HEADER    MEMBRANE PROTEIN/ANTAGONIST             13-APR-18   6D26              
TITLE     CRYSTAL STRUCTURE OF THE PROSTAGLANDIN D2 RECEPTOR CRTH2 WITH         
TITLE    2 FEVIPIPRANT                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN D2 RECEPTOR 2, ENDOLYSIN CHIMERA;            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CRTH2 (UNP RESIDUES 1-236), T4 LIGASE (UNP RESIDUES 2-12,  
COMPND   5 61-161), CRTH2 (UNP RESIDUES 238-339);                               
COMPND   6 SYNONYM: CHEMOATTRACTANT RECEPTOR-HOMOLOGOUS MOLECULE EXPRESSED ON   
COMPND   7 TH2 CELLS,G-PROTEIN COUPLED RECEPTOR 44,LYSIS PROTEIN,LYSOZYME,      
COMPND   8 MURAMIDASE;                                                          
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          
SOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            
SOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   5 GENE: PTGDR2, CRTH2, DL1R, GPR44, E, T4TP126;                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9                                     
KEYWDS    GPCR, MEMBRANE PROTEIN-ANTAGONIST COMPLEX                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.WANG,D.YAO,K.DEEPAK,H.LIU,W.GONG,H.FAN,Z.WEI,C.ZHANG                
REVDAT   3   08-JAN-20 6D26    1       REMARK                                   
REVDAT   2   17-APR-19 6D26    1       JRNL                                     
REVDAT   1   03-OCT-18 6D26    0                                                
JRNL        AUTH   L.WANG,D.YAO,R.N.V.K.DEEPAK,H.LIU,Q.XIAO,H.FAN,W.GONG,Z.WEI, 
JRNL        AUTH 2 C.ZHANG                                                      
JRNL        TITL   STRUCTURES OF THE HUMAN PGD2RECEPTOR CRTH2 REVEAL NOVEL      
JRNL        TITL 2 MECHANISMS FOR LIGAND RECOGNITION.                           
JRNL        REF    MOL. CELL                     V.  72    48 2018              
JRNL        REFN                   ISSN 1097-4164                               
JRNL        PMID   30220562                                                     
JRNL        DOI    10.1016/J.MOLCEL.2018.08.009                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.33                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 19525                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.252                           
REMARK   3   R VALUE            (WORKING SET) : 0.250                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 973                             
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 29.3348 -  5.3436    0.89     2767   147  0.2196 0.2553        
REMARK   3     2  5.3436 -  4.2455    0.91     2653   140  0.2266 0.2460        
REMARK   3     3  4.2455 -  3.7100    0.96     2783   143  0.2351 0.2631        
REMARK   3     4  3.7100 -  3.3713    0.98     2799   149  0.2682 0.2696        
REMARK   3     5  3.3713 -  3.1300    0.96     2780   146  0.3095 0.3455        
REMARK   3     6  3.1300 -  2.9456    0.92     2589   136  0.3329 0.3880        
REMARK   3     7  2.9456 -  2.7982    0.77     2181   112  0.3589 0.4439        
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)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.660           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.26                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 84.99                          
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      :  0.002           3715                                  
REMARK   3   ANGLE     :  0.594           5042                                  
REMARK   3   CHIRALITY :  0.019            568                                  
REMARK   3   PLANARITY :  0.003            629                                  
REMARK   3   DIHEDRAL  : 11.100           1331                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 1241 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0147  82.2726 292.5409              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4561 T22:   0.5577                                     
REMARK   3      T33:   0.5069 T12:  -0.0188                                     
REMARK   3      T13:  -0.0205 T23:  -0.0964                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2941 L22:   1.8104                                     
REMARK   3      L33:   4.3495 L12:  -0.2713                                     
REMARK   3      L13:  -0.6671 L23:   0.3954                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0373 S12:   0.5648 S13:  -0.1754                       
REMARK   3      S21:  -0.2451 S22:   0.0814 S23:  -0.0850                       
REMARK   3      S31:   0.0602 S32:   0.1481 S33:  -0.0170                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1242 THROUGH 2327 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.2173  82.2904 318.7889              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5107 T22:   0.4026                                     
REMARK   3      T33:   0.5720 T12:   0.0655                                     
REMARK   3      T13:  -0.0559 T23:  -0.0222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7385 L22:   1.7285                                     
REMARK   3      L33:   5.0665 L12:   0.5316                                     
REMARK   3      L13:  -1.6705 L23:  -1.3274                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0244 S12:  -0.0964 S13:   0.0307                       
REMARK   3      S21:   0.2181 S22:   0.1474 S23:   0.0996                       
REMARK   3      S31:  -0.2918 S32:  -0.3313 S33:  -0.2070                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6D26 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000233838.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUN-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19625                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.18300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 6C1Q                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, PH 6.5, 100 MM AMMONIUM      
REMARK 280  SULFATE, 30% PEG400, 2% P400, 1 MM SUCCINIC ACID, LIPIDIC CUBIC     
REMARK 280  PHASE, TEMPERATURE 289K                                             
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       25.22850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      133.25850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.85500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      133.25850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.22850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.85500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     VAL A  2328                                                      
REMARK 465     ASP A  2329                                                      
REMARK 465     ASP A  2330                                                      
REMARK 465     SER A  2331                                                      
REMARK 465     GLU A  2332                                                      
REMARK 465     LEU A  2333                                                      
REMARK 465     GLY A  2334                                                      
REMARK 465     GLY A  2335                                                      
REMARK 465     ALA A  2336                                                      
REMARK 465     GLY A  2337                                                      
REMARK 465     SER A  2338                                                      
REMARK 465     SER A  2339                                                      
REMARK 465     LEU A  2340                                                      
REMARK 465     GLU A  2341                                                      
REMARK 465     VAL A  2342                                                      
REMARK 465     LEU A  2343                                                      
REMARK 465     PHE A  2344                                                      
REMARK 465     GLN A  2345                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A  23    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A  24    OG                                                  
REMARK 470     TYR A  30    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A1247    CG1  CG2  CD1                                       
REMARK 470     ASP A1262    CG   OD1  OD2                                       
REMARK 470     ARG A1281    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A2327    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  25       85.62     57.75                                   
REMARK 500    CYS A  59      -38.10   -130.07                                   
REMARK 500    ASN A 190       70.52     49.44                                   
REMARK 500    PHE A 215      -67.04   -153.82                                   
REMARK 500    ASN A1246       42.02    -95.72                                   
REMARK 500    ASP A1271       91.99    -63.38                                   
REMARK 500    ASN A1317       35.27    -82.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FSY A 2401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2402                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2403                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2404                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2405                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2406                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2407                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2408                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2409                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2410                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SIN A 2411                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SIN A 2412                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SIN A 2413                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SIN A 2414                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SIN A 2415                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 2416                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2417                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGO A 2418                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6D27   RELATED DB: PDB                                   
DBREF  6D26 A    1   236  UNP    Q9Y5Y4   PD2R2_HUMAN      1    236             
DBREF  6D26 A 1246  1256  UNP    D9IEF7   D9IEF7_BPT4      2     12             
DBREF  6D26 A 1262  1362  UNP    D9IEF7   D9IEF7_BPT4     61    161             
DBREF  6D26 A 2238  2339  UNP    Q9Y5Y4   PD2R2_HUMAN    238    339             
SEQADV 6D26 GLY A    0  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQADV 6D26 ALA A   25  UNP  Q9Y5Y4    ASN    25 ENGINEERED MUTATION            
SEQADV 6D26 ALA A  204  UNP  Q9Y5Y4    VAL   204 VARIANT                        
SEQADV 6D26 ALA A 1238  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D26 ASP A 1239  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D26 LEU A 1240  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D26 GLY A 1241  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D26 LEU A 1242  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D26 GLN A 1243  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D26 HIS A 1244  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D26 ARG A 1245  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D26 GLY A 1257  UNP  D9IEF7              INSERTION                      
SEQADV 6D26 GLY A 1258  UNP  D9IEF7              INSERTION                      
SEQADV 6D26 SER A 1259  UNP  D9IEF7              INSERTION                      
SEQADV 6D26 GLY A 1260  UNP  D9IEF7              INSERTION                      
SEQADV 6D26 GLY A 1261  UNP  D9IEF7              INSERTION                      
SEQADV 6D26 ALA A 1298  UNP  D9IEF7    CYS    97 ENGINEERED MUTATION            
SEQADV 6D26 LEU A 2340  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQADV 6D26 GLU A 2341  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQADV 6D26 VAL A 2342  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQADV 6D26 LEU A 2343  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQADV 6D26 PHE A 2344  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQADV 6D26 GLN A 2345  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQRES   1 A  470  GLY MET SER ALA ASN ALA THR LEU LYS PRO LEU CYS PRO          
SEQRES   2 A  470  ILE LEU GLU GLN MET SER ARG LEU GLN SER HIS SER ALA          
SEQRES   3 A  470  THR SER ILE ARG TYR ILE ASP HIS ALA ALA VAL LEU LEU          
SEQRES   4 A  470  HIS GLY LEU ALA SER LEU LEU GLY LEU VAL GLU ASN GLY          
SEQRES   5 A  470  VAL ILE LEU PHE VAL VAL GLY CYS ARG MET ARG GLN THR          
SEQRES   6 A  470  VAL VAL THR THR TRP VAL LEU HIS LEU ALA LEU SER ASP          
SEQRES   7 A  470  LEU LEU ALA SER ALA SER LEU PRO PHE PHE THR TYR PHE          
SEQRES   8 A  470  LEU ALA VAL GLY HIS SER TRP GLU LEU GLY THR THR PHE          
SEQRES   9 A  470  CYS LYS LEU HIS SER SER ILE PHE PHE LEU ASN MET PHE          
SEQRES  10 A  470  ALA SER GLY PHE LEU LEU SER ALA ILE SER LEU ASP ARG          
SEQRES  11 A  470  CYS LEU GLN VAL VAL ARG PRO VAL TRP ALA GLN ASN HIS          
SEQRES  12 A  470  ARG THR VAL ALA ALA ALA HIS LYS VAL CYS LEU VAL LEU          
SEQRES  13 A  470  TRP ALA LEU ALA VAL LEU ASN THR VAL PRO TYR PHE VAL          
SEQRES  14 A  470  PHE ARG ASP THR ILE SER ARG LEU ASP GLY ARG ILE MET          
SEQRES  15 A  470  CYS TYR TYR ASN VAL LEU LEU LEU ASN PRO GLY PRO ASP          
SEQRES  16 A  470  ARG ASP ALA THR CYS ASN SER ARG GLN ALA ALA LEU ALA          
SEQRES  17 A  470  VAL SER LYS PHE LEU LEU ALA PHE LEU VAL PRO LEU ALA          
SEQRES  18 A  470  ILE ILE ALA SER SER HIS ALA ALA VAL SER LEU ARG LEU          
SEQRES  19 A  470  GLN HIS ARG ALA ASP LEU GLY LEU GLN HIS ARG ASN ILE          
SEQRES  20 A  470  PHE GLU MET LEU ARG ILE ASP GLU GLY GLY GLY SER GLY          
SEQRES  21 A  470  GLY ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP          
SEQRES  22 A  470  ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS          
SEQRES  23 A  470  PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA          
SEQRES  24 A  470  LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL          
SEQRES  25 A  470  ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS          
SEQRES  26 A  470  ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG          
SEQRES  27 A  470  TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE          
SEQRES  28 A  470  THR THR PHE ARG THR GLY THR TRP ASP ALA TYR ARG ARG          
SEQRES  29 A  470  ARG PRO GLY ARG PHE VAL ARG LEU VAL ALA ALA VAL VAL          
SEQRES  30 A  470  ALA ALA PHE ALA LEU CYS TRP GLY PRO TYR HIS VAL PHE          
SEQRES  31 A  470  SER LEU LEU GLU ALA ARG ALA HIS ALA ASN PRO GLY LEU          
SEQRES  32 A  470  ARG PRO LEU VAL TRP ARG GLY LEU PRO PHE VAL THR SER          
SEQRES  33 A  470  LEU ALA PHE PHE ASN SER VAL ALA ASN PRO VAL LEU TYR          
SEQRES  34 A  470  VAL LEU THR YCM PRO ASP MET LEU ARG LYS LEU ARG ARG          
SEQRES  35 A  470  SER LEU ARG THR VAL LEU GLU SER VAL LEU VAL ASP ASP          
SEQRES  36 A  470  SER GLU LEU GLY GLY ALA GLY SER SER LEU GLU VAL LEU          
SEQRES  37 A  470  PHE GLN                                                      
MODRES 6D26 YCM A 2308  CYS  MODIFIED RESIDUE                                   
HET    YCM  A2308      10                                                       
HET    FSY  A2401      29                                                       
HET    SO4  A2402       5                                                       
HET    SO4  A2403       5                                                       
HET    SO4  A2404       5                                                       
HET    SO4  A2405       5                                                       
HET    SO4  A2406       5                                                       
HET    SO4  A2407       5                                                       
HET    SO4  A2408       5                                                       
HET    SO4  A2409       5                                                       
HET    SO4  A2410       5                                                       
HET    SIN  A2411       8                                                       
HET    SIN  A2412       8                                                       
HET    SIN  A2413       8                                                       
HET    SIN  A2414       8                                                       
HET    SIN  A2415       8                                                       
HET    PGE  A2416      10                                                       
HET    OLA  A2417      20                                                       
HET    PGO  A2418       5                                                       
HETNAM     YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                                
HETNAM     FSY FEVIPIPRANT                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     SIN SUCCINIC ACID                                                    
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     OLA OLEIC ACID                                                       
HETNAM     PGO S-1,2-PROPANEDIOL                                                
HETSYN     YCM CYSTEINE-S-ACETAMIDE                                             
HETSYN     FSY (2-METHYL-1-{[4-(METHYLSULFONYL)-2-(TRIFLUOROMETHYL)             
HETSYN   2 FSY  PHENYL]METHYL}-1H-PYRROLO[2,3-B]PYRIDIN-3-YL)ACETIC             
HETSYN   3 FSY  ACID                                                            
FORMUL   1  YCM    C5 H10 N2 O3 S                                               
FORMUL   2  FSY    C19 H17 F3 N2 O4 S                                           
FORMUL   3  SO4    9(O4 S 2-)                                                   
FORMUL  12  SIN    5(C4 H6 O4)                                                  
FORMUL  17  PGE    C6 H14 O4                                                    
FORMUL  18  OLA    C18 H34 O2                                                   
FORMUL  19  PGO    C3 H8 O2                                                     
FORMUL  20  HOH   *3(H2 O)                                                      
HELIX    1 AA1 CYS A   11  SER A   18  1                                   8    
HELIX    2 AA2 ASP A   32  ARG A   60  1                                  29    
HELIX    3 AA3 THR A   64  VAL A   93  1                                  30    
HELIX    4 AA4 THR A  101  ARG A  135  1                                  35    
HELIX    5 AA5 ARG A  135  ARG A  143  1                                   9    
HELIX    6 AA6 THR A  144  ASN A  162  1                                  19    
HELIX    7 AA7 THR A  163  PHE A  169  1                                   7    
HELIX    8 AA8 VAL A  186  LEU A  189  5                                   4    
HELIX    9 AA9 ASP A  194  ALA A  214  1                                  21    
HELIX   10 AB1 PHE A  215  LEU A 1242  1                                  27    
HELIX   11 AB2 GLN A 1243  ILE A 1247  5                                   5    
HELIX   12 AB3 ILE A 1253  GLY A 1257  5                                   5    
HELIX   13 AB4 ASP A 1271  ASN A 1282  1                                  12    
HELIX   14 AB5 LEU A 1285  SER A 1291  1                                   7    
HELIX   15 AB6 ASP A 1293  GLY A 1308  1                                  16    
HELIX   16 AB7 GLY A 1308  ALA A 1313  1                                   6    
HELIX   17 AB8 PHE A 1315  GLN A 1324  1                                  10    
HELIX   18 AB9 ARG A 1326  ALA A 1335  1                                  10    
HELIX   19 AC1 SER A 1337  THR A 1343  1                                   7    
HELIX   20 AC2 THR A 1343  GLY A 1357  1                                  15    
HELIX   21 AC3 PHE A 2244  TRP A 2259  1                                  16    
HELIX   22 AC4 TRP A 2259  ALA A 2272  1                                  14    
HELIX   23 AC5 ASN A 2275  GLY A 2277  5                                   3    
HELIX   24 AC6 LEU A 2278  TRP A 2283  1                                   6    
HELIX   25 AC7 GLY A 2285  PHE A 2295  1                                  11    
HELIX   26 AC8 PHE A 2295  YCM A 2308  1                                  14    
HELIX   27 AC9 YCM A 2308  GLU A 2324  1                                  17    
SHEET    1 AA1 2 ARG A 170  SER A 174  0                                        
SHEET    2 AA1 2 ILE A 180  TYR A 184 -1  O  MET A 181   N  ILE A 173           
SSBOND   1 CYS A   11    CYS A  199                          1555   1555  2.03  
SSBOND   2 CYS A  104    CYS A  182                          1555   1555  2.03  
LINK         C   THR A2307                 N   YCM A2308     1555   1555  1.33  
LINK         C   YCM A2308                 N   PRO A2309     1555   1555  1.34  
SITE     1 AC1 16 MET A  17  PHE A  87  PHE A  90  HIS A  95                    
SITE     2 AC1 16 PHE A 111  PHE A 112  ARG A 170  ARG A 175                    
SITE     3 AC1 16 MET A 181  CYS A 182  TYR A 183  TYR A 184                    
SITE     4 AC1 16 TYR A2262  TRP A2283  PRO A2287  THR A2290                    
SITE     1 AC2  8 GLN A 140  MET A1250  LEU A1251  ARG A1349                    
SITE     2 AC2  8 TRP A1359  ALA A1361  TYR A1362  ARG A2238                    
SITE     1 AC3  7 GLY A1314  PHE A1315  THR A1316  ASN A1317                    
SITE     2 AC3  7 SER A1318  ASN A1333  ARG A2239                               
SITE     1 AC4  9 ARG A1320  GLN A1324  ARG A1326  GLY A2242                    
SITE     2 AC4  9 ARG A2243  PHE A2244  VAL A2245  ARG A2246                    
SITE     3 AC4  9 YCM A2308                                                     
SITE     1 AC5  3 MET A  61  ARG A  62  LYS A2314                               
SITE     1 AC6  7 THR A  64  VAL A  65  VAL A  66  GLN A 132                    
SITE     2 AC6  7 ARG A 143  ARG A2240  ARG A2243                               
SITE     1 AC7  6 THR A 144  VAL A 145  THR A1343  PRO A1344                    
SITE     2 AC7  6 ASN A1345  ARG A1346                                          
SITE     1 AC8  4 ARG A 135  GLY A1256  GLY A1257  LYS A1266                    
SITE     1 AC9  2 ALA A1274  ARG A1277                                          
SITE     1 AD1  1 ARG A1297                                                     
SITE     1 AD2  3 PHE A 120  LEU A 127  LEU A 155                               
SITE     1 AD3  5 ARG A1320  ARG A2246  YCM A2308  PRO A2309                    
SITE     2 AD3  5 ASP A2310                                                     
SITE     1 AD4  2 ARG A 175  ARG A 179                                          
SITE     1 AD5  4 HIS A 142  THR A 144  ARG A1346  LEU A2327                    
SITE     1 AD6  2 SER A1337  ARG A1338                                          
SITE     1 AD7  3 GLU A1249  MET A1250  LEU A1251                               
SITE     1 AD8  6 LEU A  47  GLY A  51  PHE A  55  GLY A  58                    
SITE     2 AD8  6 CYS A  59  HIS A 149                                          
SITE     1 AD9  1 ASP A 128                                                     
CRYST1   50.457   61.710  266.517  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019819  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016205  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003752        0.00000                         
ATOM      1  N   ALA A   5       1.714  67.483 261.031  1.00123.14           N  
ANISOU    1  N   ALA A   5    16717  20114   9958   -561    214  -6008       N  
ATOM      2  CA  ALA A   5       1.503  68.925 261.033  1.00120.00           C  
ANISOU    2  CA  ALA A   5    16133  20041   9419   -545    139  -5658       C  
ATOM      3  C   ALA A   5       0.113  69.274 261.549  1.00119.41           C  
ANISOU    3  C   ALA A   5    15940  19995   9434   -722   -124  -5559       C  
ATOM      4  O   ALA A   5      -0.894  68.813 261.013  1.00116.84           O  
ANISOU    4  O   ALA A   5    15641  19739   9013   -870   -300  -5706       O  
ATOM      5  CB  ALA A   5       1.709  69.493 259.639  1.00121.47           C  
ANISOU    5  CB  ALA A   5    16342  20622   9190   -480    166  -5579       C  
ATOM      6  N   THR A   6       0.065  70.089 262.597  1.00123.80           N  
ANISOU    6  N   THR A   6    16356  20511  10173   -704   -147  -5310       N  
ATOM      7  CA  THR A   6      -1.201  70.497 263.194  1.00125.88           C  
ANISOU    7  CA  THR A   6    16485  20804  10539   -845   -381  -5189       C  
ATOM      8  C   THR A   6      -1.284  72.014 263.328  1.00128.25           C  
ANISOU    8  C   THR A   6    16641  21376  10711   -758   -431  -4806       C  
ATOM      9  O   THR A   6      -0.279  72.683 263.570  1.00129.79           O  
ANISOU    9  O   THR A   6    16827  21591  10897   -624   -260  -4628       O  
ATOM     10  CB  THR A   6      -1.405  69.860 264.584  1.00126.86           C  
ANISOU   10  CB  THR A   6    16600  20527  11074   -935   -386  -5281       C  
ATOM     11  OG1 THR A   6      -0.332  70.245 265.453  1.00127.65           O  
ANISOU   11  OG1 THR A   6    16680  20476  11346   -789   -206  -5152       O  
ATOM     12  CG2 THR A   6      -1.446  68.342 264.478  1.00129.81           C  
ANISOU   12  CG2 THR A   6    17153  20592  11578  -1031   -345  -5639       C  
ATOM     13  N   LEU A   7      -2.489  72.551 263.168  1.00123.83           N  
ANISOU   13  N   LEU A   7    15972  21025  10053   -833   -661  -4676       N  
ATOM     14  CA  LEU A   7      -2.712  73.986 263.294  1.00116.66           C  
ANISOU   14  CA  LEU A   7    14954  20352   9020   -735   -730  -4299       C  
ATOM     15  C   LEU A   7      -3.636  74.298 264.466  1.00110.22           C  
ANISOU   15  C   LEU A   7    13992  19431   8458   -808   -890  -4183       C  
ATOM     16  O   LEU A   7      -4.703  73.700 264.602  1.00113.04           O  
ANISOU   16  O   LEU A   7    14279  19752   8919   -953  -1059  -4331       O  
ATOM     17  CB  LEU A   7      -3.296  74.555 261.999  1.00114.86           C  
ANISOU   17  CB  LEU A   7    14722  20509   8410   -690   -858  -4183       C  
ATOM     18  CG  LEU A   7      -3.599  76.054 262.003  1.00111.40           C  
ANISOU   18  CG  LEU A   7    14209  20306   7811   -561   -935  -3769       C  
ATOM     19  CD1 LEU A   7      -2.316  76.864 262.111  1.00111.98           C  
ANISOU   19  CD1 LEU A   7    14361  20365   7823   -430   -697  -3538       C  
ATOM     20  CD2 LEU A   7      -4.387  76.452 260.768  1.00112.95           C  
ANISOU   20  CD2 LEU A   7    14402  20857   7658   -516  -1099  -3685       C  
ATOM     21  N   LYS A   8      -3.219  75.234 265.312  1.00103.26           N  
ANISOU   21  N   LYS A   8    13060  18502   7671   -714   -828  -3919       N  
ATOM     22  CA  LYS A   8      -4.036  75.648 266.447  1.00 98.31           C  
ANISOU   22  CA  LYS A   8    12299  17738   7315   -751   -961  -3748       C  
ATOM     23  C   LYS A   8      -4.403  77.127 266.345  1.00 96.14           C  
ANISOU   23  C   LYS A   8    11959  17671   6899   -607  -1042  -3331       C  
ATOM     24  O   LYS A   8      -3.552  77.966 266.041  1.00 96.36           O  
ANISOU   24  O   LYS A   8    12067  17735   6812   -476   -897  -3084       O  
ATOM     25  CB  LYS A   8      -3.310  75.369 267.768  1.00 93.63           C  
ANISOU   25  CB  LYS A   8    11721  16677   7176   -747   -802  -3700       C  
ATOM     26  CG  LYS A   8      -1.964  76.066 267.910  1.00 94.43           C  
ANISOU   26  CG  LYS A   8    11884  16671   7325   -598   -576  -3462       C  
ATOM     27  CD  LYS A   8      -1.332  75.808 269.272  1.00 91.15           C  
ANISOU   27  CD  LYS A   8    11456  15830   7346   -589   -454  -3414       C  
ATOM     28  CE  LYS A   8      -0.916  74.355 269.423  1.00 88.20           C  
ANISOU   28  CE  LYS A   8    11167  15231   7115   -649   -367  -3781       C  
ATOM     29  NZ  LYS A   8      -0.214  74.117 270.712  1.00 81.58           N  
ANISOU   29  NZ  LYS A   8    10326  14003   6670   -603   -245  -3715       N  
ATOM     30  N   PRO A   9      -5.684  77.448 266.580  1.00 94.11           N  
ANISOU   30  N   PRO A   9    11560  17557   6640   -631  -1269  -3254       N  
ATOM     31  CA  PRO A   9      -6.138  78.841 266.613  1.00 93.45           C  
ANISOU   31  CA  PRO A   9    11424  17627   6455   -464  -1355  -2851       C  
ATOM     32  C   PRO A   9      -5.661  79.557 267.873  1.00 90.74           C  
ANISOU   32  C   PRO A   9    11086  16909   6483   -391  -1231  -2557       C  
ATOM     33  O   PRO A   9      -5.755  79.005 268.970  1.00 86.14           O  
ANISOU   33  O   PRO A   9    10441  16023   6263   -487  -1213  -2652       O  
ATOM     34  CB  PRO A   9      -7.663  78.715 266.592  1.00 96.83           C  
ANISOU   34  CB  PRO A   9    11667  18311   6814   -520  -1633  -2933       C  
ATOM     35  CG  PRO A   9      -7.934  77.374 267.183  1.00 98.56           C  
ANISOU   35  CG  PRO A   9    11831  18298   7320   -751  -1640  -3287       C  
ATOM     36  CD  PRO A   9      -6.796  76.497 266.747  1.00 97.13           C  
ANISOU   36  CD  PRO A   9    11827  17958   7120   -815  -1445  -3536       C  
ATOM     37  N   LEU A  10      -5.150  80.772 267.711  1.00 92.86           N  
ANISOU   37  N   LEU A  10    11440  17195   6648   -234  -1140  -2207       N  
ATOM     38  CA  LEU A  10      -4.612  81.534 268.832  1.00 88.87           C  
ANISOU   38  CA  LEU A  10    10959  16345   6461   -177  -1012  -1933       C  
ATOM     39  C   LEU A  10      -5.306  82.882 268.984  1.00 91.65           C  
ANISOU   39  C   LEU A  10    11305  16772   6746    -14  -1112  -1563       C  
ATOM     40  O   LEU A  10      -6.051  83.313 268.105  1.00101.14           O  
ANISOU   40  O   LEU A  10    12499  18312   7619     87  -1261  -1480       O  
ATOM     41  CB  LEU A  10      -3.108  81.749 268.654  1.00 90.70           C  
ANISOU   41  CB  LEU A  10    11327  16444   6691   -166   -752  -1861       C  
ATOM     42  CG  LEU A  10      -2.239  80.511 268.430  1.00 92.94           C  
ANISOU   42  CG  LEU A  10    11638  16660   7016   -269   -617  -2202       C  
ATOM     43  CD1 LEU A  10      -0.807  80.925 268.138  1.00 90.87           C  
ANISOU   43  CD1 LEU A  10    11474  16355   6698   -231   -364  -2087       C  
ATOM     44  CD2 LEU A  10      -2.299  79.584 269.634  1.00 93.77           C  
ANISOU   44  CD2 LEU A  10    11668  16433   7527   -365   -621  -2394       C  
ATOM     45  N   CYS A  11      -5.056  83.545 270.108  1.00 90.70           N  
ANISOU   45  N   CYS A  11    11197  16335   6931     24  -1032  -1345       N  
ATOM     46  CA  CYS A  11      -5.557  84.894 270.327  1.00 93.46           C  
ANISOU   46  CA  CYS A  11    11586  16682   7242    196  -1086   -981       C  
ATOM     47  C   CYS A  11      -4.744  85.877 269.494  1.00 98.10           C  
ANISOU   47  C   CYS A  11    12373  17335   7565    288   -942   -720       C  
ATOM     48  O   CYS A  11      -3.585  85.609 269.183  1.00105.19           O  
ANISOU   48  O   CYS A  11    13354  18172   8439    197   -751   -791       O  
ATOM     49  CB  CYS A  11      -5.488  85.263 271.812  1.00 89.66           C  
ANISOU   49  CB  CYS A  11    11077  15823   7167    192  -1031   -858       C  
ATOM     50  SG  CYS A  11      -6.278  84.071 272.914  1.00221.59           S  
ANISOU   50  SG  CYS A  11    27577  32403  24212     55  -1147  -1147       S  
ATOM     51  N   PRO A  12      -5.347  87.019 269.123  1.00 96.03           N  
ANISOU   51  N   PRO A  12    12193  17200   7096    476  -1023   -412       N  
ATOM     52  CA  PRO A  12      -4.617  88.049 268.372  1.00 97.08           C  
ANISOU   52  CA  PRO A  12    12552  17359   6975    559   -871   -122       C  
ATOM     53  C   PRO A  12      -3.396  88.578 269.126  1.00 96.05           C  
ANISOU   53  C   PRO A  12    12540  16849   7107    464   -619     20       C  
ATOM     54  O   PRO A  12      -2.481  89.122 268.504  1.00 95.50           O  
ANISOU   54  O   PRO A  12    12637  16785   6863    440   -435    173       O  
ATOM     55  CB  PRO A  12      -5.664  89.156 268.177  1.00 96.00           C  
ANISOU   55  CB  PRO A  12    12476  17341   6658    805  -1025    190       C  
ATOM     56  CG  PRO A  12      -6.736  88.869 269.180  1.00 92.27           C  
ANISOU   56  CG  PRO A  12    11797  16806   6455    840  -1207     95       C  
ATOM     57  CD  PRO A  12      -6.760  87.383 269.316  1.00 92.44           C  
ANISOU   57  CD  PRO A  12    11624  16895   6605    633  -1257   -320       C  
ATOM     58  N   ILE A  13      -3.389  88.417 270.446  1.00 91.96           N  
ANISOU   58  N   ILE A  13    11928  16022   6989    401   -611    -34       N  
ATOM     59  CA  ILE A  13      -2.244  88.805 271.261  1.00 87.80           C  
ANISOU   59  CA  ILE A  13    11475  15157   6728    292   -396     53       C  
ATOM     60  C   ILE A  13      -1.070  87.857 271.035  1.00 90.17           C  
ANISOU   60  C   ILE A  13    11725  15472   7065    124   -236   -197       C  
ATOM     61  O   ILE A  13       0.064  88.295 270.843  1.00 92.20           O  
ANISOU   61  O   ILE A  13    12079  15661   7293     47    -26    -95       O  
ATOM     62  CB  ILE A  13      -2.601  88.830 272.757  1.00 85.53           C  
ANISOU   62  CB  ILE A  13    11095  14565   6837    282   -447     44       C  
ATOM     63  CG1 ILE A  13      -3.703  89.856 273.021  1.00 89.83           C  
ANISOU   63  CG1 ILE A  13    11697  15083   7351    476   -580    302       C  
ATOM     64  CG2 ILE A  13      -1.373  89.142 273.598  1.00 82.25           C  
ANISOU   64  CG2 ILE A  13    10734  13835   6681    153   -240     97       C  
ATOM     65  CD1 ILE A  13      -4.101  89.962 274.478  1.00 89.67           C  
ANISOU   65  CD1 ILE A  13    11597  14780   7693    482   -621    304       C  
ATOM     66  N   LEU A  14      -1.346  86.557 271.054  1.00 87.23           N  
ANISOU   66  N   LEU A  14    11201  15189   6755     67   -328   -527       N  
ATOM     67  CA  LEU A  14      -0.312  85.555 270.815  1.00 90.44           C  
ANISOU   67  CA  LEU A  14    11565  15611   7188    -51   -186   -789       C  
ATOM     68  C   LEU A  14       0.129  85.530 269.355  1.00102.91           C  
ANISOU   68  C   LEU A  14    13234  17501   8367    -41   -103   -812       C  
ATOM     69  O   LEU A  14       1.306  85.327 269.057  1.00106.96           O  
ANISOU   69  O   LEU A  14    13768  18022   8849   -111    100   -875       O  
ATOM     70  CB  LEU A  14      -0.801  84.166 271.227  1.00 84.81           C  
ANISOU   70  CB  LEU A  14    10709  14870   6643   -108   -304  -1135       C  
ATOM     71  CG  LEU A  14      -0.425  83.690 272.630  1.00 79.10           C  
ANISOU   71  CG  LEU A  14     9904  13810   6339   -174   -257  -1224       C  
ATOM     72  CD1 LEU A  14      -1.217  84.434 273.698  1.00 76.55           C  
ANISOU   72  CD1 LEU A  14     9556  13301   6230   -127   -363  -1021       C  
ATOM     73  CD2 LEU A  14      -0.621  82.187 272.746  1.00 77.50           C  
ANISOU   73  CD2 LEU A  14     9619  13590   6240   -244   -314  -1585       C  
ATOM     74  N   GLU A  15      -0.824  85.731 268.451  1.00111.69           N  
ANISOU   74  N   GLU A  15    14385  18894   9160     55   -261   -763       N  
ATOM     75  CA  GLU A  15      -0.548  85.708 267.019  1.00119.99           C  
ANISOU   75  CA  GLU A  15    15529  20277   9784     79   -207   -782       C  
ATOM     76  C   GLU A  15       0.395  86.843 266.632  1.00127.50           C  
ANISOU   76  C   GLU A  15    16650  21200  10593     84     15   -467       C  
ATOM     77  O   GLU A  15       1.303  86.661 265.822  1.00132.90           O  
ANISOU   77  O   GLU A  15    17388  22038  11069     30    193   -525       O  
ATOM     78  CB  GLU A  15      -1.853  85.800 266.225  1.00125.14           C  
ANISOU   78  CB  GLU A  15    16180  21249  10119    199   -452   -763       C  
ATOM     79  CG  GLU A  15      -1.691  85.643 264.724  1.00131.90           C  
ANISOU   79  CG  GLU A  15    17127  22490  10500    229   -430   -824       C  
ATOM     80  CD  GLU A  15      -3.023  85.583 264.003  1.00137.50           C  
ANISOU   80  CD  GLU A  15    17793  23549  10901    341   -706   -857       C  
ATOM     81  OE1 GLU A  15      -4.070  85.645 264.682  1.00134.54           O  
ANISOU   81  OE1 GLU A  15    17297  23123  10698    392   -907   -838       O  
ATOM     82  OE2 GLU A  15      -3.024  85.472 262.759  1.00144.72           O  
ANISOU   82  OE2 GLU A  15    18782  24814  11391    380   -723   -907       O  
ATOM     83  N   GLN A  16       0.174  88.012 267.224  1.00117.11           N  
ANISOU   83  N   GLN A  16    15424  19681   9390    140     15   -139       N  
ATOM     84  CA  GLN A  16       1.052  89.157 267.023  1.00114.92           C  
ANISOU   84  CA  GLN A  16    15328  19306   9030    107    238    174       C  
ATOM     85  C   GLN A  16       2.399  88.896 267.689  1.00110.15           C  
ANISOU   85  C   GLN A  16    14652  18494   8706    -71    468     72       C  
ATOM     86  O   GLN A  16       3.432  89.422 267.271  1.00114.71           O  
ANISOU   86  O   GLN A  16    15322  19089   9173   -164    701    205       O  
ATOM     87  CB  GLN A  16       0.408  90.431 267.581  1.00114.88           C  
ANISOU   87  CB  GLN A  16    15457  19088   9103    217    172    524       C  
ATOM     88  CG  GLN A  16       1.241  91.695 267.422  1.00118.28           C  
ANISOU   88  CG  GLN A  16    16118  19364   9460    162    405    864       C  
ATOM     89  CD  GLN A  16       0.508  92.938 267.891  1.00117.36           C  
ANISOU   89  CD  GLN A  16    16177  19024   9391    303    332   1202       C  
ATOM     90  OE1 GLN A  16      -0.722  92.969 267.930  1.00114.93           O  
ANISOU   90  OE1 GLN A  16    15838  18797   9031    501     98   1231       O  
ATOM     91  NE2 GLN A  16       1.262  93.970 268.253  1.00118.67           N  
ANISOU   91  NE2 GLN A  16    16524  18909   9655    202    538   1449       N  
ATOM     92  N   MET A  17       2.375  88.059 268.720  1.00100.99           N  
ANISOU   92  N   MET A  17    13317  17158   7898   -117    402   -165       N  
ATOM     93  CA  MET A  17       3.562  87.742 269.501  1.00 94.94           C  
ANISOU   93  CA  MET A  17    12451  16201   7422   -251    581   -274       C  
ATOM     94  C   MET A  17       4.407  86.658 268.838  1.00 94.89           C  
ANISOU   94  C   MET A  17    12352  16396   7306   -299    704   -565       C  
ATOM     95  O   MET A  17       5.603  86.539 269.105  1.00 91.69           O  
ANISOU   95  O   MET A  17    11876  15937   7026   -394    903   -618       O  
ATOM     96  CB  MET A  17       3.151  87.297 270.902  1.00 93.74           C  
ANISOU   96  CB  MET A  17    12170  15775   7673   -252    454   -389       C  
ATOM     97  CG  MET A  17       4.265  87.285 271.925  1.00 94.28           C  
ANISOU   97  CG  MET A  17    12152  15612   8057   -366    608   -419       C  
ATOM     98  SD  MET A  17       3.655  86.650 273.492  1.00129.91           S  
ANISOU   98  SD  MET A  17    16533  19839  12988   -342    441   -561       S  
ATOM     99  CE  MET A  17       2.085  87.508 273.605  1.00 66.87           C  
ANISOU   99  CE  MET A  17     8651  11814   4943   -224    230   -336       C  
ATOM    100  N   SER A  18       3.780  85.872 267.970  1.00 99.67           N  
ANISOU  100  N   SER A  18    12953  17247   7670   -230    585   -763       N  
ATOM    101  CA  SER A  18       4.454  84.748 267.330  1.00104.36           C  
ANISOU  101  CA  SER A  18    13479  18019   8152   -251    686  -1078       C  
ATOM    102  C   SER A  18       5.204  85.166 266.067  1.00118.38           C  
ANISOU  102  C   SER A  18    15355  20078   9545   -267    884   -985       C  
ATOM    103  O   SER A  18       5.648  84.317 265.293  1.00123.55           O  
ANISOU  103  O   SER A  18    15983  20946  10015   -258    966  -1236       O  
ATOM    104  CB  SER A  18       3.447  83.646 266.996  1.00 97.25           C  
ANISOU  104  CB  SER A  18    12541  17240   7170   -198    473  -1373       C  
ATOM    105  OG  SER A  18       2.429  84.129 266.137  1.00 93.72           O  
ANISOU  105  OG  SER A  18    12187  17030   6391   -127    315  -1249       O  
ATOM    106  N   ARG A  19       5.344  86.472 265.862  1.00127.10           N  
ANISOU  106  N   ARG A  19    16591  21174  10525   -291    973   -625       N  
ATOM    107  CA  ARG A  19       6.084  86.987 264.715  1.00141.60           C  
ANISOU  107  CA  ARG A  19    18542  23261  11998   -328   1188   -489       C  
ATOM    108  C   ARG A  19       7.037  88.105 265.131  1.00153.77           C  
ANISOU  108  C   ARG A  19    20133  24635  13657   -462   1419   -198       C  
ATOM    109  O   ARG A  19       7.664  88.744 264.287  1.00158.62           O  
ANISOU  109  O   ARG A  19    20863  25414  13992   -527   1623    -18       O  
ATOM    110  CB  ARG A  19       5.125  87.489 263.632  1.00143.91           C  
ANISOU  110  CB  ARG A  19    19014  23795  11868   -216   1058   -320       C  
ATOM    111  CG  ARG A  19       4.344  88.736 264.013  1.00143.10           C  
ANISOU  111  CG  ARG A  19    19058  23516  11795   -154    947     55       C  
ATOM    112  CD  ARG A  19       3.568  89.281 262.823  1.00146.15           C  
ANISOU  112  CD  ARG A  19    19633  24184  11713    -16    850    251       C  
ATOM    113  NE  ARG A  19       2.928  90.559 263.122  1.00147.14           N  
ANISOU  113  NE  ARG A  19    19932  24131  11843     76    778    641       N  
ATOM    114  CZ  ARG A  19       1.667  90.688 263.522  1.00146.05           C  
ANISOU  114  CZ  ARG A  19    19777  23945  11773    232    507    689       C  
ATOM    115  NH1 ARG A  19       0.902  89.615 263.669  1.00144.59           N  
ANISOU  115  NH1 ARG A  19    19399  23882  11656    279    282    370       N  
ATOM    116  NH2 ARG A  19       1.169  91.892 263.772  1.00146.12           N  
ANISOU  116  NH2 ARG A  19    19962  23781  11776    341    469   1051       N  
ATOM    117  N   LEU A  20       7.143  88.333 266.436  1.00164.60           N  
ANISOU  117  N   LEU A  20    21424  25685  15434   -520   1389   -157       N  
ATOM    118  CA  LEU A  20       8.025  89.368 266.965  1.00168.06           C  
ANISOU  118  CA  LEU A  20    21896  25939  16019   -679   1591     86       C  
ATOM    119  C   LEU A  20       9.478  88.907 267.007  1.00173.19           C  
ANISOU  119  C   LEU A  20    22365  26687  16753   -813   1840    -82       C  
ATOM    120  O   LEU A  20       9.808  87.922 267.667  1.00171.14           O  
ANISOU  120  O   LEU A  20    21901  26381  16742   -788   1807   -360       O  
ATOM    121  CB  LEU A  20       7.579  89.794 268.366  1.00165.85           C  
ANISOU  121  CB  LEU A  20    21598  25294  16125   -689   1457    175       C  
ATOM    122  CG  LEU A  20       6.395  90.759 268.451  1.00168.22           C  
ANISOU  122  CG  LEU A  20    22105  25447  16364   -585   1291    456       C  
ATOM    123  CD1 LEU A  20       6.057  91.061 269.903  1.00164.97           C  
ANISOU  123  CD1 LEU A  20    21651  24683  16349   -595   1182    495       C  
ATOM    124  CD2 LEU A  20       6.694  92.042 267.689  1.00172.49           C  
ANISOU  124  CD2 LEU A  20    22896  26010  16632   -649   1466    809       C  
ATOM    125  N   GLN A  21      10.339  89.632 266.300  1.00174.05           N  
ANISOU  125  N   GLN A  21    22549  26939  16644   -948   2097     98       N  
ATOM    126  CA  GLN A  21      11.768  89.344 266.287  1.00171.32           C  
ANISOU  126  CA  GLN A  21    22010  26732  16353  -1088   2360    -30       C  
ATOM    127  C   GLN A  21      12.546  90.547 265.760  1.00170.48           C  
ANISOU  127  C   GLN A  21    22026  26687  16060  -1298   2635    272       C  
ATOM    128  O   GLN A  21      12.025  91.333 264.970  1.00172.74           O  
ANISOU  128  O   GLN A  21    22574  27010  16049  -1287   2647    535       O  
ATOM    129  CB  GLN A  21      12.061  88.103 265.438  1.00171.61           C  
ANISOU  129  CB  GLN A  21    21927  27090  16188   -971   2405   -351       C  
ATOM    130  CG  GLN A  21      13.456  87.524 265.634  1.00169.72           C  
ANISOU  130  CG  GLN A  21    21425  26988  16074  -1043   2632   -559       C  
ATOM    131  CD  GLN A  21      13.703  87.055 267.056  1.00163.12           C  
ANISOU  131  CD  GLN A  21    20382  25905  15691  -1032   2535   -709       C  
ATOM    132  OE1 GLN A  21      12.778  86.648 267.759  1.00159.22           O  
ANISOU  132  OE1 GLN A  21    19916  25185  15396   -919   2284   -784       O  
ATOM    133  NE2 GLN A  21      14.958  87.114 267.489  1.00162.37           N  
ANISOU  133  NE2 GLN A  21    20069  25874  15749  -1152   2737   -751       N  
ATOM    134  N   SER A  22      13.790  90.688 266.207  1.00168.86           N  
ANISOU  134  N   SER A  22    21634  26499  16026  -1491   2855    238       N  
ATOM    135  CA  SER A  22      14.638  91.798 265.784  1.00168.18           C  
ANISOU  135  CA  SER A  22    21637  26468  15794  -1747   3145    503       C  
ATOM    136  C   SER A  22      15.073  91.654 264.326  1.00170.80           C  
ANISOU  136  C   SER A  22    22021  27188  15689  -1749   3360    511       C  
ATOM    137  O   SER A  22      14.903  92.574 263.526  1.00170.66           O  
ANISOU  137  O   SER A  22    22271  27201  15372  -1827   3473    809       O  
ATOM    138  CB  SER A  22      15.865  91.906 266.693  1.00166.60           C  
ANISOU  138  CB  SER A  22    21170  26229  15903  -1968   3311    425       C  
ATOM    139  OG  SER A  22      16.582  90.684 266.734  1.00166.82           O  
ANISOU  139  OG  SER A  22    20876  26505  16003  -1872   3354     79       O  
ATOM    140  N   HIS A  23      15.636  90.499 263.987  1.00170.04           N  
ANISOU  140  N   HIS A  23    21684  27378  15544  -1651   3422    186       N  
ATOM    141  CA  HIS A  23      16.073  90.235 262.621  1.00167.54           C  
ANISOU  141  CA  HIS A  23    21395  27457  14807  -1632   3629    144       C  
ATOM    142  C   HIS A  23      14.945  89.621 261.799  1.00167.91           C  
ANISOU  142  C   HIS A  23    21615  27616  14565  -1377   3415     49       C  
ATOM    143  O   HIS A  23      14.189  88.786 262.292  1.00164.46           O  
ANISOU  143  O   HIS A  23    21124  27059  14305  -1193   3147   -173       O  
ATOM    144  CB  HIS A  23      17.295  89.314 262.615  1.00160.80           C  
ANISOU  144  CB  HIS A  23    20197  26875  14026  -1637   3825   -170       C  
ATOM    145  N   SER A  24      14.841  90.040 260.542  1.00173.17           N  
ANISOU  145  N   SER A  24    22497  28468  14832  -1365   3517    216       N  
ATOM    146  CA  SER A  24      13.766  89.585 259.666  1.00174.43           C  
ANISOU  146  CA  SER A  24    22837  28738  14701  -1135   3301    151       C  
ATOM    147  C   SER A  24      13.971  88.145 259.201  1.00173.44           C  
ANISOU  147  C   SER A  24    22541  28812  14546   -968   3263   -275       C  
ATOM    148  O   SER A  24      14.831  87.872 258.362  1.00176.77           O  
ANISOU  148  O   SER A  24    22913  29415  14836   -973   3469   -362       O  
ATOM    149  CB  SER A  24      13.643  90.510 258.452  1.00179.42           C  
ANISOU  149  CB  SER A  24    23771  29433  14969  -1149   3403    473       C  
ATOM    150  N   ALA A  25      13.171  87.239 259.758  1.00168.44           N  
ANISOU  150  N   ALA A  25    21833  28125  14041   -821   3005   -538       N  
ATOM    151  CA  ALA A  25      13.160  85.827 259.374  1.00162.82           C  
ANISOU  151  CA  ALA A  25    21014  27532  13317   -653   2929   -953       C  
ATOM    152  C   ALA A  25      14.523  85.154 259.530  1.00158.60           C  
ANISOU  152  C   ALA A  25    20229  27069  12962   -670   3166  -1185       C  
ATOM    153  O   ALA A  25      15.297  85.070 258.577  1.00164.58           O  
ANISOU  153  O   ALA A  25    20983  28008  13540   -669   3369  -1209       O  
ATOM    154  CB  ALA A  25      12.661  85.676 257.940  1.00165.54           C  
ANISOU  154  CB  ALA A  25    21561  28062  13274   -544   2872   -963       C  
ATOM    155  N   THR A  26      14.803  84.673 260.738  1.00143.93           N  
ANISOU  155  N   THR A  26    18158  25075  11455   -669   3137  -1353       N  
ATOM    156  CA  THR A  26      16.022  83.917 261.008  1.00130.95           C  
ANISOU  156  CA  THR A  26    16252  23489  10013   -630   3318  -1596       C  
ATOM    157  C   THR A  26      15.860  83.104 262.289  1.00121.36           C  
ANISOU  157  C   THR A  26    14873  22091   9148   -539   3175  -1839       C  
ATOM    158  O   THR A  26      15.020  83.422 263.131  1.00120.74           O  
ANISOU  158  O   THR A  26    14863  21718   9292   -566   2947  -1718       O  
ATOM    159  CB  THR A  26      17.254  84.836 261.132  1.00125.18           C  
ANISOU  159  CB  THR A  26    15381  22827   9354   -832   3601  -1369       C  
ATOM    160  OG1 THR A  26      18.443  84.039 261.207  1.00122.46           O  
ANISOU  160  OG1 THR A  26    14770  22596   9163   -754   3767  -1616       O  
ATOM    161  CG2 THR A  26      17.151  85.707 262.373  1.00120.78           C  
ANISOU  161  CG2 THR A  26    14771  22074   9045  -1012   3566  -1153       C  
ATOM    162  N   SER A  27      16.663  82.054 262.432  1.00114.58           N  
ANISOU  162  N   SER A  27    13825  21263   8448   -399   3258  -2137       N  
ATOM    163  CA  SER A  27      16.582  81.190 263.606  1.00104.97           C  
ANISOU  163  CA  SER A  27    12471  19838   7575   -277   3128  -2370       C  
ATOM    164  C   SER A  27      17.630  81.561 264.653  1.00101.32           C  
ANISOU  164  C   SER A  27    11745  19312   7440   -359   3248  -2280       C  
ATOM    165  O   SER A  27      17.711  80.939 265.712  1.00 96.37           O  
ANISOU  165  O   SER A  27    10995  18463   7156   -253   3134  -2417       O  
ATOM    166  CB  SER A  27      16.743  79.722 263.202  1.00101.74           C  
ANISOU  166  CB  SER A  27    12052  19440   7165    -37   3114  -2756       C  
ATOM    167  OG  SER A  27      18.008  79.489 262.606  1.00103.32           O  
ANISOU  167  OG  SER A  27    12106  19832   7320     19   3357  -2820       O  
ATOM    168  N   ILE A  28      18.428  82.580 264.349  1.00104.46           N  
ANISOU  168  N   ILE A  28    12059  19912   7718   -558   3480  -2048       N  
ATOM    169  CA  ILE A  28      19.477  83.032 265.254  1.00104.93           C  
ANISOU  169  CA  ILE A  28    11847  19969   8052   -682   3609  -1963       C  
ATOM    170  C   ILE A  28      18.884  83.778 266.445  1.00103.74           C  
ANISOU  170  C   ILE A  28    11754  19445   8216   -815   3401  -1740       C  
ATOM    171  O   ILE A  28      18.334  84.869 266.296  1.00104.52           O  
ANISOU  171  O   ILE A  28    12049  19440   8225   -997   3368  -1446       O  
ATOM    172  CB  ILE A  28      20.489  83.942 264.533  1.00106.96           C  
ANISOU  172  CB  ILE A  28    12034  20445   8162   -889   3878  -1751       C  
ATOM    173  CG1 ILE A  28      21.062  83.232 263.303  1.00112.55           C  
ANISOU  173  CG1 ILE A  28    12734  21375   8656   -733   4016  -1919       C  
ATOM    174  CG2 ILE A  28      21.599  84.363 265.484  1.00102.03           C  
ANISOU  174  CG2 ILE A  28    11100  19843   7825  -1038   3997  -1696       C  
ATOM    175  CD1 ILE A  28      22.034  84.075 262.501  1.00117.48           C  
ANISOU  175  CD1 ILE A  28    13305  22211   9122   -928   4285  -1718       C  
ATOM    176  N   ARG A  29      19.004  83.183 267.627  1.00103.36           N  
ANISOU  176  N   ARG A  29    11550  19195   8528   -705   3265  -1880       N  
ATOM    177  CA  ARG A  29      18.433  83.757 268.840  1.00100.35           C  
ANISOU  177  CA  ARG A  29    11216  18460   8454   -801   3059  -1710       C  
ATOM    178  C   ARG A  29      19.425  84.651 269.574  1.00100.05           C  
ANISOU  178  C   ARG A  29    10965  18455   8593  -1026   3195  -1551       C  
ATOM    179  O   ARG A  29      20.543  84.234 269.878  1.00101.17           O  
ANISOU  179  O   ARG A  29    10809  18793   8838   -987   3330  -1700       O  
ATOM    180  CB  ARG A  29      17.951  82.646 269.775  1.00 99.95           C  
ANISOU  180  CB  ARG A  29    11136  18155   8685   -573   2830  -1932       C  
ATOM    181  CG  ARG A  29      16.877  81.760 269.172  1.00106.71           C  
ANISOU  181  CG  ARG A  29    12209  18935   9400   -394   2673  -2103       C  
ATOM    182  CD  ARG A  29      16.683  80.489 269.978  1.00108.51           C  
ANISOU  182  CD  ARG A  29    12390  18954   9887   -169   2522  -2366       C  
ATOM    183  NE  ARG A  29      15.768  79.568 269.311  1.00112.28           N  
ANISOU  183  NE  ARG A  29    13065  19384  10214    -29   2404  -2570       N  
ATOM    184  CZ  ARG A  29      15.663  78.276 269.603  1.00112.54           C  
ANISOU  184  CZ  ARG A  29    13106  19282  10373    177   2331  -2855       C  
ATOM    185  NH1 ARG A  29      16.421  77.743 270.550  1.00109.82           N  
ANISOU  185  NH1 ARG A  29    12582  18844  10300    305   2360  -2951       N  
ATOM    186  NH2 ARG A  29      14.804  77.513 268.942  1.00115.03           N  
ANISOU  186  NH2 ARG A  29    13616  19557  10534    255   2231  -3045       N  
ATOM    187  N   TYR A  30      19.010  85.881 269.855  1.00 97.36           N  
ANISOU  187  N   TYR A  30    10780  17930   8283  -1258   3157  -1257       N  
ATOM    188  CA  TYR A  30      19.815  86.793 270.656  1.00 96.82           C  
ANISOU  188  CA  TYR A  30    10549  17833   8404  -1510   3255  -1110       C  
ATOM    189  C   TYR A  30      19.665  86.443 272.133  1.00 94.23           C  
ANISOU  189  C   TYR A  30    10107  17242   8454  -1426   3038  -1197       C  
ATOM    190  O   TYR A  30      18.555  86.214 272.613  1.00 91.69           O  
ANISOU  190  O   TYR A  30     9971  16623   8246  -1302   2795  -1188       O  
ATOM    191  CB  TYR A  30      19.407  88.244 270.402  1.00 95.14           C  
ANISOU  191  CB  TYR A  30    10593  17477   8078  -1785   3304   -767       C  
ATOM    192  N   ILE A  31      20.783  86.398 272.850  1.00 97.39           N  
ANISOU  192  N   ILE A  31    10191  17776   9035  -1491   3127  -1280       N  
ATOM    193  CA  ILE A  31      20.769  85.968 274.244  1.00 95.52           C  
ANISOU  193  CA  ILE A  31     9821  17340   9131  -1383   2932  -1379       C  
ATOM    194  C   ILE A  31      21.253  87.048 275.206  1.00 93.52           C  
ANISOU  194  C   ILE A  31     9468  17002   9064  -1671   2945  -1224       C  
ATOM    195  O   ILE A  31      22.351  87.583 275.058  1.00 93.49           O  
ANISOU  195  O   ILE A  31     9243  17260   9019  -1892   3155  -1196       O  
ATOM    196  CB  ILE A  31      21.635  84.709 274.447  1.00 95.81           C  
ANISOU  196  CB  ILE A  31     9550  17605   9247  -1121   2969  -1667       C  
ATOM    197  CG1 ILE A  31      21.156  83.582 273.532  1.00 98.92           C  
ANISOU  197  CG1 ILE A  31    10070  18049   9465   -836   2958  -1854       C  
ATOM    198  CG2 ILE A  31      21.603  84.266 275.900  1.00 89.84           C  
ANISOU  198  CG2 ILE A  31     8680  16641   8813   -993   2762  -1746       C  
ATOM    199  CD1 ILE A  31      21.970  82.315 273.655  1.00103.07           C  
ANISOU  199  CD1 ILE A  31    10342  18766  10053   -540   3009  -2139       C  
ATOM    200  N   ASP A  32      20.418  87.361 276.191  1.00 96.26           N  
ANISOU  200  N   ASP A  32     9976  16988   9612  -1679   2724  -1134       N  
ATOM    201  CA  ASP A  32      20.796  88.271 277.264  1.00100.23           C  
ANISOU  201  CA  ASP A  32    10399  17369  10314  -1922   2699  -1028       C  
ATOM    202  C   ASP A  32      21.428  87.477 278.402  1.00102.06           C  
ANISOU  202  C   ASP A  32    10325  17668  10786  -1767   2592  -1227       C  
ATOM    203  O   ASP A  32      20.732  86.995 279.296  1.00102.30           O  
ANISOU  203  O   ASP A  32    10435  17441  10995  -1586   2368  -1273       O  
ATOM    204  CB  ASP A  32      19.578  89.056 277.760  1.00100.34           C  
ANISOU  204  CB  ASP A  32    10751  16968  10406  -1992   2525   -831       C  
ATOM    205  CG  ASP A  32      19.935  90.095 278.806  1.00102.00           C  
ANISOU  205  CG  ASP A  32    10929  17030  10799  -2267   2513   -723       C  
ATOM    206  OD1 ASP A  32      21.119  90.486 278.885  1.00110.98           O  
ANISOU  206  OD1 ASP A  32    11818  18404  11945  -2494   2682   -750       O  
ATOM    207  OD2 ASP A  32      19.027  90.530 279.545  1.00 94.44           O  
ANISOU  207  OD2 ASP A  32    10187  15729   9967  -2262   2340   -622       O  
ATOM    208  N   HIS A  33      22.751  87.339 278.361  1.00107.02           N  
ANISOU  208  N   HIS A  33    10598  18659  11406  -1829   2758  -1339       N  
ATOM    209  CA  HIS A  33      23.470  86.529 279.339  1.00110.28           C  
ANISOU  209  CA  HIS A  33    10687  19203  12010  -1639   2669  -1532       C  
ATOM    210  C   HIS A  33      23.492  87.197 280.711  1.00109.05           C  
ANISOU  210  C   HIS A  33    10490  18863  12080  -1809   2521  -1464       C  
ATOM    211  O   HIS A  33      23.711  86.539 281.729  1.00108.47           O  
ANISOU  211  O   HIS A  33    10248  18784  12182  -1614   2368  -1588       O  
ATOM    212  CB  HIS A  33      24.900  86.259 278.860  1.00121.11           C  
ANISOU  212  CB  HIS A  33    11659  21068  13291  -1655   2895  -1667       C  
ATOM    213  CG  HIS A  33      25.497  85.003 279.413  1.00129.46           C  
ANISOU  213  CG  HIS A  33    12427  22301  14462  -1290   2819  -1900       C  
ATOM    214  ND1 HIS A  33      26.142  84.955 280.629  1.00132.77           N  
ANISOU  214  ND1 HIS A  33    12569  22799  15079  -1273   2710  -1964       N  
ATOM    215  CD2 HIS A  33      25.548  83.745 278.911  1.00132.97           C  
ANISOU  215  CD2 HIS A  33    12834  22849  14840   -913   2837  -2083       C  
ATOM    216  CE1 HIS A  33      26.564  83.723 280.855  1.00134.74           C  
ANISOU  216  CE1 HIS A  33    12623  23194  15377   -880   2663  -2159       C  
ATOM    217  NE2 HIS A  33      26.216  82.970 279.825  1.00135.69           N  
ANISOU  217  NE2 HIS A  33    12895  23315  15347   -659   2745  -2238       N  
ATOM    218  N   ALA A  34      23.266  88.507 280.731  1.00105.43           N  
ANISOU  218  N   ALA A  34    10208  18247  11605  -2164   2570  -1267       N  
ATOM    219  CA  ALA A  34      23.213  89.256 281.980  1.00 94.93           C  
ANISOU  219  CA  ALA A  34     8890  16711  10467  -2354   2439  -1205       C  
ATOM    220  C   ALA A  34      22.015  88.819 282.814  1.00 90.21           C  
ANISOU  220  C   ALA A  34     8531  15731  10016  -2111   2172  -1196       C  
ATOM    221  O   ALA A  34      22.088  88.753 284.041  1.00 92.52           O  
ANISOU  221  O   ALA A  34     8732  15932  10490  -2079   2015  -1249       O  
ATOM    222  CB  ALA A  34      23.153  90.750 281.704  1.00 94.24           C  
ANISOU  222  CB  ALA A  34     9005  16489  10313  -2776   2571   -994       C  
ATOM    223  N   ALA A  35      20.912  88.516 282.136  1.00 83.75           N  
ANISOU  223  N   ALA A  35     8007  14711   9102  -1946   2124  -1134       N  
ATOM    224  CA  ALA A  35      19.697  88.077 282.809  1.00 76.97           C  
ANISOU  224  CA  ALA A  35     7372  13510   8363  -1728   1890  -1125       C  
ATOM    225  C   ALA A  35      19.786  86.605 283.195  1.00 78.03           C  
ANISOU  225  C   ALA A  35     7351  13711   8585  -1373   1779  -1329       C  
ATOM    226  O   ALA A  35      19.166  86.171 284.165  1.00 79.62           O  
ANISOU  226  O   ALA A  35     7627  13682   8942  -1217   1588  -1355       O  
ATOM    227  CB  ALA A  35      18.485  88.320 281.927  1.00 71.45           C  
ANISOU  227  CB  ALA A  35     7019  12608   7520  -1698   1875   -990       C  
ATOM    228  N   VAL A  36      20.559  85.839 282.431  1.00 81.31           N  
ANISOU  228  N   VAL A  36     7567  14434   8893  -1240   1911  -1470       N  
ATOM    229  CA  VAL A  36      20.728  84.416 282.700  1.00 83.13           C  
ANISOU  229  CA  VAL A  36     7673  14721   9192   -882   1834  -1667       C  
ATOM    230  C   VAL A  36      21.468  84.196 284.013  1.00 88.80           C  
ANISOU  230  C   VAL A  36     8136  15507  10099   -813   1737  -1741       C  
ATOM    231  O   VAL A  36      21.057  83.382 284.838  1.00 91.86           O  
ANISOU  231  O   VAL A  36     8571  15712  10619   -567   1569  -1806       O  
ATOM    232  CB  VAL A  36      21.491  83.709 281.564  1.00 84.92           C  
ANISOU  232  CB  VAL A  36     7736  15282   9247   -745   2022  -1812       C  
ATOM    233  CG1 VAL A  36      21.736  82.248 281.917  1.00 83.22           C  
ANISOU  233  CG1 VAL A  36     7408  15096   9115   -354   1951  -2020       C  
ATOM    234  CG2 VAL A  36      20.723  83.826 280.257  1.00 84.38           C  
ANISOU  234  CG2 VAL A  36     7931  15164   8965   -785   2102  -1754       C  
ATOM    235  N   LEU A  37      22.560  84.930 284.201  1.00 94.72           N  
ANISOU  235  N   LEU A  37     8614  16529  10848  -1041   1844  -1730       N  
ATOM    236  CA  LEU A  37      23.327  84.853 285.438  1.00100.58           C  
ANISOU  236  CA  LEU A  37     9082  17391  11742  -1011   1744  -1799       C  
ATOM    237  C   LEU A  37      22.524  85.416 286.605  1.00 94.71           C  
ANISOU  237  C   LEU A  37     8540  16298  11147  -1111   1548  -1692       C  
ATOM    238  O   LEU A  37      22.558  84.878 287.711  1.00 92.27           O  
ANISOU  238  O   LEU A  37     8157  15931  10971   -924   1384  -1752       O  
ATOM    239  CB  LEU A  37      24.653  85.605 285.301  1.00110.46           C  
ANISOU  239  CB  LEU A  37     9983  19043  12944  -1292   1912  -1819       C  
ATOM    240  CG  LEU A  37      25.499  85.712 286.573  1.00116.23           C  
ANISOU  240  CG  LEU A  37    10400  19952  13811  -1322   1803  -1891       C  
ATOM    241  CD1 LEU A  37      25.891  84.333 287.082  1.00118.74           C  
ANISOU  241  CD1 LEU A  37    10519  20405  14193   -865   1695  -2051       C  
ATOM    242  CD2 LEU A  37      26.731  86.571 286.334  1.00121.62           C  
ANISOU  242  CD2 LEU A  37    10742  21036  14431  -1675   1983  -1910       C  
ATOM    243  N   LEU A  38      21.800  86.500 286.343  1.00 92.24           N  
ANISOU  243  N   LEU A  38     8493  15756  10797  -1389   1573  -1527       N  
ATOM    244  CA  LEU A  38      20.972  87.146 287.354  1.00 88.86           C  
ANISOU  244  CA  LEU A  38     8285  14987  10492  -1492   1411  -1420       C  
ATOM    245  C   LEU A  38      19.935  86.184 287.924  1.00 83.32           C  
ANISOU  245  C   LEU A  38     7765  14008   9883  -1171   1221  -1447       C  
ATOM    246  O   LEU A  38      19.857  85.990 289.137  1.00 87.17           O  
ANISOU  246  O   LEU A  38     8223  14393  10504  -1084   1066  -1472       O  
ATOM    247  CB  LEU A  38      20.278  88.376 286.768  1.00 90.93           C  
ANISOU  247  CB  LEU A  38     8841  15034  10673  -1779   1489  -1234       C  
ATOM    248  CG  LEU A  38      19.291  89.099 287.685  1.00 91.69           C  
ANISOU  248  CG  LEU A  38     9208  14753  10878  -1861   1340  -1116       C  
ATOM    249  CD1 LEU A  38      19.996  89.616 288.929  1.00 95.79           C  
ANISOU  249  CD1 LEU A  38     9556  15319  11521  -2027   1275  -1163       C  
ATOM    250  CD2 LEU A  38      18.601  90.233 286.943  1.00 92.15           C  
ANISOU  250  CD2 LEU A  38     9575  14606  10834  -2081   1433   -925       C  
ATOM    251  N   HIS A  39      19.143  85.582 287.044  1.00 72.54           N  
ANISOU  251  N   HIS A  39     6591  12535   8436  -1010   1238  -1445       N  
ATOM    252  CA  HIS A  39      18.140  84.612 287.463  1.00 66.27           C  
ANISOU  252  CA  HIS A  39     5973  11486   7722   -738   1080  -1481       C  
ATOM    253  C   HIS A  39      18.793  83.308 287.905  1.00 65.73           C  
ANISOU  253  C   HIS A  39     5708  11549   7719   -431   1038  -1648       C  
ATOM    254  O   HIS A  39      18.205  82.533 288.655  1.00 66.02           O  
ANISOU  254  O   HIS A  39     5848  11376   7860   -223    898  -1677       O  
ATOM    255  CB  HIS A  39      17.141  84.348 286.335  1.00 64.72           C  
ANISOU  255  CB  HIS A  39     6017  11169   7403   -683   1111  -1452       C  
ATOM    256  CG  HIS A  39      16.303  85.537 285.983  1.00 67.08           C  
ANISOU  256  CG  HIS A  39     6550  11299   7637   -910   1119  -1270       C  
ATOM    257  ND1 HIS A  39      16.817  86.652 285.362  1.00 71.84           N  
ANISOU  257  ND1 HIS A  39     7137  12028   8129  -1175   1269  -1164       N  
ATOM    258  CD2 HIS A  39      14.984  85.786 286.174  1.00 69.33           C  
ANISOU  258  CD2 HIS A  39     7094  11299   7948   -899   1002  -1167       C  
ATOM    259  CE1 HIS A  39      15.852  87.537 285.178  1.00 75.77           C  
ANISOU  259  CE1 HIS A  39     7899  12304   8587  -1296   1240   -997       C  
ATOM    260  NE2 HIS A  39      14.731  87.035 285.663  1.00 73.91           N  
ANISOU  260  NE2 HIS A  39     7817  11834   8432  -1123   1075  -1000       N  
ATOM    261  N   GLY A  40      20.012  83.070 287.432  1.00 71.14           N  
ANISOU  261  N   GLY A  40     6112  12583   8337   -397   1170  -1751       N  
ATOM    262  CA  GLY A  40      20.764  81.894 287.829  1.00 78.53           C  
ANISOU  262  CA  GLY A  40     6839  13675   9323    -77   1144  -1904       C  
ATOM    263  C   GLY A  40      21.168  81.977 289.288  1.00 81.05           C  
ANISOU  263  C   GLY A  40     7014  14000   9781    -40    998  -1898       C  
ATOM    264  O   GLY A  40      20.972  81.033 290.054  1.00 76.57           O  
ANISOU  264  O   GLY A  40     6488  13301   9303    244    873  -1945       O  
ATOM    265  N   LEU A  41      21.733  83.118 289.670  1.00 87.30           N  
ANISOU  265  N   LEU A  41     7649  14940  10579   -340   1017  -1839       N  
ATOM    266  CA  LEU A  41      22.099  83.366 291.058  1.00 92.26           C  
ANISOU  266  CA  LEU A  41     8145  15594  11315   -358    872  -1836       C  
ATOM    267  C   LEU A  41      20.852  83.445 291.927  1.00 91.32           C  
ANISOU  267  C   LEU A  41     8344  15061  11292   -339    705  -1737       C  
ATOM    268  O   LEU A  41      20.844  82.970 293.062  1.00 92.05           O  
ANISOU  268  O   LEU A  41     8413  15091  11470   -161    556  -1756       O  
ATOM    269  CB  LEU A  41      22.914  84.656 291.181  1.00 99.74           C  
ANISOU  269  CB  LEU A  41     8885  16774  12239   -745    943  -1809       C  
ATOM    270  CG  LEU A  41      24.269  84.672 290.471  1.00111.05           C  
ANISOU  270  CG  LEU A  41     9937  18676  13579   -809   1114  -1910       C  
ATOM    271  CD1 LEU A  41      24.949  86.023 290.635  1.00114.66           C  
ANISOU  271  CD1 LEU A  41    10230  19315  14022  -1259   1188  -1877       C  
ATOM    272  CD2 LEU A  41      25.158  83.552 290.987  1.00115.31           C  
ANISOU  272  CD2 LEU A  41    10162  19502  14147   -440   1048  -2054       C  
ATOM    273  N   ALA A  42      19.800  84.049 291.383  1.00 80.84           N  
ANISOU  273  N   ALA A  42     7307  13471   9937   -510    734  -1628       N  
ATOM    274  CA  ALA A  42      18.531  84.169 292.089  1.00 70.76           C  
ANISOU  274  CA  ALA A  42     6325  11819   8739   -495    597  -1533       C  
ATOM    275  C   ALA A  42      17.941  82.793 292.369  1.00 70.66           C  
ANISOU  275  C   ALA A  42     6426  11641   8781   -151    505  -1586       C  
ATOM    276  O   ALA A  42      17.304  82.576 293.398  1.00 72.31           O  
ANISOU  276  O   ALA A  42     6764  11631   9079    -64    370  -1546       O  
ATOM    277  CB  ALA A  42      17.555  85.013 291.290  1.00 63.76           C  
ANISOU  277  CB  ALA A  42     5702  10733   7792   -702    658  -1410       C  
ATOM    278  N   SER A  43      18.157  81.864 291.444  1.00 73.28           N  
ANISOU  278  N   SER A  43     6724  12068   9053     35    591  -1680       N  
ATOM    279  CA  SER A  43      17.723  80.487 291.632  1.00 76.16           C  
ANISOU  279  CA  SER A  43     7203  12268   9465    356    528  -1752       C  
ATOM    280  C   SER A  43      18.536  79.828 292.735  1.00 76.64           C  
ANISOU  280  C   SER A  43     7087  12433   9600    592    442  -1807       C  
ATOM    281  O   SER A  43      18.009  79.055 293.535  1.00 76.22           O  
ANISOU  281  O   SER A  43     7180  12155   9625    792    334  -1795       O  
ATOM    282  CB  SER A  43      17.857  79.691 290.332  1.00 79.12           C  
ANISOU  282  CB  SER A  43     7588  12731   9743    491    655  -1863       C  
ATOM    283  OG  SER A  43      16.989  80.193 289.332  1.00 80.07           O  
ANISOU  283  OG  SER A  43     7898  12751   9776    306    711  -1809       O  
ATOM    284  N   LEU A  44      19.826  80.142 292.770  1.00 79.42           N  
ANISOU  284  N   LEU A  44     7117  13141   9916    567    492  -1862       N  
ATOM    285  CA  LEU A  44      20.727  79.570 293.761  1.00 83.75           C  
ANISOU  285  CA  LEU A  44     7447  13866  10508    809    405  -1917       C  
ATOM    286  C   LEU A  44      20.440  80.130 295.150  1.00 84.65           C  
ANISOU  286  C   LEU A  44     7604  13865  10696    712    243  -1828       C  
ATOM    287  O   LEU A  44      20.325  79.378 296.117  1.00 85.38           O  
ANISOU  287  O   LEU A  44     7753  13846  10841    965    122  -1819       O  
ATOM    288  CB  LEU A  44      22.183  79.834 293.376  1.00 89.57           C  
ANISOU  288  CB  LEU A  44     7784  15073  11176    780    504  -2010       C  
ATOM    289  CG  LEU A  44      23.242  79.257 294.317  1.00 95.71           C  
ANISOU  289  CG  LEU A  44     8273  16118  11976   1056    411  -2078       C  
ATOM    290  CD1 LEU A  44      23.060  77.754 294.472  1.00 97.48           C  
ANISOU  290  CD1 LEU A  44     8634  16174  12229   1519    371  -2124       C  
ATOM    291  CD2 LEU A  44      24.642  79.584 293.814  1.00 99.71           C  
ANISOU  291  CD2 LEU A  44     8348  17133  12405    994    526  -2178       C  
ATOM    292  N   LEU A  45      20.324  81.452 295.238  1.00 83.50           N  
ANISOU  292  N   LEU A  45     7452  13734  10541    350    250  -1762       N  
ATOM    293  CA  LEU A  45      20.052  82.116 296.508  1.00 80.07           C  
ANISOU  293  CA  LEU A  45     7070  13195  10160    225    110  -1694       C  
ATOM    294  C   LEU A  45      18.717  81.675 297.095  1.00 77.60           C  
ANISOU  294  C   LEU A  45     7095  12478   9912    343     12  -1609       C  
ATOM    295  O   LEU A  45      18.633  81.346 298.277  1.00 82.82           O  
ANISOU  295  O   LEU A  45     7786  13071  10613    486   -119  -1587       O  
ATOM    296  CB  LEU A  45      20.068  83.637 296.335  1.00 79.72           C  
ANISOU  296  CB  LEU A  45     7020  13179  10093   -198    164  -1644       C  
ATOM    297  CG  LEU A  45      21.409  84.282 295.979  1.00 83.16           C  
ANISOU  297  CG  LEU A  45     7108  14020  10470   -406    257  -1721       C  
ATOM    298  CD1 LEU A  45      21.292  85.798 295.984  1.00 83.71           C  
ANISOU  298  CD1 LEU A  45     7249  14026  10529   -841    303  -1658       C  
ATOM    299  CD2 LEU A  45      22.502  83.821 296.930  1.00 83.64           C  
ANISOU  299  CD2 LEU A  45     6844  14401  10535   -232    149  -1817       C  
ATOM    300  N   GLY A  46      17.682  81.666 296.262  1.00 72.75           N  
ANISOU  300  N   GLY A  46     6726  11622   9295    281     79  -1562       N  
ATOM    301  CA  GLY A  46      16.347  81.296 296.696  1.00 71.63           C  
ANISOU  301  CA  GLY A  46     6883  11122   9210    353      5  -1487       C  
ATOM    302  C   GLY A  46      16.267  79.909 297.307  1.00 75.44           C  
ANISOU  302  C   GLY A  46     7427  11498   9738    691    -64  -1517       C  
ATOM    303  O   GLY A  46      15.590  79.707 298.315  1.00 78.88           O  
ANISOU  303  O   GLY A  46     8020  11725  10226    753   -162  -1450       O  
ATOM    304  N   LEU A  47      16.967  78.954 296.703  1.00 75.50           N  
ANISOU  304  N   LEU A  47     7325  11641   9720    915     -1  -1614       N  
ATOM    305  CA  LEU A  47      16.953  77.577 297.184  1.00 75.08           C  
ANISOU  305  CA  LEU A  47     7362  11459   9705   1261    -45  -1643       C  
ATOM    306  C   LEU A  47      17.724  77.421 298.492  1.00 78.64           C  
ANISOU  306  C   LEU A  47     7665  12047  10166   1436   -163  -1622       C  
ATOM    307  O   LEU A  47      17.324  76.657 299.369  1.00 81.13           O  
ANISOU  307  O   LEU A  47     8145  12161  10521   1640   -243  -1570       O  
ATOM    308  CB  LEU A  47      17.529  76.635 296.125  1.00 75.42           C  
ANISOU  308  CB  LEU A  47     7342  11606   9708   1472     68  -1767       C  
ATOM    309  CG  LEU A  47      16.640  76.378 294.908  1.00 74.52           C  
ANISOU  309  CG  LEU A  47     7435  11308   9572   1383    166  -1806       C  
ATOM    310  CD1 LEU A  47      17.352  75.495 293.896  1.00 74.68           C  
ANISOU  310  CD1 LEU A  47     7377  11465   9535   1598    284  -1952       C  
ATOM    311  CD2 LEU A  47      15.322  75.752 295.338  1.00 73.13           C  
ANISOU  311  CD2 LEU A  47     7582  10738   9466   1416    106  -1753       C  
ATOM    312  N   VAL A  48      18.828  78.149 298.618  1.00 78.33           N  
ANISOU  312  N   VAL A  48     7315  12365  10082   1344   -173  -1661       N  
ATOM    313  CA  VAL A  48      19.661  78.066 299.813  1.00 77.73           C  
ANISOU  313  CA  VAL A  48     7049  12494   9991   1500   -299  -1659       C  
ATOM    314  C   VAL A  48      19.054  78.848 300.978  1.00 80.05           C  
ANISOU  314  C   VAL A  48     7460  12654  10303   1318   -421  -1564       C  
ATOM    315  O   VAL A  48      19.013  78.359 302.108  1.00 83.35           O  
ANISOU  315  O   VAL A  48     7938  13013  10719   1518   -540  -1515       O  
ATOM    316  CB  VAL A  48      21.086  78.585 299.538  1.00 74.60           C  
ANISOU  316  CB  VAL A  48     6239  12573   9532   1438   -269  -1756       C  
ATOM    317  CG1 VAL A  48      21.897  78.632 300.824  1.00 75.41           C  
ANISOU  317  CG1 VAL A  48     6124  12926   9604   1561   -425  -1759       C  
ATOM    318  CG2 VAL A  48      21.772  77.709 298.502  1.00 74.64           C  
ANISOU  318  CG2 VAL A  48     6107  12745   9507   1682   -147  -1858       C  
ATOM    319  N   GLU A  49      18.580  80.058 300.696  1.00 76.17           N  
ANISOU  319  N   GLU A  49     7018  12107   9816    952   -385  -1537       N  
ATOM    320  CA  GLU A  49      18.001  80.915 301.728  1.00 70.69           C  
ANISOU  320  CA  GLU A  49     6442  11284   9132    764   -481  -1465       C  
ATOM    321  C   GLU A  49      16.767  80.290 302.368  1.00 71.44           C  
ANISOU  321  C   GLU A  49     6858  11014   9272    903   -533  -1368       C  
ATOM    322  O   GLU A  49      16.713  80.119 303.582  1.00 77.51           O  
ANISOU  322  O   GLU A  49     7672  11752  10028   1014   -647  -1324       O  
ATOM    323  CB  GLU A  49      17.647  82.286 301.153  1.00 66.73           C  
ANISOU  323  CB  GLU A  49     5983  10740   8630    374   -407  -1448       C  
ATOM    324  CG  GLU A  49      18.847  83.175 300.883  1.00 68.12           C  
ANISOU  324  CG  GLU A  49     5857  11265   8759    148   -369  -1529       C  
ATOM    325  CD  GLU A  49      18.443  84.532 300.348  1.00 67.98           C  
ANISOU  325  CD  GLU A  49     5944  11146   8740   -235   -283  -1492       C  
ATOM    326  OE1 GLU A  49      19.332  85.383 300.138  1.00 73.77           O  
ANISOU  326  OE1 GLU A  49     6470  12120   9438   -485   -234  -1548       O  
ATOM    327  OE2 GLU A  49      17.230  84.743 300.139  1.00 60.23           O  
ANISOU  327  OE2 GLU A  49     5251   9844   7789   -284   -260  -1403       O  
ATOM    328  N   ASN A  50      15.776  79.951 301.551  1.00 73.10           N  
ANISOU  328  N   ASN A  50     7283  10967   9524    885   -447  -1338       N  
ATOM    329  CA  ASN A  50      14.575  79.302 302.062  1.00 72.81           C  
ANISOU  329  CA  ASN A  50     7533  10598   9533    988   -476  -1256       C  
ATOM    330  C   ASN A  50      14.883  77.910 302.599  1.00 78.75           C  
ANISOU  330  C   ASN A  50     8327  11305  10291   1340   -516  -1254       C  
ATOM    331  O   ASN A  50      14.149  77.379 303.433  1.00 82.97           O  
ANISOU  331  O   ASN A  50     9069  11610  10847   1443   -561  -1172       O  
ATOM    332  CB  ASN A  50      13.501  79.221 300.979  1.00 69.09           C  
ANISOU  332  CB  ASN A  50     7246   9910   9096    878   -379  -1246       C  
ATOM    333  CG  ASN A  50      12.896  80.571 300.659  1.00 68.64           C  
ANISOU  333  CG  ASN A  50     7229   9819   9031    572   -355  -1203       C  
ATOM    334  OD1 ASN A  50      12.044  81.073 301.395  1.00 68.91           O  
ANISOU  334  OD1 ASN A  50     7407   9692   9086    484   -402  -1127       O  
ATOM    335  ND2 ASN A  50      13.334  81.170 299.558  1.00 67.13           N  
ANISOU  335  ND2 ASN A  50     6925   9778   8802    422   -271  -1246       N  
ATOM    336  N   GLY A  51      15.975  77.326 302.117  1.00 79.27           N  
ANISOU  336  N   GLY A  51     8201  11588  10329   1532   -488  -1338       N  
ATOM    337  CA  GLY A  51      16.409  76.022 302.580  1.00 79.73           C  
ANISOU  337  CA  GLY A  51     8295  11615  10383   1909   -520  -1336       C  
ATOM    338  C   GLY A  51      16.794  76.045 304.046  1.00 77.59           C  
ANISOU  338  C   GLY A  51     7977  11436  10066   2045   -662  -1265       C  
ATOM    339  O   GLY A  51      16.338  75.213 304.828  1.00 80.10           O  
ANISOU  339  O   GLY A  51     8511  11534  10390   2252   -703  -1178       O  
ATOM    340  N   VAL A  52      17.632  77.008 304.420  1.00 73.27           N  
ANISOU  340  N   VAL A  52     7157  11219   9464   1914   -734  -1304       N  
ATOM    341  CA  VAL A  52      18.092  77.117 305.799  1.00 74.56           C  
ANISOU  341  CA  VAL A  52     7241  11533   9556   2027   -885  -1260       C  
ATOM    342  C   VAL A  52      17.013  77.718 306.698  1.00 73.01           C  
ANISOU  342  C   VAL A  52     7277  11101   9362   1838   -937  -1165       C  
ATOM    343  O   VAL A  52      16.973  77.435 307.894  1.00 77.28           O  
ANISOU  343  O   VAL A  52     7895  11625   9844   1993  -1044  -1092       O  
ATOM    344  CB  VAL A  52      19.386  77.962 305.907  1.00 71.05           C  
ANISOU  344  CB  VAL A  52     6401  11552   9042   1919   -951  -1361       C  
ATOM    345  CG1 VAL A  52      20.516  77.303 305.131  1.00 70.15           C  
ANISOU  345  CG1 VAL A  52     6021  11721   8912   2152   -900  -1454       C  
ATOM    346  CG2 VAL A  52      19.156  79.382 305.416  1.00 67.95           C  
ANISOU  346  CG2 VAL A  52     5954  11192   8671   1468   -896  -1406       C  
ATOM    347  N   ILE A  53      16.136  78.536 306.121  1.00 66.10           N  
ANISOU  347  N   ILE A  53     6518  10055   8543   1523   -858  -1163       N  
ATOM    348  CA  ILE A  53      15.036  79.127 306.877  1.00 63.35           C  
ANISOU  348  CA  ILE A  53     6389   9480   8200   1356   -886  -1080       C  
ATOM    349  C   ILE A  53      14.088  78.038 307.367  1.00 67.60           C  
ANISOU  349  C   ILE A  53     7216   9706   8765   1557   -874   -973       C  
ATOM    350  O   ILE A  53      13.672  78.037 308.526  1.00 71.65           O  
ANISOU  350  O   ILE A  53     7856  10135   9232   1602   -944   -892       O  
ATOM    351  CB  ILE A  53      14.253  80.157 306.038  1.00 56.40           C  
ANISOU  351  CB  ILE A  53     5581   8475   7374   1025   -794  -1092       C  
ATOM    352  CG1 ILE A  53      15.062  81.445 305.888  1.00 54.82           C  
ANISOU  352  CG1 ILE A  53     5159   8532   7137    769   -809  -1172       C  
ATOM    353  CG2 ILE A  53      12.913  80.471 306.683  1.00 50.53           C  
ANISOU  353  CG2 ILE A  53     5098   7451   6649    928   -797  -1000       C  
ATOM    354  CD1 ILE A  53      15.341  82.148 307.195  1.00 52.74           C  
ANISOU  354  CD1 ILE A  53     4854   8379   6804    697   -930  -1179       C  
ATOM    355  N   LEU A  54      13.761  77.105 306.478  1.00 69.82           N  
ANISOU  355  N   LEU A  54     7604   9814   9109   1665   -778   -979       N  
ATOM    356  CA  LEU A  54      12.921  75.966 306.831  1.00 70.86           C  
ANISOU  356  CA  LEU A  54     8016   9634   9274   1836   -745   -890       C  
ATOM    357  C   LEU A  54      13.549  75.153 307.954  1.00 70.75           C  
ANISOU  357  C   LEU A  54     8027   9668   9188   2157   -835   -820       C  
ATOM    358  O   LEU A  54      12.857  74.690 308.859  1.00 73.66           O  
ANISOU  358  O   LEU A  54     8622   9827   9539   2233   -848   -705       O  
ATOM    359  CB  LEU A  54      12.680  75.073 305.612  1.00 75.83           C  
ANISOU  359  CB  LEU A  54     8735  10104   9975   1898   -630   -946       C  
ATOM    360  CG  LEU A  54      11.326  75.204 304.910  1.00 75.11           C  
ANISOU  360  CG  LEU A  54     8824   9761   9953   1663   -540   -941       C  
ATOM    361  CD1 LEU A  54      11.127  76.609 304.368  1.00 74.10           C  
ANISOU  361  CD1 LEU A  54     8564   9770   9822   1364   -534   -976       C  
ATOM    362  CD2 LEU A  54      11.203  74.172 303.800  1.00 77.66           C  
ANISOU  362  CD2 LEU A  54     9242   9942  10324   1752   -440  -1018       C  
ATOM    363  N   PHE A  55      14.866  74.986 307.890  1.00 70.50           N  
ANISOU  363  N   PHE A  55     7753   9931   9104   2353   -892   -884       N  
ATOM    364  CA  PHE A  55      15.591  74.234 308.905  1.00 75.10           C  
ANISOU  364  CA  PHE A  55     8324  10613   9596   2703   -993   -817       C  
ATOM    365  C   PHE A  55      15.578  74.956 310.248  1.00 77.03           C  
ANISOU  365  C   PHE A  55     8544  10985   9738   2636  -1125   -753       C  
ATOM    366  O   PHE A  55      15.327  74.346 311.287  1.00 80.47           O  
ANISOU  366  O   PHE A  55     9167  11302  10107   2836  -1176   -630       O  
ATOM    367  CB  PHE A  55      17.034  73.986 308.460  1.00 77.33           C  
ANISOU  367  CB  PHE A  55     8297  11245   9839   2928  -1029   -917       C  
ATOM    368  CG  PHE A  55      17.874  73.285 309.490  1.00 82.45           C  
ANISOU  368  CG  PHE A  55     8892  12058  10377   3321  -1153   -849       C  
ATOM    369  CD1 PHE A  55      17.806  71.910 309.639  1.00 86.64           C  
ANISOU  369  CD1 PHE A  55     9660  12348  10910   3694  -1117   -761       C  
ATOM    370  CD2 PHE A  55      18.734  74.001 310.307  1.00 84.03           C  
ANISOU  370  CD2 PHE A  55     8814  12653  10461   3319  -1308   -876       C  
ATOM    371  CE1 PHE A  55      18.576  71.262 310.586  1.00 90.66           C  
ANISOU  371  CE1 PHE A  55    10137  13008  11302   4093  -1235   -678       C  
ATOM    372  CE2 PHE A  55      19.507  73.359 311.255  1.00 86.83           C  
ANISOU  372  CE2 PHE A  55     9105  13195  10691   3702  -1439   -809       C  
ATOM    373  CZ  PHE A  55      19.429  71.988 311.394  1.00 90.45           C  
ANISOU  373  CZ  PHE A  55     9808  13412  11147   4107  -1403   -699       C  
ATOM    374  N   VAL A  56      15.853  76.256 310.219  1.00 74.43           N  
ANISOU  374  N   VAL A  56     8002  10890   9387   2351  -1171   -839       N  
ATOM    375  CA  VAL A  56      15.910  77.057 311.437  1.00 73.42           C  
ANISOU  375  CA  VAL A  56     7837  10906   9152   2256  -1296   -817       C  
ATOM    376  C   VAL A  56      14.551  77.133 312.126  1.00 73.91           C  
ANISOU  376  C   VAL A  56     8220  10643   9220   2153  -1260   -703       C  
ATOM    377  O   VAL A  56      14.416  76.762 313.290  1.00 75.22           O  
ANISOU  377  O   VAL A  56     8516  10781   9284   2318  -1334   -603       O  
ATOM    378  CB  VAL A  56      16.411  78.486 311.147  1.00 72.10           C  
ANISOU  378  CB  VAL A  56     7414  11003   8978   1920  -1325   -951       C  
ATOM    379  CG1 VAL A  56      16.184  79.387 312.352  1.00 74.80           C  
ANISOU  379  CG1 VAL A  56     7796  11403   9221   1766  -1430   -943       C  
ATOM    380  CG2 VAL A  56      17.882  78.463 310.765  1.00 72.46           C  
ANISOU  380  CG2 VAL A  56     7093  11456   8983   2019  -1382  -1063       C  
ATOM    381  N   VAL A  57      13.547  77.609 311.398  1.00 75.09           N  
ANISOU  381  N   VAL A  57     8488  10568   9475   1891  -1144   -715       N  
ATOM    382  CA  VAL A  57      12.205  77.766 311.946  1.00 73.75           C  
ANISOU  382  CA  VAL A  57     8583  10120   9318   1773  -1095   -621       C  
ATOM    383  C   VAL A  57      11.573  76.416 312.282  1.00 82.24           C  
ANISOU  383  C   VAL A  57     9920  10922  10406   1998  -1039   -491       C  
ATOM    384  O   VAL A  57      10.830  76.291 313.257  1.00 84.04           O  
ANISOU  384  O   VAL A  57    10343  11009  10578   2013  -1038   -384       O  
ATOM    385  CB  VAL A  57      11.292  78.528 310.962  1.00 60.31           C  
ANISOU  385  CB  VAL A  57     6923   8267   7725   1474   -985   -665       C  
ATOM    386  CG1 VAL A  57       9.902  78.720 311.548  1.00 54.29           C  
ANISOU  386  CG1 VAL A  57     6397   7260   6971   1368   -933   -575       C  
ATOM    387  CG2 VAL A  57      11.906  79.869 310.605  1.00 56.74           C  
ANISOU  387  CG2 VAL A  57     6257   8040   7261   1240  -1019   -778       C  
ATOM    388  N   GLY A  58      11.891  75.402 311.485  1.00 88.48           N  
ANISOU  388  N   GLY A  58    10725  11635  11261   2171   -982   -502       N  
ATOM    389  CA  GLY A  58      11.236  74.112 311.601  1.00 88.64           C  
ANISOU  389  CA  GLY A  58    11026  11338  11316   2339   -899   -395       C  
ATOM    390  C   GLY A  58      11.883  73.091 312.520  1.00 92.05           C  
ANISOU  390  C   GLY A  58    11552  11776  11648   2707   -964   -288       C  
ATOM    391  O   GLY A  58      11.232  72.126 312.920  1.00 95.38           O  
ANISOU  391  O   GLY A  58    12261  11905  12076   2822   -894   -165       O  
ATOM    392  N   CYS A  59      13.153  73.287 312.862  1.00 92.78           N  
ANISOU  392  N   CYS A  59    11407  12204  11642   2893  -1095   -329       N  
ATOM    393  CA  CYS A  59      13.869  72.285 313.652  1.00 94.83           C  
ANISOU  393  CA  CYS A  59    11735  12504  11792   3298  -1169   -224       C  
ATOM    394  C   CYS A  59      14.596  72.849 314.872  1.00 91.72           C  
ANISOU  394  C   CYS A  59    11182  12449  11217   3399  -1347   -196       C  
ATOM    395  O   CYS A  59      14.629  72.212 315.925  1.00 95.77           O  
ANISOU  395  O   CYS A  59    11865  12917  11605   3655  -1404    -50       O  
ATOM    396  CB  CYS A  59      14.868  71.538 312.765  1.00 99.24           C  
ANISOU  396  CB  CYS A  59    12158  13154  12393   3563  -1154   -301       C  
ATOM    397  SG  CYS A  59      14.102  70.487 311.509  1.00 76.96           S  
ANISOU  397  SG  CYS A  59     9602   9896   9743   3551   -952   -323       S  
ATOM    398  N   ARG A  60      15.182  74.034 314.735  1.00 80.68           N  
ANISOU  398  N   ARG A  60     9471  11389   9795   3190  -1434   -337       N  
ATOM    399  CA  ARG A  60      15.963  74.620 315.822  1.00 75.20           C  
ANISOU  399  CA  ARG A  60     8591  11059   8924   3253  -1616   -352       C  
ATOM    400  C   ARG A  60      15.156  75.629 316.637  1.00 73.79           C  
ANISOU  400  C   ARG A  60     8514  10840   8685   2964  -1638   -342       C  
ATOM    401  O   ARG A  60      15.602  76.088 317.690  1.00 81.33           O  
ANISOU  401  O   ARG A  60     9382  12049   9471   2999  -1784   -348       O  
ATOM    402  CB  ARG A  60      17.222  75.291 315.270  1.00 71.03           C  
ANISOU  402  CB  ARG A  60     7640  10960   8388   3195  -1704   -529       C  
ATOM    403  CG  ARG A  60      18.136  74.357 314.492  1.00 71.27           C  
ANISOU  403  CG  ARG A  60     7522  11098   8460   3508  -1685   -557       C  
ATOM    404  CD  ARG A  60      18.701  73.256 315.374  1.00 71.62           C  
ANISOU  404  CD  ARG A  60     7638  11211   8364   3994  -1788   -425       C  
ATOM    405  NE  ARG A  60      19.577  72.360 314.625  1.00 78.22           N  
ANISOU  405  NE  ARG A  60     8340  12143   9239   4331  -1761   -458       N  
ATOM    406  CZ  ARG A  60      20.247  71.347 315.161  1.00 86.97           C  
ANISOU  406  CZ  ARG A  60     9473  13334  10236   4815  -1841   -357       C  
ATOM    407  NH1 ARG A  60      20.145  71.096 316.459  1.00 92.73           N  
ANISOU  407  NH1 ARG A  60    10361  14072  10801   5009  -1959   -205       N  
ATOM    408  NH2 ARG A  60      21.022  70.584 314.401  1.00 88.97           N  
ANISOU  408  NH2 ARG A  60     9603  13669  10534   5124  -1800   -405       N  
ATOM    409  N   MET A  61      13.967  75.966 316.152  1.00 68.29           N  
ANISOU  409  N   MET A  61     7996   9838   8114   2691  -1495   -336       N  
ATOM    410  CA  MET A  61      13.136  76.970 316.801  1.00 70.05           C  
ANISOU  410  CA  MET A  61     8314  10006   8294   2422  -1491   -341       C  
ATOM    411  C   MET A  61      11.871  76.342 317.379  1.00 76.93           C  
ANISOU  411  C   MET A  61     9535  10534   9161   2461  -1386   -175       C  
ATOM    412  O   MET A  61      11.281  75.450 316.768  1.00 81.58           O  
ANISOU  412  O   MET A  61    10293  10840   9865   2516  -1259   -103       O  
ATOM    413  CB  MET A  61      12.781  78.078 315.808  1.00 71.65           C  
ANISOU  413  CB  MET A  61     8410  10181   8631   2061  -1414   -474       C  
ATOM    414  CG  MET A  61      12.132  79.300 316.428  1.00 76.38           C  
ANISOU  414  CG  MET A  61     9068  10770   9182   1795  -1423   -513       C  
ATOM    415  SD  MET A  61      11.991  80.664 315.254  1.00104.72           S  
ANISOU  415  SD  MET A  61    12521  14361  12906   1414  -1351   -665       S  
ATOM    416  CE  MET A  61      13.713  80.921 314.835  1.00 57.28           C  
ANISOU  416  CE  MET A  61     6144   8756   6864   1427  -1466   -808       C  
ATOM    417  N   ARG A  62      11.463  76.806 318.559  1.00 77.78           N  
ANISOU  417  N   ARG A  62     9749  10676   9128   2420  -1433   -125       N  
ATOM    418  CA  ARG A  62      10.273  76.281 319.222  1.00 75.92           C  
ANISOU  418  CA  ARG A  62     9827  10154   8863   2440  -1325     35       C  
ATOM    419  C   ARG A  62       9.017  76.603 318.419  1.00 73.03           C  
ANISOU  419  C   ARG A  62     9557   9521   8672   2163  -1157     13       C  
ATOM    420  O   ARG A  62       8.743  77.763 318.110  1.00 72.16           O  
ANISOU  420  O   ARG A  62     9341   9471   8607   1912  -1151   -102       O  
ATOM    421  CB  ARG A  62      10.160  76.840 320.642  1.00 81.60           C  
ANISOU  421  CB  ARG A  62    10615  11015   9373   2444  -1410     70       C  
ATOM    422  CG  ARG A  62       8.963  76.316 321.423  1.00 86.48           C  
ANISOU  422  CG  ARG A  62    11548  11375   9934   2466  -1286    243       C  
ATOM    423  CD  ARG A  62       9.033  76.701 322.897  1.00 91.04           C  
ANISOU  423  CD  ARG A  62    12200  12131  10261   2538  -1381    288       C  
ATOM    424  NE  ARG A  62      10.065  75.959 323.617  1.00 94.80           N  
ANISOU  424  NE  ARG A  62    12669  12797  10554   2875  -1527    378       N  
ATOM    425  CZ  ARG A  62      11.268  76.441 323.912  1.00 97.71           C  
ANISOU  425  CZ  ARG A  62    12793  13537  10797   2959  -1727    264       C  
ATOM    426  NH1 ARG A  62      11.597  77.674 323.551  1.00 96.78           N  
ANISOU  426  NH1 ARG A  62    12438  13609  10723   2700  -1792     52       N  
ATOM    427  NH2 ARG A  62      12.143  75.691 324.571  1.00100.41           N  
ANISOU  427  NH2 ARG A  62    13129  14062  10961   3302  -1862    363       N  
ATOM    428  N   GLN A  63       8.256  75.565 318.090  1.00 77.94           N  
ANISOU  428  N   GLN A  63    10383   9846   9384   2214  -1022    124       N  
ATOM    429  CA  GLN A  63       7.109  75.695 317.195  1.00 78.74           C  
ANISOU  429  CA  GLN A  63    10544   9720   9652   1973   -872     97       C  
ATOM    430  C   GLN A  63       5.932  76.429 317.829  1.00 77.09           C  
ANISOU  430  C   GLN A  63    10435   9448   9409   1779   -802    127       C  
ATOM    431  O   GLN A  63       5.401  76.010 318.857  1.00 79.69           O  
ANISOU  431  O   GLN A  63    10953   9693   9632   1850   -759    257       O  
ATOM    432  CB  GLN A  63       6.655  74.314 316.718  1.00 83.42           C  
ANISOU  432  CB  GLN A  63    11332  10022  10341   2065   -750    191       C  
ATOM    433  CG  GLN A  63       7.707  73.559 315.920  1.00 88.78           C  
ANISOU  433  CG  GLN A  63    11931  10727  11075   2264   -790    143       C  
ATOM    434  CD  GLN A  63       8.070  74.257 314.624  1.00 91.87           C  
ANISOU  434  CD  GLN A  63    12078  11244  11582   2107   -802    -30       C  
ATOM    435  OE1 GLN A  63       7.196  74.655 313.851  1.00 91.74           O  
ANISOU  435  OE1 GLN A  63    12061  11120  11677   1865   -713    -85       O  
ATOM    436  NE2 GLN A  63       9.366  74.412 314.380  1.00 94.08           N  
ANISOU  436  NE2 GLN A  63    12144  11776  11827   2246   -912   -112       N  
ATOM    437  N   THR A  64       5.534  77.530 317.199  1.00 73.63           N  
ANISOU  437  N   THR A  64     9874   9052   9052   1548   -783     11       N  
ATOM    438  CA  THR A  64       4.352  78.279 317.607  1.00 71.63           C  
ANISOU  438  CA  THR A  64     9695   8733   8786   1375   -701     22       C  
ATOM    439  C   THR A  64       3.397  78.413 316.425  1.00 70.06           C  
ANISOU  439  C   THR A  64     9470   8391   8758   1190   -587    -18       C  
ATOM    440  O   THR A  64       3.694  77.946 315.324  1.00 73.62           O  
ANISOU  440  O   THR A  64     9855   8796   9322   1185   -577    -61       O  
ATOM    441  CB  THR A  64       4.712  79.681 318.134  1.00 73.33           C  
ANISOU  441  CB  THR A  64     9809   9147   8906   1289   -793    -83       C  
ATOM    442  OG1 THR A  64       5.177  80.497 317.052  1.00 72.89           O  
ANISOU  442  OG1 THR A  64     9575   9167   8953   1151   -828   -219       O  
ATOM    443  CG2 THR A  64       5.792  79.591 319.201  1.00 76.57           C  
ANISOU  443  CG2 THR A  64    10200   9757   9134   1461   -936    -75       C  
ATOM    444  N   VAL A  65       2.252  79.049 316.652  1.00 63.83           N  
ANISOU  444  N   VAL A  65     8727   7552   7975   1052   -504     -9       N  
ATOM    445  CA  VAL A  65       1.282  79.273 315.586  1.00 58.46           C  
ANISOU  445  CA  VAL A  65     8000   6778   7434    889   -411    -46       C  
ATOM    446  C   VAL A  65       1.856  80.195 314.511  1.00 62.71           C  
ANISOU  446  C   VAL A  65     8372   7414   8040    802   -474   -172       C  
ATOM    447  O   VAL A  65       1.728  79.927 313.316  1.00 66.77           O  
ANISOU  447  O   VAL A  65     8824   7879   8665    739   -444   -209       O  
ATOM    448  CB  VAL A  65      -0.033  79.870 316.137  1.00 47.45           C  
ANISOU  448  CB  VAL A  65     6662   5354   6013    793   -315    -13       C  
ATOM    449  CG1 VAL A  65      -0.838  80.533 315.029  1.00 43.58           C  
ANISOU  449  CG1 VAL A  65     6071   4850   5639    647   -265    -78       C  
ATOM    450  CG2 VAL A  65      -0.854  78.794 316.828  1.00 47.05           C  
ANISOU  450  CG2 VAL A  65     6764   5179   5935    818   -202    117       C  
ATOM    451  N   VAL A  66       2.505  81.270 314.945  1.00 63.57           N  
ANISOU  451  N   VAL A  66     8421   7661   8073    787   -559   -239       N  
ATOM    452  CA  VAL A  66       3.057  82.256 314.023  1.00 64.99           C  
ANISOU  452  CA  VAL A  66     8466   7922   8304    677   -603   -348       C  
ATOM    453  C   VAL A  66       4.166  81.667 313.151  1.00 66.49           C  
ANISOU  453  C   VAL A  66     8537   8183   8545    724   -655   -392       C  
ATOM    454  O   VAL A  66       4.196  81.892 311.939  1.00 68.89           O  
ANISOU  454  O   VAL A  66     8757   8483   8936    634   -628   -443       O  
ATOM    455  CB  VAL A  66       3.605  83.482 314.778  1.00 69.53           C  
ANISOU  455  CB  VAL A  66     9024   8616   8779    629   -678   -423       C  
ATOM    456  CG1 VAL A  66       4.211  84.474 313.804  1.00 74.72           C  
ANISOU  456  CG1 VAL A  66     9563   9334   9491    489   -705   -526       C  
ATOM    457  CG2 VAL A  66       2.498  84.141 315.582  1.00 70.83           C  
ANISOU  457  CG2 VAL A  66     9313   8709   8889    598   -613   -397       C  
ATOM    458  N   THR A  67       5.068  80.909 313.767  1.00 63.29           N  
ANISOU  458  N   THR A  67     8122   7855   8071    883   -726   -370       N  
ATOM    459  CA  THR A  67       6.177  80.301 313.037  1.00 61.20           C  
ANISOU  459  CA  THR A  67     7733   7681   7841    972   -773   -414       C  
ATOM    460  C   THR A  67       5.680  79.299 312.000  1.00 61.09           C  
ANISOU  460  C   THR A  67     7765   7506   7940    991   -681   -390       C  
ATOM    461  O   THR A  67       6.347  79.057 310.995  1.00 58.64           O  
ANISOU  461  O   THR A  67     7345   7252   7684   1005   -685   -457       O  
ATOM    462  CB  THR A  67       7.162  79.592 313.984  1.00 59.79           C  
ANISOU  462  CB  THR A  67     7545   7621   7553   1192   -870   -378       C  
ATOM    463  OG1 THR A  67       6.475  78.568 314.713  1.00 64.29           O  
ANISOU  463  OG1 THR A  67     8317   8021   8091   1325   -817   -246       O  
ATOM    464  CG2 THR A  67       7.776  80.585 314.959  1.00 56.69           C  
ANISOU  464  CG2 THR A  67     7079   7431   7030   1157   -980   -433       C  
ATOM    465  N   THR A  68       4.511  78.717 312.249  1.00 63.30           N  
ANISOU  465  N   THR A  68     8207   7596   8248    978   -594   -306       N  
ATOM    466  CA  THR A  68       3.894  77.798 311.299  1.00 61.67           C  
ANISOU  466  CA  THR A  68     8060   7226   8146    951   -503   -302       C  
ATOM    467  C   THR A  68       3.521  78.531 310.011  1.00 58.70           C  
ANISOU  467  C   THR A  68     7574   6883   7847    777   -474   -387       C  
ATOM    468  O   THR A  68       3.707  78.004 308.913  1.00 53.34           O  
ANISOU  468  O   THR A  68     6857   6179   7231    771   -448   -444       O  
ATOM    469  CB  THR A  68       2.642  77.121 311.896  1.00 58.36           C  
ANISOU  469  CB  THR A  68     7821   6616   7736    922   -406   -200       C  
ATOM    470  OG1 THR A  68       3.029  76.298 313.004  1.00 60.69           O  
ANISOU  470  OG1 THR A  68     8252   6858   7949   1100   -421   -101       O  
ATOM    471  CG2 THR A  68       1.947  76.256 310.855  1.00 55.52           C  
ANISOU  471  CG2 THR A  68     7512   6098   7486    840   -315   -225       C  
ATOM    472  N   TRP A  69       3.002  79.749 310.152  1.00 58.29           N  
ANISOU  472  N   TRP A  69     7487   6884   7777    653   -477   -395       N  
ATOM    473  CA  TRP A  69       2.695  80.581 308.994  1.00 58.07           C  
ANISOU  473  CA  TRP A  69     7371   6895   7798    512   -457   -455       C  
ATOM    474  C   TRP A  69       3.960  80.854 308.190  1.00 60.37           C  
ANISOU  474  C   TRP A  69     7528   7322   8089    513   -505   -536       C  
ATOM    475  O   TRP A  69       4.005  80.618 306.983  1.00 61.72           O  
ANISOU  475  O   TRP A  69     7646   7500   8307    474   -474   -584       O  
ATOM    476  CB  TRP A  69       2.061  81.908 309.415  1.00 58.50           C  
ANISOU  476  CB  TRP A  69     7437   6970   7819    420   -453   -442       C  
ATOM    477  CG  TRP A  69       0.831  81.784 310.264  1.00 62.32           C  
ANISOU  477  CG  TRP A  69     8026   7364   8289    423   -396   -369       C  
ATOM    478  CD1 TRP A  69       0.656  82.282 311.522  1.00 63.88           C  
ANISOU  478  CD1 TRP A  69     8293   7571   8408    457   -403   -335       C  
ATOM    479  CD2 TRP A  69      -0.396  81.130 309.918  1.00 63.96           C  
ANISOU  479  CD2 TRP A  69     8268   7482   8553    379   -314   -331       C  
ATOM    480  NE1 TRP A  69      -0.601  81.980 311.982  1.00 65.56           N  
ANISOU  480  NE1 TRP A  69     8577   7708   8623    447   -320   -269       N  
ATOM    481  CE2 TRP A  69      -1.268  81.272 311.016  1.00 62.45           C  
ANISOU  481  CE2 TRP A  69     8153   7257   8316    389   -265   -266       C  
ATOM    482  CE3 TRP A  69      -0.844  80.438 308.789  1.00 68.03           C  
ANISOU  482  CE3 TRP A  69     8750   7958   9142    319   -277   -359       C  
ATOM    483  CZ2 TRP A  69      -2.557  80.747 311.020  1.00 62.89           C  
ANISOU  483  CZ2 TRP A  69     8232   7255   8408    331   -175   -221       C  
ATOM    484  CZ3 TRP A  69      -2.125  79.918 308.794  1.00 70.14           C  
ANISOU  484  CZ3 TRP A  69     9046   8161   9444    252   -201   -325       C  
ATOM    485  CH2 TRP A  69      -2.966  80.075 309.902  1.00 68.59           C  
ANISOU  485  CH2 TRP A  69     8906   7945   9210    253   -147   -254       C  
ATOM    486  N   VAL A  70       4.982  81.353 308.879  1.00 59.58           N  
ANISOU  486  N   VAL A  70     7364   7349   7925    551   -578   -560       N  
ATOM    487  CA  VAL A  70       6.273  81.660 308.272  1.00 52.20           C  
ANISOU  487  CA  VAL A  70     6268   6584   6979    537   -621   -641       C  
ATOM    488  C   VAL A  70       6.887  80.420 307.628  1.00 52.08           C  
ANISOU  488  C   VAL A  70     6206   6587   6996    676   -609   -667       C  
ATOM    489  O   VAL A  70       7.506  80.502 306.569  1.00 55.49           O  
ANISOU  489  O   VAL A  70     6520   7117   7448    640   -590   -736       O  
ATOM    490  CB  VAL A  70       7.257  82.240 309.315  1.00 46.89           C  
ANISOU  490  CB  VAL A  70     5523   6071   6221    557   -715   -670       C  
ATOM    491  CG1 VAL A  70       8.617  82.504 308.691  1.00 46.16           C  
ANISOU  491  CG1 VAL A  70     5229   6191   6118    526   -751   -761       C  
ATOM    492  CG2 VAL A  70       6.693  83.513 309.921  1.00 43.39           C  
ANISOU  492  CG2 VAL A  70     5151   5592   5742    416   -718   -668       C  
ATOM    493  N   LEU A  71       6.696  79.272 308.269  1.00 56.67           N  
ANISOU  493  N   LEU A  71     6898   7058   7575    839   -608   -610       N  
ATOM    494  CA  LEU A  71       7.220  78.005 307.768  1.00 62.60           C  
ANISOU  494  CA  LEU A  71     7654   7775   8355   1005   -587   -631       C  
ATOM    495  C   LEU A  71       6.649  77.678 306.390  1.00 65.99           C  
ANISOU  495  C   LEU A  71     8104   8112   8859    913   -502   -685       C  
ATOM    496  O   LEU A  71       7.389  77.349 305.462  1.00 66.76           O  
ANISOU  496  O   LEU A  71     8107   8291   8967    964   -486   -765       O  
ATOM    497  CB  LEU A  71       6.907  76.872 308.748  1.00 66.81           C  
ANISOU  497  CB  LEU A  71     8368   8144   8872   1179   -580   -536       C  
ATOM    498  CG  LEU A  71       7.734  75.593 308.620  1.00 72.89           C  
ANISOU  498  CG  LEU A  71     9168   8882   9643   1426   -581   -543       C  
ATOM    499  CD1 LEU A  71       9.185  75.854 308.996  1.00 75.52           C  
ANISOU  499  CD1 LEU A  71     9311   9485   9900   1584   -685   -578       C  
ATOM    500  CD2 LEU A  71       7.145  74.482 309.478  1.00 74.91           C  
ANISOU  500  CD2 LEU A  71     9670   8900   9893   1557   -541   -426       C  
ATOM    501  N   HIS A  72       5.329  77.771 306.266  1.00 66.95           N  
ANISOU  501  N   HIS A  72     8335   8086   9018    781   -449   -649       N  
ATOM    502  CA  HIS A  72       4.659  77.545 304.991  1.00 60.73           C  
ANISOU  502  CA  HIS A  72     7557   7237   8280    672   -385   -706       C  
ATOM    503  C   HIS A  72       4.921  78.700 304.033  1.00 60.00           C  
ANISOU  503  C   HIS A  72     7323   7305   8167    543   -393   -758       C  
ATOM    504  O   HIS A  72       4.985  78.508 302.820  1.00 61.82           O  
ANISOU  504  O   HIS A  72     7512   7570   8405    504   -356   -828       O  
ATOM    505  CB  HIS A  72       3.154  77.358 305.194  1.00 53.67           C  
ANISOU  505  CB  HIS A  72     6786   6186   7422    563   -336   -654       C  
ATOM    506  CG  HIS A  72       2.786  76.050 305.820  1.00 56.27           C  
ANISOU  506  CG  HIS A  72     7281   6320   7780    645   -292   -610       C  
ATOM    507  ND1 HIS A  72       2.448  74.938 305.080  1.00 56.94           N  
ANISOU  507  ND1 HIS A  72     7457   6263   7916    631   -230   -668       N  
ATOM    508  CD2 HIS A  72       2.702  75.673 307.121  1.00 57.83           C  
ANISOU  508  CD2 HIS A  72     7592   6428   7952    735   -293   -511       C  
ATOM    509  CE1 HIS A  72       2.171  73.933 305.893  1.00 60.33           C  
ANISOU  509  CE1 HIS A  72     8060   6500   8362    699   -186   -602       C  
ATOM    510  NE2 HIS A  72       2.318  74.356 307.137  1.00 60.88           N  
ANISOU  510  NE2 HIS A  72     8145   6605   8380    770   -223   -496       N  
ATOM    511  N   LEU A  73       5.074  79.897 304.588  1.00 61.77           N  
ANISOU  511  N   LEU A  73     7496   7619   8356    473   -433   -723       N  
ATOM    512  CA  LEU A  73       5.346  81.085 303.787  1.00 64.06           C  
ANISOU  512  CA  LEU A  73     7688   8030   8621    339   -429   -753       C  
ATOM    513  C   LEU A  73       6.697  80.962 303.092  1.00 68.40           C  
ANISOU  513  C   LEU A  73     8094   8745   9149    374   -428   -831       C  
ATOM    514  O   LEU A  73       6.880  81.446 301.974  1.00 73.39           O  
ANISOU  514  O   LEU A  73     8661   9461   9764    277   -388   -867       O  
ATOM    515  CB  LEU A  73       5.311  82.341 304.660  1.00 65.80           C  
ANISOU  515  CB  LEU A  73     7917   8276   8809    260   -465   -711       C  
ATOM    516  CG  LEU A  73       5.162  83.684 303.945  1.00 68.30           C  
ANISOU  516  CG  LEU A  73     8215   8631   9106    103   -440   -708       C  
ATOM    517  CD1 LEU A  73       3.837  83.744 303.203  1.00 68.72           C  
ANISOU  517  CD1 LEU A  73     8342   8592   9177     63   -396   -668       C  
ATOM    518  CD2 LEU A  73       5.277  84.833 304.935  1.00 69.55           C  
ANISOU  518  CD2 LEU A  73     8409   8784   9232     37   -473   -689       C  
ATOM    519  N   ALA A  74       7.639  80.306 303.762  1.00 65.06           N  
ANISOU  519  N   ALA A  74     7617   8386   8716    525   -469   -851       N  
ATOM    520  CA  ALA A  74       8.962  80.081 303.196  1.00 65.79           C  
ANISOU  520  CA  ALA A  74     7543   8670   8786    594   -466   -931       C  
ATOM    521  C   ALA A  74       8.989  78.786 302.392  1.00 70.46           C  
ANISOU  521  C   ALA A  74     8171   9197   9403    734   -412   -985       C  
ATOM    522  O   ALA A  74       9.925  78.533 301.634  1.00 76.95           O  
ANISOU  522  O   ALA A  74     8863  10170  10205    796   -382  -1065       O  
ATOM    523  CB  ALA A  74      10.011  80.052 304.293  1.00 63.52           C  
ANISOU  523  CB  ALA A  74     7151   8526   8459    712   -548   -934       C  
ATOM    524  N   LEU A  75       7.957  77.966 302.563  1.00 67.26           N  
ANISOU  524  N   LEU A  75     7947   8569   9041    774   -391   -950       N  
ATOM    525  CA  LEU A  75       7.829  76.731 301.798  1.00 69.17           C  
ANISOU  525  CA  LEU A  75     8270   8699   9311    874   -331  -1016       C  
ATOM    526  C   LEU A  75       7.370  77.029 300.374  1.00 67.69           C  
ANISOU  526  C   LEU A  75     8062   8547   9112    722   -274  -1084       C  
ATOM    527  O   LEU A  75       7.862  76.436 299.414  1.00 64.31           O  
ANISOU  527  O   LEU A  75     7601   8167   8667    787   -224  -1182       O  
ATOM    528  CB  LEU A  75       6.851  75.771 302.478  1.00 72.50           C  
ANISOU  528  CB  LEU A  75     8905   8860   9781    924   -317   -959       C  
ATOM    529  CG  LEU A  75       6.520  74.486 301.713  1.00 76.82           C  
ANISOU  529  CG  LEU A  75     9587   9234  10365    979   -246  -1038       C  
ATOM    530  CD1 LEU A  75       7.763  73.627 301.533  1.00 76.92           C  
ANISOU  530  CD1 LEU A  75     9571   9288  10366   1227   -232  -1105       C  
ATOM    531  CD2 LEU A  75       5.418  73.705 302.416  1.00 80.63           C  
ANISOU  531  CD2 LEU A  75    10285   9451  10898    953   -218   -972       C  
ATOM    532  N   SER A  76       6.423  77.953 300.248  1.00 68.99           N  
ANISOU  532  N   SER A  76     8247   8695   9270    539   -281  -1031       N  
ATOM    533  CA  SER A  76       5.906  78.351 298.945  1.00 70.31           C  
ANISOU  533  CA  SER A  76     8398   8915   9402    404   -242  -1072       C  
ATOM    534  C   SER A  76       6.991  79.031 298.121  1.00 75.41           C  
ANISOU  534  C   SER A  76     8892   9777   9984    373   -215  -1115       C  
ATOM    535  O   SER A  76       7.057  78.864 296.903  1.00 83.91           O  
ANISOU  535  O   SER A  76     9945  10927  11011    343   -165  -1187       O  
ATOM    536  CB  SER A  76       4.705  79.286 299.103  1.00 67.91           C  
ANISOU  536  CB  SER A  76     8141   8566   9096    256   -264   -987       C  
ATOM    537  OG  SER A  76       5.095  80.516 299.691  1.00 67.76           O  
ANISOU  537  OG  SER A  76     8064   8624   9058    203   -293   -917       O  
ATOM    538  N   ASP A  77       7.841  79.796 298.796  1.00 71.70           N  
ANISOU  538  N   ASP A  77     8317   9421   9505    365   -245  -1078       N  
ATOM    539  CA  ASP A  77       8.922  80.510 298.131  1.00 72.86           C  
ANISOU  539  CA  ASP A  77     8304   9785   9593    299   -208  -1114       C  
ATOM    540  C   ASP A  77      10.069  79.568 297.781  1.00 77.49           C  
ANISOU  540  C   ASP A  77     8772  10503  10167    466   -174  -1216       C  
ATOM    541  O   ASP A  77      10.909  79.886 296.938  1.00 79.33           O  
ANISOU  541  O   ASP A  77     8866  10935  10343    423   -114  -1271       O  
ATOM    542  CB  ASP A  77       9.421  81.658 299.009  1.00 76.13           C  
ANISOU  542  CB  ASP A  77     8645  10277  10003    200   -251  -1057       C  
ATOM    543  CG  ASP A  77       8.388  82.757 299.171  1.00 82.20           C  
ANISOU  543  CG  ASP A  77     9533  10927  10771     43   -262   -965       C  
ATOM    544  OD1 ASP A  77       7.178  82.455 299.099  1.00 85.18           O  
ANISOU  544  OD1 ASP A  77    10042  11152  11171     58   -268   -929       O  
ATOM    545  OD2 ASP A  77       8.786  83.925 299.369  1.00 84.80           O  
ANISOU  545  OD2 ASP A  77     9826  11319  11077    -96   -260   -935       O  
ATOM    546  N   LEU A  78      10.100  78.409 298.431  1.00 76.21           N  
ANISOU  546  N   LEU A  78     8675  10228  10052    665   -203  -1237       N  
ATOM    547  CA  LEU A  78      11.089  77.387 298.108  1.00 73.72           C  
ANISOU  547  CA  LEU A  78     8281  10002   9726    878   -167  -1335       C  
ATOM    548  C   LEU A  78      10.758  76.754 296.762  1.00 76.03           C  
ANISOU  548  C   LEU A  78     8643  10253   9991    879    -81  -1432       C  
ATOM    549  O   LEU A  78      11.644  76.517 295.939  1.00 78.04           O  
ANISOU  549  O   LEU A  78     8777  10682  10194    955    -14  -1528       O  
ATOM    550  CB  LEU A  78      11.145  76.316 299.198  1.00 66.53           C  
ANISOU  550  CB  LEU A  78     7470   8941   8866   1110   -216  -1310       C  
ATOM    551  CG  LEU A  78      12.199  75.224 298.995  1.00 61.38           C  
ANISOU  551  CG  LEU A  78     6754   8363   8203   1392   -184  -1400       C  
ATOM    552  CD1 LEU A  78      13.600  75.798 299.141  1.00 58.96           C  
ANISOU  552  CD1 LEU A  78     6160   8396   7847   1446   -207  -1428       C  
ATOM    553  CD2 LEU A  78      11.984  74.066 299.957  1.00 61.07           C  
ANISOU  553  CD2 LEU A  78     6901   8091   8211   1624   -218  -1353       C  
ATOM    554  N   LEU A  79       9.473  76.485 296.548  1.00 74.44           N  
ANISOU  554  N   LEU A  79     8627   9842   9813    791    -82  -1417       N  
ATOM    555  CA  LEU A  79       8.998  75.929 295.287  1.00 71.85           C  
ANISOU  555  CA  LEU A  79     8379   9476   9445    757    -18  -1521       C  
ATOM    556  C   LEU A  79       9.181  76.932 294.157  1.00 69.73           C  
ANISOU  556  C   LEU A  79     7996   9422   9076    599     26  -1531       C  
ATOM    557  O   LEU A  79       9.544  76.565 293.041  1.00 72.43           O  
ANISOU  557  O   LEU A  79     8310   9867   9343    628     99  -1640       O  
ATOM    558  CB  LEU A  79       7.528  75.525 295.396  1.00 72.74           C  
ANISOU  558  CB  LEU A  79     8684   9352   9601    661    -43  -1502       C  
ATOM    559  CG  LEU A  79       7.191  74.478 296.458  1.00 77.60           C  
ANISOU  559  CG  LEU A  79     9456   9719  10309    782    -63  -1480       C  
ATOM    560  CD1 LEU A  79       5.699  74.187 296.466  1.00 76.91           C  
ANISOU  560  CD1 LEU A  79     9524   9440  10257    630    -72  -1468       C  
ATOM    561  CD2 LEU A  79       7.989  73.205 296.223  1.00 82.89           C  
ANISOU  561  CD2 LEU A  79    10185  10320  10988   1008     -7  -1594       C  
ATOM    562  N   ALA A  80       8.926  78.202 294.458  1.00 66.05           N  
ANISOU  562  N   ALA A  80     7485   9012   8600    437    -10  -1415       N  
ATOM    563  CA  ALA A  80       9.097  79.274 293.487  1.00 68.00           C  
ANISOU  563  CA  ALA A  80     7654   9434   8747    279     38  -1389       C  
ATOM    564  C   ALA A  80      10.555  79.382 293.056  1.00 77.28           C  
ANISOU  564  C   ALA A  80     8642  10851   9868    322    113  -1451       C  
ATOM    565  O   ALA A  80      10.856  79.820 291.944  1.00 86.06           O  
ANISOU  565  O   ALA A  80     9699  12125  10876    234    193  -1474       O  
ATOM    566  CB  ALA A  80       8.613  80.595 294.062  1.00 63.89           C  
ANISOU  566  CB  ALA A  80     7153   8882   8240    122     -9  -1248       C  
ATOM    567  N   SER A  81      11.455  78.976 293.946  1.00 76.13           N  
ANISOU  567  N   SER A  81     8392  10752   9783    464     89  -1475       N  
ATOM    568  CA  SER A  81      12.882  78.978 293.656  1.00 72.93           C  
ANISOU  568  CA  SER A  81     7765  10612   9332    531    154  -1546       C  
ATOM    569  C   SER A  81      13.307  77.661 293.016  1.00 69.05           C  
ANISOU  569  C   SER A  81     7271  10145   8818    760    218  -1688       C  
ATOM    570  O   SER A  81      14.449  77.510 292.587  1.00 69.60           O  
ANISOU  570  O   SER A  81     7152  10455   8837    852    292  -1769       O  
ATOM    571  CB  SER A  81      13.689  79.229 294.932  1.00 73.06           C  
ANISOU  571  CB  SER A  81     7639  10714   9406    586     83  -1511       C  
ATOM    572  OG  SER A  81      13.333  80.465 295.527  1.00 70.85           O  
ANISOU  572  OG  SER A  81     7379  10400   9142    369     32  -1402       O  
ATOM    573  N   ALA A  82      12.382  76.708 292.958  1.00 65.88           N  
ANISOU  573  N   ALA A  82     7081   9495   8454    847    197  -1726       N  
ATOM    574  CA  ALA A  82      12.667  75.401 292.376  1.00 72.33           C  
ANISOU  574  CA  ALA A  82     7957  10270   9255   1063    261  -1874       C  
ATOM    575  C   ALA A  82      12.328  75.371 290.887  1.00 81.30           C  
ANISOU  575  C   ALA A  82     9143  11472  10277    966    348  -1970       C  
ATOM    576  O   ALA A  82      12.943  74.634 290.117  1.00 85.80           O  
ANISOU  576  O   ALA A  82     9685  12130  10785   1115    438  -2112       O  
ATOM    577  CB  ALA A  82      11.904  74.313 293.116  1.00 67.46           C  
ANISOU  577  CB  ALA A  82     7565   9329   8736   1192    206  -1878       C  
ATOM    578  N   SER A  83      11.345  76.173 290.489  1.00 83.12           N  
ANISOU  578  N   SER A  83     9449  11667  10464    734    319  -1893       N  
ATOM    579  CA  SER A  83      10.954  76.267 289.088  1.00 84.52           C  
ANISOU  579  CA  SER A  83     9674  11934  10504    631    383  -1964       C  
ATOM    580  C   SER A  83      11.782  77.329 288.377  1.00 85.47           C  
ANISOU  580  C   SER A  83     9618  12349  10506    519    467  -1920       C  
ATOM    581  O   SER A  83      11.918  77.314 287.153  1.00 84.93           O  
ANISOU  581  O   SER A  83     9543  12431  10294    488    555  -1996       O  
ATOM    582  CB  SER A  83       9.465  76.591 288.962  1.00 83.45           C  
ANISOU  582  CB  SER A  83     9699  11646  10362    461    305  -1898       C  
ATOM    583  OG  SER A  83       9.178  77.871 289.498  1.00 85.12           O  
ANISOU  583  OG  SER A  83     9867  11880  10595    309    251  -1721       O  
ATOM    584  N   LEU A  84      12.333  78.248 289.161  1.00 77.54           N  
ANISOU  584  N   LEU A  84     8480  11426   9554    444    445  -1800       N  
ATOM    585  CA  LEU A  84      13.128  79.354 288.634  1.00 74.06           C  
ANISOU  585  CA  LEU A  84     7880  11241   9018    290    533  -1741       C  
ATOM    586  C   LEU A  84      14.349  78.935 287.795  1.00 76.38           C  
ANISOU  586  C   LEU A  84     7996  11810   9213    390    671  -1870       C  
ATOM    587  O   LEU A  84      14.652  79.599 286.804  1.00 83.51           O  
ANISOU  587  O   LEU A  84     8843  12908   9979    251    778  -1851       O  
ATOM    588  CB  LEU A  84      13.586  80.259 289.782  1.00 73.33           C  
ANISOU  588  CB  LEU A  84     7676  11170   9018    193    480  -1627       C  
ATOM    589  CG  LEU A  84      14.102  81.642 289.378  1.00 72.92           C  
ANISOU  589  CG  LEU A  84     7523  11298   8885    -52    559  -1531       C  
ATOM    590  CD1 LEU A  84      13.003  82.444 288.702  1.00 71.89           C  
ANISOU  590  CD1 LEU A  84     7589  11052   8673   -219    557  -1415       C  
ATOM    591  CD2 LEU A  84      14.650  82.389 290.581  1.00 71.84           C  
ANISOU  591  CD2 LEU A  84     7272  11181   8843   -145    503  -1462       C  
ATOM    592  N   PRO A  85      15.063  77.855 288.183  1.00 71.20           N  
ANISOU  592  N   PRO A  85     7255  11179   8618    644    680  -1994       N  
ATOM    593  CA  PRO A  85      16.174  77.442 287.313  1.00 72.70           C  
ANISOU  593  CA  PRO A  85     7271  11648   8703    765    825  -2128       C  
ATOM    594  C   PRO A  85      15.736  77.068 285.898  1.00 75.64           C  
ANISOU  594  C   PRO A  85     7774  12044   8921    755    917  -2229       C  
ATOM    595  O   PRO A  85      16.495  77.266 284.952  1.00 78.23           O  
ANISOU  595  O   PRO A  85     7967  12648   9110    734   1059  -2287       O  
ATOM    596  CB  PRO A  85      16.744  76.219 288.035  1.00 69.65           C  
ANISOU  596  CB  PRO A  85     6840  11207   8416   1092    795  -2237       C  
ATOM    597  CG  PRO A  85      16.420  76.447 289.452  1.00 68.09           C  
ANISOU  597  CG  PRO A  85     6674  10833   8364   1079    648  -2117       C  
ATOM    598  CD  PRO A  85      15.075  77.108 289.454  1.00 67.79           C  
ANISOU  598  CD  PRO A  85     6849  10571   8336    839    575  -2000       C  
ATOM    599  N   PHE A  86      14.526  76.535 285.761  1.00 76.72           N  
ANISOU  599  N   PHE A  86     8163  11916   9072    759    840  -2256       N  
ATOM    600  CA  PHE A  86      13.995  76.182 284.449  1.00 77.55           C  
ANISOU  600  CA  PHE A  86     8404  12045   9017    731    901  -2363       C  
ATOM    601  C   PHE A  86      13.676  77.436 283.642  1.00 79.12           C  
ANISOU  601  C   PHE A  86     8600  12400   9064    475    936  -2233       C  
ATOM    602  O   PHE A  86      13.636  77.401 282.412  1.00 83.96           O  
ANISOU  602  O   PHE A  86     9251  13161   9489    443   1025  -2304       O  
ATOM    603  CB  PHE A  86      12.748  75.307 284.590  1.00 80.19           C  
ANISOU  603  CB  PHE A  86     8991  12066   9410    767    797  -2432       C  
ATOM    604  CG  PHE A  86      13.003  74.002 285.286  1.00 84.96           C  
ANISOU  604  CG  PHE A  86     9661  12472  10149   1020    782  -2556       C  
ATOM    605  CD1 PHE A  86      12.834  73.888 286.656  1.00 81.32           C  
ANISOU  605  CD1 PHE A  86     9222  11808   9868   1074    679  -2456       C  
ATOM    606  CD2 PHE A  86      13.417  72.889 284.572  1.00 89.45           C  
ANISOU  606  CD2 PHE A  86    10290  13047  10650   1218    879  -2769       C  
ATOM    607  CE1 PHE A  86      13.069  72.689 287.301  1.00 81.30           C  
ANISOU  607  CE1 PHE A  86     9309  11607   9975   1321    671  -2546       C  
ATOM    608  CE2 PHE A  86      13.654  71.686 285.212  1.00 89.74           C  
ANISOU  608  CE2 PHE A  86    10424  12866  10808   1472    874  -2871       C  
ATOM    609  CZ  PHE A  86      13.479  71.587 286.578  1.00 85.32           C  
ANISOU  609  CZ  PHE A  86     9893  12098  10425   1525    770  -2749       C  
ATOM    610  N   PHE A  87      13.450  78.542 284.342  1.00 81.33           N  
ANISOU  610  N   PHE A  87     8852  12635   9414    304    870  -2040       N  
ATOM    611  CA  PHE A  87      13.241  79.827 283.689  1.00 84.26           C  
ANISOU  611  CA  PHE A  87     9239  13125   9653     74    912  -1887       C  
ATOM    612  C   PHE A  87      14.578  80.410 283.245  1.00 92.93           C  
ANISOU  612  C   PHE A  87    10124  14526  10659      5   1076  -1874       C  
ATOM    613  O   PHE A  87      14.643  81.176 282.284  1.00 97.08           O  
ANISOU  613  O   PHE A  87    10667  15209  11012   -148   1176  -1798       O  
ATOM    614  CB  PHE A  87      12.513  80.799 284.621  1.00 82.05           C  
ANISOU  614  CB  PHE A  87     9033  12658   9485    -71    794  -1696       C  
ATOM    615  CG  PHE A  87      12.312  82.166 284.033  1.00 85.46           C  
ANISOU  615  CG  PHE A  87     9514  13166   9789   -287    842  -1520       C  
ATOM    616  CD1 PHE A  87      11.321  82.390 283.092  1.00 87.92           C  
ANISOU  616  CD1 PHE A  87     9993  13464   9948   -334    820  -1472       C  
ATOM    617  CD2 PHE A  87      13.110  83.228 284.424  1.00 90.22           C  
ANISOU  617  CD2 PHE A  87    10006  13852  10419   -443    908  -1403       C  
ATOM    618  CE1 PHE A  87      11.133  83.646 282.549  1.00 90.65           C  
ANISOU  618  CE1 PHE A  87    10414  13865  10166   -500    867  -1289       C  
ATOM    619  CE2 PHE A  87      12.925  84.487 283.885  1.00 93.73           C  
ANISOU  619  CE2 PHE A  87    10540  14324  10748   -643    968  -1230       C  
ATOM    620  CZ  PHE A  87      11.936  84.696 282.946  1.00 92.90           C  
ANISOU  620  CZ  PHE A  87    10621  14189  10487   -656    949  -1162       C  
ATOM    621  N   THR A  88      15.644  80.041 283.949  1.00 96.27           N  
ANISOU  621  N   THR A  88    10341  15047  11190    118   1106  -1945       N  
ATOM    622  CA  THR A  88      16.989  80.463 283.577  1.00 99.55           C  
ANISOU  622  CA  THR A  88    10503  15794  11528     61   1267  -1962       C  
ATOM    623  C   THR A  88      17.423  79.752 282.302  1.00 95.57           C  
ANISOU  623  C   THR A  88     9965  15503  10845    185   1417  -2120       C  
ATOM    624  O   THR A  88      18.035  80.352 281.417  1.00 96.95           O  
ANISOU  624  O   THR A  88    10038  15943  10857     51   1578  -2093       O  
ATOM    625  CB  THR A  88      18.010  80.173 284.691  1.00107.85           C  
ANISOU  625  CB  THR A  88    11310  16935  12733    182   1240  -2013       C  
ATOM    626  OG1 THR A  88      18.195  78.758 284.819  1.00114.38           O  
ANISOU  626  OG1 THR A  88    12130  17720  13608    509   1220  -2187       O  
ATOM    627  CG2 THR A  88      17.528  80.738 286.012  1.00104.69           C  
ANISOU  627  CG2 THR A  88    10966  16312  12500     87   1080  -1883       C  
ATOM    628  N   TYR A  89      17.103  78.464 282.226  1.00 85.47           N  
ANISOU  628  N   TYR A  89     8787  14096   9591    437   1375  -2289       N  
ATOM    629  CA  TYR A  89      17.378  77.662 281.042  1.00 80.95           C  
ANISOU  629  CA  TYR A  89     8232  13678   8847    581   1505  -2472       C  
ATOM    630  C   TYR A  89      16.630  78.236 279.845  1.00 79.73           C  
ANISOU  630  C   TYR A  89     8246  13570   8477    394   1546  -2413       C  
ATOM    631  O   TYR A  89      17.147  78.270 278.730  1.00 77.26           O  
ANISOU  631  O   TYR A  89     7878  13520   7958    384   1709  -2479       O  
ATOM    632  CB  TYR A  89      16.975  76.205 281.281  1.00 74.94           C  
ANISOU  632  CB  TYR A  89     7620  12682   8172    858   1433  -2658       C  
ATOM    633  CG  TYR A  89      17.391  75.253 280.183  1.00 76.81           C  
ANISOU  633  CG  TYR A  89     7876  13059   8249   1050   1574  -2886       C  
ATOM    634  CD1 TYR A  89      16.523  74.935 279.145  1.00 78.25           C  
ANISOU  634  CD1 TYR A  89     8285  13178   8267   1001   1577  -2979       C  
ATOM    635  CD2 TYR A  89      18.648  74.664 280.188  1.00 78.52           C  
ANISOU  635  CD2 TYR A  89     7879  13487   8468   1291   1701  -3019       C  
ATOM    636  CE1 TYR A  89      16.899  74.061 278.140  1.00 78.79           C  
ANISOU  636  CE1 TYR A  89     8390  13370   8176   1174   1710  -3208       C  
ATOM    637  CE2 TYR A  89      19.033  73.790 279.188  1.00 81.89           C  
ANISOU  637  CE2 TYR A  89     8334  14037   8743   1489   1843  -3241       C  
ATOM    638  CZ  TYR A  89      18.155  73.492 278.167  1.00 80.84           C  
ANISOU  638  CZ  TYR A  89     8452  13817   8446   1423   1849  -3339       C  
ATOM    639  OH  TYR A  89      18.536  72.623 277.170  1.00 78.95           O  
ANISOU  639  OH  TYR A  89     8259  13697   8043   1616   1993  -3579       O  
ATOM    640  N   PHE A  90      15.409  78.697 280.100  1.00 78.47           N  
ANISOU  640  N   PHE A  90     8286  13173   8355    258   1398  -2283       N  
ATOM    641  CA  PHE A  90      14.572  79.326 279.086  1.00 73.77           C  
ANISOU  641  CA  PHE A  90     7858  12612   7557     97   1400  -2194       C  
ATOM    642  C   PHE A  90      15.258  80.540 278.468  1.00 78.13           C  
ANISOU  642  C   PHE A  90     8310  13421   7953   -102   1554  -2037       C  
ATOM    643  O   PHE A  90      15.183  80.757 277.259  1.00 86.45           O  
ANISOU  643  O   PHE A  90     9434  14652   8763   -160   1654  -2033       O  
ATOM    644  CB  PHE A  90      13.228  79.727 279.700  1.00 69.08           C  
ANISOU  644  CB  PHE A  90     7446  11736   7065      4   1208  -2057       C  
ATOM    645  CG  PHE A  90      12.353  80.536 278.787  1.00 68.77           C  
ANISOU  645  CG  PHE A  90     7562  11744   6825   -146   1188  -1924       C  
ATOM    646  CD1 PHE A  90      11.574  79.918 277.825  1.00 72.91           C  
ANISOU  646  CD1 PHE A  90     8228  12298   7176    -95   1150  -2046       C  
ATOM    647  CD2 PHE A  90      12.294  81.916 278.906  1.00 66.92           C  
ANISOU  647  CD2 PHE A  90     7343  11518   6566   -330   1201  -1680       C  
ATOM    648  CE1 PHE A  90      10.761  80.661 276.988  1.00 75.13           C  
ANISOU  648  CE1 PHE A  90     8642  12654   7252   -205   1115  -1917       C  
ATOM    649  CE2 PHE A  90      11.484  82.663 278.075  1.00 68.75           C  
ANISOU  649  CE2 PHE A  90     7735  11786   6602   -428   1180  -1539       C  
ATOM    650  CZ  PHE A  90      10.715  82.035 277.114  1.00 73.60           C  
ANISOU  650  CZ  PHE A  90     8466  12464   7032   -356   1130  -1652       C  
ATOM    651  N   LEU A  91      15.932  81.323 279.303  1.00 75.01           N  
ANISOU  651  N   LEU A  91     7762  13048   7693   -220   1577  -1910       N  
ATOM    652  CA  LEU A  91      16.635  82.512 278.837  1.00 77.39           C  
ANISOU  652  CA  LEU A  91     7971  13562   7871   -451   1736  -1756       C  
ATOM    653  C   LEU A  91      17.966  82.153 278.185  1.00 84.33           C  
ANISOU  653  C   LEU A  91     8610  14797   8635   -399   1949  -1890       C  
ATOM    654  O   LEU A  91      18.379  82.785 277.212  1.00 89.01           O  
ANISOU  654  O   LEU A  91     9182  15617   9018   -550   2123  -1819       O  
ATOM    655  CB  LEU A  91      16.868  83.485 279.994  1.00 77.19           C  
ANISOU  655  CB  LEU A  91     7873  13423   8032   -626   1683  -1596       C  
ATOM    656  CG  LEU A  91      15.614  83.983 280.714  1.00 78.82           C  
ANISOU  656  CG  LEU A  91     8302  13292   8353   -680   1491  -1451       C  
ATOM    657  CD1 LEU A  91      15.972  84.994 281.795  1.00 75.41           C  
ANISOU  657  CD1 LEU A  91     7803  12769   8079   -864   1466  -1314       C  
ATOM    658  CD2 LEU A  91      14.629  84.575 279.718  1.00 81.08           C  
ANISOU  658  CD2 LEU A  91     8835  13533   8441   -765   1489  -1317       C  
ATOM    659  N   ALA A  92      18.630  81.137 278.727  1.00 84.50           N  
ANISOU  659  N   ALA A  92     8451  14870   8785   -171   1942  -2077       N  
ATOM    660  CA  ALA A  92      19.929  80.705 278.219  1.00 86.95           C  
ANISOU  660  CA  ALA A  92     8496  15536   9004    -70   2139  -2224       C  
ATOM    661  C   ALA A  92      19.823  80.195 276.786  1.00 90.86           C  
ANISOU  661  C   ALA A  92     9094  16193   9236     17   2272  -2345       C  
ATOM    662  O   ALA A  92      20.737  80.375 275.980  1.00 95.07           O  
ANISOU  662  O   ALA A  92     9459  17067   9597    -26   2487  -2381       O  
ATOM    663  CB  ALA A  92      20.517  79.632 279.120  1.00 85.87           C  
ANISOU  663  CB  ALA A  92     8186  15385   9057    221   2078  -2396       C  
ATOM    664  N   VAL A  93      18.701  79.554 276.476  1.00 87.79           N  
ANISOU  664  N   VAL A  93     8974  15574   8808    127   2146  -2416       N  
ATOM    665  CA  VAL A  93      18.456  79.039 275.136  1.00 86.80           C  
ANISOU  665  CA  VAL A  93     8980  15581   8419    203   2241  -2550       C  
ATOM    666  C   VAL A  93      18.154  80.189 274.174  1.00 90.32           C  
ANISOU  666  C   VAL A  93     9533  16166   8618    -56   2326  -2353       C  
ATOM    667  O   VAL A  93      18.553  80.161 273.010  1.00100.06           O  
ANISOU  667  O   VAL A  93    10756  17675   9587    -60   2504  -2412       O  
ATOM    668  CB  VAL A  93      17.297  78.020 275.135  1.00 85.67           C  
ANISOU  668  CB  VAL A  93     9092  15149   8310    362   2066  -2697       C  
ATOM    669  CG1 VAL A  93      16.933  77.615 273.721  1.00 97.17           C  
ANISOU  669  CG1 VAL A  93    10706  16748   9468    396   2143  -2833       C  
ATOM    670  CG2 VAL A  93      17.674  76.794 275.950  1.00 81.63           C  
ANISOU  670  CG2 VAL A  93     8512  14493   8009    641   2020  -2896       C  
ATOM    671  N   GLY A  94      17.464  81.208 274.673  1.00 83.49           N  
ANISOU  671  N   GLY A  94     8783  15109   7830   -258   2208  -2113       N  
ATOM    672  CA  GLY A  94      17.133  82.370 273.869  1.00 80.95           C  
ANISOU  672  CA  GLY A  94     8598  14871   7289   -487   2279  -1889       C  
ATOM    673  C   GLY A  94      15.642  82.627 273.845  1.00 80.13           C  
ANISOU  673  C   GLY A  94     8774  14510   7160   -510   2072  -1777       C  
ATOM    674  O   GLY A  94      15.058  82.847 272.782  1.00 83.51           O  
ANISOU  674  O   GLY A  94     9375  15032   7324   -540   2087  -1726       O  
ATOM    675  N   HIS A  95      15.033  82.595 275.029  1.00 75.27           N  
ANISOU  675  N   HIS A  95     8191  13596   6810   -488   1879  -1738       N  
ATOM    676  CA  HIS A  95      13.591  82.762 275.189  1.00 72.51           C  
ANISOU  676  CA  HIS A  95     8066  13006   6479   -490   1670  -1648       C  
ATOM    677  C   HIS A  95      12.813  81.716 274.395  1.00 72.04           C  
ANISOU  677  C   HIS A  95     8132  12972   6269   -341   1591  -1848       C  
ATOM    678  O   HIS A  95      12.001  82.049 273.533  1.00 71.10           O  
ANISOU  678  O   HIS A  95     8176  12915   5926   -381   1544  -1775       O  
ATOM    679  CB  HIS A  95      13.161  84.174 274.780  1.00 77.62           C  
ANISOU  679  CB  HIS A  95     8860  13650   6979   -678   1690  -1358       C  
ATOM    680  CG  HIS A  95      13.687  85.247 275.682  1.00 82.31           C  
ANISOU  680  CG  HIS A  95     9389  14138   7746   -852   1734  -1164       C  
ATOM    681  ND1 HIS A  95      12.901  85.887 276.615  1.00 83.44           N  
ANISOU  681  ND1 HIS A  95     9642  14000   8064   -901   1578  -1011       N  
ATOM    682  CD2 HIS A  95      14.924  85.786 275.799  1.00 85.91           C  
ANISOU  682  CD2 HIS A  95     9677  14739   8224  -1001   1920  -1116       C  
ATOM    683  CE1 HIS A  95      13.629  86.778 277.265  1.00 84.39           C  
ANISOU  683  CE1 HIS A  95     9687  14077   8301  -1074   1663   -883       C  
ATOM    684  NE2 HIS A  95      14.860  86.736 276.789  1.00 87.31           N  
ANISOU  684  NE2 HIS A  95     9881  14708   8585  -1151   1866   -944       N  
ATOM    685  N   SER A  96      13.073  80.449 274.699  1.00 74.39           N  
ANISOU  685  N   SER A  96     8359  13220   6685   -168   1574  -2103       N  
ATOM    686  CA  SER A  96      12.373  79.337 274.068  1.00 76.12           C  
ANISOU  686  CA  SER A  96     8706  13420   6796    -42   1499  -2334       C  
ATOM    687  C   SER A  96      12.207  78.179 275.049  1.00 78.09           C  
ANISOU  687  C   SER A  96     8949  13410   7311    108   1393  -2520       C  
ATOM    688  O   SER A  96      13.144  77.823 275.766  1.00 84.04           O  
ANISOU  688  O   SER A  96     9553  14137   8240    208   1463  -2576       O  
ATOM    689  CB  SER A  96      13.119  78.866 272.820  1.00 78.20           C  
ANISOU  689  CB  SER A  96     8940  13983   6789     30   1688  -2507       C  
ATOM    690  OG  SER A  96      12.489  77.732 272.252  1.00 81.18           O  
ANISOU  690  OG  SER A  96     9453  14324   7068    146   1619  -2766       O  
ATOM    691  N   TRP A  97      11.012  77.600 275.085  1.00 71.66           N  
ANISOU  691  N   TRP A  97     8294  12414   6519    119   1225  -2609       N  
ATOM    692  CA  TRP A  97      10.743  76.474 275.971  1.00 71.82           C  
ANISOU  692  CA  TRP A  97     8353  12158   6779    238   1132  -2775       C  
ATOM    693  C   TRP A  97      10.990  75.146 275.262  1.00 78.29           C  
ANISOU  693  C   TRP A  97     9245  13003   7498    389   1206  -3091       C  
ATOM    694  O   TRP A  97      10.245  74.767 274.359  1.00 85.20           O  
ANISOU  694  O   TRP A  97    10260  13931   8183    350   1160  -3227       O  
ATOM    695  CB  TRP A  97       9.308  76.532 276.492  1.00 72.08           C  
ANISOU  695  CB  TRP A  97     8510  11966   6912    144    924  -2707       C  
ATOM    696  CG  TRP A  97       9.053  75.542 277.576  1.00 72.02           C  
ANISOU  696  CG  TRP A  97     8543  11651   7169    231    842  -2820       C  
ATOM    697  CD1 TRP A  97       8.482  74.312 277.444  1.00 74.91           C  
ANISOU  697  CD1 TRP A  97     9048  11858   7558    281    792  -3058       C  
ATOM    698  CD2 TRP A  97       9.377  75.689 278.961  1.00 71.56           C  
ANISOU  698  CD2 TRP A  97     8406  11403   7381    270    810  -2699       C  
ATOM    699  NE1 TRP A  97       8.424  73.684 278.664  1.00 74.03           N  
ANISOU  699  NE1 TRP A  97     8961  11451   7716    353    740  -3073       N  
ATOM    700  CE2 TRP A  97       8.967  74.510 279.614  1.00 75.11           C  
ANISOU  700  CE2 TRP A  97     8960  11579   8001    358    745  -2853       C  
ATOM    701  CE3 TRP A  97       9.972  76.705 279.716  1.00 72.52           C  
ANISOU  701  CE3 TRP A  97     8389  11557   7606    228    832  -2481       C  
ATOM    702  CZ2 TRP A  97       9.132  74.318 280.984  1.00 78.19           C  
ANISOU  702  CZ2 TRP A  97     9321  11743   8646    427    699  -2778       C  
ATOM    703  CZ3 TRP A  97      10.135  76.514 281.076  1.00 74.88           C  
ANISOU  703  CZ3 TRP A  97     8645  11647   8157    290    775  -2429       C  
ATOM    704  CH2 TRP A  97       9.716  75.330 281.696  1.00 77.22           C  
ANISOU  704  CH2 TRP A  97     9047  11687   8605    399    709  -2569       C  
ATOM    705  N   GLU A  98      12.032  74.437 275.682  1.00 77.54           N  
ANISOU  705  N   GLU A  98     9059  12875   7527    573   1316  -3217       N  
ATOM    706  CA  GLU A  98      12.446  73.217 274.998  1.00 80.46           C  
ANISOU  706  CA  GLU A  98     9502  13271   7798    755   1421  -3520       C  
ATOM    707  C   GLU A  98      12.267  71.965 275.853  1.00 80.94           C  
ANISOU  707  C   GLU A  98     9677  12983   8095    915   1359  -3688       C  
ATOM    708  O   GLU A  98      12.912  70.946 275.608  1.00 83.12           O  
ANISOU  708  O   GLU A  98     9992  13230   8359   1128   1470  -3918       O  
ATOM    709  CB  GLU A  98      13.910  73.334 274.563  1.00 84.25           C  
ANISOU  709  CB  GLU A  98     9787  14045   8178    887   1640  -3557       C  
ATOM    710  CG  GLU A  98      14.232  74.597 273.775  1.00 87.97           C  
ANISOU  710  CG  GLU A  98    10146  14857   8424    714   1739  -3369       C  
ATOM    711  CD  GLU A  98      13.658  74.578 272.371  1.00 91.82           C  
ANISOU  711  CD  GLU A  98    10784  15521   8581    640   1762  -3467       C  
ATOM    712  OE1 GLU A  98      13.351  73.477 271.865  1.00 91.70           O  
ANISOU  712  OE1 GLU A  98    10919  15435   8488    752   1755  -3742       O  
ATOM    713  OE2 GLU A  98      13.518  75.665 271.772  1.00 94.32           O  
ANISOU  713  OE2 GLU A  98    11085  16044   8706    470   1788  -3270       O  
ATOM    714  N   LEU A  99      11.390  72.036 276.849  1.00 80.23           N  
ANISOU  714  N   LEU A  99     9655  12619   8210    821   1192  -3571       N  
ATOM    715  CA  LEU A  99      11.230  70.928 277.786  1.00 82.42           C  
ANISOU  715  CA  LEU A  99    10052  12543   8720    957   1142  -3683       C  
ATOM    716  C   LEU A  99       9.813  70.362 277.810  1.00 85.48           C  
ANISOU  716  C   LEU A  99    10663  12676   9140    811    998  -3776       C  
ATOM    717  O   LEU A  99       9.263  70.096 278.878  1.00 85.80           O  
ANISOU  717  O   LEU A  99    10769  12433   9399    786    897  -3706       O  
ATOM    718  CB  LEU A  99      11.633  71.370 279.193  1.00 79.95           C  
ANISOU  718  CB  LEU A  99     9604  12119   8654   1004   1094  -3467       C  
ATOM    719  CG  LEU A  99      13.059  71.908 279.332  1.00 78.63           C  
ANISOU  719  CG  LEU A  99     9183  12212   8483   1129   1223  -3382       C  
ATOM    720  CD1 LEU A  99      13.383  72.219 280.787  1.00 79.36           C  
ANISOU  720  CD1 LEU A  99     9158  12180   8816   1175   1150  -3203       C  
ATOM    721  CD2 LEU A  99      14.063  70.925 278.750  1.00 75.79           C  
ANISOU  721  CD2 LEU A  99     8807  11944   8045   1396   1385  -3622       C  
ATOM    722  N   GLY A 100       9.226  70.173 276.633  1.00 87.64           N  
ANISOU  722  N   GLY A 100    11043  13072   9185    706    991  -3937       N  
ATOM    723  CA  GLY A 100       7.914  69.559 276.535  1.00 88.33           C  
ANISOU  723  CA  GLY A 100    11320  12962   9278    549    860  -4070       C  
ATOM    724  C   GLY A 100       6.768  70.495 276.866  1.00 87.18           C  
ANISOU  724  C   GLY A 100    11120  12848   9155    321    689  -3851       C  
ATOM    725  O   GLY A 100       6.972  71.686 277.100  1.00 82.53           O  
ANISOU  725  O   GLY A 100    10375  12422   8561    285    675  -3591       O  
ATOM    726  N   THR A 101       5.557  69.948 276.892  1.00 91.59           N  
ANISOU  726  N   THR A 101    11810  13250   9740    165    566  -3964       N  
ATOM    727  CA  THR A 101       4.352  70.745 277.097  1.00 87.33           C  
ANISOU  727  CA  THR A 101    11211  12774   9198    -37    400  -3791       C  
ATOM    728  C   THR A 101       3.782  70.565 278.501  1.00 77.54           C  
ANISOU  728  C   THR A 101     9986  11224   8250    -85    319  -3677       C  
ATOM    729  O   THR A 101       3.312  71.524 279.115  1.00 69.61           O  
ANISOU  729  O   THR A 101     8872  10260   7318   -156    231  -3431       O  
ATOM    730  CB  THR A 101       3.264  70.389 276.063  1.00 70.13           C  
ANISOU  730  CB  THR A 101     9118  10724   6805   -211    299  -3991       C  
ATOM    731  OG1 THR A 101       3.820  70.448 274.744  1.00 94.95           O  
ANISOU  731  OG1 THR A 101    12272  14152   9654   -154    384  -4119       O  
ATOM    732  CG2 THR A 101       2.093  71.354 276.158  1.00 68.63           C  
ANISOU  732  CG2 THR A 101     8821  10681   6572   -377    129  -3791       C  
ATOM    733  N   THR A 102       3.819  69.334 279.003  1.00 80.91           N  
ANISOU  733  N   THR A 102    10570  11335   8836    -40    359  -3854       N  
ATOM    734  CA  THR A 102       3.316  69.042 280.341  1.00 85.01           C  
ANISOU  734  CA  THR A 102    11133  11546   9621    -81    305  -3752       C  
ATOM    735  C   THR A 102       4.169  69.725 281.405  1.00 81.81           C  
ANISOU  735  C   THR A 102    10603  11106   9375     76    341  -3497       C  
ATOM    736  O   THR A 102       3.647  70.276 282.373  1.00 79.14           O  
ANISOU  736  O   THR A 102    10203  10692   9177      5    261  -3296       O  
ATOM    737  CB  THR A 102       3.281  67.527 280.616  1.00 93.28           C  
ANISOU  737  CB  THR A 102    12418  12231  10792    -52    366  -3991       C  
ATOM    738  OG1 THR A 102       4.609  66.995 280.537  1.00101.92           O  
ANISOU  738  OG1 THR A 102    13568  13260  11898    219    512  -4078       O  
ATOM    739  CG2 THR A 102       2.392  66.822 279.604  1.00 94.32           C  
ANISOU  739  CG2 THR A 102    12682  12383  10771   -250    324  -4273       C  
ATOM    740  N   PHE A 103       5.485  69.684 281.215  1.00 86.84           N  
ANISOU  740  N   PHE A 103    11195  11821   9981    286    465  -3517       N  
ATOM    741  CA APHE A 103       6.411  70.335 282.134  0.50 89.50           C  
ANISOU  741  CA APHE A 103    11385  12179  10443    428    499  -3303       C  
ATOM    742  CA BPHE A 103       6.415  70.332 282.131  0.50 89.51           C  
ANISOU  742  CA BPHE A 103    11387  12181  10444    429    500  -3304       C  
ATOM    743  C   PHE A 103       6.239  71.848 282.090  1.00 87.08           C  
ANISOU  743  C   PHE A 103    10900  12121  10064    308    439  -3061       C  
ATOM    744  O   PHE A 103       6.516  72.542 283.067  1.00 92.10           O  
ANISOU  744  O   PHE A 103    11434  12730  10830    330    415  -2856       O  
ATOM    745  CB APHE A 103       7.857  69.958 281.804  0.50 89.82           C  
ANISOU  745  CB APHE A 103    11378  12311  10438    673    648  -3402       C  
ATOM    746  CB BPHE A 103       7.857  69.951 281.786  0.50 89.85           C  
ANISOU  746  CB BPHE A 103    11383  12316  10440    673    648  -3405       C  
ATOM    747  CG APHE A 103       8.204  68.535 282.137  0.50 94.48           C  
ANISOU  747  CG APHE A 103    12150  12607  11141    864    716  -3591       C  
ATOM    748  CG BPHE A 103       8.789  69.967 282.963  0.50 90.83           C  
ANISOU  748  CG BPHE A 103    11417  12349  10746    865    680  -3275       C  
ATOM    749  CD1APHE A 103       8.719  68.208 283.381  0.50 92.20           C  
ANISOU  749  CD1APHE A 103    11864  12112  11054   1039    721  -3490       C  
ATOM    750  CD1BPHE A 103       9.027  68.810 283.688  0.50 90.73           C  
ANISOU  750  CD1BPHE A 103    11551  12034  10887   1048    709  -3365       C  
ATOM    751  CD2APHE A 103       8.018  67.525 281.207  0.50 94.70           C  
ANISOU  751  CD2APHE A 103    12365  12557  11060    879    775  -3872       C  
ATOM    752  CD2BPHE A 103       9.429  71.134 283.344  0.50 86.74           C  
ANISOU  752  CD2BPHE A 103    10676  12045  10235    861    679  -3064       C  
ATOM    753  CE1APHE A 103       9.040  66.901 283.692  0.50 93.45           C  
ANISOU  753  CE1APHE A 103    12221  11977  11308   1244    789  -3643       C  
ATOM    754  CE1BPHE A 103       9.885  68.818 284.771  0.50 89.10           C  
ANISOU  754  CE1BPHE A 103    11255  11776  10825   1248    722  -3240       C  
ATOM    755  CE2APHE A 103       8.338  66.216 281.512  0.50 96.06           C  
ANISOU  755  CE2APHE A 103    12745  12417  11338   1067    850  -4045       C  
ATOM    756  CE2BPHE A 103      10.288  71.148 284.426  0.50 85.43           C  
ANISOU  756  CE2BPHE A 103    10408  11832  10220   1027    692  -2961       C  
ATOM    757  CZ APHE A 103       8.849  65.903 282.756  0.50 95.70           C  
ANISOU  757  CZ APHE A 103    12713  12153  11498   1259    859  -3920       C  
ATOM    758  CZ BPHE A 103      10.516  69.988 285.140  0.50 86.52           C  
ANISOU  758  CZ BPHE A 103    10677  11702  10496   1233    706  -3046       C  
ATOM    759  N   CYS A 104       5.779  72.351 280.949  1.00 86.07           N  
ANISOU  759  N   CYS A 104    10755  12231   9718    187    417  -3088       N  
ATOM    760  CA  CYS A 104       5.504  73.774 280.784  1.00 84.16           C  
ANISOU  760  CA  CYS A 104    10392  12203   9384     79    363  -2857       C  
ATOM    761  C   CYS A 104       4.331  74.184 281.664  1.00 80.55           C  
ANISOU  761  C   CYS A 104     9939  11606   9059    -43    222  -2708       C  
ATOM    762  O   CYS A 104       4.320  75.271 282.243  1.00 75.71           O  
ANISOU  762  O   CYS A 104     9238  11028   8499    -70    189  -2478       O  
ATOM    763  CB  CYS A 104       5.210  74.101 279.316  1.00 87.14           C  
ANISOU  763  CB  CYS A 104    10778  12860   9469      2    366  -2924       C  
ATOM    764  SG  CYS A 104       4.564  75.763 279.019  1.00 74.32           S  
ANISOU  764  SG  CYS A 104     9073  11458   7709   -123    280  -2636       S  
ATOM    765  N   LYS A 105       3.343  73.300 281.759  1.00 82.44           N  
ANISOU  765  N   LYS A 105    10286  11687   9350   -126    149  -2850       N  
ATOM    766  CA  LYS A 105       2.177  73.534 282.599  1.00 80.08           C  
ANISOU  766  CA  LYS A 105     9981  11267   9178   -245     29  -2736       C  
ATOM    767  C   LYS A 105       2.556  73.495 284.077  1.00 75.10           C  
ANISOU  767  C   LYS A 105     9345  10397   8793   -165     48  -2606       C  
ATOM    768  O   LYS A 105       2.089  74.313 284.870  1.00 72.49           O  
ANISOU  768  O   LYS A 105     8948  10048   8547   -209    -17  -2410       O  
ATOM    769  CB  LYS A 105       1.089  72.498 282.307  1.00 78.96           C  
ANISOU  769  CB  LYS A 105     9946  11029   9029   -383    -35  -2947       C  
ATOM    770  CG  LYS A 105       0.491  72.573 280.911  1.00 77.73           C  
ANISOU  770  CG  LYS A 105     9781  11139   8613   -486    -91  -3079       C  
ATOM    771  CD  LYS A 105      -0.460  71.407 280.673  1.00 80.23           C  
ANISOU  771  CD  LYS A 105    10206  11343   8935   -646   -144  -3332       C  
ATOM    772  CE  LYS A 105      -1.182  71.527 279.341  1.00 79.12           C  
ANISOU  772  CE  LYS A 105    10034  11507   8521   -766   -233  -3466       C  
ATOM    773  NZ  LYS A 105      -2.129  72.678 279.318  1.00 75.11           N  
ANISOU  773  NZ  LYS A 105     9368  11236   7933   -832   -370  -3258       N  
ATOM    774  N   LEU A 106       3.406  72.538 284.437  1.00 74.39           N  
ANISOU  774  N   LEU A 106     9332  10130   8803    -30    136  -2719       N  
ATOM    775  CA  LEU A 106       3.865  72.384 285.813  1.00 73.75           C  
ANISOU  775  CA  LEU A 106     9256   9836   8929     77    152  -2607       C  
ATOM    776  C   LEU A 106       4.693  73.583 286.263  1.00 71.90           C  
ANISOU  776  C   LEU A 106     8863   9751   8706    144    165  -2400       C  
ATOM    777  O   LEU A 106       4.421  74.180 287.305  1.00 73.88           O  
ANISOU  777  O   LEU A 106     9073   9927   9071    117    110  -2228       O  
ATOM    778  CB  LEU A 106       4.686  71.101 285.966  1.00 77.13           C  
ANISOU  778  CB  LEU A 106     9807  10069   9428    253    247  -2772       C  
ATOM    779  CG  LEU A 106       3.955  69.771 285.766  1.00 82.50           C  
ANISOU  779  CG  LEU A 106    10699  10506  10141    186    254  -2983       C  
ATOM    780  CD1 LEU A 106       4.924  68.605 285.900  1.00 86.07           C  
ANISOU  780  CD1 LEU A 106    11293  10754  10655    413    365  -3126       C  
ATOM    781  CD2 LEU A 106       2.808  69.632 286.753  1.00 82.61           C  
ANISOU  781  CD2 LEU A 106    10776  10311  10299     33    177  -2893       C  
ATOM    782  N   HIS A 107       5.705  73.921 285.468  1.00 66.48           N  
ANISOU  782  N   HIS A 107     8091   9276   7893    218    247  -2430       N  
ATOM    783  CA  HIS A 107       6.593  75.041 285.762  1.00 64.65           C  
ANISOU  783  CA  HIS A 107     7703   9204   7656    246    280  -2260       C  
ATOM    784  C   HIS A 107       5.828  76.349 285.931  1.00 65.96           C  
ANISOU  784  C   HIS A 107     7827   9436   7797     93    200  -2058       C  
ATOM    785  O   HIS A 107       6.164  77.173 286.782  1.00 67.22           O  
ANISOU  785  O   HIS A 107     7913   9584   8042     87    186  -1897       O  
ATOM    786  CB  HIS A 107       7.640  75.189 284.656  1.00 63.84           C  
ANISOU  786  CB  HIS A 107     7516   9353   7387    303    396  -2338       C  
ATOM    787  CG  HIS A 107       8.304  76.528 284.628  1.00 65.22           C  
ANISOU  787  CG  HIS A 107     7542   9731   7506    240    435  -2161       C  
ATOM    788  ND1 HIS A 107       9.242  76.916 285.558  1.00 69.43           N  
ANISOU  788  ND1 HIS A 107     7950  10274   8156    298    460  -2068       N  
ATOM    789  CD2 HIS A 107       8.163  77.577 283.778  1.00 68.07           C  
ANISOU  789  CD2 HIS A 107     7874  10288   7702    114    455  -2060       C  
ATOM    790  CE1 HIS A 107       9.653  78.142 285.286  1.00 72.76           C  
ANISOU  790  CE1 HIS A 107     8273  10877   8497    182    502  -1930       C  
ATOM    791  NE2 HIS A 107       9.011  78.563 284.208  1.00 71.89           N  
ANISOU  791  NE2 HIS A 107     8232  10867   8216     77    506  -1912       N  
ATOM    792  N   SER A 108       4.795  76.532 285.118  1.00 66.35           N  
ANISOU  792  N   SER A 108     7928   9560   7723    -19    143  -2076       N  
ATOM    793  CA  SER A 108       3.975  77.733 285.187  1.00 65.60           C  
ANISOU  793  CA  SER A 108     7809   9530   7588   -125     65  -1888       C  
ATOM    794  C   SER A 108       3.072  77.710 286.415  1.00 60.60           C  
ANISOU  794  C   SER A 108     7202   8695   7129   -156    -26  -1806       C  
ATOM    795  O   SER A 108       2.835  78.744 287.038  1.00 55.62           O  
ANISOU  795  O   SER A 108     6538   8053   6542   -184    -62  -1625       O  
ATOM    796  CB  SER A 108       3.133  77.882 283.918  1.00 68.71           C  
ANISOU  796  CB  SER A 108     8234  10100   7774   -204     20  -1934       C  
ATOM    797  OG  SER A 108       3.957  77.961 282.768  1.00 73.93           O  
ANISOU  797  OG  SER A 108     8879  10963   8247   -178    115  -1997       O  
ATOM    798  N   SER A 109       2.575  76.524 286.755  1.00 59.04           N  
ANISOU  798  N   SER A 109     7079   8331   7025   -155    -49  -1944       N  
ATOM    799  CA  SER A 109       1.669  76.357 287.886  1.00 58.07           C  
ANISOU  799  CA  SER A 109     6987   8022   7056   -199   -116  -1880       C  
ATOM    800  C   SER A 109       2.341  76.725 289.205  1.00 61.86           C  
ANISOU  800  C   SER A 109     7441   8379   7684   -116    -97  -1745       C  
ATOM    801  O   SER A 109       1.702  77.263 290.111  1.00 58.87           O  
ANISOU  801  O   SER A 109     7052   7927   7387   -152   -150  -1615       O  
ATOM    802  CB  SER A 109       1.160  74.917 287.948  1.00 57.72           C  
ANISOU  802  CB  SER A 109     7051   7801   7077   -232   -115  -2064       C  
ATOM    803  OG  SER A 109       0.570  74.533 286.719  1.00 60.41           O  
ANISOU  803  OG  SER A 109     7414   8268   7269   -326   -138  -2221       O  
ATOM    804  N   ILE A 110       3.634  76.433 289.302  1.00 61.96           N  
ANISOU  804  N   ILE A 110     7432   8392   7719      2    -24  -1786       N  
ATOM    805  CA  ILE A 110       4.404  76.723 290.505  1.00 57.06           C  
ANISOU  805  CA  ILE A 110     6766   7697   7215     88    -15  -1681       C  
ATOM    806  C   ILE A 110       4.437  78.225 290.784  1.00 57.52           C  
ANISOU  806  C   ILE A 110     6744   7861   7250     18    -41  -1503       C  
ATOM    807  O   ILE A 110       4.374  78.655 291.936  1.00 62.75           O  
ANISOU  807  O   ILE A 110     7401   8430   8011     25    -77  -1394       O  
ATOM    808  CB  ILE A 110       5.841  76.181 290.388  1.00 57.07           C  
ANISOU  808  CB  ILE A 110     6718   7750   7216    241     65  -1769       C  
ATOM    809  CG1 ILE A 110       5.816  74.658 290.242  1.00 58.70           C  
ANISOU  809  CG1 ILE A 110     7048   7794   7460    342     99  -1942       C  
ATOM    810  CG2 ILE A 110       6.667  76.580 291.596  1.00 59.43           C  
ANISOU  810  CG2 ILE A 110     6937   8033   7612    323     55  -1662       C  
ATOM    811  CD1 ILE A 110       7.187  74.021 290.189  1.00 65.23           C  
ANISOU  811  CD1 ILE A 110     7831   8661   8291    546    179  -2034       C  
ATOM    812  N   PHE A 111       4.521  79.016 289.720  1.00 57.54           N  
ANISOU  812  N   PHE A 111     6706   8045   7111    -49    -17  -1476       N  
ATOM    813  CA  PHE A 111       4.501  80.470 289.839  1.00 57.24           C  
ANISOU  813  CA  PHE A 111     6635   8077   7036   -124    -27  -1306       C  
ATOM    814  C   PHE A 111       3.203  80.956 290.473  1.00 59.54           C  
ANISOU  814  C   PHE A 111     6982   8260   7379   -169   -113  -1199       C  
ATOM    815  O   PHE A 111       3.219  81.766 291.398  1.00 60.15           O  
ANISOU  815  O   PHE A 111     7061   8268   7527   -180   -131  -1079       O  
ATOM    816  CB  PHE A 111       4.687  81.123 288.466  1.00 53.23           C  
ANISOU  816  CB  PHE A 111     6114   7766   6344   -183     23  -1287       C  
ATOM    817  CG  PHE A 111       4.490  82.616 288.470  1.00 47.49           C  
ANISOU  817  CG  PHE A 111     5407   7071   5566   -263     19  -1100       C  
ATOM    818  CD1 PHE A 111       3.264  83.171 288.132  1.00 44.73           C  
ANISOU  818  CD1 PHE A 111     5126   6723   5146   -287    -49  -1010       C  
ATOM    819  CD2 PHE A 111       5.532  83.463 288.807  1.00 48.59           C  
ANISOU  819  CD2 PHE A 111     5500   7240   5724   -310     86  -1020       C  
ATOM    820  CE1 PHE A 111       3.082  84.542 288.136  1.00 45.68           C  
ANISOU  820  CE1 PHE A 111     5299   6841   5218   -329    -44   -831       C  
ATOM    821  CE2 PHE A 111       5.357  84.835 288.811  1.00 49.10           C  
ANISOU  821  CE2 PHE A 111     5624   7289   5743   -394     96   -853       C  
ATOM    822  CZ  PHE A 111       4.130  85.375 288.475  1.00 48.04           C  
ANISOU  822  CZ  PHE A 111     5589   7123   5541   -389     34   -753       C  
ATOM    823  N   PHE A 112       2.080  80.458 289.965  1.00 63.44           N  
ANISOU  823  N   PHE A 112     7515   8759   7831   -197   -163  -1256       N  
ATOM    824  CA  PHE A 112       0.771  80.884 290.444  1.00 67.46           C  
ANISOU  824  CA  PHE A 112     8042   9217   8372   -231   -240  -1166       C  
ATOM    825  C   PHE A 112       0.441  80.249 291.790  1.00 65.84           C  
ANISOU  825  C   PHE A 112     7860   8823   8333   -212   -260  -1173       C  
ATOM    826  O   PHE A 112      -0.258  80.847 292.609  1.00 63.00           O  
ANISOU  826  O   PHE A 112     7503   8404   8028   -217   -296  -1065       O  
ATOM    827  CB  PHE A 112      -0.314  80.547 289.418  1.00 71.20           C  
ANISOU  827  CB  PHE A 112     8513   9809   8731   -280   -294  -1237       C  
ATOM    828  CG  PHE A 112      -0.143  81.251 288.102  1.00 74.87           C  
ANISOU  828  CG  PHE A 112     8970  10475   9001   -287   -285  -1203       C  
ATOM    829  CD1 PHE A 112      -0.505  82.581 287.958  1.00 75.85           C  
ANISOU  829  CD1 PHE A 112     9105  10665   9048   -273   -308  -1025       C  
ATOM    830  CD2 PHE A 112       0.379  80.583 287.007  1.00 76.96           C  
ANISOU  830  CD2 PHE A 112     9239  10853   9148   -296   -244  -1346       C  
ATOM    831  CE1 PHE A 112      -0.348  83.230 286.747  1.00 76.50           C  
ANISOU  831  CE1 PHE A 112     9209  10922   8936   -273   -291   -970       C  
ATOM    832  CE2 PHE A 112       0.539  81.227 285.794  1.00 76.25           C  
ANISOU  832  CE2 PHE A 112     9153  10962   8856   -302   -226  -1305       C  
ATOM    833  CZ  PHE A 112       0.175  82.552 285.664  1.00 76.00           C  
ANISOU  833  CZ  PHE A 112     9140  10993   8745   -292   -250  -1107       C  
ATOM    834  N   LEU A 113       0.945  79.038 292.012  1.00 66.07           N  
ANISOU  834  N   LEU A 113     7919   8753   8430   -175   -226  -1297       N  
ATOM    835  CA  LEU A 113       0.756  78.361 293.290  1.00 61.38           C  
ANISOU  835  CA  LEU A 113     7375   7968   7979   -145   -230  -1290       C  
ATOM    836  C   LEU A 113       1.394  79.177 294.402  1.00 58.94           C  
ANISOU  836  C   LEU A 113     7045   7620   7731    -89   -230  -1162       C  
ATOM    837  O   LEU A 113       0.789  79.394 295.449  1.00 58.37           O  
ANISOU  837  O   LEU A 113     6997   7452   7729    -94   -257  -1080       O  
ATOM    838  CB  LEU A 113       1.346  76.951 293.259  1.00 58.58           C  
ANISOU  838  CB  LEU A 113     7089   7498   7672    -83   -183  -1433       C  
ATOM    839  CG  LEU A 113       1.182  76.136 294.542  1.00 55.30           C  
ANISOU  839  CG  LEU A 113     6761   6861   7388    -39   -176  -1414       C  
ATOM    840  CD1 LEU A 113      -0.274  76.108 294.959  1.00 57.15           C  
ANISOU  840  CD1 LEU A 113     7020   7033   7661   -162   -209  -1374       C  
ATOM    841  CD2 LEU A 113       1.711  74.724 294.356  1.00 53.69           C  
ANISOU  841  CD2 LEU A 113     6664   6518   7218     41   -121  -1555       C  
ATOM    842  N   ASN A 114       2.618  79.632 294.157  1.00 58.44           N  
ANISOU  842  N   ASN A 114     6927   7648   7629    -47   -196  -1156       N  
ATOM    843  CA  ASN A 114       3.313  80.515 295.081  1.00 60.13           C  
ANISOU  843  CA  ASN A 114     7106   7861   7880    -28   -201  -1057       C  
ATOM    844  C   ASN A 114       2.542  81.811 295.292  1.00 60.47           C  
ANISOU  844  C   ASN A 114     7167   7908   7900   -100   -231   -929       C  
ATOM    845  O   ASN A 114       2.467  82.325 296.406  1.00 65.61           O  
ANISOU  845  O   ASN A 114     7839   8480   8608    -91   -253   -854       O  
ATOM    846  CB  ASN A 114       4.720  80.825 294.569  1.00 65.90           C  
ANISOU  846  CB  ASN A 114     7747   8736   8558    -13   -150  -1089       C  
ATOM    847  CG  ASN A 114       5.438  81.853 295.422  1.00 74.48           C  
ANISOU  847  CG  ASN A 114     8784   9848   9669    -42   -157  -1003       C  
ATOM    848  OD1 ASN A 114       5.353  81.829 296.650  1.00 81.20           O  
ANISOU  848  OD1 ASN A 114     9658  10599  10595     -3   -200   -964       O  
ATOM    849  ND2 ASN A 114       6.145  82.771 294.772  1.00 74.86           N  
ANISOU  849  ND2 ASN A 114     8770  10030   9643   -126   -110   -977       N  
ATOM    850  N   MET A 115       1.966  82.328 294.212  1.00 59.08           N  
ANISOU  850  N   MET A 115     6995   7826   7627   -154   -232   -907       N  
ATOM    851  CA  MET A 115       1.232  83.586 294.259  1.00 56.22           C  
ANISOU  851  CA  MET A 115     6668   7468   7227   -185   -255   -778       C  
ATOM    852  C   MET A 115      -0.002  83.495 295.151  1.00 53.70           C  
ANISOU  852  C   MET A 115     6375   7051   6977   -162   -303   -738       C  
ATOM    853  O   MET A 115      -0.186  84.313 296.052  1.00 51.35           O  
ANISOU  853  O   MET A 115     6114   6680   6718   -146   -310   -648       O  
ATOM    854  CB  MET A 115       0.821  84.013 292.851  1.00 52.19           C  
ANISOU  854  CB  MET A 115     6161   7095   6576   -213   -254   -758       C  
ATOM    855  CG  MET A 115       0.021  85.301 292.807  1.00 52.54           C  
ANISOU  855  CG  MET A 115     6260   7137   6566   -204   -278   -612       C  
ATOM    856  SD  MET A 115      -0.740  85.563 291.198  1.00 73.29           S  
ANISOU  856  SD  MET A 115     8891   9947   9009   -195   -305   -584       S  
ATOM    857  CE  MET A 115      -1.674  84.045 291.032  1.00 85.10           C  
ANISOU  857  CE  MET A 115    10308  11496  10532   -204   -369   -744       C  
ATOM    858  N   PHE A 116      -0.845  82.500 294.895  1.00 52.19           N  
ANISOU  858  N   PHE A 116     6168   6867   6797   -172   -326   -814       N  
ATOM    859  CA  PHE A 116      -2.066  82.326 295.671  1.00 54.55           C  
ANISOU  859  CA  PHE A 116     6466   7105   7156   -173   -356   -784       C  
ATOM    860  C   PHE A 116      -1.756  81.980 297.124  1.00 54.38           C  
ANISOU  860  C   PHE A 116     6484   6931   7245   -141   -337   -766       C  
ATOM    861  O   PHE A 116      -2.416  82.471 298.037  1.00 51.94           O  
ANISOU  861  O   PHE A 116     6190   6575   6971   -121   -344   -689       O  
ATOM    862  CB  PHE A 116      -2.953  81.243 295.053  1.00 58.01           C  
ANISOU  862  CB  PHE A 116     6868   7590   7582   -234   -377   -892       C  
ATOM    863  CG  PHE A 116      -3.689  81.689 293.822  1.00 61.18           C  
ANISOU  863  CG  PHE A 116     7213   8175   7856   -257   -424   -892       C  
ATOM    864  CD1 PHE A 116      -4.648  82.687 293.895  1.00 61.12           C  
ANISOU  864  CD1 PHE A 116     7167   8248   7807   -215   -464   -780       C  
ATOM    865  CD2 PHE A 116      -3.435  81.100 292.595  1.00 63.55           C  
ANISOU  865  CD2 PHE A 116     7502   8579   8066   -299   -429  -1007       C  
ATOM    866  CE1 PHE A 116      -5.330  83.096 292.764  1.00 63.67           C  
ANISOU  866  CE1 PHE A 116     7435   8762   7994   -204   -519   -768       C  
ATOM    867  CE2 PHE A 116      -4.115  81.503 291.461  1.00 63.67           C  
ANISOU  867  CE2 PHE A 116     7465   8789   7937   -311   -483  -1005       C  
ATOM    868  CZ  PHE A 116      -5.064  82.503 291.545  1.00 63.92           C  
ANISOU  868  CZ  PHE A 116     7453   8911   7924   -258   -534   -878       C  
ATOM    869  N   ALA A 117      -0.749  81.136 297.330  1.00 54.00           N  
ANISOU  869  N   ALA A 117     6458   6823   7239   -116   -312   -836       N  
ATOM    870  CA  ALA A 117      -0.357  80.730 298.675  1.00 52.10           C  
ANISOU  870  CA  ALA A 117     6262   6454   7079    -62   -302   -813       C  
ATOM    871  C   ALA A 117       0.141  81.922 299.484  1.00 59.21           C  
ANISOU  871  C   ALA A 117     7165   7359   7974    -35   -314   -723       C  
ATOM    872  O   ALA A 117      -0.275  82.122 300.625  1.00 63.56           O  
ANISOU  872  O   ALA A 117     7755   7834   8559    -12   -320   -665       O  
ATOM    873  CB  ALA A 117       0.709  79.649 298.616  1.00 49.18           C  
ANISOU  873  CB  ALA A 117     5910   6040   6735     -1   -279   -899       C  
ATOM    874  N   SER A 118       1.028  82.714 298.886  1.00 60.59           N  
ANISOU  874  N   SER A 118     7304   7620   8096    -53   -309   -719       N  
ATOM    875  CA  SER A 118       1.578  83.889 299.556  1.00 61.41           C  
ANISOU  875  CA  SER A 118     7422   7721   8191    -66   -314   -656       C  
ATOM    876  C   SER A 118       0.500  84.935 299.823  1.00 65.20           C  
ANISOU  876  C   SER A 118     7961   8157   8656    -78   -321   -567       C  
ATOM    877  O   SER A 118       0.644  85.770 300.713  1.00 71.02           O  
ANISOU  877  O   SER A 118     8747   8838   9400    -77   -324   -522       O  
ATOM    878  CB  SER A 118       2.711  84.502 298.728  1.00 60.41           C  
ANISOU  878  CB  SER A 118     7245   7700   8009   -122   -288   -674       C  
ATOM    879  OG  SER A 118       3.851  83.658 298.712  1.00 60.92           O  
ANISOU  879  OG  SER A 118     7232   7825   8089    -83   -279   -757       O  
ATOM    880  N   GLY A 119      -0.579  84.887 299.051  1.00 60.55           N  
ANISOU  880  N   GLY A 119     7363   7606   8036    -78   -325   -550       N  
ATOM    881  CA  GLY A 119      -1.690  85.798 299.248  1.00 61.50           C  
ANISOU  881  CA  GLY A 119     7522   7710   8137    -47   -332   -465       C  
ATOM    882  C   GLY A 119      -2.651  85.297 300.309  1.00 61.49           C  
ANISOU  882  C   GLY A 119     7518   7654   8193     -9   -335   -458       C  
ATOM    883  O   GLY A 119      -3.214  86.081 301.072  1.00 61.29           O  
ANISOU  883  O   GLY A 119     7536   7583   8169     39   -327   -396       O  
ATOM    884  N   PHE A 120      -2.835  83.981 300.357  1.00 61.02           N  
ANISOU  884  N   PHE A 120     7419   7588   8176    -34   -333   -524       N  
ATOM    885  CA  PHE A 120      -3.748  83.371 301.315  1.00 62.28           C  
ANISOU  885  CA  PHE A 120     7580   7697   8388    -29   -315   -514       C  
ATOM    886  C   PHE A 120      -3.123  83.296 302.704  1.00 65.43           C  
ANISOU  886  C   PHE A 120     8051   7988   8820     13   -300   -490       C  
ATOM    887  O   PHE A 120      -3.806  83.483 303.712  1.00 68.77           O  
ANISOU  887  O   PHE A 120     8501   8376   9254     41   -277   -443       O  
ATOM    888  CB  PHE A 120      -4.163  81.974 300.850  1.00 62.56           C  
ANISOU  888  CB  PHE A 120     7580   7734   8454    -98   -306   -594       C  
ATOM    889  CG  PHE A 120      -4.953  81.968 299.569  1.00 64.34           C  
ANISOU  889  CG  PHE A 120     7721   8096   8629   -150   -334   -634       C  
ATOM    890  CD1 PHE A 120      -5.614  83.107 299.138  1.00 66.09           C  
ANISOU  890  CD1 PHE A 120     7894   8431   8786   -105   -362   -567       C  
ATOM    891  CD2 PHE A 120      -5.034  80.820 298.798  1.00 64.52           C  
ANISOU  891  CD2 PHE A 120     7725   8133   8657   -233   -334   -742       C  
ATOM    892  CE1 PHE A 120      -6.340  83.101 297.961  1.00 64.95           C  
ANISOU  892  CE1 PHE A 120     7663   8445   8572   -133   -403   -598       C  
ATOM    893  CE2 PHE A 120      -5.758  80.808 297.622  1.00 65.01           C  
ANISOU  893  CE2 PHE A 120     7701   8348   8650   -289   -373   -794       C  
ATOM    894  CZ  PHE A 120      -6.412  81.950 297.203  1.00 63.91           C  
ANISOU  894  CZ  PHE A 120     7493   8354   8435   -234   -414   -717       C  
ATOM    895  N   LEU A 121      -1.822  83.020 302.751  1.00 61.91           N  
ANISOU  895  N   LEU A 121     7625   7518   8379     25   -313   -527       N  
ATOM    896  CA  LEU A 121      -1.109  82.939 304.020  1.00 57.74           C  
ANISOU  896  CA  LEU A 121     7151   6927   7861     77   -319   -510       C  
ATOM    897  C   LEU A 121      -1.018  84.305 304.686  1.00 60.43           C  
ANISOU  897  C   LEU A 121     7529   7269   8165     88   -329   -466       C  
ATOM    898  O   LEU A 121      -1.276  84.432 305.883  1.00 67.03           O  
ANISOU  898  O   LEU A 121     8420   8056   8991    127   -322   -434       O  
ATOM    899  CB  LEU A 121       0.289  82.352 303.822  1.00 55.05           C  
ANISOU  899  CB  LEU A 121     6787   6606   7523    107   -340   -567       C  
ATOM    900  CG  LEU A 121       0.344  80.836 303.618  1.00 57.95           C  
ANISOU  900  CG  LEU A 121     7175   6914   7930    140   -321   -612       C  
ATOM    901  CD1 LEU A 121       1.759  80.380 303.307  1.00 63.45           C  
ANISOU  901  CD1 LEU A 121     7832   7657   8620    208   -338   -672       C  
ATOM    902  CD2 LEU A 121      -0.195  80.109 304.841  1.00 56.55           C  
ANISOU  902  CD2 LEU A 121     7088   6622   7777    182   -298   -560       C  
ATOM    903  N   LEU A 122      -0.663  85.327 303.912  1.00 53.81           N  
ANISOU  903  N   LEU A 122     6678   6472   7295     48   -337   -466       N  
ATOM    904  CA  LEU A 122      -0.583  86.684 304.446  1.00 53.58           C  
ANISOU  904  CA  LEU A 122     6719   6405   7232     42   -335   -434       C  
ATOM    905  C   LEU A 122      -1.949  87.165 304.923  1.00 58.41           C  
ANISOU  905  C   LEU A 122     7380   6975   7838    101   -307   -378       C  
ATOM    906  O   LEU A 122      -2.042  88.019 305.803  1.00 63.12           O  
ANISOU  906  O   LEU A 122     8061   7512   8411    130   -296   -363       O  
ATOM    907  CB  LEU A 122      -0.019  87.649 303.402  1.00 49.89           C  
ANISOU  907  CB  LEU A 122     6258   5965   6732    -27   -328   -430       C  
ATOM    908  CG  LEU A 122       1.493  87.585 303.175  1.00 52.05           C  
ANISOU  908  CG  LEU A 122     6477   6300   6999   -102   -341   -488       C  
ATOM    909  CD1 LEU A 122       1.944  88.716 302.268  1.00 51.88           C  
ANISOU  909  CD1 LEU A 122     6489   6287   6936   -198   -309   -466       C  
ATOM    910  CD2 LEU A 122       2.242  87.627 304.497  1.00 58.43           C  
ANISOU  910  CD2 LEU A 122     7296   7097   7807   -102   -375   -527       C  
ATOM    911  N   SER A 123      -3.005  86.611 304.337  1.00 61.08           N  
ANISOU  911  N   SER A 123     7657   7360   8192    119   -294   -360       N  
ATOM    912  CA  SER A 123      -4.360  86.891 304.792  1.00 63.05           C  
ANISOU  912  CA  SER A 123     7904   7615   8436    184   -263   -314       C  
ATOM    913  C   SER A 123      -4.625  86.169 306.107  1.00 63.51           C  
ANISOU  913  C   SER A 123     7981   7637   8514    201   -233   -315       C  
ATOM    914  O   SER A 123      -5.198  86.739 307.035  1.00 65.13           O  
ANISOU  914  O   SER A 123     8234   7819   8695    264   -199   -285       O  
ATOM    915  CB  SER A 123      -5.386  86.470 303.739  1.00 63.59           C  
ANISOU  915  CB  SER A 123     7866   7790   8506    177   -267   -308       C  
ATOM    916  OG  SER A 123      -5.232  87.221 302.549  1.00 63.82           O  
ANISOU  916  OG  SER A 123     7894   7865   8488    185   -293   -288       O  
ATOM    917  N   ALA A 124      -4.196  84.912 306.176  1.00 61.86           N  
ANISOU  917  N   ALA A 124     7751   7414   8339    156   -239   -345       N  
ATOM    918  CA  ALA A 124      -4.363  84.103 307.377  1.00 61.10           C  
ANISOU  918  CA  ALA A 124     7699   7267   8250    172   -204   -327       C  
ATOM    919  C   ALA A 124      -3.604  84.708 308.554  1.00 62.95           C  
ANISOU  919  C   ALA A 124     8025   7460   8433    227   -221   -319       C  
ATOM    920  O   ALA A 124      -4.104  84.733 309.677  1.00 65.17           O  
ANISOU  920  O   ALA A 124     8360   7722   8679    269   -181   -286       O  
ATOM    921  CB  ALA A 124      -3.899  82.678 307.123  1.00 57.56           C  
ANISOU  921  CB  ALA A 124     7249   6778   7843    133   -206   -356       C  
ATOM    922  N   ILE A 125      -2.398  85.196 308.283  1.00 59.55           N  
ANISOU  922  N   ILE A 125     7604   7034   7987    214   -277   -359       N  
ATOM    923  CA  ILE A 125      -1.569  85.833 309.301  1.00 50.35           C  
ANISOU  923  CA  ILE A 125     6508   5858   6766    237   -311   -379       C  
ATOM    924  C   ILE A 125      -2.256  87.064 309.884  1.00 57.14           C  
ANISOU  924  C   ILE A 125     7445   6684   7581    264   -278   -367       C  
ATOM    925  O   ILE A 125      -2.287  87.254 311.100  1.00 65.60           O  
ANISOU  925  O   ILE A 125     8591   7740   8594    307   -270   -370       O  
ATOM    926  CB  ILE A 125      -0.197  86.239 308.728  1.00 45.56           C  
ANISOU  926  CB  ILE A 125     5864   5293   6155    180   -370   -436       C  
ATOM    927  CG1 ILE A 125       0.612  84.996 308.360  1.00 47.21           C  
ANISOU  927  CG1 ILE A 125     6001   5546   6393    197   -400   -458       C  
ATOM    928  CG2 ILE A 125       0.575  87.080 309.724  1.00 44.36           C  
ANISOU  928  CG2 ILE A 125     5770   5149   5938    166   -410   -478       C  
ATOM    929  CD1 ILE A 125       1.946  85.309 307.731  1.00 52.89           C  
ANISOU  929  CD1 ILE A 125     6643   6348   7107    145   -444   -519       C  
ATOM    930  N   SER A 126      -2.815  87.894 309.011  1.00 62.40           N  
ANISOU  930  N   SER A 126     8105   7340   8265    257   -256   -354       N  
ATOM    931  CA  SER A 126      -3.501  89.108 309.442  1.00 63.95           C  
ANISOU  931  CA  SER A 126     8392   7484   8424    316   -216   -343       C  
ATOM    932  C   SER A 126      -4.754  88.781 310.246  1.00 64.51           C  
ANISOU  932  C   SER A 126     8454   7578   8478    403   -151   -304       C  
ATOM    933  O   SER A 126      -5.049  89.438 311.244  1.00 63.77           O  
ANISOU  933  O   SER A 126     8454   7449   8328    468   -116   -315       O  
ATOM    934  CB  SER A 126      -3.862  89.977 308.236  1.00 65.87           C  
ANISOU  934  CB  SER A 126     8637   7709   8680    322   -206   -314       C  
ATOM    935  OG  SER A 126      -2.695  90.394 307.551  1.00 72.51           O  
ANISOU  935  OG  SER A 126     9500   8526   9523    223   -243   -343       O  
ATOM    936  N   LEU A 127      -5.486  87.762 309.809  1.00 62.59           N  
ANISOU  936  N   LEU A 127     8100   7403   8279    392   -129   -270       N  
ATOM    937  CA  LEU A 127      -6.707  87.353 310.490  1.00 62.86           C  
ANISOU  937  CA  LEU A 127     8095   7487   8303    440    -52   -232       C  
ATOM    938  C   LEU A 127      -6.402  86.682 311.827  1.00 69.51           C  
ANISOU  938  C   LEU A 127     9008   8303   9100    440    -27   -225       C  
ATOM    939  O   LEU A 127      -7.140  86.855 312.798  1.00 74.46           O  
ANISOU  939  O   LEU A 127     9666   8950   9673    500     46   -203       O  
ATOM    940  CB  LEU A 127      -7.527  86.415 309.603  1.00 58.08           C  
ANISOU  940  CB  LEU A 127     7345   6966   7757    382    -35   -213       C  
ATOM    941  CG  LEU A 127      -8.215  87.065 308.400  1.00 56.73           C  
ANISOU  941  CG  LEU A 127     7081   6875   7598    416    -53   -206       C  
ATOM    942  CD1 LEU A 127      -8.989  86.033 307.599  1.00 53.40           C  
ANISOU  942  CD1 LEU A 127     6505   6564   7221    332    -49   -212       C  
ATOM    943  CD2 LEU A 127      -9.133  88.194 308.845  1.00 59.42           C  
ANISOU  943  CD2 LEU A 127     7436   7248   7894    558     -3   -177       C  
ATOM    944  N   ASP A 128      -5.315  85.919 311.872  1.00 67.88           N  
ANISOU  944  N   ASP A 128     8826   8062   8902    390    -84   -238       N  
ATOM    945  CA  ASP A 128      -4.887  85.269 313.107  1.00 66.13           C  
ANISOU  945  CA  ASP A 128     8688   7821   8619    415    -77   -217       C  
ATOM    946  C   ASP A 128      -4.498  86.307 314.153  1.00 65.60           C  
ANISOU  946  C   ASP A 128     8725   7749   8450    474    -94   -253       C  
ATOM    947  O   ASP A 128      -4.883  86.208 315.318  1.00 64.27           O  
ANISOU  947  O   ASP A 128     8627   7594   8197    526    -43   -227       O  
ATOM    948  CB  ASP A 128      -3.714  84.325 312.840  1.00 66.71           C  
ANISOU  948  CB  ASP A 128     8760   7871   8716    390   -148   -226       C  
ATOM    949  CG  ASP A 128      -3.220  83.640 314.097  1.00 71.53           C  
ANISOU  949  CG  ASP A 128     9466   8469   9244    451   -154   -186       C  
ATOM    950  OD1 ASP A 128      -4.065  83.173 314.888  1.00 79.33           O  
ANISOU  950  OD1 ASP A 128    10505   9443  10193    468    -68   -120       O  
ATOM    951  OD2 ASP A 128      -1.989  83.575 314.298  1.00 68.37           O  
ANISOU  951  OD2 ASP A 128     9081   8090   8806    484   -244   -217       O  
ATOM    952  N   ARG A 129      -3.731  87.303 313.722  1.00 65.83           N  
ANISOU  952  N   ARG A 129     8774   7760   8480    451   -160   -319       N  
ATOM    953  CA  ARG A 129      -3.323  88.402 314.587  1.00 64.80           C  
ANISOU  953  CA  ARG A 129     8756   7607   8258    473   -179   -383       C  
ATOM    954  C   ARG A 129      -4.538  89.217 315.022  1.00 65.24           C  
ANISOU  954  C   ARG A 129     8872   7638   8278    555    -85   -376       C  
ATOM    955  O   ARG A 129      -4.579  89.751 316.131  1.00 70.69           O  
ANISOU  955  O   ARG A 129     9673   8320   8867    605    -63   -417       O  
ATOM    956  CB  ARG A 129      -2.301  89.288 313.867  1.00 67.76           C  
ANISOU  956  CB  ARG A 129     9139   7950   8658    389   -251   -456       C  
ATOM    957  CG  ARG A 129      -1.911  90.554 314.613  1.00 69.88           C  
ANISOU  957  CG  ARG A 129     9541   8166   8844    371   -264   -544       C  
ATOM    958  CD  ARG A 129      -1.353  90.246 315.990  1.00 73.01           C  
ANISOU  958  CD  ARG A 129     9990   8630   9122    391   -310   -587       C  
ATOM    959  NE  ARG A 129      -0.998  91.465 316.711  1.00 75.97           N  
ANISOU  959  NE  ARG A 129    10501   8957   9407    353   -326   -699       N  
ATOM    960  CZ  ARG A 129      -0.872  91.541 318.031  1.00 76.86           C  
ANISOU  960  CZ  ARG A 129    10702   9118   9382    392   -343   -753       C  
ATOM    961  NH1 ARG A 129      -1.082  90.466 318.779  1.00 77.70           N  
ANISOU  961  NH1 ARG A 129    10780   9319   9424    481   -341   -681       N  
ATOM    962  NH2 ARG A 129      -0.545  92.691 318.605  1.00 78.23           N  
ANISOU  962  NH2 ARG A 129    11012   9238   9475    338   -357   -879       N  
ATOM    963  N   CYS A 130      -5.533  89.298 314.144  1.00 63.08           N  
ANISOU  963  N   CYS A 130     8518   7371   8077    582    -30   -332       N  
ATOM    964  CA  CYS A 130      -6.770  90.008 314.443  1.00 61.41           C  
ANISOU  964  CA  CYS A 130     8327   7169   7838    694     64   -319       C  
ATOM    965  C   CYS A 130      -7.545  89.309 315.556  1.00 61.78           C  
ANISOU  965  C   CYS A 130     8360   7292   7823    741    152   -280       C  
ATOM    966  O   CYS A 130      -8.031  89.953 316.483  1.00 58.00           O  
ANISOU  966  O   CYS A 130     7965   6816   7256    836    220   -305       O  
ATOM    967  CB  CYS A 130      -7.636  90.125 313.186  1.00 58.31           C  
ANISOU  967  CB  CYS A 130     7813   6816   7527    722     83   -273       C  
ATOM    968  SG  CYS A 130      -9.174  91.054 313.400  1.00 58.75           S  
ANISOU  968  SG  CYS A 130     7855   6919   7549    907    191   -253       S  
ATOM    969  N   LEU A 131      -7.651  87.987 315.459  1.00 68.30           N  
ANISOU  969  N   LEU A 131     9096   8168   8687    670    161   -220       N  
ATOM    970  CA  LEU A 131      -8.371  87.194 316.449  1.00 74.81           C  
ANISOU  970  CA  LEU A 131     9917   9055   9454    682    261   -163       C  
ATOM    971  C   LEU A 131      -7.662  87.199 317.800  1.00 76.69           C  
ANISOU  971  C   LEU A 131    10308   9273   9559    718    249   -177       C  
ATOM    972  O   LEU A 131      -8.299  87.072 318.846  1.00 79.88           O  
ANISOU  972  O   LEU A 131    10757   9730   9865    769    348   -146       O  
ATOM    973  CB  LEU A 131      -8.544  85.755 315.958  1.00 80.27           C  
ANISOU  973  CB  LEU A 131    10515   9760  10224    573    276    -98       C  
ATOM    974  CG  LEU A 131      -9.431  85.547 314.731  1.00 84.54           C  
ANISOU  974  CG  LEU A 131    10885  10363  10873    516    297    -91       C  
ATOM    975  CD1 LEU A 131      -9.345  84.108 314.248  1.00 86.19           C  
ANISOU  975  CD1 LEU A 131    11047  10545  11156    382    297    -58       C  
ATOM    976  CD2 LEU A 131     -10.873  85.928 315.038  1.00 86.27           C  
ANISOU  976  CD2 LEU A 131    11003  10707  11068    574    415    -72       C  
ATOM    977  N   GLN A 132      -6.341  87.343 317.768  1.00 71.85           N  
ANISOU  977  N   GLN A 132     9762   8610   8929    689    127   -227       N  
ATOM    978  CA  GLN A 132      -5.535  87.348 318.983  1.00 65.57           C  
ANISOU  978  CA  GLN A 132     9092   7829   7992    721     81   -253       C  
ATOM    979  C   GLN A 132      -5.839  88.567 319.845  1.00 63.98           C  
ANISOU  979  C   GLN A 132     9004   7632   7675    796    122   -333       C  
ATOM    980  O   GLN A 132      -5.827  88.490 321.073  1.00 70.44           O  
ANISOU  980  O   GLN A 132     9922   8499   8343    848    150   -336       O  
ATOM    981  CB  GLN A 132      -4.047  87.312 318.630  1.00 63.91           C  
ANISOU  981  CB  GLN A 132     8882   7606   7796    668    -68   -306       C  
ATOM    982  CG  GLN A 132      -3.120  87.129 319.820  1.00 66.30           C  
ANISOU  982  CG  GLN A 132     9278   7968   7944    705   -143   -329       C  
ATOM    983  CD  GLN A 132      -1.658  87.140 319.417  1.00 68.56           C  
ANISOU  983  CD  GLN A 132     9516   8287   8247    653   -293   -394       C  
ATOM    984  OE1 GLN A 132      -1.289  87.723 318.397  1.00 71.02           O  
ANISOU  984  OE1 GLN A 132     9760   8562   8661    573   -331   -454       O  
ATOM    985  NE2 GLN A 132      -0.818  86.489 320.213  1.00 69.48           N  
ANISOU  985  NE2 GLN A 132     9658   8489   8252    706   -375   -375       N  
ATOM    986  N   VAL A 133      -6.118  89.690 319.192  1.00 56.88           N  
ANISOU  986  N   VAL A 133     8106   6671   6834    810    131   -398       N  
ATOM    987  CA  VAL A 133      -6.362  90.947 319.887  1.00 52.61           C  
ANISOU  987  CA  VAL A 133     7702   6090   6196    889    173   -494       C  
ATOM    988  C   VAL A 133      -7.853  91.200 320.104  1.00 56.03           C  
ANISOU  988  C   VAL A 133     8106   6564   6616   1016    326   -457       C  
ATOM    989  O   VAL A 133      -8.274  91.595 321.190  1.00 65.80           O  
ANISOU  989  O   VAL A 133     9445   7833   7722   1107    406   -498       O  
ATOM    990  CB  VAL A 133      -5.759  92.133 319.111  1.00 48.29           C  
ANISOU  990  CB  VAL A 133     7220   5420   5710    843    107   -586       C  
ATOM    991  CG1 VAL A 133      -5.945  93.426 319.883  1.00 52.45           C  
ANISOU  991  CG1 VAL A 133     7933   5863   6131    918    155   -700       C  
ATOM    992  CG2 VAL A 133      -4.286  91.885 318.833  1.00 43.02           C  
ANISOU  992  CG2 VAL A 133     6538   4751   5058    702    -34   -628       C  
ATOM    993  N   VAL A 134      -8.647  90.963 319.064  1.00 57.57           N  
ANISOU  993  N   VAL A 134     8151   6786   6939   1024    366   -388       N  
ATOM    994  CA  VAL A 134     -10.077  91.255 319.097  1.00 55.59           C  
ANISOU  994  CA  VAL A 134     7821   6613   6688   1153    501   -358       C  
ATOM    995  C   VAL A 134     -10.858  90.190 319.865  1.00 53.83           C  
ANISOU  995  C   VAL A 134     7509   6533   6412   1142    613   -279       C  
ATOM    996  O   VAL A 134     -11.825  90.499 320.561  1.00 53.72           O  
ANISOU  996  O   VAL A 134     7485   6608   6319   1256    745   -282       O  
ATOM    997  CB  VAL A 134     -10.643  91.384 317.664  1.00 52.38           C  
ANISOU  997  CB  VAL A 134     7260   6221   6420   1165    485   -315       C  
ATOM    998  CG1 VAL A 134     -12.152  91.564 317.683  1.00 57.89           C  
ANISOU  998  CG1 VAL A 134     7823   7057   7114   1306    614   -281       C  
ATOM    999  CG2 VAL A 134      -9.973  92.541 316.942  1.00 48.58           C  
ANISOU  999  CG2 VAL A 134     6898   5585   5974   1187    404   -375       C  
ATOM   1000  N   ARG A 135     -10.428  88.937 319.750  1.00 53.57           N  
ANISOU 1000  N   ARG A 135     7424   6515   6416   1007    574   -207       N  
ATOM   1001  CA  ARG A 135     -11.112  87.834 320.419  1.00 57.64           C  
ANISOU 1001  CA  ARG A 135     7883   7130   6887    961    691   -115       C  
ATOM   1002  C   ARG A 135     -10.190  87.081 321.381  1.00 55.88           C  
ANISOU 1002  C   ARG A 135     7807   6870   6554    916    653    -78       C  
ATOM   1003  O   ARG A 135      -9.849  85.925 321.131  1.00 56.61           O  
ANISOU 1003  O   ARG A 135     7878   6932   6698    814    626      0       O  
ATOM   1004  CB  ARG A 135     -11.679  86.862 319.383  1.00 63.96           C  
ANISOU 1004  CB  ARG A 135     8496   7974   7831    840    708    -45       C  
ATOM   1005  CG  ARG A 135     -12.428  87.534 318.242  1.00 66.15           C  
ANISOU 1005  CG  ARG A 135     8611   8309   8212    887    702    -78       C  
ATOM   1006  CD  ARG A 135     -13.772  88.073 318.696  1.00 69.89           C  
ANISOU 1006  CD  ARG A 135     8983   8937   8633   1011    848    -79       C  
ATOM   1007  NE  ARG A 135     -14.666  87.001 319.120  1.00 73.95           N  
ANISOU 1007  NE  ARG A 135     9370   9588   9138    904    984     -6       N  
ATOM   1008  CZ  ARG A 135     -15.941  87.179 319.447  1.00 84.89           C  
ANISOU 1008  CZ  ARG A 135    10601  11163  10489    969   1131      4       C  
ATOM   1009  NH1 ARG A 135     -16.478  88.391 319.394  1.00 92.37           N  
ANISOU 1009  NH1 ARG A 135    11512  12178  11406   1179   1155    -54       N  
ATOM   1010  NH2 ARG A 135     -16.682  86.146 319.823  1.00 89.10           N  
ANISOU 1010  NH2 ARG A 135    11020  11816  11016    826   1263     71       N  
ATOM   1011  N   PRO A 136      -9.805  87.726 322.496  1.00 53.30           N  
ANISOU 1011  N   PRO A 136     7639   6549   6063   1004    651   -137       N  
ATOM   1012  CA  PRO A 136      -8.804  87.174 323.417  1.00 51.82           C  
ANISOU 1012  CA  PRO A 136     7596   6353   5742    991    581   -114       C  
ATOM   1013  C   PRO A 136      -9.227  85.856 324.061  1.00 57.10           C  
ANISOU 1013  C   PRO A 136     8278   7070   6348    952    689     33       C  
ATOM   1014  O   PRO A 136      -8.422  84.927 324.132  1.00 63.29           O  
ANISOU 1014  O   PRO A 136     9118   7807   7122    912    612    105       O  
ATOM   1015  CB  PRO A 136      -8.664  88.269 324.484  1.00 53.23           C  
ANISOU 1015  CB  PRO A 136     7924   6561   5739   1098    590   -225       C  
ATOM   1016  CG  PRO A 136      -9.257  89.498 323.871  1.00 54.95           C  
ANISOU 1016  CG  PRO A 136     8102   6738   6037   1160    624   -324       C  
ATOM   1017  CD  PRO A 136     -10.348  89.002 322.988  1.00 55.86           C  
ANISOU 1017  CD  PRO A 136     8024   6898   6302   1137    720   -234       C  
ATOM   1018  N   VAL A 137     -10.472  85.784 324.524  1.00 56.39           N  
ANISOU 1018  N   VAL A 137     8140   7072   6213    969    872     81       N  
ATOM   1019  CA  VAL A 137     -10.963  84.606 325.232  1.00 57.15           C  
ANISOU 1019  CA  VAL A 137     8272   7211   6233    911   1008    227       C  
ATOM   1020  C   VAL A 137     -10.988  83.370 324.333  1.00 60.62           C  
ANISOU 1020  C   VAL A 137     8629   7564   6838    761   1004    325       C  
ATOM   1021  O   VAL A 137     -10.624  82.275 324.765  1.00 65.17           O  
ANISOU 1021  O   VAL A 137     9320   8077   7364    714   1022    443       O  
ATOM   1022  CB  VAL A 137     -12.373  84.844 325.804  1.00 56.45           C  
ANISOU 1022  CB  VAL A 137     8107   7267   6074    937   1226    246       C  
ATOM   1023  CG1 VAL A 137     -12.837  83.633 326.599  1.00 54.58           C  
ANISOU 1023  CG1 VAL A 137     7928   7067   5742    849   1386    407       C  
ATOM   1024  CG2 VAL A 137     -12.388  86.091 326.675  1.00 53.75           C  
ANISOU 1024  CG2 VAL A 137     7865   6995   5563   1103   1243    130       C  
ATOM   1025  N   TRP A 138     -11.412  83.548 323.086  1.00 62.12           N  
ANISOU 1025  N   TRP A 138     8640   7748   7216    695    981    275       N  
ATOM   1026  CA  TRP A 138     -11.433  82.445 322.132  1.00 61.18           C  
ANISOU 1026  CA  TRP A 138     8444   7546   7255    544    968    333       C  
ATOM   1027  C   TRP A 138     -10.017  82.057 321.729  1.00 56.74           C  
ANISOU 1027  C   TRP A 138     7984   6846   6730    555    792    326       C  
ATOM   1028  O   TRP A 138      -9.696  80.873 321.615  1.00 55.25           O  
ANISOU 1028  O   TRP A 138     7861   6552   6578    481    796    412       O  
ATOM   1029  CB  TRP A 138     -12.246  82.810 320.886  1.00 60.53           C  
ANISOU 1029  CB  TRP A 138     8134   7528   7335    483    973    267       C  
ATOM   1030  CG  TRP A 138     -12.346  81.685 319.888  1.00 60.25           C  
ANISOU 1030  CG  TRP A 138     8019   7423   7450    308    964    301       C  
ATOM   1031  CD1 TRP A 138     -13.331  80.744 319.812  1.00 61.99           C  
ANISOU 1031  CD1 TRP A 138     8152   7682   7721    139   1107    362       C  
ATOM   1032  CD2 TRP A 138     -11.421  81.381 318.835  1.00 56.88           C  
ANISOU 1032  CD2 TRP A 138     7600   6876   7137    273    812    261       C  
ATOM   1033  NE1 TRP A 138     -13.081  79.877 318.776  1.00 56.57           N  
ANISOU 1033  NE1 TRP A 138     7435   6889   7170     -1   1048    352       N  
ATOM   1034  CE2 TRP A 138     -11.915  80.245 318.162  1.00 55.78           C  
ANISOU 1034  CE2 TRP A 138     7392   6694   7107     93    870    292       C  
ATOM   1035  CE3 TRP A 138     -10.226  81.960 318.396  1.00 56.05           C  
ANISOU 1035  CE3 TRP A 138     7549   6703   7045    364    644    194       C  
ATOM   1036  CZ2 TRP A 138     -11.254  79.679 317.074  1.00 61.29           C  
ANISOU 1036  CZ2 TRP A 138     8088   7279   7919     26    763    253       C  
ATOM   1037  CZ3 TRP A 138      -9.571  81.395 317.317  1.00 55.64           C  
ANISOU 1037  CZ3 TRP A 138     7474   6561   7108    297    545    168       C  
ATOM   1038  CH2 TRP A 138     -10.086  80.267 316.668  1.00 61.31           C  
ANISOU 1038  CH2 TRP A 138     8136   7233   7926    142    604    195       C  
ATOM   1039  N   ALA A 139      -9.176  83.064 321.517  1.00 55.93           N  
ANISOU 1039  N   ALA A 139     7895   6740   6615    648    647    221       N  
ATOM   1040  CA  ALA A 139      -7.820  82.848 321.024  1.00 61.30           C  
ANISOU 1040  CA  ALA A 139     8620   7334   7338    658    477    192       C  
ATOM   1041  C   ALA A 139      -6.968  82.057 322.009  1.00 68.74           C  
ANISOU 1041  C   ALA A 139     9729   8244   8145    719    440    275       C  
ATOM   1042  O   ALA A 139      -6.201  81.185 321.613  1.00 74.64           O  
ANISOU 1042  O   ALA A 139    10507   8908   8945    712    367    317       O  
ATOM   1043  CB  ALA A 139      -7.158  84.179 320.709  1.00 64.00           C  
ANISOU 1043  CB  ALA A 139     8943   7695   7678    717    353     59       C  
ATOM   1044  N   GLN A 140      -7.108  82.354 323.295  1.00 70.01           N  
ANISOU 1044  N   GLN A 140    10004   8480   8118    799    492    301       N  
ATOM   1045  CA  GLN A 140      -6.308  81.680 324.311  1.00 67.04           C  
ANISOU 1045  CA  GLN A 140     9795   8102   7574    886    447    389       C  
ATOM   1046  C   GLN A 140      -6.743  80.230 324.518  1.00 65.65           C  
ANISOU 1046  C   GLN A 140     9708   7832   7405    838    572    564       C  
ATOM   1047  O   GLN A 140      -6.091  79.481 325.243  1.00 70.29           O  
ANISOU 1047  O   GLN A 140    10453   8388   7865    926    540    671       O  
ATOM   1048  CB  GLN A 140      -6.380  82.441 325.636  1.00 68.10           C  
ANISOU 1048  CB  GLN A 140    10037   8360   7480    983    471    358       C  
ATOM   1049  CG  GLN A 140      -7.760  82.465 326.265  1.00 69.98           C  
ANISOU 1049  CG  GLN A 140    10286   8654   7649    957    687    417       C  
ATOM   1050  CD  GLN A 140      -7.829  83.367 327.480  1.00 71.23           C  
ANISOU 1050  CD  GLN A 140    10547   8939   7578   1063    711    351       C  
ATOM   1051  OE1 GLN A 140      -8.039  82.903 328.602  1.00 72.64           O  
ANISOU 1051  OE1 GLN A 140    10862   9178   7559   1113    804    454       O  
ATOM   1052  NE2 GLN A 140      -7.654  84.666 327.263  1.00 67.77           N  
ANISOU 1052  NE2 GLN A 140    10065   8530   7153   1097    635    178       N  
ATOM   1053  N   ASN A 141      -7.836  79.833 323.873  1.00 61.98           N  
ANISOU 1053  N   ASN A 141     9148   7321   7082    697    712    594       N  
ATOM   1054  CA  ASN A 141      -8.393  78.498 324.073  1.00 61.10           C  
ANISOU 1054  CA  ASN A 141     9130   7101   6983    601    862    750       C  
ATOM   1055  C   ASN A 141      -8.417  77.616 322.825  1.00 59.45           C  
ANISOU 1055  C   ASN A 141     8860   6741   6985    470    855    749       C  
ATOM   1056  O   ASN A 141      -8.538  76.396 322.934  1.00 56.69           O  
ANISOU 1056  O   ASN A 141     8645   6244   6652    401    947    871       O  
ATOM   1057  CB  ASN A 141      -9.813  78.611 324.633  1.00 61.40           C  
ANISOU 1057  CB  ASN A 141     9124   7237   6970    506   1078    795       C  
ATOM   1058  CG  ASN A 141      -9.833  79.048 326.083  1.00 61.81           C  
ANISOU 1058  CG  ASN A 141     9309   7405   6772    630   1134    842       C  
ATOM   1059  OD1 ASN A 141      -9.070  78.542 326.908  1.00 57.94           O  
ANISOU 1059  OD1 ASN A 141     9018   6874   6124    733   1091    942       O  
ATOM   1060  ND2 ASN A 141     -10.709  79.996 326.403  1.00 63.03           N  
ANISOU 1060  ND2 ASN A 141     9356   7716   6875    640   1230    768       N  
ATOM   1061  N   HIS A 142      -8.305  78.220 321.645  1.00 60.29           N  
ANISOU 1061  N   HIS A 142     8790   6875   7243    435    754    613       N  
ATOM   1062  CA  HIS A 142      -8.438  77.455 320.407  1.00 61.78           C  
ANISOU 1062  CA  HIS A 142     8908   6949   7619    300    753    588       C  
ATOM   1063  C   HIS A 142      -7.326  77.716 319.390  1.00 62.36           C  
ANISOU 1063  C   HIS A 142     8921   6991   7784    366    569    484       C  
ATOM   1064  O   HIS A 142      -7.247  77.035 318.367  1.00 63.54           O  
ANISOU 1064  O   HIS A 142     9036   7038   8067    280    554    454       O  
ATOM   1065  CB  HIS A 142      -9.798  77.738 319.764  1.00 60.79           C  
ANISOU 1065  CB  HIS A 142     8582   6917   7596    135    862    532       C  
ATOM   1066  CG  HIS A 142     -10.960  77.318 320.608  1.00 64.50           C  
ANISOU 1066  CG  HIS A 142     9075   7434   8000     28   1068    630       C  
ATOM   1067  ND1 HIS A 142     -11.601  78.176 321.475  1.00 64.20           N  
ANISOU 1067  ND1 HIS A 142     8988   7565   7839     93   1150    633       N  
ATOM   1068  CD2 HIS A 142     -11.591  76.124 320.726  1.00 68.61           C  
ANISOU 1068  CD2 HIS A 142     9665   7849   8553   -150   1223    725       C  
ATOM   1069  CE1 HIS A 142     -12.581  77.533 322.086  1.00 66.56           C  
ANISOU 1069  CE1 HIS A 142     9304   7890   8095    -37   1349    730       C  
ATOM   1070  NE2 HIS A 142     -12.595  76.286 321.649  1.00 69.24           N  
ANISOU 1070  NE2 HIS A 142     9719   8059   8530   -201   1398    791       N  
ATOM   1071  N   ARG A 143      -6.467  78.691 319.669  1.00 58.66           N  
ANISOU 1071  N   ARG A 143     8440   6613   7236    503    437    420       N  
ATOM   1072  CA  ARG A 143      -5.352  78.993 318.776  1.00 53.59           C  
ANISOU 1072  CA  ARG A 143     7730   5966   6665    553    274    324       C  
ATOM   1073  C   ARG A 143      -4.166  78.058 318.982  1.00 58.61           C  
ANISOU 1073  C   ARG A 143     8490   6515   7265    666    194    380       C  
ATOM   1074  O   ARG A 143      -3.062  78.509 319.285  1.00 59.90           O  
ANISOU 1074  O   ARG A 143     8654   6757   7349    789     60    340       O  
ATOM   1075  CB  ARG A 143      -4.883  80.433 318.965  1.00 50.79           C  
ANISOU 1075  CB  ARG A 143     7312   5740   6245    622    173    222       C  
ATOM   1076  CG  ARG A 143      -5.529  81.445 318.047  1.00 52.11           C  
ANISOU 1076  CG  ARG A 143     7328   5961   6510    548    180    126       C  
ATOM   1077  CD  ARG A 143      -4.662  82.685 317.982  1.00 56.55           C  
ANISOU 1077  CD  ARG A 143     7867   6584   7033    603     57     20       C  
ATOM   1078  NE  ARG A 143      -3.255  82.324 317.821  1.00 60.28           N  
ANISOU 1078  NE  ARG A 143     8356   7050   7500    647    -73     -2       N  
ATOM   1079  CZ  ARG A 143      -2.252  83.195 317.806  1.00 64.44           C  
ANISOU 1079  CZ  ARG A 143     8856   7639   7987    669   -189    -94       C  
ATOM   1080  NH1 ARG A 143      -2.494  84.491 317.942  1.00 66.48           N  
ANISOU 1080  NH1 ARG A 143     9113   7932   8214    646   -190   -172       N  
ATOM   1081  NH2 ARG A 143      -1.005  82.770 317.657  1.00 64.88           N  
ANISOU 1081  NH2 ARG A 143     8890   7725   8035    712   -300   -113       N  
ATOM   1082  N   THR A 144      -4.388  76.760 318.811  1.00 66.65           N  
ANISOU 1082  N   THR A 144     9612   7374   8339    625    276    467       N  
ATOM   1083  CA  THR A 144      -3.306  75.793 318.935  1.00 74.45           C  
ANISOU 1083  CA  THR A 144    10734   8255   9300    767    210    529       C  
ATOM   1084  C   THR A 144      -2.522  75.672 317.630  1.00 72.26           C  
ANISOU 1084  C   THR A 144    10349   7952   9154    777    110    418       C  
ATOM   1085  O   THR A 144      -3.024  76.011 316.557  1.00 69.22           O  
ANISOU 1085  O   THR A 144     9825   7581   8894    637    125    320       O  
ATOM   1086  CB  THR A 144      -3.828  74.404 319.345  1.00 85.67           C  
ANISOU 1086  CB  THR A 144    12365   9468  10716    733    357    677       C  
ATOM   1087  OG1 THR A 144      -2.759  73.453 319.279  1.00 94.02           O  
ANISOU 1087  OG1 THR A 144    13559  10397  11766    902    291    730       O  
ATOM   1088  CG2 THR A 144      -4.951  73.956 318.423  1.00 86.13           C  
ANISOU 1088  CG2 THR A 144    12367   9422  10936    496    485    638       C  
ATOM   1089  N   VAL A 145      -1.285  75.195 317.737  1.00 71.71           N  
ANISOU 1089  N   VAL A 145    10336   7869   9041    959      7    436       N  
ATOM   1090  CA  VAL A 145      -0.424  74.998 316.576  1.00 67.69           C  
ANISOU 1090  CA  VAL A 145     9729   7352   8637    999    -78    335       C  
ATOM   1091  C   VAL A 145      -1.033  73.983 315.615  1.00 67.68           C  
ANISOU 1091  C   VAL A 145     9788   7147   8779    881     28    324       C  
ATOM   1092  O   VAL A 145      -0.977  74.154 314.395  1.00 70.05           O  
ANISOU 1092  O   VAL A 145     9959   7466   9191    797      3    204       O  
ATOM   1093  CB  VAL A 145       0.986  74.530 316.998  1.00 68.07           C  
ANISOU 1093  CB  VAL A 145     9826   7439   8597   1251   -195    371       C  
ATOM   1094  CG1 VAL A 145       1.807  74.113 315.787  1.00 68.54           C  
ANISOU 1094  CG1 VAL A 145     9799   7476   8768   1306   -248    274       C  
ATOM   1095  CG2 VAL A 145       1.696  75.627 317.778  1.00 65.94           C  
ANISOU 1095  CG2 VAL A 145     9452   7413   8189   1332   -326    335       C  
ATOM   1096  N   ALA A 146      -1.626  72.933 316.176  1.00 66.99           N  
ANISOU 1096  N   ALA A 146     9909   6864   8678    860    152    447       N  
ATOM   1097  CA  ALA A 146      -2.283  71.897 315.387  1.00 67.70           C  
ANISOU 1097  CA  ALA A 146    10092   6735   8897    712    269    431       C  
ATOM   1098  C   ALA A 146      -3.380  72.488 314.507  1.00 69.73           C  
ANISOU 1098  C   ALA A 146    10165   7074   9256    456    316    319       C  
ATOM   1099  O   ALA A 146      -3.595  72.039 313.382  1.00 73.82           O  
ANISOU 1099  O   ALA A 146    10647   7513   9888    340    336    220       O  
ATOM   1100  CB  ALA A 146      -2.855  70.821 316.296  1.00 69.70           C  
ANISOU 1100  CB  ALA A 146    10612   6766   9103    690    417    596       C  
ATOM   1101  N   ALA A 147      -4.068  73.502 315.023  1.00 66.53           N  
ANISOU 1101  N   ALA A 147     9644   6837   8796    387    328    331       N  
ATOM   1102  CA  ALA A 147      -5.100  74.187 314.255  1.00 62.63           C  
ANISOU 1102  CA  ALA A 147     8957   6460   8379    194    358    236       C  
ATOM   1103  C   ALA A 147      -4.478  74.993 313.120  1.00 63.73           C  
ANISOU 1103  C   ALA A 147     8919   6726   8571    225    228    101       C  
ATOM   1104  O   ALA A 147      -4.973  74.980 311.994  1.00 62.62           O  
ANISOU 1104  O   ALA A 147     8669   6605   8520     92    235      7       O  
ATOM   1105  CB  ALA A 147      -5.928  75.091 315.157  1.00 56.00           C  
ANISOU 1105  CB  ALA A 147     8053   5768   7457    163    409    286       C  
ATOM   1106  N   ALA A 148      -3.386  75.688 313.426  1.00 64.39           N  
ANISOU 1106  N   ALA A 148     8974   6906   8585    391    113     91       N  
ATOM   1107  CA  ALA A 148      -2.699  76.521 312.446  1.00 63.54           C  
ANISOU 1107  CA  ALA A 148     8709   6922   8511    411      3    -23       C  
ATOM   1108  C   ALA A 148      -2.123  75.685 311.309  1.00 72.21           C  
ANISOU 1108  C   ALA A 148     9809   7935   9692    415    -17    -96       C  
ATOM   1109  O   ALA A 148      -2.023  76.150 310.175  1.00 70.94           O  
ANISOU 1109  O   ALA A 148     9517   7855   9581    356    -59   -196       O  
ATOM   1110  CB  ALA A 148      -1.600  77.330 313.117  1.00 54.69           C  
ANISOU 1110  CB  ALA A 148     7565   5920   7294    558   -106    -22       C  
ATOM   1111  N   HIS A 149      -1.745  74.449 311.619  1.00 80.98           N  
ANISOU 1111  N   HIS A 149    11086   8875  10806    497     20    -43       N  
ATOM   1112  CA  HIS A 149      -1.205  73.543 310.614  1.00 83.55           C  
ANISOU 1112  CA  HIS A 149    11449   9090  11204    526     18   -120       C  
ATOM   1113  C   HIS A 149      -2.306  73.070 309.673  1.00 81.94           C  
ANISOU 1113  C   HIS A 149    11238   8802  11094    306    103   -193       C  
ATOM   1114  O   HIS A 149      -2.094  72.946 308.466  1.00 84.92           O  
ANISOU 1114  O   HIS A 149    11545   9196  11524    264     78   -312       O  
ATOM   1115  CB  HIS A 149      -0.523  72.343 311.274  1.00 91.57           C  
ANISOU 1115  CB  HIS A 149    12680   9920  12192    707     43    -34       C  
ATOM   1116  CG  HIS A 149       0.166  71.432 310.305  1.00102.57           C  
ANISOU 1116  CG  HIS A 149    14128  11194  13649    787     42   -120       C  
ATOM   1117  ND1 HIS A 149      -0.486  70.404 309.658  1.00108.19           N  
ANISOU 1117  ND1 HIS A 149    14975  11686  14447    657    146   -168       N  
ATOM   1118  CD2 HIS A 149       1.448  71.397 309.873  1.00108.13           C  
ANISOU 1118  CD2 HIS A 149    14768  11977  14340    984    -42   -181       C  
ATOM   1119  CE1 HIS A 149       0.366  69.774 308.869  1.00111.63           C  
ANISOU 1119  CE1 HIS A 149    15447  12050  14915    785    127   -257       C  
ATOM   1120  NE2 HIS A 149       1.546  70.356 308.980  1.00111.02           N  
ANISOU 1120  NE2 HIS A 149    15240  12163  14780    993     16   -262       N  
ATOM   1121  N   LYS A 150      -3.484  72.812 310.232  1.00 76.39           N  
ANISOU 1121  N   LYS A 150    10595   8031  10398    157    205   -127       N  
ATOM   1122  CA  LYS A 150      -4.623  72.358 309.443  1.00 72.20           C  
ANISOU 1122  CA  LYS A 150    10033   7453   9946    -82    284   -202       C  
ATOM   1123  C   LYS A 150      -5.176  73.479 308.566  1.00 67.12           C  
ANISOU 1123  C   LYS A 150     9144   7045   9313   -183    224   -294       C  
ATOM   1124  O   LYS A 150      -5.711  73.225 307.489  1.00 66.69           O  
ANISOU 1124  O   LYS A 150     9015   7013   9311   -332    231   -403       O  
ATOM   1125  CB  LYS A 150      -5.723  71.808 310.354  1.00 71.33           C  
ANISOU 1125  CB  LYS A 150    10030   7238   9833   -228    421   -101       C  
ATOM   1126  CG  LYS A 150      -5.351  70.520 311.082  1.00 75.10           C  
ANISOU 1126  CG  LYS A 150    10799   7433  10304   -162    509      1       C  
ATOM   1127  CD  LYS A 150      -5.998  69.290 310.448  1.00 79.90           C  
ANISOU 1127  CD  LYS A 150    11538   7815  11005   -380    622    -66       C  
ATOM   1128  CE  LYS A 150      -5.361  68.925 309.113  1.00 79.97           C  
ANISOU 1128  CE  LYS A 150    11534   7773  11078   -353    555   -230       C  
ATOM   1129  NZ  LYS A 150      -5.991  67.725 308.493  1.00 78.61           N  
ANISOU 1129  NZ  LYS A 150    11511   7368  10990   -581    665   -321       N  
ATOM   1130  N   VAL A 151      -5.044  74.716 309.032  1.00 62.37           N  
ANISOU 1130  N   VAL A 151     8432   6615   8651    -95    164   -251       N  
ATOM   1131  CA  VAL A 151      -5.462  75.873 308.249  1.00 61.91           C  
ANISOU 1131  CA  VAL A 151     8175   6758   8591   -143    106   -315       C  
ATOM   1132  C   VAL A 151      -4.601  76.001 306.998  1.00 67.12           C  
ANISOU 1132  C   VAL A 151     8773   7461   9267   -104     22   -419       C  
ATOM   1133  O   VAL A 151      -5.112  76.230 305.901  1.00 71.59           O  
ANISOU 1133  O   VAL A 151     9225   8124   9851   -204      2   -501       O  
ATOM   1134  CB  VAL A 151      -5.379  77.177 309.067  1.00 60.66           C  
ANISOU 1134  CB  VAL A 151     7961   6726   8361    -41     69   -252       C  
ATOM   1135  CG1 VAL A 151      -5.537  78.389 308.160  1.00 58.38           C  
ANISOU 1135  CG1 VAL A 151     7513   6603   8067    -50      2   -310       C  
ATOM   1136  CG2 VAL A 151      -6.432  77.184 310.163  1.00 62.02           C  
ANISOU 1136  CG2 VAL A 151     8159   6903   8503    -90    165   -165       C  
ATOM   1137  N   CYS A 152      -3.293  75.839 307.170  1.00 67.10           N  
ANISOU 1137  N   CYS A 152     8839   7410   9246     47    -26   -416       N  
ATOM   1138  CA  CYS A 152      -2.356  75.912 306.055  1.00 65.34           C  
ANISOU 1138  CA  CYS A 152     8555   7242   9030     96    -88   -512       C  
ATOM   1139  C   CYS A 152      -2.649  74.847 305.006  1.00 67.33           C  
ANISOU 1139  C   CYS A 152     8846   7401   9334      0    -48   -614       C  
ATOM   1140  O   CYS A 152      -2.530  75.099 303.808  1.00 69.83           O  
ANISOU 1140  O   CYS A 152     9069   7818   9646    -42    -82   -711       O  
ATOM   1141  CB  CYS A 152      -0.918  75.769 306.553  1.00 63.41           C  
ANISOU 1141  CB  CYS A 152     8360   6980   8753    284   -136   -490       C  
ATOM   1142  SG  CYS A 152      -0.322  77.182 307.503  1.00 63.68           S  
ANISOU 1142  SG  CYS A 152     8317   7168   8710    369   -211   -426       S  
ATOM   1143  N   LEU A 153      -3.036  73.659 305.461  1.00 68.29           N  
ANISOU 1143  N   LEU A 153     9126   7324   9495    -42     32   -595       N  
ATOM   1144  CA  LEU A 153      -3.354  72.562 304.553  1.00 70.83           C  
ANISOU 1144  CA  LEU A 153     9524   7519   9869   -157     82   -708       C  
ATOM   1145  C   LEU A 153      -4.585  72.888 303.712  1.00 70.24           C  
ANISOU 1145  C   LEU A 153     9307   7579   9803   -377     82   -788       C  
ATOM   1146  O   LEU A 153      -4.676  72.492 302.550  1.00 70.29           O  
ANISOU 1146  O   LEU A 153     9289   7601   9816   -465     72   -923       O  
ATOM   1147  CB  LEU A 153      -3.569  71.262 305.332  1.00 73.38           C  
ANISOU 1147  CB  LEU A 153    10081   7568  10234   -177    184   -655       C  
ATOM   1148  CG  LEU A 153      -2.351  70.730 306.091  1.00 75.13           C  
ANISOU 1148  CG  LEU A 153    10468   7644  10435     75    180   -575       C  
ATOM   1149  CD1 LEU A 153      -2.637  69.356 306.677  1.00 78.80           C  
ANISOU 1149  CD1 LEU A 153    11206   7795  10937     50    296   -521       C  
ATOM   1150  CD2 LEU A 153      -1.126  70.691 305.190  1.00 74.43           C  
ANISOU 1150  CD2 LEU A 153    10335   7608  10337    240    115   -679       C  
ATOM   1151  N   VAL A 154      -5.528  73.612 304.305  1.00 67.25           N  
ANISOU 1151  N   VAL A 154     8826   7315   9409   -451     92   -709       N  
ATOM   1152  CA  VAL A 154      -6.706  74.067 303.579  1.00 64.37           C  
ANISOU 1152  CA  VAL A 154     8287   7133   9037   -619     77   -769       C  
ATOM   1153  C   VAL A 154      -6.314  75.168 302.600  1.00 64.35           C  
ANISOU 1153  C   VAL A 154     8136   7335   8977   -540    -24   -809       C  
ATOM   1154  O   VAL A 154      -6.816  75.222 301.477  1.00 73.89           O  
ANISOU 1154  O   VAL A 154     9239   8672  10163   -640    -61   -907       O  
ATOM   1155  CB  VAL A 154      -7.801  74.583 304.534  1.00 62.55           C  
ANISOU 1155  CB  VAL A 154     7977   6990   8800   -680    124   -668       C  
ATOM   1156  CG1 VAL A 154      -8.982  75.139 303.750  1.00 61.15           C  
ANISOU 1156  CG1 VAL A 154     7583   7048   8603   -809     93   -728       C  
ATOM   1157  CG2 VAL A 154      -8.255  73.472 305.464  1.00 64.49           C  
ANISOU 1157  CG2 VAL A 154     8376   7037   9090   -789    245   -617       C  
ATOM   1158  N   LEU A 155      -5.404  76.036 303.028  1.00 60.23           N  
ANISOU 1158  N   LEU A 155     7615   6848   8424   -371    -68   -734       N  
ATOM   1159  CA  LEU A 155      -4.935  77.127 302.183  1.00 60.69           C  
ANISOU 1159  CA  LEU A 155     7564   7070   8425   -306   -144   -753       C  
ATOM   1160  C   LEU A 155      -4.191  76.606 300.955  1.00 66.08           C  
ANISOU 1160  C   LEU A 155     8258   7757   9094   -306   -167   -871       C  
ATOM   1161  O   LEU A 155      -4.361  77.127 299.853  1.00 70.40           O  
ANISOU 1161  O   LEU A 155     8708   8456   9587   -341   -211   -922       O  
ATOM   1162  CB  LEU A 155      -4.040  78.077 302.978  1.00 60.49           C  
ANISOU 1162  CB  LEU A 155     7555   7055   8373   -161   -173   -663       C  
ATOM   1163  CG  LEU A 155      -4.756  78.917 304.036  1.00 63.32           C  
ANISOU 1163  CG  LEU A 155     7893   7449   8717   -142   -158   -562       C  
ATOM   1164  CD1 LEU A 155      -3.825  79.969 304.608  1.00 64.25           C  
ANISOU 1164  CD1 LEU A 155     8028   7590   8796    -27   -198   -510       C  
ATOM   1165  CD2 LEU A 155      -5.996  79.561 303.444  1.00 64.34           C  
ANISOU 1165  CD2 LEU A 155     7895   7725   8825   -211   -166   -565       C  
ATOM   1166  N   TRP A 156      -3.371  75.577 301.149  1.00 63.96           N  
ANISOU 1166  N   TRP A 156     8116   7324   8862   -249   -134   -910       N  
ATOM   1167  CA  TRP A 156      -2.676  74.940 300.035  1.00 62.15           C  
ANISOU 1167  CA  TRP A 156     7913   7082   8618   -233   -136  -1038       C  
ATOM   1168  C   TRP A 156      -3.671  74.277 299.089  1.00 69.17           C  
ANISOU 1168  C   TRP A 156     8794   7983   9506   -411   -122  -1162       C  
ATOM   1169  O   TRP A 156      -3.518  74.338 297.870  1.00 74.92           O  
ANISOU 1169  O   TRP A 156     9466   8826  10174   -439   -152  -1268       O  
ATOM   1170  CB  TRP A 156      -1.664  73.910 300.541  1.00 60.04           C  
ANISOU 1170  CB  TRP A 156     7798   6621   8392    -99    -95  -1050       C  
ATOM   1171  CG  TRP A 156      -0.360  74.507 300.981  1.00 62.04           C  
ANISOU 1171  CG  TRP A 156     8012   6941   8618     86   -132   -989       C  
ATOM   1172  CD1 TRP A 156       0.070  74.685 302.264  1.00 63.41           C  
ANISOU 1172  CD1 TRP A 156     8226   7068   8799    198   -142   -875       C  
ATOM   1173  CD2 TRP A 156       0.684  75.004 300.136  1.00 66.86           C  
ANISOU 1173  CD2 TRP A 156     8523   7704   9178    162   -163  -1047       C  
ATOM   1174  NE1 TRP A 156       1.317  75.261 302.270  1.00 65.38           N  
ANISOU 1174  NE1 TRP A 156     8392   7441   9010    331   -188   -870       N  
ATOM   1175  CE2 TRP A 156       1.716  75.468 300.976  1.00 67.33           C  
ANISOU 1175  CE2 TRP A 156     8548   7808   9226    305   -193   -971       C  
ATOM   1176  CE3 TRP A 156       0.847  75.103 298.751  1.00 68.89           C  
ANISOU 1176  CE3 TRP A 156     8711   8079   9384    116   -165  -1157       C  
ATOM   1177  CZ2 TRP A 156       2.893  76.023 300.476  1.00 70.28           C  
ANISOU 1177  CZ2 TRP A 156     8805   8344   9554    381   -218  -1006       C  
ATOM   1178  CZ3 TRP A 156       2.016  75.653 298.257  1.00 69.13           C  
ANISOU 1178  CZ3 TRP A 156     8644   8259   9362    205   -178  -1177       C  
ATOM   1179  CH2 TRP A 156       3.024  76.106 299.117  1.00 68.91           C  
ANISOU 1179  CH2 TRP A 156     8569   8276   9339    326   -200  -1104       C  
ATOM   1180  N   ALA A 157      -4.692  73.646 299.661  1.00 68.32           N  
ANISOU 1180  N   ALA A 157     8736   7771   9451   -546    -73  -1153       N  
ATOM   1181  CA  ALA A 157      -5.725  72.981 298.875  1.00 67.97           C  
ANISOU 1181  CA  ALA A 157     8669   7750   9408   -757    -60  -1283       C  
ATOM   1182  C   ALA A 157      -6.513  73.990 298.048  1.00 71.69           C  
ANISOU 1182  C   ALA A 157     8928   8513   9799   -825   -141  -1299       C  
ATOM   1183  O   ALA A 157      -6.899  73.710 296.913  1.00 77.65           O  
ANISOU 1183  O   ALA A 157     9628   9375  10499   -936   -175  -1436       O  
ATOM   1184  CB  ALA A 157      -6.657  72.194 299.780  1.00 68.85           C  
ANISOU 1184  CB  ALA A 157     8860   7704   9594   -911     23  -1253       C  
ATOM   1185  N   LEU A 158      -6.752  75.164 298.620  1.00 69.56           N  
ANISOU 1185  N   LEU A 158     8552   8369   9508   -742   -172  -1160       N  
ATOM   1186  CA  LEU A 158      -7.449  76.224 297.902  1.00 71.31           C  
ANISOU 1186  CA  LEU A 158     8594   8855   9647   -750   -247  -1145       C  
ATOM   1187  C   LEU A 158      -6.526  76.888 296.889  1.00 71.42           C  
ANISOU 1187  C   LEU A 158     8593   8971   9572   -640   -303  -1162       C  
ATOM   1188  O   LEU A 158      -6.980  77.414 295.873  1.00 70.10           O  
ANISOU 1188  O   LEU A 158     8318   9009   9310   -661   -366  -1193       O  
ATOM   1189  CB  LEU A 158      -8.002  77.264 298.877  1.00 69.40           C  
ANISOU 1189  CB  LEU A 158     8276   8683   9412   -676   -246   -993       C  
ATOM   1190  CG  LEU A 158      -9.204  76.811 299.706  1.00 76.45           C  
ANISOU 1190  CG  LEU A 158     9120   9568  10360   -803   -188   -974       C  
ATOM   1191  CD1 LEU A 158      -9.663  77.921 300.638  1.00 83.07           C  
ANISOU 1191  CD1 LEU A 158     9888  10487  11188   -692   -180   -833       C  
ATOM   1192  CD2 LEU A 158     -10.339  76.363 298.797  1.00 76.37           C  
ANISOU 1192  CD2 LEU A 158     8965   9733  10318   -989   -218  -1095       C  
ATOM   1193  N   ALA A 159      -5.228  76.857 297.173  1.00 71.37           N  
ANISOU 1193  N   ALA A 159     8689   8841   9589   -520   -278  -1138       N  
ATOM   1194  CA  ALA A 159      -4.234  77.443 296.283  1.00 66.72           C  
ANISOU 1194  CA  ALA A 159     8084   8347   8920   -431   -306  -1152       C  
ATOM   1195  C   ALA A 159      -4.067  76.603 295.022  1.00 69.36           C  
ANISOU 1195  C   ALA A 159     8437   8720   9197   -496   -307  -1318       C  
ATOM   1196  O   ALA A 159      -4.022  77.139 293.915  1.00 71.21           O  
ANISOU 1196  O   ALA A 159     8606   9134   9319   -495   -348  -1347       O  
ATOM   1197  CB  ALA A 159      -2.904  77.596 297.000  1.00 62.98           C  
ANISOU 1197  CB  ALA A 159     7679   7765   8486   -299   -277  -1093       C  
ATOM   1198  N   VAL A 160      -3.977  75.286 295.188  1.00 70.03           N  
ANISOU 1198  N   VAL A 160     8633   8626   9349   -546   -257  -1427       N  
ATOM   1199  CA  VAL A 160      -3.837  74.389 294.046  1.00 71.10           C  
ANISOU 1199  CA  VAL A 160     8817   8765   9432   -611   -247  -1612       C  
ATOM   1200  C   VAL A 160      -5.136  74.331 293.247  1.00 73.54           C  
ANISOU 1200  C   VAL A 160     9031   9240   9672   -790   -302  -1703       C  
ATOM   1201  O   VAL A 160      -5.136  73.963 292.073  1.00 74.82           O  
ANISOU 1201  O   VAL A 160     9191   9500   9738   -849   -324  -1853       O  
ATOM   1202  CB  VAL A 160      -3.433  72.959 294.477  1.00 67.35           C  
ANISOU 1202  CB  VAL A 160     8526   8011   9053   -610   -168  -1708       C  
ATOM   1203  CG1 VAL A 160      -2.121  72.984 295.243  1.00 64.99           C  
ANISOU 1203  CG1 VAL A 160     8298   7591   8805   -401   -129  -1621       C  
ATOM   1204  CG2 VAL A 160      -4.527  72.313 295.310  1.00 65.89           C  
ANISOU 1204  CG2 VAL A 160     8396   7679   8961   -765   -135  -1694       C  
ATOM   1205  N   LEU A 161      -6.238  74.704 293.888  1.00 73.35           N  
ANISOU 1205  N   LEU A 161     8915   9271   9684   -870   -326  -1617       N  
ATOM   1206  CA  LEU A 161      -7.543  74.703 293.240  1.00 71.81           C  
ANISOU 1206  CA  LEU A 161     8584   9280   9422  -1034   -389  -1694       C  
ATOM   1207  C   LEU A 161      -7.684  75.894 292.297  1.00 71.03           C  
ANISOU 1207  C   LEU A 161     8345   9472   9170   -950   -481  -1640       C  
ATOM   1208  O   LEU A 161      -8.398  75.827 291.299  1.00 74.52           O  
ANISOU 1208  O   LEU A 161     8687  10127   9499  -1046   -553  -1743       O  
ATOM   1209  CB  LEU A 161      -8.658  74.722 294.287  1.00 73.88           C  
ANISOU 1209  CB  LEU A 161     8770   9530   9770  -1130   -370  -1615       C  
ATOM   1210  CG  LEU A 161     -10.097  74.606 293.782  1.00 77.50           C  
ANISOU 1210  CG  LEU A 161     9049  10222  10176  -1320   -429  -1703       C  
ATOM   1211  CD1 LEU A 161     -10.341  73.232 293.177  1.00 83.16           C  
ANISOU 1211  CD1 LEU A 161     9842  10852  10901  -1549   -405  -1930       C  
ATOM   1212  CD2 LEU A 161     -11.087  74.890 294.903  1.00 75.56           C  
ANISOU 1212  CD2 LEU A 161     8696  10008  10007  -1365   -397  -1589       C  
ATOM   1213  N   ASN A 162      -6.994  76.984 292.618  1.00 71.66           N  
ANISOU 1213  N   ASN A 162     8428   9559   9239   -776   -480  -1477       N  
ATOM   1214  CA  ASN A 162      -7.070  78.198 291.815  1.00 73.29           C  
ANISOU 1214  CA  ASN A 162     8546   9995   9303   -682   -549  -1390       C  
ATOM   1215  C   ASN A 162      -5.953  78.289 290.781  1.00 73.77           C  
ANISOU 1215  C   ASN A 162     8673  10099   9258   -621   -538  -1438       C  
ATOM   1216  O   ASN A 162      -5.879  79.256 290.023  1.00 79.03           O  
ANISOU 1216  O   ASN A 162     9300  10938   9789   -547   -578  -1359       O  
ATOM   1217  CB  ASN A 162      -7.041  79.436 292.715  1.00 74.98           C  
ANISOU 1217  CB  ASN A 162     8745  10186   9557   -548   -542  -1187       C  
ATOM   1218  CG  ASN A 162      -8.262  79.535 293.609  1.00 79.70           C  
ANISOU 1218  CG  ASN A 162     9251  10808  10224   -583   -552  -1131       C  
ATOM   1219  OD1 ASN A 162      -9.287  78.906 293.350  1.00 88.63           O  
ANISOU 1219  OD1 ASN A 162    10281  12050  11344   -712   -583  -1228       O  
ATOM   1220  ND2 ASN A 162      -8.159  80.332 294.665  1.00 76.11           N  
ANISOU 1220  ND2 ASN A 162     8822  10264   9833   -477   -521   -986       N  
ATOM   1221  N   THR A 163      -5.085  77.283 290.752  1.00 69.82           N  
ANISOU 1221  N   THR A 163     8280   9439   8809   -641   -473  -1561       N  
ATOM   1222  CA  THR A 163      -4.009  77.237 289.767  1.00 73.38           C  
ANISOU 1222  CA  THR A 163     8780   9945   9158   -583   -444  -1630       C  
ATOM   1223  C   THR A 163      -4.304  76.209 288.683  1.00 75.87           C  
ANISOU 1223  C   THR A 163     9118  10329   9380   -692   -459  -1851       C  
ATOM   1224  O   THR A 163      -3.581  76.115 287.690  1.00 76.36           O  
ANISOU 1224  O   THR A 163     9212  10480   9321   -654   -436  -1936       O  
ATOM   1225  CB  THR A 163      -2.657  76.906 290.415  1.00 75.76           C  
ANISOU 1225  CB  THR A 163     9173  10053   9560   -482   -356  -1621       C  
ATOM   1226  OG1 THR A 163      -2.759  75.672 291.135  1.00 82.63           O  
ANISOU 1226  OG1 THR A 163    10134  10698  10562   -524   -315  -1715       O  
ATOM   1227  CG2 THR A 163      -2.247  78.011 291.366  1.00 70.36           C  
ANISOU 1227  CG2 THR A 163     8463   9334   8936   -391   -348  -1425       C  
ATOM   1228  N   VAL A 164      -5.364  75.434 288.887  1.00 76.50           N  
ANISOU 1228  N   VAL A 164     9183  10372   9512   -841   -488  -1954       N  
ATOM   1229  CA  VAL A 164      -5.834  74.491 287.878  1.00 75.85           C  
ANISOU 1229  CA  VAL A 164     9118  10366   9336   -987   -516  -2184       C  
ATOM   1230  C   VAL A 164      -6.178  75.182 286.548  1.00 77.44           C  
ANISOU 1230  C   VAL A 164     9214  10903   9307   -983   -609  -2204       C  
ATOM   1231  O   VAL A 164      -5.761  74.700 285.494  1.00 83.93           O  
ANISOU 1231  O   VAL A 164    10093  11799   9999  -1002   -601  -2367       O  
ATOM   1232  CB  VAL A 164      -7.062  73.690 288.379  1.00 68.60           C  
ANISOU 1232  CB  VAL A 164     8171   9382   8512  -1193   -536  -2277       C  
ATOM   1233  CG1 VAL A 164      -7.685  72.893 287.243  1.00 67.94           C  
ANISOU 1233  CG1 VAL A 164     8077   9435   8304  -1379   -589  -2527       C  
ATOM   1234  CG2 VAL A 164      -6.667  72.772 289.522  1.00 68.74           C  
ANISOU 1234  CG2 VAL A 164     8347   9042   8727  -1209   -429  -2284       C  
ATOM   1235  N   PRO A 165      -6.926  76.309 286.581  1.00 73.72           N  
ANISOU 1235  N   PRO A 165     8603  10638   8771   -937   -693  -2036       N  
ATOM   1236  CA  PRO A 165      -7.197  76.967 285.295  1.00 75.34           C  
ANISOU 1236  CA  PRO A 165     8731  11159   8735   -900   -782  -2033       C  
ATOM   1237  C   PRO A 165      -5.930  77.394 284.559  1.00 79.60           C  
ANISOU 1237  C   PRO A 165     9365  11724   9157   -775   -720  -1995       C  
ATOM   1238  O   PRO A 165      -5.891  77.353 283.328  1.00 87.82           O  
ANISOU 1238  O   PRO A 165    10405  12974   9987   -785   -756  -2089       O  
ATOM   1239  CB  PRO A 165      -8.024  78.193 285.696  1.00 71.84           C  
ANISOU 1239  CB  PRO A 165     8158  10862   8275   -808   -857  -1813       C  
ATOM   1240  CG  PRO A 165      -8.667  77.805 286.971  1.00 72.18           C  
ANISOU 1240  CG  PRO A 165     8157  10743   8524   -886   -836  -1799       C  
ATOM   1241  CD  PRO A 165      -7.642  76.981 287.684  1.00 71.30           C  
ANISOU 1241  CD  PRO A 165     8206  10305   8580   -907   -714  -1858       C  
ATOM   1242  N   TYR A 166      -4.909  77.795 285.306  1.00 71.48           N  
ANISOU 1242  N   TYR A 166     8406  10505   8249   -668   -625  -1864       N  
ATOM   1243  CA  TYR A 166      -3.644  78.194 284.706  1.00 67.04           C  
ANISOU 1243  CA  TYR A 166     7909   9972   7592   -571   -545  -1828       C  
ATOM   1244  C   TYR A 166      -2.885  76.982 284.182  1.00 70.38           C  
ANISOU 1244  C   TYR A 166     8418  10325   8000   -603   -472  -2059       C  
ATOM   1245  O   TYR A 166      -2.226  77.054 283.146  1.00 73.79           O  
ANISOU 1245  O   TYR A 166     8877  10899   8262   -565   -432  -2116       O  
ATOM   1246  CB  TYR A 166      -2.796  78.967 285.714  1.00 62.36           C  
ANISOU 1246  CB  TYR A 166     7340   9217   7137   -473   -472  -1639       C  
ATOM   1247  CG  TYR A 166      -3.420  80.282 286.117  1.00 62.42           C  
ANISOU 1247  CG  TYR A 166     7300   9281   7136   -420   -527  -1414       C  
ATOM   1248  CD1 TYR A 166      -3.120  81.451 285.432  1.00 64.18           C  
ANISOU 1248  CD1 TYR A 166     7540   9643   7204   -350   -520  -1262       C  
ATOM   1249  CD2 TYR A 166      -4.322  80.352 287.170  1.00 59.67           C  
ANISOU 1249  CD2 TYR A 166     6905   8840   6927   -434   -573  -1353       C  
ATOM   1250  CE1 TYR A 166      -3.692  82.654 285.789  1.00 64.58           C  
ANISOU 1250  CE1 TYR A 166     7582   9710   7245   -280   -562  -1057       C  
ATOM   1251  CE2 TYR A 166      -4.900  81.551 287.534  1.00 58.35           C  
ANISOU 1251  CE2 TYR A 166     6705   8719   6747   -357   -615  -1159       C  
ATOM   1252  CZ  TYR A 166      -4.581  82.699 286.840  1.00 60.56           C  
ANISOU 1252  CZ  TYR A 166     7022   9109   6878   -272   -611  -1013       C  
ATOM   1253  OH  TYR A 166      -5.151  83.897 287.197  1.00 59.10           O  
ANISOU 1253  OH  TYR A 166     6839   8936   6680   -175   -644   -820       O  
ATOM   1254  N   PHE A 167      -2.985  75.867 284.898  1.00 68.95           N  
ANISOU 1254  N   PHE A 167     8294   9916   7988   -663   -443  -2189       N  
ATOM   1255  CA  PHE A 167      -2.367  74.620 284.461  1.00 67.55           C  
ANISOU 1255  CA  PHE A 167     8231   9628   7809   -677   -369  -2423       C  
ATOM   1256  C   PHE A 167      -2.993  74.148 283.153  1.00 68.35           C  
ANISOU 1256  C   PHE A 167     8334   9930   7707   -790   -429  -2628       C  
ATOM   1257  O   PHE A 167      -2.303  73.646 282.267  1.00 67.27           O  
ANISOU 1257  O   PHE A 167     8272   9839   7450   -756   -370  -2789       O  
ATOM   1258  CB  PHE A 167      -2.507  73.540 285.538  1.00 65.04           C  
ANISOU 1258  CB  PHE A 167     8007   8995   7710   -724   -328  -2499       C  
ATOM   1259  CG  PHE A 167      -1.944  72.202 285.138  1.00 63.86           C  
ANISOU 1259  CG  PHE A 167     8013   8681   7570   -722   -246  -2742       C  
ATOM   1260  CD1 PHE A 167      -0.611  71.901 285.365  1.00 61.08           C  
ANISOU 1260  CD1 PHE A 167     7736   8196   7274   -543   -138  -2748       C  
ATOM   1261  CD2 PHE A 167      -2.751  71.243 284.544  1.00 64.38           C  
ANISOU 1261  CD2 PHE A 167     8149   8729   7585   -896   -276  -2974       C  
ATOM   1262  CE1 PHE A 167      -0.093  70.672 285.001  1.00 60.98           C  
ANISOU 1262  CE1 PHE A 167     7881   8020   7268   -502    -54  -2972       C  
ATOM   1263  CE2 PHE A 167      -2.237  70.014 284.177  1.00 63.42           C  
ANISOU 1263  CE2 PHE A 167     8205   8420   7471   -888   -190  -3209       C  
ATOM   1264  CZ  PHE A 167      -0.906  69.728 284.407  1.00 62.96           C  
ANISOU 1264  CZ  PHE A 167     8237   8213   7470   -673    -76  -3203       C  
ATOM   1265  N   VAL A 168      -4.306  74.315 283.041  1.00 69.47           N  
ANISOU 1265  N   VAL A 168     8382  10212   7801   -919   -549  -2629       N  
ATOM   1266  CA  VAL A 168      -5.035  73.885 281.855  1.00 73.98           C  
ANISOU 1266  CA  VAL A 168     8929  11012   8168  -1047   -634  -2833       C  
ATOM   1267  C   VAL A 168      -4.723  74.766 280.649  1.00 73.95           C  
ANISOU 1267  C   VAL A 168     8883  11323   7892   -950   -666  -2768       C  
ATOM   1268  O   VAL A 168      -4.412  74.268 279.567  1.00 73.53           O  
ANISOU 1268  O   VAL A 168     8893  11391   7656   -971   -651  -2959       O  
ATOM   1269  CB  VAL A 168      -6.557  73.890 282.103  1.00 73.70           C  
ANISOU 1269  CB  VAL A 168     8758  11096   8149  -1210   -764  -2842       C  
ATOM   1270  CG1 VAL A 168      -7.311  73.622 280.808  1.00 76.38           C  
ANISOU 1270  CG1 VAL A 168     9034  11747   8239  -1335   -879  -3041       C  
ATOM   1271  CG2 VAL A 168      -6.925  72.863 283.165  1.00 71.76           C  
ANISOU 1271  CG2 VAL A 168     8574  10544   8147  -1353   -714  -2936       C  
ATOM   1272  N   PHE A 169      -4.795  76.078 280.845  1.00 75.50           N  
ANISOU 1272  N   PHE A 169     8994  11637   8054   -839   -701  -2498       N  
ATOM   1273  CA  PHE A 169      -4.645  77.028 279.748  1.00 78.26           C  
ANISOU 1273  CA  PHE A 169     9319  12279   8135   -749   -734  -2391       C  
ATOM   1274  C   PHE A 169      -3.192  77.414 279.480  1.00 82.87           C  
ANISOU 1274  C   PHE A 169     9990  12818   8677   -629   -589  -2313       C  
ATOM   1275  O   PHE A 169      -2.918  78.480 278.928  1.00 84.98           O  
ANISOU 1275  O   PHE A 169    10253  13254   8780   -543   -580  -2130       O  
ATOM   1276  CB  PHE A 169      -5.476  78.283 280.025  1.00 79.90           C  
ANISOU 1276  CB  PHE A 169     9421  12626   8312   -678   -835  -2131       C  
ATOM   1277  CG  PHE A 169      -6.958  78.062 279.916  1.00 85.31           C  
ANISOU 1277  CG  PHE A 169     9970  13497   8946   -776   -994  -2208       C  
ATOM   1278  CD1 PHE A 169      -7.484  77.315 278.874  1.00 85.72           C  
ANISOU 1278  CD1 PHE A 169     9993  13774   8804   -894  -1080  -2449       C  
ATOM   1279  CD2 PHE A 169      -7.824  78.588 280.861  1.00 85.81           C  
ANISOU 1279  CD2 PHE A 169     9924  13530   9149   -755  -1056  -2056       C  
ATOM   1280  CE1 PHE A 169      -8.846  77.104 278.769  1.00 86.09           C  
ANISOU 1280  CE1 PHE A 169     9882  14031   8799  -1006  -1234  -2535       C  
ATOM   1281  CE2 PHE A 169      -9.189  78.380 280.762  1.00 87.25           C  
ANISOU 1281  CE2 PHE A 169     9943  13925   9282   -847  -1197  -2133       C  
ATOM   1282  CZ  PHE A 169      -9.699  77.637 279.714  1.00 87.39           C  
ANISOU 1282  CZ  PHE A 169     9912  14185   9109   -981  -1290  -2373       C  
ATOM   1283  N   ARG A 170      -2.263  76.548 279.872  1.00 85.33           N  
ANISOU 1283  N   ARG A 170    10380  12907   9133   -622   -470  -2446       N  
ATOM   1284  CA  ARG A 170      -0.867  76.700 279.479  1.00 83.66           C  
ANISOU 1284  CA  ARG A 170    10220  12705   8861   -520   -327  -2433       C  
ATOM   1285  C   ARG A 170      -0.560  75.742 278.336  1.00 88.20           C  
ANISOU 1285  C   ARG A 170    10868  13390   9255   -541   -284  -2707       C  
ATOM   1286  O   ARG A 170      -0.982  74.587 278.355  1.00 89.76           O  
ANISOU 1286  O   ARG A 170    11124  13474   9509   -624   -309  -2945       O  
ATOM   1287  CB  ARG A 170       0.075  76.447 280.657  1.00 76.11           C  
ANISOU 1287  CB  ARG A 170     9283  11471   8166   -450   -221  -2390       C  
ATOM   1288  CG  ARG A 170       0.343  77.677 281.509  1.00 69.64           C  
ANISOU 1288  CG  ARG A 170     8406  10602   7452   -398   -210  -2107       C  
ATOM   1289  CD  ARG A 170       1.120  78.730 280.738  1.00 63.47           C  
ANISOU 1289  CD  ARG A 170     7611  10016   6489   -350   -136  -1964       C  
ATOM   1290  NE  ARG A 170       1.038  80.041 281.374  1.00 58.05           N  
ANISOU 1290  NE  ARG A 170     6898   9296   5861   -336   -152  -1693       N  
ATOM   1291  CZ  ARG A 170       2.067  80.868 281.524  1.00 59.08           C  
ANISOU 1291  CZ  ARG A 170     7021   9426   6000   -311    -47  -1549       C  
ATOM   1292  NH1 ARG A 170       3.270  80.523 281.085  1.00 63.90           N  
ANISOU 1292  NH1 ARG A 170     7616  10101   6562   -288     82  -1640       N  
ATOM   1293  NH2 ARG A 170       1.893  82.041 282.115  1.00 58.09           N  
ANISOU 1293  NH2 ARG A 170     6902   9240   5930   -314    -65  -1322       N  
ATOM   1294  N   ASP A 171       0.170  76.227 277.337  1.00 92.30           N  
ANISOU 1294  N   ASP A 171    11398  14124   9548   -476   -209  -2678       N  
ATOM   1295  CA  ASP A 171       0.470  75.423 276.159  1.00 94.95           C  
ANISOU 1295  CA  ASP A 171    11805  14603   9669   -483   -161  -2936       C  
ATOM   1296  C   ASP A 171       1.765  75.884 275.501  1.00 92.78           C  
ANISOU 1296  C   ASP A 171    11536  14472   9244   -376      1  -2878       C  
ATOM   1297  O   ASP A 171       2.225  77.003 275.733  1.00 89.87           O  
ANISOU 1297  O   ASP A 171    11113  14151   8881   -334     48  -2617       O  
ATOM   1298  CB  ASP A 171      -0.690  75.495 275.161  1.00 98.12           C  
ANISOU 1298  CB  ASP A 171    12196  15276   9810   -578   -312  -3013       C  
ATOM   1299  CG  ASP A 171      -0.554  74.492 274.032  1.00106.48           C  
ANISOU 1299  CG  ASP A 171    13344  16459  10653   -615   -284  -3336       C  
ATOM   1300  OD1 ASP A 171      -0.063  73.372 274.284  1.00108.89           O  
ANISOU 1300  OD1 ASP A 171    13739  16541  11093   -612   -194  -3565       O  
ATOM   1301  OD2 ASP A 171      -0.937  74.826 272.890  1.00113.41           O  
ANISOU 1301  OD2 ASP A 171    14219  17655  11217   -634   -351  -3361       O  
ATOM   1302  N   THR A 172       2.355  75.011 274.691  1.00 89.88           N  
ANISOU 1302  N   THR A 172    11238  14170   8743   -342     96  -3130       N  
ATOM   1303  CA  THR A 172       3.528  75.370 273.910  1.00 83.11           C  
ANISOU 1303  CA  THR A 172    10372  13505   7701   -250    261  -3105       C  
ATOM   1304  C   THR A 172       3.102  75.899 272.547  1.00 83.07           C  
ANISOU 1304  C   THR A 172    10393  13847   7322   -289    219  -3088       C  
ATOM   1305  O   THR A 172       2.418  75.210 271.789  1.00 88.38           O  
ANISOU 1305  O   THR A 172    11130  14628   7821   -346    134  -3316       O  
ATOM   1306  CB  THR A 172       4.481  74.176 273.725  1.00 79.96           C  
ANISOU 1306  CB  THR A 172    10031  13015   7333   -151    409  -3385       C  
ATOM   1307  OG1 THR A 172       3.769  73.079 273.138  1.00 85.96           O  
ANISOU 1307  OG1 THR A 172    10910  13755   7995   -213    339  -3692       O  
ATOM   1308  CG2 THR A 172       5.055  73.743 275.062  1.00 72.93           C  
ANISOU 1308  CG2 THR A 172     9114  11809   6787    -69    460  -3363       C  
ATOM   1309  N   ILE A 173       3.500  77.130 272.242  1.00 79.93           N  
ANISOU 1309  N   ILE A 173     9957  13621   6792   -267    278  -2817       N  
ATOM   1310  CA  ILE A 173       3.165  77.739 270.962  1.00 83.24           C  
ANISOU 1310  CA  ILE A 173    10420  14373   6835   -281    250  -2751       C  
ATOM   1311  C   ILE A 173       4.423  78.023 270.150  1.00 85.49           C  
ANISOU 1311  C   ILE A 173    10716  14851   6917   -225    468  -2728       C  
ATOM   1312  O   ILE A 173       5.316  78.743 270.599  1.00 85.35           O  
ANISOU 1312  O   ILE A 173    10641  14782   7006   -209    604  -2527       O  
ATOM   1313  CB  ILE A 173       2.374  79.050 271.138  1.00 83.38           C  
ANISOU 1313  CB  ILE A 173    10421  14449   6811   -300    129  -2418       C  
ATOM   1314  CG1 ILE A 173       1.012  78.781 271.784  1.00 82.33           C  
ANISOU 1314  CG1 ILE A 173    10252  14203   6828   -351    -90  -2454       C  
ATOM   1315  CG2 ILE A 173       2.185  79.733 269.795  1.00 89.01           C  
ANISOU 1315  CG2 ILE A 173    11199  15508   7113   -281    122  -2314       C  
ATOM   1316  CD1 ILE A 173       1.013  78.853 273.296  1.00 80.50           C  
ANISOU 1316  CD1 ILE A 173     9961  13641   6984   -359   -100  -2353       C  
ATOM   1317  N   SER A 174       4.488  77.453 268.951  1.00 87.82           N  
ANISOU 1317  N   SER A 174    11078  15382   6908   -210    505  -2945       N  
ATOM   1318  CA  SER A 174       5.644  77.635 268.084  1.00 91.60           C  
ANISOU 1318  CA  SER A 174    11564  16082   7159   -157    726  -2951       C  
ATOM   1319  C   SER A 174       5.687  79.039 267.491  1.00 96.07           C  
ANISOU 1319  C   SER A 174    12152  16870   7480   -185    767  -2612       C  
ATOM   1320  O   SER A 174       4.680  79.550 267.001  1.00 96.52           O  
ANISOU 1320  O   SER A 174    12272  17065   7334   -207    609  -2496       O  
ATOM   1321  CB  SER A 174       5.638  76.594 266.962  1.00 89.55           C  
ANISOU 1321  CB  SER A 174    11390  16012   6624   -127    754  -3299       C  
ATOM   1322  OG  SER A 174       5.779  75.282 267.476  1.00 86.45           O  
ANISOU 1322  OG  SER A 174    11013  15377   6456    -89    762  -3613       O  
ATOM   1323  N   ARG A 175       6.859  79.663 267.554  1.00100.37           N  
ANISOU 1323  N   ARG A 175    12644  17449   8043   -183    982  -2451       N  
ATOM   1324  CA  ARG A 175       7.084  80.943 266.893  1.00102.98           C  
ANISOU 1324  CA  ARG A 175    13029  17980   8120   -225   1075  -2140       C  
ATOM   1325  C   ARG A 175       7.560  80.716 265.465  1.00107.32           C  
ANISOU 1325  C   ARG A 175    13641  18878   8258   -197   1219  -2258       C  
ATOM   1326  O   ARG A 175       7.844  79.586 265.071  1.00107.21           O  
ANISOU 1326  O   ARG A 175    13615  18934   8187   -138   1266  -2590       O  
ATOM   1327  CB  ARG A 175       8.109  81.786 267.659  1.00102.92           C  
ANISOU 1327  CB  ARG A 175    12934  17844   8327   -284   1247  -1906       C  
ATOM   1328  CG  ARG A 175       7.523  82.685 268.734  1.00100.11           C  
ANISOU 1328  CG  ARG A 175    12585  17228   8224   -334   1118  -1637       C  
ATOM   1329  CD  ARG A 175       8.502  83.794 269.091  1.00101.75           C  
ANISOU 1329  CD  ARG A 175    12761  17393   8508   -432   1307  -1370       C  
ATOM   1330  NE  ARG A 175       7.930  84.785 269.999  1.00104.93           N  
ANISOU 1330  NE  ARG A 175    13212  17551   9104   -481   1198  -1103       N  
ATOM   1331  CZ  ARG A 175       8.248  84.892 271.285  1.00106.47           C  
ANISOU 1331  CZ  ARG A 175    13310  17492   9652   -520   1190  -1075       C  
ATOM   1332  NH1 ARG A 175       7.677  85.824 272.037  1.00103.01           N  
ANISOU 1332  NH1 ARG A 175    12941  16841   9357   -556   1095   -841       N  
ATOM   1333  NH2 ARG A 175       9.140  84.069 271.820  1.00107.84           N  
ANISOU 1333  NH2 ARG A 175    13323  17629  10021   -506   1276  -1283       N  
ATOM   1334  N   LEU A 176       7.646  81.794 264.693  1.00112.76           N  
ANISOU 1334  N   LEU A 176    14416  19774   8652   -233   1299  -1984       N  
ATOM   1335  CA  LEU A 176       8.152  81.714 263.329  1.00117.95           C  
ANISOU 1335  CA  LEU A 176    15142  20785   8888   -213   1462  -2052       C  
ATOM   1336  C   LEU A 176       9.676  81.675 263.319  1.00121.69           C  
ANISOU 1336  C   LEU A 176    15502  21325   9408   -237   1771  -2084       C  
ATOM   1337  O   LEU A 176      10.292  81.331 262.310  1.00128.74           O  
ANISOU 1337  O   LEU A 176    16411  22501  10003   -204   1945  -2223       O  
ATOM   1338  CB  LEU A 176       7.649  82.893 262.495  1.00117.45           C  
ANISOU 1338  CB  LEU A 176    15235  20920   8469   -234   1436  -1721       C  
ATOM   1339  CG  LEU A 176       6.157  82.904 262.163  1.00114.83           C  
ANISOU 1339  CG  LEU A 176    15002  20658   7969   -175   1137  -1711       C  
ATOM   1340  CD1 LEU A 176       5.789  84.158 261.387  1.00118.98           C  
ANISOU 1340  CD1 LEU A 176    15692  21370   8145   -157   1133  -1339       C  
ATOM   1341  CD2 LEU A 176       5.777  81.656 261.381  1.00111.87           C  
ANISOU 1341  CD2 LEU A 176    14635  20492   7377   -126   1046  -2111       C  
ATOM   1342  N   ASP A 177      10.279  82.028 264.450  1.00123.23           N  
ANISOU 1342  N   ASP A 177    15571  21282   9968   -292   1837  -1964       N  
ATOM   1343  CA  ASP A 177      11.730  82.027 264.581  1.00127.51           C  
ANISOU 1343  CA  ASP A 177    15956  21902  10591   -323   2114  -1990       C  
ATOM   1344  C   ASP A 177      12.240  80.648 264.987  1.00127.32           C  
ANISOU 1344  C   ASP A 177    15796  21812  10769   -193   2141  -2364       C  
ATOM   1345  O   ASP A 177      13.441  80.449 265.168  1.00133.02           O  
ANISOU 1345  O   ASP A 177    16350  22611  11582   -171   2353  -2437       O  
ATOM   1346  CB  ASP A 177      12.177  83.070 265.607  1.00132.28           C  
ANISOU 1346  CB  ASP A 177    16478  22305  11477   -454   2168  -1697       C  
ATOM   1347  CG  ASP A 177      11.091  84.080 265.923  1.00135.53           C  
ANISOU 1347  CG  ASP A 177    17048  22535  11913   -516   1978  -1396       C  
ATOM   1348  OD1 ASP A 177      10.325  84.440 265.005  1.00141.41           O  
ANISOU 1348  OD1 ASP A 177    17968  23427  12335   -494   1904  -1289       O  
ATOM   1349  OD2 ASP A 177      11.002  84.508 267.093  1.00130.73           O  
ANISOU 1349  OD2 ASP A 177    16389  21647  11635   -570   1902  -1271       O  
ATOM   1350  N   GLY A 178      11.320  79.701 265.131  1.00123.06           N  
ANISOU 1350  N   GLY A 178    15330  21131  10296   -105   1929  -2598       N  
ATOM   1351  CA  GLY A 178      11.663  78.370 265.594  1.00117.77           C  
ANISOU 1351  CA  GLY A 178    14587  20324   9837     28   1935  -2941       C  
ATOM   1352  C   GLY A 178      11.525  78.268 267.100  1.00105.70           C  
ANISOU 1352  C   GLY A 178    12971  18434   8757     29   1811  -2889       C  
ATOM   1353  O   GLY A 178      11.597  77.179 267.671  1.00102.46           O  
ANISOU 1353  O   GLY A 178    12535  17834   8562    142   1771  -3137       O  
ATOM   1354  N   ARG A 179      11.329  79.415 267.745  1.00 98.36           N  
ANISOU 1354  N   ARG A 179    12016  17398   7957    -92   1757  -2564       N  
ATOM   1355  CA  ARG A 179      11.140  79.463 269.190  1.00 91.99           C  
ANISOU 1355  CA  ARG A 179    11138  16265   7550   -103   1634  -2486       C  
ATOM   1356  C   ARG A 179       9.846  78.783 269.610  1.00 88.57           C  
ANISOU 1356  C   ARG A 179    10810  15604   7238    -73   1382  -2611       C  
ATOM   1357  O   ARG A 179       8.856  78.796 268.880  1.00 89.54           O  
ANISOU 1357  O   ARG A 179    11060  15821   7140   -101   1255  -2630       O  
ATOM   1358  CB  ARG A 179      11.135  80.910 269.689  1.00 92.12           C  
ANISOU 1358  CB  ARG A 179    11140  16222   7639   -249   1635  -2118       C  
ATOM   1359  CG  ARG A 179      12.477  81.609 269.647  1.00 94.86           C  
ANISOU 1359  CG  ARG A 179    11348  16724   7969   -330   1882  -1985       C  
ATOM   1360  CD  ARG A 179      12.347  83.023 270.184  1.00 97.87           C  
ANISOU 1360  CD  ARG A 179    11763  16987   8436   -496   1867  -1637       C  
ATOM   1361  NE  ARG A 179      13.584  83.785 270.054  1.00108.38           N  
ANISOU 1361  NE  ARG A 179    12976  18479   9724   -630   2113  -1501       N  
ATOM   1362  CZ  ARG A 179      13.703  85.071 270.366  1.00114.37           C  
ANISOU 1362  CZ  ARG A 179    13778  19158  10520   -810   2163  -1206       C  
ATOM   1363  NH1 ARG A 179      14.867  85.689 270.215  1.00117.36           N  
ANISOU 1363  NH1 ARG A 179    14037  19698  10856   -965   2402  -1110       N  
ATOM   1364  NH2 ARG A 179      12.654  85.742 270.828  1.00114.06           N  
ANISOU 1364  NH2 ARG A 179    13903  18878  10557   -841   1981  -1014       N  
ATOM   1365  N   ILE A 180       9.860  78.195 270.799  1.00 86.49           N  
ANISOU 1365  N   ILE A 180    10485  15058   7319    -22   1311  -2691       N  
ATOM   1366  CA  ILE A 180       8.661  77.606 271.373  1.00 81.45           C  
ANISOU 1366  CA  ILE A 180     9933  14179   6837    -25   1089  -2782       C  
ATOM   1367  C   ILE A 180       8.222  78.419 272.582  1.00 75.32           C  
ANISOU 1367  C   ILE A 180     9115  13179   6323    -96    973  -2524       C  
ATOM   1368  O   ILE A 180       8.926  78.476 273.589  1.00 78.68           O  
ANISOU 1368  O   ILE A 180     9436  13455   7002    -70   1027  -2469       O  
ATOM   1369  CB  ILE A 180       8.889  76.142 271.783  1.00 80.07           C  
ANISOU 1369  CB  ILE A 180     9768  13816   6837     96   1097  -3097       C  
ATOM   1370  CG1 ILE A 180       9.286  75.305 270.565  1.00 81.21           C  
ANISOU 1370  CG1 ILE A 180     9979  14165   6712    180   1216  -3382       C  
ATOM   1371  CG2 ILE A 180       7.645  75.575 272.445  1.00 78.17           C  
ANISOU 1371  CG2 ILE A 180     9618  13311   6771     51    884  -3172       C  
ATOM   1372  CD1 ILE A 180       9.562  73.852 270.883  1.00 80.48           C  
ANISOU 1372  CD1 ILE A 180     9939  13866   6774    322   1247  -3701       C  
ATOM   1373  N   MET A 181       7.063  79.060 272.475  1.00 70.23           N  
ANISOU 1373  N   MET A 181     8548  12533   5602   -173    811  -2370       N  
ATOM   1374  CA  MET A 181       6.547  79.880 273.564  1.00 71.82           C  
ANISOU 1374  CA  MET A 181     8729  12532   6027   -227    703  -2129       C  
ATOM   1375  C   MET A 181       5.831  79.042 274.616  1.00 75.92           C  
ANISOU 1375  C   MET A 181     9244  12778   6823   -207    556  -2256       C  
ATOM   1376  O   MET A 181       5.210  78.027 274.299  1.00 77.96           O  
ANISOU 1376  O   MET A 181     9557  13020   7043   -196    475  -2489       O  
ATOM   1377  CB  MET A 181       5.596  80.956 273.031  1.00 68.57           C  
ANISOU 1377  CB  MET A 181     8402  12237   5415   -280    598  -1897       C  
ATOM   1378  CG  MET A 181       6.283  82.111 272.327  1.00 70.34           C  
ANISOU 1378  CG  MET A 181     8658  12646   5423   -322    749  -1665       C  
ATOM   1379  SD  MET A 181       5.158  83.485 272.002  1.00 85.68           S  
ANISOU 1379  SD  MET A 181    10729  14634   7189   -341    619  -1335       S  
ATOM   1380  CE  MET A 181       3.953  82.701 270.934  1.00 71.60           C  
ANISOU 1380  CE  MET A 181     9001  13079   5124   -284    438  -1533       C  
ATOM   1381  N   CYS A 182       5.932  79.476 275.868  1.00 74.99           N  
ANISOU 1381  N   CYS A 182     9070  12446   6977   -219    530  -2104       N  
ATOM   1382  CA  CYS A 182       5.197  78.864 276.967  1.00 71.19           C  
ANISOU 1382  CA  CYS A 182     8592  11702   6755   -213    398  -2167       C  
ATOM   1383  C   CYS A 182       4.360  79.929 277.663  1.00 67.82           C  
ANISOU 1383  C   CYS A 182     8168  11183   6416   -269    281  -1912       C  
ATOM   1384  O   CYS A 182       4.850  80.636 278.542  1.00 72.86           O  
ANISOU 1384  O   CYS A 182     8762  11705   7216   -277    321  -1744       O  
ATOM   1385  CB  CYS A 182       6.152  78.198 277.959  1.00 70.31           C  
ANISOU 1385  CB  CYS A 182     8415  11403   6895   -136    480  -2255       C  
ATOM   1386  SG  CYS A 182       5.354  77.584 279.458  1.00101.33           S  
ANISOU 1386  SG  CYS A 182    12366  14993  11144   -132    342  -2274       S  
ATOM   1387  N   TYR A 183       3.098  80.045 277.262  1.00 62.45           N  
ANISOU 1387  N   TYR A 183     7534  10571   5622   -300    135  -1896       N  
ATOM   1388  CA  TYR A 183       2.253  81.135 277.737  1.00 60.81           C  
ANISOU 1388  CA  TYR A 183     7333  10321   5451   -317     31  -1649       C  
ATOM   1389  C   TYR A 183       0.772  80.753 277.717  1.00 66.53           C  
ANISOU 1389  C   TYR A 183     8053  11069   6157   -336   -154  -1719       C  
ATOM   1390  O   TYR A 183       0.427  79.586 277.526  1.00 70.14           O  
ANISOU 1390  O   TYR A 183     8506  11522   6620   -370   -199  -1967       O  
ATOM   1391  CB  TYR A 183       2.493  82.385 276.885  1.00 62.32           C  
ANISOU 1391  CB  TYR A 183     7579  10697   5402   -314     90  -1425       C  
ATOM   1392  CG  TYR A 183       2.261  83.689 277.613  1.00 60.30           C  
ANISOU 1392  CG  TYR A 183     7353  10313   5243   -314     70  -1137       C  
ATOM   1393  CD1 TYR A 183       1.255  84.561 277.216  1.00 65.13           C  
ANISOU 1393  CD1 TYR A 183     8031  11012   5701   -271    -35   -953       C  
ATOM   1394  CD2 TYR A 183       3.048  84.047 278.698  1.00 57.90           C  
ANISOU 1394  CD2 TYR A 183     7018   9806   5174   -343    154  -1057       C  
ATOM   1395  CE1 TYR A 183       1.043  85.754 277.879  1.00 70.02           C  
ANISOU 1395  CE1 TYR A 183     8709  11487   6409   -249    -41   -698       C  
ATOM   1396  CE2 TYR A 183       2.843  85.236 279.368  1.00 62.00           C  
ANISOU 1396  CE2 TYR A 183     7590  10190   5778   -352    142   -818       C  
ATOM   1397  CZ  TYR A 183       1.839  86.085 278.955  1.00 70.34           C  
ANISOU 1397  CZ  TYR A 183     8736  11303   6688   -301     51   -639       C  
ATOM   1398  OH  TYR A 183       1.629  87.271 279.620  1.00 75.29           O  
ANISOU 1398  OH  TYR A 183     9443  11767   7398   -289     50   -408       O  
ATOM   1399  N   TYR A 184      -0.095  81.742 277.917  1.00 68.18           N  
ANISOU 1399  N   TYR A 184     8261  11302   6341   -317   -254  -1505       N  
ATOM   1400  CA  TYR A 184      -1.538  81.522 277.925  1.00 68.51           C  
ANISOU 1400  CA  TYR A 184     8257  11416   6358   -328   -433  -1548       C  
ATOM   1401  C   TYR A 184      -2.079  81.098 276.566  1.00 72.73           C  
ANISOU 1401  C   TYR A 184     8796  12248   6592   -344   -513  -1695       C  
ATOM   1402  O   TYR A 184      -1.977  81.843 275.594  1.00 75.25           O  
ANISOU 1402  O   TYR A 184     9166  12780   6646   -289   -502  -1568       O  
ATOM   1403  CB  TYR A 184      -2.279  82.789 278.363  1.00 68.97           C  
ANISOU 1403  CB  TYR A 184     8312  11464   6429   -257   -510  -1270       C  
ATOM   1404  CG  TYR A 184      -2.027  83.230 279.785  1.00 65.17           C  
ANISOU 1404  CG  TYR A 184     7827  10700   6236   -247   -465  -1141       C  
ATOM   1405  CD1 TYR A 184      -2.547  82.519 280.857  1.00 62.74           C  
ANISOU 1405  CD1 TYR A 184     7450  10223   6165   -287   -520  -1245       C  
ATOM   1406  CD2 TYR A 184      -1.297  84.380 280.052  1.00 66.38           C  
ANISOU 1406  CD2 TYR A 184     8055  10758   6409   -212   -365   -916       C  
ATOM   1407  CE1 TYR A 184      -2.328  82.929 282.156  1.00 63.77           C  
ANISOU 1407  CE1 TYR A 184     7582  10115   6532   -271   -482  -1129       C  
ATOM   1408  CE2 TYR A 184      -1.075  84.797 281.343  1.00 69.13           C  
ANISOU 1408  CE2 TYR A 184     8404  10861   7001   -212   -332   -817       C  
ATOM   1409  CZ  TYR A 184      -1.591  84.071 282.392  1.00 66.38           C  
ANISOU 1409  CZ  TYR A 184     7982  10367   6871   -231   -395   -924       C  
ATOM   1410  OH  TYR A 184      -1.365  84.493 283.681  1.00 62.88           O  
ANISOU 1410  OH  TYR A 184     7547   9698   6646   -225   -364   -828       O  
ATOM   1411  N   ASN A 185      -2.665  79.909 276.502  1.00 72.37           N  
ANISOU 1411  N   ASN A 185     8708  12212   6576   -429   -591  -1962       N  
ATOM   1412  CA  ASN A 185      -3.447  79.523 275.337  1.00 72.97           C  
ANISOU 1412  CA  ASN A 185     8766  12587   6374   -468   -711  -2117       C  
ATOM   1413  C   ASN A 185      -4.911  79.422 275.734  1.00 76.15           C  
ANISOU 1413  C   ASN A 185     9048  13053   6831   -521   -897  -2137       C  
ATOM   1414  O   ASN A 185      -5.407  78.341 276.046  1.00 83.01           O  
ANISOU 1414  O   ASN A 185     9876  13844   7821   -653   -945  -2374       O  
ATOM   1415  CB  ASN A 185      -2.955  78.202 274.745  1.00 73.42           C  
ANISOU 1415  CB  ASN A 185     8878  12645   6374   -551   -648  -2452       C  
ATOM   1416  CG  ASN A 185      -3.586  77.894 273.400  1.00 73.68           C  
ANISOU 1416  CG  ASN A 185     8911  13019   6066   -594   -758  -2621       C  
ATOM   1417  OD1 ASN A 185      -4.228  78.752 272.791  1.00 71.49           O  
ANISOU 1417  OD1 ASN A 185     8593  13011   5558   -534   -870  -2459       O  
ATOM   1418  ND2 ASN A 185      -3.398  76.669 272.925  1.00 76.70           N  
ANISOU 1418  ND2 ASN A 185     9350  13392   6402   -686   -729  -2952       N  
ATOM   1419  N   VAL A 186      -5.587  80.566 275.740  1.00 73.36           N  
ANISOU 1419  N   VAL A 186     8645  12837   6393   -415   -990  -1882       N  
ATOM   1420  CA  VAL A 186      -6.987  80.650 276.139  1.00 75.82           C  
ANISOU 1420  CA  VAL A 186     8809  13254   6747   -428  -1162  -1865       C  
ATOM   1421  C   VAL A 186      -7.886  79.749 275.291  1.00 82.98           C  
ANISOU 1421  C   VAL A 186     9619  14446   7465   -552  -1311  -2139       C  
ATOM   1422  O   VAL A 186      -8.766  79.062 275.814  1.00 86.20           O  
ANISOU 1422  O   VAL A 186     9904  14839   8010   -684  -1399  -2292       O  
ATOM   1423  CB  VAL A 186      -7.488  82.108 276.054  1.00 78.65           C  
ANISOU 1423  CB  VAL A 186     9151  13750   6981   -238  -1232  -1538       C  
ATOM   1424  CG1 VAL A 186      -9.005  82.167 276.036  1.00 81.10           C  
ANISOU 1424  CG1 VAL A 186     9276  14315   7223   -218  -1435  -1550       C  
ATOM   1425  CG2 VAL A 186      -6.924  82.929 277.207  1.00 80.45           C  
ANISOU 1425  CG2 VAL A 186     9448  13658   7460   -159  -1113  -1301       C  
ATOM   1426  N   LEU A 187      -7.642  79.737 273.985  1.00 83.34           N  
ANISOU 1426  N   LEU A 187     9723  14755   7188   -528  -1331  -2210       N  
ATOM   1427  CA  LEU A 187      -8.484  78.998 273.052  1.00 85.02           C  
ANISOU 1427  CA  LEU A 187     9848  15290   7166   -643  -1487  -2472       C  
ATOM   1428  C   LEU A 187      -8.144  77.509 272.985  1.00 84.60           C  
ANISOU 1428  C   LEU A 187     9855  15088   7202   -852  -1424  -2848       C  
ATOM   1429  O   LEU A 187      -8.639  76.798 272.110  1.00 91.52           O  
ANISOU 1429  O   LEU A 187    10701  16206   7868   -975  -1526  -3113       O  
ATOM   1430  CB  LEU A 187      -8.376  79.612 271.653  1.00 91.39           C  
ANISOU 1430  CB  LEU A 187    10711  16459   7555   -519  -1538  -2393       C  
ATOM   1431  CG  LEU A 187      -8.760  81.087 271.520  1.00 91.01           C  
ANISOU 1431  CG  LEU A 187    10646  16575   7359   -288  -1607  -2016       C  
ATOM   1432  CD1 LEU A 187      -8.518  81.570 270.101  1.00 96.23           C  
ANISOU 1432  CD1 LEU A 187    11405  17568   7590   -175  -1631  -1944       C  
ATOM   1433  CD2 LEU A 187     -10.208  81.294 271.914  1.00 88.19           C  
ANISOU 1433  CD2 LEU A 187    10073  16404   7033   -263  -1814  -1978       C  
ATOM   1434  N   LEU A 188      -7.307  77.038 273.906  1.00 79.36           N  
ANISOU 1434  N   LEU A 188     9285  14028   6841   -885  -1258  -2876       N  
ATOM   1435  CA  LEU A 188      -6.876  75.642 273.897  1.00 81.14           C  
ANISOU 1435  CA  LEU A 188     9609  14054   7164  -1042  -1173  -3210       C  
ATOM   1436  C   LEU A 188      -8.025  74.687 274.203  1.00 84.06           C  
ANISOU 1436  C   LEU A 188     9885  14420   7634  -1270  -1293  -3454       C  
ATOM   1437  O   LEU A 188      -8.085  73.582 273.664  1.00 88.56           O  
ANISOU 1437  O   LEU A 188    10526  14988   8133  -1433  -1296  -3783       O  
ATOM   1438  CB  LEU A 188      -5.740  75.422 274.899  1.00 77.96           C  
ANISOU 1438  CB  LEU A 188     9319  13238   7063   -986   -979  -3148       C  
ATOM   1439  CG  LEU A 188      -5.148  74.012 274.956  1.00 77.75           C  
ANISOU 1439  CG  LEU A 188     9431  12957   7152  -1086   -865  -3461       C  
ATOM   1440  CD1 LEU A 188      -4.624  73.590 273.589  1.00 79.80           C  
ANISOU 1440  CD1 LEU A 188     9792  13418   7112  -1076   -826  -3679       C  
ATOM   1441  CD2 LEU A 188      -4.050  73.928 276.004  1.00 67.78           C  
ANISOU 1441  CD2 LEU A 188     8250  11329   6174   -983   -694  -3355       C  
ATOM   1442  N   LEU A 189      -8.939  75.117 275.066  1.00 85.68           N  
ANISOU 1442  N   LEU A 189     9934  14623   7998  -1290  -1384  -3301       N  
ATOM   1443  CA  LEU A 189     -10.036  74.260 275.497  1.00 92.02           C  
ANISOU 1443  CA  LEU A 189    10625  15415   8924  -1530  -1476  -3507       C  
ATOM   1444  C   LEU A 189     -11.390  74.955 275.368  1.00 94.33           C  
ANISOU 1444  C   LEU A 189    10661  16089   9090  -1530  -1679  -3402       C  
ATOM   1445  O   LEU A 189     -11.570  76.076 275.842  1.00 94.52           O  
ANISOU 1445  O   LEU A 189    10598  16162   9151  -1339  -1703  -3093       O  
ATOM   1446  CB  LEU A 189      -9.812  73.806 276.941  1.00 97.00           C  
ANISOU 1446  CB  LEU A 189    11310  15607   9938  -1589  -1350  -3465       C  
ATOM   1447  CG  LEU A 189     -10.819  72.813 277.526  1.00103.76           C  
ANISOU 1447  CG  LEU A 189    12090  16373  10961  -1868  -1395  -3672       C  
ATOM   1448  CD1 LEU A 189     -10.859  71.537 276.698  1.00108.87           C  
ANISOU 1448  CD1 LEU A 189    12849  17018  11498  -2098  -1399  -4063       C  
ATOM   1449  CD2 LEU A 189     -10.486  72.507 278.980  1.00101.81           C  
ANISOU 1449  CD2 LEU A 189    11926  15689  11067  -1879  -1254  -3570       C  
ATOM   1450  N   ASN A 190     -12.331  74.270 274.724  1.00103.73           N  
ANISOU 1450  N   ASN A 190    11732  17554  10129  -1742  -1823  -3673       N  
ATOM   1451  CA  ASN A 190     -13.689  74.775 274.517  1.00111.12           C  
ANISOU 1451  CA  ASN A 190    12385  18908  10926  -1755  -2032  -3620       C  
ATOM   1452  C   ASN A 190     -13.763  76.196 273.955  1.00109.57           C  
ANISOU 1452  C   ASN A 190    12114  19041  10476  -1443  -2132  -3313       C  
ATOM   1453  O   ASN A 190     -14.146  77.125 274.667  1.00109.67           O  
ANISOU 1453  O   ASN A 190    12016  19058  10594  -1273  -2153  -3031       O  
ATOM   1454  CB  ASN A 190     -14.474  74.712 275.831  1.00117.24           C  
ANISOU 1454  CB  ASN A 190    12998  19546  12003  -1858  -2029  -3552       C  
ATOM   1455  CG  ASN A 190     -14.675  73.292 276.323  1.00124.24           C  
ANISOU 1455  CG  ASN A 190    13951  20128  13126  -2185  -1938  -3825       C  
ATOM   1456  OD1 ASN A 190     -14.741  72.352 275.531  1.00129.62           O  
ANISOU 1456  OD1 ASN A 190    14727  20790  13735  -2349  -1927  -4060       O  
ATOM   1457  ND2 ASN A 190     -14.777  73.131 277.638  1.00124.71           N  
ANISOU 1457  ND2 ASN A 190    13992  19911  13483  -2263  -1852  -3765       N  
ATOM   1458  N   PRO A 191     -13.390  76.374 272.678  1.00107.27           N  
ANISOU 1458  N   PRO A 191    11916  18976   9867  -1348  -2166  -3338       N  
ATOM   1459  CA  PRO A 191     -13.549  77.687 272.047  1.00110.38           C  
ANISOU 1459  CA  PRO A 191    12261  19695   9985  -1057  -2267  -3043       C  
ATOM   1460  C   PRO A 191     -14.995  77.930 271.623  1.00117.77           C  
ANISOU 1460  C   PRO A 191    12949  20977  10821  -1027  -2450  -2993       C  
ATOM   1461  O   PRO A 191     -15.577  77.099 270.925  1.00122.54           O  
ANISOU 1461  O   PRO A 191    13492  21707  11359  -1204  -2509  -3222       O  
ATOM   1462  CB  PRO A 191     -12.624  77.611 270.823  1.00110.31           C  
ANISOU 1462  CB  PRO A 191    12460  19759   9694   -999  -2202  -3105       C  
ATOM   1463  CG  PRO A 191     -11.796  76.363 271.013  1.00106.51           C  
ANISOU 1463  CG  PRO A 191    12146  18947   9378  -1218  -2046  -3413       C  
ATOM   1464  CD  PRO A 191     -12.657  75.441 271.809  1.00106.09           C  
ANISOU 1464  CD  PRO A 191    11965  18730   9613  -1465  -2075  -3596       C  
ATOM   1465  N   GLY A 192     -15.565  79.055 272.040  1.00118.75           N  
ANISOU 1465  N   GLY A 192    12935  21253  10933   -794  -2534  -2699       N  
ATOM   1466  CA  GLY A 192     -16.939  79.378 271.701  1.00122.86           C  
ANISOU 1466  CA  GLY A 192    13204  22114  11364   -718  -2699  -2633       C  
ATOM   1467  C   GLY A 192     -17.104  79.769 270.246  1.00127.98           C  
ANISOU 1467  C   GLY A 192    13882  23097  11648   -565  -2800  -2578       C  
ATOM   1468  O   GLY A 192     -16.118  79.881 269.516  1.00130.74           O  
ANISOU 1468  O   GLY A 192    14459  23410  11807   -503  -2732  -2561       O  
ATOM   1469  N   PRO A 193     -18.358  79.974 269.813  1.00131.39           N  
ANISOU 1469  N   PRO A 193    14080  23869  11974   -501  -2958  -2550       N  
ATOM   1470  CA  PRO A 193     -18.676  80.403 268.446  1.00136.57           C  
ANISOU 1470  CA  PRO A 193    14736  24880  12276   -332  -3077  -2482       C  
ATOM   1471  C   PRO A 193     -17.982  81.713 268.085  1.00134.12           C  
ANISOU 1471  C   PRO A 193    14623  24582  11754     24  -3050  -2128       C  
ATOM   1472  O   PRO A 193     -17.593  81.915 266.934  1.00137.01           O  
ANISOU 1472  O   PRO A 193    15135  25098  11824    117  -3066  -2091       O  
ATOM   1473  CB  PRO A 193     -20.197  80.580 268.478  1.00142.07           C  
ANISOU 1473  CB  PRO A 193    15107  25902  12973   -283  -3237  -2461       C  
ATOM   1474  CG  PRO A 193     -20.656  79.692 269.585  1.00139.89           C  
ANISOU 1474  CG  PRO A 193    14670  25447  13035   -578  -3187  -2666       C  
ATOM   1475  CD  PRO A 193     -19.572  79.752 270.618  1.00132.28           C  
ANISOU 1475  CD  PRO A 193    13901  24060  12299   -598  -3022  -2598       C  
ATOM   1476  N   ASP A 194     -17.834  82.589 269.072  1.00125.18           N  
ANISOU 1476  N   ASP A 194    13510  23283  10771    215  -3001  -1865       N  
ATOM   1477  CA  ASP A 194     -17.115  83.843 268.895  1.00120.63           C  
ANISOU 1477  CA  ASP A 194    13158  22644  10030    532  -2945  -1511       C  
ATOM   1478  C   ASP A 194     -15.741  83.732 269.545  1.00115.36           C  
ANISOU 1478  C   ASP A 194    12723  21615   9495    439  -2761  -1512       C  
ATOM   1479  O   ASP A 194     -15.617  83.833 270.765  1.00116.34           O  
ANISOU 1479  O   ASP A 194    12812  21509   9881    418  -2704  -1467       O  
ATOM   1480  CB  ASP A 194     -17.907  85.008 269.497  1.00120.07           C  
ANISOU 1480  CB  ASP A 194    12977  22631  10012    847  -3013  -1194       C  
ATOM   1481  CG  ASP A 194     -17.374  86.368 269.073  1.00120.74           C  
ANISOU 1481  CG  ASP A 194    13317  22679   9880   1200  -2971   -805       C  
ATOM   1482  OD1 ASP A 194     -16.181  86.472 268.717  1.00119.54           O  
ANISOU 1482  OD1 ASP A 194    13437  22371   9612   1175  -2844   -751       O  
ATOM   1483  OD2 ASP A 194     -18.155  87.343 269.104  1.00123.60           O  
ANISOU 1483  OD2 ASP A 194    13616  23156  10189   1504  -3049   -549       O  
ATOM   1484  N   ARG A 195     -14.713  83.523 268.728  1.00111.53           N  
ANISOU 1484  N   ARG A 195    12462  21094   8819    386  -2664  -1569       N  
ATOM   1485  CA  ARG A 195     -13.357  83.359 269.238  1.00103.84           C  
ANISOU 1485  CA  ARG A 195    11697  19814   7943    291  -2476  -1597       C  
ATOM   1486  C   ARG A 195     -12.844  84.626 269.906  1.00100.49           C  
ANISOU 1486  C   ARG A 195    11436  19103   7643    526  -2344  -1201       C  
ATOM   1487  O   ARG A 195     -12.247  84.566 270.977  1.00 97.31           O  
ANISOU 1487  O   ARG A 195    11100  18273   7599    444  -2177  -1174       O  
ATOM   1488  CB  ARG A 195     -12.400  82.945 268.119  1.00106.13           C  
ANISOU 1488  CB  ARG A 195    12189  20141   7995    214  -2373  -1721       C  
ATOM   1489  CG  ARG A 195     -12.643  81.553 267.570  1.00108.99           C  
ANISOU 1489  CG  ARG A 195    12474  20564   8374    -58  -2407  -2125       C  
ATOM   1490  CD  ARG A 195     -11.440  81.064 266.785  1.00109.08           C  
ANISOU 1490  CD  ARG A 195    12709  20510   8226   -140  -2249  -2270       C  
ATOM   1491  NE  ARG A 195     -11.768  79.912 265.952  1.00109.54           N  
ANISOU 1491  NE  ARG A 195    12728  20679   8213   -337  -2301  -2612       N  
ATOM   1492  CZ  ARG A 195     -12.175  80.001 264.691  1.00107.65           C  
ANISOU 1492  CZ  ARG A 195    12491  20743   7669   -272  -2399  -2614       C  
ATOM   1493  NH1 ARG A 195     -12.302  81.189 264.118  1.00106.46           N  
ANISOU 1493  NH1 ARG A 195    12388  20800   7263     -7  -2450  -2282       N  
ATOM   1494  NH2 ARG A 195     -12.456  78.904 264.003  1.00111.09           N  
ANISOU 1494  NH2 ARG A 195    12899  21259   8050   -469  -2443  -2944       N  
ATOM   1495  N   ASP A 196     -13.082  85.772 269.275  1.00103.17           N  
ANISOU 1495  N   ASP A 196    11856  19646   7696    816  -2411   -890       N  
ATOM   1496  CA  ASP A 196     -12.586  87.043 269.791  1.00105.63           C  
ANISOU 1496  CA  ASP A 196    12375  19647   8113   1035  -2267   -502       C  
ATOM   1497  C   ASP A 196     -13.219  87.396 271.135  1.00105.90           C  
ANISOU 1497  C   ASP A 196    12279  19466   8493   1104  -2282   -405       C  
ATOM   1498  O   ASP A 196     -12.612  88.082 271.957  1.00103.86           O  
ANISOU 1498  O   ASP A 196    12185  18810   8467   1163  -2115   -200       O  
ATOM   1499  CB  ASP A 196     -12.841  88.164 268.781  1.00111.30           C  
ANISOU 1499  CB  ASP A 196    13224  20639   8426   1347  -2347   -187       C  
ATOM   1500  CG  ASP A 196     -12.114  89.446 269.138  1.00111.36           C  
ANISOU 1500  CG  ASP A 196    13524  20280   8508   1528  -2157    201       C  
ATOM   1501  OD1 ASP A 196     -10.959  89.620 268.694  1.00107.77           O  
ANISOU 1501  OD1 ASP A 196    13313  19660   7974   1453  -1965    274       O  
ATOM   1502  OD2 ASP A 196     -12.698  90.281 269.862  1.00113.26           O  
ANISOU 1502  OD2 ASP A 196    13751  20399   8883   1737  -2191    425       O  
ATOM   1503  N   ALA A 197     -14.441  86.919 271.353  1.00108.59           N  
ANISOU 1503  N   ALA A 197    12318  20087   8857   1084  -2479   -566       N  
ATOM   1504  CA  ALA A 197     -15.148  87.173 272.603  1.00106.00           C  
ANISOU 1504  CA  ALA A 197    11830  19611   8833   1145  -2497   -500       C  
ATOM   1505  C   ALA A 197     -14.652  86.254 273.714  1.00104.55           C  
ANISOU 1505  C   ALA A 197    11623  19048   9053    846  -2351   -719       C  
ATOM   1506  O   ALA A 197     -14.374  86.706 274.826  1.00101.95           O  
ANISOU 1506  O   ALA A 197    11368  18356   9014    889  -2222   -578       O  
ATOM   1507  CB  ALA A 197     -16.647  87.007 272.409  1.00107.45           C  
ANISOU 1507  CB  ALA A 197    11669  20277   8880   1228  -2754   -590       C  
ATOM   1508  N   THR A 198     -14.538  84.965 273.410  1.00105.29           N  
ANISOU 1508  N   THR A 198    11632  19219   9153    551  -2370  -1064       N  
ATOM   1509  CA  THR A 198     -14.093  83.987 274.396  1.00101.41           C  
ANISOU 1509  CA  THR A 198    11136  18376   9021    275  -2237  -1279       C  
ATOM   1510  C   THR A 198     -12.596  84.117 274.663  1.00 99.11           C  
ANISOU 1510  C   THR A 198    11130  17659   8870    243  -2002  -1198       C  
ATOM   1511  O   THR A 198     -12.083  83.588 275.648  1.00 96.47           O  
ANISOU 1511  O   THR A 198    10831  16975   8849     93  -1870  -1287       O  
ATOM   1512  CB  THR A 198     -14.412  82.544 273.950  1.00101.31           C  
ANISOU 1512  CB  THR A 198    10984  18543   8965    -30  -2317  -1680       C  
ATOM   1513  OG1 THR A 198     -14.047  81.627 274.988  1.00103.41           O  
ANISOU 1513  OG1 THR A 198    11267  18437   9588   -270  -2184  -1858       O  
ATOM   1514  CG2 THR A 198     -13.653  82.192 272.686  1.00 99.21           C  
ANISOU 1514  CG2 THR A 198    10881  18401   8414    -82  -2297  -1804       C  
ATOM   1515  N   CYS A 199     -11.900  84.827 273.781  1.00102.28           N  
ANISOU 1515  N   CYS A 199    11726  18112   9025    384  -1949  -1024       N  
ATOM   1516  CA  CYS A 199     -10.476  85.095 273.959  1.00 99.16           C  
ANISOU 1516  CA  CYS A 199    11577  17366   8733    361  -1724   -923       C  
ATOM   1517  C   CYS A 199     -10.290  86.259 274.922  1.00 95.11           C  
ANISOU 1517  C   CYS A 199    11165  16559   8413    525  -1630   -612       C  
ATOM   1518  O   CYS A 199      -9.357  86.276 275.723  1.00 93.16           O  
ANISOU 1518  O   CYS A 199    11030  15951   8417    444  -1459   -586       O  
ATOM   1519  CB  CYS A 199      -9.808  85.401 272.613  1.00101.99           C  
ANISOU 1519  CB  CYS A 199    12104  17911   8738    422  -1684   -860       C  
ATOM   1520  SG  CYS A 199      -8.117  84.797 272.436  1.00114.76           S  
ANISOU 1520  SG  CYS A 199    13907  19272  10425    245  -1437   -995       S  
ATOM   1521  N   ASN A 200     -11.193  87.229 274.835  1.00 95.56           N  
ANISOU 1521  N   ASN A 200    11183  16781   8344    764  -1748   -386       N  
ATOM   1522  CA  ASN A 200     -11.133  88.419 275.673  1.00 95.01           C  
ANISOU 1522  CA  ASN A 200    11234  16441   8426    949  -1668    -90       C  
ATOM   1523  C   ASN A 200     -11.675  88.174 277.077  1.00 91.80           C  
ANISOU 1523  C   ASN A 200    10675  15846   8359    903  -1673   -155       C  
ATOM   1524  O   ASN A 200     -11.063  88.576 278.069  1.00 87.16           O  
ANISOU 1524  O   ASN A 200    10207  14891   8019    890  -1530    -57       O  
ATOM   1525  CB  ASN A 200     -11.906  89.563 275.015  1.00 97.93           C  
ANISOU 1525  CB  ASN A 200    11646  17049   8514   1266  -1787    187       C  
ATOM   1526  CG  ASN A 200     -11.755  90.874 275.760  1.00 99.51           C  
ANISOU 1526  CG  ASN A 200    12037  16932   8840   1471  -1683    501       C  
ATOM   1527  OD1 ASN A 200     -10.774  91.090 276.472  1.00101.52           O  
ANISOU 1527  OD1 ASN A 200    12456  16799   9319   1359  -1498    545       O  
ATOM   1528  ND2 ASN A 200     -12.731  91.760 275.598  1.00 99.61           N  
ANISOU 1528  ND2 ASN A 200    12031  17113   8704   1779  -1804    714       N  
ATOM   1529  N   SER A 201     -12.826  87.512 277.152  1.00 92.81           N  
ANISOU 1529  N   SER A 201    10532  16244   8486    866  -1837   -327       N  
ATOM   1530  CA  SER A 201     -13.498  87.275 278.425  1.00 90.94           C  
ANISOU 1530  CA  SER A 201    10126  15889   8538    827  -1846   -383       C  
ATOM   1531  C   SER A 201     -12.657  86.413 279.359  1.00 89.26           C  
ANISOU 1531  C   SER A 201     9965  15315   8633    570  -1693   -553       C  
ATOM   1532  O   SER A 201     -12.472  86.751 280.526  1.00 88.59           O  
ANISOU 1532  O   SER A 201     9928  14934   8797    593  -1595   -462       O  
ATOM   1533  CB  SER A 201     -14.861  86.617 278.197  1.00 91.36           C  
ANISOU 1533  CB  SER A 201     9855  16350   8507    785  -2043   -564       C  
ATOM   1534  OG  SER A 201     -14.710  85.288 277.734  1.00 94.34           O  
ANISOU 1534  OG  SER A 201    10154  16827   8863    490  -2069   -881       O  
ATOM   1535  N   ARG A 202     -12.150  85.300 278.836  1.00 86.19           N  
ANISOU 1535  N   ARG A 202     9579  14957   8215    342  -1674   -800       N  
ATOM   1536  CA  ARG A 202     -11.362  84.371 279.637  1.00 80.08           C  
ANISOU 1536  CA  ARG A 202     8858  13859   7710    122  -1538   -972       C  
ATOM   1537  C   ARG A 202     -10.065  84.999 280.134  1.00 77.96           C  
ANISOU 1537  C   ARG A 202     8816  13238   7568    170  -1358   -807       C  
ATOM   1538  O   ARG A 202      -9.630  84.732 281.255  1.00 73.60           O  
ANISOU 1538  O   ARG A 202     8292  12388   7284     91  -1257   -832       O  
ATOM   1539  CB  ARG A 202     -11.052  83.105 278.839  1.00 75.21           C  
ANISOU 1539  CB  ARG A 202     8229  13345   7000    -93  -1550  -1267       C  
ATOM   1540  CG  ARG A 202     -12.190  82.099 278.808  1.00 76.31           C  
ANISOU 1540  CG  ARG A 202     8145  13704   7146   -264  -1684  -1517       C  
ATOM   1541  CD  ARG A 202     -11.798  80.847 278.044  1.00 80.84           C  
ANISOU 1541  CD  ARG A 202     8758  14321   7636   -485  -1677  -1826       C  
ATOM   1542  NE  ARG A 202     -12.780  79.779 278.204  1.00 86.32           N  
ANISOU 1542  NE  ARG A 202     9270  15136   8394   -712  -1771  -2089       N  
ATOM   1543  CZ  ARG A 202     -12.815  78.679 277.459  1.00 91.30           C  
ANISOU 1543  CZ  ARG A 202     9899  15872   8917   -923  -1808  -2393       C  
ATOM   1544  NH1 ARG A 202     -11.925  78.501 276.491  1.00 92.47           N  
ANISOU 1544  NH1 ARG A 202    10213  16040   8881   -907  -1760  -2471       N  
ATOM   1545  NH2 ARG A 202     -13.745  77.758 277.675  1.00 94.16           N  
ANISOU 1545  NH2 ARG A 202    10100  16324   9353  -1159  -1885  -2626       N  
ATOM   1546  N   GLN A 203      -9.449  85.831 279.300  1.00 80.95           N  
ANISOU 1546  N   GLN A 203     9352  13662   7742    289  -1317   -639       N  
ATOM   1547  CA  GLN A 203      -8.206  86.491 279.681  1.00 79.75           C  
ANISOU 1547  CA  GLN A 203     9404  13210   7689    305  -1143   -486       C  
ATOM   1548  C   GLN A 203      -8.469  87.549 280.747  1.00 77.33           C  
ANISOU 1548  C   GLN A 203     9146  12691   7545    444  -1113   -263       C  
ATOM   1549  O   GLN A 203      -7.668  87.732 281.664  1.00 72.87           O  
ANISOU 1549  O   GLN A 203     8674  11823   7192    389   -987   -225       O  
ATOM   1550  CB  GLN A 203      -7.528  87.119 278.462  1.00 79.76           C  
ANISOU 1550  CB  GLN A 203     9565  13329   7412    371  -1092   -359       C  
ATOM   1551  CG  GLN A 203      -6.137  87.662 278.751  1.00 75.00           C  
ANISOU 1551  CG  GLN A 203     9147  12446   6901    327   -896   -241       C  
ATOM   1552  CD  GLN A 203      -5.189  86.590 279.258  1.00 72.14           C  
ANISOU 1552  CD  GLN A 203     8751  11918   6742    139   -791   -465       C  
ATOM   1553  OE1 GLN A 203      -5.284  85.426 278.867  1.00 69.85           O  
ANISOU 1553  OE1 GLN A 203     8368  11749   6421     37   -834   -711       O  
ATOM   1554  NE2 GLN A 203      -4.272  86.978 280.138  1.00 72.75           N  
ANISOU 1554  NE2 GLN A 203     8908  11714   7020     99   -657   -387       N  
ATOM   1555  N   ALA A 204      -9.597  88.240 280.620  1.00 79.71           N  
ANISOU 1555  N   ALA A 204     9382  13168   7737    635  -1234   -126       N  
ATOM   1556  CA  ALA A 204     -10.002  89.227 281.612  1.00 79.23           C  
ANISOU 1556  CA  ALA A 204     9365  12924   7815    798  -1213     68       C  
ATOM   1557  C   ALA A 204     -10.403  88.537 282.909  1.00 74.58           C  
ANISOU 1557  C   ALA A 204     8625  12204   7507    694  -1210    -75       C  
ATOM   1558  O   ALA A 204     -10.070  89.003 283.996  1.00 69.87           O  
ANISOU 1558  O   ALA A 204     8115  11324   7109    713  -1116      8       O  
ATOM   1559  CB  ALA A 204     -11.146  90.077 281.084  1.00 83.98           C  
ANISOU 1559  CB  ALA A 204     9921  13777   8209   1067  -1347    243       C  
ATOM   1560  N   ALA A 205     -11.115  87.421 282.785  1.00 74.58           N  
ANISOU 1560  N   ALA A 205     8409  12415   7513    569  -1309   -293       N  
ATOM   1561  CA  ALA A 205     -11.558  86.656 283.945  1.00 71.65           C  
ANISOU 1561  CA  ALA A 205     7896  11939   7389    444  -1298   -432       C  
ATOM   1562  C   ALA A 205     -10.373  86.102 284.726  1.00 72.16           C  
ANISOU 1562  C   ALA A 205     8085  11662   7670    277  -1152   -514       C  
ATOM   1563  O   ALA A 205     -10.442  85.946 285.943  1.00 74.87           O  
ANISOU 1563  O   ALA A 205     8408  11809   8231    240  -1097   -524       O  
ATOM   1564  CB  ALA A 205     -12.480  85.528 283.517  1.00 73.45           C  
ANISOU 1564  CB  ALA A 205     7891  12456   7560    298  -1420   -662       C  
ATOM   1565  N   LEU A 206      -9.287  85.804 284.021  1.00 71.68           N  
ANISOU 1565  N   LEU A 206     8146  11554   7535    191  -1087   -572       N  
ATOM   1566  CA  LEU A 206      -8.078  85.302 284.664  1.00 67.14           C  
ANISOU 1566  CA  LEU A 206     7674  10695   7141     65   -954   -645       C  
ATOM   1567  C   LEU A 206      -7.327  86.419 285.376  1.00 61.58           C  
ANISOU 1567  C   LEU A 206     7123   9746   6529    154   -850   -445       C  
ATOM   1568  O   LEU A 206      -7.005  86.299 286.554  1.00 56.04           O  
ANISOU 1568  O   LEU A 206     6438   8817   6036    114   -787   -454       O  
ATOM   1569  CB  LEU A 206      -7.163  84.625 283.641  1.00 71.54           C  
ANISOU 1569  CB  LEU A 206     8291  11315   7578    -38   -911   -783       C  
ATOM   1570  CG  LEU A 206      -7.549  83.203 283.233  1.00 70.75           C  
ANISOU 1570  CG  LEU A 206     8086  11334   7462   -191   -968  -1053       C  
ATOM   1571  CD1 LEU A 206      -6.631  82.686 282.135  1.00 65.33           C  
ANISOU 1571  CD1 LEU A 206     7479  10720   6621   -252   -917  -1180       C  
ATOM   1572  CD2 LEU A 206      -7.521  82.280 284.444  1.00 69.36           C  
ANISOU 1572  CD2 LEU A 206     7880  10921   7552   -308   -919  -1175       C  
ATOM   1573  N   ALA A 207      -7.060  87.506 284.659  1.00 62.83           N  
ANISOU 1573  N   ALA A 207     7403   9949   6519    268   -833   -265       N  
ATOM   1574  CA  ALA A 207      -6.296  88.623 285.206  1.00 58.33           C  
ANISOU 1574  CA  ALA A 207     7006   9139   6017    320   -724    -82       C  
ATOM   1575  C   ALA A 207      -7.007  89.293 286.381  1.00 60.52           C  
ANISOU 1575  C   ALA A 207     7286   9272   6439    433   -739     24       C  
ATOM   1576  O   ALA A 207      -6.369  89.668 287.366  1.00 60.65           O  
ANISOU 1576  O   ALA A 207     7393   9038   6615    399   -650     63       O  
ATOM   1577  CB  ALA A 207      -6.009  89.644 284.118  1.00 54.39           C  
ANISOU 1577  CB  ALA A 207     6660   8718   5289    412   -697    101       C  
ATOM   1578  N   VAL A 208      -8.324  89.442 286.273  1.00 62.99           N  
ANISOU 1578  N   VAL A 208     7485   9764   6682    572   -852     59       N  
ATOM   1579  CA  VAL A 208      -9.101  90.111 287.313  1.00 63.43           C  
ANISOU 1579  CA  VAL A 208     7531   9720   6850    714   -861    158       C  
ATOM   1580  C   VAL A 208      -9.216  89.263 288.578  1.00 64.58           C  
ANISOU 1580  C   VAL A 208     7563   9748   7224    594   -837     14       C  
ATOM   1581  O   VAL A 208      -8.878  89.726 289.668  1.00 68.16           O  
ANISOU 1581  O   VAL A 208     8110   9963   7824    609   -760     67       O  
ATOM   1582  CB  VAL A 208     -10.515  90.473 286.820  1.00 62.52           C  
ANISOU 1582  CB  VAL A 208     7288   9881   6586    920   -991    232       C  
ATOM   1583  CG1 VAL A 208     -11.414  90.837 287.993  1.00 60.84           C  
ANISOU 1583  CG1 VAL A 208     6998   9608   6511   1049   -997    273       C  
ATOM   1584  CG2 VAL A 208     -10.450  91.617 285.818  1.00 61.91           C  
ANISOU 1584  CG2 VAL A 208     7382   9856   6286   1109  -1001    443       C  
ATOM   1585  N   SER A 209      -9.687  88.027 288.432  1.00 61.78           N  
ANISOU 1585  N   SER A 209     7026   9555   6891    467   -898   -169       N  
ATOM   1586  CA  SER A 209      -9.847  87.130 289.575  1.00 61.08           C  
ANISOU 1586  CA  SER A 209     6847   9355   7004    342   -867   -297       C  
ATOM   1587  C   SER A 209      -8.514  86.892 290.281  1.00 66.99           C  
ANISOU 1587  C   SER A 209     7735   9820   7896    233   -755   -329       C  
ATOM   1588  O   SER A 209      -8.463  86.755 291.503  1.00 72.67           O  
ANISOU 1588  O   SER A 209     8464  10370   8777    210   -705   -338       O  
ATOM   1589  CB  SER A 209     -10.456  85.796 289.135  1.00 56.41           C  
ANISOU 1589  CB  SER A 209     6078   8959   6397    186   -936   -498       C  
ATOM   1590  OG  SER A 209      -9.560  85.075 288.307  1.00 56.11           O  
ANISOU 1590  OG  SER A 209     6102   8918   6300     58   -918   -617       O  
ATOM   1591  N   LYS A 210      -7.439  86.846 289.502  1.00 66.69           N  
ANISOU 1591  N   LYS A 210     7795   9760   7784    174   -716   -346       N  
ATOM   1592  CA  LYS A 210      -6.094  86.732 290.050  1.00 66.10           C  
ANISOU 1592  CA  LYS A 210     7827   9467   7820     91   -616   -368       C  
ATOM   1593  C   LYS A 210      -5.741  87.963 290.876  1.00 64.98           C  
ANISOU 1593  C   LYS A 210     7815   9136   7739    170   -557   -212       C  
ATOM   1594  O   LYS A 210      -5.194  87.853 291.973  1.00 64.76           O  
ANISOU 1594  O   LYS A 210     7821   8929   7857    124   -504   -236       O  
ATOM   1595  CB  LYS A 210      -5.074  86.543 288.926  1.00 72.07           C  
ANISOU 1595  CB  LYS A 210     8637  10289   8458     26   -578   -411       C  
ATOM   1596  CG  LYS A 210      -3.630  86.570 289.372  1.00 75.01           C  
ANISOU 1596  CG  LYS A 210     9090  10490   8919    -46   -474   -423       C  
ATOM   1597  CD  LYS A 210      -2.688  86.348 288.197  1.00 74.34           C  
ANISOU 1597  CD  LYS A 210     9030  10514   8703   -103   -425   -473       C  
ATOM   1598  CE  LYS A 210      -2.827  87.447 287.157  1.00 68.98           C  
ANISOU 1598  CE  LYS A 210     8436   9948   7825    -41   -423   -317       C  
ATOM   1599  NZ  LYS A 210      -1.814  87.308 286.076  1.00 66.96           N  
ANISOU 1599  NZ  LYS A 210     8212   9798   7432   -107   -349   -353       N  
ATOM   1600  N   PHE A 211      -6.064  89.134 290.337  1.00 64.84           N  
ANISOU 1600  N   PHE A 211     7883   9155   7597    294   -567    -54       N  
ATOM   1601  CA  PHE A 211      -5.778  90.399 291.004  1.00 64.12           C  
ANISOU 1601  CA  PHE A 211     7955   8861   7547    369   -504     93       C  
ATOM   1602  C   PHE A 211      -6.541  90.523 292.317  1.00 70.57           C  
ANISOU 1602  C   PHE A 211     8738   9580   8497    445   -514     96       C  
ATOM   1603  O   PHE A 211      -6.037  91.089 293.287  1.00 73.30           O  
ANISOU 1603  O   PHE A 211     9194   9716   8939    435   -451    129       O  
ATOM   1604  CB  PHE A 211      -6.120  91.573 290.083  1.00 62.78           C  
ANISOU 1604  CB  PHE A 211     7911   8741   7203    513   -513    273       C  
ATOM   1605  CG  PHE A 211      -6.079  92.911 290.764  1.00 61.91           C  
ANISOU 1605  CG  PHE A 211     7994   8399   7129    614   -450    423       C  
ATOM   1606  CD1 PHE A 211      -4.872  93.481 291.129  1.00 62.81           C  
ANISOU 1606  CD1 PHE A 211     8272   8292   7302    488   -344    450       C  
ATOM   1607  CD2 PHE A 211      -7.249  93.604 291.027  1.00 65.32           C  
ANISOU 1607  CD2 PHE A 211     8443   8841   7533    834   -495    527       C  
ATOM   1608  CE1 PHE A 211      -4.832  94.715 291.752  1.00 64.62           C  
ANISOU 1608  CE1 PHE A 211     8705   8284   7563    557   -282    569       C  
ATOM   1609  CE2 PHE A 211      -7.215  94.837 291.649  1.00 69.17           C  
ANISOU 1609  CE2 PHE A 211     9142   9088   8053    941   -427    654       C  
ATOM   1610  CZ  PHE A 211      -6.005  95.393 292.012  1.00 68.09           C  
ANISOU 1610  CZ  PHE A 211     9195   8702   7976    791   -320    670       C  
ATOM   1611  N   LEU A 212      -7.756  89.988 292.345  1.00 71.08           N  
ANISOU 1611  N   LEU A 212     8639   9813   8555    510   -591     51       N  
ATOM   1612  CA  LEU A 212      -8.585  90.055 293.540  1.00 68.15           C  
ANISOU 1612  CA  LEU A 212     8209   9392   8293    585   -589     52       C  
ATOM   1613  C   LEU A 212      -8.149  89.032 294.582  1.00 69.05           C  
ANISOU 1613  C   LEU A 212     8275   9397   8565    433   -550    -77       C  
ATOM   1614  O   LEU A 212      -7.732  89.395 295.682  1.00 71.88           O  
ANISOU 1614  O   LEU A 212     8727   9567   9019    436   -491    -57       O  
ATOM   1615  CB  LEU A 212     -10.057  89.844 293.183  1.00 63.83           C  
ANISOU 1615  CB  LEU A 212     7473   9104   7676    694   -677     49       C  
ATOM   1616  CG  LEU A 212     -10.653  90.826 292.172  1.00 62.64           C  
ANISOU 1616  CG  LEU A 212     7352   9101   7348    897   -737    190       C  
ATOM   1617  CD1 LEU A 212     -12.137  90.560 291.970  1.00 64.37           C  
ANISOU 1617  CD1 LEU A 212     7333   9620   7506   1010   -835    168       C  
ATOM   1618  CD2 LEU A 212     -10.415  92.263 292.605  1.00 62.12           C  
ANISOU 1618  CD2 LEU A 212     7513   8811   7279   1067   -669    357       C  
ATOM   1619  N   LEU A 213      -8.235  87.755 294.222  1.00 65.11           N  
ANISOU 1619  N   LEU A 213     7648   9011   8080    304   -582   -210       N  
ATOM   1620  CA  LEU A 213      -7.997  86.663 295.161  1.00 61.13           C  
ANISOU 1620  CA  LEU A 213     7105   8406   7713    180   -546   -322       C  
ATOM   1621  C   LEU A 213      -6.577  86.623 295.723  1.00 61.18           C  
ANISOU 1621  C   LEU A 213     7240   8211   7795    117   -482   -337       C  
ATOM   1622  O   LEU A 213      -6.355  86.105 296.819  1.00 61.96           O  
ANISOU 1622  O   LEU A 213     7350   8190   8001     77   -447   -376       O  
ATOM   1623  CB  LEU A 213      -8.307  85.322 294.492  1.00 60.46           C  
ANISOU 1623  CB  LEU A 213     6900   8454   7617     49   -585   -467       C  
ATOM   1624  CG  LEU A 213      -9.741  85.093 294.012  1.00 68.16           C  
ANISOU 1624  CG  LEU A 213     7700   9670   8527     58   -659   -498       C  
ATOM   1625  CD1 LEU A 213      -9.875  83.720 293.369  1.00 72.33           C  
ANISOU 1625  CD1 LEU A 213     8143  10290   9048   -119   -688   -671       C  
ATOM   1626  CD2 LEU A 213     -10.726  85.251 295.159  1.00 70.35           C  
ANISOU 1626  CD2 LEU A 213     7895   9948   8887    107   -636   -457       C  
ATOM   1627  N   ALA A 214      -5.618  87.167 294.982  1.00 62.30           N  
ANISOU 1627  N   ALA A 214     7469   8336   7868    109   -466   -302       N  
ATOM   1628  CA  ALA A 214      -4.214  87.017 295.354  1.00 61.57           C  
ANISOU 1628  CA  ALA A 214     7447   8115   7833     32   -412   -340       C  
ATOM   1629  C   ALA A 214      -3.495  88.343 295.594  1.00 62.31           C  
ANISOU 1629  C   ALA A 214     7672   8094   7909     53   -367   -236       C  
ATOM   1630  O   ALA A 214      -2.270  88.369 295.716  1.00 64.51           O  
ANISOU 1630  O   ALA A 214     7987   8311   8211    -27   -326   -265       O  
ATOM   1631  CB  ALA A 214      -3.481  86.218 294.285  1.00 63.32           C  
ANISOU 1631  CB  ALA A 214     7632   8427   8000    -48   -409   -434       C  
ATOM   1632  N   PHE A 215      -4.244  89.439 295.668  1.00 61.41           N  
ANISOU 1632  N   PHE A 215     7631   7951   7753    159   -372   -122       N  
ATOM   1633  CA  PHE A 215      -3.621  90.740 295.884  1.00 60.43           C  
ANISOU 1633  CA  PHE A 215     7672   7679   7612    164   -318    -27       C  
ATOM   1634  C   PHE A 215      -4.552  91.745 296.558  1.00 64.86           C  
ANISOU 1634  C   PHE A 215     8325   8141   8176    309   -313     67       C  
ATOM   1635  O   PHE A 215      -4.316  92.143 297.698  1.00 71.25           O  
ANISOU 1635  O   PHE A 215     9212   8801   9060    304   -281     55       O  
ATOM   1636  CB  PHE A 215      -3.117  91.309 294.556  1.00 57.35           C  
ANISOU 1636  CB  PHE A 215     7353   7342   7096    134   -292     44       C  
ATOM   1637  CG  PHE A 215      -2.216  92.499 294.709  1.00 53.90           C  
ANISOU 1637  CG  PHE A 215     7093   6737   6650     69   -214    122       C  
ATOM   1638  CD1 PHE A 215      -0.881  92.335 295.038  1.00 49.50           C  
ANISOU 1638  CD1 PHE A 215     6526   6134   6147    -96   -165     47       C  
ATOM   1639  CD2 PHE A 215      -2.701  93.783 294.516  1.00 53.86           C  
ANISOU 1639  CD2 PHE A 215     7266   6620   6577    170   -187    266       C  
ATOM   1640  CE1 PHE A 215      -0.048  93.428 295.177  1.00 48.68           C  
ANISOU 1640  CE1 PHE A 215     6573   5888   6036   -200    -89    102       C  
ATOM   1641  CE2 PHE A 215      -1.872  94.879 294.653  1.00 50.76           C  
ANISOU 1641  CE2 PHE A 215     7066   6041   6179     78   -101    330       C  
ATOM   1642  CZ  PHE A 215      -0.545  94.702 294.984  1.00 49.57           C  
ANISOU 1642  CZ  PHE A 215     6890   5858   6088   -129    -52    242       C  
ATOM   1643  N   LEU A 216      -5.605  92.153 295.857  1.00 63.78           N  
ANISOU 1643  N   LEU A 216     8179   8105   7950    454   -349    153       N  
ATOM   1644  CA  LEU A 216      -6.492  93.199 296.361  1.00 64.62           C  
ANISOU 1644  CA  LEU A 216     8382   8128   8043    638   -338    253       C  
ATOM   1645  C   LEU A 216      -7.232  92.771 297.625  1.00 67.29           C  
ANISOU 1645  C   LEU A 216     8625   8464   8478    691   -342    189       C  
ATOM   1646  O   LEU A 216      -7.247  93.500 298.616  1.00 66.36           O  
ANISOU 1646  O   LEU A 216     8629   8180   8403    752   -294    209       O  
ATOM   1647  CB  LEU A 216      -7.500  93.616 295.289  1.00 64.57           C  
ANISOU 1647  CB  LEU A 216     8350   8279   7903    817   -390    360       C  
ATOM   1648  CG  LEU A 216      -8.293  94.882 295.624  1.00 66.06           C  
ANISOU 1648  CG  LEU A 216     8680   8363   8056   1054   -368    489       C  
ATOM   1649  CD1 LEU A 216      -7.351  96.057 295.839  1.00 63.16           C  
ANISOU 1649  CD1 LEU A 216     8604   7701   7692   1015   -276    565       C  
ATOM   1650  CD2 LEU A 216      -9.303  95.197 294.534  1.00 71.63           C  
ANISOU 1650  CD2 LEU A 216     9331   9270   8613   1262   -438    600       C  
ATOM   1651  N   VAL A 217      -7.847  91.592 297.588  1.00 68.35           N  
ANISOU 1651  N   VAL A 217     8554   8778   8640    655   -390    107       N  
ATOM   1652  CA  VAL A 217      -8.549  91.062 298.756  1.00 67.67           C  
ANISOU 1652  CA  VAL A 217     8368   8705   8638    674   -377     50       C  
ATOM   1653  C   VAL A 217      -7.605  90.806 299.944  1.00 63.37           C  
ANISOU 1653  C   VAL A 217     7907   7982   8188    562   -327    -13       C  
ATOM   1654  O   VAL A 217      -7.943  91.167 301.072  1.00 61.50           O  
ANISOU 1654  O   VAL A 217     7717   7662   7988    631   -288     -8       O  
ATOM   1655  CB  VAL A 217      -9.325  89.764 298.412  1.00 55.55           C  
ANISOU 1655  CB  VAL A 217     6608   7385   7113    605   -426    -32       C  
ATOM   1656  CG1 VAL A 217      -9.767  89.041 299.676  1.00 52.04           C  
ANISOU 1656  CG1 VAL A 217     6087   6921   6766    560   -387    -94       C  
ATOM   1657  CG2 VAL A 217     -10.516  90.081 297.519  1.00 56.04           C  
ANISOU 1657  CG2 VAL A 217     6547   7672   7074    744   -488     22       C  
ATOM   1658  N   PRO A 218      -6.426  90.187 299.708  1.00 65.31           N  
ANISOU 1658  N   PRO A 218     8165   8190   8461    406   -330    -76       N  
ATOM   1659  CA  PRO A 218      -5.485  90.091 300.831  1.00 64.89           C  
ANISOU 1659  CA  PRO A 218     8187   7993   8475    329   -297   -126       C  
ATOM   1660  C   PRO A 218      -5.106  91.446 301.424  1.00 64.89           C  
ANISOU 1660  C   PRO A 218     8368   7828   8461    373   -257    -78       C  
ATOM   1661  O   PRO A 218      -5.240  91.633 302.634  1.00 64.20           O  
ANISOU 1661  O   PRO A 218     8330   7657   8405    406   -233    -99       O  
ATOM   1662  CB  PRO A 218      -4.262  89.420 300.204  1.00 65.61           C  
ANISOU 1662  CB  PRO A 218     8251   8105   8573    193   -310   -187       C  
ATOM   1663  CG  PRO A 218      -4.822  88.591 299.118  1.00 66.83           C  
ANISOU 1663  CG  PRO A 218     8282   8414   8694    182   -345   -212       C  
ATOM   1664  CD  PRO A 218      -5.959  89.395 298.553  1.00 67.88           C  
ANISOU 1664  CD  PRO A 218     8411   8625   8754    306   -364   -124       C  
ATOM   1665  N   LEU A 219      -4.650  92.374 300.586  1.00 60.33           N  
ANISOU 1665  N   LEU A 219     7901   7195   7826    363   -243    -17       N  
ATOM   1666  CA  LEU A 219      -4.268  93.704 301.054  1.00 62.05           C  
ANISOU 1666  CA  LEU A 219     8325   7221   8030    376   -194     23       C  
ATOM   1667  C   LEU A 219      -5.435  94.424 301.725  1.00 65.64           C  
ANISOU 1667  C   LEU A 219     8855   7609   8475    569   -170     72       C  
ATOM   1668  O   LEU A 219      -5.237  95.249 302.616  1.00 69.21           O  
ANISOU 1668  O   LEU A 219     9469   7891   8937    586   -126     57       O  
ATOM   1669  CB  LEU A 219      -3.730  94.549 299.899  1.00 62.27           C  
ANISOU 1669  CB  LEU A 219     8475   7195   7989    331   -166    104       C  
ATOM   1670  CG  LEU A 219      -2.368  94.144 299.334  1.00 64.47           C  
ANISOU 1670  CG  LEU A 219     8709   7517   8268    127   -159     54       C  
ATOM   1671  CD1 LEU A 219      -1.909  95.143 298.284  1.00 68.99           C  
ANISOU 1671  CD1 LEU A 219     9434   8020   8760     76   -105    152       C  
ATOM   1672  CD2 LEU A 219      -1.337  94.016 300.442  1.00 64.48           C  
ANISOU 1672  CD2 LEU A 219     8713   7449   8338    -11   -150    -51       C  
ATOM   1673  N   ALA A 220      -6.652  94.109 301.291  1.00 67.78           N  
ANISOU 1673  N   ALA A 220     9001   8034   8720    716   -198    117       N  
ATOM   1674  CA  ALA A 220      -7.846  94.642 301.932  1.00 66.87           C  
ANISOU 1674  CA  ALA A 220     8901   7913   8593    924   -174    154       C  
ATOM   1675  C   ALA A 220      -7.974  94.077 303.341  1.00 65.10           C  
ANISOU 1675  C   ALA A 220     8624   7682   8431    895   -149     66       C  
ATOM   1676  O   ALA A 220      -8.160  94.822 304.302  1.00 66.56           O  
ANISOU 1676  O   ALA A 220     8939   7737   8613    986    -96     58       O  
ATOM   1677  CB  ALA A 220      -9.087  94.322 301.113  1.00 68.34           C  
ANISOU 1677  CB  ALA A 220     8910   8327   8730   1070   -220    209       C  
ATOM   1678  N   ILE A 221      -7.866  92.756 303.452  1.00 61.18           N  
ANISOU 1678  N   ILE A 221     7955   7312   7979    771   -179      2       N  
ATOM   1679  CA  ILE A 221      -7.921  92.078 304.743  1.00 57.52           C  
ANISOU 1679  CA  ILE A 221     7450   6845   7561    731   -152    -63       C  
ATOM   1680  C   ILE A 221      -6.805  92.561 305.662  1.00 64.33           C  
ANISOU 1680  C   ILE A 221     8482   7530   8429    656   -133   -112       C  
ATOM   1681  O   ILE A 221      -7.038  92.859 306.835  1.00 70.27           O  
ANISOU 1681  O   ILE A 221     9306   8221   9172    714    -92   -139       O  
ATOM   1682  CB  ILE A 221      -7.817  90.548 304.579  1.00 45.28           C  
ANISOU 1682  CB  ILE A 221     5732   5415   6056    597   -183   -114       C  
ATOM   1683  CG1 ILE A 221      -9.062  90.002 303.878  1.00 38.99           C  
ANISOU 1683  CG1 ILE A 221     4749   4813   5251    642   -200    -95       C  
ATOM   1684  CG2 ILE A 221      -7.633  89.873 305.928  1.00 43.08           C  
ANISOU 1684  CG2 ILE A 221     5462   5096   5810    548   -151   -161       C  
ATOM   1685  CD1 ILE A 221      -9.027  88.505 303.654  1.00 38.14           C  
ANISOU 1685  CD1 ILE A 221     4509   4794   5190    490   -220   -158       C  
ATOM   1686  N   ILE A 222      -5.596  92.643 305.116  1.00 62.59           N  
ANISOU 1686  N   ILE A 222     8316   7252   8214    520   -162   -132       N  
ATOM   1687  CA  ILE A 222      -4.430  93.089 305.872  1.00 57.16           C  
ANISOU 1687  CA  ILE A 222     7756   6437   7526    414   -158   -194       C  
ATOM   1688  C   ILE A 222      -4.636  94.488 306.445  1.00 62.37           C  
ANISOU 1688  C   ILE A 222     8623   6926   8150    494   -107   -187       C  
ATOM   1689  O   ILE A 222      -4.419  94.719 307.634  1.00 64.11           O  
ANISOU 1689  O   ILE A 222     8926   7075   8356    485    -91   -254       O  
ATOM   1690  CB  ILE A 222      -3.159  93.081 304.998  1.00 50.02           C  
ANISOU 1690  CB  ILE A 222     6849   5531   6627    254   -185   -210       C  
ATOM   1691  CG1 ILE A 222      -2.806  91.651 304.585  1.00 50.58           C  
ANISOU 1691  CG1 ILE A 222     6738   5749   6731    187   -228   -243       C  
ATOM   1692  CG2 ILE A 222      -1.995  93.715 305.738  1.00 49.33           C  
ANISOU 1692  CG2 ILE A 222     6877   5336   6531    128   -182   -282       C  
ATOM   1693  CD1 ILE A 222      -1.644  91.562 303.616  1.00 53.55           C  
ANISOU 1693  CD1 ILE A 222     7081   6164   7103     56   -243   -262       C  
ATOM   1694  N   ALA A 223      -5.068  95.413 305.594  1.00 64.29           N  
ANISOU 1694  N   ALA A 223     8964   7098   8365    582    -80   -108       N  
ATOM   1695  CA  ALA A 223      -5.274  96.796 306.006  1.00 66.26           C  
ANISOU 1695  CA  ALA A 223     9453   7143   8581    675    -19    -95       C  
ATOM   1696  C   ALA A 223      -6.470  96.934 306.945  1.00 66.89           C  
ANISOU 1696  C   ALA A 223     9536   7236   8645    885     21   -101       C  
ATOM   1697  O   ALA A 223      -6.485  97.802 307.817  1.00 65.89           O  
ANISOU 1697  O   ALA A 223     9598   6945   8491    941     73   -149       O  
ATOM   1698  CB  ALA A 223      -5.455  97.688 304.788  1.00 64.31           C  
ANISOU 1698  CB  ALA A 223     9327   6808   8298    744      4     17       C  
ATOM   1699  N   SER A 224      -7.470  96.077 306.764  1.00 66.36           N  
ANISOU 1699  N   SER A 224     9255   7372   8587    990      5    -63       N  
ATOM   1700  CA  SER A 224      -8.677  96.135 307.581  1.00 65.25           C  
ANISOU 1700  CA  SER A 224     9070   7295   8427   1186     57    -64       C  
ATOM   1701  C   SER A 224      -8.444  95.520 308.957  1.00 69.60           C  
ANISOU 1701  C   SER A 224     9598   7866   8981   1109     76   -155       C  
ATOM   1702  O   SER A 224      -8.932  96.033 309.964  1.00 75.29           O  
ANISOU 1702  O   SER A 224    10412   8534   9662   1232    141   -191       O  
ATOM   1703  CB  SER A 224      -9.839  95.429 306.881  1.00 64.50           C  
ANISOU 1703  CB  SER A 224     8728   7441   8336   1292     35      1       C  
ATOM   1704  OG  SER A 224     -11.063  95.672 307.553  1.00 68.28           O  
ANISOU 1704  OG  SER A 224     9151   8002   8788   1502     98      9       O  
ATOM   1705  N   SER A 225      -7.700  94.418 308.997  1.00 66.28           N  
ANISOU 1705  N   SER A 225     9066   7524   8595    925     23   -189       N  
ATOM   1706  CA  SER A 225      -7.362  93.775 310.263  1.00 63.15           C  
ANISOU 1706  CA  SER A 225     8663   7148   8183    857     31   -256       C  
ATOM   1707  C   SER A 225      -6.376  94.624 311.054  1.00 64.92           C  
ANISOU 1707  C   SER A 225     9096   7207   8365    792     28   -340       C  
ATOM   1708  O   SER A 225      -6.405  94.643 312.282  1.00 71.61           O  
ANISOU 1708  O   SER A 225    10008   8043   9157    818     56   -399       O  
ATOM   1709  CB  SER A 225      -6.780  92.380 310.028  1.00 60.72           C  
ANISOU 1709  CB  SER A 225     8203   6947   7919    706    -27   -261       C  
ATOM   1710  OG  SER A 225      -7.752  91.506 309.481  1.00 61.67           O  
ANISOU 1710  OG  SER A 225     8141   7216   8075    736    -16   -210       O  
ATOM   1711  N   HIS A 226      -5.503  95.324 310.337  1.00 66.36           N  
ANISOU 1711  N   HIS A 226     9381   7271   8560    693     -2   -350       N  
ATOM   1712  CA  HIS A 226      -4.524  96.206 310.959  1.00 66.92           C  
ANISOU 1712  CA  HIS A 226     9648   7185   8594    585     -5   -444       C  
ATOM   1713  C   HIS A 226      -5.205  97.349 311.705  1.00 64.99           C  
ANISOU 1713  C   HIS A 226     9612   6786   8294    735     74   -480       C  
ATOM   1714  O   HIS A 226      -4.715  97.810 312.736  1.00 67.42           O  
ANISOU 1714  O   HIS A 226    10063   7009   8546    679     80   -590       O  
ATOM   1715  CB  HIS A 226      -3.566  96.766 309.905  1.00 70.47           C  
ANISOU 1715  CB  HIS A 226    10161   7541   9072    431    -29   -433       C  
ATOM   1716  CG  HIS A 226      -2.547  97.713 310.455  1.00 75.08           C  
ANISOU 1716  CG  HIS A 226    10937   7966   9623    274    -27   -541       C  
ATOM   1717  ND1 HIS A 226      -1.385  97.289 311.060  1.00 77.50           N  
ANISOU 1717  ND1 HIS A 226    11180   8353   9913     90    -94   -644       N  
ATOM   1718  CD2 HIS A 226      -2.516  99.069 310.492  1.00 79.00           C  
ANISOU 1718  CD2 HIS A 226    11692   8227  10096    266     35   -570       C  
ATOM   1719  CE1 HIS A 226      -0.680  98.338 311.446  1.00 79.70           C  
ANISOU 1719  CE1 HIS A 226    11647   8478  10159    -50    -80   -744       C  
ATOM   1720  NE2 HIS A 226      -1.347  99.430 311.112  1.00 79.93           N  
ANISOU 1720  NE2 HIS A 226    11891   8292  10187     44      5   -702       N  
ATOM   1721  N   ALA A 227      -6.339  97.799 311.179  1.00 61.17           N  
ANISOU 1721  N   ALA A 227     9144   6281   7817    939    132   -394       N  
ATOM   1722  CA  ALA A 227      -7.085  98.893 311.787  1.00 59.55           C  
ANISOU 1722  CA  ALA A 227     9140   5927   7560   1134    220   -420       C  
ATOM   1723  C   ALA A 227      -7.915  98.404 312.969  1.00 64.72           C  
ANISOU 1723  C   ALA A 227     9711   6715   8166   1267    268   -460       C  
ATOM   1724  O   ALA A 227      -8.228  99.171 313.882  1.00 64.91           O  
ANISOU 1724  O   ALA A 227     9911   6628   8123   1383    339   -535       O  
ATOM   1725  CB  ALA A 227      -7.977  99.563 310.753  1.00 51.85           C  
ANISOU 1725  CB  ALA A 227     8202   4900   6598   1341    260   -303       C  
ATOM   1726  N   ALA A 228      -8.269  97.123 312.947  1.00 64.19           N  
ANISOU 1726  N   ALA A 228     9389   6877   8124   1241    240   -412       N  
ATOM   1727  CA  ALA A 228      -9.067  96.532 314.013  1.00 57.82           C  
ANISOU 1727  CA  ALA A 228     8486   6215   7267   1337    301   -428       C  
ATOM   1728  C   ALA A 228      -8.273  96.454 315.311  1.00 63.23           C  
ANISOU 1728  C   ALA A 228     9292   6860   7874   1232    291   -538       C  
ATOM   1729  O   ALA A 228      -8.742  96.891 316.363  1.00 65.83           O  
ANISOU 1729  O   ALA A 228     9727   7169   8115   1350    368   -600       O  
ATOM   1730  CB  ALA A 228      -9.555  95.149 313.608  1.00 49.13           C  
ANISOU 1730  CB  ALA A 228     7109   5339   6218   1290    280   -349       C  
ATOM   1731  N   VAL A 229      -7.067  95.901 315.231  1.00 66.70           N  
ANISOU 1731  N   VAL A 229     9707   7304   8331   1023    195   -566       N  
ATOM   1732  CA  VAL A 229      -6.238  95.717 316.415  1.00 69.19           C  
ANISOU 1732  CA  VAL A 229    10103   7629   8558    924    158   -664       C  
ATOM   1733  C   VAL A 229      -5.710  97.049 316.941  1.00 72.69           C  
ANISOU 1733  C   VAL A 229    10803   7883   8933    899    167   -795       C  
ATOM   1734  O   VAL A 229      -5.398  97.172 318.122  1.00 78.17           O  
ANISOU 1734  O   VAL A 229    11598   8587   9515    880    164   -899       O  
ATOM   1735  CB  VAL A 229      -5.048  94.768 316.138  1.00 69.59           C  
ANISOU 1735  CB  VAL A 229    10037   7762   8643    733     43   -659       C  
ATOM   1736  CG1 VAL A 229      -5.539  93.475 315.503  1.00 68.44           C  
ANISOU 1736  CG1 VAL A 229     9675   7757   8574    744     41   -543       C  
ATOM   1737  CG2 VAL A 229      -4.012  95.439 315.252  1.00 71.90           C  
ANISOU 1737  CG2 VAL A 229    10387   7941   8989    584    -20   -698       C  
ATOM   1738  N   SER A 230      -5.625  98.049 316.069  1.00 70.85           N  
ANISOU 1738  N   SER A 230    10691   7472   8756    895    182   -792       N  
ATOM   1739  CA  SER A 230      -5.110  99.356 316.461  1.00 70.87           C  
ANISOU 1739  CA  SER A 230    10971   7249   8708    840    203   -920       C  
ATOM   1740  C   SER A 230      -6.107 100.094 317.348  1.00 76.48           C  
ANISOU 1740  C   SER A 230    11853   7873   9333   1065    317   -978       C  
ATOM   1741  O   SER A 230      -5.726 100.733 318.330  1.00 83.09           O  
ANISOU 1741  O   SER A 230    12890   8609  10072   1022    330  -1129       O  
ATOM   1742  CB  SER A 230      -4.777 100.192 315.225  1.00 66.39           C  
ANISOU 1742  CB  SER A 230    10513   6489   8223    773    208   -876       C  
ATOM   1743  OG  SER A 230      -4.195 101.431 315.591  1.00 67.31           O  
ANISOU 1743  OG  SER A 230    10920   6357   8297    674    236  -1006       O  
ATOM   1744  N   LEU A 231      -7.385 100.003 316.993  1.00 74.77           N  
ANISOU 1744  N   LEU A 231    11547   7716   9145   1306    398   -870       N  
ATOM   1745  CA  LEU A 231      -8.448 100.605 317.789  1.00 77.00           C  
ANISOU 1745  CA  LEU A 231    11945   7965   9347   1560    520   -913       C  
ATOM   1746  C   LEU A 231      -8.673  99.810 319.071  1.00 76.02           C  
ANISOU 1746  C   LEU A 231    11726   8041   9115   1574    543   -963       C  
ATOM   1747  O   LEU A 231      -8.966 100.374 320.126  1.00 77.84           O  
ANISOU 1747  O   LEU A 231    12124   8223   9230   1683    621  -1075       O  
ATOM   1748  CB  LEU A 231      -9.744 100.685 316.980  1.00 80.39           C  
ANISOU 1748  CB  LEU A 231    12253   8456   9834   1820    591   -777       C  
ATOM   1749  CG  LEU A 231     -11.002 101.128 317.729  1.00 87.52           C  
ANISOU 1749  CG  LEU A 231    13193   9401  10659   2126    728   -803       C  
ATOM   1750  CD1 LEU A 231     -10.841 102.541 318.273  1.00 95.37           C  
ANISOU 1750  CD1 LEU A 231    14557  10096  11583   2227    801   -938       C  
ATOM   1751  CD2 LEU A 231     -12.228 101.026 316.833  1.00 86.27           C  
ANISOU 1751  CD2 LEU A 231    12834   9384  10561   2365    771   -659       C  
ATOM   1752  N   ARG A 232      -8.527  98.493 318.965  1.00 74.18           N  
ANISOU 1752  N   ARG A 232    11246   8024   8914   1465    481   -877       N  
ATOM   1753  CA  ARG A 232      -8.734  97.592 320.093  1.00 72.16           C  
ANISOU 1753  CA  ARG A 232    10901   7961   8557   1468    507   -885       C  
ATOM   1754  C   ARG A 232      -7.692  97.817 321.183  1.00 71.20           C  
ANISOU 1754  C   ARG A 232    10953   7795   8304   1339    447  -1031       C  
ATOM   1755  O   ARG A 232      -8.032  97.934 322.360  1.00 74.54           O  
ANISOU 1755  O   ARG A 232    11469   8271   8582   1429    516  -1105       O  
ATOM   1756  CB  ARG A 232      -8.701  96.138 319.617  1.00 71.35           C  
ANISOU 1756  CB  ARG A 232    10535   8046   8529   1364    452   -754       C  
ATOM   1757  CG  ARG A 232      -9.113  95.118 320.665  1.00 71.50           C  
ANISOU 1757  CG  ARG A 232    10463   8252   8452   1382    507   -718       C  
ATOM   1758  CD  ARG A 232     -10.498  95.412 321.208  1.00 74.07           C  
ANISOU 1758  CD  ARG A 232    10768   8660   8715   1594    669   -708       C  
ATOM   1759  NE  ARG A 232     -11.091  94.241 321.847  1.00 78.23           N  
ANISOU 1759  NE  ARG A 232    11145   9390   9189   1584    743   -622       N  
ATOM   1760  CZ  ARG A 232     -12.047  93.498 321.300  1.00 82.81           C  
ANISOU 1760  CZ  ARG A 232    11496  10114   9853   1601    809   -509       C  
ATOM   1761  NH1 ARG A 232     -12.529  92.447 321.951  1.00 86.68           N  
ANISOU 1761  NH1 ARG A 232    11881  10764  10289   1557    892   -434       N  
ATOM   1762  NH2 ARG A 232     -12.526  93.809 320.104  1.00 82.10           N  
ANISOU 1762  NH2 ARG A 232    11289  10014   9892   1653    793   -470       N  
ATOM   1763  N   LEU A 233      -6.424  97.881 320.786  1.00 66.18           N  
ANISOU 1763  N   LEU A 233    10350   7089   7708   1126    319  -1078       N  
ATOM   1764  CA  LEU A 233      -5.333  98.114 321.729  1.00 64.59           C  
ANISOU 1764  CA  LEU A 233    10281   6880   7381    978    236  -1231       C  
ATOM   1765  C   LEU A 233      -5.445  99.490 322.379  1.00 72.28           C  
ANISOU 1765  C   LEU A 233    11545   7661   8258   1032    304  -1402       C  
ATOM   1766  O   LEU A 233      -4.995  99.692 323.507  1.00 78.28           O  
ANISOU 1766  O   LEU A 233    12429   8453   8858    982    276  -1547       O  
ATOM   1767  CB  LEU A 233      -3.978  97.974 321.032  1.00 56.36           C  
ANISOU 1767  CB  LEU A 233     9177   5822   6414    736     93  -1250       C  
ATOM   1768  CG  LEU A 233      -3.562  96.562 320.613  1.00 52.72           C  
ANISOU 1768  CG  LEU A 233     8463   5555   6014    669      7  -1123       C  
ATOM   1769  CD1 LEU A 233      -2.163  96.570 320.016  1.00 50.18           C  
ANISOU 1769  CD1 LEU A 233     8086   5234   5746    446   -123  -1172       C  
ATOM   1770  CD2 LEU A 233      -3.641  95.604 321.789  1.00 62.06           C  
ANISOU 1770  CD2 LEU A 233     9593   6928   7060    728     -5  -1104       C  
ATOM   1771  N   GLN A 234      -6.048 100.432 321.662  1.00 70.65           N  
ANISOU 1771  N   GLN A 234    11457   7249   8136   1144    390  -1388       N  
ATOM   1772  CA  GLN A 234      -6.259 101.774 322.186  1.00 71.24           C  
ANISOU 1772  CA  GLN A 234    11844   7092   8134   1229    477  -1545       C  
ATOM   1773  C   GLN A 234      -7.324 101.762 323.276  1.00 72.27           C  
ANISOU 1773  C   GLN A 234    12014   7317   8126   1476    602  -1582       C  
ATOM   1774  O   GLN A 234      -7.172 102.407 324.312  1.00 76.99           O  
ANISOU 1774  O   GLN A 234    12835   7842   8575   1486    636  -1760       O  
ATOM   1775  CB  GLN A 234      -6.654 102.734 321.061  1.00 75.02           C  
ANISOU 1775  CB  GLN A 234    12452   7314   8739   1321    543  -1488       C  
ATOM   1776  CG  GLN A 234      -6.893 104.164 321.511  1.00 83.84           C  
ANISOU 1776  CG  GLN A 234    13934   8133   9789   1430    647  -1642       C  
ATOM   1777  CD  GLN A 234      -7.147 105.104 320.350  1.00 91.02           C  
ANISOU 1777  CD  GLN A 234    15004   8760  10818   1515    704  -1564       C  
ATOM   1778  OE1 GLN A 234      -8.208 105.722 320.256  1.00 95.03           O  
ANISOU 1778  OE1 GLN A 234    15626   9157  11325   1821    827  -1527       O  
ATOM   1779  NE2 GLN A 234      -6.169 105.221 319.458  1.00 92.89           N  
ANISOU 1779  NE2 GLN A 234    15252   8893  11151   1257    620  -1532       N  
ATOM   1780  N   HIS A 235      -8.399 101.018 323.036  1.00 72.47           N  
ANISOU 1780  N   HIS A 235    11818   7523   8196   1660    676  -1421       N  
ATOM   1781  CA  HIS A 235      -9.483 100.902 324.003  1.00 73.77           C  
ANISOU 1781  CA  HIS A 235    11970   7824   8234   1890    815  -1434       C  
ATOM   1782  C   HIS A 235      -9.075 100.010 325.174  1.00 74.46           C  
ANISOU 1782  C   HIS A 235    12002   8128   8164   1787    777  -1468       C  
ATOM   1783  O   HIS A 235      -9.533 100.202 326.302  1.00 76.22           O  
ANISOU 1783  O   HIS A 235    12329   8417   8214   1912    874  -1558       O  
ATOM   1784  CB  HIS A 235     -10.745 100.352 323.332  1.00 74.61           C  
ANISOU 1784  CB  HIS A 235    11821   8088   8440   2084    906  -1253       C  
ATOM   1785  CG  HIS A 235     -11.925 100.266 324.244  1.00 82.31           C  
ANISOU 1785  CG  HIS A 235    12750   9228   9294   2319   1070  -1260       C  
ATOM   1786  ND1 HIS A 235     -12.433 101.355 324.919  1.00 87.62           N  
ANISOU 1786  ND1 HIS A 235    13653   9782   9857   2538   1195  -1398       N  
ATOM   1787  CD2 HIS A 235     -12.711  99.215 324.597  1.00 83.71           C  
ANISOU 1787  CD2 HIS A 235    12680   9686   9440   2366   1146  -1150       C  
ATOM   1788  CE1 HIS A 235     -13.470 100.985 325.645  1.00 88.00           C  
ANISOU 1788  CE1 HIS A 235    13577  10052   9805   2720   1340  -1372       C  
ATOM   1789  NE2 HIS A 235     -13.658  99.686 325.465  1.00 86.19           N  
ANISOU 1789  NE2 HIS A 235    13056  10070   9623   2604   1315  -1218       N  
ATOM   1790  N   ARG A 236      -8.211  99.038 324.900  1.00 68.82           N  
ANISOU 1790  N   ARG A 236    11130   7524   7494   1577    638  -1392       N  
ATOM   1791  CA  ARG A 236      -7.739  98.120 325.931  1.00 62.84           C  
ANISOU 1791  CA  ARG A 236    10323   6968   6584   1493    583  -1395       C  
ATOM   1792  C   ARG A 236      -6.787  98.817 326.894  1.00 70.04           C  
ANISOU 1792  C   ARG A 236    11469   7822   7323   1389    506  -1608       C  
ATOM   1793  O   ARG A 236      -6.857  98.613 328.106  1.00 79.66           O  
ANISOU 1793  O   ARG A 236    12757   9175   8335   1438    534  -1671       O  
ATOM   1794  CB  ARG A 236      -7.056  96.907 325.299  1.00 56.21           C  
ANISOU 1794  CB  ARG A 236     9265   6244   5848   1330    455  -1254       C  
ATOM   1795  CG  ARG A 236      -6.489  95.916 326.300  1.00 55.18           C  
ANISOU 1795  CG  ARG A 236     9099   6308   5560   1266    387  -1232       C  
ATOM   1796  CD  ARG A 236      -5.904  94.704 325.598  1.00 54.31           C  
ANISOU 1796  CD  ARG A 236     8786   6283   5566   1149    279  -1084       C  
ATOM   1797  NE  ARG A 236      -6.934  93.923 324.919  1.00 62.11           N  
ANISOU 1797  NE  ARG A 236     9595   7318   6686   1219    381   -910       N  
ATOM   1798  CZ  ARG A 236      -6.687  93.012 323.983  1.00 68.24           C  
ANISOU 1798  CZ  ARG A 236    10201   8117   7612   1133    320   -787       C  
ATOM   1799  NH1 ARG A 236      -5.439  92.767 323.603  1.00 71.68           N  
ANISOU 1799  NH1 ARG A 236    10612   8539   8086    998    164   -810       N  
ATOM   1800  NH2 ARG A 236      -7.689  92.350 323.419  1.00 66.68           N  
ANISOU 1800  NH2 ARG A 236     9850   7968   7520   1179    417   -655       N  
ATOM   1801  N   ALA A1238      -5.897  99.639 326.350  1.00 68.08           N  
ANISOU 1801  N   ALA A1238    11338   7381   7146   1230    412  -1722       N  
ATOM   1802  CA  ALA A1238      -4.955 100.391 327.171  1.00 71.10           C  
ANISOU 1802  CA  ALA A1238    11938   7701   7375   1086    331  -1952       C  
ATOM   1803  C   ALA A1238      -5.690 101.405 328.042  1.00 74.80           C  
ANISOU 1803  C   ALA A1238    12673   8048   7698   1257    474  -2115       C  
ATOM   1804  O   ALA A1238      -5.239 101.739 329.137  1.00 77.21           O  
ANISOU 1804  O   ALA A1238    13144   8396   7799   1201    439  -2301       O  
ATOM   1805  CB  ALA A1238      -3.925 101.085 326.302  1.00 61.00           C  
ANISOU 1805  CB  ALA A1238    10723   6231   6224    853    227  -2034       C  
ATOM   1806  N   ASP A1239      -6.826 101.889 327.548  1.00 76.41           N  
ANISOU 1806  N   ASP A1239    12916   8119   7998   1479    632  -2050       N  
ATOM   1807  CA  ASP A1239      -7.670 102.800 328.312  1.00 80.72           C  
ANISOU 1807  CA  ASP A1239    13698   8558   8416   1702    794  -2188       C  
ATOM   1808  C   ASP A1239      -8.289 102.087 329.509  1.00 79.75           C  
ANISOU 1808  C   ASP A1239    13503   8711   8088   1844    876  -2171       C  
ATOM   1809  O   ASP A1239      -8.442 102.672 330.580  1.00 82.12           O  
ANISOU 1809  O   ASP A1239    14020   8998   8186   1929    948  -2352       O  
ATOM   1810  CB  ASP A1239      -8.767 103.392 327.425  1.00 87.90           C  
ANISOU 1810  CB  ASP A1239    14620   9298   9479   1948    938  -2093       C  
ATOM   1811  CG  ASP A1239      -8.235 104.422 326.450  1.00 95.76           C  
ANISOU 1811  CG  ASP A1239    15806   9955  10621   1847    898  -2145       C  
ATOM   1812  OD1 ASP A1239      -7.299 105.161 326.820  1.00 99.68           O  
ANISOU 1812  OD1 ASP A1239    16551  10272  11050   1649    834  -2345       O  
ATOM   1813  OD2 ASP A1239      -8.751 104.495 325.315  1.00 98.20           O  
ANISOU 1813  OD2 ASP A1239    16022  10186  11103   1956    933  -1986       O  
ATOM   1814  N   LEU A1240      -8.643 100.821 329.317  1.00 74.27           N  
ANISOU 1814  N   LEU A1240    12520   8259   7442   1861    873  -1955       N  
ATOM   1815  CA  LEU A1240      -9.201 100.013 330.394  1.00 77.02           C  
ANISOU 1815  CA  LEU A1240    12790   8874   7600   1964    960  -1900       C  
ATOM   1816  C   LEU A1240      -8.121  99.643 331.403  1.00 81.78           C  
ANISOU 1816  C   LEU A1240    13474   9607   7991   1796    820  -1998       C  
ATOM   1817  O   LEU A1240      -8.391  99.527 332.599  1.00 85.98           O  
ANISOU 1817  O   LEU A1240    14097  10292   8281   1885    891  -2060       O  
ATOM   1818  CB  LEU A1240      -9.857  98.748 329.837  1.00 73.94           C  
ANISOU 1818  CB  LEU A1240    12086   8673   7333   1993   1003  -1639       C  
ATOM   1819  CG  LEU A1240     -11.076  98.954 328.938  1.00 76.31           C  
ANISOU 1819  CG  LEU A1240    12248   8937   7809   2177   1142  -1531       C  
ATOM   1820  CD1 LEU A1240     -11.576  97.622 328.399  1.00 78.70           C  
ANISOU 1820  CD1 LEU A1240    12238   9437   8227   2136   1159  -1298       C  
ATOM   1821  CD2 LEU A1240     -12.180  99.685 329.688  1.00 75.22           C  
ANISOU 1821  CD2 LEU A1240    12220   8823   7538   2448   1348  -1624       C  
ATOM   1822  N   GLY A1241      -6.899  99.459 330.913  1.00 80.97           N  
ANISOU 1822  N   GLY A1241    13328   9468   7967   1563    621  -2010       N  
ATOM   1823  CA  GLY A1241      -5.777  99.116 331.766  1.00 83.27           C  
ANISOU 1823  CA  GLY A1241    13662   9912   8065   1407    457  -2103       C  
ATOM   1824  C   GLY A1241      -5.396 100.240 332.709  1.00 90.03           C  
ANISOU 1824  C   GLY A1241    14806  10689   8710   1374    443  -2394       C  
ATOM   1825  O   GLY A1241      -4.880  99.998 333.800  1.00 94.35           O  
ANISOU 1825  O   GLY A1241    15418  11426   9006   1333    364  -2487       O  
ATOM   1826  N   LEU A1242      -5.653 101.475 332.289  1.00103.34           N  
ANISOU 1826  N   LEU A1242    19438   8636  11190   1728   3141  -1372       N  
ATOM   1827  CA  LEU A1242      -5.340 102.645 333.104  1.00112.55           C  
ANISOU 1827  CA  LEU A1242    21120   9543  12103   1496   3348  -1491       C  
ATOM   1828  C   LEU A1242      -6.342 102.818 334.241  1.00119.91           C  
ANISOU 1828  C   LEU A1242    22229  10436  12896   1751   3618  -1433       C  
ATOM   1829  O   LEU A1242      -6.118 103.602 335.163  1.00124.81           O  
ANISOU 1829  O   LEU A1242    23284  10859  13279   1541   3782  -1551       O  
ATOM   1830  CB  LEU A1242      -5.304 103.907 332.240  1.00117.73           C  
ANISOU 1830  CB  LEU A1242    22009   9949  12773   1558   3538  -1397       C  
ATOM   1831  CG  LEU A1242      -4.195 103.970 331.189  1.00118.68           C  
ANISOU 1831  CG  LEU A1242    22043  10065  12985   1246   3310  -1473       C  
ATOM   1832  CD1 LEU A1242      -4.309 105.236 330.352  1.00123.85           C  
ANISOU 1832  CD1 LEU A1242    22945  10473  13639   1364   3541  -1354       C  
ATOM   1833  CD2 LEU A1242      -2.827 103.877 331.848  1.00117.56           C  
ANISOU 1833  CD2 LEU A1242    22058   9944  12664    634   3091  -1743       C  
ATOM   1834  N   GLN A1243      -7.450 102.088 334.168  1.00122.44           N  
ANISOU 1834  N   GLN A1243    22205  10956  13360   2193   3669  -1243       N  
ATOM   1835  CA  GLN A1243      -8.456 102.125 335.221  1.00129.35           C  
ANISOU 1835  CA  GLN A1243    23181  11844  14122   2458   3917  -1165       C  
ATOM   1836  C   GLN A1243      -8.034 101.242 336.391  1.00134.78           C  
ANISOU 1836  C   GLN A1243    23875  12675  14660   2182   3758  -1363       C  
ATOM   1837  O   GLN A1243      -7.664 100.083 336.208  1.00134.35           O  
ANISOU 1837  O   GLN A1243    23490  12858  14698   2082   3479  -1418       O  
ATOM   1838  CB  GLN A1243      -9.819 101.688 334.683  1.00128.12           C  
ANISOU 1838  CB  GLN A1243    22609  11904  14167   3021   4029   -857       C  
ATOM   1839  CG  GLN A1243     -10.386 102.617 333.621  1.00129.28           C  
ANISOU 1839  CG  GLN A1243    22754  11949  14416   3333   4214   -623       C  
ATOM   1840  CD  GLN A1243     -11.760 102.192 333.143  1.00128.70           C  
ANISOU 1840  CD  GLN A1243    22231  12159  14509   3859   4308   -297       C  
ATOM   1841  OE1 GLN A1243     -12.293 101.171 333.577  1.00127.46           O  
ANISOU 1841  OE1 GLN A1243    21745  12276  14407   3986   4235   -245       O  
ATOM   1842  NE2 GLN A1243     -12.343 102.976 332.243  1.00130.53           N  
ANISOU 1842  NE2 GLN A1243    22437  12353  14805   4155   4469    -64       N  
ATOM   1843  N   HIS A1244      -8.095 101.805 337.592  1.00141.75           N  
ANISOU 1843  N   HIS A1244    25154  13409  15295   2061   3946  -1463       N  
ATOM   1844  CA  HIS A1244      -7.638 101.127 338.800  1.00144.32           C  
ANISOU 1844  CA  HIS A1244    25551  13864  15420   1754   3809  -1657       C  
ATOM   1845  C   HIS A1244      -8.501  99.923 339.174  1.00142.33           C  
ANISOU 1845  C   HIS A1244    24930  13905  15243   2065   3789  -1545       C  
ATOM   1846  O   HIS A1244      -8.004  98.942 339.728  1.00140.32           O  
ANISOU 1846  O   HIS A1244    24557  13859  14899   1832   3563  -1676       O  
ATOM   1847  CB  HIS A1244      -7.599 102.120 339.963  1.00152.48           C  
ANISOU 1847  CB  HIS A1244    27114  14652  16168   1576   4048  -1766       C  
ATOM   1848  CG  HIS A1244      -8.713 103.120 339.935  1.00157.59           C  
ANISOU 1848  CG  HIS A1244    27978  15069  16830   2005   4454  -1566       C  
ATOM   1849  ND1 HIS A1244      -9.971 102.850 340.428  1.00159.32           N  
ANISOU 1849  ND1 HIS A1244    28076  15383  17074   2448   4675  -1386       N  
ATOM   1850  CD2 HIS A1244      -8.761 104.389 339.461  1.00160.82           C  
ANISOU 1850  CD2 HIS A1244    28714  15171  17219   2065   4686  -1499       C  
ATOM   1851  CE1 HIS A1244     -10.744 103.909 340.266  1.00163.09           C  
ANISOU 1851  CE1 HIS A1244    28790  15629  17547   2769   5019  -1211       C  
ATOM   1852  NE2 HIS A1244     -10.032 104.856 339.681  1.00164.02           N  
ANISOU 1852  NE2 HIS A1244    29197  15489  17632   2549   5038  -1277       N  
ATOM   1853  N   ARG A1245      -9.791 100.001 338.864  1.00144.88           N  
ANISOU 1853  N   ARG A1245    25060  14273  15715   2584   4025  -1285       N  
ATOM   1854  CA  ARG A1245     -10.739  98.962 339.256  1.00145.72           C  
ANISOU 1854  CA  ARG A1245    24809  14673  15884   2897   4057  -1143       C  
ATOM   1855  C   ARG A1245     -10.535  97.658 338.489  1.00141.70           C  
ANISOU 1855  C   ARG A1245    23716  14514  15611   2856   3698  -1061       C  
ATOM   1856  O   ARG A1245     -10.901  96.585 338.969  1.00139.15           O  
ANISOU 1856  O   ARG A1245    23009  14526  15336   2854   3544   -962       O  
ATOM   1857  CB  ARG A1245     -12.173  99.458 339.060  1.00149.35           C  
ANISOU 1857  CB  ARG A1245    25151  15149  16447   3429   4378   -840       C  
ATOM   1858  CG  ARG A1245     -12.520 100.689 339.880  1.00156.36           C  
ANISOU 1858  CG  ARG A1245    26539  15740  17131   3479   4711   -845       C  
ATOM   1859  CD  ARG A1245     -13.926 101.177 339.575  1.00159.80           C  
ANISOU 1859  CD  ARG A1245    26834  16216  17668   4024   5017   -513       C  
ATOM   1860  NE  ARG A1245     -14.104 101.463 338.154  1.00158.04           N  
ANISOU 1860  NE  ARG A1245    26365  16028  17657   4226   4975   -325       N  
ATOM   1861  CZ  ARG A1245     -13.817 102.629 337.584  1.00158.12           C  
ANISOU 1861  CZ  ARG A1245    26695  15744  17639   4205   5098   -312       C  
ATOM   1862  NH1 ARG A1245     -14.012 102.799 336.284  1.00155.20           N  
ANISOU 1862  NH1 ARG A1245    26066  15449  17453   4396   5047   -128       N  
ATOM   1863  NH2 ARG A1245     -13.334 103.625 338.314  1.00161.51           N  
ANISOU 1863  NH2 ARG A1245    27709  15814  17843   3980   5275   -478       N  
ATOM   1864  N   ASN A1246      -9.949  97.751 337.301  1.00141.58           N  
ANISOU 1864  N   ASN A1246    23549  14474  15772   2752   3503  -1048       N  
ATOM   1865  CA  ASN A1246      -9.745  96.578 336.458  1.00137.79           C  
ANISOU 1865  CA  ASN A1246    22438  14360  15557   2652   3107   -914       C  
ATOM   1866  C   ASN A1246      -8.354  95.974 336.621  1.00138.54           C  
ANISOU 1866  C   ASN A1246    22467  14559  15614   2124   2717  -1096       C  
ATOM   1867  O   ASN A1246      -7.721  95.580 335.642  1.00136.96           O  
ANISOU 1867  O   ASN A1246    21982  14464  15592   1970   2444  -1071       O  
ATOM   1868  CB  ASN A1246      -9.985  96.934 334.991  1.00134.69           C  
ANISOU 1868  CB  ASN A1246    21861  13929  15388   2877   3118   -760       C  
ATOM   1869  CG  ASN A1246     -11.348  97.555 334.758  1.00137.33           C  
ANISOU 1869  CG  ASN A1246    22218  14204  15756   3433   3501   -537       C  
ATOM   1870  OD1 ASN A1246     -12.302  97.280 335.487  1.00139.43           O  
ANISOU 1870  OD1 ASN A1246    22391  14613  15973   3683   3675   -420       O  
ATOM   1871  ND2 ASN A1246     -11.446  98.400 333.738  1.00138.20           N  
ANISOU 1871  ND2 ASN A1246    22444  14120  15947   3643   3642   -457       N  
ATOM   1872  N   ILE A1247      -7.886  95.897 337.862  1.00142.11           N  
ANISOU 1872  N   ILE A1247    23173  15002  15819   1858   2698  -1265       N  
ATOM   1873  CA  ILE A1247      -6.550  95.383 338.145  1.00141.19           C  
ANISOU 1873  CA  ILE A1247    23002  15020  15622   1367   2345  -1418       C  
ATOM   1874  C   ILE A1247      -6.509  93.856 338.150  1.00138.71           C  
ANISOU 1874  C   ILE A1247    22120  15111  15472   1314   2019  -1275       C  
ATOM   1875  O   ILE A1247      -5.589  93.252 337.599  1.00132.61           O  
ANISOU 1875  O   ILE A1247    21081  14494  14811   1069   1700  -1280       O  
ATOM   1876  CB  ILE A1247      -6.027  95.901 339.499  1.00142.90           C  
ANISOU 1876  CB  ILE A1247    23717  15106  15474   1071   2436  -1648       C  
ATOM   1877  N   PHE A1248      -7.511  93.236 338.767  1.00142.53           N  
ANISOU 1877  N   PHE A1248    22436  15755  15966   1549   2120  -1140       N  
ATOM   1878  CA  PHE A1248      -7.537  91.782 338.912  1.00139.58           C  
ANISOU 1878  CA  PHE A1248    21591  15729  15715   1492   1854  -1007       C  
ATOM   1879  C   PHE A1248      -8.623  91.104 338.077  1.00137.01           C  
ANISOU 1879  C   PHE A1248    20819  15576  15662   1808   1871   -764       C  
ATOM   1880  O   PHE A1248      -8.829  89.895 338.190  1.00133.40           O  
ANISOU 1880  O   PHE A1248    20001  15381  15306   1783   1702   -642       O  
ATOM   1881  CB  PHE A1248      -7.723  91.401 340.383  1.00139.50           C  
ANISOU 1881  CB  PHE A1248    21710  15820  15474   1425   1908  -1041       C  
ATOM   1882  CG  PHE A1248      -6.436  91.146 341.113  1.00138.80           C  
ANISOU 1882  CG  PHE A1248    21737  15816  15187   1006   1659  -1193       C  
ATOM   1883  CD1 PHE A1248      -6.448  90.692 342.421  1.00142.31           C  
ANISOU 1883  CD1 PHE A1248    22267  16396  15410    902   1652  -1215       C  
ATOM   1884  CD2 PHE A1248      -5.216  91.358 340.493  1.00136.47           C  
ANISOU 1884  CD2 PHE A1248    21445  15495  14913    717   1433  -1297       C  
ATOM   1885  CE1 PHE A1248      -5.268  90.452 343.096  1.00144.21           C  
ANISOU 1885  CE1 PHE A1248    22582  16765  15446    522   1411  -1326       C  
ATOM   1886  CE2 PHE A1248      -4.032  91.121 341.164  1.00137.59           C  
ANISOU 1886  CE2 PHE A1248    21645  15776  14858    334   1197  -1407       C  
ATOM   1887  CZ  PHE A1248      -4.058  90.668 342.467  1.00141.84           C  
ANISOU 1887  CZ  PHE A1248    22257  16468  15168    239   1180  -1416       C  
ATOM   1888  N   GLU A1249      -9.312  91.875 337.242  1.00138.33           N  
ANISOU 1888  N   GLU A1249    21020  15607  15932   2094   2078   -686       N  
ATOM   1889  CA  GLU A1249     -10.390  91.327 336.424  1.00136.23           C  
ANISOU 1889  CA  GLU A1249    20325  15544  15893   2381   2099   -445       C  
ATOM   1890  C   GLU A1249      -9.828  90.427 335.323  1.00121.31           C  
ANISOU 1890  C   GLU A1249    18042  13822  14227   2206   1765   -391       C  
ATOM   1891  O   GLU A1249      -8.679  90.585 334.911  1.00119.99           O  
ANISOU 1891  O   GLU A1249    17968  13554  14069   1957   1583   -523       O  
ATOM   1892  CB  GLU A1249     -11.232  92.456 335.825  1.00148.32           C  
ANISOU 1892  CB  GLU A1249    21998  16906  17450   2752   2414   -353       C  
ATOM   1893  CG  GLU A1249     -12.736  92.256 335.971  1.00157.12           C  
ANISOU 1893  CG  GLU A1249    22870  18221  18609   3135   2640   -115       C  
ATOM   1894  CD  GLU A1249     -13.349  91.520 334.796  1.00159.64           C  
ANISOU 1894  CD  GLU A1249    22652  18836  19170   3239   2486    110       C  
ATOM   1895  OE1 GLU A1249     -12.805  91.628 333.678  1.00159.61           O  
ANISOU 1895  OE1 GLU A1249    22564  18787  19296   3151   2321     96       O  
ATOM   1896  OE2 GLU A1249     -14.377  90.835 334.989  1.00161.48           O  
ANISOU 1896  OE2 GLU A1249    22551  19356  19448   3387   2531    299       O  
ATOM   1897  N   MET A1250     -10.639  89.482 334.856  1.00108.60           N  
ANISOU 1897  N   MET A1250    16004  12475  12783   2321   1695   -196       N  
ATOM   1898  CA  MET A1250     -10.171  88.485 333.897  1.00 97.97           C  
ANISOU 1898  CA  MET A1250    14309  11287  11629   2143   1397   -148       C  
ATOM   1899  C   MET A1250     -11.259  88.051 332.915  1.00 91.56           C  
ANISOU 1899  C   MET A1250    13110  10686  10991   2335   1412     67       C  
ATOM   1900  O   MET A1250     -12.447  88.082 333.237  1.00 90.46           O  
ANISOU 1900  O   MET A1250    12860  10682  10829   2569   1604    215       O  
ATOM   1901  CB  MET A1250      -9.624  87.264 334.643  1.00 97.02           C  
ANISOU 1901  CB  MET A1250    14074  11310  11481   1895   1190   -177       C  
ATOM   1902  CG  MET A1250     -10.628  86.613 335.585  1.00102.65           C  
ANISOU 1902  CG  MET A1250    14672  12197  12133   2000   1305    -59       C  
ATOM   1903  SD  MET A1250      -9.869  85.484 336.773  1.00117.94           S  
ANISOU 1903  SD  MET A1250    16623  14229  13959   1733   1123   -112       S  
ATOM   1904  CE  MET A1250      -8.876  86.621 337.739  1.00 60.52           C  
ANISOU 1904  CE  MET A1250     9834   6736   6424   1608   1182   -339       C  
ATOM   1905  N   LEU A1251     -10.829  87.651 331.720  1.00 85.46           N  
ANISOU 1905  N   LEU A1251    12130   9962  10378   2220   1209     85       N  
ATOM   1906  CA  LEU A1251     -11.716  87.161 330.663  1.00 82.16           C  
ANISOU 1906  CA  LEU A1251    11338   9771  10108   2323   1171    273       C  
ATOM   1907  C   LEU A1251     -12.801  88.164 330.276  1.00 90.79           C  
ANISOU 1907  C   LEU A1251    12416  10891  11189   2674   1421    422       C  
ATOM   1908  O   LEU A1251     -13.991  87.885 330.418  1.00 93.19           O  
ANISOU 1908  O   LEU A1251    12478  11437  11494   2848   1535    607       O  
ATOM   1909  CB  LEU A1251     -12.368  85.838 331.081  1.00 74.90           C  
ANISOU 1909  CB  LEU A1251    10127   9115   9217   2235   1100    385       C  
ATOM   1910  CG  LEU A1251     -11.443  84.631 331.243  1.00 69.44           C  
ANISOU 1910  CG  LEU A1251     9385   8432   8567   1926    856    299       C  
ATOM   1911  CD1 LEU A1251     -12.242  83.390 331.602  1.00 65.08           C  
ANISOU 1911  CD1 LEU A1251     8576   8114   8036   1856    833    429       C  
ATOM   1912  CD2 LEU A1251     -10.638  84.401 329.976  1.00 71.07           C  
ANISOU 1912  CD2 LEU A1251     9508   8591   8906   1779    657    251       C  
ATOM   1913  N   ARG A1252     -12.387  89.325 329.779  1.00 96.66           N  
ANISOU 1913  N   ARG A1252    13413  11399  11916   2783   1515    359       N  
ATOM   1914  CA  ARG A1252     -13.335  90.337 329.327  1.00104.00           C  
ANISOU 1914  CA  ARG A1252    14355  12326  12833   3156   1769    522       C  
ATOM   1915  C   ARG A1252     -13.891  89.989 327.951  1.00109.02           C  
ANISOU 1915  C   ARG A1252    14593  13221  13608   3216   1651    711       C  
ATOM   1916  O   ARG A1252     -13.235  89.312 327.160  1.00108.81           O  
ANISOU 1916  O   ARG A1252    14417  13241  13682   2956   1391    652       O  
ATOM   1917  CB  ARG A1252     -12.679  91.718 329.284  1.00107.75           C  
ANISOU 1917  CB  ARG A1252    15294  12420  13227   3243   1934    388       C  
ATOM   1918  CG  ARG A1252     -12.070  92.169 330.596  1.00113.03           C  
ANISOU 1918  CG  ARG A1252    16404  12824  13720   3135   2051    179       C  
ATOM   1919  CD  ARG A1252     -11.502  93.573 330.473  1.00116.99           C  
ANISOU 1919  CD  ARG A1252    17389  12937  14125   3195   2240     50       C  
ATOM   1920  NE  ARG A1252     -12.505  94.524 330.002  1.00118.70           N  
ANISOU 1920  NE  ARG A1252    17664  13095  14343   3634   2547    240       N  
ATOM   1921  CZ  ARG A1252     -13.331  95.194 330.799  1.00120.71           C  
ANISOU 1921  CZ  ARG A1252    18144  13254  14468   3956   2896    308       C  
ATOM   1922  NH1 ARG A1252     -13.276  95.019 332.112  1.00120.51           N  
ANISOU 1922  NH1 ARG A1252    18318  13176  14293   3858   2974    182       N  
ATOM   1923  NH2 ARG A1252     -14.212  96.039 330.283  1.00123.00           N  
ANISOU 1923  NH2 ARG A1252    18461  13506  14766   4392   3179    514       N  
ATOM   1924  N   ILE A1253     -15.105  90.453 327.673  1.00114.85           N  
ANISOU 1924  N   ILE A1253    15158  14145  14337   3564   1850    948       N  
ATOM   1925  CA  ILE A1253     -15.737  90.226 326.378  1.00114.59           C  
ANISOU 1925  CA  ILE A1253    14734  14406  14398   3636   1751   1157       C  
ATOM   1926  C   ILE A1253     -16.263  91.534 325.792  1.00114.05           C  
ANISOU 1926  C   ILE A1253    14763  14271  14301   4048   1997   1324       C  
ATOM   1927  O   ILE A1253     -16.293  91.716 324.575  1.00114.15           O  
ANISOU 1927  O   ILE A1253    14618  14378  14377   4086   1906   1428       O  
ATOM   1928  CB  ILE A1253     -16.905  89.219 326.479  1.00118.44           C  
ANISOU 1928  CB  ILE A1253    14755  15350  14898   3629   1708   1363       C  
ATOM   1929  CG1 ILE A1253     -16.516  88.012 327.334  1.00115.19           C  
ANISOU 1929  CG1 ILE A1253    14319  14961  14488   3287   1550   1219       C  
ATOM   1930  CG2 ILE A1253     -17.344  88.771 325.093  1.00121.23           C  
ANISOU 1930  CG2 ILE A1253    14704  16029  15330   3562   1527   1531       C  
ATOM   1931  CD1 ILE A1253     -17.655  87.047 327.571  1.00117.17           C  
ANISOU 1931  CD1 ILE A1253    14164  15625  14731   3249   1538   1407       C  
ATOM   1932  N   ASP A1254     -16.664  92.450 326.669  1.00109.30           N  
ANISOU 1932  N   ASP A1254    14447  13492  13591   4365   2324   1352       N  
ATOM   1933  CA  ASP A1254     -17.303  93.694 326.249  1.00107.39           C  
ANISOU 1933  CA  ASP A1254    14319  13178  13306   4830   2623   1549       C  
ATOM   1934  C   ASP A1254     -16.309  94.762 325.797  1.00104.10           C  
ANISOU 1934  C   ASP A1254    14371  12306  12877   4832   2690   1390       C  
ATOM   1935  O   ASP A1254     -16.629  95.951 325.794  1.00103.38           O  
ANISOU 1935  O   ASP A1254    14571  11994  12715   5210   3012   1485       O  
ATOM   1936  CB  ASP A1254     -18.168  94.248 327.384  1.00109.77           C  
ANISOU 1936  CB  ASP A1254    14772  13450  13484   5199   2994   1652       C  
ATOM   1937  CG  ASP A1254     -17.370  94.526 328.642  1.00109.53           C  
ANISOU 1937  CG  ASP A1254    15262  13011  13342   5040   3101   1355       C  
ATOM   1938  OD1 ASP A1254     -16.383  93.804 328.894  1.00106.42           O  
ANISOU 1938  OD1 ASP A1254    14924  12536  12974   4598   2826   1113       O  
ATOM   1939  OD2 ASP A1254     -17.730  95.469 329.379  1.00112.79           O  
ANISOU 1939  OD2 ASP A1254    16034  13192  13629   5362   3468   1372       O  
ATOM   1940  N   GLU A1255     -15.106  94.342 325.416  1.00102.58           N  
ANISOU 1940  N   GLU A1255    14260  11970  12747   4416   2406   1159       N  
ATOM   1941  CA  GLU A1255     -14.120  95.268 324.873  1.00102.93           C  
ANISOU 1941  CA  GLU A1255    14698  11627  12785   4357   2435   1013       C  
ATOM   1942  C   GLU A1255     -14.561  95.776 323.506  1.00107.56           C  
ANISOU 1942  C   GLU A1255    15113  12324  13433   4610   2463   1245       C  
ATOM   1943  O   GLU A1255     -14.273  96.913 323.132  1.00105.90           O  
ANISOU 1943  O   GLU A1255    15258  11795  13183   4786   2656   1244       O  
ATOM   1944  CB  GLU A1255     -12.745  94.607 324.764  1.00 95.38           C  
ANISOU 1944  CB  GLU A1255    13797  10561  11881   3855   2114    741       C  
ATOM   1945  CG  GLU A1255     -11.964  94.557 326.064  1.00 91.66           C  
ANISOU 1945  CG  GLU A1255    13665   9856  11307   3609   2126    480       C  
ATOM   1946  CD  GLU A1255     -10.514  94.168 325.852  1.00 87.92           C  
ANISOU 1946  CD  GLU A1255    13277   9258  10869   3166   1847    243       C  
ATOM   1947  OE1 GLU A1255     -10.146  93.844 324.704  1.00 81.45           O  
ANISOU 1947  OE1 GLU A1255    12245   8534  10168   3053   1648    276       O  
ATOM   1948  OE2 GLU A1255      -9.741  94.185 326.833  1.00 92.83           O  
ANISOU 1948  OE2 GLU A1255    14171   9710  11389   2933   1830     33       O  
ATOM   1949  N   GLY A1256     -15.265  94.926 322.767  1.00117.18           N  
ANISOU 1949  N   GLY A1256    15796  13998  14731   4609   2273   1448       N  
ATOM   1950  CA  GLY A1256     -15.745  95.278 321.444  1.00120.81           C  
ANISOU 1950  CA  GLY A1256    16024  14649  15229   4822   2261   1692       C  
ATOM   1951  C   GLY A1256     -17.014  96.107 321.481  1.00127.07           C  
ANISOU 1951  C   GLY A1256    16746  15595  15939   5317   2570   2004       C  
ATOM   1952  O   GLY A1256     -17.566  96.460 320.439  1.00130.79           O  
ANISOU 1952  O   GLY A1256    17002  16295  16397   5449   2553   2233       O  
ATOM   1953  N   GLY A1257     -17.477  96.420 322.687  1.00128.11           N  
ANISOU 1953  N   GLY A1257    17063  15638  15975   5454   2809   1991       N  
ATOM   1954  CA  GLY A1257     -18.677  97.217 322.858  1.00129.69           C  
ANISOU 1954  CA  GLY A1257    17229  15994  16054   5788   3079   2259       C  
ATOM   1955  C   GLY A1257     -19.936  96.438 322.537  1.00126.98           C  
ANISOU 1955  C   GLY A1257    16259  16266  15721   5896   2986   2565       C  
ATOM   1956  O   GLY A1257     -19.900  95.217 322.385  1.00122.66           O  
ANISOU 1956  O   GLY A1257    15326  16013  15269   5686   2728   2546       O  
ATOM   1957  N   GLY A1258     -21.054  97.148 322.434  1.00132.01           N  
ANISOU 1957  N   GLY A1258    16803  17109  16247   6207   3201   2857       N  
ATOM   1958  CA  GLY A1258     -22.329  96.525 322.137  1.00137.83           C  
ANISOU 1958  CA  GLY A1258    16953  18460  16957   6298   3131   3172       C  
ATOM   1959  C   GLY A1258     -22.998  95.959 323.374  1.00142.83           C  
ANISOU 1959  C   GLY A1258    17451  19265  17552   6337   3233   3203       C  
ATOM   1960  O   GLY A1258     -23.130  96.642 324.389  1.00144.53           O  
ANISOU 1960  O   GLY A1258    18030  19205  17678   6526   3519   3164       O  
ATOM   1961  N   SER A1259     -23.419  94.702 323.287  1.00145.60           N  
ANISOU 1961  N   SER A1259    17288  20074  17959   6137   3002   3272       N  
ATOM   1962  CA  SER A1259     -24.092  94.042 324.399  1.00149.47           C  
ANISOU 1962  CA  SER A1259    17592  20785  18415   6140   3078   3318       C  
ATOM   1963  C   SER A1259     -23.723  92.565 324.476  1.00150.26           C  
ANISOU 1963  C   SER A1259    17365  21101  18627   5772   2788   3183       C  
ATOM   1964  O   SER A1259     -23.081  92.027 323.575  1.00148.09           O  
ANISOU 1964  O   SER A1259    16955  20865  18449   5528   2517   3096       O  
ATOM   1965  CB  SER A1259     -25.609  94.197 324.272  1.00154.57           C  
ANISOU 1965  CB  SER A1259    17847  21940  18943   6367   3193   3706       C  
ATOM   1966  OG  SER A1259     -26.281  93.442 325.265  1.00157.08           O  
ANISOU 1966  OG  SER A1259    17928  22523  19232   6327   3236   3762       O  
ATOM   1967  N   GLY A1260     -24.134  91.916 325.561  1.00153.46           N  
ANISOU 1967  N   GLY A1260    17654  21643  19010   5736   2860   3175       N  
ATOM   1968  CA  GLY A1260     -23.874  90.501 325.750  1.00152.50           C  
ANISOU 1968  CA  GLY A1260    17239  21734  18972   5367   2616   3064       C  
ATOM   1969  C   GLY A1260     -25.107  89.656 325.496  1.00153.52           C  
ANISOU 1969  C   GLY A1260    16740  22529  19061   5263   2517   3350       C  
ATOM   1970  O   GLY A1260     -25.238  88.552 326.023  1.00150.38           O  
ANISOU 1970  O   GLY A1260    16159  22310  18669   4928   2390   3283       O  
ATOM   1971  N   GLY A1261     -26.016  90.181 324.680  1.00158.84           N  
ANISOU 1971  N   GLY A1261    17187  23515  19650   5406   2529   3629       N  
ATOM   1972  CA  GLY A1261     -27.255  89.494 324.371  1.00162.76           C  
ANISOU 1972  CA  GLY A1261    17121  24655  20065   5269   2426   3911       C  
ATOM   1973  C   GLY A1261     -27.087  88.409 323.325  1.00161.77           C  
ANISOU 1973  C   GLY A1261    16611  24865  19989   4821   2062   3894       C  
ATOM   1974  O   GLY A1261     -27.894  87.484 323.243  1.00163.87           O  
ANISOU 1974  O   GLY A1261    16437  25630  20196   4544   1929   4035       O  
ATOM   1975  N   ASP A1262     -26.033  88.521 322.523  1.00158.38           N  
ANISOU 1975  N   ASP A1262    16370  24153  19654   4722   1903   3715       N  
ATOM   1976  CA  ASP A1262     -25.774  87.551 321.466  1.00154.14           C  
ANISOU 1976  CA  ASP A1262    15527  23885  19154   4291   1559   3680       C  
ATOM   1977  C   ASP A1262     -24.388  86.930 321.603  1.00145.88           C  
ANISOU 1977  C   ASP A1262    14907  22312  18210   3873   1368   3261       C  
ATOM   1978  O   ASP A1262     -23.665  86.785 320.618  1.00143.60           O  
ANISOU 1978  O   ASP A1262    14706  21893  17962   3646   1156   3131       O  
ATOM   1979  CB  ASP A1262     -25.920  88.208 320.091  1.00154.96           C  
ANISOU 1979  CB  ASP A1262    15576  24105  19198   4362   1468   3820       C  
ATOM   1980  N   GLU A1263     -24.025  86.560 322.827  1.00139.92           N  
ANISOU 1980  N   GLU A1263    14411  21270  17482   3778   1449   3062       N  
ATOM   1981  CA  GLU A1263     -22.724  85.956 323.092  1.00130.96           C  
ANISOU 1981  CA  GLU A1263    13668  19661  16430   3410   1284   2692       C  
ATOM   1982  C   GLU A1263     -22.687  84.489 322.681  1.00127.36           C  
ANISOU 1982  C   GLU A1263    12999  19409  15982   2857   1003   2609       C  
ATOM   1983  O   GLU A1263     -21.626  83.949 322.367  1.00125.23           O  
ANISOU 1983  O   GLU A1263    12971  18832  15781   2543    818   2355       O  
ATOM   1984  CB  GLU A1263     -22.362  86.091 324.573  1.00126.57           C  
ANISOU 1984  CB  GLU A1263    13461  18755  15873   3512   1471   2531       C  
ATOM   1985  CG  GLU A1263     -21.957  87.495 324.983  1.00124.34           C  
ANISOU 1985  CG  GLU A1263    13581  18082  15582   3948   1728   2486       C  
ATOM   1986  CD  GLU A1263     -20.690  87.959 324.291  1.00120.27           C  
ANISOU 1986  CD  GLU A1263    13417  17146  15136   3861   1607   2265       C  
ATOM   1987  OE1 GLU A1263     -19.855  87.100 323.933  1.00115.82           O  
ANISOU 1987  OE1 GLU A1263    12900  16472  14635   3449   1345   2064       O  
ATOM   1988  OE2 GLU A1263     -20.529  89.183 324.101  1.00121.88           O  
ANISOU 1988  OE2 GLU A1263    13859  17125  15324   4210   1790   2300       O  
ATOM   1989  N   ALA A1264     -23.850  83.850 322.684  1.00126.04           N  
ANISOU 1989  N   ALA A1264    12389  19766  15736   2736    988   2831       N  
ATOM   1990  CA  ALA A1264     -23.946  82.439 322.330  1.00123.54           C  
ANISOU 1990  CA  ALA A1264    11887  19653  15399   2184    754   2765       C  
ATOM   1991  C   ALA A1264     -24.106  82.254 320.824  1.00126.56           C  
ANISOU 1991  C   ALA A1264    12018  20328  15740   1973    540   2848       C  
ATOM   1992  O   ALA A1264     -24.329  81.141 320.349  1.00130.39           O  
ANISOU 1992  O   ALA A1264    12326  21043  16174   1501    353   2822       O  
ATOM   1993  CB  ALA A1264     -25.104  81.787 323.069  1.00123.59           C  
ANISOU 1993  CB  ALA A1264    11551  20088  15319   2083    837   2950       C  
ATOM   1994  N   GLU A1265     -23.989  83.348 320.077  1.00125.34           N  
ANISOU 1994  N   GLU A1265    11877  20155  15593   2312    577   2947       N  
ATOM   1995  CA  GLU A1265     -24.162  83.306 318.628  1.00123.98           C  
ANISOU 1995  CA  GLU A1265    11465  20280  15360   2158    385   3052       C  
ATOM   1996  C   GLU A1265     -22.974  83.920 317.896  1.00117.17           C  
ANISOU 1996  C   GLU A1265    10968  18969  14581   2240    322   2864       C  
ATOM   1997  O   GLU A1265     -22.839  83.769 316.682  1.00116.86           O  
ANISOU 1997  O   GLU A1265    10829  19069  14503   2049    141   2875       O  
ATOM   1998  CB  GLU A1265     -25.453  84.023 318.222  1.00132.52           C  
ANISOU 1998  CB  GLU A1265    12071  21953  16326   2499    482   3461       C  
ATOM   1999  CG  GLU A1265     -26.727  83.295 318.625  1.00139.97           C  
ANISOU 1999  CG  GLU A1265    12535  23491  17155   2323    489   3689       C  
ATOM   2000  CD  GLU A1265     -27.039  83.425 320.105  1.00146.27           C  
ANISOU 2000  CD  GLU A1265    13412  24176  17986   2569    743   3708       C  
ATOM   2001  OE1 GLU A1265     -26.485  84.337 320.753  1.00149.05           O  
ANISOU 2001  OE1 GLU A1265    14134  24076  18422   2984    949   3621       O  
ATOM   2002  OE2 GLU A1265     -27.839  82.614 320.618  1.00148.53           O  
ANISOU 2002  OE2 GLU A1265    13406  24826  18201   2327    741   3808       O  
ATOM   2003  N   LYS A1266     -22.117  84.613 318.637  1.00108.39           N  
ANISOU 2003  N   LYS A1266    10281  17334  13569   2502    473   2692       N  
ATOM   2004  CA  LYS A1266     -20.922  85.210 318.055  1.00100.38           C  
ANISOU 2004  CA  LYS A1266     9632  15874  12633   2558    429   2501       C  
ATOM   2005  C   LYS A1266     -19.961  84.143 317.546  1.00 94.12           C  
ANISOU 2005  C   LYS A1266     8993  14878  11889   2067    189   2230       C  
ATOM   2006  O   LYS A1266     -19.631  83.201 318.265  1.00 91.67           O  
ANISOU 2006  O   LYS A1266     8795  14422  11613   1793    146   2060       O  
ATOM   2007  CB  LYS A1266     -20.209  86.099 319.077  1.00 96.25           C  
ANISOU 2007  CB  LYS A1266     9539  14850  12180   2871    641   2358       C  
ATOM   2008  CG  LYS A1266     -20.851  87.458 319.291  1.00 98.74           C  
ANISOU 2008  CG  LYS A1266     9853  15211  12453   3424    915   2591       C  
ATOM   2009  CD  LYS A1266     -20.056  88.283 320.290  1.00 98.87           C  
ANISOU 2009  CD  LYS A1266    10367  14687  12513   3651   1122   2403       C  
ATOM   2010  CE  LYS A1266     -20.669  89.661 320.486  1.00104.88           C  
ANISOU 2010  CE  LYS A1266    11201  15428  13221   4215   1437   2624       C  
ATOM   2011  NZ  LYS A1266     -19.912  90.475 321.480  1.00105.79           N  
ANISOU 2011  NZ  LYS A1266    11847  15001  13347   4391   1655   2421       N  
ATOM   2012  N   LEU A1267     -19.522  84.291 316.299  1.00 91.39           N  
ANISOU 2012  N   LEU A1267     8661  14523  11540   1974     51   2205       N  
ATOM   2013  CA  LEU A1267     -18.472  83.436 315.760  1.00 86.17           C  
ANISOU 2013  CA  LEU A1267     8206  13605  10929   1575   -136   1942       C  
ATOM   2014  C   LEU A1267     -17.208  83.636 316.583  1.00 85.55           C  
ANISOU 2014  C   LEU A1267     8561  12972  10970   1634    -69   1683       C  
ATOM   2015  O   LEU A1267     -16.970  84.731 317.097  1.00 85.52           O  
ANISOU 2015  O   LEU A1267     8746  12750  10999   1982     95   1693       O  
ATOM   2016  CB  LEU A1267     -18.215  83.740 314.284  1.00 82.96           C  
ANISOU 2016  CB  LEU A1267     7759  13277  10487   1524   -264   1973       C  
ATOM   2017  CG  LEU A1267     -19.253  83.197 313.301  1.00 85.57           C  
ANISOU 2017  CG  LEU A1267     7677  14167  10670   1294   -408   2171       C  
ATOM   2018  CD1 LEU A1267     -18.920  83.615 311.877  1.00 86.55           C  
ANISOU 2018  CD1 LEU A1267     7799  14339  10745   1278   -522   2199       C  
ATOM   2019  CD2 LEU A1267     -19.347  81.682 313.410  1.00 82.90           C  
ANISOU 2019  CD2 LEU A1267     7290  13917  10293    780   -541   2037       C  
ATOM   2020  N   PHE A1268     -16.407  82.579 316.701  1.00 85.01           N  
ANISOU 2020  N   PHE A1268     8657  12690  10951   1289   -185   1461       N  
ATOM   2021  CA  PHE A1268     -15.281  82.551 317.631  1.00 82.58           C  
ANISOU 2021  CA  PHE A1268     8699  11942  10736   1301   -139   1241       C  
ATOM   2022  C   PHE A1268     -15.806  82.857 319.032  1.00 86.19           C  
ANISOU 2022  C   PHE A1268     9169  12402  11177   1516     32   1304       C  
ATOM   2023  O   PHE A1268     -15.473  83.882 319.627  1.00 87.14           O  
ANISOU 2023  O   PHE A1268     9495  12299  11314   1803    174   1278       O  
ATOM   2024  CB  PHE A1268     -14.190  83.545 317.217  1.00 77.01           C  
ANISOU 2024  CB  PHE A1268     8265  10904  10091   1465   -121   1129       C  
ATOM   2025  CG  PHE A1268     -13.819  83.469 315.762  1.00 74.68           C  
ANISOU 2025  CG  PHE A1268     7934  10647   9794   1321   -258   1110       C  
ATOM   2026  CD1 PHE A1268     -12.865  82.567 315.321  1.00 72.31           C  
ANISOU 2026  CD1 PHE A1268     7767  10169   9539   1020   -388    923       C  
ATOM   2027  CD2 PHE A1268     -14.425  84.302 314.834  1.00 71.85           C  
ANISOU 2027  CD2 PHE A1268     7417  10506   9378   1507   -241   1293       C  
ATOM   2028  CE1 PHE A1268     -12.524  82.497 313.982  1.00 68.16           C  
ANISOU 2028  CE1 PHE A1268     7227   9673   8998    889   -497    900       C  
ATOM   2029  CE2 PHE A1268     -14.089  84.236 313.496  1.00 65.40           C  
ANISOU 2029  CE2 PHE A1268     6574   9734   8541   1368   -367   1278       C  
ATOM   2030  CZ  PHE A1268     -13.137  83.333 313.070  1.00 63.18           C  
ANISOU 2030  CZ  PHE A1268     6438   9266   8302   1049   -494   1072       C  
ATOM   2031  N   ASN A1269     -16.635  81.950 319.540  1.00 89.25           N  
ANISOU 2031  N   ASN A1269     9352  13041  11518   1354     29   1382       N  
ATOM   2032  CA  ASN A1269     -17.417  82.175 320.752  1.00 95.20           C  
ANISOU 2032  CA  ASN A1269    10035  13905  12230   1553    200   1494       C  
ATOM   2033  C   ASN A1269     -16.584  82.413 322.007  1.00 94.77           C  
ANISOU 2033  C   ASN A1269    10324  13468  12216   1658    299   1326       C  
ATOM   2034  O   ASN A1269     -15.509  81.838 322.178  1.00 91.91           O  
ANISOU 2034  O   ASN A1269    10189  12826  11908   1457    202   1127       O  
ATOM   2035  CB  ASN A1269     -18.356  80.990 320.984  1.00101.73           C  
ANISOU 2035  CB  ASN A1269    10587  15069  12997   1275    155   1591       C  
ATOM   2036  CG  ASN A1269     -19.299  81.212 322.148  1.00109.70           C  
ANISOU 2036  CG  ASN A1269    11468  16261  13953   1483    340   1742       C  
ATOM   2037  OD1 ASN A1269     -19.038  80.770 323.267  1.00113.08           O  
ANISOU 2037  OD1 ASN A1269    12062  16511  14391   1432    401   1645       O  
ATOM   2038  ND2 ASN A1269     -20.403  81.904 321.890  1.00113.82           N  
ANISOU 2038  ND2 ASN A1269    11686  17154  14407   1736    441   1997       N  
ATOM   2039  N   GLN A1270     -17.100  83.270 322.882  1.00 94.24           N  
ANISOU 2039  N   GLN A1270    10291  13410  12104   1981    503   1419       N  
ATOM   2040  CA  GLN A1270     -16.451  83.581 324.148  1.00 85.94           C  
ANISOU 2040  CA  GLN A1270     9564  12040  11049   2080    616   1273       C  
ATOM   2041  C   GLN A1270     -17.458  83.576 325.289  1.00 83.76           C  
ANISOU 2041  C   GLN A1270     9185  11945  10696   2237    801   1405       C  
ATOM   2042  O   GLN A1270     -17.166  84.066 326.380  1.00 83.40           O  
ANISOU 2042  O   GLN A1270     9398  11681  10610   2389    946   1324       O  
ATOM   2043  CB  GLN A1270     -15.761  84.944 324.081  1.00 80.65           C  
ANISOU 2043  CB  GLN A1270     9194  11066  10384   2340    721   1194       C  
ATOM   2044  CG  GLN A1270     -14.708  85.070 322.999  1.00 69.55           C  
ANISOU 2044  CG  GLN A1270     7908   9469   9049   2203    561   1065       C  
ATOM   2045  CD  GLN A1270     -14.124  86.465 322.929  1.00 63.28           C  
ANISOU 2045  CD  GLN A1270     7412   8386   8245   2443    687   1004       C  
ATOM   2046  OE1 GLN A1270     -12.911  86.637 322.833  1.00 64.48           O  
ANISOU 2046  OE1 GLN A1270     7818   8251   8432   2314    608    815       O  
ATOM   2047  NE2 GLN A1270     -14.987  87.472 322.977  1.00 59.04           N  
ANISOU 2047  NE2 GLN A1270     6853   7927   7653   2794    898   1174       N  
ATOM   2048  N   ASP A1271     -18.642  83.026 325.033  1.00 85.54           N  
ANISOU 2048  N   ASP A1271     9031  12585  10885   2183    799   1609       N  
ATOM   2049  CA  ASP A1271     -19.738  83.071 325.998  1.00 89.85           C  
ANISOU 2049  CA  ASP A1271     9414  13373  11352   2356    993   1779       C  
ATOM   2050  C   ASP A1271     -19.394  82.317 327.280  1.00 90.09           C  
ANISOU 2050  C   ASP A1271     9627  13239  11363   2193   1014   1647       C  
ATOM   2051  O   ASP A1271     -19.620  81.110 327.389  1.00 89.40           O  
ANISOU 2051  O   ASP A1271     9396  13297  11274   1878    908   1653       O  
ATOM   2052  CB  ASP A1271     -21.019  82.506 325.381  1.00 91.20           C  
ANISOU 2052  CB  ASP A1271     9098  14074  11478   2253    950   2028       C  
ATOM   2053  CG  ASP A1271     -22.255  82.846 326.191  1.00 94.51           C  
ANISOU 2053  CG  ASP A1271     9290  14807  11811   2529   1186   2263       C  
ATOM   2054  OD1 ASP A1271     -22.151  83.680 327.115  1.00 97.53           O  
ANISOU 2054  OD1 ASP A1271     9919  14971  12169   2857   1407   2238       O  
ATOM   2055  OD2 ASP A1271     -23.334  82.292 325.896  1.00 94.63           O  
ANISOU 2055  OD2 ASP A1271     8884  15300  11772   2409   1159   2476       O  
ATOM   2056  N   VAL A1272     -18.848  83.050 328.245  1.00 88.69           N  
ANISOU 2056  N   VAL A1272     9788  12756  11153   2399   1158   1531       N  
ATOM   2057  CA  VAL A1272     -18.430  82.483 329.519  1.00 86.72           C  
ANISOU 2057  CA  VAL A1272     9749  12340  10862   2277   1184   1406       C  
ATOM   2058  C   VAL A1272     -19.619  81.950 330.311  1.00 87.83           C  
ANISOU 2058  C   VAL A1272     9649  12793  10928   2293   1318   1582       C  
ATOM   2059  O   VAL A1272     -19.547  80.876 330.908  1.00 84.21           O  
ANISOU 2059  O   VAL A1272     9188  12350  10457   2036   1252   1542       O  
ATOM   2060  CB  VAL A1272     -17.679  83.527 330.373  1.00 86.42           C  
ANISOU 2060  CB  VAL A1272    10125  11946  10764   2492   1325   1254       C  
ATOM   2061  CG1 VAL A1272     -17.253  82.926 331.701  1.00 86.58           C  
ANISOU 2061  CG1 VAL A1272    10346  11836  10714   2356   1336   1140       C  
ATOM   2062  CG2 VAL A1272     -16.472  84.062 329.618  1.00 84.21           C  
ANISOU 2062  CG2 VAL A1272    10078  11371  10549   2442   1195   1083       C  
ATOM   2063  N   ASP A1273     -20.714  82.704 330.302  1.00 91.46           N  
ANISOU 2063  N   ASP A1273     9905  13509  11336   2608   1520   1792       N  
ATOM   2064  CA  ASP A1273     -21.909  82.343 331.059  1.00 94.28           C  
ANISOU 2064  CA  ASP A1273    10008  14203  11614   2670   1683   1987       C  
ATOM   2065  C   ASP A1273     -22.480  80.997 330.623  1.00 98.61           C  
ANISOU 2065  C   ASP A1273    10198  15089  12179   2283   1514   2085       C  
ATOM   2066  O   ASP A1273     -22.973  80.230 331.449  1.00 99.12           O  
ANISOU 2066  O   ASP A1273    10177  15294  12190   2140   1571   2138       O  
ATOM   2067  CB  ASP A1273     -22.974  83.430 330.916  1.00 95.31           C  
ANISOU 2067  CB  ASP A1273     9937  14585  11690   3113   1931   2232       C  
ATOM   2068  CG  ASP A1273     -22.479  84.790 331.364  1.00 92.72           C  
ANISOU 2068  CG  ASP A1273    10016  13887  11325   3497   2146   2136       C  
ATOM   2069  OD1 ASP A1273     -23.314  85.626 331.768  1.00 92.44           O  
ANISOU 2069  OD1 ASP A1273     9937  13971  11214   3901   2437   2313       O  
ATOM   2070  OD2 ASP A1273     -21.252  85.022 331.314  1.00 90.62           O  
ANISOU 2070  OD2 ASP A1273    10124  13213  11094   3390   2036   1888       O  
ATOM   2071  N   ALA A1274     -22.407  80.717 329.325  1.00104.98           N  
ANISOU 2071  N   ALA A1274    10824  16016  13048   2093   1316   2103       N  
ATOM   2072  CA  ALA A1274     -22.907  79.459 328.781  1.00110.33           C  
ANISOU 2072  CA  ALA A1274    11206  16993  13722   1674   1152   2172       C  
ATOM   2073  C   ALA A1274     -22.133  78.272 329.339  1.00112.73           C  
ANISOU 2073  C   ALA A1274    11759  17022  14050   1313   1041   1979       C  
ATOM   2074  O   ALA A1274     -22.709  77.224 329.631  1.00114.37           O  
ANISOU 2074  O   ALA A1274    11813  17428  14214   1024   1028   2047       O  
ATOM   2075  CB  ALA A1274     -22.832  79.470 327.263  1.00109.88           C  
ANISOU 2075  CB  ALA A1274    10980  17064  13706   1538    963   2195       C  
ATOM   2076  N   ALA A1275     -20.823  78.445 329.485  1.00115.51           N  
ANISOU 2076  N   ALA A1275    12495  16929  14463   1334    971   1753       N  
ATOM   2077  CA  ALA A1275     -19.965  77.387 330.002  1.00108.36           C  
ANISOU 2077  CA  ALA A1275    11841  15750  13580   1054    873   1589       C  
ATOM   2078  C   ALA A1275     -20.226  77.137 331.483  1.00105.87           C  
ANISOU 2078  C   ALA A1275    11624  15415  13185   1111   1029   1615       C  
ATOM   2079  O   ALA A1275     -20.203  75.995 331.940  1.00104.25           O  
ANISOU 2079  O   ALA A1275    11458  15188  12963    839    994   1603       O  
ATOM   2080  CB  ALA A1275     -18.504  77.736 329.774  1.00106.56           C  
ANISOU 2080  CB  ALA A1275    11951  15112  13424   1095    763   1373       C  
ATOM   2081  N   VAL A1276     -20.479  78.210 332.226  1.00100.73           N  
ANISOU 2081  N   VAL A1276    11040  14757  12475   1467   1217   1654       N  
ATOM   2082  CA  VAL A1276     -20.716  78.115 333.663  1.00 92.67           C  
ANISOU 2082  CA  VAL A1276    10141  13714  11358   1553   1386   1673       C  
ATOM   2083  C   VAL A1276     -22.000  77.343 333.968  1.00 92.83           C  
ANISOU 2083  C   VAL A1276     9833  14119  11319   1415   1477   1878       C  
ATOM   2084  O   VAL A1276     -22.042  76.542 334.903  1.00 95.69           O  
ANISOU 2084  O   VAL A1276    10279  14454  11626   1262   1519   1875       O  
ATOM   2085  CB  VAL A1276     -20.790  79.513 334.313  1.00 87.96           C  
ANISOU 2085  CB  VAL A1276     9707  13024  10688   1973   1602   1670       C  
ATOM   2086  CG1 VAL A1276     -21.100  79.399 335.798  1.00 90.00           C  
ANISOU 2086  CG1 VAL A1276    10093  13280  10822   2052   1790   1691       C  
ATOM   2087  CG2 VAL A1276     -19.485  80.264 334.103  1.00 82.26           C  
ANISOU 2087  CG2 VAL A1276     9338  11915  10001   2053   1517   1456       C  
ATOM   2088  N   ARG A1277     -23.040  77.579 333.172  1.00 90.29           N  
ANISOU 2088  N   ARG A1277     9128  14180  10999   1459   1506   2068       N  
ATOM   2089  CA  ARG A1277     -24.313  76.887 333.358  1.00 93.26           C  
ANISOU 2089  CA  ARG A1277     9135  14992  11307   1297   1584   2284       C  
ATOM   2090  C   ARG A1277     -24.161  75.385 333.143  1.00 94.32           C  
ANISOU 2090  C   ARG A1277     9266  15115  11457    787   1417   2230       C  
ATOM   2091  O   ARG A1277     -24.830  74.584 333.794  1.00 95.50           O  
ANISOU 2091  O   ARG A1277     9302  15448  11537    590   1496   2331       O  
ATOM   2092  CB  ARG A1277     -25.377  77.440 332.408  1.00 98.41           C  
ANISOU 2092  CB  ARG A1277     9344  16102  11947   1424   1613   2513       C  
ATOM   2093  CG  ARG A1277     -25.649  78.927 332.553  1.00103.77           C  
ANISOU 2093  CG  ARG A1277    10020  16804  12605   1966   1819   2608       C  
ATOM   2094  CD  ARG A1277     -26.887  79.328 331.765  1.00111.34           C  
ANISOU 2094  CD  ARG A1277    10470  18308  13526   2108   1877   2907       C  
ATOM   2095  NE  ARG A1277     -26.899  80.750 331.431  1.00114.51           N  
ANISOU 2095  NE  ARG A1277    10912  18658  13938   2610   2017   2979       N  
ATOM   2096  CZ  ARG A1277     -26.531  81.243 330.252  1.00112.77           C  
ANISOU 2096  CZ  ARG A1277    10674  18395  13779   2661   1881   2961       C  
ATOM   2097  NH1 ARG A1277     -26.123  80.429 329.288  1.00106.93           N  
ANISOU 2097  NH1 ARG A1277     9869  17670  13091   2239   1598   2866       N  
ATOM   2098  NH2 ARG A1277     -26.573  82.550 330.034  1.00115.61           N  
ANISOU 2098  NH2 ARG A1277    11104  18683  14138   3137   2046   3042       N  
ATOM   2099  N   GLY A1278     -23.278  75.012 332.223  1.00 96.97           N  
ANISOU 2099  N   GLY A1278     9748  15219  11877    579   1208   2075       N  
ATOM   2100  CA  GLY A1278     -23.017  73.613 331.940  1.00106.39           C  
ANISOU 2100  CA  GLY A1278    11015  16324  13083    116   1073   2004       C  
ATOM   2101  C   GLY A1278     -22.209  72.958 333.042  1.00113.98           C  
ANISOU 2101  C   GLY A1278    12342  16925  14039     60   1104   1882       C  
ATOM   2102  O   GLY A1278     -22.353  71.763 333.304  1.00116.58           O  
ANISOU 2102  O   GLY A1278    12719  17238  14338   -270   1098   1896       O  
ATOM   2103  N   ILE A1279     -21.354  73.746 333.687  1.00118.43           N  
ANISOU 2103  N   ILE A1279    13175  17205  14618    373   1141   1769       N  
ATOM   2104  CA  ILE A1279     -20.533  73.259 334.791  1.00118.11           C  
ANISOU 2104  CA  ILE A1279    13469  16859  14548    362   1163   1670       C  
ATOM   2105  C   ILE A1279     -21.393  72.939 336.010  1.00118.08           C  
ANISOU 2105  C   ILE A1279    13400  17034  14431    368   1348   1803       C  
ATOM   2106  O   ILE A1279     -21.237  71.890 336.636  1.00117.54           O  
ANISOU 2106  O   ILE A1279    13471  16861  14326    154   1357   1806       O  
ATOM   2107  CB  ILE A1279     -19.449  74.285 335.185  1.00116.60           C  
ANISOU 2107  CB  ILE A1279    13559  16378  14366    668   1151   1521       C  
ATOM   2108  CG1 ILE A1279     -18.424  74.436 334.060  1.00113.85           C  
ANISOU 2108  CG1 ILE A1279    13312  15817  14129    623    963   1380       C  
ATOM   2109  CG2 ILE A1279     -18.754  73.867 336.469  1.00116.83           C  
ANISOU 2109  CG2 ILE A1279    13884  16186  14322    674   1186   1458       C  
ATOM   2110  CD1 ILE A1279     -17.342  75.454 334.353  1.00112.39           C  
ANISOU 2110  CD1 ILE A1279    13387  15372  13945    869    940   1233       C  
ATOM   2111  N   LEU A1280     -22.309  73.846 336.334  1.00110.38           N  
ANISOU 2111  N   LEU A1280    12218  16325  13394    629   1515   1928       N  
ATOM   2112  CA  LEU A1280     -23.200  73.664 337.475  1.00105.27           C  
ANISOU 2112  CA  LEU A1280    11483  15884  12632    673   1720   2070       C  
ATOM   2113  C   LEU A1280     -24.228  72.566 337.216  1.00104.38           C  
ANISOU 2113  C   LEU A1280    11073  16094  12494    308   1727   2231       C  
ATOM   2114  O   LEU A1280     -24.863  72.068 338.145  1.00105.55           O  
ANISOU 2114  O   LEU A1280    11173  16383  12550    233   1873   2341       O  
ATOM   2115  CB  LEU A1280     -23.912  74.977 337.809  1.00101.85           C  
ANISOU 2115  CB  LEU A1280    10910  15650  12138   1087   1925   2172       C  
ATOM   2116  CG  LEU A1280     -23.019  76.164 338.177  1.00 95.77           C  
ANISOU 2116  CG  LEU A1280    10470  14561  11355   1436   1967   2013       C  
ATOM   2117  CD1 LEU A1280     -23.858  77.402 338.454  1.00 97.85           C  
ANISOU 2117  CD1 LEU A1280    10614  15015  11550   1848   2218   2135       C  
ATOM   2118  CD2 LEU A1280     -22.140  75.829 339.373  1.00 91.32           C  
ANISOU 2118  CD2 LEU A1280    10291  13694  10713   1400   1972   1876       C  
ATOM   2119  N   ARG A1281     -24.384  72.192 335.950  1.00103.96           N  
ANISOU 2119  N   ARG A1281    10831  16162  12508     57   1574   2240       N  
ATOM   2120  CA  ARG A1281     -25.345  71.166 335.563  1.00105.65           C  
ANISOU 2120  CA  ARG A1281    10767  16697  12678   -358   1562   2377       C  
ATOM   2121  C   ARG A1281     -24.764  69.763 335.715  1.00106.16           C  
ANISOU 2121  C   ARG A1281    11120  16467  12748   -759   1487   2277       C  
ATOM   2122  O   ARG A1281     -25.490  68.809 335.997  1.00107.94           O  
ANISOU 2122  O   ARG A1281    11249  16865  12900  -1092   1554   2382       O  
ATOM   2123  CB  ARG A1281     -25.808  71.387 334.121  1.00105.45           C  
ANISOU 2123  CB  ARG A1281    10420  16959  12686   -482   1431   2434       C  
ATOM   2124  N   ASN A1282     -23.454  69.641 335.524  1.00107.18           N  
ANISOU 2124  N   ASN A1282    11609  16156  12959   -721   1364   2086       N  
ATOM   2125  CA  ASN A1282     -22.782  68.352 335.639  1.00105.46           C  
ANISOU 2125  CA  ASN A1282    11703  15614  12752  -1029   1313   2002       C  
ATOM   2126  C   ASN A1282     -22.524  67.988 337.098  1.00104.55           C  
ANISOU 2126  C   ASN A1282    11830  15328  12568   -934   1443   2026       C  
ATOM   2127  O   ASN A1282     -22.182  68.845 337.912  1.00105.02           O  
ANISOU 2127  O   ASN A1282    11974  15326  12601   -578   1502   2003       O  
ATOM   2128  CB  ASN A1282     -21.467  68.362 334.853  1.00101.92           C  
ANISOU 2128  CB  ASN A1282    11517  14794  12413   -992   1145   1817       C  
ATOM   2129  CG  ASN A1282     -20.931  66.965 334.583  1.00101.38           C  
ANISOU 2129  CG  ASN A1282    11724  14435  12361  -1342   1103   1753       C  
ATOM   2130  OD1 ASN A1282     -20.939  66.099 335.458  1.00103.99           O  
ANISOU 2130  OD1 ASN A1282    12238  14642  12634  -1463   1204   1803       O  
ATOM   2131  ND2 ASN A1282     -20.465  66.739 333.360  1.00100.34           N  
ANISOU 2131  ND2 ASN A1282    11647  14181  12299  -1497    973   1650       N  
ATOM   2132  N   ALA A1283     -22.688  66.709 337.419  1.00103.07           N  
ANISOU 2132  N   ALA A1283    11775  15054  12334  -1269   1494   2071       N  
ATOM   2133  CA  ALA A1283     -22.528  66.233 338.787  1.00101.23           C  
ANISOU 2133  CA  ALA A1283    11764  14681  12017  -1214   1624   2124       C  
ATOM   2134  C   ALA A1283     -21.062  66.174 339.203  1.00 96.78           C  
ANISOU 2134  C   ALA A1283    11589  13692  11492  -1011   1548   1999       C  
ATOM   2135  O   ALA A1283     -20.745  66.218 340.392  1.00100.96           O  
ANISOU 2135  O   ALA A1283    12289  14130  11942   -833   1627   2028       O  
ATOM   2136  CB  ALA A1283     -23.174  64.867 338.944  1.00104.15           C  
ANISOU 2136  CB  ALA A1283    12173  15080  12321  -1651   1716   2224       C  
ATOM   2137  N   LYS A1284     -20.170  66.075 338.222  1.00 88.98           N  
ANISOU 2137  N   LYS A1284    10725  12472  10609  -1041   1395   1872       N  
ATOM   2138  CA  LYS A1284     -18.743  65.964 338.499  1.00 85.68           C  
ANISOU 2138  CA  LYS A1284    10635  11691  10228   -863   1313   1775       C  
ATOM   2139  C   LYS A1284     -18.037  67.316 338.470  1.00 80.41           C  
ANISOU 2139  C   LYS A1284     9945  11012   9596   -507   1218   1669       C  
ATOM   2140  O   LYS A1284     -16.859  67.414 338.810  1.00 78.92           O  
ANISOU 2140  O   LYS A1284     9982  10590   9414   -339   1144   1597       O  
ATOM   2141  CB  LYS A1284     -18.076  65.019 337.497  1.00 89.42           C  
ANISOU 2141  CB  LYS A1284    11292  11892  10790  -1084   1228   1705       C  
ATOM   2142  CG  LYS A1284     -18.493  63.563 337.626  1.00 97.85           C  
ANISOU 2142  CG  LYS A1284    12521  12849  11809  -1438   1342   1790       C  
ATOM   2143  CD  LYS A1284     -17.678  62.684 336.688  1.00101.98           C  
ANISOU 2143  CD  LYS A1284    13304  13035  12409  -1599   1289   1707       C  
ATOM   2144  CE  LYS A1284     -18.024  61.213 336.853  1.00106.38           C  
ANISOU 2144  CE  LYS A1284    14102  13412  12904  -1949   1436   1785       C  
ATOM   2145  NZ  LYS A1284     -17.184  60.345 335.980  1.00105.69           N  
ANISOU 2145  NZ  LYS A1284    14328  12949  12881  -2070   1425   1704       N  
ATOM   2146  N   LEU A1285     -18.758  68.358 338.068  1.00 80.22           N  
ANISOU 2146  N   LEU A1285     9651  11247   9582   -396   1229   1670       N  
ATOM   2147  CA  LEU A1285     -18.150  69.674 337.898  1.00 81.40           C  
ANISOU 2147  CA  LEU A1285     9803  11362   9765    -88   1158   1563       C  
ATOM   2148  C   LEU A1285     -18.662  70.699 338.906  1.00 83.46           C  
ANISOU 2148  C   LEU A1285    10008  11786   9917    181   1297   1604       C  
ATOM   2149  O   LEU A1285     -17.944  71.632 339.268  1.00 79.33           O  
ANISOU 2149  O   LEU A1285     9629  11147   9366    426   1273   1505       O  
ATOM   2150  CB  LEU A1285     -18.391  70.184 336.475  1.00 81.63           C  
ANISOU 2150  CB  LEU A1285     9621  11498   9896   -124   1063   1520       C  
ATOM   2151  CG  LEU A1285     -17.817  69.322 335.349  1.00 78.48           C  
ANISOU 2151  CG  LEU A1285     9304  10920   9594   -374    929   1450       C  
ATOM   2152  CD1 LEU A1285     -18.073  69.964 333.995  1.00 78.28           C  
ANISOU 2152  CD1 LEU A1285     9066  11032   9645   -386    836   1411       C  
ATOM   2153  CD2 LEU A1285     -16.331  69.085 335.562  1.00 74.83           C  
ANISOU 2153  CD2 LEU A1285     9152  10110   9170   -277    839   1343       C  
ATOM   2154  N   LYS A1286     -19.902  70.527 339.353  1.00 88.72           N  
ANISOU 2154  N   LYS A1286    10476  12724  10511    123   1455   1749       N  
ATOM   2155  CA  LYS A1286     -20.505  71.453 340.308  1.00 89.27           C  
ANISOU 2155  CA  LYS A1286    10492  12960  10467    391   1631   1805       C  
ATOM   2156  C   LYS A1286     -19.770  71.513 341.657  1.00 92.12           C  
ANISOU 2156  C   LYS A1286    11168  13129  10704    528   1678   1753       C  
ATOM   2157  O   LYS A1286     -19.476  72.607 342.140  1.00 91.21           O  
ANISOU 2157  O   LYS A1286    11166  12969  10519    793   1730   1676       O  
ATOM   2158  CB  LYS A1286     -21.980  71.101 340.536  1.00 87.34           C  
ANISOU 2158  CB  LYS A1286     9950  13074  10163    279   1800   1997       C  
ATOM   2159  CG  LYS A1286     -22.717  72.089 341.426  1.00 86.34           C  
ANISOU 2159  CG  LYS A1286     9739  13146   9921    589   2019   2077       C  
ATOM   2160  CD  LYS A1286     -24.170  71.689 341.617  1.00 91.50           C  
ANISOU 2160  CD  LYS A1286    10053  14197  10515    472   2188   2291       C  
ATOM   2161  CE  LYS A1286     -24.286  70.357 342.340  1.00 95.70           C  
ANISOU 2161  CE  LYS A1286    10687  14692  10982    164   2223   2358       C  
ATOM   2162  NZ  LYS A1286     -23.678  70.405 343.699  1.00 96.05           N  
ANISOU 2162  NZ  LYS A1286    11067  14520  10907    322   2307   2306       N  
ATOM   2163  N   PRO A1287     -19.466  70.352 342.275  1.00100.79           N  
ANISOU 2163  N   PRO A1287    12426  14112  11757    341   1669   1798       N  
ATOM   2164  CA  PRO A1287     -18.789  70.467 343.572  1.00104.49           C  
ANISOU 2164  CA  PRO A1287    13172  14448  12082    481   1705   1767       C  
ATOM   2165  C   PRO A1287     -17.340  70.932 343.448  1.00102.51           C  
ANISOU 2165  C   PRO A1287    13148  13952  11848    595   1528   1609       C  
ATOM   2166  O   PRO A1287     -16.762  71.410 344.425  1.00105.40           O  
ANISOU 2166  O   PRO A1287    13718  14257  12073    738   1542   1557       O  
ATOM   2167  CB  PRO A1287     -18.853  69.042 344.125  1.00109.57           C  
ANISOU 2167  CB  PRO A1287    13914  15037  12682    252   1739   1884       C  
ATOM   2168  CG  PRO A1287     -18.886  68.184 342.917  1.00107.57           C  
ANISOU 2168  CG  PRO A1287    13568  14721  12581     -7   1640   1893       C  
ATOM   2169  CD  PRO A1287     -19.713  68.940 341.918  1.00103.16           C  
ANISOU 2169  CD  PRO A1287    12701  14389  12107      7   1645   1882       C  
ATOM   2170  N   VAL A1288     -16.764  70.789 342.260  1.00 95.20           N  
ANISOU 2170  N   VAL A1288    12184  12909  11078    515   1366   1537       N  
ATOM   2171  CA  VAL A1288     -15.387  71.202 342.025  1.00 87.31           C  
ANISOU 2171  CA  VAL A1288    11359  11708  10106    604   1196   1401       C  
ATOM   2172  C   VAL A1288     -15.316  72.703 341.758  1.00 84.64           C  
ANISOU 2172  C   VAL A1288    10999  11398   9761    806   1198   1279       C  
ATOM   2173  O   VAL A1288     -14.381  73.377 342.186  1.00 83.17           O  
ANISOU 2173  O   VAL A1288    11001  11105   9495    914   1132   1170       O  
ATOM   2174  CB  VAL A1288     -14.766  70.437 340.843  1.00 80.88           C  
ANISOU 2174  CB  VAL A1288    10530  10745   9457    448   1044   1374       C  
ATOM   2175  CG1 VAL A1288     -13.286  70.763 340.716  1.00 73.90           C  
ANISOU 2175  CG1 VAL A1288     9811   9681   8587    543    878   1262       C  
ATOM   2176  CG2 VAL A1288     -14.968  68.941 341.021  1.00 84.23           C  
ANISOU 2176  CG2 VAL A1288    11009  11107   9886    239   1086   1497       C  
ATOM   2177  N   TYR A1289     -16.319  73.220 341.056  1.00 85.95           N  
ANISOU 2177  N   TYR A1289    10940  11720   9997    847   1282   1311       N  
ATOM   2178  CA  TYR A1289     -16.364  74.637 340.714  1.00 87.84           C  
ANISOU 2178  CA  TYR A1289    11168  11971  10237   1062   1320   1222       C  
ATOM   2179  C   TYR A1289     -16.586  75.511 341.944  1.00 86.97           C  
ANISOU 2179  C   TYR A1289    11221  11885   9940   1265   1496   1200       C  
ATOM   2180  O   TYR A1289     -15.929  76.539 342.110  1.00 85.54           O  
ANISOU 2180  O   TYR A1289    11235  11573   9694   1399   1487   1065       O  
ATOM   2181  CB  TYR A1289     -17.465  74.901 339.684  1.00 94.24           C  
ANISOU 2181  CB  TYR A1289    11671  12983  11152   1081   1382   1308       C  
ATOM   2182  CG  TYR A1289     -17.579  76.349 339.257  1.00 95.77           C  
ANISOU 2182  CG  TYR A1289    11855  13180  11353   1337   1448   1248       C  
ATOM   2183  CD1 TYR A1289     -16.752  76.870 338.271  1.00 92.98           C  
ANISOU 2183  CD1 TYR A1289    11556  12671  11100   1352   1298   1128       C  
ATOM   2184  CD2 TYR A1289     -18.519  77.193 339.836  1.00 98.59           C  
ANISOU 2184  CD2 TYR A1289    12165  13684  11609   1576   1682   1323       C  
ATOM   2185  CE1 TYR A1289     -16.852  78.191 337.877  1.00 92.59           C  
ANISOU 2185  CE1 TYR A1289    11531  12597  11051   1585   1377   1083       C  
ATOM   2186  CE2 TYR A1289     -18.627  78.516 339.449  1.00 98.61           C  
ANISOU 2186  CE2 TYR A1289    12201  13654  11612   1837   1777   1282       C  
ATOM   2187  CZ  TYR A1289     -17.792  79.009 338.469  1.00 95.28           C  
ANISOU 2187  CZ  TYR A1289    11850  13060  11291   1833   1621   1162       C  
ATOM   2188  OH  TYR A1289     -17.896  80.325 338.079  1.00 95.25           O  
ANISOU 2188  OH  TYR A1289    11911  12999  11283   2092   1732   1129       O  
ATOM   2189  N   ASP A1290     -17.513  75.097 342.802  1.00 89.31           N  
ANISOU 2189  N   ASP A1290    11454  12343  10138   1266   1667   1328       N  
ATOM   2190  CA  ASP A1290     -17.872  75.879 343.982  1.00 88.18           C  
ANISOU 2190  CA  ASP A1290    11466  12237   9802   1462   1874   1320       C  
ATOM   2191  C   ASP A1290     -16.761  75.898 345.031  1.00 83.36           C  
ANISOU 2191  C   ASP A1290    11192  11457   9025   1436   1802   1207       C  
ATOM   2192  O   ASP A1290     -16.682  76.820 345.842  1.00 83.74           O  
ANISOU 2192  O   ASP A1290    11458  11462   8898   1585   1928   1124       O  
ATOM   2193  CB  ASP A1290     -19.164  75.342 344.604  1.00 93.33           C  
ANISOU 2193  CB  ASP A1290    11938  13134  10391   1456   2080   1504       C  
ATOM   2194  CG  ASP A1290     -20.354  75.460 343.670  1.00 97.92           C  
ANISOU 2194  CG  ASP A1290    12149  13962  11094   1493   2168   1639       C  
ATOM   2195  OD1 ASP A1290     -20.307  76.300 342.747  1.00100.64           O  
ANISOU 2195  OD1 ASP A1290    12420  14287  11530   1625   2135   1588       O  
ATOM   2196  OD2 ASP A1290     -21.340  74.718 343.863  1.00 98.48           O  
ANISOU 2196  OD2 ASP A1290    11996  14266  11155   1382   2269   1807       O  
ATOM   2197  N   SER A1291     -15.905  74.881 345.013  1.00 76.29           N  
ANISOU 2197  N   SER A1291    10348  10474   8167   1248   1609   1214       N  
ATOM   2198  CA  SER A1291     -14.826  74.780 345.991  1.00 75.28           C  
ANISOU 2198  CA  SER A1291    10490  10243   7869   1214   1516   1148       C  
ATOM   2199  C   SER A1291     -13.612  75.606 345.576  1.00 74.40           C  
ANISOU 2199  C   SER A1291    10526   9983   7758   1232   1348    973       C  
ATOM   2200  O   SER A1291     -12.676  75.785 346.356  1.00 75.69           O  
ANISOU 2200  O   SER A1291    10906  10100   7752   1201   1264    901       O  
ATOM   2201  CB  SER A1291     -14.417  73.319 346.191  1.00 75.47           C  
ANISOU 2201  CB  SER A1291    10505  10248   7922   1044   1404   1267       C  
ATOM   2202  OG  SER A1291     -13.729  72.817 345.059  1.00 65.40           O  
ANISOU 2202  OG  SER A1291     9148   8864   6839    946   1217   1247       O  
ATOM   2203  N   LEU A1292     -13.632  76.110 344.347  1.00 74.09           N  
ANISOU 2203  N   LEU A1292    10360   9893   7896   1265   1298    913       N  
ATOM   2204  CA  LEU A1292     -12.508  76.872 343.813  1.00 74.48           C  
ANISOU 2204  CA  LEU A1292    10529   9803   7967   1260   1143    754       C  
ATOM   2205  C   LEU A1292     -12.705  78.376 343.975  1.00 78.57           C  
ANISOU 2205  C   LEU A1292    11212  10262   8378   1413   1287    623       C  
ATOM   2206  O   LEU A1292     -13.835  78.862 344.028  1.00 81.75           O  
ANISOU 2206  O   LEU A1292    11556  10733   8772   1570   1507    674       O  
ATOM   2207  CB  LEU A1292     -12.291  76.534 342.336  1.00 72.17           C  
ANISOU 2207  CB  LEU A1292    10038   9462   7921   1197   1001    759       C  
ATOM   2208  CG  LEU A1292     -11.194  75.523 341.999  1.00 72.60           C  
ANISOU 2208  CG  LEU A1292    10083   9447   8056   1051    785    778       C  
ATOM   2209  CD1 LEU A1292     -11.337  74.254 342.820  1.00 71.84           C  
ANISOU 2209  CD1 LEU A1292     9997   9404   7897    973    804    923       C  
ATOM   2210  CD2 LEU A1292     -11.215  75.203 340.510  1.00 75.17           C  
ANISOU 2210  CD2 LEU A1292    10222   9726   8612    995    696    783       C  
ATOM   2211  N   ASP A1293     -11.597  79.106 344.054  1.00 78.70           N  
ANISOU 2211  N   ASP A1293    11443  10157   8302   1364   1177    465       N  
ATOM   2212  CA  ASP A1293     -11.642  80.561 344.130  1.00 80.11           C  
ANISOU 2212  CA  ASP A1293    11845  10222   8372   1477   1317    318       C  
ATOM   2213  C   ASP A1293     -11.829  81.153 342.735  1.00 79.60           C  
ANISOU 2213  C   ASP A1293    11649  10080   8516   1565   1315    294       C  
ATOM   2214  O   ASP A1293     -11.717  80.443 341.737  1.00 76.28           O  
ANISOU 2214  O   ASP A1293    10984   9695   8302   1498   1164    362       O  
ATOM   2215  CB  ASP A1293     -10.372  81.111 344.780  1.00 82.72           C  
ANISOU 2215  CB  ASP A1293    12471  10466   8492   1331   1197    152       C  
ATOM   2216  CG  ASP A1293      -9.123  80.790 343.983  1.00 86.31           C  
ANISOU 2216  CG  ASP A1293    12836  10892   9067   1169    915    111       C  
ATOM   2217  OD1 ASP A1293      -8.572  79.683 344.158  1.00 86.72           O  
ANISOU 2217  OD1 ASP A1293    12767  11041   9143   1063    744    208       O  
ATOM   2218  OD2 ASP A1293      -8.689  81.647 343.185  1.00 88.77           O  
ANISOU 2218  OD2 ASP A1293    13206  11081   9441   1162    881     -6       O  
ATOM   2219  N   ALA A1294     -12.104  82.454 342.678  1.00 77.81           N  
ANISOU 2219  N   ALA A1294    11613   9734   8219   1717   1495    198       N  
ATOM   2220  CA  ALA A1294     -12.444  83.134 341.428  1.00 74.30           C  
ANISOU 2220  CA  ALA A1294    11060   9222   7947   1853   1541    203       C  
ATOM   2221  C   ALA A1294     -11.398  82.940 340.331  1.00 73.46           C  
ANISOU 2221  C   ALA A1294    10864   9047   8000   1692   1278    140       C  
ATOM   2222  O   ALA A1294     -11.744  82.749 339.165  1.00 75.30           O  
ANISOU 2222  O   ALA A1294    10854   9322   8434   1737   1230    217       O  
ATOM   2223  CB  ALA A1294     -12.655  84.617 341.687  1.00 66.27           C  
ANISOU 2223  CB  ALA A1294    10362   8029   6789   2034   1787     92       C  
ATOM   2224  N   VAL A1295     -10.124  82.992 340.707  1.00 72.92           N  
ANISOU 2224  N   VAL A1295    10982   8897   7826   1499   1109      8       N  
ATOM   2225  CA  VAL A1295      -9.038  82.832 339.745  1.00 68.19           C  
ANISOU 2225  CA  VAL A1295    10304   8247   7359   1350    871    -48       C  
ATOM   2226  C   VAL A1295      -9.018  81.417 339.172  1.00 70.78           C  
ANISOU 2226  C   VAL A1295    10322   8699   7872   1275    705     89       C  
ATOM   2227  O   VAL A1295      -8.845  81.227 337.969  1.00 74.46           O  
ANISOU 2227  O   VAL A1295    10621   9144   8527   1256    604    106       O  
ATOM   2228  CB  VAL A1295      -7.669  83.147 340.383  1.00 64.90           C  
ANISOU 2228  CB  VAL A1295    10121   7780   6761   1145    726   -193       C  
ATOM   2229  CG1 VAL A1295      -6.546  82.919 339.382  1.00 61.96           C  
ANISOU 2229  CG1 VAL A1295     9624   7389   6528   1004    489   -225       C  
ATOM   2230  CG2 VAL A1295      -7.642  84.577 340.897  1.00 65.12           C  
ANISOU 2230  CG2 VAL A1295    10513   7647   6583   1166    900   -357       C  
ATOM   2231  N   ARG A1296      -9.205  80.428 340.039  1.00 72.64           N  
ANISOU 2231  N   ARG A1296    10511   9048   8041   1229    696    185       N  
ATOM   2232  CA  ARG A1296      -9.199  79.032 339.614  1.00 72.65           C  
ANISOU 2232  CA  ARG A1296    10284   9128   8192   1149    575    315       C  
ATOM   2233  C   ARG A1296     -10.526  78.617 338.985  1.00 71.79           C  
ANISOU 2233  C   ARG A1296     9946   9104   8226   1224    691    439       C  
ATOM   2234  O   ARG A1296     -10.580  77.654 338.222  1.00 72.47           O  
ANISOU 2234  O   ARG A1296     9852   9219   8464   1136    601    517       O  
ATOM   2235  CB  ARG A1296      -8.875  78.114 340.793  1.00 77.36           C  
ANISOU 2235  CB  ARG A1296    10940   9802   8651   1072    533    388       C  
ATOM   2236  CG  ARG A1296      -7.419  78.144 341.219  1.00 77.24           C  
ANISOU 2236  CG  ARG A1296    11053   9775   8519    959    351    320       C  
ATOM   2237  CD  ARG A1296      -7.153  77.121 342.306  1.00 75.22           C  
ANISOU 2237  CD  ARG A1296    10823   9623   8135    911    308    438       C  
ATOM   2238  NE  ARG A1296      -5.744  77.070 342.678  1.00 74.10           N  
ANISOU 2238  NE  ARG A1296    10748   9532   7874    813    118    415       N  
ATOM   2239  CZ  ARG A1296      -5.190  77.843 343.606  1.00 77.60           C  
ANISOU 2239  CZ  ARG A1296    11382  10036   8068    741     90    319       C  
ATOM   2240  NH1 ARG A1296      -3.898  77.729 343.882  1.00 82.76           N  
ANISOU 2240  NH1 ARG A1296    12042  10793   8609    631   -103    324       N  
ATOM   2241  NH2 ARG A1296      -5.928  78.732 344.258  1.00 77.40           N  
ANISOU 2241  NH2 ARG A1296    11542   9978   7888    774    265    223       N  
ATOM   2242  N   ARG A1297     -11.594  79.338 339.311  1.00 74.21           N  
ANISOU 2242  N   ARG A1297    10264   9464   8468   1380    901    464       N  
ATOM   2243  CA  ARG A1297     -12.894  79.072 338.705  1.00 78.13           C  
ANISOU 2243  CA  ARG A1297    10502  10104   9078   1454   1013    601       C  
ATOM   2244  C   ARG A1297     -12.874  79.448 337.229  1.00 81.76           C  
ANISOU 2244  C   ARG A1297    10819  10539   9709   1473    938    585       C  
ATOM   2245  O   ARG A1297     -13.477  78.770 336.397  1.00 83.79           O  
ANISOU 2245  O   ARG A1297    10826  10916  10093   1406    902    688       O  
ATOM   2246  CB  ARG A1297     -14.005  79.834 339.432  1.00 82.96           C  
ANISOU 2246  CB  ARG A1297    11150  10804   9568   1662   1277    654       C  
ATOM   2247  CG  ARG A1297     -14.429  79.210 340.753  1.00 89.20           C  
ANISOU 2247  CG  ARG A1297    11991  11691  10212   1638   1381    728       C  
ATOM   2248  CD  ARG A1297     -15.598  79.959 341.374  1.00 95.26           C  
ANISOU 2248  CD  ARG A1297    12769  12559  10867   1869   1671    796       C  
ATOM   2249  NE  ARG A1297     -15.997  79.383 342.655  1.00 97.35           N  
ANISOU 2249  NE  ARG A1297    13091  12918  10978   1843   1781    865       N  
ATOM   2250  CZ  ARG A1297     -17.032  79.804 343.376  1.00100.19           C  
ANISOU 2250  CZ  ARG A1297    13454  13392  11222   2030   2049    947       C  
ATOM   2251  NH1 ARG A1297     -17.780  80.809 342.942  1.00101.29           N  
ANISOU 2251  NH1 ARG A1297    13536  13566  11383   2282   2242    983       N  
ATOM   2252  NH2 ARG A1297     -17.320  79.219 344.530  1.00103.31           N  
ANISOU 2252  NH2 ARG A1297    13909  13872  11473   1985   2138   1008       N  
ATOM   2253  N   ALA A1298     -12.168  80.529 336.911  1.00 80.89           N  
ANISOU 2253  N   ALA A1298    10880  10273   9582   1538    917    453       N  
ATOM   2254  CA  ALA A1298     -12.046  80.991 335.535  1.00 76.99           C  
ANISOU 2254  CA  ALA A1298    10284   9735   9232   1565    850    432       C  
ATOM   2255  C   ALA A1298     -11.179  80.041 334.716  1.00 78.93           C  
ANISOU 2255  C   ALA A1298    10432   9946   9610   1361    620    410       C  
ATOM   2256  O   ALA A1298     -11.379  79.886 333.511  1.00 79.47           O  
ANISOU 2256  O   ALA A1298    10328  10053   9815   1333    557    446       O  
ATOM   2257  CB  ALA A1298     -11.473  82.398 335.496  1.00 71.57           C  
ANISOU 2257  CB  ALA A1298     9853   8864   8476   1671    909    294       C  
ATOM   2258  N   ALA A1299     -10.216  79.406 335.376  1.00 80.14           N  
ANISOU 2258  N   ALA A1299    10701  10038   9708   1230    505    363       N  
ATOM   2259  CA  ALA A1299      -9.333  78.454 334.712  1.00 78.38           C  
ANISOU 2259  CA  ALA A1299    10411   9771   9597   1075    320    359       C  
ATOM   2260  C   ALA A1299     -10.083  77.173 334.366  1.00 79.83           C  
ANISOU 2260  C   ALA A1299    10407  10052   9872    981    323    488       C  
ATOM   2261  O   ALA A1299      -9.714  76.457 333.435  1.00 81.07           O  
ANISOU 2261  O   ALA A1299    10487  10167  10148    871    217    494       O  
ATOM   2262  CB  ALA A1299      -8.130  78.145 335.586  1.00 78.12           C  
ANISOU 2262  CB  ALA A1299    10536   9683   9462    998    215    311       C  
ATOM   2263  N   LEU A1300     -11.137  76.890 335.123  1.00 81.43           N  
ANISOU 2263  N   LEU A1300    10557  10380  10004   1010    458    586       N  
ATOM   2264  CA  LEU A1300     -11.980  75.731 334.862  1.00 82.12           C  
ANISOU 2264  CA  LEU A1300    10473  10577  10151    882    483    710       C  
ATOM   2265  C   LEU A1300     -12.864  75.988 333.646  1.00 83.49           C  
ANISOU 2265  C   LEU A1300    10424  10876  10422    875    501    754       C  
ATOM   2266  O   LEU A1300     -13.187  75.070 332.891  1.00 84.81           O  
ANISOU 2266  O   LEU A1300    10463  11095  10667    698    451    807       O  
ATOM   2267  CB  LEU A1300     -12.837  75.402 336.086  1.00 79.51           C  
ANISOU 2267  CB  LEU A1300    10142  10368   9700    905    630    810       C  
ATOM   2268  CG  LEU A1300     -13.666  74.117 336.025  1.00 73.74           C  
ANISOU 2268  CG  LEU A1300     9271   9747   9000    725    669    941       C  
ATOM   2269  CD1 LEU A1300     -12.763  72.896 335.929  1.00 68.84           C  
ANISOU 2269  CD1 LEU A1300     8768   8962   8425    563    558    937       C  
ATOM   2270  CD2 LEU A1300     -14.589  74.014 337.229  1.00 75.78           C  
ANISOU 2270  CD2 LEU A1300     9513  10151   9131    771    838   1044       C  
ATOM   2271  N   ILE A1301     -13.248  77.248 333.465  1.00 83.89           N  
ANISOU 2271  N   ILE A1301    10447  10975  10453   1064    580    737       N  
ATOM   2272  CA  ILE A1301     -14.073  77.654 332.332  1.00 82.47           C  
ANISOU 2272  CA  ILE A1301    10043  10947  10346   1105    600    805       C  
ATOM   2273  C   ILE A1301     -13.291  77.530 331.026  1.00 80.40           C  
ANISOU 2273  C   ILE A1301     9772  10576  10200    995    434    726       C  
ATOM   2274  O   ILE A1301     -13.856  77.228 329.975  1.00 81.86           O  
ANISOU 2274  O   ILE A1301     9759  10896  10448    898    391    788       O  
ATOM   2275  CB  ILE A1301     -14.581  79.100 332.503  1.00 84.97           C  
ANISOU 2275  CB  ILE A1301    10377  11305  10604   1390    755    821       C  
ATOM   2276  CG1 ILE A1301     -15.315  79.247 333.838  1.00 91.42           C  
ANISOU 2276  CG1 ILE A1301    11232  12213  11291   1517    947    892       C  
ATOM   2277  CG2 ILE A1301     -15.491  79.496 331.353  1.00 84.53           C  
ANISOU 2277  CG2 ILE A1301    10056  11452  10610   1464    780    937       C  
ATOM   2278  CD1 ILE A1301     -15.719  80.668 334.168  1.00 94.87           C  
ANISOU 2278  CD1 ILE A1301    11769  12631  11648   1825   1145    896       C  
ATOM   2279  N   ASN A1302     -11.984  77.756 331.099  1.00 76.17           N  
ANISOU 2279  N   ASN A1302     9445   9820   9677    996    340    593       N  
ATOM   2280  CA  ASN A1302     -11.123  77.606 329.933  1.00 67.68           C  
ANISOU 2280  CA  ASN A1302     8377   8631   8707    899    194    517       C  
ATOM   2281  C   ASN A1302     -11.010  76.151 329.491  1.00 67.75           C  
ANISOU 2281  C   ASN A1302     8335   8630   8777    674    114    547       C  
ATOM   2282  O   ASN A1302     -10.963  75.864 328.297  1.00 71.80           O  
ANISOU 2282  O   ASN A1302     8768   9143   9368    566     41    534       O  
ATOM   2283  CB  ASN A1302      -9.732  78.175 330.218  1.00 61.93           C  
ANISOU 2283  CB  ASN A1302     7864   7706   7961    943    122    385       C  
ATOM   2284  CG  ASN A1302      -9.662  79.674 330.005  1.00 60.40           C  
ANISOU 2284  CG  ASN A1302     7749   7460   7740   1106    178    322       C  
ATOM   2285  OD1 ASN A1302     -10.686  80.340 329.854  1.00 64.66           O  
ANISOU 2285  OD1 ASN A1302     8203   8103   8261   1247    300    392       O  
ATOM   2286  ND2 ASN A1302      -8.448  80.213 329.990  1.00 55.51           N  
ANISOU 2286  ND2 ASN A1302     7296   6686   7109   1091    101    201       N  
ATOM   2287  N   MET A1303     -10.971  75.237 330.455  1.00 68.45           N  
ANISOU 2287  N   MET A1303     8496   8696   8817    602    144    588       N  
ATOM   2288  CA  MET A1303     -10.851  73.815 330.149  1.00 71.53           C  
ANISOU 2288  CA  MET A1303     8902   9026   9249    397    107    621       C  
ATOM   2289  C   MET A1303     -12.075  73.289 329.407  1.00 73.41           C  
ANISOU 2289  C   MET A1303     8952   9438   9502    222    143    700       C  
ATOM   2290  O   MET A1303     -11.946  72.509 328.464  1.00 76.90           O  
ANISOU 2290  O   MET A1303     9398   9822   9997     35     89    680       O  
ATOM   2291  CB  MET A1303     -10.631  73.001 331.425  1.00 76.49           C  
ANISOU 2291  CB  MET A1303     9662   9596   9806    380    156    673       C  
ATOM   2292  CG  MET A1303      -9.196  73.003 331.920  1.00 79.85           C  
ANISOU 2292  CG  MET A1303    10265   9859  10218    467     79    617       C  
ATOM   2293  SD  MET A1303      -8.882  71.710 333.142  1.00 76.90           S  
ANISOU 2293  SD  MET A1303    10037   9414   9767    429    124    720       S  
ATOM   2294  CE  MET A1303      -9.191  70.236 332.166  1.00 56.95           C  
ANISOU 2294  CE  MET A1303     7525   6778   7333    211    156    769       C  
ATOM   2295  N   VAL A1304     -13.261  73.714 329.830  1.00 73.64           N  
ANISOU 2295  N   VAL A1304     8817   9694   9469    274    240    793       N  
ATOM   2296  CA  VAL A1304     -14.485  73.285 329.164  1.00 77.02           C  
ANISOU 2296  CA  VAL A1304     9014  10364   9886     93    265    892       C  
ATOM   2297  C   VAL A1304     -14.641  74.015 327.833  1.00 78.08           C  
ANISOU 2297  C   VAL A1304     8998  10602  10069    120    191    876       C  
ATOM   2298  O   VAL A1304     -15.407  73.592 326.968  1.00 80.70           O  
ANISOU 2298  O   VAL A1304     9146  11126  10389    -81    161    937       O  
ATOM   2299  CB  VAL A1304     -15.733  73.519 330.042  1.00 79.23           C  
ANISOU 2299  CB  VAL A1304     9121  10905  10077    160    404   1030       C  
ATOM   2300  CG1 VAL A1304     -15.514  72.949 331.433  1.00 77.51           C  
ANISOU 2300  CG1 VAL A1304     9075  10578   9797    169    483   1044       C  
ATOM   2301  CG2 VAL A1304     -16.068  74.996 330.119  1.00 83.72           C  
ANISOU 2301  CG2 VAL A1304     9593  11591  10627    470    470   1057       C  
ATOM   2302  N   PHE A1305     -13.908  75.114 327.674  1.00 75.22           N  
ANISOU 2302  N   PHE A1305     8718  10119   9742    348    161    797       N  
ATOM   2303  CA  PHE A1305     -13.856  75.820 326.400  1.00 71.95           C  
ANISOU 2303  CA  PHE A1305     8210   9754   9376    390     90    776       C  
ATOM   2304  C   PHE A1305     -13.000  75.045 325.405  1.00 68.83           C  
ANISOU 2304  C   PHE A1305     7918   9188   9047    183    -32    676       C  
ATOM   2305  O   PHE A1305     -13.274  75.039 324.205  1.00 73.14           O  
ANISOU 2305  O   PHE A1305     8346   9837   9606     72    -97    684       O  
ATOM   2306  CB  PHE A1305     -13.295  77.234 326.577  1.00 70.55           C  
ANISOU 2306  CB  PHE A1305     8136   9462   9207    681    119    718       C  
ATOM   2307  CG  PHE A1305     -14.337  78.278 326.875  1.00 72.62           C  
ANISOU 2307  CG  PHE A1305     8255   9927   9411    919    254    837       C  
ATOM   2308  CD1 PHE A1305     -15.675  78.045 326.605  1.00 79.12           C  
ANISOU 2308  CD1 PHE A1305     8788  11081  10193    876    305   1004       C  
ATOM   2309  CD2 PHE A1305     -13.971  79.501 327.415  1.00 68.83           C  
ANISOU 2309  CD2 PHE A1305     7939   9312   8903   1183    345    788       C  
ATOM   2310  CE1 PHE A1305     -16.631  79.011 326.876  1.00 80.36           C  
ANISOU 2310  CE1 PHE A1305     8796  11443  10295   1144    452   1144       C  
ATOM   2311  CE2 PHE A1305     -14.919  80.469 327.687  1.00 69.72           C  
ANISOU 2311  CE2 PHE A1305     7957   9575   8956   1442    509    906       C  
ATOM   2312  CZ  PHE A1305     -16.250  80.224 327.418  1.00 75.84           C  
ANISOU 2312  CZ  PHE A1305     8419  10693   9704   1448    568   1095       C  
ATOM   2313  N   GLN A1306     -11.965  74.388 325.918  1.00 64.79           N  
ANISOU 2313  N   GLN A1306     7627   8428   8562    144    -54    594       N  
ATOM   2314  CA  GLN A1306     -10.973  73.725 325.078  1.00 62.11           C  
ANISOU 2314  CA  GLN A1306     7424   7888   8287     16   -137    500       C  
ATOM   2315  C   GLN A1306     -11.356  72.297 324.690  1.00 71.74           C  
ANISOU 2315  C   GLN A1306     8673   9093   9491   -278   -123    521       C  
ATOM   2316  O   GLN A1306     -11.068  71.859 323.575  1.00 82.24           O  
ANISOU 2316  O   GLN A1306    10048  10353  10848   -431   -173    463       O  
ATOM   2317  CB  GLN A1306      -9.612  73.713 325.784  1.00 55.16           C  
ANISOU 2317  CB  GLN A1306     6752   6772   7435    142   -156    429       C  
ATOM   2318  CG  GLN A1306      -8.992  75.091 325.966  1.00 50.52           C  
ANISOU 2318  CG  GLN A1306     6189   6153   6852    361   -184    370       C  
ATOM   2319  CD  GLN A1306      -7.745  75.060 326.832  1.00 52.22           C  
ANISOU 2319  CD  GLN A1306     6574   6212   7057    445   -212    320       C  
ATOM   2320  OE1 GLN A1306      -7.152  74.002 327.051  1.00 52.20           O  
ANISOU 2320  OE1 GLN A1306     6663   6103   7068    376   -223    335       O  
ATOM   2321  NE2 GLN A1306      -7.343  76.224 327.333  1.00 51.26           N  
ANISOU 2321  NE2 GLN A1306     6501   6081   6894    592   -215    271       N  
ATOM   2322  N   MET A1307     -11.997  71.571 325.601  1.00 70.71           N  
ANISOU 2322  N   MET A1307     8546   9016   9303   -373    -42    599       N  
ATOM   2323  CA  MET A1307     -12.286  70.159 325.361  1.00 73.38           C  
ANISOU 2323  CA  MET A1307     8981   9288   9614   -674     -2    611       C  
ATOM   2324  C   MET A1307     -13.718  69.767 325.718  1.00 78.62           C  
ANISOU 2324  C   MET A1307     9471  10214  10187   -871     65    724       C  
ATOM   2325  O   MET A1307     -14.076  68.590 325.667  1.00 79.59           O  
ANISOU 2325  O   MET A1307     9687  10289  10263  -1160    118    741       O  
ATOM   2326  CB  MET A1307     -11.301  69.286 326.143  1.00 75.67           C  
ANISOU 2326  CB  MET A1307     9544   9284   9924   -630     49    594       C  
ATOM   2327  CG  MET A1307     -11.402  69.435 327.652  1.00 78.37           C  
ANISOU 2327  CG  MET A1307     9898   9659  10221   -471    112    670       C  
ATOM   2328  SD  MET A1307      -9.964  68.780 328.526  1.00 86.51           S  
ANISOU 2328  SD  MET A1307    11206  10392  11270   -317    132    669       S  
ATOM   2329  CE  MET A1307      -9.918  67.104 327.896  1.00118.03           C  
ANISOU 2329  CE  MET A1307    15421  14154  15270   -587    219    677       C  
ATOM   2330  N   GLY A1308     -14.536  70.751 326.074  1.00 82.91           N  
ANISOU 2330  N   GLY A1308     9770  11035  10697   -718     81    809       N  
ATOM   2331  CA  GLY A1308     -15.921  70.489 326.419  1.00 90.51           C  
ANISOU 2331  CA  GLY A1308    10511  12308  11570   -875    151    943       C  
ATOM   2332  C   GLY A1308     -16.095  70.078 327.867  1.00 94.17           C  
ANISOU 2332  C   GLY A1308    11058  12728  11992   -825    267   1007       C  
ATOM   2333  O   GLY A1308     -15.118  69.905 328.595  1.00 93.00           O  
ANISOU 2333  O   GLY A1308    11152  12307  11876   -686    283    951       O  
ATOM   2334  N   GLU A1309     -17.347  69.916 328.284  1.00102.28           N  
ANISOU 2334  N   GLU A1309    11869  14056  12935   -943    347   1140       N  
ATOM   2335  CA  GLU A1309     -17.661  69.570 329.666  1.00107.47           C  
ANISOU 2335  CA  GLU A1309    12580  14716  13537   -900    472   1219       C  
ATOM   2336  C   GLU A1309     -17.552  68.069 329.925  1.00106.76           C  
ANISOU 2336  C   GLU A1309    12712  14435  13416  -1217    522   1215       C  
ATOM   2337  O   GLU A1309     -17.251  67.647 331.040  1.00109.80           O  
ANISOU 2337  O   GLU A1309    13276  14664  13777  -1146    605   1241       O  
ATOM   2338  CB  GLU A1309     -19.062  70.066 330.029  1.00117.21           C  
ANISOU 2338  CB  GLU A1309    13474  16370  14689   -871    561   1382       C  
ATOM   2339  CG  GLU A1309     -20.134  69.684 329.022  1.00127.57           C  
ANISOU 2339  CG  GLU A1309    14501  18024  15946  -1199    521   1468       C  
ATOM   2340  CD  GLU A1309     -21.486  70.280 329.355  1.00135.71           C  
ANISOU 2340  CD  GLU A1309    15141  19525  16896  -1115    612   1663       C  
ATOM   2341  OE1 GLU A1309     -21.687  70.691 330.517  1.00137.36           O  
ANISOU 2341  OE1 GLU A1309    15350  19759  17081   -865    743   1729       O  
ATOM   2342  OE2 GLU A1309     -22.348  70.340 328.452  1.00140.25           O  
ANISOU 2342  OE2 GLU A1309    15404  20465  17420  -1293    557   1760       O  
ATOM   2343  N   THR A1310     -17.801  67.267 328.895  1.00105.11           N  
ANISOU 2343  N   THR A1310    12515  14230  13192  -1572    481   1184       N  
ATOM   2344  CA  THR A1310     -17.687  65.818 329.021  1.00102.87           C  
ANISOU 2344  CA  THR A1310    12501  13714  12871  -1895    555   1169       C  
ATOM   2345  C   THR A1310     -16.223  65.394 329.021  1.00 99.37           C  
ANISOU 2345  C   THR A1310    12428  12818  12508  -1752    544   1060       C  
ATOM   2346  O   THR A1310     -15.878  64.314 329.500  1.00 99.35           O  
ANISOU 2346  O   THR A1310    12711  12550  12486  -1863    642   1071       O  
ATOM   2347  CB  THR A1310     -18.428  65.086 327.887  1.00102.85           C  
ANISOU 2347  CB  THR A1310    12433  13848  12795  -2364    529   1155       C  
ATOM   2348  OG1 THR A1310     -17.908  65.510 326.621  1.00103.82           O  
ANISOU 2348  OG1 THR A1310    12550  13928  12970  -2345    402   1045       O  
ATOM   2349  CG2 THR A1310     -19.918  65.382 327.943  1.00102.50           C  
ANISOU 2349  CG2 THR A1310    11983  14312  12649  -2537    542   1301       C  
ATOM   2350  N   GLY A1311     -15.367  66.255 328.481  1.00 95.53           N  
ANISOU 2350  N   GLY A1311    11931  12256  12108  -1495    436    971       N  
ATOM   2351  CA  GLY A1311     -13.944  65.980 328.420  1.00 93.58           C  
ANISOU 2351  CA  GLY A1311    11975  11643  11939  -1330    417    886       C  
ATOM   2352  C   GLY A1311     -13.242  66.258 329.734  1.00 91.63           C  
ANISOU 2352  C   GLY A1311    11826  11292  11700  -1017    447    929       C  
ATOM   2353  O   GLY A1311     -12.334  65.527 330.130  1.00 90.20           O  
ANISOU 2353  O   GLY A1311    11904  10835  11534   -950    490    934       O  
ATOM   2354  N   VAL A1312     -13.664  67.319 330.414  1.00 93.17           N  
ANISOU 2354  N   VAL A1312    11819  11714  11868   -818    433    969       N  
ATOM   2355  CA  VAL A1312     -13.067  67.692 331.692  1.00 91.10           C  
ANISOU 2355  CA  VAL A1312    11646  11391  11578   -549    455    999       C  
ATOM   2356  C   VAL A1312     -13.602  66.821 332.825  1.00 90.84           C  
ANISOU 2356  C   VAL A1312    11701  11359  11456   -644    584   1116       C  
ATOM   2357  O   VAL A1312     -12.976  66.706 333.878  1.00 90.46           O  
ANISOU 2357  O   VAL A1312    11800  11205  11366   -477    611   1156       O  
ATOM   2358  CB  VAL A1312     -13.323  69.176 332.029  1.00 95.32           C  
ANISOU 2358  CB  VAL A1312    11992  12131  12094   -307    424    985       C  
ATOM   2359  CG1 VAL A1312     -12.750  70.072 330.945  1.00 95.75           C  
ANISOU 2359  CG1 VAL A1312    11987  12163  12232   -206    308    878       C  
ATOM   2360  CG2 VAL A1312     -14.808  69.435 332.208  1.00 99.73           C  
ANISOU 2360  CG2 VAL A1312    12306  12998  12589   -388    510   1081       C  
ATOM   2361  N   ALA A1313     -14.759  66.205 332.601  1.00 87.54           N  
ANISOU 2361  N   ALA A1313    11185  11081  10993   -931    661   1179       N  
ATOM   2362  CA  ALA A1313     -15.364  65.330 333.597  1.00 85.06           C  
ANISOU 2362  CA  ALA A1313    10954  10776  10590  -1069    799   1295       C  
ATOM   2363  C   ALA A1313     -14.741  63.940 333.545  1.00 85.24           C  
ANISOU 2363  C   ALA A1313    11310  10459  10619  -1226    865   1305       C  
ATOM   2364  O   ALA A1313     -15.033  63.085 334.380  1.00 86.77           O  
ANISOU 2364  O   ALA A1313    11648  10581  10740  -1329    991   1405       O  
ATOM   2365  CB  ALA A1313     -16.866  65.248 333.390  1.00 86.59           C  
ANISOU 2365  CB  ALA A1313    10890  11290  10720  -1338    861   1371       C  
ATOM   2366  N   GLY A1314     -13.883  63.723 332.554  1.00 85.71           N  
ANISOU 2366  N   GLY A1314    11507  10300  10760  -1229    799   1208       N  
ATOM   2367  CA  GLY A1314     -13.191  62.457 332.402  1.00 87.28           C  
ANISOU 2367  CA  GLY A1314    12054  10140  10969  -1322    887   1217       C  
ATOM   2368  C   GLY A1314     -11.996  62.357 333.329  1.00 84.29           C  
ANISOU 2368  C   GLY A1314    11860   9569  10597   -988    897   1279       C  
ATOM   2369  O   GLY A1314     -11.484  61.267 333.581  1.00 82.07           O  
ANISOU 2369  O   GLY A1314    11874   9008  10302   -995   1011   1349       O  
ATOM   2370  N   PHE A1315     -11.548  63.502 333.832  1.00 90.50           N  
ANISOU 2370  N   PHE A1315    12481  10514  11392   -699    783   1263       N  
ATOM   2371  CA  PHE A1315     -10.455  63.535 334.796  1.00 93.86           C  
ANISOU 2371  CA  PHE A1315    13030  10844  11789   -405    764   1331       C  
ATOM   2372  C   PHE A1315     -10.998  63.397 336.215  1.00 96.04           C  
ANISOU 2372  C   PHE A1315    13317  11231  11944   -374    850   1455       C  
ATOM   2373  O   PHE A1315     -11.160  64.388 336.927  1.00 94.83           O  
ANISOU 2373  O   PHE A1315    13010  11290  11732   -230    796   1446       O  
ATOM   2374  CB  PHE A1315      -9.648  64.829 334.663  1.00 97.22           C  
ANISOU 2374  CB  PHE A1315    13304  11382  12253   -158    601   1240       C  
ATOM   2375  CG  PHE A1315      -9.063  65.047 333.293  1.00 99.50           C  
ANISOU 2375  CG  PHE A1315    13573  11577  12656   -170    517   1124       C  
ATOM   2376  CD1 PHE A1315      -8.089  64.196 332.796  1.00100.60           C  
ANISOU 2376  CD1 PHE A1315    13915  11459  12849   -126    548   1142       C  
ATOM   2377  CD2 PHE A1315      -9.476  66.113 332.511  1.00 96.81           C  
ANISOU 2377  CD2 PHE A1315    13019  11404  12362   -201    424   1011       C  
ATOM   2378  CE1 PHE A1315      -7.548  64.399 331.539  1.00 97.97           C  
ANISOU 2378  CE1 PHE A1315    13569  11042  12612   -134    485   1035       C  
ATOM   2379  CE2 PHE A1315      -8.938  66.321 331.255  1.00 93.42           C  
ANISOU 2379  CE2 PHE A1315    12577  10894  12026   -214    349    909       C  
ATOM   2380  CZ  PHE A1315      -7.973  65.463 330.768  1.00 94.82           C  
ANISOU 2380  CZ  PHE A1315    12955  10819  12255   -190    378    914       C  
ATOM   2381  N   THR A1316     -11.280  62.161 336.616  1.00 98.50           N  
ANISOU 2381  N   THR A1316    13839  11381  12207   -515   1001   1568       N  
ATOM   2382  CA  THR A1316     -11.871  61.891 337.921  1.00 99.91           C  
ANISOU 2382  CA  THR A1316    14047  11651  12262   -521   1104   1699       C  
ATOM   2383  C   THR A1316     -10.939  62.286 339.063  1.00102.94           C  
ANISOU 2383  C   THR A1316    14476  12071  12566   -202   1046   1773       C  
ATOM   2384  O   THR A1316     -11.226  63.225 339.805  1.00104.40           O  
ANISOU 2384  O   THR A1316    14508  12487  12672    -99   1000   1757       O  
ATOM   2385  CB  THR A1316     -12.244  60.405 338.068  1.00 98.76           C  
ANISOU 2385  CB  THR A1316    14172  11276  12078   -746   1293   1813       C  
ATOM   2386  OG1 THR A1316     -11.065  59.600 337.948  1.00100.84           O  
ANISOU 2386  OG1 THR A1316    14719  11222  12374   -590   1331   1872       O  
ATOM   2387  CG2 THR A1316     -13.242  59.998 336.996  1.00 96.00           C  
ANISOU 2387  CG2 THR A1316    13781  10928  11766  -1134   1349   1735       C  
ATOM   2388  N   ASN A1317      -9.822  61.576 339.197  1.00105.56           N  
ANISOU 2388  N   ASN A1317    15020  12184  12902    -44   1055   1860       N  
ATOM   2389  CA  ASN A1317      -8.869  61.861 340.266  1.00105.30           C  
ANISOU 2389  CA  ASN A1317    15016  12223  12769    240    984   1957       C  
ATOM   2390  C   ASN A1317      -7.934  63.015 339.919  1.00 95.63           C  
ANISOU 2390  C   ASN A1317    13629  11124  11581    423    788   1840       C  
ATOM   2391  O   ASN A1317      -6.758  63.008 340.281  1.00 94.49           O  
ANISOU 2391  O   ASN A1317    13529  10977  11396    637    708   1914       O  
ATOM   2392  CB  ASN A1317      -8.055  60.611 340.611  1.00112.87           C  
ANISOU 2392  CB  ASN A1317    16246  12938  13700    366   1085   2144       C  
ATOM   2393  CG  ASN A1317      -7.384  60.000 339.402  1.00119.80           C  
ANISOU 2393  CG  ASN A1317    17251  13551  14715    375   1112   2113       C  
ATOM   2394  OD1 ASN A1317      -7.928  60.026 338.299  1.00123.62           O  
ANISOU 2394  OD1 ASN A1317    17703  13965  15302    160   1127   1971       O  
ATOM   2395  ND2 ASN A1317      -6.197  59.440 339.602  1.00123.50           N  
ANISOU 2395  ND2 ASN A1317    17863  13888  15173    634   1127   2258       N  
ATOM   2396  N   SER A1318      -8.468  63.998 339.202  1.00 83.43           N  
ANISOU 2396  N   SER A1318    11892   9703  10105    331    715   1671       N  
ATOM   2397  CA  SER A1318      -7.782  65.261 338.976  1.00 78.99           C  
ANISOU 2397  CA  SER A1318    11184   9275   9556    468    548   1548       C  
ATOM   2398  C   SER A1318      -8.648  66.376 339.541  1.00 74.33           C  
ANISOU 2398  C   SER A1318    10451   8909   8881    451    545   1472       C  
ATOM   2399  O   SER A1318      -8.149  67.335 340.129  1.00 70.77           O  
ANISOU 2399  O   SER A1318     9966   8586   8338    580    455   1421       O  
ATOM   2400  CB  SER A1318      -7.507  65.486 337.490  1.00 82.18           C  
ANISOU 2400  CB  SER A1318    11518   9585  10120    415    482   1420       C  
ATOM   2401  OG  SER A1318      -6.549  64.565 337.001  1.00 85.34           O  
ANISOU 2401  OG  SER A1318    12064   9774  10586    481    497   1487       O  
ATOM   2402  N   LEU A1319      -9.956  66.233 339.351  1.00 75.53           N  
ANISOU 2402  N   LEU A1319    10531   9115   9054    283    656   1469       N  
ATOM   2403  CA  LEU A1319     -10.934  67.102 339.990  1.00 76.10           C  
ANISOU 2403  CA  LEU A1319    10479   9402   9035    291    712   1445       C  
ATOM   2404  C   LEU A1319     -10.983  66.782 341.478  1.00 77.43           C  
ANISOU 2404  C   LEU A1319    10766   9625   9031    355    790   1566       C  
ATOM   2405  O   LEU A1319     -11.245  67.651 342.309  1.00 75.97           O  
ANISOU 2405  O   LEU A1319    10549   9595   8720    449    809   1538       O  
ATOM   2406  CB  LEU A1319     -12.315  66.925 339.358  1.00 73.51           C  
ANISOU 2406  CB  LEU A1319    10000   9163   8768     91    813   1449       C  
ATOM   2407  CG  LEU A1319     -12.426  67.218 337.861  1.00 65.75           C  
ANISOU 2407  CG  LEU A1319     8885   8167   7932     -1    739   1343       C  
ATOM   2408  CD1 LEU A1319     -13.801  66.828 337.344  1.00 66.52           C  
ANISOU 2408  CD1 LEU A1319     8828   8398   8050   -243    835   1386       C  
ATOM   2409  CD2 LEU A1319     -12.139  68.684 337.578  1.00 59.27           C  
ANISOU 2409  CD2 LEU A1319     7948   7445   7129    177    643   1222       C  
ATOM   2410  N   ARG A1320     -10.723  65.517 341.798  1.00 81.66           N  
ANISOU 2410  N   ARG A1320    11463  10017   9549    309    851   1704       N  
ATOM   2411  CA  ARG A1320     -10.624  65.060 343.177  1.00 86.80           C  
ANISOU 2411  CA  ARG A1320    12251  10700  10030    379    919   1847       C  
ATOM   2412  C   ARG A1320      -9.492  65.790 343.892  1.00 90.48           C  
ANISOU 2412  C   ARG A1320    12753  11253  10373    584    780   1827       C  
ATOM   2413  O   ARG A1320      -9.512  65.953 345.111  1.00 95.67           O  
ANISOU 2413  O   ARG A1320    13475  12030  10845    651    808   1893       O  
ATOM   2414  CB  ARG A1320     -10.396  63.545 343.221  1.00 89.69           C  
ANISOU 2414  CB  ARG A1320    12815  10848  10414    318   1014   2010       C  
ATOM   2415  CG  ARG A1320     -10.395  62.946 344.620  1.00 94.25           C  
ANISOU 2415  CG  ARG A1320    13545  11451  10813    383   1107   2190       C  
ATOM   2416  CD  ARG A1320      -9.935  61.494 344.609  1.00 96.10           C  
ANISOU 2416  CD  ARG A1320    14017  11429  11069    382   1203   2364       C  
ATOM   2417  NE  ARG A1320      -8.533  61.364 344.219  1.00 96.43           N  
ANISOU 2417  NE  ARG A1320    14115  11362  11160    583   1085   2392       N  
ATOM   2418  CZ  ARG A1320      -7.698  60.459 344.719  1.00 99.64           C  
ANISOU 2418  CZ  ARG A1320    14709  11644  11505    748   1126   2592       C  
ATOM   2419  NH1 ARG A1320      -8.120  59.600 345.637  1.00104.31           N  
ANISOU 2419  NH1 ARG A1320    15477  12177  11980    727   1282   2773       N  
ATOM   2420  NH2 ARG A1320      -6.439  60.415 344.305  1.00 98.54           N  
ANISOU 2420  NH2 ARG A1320    14574  11453  11414    949   1021   2628       N  
ATOM   2421  N   MET A1321      -8.510  66.235 343.116  1.00 89.16           N  
ANISOU 2421  N   MET A1321    12541  11041  10295    659    630   1735       N  
ATOM   2422  CA  MET A1321      -7.346  66.925 343.654  1.00 87.67           C  
ANISOU 2422  CA  MET A1321    12364  10958   9987    804    478   1711       C  
ATOM   2423  C   MET A1321      -7.589  68.423 343.786  1.00 84.16           C  
ANISOU 2423  C   MET A1321    11840  10664   9475    809    428   1532       C  
ATOM   2424  O   MET A1321      -7.135  69.055 344.740  1.00 86.51           O  
ANISOU 2424  O   MET A1321    12194  11096   9581    866    370   1514       O  
ATOM   2425  CB  MET A1321      -6.130  66.668 342.769  1.00 87.45           C  
ANISOU 2425  CB  MET A1321    12321  10827  10078    877    354   1713       C  
ATOM   2426  CG  MET A1321      -5.908  65.202 342.467  1.00 89.85           C  
ANISOU 2426  CG  MET A1321    12744  10928  10467    895    444   1879       C  
ATOM   2427  SD  MET A1321      -5.687  64.249 343.977  1.00 88.92           S  
ANISOU 2427  SD  MET A1321    12791  10847  10147   1002    521   2135       S  
ATOM   2428  CE  MET A1321      -4.132  64.925 344.538  1.00113.66           C  
ANISOU 2428  CE  MET A1321    15851  14203  13132   1189    303   2172       C  
ATOM   2429  N   LEU A1322      -8.302  68.989 342.818  1.00 81.64           N  
ANISOU 2429  N   LEU A1322    11405  10317   9297    745    460   1405       N  
ATOM   2430  CA  LEU A1322      -8.641  70.406 342.851  1.00 80.76           C  
ANISOU 2430  CA  LEU A1322    11244  10309   9134    776    458   1249       C  
ATOM   2431  C   LEU A1322      -9.638  70.682 343.969  1.00 84.21           C  
ANISOU 2431  C   LEU A1322    11724  10866   9407    789    612   1281       C  
ATOM   2432  O   LEU A1322      -9.635  71.756 344.571  1.00 88.30           O  
ANISOU 2432  O   LEU A1322    12304  11465   9780    850    627   1183       O  
ATOM   2433  CB  LEU A1322      -9.211  70.853 341.506  1.00 76.03           C  
ANISOU 2433  CB  LEU A1322    10500   9664   8726    732    469   1148       C  
ATOM   2434  CG  LEU A1322      -8.307  70.621 340.296  1.00 71.57           C  
ANISOU 2434  CG  LEU A1322     9895   8975   8325    713    336   1103       C  
ATOM   2435  CD1 LEU A1322      -8.990  71.089 339.023  1.00 73.16           C  
ANISOU 2435  CD1 LEU A1322     9954   9160   8684    660    353   1013       C  
ATOM   2436  CD2 LEU A1322      -6.971  71.324 340.483  1.00 69.09           C  
ANISOU 2436  CD2 LEU A1322     9634   8680   7937    790    183   1030       C  
ATOM   2437  N   GLN A1323     -10.486  69.697 344.242  1.00 81.07           N  
ANISOU 2437  N   GLN A1323    11314  10468   9020    721    742   1417       N  
ATOM   2438  CA  GLN A1323     -11.492  69.814 345.287  1.00 79.72           C  
ANISOU 2438  CA  GLN A1323    11168  10424   8700    728    910   1474       C  
ATOM   2439  C   GLN A1323     -10.833  69.778 346.661  1.00 81.27           C  
ANISOU 2439  C   GLN A1323    11542  10678   8658    793    886   1528       C  
ATOM   2440  O   GLN A1323     -11.301  70.419 347.602  1.00 88.46           O  
ANISOU 2440  O   GLN A1323    12520  11701   9389    840    987   1502       O  
ATOM   2441  CB  GLN A1323     -12.525  68.694 345.153  1.00 80.60           C  
ANISOU 2441  CB  GLN A1323    11211  10528   8885    594   1051   1614       C  
ATOM   2442  CG  GLN A1323     -13.882  69.009 345.748  1.00 82.10           C  
ANISOU 2442  CG  GLN A1323    11318  10888   8989    586   1246   1655       C  
ATOM   2443  CD  GLN A1323     -14.956  68.057 345.259  1.00 86.92           C  
ANISOU 2443  CD  GLN A1323    11795  11527   9704    397   1362   1768       C  
ATOM   2444  OE1 GLN A1323     -14.748  67.309 344.304  1.00 87.17           O  
ANISOU 2444  OE1 GLN A1323    11805  11432   9884    261   1296   1777       O  
ATOM   2445  NE2 GLN A1323     -16.112  68.079 345.913  1.00 90.08           N  
ANISOU 2445  NE2 GLN A1323    12113  12101  10013    370   1544   1852       N  
ATOM   2446  N   GLN A1324      -9.738  69.031 346.766  1.00 75.09           N  
ANISOU 2446  N   GLN A1324    10838   9831   7862    804    758   1615       N  
ATOM   2447  CA  GLN A1324      -8.995  68.919 348.016  1.00 71.22           C  
ANISOU 2447  CA  GLN A1324    10492   9436   7133    862    703   1697       C  
ATOM   2448  C   GLN A1324      -7.833  69.908 348.060  1.00 71.34           C  
ANISOU 2448  C   GLN A1324    10534   9525   7048    902    517   1569       C  
ATOM   2449  O   GLN A1324      -6.993  69.852 348.960  1.00 72.66           O  
ANISOU 2449  O   GLN A1324    10792   9809   7009    928    420   1635       O  
ATOM   2450  CB  GLN A1324      -8.481  67.491 348.206  1.00 68.89           C  
ANISOU 2450  CB  GLN A1324    10262   9061   6853    878    689   1912       C  
ATOM   2451  CG  GLN A1324      -9.579  66.444 348.254  1.00 70.58           C  
ANISOU 2451  CG  GLN A1324    10497   9186   7134    793    883   2043       C  
ATOM   2452  CD  GLN A1324      -9.035  65.031 348.330  1.00 76.89           C  
ANISOU 2452  CD  GLN A1324    11412   9843   7958    818    898   2253       C  
ATOM   2453  OE1 GLN A1324      -7.912  64.808 348.786  1.00 78.08           O  
ANISOU 2453  OE1 GLN A1324    11632  10029   8005    944    784   2353       O  
ATOM   2454  NE2 GLN A1324      -9.827  64.068 347.877  1.00 81.27           N  
ANISOU 2454  NE2 GLN A1324    11995  10243   8640    696   1049   2329       N  
ATOM   2455  N   LYS A1325      -7.794  70.797 347.072  1.00 69.88           N  
ANISOU 2455  N   LYS A1325    10264   9287   6999    889    469   1396       N  
ATOM   2456  CA  LYS A1325      -6.799  71.867 346.995  1.00 68.40           C  
ANISOU 2456  CA  LYS A1325    10109   9155   6727    885    313   1247       C  
ATOM   2457  C   LYS A1325      -5.360  71.357 346.919  1.00 67.88           C  
ANISOU 2457  C   LYS A1325    10014   9135   6641    898    112   1337       C  
ATOM   2458  O   LYS A1325      -4.426  72.064 347.299  1.00 65.65           O  
ANISOU 2458  O   LYS A1325     9772   8980   6194    862    -29   1267       O  
ATOM   2459  CB  LYS A1325      -6.954  72.818 348.186  1.00 72.62           C  
ANISOU 2459  CB  LYS A1325    10806   9811   6974    868    366   1155       C  
ATOM   2460  CG  LYS A1325      -8.338  73.437 348.294  1.00 78.20           C  
ANISOU 2460  CG  LYS A1325    11542  10487   7684    902    591   1076       C  
ATOM   2461  CD  LYS A1325      -8.416  74.437 349.434  1.00 86.83           C  
ANISOU 2461  CD  LYS A1325    12848  11665   8480    895    668    966       C  
ATOM   2462  CE  LYS A1325      -9.819  75.010 349.559  1.00 92.14           C  
ANISOU 2462  CE  LYS A1325    13543  12310   9156    980    931    918       C  
ATOM   2463  NZ  LYS A1325     -10.290  75.603 348.277  1.00 93.59           N  
ANISOU 2463  NZ  LYS A1325    13592  12387   9581   1037    975    830       N  
ATOM   2464  N   ARG A1326      -5.188  70.134 346.428  1.00 67.76           N  
ANISOU 2464  N   ARG A1326     9938   9025   6784    944    113   1498       N  
ATOM   2465  CA  ARG A1326      -3.859  69.593 346.169  1.00 69.93           C  
ANISOU 2465  CA  ARG A1326    10160   9329   7079   1008    -45   1609       C  
ATOM   2466  C   ARG A1326      -3.417  69.979 344.765  1.00 72.20           C  
ANISOU 2466  C   ARG A1326    10332   9513   7588    995   -125   1486       C  
ATOM   2467  O   ARG A1326      -3.538  69.190 343.828  1.00 75.28           O  
ANISOU 2467  O   ARG A1326    10679   9735   8190   1023    -76   1540       O  
ATOM   2468  CB  ARG A1326      -3.842  68.073 346.332  1.00 71.04           C  
ANISOU 2468  CB  ARG A1326    10340   9381   7271   1096     32   1854       C  
ATOM   2469  CG  ARG A1326      -4.080  67.590 347.752  1.00 68.40           C  
ANISOU 2469  CG  ARG A1326    10124   9163   6701   1126     96   2016       C  
ATOM   2470  CD  ARG A1326      -3.762  66.110 347.886  1.00 69.83           C  
ANISOU 2470  CD  ARG A1326    10365   9247   6918   1244    157   2283       C  
ATOM   2471  NE  ARG A1326      -4.956  65.270 347.836  1.00 70.14           N  
ANISOU 2471  NE  ARG A1326    10500   9095   7056   1186    371   2343       N  
ATOM   2472  CZ  ARG A1326      -4.931  63.950 347.673  1.00 71.22           C  
ANISOU 2472  CZ  ARG A1326    10738   9046   7277   1247    484   2538       C  
ATOM   2473  NH1 ARG A1326      -3.773  63.320 347.522  1.00 72.05           N  
ANISOU 2473  NH1 ARG A1326    10855   9128   7394   1416    415   2703       N  
ATOM   2474  NH2 ARG A1326      -6.064  63.262 347.644  1.00 83.61           N  
ANISOU 2474  NH2 ARG A1326    12402  10454   8912   1135    679   2573       N  
ATOM   2475  N   TRP A1327      -2.906  71.198 344.627  1.00 71.13           N  
ANISOU 2475  N   TRP A1327    10172   9468   7386    935   -239   1316       N  
ATOM   2476  CA  TRP A1327      -2.619  71.769 343.315  1.00 69.79           C  
ANISOU 2476  CA  TRP A1327     9907   9201   7410    908   -297   1176       C  
ATOM   2477  C   TRP A1327      -1.480  71.062 342.585  1.00 71.88           C  
ANISOU 2477  C   TRP A1327    10066   9452   7796    979   -408   1286       C  
ATOM   2478  O   TRP A1327      -1.640  70.635 341.443  1.00 73.01           O  
ANISOU 2478  O   TRP A1327    10153   9423   8163   1002   -364   1275       O  
ATOM   2479  CB  TRP A1327      -2.296  73.255 343.454  1.00 69.60           C  
ANISOU 2479  CB  TRP A1327     9924   9266   7254    812   -375    975       C  
ATOM   2480  CG  TRP A1327      -3.215  73.984 344.389  1.00 70.73           C  
ANISOU 2480  CG  TRP A1327    10215   9439   7219    772   -253    882       C  
ATOM   2481  CD1 TRP A1327      -2.860  74.689 345.502  1.00 71.20           C  
ANISOU 2481  CD1 TRP A1327    10412   9649   6992    694   -295    823       C  
ATOM   2482  CD2 TRP A1327      -4.644  74.069 344.301  1.00 71.83           C  
ANISOU 2482  CD2 TRP A1327    10383   9470   7438    807    -55    847       C  
ATOM   2483  NE1 TRP A1327      -3.975  75.214 346.107  1.00 72.04           N  
ANISOU 2483  NE1 TRP A1327    10659   9714   7001    699   -115    744       N  
ATOM   2484  CE2 TRP A1327      -5.083  74.847 345.390  1.00 72.36           C  
ANISOU 2484  CE2 TRP A1327    10614   9611   7267    783     34    770       C  
ATOM   2485  CE3 TRP A1327      -5.593  73.566 343.405  1.00 70.55           C  
ANISOU 2485  CE3 TRP A1327    10117   9181   7508    844     57    880       C  
ATOM   2486  CZ2 TRP A1327      -6.429  75.135 345.607  1.00 74.39           C  
ANISOU 2486  CZ2 TRP A1327    10916   9820   7528    835    245    741       C  
ATOM   2487  CZ3 TRP A1327      -6.928  73.850 343.623  1.00 70.77           C  
ANISOU 2487  CZ3 TRP A1327    10162   9197   7531    868    241    857       C  
ATOM   2488  CH2 TRP A1327      -7.334  74.626 344.716  1.00 74.08           C  
ANISOU 2488  CH2 TRP A1327    10728   9693   7726    883    341    797       C  
ATOM   2489  N   ASP A1328      -0.332  70.949 343.246  1.00 77.01           N  
ANISOU 2489  N   ASP A1328    10682  10299   8278   1015   -545   1399       N  
ATOM   2490  CA  ASP A1328       0.862  70.366 342.641  1.00 77.16           C  
ANISOU 2490  CA  ASP A1328    10575  10357   8384   1117   -645   1529       C  
ATOM   2491  C   ASP A1328       0.638  68.929 342.180  1.00 80.97           C  
ANISOU 2491  C   ASP A1328    11087  10638   9041   1263   -514   1708       C  
ATOM   2492  O   ASP A1328       1.074  68.542 341.095  1.00 83.89           O  
ANISOU 2492  O   ASP A1328    11397  10880   9598   1328   -506   1723       O  
ATOM   2493  CB  ASP A1328       2.029  70.420 343.627  1.00 78.60           C  
ANISOU 2493  CB  ASP A1328    10693  10855   8315   1139   -807   1669       C  
ATOM   2494  CG  ASP A1328       2.387  71.837 344.022  1.00 81.72           C  
ANISOU 2494  CG  ASP A1328    11090  11445   8515    942   -942   1478       C  
ATOM   2495  OD1 ASP A1328       3.343  72.017 344.804  1.00 86.58           O  
ANISOU 2495  OD1 ASP A1328    11642  12362   8893    897  -1097   1567       O  
ATOM   2496  OD2 ASP A1328       1.714  72.772 343.543  1.00 80.04           O  
ANISOU 2496  OD2 ASP A1328    10950  11087   8373    827   -886   1244       O  
ATOM   2497  N   GLU A1329      -0.048  68.146 343.004  1.00 84.41           N  
ANISOU 2497  N   GLU A1329    11641  11028   9402   1301   -394   1839       N  
ATOM   2498  CA  GLU A1329      -0.309  66.748 342.688  1.00 83.33           C  
ANISOU 2498  CA  GLU A1329    11591  10671   9398   1411   -241   2012       C  
ATOM   2499  C   GLU A1329      -1.347  66.636 341.575  1.00 76.69           C  
ANISOU 2499  C   GLU A1329    10791   9568   8780   1299   -112   1864       C  
ATOM   2500  O   GLU A1329      -1.424  65.622 340.878  1.00 76.33           O  
ANISOU 2500  O   GLU A1329    10820   9300   8881   1342      3   1944       O  
ATOM   2501  CB  GLU A1329      -0.770  66.001 343.940  1.00 88.08           C  
ANISOU 2501  CB  GLU A1329    12324  11307   9837   1457   -144   2193       C  
ATOM   2502  CG  GLU A1329      -0.528  64.504 343.909  1.00 90.00           C  
ANISOU 2502  CG  GLU A1329    12681  11375  10140   1624    -11   2447       C  
ATOM   2503  CD  GLU A1329      -0.781  63.856 345.256  1.00 92.58           C  
ANISOU 2503  CD  GLU A1329    13130  11777  10267   1688     61   2654       C  
ATOM   2504  OE1 GLU A1329      -0.533  62.639 345.391  1.00 97.15           O  
ANISOU 2504  OE1 GLU A1329    13833  12217  10862   1848    183   2893       O  
ATOM   2505  OE2 GLU A1329      -1.226  64.568 346.181  1.00 88.85           O  
ANISOU 2505  OE2 GLU A1329    12652  11491   9614   1585     13   2582       O  
ATOM   2506  N   ALA A1330      -2.145  67.687 341.415  1.00 71.44           N  
ANISOU 2506  N   ALA A1330    10086   8936   8123   1155   -123   1656       N  
ATOM   2507  CA  ALA A1330      -3.085  67.777 340.305  1.00 67.31           C  
ANISOU 2507  CA  ALA A1330     9546   8240   7790   1043    -35   1517       C  
ATOM   2508  C   ALA A1330      -2.351  68.209 339.042  1.00 70.56           C  
ANISOU 2508  C   ALA A1330     9861   8600   8350   1052   -130   1410       C  
ATOM   2509  O   ALA A1330      -2.672  67.766 337.940  1.00 71.20           O  
ANISOU 2509  O   ALA A1330     9947   8504   8601   1004    -64   1371       O  
ATOM   2510  CB  ALA A1330      -4.203  68.750 340.627  1.00 63.52           C  
ANISOU 2510  CB  ALA A1330     9044   7840   7252    935      6   1374       C  
ATOM   2511  N   ALA A1331      -1.365  69.082 339.219  1.00 71.90           N  
ANISOU 2511  N   ALA A1331     9947   8936   8436   1087   -284   1360       N  
ATOM   2512  CA  ALA A1331      -0.550  69.565 338.113  1.00 55.42           C  
ANISOU 2512  CA  ALA A1331     7759   6832   6467   1093   -380   1269       C  
ATOM   2513  C   ALA A1331       0.208  68.418 337.459  1.00 59.88           C  
ANISOU 2513  C   ALA A1331     8329   7274   7149   1220   -344   1416       C  
ATOM   2514  O   ALA A1331       0.348  68.370 336.238  1.00 54.72           O  
ANISOU 2514  O   ALA A1331     7647   6486   6658   1207   -328   1343       O  
ATOM   2515  CB  ALA A1331       0.416  70.628 338.597  1.00 55.76           C  
ANISOU 2515  CB  ALA A1331     7724   7104   6360   1075   -547   1213       C  
ATOM   2516  N   VAL A1332       0.695  67.499 338.285  1.00 63.88           N  
ANISOU 2516  N   VAL A1332     8888   7825   7561   1357   -316   1632       N  
ATOM   2517  CA  VAL A1332       1.420  66.330 337.805  1.00 67.49           C  
ANISOU 2517  CA  VAL A1332     9389   8147   8108   1531   -238   1810       C  
ATOM   2518  C   VAL A1332       0.516  65.435 336.964  1.00 69.90           C  
ANISOU 2518  C   VAL A1332     9856   8128   8573   1466    -50   1779       C  
ATOM   2519  O   VAL A1332       0.924  64.925 335.921  1.00 75.83           O  
ANISOU 2519  O   VAL A1332    10646   8704   9461   1522     15   1783       O  
ATOM   2520  CB  VAL A1332       2.005  65.515 338.979  1.00 61.62           C  
ANISOU 2520  CB  VAL A1332     8686   7519   7207   1715   -222   2081       C  
ATOM   2521  CG1 VAL A1332       2.593  64.201 338.486  1.00 63.11           C  
ANISOU 2521  CG1 VAL A1332     8976   7509   7495   1932    -78   2285       C  
ATOM   2522  CG2 VAL A1332       3.054  66.331 339.716  1.00 62.47           C  
ANISOU 2522  CG2 VAL A1332     8611   7992   7133   1756   -428   2128       C  
ATOM   2523  N   ASN A1333      -0.721  65.262 337.416  1.00 68.60           N  
ANISOU 2523  N   ASN A1333     9789   7897   8377   1327     43   1745       N  
ATOM   2524  CA  ASN A1333      -1.667  64.392 336.730  1.00 68.60           C  
ANISOU 2524  CA  ASN A1333     9945   7629   8492   1202    217   1720       C  
ATOM   2525  C   ASN A1333      -2.166  65.003 335.422  1.00 70.80           C  
ANISOU 2525  C   ASN A1333    10147   7844   8909   1035    191   1505       C  
ATOM   2526  O   ASN A1333      -2.359  64.299 334.430  1.00 71.98           O  
ANISOU 2526  O   ASN A1333    10405   7774   9170    963    295   1478       O  
ATOM   2527  CB  ASN A1333      -2.848  64.073 337.648  1.00 67.68           C  
ANISOU 2527  CB  ASN A1333     9917   7516   8283   1082    318   1762       C  
ATOM   2528  CG  ASN A1333      -3.647  62.876 337.176  1.00 67.78           C  
ANISOU 2528  CG  ASN A1333    10130   7255   8369    947    517   1800       C  
ATOM   2529  OD1 ASN A1333      -3.253  61.730 337.390  1.00 70.74           O  
ANISOU 2529  OD1 ASN A1333    10702   7445   8731   1054    647   1972       O  
ATOM   2530  ND2 ASN A1333      -4.780  63.135 336.536  1.00 68.74           N  
ANISOU 2530  ND2 ASN A1333    10209   7356   8552    705    549   1651       N  
ATOM   2531  N   LEU A1334      -2.367  66.317 335.426  1.00 68.70           N  
ANISOU 2531  N   LEU A1334     9716   7767   8621    974     60   1357       N  
ATOM   2532  CA  LEU A1334      -2.852  67.027 334.247  1.00 66.32           C  
ANISOU 2532  CA  LEU A1334     9324   7441   8432    841     27   1173       C  
ATOM   2533  C   LEU A1334      -1.809  67.069 333.134  1.00 69.76           C  
ANISOU 2533  C   LEU A1334     9729   7801   8978    912    -27   1132       C  
ATOM   2534  O   LEU A1334      -2.142  66.943 331.956  1.00 74.49           O  
ANISOU 2534  O   LEU A1334    10343   8272   9687    808     12   1039       O  
ATOM   2535  CB  LEU A1334      -3.270  68.453 334.615  1.00 66.62           C  
ANISOU 2535  CB  LEU A1334     9229   7679   8405    800    -69   1047       C  
ATOM   2536  CG  LEU A1334      -4.746  68.716 334.923  1.00 71.22           C  
ANISOU 2536  CG  LEU A1334     9789   8317   8954    674     12   1006       C  
ATOM   2537  CD1 LEU A1334      -5.245  67.808 336.028  1.00 78.37           C  
ANISOU 2537  CD1 LEU A1334    10801   9214   9761    666    121   1149       C  
ATOM   2538  CD2 LEU A1334      -4.956  70.173 335.300  1.00 70.85           C  
ANISOU 2538  CD2 LEU A1334     9651   8435   8832    696    -55    893       C  
ATOM   2539  N   ALA A1335      -0.547  67.244 333.514  1.00 69.08           N  
ANISOU 2539  N   ALA A1335     9586   7817   8842   1081   -116   1211       N  
ATOM   2540  CA  ALA A1335       0.537  67.373 332.545  1.00 68.42           C  
ANISOU 2540  CA  ALA A1335     9439   7708   8849   1166   -169   1189       C  
ATOM   2541  C   ALA A1335       0.966  66.019 331.987  1.00 76.81           C  
ANISOU 2541  C   ALA A1335    10653   8540   9990   1276    -20   1313       C  
ATOM   2542  O   ALA A1335       1.900  65.934 331.187  1.00 84.91           O  
ANISOU 2542  O   ALA A1335    11647   9526  11089   1382    -24   1325       O  
ATOM   2543  CB  ALA A1335       1.724  68.083 333.176  1.00 66.07           C  
ANISOU 2543  CB  ALA A1335     8996   7656   8451   1282   -321   1242       C  
ATOM   2544  N   LYS A1336       0.282  64.962 332.411  1.00 77.32           N  
ANISOU 2544  N   LYS A1336    10903   8443  10032   1250    131   1408       N  
ATOM   2545  CA  LYS A1336       0.581  63.618 331.936  1.00 81.82           C  
ANISOU 2545  CA  LYS A1336    11692   8736  10660   1342    318   1523       C  
ATOM   2546  C   LYS A1336      -0.600  63.061 331.147  1.00 85.41           C  
ANISOU 2546  C   LYS A1336    12323   8953  11175   1087    453   1405       C  
ATOM   2547  O   LYS A1336      -0.877  61.862 331.187  1.00 91.49           O  
ANISOU 2547  O   LYS A1336    13348   9476  11939   1067    643   1495       O  
ATOM   2548  CB  LYS A1336       0.921  62.699 333.110  1.00 86.45           C  
ANISOU 2548  CB  LYS A1336    12398   9302  11146   1533    411   1767       C  
ATOM   2549  CG  LYS A1336       1.949  61.626 332.789  1.00 91.67           C  
ANISOU 2549  CG  LYS A1336    13211   9775  11845   1796    564   1953       C  
ATOM   2550  CD  LYS A1336       3.321  62.235 332.553  1.00 95.77           C  
ANISOU 2550  CD  LYS A1336    13498  10514  12377   2013    430   2007       C  
ATOM   2551  CE  LYS A1336       4.375  61.161 332.337  1.00101.65           C  
ANISOU 2551  CE  LYS A1336    14366  11110  13147   2337    603   2239       C  
ATOM   2552  NZ  LYS A1336       5.733  61.746 332.163  1.00103.06           N  
ANISOU 2552  NZ  LYS A1336    14270  11565  13324   2549    471   2323       N  
ATOM   2553  N   SER A1337      -1.292  63.942 330.431  1.00 83.59           N  
ANISOU 2553  N   SER A1337    11962   8807  10989    883    359   1211       N  
ATOM   2554  CA  SER A1337      -2.484  63.555 329.686  1.00 84.59           C  
ANISOU 2554  CA  SER A1337    12195   8800  11147    601    450   1101       C  
ATOM   2555  C   SER A1337      -2.347  63.842 328.196  1.00 90.20           C  
ANISOU 2555  C   SER A1337    12885   9440  11947    505    425    950       C  
ATOM   2556  O   SER A1337      -1.383  64.471 327.758  1.00 90.35           O  
ANISOU 2556  O   SER A1337    12788   9526  12015    657    333    920       O  
ATOM   2557  CB  SER A1337      -3.712  64.280 330.240  1.00 77.61           C  
ANISOU 2557  CB  SER A1337    11158   8124  10206    427    378   1039       C  
ATOM   2558  OG  SER A1337      -3.583  65.684 330.089  1.00 69.21           O  
ANISOU 2558  OG  SER A1337     9858   7283   9157    468    210    934       O  
ATOM   2559  N   ARG A1338      -3.324  63.377 327.423  1.00 94.11           N  
ANISOU 2559  N   ARG A1338    13490   9820  12448    229    507    859       N  
ATOM   2560  CA  ARG A1338      -3.354  63.619 325.986  1.00 93.26           C  
ANISOU 2560  CA  ARG A1338    13373   9665  12398     93    484    712       C  
ATOM   2561  C   ARG A1338      -3.620  65.094 325.710  1.00 90.19           C  
ANISOU 2561  C   ARG A1338    12683   9554  12030     76    292    608       C  
ATOM   2562  O   ARG A1338      -3.137  65.653 324.726  1.00 90.54           O  
ANISOU 2562  O   ARG A1338    12659   9613  12131     99    225    517       O  
ATOM   2563  CB  ARG A1338      -4.424  62.753 325.317  1.00100.02           C  
ANISOU 2563  CB  ARG A1338    14417  10374  13214   -249    607    647       C  
ATOM   2564  CG  ARG A1338      -4.253  62.598 323.813  1.00107.54           C  
ANISOU 2564  CG  ARG A1338    15471  11194  14195   -387    636    516       C  
ATOM   2565  CD  ARG A1338      -5.546  62.880 323.058  1.00113.31           C  
ANISOU 2565  CD  ARG A1338    16098  12081  14875   -754    574    399       C  
ATOM   2566  NE  ARG A1338      -6.675  62.101 323.559  1.00119.51           N  
ANISOU 2566  NE  ARG A1338    16985  12853  15570  -1033    669    438       N  
ATOM   2567  CZ  ARG A1338      -7.858  62.029 322.956  1.00120.59           C  
ANISOU 2567  CZ  ARG A1338    17065  13123  15631  -1407    648    367       C  
ATOM   2568  NH1 ARG A1338      -8.066  62.684 321.821  1.00119.41           N  
ANISOU 2568  NH1 ARG A1338    16765  13125  15481  -1526    535    258       N  
ATOM   2569  NH2 ARG A1338      -8.832  61.299 323.483  1.00121.71           N  
ANISOU 2569  NH2 ARG A1338    17291  13270  15684  -1673    740    416       N  
ATOM   2570  N   TRP A1339      -4.393  65.713 326.596  1.00 88.06           N  
ANISOU 2570  N   TRP A1339    12257   9492  11710     47    224    630       N  
ATOM   2571  CA  TRP A1339      -4.774  67.116 326.466  1.00 81.91           C  
ANISOU 2571  CA  TRP A1339    11230   8956  10937     51     82    549       C  
ATOM   2572  C   TRP A1339      -3.569  68.052 326.526  1.00 78.19           C  
ANISOU 2572  C   TRP A1339    10663   8547  10500    276    -30    527       C  
ATOM   2573  O   TRP A1339      -3.511  69.049 325.806  1.00 70.70           O  
ANISOU 2573  O   TRP A1339     9588   7688   9587    271   -121    432       O  
ATOM   2574  CB  TRP A1339      -5.783  67.480 327.558  1.00 78.41           C  
ANISOU 2574  CB  TRP A1339    10680   8693  10417     16     79    598       C  
ATOM   2575  CG  TRP A1339      -6.000  68.951 327.738  1.00 74.19           C  
ANISOU 2575  CG  TRP A1339     9942   8375   9873    104    -30    543       C  
ATOM   2576  CD1 TRP A1339      -6.480  69.829 326.812  1.00 73.13           C  
ANISOU 2576  CD1 TRP A1339     9664   8351   9769     47    -90    459       C  
ATOM   2577  CD2 TRP A1339      -5.767  69.710 328.931  1.00 73.76           C  
ANISOU 2577  CD2 TRP A1339     9835   8436   9754    265    -71    574       C  
ATOM   2578  NE1 TRP A1339      -6.549  71.092 327.351  1.00 71.77           N  
ANISOU 2578  NE1 TRP A1339     9375   8327   9568    183   -147    438       N  
ATOM   2579  CE2 TRP A1339      -6.119  71.046 328.649  1.00 72.51           C  
ANISOU 2579  CE2 TRP A1339     9533   8422   9597    301   -135    495       C  
ATOM   2580  CE3 TRP A1339      -5.290  69.392 330.206  1.00 71.75           C  
ANISOU 2580  CE3 TRP A1339     9658   8178   9424    379    -53    664       C  
ATOM   2581  CZ2 TRP A1339      -6.008  72.061 329.598  1.00 72.64           C  
ANISOU 2581  CZ2 TRP A1339     9516   8544   9539    429   -165    483       C  
ATOM   2582  CZ3 TRP A1339      -5.182  70.401 331.145  1.00 69.85           C  
ANISOU 2582  CZ3 TRP A1339     9358   8080   9100    488   -107    652       C  
ATOM   2583  CH2 TRP A1339      -5.539  71.720 330.837  1.00 71.01           C  
ANISOU 2583  CH2 TRP A1339     9395   8336   9247    505   -154    552       C  
ATOM   2584  N   TYR A1340      -2.608  67.724 327.382  1.00 82.46           N  
ANISOU 2584  N   TYR A1340    11261   9053  11016    460    -22    628       N  
ATOM   2585  CA  TYR A1340      -1.409  68.540 327.537  1.00 78.00           C  
ANISOU 2585  CA  TYR A1340    10592   8586  10457    638   -133    625       C  
ATOM   2586  C   TYR A1340      -0.340  68.161 326.518  1.00 82.02           C  
ANISOU 2586  C   TYR A1340    11149   8968  11046    718   -110    620       C  
ATOM   2587  O   TYR A1340       0.424  69.011 326.062  1.00 75.67           O  
ANISOU 2587  O   TYR A1340    10229   8250  10272    778   -206    564       O  
ATOM   2588  CB  TYR A1340      -0.851  68.408 328.957  1.00 69.00           C  
ANISOU 2588  CB  TYR A1340     9454   7538   9226    789   -154    755       C  
ATOM   2589  CG  TYR A1340       0.482  69.094 329.157  1.00 58.74           C  
ANISOU 2589  CG  TYR A1340     8043   6373   7904    936   -272    774       C  
ATOM   2590  CD1 TYR A1340       0.554  70.462 329.388  1.00 53.60           C  
ANISOU 2590  CD1 TYR A1340     7266   5895   7205    901   -398    675       C  
ATOM   2591  CD2 TYR A1340       1.669  68.374 329.119  1.00 57.86           C  
ANISOU 2591  CD2 TYR A1340     7955   6222   7807   1106   -244    903       C  
ATOM   2592  CE1 TYR A1340       1.770  71.093 329.571  1.00 52.37           C  
ANISOU 2592  CE1 TYR A1340     7011   5880   7007    977   -510    687       C  
ATOM   2593  CE2 TYR A1340       2.888  68.995 329.300  1.00 58.67           C  
ANISOU 2593  CE2 TYR A1340     7914   6504   7874   1215   -361    939       C  
ATOM   2594  CZ  TYR A1340       2.934  70.354 329.526  1.00 57.79           C  
ANISOU 2594  CZ  TYR A1340     7677   6574   7706   1124   -502    823       C  
ATOM   2595  OH  TYR A1340       4.151  70.972 329.707  1.00 61.59           O  
ANISOU 2595  OH  TYR A1340     8019   7251   8132   1178   -622    853       O  
ATOM   2596  N   ASN A1341      -0.290  66.881 326.164  1.00 95.40           N  
ANISOU 2596  N   ASN A1341    13036  10446  12766    715     38    681       N  
ATOM   2597  CA  ASN A1341       0.719  66.383 325.236  1.00 98.21           C  
ANISOU 2597  CA  ASN A1341    13476  10653  13187    823    107    694       C  
ATOM   2598  C   ASN A1341       0.524  66.912 323.818  1.00 97.01           C  
ANISOU 2598  C   ASN A1341    13288  10475  13095    682     74    534       C  
ATOM   2599  O   ASN A1341       1.487  67.068 323.068  1.00102.00           O  
ANISOU 2599  O   ASN A1341    13896  11080  13778    786     71    518       O  
ATOM   2600  CB  ASN A1341       0.719  64.852 325.226  1.00103.76           C  
ANISOU 2600  CB  ASN A1341    14458  11081  13886    853    317    794       C  
ATOM   2601  CG  ASN A1341       1.742  64.274 324.266  1.00108.16           C  
ANISOU 2601  CG  ASN A1341    15138  11454  14502    996    435    815       C  
ATOM   2602  OD1 ASN A1341       2.927  64.183 324.584  1.00111.30           O  
ANISOU 2602  OD1 ASN A1341    15478  11902  14910   1267    444    950       O  
ATOM   2603  ND2 ASN A1341       1.285  63.877 323.084  1.00109.71           N  
ANISOU 2603  ND2 ASN A1341    15502  11460  14724    811    531    690       N  
ATOM   2604  N   GLN A1342      -0.723  67.192 323.457  1.00 84.77           N  
ANISOU 2604  N   GLN A1342    11718   8962  11529    450     49    432       N  
ATOM   2605  CA  GLN A1342      -1.042  67.661 322.113  1.00 74.40           C  
ANISOU 2605  CA  GLN A1342    10368   7653  10249    300     12    298       C  
ATOM   2606  C   GLN A1342      -1.049  69.184 322.020  1.00 75.67           C  
ANISOU 2606  C   GLN A1342    10298   8031  10422    327   -149    230       C  
ATOM   2607  O   GLN A1342      -0.530  69.756 321.063  1.00 80.84           O  
ANISOU 2607  O   GLN A1342    10901   8695  11119    341   -194    159       O  
ATOM   2608  CB  GLN A1342      -2.393  67.102 321.665  1.00 66.97           C  
ANISOU 2608  CB  GLN A1342     9515   6668   9262     17     73    245       C  
ATOM   2609  CG  GLN A1342      -2.388  65.598 321.441  1.00 68.81           C  
ANISOU 2609  CG  GLN A1342    10046   6626   9472    -73    259    273       C  
ATOM   2610  CD  GLN A1342      -3.741  65.064 321.014  1.00 76.72           C  
ANISOU 2610  CD  GLN A1342    11131   7618  10401   -420    308    214       C  
ATOM   2611  OE1 GLN A1342      -4.771  65.706 321.227  1.00 80.04           O  
ANISOU 2611  OE1 GLN A1342    11353   8273  10786   -554    208    201       O  
ATOM   2612  NE2 GLN A1342      -3.745  63.883 320.406  1.00 80.11           N  
ANISOU 2612  NE2 GLN A1342    11860   7785  10794   -573    472    184       N  
ATOM   2613  N   THR A1343      -1.642  69.837 323.013  1.00 78.05           N  
ANISOU 2613  N   THR A1343    10487   8491  10677    336   -214    253       N  
ATOM   2614  CA  THR A1343      -1.697  71.296 323.050  1.00 75.73           C  
ANISOU 2614  CA  THR A1343    10028   8367  10379    373   -330    193       C  
ATOM   2615  C   THR A1343      -1.149  71.825 324.371  1.00 73.36           C  
ANISOU 2615  C   THR A1343     9681   8167  10026    511   -384    245       C  
ATOM   2616  O   THR A1343      -1.915  72.225 325.247  1.00 74.52           O  
ANISOU 2616  O   THR A1343     9793   8413  10111    499   -391    259       O  
ATOM   2617  CB  THR A1343      -3.134  71.815 322.859  1.00 78.64           C  
ANISOU 2617  CB  THR A1343    10308   8854  10716    241   -342    158       C  
ATOM   2618  OG1 THR A1343      -3.946  71.399 323.965  1.00 79.17           O  
ANISOU 2618  OG1 THR A1343    10384   8974  10723    214   -293    230       O  
ATOM   2619  CG2 THR A1343      -3.731  71.283 321.566  1.00 80.05           C  
ANISOU 2619  CG2 THR A1343    10517   8985  10911     58   -308    112       C  
ATOM   2620  N   PRO A1344       0.186  71.838 324.511  1.00 69.03           N  
ANISOU 2620  N   PRO A1344     9126   7616   9488    635   -421    279       N  
ATOM   2621  CA  PRO A1344       0.848  72.176 325.776  1.00 68.61           C  
ANISOU 2621  CA  PRO A1344     9030   7686   9354    737   -482    344       C  
ATOM   2622  C   PRO A1344       0.693  73.635 326.193  1.00 70.27           C  
ANISOU 2622  C   PRO A1344     9168   8032   9501    704   -572    258       C  
ATOM   2623  O   PRO A1344       0.599  73.909 327.388  1.00 75.41           O  
ANISOU 2623  O   PRO A1344     9826   8778  10050    725   -595    289       O  
ATOM   2624  CB  PRO A1344       2.318  71.853 325.492  1.00 64.20           C  
ANISOU 2624  CB  PRO A1344     8441   7127   8824    856   -500    409       C  
ATOM   2625  CG  PRO A1344       2.457  72.016 324.025  1.00 63.18           C  
ANISOU 2625  CG  PRO A1344     8310   6906   8789    807   -482    319       C  
ATOM   2626  CD  PRO A1344       1.157  71.545 323.443  1.00 67.25           C  
ANISOU 2626  CD  PRO A1344     8917   7302   9335    677   -404    266       C  
ATOM   2627  N   ASN A1345       0.664  74.552 325.231  1.00 66.32           N  
ANISOU 2627  N   ASN A1345     8626   7524   9048    655   -605    154       N  
ATOM   2628  CA  ASN A1345       0.652  75.978 325.544  1.00 67.32           C  
ANISOU 2628  CA  ASN A1345     8734   7734   9111    633   -662     71       C  
ATOM   2629  C   ASN A1345      -0.667  76.467 326.135  1.00 64.93           C  
ANISOU 2629  C   ASN A1345     8460   7459   8751    621   -610     51       C  
ATOM   2630  O   ASN A1345      -0.672  77.301 327.040  1.00 70.57           O  
ANISOU 2630  O   ASN A1345     9217   8233   9363    632   -621     19       O  
ATOM   2631  CB  ASN A1345       0.995  76.791 324.297  1.00 72.21           C  
ANISOU 2631  CB  ASN A1345     9324   8316   9797    598   -691    -18       C  
ATOM   2632  CG  ASN A1345       2.451  76.651 323.897  1.00 79.00           C  
ANISOU 2632  CG  ASN A1345    10136   9195  10685    615   -745     -2       C  
ATOM   2633  OD1 ASN A1345       3.333  76.550 324.753  1.00 73.83           O  
ANISOU 2633  OD1 ASN A1345     9451   8641   9961    643   -796     55       O  
ATOM   2634  ND2 ASN A1345       2.711  76.640 322.593  1.00 86.11           N  
ANISOU 2634  ND2 ASN A1345    11016  10027  11675    599   -732    -38       N  
ATOM   2635  N   ARG A1346      -1.783  75.953 325.628  1.00 57.45           N  
ANISOU 2635  N   ARG A1346     7492   6482   7854    589   -544     73       N  
ATOM   2636  CA  ARG A1346      -3.087  76.330 326.161  1.00 57.78           C  
ANISOU 2636  CA  ARG A1346     7521   6590   7843    595   -479     86       C  
ATOM   2637  C   ARG A1346      -3.396  75.535 327.426  1.00 65.09           C  
ANISOU 2637  C   ARG A1346     8485   7550   8696    604   -436    168       C  
ATOM   2638  O   ARG A1346      -4.283  75.898 328.199  1.00 69.70           O  
ANISOU 2638  O   ARG A1346     9069   8206   9206    630   -376    187       O  
ATOM   2639  CB  ARG A1346      -4.187  76.114 325.121  1.00 54.28           C  
ANISOU 2639  CB  ARG A1346     6997   6166   7459    531   -438     98       C  
ATOM   2640  CG  ARG A1346      -4.476  74.657 324.811  1.00 53.70           C  
ANISOU 2640  CG  ARG A1346     6932   6048   7422    422   -406    154       C  
ATOM   2641  CD  ARG A1346      -5.726  74.520 323.956  1.00 54.83           C  
ANISOU 2641  CD  ARG A1346     6979   6276   7578    309   -374    171       C  
ATOM   2642  NE  ARG A1346      -6.069  73.124 323.704  1.00 57.93           N  
ANISOU 2642  NE  ARG A1346     7420   6614   7977    149   -329    209       N  
ATOM   2643  CZ  ARG A1346      -7.185  72.725 323.102  1.00 58.99           C  
ANISOU 2643  CZ  ARG A1346     7476   6846   8090    -19   -303    234       C  
ATOM   2644  NH1 ARG A1346      -7.413  71.431 322.916  1.00 61.29           N  
ANISOU 2644  NH1 ARG A1346     7863   7056   8369   -203   -249    252       N  
ATOM   2645  NH2 ARG A1346      -8.075  73.617 322.689  1.00 55.99           N  
ANISOU 2645  NH2 ARG A1346     6931   6656   7688     -9   -322    252       N  
ATOM   2646  N   ALA A1347      -2.656  74.450 327.630  1.00 62.31           N  
ANISOU 2646  N   ALA A1347     8173   7144   8359    603   -450    231       N  
ATOM   2647  CA  ALA A1347      -2.850  73.598 328.794  1.00 59.63           C  
ANISOU 2647  CA  ALA A1347     7888   6822   7948    621   -404    330       C  
ATOM   2648  C   ALA A1347      -2.005  74.071 329.970  1.00 67.15           C  
ANISOU 2648  C   ALA A1347     8873   7859   8782    692   -465    344       C  
ATOM   2649  O   ALA A1347      -2.490  74.153 331.098  1.00 75.27           O  
ANISOU 2649  O   ALA A1347     9940   8957   9702    706   -430    378       O  
ATOM   2650  CB  ALA A1347      -2.522  72.153 328.454  1.00 57.09           C  
ANISOU 2650  CB  ALA A1347     7624   6382   7685    604   -359    412       C  
ATOM   2651  N   LYS A1348      -0.740  74.382 329.700  1.00 66.72           N  
ANISOU 2651  N   LYS A1348     8796   7821   8735    718   -555    321       N  
ATOM   2652  CA  LYS A1348       0.186  74.823 330.738  1.00 66.11           C  
ANISOU 2652  CA  LYS A1348     8728   7869   8521    741   -638    339       C  
ATOM   2653  C   LYS A1348      -0.286  76.122 331.382  1.00 69.35           C  
ANISOU 2653  C   LYS A1348     9198   8338   8813    695   -637    233       C  
ATOM   2654  O   LYS A1348      -0.080  76.345 332.574  1.00 74.50           O  
ANISOU 2654  O   LYS A1348     9907   9093   9307    685   -661    250       O  
ATOM   2655  CB  LYS A1348       1.593  75.001 330.162  1.00 63.56           C  
ANISOU 2655  CB  LYS A1348     8332   7590   8228    750   -736    336       C  
ATOM   2656  CG  LYS A1348       2.650  75.388 331.182  1.00 59.06           C  
ANISOU 2656  CG  LYS A1348     7735   7209   7498    736   -843    374       C  
ATOM   2657  CD  LYS A1348       4.021  75.497 330.535  1.00 56.80           C  
ANISOU 2657  CD  LYS A1348     7331   7006   7245    737   -934    396       C  
ATOM   2658  CE  LYS A1348       5.083  75.893 331.545  1.00 61.65           C  
ANISOU 2658  CE  LYS A1348     7882   7870   7673    683  -1060    446       C  
ATOM   2659  NZ  LYS A1348       6.432  75.973 330.923  1.00 64.95           N  
ANISOU 2659  NZ  LYS A1348     8142   8420   8117    681  -1146    494       N  
ATOM   2660  N   ARG A1349      -0.928  76.973 330.589  1.00 72.12           N  
ANISOU 2660  N   ARG A1349     9554   8621   9228    674   -595    131       N  
ATOM   2661  CA  ARG A1349      -1.452  78.237 331.091  1.00 72.43           C  
ANISOU 2661  CA  ARG A1349     9689   8669   9161    664   -547     35       C  
ATOM   2662  C   ARG A1349      -2.594  77.994 332.077  1.00 70.71           C  
ANISOU 2662  C   ARG A1349     9517   8486   8863    711   -439     86       C  
ATOM   2663  O   ARG A1349      -2.796  78.767 333.013  1.00 72.93           O  
ANISOU 2663  O   ARG A1349     9916   8798   8997    716   -393     36       O  
ATOM   2664  CB  ARG A1349      -1.921  79.122 329.933  1.00 72.63           C  
ANISOU 2664  CB  ARG A1349     9706   8610   9282    676   -505    -48       C  
ATOM   2665  CG  ARG A1349      -2.375  80.508 330.359  1.00 75.55           C  
ANISOU 2665  CG  ARG A1349    10214   8946   9544    700   -422   -141       C  
ATOM   2666  CD  ARG A1349      -2.655  81.402 329.163  1.00 78.95           C  
ANISOU 2666  CD  ARG A1349    10645   9288  10065    734   -381   -198       C  
ATOM   2667  NE  ARG A1349      -3.208  82.687 329.576  1.00 82.76           N  
ANISOU 2667  NE  ARG A1349    11296   9704  10444    799   -255   -266       N  
ATOM   2668  CZ  ARG A1349      -4.509  82.948 329.656  1.00 85.95           C  
ANISOU 2668  CZ  ARG A1349    11694  10117  10848    940   -109   -213       C  
ATOM   2669  NH1 ARG A1349      -5.395  82.011 329.342  1.00 85.84           N  
ANISOU 2669  NH1 ARG A1349    11492  10200  10925    984    -95    -99       N  
ATOM   2670  NH2 ARG A1349      -4.925  84.144 330.046  1.00 88.75           N  
ANISOU 2670  NH2 ARG A1349    12235  10385  11100   1031     35   -268       N  
ATOM   2671  N   VAL A1350      -3.331  76.909 331.864  1.00 67.78           N  
ANISOU 2671  N   VAL A1350     9069   8108   8578    729   -388    184       N  
ATOM   2672  CA  VAL A1350      -4.419  76.530 332.758  1.00 67.86           C  
ANISOU 2672  CA  VAL A1350     9095   8169   8518    756   -280    254       C  
ATOM   2673  C   VAL A1350      -3.885  75.880 334.031  1.00 68.88           C  
ANISOU 2673  C   VAL A1350     9294   8359   8520    755   -308    330       C  
ATOM   2674  O   VAL A1350      -4.308  76.218 335.139  1.00 71.16           O  
ANISOU 2674  O   VAL A1350     9665   8711   8663    776   -248    332       O  
ATOM   2675  CB  VAL A1350      -5.401  75.561 332.071  1.00 68.04           C  
ANISOU 2675  CB  VAL A1350     9014   8178   8659    723   -216    334       C  
ATOM   2676  CG1 VAL A1350      -6.393  75.003 333.078  1.00 71.89           C  
ANISOU 2676  CG1 VAL A1350     9510   8738   9066    724   -108    427       C  
ATOM   2677  CG2 VAL A1350      -6.126  76.259 330.932  1.00 67.66           C  
ANISOU 2677  CG2 VAL A1350     8874   8132   8700    728   -184    285       C  
ATOM   2678  N   ILE A1351      -2.950  74.950 333.862  1.00 65.88           N  
ANISOU 2678  N   ILE A1351     8885   7962   8183    748   -389    404       N  
ATOM   2679  CA  ILE A1351      -2.396  74.188 334.977  1.00 66.99           C  
ANISOU 2679  CA  ILE A1351     9071   8175   8208    776   -417    520       C  
ATOM   2680  C   ILE A1351      -1.705  75.081 336.007  1.00 73.36           C  
ANISOU 2680  C   ILE A1351     9945   9112   8816    755   -494    470       C  
ATOM   2681  O   ILE A1351      -1.900  74.914 337.212  1.00 81.23           O  
ANISOU 2681  O   ILE A1351    11014  10196   9654    762   -468    527       O  
ATOM   2682  CB  ILE A1351      -1.398  73.124 334.479  1.00 66.48           C  
ANISOU 2682  CB  ILE A1351     8961   8068   8229    817   -474    626       C  
ATOM   2683  CG1 ILE A1351      -2.105  72.119 333.567  1.00 73.94           C  
ANISOU 2683  CG1 ILE A1351     9902   8859   9334    801   -376    668       C  
ATOM   2684  CG2 ILE A1351      -0.751  72.402 335.646  1.00 67.20           C  
ANISOU 2684  CG2 ILE A1351     9087   8260   8186    883   -504    777       C  
ATOM   2685  CD1 ILE A1351      -1.188  71.058 332.998  1.00 79.93           C  
ANISOU 2685  CD1 ILE A1351    10667   9523  10178    863   -382    765       C  
ATOM   2686  N   THR A1352      -0.906  76.030 335.529  1.00 70.08           N  
ANISOU 2686  N   THR A1352     9520   8715   8394    703   -585    360       N  
ATOM   2687  CA  THR A1352      -0.188  76.942 336.416  1.00 71.01           C  
ANISOU 2687  CA  THR A1352     9720   8959   8302    621   -664    289       C  
ATOM   2688  C   THR A1352      -1.144  77.818 337.219  1.00 70.72           C  
ANISOU 2688  C   THR A1352     9846   8902   8124    601   -549    192       C  
ATOM   2689  O   THR A1352      -0.815  78.255 338.323  1.00 72.22           O  
ANISOU 2689  O   THR A1352    10152   9198   8090    530   -577    161       O  
ATOM   2690  CB  THR A1352       0.778  77.849 335.634  1.00 69.65           C  
ANISOU 2690  CB  THR A1352     9520   8791   8152    530   -765    177       C  
ATOM   2691  OG1 THR A1352       0.064  78.521 334.589  1.00 71.32           O  
ANISOU 2691  OG1 THR A1352     9753   8839   8506    546   -679     68       O  
ATOM   2692  CG2 THR A1352       1.907  77.030 335.029  1.00 66.03           C  
ANISOU 2692  CG2 THR A1352     8896   8401   7791    561   -876    289       C  
ATOM   2693  N   THR A1353      -2.323  78.077 336.661  1.00 67.04           N  
ANISOU 2693  N   THR A1353     9387   8314   7773    667   -412    152       N  
ATOM   2694  CA  THR A1353      -3.340  78.852 337.362  1.00 67.39           C  
ANISOU 2694  CA  THR A1353     9572   8334   7698    703   -260     88       C  
ATOM   2695  C   THR A1353      -3.876  78.062 338.554  1.00 68.74           C  
ANISOU 2695  C   THR A1353     9772   8595   7753    736   -197    200       C  
ATOM   2696  O   THR A1353      -4.100  78.617 339.628  1.00 70.21           O  
ANISOU 2696  O   THR A1353    10117   8823   7736    724   -127    154       O  
ATOM   2697  CB  THR A1353      -4.503  79.240 336.431  1.00 63.13           C  
ANISOU 2697  CB  THR A1353     8979   7695   7313    799   -125     67       C  
ATOM   2698  OG1 THR A1353      -3.991  79.957 335.302  1.00 63.44           O  
ANISOU 2698  OG1 THR A1353     9001   7648   7455    774   -181    -24       O  
ATOM   2699  CG2 THR A1353      -5.504  80.118 337.165  1.00 64.09           C  
ANISOU 2699  CG2 THR A1353     9247   7799   7304    882     60     20       C  
ATOM   2700  N   PHE A1354      -4.074  76.762 338.356  1.00 67.23           N  
ANISOU 2700  N   PHE A1354     9451   8416   7677    769   -207    345       N  
ATOM   2701  CA  PHE A1354      -4.470  75.874 339.443  1.00 67.78           C  
ANISOU 2701  CA  PHE A1354     9551   8561   7643    791   -152    474       C  
ATOM   2702  C   PHE A1354      -3.368  75.794 340.491  1.00 74.17           C  
ANISOU 2702  C   PHE A1354    10437   9499   8246    744   -273    508       C  
ATOM   2703  O   PHE A1354      -3.636  75.669 341.686  1.00 78.37           O  
ANISOU 2703  O   PHE A1354    11068  10119   8592    745   -223    556       O  
ATOM   2704  CB  PHE A1354      -4.789  74.474 338.912  1.00 64.08           C  
ANISOU 2704  CB  PHE A1354     8967   8041   7340    810   -131    618       C  
ATOM   2705  CG  PHE A1354      -6.064  74.397 338.124  1.00 61.92           C  
ANISOU 2705  CG  PHE A1354     8606   7708   7214    813     -8    614       C  
ATOM   2706  CD1 PHE A1354      -7.104  75.277 338.372  1.00 62.54           C  
ANISOU 2706  CD1 PHE A1354     8699   7824   7238    855    121    558       C  
ATOM   2707  CD2 PHE A1354      -6.222  73.441 337.134  1.00 60.16           C  
ANISOU 2707  CD2 PHE A1354     8286   7405   7165    773    -11    677       C  
ATOM   2708  CE1 PHE A1354      -8.279  75.204 337.648  1.00 63.16           C  
ANISOU 2708  CE1 PHE A1354     8649   7911   7437    862    224    586       C  
ATOM   2709  CE2 PHE A1354      -7.394  73.363 336.406  1.00 59.86           C  
ANISOU 2709  CE2 PHE A1354     8147   7362   7234    734     83    680       C  
ATOM   2710  CZ  PHE A1354      -8.424  74.246 336.663  1.00 62.09           C  
ANISOU 2710  CZ  PHE A1354     8396   7733   7463    782    191    647       C  
ATOM   2711  N   ARG A1355      -2.124  75.869 340.028  1.00 73.92           N  
ANISOU 2711  N   ARG A1355    10345   9506   8235    700   -432    495       N  
ATOM   2712  CA  ARG A1355      -0.963  75.787 340.904  1.00 75.77           C  
ANISOU 2712  CA  ARG A1355    10596   9925   8268    644   -576    553       C  
ATOM   2713  C   ARG A1355      -0.804  77.027 341.777  1.00 79.51           C  
ANISOU 2713  C   ARG A1355    11241  10485   8485    516   -589    404       C  
ATOM   2714  O   ARG A1355      -0.791  76.937 343.004  1.00 86.65           O  
ANISOU 2714  O   ARG A1355    12244  11522   9158    481   -591    448       O  
ATOM   2715  CB  ARG A1355       0.307  75.577 340.079  1.00 71.42           C  
ANISOU 2715  CB  ARG A1355     9897   9424   7815    633   -731    592       C  
ATOM   2716  CG  ARG A1355       0.517  74.153 339.601  1.00 71.11           C  
ANISOU 2716  CG  ARG A1355     9737   9340   7942    766   -727    783       C  
ATOM   2717  CD  ARG A1355       1.763  73.560 340.231  1.00 75.08           C  
ANISOU 2717  CD  ARG A1355    10157  10059   8311    807   -861    958       C  
ATOM   2718  NE  ARG A1355       2.956  74.335 339.904  1.00 78.84           N  
ANISOU 2718  NE  ARG A1355    10535  10690   8730    711  -1020    894       N  
ATOM   2719  CZ  ARG A1355       4.143  74.156 340.475  1.00 88.37           C  
ANISOU 2719  CZ  ARG A1355    11632  12171   9774    703  -1169   1028       C  
ATOM   2720  NH1 ARG A1355       4.299  73.230 341.410  1.00 90.71           N  
ANISOU 2720  NH1 ARG A1355    11914  12603   9950    815  -1176   1242       N  
ATOM   2721  NH2 ARG A1355       5.173  74.909 340.114  1.00 94.14           N  
ANISOU 2721  NH2 ARG A1355    12256  13059  10452    579  -1309    963       N  
ATOM   2722  N   THR A1356      -0.683  78.183 341.134  1.00 74.71           N  
ANISOU 2722  N   THR A1356    10695   9788   7903    436   -587    225       N  
ATOM   2723  CA  THR A1356      -0.347  79.419 341.832  1.00 73.80           C  
ANISOU 2723  CA  THR A1356    10787   9720   7534    274   -598     60       C  
ATOM   2724  C   THR A1356      -1.570  80.158 342.363  1.00 77.76           C  
ANISOU 2724  C   THR A1356    11513  10088   7944    321   -380    -49       C  
ATOM   2725  O   THR A1356      -1.482  80.884 343.353  1.00 87.25           O  
ANISOU 2725  O   THR A1356    12941  11334   8875    205   -345   -152       O  
ATOM   2726  CB  THR A1356       0.433  80.377 340.916  1.00 72.58           C  
ANISOU 2726  CB  THR A1356    10637   9511   7429    148   -679    -83       C  
ATOM   2727  OG1 THR A1356      -0.449  80.920 339.926  1.00 70.39           O  
ANISOU 2727  OG1 THR A1356    10395   8999   7349    250   -530   -172       O  
ATOM   2728  CG2 THR A1356       1.577  79.645 340.229  1.00 72.39           C  
ANISOU 2728  CG2 THR A1356    10362   9615   7527    139   -865     37       C  
ATOM   2729  N   GLY A1357      -2.708  79.981 341.700  1.00 74.41           N  
ANISOU 2729  N   GLY A1357    11027   9516   7731    486   -225    -22       N  
ATOM   2730  CA  GLY A1357      -3.902  80.730 342.042  1.00 75.83           C  
ANISOU 2730  CA  GLY A1357    11379   9582   7851    577      5   -100       C  
ATOM   2731  C   GLY A1357      -3.787  82.162 341.555  1.00 79.15           C  
ANISOU 2731  C   GLY A1357    11987   9847   8240    534     75   -288       C  
ATOM   2732  O   GLY A1357      -4.550  83.036 341.965  1.00 80.74           O  
ANISOU 2732  O   GLY A1357    12408   9938   8331    602    281   -377       O  
ATOM   2733  N   THR A1358      -2.819  82.395 340.675  1.00 81.91           N  
ANISOU 2733  N   THR A1358    12263  10179   8682    429    -79   -339       N  
ATOM   2734  CA  THR A1358      -2.592  83.713 340.098  1.00 84.14           C  
ANISOU 2734  CA  THR A1358    12727  10298   8947    365    -22   -510       C  
ATOM   2735  C   THR A1358      -2.936  83.699 338.615  1.00 85.49           C  
ANISOU 2735  C   THR A1358    12719  10354   9410    493     -4   -476       C  
ATOM   2736  O   THR A1358      -2.523  82.801 337.882  1.00 84.80           O  
ANISOU 2736  O   THR A1358    12378  10340   9502    496   -150   -376       O  
ATOM   2737  CB  THR A1358      -1.132  84.171 340.280  1.00 86.56           C  
ANISOU 2737  CB  THR A1358    13113  10691   9086     91   -210   -611       C  
ATOM   2738  OG1 THR A1358      -0.800  84.176 341.673  1.00 94.31           O  
ANISOU 2738  OG1 THR A1358    14254  11818   9763    -57   -244   -637       O  
ATOM   2739  CG2 THR A1358      -0.932  85.569 339.710  1.00 85.99           C  
ANISOU 2739  CG2 THR A1358    13276  10416   8980     -3   -125   -796       C  
ATOM   2740  N   TRP A1359      -3.696  84.697 338.179  1.00 87.49           N  
ANISOU 2740  N   TRP A1359    13119  10427   9696    611    187   -551       N  
ATOM   2741  CA  TRP A1359      -4.134  84.768 336.792  1.00 81.31           C  
ANISOU 2741  CA  TRP A1359    12173   9557   9162    744    216   -507       C  
ATOM   2742  C   TRP A1359      -3.068  85.377 335.887  1.00 76.57           C  
ANISOU 2742  C   TRP A1359    11603   8878   8612    602     98   -605       C  
ATOM   2743  O   TRP A1359      -2.579  86.477 336.139  1.00 73.30           O  
ANISOU 2743  O   TRP A1359    11462   8349   8041    480    146   -752       O  
ATOM   2744  CB  TRP A1359      -5.428  85.574 336.685  1.00 78.17           C  
ANISOU 2744  CB  TRP A1359    11895   9033   8775    970    482   -503       C  
ATOM   2745  CG  TRP A1359      -6.017  85.569 335.313  1.00 73.52           C  
ANISOU 2745  CG  TRP A1359    11101   8412   8421   1121    509   -421       C  
ATOM   2746  CD1 TRP A1359      -5.894  86.541 334.363  1.00 73.50           C  
ANISOU 2746  CD1 TRP A1359    11187   8256   8481   1166    561   -481       C  
ATOM   2747  CD2 TRP A1359      -6.818  84.538 334.730  1.00 72.21           C  
ANISOU 2747  CD2 TRP A1359    10617   8382   8437   1224    482   -259       C  
ATOM   2748  NE1 TRP A1359      -6.572  86.180 333.225  1.00 71.16           N  
ANISOU 2748  NE1 TRP A1359    10630   8016   8392   1304    558   -359       N  
ATOM   2749  CE2 TRP A1359      -7.150  84.950 333.425  1.00 70.91           C  
ANISOU 2749  CE2 TRP A1359    10346   8166   8430   1324    507   -228       C  
ATOM   2750  CE3 TRP A1359      -7.291  83.302 335.184  1.00 73.48           C  
ANISOU 2750  CE3 TRP A1359    10588   8703   8629   1220    445   -137       C  
ATOM   2751  CZ2 TRP A1359      -7.930  84.177 332.570  1.00 71.73           C  
ANISOU 2751  CZ2 TRP A1359    10153   8398   8704   1396    481    -88       C  
ATOM   2752  CZ3 TRP A1359      -8.065  82.534 334.336  1.00 73.19           C  
ANISOU 2752  CZ3 TRP A1359    10277   8766   8768   1280    433     -6       C  
ATOM   2753  CH2 TRP A1359      -8.377  82.973 333.044  1.00 71.97           C  
ANISOU 2753  CH2 TRP A1359    10013   8582   8753   1356    444     14       C  
ATOM   2754  N   ASP A1360      -2.713  84.649 334.833  1.00 78.36           N  
ANISOU 2754  N   ASP A1360    11566   9160   9047    602    -44   -527       N  
ATOM   2755  CA  ASP A1360      -1.794  85.153 333.821  1.00 80.65           C  
ANISOU 2755  CA  ASP A1360    11844   9385   9414    493   -143   -598       C  
ATOM   2756  C   ASP A1360      -2.578  85.631 332.604  1.00 75.17           C  
ANISOU 2756  C   ASP A1360    11111   8556   8894    658    -28   -578       C  
ATOM   2757  O   ASP A1360      -3.112  84.824 331.844  1.00 71.56           O  
ANISOU 2757  O   ASP A1360    10416   8158   8617    765    -54   -464       O  
ATOM   2758  CB  ASP A1360      -0.784  84.077 333.418  1.00 88.23           C  
ANISOU 2758  CB  ASP A1360    12554  10495  10473    396   -360   -520       C  
ATOM   2759  CG  ASP A1360       0.178  84.554 332.346  1.00 94.95           C  
ANISOU 2759  CG  ASP A1360    13368  11302  11405    286   -454   -581       C  
ATOM   2760  OD1 ASP A1360       0.563  85.742 332.374  1.00 98.23           O  
ANISOU 2760  OD1 ASP A1360    14001  11616  11706    166   -412   -713       O  
ATOM   2761  OD2 ASP A1360       0.549  83.740 331.473  1.00 97.30           O  
ANISOU 2761  OD2 ASP A1360    13443  11655  11872    313   -555   -499       O  
ATOM   2762  N   ALA A1361      -2.645  86.947 332.428  1.00 75.64           N  
ANISOU 2762  N   ALA A1361    11421   8438   8881    669    106   -685       N  
ATOM   2763  CA  ALA A1361      -3.450  87.540 331.366  1.00 77.24           C  
ANISOU 2763  CA  ALA A1361    11613   8518   9216    862    241   -645       C  
ATOM   2764  C   ALA A1361      -2.893  87.228 329.979  1.00 78.26           C  
ANISOU 2764  C   ALA A1361    11537   8668   9532    813     97   -614       C  
ATOM   2765  O   ALA A1361      -1.692  87.351 329.735  1.00 79.26           O  
ANISOU 2765  O   ALA A1361    11686   8788   9642    616    -36   -692       O  
ATOM   2766  CB  ALA A1361      -3.555  89.042 331.567  1.00 77.81           C  
ANISOU 2766  CB  ALA A1361    12058   8359   9149    893    443   -761       C  
ATOM   2767  N   TYR A1362      -3.781  86.824 329.076  1.00 80.69           N  
ANISOU 2767  N   TYR A1362    11637   9022  10001    984    128   -494       N  
ATOM   2768  CA  TYR A1362      -3.402  86.489 327.708  1.00 79.32           C  
ANISOU 2768  CA  TYR A1362    11277   8869   9993    950     11   -459       C  
ATOM   2769  C   TYR A1362      -3.313  87.742 326.843  1.00 78.15           C  
ANISOU 2769  C   TYR A1362    11286   8552   9856    999    102   -508       C  
ATOM   2770  O   TYR A1362      -2.423  87.865 326.002  1.00 79.19           O  
ANISOU 2770  O   TYR A1362    11395   8647  10048    878      1   -553       O  
ATOM   2771  CB  TYR A1362      -4.401  85.497 327.106  1.00 80.98           C  
ANISOU 2771  CB  TYR A1362    11210   9219  10338   1064     -2   -315       C  
ATOM   2772  CG  TYR A1362      -4.082  85.079 325.690  1.00 83.39           C  
ANISOU 2772  CG  TYR A1362    11342   9549  10791   1017   -113   -284       C  
ATOM   2773  CD1 TYR A1362      -4.771  85.622 324.613  1.00 85.51           C  
ANISOU 2773  CD1 TYR A1362    11557   9807  11126   1141    -46   -224       C  
ATOM   2774  CD2 TYR A1362      -3.095  84.139 325.430  1.00 85.07           C  
ANISOU 2774  CD2 TYR A1362    11452   9805  11065    864   -272   -303       C  
ATOM   2775  CE1 TYR A1362      -4.484  85.241 323.316  1.00 83.98           C  
ANISOU 2775  CE1 TYR A1362    11221   9643  11044   1082   -146   -202       C  
ATOM   2776  CE2 TYR A1362      -2.800  83.752 324.138  1.00 85.98           C  
ANISOU 2776  CE2 TYR A1362    11439   9928  11301    824   -350   -284       C  
ATOM   2777  CZ  TYR A1362      -3.497  84.305 323.084  1.00 84.62           C  
ANISOU 2777  CZ  TYR A1362    11226   9743  11182    917   -293   -243       C  
ATOM   2778  OH  TYR A1362      -3.205  83.921 321.796  1.00 82.09           O  
ANISOU 2778  OH  TYR A1362    10793   9438  10960    862   -370   -229       O  
ATOM   2779  N   ARG A2238      -4.235  88.674 327.063  1.00 73.62           N  
ANISOU 2779  N   ARG A2238    10883   7873   9217   1191    313   -486       N  
ATOM   2780  CA  ARG A2238      -4.267  89.919 326.304  1.00 72.92           C  
ANISOU 2780  CA  ARG A2238    10987   7595   9126   1283    444   -509       C  
ATOM   2781  C   ARG A2238      -3.224  90.906 326.820  1.00 80.39           C  
ANISOU 2781  C   ARG A2238    12287   8335   9921   1087    481   -685       C  
ATOM   2782  O   ARG A2238      -3.160  92.053 326.378  1.00 80.71           O  
ANISOU 2782  O   ARG A2238    12579   8163   9923   1131    623   -728       O  
ATOM   2783  CB  ARG A2238      -5.662  90.544 326.359  1.00 68.41           C  
ANISOU 2783  CB  ARG A2238    10470   6989   8532   1604    686   -390       C  
ATOM   2784  CG  ARG A2238      -6.086  91.012 327.737  1.00 68.33           C  
ANISOU 2784  CG  ARG A2238    10718   6892   8354   1683    875   -438       C  
ATOM   2785  CD  ARG A2238      -7.560  91.372 327.756  1.00 70.47           C  
ANISOU 2785  CD  ARG A2238    10947   7203   8626   2043   1111   -272       C  
ATOM   2786  NE  ARG A2238      -8.412  90.186 327.719  1.00 68.44           N  
ANISOU 2786  NE  ARG A2238    10295   7247   8463   2110   1023   -117       N  
ATOM   2787  CZ  ARG A2238      -9.710  90.209 327.436  1.00 66.07           C  
ANISOU 2787  CZ  ARG A2238     9801   7101   8200   2388   1159     77       C  
ATOM   2788  NH1 ARG A2238     -10.307  91.358 327.150  1.00 63.64           N  
ANISOU 2788  NH1 ARG A2238     9654   6672   7854   2677   1399    158       N  
ATOM   2789  NH2 ARG A2238     -10.410  89.082 327.428  1.00 64.84           N  
ANISOU 2789  NH2 ARG A2238     9292   7232   8112   2376   1063    203       N  
ATOM   2790  N   ARG A2239      -2.413  90.444 327.766  1.00 88.11           N  
ANISOU 2790  N   ARG A2239    13290   9388  10799    858    356   -779       N  
ATOM   2791  CA  ARG A2239      -1.291  91.213 328.285  1.00 92.73           C  
ANISOU 2791  CA  ARG A2239    14162   9854  11218    588    339   -948       C  
ATOM   2792  C   ARG A2239      -0.071  91.024 327.393  1.00 89.52           C  
ANISOU 2792  C   ARG A2239    13613   9506  10893    369    145   -980       C  
ATOM   2793  O   ARG A2239       0.669  91.970 327.121  1.00 87.96           O  
ANISOU 2793  O   ARG A2239    13638   9161  10620    196    175  -1087       O  
ATOM   2794  CB  ARG A2239      -0.979  90.786 329.721  1.00100.58           C  
ANISOU 2794  CB  ARG A2239    15215  10962  12041    435    279  -1010       C  
ATOM   2795  CG  ARG A2239       0.386  91.208 330.237  1.00109.04           C  
ANISOU 2795  CG  ARG A2239    16457  12039  12934     74    166  -1162       C  
ATOM   2796  CD  ARG A2239       0.619  90.643 331.630  1.00119.26           C  
ANISOU 2796  CD  ARG A2239    17755  13506  14053    -56     83  -1187       C  
ATOM   2797  NE  ARG A2239       1.914  91.025 332.185  1.00127.71           N  
ANISOU 2797  NE  ARG A2239    18956  14648  14919   -429    -44  -1316       N  
ATOM   2798  CZ  ARG A2239       3.007  90.273 332.114  1.00130.51           C  
ANISOU 2798  CZ  ARG A2239    19034  15262  15291   -617   -292  -1271       C  
ATOM   2799  NH1 ARG A2239       2.964  89.094 331.508  1.00128.99           N  
ANISOU 2799  NH1 ARG A2239    18465  15228  15316   -455   -416  -1116       N  
ATOM   2800  NH2 ARG A2239       4.144  90.698 332.649  1.00132.85           N  
ANISOU 2800  NH2 ARG A2239    19434  15667  15374   -971   -404  -1375       N  
ATOM   2801  N   ARG A2240       0.122  89.789 326.940  1.00 87.50           N  
ANISOU 2801  N   ARG A2240    13001   9459  10787    378    -36   -882       N  
ATOM   2802  CA  ARG A2240       1.237  89.437 326.069  1.00 88.49           C  
ANISOU 2802  CA  ARG A2240    12952   9667  11005    216   -207   -886       C  
ATOM   2803  C   ARG A2240       1.157  90.155 324.727  1.00 86.04           C  
ANISOU 2803  C   ARG A2240    12686   9210  10797    280   -137   -878       C  
ATOM   2804  O   ARG A2240       0.188  89.988 323.986  1.00 86.04           O  
ANISOU 2804  O   ARG A2240    12580   9196  10917    506    -71   -776       O  
ATOM   2805  CB  ARG A2240       1.274  87.927 325.839  1.00 92.67           C  
ANISOU 2805  CB  ARG A2240    13134  10404  11671    269   -360   -771       C  
ATOM   2806  CG  ARG A2240       1.530  87.102 327.088  1.00100.10           C  
ANISOU 2806  CG  ARG A2240    14009  11508  12517    202   -447   -752       C  
ATOM   2807  CD  ARG A2240       1.115  85.660 326.862  1.00103.99           C  
ANISOU 2807  CD  ARG A2240    14230  12130  13150    328   -515   -621       C  
ATOM   2808  NE  ARG A2240       1.417  85.223 325.502  1.00107.13           N  
ANISOU 2808  NE  ARG A2240    14456  12533  13716    347   -576   -576       N  
ATOM   2809  CZ  ARG A2240       1.047  84.053 324.992  1.00108.90           C  
ANISOU 2809  CZ  ARG A2240    14487  12821  14069    435   -611   -478       C  
ATOM   2810  NH1 ARG A2240       0.356  83.195 325.730  1.00110.42           N  
ANISOU 2810  NH1 ARG A2240    14623  13080  14250    507   -594   -407       N  
ATOM   2811  NH2 ARG A2240       1.365  83.743 323.743  1.00107.87           N  
ANISOU 2811  NH2 ARG A2240    14243  12679  14064    435   -652   -457       N  
ATOM   2812  N   PRO A2241       2.181  90.959 324.411  1.00 86.55           N  
ANISOU 2812  N   PRO A2241    12900   9187  10799     65   -155   -977       N  
ATOM   2813  CA  PRO A2241       2.262  91.652 323.122  1.00 85.66           C  
ANISOU 2813  CA  PRO A2241    12842   8934  10772     99    -94   -968       C  
ATOM   2814  C   PRO A2241       2.400  90.673 321.960  1.00 87.90           C  
ANISOU 2814  C   PRO A2241    12789   9366  11244    165   -226   -865       C  
ATOM   2815  O   PRO A2241       2.831  89.538 322.162  1.00 87.98           O  
ANISOU 2815  O   PRO A2241    12556   9569  11302    113   -375   -828       O  
ATOM   2816  CB  PRO A2241       3.523  92.511 323.261  1.00 84.94           C  
ANISOU 2816  CB  PRO A2241    12957   8770  10548   -224   -117  -1104       C  
ATOM   2817  CG  PRO A2241       3.743  92.640 324.731  1.00 88.37           C  
ANISOU 2817  CG  PRO A2241    13555   9238  10784   -388   -119  -1199       C  
ATOM   2818  CD  PRO A2241       3.284  91.340 325.308  1.00 89.28           C  
ANISOU 2818  CD  PRO A2241    13393   9570  10961   -244   -223  -1101       C  
ATOM   2819  N   GLY A2242       2.039  91.111 320.758  1.00 87.77           N  
ANISOU 2819  N   GLY A2242    12781   9250  11317    283   -157   -814       N  
ATOM   2820  CA  GLY A2242       2.141  90.268 319.582  1.00 86.91           C  
ANISOU 2820  CA  GLY A2242    12399   9263  11361    328   -263   -732       C  
ATOM   2821  C   GLY A2242       3.575  90.098 319.124  1.00 86.24           C  
ANISOU 2821  C   GLY A2242    12229   9245  11294    100   -385   -783       C  
ATOM   2822  O   GLY A2242       4.407  90.982 319.325  1.00 85.63           O  
ANISOU 2822  O   GLY A2242    12330   9085  11120    -95   -364   -875       O  
ATOM   2823  N   ARG A2243       3.866  88.958 318.504  1.00 86.90           N  
ANISOU 2823  N   ARG A2243    12047   9479  11491    115   -499   -721       N  
ATOM   2824  CA  ARG A2243       5.211  88.677 318.018  1.00 88.65           C  
ANISOU 2824  CA  ARG A2243    12148   9795  11740    -55   -599   -741       C  
ATOM   2825  C   ARG A2243       5.263  88.687 316.494  1.00 84.60           C  
ANISOU 2825  C   ARG A2243    11568   9245  11329     -8   -583   -702       C  
ATOM   2826  O   ARG A2243       4.229  88.599 315.832  1.00 85.31           O  
ANISOU 2826  O   ARG A2243    11648   9290  11476    158   -532   -643       O  
ATOM   2827  CB  ARG A2243       5.704  87.329 318.547  1.00 94.45           C  
ANISOU 2827  CB  ARG A2243    12656  10724  12507    -64   -716   -693       C  
ATOM   2828  CG  ARG A2243       5.452  87.103 320.027  1.00101.02           C  
ANISOU 2828  CG  ARG A2243    13527  11616  13241    -71   -736   -703       C  
ATOM   2829  CD  ARG A2243       6.244  85.909 320.531  1.00105.26           C  
ANISOU 2829  CD  ARG A2243    13853  12353  13787    -98   -852   -640       C  
ATOM   2830  NE  ARG A2243       6.225  84.804 319.577  1.00107.06           N  
ANISOU 2830  NE  ARG A2243    13905  12613  14159     22   -866   -559       N  
ATOM   2831  CZ  ARG A2243       6.952  83.698 319.700  1.00109.31           C  
ANISOU 2831  CZ  ARG A2243    14016  13035  14480     48   -928   -481       C  
ATOM   2832  NH1 ARG A2243       7.761  83.546 320.740  1.00113.71           N  
ANISOU 2832  NH1 ARG A2243    14510  13755  14941    -29  -1003   -452       N  
ATOM   2833  NH2 ARG A2243       6.874  82.745 318.782  1.00106.90           N  
ANISOU 2833  NH2 ARG A2243    13615  12709  14291    155   -905   -423       N  
ATOM   2834  N   PHE A2244       6.475  88.801 315.955  1.00 81.71           N  
ANISOU 2834  N   PHE A2244    11145   8928  10971   -165   -630   -725       N  
ATOM   2835  CA  PHE A2244       6.717  88.804 314.511  1.00 76.63           C  
ANISOU 2835  CA  PHE A2244    10443   8262  10409   -146   -614   -694       C  
ATOM   2836  C   PHE A2244       5.970  89.929 313.796  1.00 68.29           C  
ANISOU 2836  C   PHE A2244     9587   7022   9336    -73   -498   -692       C  
ATOM   2837  O   PHE A2244       5.699  89.842 312.599  1.00 68.93           O  
ANISOU 2837  O   PHE A2244     9623   7088   9479      7   -479   -640       O  
ATOM   2838  CB  PHE A2244       6.335  87.451 313.900  1.00 77.81           C  
ANISOU 2838  CB  PHE A2244    10395   8505  10664     -9   -657   -622       C  
ATOM   2839  CG  PHE A2244       7.176  86.305 314.388  1.00 82.64           C  
ANISOU 2839  CG  PHE A2244    10826   9273  11302    -42   -737   -598       C  
ATOM   2840  CD1 PHE A2244       8.235  85.835 313.632  1.00 82.44           C  
ANISOU 2840  CD1 PHE A2244    10669   9331  11325    -87   -757   -574       C  
ATOM   2841  CD2 PHE A2244       6.908  85.697 315.603  1.00 87.24           C  
ANISOU 2841  CD2 PHE A2244    11372   9923  11854     -4   -776   -582       C  
ATOM   2842  CE1 PHE A2244       9.010  84.782 314.075  1.00 84.35           C  
ANISOU 2842  CE1 PHE A2244    10744   9718  11587    -68   -805   -521       C  
ATOM   2843  CE2 PHE A2244       7.679  84.644 316.053  1.00 88.49           C  
ANISOU 2843  CE2 PHE A2244    11370  10224  12030     -1   -837   -531       C  
ATOM   2844  CZ  PHE A2244       8.732  84.185 315.288  1.00 86.11           C  
ANISOU 2844  CZ  PHE A2244    10935  10003  11779    -19   -846   -493       C  
ATOM   2845  N   VAL A2245       5.646  90.986 314.536  1.00 63.45           N  
ANISOU 2845  N   VAL A2245     9214   6267   8627    -95   -410   -740       N  
ATOM   2846  CA  VAL A2245       4.948  92.134 313.971  1.00 58.91           C  
ANISOU 2846  CA  VAL A2245     8868   5491   8023     11   -266   -717       C  
ATOM   2847  C   VAL A2245       5.849  92.873 312.988  1.00 62.72           C  
ANISOU 2847  C   VAL A2245     9439   5891   8499   -139   -233   -741       C  
ATOM   2848  O   VAL A2245       5.411  93.270 311.908  1.00 70.48           O  
ANISOU 2848  O   VAL A2245    10469   6796   9515    -19   -164   -671       O  
ATOM   2849  CB  VAL A2245       4.474  93.102 315.072  1.00 56.03           C  
ANISOU 2849  CB  VAL A2245     8793   4956   7541     26   -140   -772       C  
ATOM   2850  CG1 VAL A2245       3.855  94.352 314.463  1.00 53.62           C  
ANISOU 2850  CG1 VAL A2245     8760   4412   7199    162     45   -730       C  
ATOM   2851  CG2 VAL A2245       3.485  92.404 315.994  1.00 53.48           C  
ANISOU 2851  CG2 VAL A2245     8380   4719   7221    195   -153   -733       C  
ATOM   2852  N   ARG A2246       7.112  93.046 313.367  1.00 58.53           N  
ANISOU 2852  N   ARG A2246     8915   5407   7915   -409   -285   -826       N  
ATOM   2853  CA  ARG A2246       8.103  93.641 312.480  1.00 55.94           C  
ANISOU 2853  CA  ARG A2246     8633   5044   7578   -594   -264   -846       C  
ATOM   2854  C   ARG A2246       8.282  92.797 311.226  1.00 52.55           C  
ANISOU 2854  C   ARG A2246     7954   4745   7267   -504   -325   -767       C  
ATOM   2855  O   ARG A2246       8.504  93.321 310.134  1.00 51.19           O  
ANISOU 2855  O   ARG A2246     7846   4497   7107   -524   -265   -740       O  
ATOM   2856  CB  ARG A2246       9.445  93.794 313.194  1.00 54.47           C  
ANISOU 2856  CB  ARG A2246     8421   4972   7302   -924   -336   -933       C  
ATOM   2857  CG  ARG A2246       9.527  94.974 314.135  1.00 59.24           C  
ANISOU 2857  CG  ARG A2246     9365   5400   7744  -1122   -244  -1041       C  
ATOM   2858  CD  ARG A2246      10.814  94.920 314.935  1.00 69.73           C  
ANISOU 2858  CD  ARG A2246    10600   6932   8962  -1474   -358  -1114       C  
ATOM   2859  NE  ARG A2246      10.844  93.764 315.826  1.00 74.36           N  
ANISOU 2859  NE  ARG A2246    10919   7768   9565  -1408   -502  -1082       N  
ATOM   2860  CZ  ARG A2246      11.891  93.418 316.570  1.00 74.77           C  
ANISOU 2860  CZ  ARG A2246    10794   8086   9530  -1646   -634  -1097       C  
ATOM   2861  NH1 ARG A2246      13.004  94.137 316.527  1.00 76.31           N  
ANISOU 2861  NH1 ARG A2246    11030   8355   9609  -1999   -649  -1152       N  
ATOM   2862  NH2 ARG A2246      11.824  92.351 317.354  1.00 73.10           N  
ANISOU 2862  NH2 ARG A2246    10358   8082   9336  -1537   -747  -1044       N  
ATOM   2863  N   LEU A2247       8.184  91.483 311.397  1.00 46.71           N  
ANISOU 2863  N   LEU A2247     6959   4188   6601   -409   -431   -730       N  
ATOM   2864  CA  LEU A2247       8.355  90.553 310.294  1.00 45.42           C  
ANISOU 2864  CA  LEU A2247     6591   4135   6532   -333   -473   -671       C  
ATOM   2865  C   LEU A2247       7.245  90.686 309.262  1.00 54.98           C  
ANISOU 2865  C   LEU A2247     7858   5259   7771   -147   -415   -604       C  
ATOM   2866  O   LEU A2247       7.506  90.931 308.084  1.00 61.29           O  
ANISOU 2866  O   LEU A2247     8667   6036   8584   -161   -381   -576       O  
ATOM   2867  CB  LEU A2247       8.410  89.116 310.815  1.00 43.79           C  
ANISOU 2867  CB  LEU A2247     6159   4098   6382   -265   -567   -648       C  
ATOM   2868  CG  LEU A2247       8.499  88.060 309.715  1.00 47.83           C  
ANISOU 2868  CG  LEU A2247     6512   4685   6975   -180   -581   -598       C  
ATOM   2869  CD1 LEU A2247       9.640  88.408 308.790  1.00 60.47           C  
ANISOU 2869  CD1 LEU A2247     8081   6314   8580   -300   -553   -601       C  
ATOM   2870  CD2 LEU A2247       8.689  86.671 310.293  1.00 42.93           C  
ANISOU 2870  CD2 LEU A2247     5720   4193   6400   -119   -640   -573       C  
ATOM   2871  N   VAL A2248       6.007  90.514 309.714  1.00 55.37           N  
ANISOU 2871  N   VAL A2248     7928   5292   7819     21   -406   -566       N  
ATOM   2872  CA  VAL A2248       4.849  90.531 308.829  1.00 54.58           C  
ANISOU 2872  CA  VAL A2248     7825   5185   7727    201   -371   -475       C  
ATOM   2873  C   VAL A2248       4.732  91.855 308.078  1.00 60.08           C  
ANISOU 2873  C   VAL A2248     8723   5729   8375    235   -260   -434       C  
ATOM   2874  O   VAL A2248       4.464  91.870 306.877  1.00 64.84           O  
ANISOU 2874  O   VAL A2248     9293   6360   8981    298   -250   -362       O  
ATOM   2875  CB  VAL A2248       3.551  90.267 309.614  1.00 49.08           C  
ANISOU 2875  CB  VAL A2248     7105   4523   7020    366   -367   -426       C  
ATOM   2876  CG1 VAL A2248       2.338  90.377 308.705  1.00 51.29           C  
ANISOU 2876  CG1 VAL A2248     7349   4853   7286    542   -337   -304       C  
ATOM   2877  CG2 VAL A2248       3.612  88.896 310.267  1.00 45.84           C  
ANISOU 2877  CG2 VAL A2248     6512   4250   6655    333   -466   -453       C  
ATOM   2878  N   ALA A2249       4.950  92.960 308.785  1.00 59.90           N  
ANISOU 2878  N   ALA A2249     8933   5535   8292    183   -166   -480       N  
ATOM   2879  CA  ALA A2249       4.885  94.285 308.178  1.00 60.48           C  
ANISOU 2879  CA  ALA A2249     9259   5411   8308    215    -25   -440       C  
ATOM   2880  C   ALA A2249       5.890  94.420 307.039  1.00 64.35           C  
ANISOU 2880  C   ALA A2249     9730   5907   8812     61    -35   -449       C  
ATOM   2881  O   ALA A2249       5.631  95.096 306.045  1.00 67.44           O  
ANISOU 2881  O   ALA A2249    10234   6211   9180    143     49   -367       O  
ATOM   2882  CB  ALA A2249       5.125  95.361 309.226  1.00 57.74           C  
ANISOU 2882  CB  ALA A2249     9211   4851   7877    123     91   -522       C  
ATOM   2883  N   ALA A2250       7.037  93.767 307.193  1.00 64.38           N  
ANISOU 2883  N   ALA A2250     9581   6032   8850   -147   -130   -532       N  
ATOM   2884  CA  ALA A2250       8.073  93.790 306.169  1.00 64.07           C  
ANISOU 2884  CA  ALA A2250     9487   6031   8824   -295   -133   -537       C  
ATOM   2885  C   ALA A2250       7.695  92.889 304.999  1.00 66.25           C  
ANISOU 2885  C   ALA A2250     9581   6440   9153   -166   -183   -464       C  
ATOM   2886  O   ALA A2250       7.843  93.270 303.837  1.00 69.29           O  
ANISOU 2886  O   ALA A2250    10014   6793   9519   -166   -133   -414       O  
ATOM   2887  CB  ALA A2250       9.410  93.369 306.756  1.00 60.98           C  
ANISOU 2887  CB  ALA A2250     8960   5769   8442   -533   -207   -621       C  
ATOM   2888  N   VAL A2251       7.206  91.693 305.314  1.00 62.80           N  
ANISOU 2888  N   VAL A2251     8955   6144   8763    -74   -275   -460       N  
ATOM   2889  CA  VAL A2251       6.793  90.738 304.293  1.00 62.18           C  
ANISOU 2889  CA  VAL A2251     8732   6185   8708     10   -320   -411       C  
ATOM   2890  C   VAL A2251       5.630  91.293 303.474  1.00 67.26           C  
ANISOU 2890  C   VAL A2251     9456   6801   9297    165   -280   -304       C  
ATOM   2891  O   VAL A2251       5.589  91.137 302.251  1.00 71.69           O  
ANISOU 2891  O   VAL A2251     9990   7419   9832    172   -279   -257       O  
ATOM   2892  CB  VAL A2251       6.391  89.385 304.916  1.00 56.53           C  
ANISOU 2892  CB  VAL A2251     7849   5593   8037     59   -406   -430       C  
ATOM   2893  CG1 VAL A2251       5.863  88.438 303.851  1.00 53.66           C  
ANISOU 2893  CG1 VAL A2251     7391   5330   7668    106   -438   -394       C  
ATOM   2894  CG2 VAL A2251       7.575  88.767 305.641  1.00 58.60           C  
ANISOU 2894  CG2 VAL A2251     8008   5911   8345    -56   -442   -499       C  
ATOM   2895  N   VAL A2252       4.695  91.950 304.155  1.00 64.80           N  
ANISOU 2895  N   VAL A2252     9244   6420   8956    299   -237   -253       N  
ATOM   2896  CA  VAL A2252       3.561  92.583 303.490  1.00 62.69           C  
ANISOU 2896  CA  VAL A2252     9038   6153   8628    489   -184   -112       C  
ATOM   2897  C   VAL A2252       4.040  93.696 302.563  1.00 69.60           C  
ANISOU 2897  C   VAL A2252    10098   6891   9457    472    -81    -65       C  
ATOM   2898  O   VAL A2252       3.564  93.822 301.432  1.00 75.78           O  
ANISOU 2898  O   VAL A2252    10861   7745  10189    562    -75     48       O  
ATOM   2899  CB  VAL A2252       2.550  93.151 304.512  1.00 54.61           C  
ANISOU 2899  CB  VAL A2252     8100   5066   7582    669   -119    -55       C  
ATOM   2900  CG1 VAL A2252       1.599  94.136 303.850  1.00 56.07           C  
ANISOU 2900  CG1 VAL A2252     8393   5217   7696    897    -14    120       C  
ATOM   2901  CG2 VAL A2252       1.776  92.023 305.169  1.00 53.01           C  
ANISOU 2901  CG2 VAL A2252     7689   5043   7407    716   -218    -55       C  
ATOM   2902  N   ALA A2253       4.996  94.487 303.041  1.00 66.24           N  
ANISOU 2902  N   ALA A2253     9855   6280   9034    332     -2   -149       N  
ATOM   2903  CA  ALA A2253       5.555  95.581 302.255  1.00 64.88           C  
ANISOU 2903  CA  ALA A2253     9892   5946   8814    274    115   -116       C  
ATOM   2904  C   ALA A2253       6.207  95.073 300.971  1.00 67.36           C  
ANISOU 2904  C   ALA A2253    10081   6379   9132    173     66   -109       C  
ATOM   2905  O   ALA A2253       6.064  95.680 299.909  1.00 70.88           O  
ANISOU 2905  O   ALA A2253    10627   6783   9522    232    134     -9       O  
ATOM   2906  CB  ALA A2253       6.560  96.366 303.082  1.00 61.03           C  
ANISOU 2906  CB  ALA A2253     9606   5269   8314     61    192   -234       C  
ATOM   2907  N   ALA A2254       6.921  93.956 301.073  1.00 65.86           N  
ANISOU 2907  N   ALA A2254     9686   6335   9001     37    -36   -205       N  
ATOM   2908  CA  ALA A2254       7.581  93.360 299.918  1.00 67.84           C  
ANISOU 2908  CA  ALA A2254     9826   6696   9253    -49    -61   -210       C  
ATOM   2909  C   ALA A2254       6.560  92.755 298.963  1.00 72.09           C  
ANISOU 2909  C   ALA A2254    10273   7373   9744     93   -113   -120       C  
ATOM   2910  O   ALA A2254       6.681  92.882 297.744  1.00 73.11           O  
ANISOU 2910  O   ALA A2254    10428   7536   9815     82    -86    -66       O  
ATOM   2911  CB  ALA A2254       8.577  92.306 300.363  1.00 65.90           C  
ANISOU 2911  CB  ALA A2254     9399   6562   9079   -186   -126   -317       C  
ATOM   2912  N   PHE A2255       5.555  92.097 299.532  1.00 72.70           N  
ANISOU 2912  N   PHE A2255    10245   7548   9832    202   -191   -103       N  
ATOM   2913  CA  PHE A2255       4.493  91.461 298.760  1.00 70.84           C  
ANISOU 2913  CA  PHE A2255     9900   7488   9529    292   -259    -19       C  
ATOM   2914  C   PHE A2255       3.750  92.468 297.889  1.00 73.52           C  
ANISOU 2914  C   PHE A2255    10335   7832   9766    433   -207    146       C  
ATOM   2915  O   PHE A2255       3.355  92.160 296.764  1.00 74.48           O  
ANISOU 2915  O   PHE A2255    10398   8104   9798    437   -249    217       O  
ATOM   2916  CB  PHE A2255       3.519  90.756 299.706  1.00 65.67           C  
ANISOU 2916  CB  PHE A2255     9122   6932   8896    368   -336    -18       C  
ATOM   2917  CG  PHE A2255       2.365  90.089 299.015  1.00 62.01           C  
ANISOU 2917  CG  PHE A2255     8530   6688   8345    415   -418     70       C  
ATOM   2918  CD1 PHE A2255       2.507  88.828 298.462  1.00 64.70           C  
ANISOU 2918  CD1 PHE A2255     8777   7143   8662    275   -485     -5       C  
ATOM   2919  CD2 PHE A2255       1.131  90.714 298.941  1.00 62.17           C  
ANISOU 2919  CD2 PHE A2255     8523   6807   8290    592   -417    235       C  
ATOM   2920  CE1 PHE A2255       1.443  88.208 297.834  1.00 69.00           C  
ANISOU 2920  CE1 PHE A2255     9218   7904   9096    257   -566     63       C  
ATOM   2921  CE2 PHE A2255       0.063  90.101 298.315  1.00 63.05           C  
ANISOU 2921  CE2 PHE A2255     8478   7179   8297    600   -509    331       C  
ATOM   2922  CZ  PHE A2255       0.219  88.846 297.761  1.00 68.12           C  
ANISOU 2922  CZ  PHE A2255     9040   7939   8903    405   -592    234       C  
ATOM   2923  N   ALA A2256       3.569  93.675 298.414  1.00 72.19           N  
ANISOU 2923  N   ALA A2256    10334   7496   9599    550   -105    211       N  
ATOM   2924  CA  ALA A2256       2.833  94.717 297.710  1.00 70.31           C  
ANISOU 2924  CA  ALA A2256    10211   7236   9266    739    -24    399       C  
ATOM   2925  C   ALA A2256       3.695  95.413 296.663  1.00 70.46           C  
ANISOU 2925  C   ALA A2256    10388   7142   9243    654     62    419       C  
ATOM   2926  O   ALA A2256       3.176  96.005 295.718  1.00 75.14           O  
ANISOU 2926  O   ALA A2256    11040   7775   9736    788    105    586       O  
ATOM   2927  CB  ALA A2256       2.286  95.734 298.700  1.00 69.09           C  
ANISOU 2927  CB  ALA A2256    10222   6905   9122    924     94    466       C  
ATOM   2928  N   LEU A2257       5.010  95.342 296.832  1.00 68.57           N  
ANISOU 2928  N   LEU A2257    10201   6783   9068    434     88    265       N  
ATOM   2929  CA  LEU A2257       5.931  96.014 295.920  1.00 73.00           C  
ANISOU 2929  CA  LEU A2257    10908   7236   9592    321    182    275       C  
ATOM   2930  C   LEU A2257       6.394  95.100 294.790  1.00 75.04           C  
ANISOU 2930  C   LEU A2257    11021   7672   9818    207    114    243       C  
ATOM   2931  O   LEU A2257       6.794  95.573 293.727  1.00 80.26           O  
ANISOU 2931  O   LEU A2257    11775   8308  10410    169    181    303       O  
ATOM   2932  CB  LEU A2257       7.145  96.548 296.683  1.00 72.88           C  
ANISOU 2932  CB  LEU A2257    11026   7024   9643    117    262    144       C  
ATOM   2933  CG  LEU A2257       6.916  97.798 297.535  1.00 75.67           C  
ANISOU 2933  CG  LEU A2257    11652   7119   9983    175    394    170       C  
ATOM   2934  CD1 LEU A2257       8.182  98.169 298.290  1.00 79.80           C  
ANISOU 2934  CD1 LEU A2257    12277   7502  10541   -107    443     17       C  
ATOM   2935  CD2 LEU A2257       6.447  98.955 296.669  1.00 74.85           C  
ANISOU 2935  CD2 LEU A2257    11788   6867   9784    333    539    344       C  
ATOM   2936  N   CYS A2258       6.337  93.794 295.022  1.00 71.41           N  
ANISOU 2936  N   CYS A2258    10359   7374   9399    154     -1    149       N  
ATOM   2937  CA  CYS A2258       6.818  92.828 294.041  1.00 69.91           C  
ANISOU 2937  CA  CYS A2258    10069   7320   9172     43    -37     94       C  
ATOM   2938  C   CYS A2258       5.684  92.274 293.184  1.00 73.39           C  
ANISOU 2938  C   CYS A2258    10432   7964   9489    120   -124    184       C  
ATOM   2939  O   CYS A2258       5.864  92.019 291.993  1.00 80.10           O  
ANISOU 2939  O   CYS A2258    11295   8901  10238     57   -118    201       O  
ATOM   2940  CB  CYS A2258       7.558  91.687 294.741  1.00 69.48           C  
ANISOU 2940  CB  CYS A2258     9879   7298   9221    -69    -78    -61       C  
ATOM   2941  SG  CYS A2258       9.020  92.212 295.674  1.00 66.54           S  
ANISOU 2941  SG  CYS A2258     9535   6784   8961   -208     -3   -154       S  
ATOM   2942  N   TRP A2259       4.518  92.085 293.793  1.00 67.48           N  
ANISOU 2942  N   TRP A2259     9599   7309   8732    239   -203    243       N  
ATOM   2943  CA  TRP A2259       3.353  91.590 293.068  1.00 62.66           C  
ANISOU 2943  CA  TRP A2259     8881   6944   7982    283   -302    345       C  
ATOM   2944  C   TRP A2259       2.477  92.744 292.605  1.00 61.87           C  
ANISOU 2944  C   TRP A2259     8833   6896   7778    481   -274    571       C  
ATOM   2945  O   TRP A2259       1.513  92.549 291.865  1.00 60.73           O  
ANISOU 2945  O   TRP A2259     8588   7001   7487    527   -356    703       O  
ATOM   2946  CB  TRP A2259       2.545  90.628 293.938  1.00 60.37           C  
ANISOU 2946  CB  TRP A2259     8434   6778   7725    281   -406    301       C  
ATOM   2947  CG  TRP A2259       3.278  89.368 294.262  1.00 59.34           C  
ANISOU 2947  CG  TRP A2259     8263   6612   7670    112   -426    109       C  
ATOM   2948  CD1 TRP A2259       3.983  89.100 295.397  1.00 60.76           C  
ANISOU 2948  CD1 TRP A2259     8439   6649   8000     90   -398     -8       C  
ATOM   2949  CD2 TRP A2259       3.387  88.203 293.437  1.00 60.62           C  
ANISOU 2949  CD2 TRP A2259     8404   6882   7746    -48   -462     24       C  
ATOM   2950  NE1 TRP A2259       4.522  87.838 295.332  1.00 62.78           N  
ANISOU 2950  NE1 TRP A2259     8657   6916   8279    -38   -406   -139       N  
ATOM   2951  CE2 TRP A2259       4.171  87.267 294.138  1.00 61.52           C  
ANISOU 2951  CE2 TRP A2259     8510   6887   7978   -125   -433   -132       C  
ATOM   2952  CE3 TRP A2259       2.897  87.861 292.173  1.00 62.16           C  
ANISOU 2952  CE3 TRP A2259     8604   7256   7759   -137   -506     67       C  
ATOM   2953  CZ2 TRP A2259       4.475  86.010 293.620  1.00 63.35           C  
ANISOU 2953  CZ2 TRP A2259     8766   7143   8161   -263   -419   -245       C  
ATOM   2954  CZ3 TRP A2259       3.201  86.613 291.658  1.00 63.33           C  
ANISOU 2954  CZ3 TRP A2259     8786   7431   7845   -316   -505    -69       C  
ATOM   2955  CH2 TRP A2259       3.983  85.703 292.381  1.00 64.26           C  
ANISOU 2955  CH2 TRP A2259     8924   7399   8094   -366   -448   -224       C  
ATOM   2956  N   GLY A2260       2.822  93.947 293.051  1.00 64.92           N  
ANISOU 2956  N   GLY A2260     9387   7052   8228    592   -148    621       N  
ATOM   2957  CA  GLY A2260       2.101  95.148 292.670  1.00 68.54           C  
ANISOU 2957  CA  GLY A2260     9949   7495   8596    821    -71    849       C  
ATOM   2958  C   GLY A2260       2.139  95.424 291.179  1.00 72.49           C  
ANISOU 2958  C   GLY A2260    10492   8106   8944    814    -63    973       C  
ATOM   2959  O   GLY A2260       1.110  95.340 290.508  1.00 74.21           O  
ANISOU 2959  O   GLY A2260    10589   8591   9016    926   -142   1150       O  
ATOM   2960  N   PRO A2261       3.326  95.766 290.653  1.00 73.50           N  
ANISOU 2960  N   PRO A2261    10779   8055   9091    673     31    892       N  
ATOM   2961  CA  PRO A2261       3.507  96.043 289.224  1.00 75.23           C  
ANISOU 2961  CA  PRO A2261    11064   8357   9163    647     57    997       C  
ATOM   2962  C   PRO A2261       3.062  94.888 288.328  1.00 69.86           C  
ANISOU 2962  C   PRO A2261    10202   7999   8344    535    -94    981       C  
ATOM   2963  O   PRO A2261       2.589  95.132 287.220  1.00 69.04           O  
ANISOU 2963  O   PRO A2261    10098   8072   8060    585   -119   1144       O  
ATOM   2964  CB  PRO A2261       5.015  96.271 289.103  1.00 74.81           C  
ANISOU 2964  CB  PRO A2261    11161   8071   9192    450    172    846       C  
ATOM   2965  CG  PRO A2261       5.423  96.760 290.442  1.00 71.56           C  
ANISOU 2965  CG  PRO A2261    10838   7412   8939    450    247    756       C  
ATOM   2966  CD  PRO A2261       4.561  96.016 291.417  1.00 72.13           C  
ANISOU 2966  CD  PRO A2261    10731   7607   9067    529    128    717       C  
ATOM   2967  N   TYR A2262       3.209  93.655 288.803  1.00 66.86           N  
ANISOU 2967  N   TYR A2262     9688   7686   8029    376   -185    791       N  
ATOM   2968  CA  TYR A2262       2.818  92.487 288.020  1.00 67.25           C  
ANISOU 2968  CA  TYR A2262     9617   8000   7935    225   -307    742       C  
ATOM   2969  C   TYR A2262       1.338  92.513 287.658  1.00 72.41           C  
ANISOU 2969  C   TYR A2262    10124   8974   8413    333   -433    947       C  
ATOM   2970  O   TYR A2262       0.976  92.455 286.482  1.00 76.58           O  
ANISOU 2970  O   TYR A2262    10637   9726   8735    284   -488   1050       O  
ATOM   2971  CB  TYR A2262       3.134  91.194 288.775  1.00 66.21           C  
ANISOU 2971  CB  TYR A2262     9400   7843   7913     68   -356    519       C  
ATOM   2972  CG  TYR A2262       2.504  89.971 288.145  1.00 70.68           C  
ANISOU 2972  CG  TYR A2262     9875   8662   8319    -97   -474    467       C  
ATOM   2973  CD1 TYR A2262       3.024  89.420 286.980  1.00 74.07           C  
ANISOU 2973  CD1 TYR A2262    10393   9140   8612   -269   -449    388       C  
ATOM   2974  CD2 TYR A2262       1.385  89.371 288.709  1.00 72.43           C  
ANISOU 2974  CD2 TYR A2262     9939   9073   8508   -102   -599    494       C  
ATOM   2975  CE1 TYR A2262       2.450  88.306 286.397  1.00 75.85           C  
ANISOU 2975  CE1 TYR A2262    10584   9575   8662   -460   -543    322       C  
ATOM   2976  CE2 TYR A2262       0.804  88.256 288.133  1.00 76.70           C  
ANISOU 2976  CE2 TYR A2262    10420   9843   8879   -307   -703    437       C  
ATOM   2977  CZ  TYR A2262       1.340  87.728 286.978  1.00 78.00           C  
ANISOU 2977  CZ  TYR A2262    10707  10031   8899   -494   -673    344       C  
ATOM   2978  OH  TYR A2262       0.765  86.618 286.402  1.00 77.80           O  
ANISOU 2978  OH  TYR A2262    10671  10212   8678   -736   -763    269       O  
ATOM   2979  N   HIS A2263       0.486  92.598 288.674  1.00 73.76           N  
ANISOU 2979  N   HIS A2263    10176   9196   8656    477   -479   1015       N  
ATOM   2980  CA  HIS A2263      -0.958  92.583 288.469  1.00 70.74           C  
ANISOU 2980  CA  HIS A2263     9598   9165   8115    589   -599   1228       C  
ATOM   2981  C   HIS A2263      -1.426  93.785 287.657  1.00 71.80           C  
ANISOU 2981  C   HIS A2263     9774   9398   8109    822   -551   1519       C  
ATOM   2982  O   HIS A2263      -2.447  93.719 286.976  1.00 72.14           O  
ANISOU 2982  O   HIS A2263     9649   9814   7948    867   -664   1720       O  
ATOM   2983  CB  HIS A2263      -1.689  92.538 289.812  1.00 63.59           C  
ANISOU 2983  CB  HIS A2263     8564   8266   7332    728   -620   1253       C  
ATOM   2984  CG  HIS A2263      -1.527  91.245 290.546  1.00 59.66           C  
ANISOU 2984  CG  HIS A2263     7987   7756   6926    510   -694   1018       C  
ATOM   2985  ND1 HIS A2263      -0.492  91.008 291.423  1.00 60.78           N  
ANISOU 2985  ND1 HIS A2263     8243   7583   7269    444   -614    804       N  
ATOM   2986  CD2 HIS A2263      -2.271  90.110 290.530  1.00 58.56           C  
ANISOU 2986  CD2 HIS A2263     7673   7887   6692    335   -834    975       C  
ATOM   2987  CE1 HIS A2263      -0.604  89.788 291.919  1.00 59.57           C  
ANISOU 2987  CE1 HIS A2263     7996   7490   7149    274   -692    651       C  
ATOM   2988  NE2 HIS A2263      -1.677  89.224 291.390  1.00 57.58           N  
ANISOU 2988  NE2 HIS A2263     7585   7571   6720    193   -819    742       N  
ATOM   2989  N   VAL A2264      -0.679  94.881 287.730  1.00 73.31           N  
ANISOU 2989  N   VAL A2264    10192   9268   8396    960   -380   1551       N  
ATOM   2990  CA  VAL A2264      -0.996  96.063 286.940  1.00 78.75           C  
ANISOU 2990  CA  VAL A2264    10978   9986   8957   1193   -296   1829       C  
ATOM   2991  C   VAL A2264      -0.867  95.753 285.453  1.00 85.92           C  
ANISOU 2991  C   VAL A2264    11877  11122   9647   1035   -370   1873       C  
ATOM   2992  O   VAL A2264      -1.809  95.949 284.685  1.00 91.43           O  
ANISOU 2992  O   VAL A2264    12445  12160  10132   1149   -454   2125       O  
ATOM   2993  CB  VAL A2264      -0.085  97.252 287.299  1.00 75.80           C  
ANISOU 2993  CB  VAL A2264    10909   9169   8723   1306    -75   1818       C  
ATOM   2994  CG1 VAL A2264      -0.302  98.401 286.325  1.00 76.02           C  
ANISOU 2994  CG1 VAL A2264    11082   9199   8602   1522     32   2101       C  
ATOM   2995  CG2 VAL A2264      -0.340  97.702 288.729  1.00 72.90           C  
ANISOU 2995  CG2 VAL A2264    10587   8586   8526   1481     13   1804       C  
ATOM   2996  N   PHE A2265       0.300  95.254 285.057  1.00 83.17           N  
ANISOU 2996  N   PHE A2265    11655  10608   9338    775   -335   1638       N  
ATOM   2997  CA  PHE A2265       0.564  94.917 283.662  1.00 76.47           C  
ANISOU 2997  CA  PHE A2265    10839   9934   8281    601   -378   1642       C  
ATOM   2998  C   PHE A2265      -0.286  93.745 283.179  1.00 74.12           C  
ANISOU 2998  C   PHE A2265    10331  10044   7785    413   -580   1619       C  
ATOM   2999  O   PHE A2265      -0.747  93.735 282.040  1.00 80.02           O  
ANISOU 2999  O   PHE A2265    11038  11089   8276    365   -660   1763       O  
ATOM   3000  CB  PHE A2265       2.047  94.601 283.464  1.00 75.00           C  
ANISOU 3000  CB  PHE A2265    10830   9468   8200    382   -266   1388       C  
ATOM   3001  CG  PHE A2265       2.923  95.819 283.386  1.00 78.16           C  
ANISOU 3001  CG  PHE A2265    11457   9552   8688    486    -74   1448       C  
ATOM   3002  CD1 PHE A2265       3.298  96.496 284.534  1.00 77.55           C  
ANISOU 3002  CD1 PHE A2265    11472   9167   8825    591     39   1410       C  
ATOM   3003  CD2 PHE A2265       3.377  96.285 282.163  1.00 84.76           C  
ANISOU 3003  CD2 PHE A2265    12433  10399   9374    449     -1   1538       C  
ATOM   3004  CE1 PHE A2265       4.104  97.617 284.465  1.00 80.65           C  
ANISOU 3004  CE1 PHE A2265    12102   9262   9279    634    222   1455       C  
ATOM   3005  CE2 PHE A2265       4.184  97.405 282.087  1.00 88.29           C  
ANISOU 3005  CE2 PHE A2265    13104  10547   9893    513    187   1594       C  
ATOM   3006  CZ  PHE A2265       4.548  98.072 283.240  1.00 86.12           C  
ANISOU 3006  CZ  PHE A2265    12930   9961   9831    593    299   1549       C  
ATOM   3007  N   SER A2266      -0.488  92.759 284.047  1.00 68.10           N  
ANISOU 3007  N   SER A2266     9448   9300   7126    286   -659   1440       N  
ATOM   3008  CA  SER A2266      -1.268  91.577 283.694  1.00 68.21           C  
ANISOU 3008  CA  SER A2266     9294   9668   6954     53   -837   1388       C  
ATOM   3009  C   SER A2266      -2.727  91.934 283.422  1.00 70.41           C  
ANISOU 3009  C   SER A2266     9337  10385   7030    192   -978   1695       C  
ATOM   3010  O   SER A2266      -3.393  91.290 282.611  1.00 71.12           O  
ANISOU 3010  O   SER A2266     9306  10860   6857    -13  -1131   1738       O  
ATOM   3011  CB  SER A2266      -1.182  90.526 284.803  1.00 69.24           C  
ANISOU 3011  CB  SER A2266     9368   9684   7255    -87   -865   1150       C  
ATOM   3012  OG  SER A2266      -1.875  89.345 284.438  1.00 74.37           O  
ANISOU 3012  OG  SER A2266     9905  10637   7715   -359  -1015   1077       O  
ATOM   3013  N   LEU A2267      -3.220  92.960 284.108  1.00 73.07           N  
ANISOU 3013  N   LEU A2267     9612  10676   7474    538   -918   1914       N  
ATOM   3014  CA  LEU A2267      -4.566  93.466 283.866  1.00 75.40           C  
ANISOU 3014  CA  LEU A2267     9669  11393   7588    756  -1016   2263       C  
ATOM   3015  C   LEU A2267      -4.599  94.281 282.581  1.00 75.19           C  
ANISOU 3015  C   LEU A2267     9708  11519   7342    871   -997   2510       C  
ATOM   3016  O   LEU A2267      -5.644  94.417 281.945  1.00 75.50           O  
ANISOU 3016  O   LEU A2267     9527  12026   7132    946  -1126   2792       O  
ATOM   3017  CB  LEU A2267      -5.050  94.318 285.043  1.00 76.15           C  
ANISOU 3017  CB  LEU A2267     9712  11351   7871   1131   -913   2424       C  
ATOM   3018  CG  LEU A2267      -5.541  93.584 286.291  1.00 75.55           C  
ANISOU 3018  CG  LEU A2267     9466  11303   7935   1080   -973   2301       C  
ATOM   3019  CD1 LEU A2267      -5.800  94.570 287.418  1.00 76.06           C  
ANISOU 3019  CD1 LEU A2267     9566  11143   8189   1465   -818   2437       C  
ATOM   3020  CD2 LEU A2267      -6.793  92.780 285.983  1.00 77.61           C  
ANISOU 3020  CD2 LEU A2267     9388  12131   7970    932  -1190   2426       C  
ATOM   3021  N   LEU A2268      -3.445  94.823 282.206  1.00 74.99           N  
ANISOU 3021  N   LEU A2268     9973  11119   7400    878   -837   2417       N  
ATOM   3022  CA  LEU A2268      -3.336  95.627 280.996  1.00 80.11           C  
ANISOU 3022  CA  LEU A2268    10731  11852   7854    983   -790   2637       C  
ATOM   3023  C   LEU A2268      -3.273  94.751 279.748  1.00 85.55           C  
ANISOU 3023  C   LEU A2268    11394  12847   8265    635   -932   2551       C  
ATOM   3024  O   LEU A2268      -3.743  95.149 278.683  1.00 90.45           O  
ANISOU 3024  O   LEU A2268    11966  13784   8616    690   -995   2801       O  
ATOM   3025  CB  LEU A2268      -2.106  96.536 281.066  1.00 77.28           C  
ANISOU 3025  CB  LEU A2268    10704  10978   7679   1086   -553   2565       C  
ATOM   3026  CG  LEU A2268      -2.168  97.682 282.079  1.00 74.74           C  
ANISOU 3026  CG  LEU A2268    10493  10336   7568   1443   -375   2698       C  
ATOM   3027  CD1 LEU A2268      -0.839  98.419 282.150  1.00 72.04           C  
ANISOU 3027  CD1 LEU A2268    10492   9488   7390   1425   -154   2568       C  
ATOM   3028  CD2 LEU A2268      -3.298  98.641 281.738  1.00 77.72           C  
ANISOU 3028  CD2 LEU A2268    10776  10970   7783   1831   -362   3129       C  
ATOM   3029  N   GLU A2269      -2.697  93.559 279.878  1.00 84.06           N  
ANISOU 3029  N   GLU A2269    11253  12560   8125    283   -972   2204       N  
ATOM   3030  CA  GLU A2269      -2.601  92.650 278.740  1.00 87.02           C  
ANISOU 3030  CA  GLU A2269    11659  13177   8228    -73  -1077   2083       C  
ATOM   3031  C   GLU A2269      -3.954  92.001 278.465  1.00 90.79           C  
ANISOU 3031  C   GLU A2269    11850  14216   8430   -224  -1316   2212       C  
ATOM   3032  O   GLU A2269      -4.218  91.546 277.352  1.00 93.83           O  
ANISOU 3032  O   GLU A2269    12225  14932   8494   -476  -1433   2231       O  
ATOM   3033  CB  GLU A2269      -1.530  91.580 278.971  1.00 86.31           C  
ANISOU 3033  CB  GLU A2269    11749  12772   8275   -371  -1001   1680       C  
ATOM   3034  CG  GLU A2269      -1.985  90.382 279.785  1.00 90.57           C  
ANISOU 3034  CG  GLU A2269    12159  13383   8871   -576  -1107   1485       C  
ATOM   3035  CD  GLU A2269      -1.065  89.187 279.619  1.00 92.78           C  
ANISOU 3035  CD  GLU A2269    12637  13444   9170   -896  -1038   1130       C  
ATOM   3036  OE1 GLU A2269      -0.180  89.235 278.738  1.00 91.02           O  
ANISOU 3036  OE1 GLU A2269    12622  13088   8872   -978   -928   1048       O  
ATOM   3037  OE2 GLU A2269      -1.226  88.200 280.367  1.00 96.52           O  
ANISOU 3037  OE2 GLU A2269    13068  13874   9730  -1050  -1076    944       O  
ATOM   3038  N   ALA A2270      -4.807  91.958 279.483  1.00 89.52           N  
ANISOU 3038  N   ALA A2270    11455  14178   8379    -91  -1387   2302       N  
ATOM   3039  CA  ALA A2270      -6.185  91.520 279.303  1.00 89.07           C  
ANISOU 3039  CA  ALA A2270    11071  14705   8064   -196  -1612   2489       C  
ATOM   3040  C   ALA A2270      -6.979  92.664 278.685  1.00 94.37           C  
ANISOU 3040  C   ALA A2270    11573  15738   8546    139  -1652   2939       C  
ATOM   3041  O   ALA A2270      -7.987  92.454 278.009  1.00 95.24           O  
ANISOU 3041  O   ALA A2270    11426  16428   8333     31  -1848   3156       O  
ATOM   3042  CB  ALA A2270      -6.794  91.087 280.626  1.00 79.44           C  
ANISOU 3042  CB  ALA A2270     9655  13496   7035   -158  -1654   2439       C  
ATOM   3043  N   ARG A2271      -6.500  93.880 278.928  1.00 96.61           N  
ANISOU 3043  N   ARG A2271    12013  15674   9021    541  -1455   3085       N  
ATOM   3044  CA  ARG A2271      -7.089  95.086 278.366  1.00104.60           C  
ANISOU 3044  CA  ARG A2271    12942  16916   9884    927  -1427   3522       C  
ATOM   3045  C   ARG A2271      -6.565  95.311 276.953  1.00112.96           C  
ANISOU 3045  C   ARG A2271    14180  18040  10698    807  -1423   3569       C  
ATOM   3046  O   ARG A2271      -7.192  95.997 276.145  1.00118.75           O  
ANISOU 3046  O   ARG A2271    14800  19136  11184   1009  -1473   3939       O  
ATOM   3047  CB  ARG A2271      -6.769  96.293 279.253  1.00103.78           C  
ANISOU 3047  CB  ARG A2271    12999  16350  10081   1390  -1182   3639       C  
ATOM   3048  CG  ARG A2271      -7.494  97.578 278.887  1.00107.95           C  
ANISOU 3048  CG  ARG A2271    13456  17072  10487   1871  -1109   4123       C  
ATOM   3049  CD  ARG A2271      -8.950  97.540 279.318  1.00111.22           C  
ANISOU 3049  CD  ARG A2271    13454  18008  10796   2083  -1242   4432       C  
ATOM   3050  NE  ARG A2271      -9.527  98.880 279.378  1.00115.27           N  
ANISOU 3050  NE  ARG A2271    13950  18545  11301   2659  -1083   4879       N  
ATOM   3051  CZ  ARG A2271     -10.074  99.506 278.341  1.00121.32           C  
ANISOU 3051  CZ  ARG A2271    14612  19700  11786   2879  -1119   5283       C  
ATOM   3052  NH1 ARG A2271     -10.122  98.913 277.156  1.00122.30           N  
ANISOU 3052  NH1 ARG A2271    14630  20240  11598   2537  -1329   5281       N  
ATOM   3053  NH2 ARG A2271     -10.573 100.726 278.489  1.00126.29           N  
ANISOU 3053  NH2 ARG A2271    15264  20220  12500   3383   -909   5585       N  
ATOM   3054  N   ALA A2272      -5.412  94.715 276.662  1.00114.48           N  
ANISOU 3054  N   ALA A2272    14649  17895  10955    490  -1354   3206       N  
ATOM   3055  CA  ALA A2272      -4.736  94.913 275.384  1.00118.23           C  
ANISOU 3055  CA  ALA A2272    15342  18352  11230    367  -1309   3204       C  
ATOM   3056  C   ALA A2272      -5.388  94.130 274.247  1.00124.89           C  
ANISOU 3056  C   ALA A2272    16039  19767  11648     24  -1540   3247       C  
ATOM   3057  O   ALA A2272      -5.047  94.324 273.080  1.00129.42           O  
ANISOU 3057  O   ALA A2272    16755  20436  11983    -68  -1531   3306       O  
ATOM   3058  CB  ALA A2272      -3.269  94.533 275.505  1.00115.29           C  
ANISOU 3058  CB  ALA A2272    15294  17437  11073    164  -1135   2812       C  
ATOM   3059  N   HIS A2273      -6.318  93.242 274.584  1.00121.12           N  
ANISOU 3059  N   HIS A2273    15288  19674  11057   -193  -1743   3213       N  
ATOM   3060  CA  HIS A2273      -7.047  92.495 273.566  1.00120.08           C  
ANISOU 3060  CA  HIS A2273    15002  20134  10488   -566  -1980   3260       C  
ATOM   3061  C   HIS A2273      -7.925  93.437 272.751  1.00118.78           C  
ANISOU 3061  C   HIS A2273    14615  20491  10026   -300  -2086   3754       C  
ATOM   3062  O   HIS A2273      -8.069  93.278 271.540  1.00121.21           O  
ANISOU 3062  O   HIS A2273    14933  21165   9956   -525  -2204   3835       O  
ATOM   3063  CB  HIS A2273      -7.900  91.393 274.197  1.00120.62           C  
ANISOU 3063  CB  HIS A2273    14819  20506  10507   -868  -2167   3134       C  
ATOM   3064  CG  HIS A2273      -8.687  90.598 273.202  1.00124.91           C  
ANISOU 3064  CG  HIS A2273    15208  21676  10577  -1315  -2418   3169       C  
ATOM   3065  ND1 HIS A2273      -8.249  89.393 272.697  1.00125.62           N  
ANISOU 3065  ND1 HIS A2273    15528  21706  10495  -1854  -2452   2790       N  
ATOM   3066  CD2 HIS A2273      -9.881  90.842 272.608  1.00127.20           C  
ANISOU 3066  CD2 HIS A2273    15144  22680  10506  -1315  -2643   3544       C  
ATOM   3067  CE1 HIS A2273      -9.141  88.924 271.842  1.00127.42           C  
ANISOU 3067  CE1 HIS A2273    15574  22569  10268  -2207  -2691   2907       C  
ATOM   3068  NE2 HIS A2273     -10.140  89.786 271.771  1.00128.25           N  
ANISOU 3068  NE2 HIS A2273    15303  23114  10313  -1879  -2793   3338       N  
ATOM   3069  N   ALA A2274      -8.510  94.419 273.429  1.00116.83           N  
ANISOU 3069  N   ALA A2274    14177  20274   9938    194  -2029   4091       N  
ATOM   3070  CA  ALA A2274      -9.349  95.413 272.774  1.00119.31           C  
ANISOU 3070  CA  ALA A2274    14274  21054  10004    550  -2089   4612       C  
ATOM   3071  C   ALA A2274      -8.503  96.557 272.229  1.00121.50           C  
ANISOU 3071  C   ALA A2274    14879  20936  10349    871  -1859   4745       C  
ATOM   3072  O   ALA A2274      -8.775  97.085 271.150  1.00128.99           O  
ANISOU 3072  O   ALA A2274    15795  22225  10989    967  -1911   5055       O  
ATOM   3073  CB  ALA A2274     -10.399  95.940 273.738  1.00118.68           C  
ANISOU 3073  CB  ALA A2274    13859  21153  10081    963  -2087   4908       C  
ATOM   3074  N   ASN A2275      -7.477  96.935 272.985  1.00117.18           N  
ANISOU 3074  N   ASN A2275    14644  19685  10193   1017  -1606   4516       N  
ATOM   3075  CA  ASN A2275      -6.569  98.000 272.574  1.00118.56           C  
ANISOU 3075  CA  ASN A2275    15164  19419  10462   1270  -1361   4599       C  
ATOM   3076  C   ASN A2275      -5.222  97.448 272.124  1.00115.40           C  
ANISOU 3076  C   ASN A2275    15107  18621  10118    892  -1267   4181       C  
ATOM   3077  O   ASN A2275      -4.384  97.098 272.954  1.00113.73           O  
ANISOU 3077  O   ASN A2275    15062  17925  10226    783  -1143   3832       O  
ATOM   3078  CB  ASN A2275      -6.363  99.000 273.713  1.00119.81           C  
ANISOU 3078  CB  ASN A2275    15451  19076  10997   1720  -1115   4682       C  
ATOM   3079  CG  ASN A2275      -7.667  99.571 274.232  1.00127.21           C  
ANISOU 3079  CG  ASN A2275    16071  20363  11901   2150  -1159   5100       C  
ATOM   3080  OD1 ASN A2275      -8.684  99.557 273.541  1.00134.61           O  
ANISOU 3080  OD1 ASN A2275    16701  21937  12510   2211  -1346   5439       O  
ATOM   3081  ND2 ASN A2275      -7.640 100.086 275.456  1.00127.79           N  
ANISOU 3081  ND2 ASN A2275    16212  20041  12299   2452   -981   5087       N  
ATOM   3082  N   PRO A2276      -5.005  97.377 270.802  1.00113.82           N  
ANISOU 3082  N   PRO A2276    15006  18645   9596    702  -1319   4232       N  
ATOM   3083  CA  PRO A2276      -3.747  96.859 270.254  1.00112.07           C  
ANISOU 3083  CA  PRO A2276    15105  18088   9389    360  -1212   3866       C  
ATOM   3084  C   PRO A2276      -2.555  97.751 270.591  1.00109.50           C  
ANISOU 3084  C   PRO A2276    15106  17115   9383    576   -910   3794       C  
ATOM   3085  O   PRO A2276      -1.413  97.293 270.553  1.00108.22           O  
ANISOU 3085  O   PRO A2276    15177  16591   9353    331   -786   3450       O  
ATOM   3086  CB  PRO A2276      -4.007  96.838 268.744  1.00117.38           C  
ANISOU 3086  CB  PRO A2276    15783  19214   9601    201  -1331   4047       C  
ATOM   3087  CG  PRO A2276      -5.056  97.874 268.528  1.00120.71           C  
ANISOU 3087  CG  PRO A2276    15983  20021   9860    622  -1396   4580       C  
ATOM   3088  CD  PRO A2276      -5.933  97.814 269.745  1.00117.45           C  
ANISOU 3088  CD  PRO A2276    15274  19706   9646    821  -1472   4663       C  
ATOM   3089  N   GLY A2277      -2.826  99.008 270.925  1.00111.05           N  
ANISOU 3089  N   GLY A2277    15325  17177   9692   1026   -781   4125       N  
ATOM   3090  CA  GLY A2277      -1.777  99.962 271.237  1.00110.95           C  
ANISOU 3090  CA  GLY A2277    15641  16566   9950   1212   -490   4088       C  
ATOM   3091  C   GLY A2277      -1.070  99.687 272.550  1.00112.95           C  
ANISOU 3091  C   GLY A2277    15975  16336  10607   1147   -375   3747       C  
ATOM   3092  O   GLY A2277       0.048 100.152 272.768  1.00113.24           O  
ANISOU 3092  O   GLY A2277    16285  15886  10855   1135   -156   3597       O  
ATOM   3093  N   LEU A2278      -1.721  98.930 273.429  1.00114.90           N  
ANISOU 3093  N   LEU A2278    15973  16737  10946   1090   -525   3633       N  
ATOM   3094  CA  LEU A2278      -1.150  98.613 274.735  1.00109.29           C  
ANISOU 3094  CA  LEU A2278    15309  15618  10599   1036   -438   3328       C  
ATOM   3095  C   LEU A2278      -0.200  97.420 274.671  1.00107.25           C  
ANISOU 3095  C   LEU A2278    15123  15226  10400    613   -456   2899       C  
ATOM   3096  O   LEU A2278       0.645  97.244 275.548  1.00105.09           O  
ANISOU 3096  O   LEU A2278    14953  14559  10419    548   -339   2638       O  
ATOM   3097  CB  LEU A2278      -2.262  98.335 275.751  1.00103.72           C  
ANISOU 3097  CB  LEU A2278    14315  15123   9970   1179   -572   3405       C  
ATOM   3098  CG  LEU A2278      -3.161  99.511 276.140  1.00101.03           C  
ANISOU 3098  CG  LEU A2278    13906  14835   9644   1663   -502   3810       C  
ATOM   3099  CD1 LEU A2278      -4.222  99.065 277.134  1.00 99.57           C  
ANISOU 3099  CD1 LEU A2278    13409  14896   9528   1760   -636   3854       C  
ATOM   3100  CD2 LEU A2278      -2.337 100.655 276.709  1.00 98.11           C  
ANISOU 3100  CD2 LEU A2278    13871  13873   9534   1898   -210   3813       C  
ATOM   3101  N   ARG A2279      -0.343  96.609 273.627  1.00108.24           N  
ANISOU 3101  N   ARG A2279    15205  15690  10232    334   -592   2839       N  
ATOM   3102  CA  ARG A2279       0.450  95.389 273.471  1.00105.06           C  
ANISOU 3102  CA  ARG A2279    14890  15188   9840    -52   -593   2451       C  
ATOM   3103  C   ARG A2279       1.968  95.626 273.422  1.00104.60           C  
ANISOU 3103  C   ARG A2279    15105  14659   9977   -109   -351   2246       C  
ATOM   3104  O   ARG A2279       2.721  94.865 274.032  1.00102.28           O  
ANISOU 3104  O   ARG A2279    14853  14122   9886   -275   -289   1936       O  
ATOM   3105  CB  ARG A2279      -0.005  94.630 272.218  1.00106.07           C  
ANISOU 3105  CB  ARG A2279    14981  15758   9561   -337   -754   2454       C  
ATOM   3106  CG  ARG A2279      -1.455  94.178 272.280  1.00105.41           C  
ANISOU 3106  CG  ARG A2279    14593  16195   9262   -381  -1016   2611       C  
ATOM   3107  CD  ARG A2279      -1.941  93.635 270.950  1.00106.15           C  
ANISOU 3107  CD  ARG A2279    14662  16768   8900   -669  -1180   2665       C  
ATOM   3108  NE  ARG A2279      -3.347  93.247 271.011  1.00108.15           N  
ANISOU 3108  NE  ARG A2279    14590  17575   8927   -740  -1443   2840       N  
ATOM   3109  CZ  ARG A2279      -4.063  92.854 269.962  1.00110.70           C  
ANISOU 3109  CZ  ARG A2279    14811  18435   8813   -988  -1639   2955       C  
ATOM   3110  NH1 ARG A2279      -3.506  92.798 268.760  1.00115.53           N  
ANISOU 3110  NH1 ARG A2279    15649  19080   9166  -1176  -1594   2905       N  
ATOM   3111  NH2 ARG A2279      -5.337  92.519 270.115  1.00108.92           N  
ANISOU 3111  NH2 ARG A2279    14252  18739   8394  -1064  -1881   3125       N  
ATOM   3112  N   PRO A2280       2.433  96.666 272.700  1.00107.97           N  
ANISOU 3112  N   PRO A2280    15711  14974  10339     26   -208   2433       N  
ATOM   3113  CA  PRO A2280       3.878  96.912 272.784  1.00105.00           C  
ANISOU 3113  CA  PRO A2280    15560  14166  10169    -43     24   2244       C  
ATOM   3114  C   PRO A2280       4.318  97.411 274.161  1.00100.64           C  
ANISOU 3114  C   PRO A2280    15024  13225   9988    101    141   2170       C  
ATOM   3115  O   PRO A2280       5.448  97.148 274.569  1.00100.68           O  
ANISOU 3115  O   PRO A2280    15117  12940  10198    -36    273   1926       O  
ATOM   3116  CB  PRO A2280       4.115  97.989 271.718  1.00106.22           C  
ANISOU 3116  CB  PRO A2280    15899  14314  10147     73    144   2500       C  
ATOM   3117  CG  PRO A2280       2.972  97.854 270.779  1.00109.65           C  
ANISOU 3117  CG  PRO A2280    16211  15241  10213     91    -51   2736       C  
ATOM   3118  CD  PRO A2280       1.809  97.481 271.641  1.00110.59           C  
ANISOU 3118  CD  PRO A2280    16059  15587  10375    185   -245   2790       C  
ATOM   3119  N   LEU A2281       3.435  98.120 274.860  1.00 96.26           N  
ANISOU 3119  N   LEU A2281    14384  12686   9505    376     99   2386       N  
ATOM   3120  CA  LEU A2281       3.753  98.660 276.180  1.00 92.60           C  
ANISOU 3120  CA  LEU A2281    13965  11859   9360    512    212   2327       C  
ATOM   3121  C   LEU A2281       3.903  97.540 277.206  1.00 85.82           C  
ANISOU 3121  C   LEU A2281    12954  10961   8693    348    126   2026       C  
ATOM   3122  O   LEU A2281       4.733  97.621 278.112  1.00 77.50           O  
ANISOU 3122  O   LEU A2281    11966   9585   7897    307    238   1848       O  
ATOM   3123  CB  LEU A2281       2.672  99.652 276.626  1.00 93.89           C  
ANISOU 3123  CB  LEU A2281    14091  12063   9519    875    207   2647       C  
ATOM   3124  CG  LEU A2281       3.002 100.689 277.708  1.00 90.04           C  
ANISOU 3124  CG  LEU A2281    13778  11144   9289   1069    397   2675       C  
ATOM   3125  CD1 LEU A2281       2.064 101.881 277.593  1.00 93.89           C  
ANISOU 3125  CD1 LEU A2281    14336  11660   9678   1463    468   3066       C  
ATOM   3126  CD2 LEU A2281       2.924 100.098 279.108  1.00 85.31           C  
ANISOU 3126  CD2 LEU A2281    13044  10442   8930   1029    338   2457       C  
ATOM   3127  N   VAL A2282       3.093  96.497 277.053  1.00 87.13           N  
ANISOU 3127  N   VAL A2282    12922  11467   8716    238    -72   1978       N  
ATOM   3128  CA  VAL A2282       3.097  95.368 277.977  1.00 82.48           C  
ANISOU 3128  CA  VAL A2282    12198  10862   8279     88   -156   1716       C  
ATOM   3129  C   VAL A2282       4.451  94.667 278.024  1.00 88.55           C  
ANISOU 3129  C   VAL A2282    13078  11386   9181   -142    -38   1408       C  
ATOM   3130  O   VAL A2282       5.022  94.478 279.097  1.00 91.22           O  
ANISOU 3130  O   VAL A2282    13401  11481   9776   -150     21   1242       O  
ATOM   3131  CB  VAL A2282       2.011  94.338 277.604  1.00 74.98           C  
ANISOU 3131  CB  VAL A2282    11055  10337   7099    -52   -378   1719       C  
ATOM   3132  CG1 VAL A2282       2.199  93.053 278.394  1.00 72.34           C  
ANISOU 3132  CG1 VAL A2282    10646   9940   6901   -257   -429   1418       C  
ATOM   3133  CG2 VAL A2282       0.627  94.918 277.842  1.00 71.30           C  
ANISOU 3133  CG2 VAL A2282    10396  10152   6542    194   -505   2026       C  
ATOM   3134  N   TRP A2283       4.972  94.300 276.858  1.00 95.35           N  
ANISOU 3134  N   TRP A2283    14049  12326   9856   -315      6   1348       N  
ATOM   3135  CA  TRP A2283       6.205  93.521 276.789  1.00101.43           C  
ANISOU 3135  CA  TRP A2283    14908  12911  10719   -512    133   1075       C  
ATOM   3136  C   TRP A2283       7.461  94.361 276.999  1.00106.72           C  
ANISOU 3136  C   TRP A2283    15702  13263  11584   -466    341   1060       C  
ATOM   3137  O   TRP A2283       8.578  93.879 276.808  1.00110.59           O  
ANISOU 3137  O   TRP A2283    16253  13631  12135   -602    473    883       O  
ATOM   3138  CB  TRP A2283       6.286  92.782 275.453  1.00107.82           C  
ANISOU 3138  CB  TRP A2283    15809  13920  11236   -716    126   1009       C  
ATOM   3139  CG  TRP A2283       5.335  91.631 275.382  1.00112.80           C  
ANISOU 3139  CG  TRP A2283    16344  14818  11695   -872    -53    920       C  
ATOM   3140  CD1 TRP A2283       4.272  91.492 274.538  1.00116.75           C  
ANISOU 3140  CD1 TRP A2283    16801  15687  11873   -953   -219   1056       C  
ATOM   3141  CD2 TRP A2283       5.347  90.464 276.211  1.00111.48           C  
ANISOU 3141  CD2 TRP A2283    16116  14583  11657   -988    -85    685       C  
ATOM   3142  NE1 TRP A2283       3.627  90.302 274.783  1.00117.23           N  
ANISOU 3142  NE1 TRP A2283    16784  15911  11848  -1149   -352    904       N  
ATOM   3143  CE2 TRP A2283       4.268  89.653 275.807  1.00114.36           C  
ANISOU 3143  CE2 TRP A2283    16425  15263  11764  -1163   -263    674       C  
ATOM   3144  CE3 TRP A2283       6.169  90.021 277.253  1.00105.49           C  
ANISOU 3144  CE3 TRP A2283    15346  13542  11194   -969     20    494       C  
ATOM   3145  CZ2 TRP A2283       3.990  88.428 276.409  1.00112.21           C  
ANISOU 3145  CZ2 TRP A2283    16117  14990  11527  -1325   -321    469       C  
ATOM   3146  CZ3 TRP A2283       5.892  88.805 277.847  1.00102.50           C  
ANISOU 3146  CZ3 TRP A2283    14922  13170  10854  -1090    -38    308       C  
ATOM   3147  CH2 TRP A2283       4.812  88.022 277.424  1.00106.27           C  
ANISOU 3147  CH2 TRP A2283    15376  13923  11077  -1270   -198    291       C  
ATOM   3148  N   ARG A2284       7.276  95.614 277.397  1.00114.06           N  
ANISOU 3148  N   ARG A2284    16675  14063  12600   -278    384   1252       N  
ATOM   3149  CA  ARG A2284       8.395  96.462 277.783  1.00117.93           C  
ANISOU 3149  CA  ARG A2284    17288  14240  13279   -273    573   1231       C  
ATOM   3150  C   ARG A2284       8.549  96.462 279.300  1.00118.56           C  
ANISOU 3150  C   ARG A2284    17284  14129  13634   -235    567   1119       C  
ATOM   3151  O   ARG A2284       9.542  96.956 279.834  1.00124.04           O  
ANISOU 3151  O   ARG A2284    18044  14585  14498   -292    702   1050       O  
ATOM   3152  CB  ARG A2284       8.201  97.890 277.268  1.00125.55           C  
ANISOU 3152  CB  ARG A2284    18425  15124  14156   -120    666   1499       C  
ATOM   3153  CG  ARG A2284       8.299  98.027 275.758  1.00134.40           C  
ANISOU 3153  CG  ARG A2284    19657  16399  15010   -171    708   1616       C  
ATOM   3154  CD  ARG A2284       8.026  99.456 275.314  1.00142.17           C  
ANISOU 3154  CD  ARG A2284    20823  17290  15906     16    808   1912       C  
ATOM   3155  NE  ARG A2284       8.095  99.603 273.863  1.00148.77           N  
ANISOU 3155  NE  ARG A2284    21766  18291  16471    -26    843   2043       N  
ATOM   3156  CZ  ARG A2284       7.852 100.738 273.215  1.00154.81           C  
ANISOU 3156  CZ  ARG A2284    22701  19020  17100    134    932   2325       C  
ATOM   3157  NH1 ARG A2284       7.520 101.830 273.890  1.00156.73           N  
ANISOU 3157  NH1 ARG A2284    23051  19041  17457    356   1013   2500       N  
ATOM   3158  NH2 ARG A2284       7.938 100.781 271.892  1.00157.80           N  
ANISOU 3158  NH2 ARG A2284    23169  19572  17217     79    956   2435       N  
ATOM   3159  N   GLY A2285       7.561  95.896 279.987  1.00107.13           N  
ANISOU 3159  N   GLY A2285    15684  12809  12211   -160    407   1103       N  
ATOM   3160  CA  GLY A2285       7.558  95.872 281.438  1.00 94.84           C  
ANISOU 3160  CA  GLY A2285    14049  11099  10889   -110    387   1011       C  
ATOM   3161  C   GLY A2285       7.200  94.524 282.033  1.00 83.51           C  
ANISOU 3161  C   GLY A2285    12433   9793   9503   -184    252    837       C  
ATOM   3162  O   GLY A2285       7.715  94.154 283.087  1.00 82.77           O  
ANISOU 3162  O   GLY A2285    12277   9563   9608   -225    269    684       O  
ATOM   3163  N   LEU A2286       6.318  93.789 281.361  1.00 77.00           N  
ANISOU 3163  N   LEU A2286    11532   9241   8482   -220    120    866       N  
ATOM   3164  CA  LEU A2286       5.860  92.488 281.853  1.00 74.49           C  
ANISOU 3164  CA  LEU A2286    11077   9047   8178   -317     -3    710       C  
ATOM   3165  C   LEU A2286       6.985  91.476 282.123  1.00 76.35           C  
ANISOU 3165  C   LEU A2286    11329   9143   8539   -473     86    457       C  
ATOM   3166  O   LEU A2286       6.938  90.776 283.133  1.00 75.51           O  
ANISOU 3166  O   LEU A2286    11128   8986   8578   -484     44    333       O  
ATOM   3167  CB  LEU A2286       4.849  91.873 280.879  1.00 72.52           C  
ANISOU 3167  CB  LEU A2286    10780   9127   7645   -405   -143    773       C  
ATOM   3168  CG  LEU A2286       4.157  90.599 281.369  1.00 68.04           C  
ANISOU 3168  CG  LEU A2286    10088   8707   7057   -531   -278    638       C  
ATOM   3169  CD1 LEU A2286       3.352  90.881 282.625  1.00 62.15           C  
ANISOU 3169  CD1 LEU A2286     9186   7966   6463   -369   -366    718       C  
ATOM   3170  CD2 LEU A2286       3.268  90.016 280.285  1.00 75.38           C  
ANISOU 3170  CD2 LEU A2286    10998   9978   7665   -691   -410    688       C  
ATOM   3171  N   PRO A2287       7.992  91.379 281.231  1.00 80.17           N  
ANISOU 3171  N   PRO A2287    11927   9572   8962   -574    222    393       N  
ATOM   3172  CA  PRO A2287       9.086  90.465 281.584  1.00 77.81           C  
ANISOU 3172  CA  PRO A2287    11621   9145   8797   -666    332    186       C  
ATOM   3173  C   PRO A2287       9.868  90.923 282.812  1.00 74.32           C  
ANISOU 3173  C   PRO A2287    11106   8508   8624   -601    395    152       C  
ATOM   3174  O   PRO A2287      10.464  90.098 283.504  1.00 72.41           O  
ANISOU 3174  O   PRO A2287    10792   8202   8520   -630    432     10       O  
ATOM   3175  CB  PRO A2287       9.978  90.482 280.335  1.00 77.95           C  
ANISOU 3175  CB  PRO A2287    11772   9162   8685   -755    485    168       C  
ATOM   3176  CG  PRO A2287       9.632  91.749 279.633  1.00 79.50           C  
ANISOU 3176  CG  PRO A2287    12045   9402   8758   -694    478    376       C  
ATOM   3177  CD  PRO A2287       8.170  91.932 279.875  1.00 80.31           C  
ANISOU 3177  CD  PRO A2287    12075   9663   8775   -606    288    504       C  
ATOM   3178  N   PHE A2288       9.858  92.225 283.075  1.00 76.56           N  
ANISOU 3178  N   PHE A2288    11425   8701   8965   -520    414    289       N  
ATOM   3179  CA  PHE A2288      10.567  92.782 284.220  1.00 78.35           C  
ANISOU 3179  CA  PHE A2288    11612   8749   9408   -504    470    258       C  
ATOM   3180  C   PHE A2288       9.790  92.584 285.519  1.00 75.48           C  
ANISOU 3180  C   PHE A2288    11146   8370   9164   -417    346    235       C  
ATOM   3181  O   PHE A2288      10.337  92.105 286.512  1.00 74.34           O  
ANISOU 3181  O   PHE A2288    10907   8162   9178   -448    350    118       O  
ATOM   3182  CB  PHE A2288      10.849  94.271 284.000  1.00 85.00           C  
ANISOU 3182  CB  PHE A2288    12592   9460  10244   -481    565    400       C  
ATOM   3183  CG  PHE A2288      11.307  94.990 285.237  1.00 93.21           C  
ANISOU 3183  CG  PHE A2288    13633  10317  11465   -490    603    378       C  
ATOM   3184  CD1 PHE A2288      10.448  95.834 285.924  1.00 97.15           C  
ANISOU 3184  CD1 PHE A2288    14205  10718  11989   -361    562    479       C  
ATOM   3185  CD2 PHE A2288      12.595  94.818 285.718  1.00 97.32           C  
ANISOU 3185  CD2 PHE A2288    14083  10782  12114   -631    688    263       C  
ATOM   3186  CE1 PHE A2288      10.865  96.495 287.064  1.00 98.98           C  
ANISOU 3186  CE1 PHE A2288    14481  10768  12360   -397    609    441       C  
ATOM   3187  CE2 PHE A2288      13.019  95.477 286.858  1.00 99.40           C  
ANISOU 3187  CE2 PHE A2288    14351  10907  12510   -686    709    236       C  
ATOM   3188  CZ  PHE A2288      12.153  96.317 287.532  1.00 99.55           C  
ANISOU 3188  CZ  PHE A2288    14485  10797  12542   -582    672    312       C  
ATOM   3189  N   VAL A2289       8.513  92.950 285.504  1.00 72.58           N  
ANISOU 3189  N   VAL A2289    10785   8084   8709   -299    240    363       N  
ATOM   3190  CA  VAL A2289       7.690  92.895 286.707  1.00 63.89           C  
ANISOU 3190  CA  VAL A2289     9592   6977   7706   -197    139    369       C  
ATOM   3191  C   VAL A2289       7.325  91.461 287.092  1.00 63.39           C  
ANISOU 3191  C   VAL A2289     9394   7034   7658   -256     36    234       C  
ATOM   3192  O   VAL A2289       6.925  91.200 288.226  1.00 70.11           O  
ANISOU 3192  O   VAL A2289    10155   7861   8622   -206    -29    195       O  
ATOM   3193  CB  VAL A2289       6.402  93.721 286.540  1.00 61.12           C  
ANISOU 3193  CB  VAL A2289     9266   6709   7246    -20     77    579       C  
ATOM   3194  CG1 VAL A2289       6.748  95.157 286.177  1.00 62.51           C  
ANISOU 3194  CG1 VAL A2289     9626   6720   7404     57    209    723       C  
ATOM   3195  CG2 VAL A2289       5.502  93.105 285.481  1.00 60.92           C  
ANISOU 3195  CG2 VAL A2289     9178   6964   7004    -40    -34    652       C  
ATOM   3196  N   THR A2290       7.464  90.535 286.150  1.00 57.05           N  
ANISOU 3196  N   THR A2290     8605   6343   6729   -372     38    161       N  
ATOM   3197  CA  THR A2290       7.258  89.121 286.443  1.00 55.15           C  
ANISOU 3197  CA  THR A2290     8298   6166   6491   -456    -17     16       C  
ATOM   3198  C   THR A2290       8.456  88.579 287.210  1.00 58.39           C  
ANISOU 3198  C   THR A2290     8678   6419   7089   -480     84   -128       C  
ATOM   3199  O   THR A2290       8.304  87.841 288.183  1.00 66.71           O  
ANISOU 3199  O   THR A2290     9652   7448   8248   -468     39   -209       O  
ATOM   3200  CB  THR A2290       7.051  88.291 285.163  1.00 55.77           C  
ANISOU 3200  CB  THR A2290     8457   6387   6347   -594    -19    -31       C  
ATOM   3201  OG1 THR A2290       5.816  88.667 284.542  1.00 57.42           O  
ANISOU 3201  OG1 THR A2290     8645   6812   6359   -587   -147    118       O  
ATOM   3202  CG2 THR A2290       7.013  86.808 285.493  1.00 51.93           C  
ANISOU 3202  CG2 THR A2290     7967   5896   5869   -699    -25   -203       C  
ATOM   3203  N   SER A2291       9.649  88.958 286.765  1.00 58.13           N  
ANISOU 3203  N   SER A2291     8696   6303   7089   -510    222   -142       N  
ATOM   3204  CA  SER A2291      10.875  88.570 287.448  1.00 63.38           C  
ANISOU 3204  CA  SER A2291     9291   6871   7920   -520    323   -237       C  
ATOM   3205  C   SER A2291      10.994  89.302 288.781  1.00 62.16           C  
ANISOU 3205  C   SER A2291     9051   6634   7933   -471    278   -209       C  
ATOM   3206  O   SER A2291      11.695  88.853 289.688  1.00 59.44           O  
ANISOU 3206  O   SER A2291     8604   6256   7724   -470    302   -278       O  
ATOM   3207  CB  SER A2291      12.094  88.856 286.568  1.00 69.29           C  
ANISOU 3207  CB  SER A2291    10087   7598   8640   -576    485   -234       C  
ATOM   3208  OG  SER A2291      12.114  90.208 286.150  1.00 74.52           O  
ANISOU 3208  OG  SER A2291    10823   8231   9262   -588    503   -115       O  
ATOM   3209  N   LEU A2292      10.304  90.434 288.891  1.00 64.13           N  
ANISOU 3209  N   LEU A2292     9358   6853   8156   -422    225    -98       N  
ATOM   3210  CA  LEU A2292      10.241  91.181 290.141  1.00 63.61           C  
ANISOU 3210  CA  LEU A2292     9267   6686   8214   -379    194    -78       C  
ATOM   3211  C   LEU A2292       9.480  90.382 291.195  1.00 61.21           C  
ANISOU 3211  C   LEU A2292     8860   6421   7977   -318     81   -131       C  
ATOM   3212  O   LEU A2292       9.836  90.389 292.373  1.00 56.15           O  
ANISOU 3212  O   LEU A2292     8154   5718   7462   -318     69   -180       O  
ATOM   3213  CB  LEU A2292       9.579  92.545 289.922  1.00 63.58           C  
ANISOU 3213  CB  LEU A2292     9397   6614   8146   -305    201     66       C  
ATOM   3214  CG  LEU A2292       9.305  93.399 291.163  1.00 60.84           C  
ANISOU 3214  CG  LEU A2292     9092   6132   7893   -245    192     92       C  
ATOM   3215  CD1 LEU A2292      10.592  93.683 291.927  1.00 55.40           C  
ANISOU 3215  CD1 LEU A2292     8393   5337   7320   -387    263      1       C  
ATOM   3216  CD2 LEU A2292       8.606  94.697 290.779  1.00 62.10           C  
ANISOU 3216  CD2 LEU A2292     9426   6202   7967   -129    240    256       C  
ATOM   3217  N   ALA A2293       8.433  89.690 290.757  1.00 63.27           N  
ANISOU 3217  N   ALA A2293     9106   6800   8136   -287     -3   -117       N  
ATOM   3218  CA  ALA A2293       7.654  88.832 291.640  1.00 62.36           C  
ANISOU 3218  CA  ALA A2293     8895   6736   8062   -255   -103   -165       C  
ATOM   3219  C   ALA A2293       8.441  87.574 291.988  1.00 63.28           C  
ANISOU 3219  C   ALA A2293     8958   6829   8257   -314    -61   -301       C  
ATOM   3220  O   ALA A2293       8.268  86.993 293.060  1.00 61.09           O  
ANISOU 3220  O   ALA A2293     8605   6535   8072   -286   -107   -350       O  
ATOM   3221  CB  ALA A2293       6.326  88.469 290.995  1.00 61.28           C  
ANISOU 3221  CB  ALA A2293     8750   6767   7768   -251   -203   -102       C  
ATOM   3222  N   PHE A2294       9.305  87.158 291.068  1.00 70.55           N  
ANISOU 3222  N   PHE A2294     9929   7746   9131   -377     44   -349       N  
ATOM   3223  CA  PHE A2294      10.182  86.016 291.289  1.00 73.41           C  
ANISOU 3223  CA  PHE A2294    10258   8073   9561   -389    132   -451       C  
ATOM   3224  C   PHE A2294      11.184  86.297 292.403  1.00 74.57           C  
ANISOU 3224  C   PHE A2294    10286   8171   9876   -350    164   -455       C  
ATOM   3225  O   PHE A2294      11.529  85.407 293.179  1.00 73.51           O  
ANISOU 3225  O   PHE A2294    10076   8027   9828   -308    180   -505       O  
ATOM   3226  CB  PHE A2294      10.925  85.658 290.000  1.00 75.24           C  
ANISOU 3226  CB  PHE A2294    10582   8311   9695   -439    269   -483       C  
ATOM   3227  CG  PHE A2294      10.170  84.724 289.100  1.00 77.36           C  
ANISOU 3227  CG  PHE A2294    10977   8623   9792   -510    264   -540       C  
ATOM   3228  CD1 PHE A2294       9.546  83.598 289.612  1.00 77.28           C  
ANISOU 3228  CD1 PHE A2294    10984   8601   9779   -529    222   -616       C  
ATOM   3229  CD2 PHE A2294      10.087  84.970 287.738  1.00 79.81           C  
ANISOU 3229  CD2 PHE A2294    11407   8990   9927   -585    304   -520       C  
ATOM   3230  CE1 PHE A2294       8.855  82.735 288.782  1.00 80.56           C  
ANISOU 3230  CE1 PHE A2294    11543   9055  10011   -650    222   -682       C  
ATOM   3231  CE2 PHE A2294       9.396  84.112 286.904  1.00 79.26           C  
ANISOU 3231  CE2 PHE A2294    11470   8979   9667   -695    294   -583       C  
ATOM   3232  CZ  PHE A2294       8.779  82.993 287.426  1.00 80.39           C  
ANISOU 3232  CZ  PHE A2294    11639   9106   9801   -743    252   -671       C  
ATOM   3233  N   PHE A2295      11.645  87.542 292.476  1.00 78.31           N  
ANISOU 3233  N   PHE A2295    10754   8621  10379   -379    178   -394       N  
ATOM   3234  CA  PHE A2295      12.681  87.923 293.430  1.00 81.58           C  
ANISOU 3234  CA  PHE A2295    11057   9024  10915   -404    206   -396       C  
ATOM   3235  C   PHE A2295      12.101  88.154 294.820  1.00 82.86           C  
ANISOU 3235  C   PHE A2295    11175   9156  11153   -373     95   -400       C  
ATOM   3236  O   PHE A2295      12.836  88.404 295.774  1.00 83.25           O  
ANISOU 3236  O   PHE A2295    11132   9215  11283   -413     91   -408       O  
ATOM   3237  CB  PHE A2295      13.419  89.176 292.952  1.00 83.87           C  
ANISOU 3237  CB  PHE A2295    11392   9290  11184   -501    277   -342       C  
ATOM   3238  CG  PHE A2295      14.168  88.985 291.659  1.00 88.58           C  
ANISOU 3238  CG  PHE A2295    12015   9930  11712   -538    406   -333       C  
ATOM   3239  CD1 PHE A2295      14.560  87.720 291.250  1.00 87.80           C  
ANISOU 3239  CD1 PHE A2295    11869   9886  11606   -481    482   -382       C  
ATOM   3240  CD2 PHE A2295      14.476  90.069 290.852  1.00 88.54           C  
ANISOU 3240  CD2 PHE A2295    12107   9893  11640   -621    472   -272       C  
ATOM   3241  CE1 PHE A2295      15.246  87.539 290.063  1.00 85.51           C  
ANISOU 3241  CE1 PHE A2295    11621   9628  11241   -503    623   -377       C  
ATOM   3242  CE2 PHE A2295      15.162  89.894 289.664  1.00 86.47           C  
ANISOU 3242  CE2 PHE A2295    11871   9679  11306   -655    600   -260       C  
ATOM   3243  CZ  PHE A2295      15.547  88.628 289.269  1.00 85.39           C  
ANISOU 3243  CZ  PHE A2295    11678   9606  11159   -593    676   -316       C  
ATOM   3244  N   ASN A2296      10.779  88.068 294.927  1.00 84.63           N  
ANISOU 3244  N   ASN A2296    11456   9367  11333   -310      5   -387       N  
ATOM   3245  CA  ASN A2296      10.106  88.166 296.217  1.00 84.90           C  
ANISOU 3245  CA  ASN A2296    11454   9378  11428   -260    -87   -389       C  
ATOM   3246  C   ASN A2296      10.413  86.944 297.076  1.00 84.87           C  
ANISOU 3246  C   ASN A2296    11334   9410  11503   -233   -105   -451       C  
ATOM   3247  O   ASN A2296      10.372  87.008 298.306  1.00 84.57           O  
ANISOU 3247  O   ASN A2296    11237   9363  11531   -215   -159   -460       O  
ATOM   3248  CB  ASN A2296       8.595  88.318 296.026  1.00 86.24           C  
ANISOU 3248  CB  ASN A2296    11680   9567  11520   -187   -165   -335       C  
ATOM   3249  CG  ASN A2296       7.845  88.410 297.343  1.00 85.96           C  
ANISOU 3249  CG  ASN A2296    11607   9515  11540   -119   -240   -329       C  
ATOM   3250  OD1 ASN A2296       7.350  87.409 297.860  1.00 88.97           O  
ANISOU 3250  OD1 ASN A2296    11915   9947  11941    -96   -296   -365       O  
ATOM   3251  ND2 ASN A2296       7.759  89.616 297.892  1.00 84.94           N  
ANISOU 3251  ND2 ASN A2296    11552   9297  11424    -91   -224   -286       N  
ATOM   3252  N   SER A2297      10.727  85.834 296.416  1.00 80.20           N  
ANISOU 3252  N   SER A2297    10734   8848  10890   -223    -45   -488       N  
ATOM   3253  CA  SER A2297      11.093  84.602 297.104  1.00 75.85           C  
ANISOU 3253  CA  SER A2297    10106   8306  10406   -169    -22   -529       C  
ATOM   3254  C   SER A2297      12.528  84.668 297.618  1.00 75.00           C  
ANISOU 3254  C   SER A2297     9865   8249  10382   -161     42   -508       C  
ATOM   3255  O   SER A2297      12.925  83.886 298.482  1.00 71.47           O  
ANISOU 3255  O   SER A2297     9319   7833  10001    -92     48   -506       O  
ATOM   3256  CB  SER A2297      10.917  83.400 296.176  1.00 71.15           C  
ANISOU 3256  CB  SER A2297     9603   7691   9740   -159     56   -576       C  
ATOM   3257  OG  SER A2297       9.565  83.264 295.776  1.00 71.06           O  
ANISOU 3257  OG  SER A2297     9685   7686   9629   -207    -25   -589       O  
ATOM   3258  N   VAL A2298      13.299  85.604 297.076  1.00 78.34           N  
ANISOU 3258  N   VAL A2298    10275   8699  10790   -238     91   -479       N  
ATOM   3259  CA  VAL A2298      14.678  85.808 297.499  1.00 75.32           C  
ANISOU 3259  CA  VAL A2298     9734   8419  10465   -275    143   -443       C  
ATOM   3260  C   VAL A2298      14.735  86.875 298.589  1.00 73.82           C  
ANISOU 3260  C   VAL A2298     9505   8243  10299   -381     47   -433       C  
ATOM   3261  O   VAL A2298      15.605  86.850 299.459  1.00 77.36           O  
ANISOU 3261  O   VAL A2298     9795   8810  10789   -421     31   -409       O  
ATOM   3262  CB  VAL A2298      15.577  86.224 296.314  1.00 77.19           C  
ANISOU 3262  CB  VAL A2298     9973   8698  10660   -337    266   -415       C  
ATOM   3263  CG1 VAL A2298      17.041  86.242 296.728  1.00 77.89           C  
ANISOU 3263  CG1 VAL A2298     9845   8952  10799   -372    327   -357       C  
ATOM   3264  CG2 VAL A2298      15.372  85.281 295.139  1.00 78.44           C  
ANISOU 3264  CG2 VAL A2298    10233   8812  10759   -251    371   -441       C  
ATOM   3265  N   ALA A2299      13.789  87.807 298.543  1.00 69.34           N  
ANISOU 3265  N   ALA A2299     9093   7563   9689   -423     -8   -445       N  
ATOM   3266  CA  ALA A2299      13.764  88.916 299.486  1.00 67.76           C  
ANISOU 3266  CA  ALA A2299     8935   7322   9488   -529    -64   -449       C  
ATOM   3267  C   ALA A2299      13.292  88.480 300.872  1.00 71.29           C  
ANISOU 3267  C   ALA A2299     9327   7784   9976   -475   -159   -473       C  
ATOM   3268  O   ALA A2299      13.856  88.900 301.883  1.00 74.82           O  
ANISOU 3268  O   ALA A2299     9717   8283  10429   -579   -196   -483       O  
ATOM   3269  CB  ALA A2299      12.878  90.034 298.955  1.00 62.53           C  
ANISOU 3269  CB  ALA A2299     8485   6511   8762   -541    -53   -432       C  
ATOM   3270  N   ASN A2300      12.265  87.636 300.912  1.00 67.72           N  
ANISOU 3270  N   ASN A2300     8896   7300   9534   -336   -197   -482       N  
ATOM   3271  CA  ASN A2300      11.637  87.241 302.173  1.00 61.77           C  
ANISOU 3271  CA  ASN A2300     8112   6547   8810   -277   -280   -498       C  
ATOM   3272  C   ASN A2300      12.582  86.617 303.213  1.00 66.24           C  
ANISOU 3272  C   ASN A2300     8509   7236   9423   -289   -304   -493       C  
ATOM   3273  O   ASN A2300      12.584  87.057 304.361  1.00 70.21           O  
ANISOU 3273  O   ASN A2300     9001   7756   9919   -345   -367   -504       O  
ATOM   3274  CB  ASN A2300      10.467  86.285 301.905  1.00 55.09           C  
ANISOU 3274  CB  ASN A2300     7299   5674   7959   -157   -304   -503       C  
ATOM   3275  CG  ASN A2300       9.277  86.982 301.275  1.00 53.75           C  
ANISOU 3275  CG  ASN A2300     7258   5439   7725   -132   -320   -479       C  
ATOM   3276  OD1 ASN A2300       9.142  88.203 301.357  1.00 49.83           O  
ANISOU 3276  OD1 ASN A2300     6853   4878   7202   -159   -310   -456       O  
ATOM   3277  ND2 ASN A2300       8.402  86.205 300.649  1.00 57.59           N  
ANISOU 3277  ND2 ASN A2300     7758   5950   8172    -83   -336   -474       N  
ATOM   3278  N   PRO A2301      13.389  85.601 302.831  1.00 64.78           N  
ANISOU 3278  N   PRO A2301     8197   7143   9272   -225   -245   -463       N  
ATOM   3279  CA  PRO A2301      14.266  85.018 303.858  1.00 60.54           C  
ANISOU 3279  CA  PRO A2301     7477   6757   8771   -200   -267   -419       C  
ATOM   3280  C   PRO A2301      15.255  86.025 304.439  1.00 63.57           C  
ANISOU 3280  C   PRO A2301     7760   7273   9122   -381   -305   -401       C  
ATOM   3281  O   PRO A2301      15.659  85.892 305.594  1.00 70.76           O  
ANISOU 3281  O   PRO A2301     8546   8313  10025   -410   -375   -374       O  
ATOM   3282  CB  PRO A2301      15.007  83.911 303.101  1.00 61.69           C  
ANISOU 3282  CB  PRO A2301     7531   6962   8948    -72   -150   -370       C  
ATOM   3283  CG  PRO A2301      14.132  83.589 301.946  1.00 63.21           C  
ANISOU 3283  CG  PRO A2301     7903   6998   9117    -26    -93   -422       C  
ATOM   3284  CD  PRO A2301      13.526  84.894 301.545  1.00 64.14           C  
ANISOU 3284  CD  PRO A2301     8143   7040   9186   -154   -144   -459       C  
ATOM   3285  N   VAL A2302      15.635  87.020 303.644  1.00 63.20           N  
ANISOU 3285  N   VAL A2302     7774   7199   9039   -522   -260   -415       N  
ATOM   3286  CA  VAL A2302      16.487  88.096 304.130  1.00 66.99           C  
ANISOU 3286  CA  VAL A2302     8209   7781   9465   -759   -289   -415       C  
ATOM   3287  C   VAL A2302      15.689  88.998 305.068  1.00 71.60           C  
ANISOU 3287  C   VAL A2302     8977   8230   9997   -860   -362   -484       C  
ATOM   3288  O   VAL A2302      16.184  89.419 306.115  1.00 75.93           O  
ANISOU 3288  O   VAL A2302     9475   8883  10492  -1024   -426   -497       O  
ATOM   3289  CB  VAL A2302      17.067  88.928 302.972  1.00 65.96           C  
ANISOU 3289  CB  VAL A2302     8131   7628   9302   -896   -198   -409       C  
ATOM   3290  CG1 VAL A2302      17.964  90.033 303.507  1.00 67.63           C  
ANISOU 3290  CG1 VAL A2302     8312   7945   9440  -1194   -223   -416       C  
ATOM   3291  CG2 VAL A2302      17.838  88.033 302.017  1.00 65.92           C  
ANISOU 3291  CG2 VAL A2302     7959   7750   9337   -777   -100   -341       C  
ATOM   3292  N   LEU A2303      14.445  89.276 304.688  1.00 70.30           N  
ANISOU 3292  N   LEU A2303     9026   7850   9837   -759   -344   -521       N  
ATOM   3293  CA  LEU A2303      13.552  90.094 305.502  1.00 68.94           C  
ANISOU 3293  CA  LEU A2303     9050   7526   9618   -792   -376   -572       C  
ATOM   3294  C   LEU A2303      13.204  89.406 306.819  1.00 70.30           C  
ANISOU 3294  C   LEU A2303     9143   7767   9802   -721   -463   -582       C  
ATOM   3295  O   LEU A2303      12.950  90.069 307.824  1.00 74.80           O  
ANISOU 3295  O   LEU A2303     9826   8283  10311   -812   -492   -627       O  
ATOM   3296  CB  LEU A2303      12.271  90.415 304.732  1.00 65.50           C  
ANISOU 3296  CB  LEU A2303     8806   6898   9183   -647   -330   -566       C  
ATOM   3297  CG  LEU A2303      12.408  91.291 303.486  1.00 62.62           C  
ANISOU 3297  CG  LEU A2303     8576   6432   8785   -703   -238   -544       C  
ATOM   3298  CD1 LEU A2303      11.076  91.388 302.772  1.00 59.57           C  
ANISOU 3298  CD1 LEU A2303     8320   5926   8389   -519   -215   -504       C  
ATOM   3299  CD2 LEU A2303      12.921  92.674 303.851  1.00 64.62           C  
ANISOU 3299  CD2 LEU A2303     9003   6582   8966   -920   -187   -578       C  
ATOM   3300  N   TYR A2304      13.187  88.075 306.804  1.00 66.36           N  
ANISOU 3300  N   TYR A2304     8478   7369   9367   -561   -486   -539       N  
ATOM   3301  CA  TYR A2304      12.923  87.294 308.007  1.00 65.78           C  
ANISOU 3301  CA  TYR A2304     8321   7368   9305   -481   -558   -529       C  
ATOM   3302  C   TYR A2304      13.961  87.607 309.079  1.00 74.64           C  
ANISOU 3302  C   TYR A2304     9325   8670  10365   -652   -622   -521       C  
ATOM   3303  O   TYR A2304      13.629  87.862 310.237  1.00 75.16           O  
ANISOU 3303  O   TYR A2304     9447   8735  10375   -704   -683   -554       O  
ATOM   3304  CB  TYR A2304      12.930  85.794 307.700  1.00 63.32           C  
ANISOU 3304  CB  TYR A2304     7875   7118   9066   -293   -539   -474       C  
ATOM   3305  CG  TYR A2304      11.799  85.314 306.815  1.00 68.26           C  
ANISOU 3305  CG  TYR A2304     8617   7597   9722   -164   -497   -491       C  
ATOM   3306  CD1 TYR A2304      10.705  86.124 306.541  1.00 68.56           C  
ANISOU 3306  CD1 TYR A2304     8821   7500   9728   -173   -501   -526       C  
ATOM   3307  CD2 TYR A2304      11.824  84.043 306.258  1.00 73.99           C  
ANISOU 3307  CD2 TYR A2304     9293   8330  10491    -38   -445   -463       C  
ATOM   3308  CE1 TYR A2304       9.673  85.687 305.731  1.00 69.46           C  
ANISOU 3308  CE1 TYR A2304     9002   7544   9845    -80   -481   -522       C  
ATOM   3309  CE2 TYR A2304      10.797  83.595 305.449  1.00 75.08           C  
ANISOU 3309  CE2 TYR A2304     9544   8360  10625     22   -416   -488       C  
ATOM   3310  CZ  TYR A2304       9.724  84.420 305.189  1.00 75.48           C  
ANISOU 3310  CZ  TYR A2304     9713   8330  10635    -10   -449   -513       C  
ATOM   3311  OH  TYR A2304       8.699  83.979 304.384  1.00 82.43           O  
ANISOU 3311  OH  TYR A2304    10668   9164  11488     27   -439   -519       O  
ATOM   3312  N   VAL A2305      15.223  87.593 308.668  1.00 76.27           N  
ANISOU 3312  N   VAL A2305     9360   9054  10566   -750   -606   -471       N  
ATOM   3313  CA  VAL A2305      16.344  87.813 309.570  1.00 73.43           C  
ANISOU 3313  CA  VAL A2305     8825   8947  10129   -937   -678   -436       C  
ATOM   3314  C   VAL A2305      16.436  89.263 310.047  1.00 72.35           C  
ANISOU 3314  C   VAL A2305     8869   8749   9873  -1241   -701   -528       C  
ATOM   3315  O   VAL A2305      16.642  89.520 311.232  1.00 76.62           O  
ANISOU 3315  O   VAL A2305     9398   9398  10315  -1392   -784   -551       O  
ATOM   3316  CB  VAL A2305      17.666  87.405 308.887  1.00 79.30           C  
ANISOU 3316  CB  VAL A2305     9305   9932  10895   -949   -637   -332       C  
ATOM   3317  CG1 VAL A2305      18.848  88.137 309.502  1.00 88.45           C  
ANISOU 3317  CG1 VAL A2305    10307  11362  11938  -1252   -704   -306       C  
ATOM   3318  CG2 VAL A2305      17.851  85.897 308.960  1.00 77.14           C  
ANISOU 3318  CG2 VAL A2305     8832   9779  10700   -665   -616   -220       C  
ATOM   3319  N   LEU A2306      16.265  90.204 309.124  1.00 66.15           N  
ANISOU 3319  N   LEU A2306     8279   7775   9081  -1333   -616   -581       N  
ATOM   3320  CA  LEU A2306      16.434  91.624 309.427  1.00 65.13           C  
ANISOU 3320  CA  LEU A2306     8374   7541   8831  -1634   -595   -667       C  
ATOM   3321  C   LEU A2306      15.376  92.183 310.375  1.00 64.30           C  
ANISOU 3321  C   LEU A2306     8549   7219   8664  -1628   -598   -757       C  
ATOM   3322  O   LEU A2306      15.568  93.246 310.969  1.00 64.92           O  
ANISOU 3322  O   LEU A2306     8832   7221   8613  -1893   -581   -839       O  
ATOM   3323  CB  LEU A2306      16.429  92.441 308.135  1.00 66.49           C  
ANISOU 3323  CB  LEU A2306     8716   7530   9017  -1687   -477   -681       C  
ATOM   3324  CG  LEU A2306      17.616  92.233 307.198  1.00 70.40           C  
ANISOU 3324  CG  LEU A2306     8983   8230   9538  -1774   -446   -607       C  
ATOM   3325  CD1 LEU A2306      17.491  93.150 305.995  1.00 72.52           C  
ANISOU 3325  CD1 LEU A2306     9470   8285   9801  -1837   -323   -625       C  
ATOM   3326  CD2 LEU A2306      18.926  92.474 307.930  1.00 73.29           C  
ANISOU 3326  CD2 LEU A2306     9143   8903   9799  -2089   -517   -587       C  
ATOM   3327  N   THR A2307      14.260  91.473 310.511  1.00 61.99           N  
ANISOU 3327  N   THR A2307     8277   6825   8450  -1338   -604   -741       N  
ATOM   3328  CA  THR A2307      13.159  91.937 311.347  1.00 61.60           C  
ANISOU 3328  CA  THR A2307     8474   6580   8351  -1281   -584   -805       C  
ATOM   3329  C   THR A2307      12.902  91.001 312.524  1.00 63.60           C  
ANISOU 3329  C   THR A2307     8589   6975   8603  -1181   -681   -788       C  
ATOM   3330  O   THR A2307      12.146  91.328 313.437  1.00 63.31           O  
ANISOU 3330  O   THR A2307     8727   6826   8503  -1161   -672   -840       O  
ATOM   3331  CB  THR A2307      11.865  92.077 310.538  1.00 57.19           C  
ANISOU 3331  CB  THR A2307     8083   5783   7865  -1030   -492   -787       C  
ATOM   3332  OG1 THR A2307      11.504  90.802 309.993  1.00 56.82           O  
ANISOU 3332  OG1 THR A2307     7824   5832   7932   -799   -532   -715       O  
ATOM   3333  CG2 THR A2307      12.056  93.072 309.405  1.00 55.28           C  
ANISOU 3333  CG2 THR A2307     8008   5386   7608  -1111   -386   -789       C  
HETATM 3334  N   YCM A2308      13.543  89.839 312.514  1.00 64.25           N  
ANISOU 3334  N   YCM A2308     8369   7296   8745  -1105   -757   -704       N  
HETATM 3335  CA  YCM A2308      13.382  88.903 313.603  1.00 62.83           C  
ANISOU 3335  CA  YCM A2308     8057   7255   8560  -1002   -841   -665       C  
HETATM 3336  CB  YCM A2308      12.534  87.692 313.235  1.00 61.84           C  
ANISOU 3336  CB  YCM A2308     7858   7076   8562   -699   -823   -605       C  
HETATM 3337  SG  YCM A2308      12.020  86.655 314.568  1.00 67.13           S  
ANISOU 3337  SG  YCM A2308     8452   7832   9222   -559   -893   -563       S  
HETATM 3338  CD  YCM A2308      10.982  87.681 315.563  1.00 94.63           C  
ANISOU 3338  CD  YCM A2308    12213  11143  12600   -629   -877   -665       C  
HETATM 3339  CE  YCM A2308      11.710  88.319 316.728  1.00 94.61           C  
ANISOU 3339  CE  YCM A2308    12242  11266  12438   -873   -942   -712       C  
HETATM 3340  OZ1 YCM A2308      12.802  87.871 317.151  1.00 91.40           O  
ANISOU 3340  OZ1 YCM A2308    11618  11126  11985   -974  -1034   -650       O  
HETATM 3341  NZ2 YCM A2308      11.130  89.416 317.297  1.00 98.07           N  
ANISOU 3341  NZ2 YCM A2308    12965  11528  12769   -981   -888   -817       N  
HETATM 3342  C   YCM A2308      14.696  88.449 314.217  1.00 66.69           C  
ANISOU 3342  C   YCM A2308     8275   8077   8989  -1134   -938   -593       C  
HETATM 3343  O   YCM A2308      15.332  87.497 313.771  1.00 66.90           O  
ANISOU 3343  O   YCM A2308     8052   8275   9092  -1007   -946   -484       O  
ATOM   3344  N   PRO A2309      15.121  89.151 315.276  1.00 68.09           N  
ANISOU 3344  N   PRO A2309     8504   8358   9008  -1393  -1005   -645       N  
ATOM   3345  CA  PRO A2309      16.393  88.887 315.960  1.00 62.87           C  
ANISOU 3345  CA  PRO A2309     7570   8075   8244  -1571  -1119   -565       C  
ATOM   3346  C   PRO A2309      16.528  87.460 316.486  1.00 59.21           C  
ANISOU 3346  C   PRO A2309     6835   7826   7835  -1319  -1184   -420       C  
ATOM   3347  O   PRO A2309      17.628  86.918 316.464  1.00 60.23           O  
ANISOU 3347  O   PRO A2309     6657   8274   7953  -1323  -1233   -286       O  
ATOM   3348  CB  PRO A2309      16.381  89.905 317.106  1.00 61.12           C  
ANISOU 3348  CB  PRO A2309     7555   7848   7819  -1886  -1169   -682       C  
ATOM   3349  CG  PRO A2309      15.591  91.044 316.554  1.00 65.11           C  
ANISOU 3349  CG  PRO A2309     8442   7971   8328  -1947  -1039   -821       C  
ATOM   3350  CD  PRO A2309      14.485  90.386 315.765  1.00 68.53           C  
ANISOU 3350  CD  PRO A2309     8909   8179   8950  -1565   -957   -785       C  
ATOM   3351  N   ASP A2310      15.434  86.861 316.942  1.00 62.14           N  
ANISOU 3351  N   ASP A2310     7319   8033   8260  -1095  -1169   -431       N  
ATOM   3352  CA  ASP A2310      15.478  85.469 317.384  1.00 69.99           C  
ANISOU 3352  CA  ASP A2310     8106   9175   9311   -840  -1201   -291       C  
ATOM   3353  C   ASP A2310      15.842  84.546 316.227  1.00 71.94           C  
ANISOU 3353  C   ASP A2310     8191   9433   9712   -612  -1119   -185       C  
ATOM   3354  O   ASP A2310      16.633  83.618 316.387  1.00 74.11           O  
ANISOU 3354  O   ASP A2310     8214   9943  10001   -476  -1132    -29       O  
ATOM   3355  CB  ASP A2310      14.138  85.023 317.979  1.00 72.13           C  
ANISOU 3355  CB  ASP A2310     8555   9236   9615   -663  -1179   -331       C  
ATOM   3356  CG  ASP A2310      13.803  85.732 319.275  1.00 77.15           C  
ANISOU 3356  CG  ASP A2310     9343   9883  10087   -842  -1244   -414       C  
ATOM   3357  OD1 ASP A2310      14.738  86.200 319.955  1.00 80.00           O  
ANISOU 3357  OD1 ASP A2310     9614  10490  10292  -1086  -1337   -406       O  
ATOM   3358  OD2 ASP A2310      12.605  85.812 319.624  1.00 77.76           O  
ANISOU 3358  OD2 ASP A2310     9627   9741  10176   -750  -1197   -484       O  
ATOM   3359  N   MET A2311      15.247  84.801 315.067  1.00 75.40           N  
ANISOU 3359  N   MET A2311     8786   9613  10250   -558  -1021   -263       N  
ATOM   3360  CA  MET A2311      15.486  83.988 313.880  1.00 75.83           C  
ANISOU 3360  CA  MET A2311     8749   9633  10430   -363   -923   -193       C  
ATOM   3361  C   MET A2311      16.933  84.117 313.411  1.00 72.58           C  
ANISOU 3361  C   MET A2311     8095   9484   9997   -450   -917   -101       C  
ATOM   3362  O   MET A2311      17.564  83.126 313.050  1.00 74.50           O  
ANISOU 3362  O   MET A2311     8151   9855  10303   -252   -857     32       O  
ATOM   3363  CB  MET A2311      14.518  84.382 312.763  1.00 78.37           C  
ANISOU 3363  CB  MET A2311     9297   9656  10824   -333   -838   -300       C  
ATOM   3364  CG  MET A2311      14.644  83.541 311.508  1.00 80.33           C  
ANISOU 3364  CG  MET A2311     9502   9843  11177   -156   -730   -252       C  
ATOM   3365  SD  MET A2311      13.053  83.238 310.721  1.00 85.70           S  
ANISOU 3365  SD  MET A2311    10422  10217  11923    -32   -666   -335       S  
ATOM   3366  CE  MET A2311      12.204  84.781 311.049  1.00 69.46           C  
ANISOU 3366  CE  MET A2311     8566   8029   9797   -203   -715   -447       C  
ATOM   3367  N   LEU A2312      17.456  85.339 313.431  1.00 66.46           N  
ANISOU 3367  N   LEU A2312     7337   8789   9127   -748   -963   -165       N  
ATOM   3368  CA  LEU A2312      18.855  85.577 313.091  1.00 66.17           C  
ANISOU 3368  CA  LEU A2312     7045   9052   9045   -891   -971    -73       C  
ATOM   3369  C   LEU A2312      19.777  84.945 314.129  1.00 74.69           C  
ANISOU 3369  C   LEU A2312     7809  10527  10043   -870  -1067     91       C  
ATOM   3370  O   LEU A2312      20.789  84.336 313.784  1.00 78.63           O  
ANISOU 3370  O   LEU A2312     8014  11294  10566   -755  -1031    257       O  
ATOM   3371  CB  LEU A2312      19.136  87.078 312.975  1.00 63.54           C  
ANISOU 3371  CB  LEU A2312     6842   8698   8604  -1269   -997   -191       C  
ATOM   3372  CG  LEU A2312      20.600  87.519 312.881  1.00 66.97           C  
ANISOU 3372  CG  LEU A2312     7005   9497   8942  -1527  -1035   -106       C  
ATOM   3373  CD1 LEU A2312      21.326  86.825 311.734  1.00 70.38           C  
ANISOU 3373  CD1 LEU A2312     7206  10048   9486  -1327   -927     26       C  
ATOM   3374  CD2 LEU A2312      20.687  89.032 312.735  1.00 65.91           C  
ANISOU 3374  CD2 LEU A2312     7095   9252   8697  -1925  -1035   -252       C  
ATOM   3375  N   ARG A2313      19.414  85.091 315.401  1.00 77.47           N  
ANISOU 3375  N   ARG A2313     8219  10927  10287   -966  -1180     59       N  
ATOM   3376  CA  ARG A2313      20.200  84.537 316.497  1.00 78.15           C  
ANISOU 3376  CA  ARG A2313     8017  11410  10266   -957  -1291    223       C  
ATOM   3377  C   ARG A2313      20.263  83.016 316.413  1.00 77.18           C  
ANISOU 3377  C   ARG A2313     7728  11337  10261   -535  -1216    409       C  
ATOM   3378  O   ARG A2313      21.312  82.414 316.639  1.00 78.17           O  
ANISOU 3378  O   ARG A2313     7521  11829  10351   -429  -1234    620       O  
ATOM   3379  CB  ARG A2313      19.617  84.966 317.847  1.00 82.95           C  
ANISOU 3379  CB  ARG A2313     8783  12004  10729  -1129  -1411    132       C  
ATOM   3380  CG  ARG A2313      20.402  84.470 319.048  1.00 91.74           C  
ANISOU 3380  CG  ARG A2313     9605  13555  11695  -1153  -1546    304       C  
ATOM   3381  CD  ARG A2313      19.950  85.116 320.351  1.00 93.54           C  
ANISOU 3381  CD  ARG A2313    10014  13793  11735  -1410  -1667    188       C  
ATOM   3382  NE  ARG A2313      18.651  84.621 320.794  1.00 92.54           N  
ANISOU 3382  NE  ARG A2313    10137  13346  11681  -1180  -1621    122       N  
ATOM   3383  CZ  ARG A2313      17.506  85.275 320.633  1.00 91.48           C  
ANISOU 3383  CZ  ARG A2313    10364  12812  11584  -1226  -1551    -78       C  
ATOM   3384  NH1 ARG A2313      17.494  86.461 320.040  1.00 88.99           N  
ANISOU 3384  NH1 ARG A2313    10235  12334  11241  -1478  -1510   -232       N  
ATOM   3385  NH2 ARG A2313      16.371  84.745 321.068  1.00 91.50           N  
ANISOU 3385  NH2 ARG A2313    10536  12585  11644  -1013  -1511   -107       N  
ATOM   3386  N   LYS A2314      19.136  82.399 316.077  1.00 74.28           N  
ANISOU 3386  N   LYS A2314     7598  10603  10023   -296  -1120    341       N  
ATOM   3387  CA  LYS A2314      19.060  80.947 315.991  1.00 79.98           C  
ANISOU 3387  CA  LYS A2314     8252  11290  10848     84  -1019    490       C  
ATOM   3388  C   LYS A2314      19.816  80.433 314.769  1.00 85.66           C  
ANISOU 3388  C   LYS A2314     8835  12045  11666    265   -870    591       C  
ATOM   3389  O   LYS A2314      20.250  79.281 314.734  1.00 87.62           O  
ANISOU 3389  O   LYS A2314     8951  12377  11966    573   -769    771       O  
ATOM   3390  CB  LYS A2314      17.601  80.493 315.943  1.00 80.81           C  
ANISOU 3390  CB  LYS A2314     8668  10997  11039    220   -959    370       C  
ATOM   3391  CG  LYS A2314      17.338  79.173 316.650  1.00 86.49           C  
ANISOU 3391  CG  LYS A2314     9369  11708  11784    502   -921    506       C  
ATOM   3392  CD  LYS A2314      16.372  79.353 317.817  1.00 88.96           C  
ANISOU 3392  CD  LYS A2314     9836  11940  12026    418  -1020    428       C  
ATOM   3393  CE  LYS A2314      16.917  80.329 318.850  1.00 92.17           C  
ANISOU 3393  CE  LYS A2314    10126  12634  12260    144  -1189    418       C  
ATOM   3394  NZ  LYS A2314      15.968  80.545 319.977  1.00 92.38           N  
ANISOU 3394  NZ  LYS A2314    10331  12568  12203     65  -1264    332       N  
ATOM   3395  N   LEU A2315      19.974  81.296 313.771  1.00 88.52           N  
ANISOU 3395  N   LEU A2315     9253  12333  12049     85   -837    482       N  
ATOM   3396  CA  LEU A2315      20.692  80.938 312.554  1.00 90.13           C  
ANISOU 3396  CA  LEU A2315     9344  12568  12331    226   -686    561       C  
ATOM   3397  C   LEU A2315      22.199  80.930 312.783  1.00 94.40           C  
ANISOU 3397  C   LEU A2315     9482  13586  12799    210   -711    771       C  
ATOM   3398  O   LEU A2315      22.894  80.010 312.352  1.00 99.89           O  
ANISOU 3398  O   LEU A2315     9996  14407  13550    502   -572    953       O  
ATOM   3399  CB  LEU A2315      20.339  81.900 311.417  1.00 88.28           C  
ANISOU 3399  CB  LEU A2315     9307  12107  12129     31   -643    385       C  
ATOM   3400  CG  LEU A2315      21.102  81.701 310.106  1.00 86.77           C  
ANISOU 3400  CG  LEU A2315     9015  11955  11999    130   -486    449       C  
ATOM   3401  CD1 LEU A2315      20.887  80.297 309.561  1.00 85.90           C  
ANISOU 3401  CD1 LEU A2315     8972  11677  11989    507   -309    524       C  
ATOM   3402  CD2 LEU A2315      20.692  82.747 309.081  1.00 83.81           C  
ANISOU 3402  CD2 LEU A2315     8851  11360  11633    -86   -462    278       C  
ATOM   3403  N   ARG A2316      22.700  81.956 313.465  1.00 93.20           N  
ANISOU 3403  N   ARG A2316     9194  13709  12508   -137   -876    752       N  
ATOM   3404  CA  ARG A2316      24.129  82.063 313.736  1.00 92.95           C  
ANISOU 3404  CA  ARG A2316     8742  14201  12375   -224   -931    956       C  
ATOM   3405  C   ARG A2316      24.578  80.996 314.731  1.00 98.53           C  
ANISOU 3405  C   ARG A2316     9183  15215  13039     50   -964   1204       C  
ATOM   3406  O   ARG A2316      25.764  80.682 314.822  1.00 99.66           O  
ANISOU 3406  O   ARG A2316     8930  15809  13127    138   -959   1449       O  
ATOM   3407  CB  ARG A2316      24.478  83.459 314.258  1.00 84.59           C  
ANISOU 3407  CB  ARG A2316     7649  13345  11145   -733  -1105    850       C  
ATOM   3408  CG  ARG A2316      24.021  84.591 313.351  1.00 75.85           C  
ANISOU 3408  CG  ARG A2316     6839  11914  10066  -1004  -1060    618       C  
ATOM   3409  CD  ARG A2316      24.964  85.783 313.423  1.00 79.60           C  
ANISOU 3409  CD  ARG A2316     7165  12696  10383  -1469  -1152    601       C  
ATOM   3410  NE  ARG A2316      25.195  86.226 314.795  1.00 85.71           N  
ANISOU 3410  NE  ARG A2316     7859  13749  10958  -1767  -1344    601       N  
ATOM   3411  CZ  ARG A2316      26.011  87.220 315.130  1.00 90.14           C  
ANISOU 3411  CZ  ARG A2316     8295  14622  11330  -2236  -1453    584       C  
ATOM   3412  NH1 ARG A2316      26.677  87.879 314.191  1.00 93.47           N  
ANISOU 3412  NH1 ARG A2316     8649  15113  11751  -2450  -1384    574       N  
ATOM   3413  NH2 ARG A2316      26.163  87.556 316.404  1.00 90.83           N  
ANISOU 3413  NH2 ARG A2316     8339  14957  11215  -2515  -1628    574       N  
ATOM   3414  N   ARG A2317      23.623  80.446 315.475  1.00104.68           N  
ANISOU 3414  N   ARG A2317    10173  15765  13837    194   -993   1158       N  
ATOM   3415  CA  ARG A2317      23.894  79.324 316.366  1.00108.36           C  
ANISOU 3415  CA  ARG A2317    10453  16443  14276    507   -994   1396       C  
ATOM   3416  C   ARG A2317      24.317  78.099 315.568  1.00108.48           C  
ANISOU 3416  C   ARG A2317    10381  16413  14425    969   -758   1590       C  
ATOM   3417  O   ARG A2317      25.413  77.569 315.755  1.00114.26           O  
ANISOU 3417  O   ARG A2317    10748  17551  15114   1175   -720   1873       O  
ATOM   3418  CB  ARG A2317      22.663  78.989 317.213  1.00113.34           C  
ANISOU 3418  CB  ARG A2317    11381  16772  14910    559  -1044   1286       C  
ATOM   3419  CG  ARG A2317      22.532  79.788 318.498  1.00121.56           C  
ANISOU 3419  CG  ARG A2317    12409  18011  15768    225  -1271   1219       C  
ATOM   3420  CD  ARG A2317      21.357  79.280 319.323  1.00125.75           C  
ANISOU 3420  CD  ARG A2317    13207  18262  16310    344  -1286   1149       C  
ATOM   3421  NE  ARG A2317      21.325  79.854 320.665  1.00130.15           N  
ANISOU 3421  NE  ARG A2317    13733  19047  16669     80  -1484   1126       N  
ATOM   3422  CZ  ARG A2317      20.431  79.527 321.593  1.00129.24           C  
ANISOU 3422  CZ  ARG A2317    13807  18778  16519    138  -1522   1084       C  
ATOM   3423  NH1 ARG A2317      19.494  78.628 321.324  1.00125.59           N  
ANISOU 3423  NH1 ARG A2317    13565  17943  16209    434  -1382   1065       N  
ATOM   3424  NH2 ARG A2317      20.474  80.097 322.790  1.00130.84           N  
ANISOU 3424  NH2 ARG A2317    13988  19205  16518   -121  -1695   1058       N  
ATOM   3425  N   SER A2318      23.437  77.655 314.677  1.00102.55           N  
ANISOU 3425  N   SER A2318     9974  15172  13820   1130   -590   1443       N  
ATOM   3426  CA  SER A2318      23.695  76.479 313.857  1.00 99.98           C  
ANISOU 3426  CA  SER A2318     9672  14707  13611   1549   -330   1581       C  
ATOM   3427  C   SER A2318      24.821  76.732 312.859  1.00 96.30           C  
ANISOU 3427  C   SER A2318     8956  14475  13158   1573   -219   1683       C  
ATOM   3428  O   SER A2318      25.522  75.804 312.458  1.00 96.63           O  
ANISOU 3428  O   SER A2318     8860  14609  13246   1945    -15   1901       O  
ATOM   3429  CB  SER A2318      22.422  76.052 313.125  1.00 99.99           C  
ANISOU 3429  CB  SER A2318    10127  14137  13728   1623   -198   1364       C  
ATOM   3430  OG  SER A2318      21.812  77.155 312.480  1.00102.09           O  
ANISOU 3430  OG  SER A2318    10577  14209  14004   1287   -276   1105       O  
ATOM   3431  N   LEU A2319      24.990  77.989 312.461  1.00 94.18           N  
ANISOU 3431  N   LEU A2319     8645  14293  12844   1184   -334   1534       N  
ATOM   3432  CA  LEU A2319      26.089  78.366 311.580  1.00 96.22           C  
ANISOU 3432  CA  LEU A2319     8643  14819  13098   1143   -249   1630       C  
ATOM   3433  C   LEU A2319      27.421  78.156 312.290  1.00103.12           C  
ANISOU 3433  C   LEU A2319     9004  16310  13867   1232   -302   1952       C  
ATOM   3434  O   LEU A2319      28.406  77.744 311.680  1.00103.27           O  
ANISOU 3434  O   LEU A2319     8753  16576  13909   1463   -137   2163       O  
ATOM   3435  CB  LEU A2319      25.951  79.822 311.128  1.00 89.57           C  
ANISOU 3435  CB  LEU A2319     7889  13932  12210    668   -370   1404       C  
ATOM   3436  CG  LEU A2319      27.090  80.387 310.276  1.00 86.14           C  
ANISOU 3436  CG  LEU A2319     7181  13799  11751    540   -304   1490       C  
ATOM   3437  CD1 LEU A2319      27.230  79.609 308.975  1.00 84.81           C  
ANISOU 3437  CD1 LEU A2319     7096  13422  11706    887    -23   1536       C  
ATOM   3438  CD2 LEU A2319      26.880  81.868 310.000  1.00 82.42           C  
ANISOU 3438  CD2 LEU A2319     6847  13252  11216     40   -431   1263       C  
ATOM   3439  N   ARG A2320      27.438  78.436 313.588  1.00110.70           N  
ANISOU 3439  N   ARG A2320     9824  17540  14699   1053   -528   2000       N  
ATOM   3440  CA  ARG A2320      28.634  78.256 314.397  1.00116.27           C  
ANISOU 3440  CA  ARG A2320    10021  18887  15268   1104   -620   2319       C  
ATOM   3441  C   ARG A2320      28.812  76.790 314.780  1.00120.07           C  
ANISOU 3441  C   ARG A2320    10406  19417  15800   1670   -464   2607       C  
ATOM   3442  O   ARG A2320      29.932  76.318 314.961  1.00131.40           O  
ANISOU 3442  O   ARG A2320    11406  21343  17177   1912   -411   2944       O  
ATOM   3443  CB  ARG A2320      28.565  79.134 315.648  1.00119.37           C  
ANISOU 3443  CB  ARG A2320    10332  19553  15472    662   -925   2250       C  
ATOM   3444  CG  ARG A2320      29.824  79.121 316.497  1.00129.52           C  
ANISOU 3444  CG  ARG A2320    11062  21579  16570    610  -1067   2569       C  
ATOM   3445  CD  ARG A2320      29.725  80.126 317.631  1.00133.10           C  
ANISOU 3445  CD  ARG A2320    11496  22269  16805     80  -1367   2445       C  
ATOM   3446  NE  ARG A2320      30.036  79.522 318.923  1.00136.70           N  
ANISOU 3446  NE  ARG A2320    11688  23138  17114    218  -1503   2697       N  
ATOM   3447  CZ  ARG A2320      29.133  78.962 319.720  1.00134.54           C  
ANISOU 3447  CZ  ARG A2320    11677  22590  16853    393  -1531   2651       C  
ATOM   3448  NH1 ARG A2320      27.858  78.928 319.357  1.00133.47           N  
ANISOU 3448  NH1 ARG A2320    12053  21787  16873    442  -1436   2366       N  
ATOM   3449  NH2 ARG A2320      29.502  78.436 320.880  1.00133.44           N  
ANISOU 3449  NH2 ARG A2320    11283  22859  16561    514  -1651   2901       N  
ATOM   3450  N   THR A2321      27.699  76.071 314.894  1.00114.32           N  
ANISOU 3450  N   THR A2321    10087  18180  15170   1883   -377   2485       N  
ATOM   3451  CA  THR A2321      27.733  74.656 315.250  1.00110.77           C  
ANISOU 3451  CA  THR A2321     9644  17676  14769   2412   -199   2733       C  
ATOM   3452  C   THR A2321      28.355  73.815 314.138  1.00113.01           C  
ANISOU 3452  C   THR A2321     9889  17885  15165   2847    132   2901       C  
ATOM   3453  O   THR A2321      29.200  72.957 314.395  1.00114.25           O  
ANISOU 3453  O   THR A2321     9765  18342  15301   3265    271   3251       O  
ATOM   3454  CB  THR A2321      26.322  74.119 315.558  1.00100.07           C  
ANISOU 3454  CB  THR A2321     8778  15755  13488   2481   -171   2534       C  
ATOM   3455  OG1 THR A2321      25.737  74.887 316.616  1.00100.82           O  
ANISOU 3455  OG1 THR A2321     8918  15917  13473   2107   -453   2386       O  
ATOM   3456  CG2 THR A2321      26.385  72.657 315.973  1.00 95.40           C  
ANISOU 3456  CG2 THR A2321     8224  15092  12933   3008     27   2798       C  
ATOM   3457  N   VAL A2322      27.934  74.069 312.903  1.00115.41           N  
ANISOU 3457  N   VAL A2322    10482  17793  15575   2759    268   2662       N  
ATOM   3458  CA  VAL A2322      28.440  73.332 311.750  1.00116.75           C  
ANISOU 3458  CA  VAL A2322    10686  17834  15839   3135    602   2773       C  
ATOM   3459  C   VAL A2322      29.900  73.684 311.468  1.00120.59           C  
ANISOU 3459  C   VAL A2322    10643  18912  16265   3174    631   3036       C  
ATOM   3460  O   VAL A2322      30.701  72.816 311.123  1.00124.05           O  
ANISOU 3460  O   VAL A2322    10906  19495  16731   3636    894   3320       O  
ATOM   3461  CB  VAL A2322      27.589  73.605 310.491  1.00114.98           C  
ANISOU 3461  CB  VAL A2322    10907  17066  15714   2974    714   2435       C  
ATOM   3462  CG1 VAL A2322      28.173  72.895 309.278  1.00117.06           C  
ANISOU 3462  CG1 VAL A2322    11217  17213  16048   3335   1067   2540       C  
ATOM   3463  CG2 VAL A2322      26.153  73.166 310.722  1.00113.22           C  
ANISOU 3463  CG2 VAL A2322    11175  16300  15542   2950    703   2205       C  
ATOM   3464  N   LEU A2323      30.246  74.958 311.629  1.00119.12           N  
ANISOU 3464  N   LEU A2323    10206  19069  15985   2688    374   2949       N  
ATOM   3465  CA  LEU A2323      31.620  75.405 311.419  1.00117.86           C  
ANISOU 3465  CA  LEU A2323     9512  19525  15743   2634    367   3191       C  
ATOM   3466  C   LEU A2323      32.571  74.811 312.455  1.00123.35           C  
ANISOU 3466  C   LEU A2323     9845  20722  16300   2851    323   3546       C  
ATOM   3467  O   LEU A2323      33.774  74.712 312.218  1.00127.37           O  
ANISOU 3467  O   LEU A2323    10083  21592  16719   2930    413   3760       O  
ATOM   3468  CB  LEU A2323      31.700  76.933 311.450  1.00110.34           C  
ANISOU 3468  CB  LEU A2323     8458  18774  14692   1984     94   2983       C  
ATOM   3469  CG  LEU A2323      31.219  77.666 310.196  1.00104.54           C  
ANISOU 3469  CG  LEU A2323     8054  17624  14041   1727    171   2671       C  
ATOM   3470  CD1 LEU A2323      31.266  79.172 310.402  1.00103.00           C  
ANISOU 3470  CD1 LEU A2323     7799  17606  13731   1090    -94   2481       C  
ATOM   3471  CD2 LEU A2323      32.049  77.262 308.988  1.00106.71           C  
ANISOU 3471  CD2 LEU A2323     8178  17981  14384   2020    467   2826       C  
ATOM   3472  N   GLU A2324      32.026  74.415 313.601  1.00128.51           N  
ANISOU 3472  N   GLU A2324    10607  21320  16902   2898    188   3566       N  
ATOM   3473  CA  GLU A2324      32.825  73.800 314.656  1.00136.64           C  
ANISOU 3473  CA  GLU A2324    11444  22711  17764   3058    150   3851       C  
ATOM   3474  C   GLU A2324      33.002  72.302 314.433  1.00144.37           C  
ANISOU 3474  C   GLU A2324    12621  23429  18803   3660    490   4057       C  
ATOM   3475  O   GLU A2324      33.492  71.591 315.311  1.00149.49           O  
ANISOU 3475  O   GLU A2324    13178  24290  19331   3872    505   4306       O  
ATOM   3476  CB  GLU A2324      32.193  74.050 316.027  1.00135.68           C  
ANISOU 3476  CB  GLU A2324    11356  22662  17536   2824   -136   3788       C  
ATOM   3477  CG  GLU A2324      32.476  75.427 316.604  1.00135.92           C  
ANISOU 3477  CG  GLU A2324    11132  23117  17395   2210   -477   3680       C  
ATOM   3478  CD  GLU A2324      31.796  75.649 317.941  1.00135.50           C  
ANISOU 3478  CD  GLU A2324    11166  23093  17224   1984   -737   3598       C  
ATOM   3479  OE1 GLU A2324      31.081  74.736 318.406  1.00134.29           O  
ANISOU 3479  OE1 GLU A2324    11248  22640  17138   2315   -660   3634       O  
ATOM   3480  OE2 GLU A2324      31.976  76.738 318.527  1.00137.00           O  
ANISOU 3480  OE2 GLU A2324    11222  23589  17244   1462  -1006   3489       O  
ATOM   3481  N   SER A2325      32.600  71.824 313.259  1.00148.08           N  
ANISOU 3481  N   SER A2325    13389  23430  19443   3918    775   3951       N  
ATOM   3482  CA  SER A2325      32.790  70.422 312.903  1.00150.67           C  
ANISOU 3482  CA  SER A2325    13976  23458  19813   4448   1135   4116       C  
ATOM   3483  C   SER A2325      34.147  70.219 312.237  1.00151.84           C  
ANISOU 3483  C   SER A2325    13866  23930  19896   4641   1332   4362       C  
ATOM   3484  O   SER A2325      34.399  69.188 311.616  1.00153.10           O  
ANISOU 3484  O   SER A2325    14249  23829  20095   5057   1674   4478       O  
ATOM   3485  CB  SER A2325      31.669  69.936 311.983  1.00150.11           C  
ANISOU 3485  CB  SER A2325    14421  22689  19924   4608   1364   3865       C  
ATOM   3486  OG  SER A2325      31.817  68.559 311.685  1.00155.29           O  
ANISOU 3486  OG  SER A2325    15390  23020  20592   5067   1717   4001       O  
ATOM   3487  N   VAL A2326      35.012  71.219 312.369  1.00145.49           N  
ANISOU 3487  N   VAL A2326    12609  23690  18978   4313   1121   4438       N  
ATOM   3488  CA  VAL A2326      36.379  71.130 311.874  1.00137.91           C  
ANISOU 3488  CA  VAL A2326    11338  23135  17928   4454   1266   4703       C  
ATOM   3489  C   VAL A2326      37.306  70.680 313.001  1.00137.46           C  
ANISOU 3489  C   VAL A2326    10976  23582  17672   4586   1196   5059       C  
ATOM   3490  O   VAL A2326      38.272  69.950 312.776  1.00141.99           O  
ANISOU 3490  O   VAL A2326    11426  24346  18177   4948   1427   5363       O  
ATOM   3491  CB  VAL A2326      36.863  72.478 311.305  1.00129.04           C  
ANISOU 3491  CB  VAL A2326     9898  22355  16777   3995   1096   4594       C  
ATOM   3492  CG1 VAL A2326      38.241  72.335 310.677  1.00132.96           C  
ANISOU 3492  CG1 VAL A2326    10095  23233  17190   4166   1275   4867       C  
ATOM   3493  CG2 VAL A2326      35.864  73.013 310.293  1.00120.16           C  
ANISOU 3493  CG2 VAL A2326     9059  20759  15836   3829   1141   4243       C  
ATOM   3494  N   LEU A2327      36.992  71.114 314.218  1.00133.53           N  
ANISOU 3494  N   LEU A2327    10367  23300  17070   4296    886   5027       N  
ATOM   3495  CA  LEU A2327      37.785  70.767 315.392  1.00137.55           C  
ANISOU 3495  CA  LEU A2327    10585  24308  17368   4372    791   5348       C  
ATOM   3496  C   LEU A2327      37.494  69.346 315.864  1.00140.14           C  
ANISOU 3496  C   LEU A2327    11188  24341  17717   4886   1023   5525       C  
ATOM   3497  O   LEU A2327      36.838  68.572 315.168  1.00138.53           O  
ANISOU 3497  O   LEU A2327    11399  23557  17678   5199   1293   5419       O  
ATOM   3498  CB  LEU A2327      37.520  71.759 316.527  1.00134.59           C  
ANISOU 3498  CB  LEU A2327    10035  24248  16854   3847    386   5227       C  
TER    3499      LEU A2327                                                      
HETATM 3500  O01 FSY A2401       0.687  85.789 283.702  1.00 60.96           O  
HETATM 3501  C02 FSY A2401       1.833  85.290 283.426  1.00 64.40           C  
HETATM 3502  O03 FSY A2401       1.915  84.139 283.038  1.00 65.01           O  
HETATM 3503  C04 FSY A2401       3.095  86.151 283.593  1.00 66.45           C  
HETATM 3504  C05 FSY A2401       4.456  85.378 283.390  1.00 58.99           C  
HETATM 3505  C06 FSY A2401       5.573  85.801 282.633  1.00 61.40           C  
HETATM 3506  C07 FSY A2401       5.677  87.123 281.842  1.00 60.88           C  
HETATM 3507  N08 FSY A2401       6.508  84.905 282.712  1.00 64.86           N  
HETATM 3508  C09 FSY A2401       6.110  83.871 283.483  1.00 62.38           C  
HETATM 3509  C10 FSY A2401       4.834  84.117 283.936  1.00 58.57           C  
HETATM 3510  C11 FSY A2401       4.228  83.141 284.767  1.00 57.23           C  
HETATM 3511  C12 FSY A2401       4.967  81.983 285.081  1.00 58.63           C  
HETATM 3512  C13 FSY A2401       6.240  81.834 284.578  1.00 59.52           C  
HETATM 3513  N14 FSY A2401       6.778  82.771 283.797  1.00 62.06           N  
HETATM 3514  C15 FSY A2401       7.772  85.002 282.079  1.00 69.19           C  
HETATM 3515  C16 FSY A2401       7.640  84.702 280.531  1.00 92.62           C  
HETATM 3516  C17 FSY A2401       6.819  83.642 280.138  1.00 93.95           C  
HETATM 3517  C18 FSY A2401       6.661  83.330 278.790  1.00 95.44           C  
HETATM 3518  C19 FSY A2401       7.318  84.078 277.833  1.00 96.06           C  
HETATM 3519  C20 FSY A2401       8.127  85.130 278.208  1.00 95.93           C  
HETATM 3520  C21 FSY A2401       8.302  85.455 279.568  1.00 92.88           C  
HETATM 3521  C22 FSY A2401       9.222  86.640 279.880  1.00 91.77           C  
HETATM 3522  S26 FSY A2401       7.110  83.672 276.077  1.00 74.32           S  
HETATM 3523  O27 FSY A2401       6.927  82.131 275.934  1.00 61.42           O  
HETATM 3524  O28 FSY A2401       8.329  84.118 275.314  1.00 76.97           O  
HETATM 3525  C29 FSY A2401       5.655  84.531 275.436  1.00 43.03           C  
HETATM 3526  F23 FSY A2401       8.568  87.728 279.706  1.00 88.10           F  
HETATM 3527  F24 FSY A2401      10.249  86.615 279.028  1.00 92.52           F  
HETATM 3528  F25 FSY A2401       9.750  86.609 281.208  1.00 96.41           F  
HETATM 3529  S   SO4 A2402      -7.477  87.419 329.753  1.00 69.81           S  
HETATM 3530  O1  SO4 A2402      -8.308  87.749 328.599  1.00 67.38           O  
HETATM 3531  O2  SO4 A2402      -6.127  87.927 329.531  1.00 69.99           O  
HETATM 3532  O3  SO4 A2402      -8.035  88.032 330.956  1.00 70.76           O  
HETATM 3533  O4  SO4 A2402      -7.429  85.970 329.915  1.00 67.54           O  
HETATM 3534  S   SO4 A2403      -7.359  61.163 335.352  1.00 93.61           S  
HETATM 3535  O1  SO4 A2403      -7.194  61.213 333.902  1.00100.30           O  
HETATM 3536  O2  SO4 A2403      -8.732  60.783 335.673  1.00 92.55           O  
HETATM 3537  O3  SO4 A2403      -6.438  60.178 335.913  1.00 90.95           O  
HETATM 3538  O4  SO4 A2403      -7.077  62.478 335.919  1.00 91.32           O  
HETATM 3539  S   SO4 A2404       8.127  91.380 317.239  1.00 67.83           S  
HETATM 3540  O1  SO4 A2404       8.663  92.070 316.070  1.00 72.62           O  
HETATM 3541  O2  SO4 A2404       8.278  89.937 317.076  1.00 65.53           O  
HETATM 3542  O3  SO4 A2404       6.712  91.706 317.386  1.00 63.17           O  
HETATM 3543  O4  SO4 A2404       8.860  91.809 318.427  1.00 72.53           O  
HETATM 3544  S   SO4 A2405      12.657  80.382 319.902  0.50 72.00           S  
HETATM 3545  O1  SO4 A2405      13.268  81.601 319.380  0.50 69.81           O  
HETATM 3546  O2  SO4 A2405      11.292  80.271 319.396  0.50 72.10           O  
HETATM 3547  O3  SO4 A2405      12.633  80.432 321.362  0.50 71.58           O  
HETATM 3548  O4  SO4 A2405      13.432  79.223 319.470  0.50 72.24           O  
HETATM 3549  S   SO4 A2406       2.373  83.189 319.173  1.00 92.23           S  
HETATM 3550  O1  SO4 A2406       2.231  81.819 318.691  1.00 87.75           O  
HETATM 3551  O2  SO4 A2406       1.281  84.007 318.654  1.00 92.91           O  
HETATM 3552  O3  SO4 A2406       2.328  83.195 320.633  1.00 97.86           O  
HETATM 3553  O4  SO4 A2406       3.648  83.738 318.720  1.00 88.04           O  
HETATM 3554  S   SO4 A2407      -0.183  74.784 321.445  1.00 90.50           S  
HETATM 3555  O1  SO4 A2407      -0.389  76.113 320.877  1.00 94.63           O  
HETATM 3556  O2  SO4 A2407      -0.516  73.767 320.452  1.00 92.64           O  
HETATM 3557  O3  SO4 A2407      -1.044  74.624 322.613  1.00 84.30           O  
HETATM 3558  O4  SO4 A2407       1.217  74.634 321.829  1.00 90.18           O  
HETATM 3559  S   SO4 A2408     -17.594  92.335 319.432  1.00166.91           S  
HETATM 3560  O1  SO4 A2408     -16.207  92.643 319.095  1.00164.74           O  
HETATM 3561  O2  SO4 A2408     -18.252  91.736 318.275  1.00167.28           O  
HETATM 3562  O3  SO4 A2408     -17.628  91.399 320.552  1.00167.32           O  
HETATM 3563  O4  SO4 A2408     -18.291  93.562 319.806  1.00168.01           O  
HETATM 3564  S   SO4 A2409     -27.340  77.456 328.108  1.00160.54           S  
HETATM 3565  O1  SO4 A2409     -26.142  78.279 327.969  1.00160.77           O  
HETATM 3566  O2  SO4 A2409     -27.373  76.458 327.043  1.00161.57           O  
HETATM 3567  O3  SO4 A2409     -28.525  78.304 328.013  1.00160.69           O  
HETATM 3568  O4  SO4 A2409     -27.324  76.788 329.406  1.00160.31           O  
HETATM 3569  S   SO4 A2410     -21.053  80.784 345.095  0.50 72.07           S  
HETATM 3570  O1  SO4 A2410     -20.676  81.408 343.830  0.50 74.44           O  
HETATM 3571  O2  SO4 A2410     -21.242  79.350 344.892  0.50 74.50           O  
HETATM 3572  O3  SO4 A2410     -22.300  81.373 345.577  0.50 66.44           O  
HETATM 3573  O4  SO4 A2410     -19.996  81.000 346.079  0.50 68.90           O  
HETATM 3574  C1  SIN A2411      -8.507  84.388 300.853  1.00 92.68           C  
HETATM 3575  O1  SIN A2411      -8.837  83.921 299.741  1.00 93.32           O  
HETATM 3576  O2  SIN A2411      -8.436  85.628 300.992  1.00 94.59           O  
HETATM 3577  C2  SIN A2411      -8.194  83.469 302.010  1.00 91.17           C  
HETATM 3578  C3  SIN A2411      -8.368  84.219 303.326  1.00 93.30           C  
HETATM 3579  C4  SIN A2411      -8.242  83.245 304.474  1.00100.03           C  
HETATM 3580  O3  SIN A2411      -7.733  82.120 304.293  1.00104.07           O  
HETATM 3581  O4  SIN A2411      -8.647  83.545 305.617  1.00101.99           O  
HETATM 3582  C1  SIN A2412      13.292  89.061 320.934  1.00 78.19           C  
HETATM 3583  O1  SIN A2412      14.518  88.832 320.842  1.00 82.40           O  
HETATM 3584  O2  SIN A2412      12.549  88.214 321.473  1.00 78.81           O  
HETATM 3585  C2  SIN A2412      12.719  90.348 320.394  1.00 71.72           C  
HETATM 3586  C3  SIN A2412      13.800  91.071 319.601  1.00 71.36           C  
HETATM 3587  C4  SIN A2412      14.112  92.400 320.244  1.00 77.21           C  
HETATM 3588  O3  SIN A2412      14.940  93.170 319.715  1.00 79.52           O  
HETATM 3589  O4  SIN A2412      13.551  92.747 321.306  1.00 81.35           O  
HETATM 3590  C1  SIN A2413      10.263  87.541 272.553  1.00113.74           C  
HETATM 3591  O1  SIN A2413      10.870  86.451 272.626  1.00112.71           O  
HETATM 3592  O2  SIN A2413       9.235  87.712 273.243  1.00114.37           O  
HETATM 3593  C2  SIN A2413      10.762  88.636 271.642  1.00115.19           C  
HETATM 3594  C3  SIN A2413      11.512  89.681 272.467  1.00117.56           C  
HETATM 3595  C4  SIN A2413      12.110  90.710 271.536  1.00120.77           C  
HETATM 3596  O3  SIN A2413      12.742  90.355 270.517  1.00119.43           O  
HETATM 3597  O4  SIN A2413      11.976  91.929 271.774  1.00123.57           O  
HETATM 3598  C1  SIN A2414      -8.955  72.965 319.211  1.00106.58           C  
HETATM 3599  O1  SIN A2414      -7.918  72.273 319.299  1.00105.72           O  
HETATM 3600  O2  SIN A2414      -9.915  72.720 319.974  1.00106.72           O  
HETATM 3601  C2  SIN A2414      -9.051  74.073 318.190  1.00106.77           C  
HETATM 3602  C3  SIN A2414      -9.775  73.556 316.953  1.00106.62           C  
HETATM 3603  C4  SIN A2414     -10.273  74.722 316.134  1.00104.44           C  
HETATM 3604  O3  SIN A2414      -9.845  74.911 314.974  1.00100.96           O  
HETATM 3605  O4  SIN A2414     -11.122  75.511 316.604  1.00105.09           O  
HETATM 3606  C1  SIN A2415      -8.516  58.922 329.289  1.00111.03           C  
HETATM 3607  O1  SIN A2415      -8.327  58.132 328.339  1.00110.69           O  
HETATM 3608  O2  SIN A2415      -9.672  59.058 329.743  1.00112.26           O  
HETATM 3609  C2  SIN A2415      -7.367  59.700 329.883  1.00110.17           C  
HETATM 3610  C3  SIN A2415      -6.171  59.629 328.939  1.00109.02           C  
HETATM 3611  C4  SIN A2415      -5.156  60.672 329.340  1.00106.80           C  
HETATM 3612  O3  SIN A2415      -4.166  60.903 328.613  1.00103.43           O  
HETATM 3613  O4  SIN A2415      -5.294  61.317 330.402  1.00107.28           O  
HETATM 3614  C1  PGE A2416     -18.232  84.728 335.953  1.00108.14           C  
HETATM 3615  O1  PGE A2416     -19.244  83.742 336.101  1.00108.93           O  
HETATM 3616  C2  PGE A2416     -16.907  84.036 335.703  1.00107.92           C  
HETATM 3617  O2  PGE A2416     -15.851  84.938 335.965  1.00108.68           O  
HETATM 3618  C3  PGE A2416     -15.449  85.676 334.830  1.00109.80           C  
HETATM 3619  C4  PGE A2416     -15.493  87.155 335.165  1.00111.98           C  
HETATM 3620  O4  PGE A2416     -18.093  87.942 331.288  1.00107.22           O  
HETATM 3621  C6  PGE A2416     -16.851  88.209 331.925  1.00110.67           C  
HETATM 3622  C5  PGE A2416     -16.898  87.675 333.342  1.00113.35           C  
HETATM 3623  O3  PGE A2416     -15.648  87.887 333.967  1.00113.69           O  
HETATM 3624  C1  OLA A2417       5.324  70.313 309.565  1.00102.52           C  
HETATM 3625  O1  OLA A2417       5.131  69.078 309.602  1.00102.26           O  
HETATM 3626  O2  OLA A2417       4.799  70.982 308.648  1.00102.79           O  
HETATM 3627  C2  OLA A2417       6.180  70.984 310.613  1.00100.70           C  
HETATM 3628  C3  OLA A2417       7.481  70.207 310.780  1.00 95.85           C  
HETATM 3629  C4  OLA A2417       8.688  71.097 310.508  1.00 91.20           C  
HETATM 3630  C5  OLA A2417       9.942  70.260 310.295  1.00 89.43           C  
HETATM 3631  C6  OLA A2417      10.332  70.220 308.821  1.00 89.42           C  
HETATM 3632  C7  OLA A2417      11.848  70.176 308.680  1.00 88.00           C  
HETATM 3633  C8  OLA A2417      12.323  70.778 307.362  1.00 86.06           C  
HETATM 3634  C9  OLA A2417      13.793  71.094 307.495  1.00 85.22           C  
HETATM 3635  C10 OLA A2417      14.531  71.787 306.430  1.00 84.02           C  
HETATM 3636  C11 OLA A2417      14.376  71.374 304.986  1.00 82.04           C  
HETATM 3637  C12 OLA A2417      15.599  71.846 304.208  1.00 80.93           C  
HETATM 3638  C13 OLA A2417      15.243  72.188 302.767  1.00 82.68           C  
HETATM 3639  C14 OLA A2417      16.354  71.761 301.814  1.00 86.52           C  
HETATM 3640  C15 OLA A2417      16.549  72.787 300.703  1.00 89.00           C  
HETATM 3641  C16 OLA A2417      17.451  72.242 299.601  1.00 86.90           C  
HETATM 3642  C17 OLA A2417      18.222  73.365 298.919  1.00 83.64           C  
HETATM 3643  C18 OLA A2417      19.285  73.938 299.850  1.00 82.50           C  
HETATM 3644  C1  PGO A2418      -6.994  80.197 312.751  1.00 83.70           C  
HETATM 3645  C2  PGO A2418      -5.751  79.922 313.591  1.00 84.81           C  
HETATM 3646  C3  PGO A2418      -6.012  78.803 314.589  1.00 84.72           C  
HETATM 3647  O1  PGO A2418      -6.764  81.342 311.920  1.00 84.00           O  
HETATM 3648  O2  PGO A2418      -5.403  81.106 314.315  1.00 86.21           O  
HETATM 3649  O   HOH A2501     -10.702  74.502 346.059  1.00 46.51           O  
HETATM 3650  O   HOH A2502       0.079  94.442 317.015  1.00 53.40           O  
HETATM 3651  O   HOH A2503     -15.794  91.726 332.613  1.00 66.23           O  
CONECT   50 1520                                                                
CONECT  764 1386                                                                
CONECT 1386  764                                                                
CONECT 1520   50                                                                
CONECT 3329 3334                                                                
CONECT 3334 3329 3335                                                           
CONECT 3335 3334 3336 3342                                                      
CONECT 3336 3335 3337                                                           
CONECT 3337 3336 3338                                                           
CONECT 3338 3337 3339                                                           
CONECT 3339 3338 3340 3341                                                      
CONECT 3340 3339                                                                
CONECT 3341 3339                                                                
CONECT 3342 3335 3343 3344                                                      
CONECT 3343 3342                                                                
CONECT 3344 3342                                                                
CONECT 3500 3501                                                                
CONECT 3501 3500 3502 3503                                                      
CONECT 3502 3501                                                                
CONECT 3503 3501 3504                                                           
CONECT 3504 3503 3505 3509                                                      
CONECT 3505 3504 3506 3507                                                      
CONECT 3506 3505                                                                
CONECT 3507 3505 3508 3514                                                      
CONECT 3508 3507 3509 3513                                                      
CONECT 3509 3504 3508 3510                                                      
CONECT 3510 3509 3511                                                           
CONECT 3511 3510 3512                                                           
CONECT 3512 3511 3513                                                           
CONECT 3513 3508 3512                                                           
CONECT 3514 3507 3515                                                           
CONECT 3515 3514 3516 3520                                                      
CONECT 3516 3515 3517                                                           
CONECT 3517 3516 3518                                                           
CONECT 3518 3517 3519 3522                                                      
CONECT 3519 3518 3520                                                           
CONECT 3520 3515 3519 3521                                                      
CONECT 3521 3520 3526 3527 3528                                                 
CONECT 3522 3518 3523 3524 3525                                                 
CONECT 3523 3522                                                                
CONECT 3524 3522                                                                
CONECT 3525 3522                                                                
CONECT 3526 3521                                                                
CONECT 3527 3521                                                                
CONECT 3528 3521                                                                
CONECT 3529 3530 3531 3532 3533                                                 
CONECT 3530 3529                                                                
CONECT 3531 3529                                                                
CONECT 3532 3529                                                                
CONECT 3533 3529                                                                
CONECT 3534 3535 3536 3537 3538                                                 
CONECT 3535 3534                                                                
CONECT 3536 3534                                                                
CONECT 3537 3534                                                                
CONECT 3538 3534                                                                
CONECT 3539 3540 3541 3542 3543                                                 
CONECT 3540 3539                                                                
CONECT 3541 3539                                                                
CONECT 3542 3539                                                                
CONECT 3543 3539                                                                
CONECT 3544 3545 3546 3547 3548                                                 
CONECT 3545 3544                                                                
CONECT 3546 3544                                                                
CONECT 3547 3544                                                                
CONECT 3548 3544                                                                
CONECT 3549 3550 3551 3552 3553                                                 
CONECT 3550 3549                                                                
CONECT 3551 3549                                                                
CONECT 3552 3549                                                                
CONECT 3553 3549                                                                
CONECT 3554 3555 3556 3557 3558                                                 
CONECT 3555 3554                                                                
CONECT 3556 3554                                                                
CONECT 3557 3554                                                                
CONECT 3558 3554                                                                
CONECT 3559 3560 3561 3562 3563                                                 
CONECT 3560 3559                                                                
CONECT 3561 3559                                                                
CONECT 3562 3559                                                                
CONECT 3563 3559                                                                
CONECT 3564 3565 3566 3567 3568                                                 
CONECT 3565 3564                                                                
CONECT 3566 3564                                                                
CONECT 3567 3564                                                                
CONECT 3568 3564                                                                
CONECT 3569 3570 3571 3572 3573                                                 
CONECT 3570 3569                                                                
CONECT 3571 3569                                                                
CONECT 3572 3569                                                                
CONECT 3573 3569                                                                
CONECT 3574 3575 3576 3577                                                      
CONECT 3575 3574                                                                
CONECT 3576 3574                                                                
CONECT 3577 3574 3578                                                           
CONECT 3578 3577 3579                                                           
CONECT 3579 3578 3580 3581                                                      
CONECT 3580 3579                                                                
CONECT 3581 3579                                                                
CONECT 3582 3583 3584 3585                                                      
CONECT 3583 3582                                                                
CONECT 3584 3582                                                                
CONECT 3585 3582 3586                                                           
CONECT 3586 3585 3587                                                           
CONECT 3587 3586 3588 3589                                                      
CONECT 3588 3587                                                                
CONECT 3589 3587                                                                
CONECT 3590 3591 3592 3593                                                      
CONECT 3591 3590                                                                
CONECT 3592 3590                                                                
CONECT 3593 3590 3594                                                           
CONECT 3594 3593 3595                                                           
CONECT 3595 3594 3596 3597                                                      
CONECT 3596 3595                                                                
CONECT 3597 3595                                                                
CONECT 3598 3599 3600 3601                                                      
CONECT 3599 3598                                                                
CONECT 3600 3598                                                                
CONECT 3601 3598 3602                                                           
CONECT 3602 3601 3603                                                           
CONECT 3603 3602 3604 3605                                                      
CONECT 3604 3603                                                                
CONECT 3605 3603                                                                
CONECT 3606 3607 3608 3609                                                      
CONECT 3607 3606                                                                
CONECT 3608 3606                                                                
CONECT 3609 3606 3610                                                           
CONECT 3610 3609 3611                                                           
CONECT 3611 3610 3612 3613                                                      
CONECT 3612 3611                                                                
CONECT 3613 3611                                                                
CONECT 3614 3615 3616                                                           
CONECT 3615 3614                                                                
CONECT 3616 3614 3617                                                           
CONECT 3617 3616 3618                                                           
CONECT 3618 3617 3619                                                           
CONECT 3619 3618 3623                                                           
CONECT 3620 3621                                                                
CONECT 3621 3620 3622                                                           
CONECT 3622 3621 3623                                                           
CONECT 3623 3619 3622                                                           
CONECT 3624 3625 3626 3627                                                      
CONECT 3625 3624                                                                
CONECT 3626 3624                                                                
CONECT 3627 3624 3628                                                           
CONECT 3628 3627 3629                                                           
CONECT 3629 3628 3630                                                           
CONECT 3630 3629 3631                                                           
CONECT 3631 3630 3632                                                           
CONECT 3632 3631 3633                                                           
CONECT 3633 3632 3634                                                           
CONECT 3634 3633 3635                                                           
CONECT 3635 3634 3636                                                           
CONECT 3636 3635 3637                                                           
CONECT 3637 3636 3638                                                           
CONECT 3638 3637 3639                                                           
CONECT 3639 3638 3640                                                           
CONECT 3640 3639 3641                                                           
CONECT 3641 3640 3642                                                           
CONECT 3642 3641 3643                                                           
CONECT 3643 3642                                                                
CONECT 3644 3645 3647                                                           
CONECT 3645 3644 3646 3648                                                      
CONECT 3646 3645                                                                
CONECT 3647 3644                                                                
CONECT 3648 3645                                                                
MASTER      373    0   19   27    2    0   29    6 3642    1  165   37          
END