D   9     -11.387  17.790  39.366  1.00 82.49           C  
ANISOU 4823  CA  ARG D   9    13182   8124  10036  -3827   2902  -1700       C  
ATOM   4824  C   ARG D   9     -12.832  17.652  38.899  1.00 81.52           C  
ANISOU 4824  C   ARG D   9    13225   7854   9894  -3428   2857  -1429       C  
ATOM   4825  O   ARG D   9     -13.759  17.829  39.690  1.00 80.37           O  
ANISOU 4825  O   ARG D   9    13191   7558   9786  -3159   2795  -1427       O  
ATOM   4826  CB  ARG D   9     -10.940  16.507  40.075  1.00 79.90           C  
ANISOU 4826  CB  ARG D   9    12427   8234   9698  -3750   2747  -1877       C  
ATOM   4827  CG  ARG D   9     -11.233  15.226  39.307  1.00 79.51           C  
ANISOU 4827  CG  ARG D   9    12131   8481   9596  -3535   2671  -1731       C  
ATOM   4828  CD  ARG D   9     -10.899  13.994  40.128  1.00 78.45           C  
ANISOU 4828  CD  ARG D   9    11620   8726   9462  -3416   2514  -1897       C  
ATOM   4829  NE  ARG D   9      -9.469  13.887  40.399  1.00 78.08           N  
ANISOU 4829  NE  ARG D   9    11327   8906   9431  -3736   2526  -2128       N  
ATOM   4830  CZ  ARG D   9      -8.610  13.235  39.623  1.00 77.30           C  
ANISOU 4830  CZ  ARG D   9    10973   9080   9318  -3883   2564  -2143       C  
ATOM   4831  NH1 ARG D   9      -9.034  12.630  38.522  1.00 76.27           N  
ANISOU 4831  NH1 ARG D   9    10825   9017   9136  -3745   2593  -1947       N  
ATOM   4832  NH2 ARG D   9      -7.325  13.189  39.948  1.00 77.19           N  
ANISOU 4832  NH2 ARG D   9    10713   9276   9338  -4165   2571  -2362       N  
ATOM   4833  N   PRO D  10     -13.029  17.347  37.606  1.00 60.65           N  
ANISOU 4833  N   PRO D  10    10595   5261   7187  -3388   2888  -1203       N  
ATOM   4834  CA  PRO D  10     -14.372  17.116  37.064  1.00 58.34           C  
ANISOU 4834  CA  PRO D  10    10416   4879   6872  -3015   2815   -944       C  
ATOM   4835  C   PRO D  10     -15.082  15.964  37.768  1.00 53.64           C  
ANISOU 4835  C   PRO D  10     9548   4535   6297  -2683   2641   -984       C  
ATOM   4836  O   PRO D  10     -14.434  15.129  38.399  1.00 51.83           O  
ANISOU 4836  O   PRO D  10     9015   4608   6069  -2742   2573  -1174       O  
ATOM   4837  CB  PRO D  10     -14.098  16.743  35.605  1.00 58.64           C  
ANISOU 4837  CB  PRO D  10    10429   5045   6805  -3107   2860   -767       C  
ATOM   4838  CG  PRO D  10     -12.797  17.390  35.291  1.00 62.71           C  
ANISOU 4838  CG  PRO D  10    10997   5523   7307  -3547   3032   -872       C  
ATOM   4839  CD  PRO D  10     -11.997  17.306  36.556  1.00 62.77           C  
ANISOU 4839  CD  PRO D  10    10796   5658   7396  -3707   3005  -1180       C  
ATOM   4840  N   TYR D  11     -16.405  15.931  37.663  1.00 64.54           N  
ANISOU 4840  N   TYR D  11    11035   5787   7700  -2335   2571   -800       N  
ATOM   4841  CA  TYR D  11     -17.196  14.856  38.248  1.00 63.78           C  
ANISOU 4841  CA  TYR D  11    10693   5909   7631  -2021   2423   -807       C  
ATOM   4842  C   TYR D  11     -18.048  14.189  37.175  1.00 64.03           C  
ANISOU 4842  C   TYR D  11    10668   6038   7621  -1803   2336   -568       C  
ATOM   4843  O   TYR D  11     -18.812  13.265  37.455  1.00 63.06           O  
ANISOU 4843  O   TYR D  11    10346   6088   7526  -1546   2214   -537       O  
ATOM   4844  CB  TYR D  11     -18.075  15.386  39.384  1.00 61.50           C  
ANISOU 4844  CB  TYR D  11    10535   5406   7427  -1787   2414   -844       C  
ATOM   4845  CG  TYR D  11     -18.931  16.576  39.008  1.00 62.46           C  
ANISOU 4845  CG  TYR D  11    11015   5128   7590  -1659   2488   -658       C  
ATOM   4846  CD1 TYR D  11     -18.447  17.873  39.134  1.00 63.08           C  
ANISOU 4846  CD1 TYR D  11    11404   4878   7687  -1872   2626   -716       C  
ATOM   4847  CD2 TYR D  11     -20.225  16.403  38.533  1.00 62.78           C  
ANISOU 4847  CD2 TYR D  11    11081   5114   7660  -1321   2413   -425       C  
ATOM   4848  CE1 TYR D  11     -19.225  18.963  38.793  1.00 64.28           C  
ANISOU 4848  CE1 TYR D  11    11902   4640   7882  -1735   2696   -539       C  
ATOM   4849  CE2 TYR D  11     -21.011  17.488  38.189  1.00 63.52           C  
ANISOU 4849  CE2 TYR D  11    11492   4844   7798  -1174   2469   -247       C  
ATOM   4850  CZ  TYR D  11     -20.506  18.765  38.322  1.00 64.33           C  
ANISOU 4850  CZ  TYR D  11    11921   4607   7916  -1372   2614   -300       C  
ATOM   4851  OH  TYR D  11     -21.285  19.847  37.982  1.00 65.54           O  
ANISOU 4851  OH  TYR D  11    12410   4374   8119  -1207   2673   -114       O  
ATOM   4852  N   ILE D  12     -17.902  14.665  35.943  1.00 65.29           N  
ANISOU 4852  N   ILE D  12    11013   6086   7708  -1921   2400   -400       N  
ATOM   4853  CA  ILE D  12     -18.653  14.134  34.813  1.00 65.94           C  
ANISOU 4853  CA  ILE D  12    11082   6251   7722  -1744   2310   -172       C  
ATOM   4854  C   ILE D  12     -17.761  13.311  33.891  1.00 66.15           C  
ANISOU 4854  C   ILE D  12    10939   6563   7631  -1948   2321   -199       C  
ATOM   4855  O   ILE D  12     -16.860  13.846  33.247  1.00 67.04           O  
ANISOU 4855  O   ILE D  12    11179   6623   7671  -2234   2456   -202       O  
ATOM   4856  CB  ILE D  12     -19.301  15.266  33.992  1.00 65.30           C  
ANISOU 4856  CB  ILE D  12    11368   5831   7612  -1680   2358     75       C  
ATOM   4857  CG1 ILE D  12     -20.303  16.042  34.849  1.00 65.56           C  
ANISOU 4857  CG1 ILE D  12    11562   5576   7772  -1420   2346    117       C  
ATOM   4858  CG2 ILE D  12     -19.974  14.705  32.750  1.00 65.57           C  
ANISOU 4858  CG2 ILE D  12    11390   5981   7542  -1532   2248    303       C  
ATOM   4859  CD1 ILE D  12     -20.927  17.225  34.140  1.00 66.42           C  
ANISOU 4859  CD1 ILE D  12    12048   5318   7871  -1332   2395    358       C  
ATOM   4860  N   LEU D  13     -18.013  12.007  33.833  1.00 91.66           N  
ANISOU 4860  N   LEU D  13    13889  10091  10849  -1804   2194   -223       N  
ATOM   4861  CA  LEU D  13     -17.275  11.131  32.931  1.00 91.04           C  
ANISOU 4861  CA  LEU D  13    13650  10283  10658  -1952   2202   -250       C  
ATOM   4862  C   LEU D  13     -18.206  10.543  31.875  1.00 91.25           C  
ANISOU 4862  C   LEU D  13    13696  10379  10598  -1754   2082    -46       C  
ATOM   4863  O   LEU D  13     -17.760  10.013  30.858  1.00 90.16           O  
ANISOU 4863  O   LEU D  13    13525  10404  10331  -1863   2100    -17       O  
ATOM   4864  CB  LEU D  13     -16.575  10.007  33.701  1.00 86.74           C  
ANISOU 4864  CB  LEU D  13    12755  10043  10159  -1985   2160   -480       C  
ATOM   4865  CG  LEU D  13     -17.375   8.734  33.993  1.00 85.05           C  
ANISOU 4865  CG  LEU D  13    12309  10025   9982  -1710   1992   -471       C  
ATOM   4866  CD1 LEU D  13     -16.453   7.630  34.488  1.00 82.88           C  
ANISOU 4866  CD1 LEU D  13    11722  10048   9722  -1783   1974   -679       C  
ATOM   4867  CD2 LEU D  13     -18.482   8.995  35.002  1.00 86.02           C  
ANISOU 4867  CD2 LEU D  13    12468   9996  10221  -1455   1914   -431       C  
ATOM   4868  OXT LEU D  13     -19.428  10.585  32.018  1.00 88.83           O  
ANISOU 4868  OXT LEU D  13    13432   9973  10348  -1481   1962     86       O  
TER    4869      LEU D  13                                                      
CONECT  656 1254                                                                
CONECT 1254  656                                                                
CONECT 3020 3656                                                                
CONECT 3656 3020                                                                
MASTER      349    0    0   23    4    0    0    9 4865    4    4   54          
END