HEADER    MEMBRANE PROTEIN                        31-JAN-14   4OO9              
TITLE     STRUCTURE OF THE HUMAN CLASS C GPCR METABOTROPIC GLUTAMATE RECEPTOR 5 
TITLE    2 TRANSMEMBRANE DOMAIN IN COMPLEX WITH THE NEGATIVE ALLOSTERIC         
TITLE    3 MODULATOR MAVOGLURANT                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METABOTROPIC GLUTAMATE RECEPTOR 5, LYSOZYME, METABOTROPIC  
COMPND   3 GLUTAMATE RECEPTOR 5 CHIMERA;                                        
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: SEE REMARK 999;                                            
COMPND   6 SYNONYM: MGLUR5, ENDOLYSIN, LYSIS PROTEIN, MURAMIDASE;               
COMPND   7 EC: 3.2.1.17;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          
SOURCE   3 ORGANISM_COMMON: HUMAN, T4 PHAGE, HUMAN;                             
SOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   5 GENE: GRM5, GPRC1E, MGLUR5, E;                                       
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: FASTBAC                                   
KEYWDS    7TM, RECEPTOR, G-PROTEIN, CYSTEINE-S-ACETAMIDE, MEMBRANE PROTEIN      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.S.DORE,K.OKRASA,J.C.PATEL,M.SERRANO-VEGA,K.BENNETT,R.M.COOKE,       
AUTHOR   2 J.C.ERREY,A.JAZAYERI,S.KHAN,B.TEHAN,M.WEIR,G.R.WIGGIN,F.H.MARSHALL   
REVDAT   6   26-JUL-17 4OO9    1       SOURCE REMARK                            
REVDAT   5   15-JUL-15 4OO9    1       SOURCE                                   
REVDAT   4   06-AUG-14 4OO9    1       JRNL                                     
REVDAT   3   16-JUL-14 4OO9    1       ATOM   COMPND DBREF  HETNAM              
REVDAT   3 2                   1       HETSYN REMARK SOURCE                     
REVDAT   2   09-JUL-14 4OO9    1       JRNL                                     
REVDAT   1   02-JUL-14 4OO9    0                                                
JRNL        AUTH   A.S.DORE,K.OKRASA,J.C.PATEL,M.SERRANO-VEGA,K.BENNETT,        
JRNL        AUTH 2 R.M.COOKE,J.C.ERREY,A.JAZAYERI,S.KHAN,B.TEHAN,M.WEIR,        
JRNL        AUTH 3 G.R.WIGGIN,F.H.MARSHALL                                      
JRNL        TITL   STRUCTURE OF CLASS C GPCR METABOTROPIC GLUTAMATE RECEPTOR 5  
JRNL        TITL 2 TRANSMEMBRANE DOMAIN.                                        
JRNL        REF    NATURE                        V. 511   557 2014              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   25042998                                                     
JRNL        DOI    10.1038/NATURE13396                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.74                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 14779                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.241                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.680                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 691                             
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 29.7415 -  4.4420    0.90     2768   148  0.2093 0.2374        
REMARK   3     2  4.4420 -  3.5276    0.94     2813   141  0.2213 0.2630        
REMARK   3     3  3.5276 -  3.0822    0.95     2851   131  0.2615 0.3285        
REMARK   3     4  3.0822 -  2.8006    0.96     2855   140  0.2780 0.2635        
REMARK   3     5  2.8006 -  2.6000    0.95     2801   131  0.3078 0.3762        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.70                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.750           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3373                                  
REMARK   3   ANGLE     :  0.658           4555                                  
REMARK   3   CHIRALITY :  0.043            526                                  
REMARK   3   PLANARITY :  0.003            551                                  
REMARK   3   DIHEDRAL  : 11.531           1280                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 568 THROUGH 640 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -33.6069 -13.9594  41.1170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2019 T22:   0.1974                                     
REMARK   3      T33:   0.2147 T12:  -0.0650                                     
REMARK   3      T13:  -0.0220 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3076 L22:   0.1018                                     
REMARK   3      L33:   0.0372 L12:   0.1014                                     
REMARK   3      L13:   0.2672 L23:   0.0489                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1043 S12:   0.0604 S13:  -0.2340                       
REMARK   3      S21:   0.1240 S22:   0.0169 S23:   0.2486                       
REMARK   3      S31:   0.1873 S32:   0.0725 S33:   0.0231                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 641 THROUGH 689 ) OR CHAIN 'A'    
REMARK   3               AND (RESID 1002 THROUGH 1162 )                         
REMARK   3    ORIGIN FOR THE GROUP (A): -14.3547   4.2183   7.9223              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1429 T22:   0.3198                                     
REMARK   3      T33:   0.1618 T12:   0.0647                                     
REMARK   3      T13:   0.0111 T23:  -0.0299                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.2527 L22:   0.2104                                     
REMARK   3      L33:   0.5866 L12:   0.2064                                     
REMARK   3      L13:  -0.1660 L23:  -0.0684                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1206 S12:  -0.1167 S13:  -0.0101                       
REMARK   3      S21:   0.0021 S22:   0.0662 S23:  -0.0498                       
REMARK   3      S31:  -0.1231 S32:  -0.2951 S33:  -0.1222                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 690 THROUGH 832 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -22.7584  -5.6735  38.5019              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1870 T22:   0.1195                                     
REMARK   3      T33:   0.1967 T12:  -0.0287                                     
REMARK   3      T13:  -0.0043 T23:   0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5221 L22:   0.2787                                     
REMARK   3      L33:   0.2468 L12:  -0.2132                                     
REMARK   3      L13:   0.1409 L23:  -0.1073                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0313 S12:  -0.0197 S13:  -0.0149                       
REMARK   3      S21:   0.0105 S22:  -0.0414 S23:  -0.0331                       
REMARK   3      S31:   0.0518 S32:  -0.0183 S33:  -0.0498                       
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 4OO9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000084742.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 5                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96861                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14800                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.955                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
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 ENTRIES 3EML, 3UON, 4DAJ, 4DKL, 4DJH, 3V2Y,      
REMARK 200  4EA3, AND 1U19                                                      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24-34% V/V PEG400, 0.2 M AMMONIUM        
REMARK 280  PHOSPHATE DIBASIC, 0.1 M MES, PH 6.8, LIPIDIC CUBIC PHASE,          
REMARK 280  TEMPERATURE 293.1K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       71.62100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.77750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       71.62100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       21.77750            
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 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A4143  LIES ON A SPECIAL POSITION.                          
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     ALA A   566                                                      
REMARK 465     ALA A   567                                                      
REMARK 465     CYS A   681                                                      
REMARK 465     THR A   682                                                      
REMARK 465     LYS A   683                                                      
REMARK 465     LYS A   684                                                      
REMARK 465     PRO A   685                                                      
REMARK 465     ARG A   686                                                      
REMARK 465     PHE A   687                                                      
REMARK 465     MET A   688                                                      
REMARK 465     HIS A   721                                                      
REMARK 465     ASP A   722                                                      
REMARK 465     TYR A   723                                                      
REMARK 465     PRO A   724                                                      
REMARK 465     SER A   725                                                      
REMARK 465     ILE A   726                                                      
REMARK 465     ARG A   727                                                      
REMARK 465     GLU A   728                                                      
REMARK 465     VAL A   833                                                      
REMARK 465     ARG A   834                                                      
REMARK 465     SER A   835                                                      
REMARK 465     ALA A   836                                                      
REMARK 465     ALA A   837                                                      
REMARK 465     ALA A   838                                                      
REMARK 465     ALA A   839                                                      
REMARK 465     HIS A   840                                                      
REMARK 465     HIS A   841                                                      
REMARK 465     HIS A   842                                                      
REMARK 465     HIS A   843                                                      
REMARK 465     HIS A   844                                                      
REMARK 465     HIS A   845                                                      
REMARK 465     HIS A   846                                                      
REMARK 465     HIS A   847                                                      
REMARK 465     HIS A   848                                                      
REMARK 465     HIS A   849                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLU A  1011     O    HOH A  4142              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A 639       92.50    -69.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA A 4002                                                       
REMARK 610     OLA A 4003                                                       
REMARK 610     OLA A 4004                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 4001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 4002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 4003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 4004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2U8 A 4005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 4006                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 PROTEIN IS A CHIMERA COMPRISING RESIDUES 569-678 AND 679-836 OF      
REMARK 999 GLUR5 SEPARATED BY RESIDUES 2-162 OF LYSOZYME.                       
DBREF  4OO9 A  569   678  UNP    P41594   GRM5_HUMAN     569    678             
DBREF  4OO9 A 1002  1162  UNP    P00720   LYS_BPT4         2    162             
DBREF  4OO9 A  680   836  UNP    P41594   GRM5_HUMAN     680    836             
SEQADV 4OO9 ALA A  566  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 ALA A  567  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 SER A  568  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 ALA A  579  UNP  P41594    GLU   579 ENGINEERED MUTATION            
SEQADV 4OO9 TYR A  667  UNP  P41594    ASN   667 ENGINEERED MUTATION            
SEQADV 4OO9 ALA A  669  UNP  P41594    ILE   669 ENGINEERED MUTATION            
SEQADV 4OO9 MET A  675  UNP  P41594    GLY   675 ENGINEERED MUTATION            
SEQADV 4OO9 THR A 1054  UNP  P00720    CYS    54 ENGINEERED MUTATION            
SEQADV 4OO9 ALA A 1097  UNP  P00720    CYS    97 ENGINEERED MUTATION            
SEQADV 4OO9 ALA A  742  UNP  P41594    THR   742 ENGINEERED MUTATION            
SEQADV 4OO9 ALA A  753  UNP  P41594    SER   753 ENGINEERED MUTATION            
SEQADV 4OO9 ALA A  837  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 ALA A  838  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 ALA A  839  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 HIS A  840  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 HIS A  841  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 HIS A  842  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 HIS A  843  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 HIS A  844  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 HIS A  845  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 HIS A  846  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 HIS A  847  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 HIS A  848  UNP  P41594              EXPRESSION TAG                 
SEQADV 4OO9 HIS A  849  UNP  P41594              EXPRESSION TAG                 
SEQRES   1 A  444  ALA ALA SER PRO VAL GLN TYR LEU ARG TRP GLY ASP PRO          
SEQRES   2 A  444  ALA PRO ILE ALA ALA VAL VAL PHE ALA CYS LEU GLY LEU          
SEQRES   3 A  444  LEU ALA THR LEU PHE VAL THR VAL VAL PHE ILE ILE TYR          
SEQRES   4 A  444  ARG ASP THR PRO VAL VAL LYS SER SER SER ARG GLU LEU          
SEQRES   5 A  444  CYS TYR ILE ILE LEU ALA GLY ILE CYS LEU GLY TYR LEU          
SEQRES   6 A  444  CYS THR PHE YCM LEU ILE ALA LYS PRO LYS GLN ILE TYR          
SEQRES   7 A  444  CYS TYR LEU GLN ARG ILE GLY ILE GLY LEU SER PRO ALA          
SEQRES   8 A  444  MET SER TYR SER ALA LEU VAL THR LYS THR TYR ARG ALA          
SEQRES   9 A  444  ALA ARG ILE LEU ALA MET SER LYS LYS ASN ILE PHE GLU          
SEQRES  10 A  444  MET LEU ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR          
SEQRES  11 A  444  LYS ASP THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS          
SEQRES  12 A  444  LEU LEU THR LYS SER PRO SER LEU ASN ALA ALA LYS SER          
SEQRES  13 A  444  GLU LEU ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL          
SEQRES  14 A  444  ILE THR LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP          
SEQRES  15 A  444  VAL ASP ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS          
SEQRES  16 A  444  LEU LYS PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG          
SEQRES  17 A  444  ALA ALA LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR          
SEQRES  18 A  444  GLY VAL ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN          
SEQRES  19 A  444  GLN LYS ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS          
SEQRES  20 A  444  SER ARG TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG          
SEQRES  21 A  444  VAL ILE THR THR PHE ARG THR GLY THR TRP ASP ALA TYR          
SEQRES  22 A  444  LYS ILE CYS THR LYS LYS PRO ARG PHE MET SER ALA YCM          
SEQRES  23 A  444  ALA GLN LEU VAL ILE ALA PHE ILE LEU ILE CYS ILE GLN          
SEQRES  24 A  444  LEU GLY ILE ILE VAL ALA LEU PHE ILE MET GLU PRO PRO          
SEQRES  25 A  444  ASP ILE MET HIS ASP TYR PRO SER ILE ARG GLU VAL TYR          
SEQRES  26 A  444  LEU ILE CYS ASN THR THR ASN LEU GLY VAL VAL ALA PRO          
SEQRES  27 A  444  LEU GLY TYR ASN GLY LEU LEU ILE LEU ALA CYS THR PHE          
SEQRES  28 A  444  TYR ALA PHE LYS THR ARG ASN VAL PRO ALA ASN PHE ASN          
SEQRES  29 A  444  GLU ALA LYS TYR ILE ALA PHE THR MET TYR THR THR CYS          
SEQRES  30 A  444  ILE ILE TRP LEU ALA PHE VAL PRO ILE TYR PHE GLY SER          
SEQRES  31 A  444  ASN TYR LYS ILE ILE THR MET CYS PHE SER VAL SER LEU          
SEQRES  32 A  444  SER ALA THR VAL ALA LEU GLY CYS MET PHE VAL PRO LYS          
SEQRES  33 A  444  VAL TYR ILE ILE LEU ALA LYS PRO GLU ARG ASN VAL ARG          
SEQRES  34 A  444  SER ALA ALA ALA ALA HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  35 A  444  HIS HIS                                                      
MODRES 4OO9 YCM A  634  CYS  S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                  
MODRES 4OO9 YCM A  691  CYS  S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                  
HET    YCM  A 634      10                                                       
HET    YCM  A 691      10                                                       
HET    OLA  A4001      20                                                       
HET    OLA  A4002      15                                                       
HET    OLA  A4003      14                                                       
HET    OLA  A4004      13                                                       
HET    2U8  A4005      23                                                       
HET    MES  A4006      12                                                       
HETNAM     YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                                
HETNAM     OLA OLEIC ACID                                                       
HETNAM     2U8 MAVOGLURANT                                                      
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETSYN     YCM CYSTEINE-S-ACETAMIDE                                             
HETSYN     2U8 METHYL (3AR,4S,7AR)-4-HYDROXY-4-[(3-METHYLPHENYL)                
HETSYN   2 2U8  ETHYNYL]OCTAHYDRO-1H-INDOLE-1-CARBOXYLATE                       
FORMUL   1  YCM    2(C5 H10 N2 O3 S)                                            
FORMUL   2  OLA    4(C18 H34 O2)                                                
FORMUL   6  2U8    C19 H23 N O3                                                 
FORMUL   7  MES    C6 H13 N O4 S                                                
FORMUL   8  HOH   *46(H2 O)                                                     
HELIX    1   1 SER A  568  GLY A  576  1                                   9    
HELIX    2   2 PRO A  578  TYR A  604  1                                  27    
HELIX    3   3 THR A  607  SER A  612  1                                   6    
HELIX    4   4 SER A  614  CYS A  631  1                                  18    
HELIX    5   5 CYS A  631  ILE A  636  1                                   6    
HELIX    6   6 LYS A  640  GLU A 1011  1                                  49    
HELIX    7   7 SER A 1038  GLY A 1051  1                                  14    
HELIX    8   8 THR A 1059  ARG A 1080  1                                  22    
HELIX    9   9 LEU A 1084  LEU A 1091  1                                   8    
HELIX   10  10 ASP A 1092  GLY A 1107  1                                  16    
HELIX   11  11 GLY A 1107  ALA A 1112  1                                   6    
HELIX   12  12 PHE A 1114  GLN A 1123  1                                  10    
HELIX   13  13 ARG A 1125  ALA A 1134  1                                  10    
HELIX   14  14 SER A 1136  THR A 1142  1                                   7    
HELIX   15  15 THR A 1142  GLY A 1156  1                                  15    
HELIX   16  16 ALA A  690  GLU A  715  1                                  26    
HELIX   17  17 ASN A  737  THR A  761  1                                  25    
HELIX   18  18 GLU A  770  GLY A  794  1                                  25    
HELIX   19  19 TYR A  797  PHE A  818  1                                  22    
HELIX   20  20 PHE A  818  LYS A  828  1                                  11    
SHEET    1   A 3 TYR A1018  LYS A1019  0                                        
SHEET    2   A 3 TYR A1025  ILE A1027 -1  O  THR A1026   N  TYR A1018           
SHEET    3   A 3 HIS A1031  LEU A1032 -1  O  HIS A1031   N  ILE A1027           
SSBOND   1 CYS A  644    CYS A  733                          1555   1555  2.03  
LINK         C   PHE A 633                 N   YCM A 634     1555   1555  1.33  
LINK         C   YCM A 634                 N   LEU A 635     1555   1555  1.33  
LINK         C   ALA A 690                 N   YCM A 691     1555   1555  1.33  
LINK         C   YCM A 691                 N   ALA A 692     1555   1555  1.33  
SITE     1 AC1  4 VAL A 741  GLY A 745  TRP A 785  PHE A 793                    
SITE     1 AC2  4 PRO A 569  VAL A 570  ILE A 581  OLA A4004                    
SITE     1 AC3  3 TYR A 645  VAL A 709  LYS A1048                               
SITE     1 AC4  7 PRO A 569  VAL A 584  CYS A 588  PHE A 633                    
SITE     2 AC4  7 ILE A 636  ALA A 637  OLA A4002                               
SITE     1 AC5 15 GLY A 624  ILE A 651  SER A 654  PRO A 655                    
SITE     2 AC5 15 SER A 658  TYR A 659  VAL A 740  PRO A 743                    
SITE     3 AC5 15 LEU A 744  ASN A 747  PHE A 788  SER A 805                    
SITE     4 AC5 15 VAL A 806  SER A 809  ALA A 813                               
SITE     1 AC6  8 TYR A 730  ILE A 732  ASN A 796  TYR A 797                    
SITE     2 AC6  8 LYS A 798  ILE A 799  TYR A1139  LYS A1147                    
CRYST1  143.242   43.555   82.049  90.00  99.37  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006981  0.000000  0.001152        0.00000                         
SCALE2      0.000000  0.022959  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012353        0.00000                         
ATOM      1  N   SER A 568     -38.557 -14.079  61.667  1.00 50.34           N  
ANISOU    1  N   SER A 568     6883   5814   6428   -523    814    699       N  
ATOM      2  CA  SER A 568     -39.595 -14.051  60.643  1.00 51.03           C  
ANISOU    2  CA  SER A 568     6907   5880   6603   -568    796    637       C  
ATOM      3  C   SER A 568     -39.805 -12.635  60.114  1.00 48.97           C  
ANISOU    3  C   SER A 568     6593   5684   6328   -575    736    595       C  
ATOM      4  O   SER A 568     -40.069 -11.712  60.886  1.00 48.27           O  
ANISOU    4  O   SER A 568     6497   5633   6211   -573    750    606       O  
ATOM      5  CB  SER A 568     -40.907 -14.615  61.195  1.00 52.33           C  
ANISOU    5  CB  SER A 568     7056   5984   6844   -613    873    640       C  
ATOM      6  OG  SER A 568     -41.916 -14.637  60.200  1.00 52.76           O  
ANISOU    6  OG  SER A 568     7050   6012   6985   -656    857    581       O  
ATOM      7  N   PRO A 569     -39.674 -12.460  58.790  1.00 47.38           N  
ANISOU    7  N   PRO A 569     6354   5498   6149   -583    667    546       N  
ATOM      8  CA  PRO A 569     -39.853 -11.169  58.115  1.00 45.65           C  
ANISOU    8  CA  PRO A 569     6082   5339   5924   -594    598    503       C  
ATOM      9  C   PRO A 569     -41.250 -10.579  58.309  1.00 44.36           C  
ANISOU    9  C   PRO A 569     5865   5162   5826   -639    624    473       C  
ATOM     10  O   PRO A 569     -41.415  -9.366  58.188  1.00 43.55           O  
ANISOU   10  O   PRO A 569     5725   5112   5708   -644    579    451       O  
ATOM     11  CB  PRO A 569     -39.624 -11.515  56.639  1.00 44.87           C  
ANISOU   11  CB  PRO A 569     5956   5236   5855   -605    536    458       C  
ATOM     12  CG  PRO A 569     -38.755 -12.723  56.669  1.00 45.51           C  
ANISOU   12  CG  PRO A 569     6090   5285   5915   -575    554    487       C  
ATOM     13  CD  PRO A 569     -39.214 -13.507  57.862  1.00 46.78           C  
ANISOU   13  CD  PRO A 569     6289   5388   6097   -579    644    531       C  
ATOM     14  N   VAL A 570     -42.237 -11.421  58.602  1.00 44.81           N  
ANISOU   14  N   VAL A 570     5918   5153   5957   -672    693    471       N  
ATOM     15  CA  VAL A 570     -43.593 -10.939  58.856  1.00 45.49           C  
ANISOU   15  CA  VAL A 570     5954   5223   6106   -716    725    443       C  
ATOM     16  C   VAL A 570     -43.673 -10.236  60.210  1.00 45.08           C  
ANISOU   16  C   VAL A 570     5918   5205   6006   -701    767    477       C  
ATOM     17  O   VAL A 570     -44.338  -9.208  60.347  1.00 44.37           O  
ANISOU   17  O   VAL A 570     5784   5145   5931   -719    754    449       O  
ATOM     18  CB  VAL A 570     -44.632 -12.081  58.792  1.00 45.84           C  
ANISOU   18  CB  VAL A 570     5988   5185   6243   -756    788    434       C  
ATOM     19  CG1 VAL A 570     -46.017 -11.572  59.169  1.00 45.98           C  
ANISOU   19  CG1 VAL A 570     5957   5190   6323   -799    826    407       C  
ATOM     20  CG2 VAL A 570     -44.656 -12.697  57.404  1.00 44.69           C  
ANISOU   20  CG2 VAL A 570     5820   5008   6152   -773    743    392       C  
ATOM     21  N   GLN A 571     -42.982 -10.793  61.202  1.00 45.42           N  
ANISOU   21  N   GLN A 571     6024   5243   5992   -669    814    537       N  
ATOM     22  CA  GLN A 571     -42.942 -10.216  62.543  1.00 47.99           C  
ANISOU   22  CA  GLN A 571     6372   5601   6262   -651    857    575       C  
ATOM     23  C   GLN A 571     -42.476  -8.762  62.528  1.00 47.55           C  
ANISOU   23  C   GLN A 571     6296   5623   6148   -627    792    562       C  
ATOM     24  O   GLN A 571     -43.165  -7.881  63.044  1.00 48.11           O  
ANISOU   24  O   GLN A 571     6332   5719   6226   -640    803    545       O  
ATOM     25  CB  GLN A 571     -42.038 -11.043  63.462  1.00 50.43           C  
ANISOU   25  CB  GLN A 571     6756   5896   6509   -616    903    644       C  
ATOM     26  CG  GLN A 571     -42.573 -12.428  63.795  1.00 52.99           C  
ANISOU   26  CG  GLN A 571     7103   6143   6888   -642    977    667       C  
ATOM     27  CD  GLN A 571     -41.605 -13.236  64.641  1.00 55.86           C  
ANISOU   27  CD  GLN A 571     7541   6492   7190   -607   1012    736       C  
ATOM     28  OE1 GLN A 571     -40.402 -12.972  64.650  1.00 57.37           O  
ANISOU   28  OE1 GLN A 571     7770   6722   7306   -562    971    758       O  
ATOM     29  NE2 GLN A 571     -42.127 -14.223  65.359  1.00 56.38           N  
ANISOU   29  NE2 GLN A 571     7630   6502   7289   -630   1088    770       N  
ATOM     30  N   TYR A 572     -41.312  -8.516  61.932  1.00 46.33           N  
ANISOU   30  N   TYR A 572     6161   5507   5936   -591    722    568       N  
ATOM     31  CA  TYR A 572     -40.773  -7.161  61.827  1.00 45.47           C  
ANISOU   31  CA  TYR A 572     6034   5472   5769   -567    651    558       C  
ATOM     32  C   TYR A 572     -41.717  -6.242  61.060  1.00 44.31           C  
ANISOU   32  C   TYR A 572     5811   5340   5684   -605    603    495       C  
ATOM     33  O   TYR A 572     -41.841  -5.060  61.382  1.00 43.18           O  
ANISOU   33  O   TYR A 572     5641   5247   5519   -600    572    484       O  
ATOM     34  CB  TYR A 572     -39.392  -7.170  61.168  1.00 45.05           C  
ANISOU   34  CB  TYR A 572     6012   5454   5652   -527    583    573       C  
ATOM     35  CG  TYR A 572     -38.260  -7.455  62.129  1.00 46.50           C  
ANISOU   35  CG  TYR A 572     6268   5652   5747   -476    609    637       C  
ATOM     36  CD1 TYR A 572     -38.004  -8.747  62.568  1.00 47.52           C  
ANISOU   36  CD1 TYR A 572     6450   5728   5879   -468    670    675       C  
ATOM     37  CD2 TYR A 572     -37.445  -6.430  62.597  1.00 46.52           C  
ANISOU   37  CD2 TYR A 572     6286   5720   5668   -436    569    661       C  
ATOM     38  CE1 TYR A 572     -36.969  -9.012  63.447  1.00 47.95           C  
ANISOU   38  CE1 TYR A 572     6571   5793   5855   -423    692    735       C  
ATOM     39  CE2 TYR A 572     -36.407  -6.686  63.476  1.00 46.79           C  
ANISOU   39  CE2 TYR A 572     6388   5767   5624   -389    591    720       C  
ATOM     40  CZ  TYR A 572     -36.173  -7.978  63.897  1.00 47.17           C  
ANISOU   40  CZ  TYR A 572     6487   5759   5675   -384    653    757       C  
ATOM     41  OH  TYR A 572     -35.142  -8.236  64.771  1.00 46.42           O  
ANISOU   41  OH  TYR A 572     6460   5675   5504   -339    674    816       O  
ATOM     42  N   LEU A 573     -42.381  -6.794  60.048  1.00 44.23           N  
ANISOU   42  N   LEU A 573     5766   5287   5753   -645    594    454       N  
ATOM     43  CA  LEU A 573     -43.380  -6.052  59.289  1.00 46.07           C  
ANISOU   43  CA  LEU A 573     5926   5524   6056   -688    553    393       C  
ATOM     44  C   LEU A 573     -44.539  -5.650  60.192  1.00 48.69           C  
ANISOU   44  C   LEU A 573     6229   5843   6429   -713    610    381       C  
ATOM     45  O   LEU A 573     -45.105  -4.566  60.048  1.00 49.51           O  
ANISOU   45  O   LEU A 573     6280   5976   6555   -730    571    343       O  
ATOM     46  CB  LEU A 573     -43.895  -6.889  58.115  1.00 46.10           C  
ANISOU   46  CB  LEU A 573     5903   5474   6138   -725    544    354       C  
ATOM     47  CG  LEU A 573     -45.104  -6.332  57.358  1.00 45.47           C  
ANISOU   47  CG  LEU A 573     5749   5381   6145   -777    514    291       C  
ATOM     48  CD1 LEU A 573     -44.777  -4.983  56.738  1.00 44.19           C  
ANISOU   48  CD1 LEU A 573     5548   5285   5956   -774    416    264       C  
ATOM     49  CD2 LEU A 573     -45.589  -7.313  56.298  1.00 47.06           C  
ANISOU   49  CD2 LEU A 573     5933   5524   6424   -812    516    260       C  
ATOM     50  N   ARG A 574     -44.882  -6.527  61.129  1.00 49.30           N  
ANISOU   50  N   ARG A 574     6339   5877   6515   -716    703    415       N  
ATOM     51  CA  ARG A 574     -45.981  -6.266  62.051  1.00 50.57           C  
ANISOU   51  CA  ARG A 574     6475   6028   6713   -741    767    406       C  
ATOM     52  C   ARG A 574     -45.530  -5.477  63.278  1.00 49.11           C  
ANISOU   52  C   ARG A 574     6314   5897   6448   -705    783    440       C  
ATOM     53  O   ARG A 574     -46.356  -4.907  63.991  1.00 49.83           O  
ANISOU   53  O   ARG A 574     6375   6000   6560   -721    816    424       O  
ATOM     54  CB  ARG A 574     -46.669  -7.571  62.462  1.00 53.04           C  
ANISOU   54  CB  ARG A 574     6807   6269   7077   -768    858    425       C  
ATOM     55  CG  ARG A 574     -47.281  -8.323  61.291  1.00 55.78           C  
ANISOU   55  CG  ARG A 574     7123   6558   7512   -807    846    387       C  
ATOM     56  CD  ARG A 574     -48.215  -9.435  61.738  1.00 59.25           C  
ANISOU   56  CD  ARG A 574     7568   6928   8017   -841    936    398       C  
ATOM     57  NE  ARG A 574     -48.816 -10.109  60.589  1.00 62.64           N  
ANISOU   57  NE  ARG A 574     7966   7301   8533   -877    920    359       N  
ATOM     58  CZ  ARG A 574     -49.858 -10.932  60.660  1.00 65.40           C  
ANISOU   58  CZ  ARG A 574     8301   7587   8963   -918    981    351       C  
ATOM     59  NH1 ARG A 574     -50.430 -11.186  61.829  1.00 66.47           N  
ANISOU   59  NH1 ARG A 574     8447   7709   9100   -929   1063    380       N  
ATOM     60  NH2 ARG A 574     -50.332 -11.496  59.558  1.00 66.27           N  
ANISOU   60  NH2 ARG A 574     8382   7648   9148   -947    959    314       N  
ATOM     61  N   TRP A 575     -44.224  -5.441  63.523  1.00 46.95           N  
ANISOU   61  N   TRP A 575     6094   5658   6086   -656    758    485       N  
ATOM     62  CA  TRP A 575     -43.692  -4.628  64.612  1.00 45.03           C  
ANISOU   62  CA  TRP A 575     5875   5471   5764   -617    762    517       C  
ATOM     63  C   TRP A 575     -43.484  -3.183  64.163  1.00 42.30           C  
ANISOU   63  C   TRP A 575     5486   5188   5399   -605    670    483       C  
ATOM     64  O   TRP A 575     -43.215  -2.305  64.982  1.00 42.68           O  
ANISOU   64  O   TRP A 575     5539   5284   5393   -578    664    497       O  
ATOM     65  CB  TRP A 575     -42.381  -5.200  65.170  1.00 46.02           C  
ANISOU   65  CB  TRP A 575     6079   5605   5802   -569    777    584       C  
ATOM     66  CG  TRP A 575     -42.463  -6.595  65.761  1.00 49.06           C  
ANISOU   66  CG  TRP A 575     6513   5931   6197   -576    865    627       C  
ATOM     67  CD1 TRP A 575     -41.547  -7.596  65.606  1.00 50.06           C  
ANISOU   67  CD1 TRP A 575     6697   6031   6294   -554    870    667       C  
ATOM     68  CD2 TRP A 575     -43.501  -7.129  66.599  1.00 51.29           C  
ANISOU   68  CD2 TRP A 575     6789   6175   6522   -609    956    634       C  
ATOM     69  NE1 TRP A 575     -41.948  -8.718  66.289  1.00 51.73           N  
ANISOU   69  NE1 TRP A 575     6939   6188   6529   -571    955    700       N  
ATOM     70  CE2 TRP A 575     -43.144  -8.461  66.907  1.00 52.46           C  
ANISOU   70  CE2 TRP A 575     6994   6273   6665   -606   1010    683       C  
ATOM     71  CE3 TRP A 575     -44.696  -6.622  67.119  1.00 53.89           C  
ANISOU   71  CE3 TRP A 575     7071   6509   6895   -642    996    604       C  
ATOM     72  CZ2 TRP A 575     -43.937  -9.282  67.706  1.00 56.08           C  
ANISOU   72  CZ2 TRP A 575     7463   6687   7158   -637   1100    705       C  
ATOM     73  CZ3 TRP A 575     -45.482  -7.439  67.912  1.00 56.93           C  
ANISOU   73  CZ3 TRP A 575     7465   6852   7313   -672   1088    625       C  
ATOM     74  CH2 TRP A 575     -45.099  -8.754  68.198  1.00 57.44           C  
ANISOU   74  CH2 TRP A 575     7587   6869   7370   -670   1139    677       C  
ATOM     75  N   GLY A 576     -43.601  -2.942  62.859  1.00 39.12           N  
ANISOU   75  N   GLY A 576     5041   4782   5039   -627    598    439       N  
ATOM     76  CA  GLY A 576     -43.497  -1.597  62.322  1.00 37.22           C  
ANISOU   76  CA  GLY A 576     4754   4597   4791   -624    504    404       C  
ATOM     77  C   GLY A 576     -42.346  -1.377  61.356  1.00 38.24           C  
ANISOU   77  C   GLY A 576     4896   4761   4872   -600    415    411       C  
ATOM     78  O   GLY A 576     -42.096  -0.250  60.927  1.00 37.77           O  
ANISOU   78  O   GLY A 576     4803   4752   4795   -594    331    391       O  
ATOM     79  N   ASP A 577     -41.645  -2.451  61.007  1.00 38.85           N  
ANISOU   79  N   ASP A 577     5020   4812   4928   -587    431    440       N  
ATOM     80  CA  ASP A 577     -40.502  -2.356  60.102  1.00 36.58           C  
ANISOU   80  CA  ASP A 577     4748   4559   4592   -563    352    448       C  
ATOM     81  C   ASP A 577     -40.696  -3.217  58.856  1.00 34.76           C  
ANISOU   81  C   ASP A 577     4501   4289   4418   -594    337    418       C  
ATOM     82  O   ASP A 577     -40.530  -4.434  58.906  1.00 36.32           O  
ANISOU   82  O   ASP A 577     4738   4440   4624   -591    390    438       O  
ATOM     83  CB  ASP A 577     -39.218  -2.763  60.825  1.00 36.94           C  
ANISOU   83  CB  ASP A 577     4868   4623   4545   -508    373    511       C  
ATOM     84  CG  ASP A 577     -37.998  -2.701  59.928  1.00 38.80           C  
ANISOU   84  CG  ASP A 577     5121   4897   4726   -481    295    520       C  
ATOM     85  OD1 ASP A 577     -37.978  -1.868  58.996  1.00 37.91           O  
ANISOU   85  OD1 ASP A 577     4961   4822   4621   -496    210    485       O  
ATOM     86  OD2 ASP A 577     -37.054  -3.484  60.159  1.00 42.29           O  
ANISOU   86  OD2 ASP A 577     5622   5331   5117   -448    318    561       O  
ATOM     87  N   PRO A 578     -41.030  -2.579  57.725  1.00 31.99           N  
ANISOU   87  N   PRO A 578     4093   3956   4107   -625    259    369       N  
ATOM     88  CA  PRO A 578     -41.310  -3.298  56.480  1.00 31.26           C  
ANISOU   88  CA  PRO A 578     3977   3829   4073   -659    239    333       C  
ATOM     89  C   PRO A 578     -40.067  -3.514  55.619  1.00 30.26           C  
ANISOU   89  C   PRO A 578     3873   3735   3888   -634    177    345       C  
ATOM     90  O   PRO A 578     -40.193  -3.935  54.470  1.00 32.29           O  
ANISOU   90  O   PRO A 578     4106   3979   4186   -661    144    311       O  
ATOM     91  CB  PRO A 578     -42.286  -2.363  55.762  1.00 29.53           C  
ANISOU   91  CB  PRO A 578     3682   3618   3921   -706    183    276       C  
ATOM     92  CG  PRO A 578     -41.988  -0.977  56.317  1.00 29.61           C  
ANISOU   92  CG  PRO A 578     3679   3692   3880   -684    134    285       C  
ATOM     93  CD  PRO A 578     -41.110  -1.121  57.539  1.00 30.84           C  
ANISOU   93  CD  PRO A 578     3900   3867   3951   -629    180    345       C  
ATOM     94  N   ALA A 579     -38.888  -3.234  56.164  1.00 26.93           N  
ANISOU   94  N   ALA A 579     3498   3361   3374   -584    161    391       N  
ATOM     95  CA  ALA A 579     -37.649  -3.379  55.400  1.00 24.17           C  
ANISOU   95  CA  ALA A 579     3169   3050   2963   -557    101    402       C  
ATOM     96  C   ALA A 579     -37.285  -4.827  55.030  1.00 21.73           C  
ANISOU   96  C   ALA A 579     2897   2695   2664   -551    140    409       C  
ATOM     97  O   ALA A 579     -37.045  -5.111  53.856  1.00 21.33           O  
ANISOU   97  O   ALA A 579     2826   2652   2627   -566     91    380       O  
ATOM     98  CB  ALA A 579     -36.479  -2.667  56.098  1.00 24.74           C  
ANISOU   98  CB  ALA A 579     3282   3186   2935   -504     72    450       C  
ATOM     99  N   PRO A 580     -37.243  -5.748  56.016  1.00 20.56           N  
ANISOU   99  N   PRO A 580     2802   2500   2512   -531    226    447       N  
ATOM    100  CA  PRO A 580     -36.864  -7.113  55.626  1.00 21.96           C  
ANISOU  100  CA  PRO A 580     3010   2631   2701   -525    255    451       C  
ATOM    101  C   PRO A 580     -37.883  -7.810  54.726  1.00 25.95           C  
ANISOU  101  C   PRO A 580     3474   3081   3304   -574    267    401       C  
ATOM    102  O   PRO A 580     -37.478  -8.559  53.839  1.00 27.35           O  
ANISOU  102  O   PRO A 580     3655   3247   3492   -575    245    384       O  
ATOM    103  CB  PRO A 580     -36.742  -7.847  56.965  1.00 22.86           C  
ANISOU  103  CB  PRO A 580     3185   2704   2796   -498    343    504       C  
ATOM    104  CG  PRO A 580     -37.540  -7.055  57.920  1.00 24.56           C  
ANISOU  104  CG  PRO A 580     3384   2925   3021   -510    377    511       C  
ATOM    105  CD  PRO A 580     -37.438  -5.631  57.473  1.00 22.52           C  
ANISOU  105  CD  PRO A 580     3083   2736   2738   -512    295    487       C  
ATOM    106  N   ILE A 581     -39.174  -7.568  54.942  1.00 25.98           N  
ANISOU  106  N   ILE A 581     3440   3052   3380   -615    299    377       N  
ATOM    107  CA  ILE A 581     -40.204  -8.193  54.114  1.00 24.53           C  
ANISOU  107  CA  ILE A 581     3215   2812   3293   -663    311    330       C  
ATOM    108  C   ILE A 581     -40.150  -7.690  52.665  1.00 25.04           C  
ANISOU  108  C   ILE A 581     3228   2912   3373   -688    221    280       C  
ATOM    109  O   ILE A 581     -40.393  -8.450  51.727  1.00 26.18           O  
ANISOU  109  O   ILE A 581     3355   3023   3568   -711    213    248       O  
ATOM    110  CB  ILE A 581     -41.623  -8.003  54.710  1.00 26.40           C  
ANISOU  110  CB  ILE A 581     3421   3008   3604   -702    367    315       C  
ATOM    111  CG1 ILE A 581     -42.654  -8.811  53.919  1.00 27.11           C  
ANISOU  111  CG1 ILE A 581     3475   3031   3795   -749    387    272       C  
ATOM    112  CG2 ILE A 581     -42.013  -6.534  54.757  1.00 26.81           C  
ANISOU  112  CG2 ILE A 581     3426   3110   3650   -715    318    294       C  
ATOM    113  CD1 ILE A 581     -42.461 -10.303  54.024  1.00 27.55           C  
ANISOU  113  CD1 ILE A 581     3574   3025   3869   -739    444    293       C  
ATOM    114  N   ALA A 582     -39.811  -6.415  52.491  1.00 23.39           N  
ANISOU  114  N   ALA A 582     2994   2773   3119   -683    151    276       N  
ATOM    115  CA  ALA A 582     -39.734  -5.811  51.165  1.00 23.02           C  
ANISOU  115  CA  ALA A 582     2898   2768   3080   -709     59    233       C  
ATOM    116  C   ALA A 582     -38.581  -6.392  50.351  1.00 27.40           C  
ANISOU  116  C   ALA A 582     3476   3350   3585   -685     19    236       C  
ATOM    117  O   ALA A 582     -38.734  -6.688  49.166  1.00 28.01           O  
ANISOU  117  O   ALA A 582     3520   3425   3698   -713    -21    194       O  
ATOM    118  CB  ALA A 582     -39.591  -4.300  51.280  1.00 19.99           C  
ANISOU  118  CB  ALA A 582     2486   2453   2657   -707     -8    234       C  
ATOM    119  N   ALA A 583     -37.429  -6.549  51.000  1.00 27.71           N  
ANISOU  119  N   ALA A 583     3571   3418   3541   -632     29    283       N  
ATOM    120  CA  ALA A 583     -36.237  -7.086  50.351  1.00 25.51           C  
ANISOU  120  CA  ALA A 583     3318   3169   3207   -604     -6    289       C  
ATOM    121  C   ALA A 583     -36.447  -8.527  49.903  1.00 28.22           C  
ANISOU  121  C   ALA A 583     3672   3445   3604   -612     37    269       C  
ATOM    122  O   ALA A 583     -35.905  -8.953  48.885  1.00 30.65           O  
ANISOU  122  O   ALA A 583     3971   3771   3902   -612     -5    244       O  
ATOM    123  CB  ALA A 583     -35.034  -6.990  51.283  1.00 22.78           C  
ANISOU  123  CB  ALA A 583     3033   2857   2767   -545      4    346       C  
ATOM    124  N   VAL A 584     -37.233  -9.275  50.669  1.00 30.58           N  
ANISOU  124  N   VAL A 584     3990   3670   3960   -620    121    281       N  
ATOM    125  CA  VAL A 584     -37.547 -10.653  50.316  1.00 32.48           C  
ANISOU  125  CA  VAL A 584     4239   3839   4261   -631    164    264       C  
ATOM    126  C   VAL A 584     -38.404 -10.703  49.058  1.00 34.87           C  
ANISOU  126  C   VAL A 584     4481   4127   4642   -682    129    202       C  
ATOM    127  O   VAL A 584     -38.088 -11.420  48.107  1.00 35.45           O  
ANISOU  127  O   VAL A 584     4548   4193   4729   -685    104    173       O  
ATOM    128  CB  VAL A 584     -38.280 -11.370  51.459  1.00 30.55           C  
ANISOU  128  CB  VAL A 584     4025   3520   4063   -634    260    293       C  
ATOM    129  CG1 VAL A 584     -38.777 -12.729  50.999  1.00 29.83           C  
ANISOU  129  CG1 VAL A 584     3933   3352   4048   -652    297    271       C  
ATOM    130  CG2 VAL A 584     -37.362 -11.511  52.657  1.00 31.34           C  
ANISOU  130  CG2 VAL A 584     4190   3631   4086   -583    296    355       C  
ATOM    131  N   VAL A 585     -39.487  -9.933  49.061  1.00 34.82           N  
ANISOU  131  N   VAL A 585     4430   4115   4687   -723    125    180       N  
ATOM    132  CA  VAL A 585     -40.375  -9.845  47.910  1.00 33.64           C  
ANISOU  132  CA  VAL A 585     4219   3950   4612   -775     89    122       C  
ATOM    133  C   VAL A 585     -39.608  -9.366  46.680  1.00 31.35           C  
ANISOU  133  C   VAL A 585     3903   3731   4279   -777     -5     94       C  
ATOM    134  O   VAL A 585     -39.759  -9.920  45.593  1.00 31.65           O  
ANISOU  134  O   VAL A 585     3915   3755   4357   -800    -30     52       O  
ATOM    135  CB  VAL A 585     -41.568  -8.911  48.195  1.00 33.06           C  
ANISOU  135  CB  VAL A 585     4102   3867   4592   -814     93    105       C  
ATOM    136  CG1 VAL A 585     -42.403  -8.705  46.943  1.00 33.99           C  
ANISOU  136  CG1 VAL A 585     4156   3976   4783   -869     44     45       C  
ATOM    137  CG2 VAL A 585     -42.420  -9.479  49.323  1.00 33.09           C  
ANISOU  137  CG2 VAL A 585     4127   3801   4646   -818    189    127       C  
ATOM    138  N   PHE A 586     -38.775  -8.346  46.867  1.00 29.79           N  
ANISOU  138  N   PHE A 586     3711   3610   3998   -753    -57    117       N  
ATOM    139  CA  PHE A 586     -37.914  -7.837  45.803  1.00 29.99           C  
ANISOU  139  CA  PHE A 586     3715   3712   3969   -752   -147    100       C  
ATOM    140  C   PHE A 586     -37.048  -8.974  45.260  1.00 30.18           C  
ANISOU  140  C   PHE A 586     3767   3732   3968   -726   -144     94       C  
ATOM    141  O   PHE A 586     -36.949  -9.169  44.048  1.00 32.12           O  
ANISOU  141  O   PHE A 586     3979   3998   4226   -748   -194     52       O  
ATOM    142  CB  PHE A 586     -37.032  -6.707  46.346  1.00 30.17           C  
ANISOU  142  CB  PHE A 586     3753   3812   3898   -720   -191    139       C  
ATOM    143  CG  PHE A 586     -36.416  -5.829  45.283  1.00 32.82           C  
ANISOU  143  CG  PHE A 586     4052   4233   4187   -733   -293    120       C  
ATOM    144  CD1 PHE A 586     -36.411  -6.203  43.947  1.00 34.76           C  
ANISOU  144  CD1 PHE A 586     4263   4490   4454   -763   -339     75       C  
ATOM    145  CD2 PHE A 586     -35.835  -4.621  45.632  1.00 32.29           C  
ANISOU  145  CD2 PHE A 586     3984   4234   4050   -716   -346    149       C  
ATOM    146  CE1 PHE A 586     -35.840  -5.393  42.985  1.00 34.25           C  
ANISOU  146  CE1 PHE A 586     4164   4508   4342   -778   -433     61       C  
ATOM    147  CE2 PHE A 586     -35.263  -3.806  44.674  1.00 31.62           C  
ANISOU  147  CE2 PHE A 586     3864   4229   3919   -731   -443    136       C  
ATOM    148  CZ  PHE A 586     -35.266  -4.192  43.349  1.00 33.35           C  
ANISOU  148  CZ  PHE A 586     4049   4462   4160   -763   -486     93       C  
ATOM    149  N   ALA A 587     -36.435  -9.726  46.166  1.00 27.67           N  
ANISOU  149  N   ALA A 587     3508   3387   3616   -680    -86    135       N  
ATOM    150  CA  ALA A 587     -35.567 -10.832  45.780  1.00 27.01           C  
ANISOU  150  CA  ALA A 587     3455   3297   3511   -650    -81    131       C  
ATOM    151  C   ALA A 587     -36.353 -11.969  45.143  1.00 25.51           C  
ANISOU  151  C   ALA A 587     3246   3033   3412   -679    -50     89       C  
ATOM    152  O   ALA A 587     -35.863 -12.637  44.235  1.00 27.19           O  
ANISOU  152  O   ALA A 587     3453   3256   3623   -675    -78     58       O  
ATOM    153  CB  ALA A 587     -34.784 -11.337  46.980  1.00 27.50           C  
ANISOU  153  CB  ALA A 587     3586   3342   3521   -596    -27    187       C  
ATOM    154  N   CYS A 588     -37.571 -12.191  45.622  1.00 24.26           N  
ANISOU  154  N   CYS A 588     3078   2804   3334   -708      7     87       N  
ATOM    155  CA  CYS A 588     -38.403 -13.264  45.092  1.00 23.94           C  
ANISOU  155  CA  CYS A 588     3021   2689   3387   -736     39     50       C  
ATOM    156  C   CYS A 588     -38.894 -12.938  43.691  1.00 22.55           C  
ANISOU  156  C   CYS A 588     2782   2534   3252   -782    -24    -10       C  
ATOM    157  O   CYS A 588     -38.853 -13.784  42.799  1.00 21.18           O  
ANISOU  157  O   CYS A 588     2596   2341   3112   -790    -36    -48       O  
ATOM    158  CB  CYS A 588     -39.587 -13.535  46.017  1.00 25.23           C  
ANISOU  158  CB  CYS A 588     3190   2773   3623   -757    117     67       C  
ATOM    159  SG  CYS A 588     -39.127 -14.341  47.560  1.00 47.90           S  
ANISOU  159  SG  CYS A 588     6137   5599   6466   -709    203    134       S  
ATOM    160  N   LEU A 589     -39.358 -11.707  43.504  1.00 23.50           N  
ANISOU  160  N   LEU A 589     2863   2696   3371   -814    -67    -20       N  
ATOM    161  CA  LEU A 589     -39.832 -11.266  42.198  1.00 25.47           C  
ANISOU  161  CA  LEU A 589     3051   2970   3656   -862   -134    -74       C  
ATOM    162  C   LEU A 589     -38.688 -11.267  41.191  1.00 25.31           C  
ANISOU  162  C   LEU A 589     3024   3024   3568   -847   -204    -92       C  
ATOM    163  O   LEU A 589     -38.895 -11.493  39.999  1.00 25.01           O  
ANISOU  163  O   LEU A 589     2947   2994   3562   -878   -246   -141       O  
ATOM    164  CB  LEU A 589     -40.458  -9.874  42.292  1.00 25.36           C  
ANISOU  164  CB  LEU A 589     2998   2989   3649   -895   -171    -76       C  
ATOM    165  CG  LEU A 589     -41.738  -9.756  43.122  1.00 27.20           C  
ANISOU  165  CG  LEU A 589     3223   3155   3958   -919   -109    -70       C  
ATOM    166  CD1 LEU A 589     -42.219  -8.315  43.152  1.00 27.50           C  
ANISOU  166  CD1 LEU A 589     3220   3234   3996   -949   -158    -76       C  
ATOM    167  CD2 LEU A 589     -42.825 -10.676  42.589  1.00 28.69           C  
ANISOU  167  CD2 LEU A 589     3387   3262   4252   -957    -74   -111       C  
ATOM    168  N   GLY A 590     -37.479 -11.020  41.683  1.00 24.68           N  
ANISOU  168  N   GLY A 590     2984   3001   3394   -799   -217    -53       N  
ATOM    169  CA  GLY A 590     -36.300 -11.016  40.839  1.00 23.84           C  
ANISOU  169  CA  GLY A 590     2874   2970   3214   -781   -281    -66       C  
ATOM    170  C   GLY A 590     -35.920 -12.413  40.394  1.00 25.18           C  
ANISOU  170  C   GLY A 590     3062   3103   3402   -761   -256    -90       C  
ATOM    171  O   GLY A 590     -35.565 -12.627  39.236  1.00 26.96           O  
ANISOU  171  O   GLY A 590     3258   3367   3618   -773   -307   -132       O  
ATOM    172  N   LEU A 591     -35.992 -13.366  41.318  1.00 24.52           N  
ANISOU  172  N   LEU A 591     3026   2947   3345   -731   -180    -63       N  
ATOM    173  CA  LEU A 591     -35.686 -14.758  41.006  1.00 27.15           C  
ANISOU  173  CA  LEU A 591     3378   3235   3704   -710   -153    -84       C  
ATOM    174  C   LEU A 591     -36.654 -15.316  39.969  1.00 30.12           C  
ANISOU  174  C   LEU A 591     3707   3566   4173   -756   -160   -143       C  
ATOM    175  O   LEU A 591     -36.241 -15.992  39.026  1.00 32.00           O  
ANISOU  175  O   LEU A 591     3930   3815   4412   -752   -188   -184       O  
ATOM    176  CB  LEU A 591     -35.726 -15.617  42.271  1.00 29.52           C  
ANISOU  176  CB  LEU A 591     3735   3458   4024   -676    -70    -39       C  
ATOM    177  CG  LEU A 591     -34.588 -15.429  43.275  1.00 30.43           C  
ANISOU  177  CG  LEU A 591     3907   3607   4049   -622    -58     18       C  
ATOM    178  CD1 LEU A 591     -34.809 -16.314  44.493  1.00 29.81           C  
ANISOU  178  CD1 LEU A 591     3880   3444   4001   -599     26     61       C  
ATOM    179  CD2 LEU A 591     -33.234 -15.717  42.628  1.00 29.30           C  
ANISOU  179  CD2 LEU A 591     3774   3525   3834   -586   -107      4       C  
ATOM    180  N   LEU A 592     -37.941 -15.032  40.150  1.00 30.30           N  
ANISOU  180  N   LEU A 592     3704   3538   4271   -798   -133   -149       N  
ATOM    181  CA  LEU A 592     -38.962 -15.466  39.203  1.00 30.43           C  
ANISOU  181  CA  LEU A 592     3675   3508   4380   -844   -139   -203       C  
ATOM    182  C   LEU A 592     -38.706 -14.868  37.823  1.00 29.50           C  
ANISOU  182  C   LEU A 592     3505   3467   4236   -874   -226   -250       C  
ATOM    183  O   LEU A 592     -38.822 -15.554  36.808  1.00 28.68           O  
ANISOU  183  O   LEU A 592     3375   3351   4169   -889   -246   -300       O  
ATOM    184  CB  LEU A 592     -40.359 -15.073  39.694  1.00 31.00           C  
ANISOU  184  CB  LEU A 592     3727   3521   4531   -885   -100   -198       C  
ATOM    185  CG  LEU A 592     -40.859 -15.717  40.991  1.00 33.87           C  
ANISOU  185  CG  LEU A 592     4133   3802   4935   -868    -10   -156       C  
ATOM    186  CD1 LEU A 592     -42.236 -15.182  41.360  1.00 33.56           C  
ANISOU  186  CD1 LEU A 592     4065   3717   4968   -913     19   -158       C  
ATOM    187  CD2 LEU A 592     -40.884 -17.235  40.875  1.00 34.50           C  
ANISOU  187  CD2 LEU A 592     4234   3808   5067   -853     31   -169       C  
ATOM    188  N   ALA A 593     -38.351 -13.586  37.798  1.00 28.88           N  
ANISOU  188  N   ALA A 593     3412   3468   4093   -882   -279   -235       N  
ATOM    189  CA  ALA A 593     -38.065 -12.888  36.551  1.00 28.56           C  
ANISOU  189  CA  ALA A 593     3323   3510   4020   -912   -367   -272       C  
ATOM    190  C   ALA A 593     -36.862 -13.505  35.845  1.00 29.50           C  
ANISOU  190  C   ALA A 593     3450   3682   4076   -881   -400   -292       C  
ATOM    191  O   ALA A 593     -36.899 -13.757  34.642  1.00 30.50           O  
ANISOU  191  O   ALA A 593     3538   3831   4218   -908   -443   -343       O  
ATOM    192  CB  ALA A 593     -37.828 -11.409  36.815  1.00 26.94           C  
ANISOU  192  CB  ALA A 593     3106   3377   3753   -922   -416   -242       C  
ATOM    193  N   THR A 594     -35.800 -13.749  36.607  1.00 29.23           N  
ANISOU  193  N   THR A 594     3467   3667   3972   -825   -379   -252       N  
ATOM    194  CA  THR A 594     -34.589 -14.368  36.079  1.00 27.69           C  
ANISOU  194  CA  THR A 594     3285   3521   3716   -789   -404   -268       C  
ATOM    195  C   THR A 594     -34.867 -15.797  35.620  1.00 27.37           C  
ANISOU  195  C   THR A 594     3244   3411   3745   -784   -371   -311       C  
ATOM    196  O   THR A 594     -34.310 -16.262  34.623  1.00 23.55           O  
ANISOU  196  O   THR A 594     2740   2967   3242   -781   -410   -355       O  
ATOM    197  CB  THR A 594     -33.465 -14.387  37.136  1.00 26.71           C  
ANISOU  197  CB  THR A 594     3220   3418   3511   -727   -381   -213       C  
ATOM    198  OG1 THR A 594     -33.214 -13.053  37.596  1.00 26.19           O  
ANISOU  198  OG1 THR A 594     3154   3414   3381   -729   -413   -172       O  
ATOM    199  CG2 THR A 594     -32.185 -14.966  36.553  1.00 25.96           C  
ANISOU  199  CG2 THR A 594     3135   3379   3350   -690   -412   -233       C  
ATOM    200  N   LEU A 595     -35.734 -16.488  36.355  1.00 29.44           N  
ANISOU  200  N   LEU A 595     3528   3571   4087   -784   -300   -298       N  
ATOM    201  CA  LEU A 595     -36.114 -17.852  36.010  1.00 32.70           C  
ANISOU  201  CA  LEU A 595     3941   3907   4576   -781   -266   -334       C  
ATOM    202  C   LEU A 595     -36.910 -17.866  34.713  1.00 35.44           C  
ANISOU  202  C   LEU A 595     4227   4253   4985   -834   -305   -397       C  
ATOM    203  O   LEU A 595     -36.733 -18.747  33.871  1.00 36.21           O  
ANISOU  203  O   LEU A 595     4309   4343   5106   -831   -319   -445       O  
ATOM    204  CB  LEU A 595     -36.932 -18.484  37.138  1.00 34.05           C  
ANISOU  204  CB  LEU A 595     4147   3970   4820   -775   -182   -299       C  
ATOM    205  CG  LEU A 595     -37.467 -19.896  36.888  1.00 34.27           C  
ANISOU  205  CG  LEU A 595     4175   3906   4939   -775   -144   -331       C  
ATOM    206  CD1 LEU A 595     -36.322 -20.865  36.632  1.00 34.56           C  
ANISOU  206  CD1 LEU A 595     4237   3957   4939   -727   -155   -346       C  
ATOM    207  CD2 LEU A 595     -38.320 -20.364  38.057  1.00 33.59           C  
ANISOU  207  CD2 LEU A 595     4122   3722   4920   -776    -64   -289       C  
ATOM    208  N   PHE A 596     -37.787 -16.880  34.560  1.00 35.59           N  
ANISOU  208  N   PHE A 596     4212   4281   5031   -883   -324   -398       N  
ATOM    209  CA  PHE A 596     -38.600 -16.754  33.360  1.00 35.50           C  
ANISOU  209  CA  PHE A 596     4142   4270   5078   -938   -364   -454       C  
ATOM    210  C   PHE A 596     -37.724 -16.524  32.131  1.00 36.25           C  
ANISOU  210  C   PHE A 596     4204   4463   5105   -944   -443   -495       C  
ATOM    211  O   PHE A 596     -37.871 -17.208  31.118  1.00 39.21           O  
ANISOU  211  O   PHE A 596     4560   4832   5504   -947   -460   -533       O  
ATOM    212  CB  PHE A 596     -39.600 -15.606  33.521  1.00 35.03           C  
ANISOU  212  CB  PHE A 596     4058   4209   5043   -982   -375   -436       C  
ATOM    213  CG  PHE A 596     -40.520 -15.430  32.345  1.00 37.60           C  
ANISOU  213  CG  PHE A 596     4379   4551   5357   -986   -403   -425       C  
ATOM    214  CD1 PHE A 596     -41.701 -16.150  32.258  1.00 39.26           C  
ANISOU  214  CD1 PHE A 596     4591   4683   5644   -997   -357   -437       C  
ATOM    215  CD2 PHE A 596     -40.209 -14.536  31.332  1.00 37.91           C  
ANISOU  215  CD2 PHE A 596     4417   4676   5312   -969   -473   -393       C  
ATOM    216  CE1 PHE A 596     -42.551 -15.987  31.178  1.00 39.22           C  
ANISOU  216  CE1 PHE A 596     4583   4697   5622  -1004   -378   -432       C  
ATOM    217  CE2 PHE A 596     -41.054 -14.370  30.250  1.00 38.98           C  
ANISOU  217  CE2 PHE A 596     4556   4826   5430   -973   -483   -380       C  
ATOM    218  CZ  PHE A 596     -42.228 -15.095  30.173  1.00 39.07           C  
ANISOU  218  CZ  PHE A 596     4565   4770   5511  -1005   -441   -405       C  
ATOM    219  N   VAL A 597     -36.809 -15.564  32.236  1.00 30.92           N  
ANISOU  219  N   VAL A 597     3534   3883   4332   -931   -488   -467       N  
ATOM    220  CA  VAL A 597     -35.947 -15.175  31.122  1.00 28.02           C  
ANISOU  220  CA  VAL A 597     3151   3600   3896   -887   -557   -471       C  
ATOM    221  C   VAL A 597     -35.056 -16.316  30.628  1.00 31.54           C  
ANISOU  221  C   VAL A 597     3597   4074   4313   -887   -563   -522       C  
ATOM    222  O   VAL A 597     -34.934 -16.541  29.423  1.00 33.89           O  
ANISOU  222  O   VAL A 597     3882   4390   4604   -864   -600   -533       O  
ATOM    223  CB  VAL A 597     -35.070 -13.959  31.492  1.00 23.19           C  
ANISOU  223  CB  VAL A 597     2550   3070   3191   -843   -581   -431       C  
ATOM    224  CG1 VAL A 597     -34.049 -13.674  30.399  1.00 21.69           C  
ANISOU  224  CG1 VAL A 597     2353   2951   2938   -781   -629   -438       C  
ATOM    225  CG2 VAL A 597     -35.940 -12.739  31.747  1.00 21.13           C  
ANISOU  225  CG2 VAL A 597     2275   2789   2963   -826   -571   -405       C  
ATOM    226  N   THR A 598     -34.441 -17.034  31.563  1.00 32.45           N  
ANISOU  226  N   THR A 598     3760   4160   4411   -843   -514   -502       N  
ATOM    227  CA  THR A 598     -33.545 -18.135  31.221  1.00 31.87           C  
ANISOU  227  CA  THR A 598     3700   4093   4315   -801   -512   -532       C  
ATOM    228  C   THR A 598     -34.276 -19.244  30.472  1.00 33.21           C  
ANISOU  228  C   THR A 598     3844   4194   4579   -818   -497   -592       C  
ATOM    229  O   THR A 598     -33.801 -19.721  29.439  1.00 33.65           O  
ANISOU  229  O   THR A 598     3872   4294   4620   -817   -536   -647       O  
ATOM    230  CB  THR A 598     -32.874 -18.729  32.474  1.00 30.98           C  
ANISOU  230  CB  THR A 598     3653   3938   4179   -738   -455   -483       C  
ATOM    231  OG1 THR A 598     -32.125 -17.709  33.146  1.00 30.46           O  
ANISOU  231  OG1 THR A 598     3613   3939   4023   -719   -472   -429       O  
ATOM    232  CG2 THR A 598     -31.940 -19.866  32.090  1.00 30.73           C  
ANISOU  232  CG2 THR A 598     3633   3913   4129   -694   -459   -519       C  
ATOM    233  N   VAL A 599     -35.432 -19.643  30.998  1.00 33.30           N  
ANISOU  233  N   VAL A 599     3864   4100   4687   -835   -442   -582       N  
ATOM    234  CA  VAL A 599     -36.257 -20.680  30.383  1.00 31.74           C  
ANISOU  234  CA  VAL A 599     3644   3826   4590   -853   -424   -633       C  
ATOM    235  C   VAL A 599     -36.634 -20.302  28.954  1.00 33.41           C  
ANISOU  235  C   VAL A 599     3791   4090   4812   -905   -487   -693       C  
ATOM    236  O   VAL A 599     -36.630 -21.144  28.054  1.00 33.29           O  
ANISOU  236  O   VAL A 599     3763   4068   4816   -895   -497   -734       O  
ATOM    237  CB  VAL A 599     -37.534 -20.949  31.213  1.00 29.72           C  
ANISOU  237  CB  VAL A 599     3404   3455   4433   -870   -357   -605       C  
ATOM    238  CG1 VAL A 599     -38.521 -21.810  30.433  1.00 28.59           C  
ANISOU  238  CG1 VAL A 599     3227   3239   4396   -901   -349   -660       C  
ATOM    239  CG2 VAL A 599     -37.177 -21.608  32.537  1.00 29.34           C  
ANISOU  239  CG2 VAL A 599     3418   3345   4383   -819   -292   -552       C  
ATOM    240  N   VAL A 600     -36.943 -19.026  28.751  1.00 34.81           N  
ANISOU  240  N   VAL A 600     3975   4324   4926   -914   -514   -630       N  
ATOM    241  CA  VAL A 600     -37.260 -18.517  27.423  1.00 37.32           C  
ANISOU  241  CA  VAL A 600     4291   4694   5196   -913   -557   -598       C  
ATOM    242  C   VAL A 600     -36.073 -18.688  26.476  1.00 37.74           C  
ANISOU  242  C   VAL A 600     4338   4826   5176   -883   -606   -615       C  
ATOM    243  O   VAL A 600     -36.231 -19.159  25.349  1.00 38.02           O  
ANISOU  243  O   VAL A 600     4364   4870   5213   -882   -619   -633       O  
ATOM    244  CB  VAL A 600     -37.688 -17.036  27.477  1.00 37.58           C  
ANISOU  244  CB  VAL A 600     4338   4754   5188   -918   -587   -517       C  
ATOM    245  CG1 VAL A 600     -37.722 -16.438  26.083  1.00 37.45           C  
ANISOU  245  CG1 VAL A 600     4324   4776   5128   -898   -639   -477       C  
ATOM    246  CG2 VAL A 600     -39.045 -16.901  28.156  1.00 36.94           C  
ANISOU  246  CG2 VAL A 600     4263   4604   5168   -949   -536   -502       C  
ATOM    247  N   PHE A 601     -34.882 -18.325  26.943  1.00 39.11           N  
ANISOU  247  N   PHE A 601     4518   5057   5283   -856   -628   -609       N  
ATOM    248  CA  PHE A 601     -33.677 -18.443  26.126  1.00 41.56           C  
ANISOU  248  CA  PHE A 601     4828   5442   5519   -819   -668   -619       C  
ATOM    249  C   PHE A 601     -33.297 -19.898  25.852  1.00 44.01           C  
ANISOU  249  C   PHE A 601     5123   5744   5857   -815   -651   -702       C  
ATOM    250  O   PHE A 601     -32.620 -20.193  24.868  1.00 45.47           O  
ANISOU  250  O   PHE A 601     5302   5978   5996   -791   -679   -716       O  
ATOM    251  CB  PHE A 601     -32.498 -17.699  26.763  1.00 41.00           C  
ANISOU  251  CB  PHE A 601     4775   5436   5369   -782   -689   -591       C  
ATOM    252  CG  PHE A 601     -32.544 -16.206  26.575  1.00 40.63           C  
ANISOU  252  CG  PHE A 601     4736   5399   5302   -747   -719   -525       C  
ATOM    253  CD1 PHE A 601     -31.485 -15.412  26.982  1.00 41.45           C  
ANISOU  253  CD1 PHE A 601     4856   5560   5334   -699   -729   -501       C  
ATOM    254  CD2 PHE A 601     -33.644 -15.596  25.994  1.00 40.04           C  
ANISOU  254  CD2 PHE A 601     4653   5274   5285   -753   -730   -497       C  
ATOM    255  CE1 PHE A 601     -31.521 -14.040  26.811  1.00 40.98           C  
ANISOU  255  CE1 PHE A 601     4799   5504   5268   -655   -740   -463       C  
ATOM    256  CE2 PHE A 601     -33.686 -14.225  25.823  1.00 38.47           C  
ANISOU  256  CE2 PHE A 601     4455   5079   5084   -700   -740   -464       C  
ATOM    257  CZ  PHE A 601     -32.624 -13.447  26.231  1.00 38.68           C  
ANISOU  257  CZ  PHE A 601     4490   5160   5046   -655   -746   -456       C  
ATOM    258  N   ILE A 602     -33.730 -20.803  26.723  1.00 44.73           N  
ANISOU  258  N   ILE A 602     5206   5752   6035   -830   -606   -756       N  
ATOM    259  CA  ILE A 602     -33.471 -22.226  26.529  1.00 46.74           C  
ANISOU  259  CA  ILE A 602     5446   5964   6349   -814   -595   -836       C  
ATOM    260  C   ILE A 602     -34.383 -22.802  25.450  1.00 48.19           C  
ANISOU  260  C   ILE A 602     5614   6108   6589   -825   -590   -853       C  
ATOM    261  O   ILE A 602     -33.918 -23.454  24.514  1.00 48.24           O  
ANISOU  261  O   ILE A 602     5605   6147   6577   -805   -611   -893       O  
ATOM    262  CB  ILE A 602     -33.668 -23.024  27.833  1.00 47.70           C  
ANISOU  262  CB  ILE A 602     5623   5975   6527   -774   -521   -797       C  
ATOM    263  CG1 ILE A 602     -32.600 -22.643  28.861  1.00 47.13           C  
ANISOU  263  CG1 ILE A 602     5601   5939   6366   -727   -509   -736       C  
ATOM    264  CG2 ILE A 602     -33.620 -24.519  27.557  1.00 48.47           C  
ANISOU  264  CG2 ILE A 602     5723   6005   6688   -744   -501   -845       C  
ATOM    265  CD1 ILE A 602     -32.749 -23.360  30.186  1.00 47.27           C  
ANISOU  265  CD1 ILE A 602     5678   5854   6429   -688   -437   -686       C  
ATOM    266  N   ILE A 603     -35.681 -22.552  25.589  1.00 49.41           N  
ANISOU  266  N   ILE A 603     5771   6195   6807   -856   -560   -822       N  
ATOM    267  CA  ILE A 603     -36.676 -23.050  24.645  1.00 50.32           C  
ANISOU  267  CA  ILE A 603     5874   6272   6973   -867   -552   -833       C  
ATOM    268  C   ILE A 603     -36.430 -22.521  23.235  1.00 52.31           C  
ANISOU  268  C   ILE A 603     6121   6615   7140   -864   -598   -808       C  
ATOM    269  O   ILE A 603     -36.511 -23.266  22.258  1.00 53.01           O  
ANISOU  269  O   ILE A 603     6194   6704   7245   -857   -605   -847       O  
ATOM    270  CB  ILE A 603     -38.103 -22.663  25.082  1.00 48.58           C  
ANISOU  270  CB  ILE A 603     5664   5979   6815   -897   -515   -790       C  
ATOM    271  CG1 ILE A 603     -38.420 -23.260  26.454  1.00 46.81           C  
ANISOU  271  CG1 ILE A 603     5450   5645   6688   -900   -461   -803       C  
ATOM    272  CG2 ILE A 603     -39.124 -23.121  24.052  1.00 50.17           C  
ANISOU  272  CG2 ILE A 603     5855   6151   7055   -907   -510   -800       C  
ATOM    273  CD1 ILE A 603     -39.771 -22.852  26.999  1.00 45.56           C  
ANISOU  273  CD1 ILE A 603     5306   5421   6583   -925   -419   -755       C  
ATOM    274  N   TYR A 604     -36.121 -21.233  23.138  1.00 53.21           N  
ANISOU  274  N   TYR A 604     6251   6795   7170   -867   -629   -739       N  
ATOM    275  CA  TYR A 604     -35.911 -20.597  21.845  1.00 54.79           C  
ANISOU  275  CA  TYR A 604     6456   7058   7304   -862   -673   -696       C  
ATOM    276  C   TYR A 604     -34.430 -20.340  21.577  1.00 55.04           C  
ANISOU  276  C   TYR A 604     6493   7166   7253   -826   -709   -690       C  
ATOM    277  O   TYR A 604     -34.065 -19.305  21.018  1.00 53.92           O  
ANISOU  277  O   TYR A 604     6367   7059   7061   -811   -747   -628       O  
ATOM    278  CB  TYR A 604     -36.676 -19.275  21.771  1.00 54.82           C  
ANISOU  278  CB  TYR A 604     6480   7056   7292   -881   -691   -611       C  
ATOM    279  CG  TYR A 604     -38.164 -19.381  22.023  1.00 56.71           C  
ANISOU  279  CG  TYR A 604     6719   7230   7597   -915   -653   -608       C  
ATOM    280  CD1 TYR A 604     -39.060 -19.494  20.968  1.00 57.93           C  
ANISOU  280  CD1 TYR A 604     6871   7373   7766   -933   -657   -601       C  
ATOM    281  CD2 TYR A 604     -38.673 -19.352  23.315  1.00 56.95           C  
ANISOU  281  CD2 TYR A 604     6754   7209   7674   -927   -612   -610       C  
ATOM    282  CE1 TYR A 604     -40.421 -19.584  21.194  1.00 58.27           C  
ANISOU  282  CE1 TYR A 604     6917   7358   7864   -959   -621   -598       C  
ATOM    283  CE2 TYR A 604     -40.031 -19.442  23.550  1.00 57.45           C  
ANISOU  283  CE2 TYR A 604     6820   7209   7800   -952   -574   -605       C  
ATOM    284  CZ  TYR A 604     -40.901 -19.558  22.486  1.00 58.52           C  
ANISOU  284  CZ  TYR A 604     6953   7337   7943   -965   -579   -600       C  
ATOM    285  OH  TYR A 604     -42.255 -19.648  22.717  1.00 59.99           O  
ANISOU  285  OH  TYR A 604     7144   7463   8187   -984   -542   -596       O  
ATOM    286  N   ARG A 605     -33.581 -21.284  21.970  1.00 56.20           N  
ANISOU  286  N   ARG A 605     6627   7326   7398   -804   -697   -756       N  
ATOM    287  CA  ARG A 605     -32.137 -21.124  21.817  1.00 56.25           C  
ANISOU  287  CA  ARG A 605     6642   7409   7322   -766   -724   -753       C  
ATOM    288  C   ARG A 605     -31.700 -21.063  20.352  1.00 56.87           C  
ANISOU  288  C   ARG A 605     6717   7533   7357   -752   -753   -742       C  
ATOM    289  O   ARG A 605     -30.636 -20.527  20.040  1.00 56.30           O  
ANISOU  289  O   ARG A 605     6660   7516   7217   -721   -777   -711       O  
ATOM    290  CB  ARG A 605     -31.390 -22.254  22.532  1.00 56.18           C  
ANISOU  290  CB  ARG A 605     6622   7399   7325   -744   -708   -831       C  
ATOM    291  CG  ARG A 605     -31.457 -23.590  21.809  1.00 57.52           C  
ANISOU  291  CG  ARG A 605     6765   7546   7545   -735   -701   -911       C  
ATOM    292  CD  ARG A 605     -30.331 -24.515  22.237  1.00 59.09           C  
ANISOU  292  CD  ARG A 605     6958   7762   7730   -695   -705   -977       C  
ATOM    293  NE  ARG A 605     -30.626 -25.217  23.481  1.00 59.90           N  
ANISOU  293  NE  ARG A 605     7063   7778   7920   -697   -679  -1025       N  
ATOM    294  CZ  ARG A 605     -31.091 -26.461  23.539  1.00 61.66           C  
ANISOU  294  CZ  ARG A 605     7271   7908   8249   -694   -662  -1095       C  
ATOM    295  NH1 ARG A 605     -31.312 -27.139  22.420  1.00 61.84           N  
ANISOU  295  NH1 ARG A 605     7271   7931   8294   -687   -669  -1130       N  
ATOM    296  NH2 ARG A 605     -31.332 -27.029  24.713  1.00 62.31           N  
ANISOU  296  NH2 ARG A 605     7398   7886   8392   -668   -609  -1063       N  
ATOM    297  N   ASP A 606     -32.524 -21.612  19.463  1.00 57.26           N  
ANISOU  297  N   ASP A 606     6750   7555   7452   -772   -748   -766       N  
ATOM    298  CA  ASP A 606     -32.181 -21.712  18.046  1.00 57.30           C  
ANISOU  298  CA  ASP A 606     6748   7598   7425   -762   -771   -766       C  
ATOM    299  C   ASP A 606     -32.662 -20.500  17.252  1.00 57.14           C  
ANISOU  299  C   ASP A 606     6748   7572   7392   -773   -800   -685       C  
ATOM    300  O   ASP A 606     -32.330 -20.344  16.077  1.00 57.54           O  
ANISOU  300  O   ASP A 606     6793   7653   7416   -764   -820   -682       O  
ATOM    301  CB  ASP A 606     -32.764 -22.992  17.443  1.00 57.52           C  
ANISOU  301  CB  ASP A 606     6746   7597   7511   -772   -753   -841       C  
ATOM    302  CG  ASP A 606     -32.396 -24.232  18.236  1.00 57.92           C  
ANISOU  302  CG  ASP A 606     6777   7625   7605   -752   -730   -928       C  
ATOM    303  OD1 ASP A 606     -31.315 -24.805  17.984  1.00 57.41           O  
ANISOU  303  OD1 ASP A 606     6704   7608   7504   -718   -740   -970       O  
ATOM    304  OD2 ASP A 606     -33.192 -24.638  19.110  1.00 58.71           O  
ANISOU  304  OD2 ASP A 606     6874   7650   7783   -766   -701   -952       O  
ATOM    305  N   THR A 607     -33.453 -19.650  17.899  1.00 56.11           N  
ANISOU  305  N   THR A 607     6633   7399   7287   -790   -801   -634       N  
ATOM    306  CA  THR A 607     -33.946 -18.431  17.270  1.00 54.32           C  
ANISOU  306  CA  THR A 607     6403   7173   7062   -793   -821   -592       C  
ATOM    307  C   THR A 607     -32.812 -17.420  17.114  1.00 54.90           C  
ANISOU  307  C   THR A 607     6477   7306   7079   -752   -837   -580       C  
ATOM    308  O   THR A 607     -32.016 -17.235  18.035  1.00 55.73           O  
ANISOU  308  O   THR A 607     6599   7419   7156   -726   -836   -567       O  
ATOM    309  CB  THR A 607     -35.084 -17.801  18.087  1.00 51.95           C  
ANISOU  309  CB  THR A 607     6115   6817   6808   -817   -814   -551       C  
ATOM    310  OG1 THR A 607     -34.628 -17.535  19.419  1.00 52.19           O  
ANISOU  310  OG1 THR A 607     6167   6832   6831   -797   -807   -525       O  
ATOM    311  CG2 THR A 607     -36.282 -18.738  18.143  1.00 50.40           C  
ANISOU  311  CG2 THR A 607     5918   6571   6660   -861   -784   -566       C  
ATOM    312  N   PRO A 608     -32.739 -16.766  15.944  1.00 54.42           N  
ANISOU  312  N   PRO A 608     6395   7288   6995   -749   -846   -588       N  
ATOM    313  CA  PRO A 608     -31.678 -15.817  15.583  1.00 54.15           C  
ANISOU  313  CA  PRO A 608     6357   7322   6896   -718   -848   -581       C  
ATOM    314  C   PRO A 608     -31.387 -14.761  16.649  1.00 55.50           C  
ANISOU  314  C   PRO A 608     6544   7491   7052   -694   -843   -546       C  
ATOM    315  O   PRO A 608     -30.241 -14.336  16.780  1.00 57.02           O  
ANISOU  315  O   PRO A 608     6744   7739   7182   -667   -835   -539       O  
ATOM    316  CB  PRO A 608     -32.230 -15.152  14.323  1.00 53.55           C  
ANISOU  316  CB  PRO A 608     6258   7266   6822   -735   -855   -585       C  
ATOM    317  CG  PRO A 608     -33.064 -16.207  13.698  1.00 54.01           C  
ANISOU  317  CG  PRO A 608     6305   7292   6925   -765   -858   -612       C  
ATOM    318  CD  PRO A 608     -33.699 -16.953  14.840  1.00 54.06           C  
ANISOU  318  CD  PRO A 608     6329   7230   6980   -779   -849   -603       C  
ATOM    319  N   VAL A 609     -32.402 -14.350  17.399  1.00 55.58           N  
ANISOU  319  N   VAL A 609     6560   7441   7117   -705   -843   -525       N  
ATOM    320  CA  VAL A 609     -32.219 -13.318  18.416  1.00 54.59           C  
ANISOU  320  CA  VAL A 609     6446   7316   6981   -680   -834   -499       C  
ATOM    321  C   VAL A 609     -31.413 -13.839  19.612  1.00 52.68           C  
ANISOU  321  C   VAL A 609     6227   7070   6720   -658   -828   -494       C  
ATOM    322  O   VAL A 609     -30.812 -13.065  20.357  1.00 52.00           O  
ANISOU  322  O   VAL A 609     6152   7008   6596   -631   -816   -475       O  
ATOM    323  CB  VAL A 609     -33.575 -12.729  18.867  1.00 54.71           C  
ANISOU  323  CB  VAL A 609     6453   7268   7064   -695   -834   -485       C  
ATOM    324  CG1 VAL A 609     -34.400 -13.784  19.570  1.00 54.27           C  
ANISOU  324  CG1 VAL A 609     6410   7140   7068   -717   -824   -479       C  
ATOM    325  CG2 VAL A 609     -33.372 -11.507  19.757  1.00 55.58           C  
ANISOU  325  CG2 VAL A 609     6569   7396   7153   -669   -817   -466       C  
ATOM    326  N   VAL A 610     -31.387 -15.158  19.775  1.00 52.62           N  
ANISOU  326  N   VAL A 610     6228   7034   6732   -672   -832   -510       N  
ATOM    327  CA  VAL A 610     -30.603 -15.785  20.832  1.00 53.90           C  
ANISOU  327  CA  VAL A 610     6416   7191   6875   -653   -829   -508       C  
ATOM    328  C   VAL A 610     -29.319 -16.377  20.255  1.00 57.58           C  
ANISOU  328  C   VAL A 610     6884   7718   7277   -634   -831   -530       C  
ATOM    329  O   VAL A 610     -28.288 -16.438  20.926  1.00 56.87           O  
ANISOU  329  O   VAL A 610     6813   7652   7141   -604   -829   -524       O  
ATOM    330  CB  VAL A 610     -31.405 -16.897  21.533  1.00 53.36           C  
ANISOU  330  CB  VAL A 610     6342   7081   6853   -697   -811   -532       C  
ATOM    331  CG1 VAL A 610     -30.638 -17.445  22.728  1.00 53.95           C  
ANISOU  331  CG1 VAL A 610     6419   7188   6892   -692   -788   -563       C  
ATOM    332  CG2 VAL A 610     -32.753 -16.369  21.972  1.00 53.08           C  
ANISOU  332  CG2 VAL A 610     6304   6983   6882   -723   -804   -506       C  
ATOM    333  N   LYS A 611     -29.390 -16.800  18.997  1.00 60.91           N  
ANISOU  333  N   LYS A 611     7284   8166   7694   -649   -834   -557       N  
ATOM    334  CA  LYS A 611     -28.271 -17.464  18.340  1.00 64.60           C  
ANISOU  334  CA  LYS A 611     7747   8690   8109   -632   -833   -587       C  
ATOM    335  C   LYS A 611     -27.154 -16.492  17.961  1.00 67.65           C  
ANISOU  335  C   LYS A 611     8129   9153   8423   -603   -826   -573       C  
ATOM    336  O   LYS A 611     -25.985 -16.874  17.898  1.00 68.03           O  
ANISOU  336  O   LYS A 611     8181   9247   8419   -580   -821   -585       O  
ATOM    337  CB  LYS A 611     -28.757 -18.197  17.086  1.00 66.52           C  
ANISOU  337  CB  LYS A 611     7962   8939   8373   -657   -835   -626       C  
ATOM    338  CG  LYS A 611     -28.064 -19.527  16.825  1.00 68.13           C  
ANISOU  338  CG  LYS A 611     8164   9161   8562   -647   -833   -670       C  
ATOM    339  CD  LYS A 611     -28.085 -19.884  15.342  1.00 69.62           C  
ANISOU  339  CD  LYS A 611     8319   9390   8744   -655   -833   -711       C  
ATOM    340  CE  LYS A 611     -29.465 -19.689  14.730  1.00 70.55           C  
ANISOU  340  CE  LYS A 611     8421   9470   8915   -691   -835   -709       C  
ATOM    341  NZ  LYS A 611     -29.467 -19.929  13.258  1.00 71.66           N  
ANISOU  341  NZ  LYS A 611     8530   9654   9045   -698   -837   -746       N  
ATOM    342  N   SER A 612     -27.515 -15.236  17.712  1.00 70.16           N  
ANISOU  342  N   SER A 612     8438   9483   8735   -608   -821   -546       N  
ATOM    343  CA  SER A 612     -26.565 -14.252  17.196  1.00 72.88           C  
ANISOU  343  CA  SER A 612     8777   9904   9011   -593   -808   -529       C  
ATOM    344  C   SER A 612     -25.592 -13.732  18.259  1.00 73.02           C  
ANISOU  344  C   SER A 612     8819   9942   8983   -562   -796   -497       C  
ATOM    345  O   SER A 612     -24.620 -13.046  17.939  1.00 73.39           O  
ANISOU  345  O   SER A 612     8862  10053   8970   -551   -780   -479       O  
ATOM    346  CB  SER A 612     -27.309 -13.089  16.526  1.00 74.38           C  
ANISOU  346  CB  SER A 612     8951  10101   9209   -614   -806   -510       C  
ATOM    347  OG  SER A 612     -26.407 -12.164  15.942  1.00 75.13           O  
ANISOU  347  OG  SER A 612     9038  10270   9237   -609   -791   -490       O  
ATOM    348  N   SER A 613     -25.855 -14.061  19.520  1.00 70.89           N  
ANISOU  348  N   SER A 613     8572   9618   8743   -552   -800   -489       N  
ATOM    349  CA  SER A 613     -24.981 -13.646  20.613  1.00 68.13           C  
ANISOU  349  CA  SER A 613     8249   9283   8353   -521   -789   -460       C  
ATOM    350  C   SER A 613     -24.340 -14.856  21.287  1.00 65.76           C  
ANISOU  350  C   SER A 613     7972   8967   8048   -502   -798   -478       C  
ATOM    351  O   SER A 613     -24.775 -15.991  21.088  1.00 66.33           O  
ANISOU  351  O   SER A 613     8041   9004   8158   -518   -811   -510       O  
ATOM    352  CB  SER A 613     -25.758 -12.820  21.642  1.00 67.40           C  
ANISOU  352  CB  SER A 613     8168   9150   8291   -521   -784   -431       C  
ATOM    353  OG  SER A 613     -24.901 -12.327  22.657  1.00 67.26           O  
ANISOU  353  OG  SER A 613     8176   9152   8229   -492   -770   -399       O  
ATOM    354  N   SER A 614     -23.300 -14.611  22.078  1.00 62.79           N  
ANISOU  354  N   SER A 614     7620   8616   7623   -471   -788   -455       N  
ATOM    355  CA  SER A 614     -22.656 -15.681  22.829  1.00 59.65           C  
ANISOU  355  CA  SER A 614     7250   8199   7214   -450   -797   -468       C  
ATOM    356  C   SER A 614     -23.597 -16.180  23.915  1.00 56.20           C  
ANISOU  356  C   SER A 614     6817   7719   6818   -470   -799   -480       C  
ATOM    357  O   SER A 614     -23.763 -15.535  24.950  1.00 55.17           O  
ANISOU  357  O   SER A 614     6701   7578   6682   -462   -791   -453       O  
ATOM    358  CB  SER A 614     -21.342 -15.199  23.445  1.00 59.66           C  
ANISOU  358  CB  SER A 614     7274   8244   7150   -413   -782   -438       C  
ATOM    359  OG  SER A 614     -20.422 -14.805  22.442  1.00 60.93           O  
ANISOU  359  OG  SER A 614     7412   8476   7264   -409   -767   -438       O  
ATOM    360  N   ARG A 615     -24.216 -17.330  23.667  1.00 53.94           N  
ANISOU  360  N   ARG A 615     6502   7430   6561   -505   -799   -535       N  
ATOM    361  CA  ARG A 615     -25.194 -17.895  24.591  1.00 51.07           C  
ANISOU  361  CA  ARG A 615     6123   7041   6239   -542   -787   -569       C  
ATOM    362  C   ARG A 615     -24.589 -18.331  25.923  1.00 49.14           C  
ANISOU  362  C   ARG A 615     5893   6823   5953   -529   -774   -584       C  
ATOM    363  O   ARG A 615     -25.228 -18.208  26.967  1.00 47.27           O  
ANISOU  363  O   ARG A 615     5659   6566   5737   -552   -761   -582       O  
ATOM    364  CB  ARG A 615     -25.942 -19.060  23.939  1.00 50.53           C  
ANISOU  364  CB  ARG A 615     6021   6953   6226   -577   -782   -635       C  
ATOM    365  CG  ARG A 615     -27.104 -18.625  23.061  1.00 51.04           C  
ANISOU  365  CG  ARG A 615     6071   6971   6349   -607   -789   -617       C  
ATOM    366  CD  ARG A 615     -27.845 -19.818  22.485  1.00 52.62           C  
ANISOU  366  CD  ARG A 615     6240   7148   6605   -640   -779   -683       C  
ATOM    367  NE  ARG A 615     -27.197 -20.345  21.287  1.00 54.84           N  
ANISOU  367  NE  ARG A 615     6511   7465   6860   -622   -790   -707       N  
ATOM    368  CZ  ARG A 615     -27.159 -21.634  20.966  1.00 56.88           C  
ANISOU  368  CZ  ARG A 615     6743   7726   7143   -623   -780   -785       C  
ATOM    369  NH1 ARG A 615     -27.722 -22.534  21.761  1.00 57.53           N  
ANISOU  369  NH1 ARG A 615     6810   7763   7287   -636   -760   -848       N  
ATOM    370  NH2 ARG A 615     -26.551 -22.025  19.855  1.00 57.99           N  
ANISOU  370  NH2 ARG A 615     6873   7903   7256   -606   -790   -804       N  
ATOM    371  N   GLU A 616     -23.362 -18.843  25.884  1.00 48.87           N  
ANISOU  371  N   GLU A 616     5872   6833   5863   -492   -777   -598       N  
ATOM    372  CA  GLU A 616     -22.691 -19.288  27.101  1.00 47.10           C  
ANISOU  372  CA  GLU A 616     5669   6635   5594   -469   -770   -611       C  
ATOM    373  C   GLU A 616     -22.423 -18.128  28.053  1.00 41.26           C  
ANISOU  373  C   GLU A 616     4965   5900   4812   -452   -765   -535       C  
ATOM    374  O   GLU A 616     -22.514 -18.284  29.270  1.00 39.70           O  
ANISOU  374  O   GLU A 616     4782   5708   4594   -458   -755   -535       O  
ATOM    375  CB  GLU A 616     -21.385 -20.014  26.774  1.00 51.22           C  
ANISOU  375  CB  GLU A 616     6197   7198   6065   -425   -775   -637       C  
ATOM    376  CG  GLU A 616     -21.563 -21.458  26.339  1.00 55.69           C  
ANISOU  376  CG  GLU A 616     6729   7757   6672   -428   -777   -736       C  
ATOM    377  CD  GLU A 616     -21.249 -21.669  24.871  1.00 59.74           C  
ANISOU  377  CD  GLU A 616     7222   8288   7190   -425   -784   -747       C  
ATOM    378  OE1 GLU A 616     -21.376 -20.704  24.088  1.00 60.41           O  
ANISOU  378  OE1 GLU A 616     7311   8371   7272   -438   -787   -688       O  
ATOM    379  OE2 GLU A 616     -20.869 -22.801  24.501  1.00 61.52           O  
ANISOU  379  OE2 GLU A 616     7427   8524   7426   -406   -787   -819       O  
ATOM    380  N   LEU A 617     -22.095 -16.968  27.495  1.00 38.73           N  
ANISOU  380  N   LEU A 617     4659   5572   4484   -428   -769   -475       N  
ATOM    381  CA  LEU A 617     -21.835 -15.781  28.302  1.00 37.21           C  
ANISOU  381  CA  LEU A 617     4497   5374   4266   -402   -760   -411       C  
ATOM    382  C   LEU A 617     -23.103 -15.268  28.973  1.00 35.53           C  
ANISOU  382  C   LEU A 617     4272   5134   4093   -438   -751   -401       C  
ATOM    383  O   LEU A 617     -23.068 -14.825  30.122  1.00 34.57           O  
ANISOU  383  O   LEU A 617     4172   5020   3944   -432   -738   -366       O  
ATOM    384  CB  LEU A 617     -21.204 -14.673  27.456  1.00 37.14           C  
ANISOU  384  CB  LEU A 617     4502   5351   4257   -367   -763   -370       C  
ATOM    385  CG  LEU A 617     -19.736 -14.866  27.079  1.00 38.30           C  
ANISOU  385  CG  LEU A 617     4672   5521   4360   -331   -764   -362       C  
ATOM    386  CD1 LEU A 617     -19.223 -13.663  26.305  1.00 38.33           C  
ANISOU  386  CD1 LEU A 617     4655   5568   4342   -329   -744   -334       C  
ATOM    387  CD2 LEU A 617     -18.898 -15.106  28.326  1.00 39.53           C  
ANISOU  387  CD2 LEU A 617     4862   5697   4462   -302   -753   -343       C  
ATOM    388  N   CYS A 618     -24.219 -15.328  28.252  1.00 34.26           N  
ANISOU  388  N   CYS A 618     4078   4940   3998   -476   -757   -427       N  
ATOM    389  CA  CYS A 618     -25.503 -14.901  28.797  1.00 34.43           C  
ANISOU  389  CA  CYS A 618     4084   4927   4070   -516   -745   -420       C  
ATOM    390  C   CYS A 618     -25.903 -15.757  29.996  1.00 34.03           C  
ANISOU  390  C   CYS A 618     4035   4878   4017   -564   -729   -445       C  
ATOM    391  O   CYS A 618     -26.432 -15.243  30.982  1.00 33.81           O  
ANISOU  391  O   CYS A 618     4019   4837   3991   -591   -713   -411       O  
ATOM    392  CB  CYS A 618     -26.595 -14.938  27.724  1.00 34.54           C  
ANISOU  392  CB  CYS A 618     4066   4896   4162   -545   -754   -445       C  
ATOM    393  SG  CYS A 618     -26.489 -13.612  26.496  1.00107.99           S  
ANISOU  393  SG  CYS A 618    13371  14180  13479   -501   -769   -410       S  
ATOM    394  N   TYR A 619     -25.641 -17.058  29.908  1.00 33.72           N  
ANISOU  394  N   TYR A 619     3987   4849   3977   -579   -729   -506       N  
ATOM    395  CA  TYR A 619     -25.929 -17.978  31.004  1.00 35.92           C  
ANISOU  395  CA  TYR A 619     4303   5047   4298   -568   -671   -502       C  
ATOM    396  C   TYR A 619     -25.169 -17.583  32.265  1.00 34.74           C  
ANISOU  396  C   TYR A 619     4213   4901   4087   -521   -647   -430       C  
ATOM    397  O   TYR A 619     -25.694 -17.682  33.374  1.00 34.59           O  
ANISOU  397  O   TYR A 619     4236   4797   4111   -508   -590   -383       O  
ATOM    398  CB  TYR A 619     -25.579 -19.416  30.612  1.00 40.91           C  
ANISOU  398  CB  TYR A 619     4937   5642   4966   -535   -654   -558       C  
ATOM    399  CG  TYR A 619     -26.623 -20.097  29.755  1.00 46.64           C  
ANISOU  399  CG  TYR A 619     5620   6314   5787   -574   -649   -620       C  
ATOM    400  CD1 TYR A 619     -27.923 -19.612  29.692  1.00 48.67           C  
ANISOU  400  CD1 TYR A 619     5855   6526   6111   -628   -640   -613       C  
ATOM    401  CD2 TYR A 619     -26.310 -21.231  29.016  1.00 49.70           C  
ANISOU  401  CD2 TYR A 619     5990   6695   6200   -556   -656   -688       C  
ATOM    402  CE1 TYR A 619     -28.881 -20.235  28.912  1.00 51.05           C  
ANISOU  402  CE1 TYR A 619     6119   6777   6501   -663   -637   -669       C  
ATOM    403  CE2 TYR A 619     -27.262 -21.861  28.234  1.00 51.62           C  
ANISOU  403  CE2 TYR A 619     6194   6887   6531   -590   -653   -744       C  
ATOM    404  CZ  TYR A 619     -28.545 -21.358  28.186  1.00 52.84           C  
ANISOU  404  CZ  TYR A 619     6329   6997   6750   -643   -643   -734       C  
ATOM    405  OH  TYR A 619     -29.495 -21.980  27.410  1.00 55.72           O  
ANISOU  405  OH  TYR A 619     6656   7310   7204   -677   -641   -789       O  
ATOM    406  N   ILE A 620     -23.932 -17.132  32.084  1.00 32.06           N  
ANISOU  406  N   ILE A 620     3875   4660   3645   -496   -692   -422       N  
ATOM    407  CA  ILE A 620     -23.101 -16.693  33.197  1.00 28.68           C  
ANISOU  407  CA  ILE A 620     3501   4246   3149   -450   -677   -354       C  
ATOM    408  C   ILE A 620     -23.634 -15.391  33.792  1.00 27.77           C  
ANISOU  408  C   ILE A 620     3390   4142   3020   -478   -683   -296       C  
ATOM    409  O   ILE A 620     -23.660 -15.220  35.012  1.00 27.91           O  
ANISOU  409  O   ILE A 620     3457   4109   3036   -450   -640   -237       O  
ATOM    410  CB  ILE A 620     -21.629 -16.520  32.763  1.00 26.04           C  
ANISOU  410  CB  ILE A 620     3167   4012   2716   -412   -723   -361       C  
ATOM    411  CG1 ILE A 620     -21.065 -17.856  32.272  1.00 25.46           C  
ANISOU  411  CG1 ILE A 620     3090   3933   2653   -384   -719   -423       C  
ATOM    412  CG2 ILE A 620     -20.789 -15.974  33.908  1.00 23.22           C  
ANISOU  412  CG2 ILE A 620     2866   3667   2291   -366   -710   -288       C  
ATOM    413  CD1 ILE A 620     -19.625 -17.787  31.818  1.00 26.41           C  
ANISOU  413  CD1 ILE A 620     3224   4100   2713   -330   -739   -415       C  
ATOM    414  N   ILE A 621     -24.070 -14.482  32.924  1.00 26.42           N  
ANISOU  414  N   ILE A 621     3178   3986   2875   -493   -708   -302       N  
ATOM    415  CA  ILE A 621     -24.655 -13.217  33.361  1.00 25.27           C  
ANISOU  415  CA  ILE A 621     3034   3818   2748   -494   -695   -252       C  
ATOM    416  C   ILE A 621     -25.968 -13.449  34.110  1.00 26.89           C  
ANISOU  416  C   ILE A 621     3234   3987   2995   -578   -688   -251       C  
ATOM    417  O   ILE A 621     -26.237 -12.811  35.128  1.00 27.91           O  
ANISOU  417  O   ILE A 621     3392   4092   3120   -574   -666   -196       O  
ATOM    418  CB  ILE A 621     -24.891 -12.260  32.171  1.00 22.26           C  
ANISOU  418  CB  ILE A 621     2625   3416   2419   -465   -699   -259       C  
ATOM    419  CG1 ILE A 621     -23.565 -11.935  31.476  1.00 22.46           C  
ANISOU  419  CG1 ILE A 621     2667   3454   2413   -397   -705   -252       C  
ATOM    420  CG2 ILE A 621     -25.575 -10.980  32.632  1.00 18.83           C  
ANISOU  420  CG2 ILE A 621     2188   2958   2008   -465   -684   -221       C  
ATOM    421  CD1 ILE A 621     -23.707 -11.015  30.278  1.00 21.19           C  
ANISOU  421  CD1 ILE A 621     2491   3264   2296   -376   -711   -255       C  
ATOM    422  N   LEU A 622     -26.777 -14.376  33.607  1.00 27.15           N  
ANISOU  422  N   LEU A 622     3247   3955   3113   -602   -663   -301       N  
ATOM    423  CA  LEU A 622     -28.050 -14.706  34.238  1.00 26.24           C  
ANISOU  423  CA  LEU A 622     3143   3729   3098   -620   -601   -291       C  
ATOM    424  C   LEU A 622     -27.844 -15.423  35.567  1.00 25.69           C  
ANISOU  424  C   LEU A 622     3141   3580   3042   -567   -527   -246       C  
ATOM    425  O   LEU A 622     -28.645 -15.280  36.491  1.00 25.95           O  
ANISOU  425  O   LEU A 622     3196   3542   3123   -573   -477   -209       O  
ATOM    426  CB  LEU A 622     -28.905 -15.560  33.301  1.00 26.85           C  
ANISOU  426  CB  LEU A 622     3182   3758   3264   -654   -595   -356       C  
ATOM    427  CG  LEU A 622     -29.481 -14.815  32.098  1.00 27.45           C  
ANISOU  427  CG  LEU A 622     3191   3890   3350   -719   -659   -396       C  
ATOM    428  CD1 LEU A 622     -30.057 -15.793  31.089  1.00 28.69           C  
ANISOU  428  CD1 LEU A 622     3312   4009   3580   -743   -657   -466       C  
ATOM    429  CD2 LEU A 622     -30.540 -13.824  32.555  1.00 28.57           C  
ANISOU  429  CD2 LEU A 622     3323   3997   3534   -751   -649   -362       C  
ATOM    430  N   ALA A 623     -26.765 -16.195  35.656  1.00 26.17           N  
ANISOU  430  N   ALA A 623     3231   3652   3060   -516   -521   -250       N  
ATOM    431  CA  ALA A 623     -26.421 -16.887  36.891  1.00 26.88           C  
ANISOU  431  CA  ALA A 623     3386   3672   3154   -465   -458   -206       C  
ATOM    432  C   ALA A 623     -25.949 -15.895  37.950  1.00 29.04           C  
ANISOU  432  C   ALA A 623     3697   3977   3358   -442   -454   -135       C  
ATOM    433  O   ALA A 623     -26.268 -16.035  39.131  1.00 32.26           O  
ANISOU  433  O   ALA A 623     4150   4316   3790   -424   -395    -87       O  
ATOM    434  CB  ALA A 623     -25.354 -17.939  36.633  1.00 26.83           C  
ANISOU  434  CB  ALA A 623     3398   3674   3122   -418   -461   -234       C  
ATOM    435  N   GLY A 624     -25.192 -14.891  37.520  1.00 27.01           N  
ANISOU  435  N   GLY A 624     3422   3827   3015   -444   -518   -128       N  
ATOM    436  CA  GLY A 624     -24.679 -13.881  38.427  1.00 27.23           C  
ANISOU  436  CA  GLY A 624     3482   3893   2972   -422   -525    -63       C  
ATOM    437  C   GLY A 624     -25.782 -13.038  39.035  1.00 28.66           C  
ANISOU  437  C   GLY A 624     3657   4039   3193   -456   -505    -31       C  
ATOM    438  O   GLY A 624     -25.710 -12.649  40.200  1.00 30.55           O  
ANISOU  438  O   GLY A 624     3938   4256   3413   -431   -472     26       O  
ATOM    439  N   ILE A 625     -26.808 -12.757  38.239  1.00 29.72           N  
ANISOU  439  N   ILE A 625     3738   4169   3387   -513   -527    -70       N  
ATOM    440  CA  ILE A 625     -27.951 -11.972  38.694  1.00 28.63           C  
ANISOU  440  CA  ILE A 625     3585   3996   3297   -550   -513    -49       C  
ATOM    441  C   ILE A 625     -28.809 -12.772  39.674  1.00 28.29           C  
ANISOU  441  C   ILE A 625     3576   3837   3334   -542   -425    -32       C  
ATOM    442  O   ILE A 625     -29.327 -12.229  40.650  1.00 27.23           O  
ANISOU  442  O   ILE A 625     3461   3672   3213   -543   -392     10       O  
ATOM    443  CB  ILE A 625     -28.810 -11.501  37.504  1.00 28.67           C  
ANISOU  443  CB  ILE A 625     3520   4025   3346   -616   -563    -99       C  
ATOM    444  CG1 ILE A 625     -27.997 -10.572  36.600  1.00 29.30           C  
ANISOU  444  CG1 ILE A 625     3565   4225   3343   -629   -654   -108       C  
ATOM    445  CG2 ILE A 625     -30.061 -10.790  37.985  1.00 27.12           C  
ANISOU  445  CG2 ILE A 625     3309   3784   3212   -654   -545    -83       C  
ATOM    446  CD1 ILE A 625     -28.773 -10.035  35.416  1.00 28.59           C  
ANISOU  446  CD1 ILE A 625     3424   4111   3328   -621   -650   -149       C  
ATOM    447  N   CYS A 626     -28.946 -14.067  39.407  1.00 30.27           N  
ANISOU  447  N   CYS A 626     3834   4027   3639   -534   -389    -66       N  
ATOM    448  CA  CYS A 626     -29.692 -14.958  40.285  1.00 32.93           C  
ANISOU  448  CA  CYS A 626     4205   4254   4053   -526   -307    -49       C  
ATOM    449  C   CYS A 626     -29.081 -14.979  41.684  1.00 35.81           C  
ANISOU  449  C   CYS A 626     4635   4599   4371   -476   -261     17       C  
ATOM    450  O   CYS A 626     -29.795 -14.894  42.683  1.00 37.68           O  
ANISOU  450  O   CYS A 626     4894   4777   4645   -481   -207     53       O  
ATOM    451  CB  CYS A 626     -29.728 -16.370  39.700  1.00 33.30           C  
ANISOU  451  CB  CYS A 626     4249   4247   4156   -520   -288    -96       C  
ATOM    452  SG  CYS A 626     -30.551 -17.595  40.738  1.00 50.70           S  
ANISOU  452  SG  CYS A 626     6495   6315   6454   -510   -192    -74       S  
ATOM    453  N   LEU A 627     -27.757 -15.084  41.748  1.00 37.59           N  
ANISOU  453  N   LEU A 627     4890   4876   4516   -430   -285     31       N  
ATOM    454  CA  LEU A 627     -27.053 -15.066  43.024  1.00 38.70           C  
ANISOU  454  CA  LEU A 627     5094   5005   4605   -381   -248     95       C  
ATOM    455  C   LEU A 627     -27.191 -13.703  43.690  1.00 35.81           C  
ANISOU  455  C   LEU A 627     4731   4681   4196   -388   -260    141       C  
ATOM    456  O   LEU A 627     -27.150 -13.593  44.915  1.00 36.98           O  
ANISOU  456  O   LEU A 627     4924   4796   4329   -363   -214    195       O  
ATOM    457  CB  LEU A 627     -25.573 -15.413  42.838  1.00 41.32           C  
ANISOU  457  CB  LEU A 627     5451   5389   4858   -332   -279     96       C  
ATOM    458  CG  LEU A 627     -25.251 -16.799  42.276  1.00 43.94           C  
ANISOU  458  CG  LEU A 627     5786   5683   5226   -315   -269     51       C  
ATOM    459  CD1 LEU A 627     -23.758 -17.068  42.346  1.00 45.11           C  
ANISOU  459  CD1 LEU A 627     5967   5879   5293   -261   -293     61       C  
ATOM    460  CD2 LEU A 627     -26.025 -17.880  43.012  1.00 45.19           C  
ANISOU  460  CD2 LEU A 627     5975   5724   5471   -314   -194     62       C  
ATOM    461  N   GLY A 628     -27.356 -12.669  42.871  1.00 32.22           N  
ANISOU  461  N   GLY A 628     4224   4297   3720   -423   -325    118       N  
ATOM    462  CA  GLY A 628     -27.553 -11.319  43.365  1.00 31.20           C  
ANISOU  462  CA  GLY A 628     4087   4209   3556   -434   -347    155       C  
ATOM    463  C   GLY A 628     -28.816 -11.203  44.195  1.00 31.35           C  
ANISOU  463  C   GLY A 628     4110   4154   3648   -458   -288    172       C  
ATOM    464  O   GLY A 628     -28.820 -10.567  45.248  1.00 32.18           O  
ANISOU  464  O   GLY A 628     4242   4258   3725   -441   -266    220       O  
ATOM    465  N   TYR A 629     -29.892 -11.822  43.720  1.00 28.65           N  
ANISOU  465  N   TYR A 629     3738   3750   3398   -497   -263    131       N  
ATOM    466  CA  TYR A 629     -31.140 -11.845  44.472  1.00 25.99           C  
ANISOU  466  CA  TYR A 629     3402   3337   3137   -522   -202    143       C  
ATOM    467  C   TYR A 629     -31.036 -12.797  45.659  1.00 25.66           C  
ANISOU  467  C   TYR A 629     3422   3222   3108   -485   -120    184       C  
ATOM    468  O   TYR A 629     -31.618 -12.550  46.716  1.00 25.20           O  
ANISOU  468  O   TYR A 629     3383   3124   3067   -486    -69    220       O  
ATOM    469  CB  TYR A 629     -32.319 -12.228  43.573  1.00 23.85           C  
ANISOU  469  CB  TYR A 629     3080   3022   2962   -576   -201     87       C  
ATOM    470  CG  TYR A 629     -32.621 -11.214  42.492  1.00 22.00           C  
ANISOU  470  CG  TYR A 629     2782   2852   2725   -621   -278     50       C  
ATOM    471  CD1 TYR A 629     -32.997  -9.916  42.815  1.00 21.11           C  
ANISOU  471  CD1 TYR A 629     2649   2775   2597   -640   -306     69       C  
ATOM    472  CD2 TYR A 629     -32.539 -11.556  41.149  1.00 20.87           C  
ANISOU  472  CD2 TYR A 629     2598   2734   2596   -645   -326     -4       C  
ATOM    473  CE1 TYR A 629     -33.276  -8.985  41.830  1.00 19.64           C  
ANISOU  473  CE1 TYR A 629     2405   2646   2412   -684   -381     38       C  
ATOM    474  CE2 TYR A 629     -32.817 -10.634  40.158  1.00 20.66           C  
ANISOU  474  CE2 TYR A 629     2514   2768   2567   -690   -399    -35       C  
ATOM    475  CZ  TYR A 629     -33.185  -9.350  40.503  1.00 21.69           C  
ANISOU  475  CZ  TYR A 629     2626   2930   2684   -710   -428    -13       C  
ATOM    476  OH  TYR A 629     -33.462  -8.431  39.516  1.00 21.44           O  
ANISOU  476  OH  TYR A 629     2538   2956   2653   -757   -505    -42       O  
ATOM    477  N   LEU A 630     -30.285 -13.881  45.483  1.00 24.81           N  
ANISOU  477  N   LEU A 630     3343   3095   2989   -453   -109    177       N  
ATOM    478  CA  LEU A 630     -30.074 -14.848  46.557  1.00 26.64           C  
ANISOU  478  CA  LEU A 630     3635   3258   3230   -418    -39    217       C  
ATOM    479  C   LEU A 630     -29.252 -14.257  47.698  1.00 29.04           C  
ANISOU  479  C   LEU A 630     3990   3593   3452   -375    -28    280       C  
ATOM    480  O   LEU A 630     -29.253 -14.786  48.809  1.00 31.92           O  
ANISOU  480  O   LEU A 630     4404   3902   3822   -352     34    324       O  
ATOM    481  CB  LEU A 630     -29.392 -16.111  46.028  1.00 24.97           C  
ANISOU  481  CB  LEU A 630     3439   3023   3027   -393    -41    190       C  
ATOM    482  CG  LEU A 630     -30.236 -17.034  45.149  1.00 24.62           C  
ANISOU  482  CG  LEU A 630     3357   2921   3076   -427    -32    134       C  
ATOM    483  CD1 LEU A 630     -29.410 -18.214  44.661  1.00 24.91           C  
ANISOU  483  CD1 LEU A 630     3410   2944   3112   -396    -41    107       C  
ATOM    484  CD2 LEU A 630     -31.463 -17.512  45.907  1.00 24.84           C  
ANISOU  484  CD2 LEU A 630     3394   2854   3190   -452     41    151       C  
ATOM    485  N   CYS A 631     -28.550 -13.162  47.417  1.00 28.63           N  
ANISOU  485  N   CYS A 631     3924   3631   3322   -365    -91    287       N  
ATOM    486  CA  CYS A 631     -27.728 -12.496  48.422  1.00 29.70           C  
ANISOU  486  CA  CYS A 631     4105   3804   3376   -324    -89    345       C  
ATOM    487  C   CYS A 631     -28.549 -11.996  49.604  1.00 30.17           C  
ANISOU  487  C   CYS A 631     4180   3827   3457   -333    -36    386       C  
ATOM    488  O   CYS A 631     -28.090 -12.035  50.743  1.00 32.39           O  
ANISOU  488  O   CYS A 631     4514   4094   3697   -297      2    439       O  
ATOM    489  CB  CYS A 631     -26.954 -11.327  47.807  1.00 30.31           C  
ANISOU  489  CB  CYS A 631     4157   3986   3374   -319   -173    342       C  
ATOM    490  SG  CYS A 631     -25.464 -11.795  46.905  1.00 43.11           S  
ANISOU  490  SG  CYS A 631     5785   5670   4927   -284   -229    321       S  
ATOM    491  N   THR A 632     -29.762 -11.527  49.331  1.00 30.63           N  
ANISOU  491  N   THR A 632     4190   3870   3577   -382    -35    359       N  
ATOM    492  CA  THR A 632     -30.611 -10.979  50.382  1.00 32.36           C  
ANISOU  492  CA  THR A 632     4415   4061   3819   -394     12    389       C  
ATOM    493  C   THR A 632     -31.056 -12.070  51.351  1.00 32.05           C  
ANISOU  493  C   THR A 632     4419   3932   3826   -387    102    416       C  
ATOM    494  O   THR A 632     -31.392 -11.789  52.500  1.00 32.90           O  
ANISOU  494  O   THR A 632     4552   4019   3928   -381    150    457       O  
ATOM    495  CB  THR A 632     -31.852 -10.267  49.811  1.00 35.31           C  
ANISOU  495  CB  THR A 632     4724   4436   4257   -451     -9    349       C  
ATOM    496  OG1 THR A 632     -32.878 -11.228  49.543  1.00 39.51           O  
ANISOU  496  OG1 THR A 632     5239   4889   4884   -485     38    318       O  
ATOM    497  CG2 THR A 632     -31.501  -9.521  48.535  1.00 35.84           C  
ANISOU  497  CG2 THR A 632     4741   4579   4297   -469   -101    311       C  
ATOM    498  N   PHE A 633     -31.048 -13.315  50.885  1.00 31.52           N  
ANISOU  498  N   PHE A 633     4358   3813   3804   -388    121    394       N  
ATOM    499  CA  PHE A 633     -31.413 -14.445  51.732  1.00 32.79           C  
ANISOU  499  CA  PHE A 633     4560   3887   4012   -383    200    420       C  
ATOM    500  C   PHE A 633     -30.281 -14.831  52.681  1.00 32.96           C  
ANISOU  500  C   PHE A 633     4651   3908   3965   -329    223    475       C  
ATOM    501  O   PHE A 633     -30.468 -15.643  53.585  1.00 34.16           O  
ANISOU  501  O   PHE A 633     4845   3995   4142   -321    288    510       O  
ATOM    502  CB  PHE A 633     -31.850 -15.643  50.884  1.00 34.97           C  
ANISOU  502  CB  PHE A 633     4817   4104   4367   -404    209    375       C  
ATOM    503  CG  PHE A 633     -33.153 -15.428  50.164  1.00 37.47           C  
ANISOU  503  CG  PHE A 633     5071   4400   4765   -460    205    327       C  
ATOM    504  CD1 PHE A 633     -34.358 -15.594  50.826  1.00 39.69           C  
ANISOU  504  CD1 PHE A 633     5348   4618   5115   -492    268    338       C  
ATOM    505  CD2 PHE A 633     -33.172 -15.055  48.831  1.00 37.79           C  
ANISOU  505  CD2 PHE A 633     5059   4485   4813   -483    138    272       C  
ATOM    506  CE1 PHE A 633     -35.558 -15.394  50.170  1.00 40.38           C  
ANISOU  506  CE1 PHE A 633     5378   4684   5279   -543    264    293       C  
ATOM    507  CE2 PHE A 633     -34.371 -14.854  48.170  1.00 38.70           C  
ANISOU  507  CE2 PHE A 633     5118   4579   5005   -536    132    228       C  
ATOM    508  CZ  PHE A 633     -35.564 -15.024  48.841  1.00 39.53           C  
ANISOU  508  CZ  PHE A 633     5220   4618   5180   -564    195    238       C  
HETATM  509  N   YCM A 634     -29.107 -14.245  52.469  1.00 33.55           N  
ANISOU  509  N   YCM A 634     4738   4056   3954   -294    168    485       N  
HETATM  510  CA  YCM A 634     -28.003 -14.411  53.384  1.00 35.51           C  
ANISOU  510  CA  YCM A 634     5050   4311   4130   -242    183    539       C  
HETATM  511  CB  YCM A 634     -26.666 -14.749  52.719  1.00 35.38           C  
ANISOU  511  CB  YCM A 634     5048   4336   4058   -204    131    527       C  
HETATM  512  SG  YCM A 634     -26.718 -15.315  51.044  1.00 73.75           S  
ANISOU  512  SG  YCM A 634     9853   9206   8962   -228     79    449       S  
HETATM  513  CD  YCM A 634     -27.210 -17.007  51.144  1.00 61.01           C  
ANISOU  513  CD  YCM A 634     8258   7483   7438   -234    139    437       C  
HETATM  514  CE  YCM A 634     -27.603 -17.621  49.816  1.00 59.91           C  
ANISOU  514  CE  YCM A 634     8069   7331   7361   -262    110    367       C  
HETATM  515  OZ1 YCM A 634     -28.767 -18.036  49.620  1.00 59.00           O  
ANISOU  515  OZ1 YCM A 634     7927   7159   7333   -302    141    344       O  
HETATM  516  NZ2 YCM A 634     -26.658 -17.720  48.830  1.00 59.03           N  
ANISOU  516  NZ2 YCM A 634     7943   7276   7210   -243     49    330       N  
HETATM  517  C   YCM A 634     -27.854 -13.196  54.296  1.00 36.03           C  
ANISOU  517  C   YCM A 634     5132   4426   4134   -227    182    584       C  
HETATM  518  O   YCM A 634     -27.300 -13.225  55.399  1.00 36.86           O  
ANISOU  518  O   YCM A 634     5292   4524   4191   -192    214    639       O  
ATOM    519  N   LEU A 635     -28.376 -12.080  53.798  1.00 34.25           N  
ANISOU  519  N   LEU A 635     4853   4249   3909   -256    140    558       N  
ATOM    520  CA  LEU A 635     -28.399 -10.833  54.550  1.00 34.94           C  
ANISOU  520  CA  LEU A 635     4944   4384   3950   -248    132    591       C  
ATOM    521  C   LEU A 635     -29.607 -10.813  55.481  1.00 38.96           C  
ANISOU  521  C   LEU A 635     5451   4838   4513   -275    202    606       C  
ATOM    522  O   LEU A 635     -29.597 -10.156  56.522  1.00 38.93           O  
ANISOU  522  O   LEU A 635     5470   4849   4472   -259    224    647       O  
ATOM    523  CB  LEU A 635     -28.437  -9.639  53.594  1.00 32.62           C  
ANISOU  523  CB  LEU A 635     4592   4166   3638   -269     50    556       C  
ATOM    524  CG  LEU A 635     -27.225  -9.499  52.667  1.00 31.03           C  
ANISOU  524  CG  LEU A 635     4386   4032   3372   -245    -25    543       C  
ATOM    525  CD1 LEU A 635     -27.490  -8.489  51.562  1.00 29.64           C  
ANISOU  525  CD1 LEU A 635     4144   3921   3198   -279   -103    502       C  
ATOM    526  CD2 LEU A 635     -25.984  -9.108  53.457  1.00 30.34           C  
ANISOU  526  CD2 LEU A 635     4352   3986   3190   -189    -36    597       C  
ATOM    527  N   ILE A 636     -30.646 -11.545  55.090  1.00 41.65           N  
ANISOU  527  N   ILE A 636     5764   5118   4943   -315    236    572       N  
ATOM    528  CA  ILE A 636     -31.853 -11.690  55.891  1.00 42.57           C  
ANISOU  528  CA  ILE A 636     5877   5178   5121   -345    306    582       C  
ATOM    529  C   ILE A 636     -32.054 -13.172  56.185  1.00 45.98           C  
ANISOU  529  C   ILE A 636     6342   5526   5603   -347    370    594       C  
ATOM    530  O   ILE A 636     -32.693 -13.886  55.410  1.00 47.79           O  
ANISOU  530  O   ILE A 636     6541   5710   5906   -379    375    553       O  
ATOM    531  CB  ILE A 636     -33.085 -11.144  55.139  1.00 41.86           C  
ANISOU  531  CB  ILE A 636     5716   5087   5101   -399    287    529       C  
ATOM    532  CG1 ILE A 636     -32.858  -9.688  54.729  1.00 40.03           C  
ANISOU  532  CG1 ILE A 636     5446   4938   4823   -400    212    515       C  
ATOM    533  CG2 ILE A 636     -34.342 -11.271  55.983  1.00 41.93           C  
ANISOU  533  CG2 ILE A 636     5719   5041   5173   -430    361    538       C  
ATOM    534  CD1 ILE A 636     -32.753  -8.733  55.897  1.00 39.44           C  
ANISOU  534  CD1 ILE A 636     5393   4896   4697   -379    227    558       C  
ATOM    535  N   ALA A 637     -31.493 -13.640  57.295  1.00 47.74           N  
ANISOU  535  N   ALA A 637     6627   5725   5787   -314    417    650       N  
ATOM    536  CA  ALA A 637     -31.531 -15.064  57.608  1.00 51.08           C  
ANISOU  536  CA  ALA A 637     7087   6070   6252   -313    470    667       C  
ATOM    537  C   ALA A 637     -31.315 -15.360  59.086  1.00 53.77           C  
ANISOU  537  C   ALA A 637     7488   6381   6559   -291    535    734       C  
ATOM    538  O   ALA A 637     -30.934 -14.482  59.864  1.00 51.26           O  
ANISOU  538  O   ALA A 637     7192   6110   6176   -268    534    770       O  
ATOM    539  CB  ALA A 637     -30.503 -15.815  56.771  1.00 51.16           C  
ANISOU  539  CB  ALA A 637     7111   6082   6246   -285    427    648       C  
ATOM    540  N   LYS A 638     -31.570 -16.612  59.458  1.00 58.60           N  
ANISOU  540  N   LYS A 638     8128   6916   7220   -299    588    752       N  
ATOM    541  CA  LYS A 638     -31.271 -17.102  60.796  1.00 61.94           C  
ANISOU  541  CA  LYS A 638     8615   7306   7615   -280    646    819       C  
ATOM    542  C   LYS A 638     -29.766 -17.025  61.019  1.00 62.83           C  
ANISOU  542  C   LYS A 638     8778   7455   7639   -224    611    851       C  
ATOM    543  O   LYS A 638     -28.988 -17.352  60.121  1.00 63.40           O  
ANISOU  543  O   LYS A 638     8848   7540   7702   -203    560    823       O  
ATOM    544  CB  LYS A 638     -31.758 -18.544  60.966  1.00 63.21           C  
ANISOU  544  CB  LYS A 638     8792   7374   7849   -301    697    828       C  
ATOM    545  CG  LYS A 638     -33.272 -18.709  60.974  1.00 63.45           C  
ANISOU  545  CG  LYS A 638     8780   7360   7966   -356    744    808       C  
ATOM    546  CD  LYS A 638     -33.659 -20.184  61.034  1.00 63.70           C  
ANISOU  546  CD  LYS A 638     8829   7302   8072   -375    785    817       C  
ATOM    547  CE  LYS A 638     -35.154 -20.356  61.283  1.00 63.25           C  
ANISOU  547  CE  LYS A 638     8737   7199   8094   -429    841    810       C  
ATOM    548  NZ  LYS A 638     -35.540 -21.796  61.322  1.00 63.39           N  
ANISOU  548  NZ  LYS A 638     8770   7128   8186   -449    877    821       N  
ATOM    549  N   PRO A 639     -29.350 -16.588  62.219  1.00 62.60           N  
ANISOU  549  N   PRO A 639     8795   7445   7546   -199    640    908       N  
ATOM    550  CA  PRO A 639     -27.931 -16.333  62.499  1.00 61.74           C  
ANISOU  550  CA  PRO A 639     8702   7395   7362   -145    582    918       C  
ATOM    551  C   PRO A 639     -27.069 -17.592  62.568  1.00 62.22           C  
ANISOU  551  C   PRO A 639     8804   7410   7427   -119    581    933       C  
ATOM    552  O   PRO A 639     -26.936 -18.200  63.629  1.00 62.50           O  
ANISOU  552  O   PRO A 639     8853   7424   7471   -113    603    956       O  
ATOM    553  CB  PRO A 639     -27.964 -15.638  63.863  1.00 62.05           C  
ANISOU  553  CB  PRO A 639     8717   7484   7376   -137    579    930       C  
ATOM    554  CG  PRO A 639     -29.217 -16.130  64.505  1.00 62.72           C  
ANISOU  554  CG  PRO A 639     8802   7510   7518   -177    653    945       C  
ATOM    555  CD  PRO A 639     -30.205 -16.274  63.379  1.00 62.68           C  
ANISOU  555  CD  PRO A 639     8790   7455   7570   -220    686    927       C  
ATOM    556  N   LYS A 640     -26.480 -17.964  61.437  1.00 63.39           N  
ANISOU  556  N   LYS A 640     8975   7545   7566   -105    554    919       N  
ATOM    557  CA  LYS A 640     -25.535 -19.071  61.388  1.00 65.28           C  
ANISOU  557  CA  LYS A 640     9254   7746   7803    -75    543    929       C  
ATOM    558  C   LYS A 640     -24.185 -18.543  60.920  1.00 66.21           C  
ANISOU  558  C   LYS A 640     9366   7941   7850    -29    468    909       C  
ATOM    559  O   LYS A 640     -24.094 -17.426  60.412  1.00 67.20           O  
ANISOU  559  O   LYS A 640     9457   8140   7937    -27    424    887       O  
ATOM    560  CB  LYS A 640     -26.034 -20.166  60.446  1.00 65.82           C  
ANISOU  560  CB  LYS A 640     9296   7754   7957   -101    542    882       C  
ATOM    561  CG  LYS A 640     -27.461 -20.612  60.722  1.00 66.83           C  
ANISOU  561  CG  LYS A 640     9402   7820   8171   -152    601    881       C  
ATOM    562  CD  LYS A 640     -27.819 -21.863  59.934  1.00 68.09           C  
ANISOU  562  CD  LYS A 640     9542   7912   8417   -171    599    841       C  
ATOM    563  CE  LYS A 640     -29.281 -22.238  60.132  1.00 69.90           C  
ANISOU  563  CE  LYS A 640     9743   8082   8732   -225    654    838       C  
ATOM    564  NZ  LYS A 640     -29.600 -23.578  59.549  1.00 71.14           N  
ANISOU  564  NZ  LYS A 640     9891   8162   8976   -241    657    810       N  
ATOM    565  N   GLN A 641     -23.140 -19.345  61.091  1.00 66.51           N  
ANISOU  565  N   GLN A 641     8691   9412   7166    -42     97   -831       N  
ATOM    566  CA  GLN A 641     -21.789 -18.911  60.750  1.00 64.62           C  
ANISOU  566  CA  GLN A 641     8441   9180   6931    -18     67   -821       C  
ATOM    567  C   GLN A 641     -21.562 -18.826  59.242  1.00 59.50           C  
ANISOU  567  C   GLN A 641     7712   8608   6285     10     86   -799       C  
ATOM    568  O   GLN A 641     -21.023 -17.837  58.744  1.00 57.76           O  
ANISOU  568  O   GLN A 641     7449   8431   6067     55     66   -791       O  
ATOM    569  CB  GLN A 641     -20.749 -19.839  61.384  1.00 66.86           C  
ANISOU  569  CB  GLN A 641     8797   9390   7218    -47     45   -821       C  
ATOM    570  CG  GLN A 641     -19.325 -19.335  61.248  1.00 68.93           C  
ANISOU  570  CG  GLN A 641     9053   9656   7482    -24      4   -813       C  
ATOM    571  CD  GLN A 641     -19.146 -17.956  61.847  1.00 71.08           C  
ANISOU  571  CD  GLN A 641     9328   9928   7753      5    -36   -822       C  
ATOM    572  OE1 GLN A 641     -18.804 -17.002  61.149  1.00 73.30           O  
ANISOU  572  OE1 GLN A 641     9553  10265   8032     53    -51   -810       O  
ATOM    573  NE2 GLN A 641     -19.382 -17.842  63.147  1.00 70.47           N  
ANISOU  573  NE2 GLN A 641     9320   9781   7675    -22    -55   -839       N  
ATOM    574  N   ILE A 642     -21.978 -19.861  58.520  1.00 56.92           N  
ANISOU  574  N   ILE A 642     7371   8296   5961    -15    121   -788       N  
ATOM    575  CA  ILE A 642     -21.705 -19.952  57.089  1.00 55.43           C  
ANISOU  575  CA  ILE A 642     7116   8167   5776      3    141   -765       C  
ATOM    576  C   ILE A 642     -22.455 -18.905  56.267  1.00 52.23           C  
ANISOU  576  C   ILE A 642     6631   7841   5372     41    150   -760       C  
ATOM    577  O   ILE A 642     -22.081 -18.619  55.133  1.00 50.48           O  
ANISOU  577  O   ILE A 642     6353   7670   5157     68    156   -740       O  
ATOM    578  CB  ILE A 642     -22.020 -21.356  56.534  1.00 55.88           C  
ANISOU  578  CB  ILE A 642     7186   8211   5833    -37    176   -753       C  
ATOM    579  CG1 ILE A 642     -23.529 -21.600  56.514  1.00 56.07           C  
ANISOU  579  CG1 ILE A 642     7195   8254   5853    -57    202   -760       C  
ATOM    580  CG2 ILE A 642     -21.307 -22.421  57.355  1.00 56.68           C  
ANISOU  580  CG2 ILE A 642     7372   8233   5932    -66    168   -757       C  
ATOM    581  CD1 ILE A 642     -23.929 -22.871  55.801  1.00 56.55           C  
ANISOU  581  CD1 ILE A 642     7262   8312   5913    -90    233   -744       C  
ATOM    582  N   TYR A 643     -23.511 -18.334  56.838  1.00 51.07           N  
ANISOU  582  N   TYR A 643     6481   7703   5220     44    152   -776       N  
ATOM    583  CA  TYR A 643     -24.260 -17.290  56.151  1.00 49.18           C  
ANISOU  583  CA  TYR A 643     6169   7539   4980     86    159   -772       C  
ATOM    584  C   TYR A 643     -23.440 -16.005  56.064  1.00 46.46           C  
ANISOU  584  C   TYR A 643     5805   7213   4635    146    128   -765       C  
ATOM    585  O   TYR A 643     -23.588 -15.228  55.122  1.00 46.17           O  
ANISOU  585  O   TYR A 643     5705   7239   4600    191    132   -750       O  
ATOM    586  CB  TYR A 643     -25.604 -17.041  56.834  1.00 49.79           C  
ANISOU  586  CB  TYR A 643     6249   7622   5047     77    171   -791       C  
ATOM    587  CG  TYR A 643     -26.705 -17.972  56.378  1.00 51.66           C  
ANISOU  587  CG  TYR A 643     6464   7882   5281     38    202   -790       C  
ATOM    588  CD1 TYR A 643     -26.662 -18.562  55.122  1.00 52.69           C  
ANISOU  588  CD1 TYR A 643     6552   8050   5418     28    220   -768       C  
ATOM    589  CD2 TYR A 643     -27.789 -18.257  57.199  1.00 52.71           C  
ANISOU  589  CD2 TYR A 643     6623   7999   5405     11    213   -809       C  
ATOM    590  CE1 TYR A 643     -27.666 -19.413  54.696  1.00 53.95           C  
ANISOU  590  CE1 TYR A 643     6695   8229   5573    -10    245   -766       C  
ATOM    591  CE2 TYR A 643     -28.798 -19.108  56.782  1.00 53.59           C  
ANISOU  591  CE2 TYR A 643     6715   8135   5513    -24    238   -807       C  
ATOM    592  CZ  TYR A 643     -28.731 -19.682  55.529  1.00 54.47           C  
ANISOU  592  CZ  TYR A 643     6785   8283   5630    -34    253   -786       C  
ATOM    593  OH  TYR A 643     -29.729 -20.529  55.105  1.00 55.74           O  
ANISOU  593  OH  TYR A 643     6929   8466   5784    -71    274   -783       O  
ATOM    594  N   CYS A 644     -22.572 -15.793  57.050  1.00 43.66           N  
ANISOU  594  N   CYS A 644     5510   6801   4277    147     95   -775       N  
ATOM    595  CA  CYS A 644     -21.611 -14.698  56.998  1.00 41.38           C  
ANISOU  595  CA  CYS A 644     5216   6520   3987    201     58   -765       C  
ATOM    596  C   CYS A 644     -20.620 -14.946  55.865  1.00 39.60           C  
ANISOU  596  C   CYS A 644     4953   6325   3769    219     56   -740       C  
ATOM    597  O   CYS A 644     -20.138 -14.009  55.230  1.00 38.50           O  
ANISOU  597  O   CYS A 644     4777   6209   3643    272     38   -714       O  
ATOM    598  CB  CYS A 644     -20.868 -14.563  58.329  1.00 40.43           C  
ANISOU  598  CB  CYS A 644     5174   6326   3861    188     17   -779       C  
ATOM    599  SG  CYS A 644     -21.883 -13.978  59.704  1.00 38.81           S  
ANISOU  599  SG  CYS A 644     5021   6080   3646    176     15   -806       S  
ATOM    600  N   TYR A 645     -20.322 -16.218  55.621  1.00 39.31           N  
ANISOU  600  N   TYR A 645     4930   6269   3739    174     74   -736       N  
ATOM    601  CA  TYR A 645     -19.472 -16.605  54.504  1.00 41.06           C  
ANISOU  601  CA  TYR A 645     5117   6517   3967    184     82   -711       C  
ATOM    602  C   TYR A 645     -20.206 -16.411  53.186  1.00 41.10           C  
ANISOU  602  C   TYR A 645     5049   6589   3980    200    116   -694       C  
ATOM    603  O   TYR A 645     -19.642 -15.901  52.219  1.00 43.24           O  
ANISOU  603  O   TYR A 645     5275   6899   4256    241    112   -672       O  
ATOM    604  CB  TYR A 645     -19.042 -18.066  54.630  1.00 43.74           C  
ANISOU  604  CB  TYR A 645     5499   6812   4308    131     98   -711       C  
ATOM    605  CG  TYR A 645     -17.808 -18.289  55.471  1.00 47.23           C  
ANISOU  605  CG  TYR A 645     5997   7198   4750    127     59   -713       C  
ATOM    606  CD1 TYR A 645     -16.541 -18.197  54.912  1.00 47.76           C  
ANISOU  606  CD1 TYR A 645     6046   7214   4886    149     35   -654       C  
ATOM    607  CD2 TYR A 645     -17.909 -18.607  56.819  1.00 48.15           C  
ANISOU  607  CD2 TYR A 645     6184   7252   4856     93     40   -740       C  
ATOM    608  CE1 TYR A 645     -15.409 -18.406  55.671  1.00 48.81           C  
ANISOU  608  CE1 TYR A 645     6226   7256   5065    141     -6   -627       C  
ATOM    609  CE2 TYR A 645     -16.781 -18.818  57.587  1.00 48.69           C  
ANISOU  609  CE2 TYR A 645     6305   7237   4959     84     -2   -721       C  
ATOM    610  CZ  TYR A 645     -15.534 -18.717  57.008  1.00 50.21           C  
ANISOU  610  CZ  TYR A 645     6473   7387   5219    109    -25   -659       C  
ATOM    611  OH  TYR A 645     -14.404 -18.925  57.765  1.00 53.15           O  
ANISOU  611  OH  TYR A 645     6890   7669   5636    100    -68   -630       O  
ATOM    612  N   LEU A 646     -21.469 -16.827  53.155  1.00 38.77           N  
ANISOU  612  N   LEU A 646     4743   6303   3683    168    145   -703       N  
ATOM    613  CA  LEU A 646     -22.274 -16.747  51.943  1.00 36.82           C  
ANISOU  613  CA  LEU A 646     4429   6117   3442    174    172   -687       C  
ATOM    614  C   LEU A 646     -22.555 -15.306  51.529  1.00 33.82           C  
ANISOU  614  C   LEU A 646     3997   5792   3062    239    159   -681       C  
ATOM    615  O   LEU A 646     -22.693 -15.014  50.342  1.00 32.67           O  
ANISOU  615  O   LEU A 646     3793   5695   2924    261    170   -661       O  
ATOM    616  CB  LEU A 646     -23.588 -17.511  52.115  1.00 37.15           C  
ANISOU  616  CB  LEU A 646     4477   6158   3479    126    199   -699       C  
ATOM    617  CG  LEU A 646     -23.474 -19.028  52.272  1.00 36.76           C  
ANISOU  617  CG  LEU A 646     4479   6057   3429     64    218   -699       C  
ATOM    618  CD1 LEU A 646     -24.852 -19.657  52.272  1.00 38.63           C  
ANISOU  618  CD1 LEU A 646     4713   6304   3660     25    242   -706       C  
ATOM    619  CD2 LEU A 646     -22.606 -19.628  51.175  1.00 35.92           C  
ANISOU  619  CD2 LEU A 646     4360   5956   3333     59    232   -672       C  
ATOM    620  N   GLN A 647     -22.645 -14.413  52.509  1.00 32.30           N  
ANISOU  620  N   GLN A 647     3829   5584   2859    269    135   -697       N  
ATOM    621  CA  GLN A 647     -22.851 -12.995  52.236  1.00 32.34           C  
ANISOU  621  CA  GLN A 647     3798   5630   2860    337    122   -690       C  
ATOM    622  C   GLN A 647     -21.702 -12.424  51.419  1.00 31.59           C  
ANISOU  622  C   GLN A 647     3681   5549   2771    384    104   -665       C  
ATOM    623  O   GLN A 647     -21.904 -11.864  50.343  1.00 29.61           O  
ANISOU  623  O   GLN A 647     3375   5347   2527    421    114   -646       O  
ATOM    624  CB  GLN A 647     -22.972 -12.208  53.540  1.00 32.35           C  
ANISOU  624  CB  GLN A 647     3849   5596   2847    357     98   -710       C  
ATOM    625  CG  GLN A 647     -24.318 -12.318  54.223  1.00 34.94           C  
ANISOU  625  CG  GLN A 647     4183   5927   3167    332    118   -732       C  
ATOM    626  CD  GLN A 647     -24.393 -11.470  55.473  1.00 36.28           C  
ANISOU  626  CD  GLN A 647     4406   6058   3323    354     97   -749       C  
ATOM    627  OE1 GLN A 647     -23.441 -10.771  55.818  1.00 37.38           O  
ANISOU  627  OE1 GLN A 647     4578   6167   3457    388     65   -742       O  
ATOM    628  NE2 GLN A 647     -25.528 -11.524  56.159  1.00 35.79           N  
ANISOU  628  NE2 GLN A 647     4354   5994   3252    333    114   -769       N  
ATOM    629  N   ARG A 648     -20.495 -12.574  51.948  1.00 32.99           N  
ANISOU  629  N   ARG A 648     3905   5653   2976    376     73   -650       N  
ATOM    630  CA  ARG A 648     -19.301 -12.014  51.333  1.00 34.47           C  
ANISOU  630  CA  ARG A 648     4080   5783   3233    405     42   -594       C  
ATOM    631  C   ARG A 648     -18.966 -12.679  50.003  1.00 33.75           C  
ANISOU  631  C   ARG A 648     3943   5726   3154    395     68   -575       C  
ATOM    632  O   ARG A 648     -18.533 -12.018  49.060  1.00 34.59           O  
ANISOU  632  O   ARG A 648     4012   5831   3299    430     60   -540       O  
ATOM    633  CB  ARG A 648     -18.128 -12.116  52.308  1.00 36.01           C  
ANISOU  633  CB  ARG A 648     4335   5872   3475    386     -1   -572       C  
ATOM    634  CG  ARG A 648     -18.399 -11.405  53.625  1.00 38.95           C  
ANISOU  634  CG  ARG A 648     4760   6202   3838    392    -28   -586       C  
ATOM    635  CD  ARG A 648     -17.368 -11.742  54.686  1.00 43.07           C  
ANISOU  635  CD  ARG A 648     5345   6625   4394    360    -67   -571       C  
ATOM    636  NE  ARG A 648     -16.008 -11.567  54.188  1.00 45.63           N  
ANISOU  636  NE  ARG A 648     5660   6895   4785    370    -98   -515       N  
ATOM    637  CZ  ARG A 648     -14.924 -11.543  54.957  1.00 45.63           C  
ANISOU  637  CZ  ARG A 648     5704   6808   4827    354   -141   -486       C  
ATOM    638  NH1 ARG A 648     -15.032 -11.672  56.273  1.00 43.80           N  
ANISOU  638  NH1 ARG A 648     5534   6528   4578    325   -160   -506       N  
ATOM    639  NH2 ARG A 648     -13.729 -11.383  54.405  1.00 46.73           N  
ANISOU  639  NH2 ARG A 648     5824   6907   5023    365   -166   -435       N  
ATOM    640  N   ILE A 649     -19.180 -13.986  49.923  1.00 34.13           N  
ANISOU  640  N   ILE A 649     3999   5802   3165    345    102   -600       N  
ATOM    641  CA  ILE A 649     -18.872 -14.718  48.703  1.00 37.02           C  
ANISOU  641  CA  ILE A 649     4332   6196   3538    328    133   -581       C  
ATOM    642  C   ILE A 649     -19.948 -14.454  47.652  1.00 35.59           C  
ANISOU  642  C   ILE A 649     4091   6106   3327    341    166   -589       C  
ATOM    643  O   ILE A 649     -19.764 -14.740  46.469  1.00 37.08           O  
ANISOU  643  O   ILE A 649     4244   6316   3531    335    187   -566       O  
ATOM    644  CB  ILE A 649     -18.726 -16.231  48.979  1.00 41.27           C  
ANISOU  644  CB  ILE A 649     4909   6727   4044    268    160   -601       C  
ATOM    645  CG1 ILE A 649     -17.619 -16.836  48.115  1.00 44.75           C  
ANISOU  645  CG1 ILE A 649     5343   7129   4530    260    168   -559       C  
ATOM    646  CG2 ILE A 649     -20.046 -16.958  48.773  1.00 41.88           C  
ANISOU  646  CG2 ILE A 649     4979   6819   4114    219    194   -612       C  
ATOM    647  CD1 ILE A 649     -17.346 -18.289  48.429  1.00 46.26           C  
ANISOU  647  CD1 ILE A 649     5584   7302   4692    207    194   -573       C  
ATOM    648  N   GLY A 650     -21.067 -13.889  48.093  1.00 34.53           N  
ANISOU  648  N   GLY A 650     3946   5990   3183    350    162   -606       N  
ATOM    649  CA  GLY A 650     -22.181 -13.613  47.207  1.00 33.22           C  
ANISOU  649  CA  GLY A 650     3726   5876   3022    354    179   -598       C  
ATOM    650  C   GLY A 650     -22.176 -12.184  46.705  1.00 32.75           C  
ANISOU  650  C   GLY A 650     3627   5853   2963    428    164   -585       C  
ATOM    651  O   GLY A 650     -22.298 -11.938  45.508  1.00 33.47           O  
ANISOU  651  O   GLY A 650     3670   5980   3066    444    173   -564       O  
ATOM    652  N   ILE A 651     -22.038 -11.238  47.627  1.00 32.08           N  
ANISOU  652  N   ILE A 651     3570   5754   2866    473    139   -597       N  
ATOM    653  CA  ILE A 651     -22.010  -9.822  47.278  1.00 32.08           C  
ANISOU  653  CA  ILE A 651     3548   5776   2864    547    123   -585       C  
ATOM    654  C   ILE A 651     -20.775  -9.488  46.437  1.00 33.24           C  
ANISOU  654  C   ILE A 651     3688   5863   3080    563    100   -536       C  
ATOM    655  O   ILE A 651     -20.774  -8.532  45.660  1.00 34.83           O  
ANISOU  655  O   ILE A 651     3860   6077   3298    610     93   -515       O  
ATOM    656  CB  ILE A 651     -22.067  -8.943  48.544  1.00 32.20           C  
ANISOU  656  CB  ILE A 651     3612   5740   2882    576     94   -591       C  
ATOM    657  CG1 ILE A 651     -23.315  -9.285  49.361  1.00 33.88           C  
ANISOU  657  CG1 ILE A 651     3831   5982   3059    550    113   -626       C  
ATOM    658  CG2 ILE A 651     -22.085  -7.469  48.185  1.00 32.09           C  
ANISOU  658  CG2 ILE A 651     3585   5720   2887    646     75   -565       C  
ATOM    659  CD1 ILE A 651     -23.365  -8.621  50.716  1.00 32.66           C  
ANISOU  659  CD1 ILE A 651     3735   5789   2886    570     93   -644       C  
ATOM    660  N   GLY A 652     -19.730 -10.295  46.578  1.00 31.76           N  
ANISOU  660  N   GLY A 652     3528   5611   2928    523     91   -520       N  
ATOM    661  CA  GLY A 652     -18.515 -10.089  45.815  1.00 28.35           C  
ANISOU  661  CA  GLY A 652     3088   5122   2561    532     71   -475       C  
ATOM    662  C   GLY A 652     -18.543 -10.746  44.449  1.00 26.87           C  
ANISOU  662  C   GLY A 652     2855   4982   2373    514    107   -466       C  
ATOM    663  O   GLY A 652     -18.229 -10.112  43.442  1.00 26.14           O  
ANISOU  663  O   GLY A 652     2731   4889   2311    544    102   -440       O  
ATOM    664  N   LEU A 653     -18.927 -12.019  44.410  1.00 28.40           N  
ANISOU  664  N   LEU A 653     3050   5214   2528    463    144   -488       N  
ATOM    665  CA  LEU A 653     -18.858 -12.799  43.175  1.00 31.63           C  
ANISOU  665  CA  LEU A 653     3427   5657   2934    434    181   -477       C  
ATOM    666  C   LEU A 653     -20.015 -12.572  42.204  1.00 27.54           C  
ANISOU  666  C   LEU A 653     2857   5230   2377    441    209   -488       C  
ATOM    667  O   LEU A 653     -19.832 -12.685  40.993  1.00 26.56           O  
ANISOU  667  O   LEU A 653     2703   5115   2274    435    225   -464       O  
ATOM    668  CB  LEU A 653     -18.727 -14.295  43.478  1.00 36.12           C  
ANISOU  668  CB  LEU A 653     4028   6221   3475    372    211   -491       C  
ATOM    669  CG  LEU A 653     -17.356 -14.794  43.935  1.00 40.55           C  
ANISOU  669  CG  LEU A 653     4632   6684   4091    357    189   -464       C  
ATOM    670  CD1 LEU A 653     -17.376 -16.305  44.108  1.00 43.23           C  
ANISOU  670  CD1 LEU A 653     5005   7030   4391    299    228   -481       C  
ATOM    671  CD2 LEU A 653     -16.264 -14.375  42.957  1.00 39.49           C  
ANISOU  671  CD2 LEU A 653     4475   6502   4028    380    176   -415       C  
ATOM    672  N   SER A 654     -21.201 -12.267  42.725  1.00 25.25           N  
ANISOU  672  N   SER A 654     2562   4963   2069    442    201   -507       N  
ATOM    673  CA  SER A 654     -22.369 -12.086  41.860  1.00 24.51           C  
ANISOU  673  CA  SER A 654     2424   4914   1974    436    207   -500       C  
ATOM    674  C   SER A 654     -22.239 -10.948  40.834  1.00 23.37           C  
ANISOU  674  C   SER A 654     2239   4798   1844    495    198   -480       C  
ATOM    675  O   SER A 654     -22.603 -11.132  39.673  1.00 22.58           O  
ANISOU  675  O   SER A 654     2107   4720   1753    476    209   -462       O  
ATOM    676  CB  SER A 654     -23.677 -11.992  42.660  1.00 26.96           C  
ANISOU  676  CB  SER A 654     2733   5248   2261    428    202   -524       C  
ATOM    677  OG  SER A 654     -23.560 -11.127  43.776  1.00 31.93           O  
ANISOU  677  OG  SER A 654     3387   5867   2879    476    183   -541       O  
ATOM    678  N   PRO A 655     -21.721  -9.774  41.245  1.00 22.57           N  
ANISOU  678  N   PRO A 655     2144   4690   1741    564    179   -481       N  
ATOM    679  CA  PRO A 655     -21.458  -8.797  40.183  1.00 22.47           C  
ANISOU  679  CA  PRO A 655     2099   4693   1747    616    173   -460       C  
ATOM    680  C   PRO A 655     -20.292  -9.249  39.312  1.00 25.17           C  
ANISOU  680  C   PRO A 655     2440   4992   2133    594    180   -433       C  
ATOM    681  O   PRO A 655     -20.294  -9.010  38.104  1.00 28.61           O  
ANISOU  681  O   PRO A 655     2842   5449   2580    603    191   -416       O  
ATOM    682  CB  PRO A 655     -21.078  -7.529  40.956  1.00 21.03           C  
ANISOU  682  CB  PRO A 655     1946   4465   1580    678    137   -456       C  
ATOM    683  CG  PRO A 655     -21.652  -7.722  42.321  1.00 20.58           C  
ANISOU  683  CG  PRO A 655     1918   4417   1484    670    136   -487       C  
ATOM    684  CD  PRO A 655     -21.517  -9.188  42.581  1.00 21.39           C  
ANISOU  684  CD  PRO A 655     2033   4520   1573    600    159   -501       C  
ATOM    685  N   ALA A 656     -19.313  -9.909  39.924  1.00 23.84           N  
ANISOU  685  N   ALA A 656     2311   4749   1998    562    170   -422       N  
ATOM    686  CA  ALA A 656     -18.144 -10.395  39.196  1.00 23.37           C  
ANISOU  686  CA  ALA A 656     2256   4629   1993    537    172   -390       C  
ATOM    687  C   ALA A 656     -18.533 -11.365  38.084  1.00 24.45           C  
ANISOU  687  C   ALA A 656     2364   4822   2104    493    221   -390       C  
ATOM    688  O   ALA A 656     -17.950 -11.344  37.006  1.00 25.12           O  
ANISOU  688  O   ALA A 656     2433   4884   2227    490    228   -363       O  
ATOM    689  CB  ALA A 656     -17.151 -11.044  40.150  1.00 22.77           C  
ANISOU  689  CB  ALA A 656     2227   4476   1949    510    155   -381       C  
ATOM    690  N   MET A 657     -19.524 -12.209  38.346  1.00 26.16           N  
ANISOU  690  N   MET A 657     2583   5085   2271    449    245   -414       N  
ATOM    691  CA  MET A 657     -19.987 -13.163  37.344  1.00 29.95           C  
ANISOU  691  CA  MET A 657     3057   5566   2756    386    268   -398       C  
ATOM    692  C   MET A 657     -20.693 -12.466  36.182  1.00 30.73           C  
ANISOU  692  C   MET A 657     3115   5699   2860    402    262   -386       C  
ATOM    693  O   MET A 657     -20.612 -12.912  35.037  1.00 31.47           O  
ANISOU  693  O   MET A 657     3202   5784   2970    368    279   -364       O  
ATOM    694  CB  MET A 657     -20.911 -14.205  37.976  1.00 33.07           C  
ANISOU  694  CB  MET A 657     3479   5961   3125    326    276   -417       C  
ATOM    695  CG  MET A 657     -20.209 -15.160  38.928  1.00 36.46           C  
ANISOU  695  CG  MET A 657     3957   6346   3549    295    287   -426       C  
ATOM    696  SD  MET A 657     -21.373 -16.189  39.839  1.00 47.95           S  
ANISOU  696  SD  MET A 657     5447   7796   4976    234    292   -453       S  
ATOM    697  CE  MET A 657     -22.293 -16.931  38.494  1.00 38.88           C  
ANISOU  697  CE  MET A 657     4283   6661   3828    177    314   -434       C  
ATOM    698  N   SER A 658     -21.378 -11.367  36.477  1.00 29.41           N  
ANISOU  698  N   SER A 658     2927   5569   2678    454    237   -398       N  
ATOM    699  CA  SER A 658     -22.126 -10.647  35.453  1.00 32.53           C  
ANISOU  699  CA  SER A 658     3285   6002   3072    475    228   -387       C  
ATOM    700  C   SER A 658     -21.248  -9.725  34.609  1.00 33.64           C  
ANISOU  700  C   SER A 658     3411   6127   3244    524    222   -368       C  
ATOM    701  O   SER A 658     -21.250  -9.810  33.382  1.00 32.40           O  
ANISOU  701  O   SER A 658     3239   5970   3103    505    231   -349       O  
ATOM    702  CB  SER A 658     -23.281  -9.858  36.077  1.00 34.47           C  
ANISOU  702  CB  SER A 658     3515   6296   3288    513    207   -406       C  
ATOM    703  OG  SER A 658     -24.285 -10.730  36.568  1.00 34.58           O  
ANISOU  703  OG  SER A 658     3532   6330   3278    460    214   -421       O  
ATOM    704  N   TYR A 659     -20.494  -8.851  35.268  1.00 36.67           N  
ANISOU  704  N   TYR A 659     3803   6492   3638    586    208   -374       N  
ATOM    705  CA  TYR A 659     -19.708  -7.842  34.562  1.00 36.90           C  
ANISOU  705  CA  TYR A 659     3818   6502   3700    639    199   -359       C  
ATOM    706  C   TYR A 659     -18.463  -8.399  33.872  1.00 35.81           C  
ANISOU  706  C   TYR A 659     3694   6290   3623    603    204   -329       C  
ATOM    707  O   TYR A 659     -18.097  -7.941  32.789  1.00 35.57           O  
ANISOU  707  O   TYR A 659     3649   6241   3624    614    202   -311       O  
ATOM    708  CB  TYR A 659     -19.331  -6.693  35.501  1.00 37.15           C  
ANISOU  708  CB  TYR A 659     3882   6481   3753    696    154   -358       C  
ATOM    709  CG  TYR A 659     -20.527  -6.000  36.114  1.00 37.18           C  
ANISOU  709  CG  TYR A 659     3875   6551   3701    742    150   -383       C  
ATOM    710  CD1 TYR A 659     -21.359  -5.200  35.345  1.00 38.28           C  
ANISOU  710  CD1 TYR A 659     3986   6737   3821    779    146   -382       C  
ATOM    711  CD2 TYR A 659     -20.821  -6.144  37.463  1.00 37.89           C  
ANISOU  711  CD2 TYR A 659     3992   6640   3765    741    143   -403       C  
ATOM    712  CE1 TYR A 659     -22.454  -4.566  35.901  1.00 40.00           C  
ANISOU  712  CE1 TYR A 659     4204   6993   4003    813    133   -394       C  
ATOM    713  CE2 TYR A 659     -21.912  -5.516  38.028  1.00 38.72           C  
ANISOU  713  CE2 TYR A 659     4090   6797   3824    781    140   -423       C  
ATOM    714  CZ  TYR A 659     -22.725  -4.728  37.245  1.00 40.41           C  
ANISOU  714  CZ  TYR A 659     4278   7046   4031    814    131   -414       C  
ATOM    715  OH  TYR A 659     -23.813  -4.101  37.806  1.00 42.37           O  
ANISOU  715  OH  TYR A 659     4523   7327   4247    848    120   -425       O  
ATOM    716  N   SER A 660     -17.813  -9.383  34.488  1.00 35.89           N  
ANISOU  716  N   SER A 660     3732   6257   3648    561    212   -325       N  
ATOM    717  CA  SER A 660     -16.599  -9.952  33.904  1.00 39.32           C  
ANISOU  717  CA  SER A 660     4179   6620   4140    529    219   -295       C  
ATOM    718  C   SER A 660     -16.910 -10.845  32.705  1.00 39.78           C  
ANISOU  718  C   SER A 660     4216   6719   4181    481    269   -288       C  
ATOM    719  O   SER A 660     -16.029 -11.154  31.905  1.00 42.22           O  
ANISOU  719  O   SER A 660     4529   6975   4537    460    281   -261       O  
ATOM    720  CB  SER A 660     -15.781 -10.718  34.945  1.00 41.03           C  
ANISOU  720  CB  SER A 660     4435   6777   4378    504    212   -289       C  
ATOM    721  OG  SER A 660     -16.464 -11.879  35.380  1.00 43.39           O  
ANISOU  721  OG  SER A 660     4741   7124   4620    459    248   -311       O  
ATOM    722  N   ALA A 661     -18.166 -11.261  32.589  1.00 38.68           N  
ANISOU  722  N   ALA A 661     4068   6642   3987    452    285   -305       N  
ATOM    723  CA  ALA A 661     -18.618 -11.992  31.414  1.00 37.67           C  
ANISOU  723  CA  ALA A 661     3942   6511   3859    392    306   -288       C  
ATOM    724  C   ALA A 661     -19.117 -10.992  30.381  1.00 38.95           C  
ANISOU  724  C   ALA A 661     4075   6697   4027    421    290   -282       C  
ATOM    725  O   ALA A 661     -19.089 -11.250  29.178  1.00 39.69           O  
ANISOU  725  O   ALA A 661     4166   6777   4137    388    306   -263       O  
ATOM    726  CB  ALA A 661     -19.719 -12.969  31.784  1.00 36.44           C  
ANISOU  726  CB  ALA A 661     3805   6377   3664    335    313   -301       C  
ATOM    727  N   LEU A 662     -19.568  -9.841  30.868  1.00 38.30           N  
ANISOU  727  N   LEU A 662     3975   6648   3929    484    260   -298       N  
ATOM    728  CA  LEU A 662     -20.061  -8.782  30.001  1.00 37.21           C  
ANISOU  728  CA  LEU A 662     3814   6534   3791    522    242   -294       C  
ATOM    729  C   LEU A 662     -18.911  -8.003  29.367  1.00 39.51           C  
ANISOU  729  C   LEU A 662     4100   6781   4131    562    239   -280       C  
ATOM    730  O   LEU A 662     -19.048  -7.478  28.263  1.00 41.84           O  
ANISOU  730  O   LEU A 662     4383   7076   4437    570    235   -269       O  
ATOM    731  CB  LEU A 662     -20.987  -7.842  30.779  1.00 34.86           C  
ANISOU  731  CB  LEU A 662     3506   6283   3458    578    213   -314       C  
ATOM    732  CG  LEU A 662     -21.708  -6.750  29.988  1.00 32.81           C  
ANISOU  732  CG  LEU A 662     3224   6056   3185    621    194   -311       C  
ATOM    733  CD1 LEU A 662     -22.513  -7.355  28.848  1.00 33.57           C  
ANISOU  733  CD1 LEU A 662     3305   6181   3270    565    205   -299       C  
ATOM    734  CD2 LEU A 662     -22.606  -5.934  30.902  1.00 30.75           C  
ANISOU  734  CD2 LEU A 662     2958   5839   2888    676    170   -329       C  
ATOM    735  N   VAL A 663     -17.775  -7.933  30.058  1.00 39.98           N  
ANISOU  735  N   VAL A 663     4169   6799   4224    586    236   -278       N  
ATOM    736  CA  VAL A 663     -16.616  -7.228  29.516  1.00 40.34           C  
ANISOU  736  CA  VAL A 663     4231   6759   4337    606    210   -256       C  
ATOM    737  C   VAL A 663     -16.030  -7.963  28.312  1.00 40.57           C  
ANISOU  737  C   VAL A 663     4256   6759   4401    555    243   -234       C  
ATOM    738  O   VAL A 663     -15.629  -7.336  27.334  1.00 41.88           O  
ANISOU  738  O   VAL A 663     4418   6892   4601    567    235   -222       O  
ATOM    739  CB  VAL A 663     -15.524  -6.950  30.588  1.00 32.98           C  
ANISOU  739  CB  VAL A 663     3336   5745   3449    623    174   -247       C  
ATOM    740  CG1 VAL A 663     -14.956  -8.241  31.146  1.00 33.83           C  
ANISOU  740  CG1 VAL A 663     3460   5824   3570    572    194   -238       C  
ATOM    741  CG2 VAL A 663     -14.417  -6.078  30.011  1.00 33.06           C  
ANISOU  741  CG2 VAL A 663     3361   5678   3522    645    145   -226       C  
ATOM    742  N   THR A 664     -16.009  -9.291  28.375  1.00 39.85           N  
ANISOU  742  N   THR A 664     4169   6677   4297    497    282   -229       N  
ATOM    743  CA  THR A 664     -15.506 -10.096  27.269  1.00 41.13           C  
ANISOU  743  CA  THR A 664     4333   6810   4485    445    321   -206       C  
ATOM    744  C   THR A 664     -16.441  -9.983  26.070  1.00 40.87           C  
ANISOU  744  C   THR A 664     4292   6808   4430    420    329   -204       C  
ATOM    745  O   THR A 664     -16.004 -10.029  24.921  1.00 39.84           O  
ANISOU  745  O   THR A 664     4162   6643   4332    398    345   -185       O  
ATOM    746  CB  THR A 664     -15.361 -11.577  27.665  1.00 41.77           C  
ANISOU  746  CB  THR A 664     4435   6885   4549    386    359   -200       C  
ATOM    747  OG1 THR A 664     -16.659 -12.153  27.857  1.00 43.07           O  
ANISOU  747  OG1 THR A 664     4616   7090   4659    346    360   -214       O  
ATOM    748  CG2 THR A 664     -14.555 -11.709  28.947  1.00 41.45           C  
ANISOU  748  CG2 THR A 664     4421   6794   4535    403    334   -199       C  
ATOM    749  N   LYS A 665     -17.731  -9.834  26.350  1.00 41.17           N  
ANISOU  749  N   LYS A 665     4325   6901   4416    422    312   -221       N  
ATOM    750  CA  LYS A 665     -18.728  -9.647  25.305  1.00 40.63           C  
ANISOU  750  CA  LYS A 665     4247   6864   4326    402    309   -217       C  
ATOM    751  C   LYS A 665     -18.530  -8.305  24.607  1.00 40.42           C  
ANISOU  751  C   LYS A 665     4203   6836   4320    460    287   -217       C  
ATOM    752  O   LYS A 665     -18.571  -8.219  23.380  1.00 39.70           O  
ANISOU  752  O   LYS A 665     4109   6732   4242    438    297   -205       O  
ATOM    753  CB  LYS A 665     -20.137  -9.738  25.894  1.00 42.44           C  
ANISOU  753  CB  LYS A 665     4468   7157   4498    398    293   -235       C  
ATOM    754  CG  LYS A 665     -21.224  -9.144  25.011  1.00 43.93           C  
ANISOU  754  CG  LYS A 665     4635   7395   4662    406    277   -234       C  
ATOM    755  CD  LYS A 665     -22.590  -9.257  25.666  1.00 44.71           C  
ANISOU  755  CD  LYS A 665     4719   7560   4709    404    261   -250       C  
ATOM    756  CE  LYS A 665     -23.213 -10.617  25.411  1.00 46.10           C  
ANISOU  756  CE  LYS A 665     4907   7742   4869    320    282   -244       C  
ATOM    757  NZ  LYS A 665     -23.577 -10.784  23.976  1.00 47.02           N  
ANISOU  757  NZ  LYS A 665     5019   7861   4987    281    292   -226       N  
ATOM    758  N   THR A 666     -18.309  -7.261  25.400  1.00 41.19           N  
ANISOU  758  N   THR A 666     4292   6939   4419    532    258   -232       N  
ATOM    759  CA  THR A 666     -18.107  -5.918  24.864  1.00 41.15           C  
ANISOU  759  CA  THR A 666     4278   6924   4432    593    233   -235       C  
ATOM    760  C   THR A 666     -16.735  -5.760  24.209  1.00 43.94           C  
ANISOU  760  C   THR A 666     4635   7210   4850    595    241   -222       C  
ATOM    761  O   THR A 666     -16.606  -5.087  23.187  1.00 45.47           O  
ANISOU  761  O   THR A 666     4827   7388   5063    609    235   -218       O  
ATOM    762  CB  THR A 666     -18.278  -4.843  25.953  1.00 38.90           C  
ANISOU  762  CB  THR A 666     3994   6657   4128    671    199   -254       C  
ATOM    763  OG1 THR A 666     -17.380  -5.111  27.038  1.00 37.74           O  
ANISOU  763  OG1 THR A 666     3863   6471   4008    677    194   -255       O  
ATOM    764  CG2 THR A 666     -19.707  -4.834  26.473  1.00 38.11           C  
ANISOU  764  CG2 THR A 666     3888   6627   3967    676    189   -268       C  
ATOM    765  N   TYR A 667     -15.716  -6.375  24.803  1.00 44.10           N  
ANISOU  765  N   TYR A 667     4676   7168   4910    571    244   -209       N  
ATOM    766  CA  TYR A 667     -14.364  -6.329  24.253  1.00 45.39           C  
ANISOU  766  CA  TYR A 667     4863   7237   5147    555    239   -188       C  
ATOM    767  C   TYR A 667     -14.317  -6.996  22.883  1.00 45.30           C  
ANISOU  767  C   TYR A 667     4844   7220   5150    501    281   -173       C  
ATOM    768  O   TYR A 667     -13.633  -6.523  21.976  1.00 45.69           O  
ANISOU  768  O   TYR A 667     4904   7212   5246    500    275   -162       O  
ATOM    769  CB  TYR A 667     -13.368  -7.000  25.204  1.00 48.21           C  
ANISOU  769  CB  TYR A 667     5242   7536   5539    538    236   -175       C  
ATOM    770  CG  TYR A 667     -11.971  -7.158  24.643  1.00 50.21           C  
ANISOU  770  CG  TYR A 667     5512   7698   5867    515    238   -149       C  
ATOM    771  CD1 TYR A 667     -11.059  -6.112  24.691  1.00 51.48           C  
ANISOU  771  CD1 TYR A 667     5691   7795   6074    551    196   -145       C  
ATOM    772  CD2 TYR A 667     -11.562  -8.359  24.076  1.00 51.53           C  
ANISOU  772  CD2 TYR A 667     5682   7844   6055    458    284   -128       C  
ATOM    773  CE1 TYR A 667      -9.780  -6.255  24.183  1.00 52.95           C  
ANISOU  773  CE1 TYR A 667     5889   7901   6327    529    198   -122       C  
ATOM    774  CE2 TYR A 667     -10.288  -8.511  23.565  1.00 52.76           C  
ANISOU  774  CE2 TYR A 667     5851   7916   6279    440    289   -104       C  
ATOM    775  CZ  TYR A 667      -9.401  -7.458  23.620  1.00 54.08           C  
ANISOU  775  CZ  TYR A 667     6028   8024   6493    476    245   -101       C  
ATOM    776  OH  TYR A 667      -8.132  -7.611  23.111  1.00 55.43           O  
ANISOU  776  OH  TYR A 667     6210   8118   6733    457    250    -77       O  
ATOM    777  N   ARG A 668     -15.048  -8.097  22.742  1.00 44.48           N  
ANISOU  777  N   ARG A 668     4725   7173   5001    452    325   -172       N  
ATOM    778  CA  ARG A 668     -15.147  -8.788  21.464  1.00 43.73           C  
ANISOU  778  CA  ARG A 668     4641   7060   4915    387    361   -153       C  
ATOM    779  C   ARG A 668     -15.843  -7.893  20.448  1.00 44.01           C  
ANISOU  779  C   ARG A 668     4667   7119   4937    404    344   -160       C  
ATOM    780  O   ARG A 668     -15.445  -7.830  19.286  1.00 44.61           O  
ANISOU  780  O   ARG A 668     4746   7158   5044    380    360   -147       O  
ATOM    781  CB  ARG A 668     -15.915 -10.102  21.620  1.00 44.35           C  
ANISOU  781  CB  ARG A 668     4742   7157   4952    320    386   -147       C  
ATOM    782  CG  ARG A 668     -16.140 -10.849  20.314  1.00 45.78           C  
ANISOU  782  CG  ARG A 668     4944   7312   5137    249    419   -126       C  
ATOM    783  CD  ARG A 668     -17.101 -12.011  20.502  1.00 49.50           C  
ANISOU  783  CD  ARG A 668     5441   7805   5563    189    434   -125       C  
ATOM    784  NE  ARG A 668     -17.502 -12.602  19.229  1.00 53.37           N  
ANISOU  784  NE  ARG A 668     5954   8272   6053    126    459   -107       N  
ATOM    785  CZ  ARG A 668     -18.532 -13.431  19.080  1.00 56.62           C  
ANISOU  785  CZ  ARG A 668     6384   8704   6426     75    465   -106       C  
ATOM    786  NH1 ARG A 668     -19.273 -13.766  20.128  1.00 57.85           N  
ANISOU  786  NH1 ARG A 668     6536   8904   6540     78    450   -122       N  
ATOM    787  NH2 ARG A 668     -18.824 -13.920  17.883  1.00 56.83           N  
ANISOU  787  NH2 ARG A 668     6434   8703   6457     20    486    -88       N  
ATOM    788  N   ALA A 669     -16.878  -7.192  20.899  1.00 42.90           N  
ANISOU  788  N   ALA A 669     4513   7038   4750    445    312   -179       N  
ATOM    789  CA  ALA A 669     -17.616  -6.274  20.041  1.00 40.33           C  
ANISOU  789  CA  ALA A 669     4176   6742   4404    471    293   -185       C  
ATOM    790  C   ALA A 669     -16.761  -5.068  19.659  1.00 40.15           C  
ANISOU  790  C   ALA A 669     4152   6680   4424    529    273   -192       C  
ATOM    791  O   ALA A 669     -16.992  -4.434  18.630  1.00 42.51           O  
ANISOU  791  O   ALA A 669     4449   6979   4725    539    267   -194       O  
ATOM    792  CB  ALA A 669     -18.900  -5.826  20.724  1.00 37.90           C  
ANISOU  792  CB  ALA A 669     3855   6507   4036    507    265   -202       C  
ATOM    793  N   ALA A 670     -15.773  -4.760  20.492  1.00 38.83           N  
ANISOU  793  N   ALA A 670     3995   6465   4293    563    255   -195       N  
ATOM    794  CA  ALA A 670     -14.875  -3.639  20.237  1.00 38.59           C  
ANISOU  794  CA  ALA A 670     3994   6357   4311    602    218   -196       C  
ATOM    795  C   ALA A 670     -13.805  -3.996  19.209  1.00 38.90           C  
ANISOU  795  C   ALA A 670     4051   6313   4414    554    236   -178       C  
ATOM    796  O   ALA A 670     -13.459  -3.180  18.355  1.00 38.81           O  
ANISOU  796  O   ALA A 670     4057   6260   4429    567    220   -181       O  
ATOM    797  CB  ALA A 670     -14.235  -3.168  21.532  1.00 38.23           C  
ANISOU  797  CB  ALA A 670     3970   6274   4280    643    182   -200       C  
ATOM    798  N   ARG A 671     -13.281  -5.215  19.298  1.00 40.40           N  
ANISOU  798  N   ARG A 671     4242   6479   4628    497    271   -158       N  
ATOM    799  CA  ARG A 671     -12.269  -5.687  18.358  1.00 42.61           C  
ANISOU  799  CA  ARG A 671     4540   6681   4970    448    297   -137       C  
ATOM    800  C   ARG A 671     -12.877  -5.901  16.977  1.00 43.18           C  
ANISOU  800  C   ARG A 671     4604   6775   5027    408    329   -134       C  
ATOM    801  O   ARG A 671     -12.271  -5.561  15.961  1.00 44.74           O  
ANISOU  801  O   ARG A 671     4820   6911   5269    393    331   -128       O  
ATOM    802  CB  ARG A 671     -11.633  -6.986  18.857  1.00 44.37           C  
ANISOU  802  CB  ARG A 671     4767   6876   5213    403    331   -115       C  
ATOM    803  CG  ARG A 671     -10.908  -6.854  20.186  1.00 48.02           C  
ANISOU  803  CG  ARG A 671     5239   7309   5696    436    299   -115       C  
ATOM    804  CD  ARG A 671      -9.709  -5.931  20.072  1.00 51.63           C  
ANISOU  804  CD  ARG A 671     5717   7684   6216    462    262   -111       C  
ATOM    805  NE  ARG A 671      -8.734  -6.431  19.108  1.00 55.30           N  
ANISOU  805  NE  ARG A 671     6193   8079   6742    418    291    -89       N  
ATOM    806  CZ  ARG A 671      -7.787  -7.318  19.396  1.00 58.43           C  
ANISOU  806  CZ  ARG A 671     6594   8427   7179    390    313    -64       C  
ATOM    807  NH1 ARG A 671      -7.685  -7.808  20.625  1.00 59.32           N  
ANISOU  807  NH1 ARG A 671     6705   8555   7280    400    305    -60       N  
ATOM    808  NH2 ARG A 671      -6.942  -7.718  18.456  1.00 59.10           N  
ANISOU  808  NH2 ARG A 671     6690   8448   7318    352    343    -44       N  
ATOM    809  N   ILE A 672     -14.078  -6.472  16.954  1.00 42.40           N  
ANISOU  809  N   ILE A 672     4481   6766   4865    387    355   -137       N  
ATOM    810  CA  ILE A 672     -14.815  -6.689  15.713  1.00 41.83           C  
ANISOU  810  CA  ILE A 672     4399   6727   4767    345    384   -132       C  
ATOM    811  C   ILE A 672     -15.074  -5.370  14.990  1.00 42.49           C  
ANISOU  811  C   ILE A 672     4482   6809   4852    391    348   -148       C  
ATOM    812  O   ILE A 672     -14.873  -5.263  13.779  1.00 44.25           O  
ANISOU  812  O   ILE A 672     4719   6994   5101    359    361   -141       O  
ATOM    813  CB  ILE A 672     -16.150  -7.420  15.979  1.00 40.94           C  
ANISOU  813  CB  ILE A 672     4290   6674   4590    309    387   -129       C  
ATOM    814  CG1 ILE A 672     -15.883  -8.878  16.360  1.00 39.74           C  
ANISOU  814  CG1 ILE A 672     4163   6494   4442    245    423   -110       C  
ATOM    815  CG2 ILE A 672     -17.058  -7.352  14.760  1.00 41.39           C  
ANISOU  815  CG2 ILE A 672     4348   6755   4622    275    391   -124       C  
ATOM    816  CD1 ILE A 672     -17.115  -9.632  16.807  1.00 40.47           C  
ANISOU  816  CD1 ILE A 672     4263   6640   4476    212    421   -112       C  
ATOM    817  N   LEU A 673     -15.505  -4.362  15.738  1.00 40.69           N  
ANISOU  817  N   LEU A 673     4246   6618   4597    464    304   -170       N  
ATOM    818  CA  LEU A 673     -15.717  -3.037  15.172  1.00 39.47           C  
ANISOU  818  CA  LEU A 673     4100   6458   4440    517    268   -187       C  
ATOM    819  C   LEU A 673     -14.410  -2.411  14.681  1.00 42.55           C  
ANISOU  819  C   LEU A 673     4531   6736   4899    520    249   -187       C  
ATOM    820  O   LEU A 673     -14.374  -1.784  13.622  1.00 44.53           O  
ANISOU  820  O   LEU A 673     4798   6959   5162    521    241   -193       O  
ATOM    821  CB  LEU A 673     -16.383  -2.124  16.198  1.00 35.35           C  
ANISOU  821  CB  LEU A 673     3567   5992   3871    598    229   -207       C  
ATOM    822  CG  LEU A 673     -16.527  -0.659  15.792  1.00 33.39           C  
ANISOU  822  CG  LEU A 673     3338   5732   3615    664    189   -226       C  
ATOM    823  CD1 LEU A 673     -17.390  -0.522  14.548  1.00 30.51           C  
ANISOU  823  CD1 LEU A 673     2956   5414   3223    651    201   -226       C  
ATOM    824  CD2 LEU A 673     -17.103   0.142  16.947  1.00 33.95           C  
ANISOU  824  CD2 LEU A 673     3406   5853   3641    743    157   -242       C  
ATOM    825  N   ALA A 674     -13.340  -2.581  15.453  1.00 42.11           N  
ANISOU  825  N   ALA A 674     4493   6620   4887    521    240   -180       N  
ATOM    826  CA  ALA A 674     -12.038  -2.034  15.082  1.00 42.20           C  
ANISOU  826  CA  ALA A 674     4541   6529   4963    521    223   -179       C  
ATOM    827  C   ALA A 674     -11.524  -2.693  13.809  1.00 44.51           C  
ANISOU  827  C   ALA A 674     4843   6767   5301    452    262   -163       C  
ATOM    828  O   ALA A 674     -10.947  -2.036  12.942  1.00 45.05           O  
ANISOU  828  O   ALA A 674     4939   6772   5405    450    250   -170       O  
ATOM    829  CB  ALA A 674     -11.042  -2.215  16.215  1.00 41.34           C  
ANISOU  829  CB  ALA A 674     4443   6377   4888    531    208   -171       C  
ATOM    830  N   MET A 675     -11.744  -3.998  13.703  1.00 45.56           N  
ANISOU  830  N   MET A 675     4959   6923   5429    394    310   -141       N  
ATOM    831  CA  MET A 675     -11.367  -4.744  12.511  1.00 45.79           C  
ANISOU  831  CA  MET A 675     5001   6905   5493    323    355   -122       C  
ATOM    832  C   MET A 675     -12.224  -4.342  11.317  1.00 43.43           C  
ANISOU  832  C   MET A 675     4701   6634   5166    309    360   -130       C  
ATOM    833  O   MET A 675     -11.813  -4.497  10.167  1.00 44.83           O  
ANISOU  833  O   MET A 675     4900   6754   5379    262    384   -121       O  
ATOM    834  CB  MET A 675     -11.484  -6.245  12.770  1.00 47.31           C  
ANISOU  834  CB  MET A 675     5182   7120   5673    266    408    -96       C  
ATOM    835  CG  MET A 675     -10.299  -6.825  13.520  1.00 47.91           C  
ANISOU  835  CG  MET A 675     5270   7136   5800    260    416    -80       C  
ATOM    836  SD  MET A 675     -10.706  -8.337  14.411  1.00 79.22           S  
ANISOU  836  SD  MET A 675     9222  11155   9723    225    459    -61       S  
ATOM    837  CE  MET A 675     -11.804  -9.134  13.238  1.00 87.49           C  
ANISOU  837  CE  MET A 675    10266  12256  10719    154    515    -50       C  
ATOM    838  N   SER A 676     -13.416  -3.828  11.597  1.00 40.26           N  
ANISOU  838  N   SER A 676     4274   6322   4699    351    338   -147       N  
ATOM    839  CA  SER A 676     -14.306  -3.345  10.549  1.00 39.00           C  
ANISOU  839  CA  SER A 676     4110   6200   4507    348    335   -155       C  
ATOM    840  C   SER A 676     -13.776  -2.051   9.946  1.00 37.70           C  
ANISOU  840  C   SER A 676     3979   5970   4375    388    296   -176       C  
ATOM    841  O   SER A 676     -13.809  -1.861   8.731  1.00 36.38           O  
ANISOU  841  O   SER A 676     3830   5772   4222    356    305   -176       O  
ATOM    842  CB  SER A 676     -15.714  -3.121  11.101  1.00 41.95           C  
ANISOU  842  CB  SER A 676     4444   6694   4803    390    321   -166       C  
ATOM    843  OG  SER A 676     -16.516  -2.410  10.173  1.00 43.73           O  
ANISOU  843  OG  SER A 676     4664   6955   4998    405    307   -176       O  
ATOM    844  N   LYS A 677     -13.289  -1.163  10.805  1.00 38.76           N  
ANISOU  844  N   LYS A 677     4127   6081   4518    453    254   -193       N  
ATOM    845  CA  LYS A 677     -12.710   0.098  10.357  1.00 40.38           C  
ANISOU  845  CA  LYS A 677     4373   6222   4748    491    216   -215       C  
ATOM    846  C   LYS A 677     -11.363  -0.137   9.680  1.00 41.81           C  
ANISOU  846  C   LYS A 677     4588   6292   5005    440    232   -207       C  
ATOM    847  O   LYS A 677     -10.861   0.724   8.959  1.00 42.38           O  
ANISOU  847  O   LYS A 677     4698   6302   5102    448    211   -225       O  
ATOM    848  CB  LYS A 677     -12.528   1.055  11.535  1.00 41.10           C  
ANISOU  848  CB  LYS A 677     4476   6318   4821    569    170   -233       C  
ATOM    849  CG  LYS A 677     -13.810   1.441  12.249  1.00 42.19           C  
ANISOU  849  CG  LYS A 677     4586   6559   4886    630    153   -243       C  
ATOM    850  CD  LYS A 677     -13.536   2.524  13.281  1.00 43.86           C  
ANISOU  850  CD  LYS A 677     4823   6759   5082    705    109   -260       C  
ATOM    851  CE  LYS A 677     -14.784   2.862  14.084  1.00 45.77           C  
ANISOU  851  CE  LYS A 677     5039   7101   5253    767     96   -268       C  
ATOM    852  NZ  LYS A 677     -14.500   3.887  15.130  1.00 46.71           N  
ANISOU  852  NZ  LYS A 677     5191   7204   5355    837     57   -281       N  
ATOM    853  N   LYS A 678     -10.779  -1.304   9.929  1.00 42.51           N  
ANISOU  853  N   LYS A 678     4665   6358   5129    388    269   -181       N  
ATOM    854  CA  LYS A 678      -9.502  -1.673   9.333  1.00 42.60           C  
ANISOU  854  CA  LYS A 678     4703   6269   5213    338    291   -169       C  
ATOM    855  C   LYS A 678      -9.633  -1.881   7.827  1.00 42.10           C  
ANISOU  855  C   LYS A 678     4657   6171   5167    279    322   -165       C  
ATOM    856  O   LYS A 678      -8.760  -1.482   7.057  1.00 41.70           O  
ANISOU  856  O   LYS A 678     4642   6035   5169    260    320   -172       O  
ATOM    857  CB  LYS A 678      -8.961  -2.940   9.998  1.00 44.61           C  
ANISOU  857  CB  LYS A 678     4940   6516   5494    301    327   -139       C  
ATOM    858  CG  LYS A 678      -7.654  -3.453   9.421  1.00 46.86           C  
ANISOU  858  CG  LYS A 678     5248   6703   5855    251    356   -121       C  
ATOM    859  CD  LYS A 678      -6.571  -2.392   9.480  1.00 48.70           C  
ANISOU  859  CD  LYS A 678     5508   6865   6133    283    315   -139       C  
ATOM    860  CE  LYS A 678      -5.199  -2.996   9.245  1.00 51.13           C  
ANISOU  860  CE  LYS A 678     5826   7086   6516    241    343   -117       C  
ATOM    861  NZ  LYS A 678      -4.823  -3.933  10.340  1.00 53.27           N  
ANISOU  861  NZ  LYS A 678     6072   7373   6794    241    358    -90       N  
ATOM    862  N   ASN A1002     -10.732  -2.504   7.412  1.00 41.46           N  
ANISOU  862  N   ASN A1002     4554   6157   5041    248    350   -154       N  
ATOM    863  CA  ASN A1002     -10.973  -2.788   6.000  1.00 40.25           C  
ANISOU  863  CA  ASN A1002     4419   5979   4897    185    383   -146       C  
ATOM    864  C   ASN A1002     -11.197  -1.536   5.155  1.00 37.29           C  
ANISOU  864  C   ASN A1002     4070   5583   4516    214    346   -175       C  
ATOM    865  O   ASN A1002     -10.654  -1.415   4.055  1.00 34.52           O  
ANISOU  865  O   ASN A1002     3755   5153   4208    171    358   -177       O  
ATOM    866  CB  ASN A1002     -12.154  -3.747   5.846  1.00 41.23           C  
ANISOU  866  CB  ASN A1002     4512   6191   4964    143    420   -125       C  
ATOM    867  CG  ASN A1002     -11.855  -5.123   6.398  1.00 40.93           C  
ANISOU  867  CG  ASN A1002     4462   6157   4933     96    469    -95       C  
ATOM    868  OD1 ASN A1002     -10.735  -5.621   6.277  1.00 41.17           O  
ANISOU  868  OD1 ASN A1002     4516   6103   5023     64    495    -79       O  
ATOM    869  ND2 ASN A1002     -12.854  -5.746   7.015  1.00 39.49           N  
ANISOU  869  ND2 ASN A1002     4246   6072   4687     94    482    -86       N  
ATOM    870  N   ILE A1003     -11.998  -0.609   5.671  1.00 35.56           N  
ANISOU  870  N   ILE A1003     3836   5431   4243    287    301   -197       N  
ATOM    871  CA  ILE A1003     -12.268   0.636   4.960  1.00 34.35           C  
ANISOU  871  CA  ILE A1003     3712   5263   4075    325    264   -226       C  
ATOM    872  C   ILE A1003     -11.007   1.496   4.867  1.00 34.04           C  
ANISOU  872  C   ILE A1003     3722   5121   4089    344    237   -249       C  
ATOM    873  O   ILE A1003     -10.821   2.237   3.900  1.00 35.78           O  
ANISOU  873  O   ILE A1003     3984   5288   4322    339    222   -269       O  
ATOM    874  CB  ILE A1003     -13.428   1.435   5.604  1.00 32.01           C  
ANISOU  874  CB  ILE A1003     3391   5066   3705    407    225   -243       C  
ATOM    875  CG1 ILE A1003     -13.831   2.607   4.709  1.00 32.05           C  
ANISOU  875  CG1 ILE A1003     3427   5060   3688    441    194   -269       C  
ATOM    876  CG2 ILE A1003     -13.051   1.935   6.988  1.00 34.31           C  
ANISOU  876  CG2 ILE A1003     3681   5367   3990    475    194   -254       C  
ATOM    877  CD1 ILE A1003     -14.921   3.472   5.294  1.00 35.87           C  
ANISOU  877  CD1 ILE A1003     3891   5636   4100    529    157   -285       C  
ATOM    878  N   PHE A1004     -10.136   1.381   5.867  1.00 29.97           N  
ANISOU  878  N   PHE A1004     3205   4580   3602    361    230   -244       N  
ATOM    879  CA  PHE A1004      -8.864   2.094   5.849  1.00 27.42           C  
ANISOU  879  CA  PHE A1004     2926   4165   3329    370    206   -262       C  
ATOM    880  C   PHE A1004      -7.963   1.582   4.729  1.00 25.27           C  
ANISOU  880  C   PHE A1004     2680   3798   3124    293    242   -253       C  
ATOM    881  O   PHE A1004      -7.371   2.370   3.996  1.00 23.98           O  
ANISOU  881  O   PHE A1004     2563   3563   2987    289    225   -277       O  
ATOM    882  CB  PHE A1004      -8.148   1.995   7.201  1.00 25.75           C  
ANISOU  882  CB  PHE A1004     2702   3952   3131    400    192   -254       C  
ATOM    883  CG  PHE A1004      -6.708   2.435   7.153  1.00 25.28           C  
ANISOU  883  CG  PHE A1004     2678   3797   3129    390    178   -263       C  
ATOM    884  CD1 PHE A1004      -6.382   3.776   7.028  1.00 24.92           C  
ANISOU  884  CD1 PHE A1004     2680   3716   3073    431    135   -297       C  
ATOM    885  CD2 PHE A1004      -5.681   1.507   7.225  1.00 24.01           C  
ANISOU  885  CD2 PHE A1004     2507   3585   3031    340    210   -237       C  
ATOM    886  CE1 PHE A1004      -5.059   4.183   6.976  1.00 22.68           C  
ANISOU  886  CE1 PHE A1004     2430   3350   2838    416    122   -306       C  
ATOM    887  CE2 PHE A1004      -4.357   1.908   7.174  1.00 22.96           C  
ANISOU  887  CE2 PHE A1004     2402   3371   2951    330    198   -244       C  
ATOM    888  CZ  PHE A1004      -4.047   3.248   7.050  1.00 22.27           C  
ANISOU  888  CZ  PHE A1004     2360   3252   2851    366    153   -279       C  
ATOM    889  N   GLU A1005      -7.868   0.262   4.599  1.00 26.22           N  
ANISOU  889  N   GLU A1005     2775   3917   3270    232    293   -219       N  
ATOM    890  CA  GLU A1005      -7.062  -0.348   3.547  1.00 28.21           C  
ANISOU  890  CA  GLU A1005     3052   4081   3585    156    336   -205       C  
ATOM    891  C   GLU A1005      -7.688  -0.094   2.183  1.00 29.27           C  
ANISOU  891  C   GLU A1005     3212   4201   3707    121    345   -216       C  
ATOM    892  O   GLU A1005      -7.004  -0.098   1.161  1.00 30.74           O  
ANISOU  892  O   GLU A1005     3436   4299   3943     70    365   -219       O  
ATOM    893  CB  GLU A1005      -6.916  -1.852   3.784  1.00 30.73           C  
ANISOU  893  CB  GLU A1005     3343   4408   3923    103    393   -163       C  
ATOM    894  CG  GLU A1005      -6.318  -2.212   5.136  1.00 35.52           C  
ANISOU  894  CG  GLU A1005     3923   5030   4541    135    386   -150       C  
ATOM    895  CD  GLU A1005      -4.896  -1.708   5.305  1.00 37.76           C  
ANISOU  895  CD  GLU A1005     4229   5230   4887    146    366   -159       C  
ATOM    896  OE1 GLU A1005      -4.167  -1.627   4.296  1.00 38.39           O  
ANISOU  896  OE1 GLU A1005     4341   5226   5018    104    384   -162       O  
ATOM    897  OE2 GLU A1005      -4.508  -1.392   6.449  1.00 39.07           O  
ANISOU  897  OE2 GLU A1005     4382   5415   5050    195    333   -162       O  
ATOM    898  N   MET A1006      -8.997   0.131   2.179  1.00 28.42           N  
ANISOU  898  N   MET A1006     3084   4181   3532    147    331   -221       N  
ATOM    899  CA  MET A1006      -9.728   0.406   0.953  1.00 26.95           C  
ANISOU  899  CA  MET A1006     2918   3996   3326    118    334   -229       C  
ATOM    900  C   MET A1006      -9.329   1.759   0.377  1.00 28.79           C  
ANISOU  900  C   MET A1006     3203   4166   3571    151    291   -270       C  
ATOM    901  O   MET A1006      -8.979   1.866  -0.800  1.00 28.00           O  
ANISOU  901  O   MET A1006     3144   3990   3505    100    305   -278       O  
ATOM    902  CB  MET A1006     -11.232   0.383   1.224  1.00 25.75           C  
ANISOU  902  CB  MET A1006     2724   3965   3095    149    324   -224       C  
ATOM    903  CG  MET A1006     -12.090   0.451  -0.024  1.00 24.34           C  
ANISOU  903  CG  MET A1006     2557   3801   2891    109    333   -224       C  
ATOM    904  SD  MET A1006     -13.815   0.804   0.350  1.00 36.66           S  
ANISOU  904  SD  MET A1006     4067   5509   4355    168    306   -225       S  
ATOM    905  CE  MET A1006     -14.587   0.392  -1.210  1.00 15.59           C  
ANISOU  905  CE  MET A1006     1408   2844   1671     85    335   -209       C  
ATOM    906  N   LEU A1007      -9.381   2.792   1.212  1.00 30.64           N  
ANISOU  906  N   LEU A1007     3440   4429   3773    234    241   -297       N  
ATOM    907  CA  LEU A1007      -9.070   4.148   0.770  1.00 31.76           C  
ANISOU  907  CA  LEU A1007     3637   4518   3911    273    198   -338       C  
ATOM    908  C   LEU A1007      -7.573   4.403   0.644  1.00 29.63           C  
ANISOU  908  C   LEU A1007     3410   4140   3708    249    196   -352       C  
ATOM    909  O   LEU A1007      -7.152   5.349  -0.020  1.00 30.24           O  
ANISOU  909  O   LEU A1007     3544   4152   3794    254    173   -387       O  
ATOM    910  CB  LEU A1007      -9.708   5.185   1.694  1.00 33.70           C  
ANISOU  910  CB  LEU A1007     3879   4834   4091    371    148   -359       C  
ATOM    911  CG  LEU A1007     -11.156   5.541   1.355  1.00 36.03           C  
ANISOU  911  CG  LEU A1007     4158   5214   4318    406    134   -364       C  
ATOM    912  CD1 LEU A1007     -12.138   4.571   1.999  1.00 35.32           C  
ANISOU  912  CD1 LEU A1007     3997   5232   4193    405    158   -330       C  
ATOM    913  CD2 LEU A1007     -11.449   6.971   1.759  1.00 38.75           C  
ANISOU  913  CD2 LEU A1007     4536   5578   4611    500     82   -398       C  
ATOM    914  N   ARG A1008      -6.775   3.561   1.291  1.00 28.92           N  
ANISOU  914  N   ARG A1008     3293   4032   3661    224    222   -326       N  
ATOM    915  CA  ARG A1008      -5.328   3.626   1.151  1.00 29.32           C  
ANISOU  915  CA  ARG A1008     3375   3986   3780    193    227   -333       C  
ATOM    916  C   ARG A1008      -4.958   3.248  -0.275  1.00 26.62           C  
ANISOU  916  C   ARG A1008     3066   3561   3489    114    265   -332       C  
ATOM    917  O   ARG A1008      -4.051   3.824  -0.874  1.00 27.20           O  
ANISOU  917  O   ARG A1008     3187   3547   3601     94    257   -357       O  
ATOM    918  CB  ARG A1008      -4.654   2.669   2.132  1.00 31.48           C  
ANISOU  918  CB  ARG A1008     3607   4267   4088    183    251   -298       C  
ATOM    919  CG  ARG A1008      -3.136   2.703   2.091  1.00 34.86           C  
ANISOU  919  CG  ARG A1008     4056   4605   4586    156    256   -301       C  
ATOM    920  CD  ARG A1008      -2.544   1.720   3.088  1.00 38.72           C  
ANISOU  920  CD  ARG A1008     4500   5109   5104    151    278   -263       C  
ATOM    921  NE  ARG A1008      -1.839   0.626   2.426  1.00 41.00           N  
ANISOU  921  NE  ARG A1008     4785   5336   5459     80    336   -234       N  
ATOM    922  CZ  ARG A1008      -2.436  -0.431   1.884  1.00 41.92           C  
ANISOU  922  CZ  ARG A1008     4888   5467   5575     31    387   -205       C  
ATOM    923  NH1 ARG A1008      -3.757  -0.543   1.917  1.00 41.18           N  
ANISOU  923  NH1 ARG A1008     4777   5452   5418     45    385   -203       N  
ATOM    924  NH2 ARG A1008      -1.710  -1.377   1.305  1.00 43.75           N  
ANISOU  924  NH2 ARG A1008     5124   5635   5866    -31    442   -177       N  
ATOM    925  N   ILE A1009      -5.681   2.272  -0.812  1.00 24.57           N  
ANISOU  925  N   ILE A1009     2783   3329   3223     65    308   -303       N  
ATOM    926  CA  ILE A1009      -5.469   1.802  -2.172  1.00 25.35           C  
ANISOU  926  CA  ILE A1009     2914   3354   3365    -17    349   -296       C  
ATOM    927  C   ILE A1009      -6.117   2.743  -3.187  1.00 27.55           C  
ANISOU  927  C   ILE A1009     3237   3620   3613    -13    322   -330       C  
ATOM    928  O   ILE A1009      -5.542   3.032  -4.237  1.00 26.73           O  
ANISOU  928  O   ILE A1009     3184   3423   3549    -59    330   -349       O  
ATOM    929  CB  ILE A1009      -6.034   0.376  -2.351  1.00 23.65           C  
ANISOU  929  CB  ILE A1009     2664   3175   3146    -76    408   -248       C  
ATOM    930  CG1 ILE A1009      -5.287  -0.608  -1.449  1.00 22.68           C  
ANISOU  930  CG1 ILE A1009     2507   3051   3058    -84    440   -215       C  
ATOM    931  CG2 ILE A1009      -5.946  -0.064  -3.803  1.00 23.26           C  
ANISOU  931  CG2 ILE A1009     2654   3051   3131   -163    452   -240       C  
ATOM    932  CD1 ILE A1009      -5.899  -1.994  -1.414  1.00 22.23           C  
ANISOU  932  CD1 ILE A1009     2419   3043   2984   -133    496   -170       C  
ATOM    933  N   ASP A1010      -7.310   3.232  -2.864  1.00 29.52           N  
ANISOU  933  N   ASP A1010     3466   3962   3790     43    289   -338       N  
ATOM    934  CA  ASP A1010      -8.060   4.071  -3.792  1.00 30.94           C  
ANISOU  934  CA  ASP A1010     3681   4141   3933     52    263   -366       C  
ATOM    935  C   ASP A1010      -7.610   5.528  -3.807  1.00 34.64           C  
ANISOU  935  C   ASP A1010     4205   4564   4391    109    210   -416       C  
ATOM    936  O   ASP A1010      -7.596   6.164  -4.861  1.00 37.41           O  
ANISOU  936  O   ASP A1010     4612   4857   4745     90    199   -445       O  
ATOM    937  CB  ASP A1010      -9.562   3.998  -3.505  1.00 28.75           C  
ANISOU  937  CB  ASP A1010     3357   3985   3579     90    252   -351       C  
ATOM    938  CG  ASP A1010     -10.185   2.708  -3.991  1.00 28.83           C  
ANISOU  938  CG  ASP A1010     3334   4031   3589     15    304   -308       C  
ATOM    939  OD1 ASP A1010      -9.495   1.946  -4.702  1.00 26.87           O  
ANISOU  939  OD1 ASP A1010     3108   3704   3398    -68    350   -291       O  
ATOM    940  OD2 ASP A1010     -11.369   2.460  -3.673  1.00 30.30           O  
ANISOU  940  OD2 ASP A1010     3474   4324   3714     36    302   -291       O  
ATOM    941  N   GLU A1011      -7.248   6.060  -2.645  1.00 35.15           N  
ANISOU  941  N   GLU A1011     4261   4655   4439    177    179   -428       N  
ATOM    942  CA  GLU A1011      -6.968   7.488  -2.546  1.00 37.71           C  
ANISOU  942  CA  GLU A1011     4641   4950   4735    237    128   -475       C  
ATOM    943  C   GLU A1011      -5.511   7.799  -2.209  1.00 36.81           C  
ANISOU  943  C   GLU A1011     4560   4756   4671    227    121   -492       C  
ATOM    944  O   GLU A1011      -4.959   8.794  -2.674  1.00 36.59           O  
ANISOU  944  O   GLU A1011     4599   4661   4643    233     95   -533       O  
ATOM    945  CB  GLU A1011      -7.914   8.153  -1.544  1.00 40.91           C  
ANISOU  945  CB  GLU A1011     5024   5456   5062    333     89   -480       C  
ATOM    946  CG  GLU A1011      -8.264   9.586  -1.904  1.00 44.72           C  
ANISOU  946  CG  GLU A1011     5570   5928   5491    392     43   -525       C  
ATOM    947  CD  GLU A1011      -9.604  10.017  -1.348  1.00 48.73           C  
ANISOU  947  CD  GLU A1011     6049   6546   5919    474     18   -521       C  
ATOM    948  OE1 GLU A1011      -9.992   9.518  -0.271  1.00 51.37           O  
ANISOU  948  OE1 GLU A1011     6325   6960   6235    505     23   -494       O  
ATOM    949  OE2 GLU A1011     -10.275  10.851  -1.993  1.00 50.07           O  
ANISOU  949  OE2 GLU A1011     6257   6723   6044    509     -6   -546       O  
ATOM    950  N   GLY A1012      -4.890   6.948  -1.403  1.00 36.24           N  
ANISOU  950  N   GLY A1012     4442   4691   4636    211    144   -460       N  
ATOM    951  CA  GLY A1012      -3.489   7.125  -1.075  1.00 34.86           C  
ANISOU  951  CA  GLY A1012     4288   4447   4511    196    140   -469       C  
ATOM    952  C   GLY A1012      -3.234   7.534   0.362  1.00 36.30           C  
ANISOU  952  C   GLY A1012     4452   4677   4664    261    107   -467       C  
ATOM    953  O   GLY A1012      -4.158   7.616   1.170  1.00 37.10           O  
ANISOU  953  O   GLY A1012     4522   4865   4709    318     90   -457       O  
ATOM    954  N   LEU A1013      -1.970   7.811   0.670  1.00 38.02           N  
ANISOU  954  N   LEU A1013     4690   4836   4919    249     98   -477       N  
ATOM    955  CA  LEU A1013      -1.535   8.035   2.043  1.00 40.03           C  
ANISOU  955  CA  LEU A1013     4925   5127   5157    294     72   -468       C  
ATOM    956  C   LEU A1013      -0.167   8.721   2.066  1.00 40.85           C  
ANISOU  956  C   LEU A1013     5074   5156   5290    278     53   -493       C  
ATOM    957  O   LEU A1013       0.682   8.443   1.223  1.00 40.95           O  
ANISOU  957  O   LEU A1013     5103   5093   5364    217     77   -497       O  
ATOM    958  CB  LEU A1013      -1.464   6.689   2.768  1.00 41.23           C  
ANISOU  958  CB  LEU A1013     5003   5318   5344    276    106   -418       C  
ATOM    959  CG  LEU A1013      -0.930   6.601   4.196  1.00 43.00           C  
ANISOU  959  CG  LEU A1013     5196   5576   5565    309     88   -398       C  
ATOM    960  CD1 LEU A1013      -1.840   7.348   5.138  1.00 44.38           C  
ANISOU  960  CD1 LEU A1013     5374   5828   5662    385     48   -409       C  
ATOM    961  CD2 LEU A1013      -0.807   5.146   4.618  1.00 42.81           C  
ANISOU  961  CD2 LEU A1013     5106   5575   5584    277    131   -350       C  
ATOM    962  N   ARG A1014       0.040   9.622   3.023  1.00 39.32           N  
ANISOU  962  N   ARG A1014     4903   4985   5050    330     10   -508       N  
ATOM    963  CA  ARG A1014       1.336  10.281   3.195  1.00 35.79           C  
ANISOU  963  CA  ARG A1014     4497   4480   4622    314    -11   -528       C  
ATOM    964  C   ARG A1014       1.787  10.215   4.649  1.00 34.03           C  
ANISOU  964  C   ARG A1014     4242   4300   4389    343    -30   -503       C  
ATOM    965  O   ARG A1014       1.107  10.725   5.540  1.00 32.90           O  
ANISOU  965  O   ARG A1014     4103   4217   4181    404    -59   -503       O  
ATOM    966  CB  ARG A1014       1.277  11.742   2.744  1.00 35.12           C  
ANISOU  966  CB  ARG A1014     4502   4362   4479    339    -48   -583       C  
ATOM    967  CG  ARG A1014       1.220  11.948   1.239  1.00 35.41           C  
ANISOU  967  CG  ARG A1014     4587   4332   4536    297    -34   -615       C  
ATOM    968  CD  ARG A1014       2.551  12.433   0.680  1.00 35.00           C  
ANISOU  968  CD  ARG A1014     4588   4190   4521    245    -37   -647       C  
ATOM    969  NE  ARG A1014       3.467  11.332   0.401  1.00 36.45           N  
ANISOU  969  NE  ARG A1014     4721   4332   4795    178      4   -617       N  
ATOM    970  CZ  ARG A1014       4.727  11.487   0.005  1.00 35.19           C  
ANISOU  970  CZ  ARG A1014     4587   4100   4683    126      9   -633       C  
ATOM    971  NH1 ARG A1014       5.485  10.424  -0.228  1.00 35.04           N  
ANISOU  971  NH1 ARG A1014     4518   4049   4746     72     51   -601       N  
ATOM    972  NH2 ARG A1014       5.232  12.703  -0.156  1.00 32.95           N  
ANISOU  972  NH2 ARG A1014     4381   3778   4361    129    -25   -682       N  
ATOM    973  N   LEU A1015       2.940   9.597   4.886  1.00 33.36           N  
ANISOU  973  N   LEU A1015     4124   4182   4367    301    -15   -479       N  
ATOM    974  CA  LEU A1015       3.430   9.412   6.249  1.00 33.37           C  
ANISOU  974  CA  LEU A1015     4090   4223   4367    321    -32   -450       C  
ATOM    975  C   LEU A1015       4.076  10.668   6.836  1.00 35.65           C  
ANISOU  975  C   LEU A1015     4436   4500   4610    342    -79   -477       C  
ATOM    976  O   LEU A1015       4.479  10.675   7.998  1.00 38.12           O  
ANISOU  976  O   LEU A1015     4728   4843   4911    359    -99   -455       O  
ATOM    977  CB  LEU A1015       4.385   8.216   6.329  1.00 31.65           C  
ANISOU  977  CB  LEU A1015     3811   3982   4231    272      3   -410       C  
ATOM    978  CG  LEU A1015       3.747   6.856   6.028  1.00 28.66           C  
ANISOU  978  CG  LEU A1015     3375   3626   3890    254     53   -374       C  
ATOM    979  CD1 LEU A1015       4.723   5.715   6.281  1.00 26.94           C  
ANISOU  979  CD1 LEU A1015     3102   3388   3745    216     86   -331       C  
ATOM    980  CD2 LEU A1015       2.475   6.667   6.842  1.00 28.60           C  
ANISOU  980  CD2 LEU A1015     3340   3703   3823    307     44   -360       C  
ATOM    981  N   LYS A1016       4.172  11.727   6.039  1.00 35.44           N  
ANISOU  981  N   LYS A1016     4486   4426   4553    338    -96   -525       N  
ATOM    982  CA  LYS A1016       4.632  13.013   6.559  1.00 37.56           C  
ANISOU  982  CA  LYS A1016     4824   4687   4762    359   -140   -554       C  
ATOM    983  C   LYS A1016       3.737  14.166   6.108  1.00 36.45           C  
ANISOU  983  C   LYS A1016     4762   4545   4540    404   -162   -599       C  
ATOM    984  O   LYS A1016       2.982  14.041   5.144  1.00 36.79           O  
ANISOU  984  O   LYS A1016     4813   4579   4586    404   -144   -614       O  
ATOM    985  CB  LYS A1016       6.103  13.272   6.210  1.00 41.13           C  
ANISOU  985  CB  LYS A1016     5300   5072   5255    300   -143   -568       C  
ATOM    986  CG  LYS A1016       6.407  13.368   4.727  1.00 44.36           C  
ANISOU  986  CG  LYS A1016     5746   5407   5701    251   -122   -604       C  
ATOM    987  CD  LYS A1016       7.902  13.511   4.490  1.00 46.43           C  
ANISOU  987  CD  LYS A1016     6021   5611   6010    190   -122   -614       C  
ATOM    988  CE  LYS A1016       8.254  13.318   3.023  1.00 48.36           C  
ANISOU  988  CE  LYS A1016     6287   5778   6309    133    -91   -640       C  
ATOM    989  NZ  LYS A1016       7.660  14.374   2.159  1.00 48.99           N  
ANISOU  989  NZ  LYS A1016     6459   5825   6331    145   -107   -698       N  
ATOM    990  N   ILE A1017       3.829  15.284   6.822  1.00 35.02           N  
ANISOU  990  N   ILE A1017     4644   4376   4286    440   -199   -618       N  
ATOM    991  CA  ILE A1017       2.928  16.417   6.634  1.00 33.88           C  
ANISOU  991  CA  ILE A1017     4579   4242   4053    497   -221   -655       C  
ATOM    992  C   ILE A1017       3.006  17.025   5.237  1.00 35.35           C  
ANISOU  992  C   ILE A1017     4835   4361   4236    471   -219   -705       C  
ATOM    993  O   ILE A1017       4.092  17.221   4.692  1.00 34.34           O  
ANISOU  993  O   ILE A1017     4739   4168   4141    413   -218   -727       O  
ATOM    994  CB  ILE A1017       3.204  17.524   7.676  1.00 33.01           C  
ANISOU  994  CB  ILE A1017     4534   4144   3862    532   -258   -665       C  
ATOM    995  CG1 ILE A1017       3.220  16.937   9.089  1.00 31.26           C  
ANISOU  995  CG1 ILE A1017     4248   3982   3646    550   -263   -616       C  
ATOM    996  CG2 ILE A1017       2.174  18.640   7.569  1.00 33.45           C  
ANISOU  996  CG2 ILE A1017     4671   4216   3822    601   -277   -698       C  
ATOM    997  CD1 ILE A1017       3.436  17.971  10.172  1.00 30.04           C  
ANISOU  997  CD1 ILE A1017     4160   3843   3412    582   -297   -620       C  
ATOM    998  N   TYR A1018       1.840  17.315   4.667  1.00 38.51           N  
ANISOU  998  N   TYR A1018     5258   4778   4596    514   -217   -723       N  
ATOM    999  CA  TYR A1018       1.746  17.983   3.374  1.00 40.88           C  
ANISOU  999  CA  TYR A1018     5634   5018   4881    499   -219   -772       C  
ATOM   1000  C   TYR A1018       0.590  18.977   3.385  1.00 43.64           C  
ANISOU 1000  C   TYR A1018     6046   5400   5135    579   -241   -797       C  
ATOM   1001  O   TYR A1018      -0.003  19.238   4.431  1.00 43.09           O  
ANISOU 1001  O   TYR A1018     5969   5393   5009    642   -255   -778       O  
ATOM   1002  CB  TYR A1018       1.559  16.961   2.250  1.00 40.01           C  
ANISOU 1002  CB  TYR A1018     5471   4882   4849    449   -183   -763       C  
ATOM   1003  CG  TYR A1018       0.271  16.168   2.329  1.00 40.47           C  
ANISOU 1003  CG  TYR A1018     5457   5010   4908    485   -165   -729       C  
ATOM   1004  CD1 TYR A1018      -0.826  16.505   1.545  1.00 40.49           C  
ANISOU 1004  CD1 TYR A1018     5487   5025   4873    516   -166   -748       C  
ATOM   1005  CD2 TYR A1018       0.154  15.078   3.183  1.00 40.33           C  
ANISOU 1005  CD2 TYR A1018     5346   5050   4928    485   -147   -677       C  
ATOM   1006  CE1 TYR A1018      -2.003  15.781   1.612  1.00 40.74           C  
ANISOU 1006  CE1 TYR A1018     5451   5127   4902    544   -150   -716       C  
ATOM   1007  CE2 TYR A1018      -1.019  14.349   3.257  1.00 40.55           C  
ANISOU 1007  CE2 TYR A1018     5311   5144   4951    512   -129   -647       C  
ATOM   1008  CZ  TYR A1018      -2.092  14.704   2.469  1.00 41.66           C  
ANISOU 1008  CZ  TYR A1018     5476   5299   5052    540   -131   -667       C  
ATOM   1009  OH  TYR A1018      -3.258  13.978   2.541  1.00 43.22           O  
ANISOU 1009  OH  TYR A1018     5609   5571   5243    563   -114   -637       O  
ATOM   1010  N   LYS A1019       0.275  19.533   2.220  1.00 46.65           N  
ANISOU 1010  N   LYS A1019     6480   5740   5506    565   -238   -823       N  
ATOM   1011  CA  LYS A1019      -0.841  20.463   2.098  1.00 49.98           C  
ANISOU 1011  CA  LYS A1019     6931   6196   5862    614   -246   -806       C  
ATOM   1012  C   LYS A1019      -1.828  19.993   1.035  1.00 51.75           C  
ANISOU 1012  C   LYS A1019     7129   6429   6106    616   -231   -808       C  
ATOM   1013  O   LYS A1019      -1.443  19.339   0.067  1.00 51.37           O  
ANISOU 1013  O   LYS A1019     7065   6332   6123    552   -209   -818       O  
ATOM   1014  CB  LYS A1019      -0.340  21.867   1.756  1.00 51.49           C  
ANISOU 1014  CB  LYS A1019     7191   6344   6030    573   -250   -793       C  
ATOM   1015  CG  LYS A1019       0.530  22.511   2.822  1.00 53.24           C  
ANISOU 1015  CG  LYS A1019     7447   6564   6219    571   -266   -788       C  
ATOM   1016  CD  LYS A1019       0.933  23.920   2.411  1.00 55.47           C  
ANISOU 1016  CD  LYS A1019     7787   6811   6477    531   -262   -776       C  
ATOM   1017  CE  LYS A1019       1.815  24.577   3.459  1.00 57.10           C  
ANISOU 1017  CE  LYS A1019     8030   7017   6649    524   -276   -771       C  
ATOM   1018  NZ  LYS A1019       2.189  25.969   3.085  1.00 58.45           N  
ANISOU 1018  NZ  LYS A1019     8251   7162   6796    486   -269   -761       N  
ATOM   1019  N   ASP A1020      -3.100  20.329   1.217  1.00 53.89           N  
ANISOU 1019  N   ASP A1020     7396   6761   6320    689   -241   -798       N  
ATOM   1020  CA  ASP A1020      -4.124  19.976   0.241  1.00 55.90           C  
ANISOU 1020  CA  ASP A1020     7627   7031   6580    698   -230   -800       C  
ATOM   1021  C   ASP A1020      -4.178  20.992  -0.894  1.00 59.96           C  
ANISOU 1021  C   ASP A1020     8196   7492   7094    655   -231   -792       C  
ATOM   1022  O   ASP A1020      -3.284  21.828  -1.033  1.00 60.68           O  
ANISOU 1022  O   ASP A1020     8332   7530   7192    605   -230   -787       O  
ATOM   1023  CB  ASP A1020      -5.494  19.849   0.910  1.00 54.89           C  
ANISOU 1023  CB  ASP A1020     7461   7004   6392    796   -239   -791       C  
ATOM   1024  CG  ASP A1020      -5.779  20.981   1.878  1.00 54.15           C  
ANISOU 1024  CG  ASP A1020     7406   6939   6229    857   -262   -770       C  
ATOM   1025  OD1 ASP A1020      -5.234  22.088   1.685  1.00 54.53           O  
ANISOU 1025  OD1 ASP A1020     7520   6931   6269    827   -272   -763       O  
ATOM   1026  OD2 ASP A1020      -6.549  20.761   2.837  1.00 53.14           O  
ANISOU 1026  OD2 ASP A1020     7241   6893   6057    932   -266   -760       O  
ATOM   1027  N   THR A1021      -5.234  20.921  -1.697  1.00 63.24           N  
ANISOU 1027  N   THR A1021     8601   7929   7499    675   -229   -792       N  
ATOM   1028  CA  THR A1021      -5.388  21.809  -2.845  1.00 65.68           C  
ANISOU 1028  CA  THR A1021     8954   8192   7809    637   -228   -785       C  
ATOM   1029  C   THR A1021      -5.621  23.259  -2.427  1.00 69.23           C  
ANISOU 1029  C   THR A1021     9454   8650   8199    681   -249   -769       C  
ATOM   1030  O   THR A1021      -5.505  24.173  -3.243  1.00 70.54           O  
ANISOU 1030  O   THR A1021     9660   8775   8367    646   -246   -764       O  
ATOM   1031  CB  THR A1021      -6.543  21.356  -3.759  1.00 64.74           C  
ANISOU 1031  CB  THR A1021     8812   8099   7686    655   -225   -790       C  
ATOM   1032  OG1 THR A1021      -7.746  21.236  -2.990  1.00 66.08           O  
ANISOU 1032  OG1 THR A1021     8949   8363   7796    757   -242   -785       O  
ATOM   1033  CG2 THR A1021      -6.221  20.014  -4.398  1.00 63.44           C  
ANISOU 1033  CG2 THR A1021     8609   7908   7588    593   -198   -805       C  
ATOM   1034  N   GLU A1022      -5.945  23.464  -1.154  1.00 70.91           N  
ANISOU 1034  N   GLU A1022     9663   8917   8361    757   -266   -760       N  
ATOM   1035  CA  GLU A1022      -6.217  24.801  -0.639  1.00 72.38           C  
ANISOU 1035  CA  GLU A1022     9900   9111   8491    805   -284   -742       C  
ATOM   1036  C   GLU A1022      -5.156  25.276   0.355  1.00 71.59           C  
ANISOU 1036  C   GLU A1022     9829   8990   8382    787   -286   -737       C  
ATOM   1037  O   GLU A1022      -5.379  26.224   1.107  1.00 72.69           O  
ANISOU 1037  O   GLU A1022    10005   9144   8471    835   -299   -721       O  
ATOM   1038  CB  GLU A1022      -7.616  24.865  -0.020  1.00 74.94           C  
ANISOU 1038  CB  GLU A1022    10202   9516   8755    913   -300   -730       C  
ATOM   1039  CG  GLU A1022      -8.023  23.607   0.727  1.00 77.70           C  
ANISOU 1039  CG  GLU A1022    10480   9937   9104    954   -295   -735       C  
ATOM   1040  CD  GLU A1022      -9.455  23.658   1.222  1.00 80.49           C  
ANISOU 1040  CD  GLU A1022    10801  10382   9400   1055   -304   -721       C  
ATOM   1041  OE1 GLU A1022     -10.137  24.675   0.976  1.00 82.02           O  
ANISOU 1041  OE1 GLU A1022    11031  10576   9555   1099   -318   -708       O  
ATOM   1042  OE2 GLU A1022      -9.900  22.678   1.857  1.00 80.93           O  
ANISOU 1042  OE2 GLU A1022    10790  10512   9449   1092   -296   -721       O  
ATOM   1043  N   GLY A1023      -4.007  24.608   0.353  1.00 69.61           N  
ANISOU 1043  N   GLY A1023     9563   8704   8182    717   -273   -750       N  
ATOM   1044  CA  GLY A1023      -2.852  25.063   1.109  1.00 67.91           C  
ANISOU 1044  CA  GLY A1023     9377   8464   7964    685   -274   -748       C  
ATOM   1045  C   GLY A1023      -2.866  24.789   2.602  1.00 66.20           C  
ANISOU 1045  C   GLY A1023     9149   8293   7710    743   -289   -742       C  
ATOM   1046  O   GLY A1023      -1.961  25.215   3.319  1.00 66.99           O  
ANISOU 1046  O   GLY A1023     9278   8375   7799    720   -293   -739       O  
ATOM   1047  N   TYR A1024      -3.883  24.080   3.078  1.00 63.68           N  
ANISOU 1047  N   TYR A1024     8785   8040   7371    816   -294   -741       N  
ATOM   1048  CA  TYR A1024      -3.973  23.755   4.498  1.00 62.20           C  
ANISOU 1048  CA  TYR A1024     8578   7906   7149    872   -303   -734       C  
ATOM   1049  C   TYR A1024      -3.155  22.513   4.840  1.00 59.56           C  
ANISOU 1049  C   TYR A1024     8196   7574   6861    840   -296   -752       C  
ATOM   1050  O   TYR A1024      -3.162  21.533   4.094  1.00 59.31           O  
ANISOU 1050  O   TYR A1024     8120   7536   6881    812   -281   -769       O  
ATOM   1051  CB  TYR A1024      -5.431  23.567   4.920  1.00 64.51           C  
ANISOU 1051  CB  TYR A1024     8833   8279   7397    965   -307   -721       C  
ATOM   1052  CG  TYR A1024      -6.253  24.834   4.841  1.00 67.57           C  
ANISOU 1052  CG  TYR A1024     9269   8671   7735   1013   -317   -700       C  
ATOM   1053  CD1 TYR A1024      -7.097  25.072   3.765  1.00 68.48           C  
ANISOU 1053  CD1 TYR A1024     9384   8786   7851   1026   -317   -701       C  
ATOM   1054  CD2 TYR A1024      -6.177  25.795   5.838  1.00 69.44           C  
ANISOU 1054  CD2 TYR A1024     9553   8906   7923   1047   -327   -681       C  
ATOM   1055  CE1 TYR A1024      -7.849  26.230   3.689  1.00 69.18           C  
ANISOU 1055  CE1 TYR A1024     9516   8877   7894   1075   -327   -683       C  
ATOM   1056  CE2 TYR A1024      -6.925  26.956   5.772  1.00 70.82           C  
ANISOU 1056  CE2 TYR A1024     9773   9079   8055   1094   -334   -662       C  
ATOM   1057  CZ  TYR A1024      -7.759  27.168   4.695  1.00 70.54           C  
ANISOU 1057  CZ  TYR A1024     9734   9046   8022   1111   -335   -664       C  
ATOM   1058  OH  TYR A1024      -8.504  28.323   4.624  1.00 71.31           O  
ANISOU 1058  OH  TYR A1024     9876   9142   8077   1163   -343   -647       O  
ATOM   1059  N   TYR A1025      -2.453  22.562   5.969  1.00 57.27           N  
ANISOU 1059  N   TYR A1025     7917   7289   6552    844   -306   -749       N  
ATOM   1060  CA  TYR A1025      -1.591  21.460   6.392  1.00 55.07           C  
ANISOU 1060  CA  TYR A1025     7597   7012   6315    818   -303   -768       C  
ATOM   1061  C   TYR A1025      -2.362  20.164   6.615  1.00 53.21           C  
ANISOU 1061  C   TYR A1025     7253   6843   6119    839   -284   -743       C  
ATOM   1062  O   TYR A1025      -3.384  20.141   7.301  1.00 53.56           O  
ANISOU 1062  O   TYR A1025     7270   6958   6122    905   -284   -722       O  
ATOM   1063  CB  TYR A1025      -0.789  21.832   7.642  1.00 55.37           C  
ANISOU 1063  CB  TYR A1025     7667   7052   6320    820   -321   -761       C  
ATOM   1064  CG  TYR A1025       0.444  22.655   7.343  1.00 55.89           C  
ANISOU 1064  CG  TYR A1025     7793   7045   6396    744   -326   -763       C  
ATOM   1065  CD1 TYR A1025       0.519  23.992   7.710  1.00 56.48           C  
ANISOU 1065  CD1 TYR A1025     7935   7105   6419    744   -333   -742       C  
ATOM   1066  CD2 TYR A1025       1.528  22.096   6.680  1.00 56.61           C  
ANISOU 1066  CD2 TYR A1025     7871   7084   6554    670   -319   -785       C  
ATOM   1067  CE1 TYR A1025       1.644  24.746   7.434  1.00 57.93           C  
ANISOU 1067  CE1 TYR A1025     8166   7234   6612    671   -332   -744       C  
ATOM   1068  CE2 TYR A1025       2.655  22.842   6.397  1.00 58.30           C  
ANISOU 1068  CE2 TYR A1025     8132   7242   6777    597   -320   -784       C  
ATOM   1069  CZ  TYR A1025       2.710  24.166   6.777  1.00 59.83           C  
ANISOU 1069  CZ  TYR A1025     8388   7432   6914    597   -325   -765       C  
ATOM   1070  OH  TYR A1025       3.833  24.912   6.497  1.00 61.83           O  
ANISOU 1070  OH  TYR A1025     8679   7641   7174    524   -320   -766       O  
ATOM   1071  N   THR A1026      -1.850  19.086   6.029  1.00 51.30           N  
ANISOU 1071  N   THR A1026     6944   6578   5971    767   -261   -728       N  
ATOM   1072  CA  THR A1026      -2.546  17.808   6.012  1.00 48.34           C  
ANISOU 1072  CA  THR A1026     6462   6256   5649    760   -234   -689       C  
ATOM   1073  C   THR A1026      -1.556  16.656   6.180  1.00 45.68           C  
ANISOU 1073  C   THR A1026     6053   5898   5404    685   -213   -658       C  
ATOM   1074  O   THR A1026      -0.369  16.798   5.884  1.00 46.41           O  
ANISOU 1074  O   THR A1026     6176   5925   5532    630   -215   -673       O  
ATOM   1075  CB  THR A1026      -3.305  17.629   4.680  1.00 46.74           C  
ANISOU 1075  CB  THR A1026     6256   6045   5459    753   -219   -706       C  
ATOM   1076  OG1 THR A1026      -3.873  18.882   4.280  1.00 47.90           O  
ANISOU 1076  OG1 THR A1026     6492   6182   5525    810   -242   -745       O  
ATOM   1077  CG2 THR A1026      -4.412  16.600   4.814  1.00 45.17           C  
ANISOU 1077  CG2 THR A1026     5962   5924   5277    770   -197   -667       C  
ATOM   1078  N   ILE A1027      -2.049  15.520   6.662  1.00 41.96           N  
ANISOU 1078  N   ILE A1027     5489   5485   4968    684   -191   -616       N  
ATOM   1079  CA  ILE A1027      -1.233  14.319   6.786  1.00 39.06           C  
ANISOU 1079  CA  ILE A1027     5052   5103   4687    619   -166   -583       C  
ATOM   1080  C   ILE A1027      -2.102  13.073   6.624  1.00 36.70           C  
ANISOU 1080  C   ILE A1027     4668   4857   4422    612   -133   -549       C  
ATOM   1081  O   ILE A1027      -3.321  13.132   6.787  1.00 38.20           O  
ANISOU 1081  O   ILE A1027     4842   5111   4563    663   -134   -545       O  
ATOM   1082  CB  ILE A1027      -0.492  14.277   8.140  1.00 39.95           C  
ANISOU 1082  CB  ILE A1027     5150   5232   4800    623   -182   -558       C  
ATOM   1083  CG1 ILE A1027       0.766  13.409   8.044  1.00 38.67           C  
ANISOU 1083  CG1 ILE A1027     4944   5025   4724    550   -163   -537       C  
ATOM   1084  CG2 ILE A1027      -1.420  13.799   9.251  1.00 40.60           C  
ANISOU 1084  CG2 ILE A1027     5175   5397   4852    673   -181   -525       C  
ATOM   1085  CD1 ILE A1027       1.559  13.345   9.328  1.00 38.25           C  
ANISOU 1085  CD1 ILE A1027     4874   4986   4674    549   -180   -511       C  
ATOM   1086  N   GLY A1028      -1.475  11.951   6.288  1.00 34.46           N  
ANISOU 1086  N   GLY A1028     4331   4546   4217    546   -101   -524       N  
ATOM   1087  CA  GLY A1028      -2.189  10.698   6.130  1.00 33.55           C  
ANISOU 1087  CA  GLY A1028     4140   4474   4132    528    -65   -490       C  
ATOM   1088  C   GLY A1028      -3.094  10.687   4.913  1.00 33.48           C  
ANISOU 1088  C   GLY A1028     4142   4465   4112    521    -49   -505       C  
ATOM   1089  O   GLY A1028      -2.717  11.168   3.844  1.00 32.99           O  
ANISOU 1089  O   GLY A1028     4132   4336   4065    491    -50   -536       O  
ATOM   1090  N   ILE A1029      -4.291  10.133   5.078  1.00 32.51           N  
ANISOU 1090  N   ILE A1029     3970   4420   3963    546    -36   -485       N  
ATOM   1091  CA  ILE A1029      -5.284  10.119   4.012  1.00 32.43           C  
ANISOU 1091  CA  ILE A1029     3962   4424   3934    542    -24   -494       C  
ATOM   1092  C   ILE A1029      -6.163  11.361   4.101  1.00 35.34           C  
ANISOU 1092  C   ILE A1029     4377   4830   4220    621    -61   -524       C  
ATOM   1093  O   ILE A1029      -7.305  11.293   4.556  1.00 36.31           O  
ANISOU 1093  O   ILE A1029     4465   5039   4294    671    -64   -511       O  
ATOM   1094  CB  ILE A1029      -6.183   8.863   4.083  1.00 29.48           C  
ANISOU 1094  CB  ILE A1029     3511   4121   3567    524     11   -456       C  
ATOM   1095  CG1 ILE A1029      -5.349   7.619   4.385  1.00 27.61           C  
ANISOU 1095  CG1 ILE A1029     3229   3862   3400    463     47   -421       C  
ATOM   1096  CG2 ILE A1029      -6.973   8.687   2.789  1.00 26.03           C  
ANISOU 1096  CG2 ILE A1029     3078   3685   3126    495     29   -461       C  
ATOM   1097  CD1 ILE A1029      -6.140   6.332   4.349  1.00 27.18           C  
ANISOU 1097  CD1 ILE A1029     3109   3867   3350    434     87   -384       C  
ATOM   1098  N   GLY A1030      -5.619  12.498   3.679  1.00 35.50           N  
ANISOU 1098  N   GLY A1030     4478   4787   4222    632    -87   -564       N  
ATOM   1099  CA  GLY A1030      -6.363  13.746   3.657  1.00 36.72           C  
ANISOU 1099  CA  GLY A1030     4690   4964   4296    707   -120   -594       C  
ATOM   1100  C   GLY A1030      -6.911  14.186   5.003  1.00 40.45           C  
ANISOU 1100  C   GLY A1030     5154   5510   4705    786   -141   -584       C  
ATOM   1101  O   GLY A1030      -8.012  14.731   5.080  1.00 41.92           O  
ANISOU 1101  O   GLY A1030     5348   5755   4826    854   -153   -590       O  
ATOM   1102  N   HIS A1031      -6.147  13.952   6.066  1.00 42.62           N  
ANISOU 1102  N   HIS A1031     5413   5782   4999    779   -144   -567       N  
ATOM   1103  CA  HIS A1031      -6.563  14.360   7.405  1.00 43.55           C  
ANISOU 1103  CA  HIS A1031     5528   5961   5060    847   -163   -556       C  
ATOM   1104  C   HIS A1031      -6.061  15.758   7.739  1.00 43.10           C  
ANISOU 1104  C   HIS A1031     5566   5862   4947    887   -196   -588       C  
ATOM   1105  O   HIS A1031      -4.862  15.971   7.914  1.00 43.10           O  
ANISOU 1105  O   HIS A1031     5601   5801   4973    849   -205   -595       O  
ATOM   1106  CB  HIS A1031      -6.060  13.371   8.458  1.00 44.92           C  
ANISOU 1106  CB  HIS A1031     5637   6155   5276    818   -150   -519       C  
ATOM   1107  CG  HIS A1031      -6.494  13.700   9.851  1.00 46.80           C  
ANISOU 1107  CG  HIS A1031     5870   6452   5460    881   -167   -506       C  
ATOM   1108  ND1 HIS A1031      -7.678  13.241  10.391  1.00 47.27           N  
ANISOU 1108  ND1 HIS A1031     5874   6599   5489    922   -157   -485       N  
ATOM   1109  CD2 HIS A1031      -5.906  14.445  10.820  1.00 47.16           C  
ANISOU 1109  CD2 HIS A1031     5964   6480   5474    907   -192   -510       C  
ATOM   1110  CE1 HIS A1031      -7.795  13.688  11.633  1.00 47.53           C  
ANISOU 1110  CE1 HIS A1031     5920   6662   5477    972   -174   -478       C  
ATOM   1111  NE2 HIS A1031      -6.736  14.418  11.912  1.00 47.67           N  
ANISOU 1111  NE2 HIS A1031     6002   6617   5493    963   -196   -492       N  
ATOM   1112  N   LEU A1032      -6.986  16.708   7.830  1.00 44.16           N  
ANISOU 1112  N   LEU A1032     5744   6032   5001    965   -213   -605       N  
ATOM   1113  CA  LEU A1032      -6.637  18.081   8.169  1.00 46.28           C  
ANISOU 1113  CA  LEU A1032     6114   6266   5203   1010   -242   -634       C  
ATOM   1114  C   LEU A1032      -6.126  18.175   9.605  1.00 48.41           C  
ANISOU 1114  C   LEU A1032     6387   6549   5458   1022   -253   -614       C  
ATOM   1115  O   LEU A1032      -6.757  17.668  10.534  1.00 49.14           O  
ANISOU 1115  O   LEU A1032     6420   6709   5541   1053   -246   -584       O  
ATOM   1116  CB  LEU A1032      -7.837  19.006   7.960  1.00 46.88           C  
ANISOU 1116  CB  LEU A1032     6234   6382   5195   1097   -253   -652       C  
ATOM   1117  CG  LEU A1032      -7.635  20.485   8.294  1.00 48.57           C  
ANISOU 1117  CG  LEU A1032     6565   6565   5326   1153   -279   -683       C  
ATOM   1118  CD1 LEU A1032      -8.142  21.361   7.160  1.00 48.58           C  
ANISOU 1118  CD1 LEU A1032     6619   6533   5307   1163   -288   -695       C  
ATOM   1119  CD2 LEU A1032      -8.333  20.840   9.600  1.00 50.28           C  
ANISOU 1119  CD2 LEU A1032     6780   6847   5477   1231   -284   -662       C  
ATOM   1120  N   LEU A1033      -4.977  18.821   9.777  1.00 49.14           N  
ANISOU 1120  N   LEU A1033     6550   6577   5546    994   -270   -631       N  
ATOM   1121  CA  LEU A1033      -4.373  18.982  11.095  1.00 50.24           C  
ANISOU 1121  CA  LEU A1033     6700   6720   5668    996   -283   -612       C  
ATOM   1122  C   LEU A1033      -4.718  20.342  11.689  1.00 52.72           C  
ANISOU 1122  C   LEU A1033     7112   7039   5881   1068   -304   -630       C  
ATOM   1123  O   LEU A1033      -5.163  20.437  12.832  1.00 51.96           O  
ANISOU 1123  O   LEU A1033     7008   6989   5744   1114   -308   -607       O  
ATOM   1124  CB  LEU A1033      -2.853  18.820  11.010  1.00 47.71           C  
ANISOU 1124  CB  LEU A1033     6393   6332   5404    916   -288   -614       C  
ATOM   1125  CG  LEU A1033      -2.332  17.450  10.577  1.00 45.26           C  
ANISOU 1125  CG  LEU A1033     5990   6011   5196    843   -264   -591       C  
ATOM   1126  CD1 LEU A1033      -0.824  17.492  10.396  1.00 45.97           C  
ANISOU 1126  CD1 LEU A1033     6103   6031   5331    772   -270   -599       C  
ATOM   1127  CD2 LEU A1033      -2.723  16.384  11.587  1.00 43.64           C  
ANISOU 1127  CD2 LEU A1033     5693   5871   5019    850   -251   -546       C  
ATOM   1128  N   THR A1034      -4.507  21.392  10.903  1.00 56.92           N  
ANISOU 1128  N   THR A1034     7741   7518   6368   1077   -316   -671       N  
ATOM   1129  CA  THR A1034      -4.802  22.753  11.334  1.00 60.29           C  
ANISOU 1129  CA  THR A1034     8257   7933   6718   1124   -330   -668       C  
ATOM   1130  C   THR A1034      -5.031  23.654  10.124  1.00 62.98           C  
ANISOU 1130  C   THR A1034     8642   8219   7067   1105   -331   -670       C  
ATOM   1131  O   THR A1034      -4.891  23.216   8.982  1.00 61.13           O  
ANISOU 1131  O   THR A1034     8387   7960   6878   1065   -324   -690       O  
ATOM   1132  CB  THR A1034      -3.662  23.332  12.193  1.00 60.14           C  
ANISOU 1132  CB  THR A1034     8300   7871   6681   1087   -345   -661       C  
ATOM   1133  OG1 THR A1034      -4.059  24.601  12.726  1.00 61.05           O  
ANISOU 1133  OG1 THR A1034     8480   7972   6745   1118   -349   -635       O  
ATOM   1134  CG2 THR A1034      -2.400  23.508  11.361  1.00 58.83           C  
ANISOU 1134  CG2 THR A1034     8169   7627   6558   1003   -350   -683       C  
ATOM   1135  N   LYS A1035      -5.384  24.911  10.374  1.00 66.94           N  
ANISOU 1135  N   LYS A1035     9207   8702   7525   1132   -337   -649       N  
ATOM   1136  CA  LYS A1035      -5.622  25.857   9.289  1.00 70.91           C  
ANISOU 1136  CA  LYS A1035     9755   9158   8031   1118   -337   -648       C  
ATOM   1137  C   LYS A1035      -4.721  27.090   9.368  1.00 72.89           C  
ANISOU 1137  C   LYS A1035    10089   9338   8268   1071   -341   -642       C  
ATOM   1138  O   LYS A1035      -4.879  28.037   8.597  1.00 73.12           O  
ANISOU 1138  O   LYS A1035    10162   9329   8293   1060   -340   -638       O  
ATOM   1139  CB  LYS A1035      -7.095  26.266   9.239  1.00 73.63           C  
ANISOU 1139  CB  LYS A1035    10089   9550   8338   1201   -337   -631       C  
ATOM   1140  CG  LYS A1035      -8.019  25.147   8.791  1.00 75.49           C  
ANISOU 1140  CG  LYS A1035    10240   9853   8590   1234   -330   -639       C  
ATOM   1141  CD  LYS A1035      -9.455  25.624   8.669  1.00 77.08           C  
ANISOU 1141  CD  LYS A1035    10431  10103   8752   1315   -331   -621       C  
ATOM   1142  CE  LYS A1035     -10.040  25.979  10.027  1.00 78.39           C  
ANISOU 1142  CE  LYS A1035    10601  10315   8868   1387   -331   -595       C  
ATOM   1143  NZ  LYS A1035     -10.017  24.820  10.961  1.00 78.51           N  
ANISOU 1143  NZ  LYS A1035    10547  10395   8887   1396   -322   -594       N  
ATOM   1144  N   SER A1036      -3.777  27.066  10.303  1.00 73.59           N  
ANISOU 1144  N   SER A1036    10198   9415   8349   1042   -345   -640       N  
ATOM   1145  CA  SER A1036      -2.785  28.126  10.424  1.00 75.20           C  
ANISOU 1145  CA  SER A1036    10473   9559   8541    985   -346   -635       C  
ATOM   1146  C   SER A1036      -1.604  27.849   9.506  1.00 75.93           C  
ANISOU 1146  C   SER A1036    10563   9603   8685    894   -343   -658       C  
ATOM   1147  O   SER A1036      -1.177  26.702   9.377  1.00 76.23           O  
ANISOU 1147  O   SER A1036    10550   9651   8762    871   -345   -677       O  
ATOM   1148  CB  SER A1036      -2.291  28.230  11.867  1.00 77.40           C  
ANISOU 1148  CB  SER A1036    10775   9849   8784    991   -352   -620       C  
ATOM   1149  OG  SER A1036      -1.191  29.120  11.963  1.00 78.53           O  
ANISOU 1149  OG  SER A1036    10979   9939   8918    924   -352   -618       O  
ATOM   1150  N   PRO A1037      -1.062  28.904   8.872  1.00 76.63           N  
ANISOU 1150  N   PRO A1037    10703   9639   8775    842   -337   -658       N  
ATOM   1151  CA  PRO A1037       0.110  28.803   7.992  1.00 76.45           C  
ANISOU 1151  CA  PRO A1037    10678   9569   8799    750   -330   -677       C  
ATOM   1152  C   PRO A1037       1.341  28.270   8.724  1.00 74.60           C  
ANISOU 1152  C   PRO A1037    10439   9330   8575    703   -337   -686       C  
ATOM   1153  O   PRO A1037       2.303  27.841   8.087  1.00 74.17           O  
ANISOU 1153  O   PRO A1037    10367   9247   8568    634   -332   -705       O  
ATOM   1154  CB  PRO A1037       0.348  30.255   7.565  1.00 77.15           C  
ANISOU 1154  CB  PRO A1037    10825   9619   8867    719   -321   -668       C  
ATOM   1155  CG  PRO A1037      -0.984  30.905   7.692  1.00 76.90           C  
ANISOU 1155  CG  PRO A1037    10815   9608   8795    800   -324   -649       C  
ATOM   1156  CD  PRO A1037      -1.602  30.275   8.904  1.00 76.80           C  
ANISOU 1156  CD  PRO A1037    10782   9645   8753    871   -334   -638       C  
ATOM   1157  N   SER A1038       1.301  28.305  10.052  1.00 73.41           N  
ANISOU 1157  N   SER A1038    10303   9208   8381    740   -348   -671       N  
ATOM   1158  CA  SER A1038       2.392  27.802  10.876  1.00 72.27           C  
ANISOU 1158  CA  SER A1038    10156   9067   8238    702   -361   -676       C  
ATOM   1159  C   SER A1038       2.602  26.303  10.709  1.00 71.28           C  
ANISOU 1159  C   SER A1038     9964   8960   8161    700   -369   -699       C  
ATOM   1160  O   SER A1038       1.721  25.504  11.026  1.00 70.64           O  
ANISOU 1160  O   SER A1038     9836   8926   8077    764   -371   -698       O  
ATOM   1161  CB  SER A1038       2.127  28.113  12.349  1.00 71.71           C  
ANISOU 1161  CB  SER A1038    10112   9027   8107    748   -371   -651       C  
ATOM   1162  OG  SER A1038       3.024  27.403  13.186  1.00 71.63           O  
ANISOU 1162  OG  SER A1038    10088   9031   8097    721   -389   -655       O  
ATOM   1163  N   LEU A1039       3.777  25.925  10.218  1.00 70.54           N  
ANISOU 1163  N   LEU A1039     9860   8831   8111    627   -370   -719       N  
ATOM   1164  CA  LEU A1039       4.151  24.520  10.146  1.00 68.92           C  
ANISOU 1164  CA  LEU A1039     9594   8635   7956    621   -379   -743       C  
ATOM   1165  C   LEU A1039       4.302  23.979  11.562  1.00 66.94           C  
ANISOU 1165  C   LEU A1039     9331   8432   7671    657   -404   -737       C  
ATOM   1166  O   LEU A1039       4.087  22.794  11.818  1.00 65.73           O  
ANISOU 1166  O   LEU A1039     9076   8315   7584    661   -395   -709       O  
ATOM   1167  CB  LEU A1039       5.453  24.357   9.362  1.00 68.64           C  
ANISOU 1167  CB  LEU A1039     9557   8546   7977    532   -375   -764       C  
ATOM   1168  CG  LEU A1039       6.060  22.960   9.229  1.00 67.43           C  
ANISOU 1168  CG  LEU A1039     9343   8387   7891    513   -384   -791       C  
ATOM   1169  CD1 LEU A1039       5.024  21.946   8.771  1.00 66.55           C  
ANISOU 1169  CD1 LEU A1039     9141   8304   7840    546   -359   -771       C  
ATOM   1170  CD2 LEU A1039       7.228  23.006   8.260  1.00 66.74           C  
ANISOU 1170  CD2 LEU A1039     9259   8238   7861    424   -373   -807       C  
ATOM   1171  N   ASN A1040       4.664  24.866  12.481  1.00 66.67           N  
ANISOU 1171  N   ASN A1040     9352   8399   7580    647   -414   -713       N  
ATOM   1172  CA  ASN A1040       4.775  24.511  13.887  1.00 66.60           C  
ANISOU 1172  CA  ASN A1040     9338   8435   7531    674   -438   -696       C  
ATOM   1173  C   ASN A1040       3.427  24.164  14.499  1.00 64.88           C  
ANISOU 1173  C   ASN A1040     9077   8277   7299    755   -427   -669       C  
ATOM   1174  O   ASN A1040       3.340  23.337  15.406  1.00 63.90           O  
ANISOU 1174  O   ASN A1040     8869   8194   7216    756   -425   -623       O  
ATOM   1175  CB  ASN A1040       5.414  25.653  14.668  1.00 67.77           C  
ANISOU 1175  CB  ASN A1040     9560   8566   7624    638   -445   -672       C  
ATOM   1176  CG  ASN A1040       6.880  25.817  14.353  1.00 68.03           C  
ANISOU 1176  CG  ASN A1040     9613   8558   7677    549   -455   -686       C  
ATOM   1177  OD1 ASN A1040       7.708  25.016  14.783  1.00 67.77           O  
ANISOU 1177  OD1 ASN A1040     9536   8537   7676    514   -476   -681       O  
ATOM   1178  ND2 ASN A1040       7.214  26.860  13.600  1.00 68.14           N  
ANISOU 1178  ND2 ASN A1040     9667   8530   7694    501   -433   -687       N  
ATOM   1179  N   ALA A1041       2.378  24.806  13.998  1.00 64.44           N  
ANISOU 1179  N   ALA A1041     9049   8219   7216    803   -411   -672       N  
ATOM   1180  CA  ALA A1041       1.029  24.573  14.497  1.00 64.38           C  
ANISOU 1180  CA  ALA A1041     9011   8269   7181    887   -403   -655       C  
ATOM   1181  C   ALA A1041       0.556  23.156  14.184  1.00 63.58           C  
ANISOU 1181  C   ALA A1041     8794   8210   7153    897   -390   -650       C  
ATOM   1182  O   ALA A1041      -0.067  22.503  15.021  1.00 63.44           O  
ANISOU 1182  O   ALA A1041     8707   8247   7150    928   -383   -614       O  
ATOM   1183  CB  ALA A1041       0.067  25.600  13.919  1.00 64.37           C  
ANISOU 1183  CB  ALA A1041     9043   8250   7164    918   -385   -643       C  
ATOM   1184  N   ALA A1042       0.861  22.687  12.976  1.00 62.28           N  
ANISOU 1184  N   ALA A1042     8597   8014   7055    854   -380   -671       N  
ATOM   1185  CA  ALA A1042       0.466  21.352  12.536  1.00 60.10           C  
ANISOU 1185  CA  ALA A1042     8200   7765   6871    840   -357   -649       C  
ATOM   1186  C   ALA A1042       1.140  20.261  13.359  1.00 59.37           C  
ANISOU 1186  C   ALA A1042     8015   7693   6851    793   -353   -603       C  
ATOM   1187  O   ALA A1042       0.511  19.267  13.724  1.00 58.33           O  
ANISOU 1187  O   ALA A1042     7793   7610   6760    809   -337   -571       O  
ATOM   1188  CB  ALA A1042       0.781  21.167  11.060  1.00 58.67           C  
ANISOU 1188  CB  ALA A1042     8018   7533   6741    795   -345   -680       C  
ATOM   1189  N   LYS A1043       2.424  20.451  13.641  1.00 59.51           N  
ANISOU 1189  N   LYS A1043     8056   7672   6882    735   -368   -601       N  
ATOM   1190  CA  LYS A1043       3.186  19.483  14.420  1.00 59.88           C  
ANISOU 1190  CA  LYS A1043     8021   7735   6997    689   -367   -557       C  
ATOM   1191  C   LYS A1043       2.659  19.357  15.847  1.00 61.66           C  
ANISOU 1191  C   LYS A1043     8226   8015   7186    731   -375   -521       C  
ATOM   1192  O   LYS A1043       2.668  18.271  16.426  1.00 62.50           O  
ANISOU 1192  O   LYS A1043     8242   8153   7351    719   -366   -482       O  
ATOM   1193  CB  LYS A1043       4.675  19.843  14.422  1.00 58.37           C  
ANISOU 1193  CB  LYS A1043     7864   7496   6817    620   -384   -563       C  
ATOM   1194  CG  LYS A1043       5.491  19.062  13.403  1.00 56.37           C  
ANISOU 1194  CG  LYS A1043     7555   7205   6660    555   -366   -568       C  
ATOM   1195  CD  LYS A1043       6.934  19.537  13.325  1.00 55.07           C  
ANISOU 1195  CD  LYS A1043     7430   6995   6500    488   -383   -579       C  
ATOM   1196  CE  LYS A1043       7.081  20.700  12.357  1.00 53.81           C  
ANISOU 1196  CE  LYS A1043     7379   6783   6284    479   -390   -637       C  
ATOM   1197  NZ  LYS A1043       8.367  20.625  11.605  1.00 53.15           N  
ANISOU 1197  NZ  LYS A1043     7295   6648   6253    401   -388   -655       N  
ATOM   1198  N   SER A1044       2.194  20.470  16.407  1.00 62.07           N  
ANISOU 1198  N   SER A1044     8368   8074   7141    780   -391   -533       N  
ATOM   1199  CA  SER A1044       1.632  20.463  17.752  1.00 61.69           C  
ANISOU 1199  CA  SER A1044     8315   8073   7053    822   -398   -501       C  
ATOM   1200  C   SER A1044       0.331  19.669  17.792  1.00 60.39           C  
ANISOU 1200  C   SER A1044     8073   7964   6908    875   -376   -487       C  
ATOM   1201  O   SER A1044       0.115  18.856  18.693  1.00 60.47           O  
ANISOU 1201  O   SER A1044     8015   8015   6947    877   -372   -451       O  
ATOM   1202  CB  SER A1044       1.392  21.891  18.244  1.00 63.42           C  
ANISOU 1202  CB  SER A1044     8658   8282   7158    865   -414   -519       C  
ATOM   1203  OG  SER A1044       2.603  22.625  18.297  1.00 64.63           O  
ANISOU 1203  OG  SER A1044     8886   8387   7283    810   -434   -530       O  
ATOM   1204  N   GLU A1045      -0.530  19.909  16.807  1.00 59.61           N  
ANISOU 1204  N   GLU A1045     7988   7870   6792    914   -363   -516       N  
ATOM   1205  CA  GLU A1045      -1.814  19.220  16.715  1.00 60.32           C  
ANISOU 1205  CA  GLU A1045     8008   8018   6895    962   -342   -506       C  
ATOM   1206  C   GLU A1045      -1.635  17.729  16.453  1.00 58.79           C  
ANISOU 1206  C   GLU A1045     7698   7839   6800    914   -321   -481       C  
ATOM   1207  O   GLU A1045      -2.469  16.915  16.849  1.00 59.01           O  
ANISOU 1207  O   GLU A1045     7654   7923   6843    937   -306   -459       O  
ATOM   1208  CB  GLU A1045      -2.678  19.837  15.611  1.00 62.07           C  
ANISOU 1208  CB  GLU A1045     8270   8238   7076   1009   -334   -542       C  
ATOM   1209  CG  GLU A1045      -3.228  21.222  15.925  1.00 63.85           C  
ANISOU 1209  CG  GLU A1045     8604   8463   7194   1079   -347   -563       C  
ATOM   1210  CD  GLU A1045      -4.489  21.183  16.774  1.00 65.66           C  
ANISOU 1210  CD  GLU A1045     8809   8762   7377   1155   -339   -543       C  
ATOM   1211  OE1 GLU A1045      -4.631  20.260  17.603  1.00 65.72           O  
ANISOU 1211  OE1 GLU A1045     8737   8809   7423   1144   -332   -509       O  
ATOM   1212  OE2 GLU A1045      -5.344  22.078  16.606  1.00 66.91           O  
ANISOU 1212  OE2 GLU A1045     9029   8933   7459   1227   -338   -561       O  
ATOM   1213  N   LEU A1046      -0.545  17.378  15.780  1.00 57.38           N  
ANISOU 1213  N   LEU A1046     7506   7612   6685    846   -319   -485       N  
ATOM   1214  CA  LEU A1046      -0.264  15.986  15.459  1.00 57.07           C  
ANISOU 1214  CA  LEU A1046     7367   7578   6739    797   -296   -461       C  
ATOM   1215  C   LEU A1046       0.167  15.214  16.704  1.00 60.58           C  
ANISOU 1215  C   LEU A1046     7755   8048   7214    778   -300   -419       C  
ATOM   1216  O   LEU A1046      -0.267  14.083  16.923  1.00 60.65           O  
ANISOU 1216  O   LEU A1046     7683   8094   7266    775   -279   -393       O  
ATOM   1217  CB  LEU A1046       0.809  15.896  14.372  1.00 53.30           C  
ANISOU 1217  CB  LEU A1046     6896   7035   6319    732   -291   -478       C  
ATOM   1218  CG  LEU A1046       1.142  14.498  13.850  1.00 49.58           C  
ANISOU 1218  CG  LEU A1046     6334   6560   5945    680   -261   -455       C  
ATOM   1219  CD1 LEU A1046      -0.115  13.799  13.355  1.00 47.88           C  
ANISOU 1219  CD1 LEU A1046     6067   6388   5737    707   -233   -451       C  
ATOM   1220  CD2 LEU A1046       2.183  14.580  12.746  1.00 48.87           C  
ANISOU 1220  CD2 LEU A1046     6264   6401   5904    620   -255   -476       C  
ATOM   1221  N   ASP A1047       1.015  15.835  17.519  1.00 63.19           N  
ANISOU 1221  N   ASP A1047     8133   8358   7518    764   -326   -412       N  
ATOM   1222  CA  ASP A1047       1.507  15.207  18.741  1.00 65.68           C  
ANISOU 1222  CA  ASP A1047     8404   8692   7858    744   -335   -372       C  
ATOM   1223  C   ASP A1047       0.383  14.951  19.742  1.00 65.35           C  
ANISOU 1223  C   ASP A1047     8340   8711   7781    797   -332   -354       C  
ATOM   1224  O   ASP A1047       0.394  13.949  20.457  1.00 65.08           O  
ANISOU 1224  O   ASP A1047     8237   8704   7786    784   -325   -322       O  
ATOM   1225  CB  ASP A1047       2.600  16.063  19.386  1.00 69.05           C  
ANISOU 1225  CB  ASP A1047     8897   9087   8254    716   -367   -369       C  
ATOM   1226  CG  ASP A1047       3.843  16.171  18.523  1.00 71.85           C  
ANISOU 1226  CG  ASP A1047     9261   9386   8651    653   -370   -383       C  
ATOM   1227  OD1 ASP A1047       4.033  15.308  17.641  1.00 73.23           O  
ANISOU 1227  OD1 ASP A1047     9374   9548   8900    624   -346   -382       O  
ATOM   1228  OD2 ASP A1047       4.633  17.116  18.731  1.00 72.77           O  
ANISOU 1228  OD2 ASP A1047     9450   9473   8726    631   -395   -393       O  
ATOM   1229  N   LYS A1048      -0.586  15.860  19.788  1.00 65.16           N  
ANISOU 1229  N   LYS A1048     8374   8705   7678    859   -336   -375       N  
ATOM   1230  CA  LYS A1048      -1.727  15.711  20.684  1.00 65.13           C  
ANISOU 1230  CA  LYS A1048     8353   8759   7634    914   -330   -362       C  
ATOM   1231  C   LYS A1048      -2.677  14.618  20.202  1.00 63.60           C  
ANISOU 1231  C   LYS A1048     8072   8612   7480    926   -300   -357       C  
ATOM   1232  O   LYS A1048      -3.354  13.975  21.004  1.00 65.42           O  
ANISOU 1232  O   LYS A1048     8255   8892   7709    946   -291   -337       O  
ATOM   1233  CB  LYS A1048      -2.479  17.037  20.825  1.00 66.34           C  
ANISOU 1233  CB  LYS A1048     8598   8919   7691    980   -340   -385       C  
ATOM   1234  CG  LYS A1048      -1.690  18.129  21.528  1.00 67.65           C  
ANISOU 1234  CG  LYS A1048     8859   9045   7800    972   -367   -385       C  
ATOM   1235  CD  LYS A1048      -2.483  19.424  21.589  1.00 69.40           C  
ANISOU 1235  CD  LYS A1048     9178   9270   7922   1042   -371   -408       C  
ATOM   1236  CE  LYS A1048      -3.818  19.222  22.288  1.00 70.07           C  
ANISOU 1236  CE  LYS A1048     9234   9416   7973   1109   -357   -396       C  
ATOM   1237  NZ  LYS A1048      -4.634  20.468  22.305  1.00 70.42           N  
ANISOU 1237  NZ  LYS A1048     9371   9465   7920   1184   -356   -416       N  
ATOM   1238  N   ALA A1049      -2.720  14.413  18.889  1.00 58.83           N  
ANISOU 1238  N   ALA A1049     7452   7992   6909    909   -284   -376       N  
ATOM   1239  CA  ALA A1049      -3.591  13.403  18.299  1.00 53.92           C  
ANISOU 1239  CA  ALA A1049     6754   7412   6321    911   -253   -372       C  
ATOM   1240  C   ALA A1049      -2.974  12.012  18.391  1.00 51.89           C  
ANISOU 1240  C   ALA A1049     6418   7153   6147    852   -235   -342       C  
ATOM   1241  O   ALA A1049      -3.676  11.025  18.611  1.00 50.42           O  
ANISOU 1241  O   ALA A1049     6166   7016   5976    854   -213   -326       O  
ATOM   1242  CB  ALA A1049      -3.904  13.752  16.852  1.00 52.75           C  
ANISOU 1242  CB  ALA A1049     6626   7245   6172    914   -243   -402       C  
ATOM   1243  N   ILE A1050      -1.657  11.939  18.222  1.00 52.09           N  
ANISOU 1243  N   ILE A1050     6450   7122   6220    798   -243   -336       N  
ATOM   1244  CA  ILE A1050      -0.950  10.663  18.261  1.00 52.52           C  
ANISOU 1244  CA  ILE A1050     6435   7168   6353    744   -225   -307       C  
ATOM   1245  C   ILE A1050      -0.548  10.284  19.684  1.00 52.65           C  
ANISOU 1245  C   ILE A1050     6430   7201   6373    740   -240   -275       C  
ATOM   1246  O   ILE A1050      -0.760   9.151  20.117  1.00 53.85           O  
ANISOU 1246  O   ILE A1050     6519   7383   6557    728   -221   -250       O  
ATOM   1247  CB  ILE A1050       0.300  10.682  17.358  1.00 53.17           C  
ANISOU 1247  CB  ILE A1050     6527   7184   6492    688   -223   -313       C  
ATOM   1248  CG1 ILE A1050      -0.090  11.014  15.916  1.00 54.25           C  
ANISOU 1248  CG1 ILE A1050     6687   7298   6629    686   -207   -345       C  
ATOM   1249  CG2 ILE A1050       1.025   9.347  17.419  1.00 52.93           C  
ANISOU 1249  CG2 ILE A1050     6425   7145   6543    637   -200   -279       C  
ATOM   1250  CD1 ILE A1050      -1.144  10.090  15.339  1.00 54.78           C  
ANISOU 1250  CD1 ILE A1050     6698   7404   6711    692   -172   -340       C  
ATOM   1251  N   GLY A1051       0.031  11.236  20.408  1.00 51.57           N  
ANISOU 1251  N   GLY A1051     6352   7044   6199    746   -273   -277       N  
ATOM   1252  CA  GLY A1051       0.435  11.003  21.782  1.00 51.32           C  
ANISOU 1252  CA  GLY A1051     6310   7025   6165    740   -292   -247       C  
ATOM   1253  C   GLY A1051       1.931  10.825  21.952  1.00 49.95           C  
ANISOU 1253  C   GLY A1051     6129   6809   6042    684   -307   -226       C  
ATOM   1254  O   GLY A1051       2.382  10.157  22.883  1.00 49.69           O  
ANISOU 1254  O   GLY A1051     6059   6785   6035    665   -314   -194       O  
ATOM   1255  N   ARG A1052       2.703  11.423  21.049  1.00 49.92           N  
ANISOU 1255  N   ARG A1052     6160   6759   6050    657   -313   -245       N  
ATOM   1256  CA  ARG A1052       4.159  11.362  21.119  1.00 50.40           C  
ANISOU 1256  CA  ARG A1052     6214   6780   6155    603   -328   -228       C  
ATOM   1257  C   ARG A1052       4.790  12.445  20.254  1.00 52.00           C  
ANISOU 1257  C   ARG A1052     6483   6936   6338    584   -341   -260       C  
ATOM   1258  O   ARG A1052       4.103  13.121  19.489  1.00 51.73           O  
ANISOU 1258  O   ARG A1052     6495   6895   6263    612   -335   -296       O  
ATOM   1259  CB  ARG A1052       4.666   9.990  20.668  1.00 48.18           C  
ANISOU 1259  CB  ARG A1052     5849   6493   5965    565   -298   -204       C  
ATOM   1260  CG  ARG A1052       4.426   9.700  19.195  1.00 46.76           C  
ANISOU 1260  CG  ARG A1052     5656   6291   5821    554   -265   -227       C  
ATOM   1261  CD  ARG A1052       5.115   8.416  18.759  1.00 45.99           C  
ANISOU 1261  CD  ARG A1052     5486   6177   5811    511   -233   -200       C  
ATOM   1262  NE  ARG A1052       4.878   8.118  17.348  1.00 44.32           N  
ANISOU 1262  NE  ARG A1052     5266   5940   5633    496   -198   -219       N  
ATOM   1263  CZ  ARG A1052       5.627   8.577  16.351  1.00 40.83           C  
ANISOU 1263  CZ  ARG A1052     4851   5446   5215    463   -196   -240       C  
ATOM   1264  NH1 ARG A1052       6.666   9.362  16.605  1.00 40.48           N  
ANISOU 1264  NH1 ARG A1052     4842   5374   5163    442   -227   -245       N  
ATOM   1265  NH2 ARG A1052       5.338   8.253  15.098  1.00 37.93           N  
ANISOU 1265  NH2 ARG A1052     4478   5054   4878    447   -163   -257       N  
ATOM   1266  N   ASN A1053       6.103  12.605  20.381  1.00 53.90           N  
ANISOU 1266  N   ASN A1053     6729   7146   6604    535   -359   -248       N  
ATOM   1267  CA  ASN A1053       6.846  13.530  19.537  1.00 57.09           C  
ANISOU 1267  CA  ASN A1053     7192   7504   6995    506   -369   -279       C  
ATOM   1268  C   ASN A1053       7.095  12.917  18.161  1.00 56.40           C  
ANISOU 1268  C   ASN A1053     7065   7385   6978    478   -337   -294       C  
ATOM   1269  O   ASN A1053       7.983  12.080  17.995  1.00 56.41           O  
ANISOU 1269  O   ASN A1053     7007   7372   7054    436   -325   -269       O  
ATOM   1270  CB  ASN A1053       8.165  13.917  20.206  1.00 61.42           C  
ANISOU 1270  CB  ASN A1053     7758   8038   7542    460   -401   -260       C  
ATOM   1271  CG  ASN A1053       9.031  14.795  19.326  1.00 66.47           C  
ANISOU 1271  CG  ASN A1053     8455   8630   8170    421   -410   -292       C  
ATOM   1272  OD1 ASN A1053      10.002  14.329  18.731  1.00 68.77           O  
ANISOU 1272  OD1 ASN A1053     8705   8896   8528    373   -400   -287       O  
ATOM   1273  ND2 ASN A1053       8.681  16.073  19.237  1.00 67.61           N  
ANISOU 1273  ND2 ASN A1053     8699   8762   8228    441   -427   -328       N  
ATOM   1274  N   THR A1054       6.303  13.339  17.179  1.00 53.89           N  
ANISOU 1274  N   THR A1054     6785   7056   6636    501   -322   -332       N  
ATOM   1275  CA  THR A1054       6.318  12.720  15.857  1.00 51.49           C  
ANISOU 1275  CA  THR A1054     6447   6723   6394    477   -288   -345       C  
ATOM   1276  C   THR A1054       7.285  13.385  14.878  1.00 49.66           C  
ANISOU 1276  C   THR A1054     6262   6431   6174    432   -293   -376       C  
ATOM   1277  O   THR A1054       7.747  12.747  13.932  1.00 49.48           O  
ANISOU 1277  O   THR A1054     6203   6374   6221    394   -265   -378       O  
ATOM   1278  CB  THR A1054       4.911  12.711  15.230  1.00 50.49           C  
ANISOU 1278  CB  THR A1054     6329   6616   6240    522   -268   -367       C  
ATOM   1279  OG1 THR A1054       4.449  14.058  15.074  1.00 50.49           O  
ANISOU 1279  OG1 THR A1054     6420   6608   6157    556   -290   -406       O  
ATOM   1280  CG2 THR A1054       3.939  11.947  16.115  1.00 50.31           C  
ANISOU 1280  CG2 THR A1054     6252   6654   6208    561   -259   -338       C  
ATOM   1281  N   ASN A1055       7.580  14.662  15.110  1.00 48.10           N  
ANISOU 1281  N   ASN A1055     6150   6219   5907    435   -325   -402       N  
ATOM   1282  CA  ASN A1055       8.443  15.445  14.223  1.00 47.00           C  
ANISOU 1282  CA  ASN A1055     6070   6024   5763    393   -332   -439       C  
ATOM   1283  C   ASN A1055       7.935  15.497  12.785  1.00 46.10           C  
ANISOU 1283  C   ASN A1055     5977   5874   5664    393   -307   -479       C  
ATOM   1284  O   ASN A1055       8.724  15.526  11.840  1.00 45.41           O  
ANISOU 1284  O   ASN A1055     5899   5737   5619    344   -297   -499       O  
ATOM   1285  CB  ASN A1055       9.886  14.926  14.250  1.00 47.64           C  
ANISOU 1285  CB  ASN A1055     6103   6084   5914    329   -332   -415       C  
ATOM   1286  CG  ASN A1055      10.570  15.164  15.581  1.00 47.81           C  
ANISOU 1286  CG  ASN A1055     6124   6133   5908    318   -365   -383       C  
ATOM   1287  OD1 ASN A1055      11.163  16.218  15.807  1.00 48.16           O  
ANISOU 1287  OD1 ASN A1055     6241   6164   5895    298   -394   -401       O  
ATOM   1288  ND2 ASN A1055      10.501  14.177  16.466  1.00 46.95           N  
ANISOU 1288  ND2 ASN A1055     5938   6063   5838    329   -361   -335       N  
ATOM   1289  N   GLY A1056       6.615  15.501  12.626  1.00 46.10           N  
ANISOU 1289  N   GLY A1056     5984   5901   5632    447   -297   -488       N  
ATOM   1290  CA  GLY A1056       5.999  15.582  11.314  1.00 44.67           C  
ANISOU 1290  CA  GLY A1056     5825   5692   5458    451   -276   -523       C  
ATOM   1291  C   GLY A1056       5.970  14.266  10.558  1.00 42.57           C  
ANISOU 1291  C   GLY A1056     5476   5416   5283    420   -236   -503       C  
ATOM   1292  O   GLY A1056       5.671  14.239   9.365  1.00 43.05           O  
ANISOU 1292  O   GLY A1056     5552   5443   5363    406   -216   -530       O  
ATOM   1293  N   VAL A1057       6.282  13.174  11.251  1.00 38.78           N  
ANISOU 1293  N   VAL A1057     4914   4964   4858    407   -222   -456       N  
ATOM   1294  CA  VAL A1057       6.294  11.850  10.637  1.00 35.67           C  
ANISOU 1294  CA  VAL A1057     4444   4562   4548    376   -180   -431       C  
ATOM   1295  C   VAL A1057       5.492  10.851  11.465  1.00 35.57           C  
ANISOU 1295  C   VAL A1057     4362   4612   4541    408   -165   -390       C  
ATOM   1296  O   VAL A1057       5.690  10.733  12.674  1.00 36.71           O  
ANISOU 1296  O   VAL A1057     4484   4792   4672    424   -184   -363       O  
ATOM   1297  CB  VAL A1057       7.732  11.316  10.465  1.00 34.22           C  
ANISOU 1297  CB  VAL A1057     4225   4337   4441    316   -168   -412       C  
ATOM   1298  CG1 VAL A1057       7.713   9.898   9.912  1.00 33.35           C  
ANISOU 1298  CG1 VAL A1057     4041   4219   4412    289   -119   -382       C  
ATOM   1299  CG2 VAL A1057       8.536  12.232   9.558  1.00 35.06           C  
ANISOU 1299  CG2 VAL A1057     4397   4380   4544    277   -178   -456       C  
ATOM   1300  N   ILE A1058       4.583  10.135  10.810  1.00 34.33           N  
ANISOU 1300  N   ILE A1058     4174   4468   4402    413   -132   -387       N  
ATOM   1301  CA  ILE A1058       3.777   9.125  11.486  1.00 32.78           C  
ANISOU 1301  CA  ILE A1058     3914   4332   4210    437   -113   -352       C  
ATOM   1302  C   ILE A1058       3.934   7.752  10.836  1.00 32.21           C  
ANISOU 1302  C   ILE A1058     3782   4244   4213    394    -64   -325       C  
ATOM   1303  O   ILE A1058       4.746   7.575   9.928  1.00 33.59           O  
ANISOU 1303  O   ILE A1058     3960   4360   4443    346    -44   -330       O  
ATOM   1304  CB  ILE A1058       2.287   9.516  11.511  1.00 32.22           C  
ANISOU 1304  CB  ILE A1058     3862   4311   4070    491   -119   -369       C  
ATOM   1305  CG1 ILE A1058       1.718   9.550  10.091  1.00 32.52           C  
ANISOU 1305  CG1 ILE A1058     3918   4324   4114    478    -95   -395       C  
ATOM   1306  CG2 ILE A1058       2.102  10.859  12.201  1.00 31.38           C  
ANISOU 1306  CG2 ILE A1058     3821   4219   3884    539   -163   -393       C  
ATOM   1307  CD1 ILE A1058       0.245   9.898  10.032  1.00 31.84           C  
ANISOU 1307  CD1 ILE A1058     3843   4292   3962    531   -100   -409       C  
ATOM   1308  N   THR A1059       3.158   6.782  11.313  1.00 30.39           N  
ANISOU 1308  N   THR A1059     3499   4066   3983    409    -42   -296       N  
ATOM   1309  CA  THR A1059       3.191   5.430  10.766  1.00 30.91           C  
ANISOU 1309  CA  THR A1059     3513   4122   4109    370      9   -267       C  
ATOM   1310  C   THR A1059       1.838   5.063  10.166  1.00 32.04           C  
ANISOU 1310  C   THR A1059     3650   4300   4224    379     35   -273       C  
ATOM   1311  O   THR A1059       0.885   5.837  10.252  1.00 32.52           O  
ANISOU 1311  O   THR A1059     3738   4398   4221    422     11   -298       O  
ATOM   1312  CB  THR A1059       3.553   4.390  11.841  1.00 31.17           C  
ANISOU 1312  CB  THR A1059     3489   4185   4170    369     20   -222       C  
ATOM   1313  OG1 THR A1059       2.500   4.312  12.809  1.00 30.03           O  
ANISOU 1313  OG1 THR A1059     3330   4111   3969    414      6   -216       O  
ATOM   1314  CG2 THR A1059       4.853   4.767  12.536  1.00 32.79           C  
ANISOU 1314  CG2 THR A1059     3696   4365   4398    361    -10   -212       C  
ATOM   1315  N   LYS A1060       1.759   3.879   9.563  1.00 31.41           N  
ANISOU 1315  N   LYS A1060     3535   4211   4190    340     85   -249       N  
ATOM   1316  CA  LYS A1060       0.515   3.409   8.962  1.00 32.64           C  
ANISOU 1316  CA  LYS A1060     3680   4403   4319    338    113   -250       C  
ATOM   1317  C   LYS A1060      -0.579   3.237  10.012  1.00 34.51           C  
ANISOU 1317  C   LYS A1060     3890   4727   4497    385    101   -240       C  
ATOM   1318  O   LYS A1060      -1.725   3.629   9.794  1.00 36.04           O  
ANISOU 1318  O   LYS A1060     4093   4965   4636    413     94   -258       O  
ATOM   1319  CB  LYS A1060       0.732   2.094   8.210  1.00 30.97           C  
ANISOU 1319  CB  LYS A1060     3441   4162   4165    279    173   -220       C  
ATOM   1320  CG  LYS A1060      -0.465   1.661   7.375  1.00 31.18           C  
ANISOU 1320  CG  LYS A1060     3465   4216   4166    263    205   -222       C  
ATOM   1321  CD  LYS A1060      -0.184   0.375   6.613  1.00 32.82           C  
ANISOU 1321  CD  LYS A1060     3655   4387   4426    199    268   -190       C  
ATOM   1322  CE  LYS A1060      -0.174  -0.832   7.537  1.00 36.28           C  
ANISOU 1322  CE  LYS A1060     4048   4865   4871    198    296   -149       C  
ATOM   1323  NZ  LYS A1060      -1.523  -1.110   8.104  1.00 37.74           N  
ANISOU 1323  NZ  LYS A1060     4211   5141   4990    225    294   -147       N  
ATOM   1324  N   ASP A1061      -0.219   2.652  11.150  1.00 35.45           N  
ANISOU 1324  N   ASP A1061     3974   4870   4625    394     99   -212       N  
ATOM   1325  CA  ASP A1061      -1.164   2.456  12.245  1.00 36.46           C  
ANISOU 1325  CA  ASP A1061     4078   5076   4699    435     87   -204       C  
ATOM   1326  C   ASP A1061      -1.675   3.784  12.797  1.00 35.84           C  
ANISOU 1326  C   ASP A1061     4034   5027   4555    494     37   -234       C  
ATOM   1327  O   ASP A1061      -2.865   3.930  13.080  1.00 35.16           O  
ANISOU 1327  O   ASP A1061     3941   5004   4412    531     32   -242       O  
ATOM   1328  CB  ASP A1061      -0.527   1.629  13.365  1.00 37.60           C  
ANISOU 1328  CB  ASP A1061     4186   5230   4870    431     91   -170       C  
ATOM   1329  CG  ASP A1061      -0.388   0.163  13.001  1.00 40.72           C  
ANISOU 1329  CG  ASP A1061     4545   5616   5308    384    147   -138       C  
ATOM   1330  OD1 ASP A1061      -0.166  -0.660  13.915  1.00 40.91           O  
ANISOU 1330  OD1 ASP A1061     4540   5662   5343    384    156   -110       O  
ATOM   1331  OD2 ASP A1061      -0.508  -0.169  11.801  1.00 41.97           O  
ANISOU 1331  OD2 ASP A1061     4711   5745   5489    346    183   -140       O  
ATOM   1332  N   GLU A1062      -0.773   4.749  12.944  1.00 35.42           N  
ANISOU 1332  N   GLU A1062     4021   4930   4508    502      3   -249       N  
ATOM   1333  CA  GLU A1062      -1.135   6.069  13.449  1.00 36.17           C  
ANISOU 1333  CA  GLU A1062     4161   5043   4538    555    -42   -276       C  
ATOM   1334  C   GLU A1062      -1.992   6.829  12.441  1.00 35.53           C  
ANISOU 1334  C   GLU A1062     4116   4964   4418    575    -44   -309       C  
ATOM   1335  O   GLU A1062      -2.854   7.623  12.818  1.00 37.07           O  
ANISOU 1335  O   GLU A1062     4337   5202   4547    630    -68   -327       O  
ATOM   1336  CB  GLU A1062       0.119   6.875  13.794  1.00 38.11           C  
ANISOU 1336  CB  GLU A1062     4446   5237   4798    548    -76   -282       C  
ATOM   1337  CG  GLU A1062       0.975   6.244  14.884  1.00 39.87           C  
ANISOU 1337  CG  GLU A1062     4633   5461   5053    533    -81   -248       C  
ATOM   1338  CD  GLU A1062       2.267   7.000  15.132  1.00 40.38           C  
ANISOU 1338  CD  GLU A1062     4732   5477   5133    518   -113   -252       C  
ATOM   1339  OE1 GLU A1062       2.536   7.980  14.407  1.00 39.92           O  
ANISOU 1339  OE1 GLU A1062     4728   5381   5061    514   -128   -284       O  
ATOM   1340  OE2 GLU A1062       3.013   6.612  16.056  1.00 41.84           O  
ANISOU 1340  OE2 GLU A1062     4892   5665   5341    507   -123   -223       O  
ATOM   1341  N   ALA A1063      -1.749   6.578  11.159  1.00 32.92           N  
ANISOU 1341  N   ALA A1063     3792   4588   4128    531    -19   -317       N  
ATOM   1342  CA  ALA A1063      -2.519   7.214  10.097  1.00 31.64           C  
ANISOU 1342  CA  ALA A1063     3664   4423   3934    543    -19   -348       C  
ATOM   1343  C   ALA A1063      -3.936   6.651  10.052  1.00 31.93           C  
ANISOU 1343  C   ALA A1063     3662   4536   3935    562      1   -338       C  
ATOM   1344  O   ALA A1063      -4.874   7.332   9.636  1.00 29.67           O  
ANISOU 1344  O   ALA A1063     3398   4279   3598    599    -11   -360       O  
ATOM   1345  CB  ALA A1063      -1.828   7.029   8.757  1.00 30.46           C  
ANISOU 1345  CB  ALA A1063     3533   4199   3843    483      5   -357       C  
ATOM   1346  N   GLU A1064      -4.081   5.401  10.480  1.00 34.68           N  
ANISOU 1346  N   GLU A1064     3952   4917   4306    538     32   -305       N  
ATOM   1347  CA  GLU A1064      -5.387   4.763  10.552  1.00 37.94           C  
ANISOU 1347  CA  GLU A1064     4324   5408   4682    549     53   -293       C  
ATOM   1348  C   GLU A1064      -6.197   5.367  11.691  1.00 40.64           C  
ANISOU 1348  C   GLU A1064     4665   5821   4956    619     22   -300       C  
ATOM   1349  O   GLU A1064      -7.420   5.489  11.603  1.00 41.87           O  
ANISOU 1349  O   GLU A1064     4806   6042   5059    651     23   -307       O  
ATOM   1350  CB  GLU A1064      -5.235   3.254  10.751  1.00 39.22           C  
ANISOU 1350  CB  GLU A1064     4435   5583   4884    500     96   -257       C  
ATOM   1351  CG  GLU A1064      -6.552   2.498  10.805  1.00 40.85           C  
ANISOU 1351  CG  GLU A1064     4600   5872   5048    501    122   -245       C  
ATOM   1352  CD  GLU A1064      -6.363   1.008  11.002  1.00 42.37           C  
ANISOU 1352  CD  GLU A1064     4753   6071   5273    450    168   -210       C  
ATOM   1353  OE1 GLU A1064      -5.200   0.558  11.076  1.00 41.02           O  
ANISOU 1353  OE1 GLU A1064     4585   5840   5161    418    180   -194       O  
ATOM   1354  OE2 GLU A1064      -7.380   0.286  11.083  1.00 44.97           O  
ANISOU 1354  OE2 GLU A1064     5051   6470   5567    442    192   -199       O  
ATOM   1355  N   LYS A1065      -5.503   5.745  12.761  1.00 41.44           N  
ANISOU 1355  N   LYS A1065     4780   5909   5058    642     -6   -297       N  
ATOM   1356  CA  LYS A1065      -6.140   6.374  13.911  1.00 43.23           C  
ANISOU 1356  CA  LYS A1065     5014   6190   5222    706    -35   -303       C  
ATOM   1357  C   LYS A1065      -6.803   7.683  13.501  1.00 39.84           C  
ANISOU 1357  C   LYS A1065     4634   5770   4734    760    -61   -335       C  
ATOM   1358  O   LYS A1065      -7.956   7.942  13.846  1.00 38.97           O  
ANISOU 1358  O   LYS A1065     4513   5728   4565    811    -65   -340       O  
ATOM   1359  CB  LYS A1065      -5.116   6.626  15.020  1.00 46.88           C  
ANISOU 1359  CB  LYS A1065     5493   6621   5698    710    -61   -293       C  
ATOM   1360  CG  LYS A1065      -5.693   7.291  16.260  1.00 51.01           C  
ANISOU 1360  CG  LYS A1065     6033   7192   6158    772    -90   -297       C  
ATOM   1361  CD  LYS A1065      -4.621   7.535  17.311  1.00 54.54           C  
ANISOU 1361  CD  LYS A1065     6499   7603   6619    767   -116   -285       C  
ATOM   1362  CE  LYS A1065      -5.215   8.134  18.578  1.00 58.00           C  
ANISOU 1362  CE  LYS A1065     6957   8086   6994    823   -141   -286       C  
ATOM   1363  NZ  LYS A1065      -4.178   8.403  19.615  1.00 58.90           N  
ANISOU 1363  NZ  LYS A1065     7095   8165   7118    813   -168   -272       N  
ATOM   1364  N   LEU A1066      -6.068   8.501  12.755  1.00 37.60           N  
ANISOU 1364  N   LEU A1066     4404   5418   4464    750    -76   -357       N  
ATOM   1365  CA  LEU A1066      -6.596   9.769  12.270  1.00 36.63           C  
ANISOU 1365  CA  LEU A1066     4340   5295   4285    800    -99   -389       C  
ATOM   1366  C   LEU A1066      -7.709   9.531  11.256  1.00 37.20           C  
ANISOU 1366  C   LEU A1066     4388   5405   4340    803    -79   -396       C  
ATOM   1367  O   LEU A1066      -8.648  10.321  11.152  1.00 38.00           O  
ANISOU 1367  O   LEU A1066     4511   5546   4380    861    -94   -413       O  
ATOM   1368  CB  LEU A1066      -5.481  10.610  11.646  1.00 34.16           C  
ANISOU 1368  CB  LEU A1066     4093   4894   3993    778   -117   -414       C  
ATOM   1369  CG  LEU A1066      -4.285  10.921  12.549  1.00 33.62           C  
ANISOU 1369  CG  LEU A1066     4051   4785   3939    767   -140   -407       C  
ATOM   1370  CD1 LEU A1066      -3.291  11.832  11.842  1.00 31.74           C  
ANISOU 1370  CD1 LEU A1066     3883   4467   3709    745   -157   -436       C  
ATOM   1371  CD2 LEU A1066      -4.747  11.539  13.862  1.00 34.83           C  
ANISOU 1371  CD2 LEU A1066     4223   4984   4027    829   -165   -404       C  
ATOM   1372  N   PHE A1067      -7.601   8.432  10.516  1.00 35.79           N  
ANISOU 1372  N   PHE A1067     4167   5216   4214    739    -44   -379       N  
ATOM   1373  CA  PHE A1067      -8.595   8.089   9.507  1.00 34.25           C  
ANISOU 1373  CA  PHE A1067     3949   5057   4008    728    -22   -380       C  
ATOM   1374  C   PHE A1067      -9.917   7.675  10.145  1.00 34.47           C  
ANISOU 1374  C   PHE A1067     3923   5189   3983    766    -14   -366       C  
ATOM   1375  O   PHE A1067     -10.986   8.008   9.637  1.00 31.73           O  
ANISOU 1375  O   PHE A1067     3572   4893   3592    796    -16   -375       O  
ATOM   1376  CB  PHE A1067      -8.074   6.983   8.586  1.00 33.81           C  
ANISOU 1376  CB  PHE A1067     3869   4958   4021    643     17   -363       C  
ATOM   1377  CG  PHE A1067      -9.015   6.635   7.466  1.00 33.97           C  
ANISOU 1377  CG  PHE A1067     3871   5006   4028    620     40   -363       C  
ATOM   1378  CD1 PHE A1067      -9.270   7.542   6.451  1.00 32.45           C  
ANISOU 1378  CD1 PHE A1067     3726   4787   3817    633     24   -391       C  
ATOM   1379  CD2 PHE A1067      -9.639   5.399   7.425  1.00 33.49           C  
ANISOU 1379  CD2 PHE A1067     3752   4999   3972    581     78   -333       C  
ATOM   1380  CE1 PHE A1067     -10.133   7.226   5.420  1.00 31.48           C  
ANISOU 1380  CE1 PHE A1067     3587   4691   3683    609     43   -388       C  
ATOM   1381  CE2 PHE A1067     -10.501   5.077   6.393  1.00 32.34           C  
ANISOU 1381  CE2 PHE A1067     3592   4883   3812    553     99   -330       C  
ATOM   1382  CZ  PHE A1067     -10.749   5.991   5.391  1.00 31.56           C  
ANISOU 1382  CZ  PHE A1067     3536   4757   3697    567     81   -356       C  
ATOM   1383  N   ASN A1068      -9.837   6.953  11.259  1.00 39.11           N  
ANISOU 1383  N   ASN A1068     4472   5810   4577    763     -6   -343       N  
ATOM   1384  CA  ASN A1068     -11.027   6.533  11.995  1.00 41.86           C  
ANISOU 1384  CA  ASN A1068     4771   6257   4876    796      2   -331       C  
ATOM   1385  C   ASN A1068     -11.890   7.716  12.417  1.00 42.50           C  
ANISOU 1385  C   ASN A1068     4876   6386   4884    882    -29   -351       C  
ATOM   1386  O   ASN A1068     -13.117   7.618  12.460  1.00 44.21           O  
ANISOU 1386  O   ASN A1068     5057   6686   5053    914    -22   -349       O  
ATOM   1387  CB  ASN A1068     -10.642   5.702  13.221  1.00 44.12           C  
ANISOU 1387  CB  ASN A1068     5025   6557   5180    781     10   -309       C  
ATOM   1388  CG  ASN A1068     -10.151   4.316  12.855  1.00 44.66           C  
ANISOU 1388  CG  ASN A1068     5058   6605   5307    702     50   -284       C  
ATOM   1389  OD1 ASN A1068      -9.928   4.013  11.682  1.00 45.44           O  
ANISOU 1389  OD1 ASN A1068     5161   6665   5438    653     72   -283       O  
ATOM   1390  ND2 ASN A1068      -9.978   3.465  13.860  1.00 43.40           N  
ANISOU 1390  ND2 ASN A1068     4867   6467   5157    688     62   -263       N  
ATOM   1391  N   GLN A1069     -11.241   8.834  12.723  1.00 41.30           N  
ANISOU 1391  N   GLN A1069     4788   6183   4723    920    -61   -369       N  
ATOM   1392  CA  GLN A1069     -11.952  10.060  13.063  1.00 43.05           C  
ANISOU 1392  CA  GLN A1069     5049   6437   4873   1004    -88   -388       C  
ATOM   1393  C   GLN A1069     -12.710  10.603  11.854  1.00 42.92           C  
ANISOU 1393  C   GLN A1069     5046   6435   4828   1026    -89   -406       C  
ATOM   1394  O   GLN A1069     -13.887  10.951  11.956  1.00 43.95           O  
ANISOU 1394  O   GLN A1069     5160   6640   4899   1085    -92   -409       O  
ATOM   1395  CB  GLN A1069     -10.980  11.116  13.591  1.00 45.66           C  
ANISOU 1395  CB  GLN A1069     5453   6698   5196   1029   -119   -403       C  
ATOM   1396  CG  GLN A1069     -10.295  10.738  14.895  1.00 48.95           C  
ANISOU 1396  CG  GLN A1069     5861   7105   5631   1016   -124   -385       C  
ATOM   1397  CD  GLN A1069      -9.319  11.799  15.367  1.00 51.40           C  
ANISOU 1397  CD  GLN A1069     6249   7350   5929   1032   -155   -397       C  
ATOM   1398  OE1 GLN A1069      -8.950  12.699  14.612  1.00 52.49           O  
ANISOU 1398  OE1 GLN A1069     6448   7437   6057   1039   -169   -421       O  
ATOM   1399  NE2 GLN A1069      -8.898  11.700  16.623  1.00 51.92           N  
ANISOU 1399  NE2 GLN A1069     6316   7416   5994   1035   -165   -381       N  
ATOM   1400  N   ASP A1070     -12.030  10.669  10.713  1.00 41.94           N  
ANISOU 1400  N   ASP A1070     4952   6239   4745    978    -86   -418       N  
ATOM   1401  CA  ASP A1070     -12.622  11.207   9.490  1.00 43.36           C  
ANISOU 1401  CA  ASP A1070     5154   6419   4902    991    -90   -437       C  
ATOM   1402  C   ASP A1070     -13.749  10.328   8.956  1.00 42.73           C  
ANISOU 1402  C   ASP A1070     5003   6419   4814    972    -63   -419       C  
ATOM   1403  O   ASP A1070     -14.680  10.821   8.321  1.00 40.89           O  
ANISOU 1403  O   ASP A1070     4771   6227   4537   1009    -70   -429       O  
ATOM   1404  CB  ASP A1070     -11.554  11.416   8.414  1.00 45.68           C  
ANISOU 1404  CB  ASP A1070     5499   6611   5247    935    -91   -455       C  
ATOM   1405  CG  ASP A1070     -10.616  12.563   8.739  1.00 48.27           C  
ANISOU 1405  CG  ASP A1070     5910   6868   5563    963   -122   -481       C  
ATOM   1406  OD1 ASP A1070     -10.297  12.751   9.931  1.00 49.55           O  
ANISOU 1406  OD1 ASP A1070     6079   7038   5711    990   -134   -473       O  
ATOM   1407  OD2 ASP A1070     -10.202  13.280   7.804  1.00 49.53           O  
ANISOU 1407  OD2 ASP A1070     6131   6962   5725    954   -133   -508       O  
ATOM   1408  N   VAL A1071     -13.657   9.026   9.211  1.00 44.32           N  
ANISOU 1408  N   VAL A1071     5144   6642   5054    911    -33   -392       N  
ATOM   1409  CA  VAL A1071     -14.722   8.101   8.842  1.00 45.38           C  
ANISOU 1409  CA  VAL A1071     5211   6858   5174    885     -5   -372       C  
ATOM   1410  C   VAL A1071     -15.972   8.385   9.664  1.00 46.59           C  
ANISOU 1410  C   VAL A1071     5329   7119   5255    960    -15   -369       C  
ATOM   1411  O   VAL A1071     -17.067   8.519   9.117  1.00 47.37           O  
ANISOU 1411  O   VAL A1071     5401   7285   5311    984    -13   -369       O  
ATOM   1412  CB  VAL A1071     -14.302   6.635   9.052  1.00 46.15           C  
ANISOU 1412  CB  VAL A1071     5261   6953   5321    805     32   -344       C  
ATOM   1413  CG1 VAL A1071     -15.497   5.708   8.892  1.00 46.46           C  
ANISOU 1413  CG1 VAL A1071     5233   7090   5329    782     60   -323       C  
ATOM   1414  CG2 VAL A1071     -13.208   6.260   8.080  1.00 46.97           C  
ANISOU 1414  CG2 VAL A1071     5394   6958   5495    728     48   -343       C  
ATOM   1415  N   ASP A1072     -15.798   8.479  10.979  1.00 48.00           N  
ANISOU 1415  N   ASP A1072     5506   7311   5421    997    -24   -366       N  
ATOM   1416  CA  ASP A1072     -16.903   8.777  11.885  1.00 49.24           C  
ANISOU 1416  CA  ASP A1072     5634   7563   5512   1070    -31   -365       C  
ATOM   1417  C   ASP A1072     -17.551  10.114  11.546  1.00 45.96           C  
ANISOU 1417  C   ASP A1072     5258   7165   5039   1154    -57   -385       C  
ATOM   1418  O   ASP A1072     -18.772  10.250  11.600  1.00 44.96           O  
ANISOU 1418  O   ASP A1072     5094   7131   4858   1204    -56   -382       O  
ATOM   1419  CB  ASP A1072     -16.427   8.777  13.340  1.00 52.52           C  
ANISOU 1419  CB  ASP A1072     6059   7969   5928   1091    -40   -360       C  
ATOM   1420  CG  ASP A1072     -16.120   7.384  13.854  1.00 55.43           C  
ANISOU 1420  CG  ASP A1072     6377   8349   6337   1022    -12   -338       C  
ATOM   1421  OD1 ASP A1072     -16.728   6.416  13.350  1.00 55.43           O  
ANISOU 1421  OD1 ASP A1072     6323   8401   6338    976     17   -324       O  
ATOM   1422  OD2 ASP A1072     -15.274   7.257  14.765  1.00 57.71           O  
ANISOU 1422  OD2 ASP A1072     6683   8594   6652   1013    -19   -333       O  
ATOM   1423  N   ALA A1073     -16.725  11.094  11.191  1.00 43.33           N  
ANISOU 1423  N   ALA A1073     5003   6744   4715   1171    -80   -406       N  
ATOM   1424  CA  ALA A1073     -17.213  12.411  10.797  1.00 41.16           C  
ANISOU 1424  CA  ALA A1073     4781   6472   4385   1250   -105   -428       C  
ATOM   1425  C   ALA A1073     -18.008  12.331   9.498  1.00 41.40           C  
ANISOU 1425  C   ALA A1073     4787   6539   4405   1241    -98   -430       C  
ATOM   1426  O   ALA A1073     -19.012  13.023   9.329  1.00 41.42           O  
ANISOU 1426  O   ALA A1073     4789   6601   4347   1314   -109   -435       O  
ATOM   1427  CB  ALA A1073     -16.055  13.384  10.651  1.00 39.47           C  
ANISOU 1427  CB  ALA A1073     4662   6151   4185   1256   -128   -452       C  
ATOM   1428  N   ALA A1074     -17.550  11.481   8.583  1.00 40.63           N  
ANISOU 1428  N   ALA A1074     4670   6402   4364   1150    -80   -423       N  
ATOM   1429  CA  ALA A1074     -18.232  11.280   7.311  1.00 39.02           C  
ANISOU 1429  CA  ALA A1074     4445   6227   4156   1124    -72   -420       C  
ATOM   1430  C   ALA A1074     -19.596  10.630   7.523  1.00 38.99           C  
ANISOU 1430  C   ALA A1074     4355   6350   4110   1138    -55   -397       C  
ATOM   1431  O   ALA A1074     -20.580  11.015   6.893  1.00 39.16           O  
ANISOU 1431  O   ALA A1074     4360   6432   4088   1174    -62   -398       O  
ATOM   1432  CB  ALA A1074     -17.377  10.435   6.377  1.00 37.04           C  
ANISOU 1432  CB  ALA A1074     4196   5900   3978   1018    -50   -415       C  
ATOM   1433  N   VAL A1075     -19.645   9.645   8.414  1.00 39.72           N  
ANISOU 1433  N   VAL A1075     4392   6485   4213   1107    -33   -377       N  
ATOM   1434  CA  VAL A1075     -20.897   8.972   8.748  1.00 42.77           C  
ANISOU 1434  CA  VAL A1075     4696   6996   4557   1114    -15   -356       C  
ATOM   1435  C   VAL A1075     -21.882   9.955   9.381  1.00 46.11           C  
ANISOU 1435  C   VAL A1075     5116   7497   4908   1226    -37   -364       C  
ATOM   1436  O   VAL A1075     -23.079   9.918   9.093  1.00 47.00           O  
ANISOU 1436  O   VAL A1075     5185   7699   4974   1243    -36   -352       O  
ATOM   1437  CB  VAL A1075     -20.660   7.770   9.691  1.00 40.61           C  
ANISOU 1437  CB  VAL A1075     4377   6744   4307   1060     11   -338       C  
ATOM   1438  CG1 VAL A1075     -21.980   7.146  10.116  1.00 39.50           C  
ANISOU 1438  CG1 VAL A1075     4158   6735   4114   1069     28   -321       C  
ATOM   1439  CG2 VAL A1075     -19.775   6.735   9.013  1.00 39.94           C  
ANISOU 1439  CG2 VAL A1075     4296   6591   4290    952     38   -326       C  
ATOM   1440  N   ARG A1076     -21.365  10.841  10.230  1.00 47.61           N  
ANISOU 1440  N   ARG A1076     5362   7640   5088   1289    -57   -380       N  
ATOM   1441  CA  ARG A1076     -22.174  11.889  10.845  1.00 49.57           C  
ANISOU 1441  CA  ARG A1076     5639   7927   5269   1379    -81   -381       C  
ATOM   1442  C   ARG A1076     -22.862  12.734   9.781  1.00 46.44           C  
ANISOU 1442  C   ARG A1076     5262   7550   4834   1426    -98   -389       C  
ATOM   1443  O   ARG A1076     -24.047  13.043   9.890  1.00 50.13           O  
ANISOU 1443  O   ARG A1076     5710   8091   5244   1466   -107   -375       O  
ATOM   1444  CB  ARG A1076     -21.311  12.787  11.738  1.00 54.80           C  
ANISOU 1444  CB  ARG A1076     6376   8516   5929   1431   -100   -398       C  
ATOM   1445  CG  ARG A1076     -20.813  12.129  13.018  1.00 58.89           C  
ANISOU 1445  CG  ARG A1076     6877   9028   6471   1404    -89   -387       C  
ATOM   1446  CD  ARG A1076     -19.789  13.008  13.725  1.00 63.54           C  
ANISOU 1446  CD  ARG A1076     7543   9536   7062   1447   -106   -405       C  
ATOM   1447  NE  ARG A1076     -19.138  12.317  14.834  1.00 69.00           N  
ANISOU 1447  NE  ARG A1076     8220  10210   7786   1410    -97   -395       N  
ATOM   1448  CZ  ARG A1076     -18.181  12.850  15.589  1.00 73.23           C  
ANISOU 1448  CZ  ARG A1076     8820  10672   8331   1418   -113   -401       C  
ATOM   1449  NH1 ARG A1076     -17.760  14.086  15.355  1.00 74.83           N  
ANISOU 1449  NH1 ARG A1076     9108  10814   8508   1464   -136   -420       N  
ATOM   1450  NH2 ARG A1076     -17.644  12.148  16.578  1.00 73.81           N  
ANISOU 1450  NH2 ARG A1076     8875  10733   8435   1379   -107   -388       N  
ATOM   1451  N   GLY A1077     -22.112  13.097   8.746  1.00 41.91           N  
ANISOU 1451  N   GLY A1077     4729   6905   4290   1418   -102   -413       N  
ATOM   1452  CA  GLY A1077     -22.640  13.904   7.664  1.00 41.38           C  
ANISOU 1452  CA  GLY A1077     4690   6844   4191   1460   -119   -425       C  
ATOM   1453  C   GLY A1077     -23.661  13.166   6.819  1.00 41.62           C  
ANISOU 1453  C   GLY A1077     4640   6963   4210   1423   -105   -405       C  
ATOM   1454  O   GLY A1077     -24.668  13.743   6.409  1.00 43.02           O  
ANISOU 1454  O   GLY A1077     4813   7196   4335   1472   -121   -399       O  
ATOM   1455  N   ILE A1078     -23.399  11.889   6.558  1.00 39.92           N  
ANISOU 1455  N   ILE A1078     4376   6748   4045   1317    -79   -387       N  
ATOM   1456  CA  ILE A1078     -24.320  11.053   5.792  1.00 40.80           C  
ANISOU 1456  CA  ILE A1078     4413   6945   4145   1266    -61   -364       C  
ATOM   1457  C   ILE A1078     -25.669  10.914   6.498  1.00 43.81           C  
ANISOU 1457  C   ILE A1078     4735   7447   4464   1302    -62   -340       C  
ATOM   1458  O   ILE A1078     -26.725  11.043   5.874  1.00 43.67           O  
ANISOU 1458  O   ILE A1078     4685   7503   4402   1315    -68   -328       O  
ATOM   1459  CB  ILE A1078     -23.722   9.653   5.526  1.00 39.00           C  
ANISOU 1459  CB  ILE A1078     4156   6685   3978   1139    -28   -346       C  
ATOM   1460  CG1 ILE A1078     -22.523   9.760   4.580  1.00 37.24           C  
ANISOU 1460  CG1 ILE A1078     4004   6327   3818   1077    -31   -361       C  
ATOM   1461  CG2 ILE A1078     -24.773   8.716   4.948  1.00 38.81           C  
ANISOU 1461  CG2 ILE A1078     4052   6764   3929   1084     -5   -319       C  
ATOM   1462  CD1 ILE A1078     -21.904   8.427   4.214  1.00 34.44           C  
ANISOU 1462  CD1 ILE A1078     3629   5932   3523    955      5   -342       C  
ATOM   1463  N   LEU A1079     -25.626  10.664   7.803  1.00 46.59           N  
ANISOU 1463  N   LEU A1079     5086   7806   4811   1306    -59   -332       N  
ATOM   1464  CA  LEU A1079     -26.839  10.506   8.601  1.00 49.75           C  
ANISOU 1464  CA  LEU A1079     5449   8301   5155   1325    -61   -310       C  
ATOM   1465  C   LEU A1079     -27.633  11.806   8.699  1.00 54.66           C  
ANISOU 1465  C   LEU A1079     6105   8951   5711   1426    -87   -315       C  
ATOM   1466  O   LEU A1079     -28.831  11.792   8.976  1.00 56.63           O  
ANISOU 1466  O   LEU A1079     6321   9291   5907   1447    -86   -298       O  
ATOM   1467  CB  LEU A1079     -26.495   9.994  10.002  1.00 47.03           C  
ANISOU 1467  CB  LEU A1079     5102   7945   4823   1309    -51   -305       C  
ATOM   1468  CG  LEU A1079     -25.910   8.584  10.063  1.00 44.53           C  
ANISOU 1468  CG  LEU A1079     4747   7616   4559   1208    -22   -295       C  
ATOM   1469  CD1 LEU A1079     -25.471   8.236  11.476  1.00 43.58           C  
ANISOU 1469  CD1 LEU A1079     4634   7473   4450   1205    -17   -295       C  
ATOM   1470  CD2 LEU A1079     -26.922   7.574   9.547  1.00 44.37           C  
ANISOU 1470  CD2 LEU A1079     4658   7685   4515   1142     -4   -271       C  
ATOM   1471  N   ARG A1080     -26.961  12.928   8.471  1.00 57.22           N  
ANISOU 1471  N   ARG A1080     6504   9197   6040   1487   -107   -339       N  
ATOM   1472  CA  ARG A1080     -27.625  14.225   8.491  1.00 59.74           C  
ANISOU 1472  CA  ARG A1080     6871   9533   6296   1583   -130   -344       C  
ATOM   1473  C   ARG A1080     -27.985  14.694   7.085  1.00 60.30           C  
ANISOU 1473  C   ARG A1080     6947   9613   6352   1602   -141   -352       C  
ATOM   1474  O   ARG A1080     -28.422  15.828   6.889  1.00 61.77           O  
ANISOU 1474  O   ARG A1080     7182   9800   6487   1682   -160   -360       O  
ATOM   1475  CB  ARG A1080     -26.760  15.256   9.214  1.00 62.04           C  
ANISOU 1475  CB  ARG A1080     7251   9734   6586   1643   -148   -364       C  
ATOM   1476  CG  ARG A1080     -26.779  15.088  10.722  1.00 64.77           C  
ANISOU 1476  CG  ARG A1080     7597  10092   6922   1652   -142   -353       C  
ATOM   1477  CD  ARG A1080     -25.455  15.472  11.350  1.00 67.27           C  
ANISOU 1477  CD  ARG A1080     7980  10306   7274   1658   -150   -370       C  
ATOM   1478  NE  ARG A1080     -25.441  15.193  12.783  1.00 71.04           N  
ANISOU 1478  NE  ARG A1080     8450  10796   7746   1659   -142   -359       N  
ATOM   1479  CZ  ARG A1080     -25.256  13.986  13.311  1.00 72.91           C  
ANISOU 1479  CZ  ARG A1080     8629  11052   8021   1590   -121   -349       C  
ATOM   1480  NH1 ARG A1080     -25.073  12.932  12.525  1.00 72.88           N  
ANISOU 1480  NH1 ARG A1080     8570  11059   8061   1513   -104   -346       N  
ATOM   1481  NH2 ARG A1080     -25.258  13.831  14.628  1.00 73.35           N  
ANISOU 1481  NH2 ARG A1080     8685  11116   8068   1599   -117   -342       N  
ATOM   1482  N   ASN A1081     -27.801  13.808   6.110  1.00 58.36           N  
ANISOU 1482  N   ASN A1081     6652   9374   6147   1526   -127   -349       N  
ATOM   1483  CA  ASN A1081     -28.200  14.082   4.735  1.00 57.19           C  
ANISOU 1483  CA  ASN A1081     6496   9245   5988   1532   -135   -353       C  
ATOM   1484  C   ASN A1081     -29.415  13.242   4.355  1.00 57.05           C  
ANISOU 1484  C   ASN A1081     6389   9345   5941   1486   -119   -321       C  
ATOM   1485  O   ASN A1081     -29.355  12.012   4.364  1.00 57.68           O  
ANISOU 1485  O   ASN A1081     6409   9454   6051   1396    -96   -304       O  
ATOM   1486  CB  ASN A1081     -27.046  13.806   3.771  1.00 55.26           C  
ANISOU 1486  CB  ASN A1081     6270   8914   5812   1480   -131   -375       C  
ATOM   1487  CG  ASN A1081     -27.339  14.284   2.362  1.00 54.41           C  
ANISOU 1487  CG  ASN A1081     6178   8803   5694   1490   -147   -383       C  
ATOM   1488  OD1 ASN A1081     -28.003  13.597   1.585  1.00 53.93           O  
ANISOU 1488  OD1 ASN A1081     6056   8806   5631   1432   -138   -361       O  
ATOM   1489  ND2 ASN A1081     -26.840  15.468   2.024  1.00 53.82           N  
ANISOU 1489  ND2 ASN A1081     6199   8640   5610   1550   -173   -414       N  
ATOM   1490  N   ALA A1082     -30.512  13.913   4.020  1.00 55.28           N  
ANISOU 1490  N   ALA A1082     6161   9188   5655   1545   -129   -314       N  
ATOM   1491  CA  ALA A1082     -31.782  13.240   3.761  1.00 53.65           C  
ANISOU 1491  CA  ALA A1082     5874   9102   5409   1510   -113   -284       C  
ATOM   1492  C   ALA A1082     -31.747  12.309   2.549  1.00 53.02           C  
ANISOU 1492  C   ALA A1082     5739   9046   5362   1418   -103   -271       C  
ATOM   1493  O   ALA A1082     -32.512  11.348   2.478  1.00 54.40           O  
ANISOU 1493  O   ALA A1082     5843   9309   5518   1353    -85   -242       O  
ATOM   1494  CB  ALA A1082     -32.899  14.263   3.612  1.00 53.18           C  
ANISOU 1494  CB  ALA A1082     5827   9101   5279   1600   -121   -282       C  
ATOM   1495  N   LYS A1083     -30.860  12.594   1.601  1.00 50.35           N  
ANISOU 1495  N   LYS A1083     5435   8626   5068   1411   -116   -291       N  
ATOM   1496  CA  LYS A1083     -30.780  11.806   0.375  1.00 48.80           C  
ANISOU 1496  CA  LYS A1083     5190   8446   4904   1325   -109   -279       C  
ATOM   1497  C   LYS A1083     -29.870  10.589   0.526  1.00 46.02           C  
ANISOU 1497  C   LYS A1083     4828   8041   4615   1210    -76   -274       C  
ATOM   1498  O   LYS A1083     -29.999   9.613  -0.213  1.00 45.15           O  
ANISOU 1498  O   LYS A1083     4685   7947   4521   1101    -55   -251       O  
ATOM   1499  CB  LYS A1083     -30.296  12.674  -0.790  1.00 49.47           C  
ANISOU 1499  CB  LYS A1083     5351   8440   5007   1343   -137   -302       C  
ATOM   1500  CG  LYS A1083     -31.217  13.833  -1.139  1.00 50.28           C  
ANISOU 1500  CG  LYS A1083     5462   8597   5045   1454   -168   -306       C  
ATOM   1501  CD  LYS A1083     -30.657  14.637  -2.303  1.00 51.06           C  
ANISOU 1501  CD  LYS A1083     5650   8588   5162   1458   -196   -332       C  
ATOM   1502  CE  LYS A1083     -31.575  15.787  -2.684  1.00 53.57           C  
ANISOU 1502  CE  LYS A1083     5983   8954   5416   1568   -223   -336       C  
ATOM   1503  NZ  LYS A1083     -31.052  16.540  -3.860  1.00 54.51           N  
ANISOU 1503  NZ  LYS A1083     6192   8971   5547   1569   -255   -362       N  
ATOM   1504  N   LEU A1084     -28.956  10.651   1.488  1.00 43.81           N  
ANISOU 1504  N   LEU A1084     4588   7688   4369   1225    -70   -292       N  
ATOM   1505  CA  LEU A1084     -27.966   9.594   1.669  1.00 40.82           C  
ANISOU 1505  CA  LEU A1084     4221   7235   4054   1118    -40   -288       C  
ATOM   1506  C   LEU A1084     -28.287   8.681   2.850  1.00 41.42           C  
ANISOU 1506  C   LEU A1084     4231   7391   4116   1101    -14   -271       C  
ATOM   1507  O   LEU A1084     -27.856   7.529   2.885  1.00 41.56           O  
ANISOU 1507  O   LEU A1084     4230   7392   4169   1002     19   -257       O  
ATOM   1508  CB  LEU A1084     -26.572  10.199   1.844  1.00 37.48           C  
ANISOU 1508  CB  LEU A1084     3894   6662   3684   1130    -52   -319       C  
ATOM   1509  CG  LEU A1084     -26.065  11.058   0.685  1.00 35.54           C  
ANISOU 1509  CG  LEU A1084     3730   6316   3459   1132    -76   -343       C  
ATOM   1510  CD1 LEU A1084     -24.734  11.704   1.037  1.00 34.74           C  
ANISOU 1510  CD1 LEU A1084     3720   6080   3400   1151    -88   -375       C  
ATOM   1511  CD2 LEU A1084     -25.944  10.225  -0.582  1.00 34.20           C  
ANISOU 1511  CD2 LEU A1084     3555   6114   3326   1012    -57   -327       C  
ATOM   1512  N   LYS A1085     -29.039   9.201   3.815  1.00 40.54           N  
ANISOU 1512  N   LYS A1085     4122   7328   3953   1172    -35   -266       N  
ATOM   1513  CA  LYS A1085     -29.378   8.441   5.019  1.00 40.86           C  
ANISOU 1513  CA  LYS A1085     4135   7410   3980   1143    -22   -248       C  
ATOM   1514  C   LYS A1085     -30.131   7.119   4.771  1.00 41.07           C  
ANISOU 1514  C   LYS A1085     4094   7520   3990   1043      2   -217       C  
ATOM   1515  O   LYS A1085     -29.731   6.085   5.307  1.00 40.43           O  
ANISOU 1515  O   LYS A1085     4003   7422   3938    971     25   -208       O  
ATOM   1516  CB  LYS A1085     -30.121   9.318   6.039  1.00 41.39           C  
ANISOU 1516  CB  LYS A1085     4221   7516   3990   1238    -44   -251       C  
ATOM   1517  CG  LYS A1085     -30.325   8.656   7.392  1.00 40.94           C  
ANISOU 1517  CG  LYS A1085     4146   7487   3924   1218    -34   -240       C  
ATOM   1518  CD  LYS A1085     -31.073   9.568   8.351  1.00 42.35           C  
ANISOU 1518  CD  LYS A1085     4343   7703   4044   1312    -51   -243       C  
ATOM   1519  CE  LYS A1085     -31.072   8.999   9.761  1.00 43.05           C  
ANISOU 1519  CE  LYS A1085     4424   7801   4134   1297    -44   -238       C  
ATOM   1520  NZ  LYS A1085     -31.695   7.648   9.814  1.00 43.62           N  
ANISOU 1520  NZ  LYS A1085     4430   7946   4197   1209    -26   -216       N  
ATOM   1521  N   PRO A1086     -31.218   7.142   3.968  1.00 40.75           N  
ANISOU 1521  N   PRO A1086     4014   7568   3902   1038     -4   -198       N  
ATOM   1522  CA  PRO A1086     -31.947   5.887   3.735  1.00 42.34           C  
ANISOU 1522  CA  PRO A1086     4159   7847   4083    938     16   -167       C  
ATOM   1523  C   PRO A1086     -31.104   4.810   3.052  1.00 45.90           C  
ANISOU 1523  C   PRO A1086     4610   8241   4591    820     49   -159       C  
ATOM   1524  O   PRO A1086     -31.258   3.627   3.360  1.00 46.60           O  
ANISOU 1524  O   PRO A1086     4678   8347   4682    733     69   -139       O  
ATOM   1525  CB  PRO A1086     -33.087   6.313   2.805  1.00 40.65           C  
ANISOU 1525  CB  PRO A1086     3910   7725   3811    960      2   -152       C  
ATOM   1526  CG  PRO A1086     -33.273   7.757   3.076  1.00 40.08           C  
ANISOU 1526  CG  PRO A1086     3874   7642   3710   1088    -24   -173       C  
ATOM   1527  CD  PRO A1086     -31.899   8.283   3.326  1.00 39.13           C  
ANISOU 1527  CD  PRO A1086     3816   7398   3652   1121    -28   -204       C  
ATOM   1528  N   VAL A1087     -30.232   5.216   2.136  1.00 47.10           N  
ANISOU 1528  N   VAL A1087     4791   8319   4787    818     56   -175       N  
ATOM   1529  CA  VAL A1087     -29.384   4.270   1.421  1.00 47.32           C  
ANISOU 1529  CA  VAL A1087     4831   8281   4866    705     97   -168       C  
ATOM   1530  C   VAL A1087     -28.363   3.637   2.360  1.00 47.44           C  
ANISOU 1530  C   VAL A1087     4876   8217   4930    673    118   -175       C  
ATOM   1531  O   VAL A1087     -28.135   2.429   2.322  1.00 47.57           O  
ANISOU 1531  O   VAL A1087     4892   8214   4968    569    150   -154       O  
ATOM   1532  CB  VAL A1087     -28.647   4.947   0.252  1.00 46.43           C  
ANISOU 1532  CB  VAL A1087     4775   8072   4795    703     89   -185       C  
ATOM   1533  CG1 VAL A1087     -27.888   3.914  -0.565  1.00 43.87           C  
ANISOU 1533  CG1 VAL A1087     4484   7661   4523    568    126   -170       C  
ATOM   1534  CG2 VAL A1087     -29.631   5.702  -0.624  1.00 48.86           C  
ANISOU 1534  CG2 VAL A1087     5063   8447   5055    747     59   -180       C  
ATOM   1535  N   TYR A1088     -27.757   4.464   3.207  1.00 48.43           N  
ANISOU 1535  N   TYR A1088     5034   8295   5074    763     98   -203       N  
ATOM   1536  CA  TYR A1088     -26.742   4.005   4.150  1.00 51.50           C  
ANISOU 1536  CA  TYR A1088     5449   8611   5508    745    114   -211       C  
ATOM   1537  C   TYR A1088     -27.301   2.994   5.153  1.00 52.57           C  
ANISOU 1537  C   TYR A1088     5557   8795   5621    700    122   -189       C  
ATOM   1538  O   TYR A1088     -26.594   2.083   5.584  1.00 51.84           O  
ANISOU 1538  O   TYR A1088     5478   8653   5566    637    148   -183       O  
ATOM   1539  CB  TYR A1088     -26.124   5.203   4.881  1.00 53.53           C  
ANISOU 1539  CB  TYR A1088     5747   8813   5777    854     84   -243       C  
ATOM   1540  CG  TYR A1088     -25.129   4.841   5.963  1.00 55.42           C  
ANISOU 1540  CG  TYR A1088     6012   8987   6059    846     95   -250       C  
ATOM   1541  CD1 TYR A1088     -23.808   4.542   5.652  1.00 55.92           C  
ANISOU 1541  CD1 TYR A1088     6122   8935   6192    791    110   -257       C  
ATOM   1542  CD2 TYR A1088     -25.508   4.816   7.300  1.00 56.58           C  
ANISOU 1542  CD2 TYR A1088     6153   9165   6179    882     80   -247       C  
ATOM   1543  CE1 TYR A1088     -22.896   4.216   6.640  1.00 55.47           C  
ANISOU 1543  CE1 TYR A1088     6084   8821   6171    785    118   -261       C  
ATOM   1544  CE2 TYR A1088     -24.603   4.492   8.294  1.00 57.57           C  
ANISOU 1544  CE2 TYR A1088     6300   9233   6342    875     89   -253       C  
ATOM   1545  CZ  TYR A1088     -23.299   4.193   7.958  1.00 57.31           C  
ANISOU 1545  CZ  TYR A1088     6292   9112   6373    834    111   -262       C  
ATOM   1546  OH  TYR A1088     -22.396   3.870   8.946  1.00 58.17           O  
ANISOU 1546  OH  TYR A1088     6417   9167   6516    828    118   -266       O  
ATOM   1547  N   ASP A1089     -28.572   3.151   5.509  1.00 53.97           N  
ANISOU 1547  N   ASP A1089     5699   9069   5736    735     99   -178       N  
ATOM   1548  CA  ASP A1089     -29.202   2.294   6.510  1.00 55.18           C  
ANISOU 1548  CA  ASP A1089     5828   9275   5862    703    101   -163       C  
ATOM   1549  C   ASP A1089     -29.588   0.919   5.962  1.00 54.39           C  
ANISOU 1549  C   ASP A1089     5706   9201   5759    582    127   -135       C  
ATOM   1550  O   ASP A1089     -29.688  -0.049   6.715  1.00 55.39           O  
ANISOU 1550  O   ASP A1089     5828   9331   5885    532    138   -126       O  
ATOM   1551  CB  ASP A1089     -30.438   2.977   7.101  1.00 58.79           C  
ANISOU 1551  CB  ASP A1089     6258   9827   6251    783     69   -162       C  
ATOM   1552  CG  ASP A1089     -30.117   4.314   7.742  1.00 61.78           C  
ANISOU 1552  CG  ASP A1089     6673  10173   6628    899     45   -187       C  
ATOM   1553  OD1 ASP A1089     -28.958   4.514   8.159  1.00 63.31           O  
ANISOU 1553  OD1 ASP A1089     6908  10276   6871    913     49   -205       O  
ATOM   1554  OD2 ASP A1089     -31.028   5.166   7.830  1.00 62.08           O  
ANISOU 1554  OD2 ASP A1089     6703  10274   6612    975     21   -188       O  
ATOM   1555  N   SER A1090     -29.807   0.841   4.653  1.00 51.75           N  
ANISOU 1555  N   SER A1090     5364   8877   5422    535    135   -121       N  
ATOM   1556  CA  SER A1090     -30.260  -0.397   4.025  1.00 50.09           C  
ANISOU 1556  CA  SER A1090     5141   8686   5205    418    156    -93       C  
ATOM   1557  C   SER A1090     -29.107  -1.335   3.681  1.00 47.64           C  
ANISOU 1557  C   SER A1090     4877   8267   4957    324    197    -87       C  
ATOM   1558  O   SER A1090     -29.291  -2.549   3.584  1.00 46.90           O  
ANISOU 1558  O   SER A1090     4791   8161   4866    229    217    -66       O  
ATOM   1559  CB  SER A1090     -31.069  -0.089   2.761  1.00 51.94           C  
ANISOU 1559  CB  SER A1090     5348   8982   5404    402    146    -77       C  
ATOM   1560  OG  SER A1090     -30.267   0.552   1.784  1.00 52.63           O  
ANISOU 1560  OG  SER A1090     5463   9005   5527    411    157    -88       O  
ATOM   1561  N   LEU A1091     -27.919  -0.768   3.501  1.00 46.81           N  
ANISOU 1561  N   LEU A1091     4807   8078   4902    353    209   -106       N  
ATOM   1562  CA  LEU A1091     -26.761  -1.535   3.051  1.00 45.98           C  
ANISOU 1562  CA  LEU A1091     4747   7866   4858    270    250    -99       C  
ATOM   1563  C   LEU A1091     -26.085  -2.312   4.178  1.00 46.24           C  
ANISOU 1563  C   LEU A1091     4800   7848   4920    252    266   -100       C  
ATOM   1564  O   LEU A1091     -26.227  -1.976   5.354  1.00 47.49           O  
ANISOU 1564  O   LEU A1091     4944   8038   5063    321    244   -115       O  
ATOM   1565  CB  LEU A1091     -25.743  -0.611   2.376  1.00 43.36           C  
ANISOU 1565  CB  LEU A1091     4441   7467   4568    307    257   -122       C  
ATOM   1566  CG  LEU A1091     -26.203   0.108   1.107  1.00 41.62           C  
ANISOU 1566  CG  LEU A1091     4211   7277   4326    315    248   -123       C  
ATOM   1567  CD1 LEU A1091     -25.162   1.121   0.660  1.00 41.66           C  
ANISOU 1567  CD1 LEU A1091     4268   7180   4383    362    234   -152       C  
ATOM   1568  CD2 LEU A1091     -26.490  -0.891  -0.002  1.00 41.14           C  
ANISOU 1568  CD2 LEU A1091     4163   7203   4266    190    277    -89       C  
ATOM   1569  N   ASP A1092     -25.347  -3.354   3.805  1.00 45.67           N  
ANISOU 1569  N   ASP A1092     4768   7694   4891    159    305    -84       N  
ATOM   1570  CA  ASP A1092     -24.559  -4.126   4.759  1.00 45.75           C  
ANISOU 1570  CA  ASP A1092     4804   7645   4935    140    324    -84       C  
ATOM   1571  C   ASP A1092     -23.259  -3.396   5.082  1.00 44.19           C  
ANISOU 1571  C   ASP A1092     4622   7381   4787    197    329   -107       C  
ATOM   1572  O   ASP A1092     -23.051  -2.266   4.644  1.00 43.63           O  
ANISOU 1572  O   ASP A1092     4544   7311   4721    258    313   -127       O  
ATOM   1573  CB  ASP A1092     -24.261  -5.522   4.209  1.00 48.31           C  
ANISOU 1573  CB  ASP A1092     5172   7899   5286     26    364    -57       C  
ATOM   1574  CG  ASP A1092     -23.481  -5.483   2.908  1.00 51.83           C  
ANISOU 1574  CG  ASP A1092     5654   8261   5776    -26    393    -48       C  
ATOM   1575  OD1 ASP A1092     -24.115  -5.380   1.836  1.00 53.77           O  
ANISOU 1575  OD1 ASP A1092     5898   8529   6002    -62    390    -37       O  
ATOM   1576  OD2 ASP A1092     -22.235  -5.559   2.957  1.00 52.32           O  
ANISOU 1576  OD2 ASP A1092     5747   8237   5894    -33    419    -52       O  
ATOM   1577  N   ALA A1093     -22.383  -4.047   5.841  1.00 43.83           N  
ANISOU 1577  N   ALA A1093     4599   7276   4779    179    349   -105       N  
ATOM   1578  CA  ALA A1093     -21.140  -3.421   6.287  1.00 42.91           C  
ANISOU 1578  CA  ALA A1093     4494   7100   4711    233    350   -126       C  
ATOM   1579  C   ALA A1093     -20.182  -3.086   5.141  1.00 40.97           C  
ANISOU 1579  C   ALA A1093     4272   6780   4515    208    373   -130       C  
ATOM   1580  O   ALA A1093     -19.601  -2.002   5.106  1.00 39.85           O  
ANISOU 1580  O   ALA A1093     4149   6590   4404    272    341   -154       O  
ATOM   1581  CB  ALA A1093     -20.446  -4.295   7.324  1.00 42.26           C  
ANISOU 1581  CB  ALA A1093     4427   6975   4654    212    368   -119       C  
ATOM   1582  N   VAL A1094     -20.021  -4.018   4.206  1.00 39.62           N  
ANISOU 1582  N   VAL A1094     4131   6559   4365    109    411   -104       N  
ATOM   1583  CA  VAL A1094     -19.095  -3.829   3.093  1.00 37.61           C  
ANISOU 1583  CA  VAL A1094     3910   6218   4164     70    435   -104       C  
ATOM   1584  C   VAL A1094     -19.585  -2.753   2.127  1.00 36.85           C  
ANISOU 1584  C   VAL A1094     3821   6125   4057     98    399   -119       C  
ATOM   1585  O   VAL A1094     -18.824  -1.872   1.728  1.00 36.06           O  
ANISOU 1585  O   VAL A1094     3763   5934   4005    130    371   -140       O  
ATOM   1586  CB  VAL A1094     -18.856  -5.146   2.325  1.00 35.82           C  
ANISOU 1586  CB  VAL A1094     3724   5923   3961    -47    484    -68       C  
ATOM   1587  CG1 VAL A1094     -17.900  -4.923   1.163  1.00 35.16           C  
ANISOU 1587  CG1 VAL A1094     3680   5744   3936    -91    509    -68       C  
ATOM   1588  CG2 VAL A1094     -18.316  -6.213   3.263  1.00 34.33           C  
ANISOU 1588  CG2 VAL A1094     3556   5692   3796    -70    505    -53       C  
ATOM   1589  N   ARG A1095     -20.862  -2.823   1.763  1.00 35.91           N  
ANISOU 1589  N   ARG A1095     3661   6113   3869     87    399   -109       N  
ATOM   1590  CA  ARG A1095     -21.437  -1.876   0.813  1.00 34.50           C  
ANISOU 1590  CA  ARG A1095     3487   5948   3674    112    366   -119       C  
ATOM   1591  C   ARG A1095     -21.535  -0.457   1.370  1.00 34.82           C  
ANISOU 1591  C   ARG A1095     3524   5999   3705    235    306   -153       C  
ATOM   1592  O   ARG A1095     -21.675   0.502   0.613  1.00 33.89           O  
ANISOU 1592  O   ARG A1095     3429   5858   3589    268    274   -169       O  
ATOM   1593  CB  ARG A1095     -22.808  -2.353   0.331  1.00 35.32           C  
ANISOU 1593  CB  ARG A1095     3550   6162   3709     68    375    -95       C  
ATOM   1594  CG  ARG A1095     -22.757  -3.541  -0.617  1.00 35.59           C  
ANISOU 1594  CG  ARG A1095     3628   6132   3764    -60    412    -59       C  
ATOM   1595  CD  ARG A1095     -24.133  -3.817  -1.198  1.00 37.58           C  
ANISOU 1595  CD  ARG A1095     3860   6459   3960    -97    395    -37       C  
ATOM   1596  NE  ARG A1095     -24.117  -4.856  -2.225  1.00 38.87           N  
ANISOU 1596  NE  ARG A1095     4075   6549   4145   -213    424     -6       N  
ATOM   1597  CZ  ARG A1095     -24.345  -6.144  -1.989  1.00 38.87           C  
ANISOU 1597  CZ  ARG A1095     4104   6517   4147   -276    438     17       C  
ATOM   1598  NH1 ARG A1095     -24.603  -6.558  -0.756  1.00 40.34           N  
ANISOU 1598  NH1 ARG A1095     4268   6744   4314   -244    428     12       N  
ATOM   1599  NH2 ARG A1095     -24.314  -7.018  -2.985  1.00 36.23           N  
ANISOU 1599  NH2 ARG A1095     3827   6104   3836   -368    462     42       N  
ATOM   1600  N   ARG A1096     -21.466  -0.323   2.690  1.00 37.89           N  
ANISOU 1600  N   ARG A1096     3892   6422   4084    301    292   -165       N  
ATOM   1601  CA  ARG A1096     -21.460   0.997   3.312  1.00 39.59           C  
ANISOU 1601  CA  ARG A1096     4114   6638   4290    415    241   -196       C  
ATOM   1602  C   ARG A1096     -20.110   1.677   3.118  1.00 39.28           C  
ANISOU 1602  C   ARG A1096     4143   6460   4320    431    222   -217       C  
ATOM   1603  O   ARG A1096     -20.039   2.890   2.924  1.00 41.11           O  
ANISOU 1603  O   ARG A1096     4407   6664   4550    499    182   -243       O  
ATOM   1604  CB  ARG A1096     -21.804   0.907   4.800  1.00 41.12           C  
ANISOU 1604  CB  ARG A1096     4267   6906   4449    474    234   -200       C  
ATOM   1605  CG  ARG A1096     -23.295   0.840   5.082  1.00 43.21           C  
ANISOU 1605  CG  ARG A1096     4467   7316   4633    502    230   -191       C  
ATOM   1606  CD  ARG A1096     -23.580   0.584   6.553  1.00 44.11           C  
ANISOU 1606  CD  ARG A1096     4570   7462   4728    534    214   -190       C  
ATOM   1607  NE  ARG A1096     -25.013   0.546   6.828  1.00 46.76           N  
ANISOU 1607  NE  ARG A1096     4869   7898   4998    549    192   -178       N  
ATOM   1608  CZ  ARG A1096     -25.540   0.291   8.021  1.00 50.89           C  
ANISOU 1608  CZ  ARG A1096     5378   8466   5492    571    179   -176       C  
ATOM   1609  NH1 ARG A1096     -24.751   0.046   9.059  1.00 51.17           N  
ANISOU 1609  NH1 ARG A1096     5433   8453   5557    580    185   -184       N  
ATOM   1610  NH2 ARG A1096     -26.858   0.279   8.178  1.00 52.81           N  
ANISOU 1610  NH2 ARG A1096     5587   8804   5675    583    160   -166       N  
ATOM   1611  N   ALA A1097     -19.042   0.887   3.164  1.00 35.77           N  
ANISOU 1611  N   ALA A1097     3724   5932   3935    366    254   -207       N  
ATOM   1612  CA  ALA A1097     -17.694   1.410   2.976  1.00 35.46           C  
ANISOU 1612  CA  ALA A1097     3746   5764   3964    370    241   -225       C  
ATOM   1613  C   ALA A1097     -17.499   1.924   1.553  1.00 33.75           C  
ANISOU 1613  C   ALA A1097     3575   5476   3772    339    235   -235       C  
ATOM   1614  O   ALA A1097     -16.829   2.932   1.334  1.00 31.75           O  
ANISOU 1614  O   ALA A1097     3371   5146   3546    379    203   -263       O  
ATOM   1615  CB  ALA A1097     -16.660   0.346   3.305  1.00 36.15           C  
ANISOU 1615  CB  ALA A1097     3842   5786   4107    306    280   -206       C  
ATOM   1616  N   ALA A1098     -18.092   1.226   0.589  1.00 34.00           N  
ANISOU 1616  N   ALA A1098     3593   5534   3790    264    266   -212       N  
ATOM   1617  CA  ALA A1098     -18.021   1.640  -0.807  1.00 33.96           C  
ANISOU 1617  CA  ALA A1098     3631   5467   3804    226    262   -219       C  
ATOM   1618  C   ALA A1098     -18.753   2.960  -1.023  1.00 35.63           C  
ANISOU 1618  C   ALA A1098     3847   5720   3970    311    210   -245       C  
ATOM   1619  O   ALA A1098     -18.395   3.743  -1.902  1.00 36.73           O  
ANISOU 1619  O   ALA A1098     4040   5783   4132    314    189   -267       O  
ATOM   1620  CB  ALA A1098     -18.589   0.560  -1.713  1.00 33.35           C  
ANISOU 1620  CB  ALA A1098     3538   5419   3714    123    307   -184       C  
ATOM   1621  N   LEU A1099     -19.780   3.204  -0.215  1.00 35.70           N  
ANISOU 1621  N   LEU A1099     3803   5847   3914    381    191   -244       N  
ATOM   1622  CA  LEU A1099     -20.521   4.456  -0.287  1.00 34.22           C  
ANISOU 1622  CA  LEU A1099     3617   5708   3678    475    144   -266       C  
ATOM   1623  C   LEU A1099     -19.703   5.597   0.307  1.00 33.26           C  
ANISOU 1623  C   LEU A1099     3548   5515   3575    558    106   -302       C  
ATOM   1624  O   LEU A1099     -19.681   6.702  -0.235  1.00 35.53           O  
ANISOU 1624  O   LEU A1099     3882   5765   3854    606     73   -328       O  
ATOM   1625  CB  LEU A1099     -21.865   4.333   0.432  1.00 33.53           C  
ANISOU 1625  CB  LEU A1099     3454   5771   3514    525    139   -252       C  
ATOM   1626  CG  LEU A1099     -22.768   5.567   0.372  1.00 33.31           C  
ANISOU 1626  CG  LEU A1099     3420   5807   3429    627     94   -270       C  
ATOM   1627  CD1 LEU A1099     -23.029   5.969  -1.071  1.00 32.34           C  
ANISOU 1627  CD1 LEU A1099     3328   5656   3305    598     83   -272       C  
ATOM   1628  CD2 LEU A1099     -24.079   5.321   1.107  1.00 32.69           C  
ANISOU 1628  CD2 LEU A1099     3261   5883   3279    671     95   -252       C  
ATOM   1629  N   ILE A1100     -19.029   5.322   1.419  1.00 29.69           N  
ANISOU 1629  N   ILE A1100     3091   5045   3146    572    113   -302       N  
ATOM   1630  CA  ILE A1100     -18.179   6.314   2.069  1.00 28.08           C  
ANISOU 1630  CA  ILE A1100     2938   4774   2958    641     81   -332       C  
ATOM   1631  C   ILE A1100     -16.978   6.635   1.184  1.00 26.56           C  
ANISOU 1631  C   ILE A1100     2817   4446   2828    596     79   -351       C  
ATOM   1632  O   ILE A1100     -16.478   7.763   1.172  1.00 25.53           O  
ANISOU 1632  O   ILE A1100     2746   4257   2699    649     46   -383       O  
ATOM   1633  CB  ILE A1100     -17.703   5.824   3.453  1.00 28.10           C  
ANISOU 1633  CB  ILE A1100     2916   4788   2973    654     90   -323       C  
ATOM   1634  CG1 ILE A1100     -18.906   5.476   4.333  1.00 28.71           C  
ANISOU 1634  CG1 ILE A1100     2923   4997   2987    694     94   -307       C  
ATOM   1635  CG2 ILE A1100     -16.839   6.875   4.134  1.00 27.51           C  
ANISOU 1635  CG2 ILE A1100     2895   4646   2909    720     56   -352       C  
ATOM   1636  CD1 ILE A1100     -18.533   4.916   5.689  1.00 29.74           C  
ANISOU 1636  CD1 ILE A1100     3030   5144   3127    701    104   -299       C  
ATOM   1637  N   ASN A1101     -16.525   5.631   0.441  1.00 26.20           N  
ANISOU 1637  N   ASN A1101     2771   4351   2832    495    118   -332       N  
ATOM   1638  CA  ASN A1101     -15.472   5.813  -0.548  1.00 25.34           C  
ANISOU 1638  CA  ASN A1101     2727   4116   2785    440    123   -347       C  
ATOM   1639  C   ASN A1101     -15.853   6.911  -1.537  1.00 24.69           C  
ANISOU 1639  C   ASN A1101     2692   4011   2677    470     91   -375       C  
ATOM   1640  O   ASN A1101     -15.067   7.820  -1.802  1.00 23.48           O  
ANISOU 1640  O   ASN A1101     2606   3770   2546    492     66   -409       O  
ATOM   1641  CB  ASN A1101     -15.212   4.495  -1.284  1.00 25.36           C  
ANISOU 1641  CB  ASN A1101     2718   4086   2833    326    176   -316       C  
ATOM   1642  CG  ASN A1101     -13.932   4.518  -2.101  1.00 24.47           C  
ANISOU 1642  CG  ASN A1101     2668   3835   2794    266    189   -328       C  
ATOM   1643  OD1 ASN A1101     -13.619   5.505  -2.764  1.00 25.30           O  
ANISOU 1643  OD1 ASN A1101     2830   3875   2907    284    161   -361       O  
ATOM   1644  ND2 ASN A1101     -13.184   3.422  -2.053  1.00 23.72           N  
ANISOU 1644  ND2 ASN A1101     2565   3695   2752    193    234   -303       N  
ATOM   1645  N   MET A1102     -17.070   6.826  -2.067  1.00 25.04           N  
ANISOU 1645  N   MET A1102     2703   4138   2674    471     90   -362       N  
ATOM   1646  CA  MET A1102     -17.571   7.816  -3.013  1.00 25.62           C  
ANISOU 1646  CA  MET A1102     2815   4202   2716    503     59   -385       C  
ATOM   1647  C   MET A1102     -17.699   9.193  -2.367  1.00 26.80           C  
ANISOU 1647  C   MET A1102     2995   4366   2820    622     11   -418       C  
ATOM   1648  O   MET A1102     -17.431  10.212  -3.003  1.00 27.87           O  
ANISOU 1648  O   MET A1102     3200   4437   2953    650    -17   -452       O  
ATOM   1649  CB  MET A1102     -18.922   7.380  -3.579  1.00 26.80           C  
ANISOU 1649  CB  MET A1102     2911   4455   2818    483     67   -357       C  
ATOM   1650  CG  MET A1102     -18.888   6.058  -4.323  1.00 26.52           C  
ANISOU 1650  CG  MET A1102     2854   4406   2816    360    116   -322       C  
ATOM   1651  SD  MET A1102     -20.528   5.590  -4.900  1.00 36.55           S  
ANISOU 1651  SD  MET A1102     4058   5812   4018    337    123   -288       S  
ATOM   1652  CE  MET A1102     -20.892   6.948  -6.008  1.00 24.00           C  
ANISOU 1652  CE  MET A1102     2524   4189   2405    384     76   -320       C  
ATOM   1653  N   VAL A1103     -18.108   9.213  -1.102  1.00 27.21           N  
ANISOU 1653  N   VAL A1103     3003   4501   2836    689      4   -410       N  
ATOM   1654  CA  VAL A1103     -18.257  10.461  -0.362  1.00 28.87           C  
ANISOU 1654  CA  VAL A1103     3243   4729   2998    802    -35   -436       C  
ATOM   1655  C   VAL A1103     -16.912  11.162  -0.194  1.00 29.67           C  
ANISOU 1655  C   VAL A1103     3425   4711   3137    809    -51   -469       C  
ATOM   1656  O   VAL A1103     -16.814  12.382  -0.327  1.00 29.14           O  
ANISOU 1656  O   VAL A1103     3423   4609   3039    874    -84   -502       O  
ATOM   1657  CB  VAL A1103     -18.898  10.220   1.023  1.00 28.43           C  
ANISOU 1657  CB  VAL A1103     3123   4780   2901    862    -33   -418       C  
ATOM   1658  CG1 VAL A1103     -18.928  11.506   1.835  1.00 27.00           C  
ANISOU 1658  CG1 VAL A1103     2983   4603   2672    975    -69   -444       C  
ATOM   1659  CG2 VAL A1103     -20.301   9.653   0.866  1.00 28.52           C  
ANISOU 1659  CG2 VAL A1103     3055   4919   2864    862    -21   -389       C  
ATOM   1660  N   PHE A1104     -15.871  10.384   0.080  1.00 32.58           N  
ANISOU 1660  N   PHE A1104     3791   5019   3569    742    -26   -460       N  
ATOM   1661  CA  PHE A1104     -14.536  10.941   0.274  1.00 36.01           C  
ANISOU 1661  CA  PHE A1104     4293   5346   4042    739    -38   -487       C  
ATOM   1662  C   PHE A1104     -13.878  11.371  -1.036  1.00 36.03           C  
ANISOU 1662  C   PHE A1104     4369   5242   4081    690    -43   -515       C  
ATOM   1663  O   PHE A1104     -12.805  11.973  -1.027  1.00 36.10           O  
ANISOU 1663  O   PHE A1104     4443   5160   4115    688    -56   -543       O  
ATOM   1664  CB  PHE A1104     -13.641   9.949   1.021  1.00 37.45           C  
ANISOU 1664  CB  PHE A1104     4444   5504   4281    686    -11   -465       C  
ATOM   1665  CG  PHE A1104     -13.705  10.084   2.515  1.00 40.13           C  
ANISOU 1665  CG  PHE A1104     4758   5899   4591    750    -23   -457       C  
ATOM   1666  CD1 PHE A1104     -13.707   8.962   3.327  1.00 40.46           C  
ANISOU 1666  CD1 PHE A1104     4734   5986   4651    720      4   -425       C  
ATOM   1667  CD2 PHE A1104     -13.757  11.334   3.108  1.00 42.09           C  
ANISOU 1667  CD2 PHE A1104     5052   6150   4789    839    -60   -484       C  
ATOM   1668  CE1 PHE A1104     -13.761   9.082   4.702  1.00 40.23           C  
ANISOU 1668  CE1 PHE A1104     4686   6004   4597    776     -7   -419       C  
ATOM   1669  CE2 PHE A1104     -13.813  11.461   4.484  1.00 43.19           C  
ANISOU 1669  CE2 PHE A1104     5173   6336   4901    895    -70   -476       C  
ATOM   1670  CZ  PHE A1104     -13.815  10.333   5.281  1.00 41.96           C  
ANISOU 1670  CZ  PHE A1104     4950   6224   4768    862    -44   -444       C  
ATOM   1671  N   GLN A1105     -14.523  11.064  -2.157  1.00 36.27           N  
ANISOU 1671  N   GLN A1105     4390   5282   4110    647    -31   -507       N  
ATOM   1672  CA  GLN A1105     -13.998  11.443  -3.465  1.00 35.39           C  
ANISOU 1672  CA  GLN A1105     4348   5068   4029    597    -34   -534       C  
ATOM   1673  C   GLN A1105     -14.733  12.646  -4.047  1.00 39.46           C  
ANISOU 1673  C   GLN A1105     4912   5596   4483    665    -72   -564       C  
ATOM   1674  O   GLN A1105     -14.111  13.561  -4.587  1.00 39.77           O  
ANISOU 1674  O   GLN A1105     5037   5548   4527    672    -94   -605       O  
ATOM   1675  CB  GLN A1105     -14.068  10.266  -4.443  1.00 31.79           C  
ANISOU 1675  CB  GLN A1105     3863   4595   3622    489      7   -505       C  
ATOM   1676  CG  GLN A1105     -13.621  10.612  -5.860  1.00 30.88           C  
ANISOU 1676  CG  GLN A1105     3820   4374   3539    430      6   -531       C  
ATOM   1677  CD  GLN A1105     -13.658   9.423  -6.804  1.00 30.61           C  
ANISOU 1677  CD  GLN A1105     3763   4316   3552    318     51   -499       C  
ATOM   1678  OE1 GLN A1105     -13.997   8.308  -6.407  1.00 31.24           O  
ANISOU 1678  OE1 GLN A1105     3774   4457   3637    282     85   -457       O  
ATOM   1679  NE2 GLN A1105     -13.307   9.657  -8.063  1.00 29.41           N  
ANISOU 1679  NE2 GLN A1105     3674   4070   3430    260     53   -520       N  
ATOM   1680  N   MET A1106     -16.058  12.642  -3.926  1.00 42.47           N  
ANISOU 1680  N   MET A1106     5241   6091   4807    715    -80   -544       N  
ATOM   1681  CA  MET A1106     -16.890  13.645  -4.583  1.00 45.91           C  
ANISOU 1681  CA  MET A1106     5711   6549   5182    777   -112   -565       C  
ATOM   1682  C   MET A1106     -17.612  14.560  -3.598  1.00 49.39           C  
ANISOU 1682  C   MET A1106     6147   7074   5547    903   -142   -572       C  
ATOM   1683  O   MET A1106     -18.041  15.656  -3.961  1.00 50.55           O  
ANISOU 1683  O   MET A1106     6346   7219   5640    974   -173   -598       O  
ATOM   1684  CB  MET A1106     -17.916  12.961  -5.488  1.00 46.26           C  
ANISOU 1684  CB  MET A1106     5703   6656   5218    729    -98   -535       C  
ATOM   1685  CG  MET A1106     -17.321  11.942  -6.444  1.00 46.55           C  
ANISOU 1685  CG  MET A1106     5743   6618   5327    599    -61   -520       C  
ATOM   1686  SD  MET A1106     -18.589  10.944  -7.242  1.00 56.38           S  
ANISOU 1686  SD  MET A1106     6912   7956   6552    535    -38   -474       S  
ATOM   1687  CE  MET A1106     -19.418  10.264  -5.810  1.00 93.92           C  
ANISOU 1687  CE  MET A1106    11559  12860  11264    583    -25   -435       C  
ATOM   1688  N   GLY A1107     -17.753  14.107  -2.357  1.00 51.05           N  
ANISOU 1688  N   GLY A1107     6296   7354   5748    932   -131   -548       N  
ATOM   1689  CA  GLY A1107     -18.480  14.863  -1.354  1.00 52.83           C  
ANISOU 1689  CA  GLY A1107     6509   7661   5901   1048   -153   -550       C  
ATOM   1690  C   GLY A1107     -19.929  14.428  -1.269  1.00 55.45           C  
ANISOU 1690  C   GLY A1107     6753   8130   6186   1078   -147   -516       C  
ATOM   1691  O   GLY A1107     -20.422  13.725  -2.150  1.00 56.42           O  
ANISOU 1691  O   GLY A1107     6834   8279   6323   1014   -132   -496       O  
ATOM   1692  N   GLU A1108     -20.613  14.849  -0.209  1.00 57.44           N  
ANISOU 1692  N   GLU A1108     6975   8468   6380   1174   -157   -509       N  
ATOM   1693  CA  GLU A1108     -22.010  14.480   0.006  1.00 57.45           C  
ANISOU 1693  CA  GLU A1108     6886   8610   6332   1211   -152   -478       C  
ATOM   1694  C   GLU A1108     -22.917  15.023  -1.092  1.00 57.52           C  
ANISOU 1694  C   GLU A1108     6902   8654   6299   1241   -170   -482       C  
ATOM   1695  O   GLU A1108     -23.806  14.324  -1.579  1.00 59.44           O  
ANISOU 1695  O   GLU A1108     7073   8981   6532   1205   -158   -452       O  
ATOM   1696  CB  GLU A1108     -22.493  14.984   1.366  1.00 58.06           C  
ANISOU 1696  CB  GLU A1108     6945   8761   6354   1317   -160   -476       C  
ATOM   1697  CG  GLU A1108     -21.699  14.457   2.543  1.00 58.51           C  
ANISOU 1697  CG  GLU A1108     6992   8793   6446   1293   -144   -470       C  
ATOM   1698  CD  GLU A1108     -22.219  14.979   3.865  1.00 60.67           C  
ANISOU 1698  CD  GLU A1108     7252   9137   6664   1394   -152   -467       C  
ATOM   1699  OE1 GLU A1108     -23.363  15.479   3.897  1.00 62.28           O  
ANISOU 1699  OE1 GLU A1108     7428   9431   6803   1476   -162   -461       O  
ATOM   1700  OE2 GLU A1108     -21.483  14.895   4.869  1.00 60.95           O  
ANISOU 1700  OE2 GLU A1108     7303   9135   6718   1393   -147   -469       O  
ATOM   1701  N   THR A1109     -22.685  16.273  -1.480  1.00 55.91           N  
ANISOU 1701  N   THR A1109     6788   8387   6068   1305   -200   -516       N  
ATOM   1702  CA  THR A1109     -23.501  16.922  -2.498  1.00 55.42           C  
ANISOU 1702  CA  THR A1109     6743   8351   5962   1345   -222   -523       C  
ATOM   1703  C   THR A1109     -23.234  16.341  -3.887  1.00 52.95           C  
ANISOU 1703  C   THR A1109     6441   7978   5700   1232   -214   -522       C  
ATOM   1704  O   THR A1109     -23.931  16.662  -4.848  1.00 53.82           O  
ANISOU 1704  O   THR A1109     6555   8112   5782   1243   -230   -521       O  
ATOM   1705  CB  THR A1109     -23.268  18.447  -2.518  1.00 56.65           C  
ANISOU 1705  CB  THR A1109     7006   8446   6071   1445   -254   -564       C  
ATOM   1706  OG1 THR A1109     -24.232  19.073  -3.374  1.00 58.62           O  
ANISOU 1706  OG1 THR A1109     7264   8742   6269   1500   -276   -565       O  
ATOM   1707  CG2 THR A1109     -21.866  18.768  -3.010  1.00 56.45           C  
ANISOU 1707  CG2 THR A1109     7085   8268   6096   1385   -259   -603       C  
ATOM   1708  N   GLY A1110     -22.223  15.482  -3.981  1.00 49.70           N  
ANISOU 1708  N   GLY A1110     6034   7488   5363   1126   -189   -520       N  
ATOM   1709  CA  GLY A1110     -21.893  14.814  -5.227  1.00 46.57           C  
ANISOU 1709  CA  GLY A1110     5648   7027   5020   1010   -174   -515       C  
ATOM   1710  C   GLY A1110     -22.504  13.428  -5.315  1.00 44.70           C  
ANISOU 1710  C   GLY A1110     5312   6875   4799    928   -140   -467       C  
ATOM   1711  O   GLY A1110     -22.996  13.025  -6.368  1.00 43.61           O  
ANISOU 1711  O   GLY A1110     5157   6750   4663    866   -134   -451       O  
ATOM   1712  N   VAL A1111     -22.473  12.697  -4.204  1.00 44.35           N  
ANISOU 1712  N   VAL A1111     5205   6885   4760    925   -117   -445       N  
ATOM   1713  CA  VAL A1111     -23.065  11.364  -4.142  1.00 43.69           C  
ANISOU 1713  CA  VAL A1111     5030   6887   4683    850    -82   -401       C  
ATOM   1714  C   VAL A1111     -24.588  11.437  -4.260  1.00 46.71           C  
ANISOU 1714  C   VAL A1111     5341   7414   4994    899    -94   -376       C  
ATOM   1715  O   VAL A1111     -25.222  10.534  -4.809  1.00 49.52           O  
ANISOU 1715  O   VAL A1111     5639   7832   5344    823    -72   -343       O  
ATOM   1716  CB  VAL A1111     -22.682  10.628  -2.840  1.00 41.92           C  
ANISOU 1716  CB  VAL A1111     4762   6690   4477    844    -58   -386       C  
ATOM   1717  CG1 VAL A1111     -23.199   9.198  -2.860  1.00 40.06           C  
ANISOU 1717  CG1 VAL A1111     4445   6530   4247    755    -18   -344       C  
ATOM   1718  CG2 VAL A1111     -21.175  10.637  -2.648  1.00 41.86           C  
ANISOU 1718  CG2 VAL A1111     4821   6546   4536    807    -50   -409       C  
ATOM   1719  N   ALA A1112     -25.170  12.523  -3.757  1.00 46.51           N  
ANISOU 1719  N   ALA A1112     5322   7442   4909   1024   -126   -392       N  
ATOM   1720  CA  ALA A1112     -26.617  12.728  -3.830  1.00 45.68           C  
ANISOU 1720  CA  ALA A1112     5149   7477   4733   1086   -140   -370       C  
ATOM   1721  C   ALA A1112     -27.085  12.946  -5.266  1.00 46.75           C  
ANISOU 1721  C   ALA A1112     5301   7605   4858   1053   -155   -367       C  
ATOM   1722  O   ALA A1112     -28.285  12.940  -5.546  1.00 51.52           O  
ANISOU 1722  O   ALA A1112     5842   8326   5408   1080   -164   -342       O  
ATOM   1723  CB  ALA A1112     -27.034  13.902  -2.954  1.00 43.98           C  
ANISOU 1723  CB  ALA A1112     4947   7306   4458   1233   -168   -388       C  
ATOM   1724  N   GLY A1113     -26.132  13.143  -6.171  1.00 42.71           N  
ANISOU 1724  N   GLY A1113     4875   6955   4397    992   -159   -392       N  
ATOM   1725  CA  GLY A1113     -26.433  13.303  -7.580  1.00 40.07           C  
ANISOU 1725  CA  GLY A1113     4570   6594   4062    946   -172   -391       C  
ATOM   1726  C   GLY A1113     -26.724  11.976  -8.253  1.00 38.51           C  
ANISOU 1726  C   GLY A1113     4314   6428   3888    814   -138   -350       C  
ATOM   1727  O   GLY A1113     -27.281  11.937  -9.348  1.00 38.03           O  
ANISOU 1727  O   GLY A1113     4252   6382   3814    771   -146   -337       O  
ATOM   1728  N   PHE A1114     -26.344  10.883  -7.598  1.00 37.76           N  
ANISOU 1728  N   PHE A1114     4177   6343   3826    747    -99   -330       N  
ATOM   1729  CA  PHE A1114     -26.607   9.549  -8.127  1.00 36.97           C  
ANISOU 1729  CA  PHE A1114     4028   6276   3744    619    -60   -288       C  
ATOM   1730  C   PHE A1114     -27.981   9.047  -7.694  1.00 38.36           C  
ANISOU 1730  C   PHE A1114     4095   6628   3851    638    -55   -249       C  
ATOM   1731  O   PHE A1114     -28.111   7.926  -7.203  1.00 37.89           O  
ANISOU 1731  O   PHE A1114     3979   6625   3794    573    -17   -220       O  
ATOM   1732  CB  PHE A1114     -25.526   8.562  -7.680  1.00 35.86           C  
ANISOU 1732  CB  PHE A1114     3899   6059   3668    534    -17   -284       C  
ATOM   1733  CG  PHE A1114     -24.177   8.822  -8.287  1.00 36.84           C  
ANISOU 1733  CG  PHE A1114     4121   6012   3864    487    -14   -315       C  
ATOM   1734  CD1 PHE A1114     -23.823   8.243  -9.493  1.00 34.78           C  
ANISOU 1734  CD1 PHE A1114     3897   5671   3646    369      9   -304       C  
ATOM   1735  CD2 PHE A1114     -23.262   9.644  -7.651  1.00 38.38           C  
ANISOU 1735  CD2 PHE A1114     4373   6126   4082    558    -34   -355       C  
ATOM   1736  CE1 PHE A1114     -22.583   8.479 -10.055  1.00 33.46           C  
ANISOU 1736  CE1 PHE A1114     3819   5347   3546    325     13   -334       C  
ATOM   1737  CE2 PHE A1114     -22.020   9.885  -8.209  1.00 36.33           C  
ANISOU 1737  CE2 PHE A1114     4202   5715   3887    512    -31   -385       C  
ATOM   1738  CZ  PHE A1114     -21.681   9.301  -9.413  1.00 34.42           C  
ANISOU 1738  CZ  PHE A1114     3993   5396   3690    397     -7   -376       C  
ATOM   1739  N   THR A1115     -28.999   9.881  -7.897  1.00 39.08           N  
ANISOU 1739  N   THR A1115     4161   6807   3880    726    -91   -249       N  
ATOM   1740  CA  THR A1115     -30.358   9.611  -7.429  1.00 39.27           C  
ANISOU 1740  CA  THR A1115     4080   7008   3833    765    -92   -215       C  
ATOM   1741  C   THR A1115     -30.878   8.240  -7.845  1.00 36.19           C  
ANISOU 1741  C   THR A1115     3624   6690   3435    636    -54   -169       C  
ATOM   1742  O   THR A1115     -31.275   7.435  -7.002  1.00 34.23           O  
ANISOU 1742  O   THR A1115     3305   6536   3164    619    -27   -147       O  
ATOM   1743  CB  THR A1115     -31.348  10.679  -7.938  1.00 42.48           C  
ANISOU 1743  CB  THR A1115     4476   7485   4179    862   -136   -217       C  
ATOM   1744  OG1 THR A1115     -30.860  11.985  -7.611  1.00 46.03           O  
ANISOU 1744  OG1 THR A1115     5000   7862   4629    980   -169   -261       O  
ATOM   1745  CG2 THR A1115     -32.719  10.479  -7.309  1.00 42.33           C  
ANISOU 1745  CG2 THR A1115     4345   7655   4086    917   -137   -185       C  
ATOM   1746  N   ASN A1116     -30.871   7.983  -9.148  1.00 37.08           N  
ANISOU 1746  N   ASN A1116     3769   6757   3565    541    -51   -156       N  
ATOM   1747  CA  ASN A1116     -31.383   6.729  -9.682  1.00 36.00           C  
ANISOU 1747  CA  ASN A1116     3581   6683   3413    410    -15   -110       C  
ATOM   1748  C   ASN A1116     -30.577   5.535  -9.182  1.00 36.49           C  
ANISOU 1748  C   ASN A1116     3650   6693   3521    314     38   -100       C  
ATOM   1749  O   ASN A1116     -31.142   4.517  -8.782  1.00 36.40           O  
ANISOU 1749  O   ASN A1116     3571   6784   3477    256     71    -66       O  
ATOM   1750  CB  ASN A1116     -31.396   6.768 -11.212  1.00 31.02           C  
ANISOU 1750  CB  ASN A1116     2999   5990   2797    325    -22   -100       C  
ATOM   1751  CG  ASN A1116     -32.107   5.576 -11.822  1.00 29.31           C  
ANISOU 1751  CG  ASN A1116     2730   5855   2551    193     12    -47       C  
ATOM   1752  OD1 ASN A1116     -32.881   4.890 -11.154  1.00 30.16           O  
ANISOU 1752  OD1 ASN A1116     2752   6099   2608    184     31    -18       O  
ATOM   1753  ND2 ASN A1116     -31.850   5.326 -13.099  1.00 30.02           N  
ANISOU 1753  ND2 ASN A1116     2876   5862   2668     87     20    -36       N  
ATOM   1754  N   SER A1117     -29.255   5.674  -9.193  1.00 36.35           N  
ANISOU 1754  N   SER A1117     3715   6520   3577    298     47   -130       N  
ATOM   1755  CA  SER A1117     -28.368   4.600  -8.759  1.00 36.46           C  
ANISOU 1755  CA  SER A1117     3744   6470   3640    213     96   -122       C  
ATOM   1756  C   SER A1117     -28.496   4.309  -7.265  1.00 34.62           C  
ANISOU 1756  C   SER A1117     3453   6317   3385    274    107   -122       C  
ATOM   1757  O   SER A1117     -28.460   3.151  -6.848  1.00 33.31           O  
ANISOU 1757  O   SER A1117     3255   6182   3219    198    151    -97       O  
ATOM   1758  CB  SER A1117     -26.917   4.926  -9.117  1.00 38.82           C  
ANISOU 1758  CB  SER A1117     4143   6587   4023    193     99   -155       C  
ATOM   1759  OG  SER A1117     -26.751   5.013 -10.523  1.00 41.00           O  
ANISOU 1759  OG  SER A1117     4475   6780   4322    117     98   -153       O  
ATOM   1760  N   LEU A1118     -28.645   5.359  -6.464  1.00 35.91           N  
ANISOU 1760  N   LEU A1118     3607   6509   3527    408     68   -151       N  
ATOM   1761  CA  LEU A1118     -28.813   5.198  -5.023  1.00 39.81           C  
ANISOU 1761  CA  LEU A1118     4050   7078   3998    474     74   -153       C  
ATOM   1762  C   LEU A1118     -30.100   4.447  -4.690  1.00 44.15           C  
ANISOU 1762  C   LEU A1118     4501   7798   4477    453     91   -117       C  
ATOM   1763  O   LEU A1118     -30.142   3.661  -3.743  1.00 45.65           O  
ANISOU 1763  O   LEU A1118     4649   8038   4656    434    119   -107       O  
ATOM   1764  CB  LEU A1118     -28.797   6.557  -4.319  1.00 39.56           C  
ANISOU 1764  CB  LEU A1118     4035   7044   3951    623     29   -189       C  
ATOM   1765  CG  LEU A1118     -27.439   7.247  -4.195  1.00 39.14           C  
ANISOU 1765  CG  LEU A1118     4075   6834   3961    653     16   -228       C  
ATOM   1766  CD1 LEU A1118     -27.599   8.630  -3.586  1.00 40.73           C  
ANISOU 1766  CD1 LEU A1118     4297   7047   4131    799    -27   -259       C  
ATOM   1767  CD2 LEU A1118     -26.478   6.403  -3.372  1.00 37.56           C  
ANISOU 1767  CD2 LEU A1118     3883   6578   3811    603     51   -227       C  
ATOM   1768  N   ARG A1119     -31.146   4.692  -5.472  1.00 46.01           N  
ANISOU 1768  N   ARG A1119     4699   8122   4662    453     72    -98       N  
ATOM   1769  CA  ARG A1119     -32.417   4.006  -5.276  1.00 49.21           C  
ANISOU 1769  CA  ARG A1119     5009   8696   4994    427     87    -63       C  
ATOM   1770  C   ARG A1119     -32.282   2.521  -5.601  1.00 46.11           C  
ANISOU 1770  C   ARG A1119     4609   8303   4609    273    141    -30       C  
ATOM   1771  O   ARG A1119     -32.843   1.670  -4.911  1.00 45.86           O  
ANISOU 1771  O   ARG A1119     4538   8332   4553    237    146     -9       O  
ATOM   1772  CB  ARG A1119     -33.515   4.641  -6.132  1.00 55.50           C  
ANISOU 1772  CB  ARG A1119     5769   9583   5736    460     52    -48       C  
ATOM   1773  CG  ARG A1119     -34.889   4.018  -5.934  1.00 62.09           C  
ANISOU 1773  CG  ARG A1119     6498  10605   6490    438     63    -10       C  
ATOM   1774  CD  ARG A1119     -35.944   4.702  -6.789  1.00 68.92           C  
ANISOU 1774  CD  ARG A1119     7324  11559   7302    476     26      6       C  
ATOM   1775  NE  ARG A1119     -35.661   4.583  -8.217  1.00 73.86           N  
ANISOU 1775  NE  ARG A1119     8007  12103   7956    379     25     19       N  
ATOM   1776  CZ  ARG A1119     -36.095   3.589  -8.986  1.00 77.59           C  
ANISOU 1776  CZ  ARG A1119     8455  12622   8405    245     53     60       C  
ATOM   1777  NH1 ARG A1119     -35.788   3.563 -10.276  1.00 78.09           N  
ANISOU 1777  NH1 ARG A1119     8577  12597   8496    160     51     69       N  
ATOM   1778  NH2 ARG A1119     -36.837   2.619  -8.465  1.00 79.22           N  
ANISOU 1778  NH2 ARG A1119     8598  12927   8576    189     67     89       N  
ATOM   1779  N   MET A1120     -31.530   2.221  -6.655  1.00 43.93           N  
ANISOU 1779  N   MET A1120     4403   7905   4384    176    157    -25       N  
ATOM   1780  CA  MET A1120     -31.285   0.841  -7.060  1.00 42.62           C  
ANISOU 1780  CA  MET A1120     4247   7717   4228     27    213      7       C  
ATOM   1781  C   MET A1120     -30.547   0.067  -5.972  1.00 42.73           C  
ANISOU 1781  C   MET A1120     4285   7663   4287     11    234      1       C  
ATOM   1782  O   MET A1120     -30.848  -1.099  -5.714  1.00 43.96           O  
ANISOU 1782  O   MET A1120     4446   7808   4448    -70    242     27       O  
ATOM   1783  CB  MET A1120     -30.492   0.801  -8.367  1.00 41.28           C  
ANISOU 1783  CB  MET A1120     4164   7403   4118    -61    223     10       C  
ATOM   1784  CG  MET A1120     -31.241   1.374  -9.558  1.00 42.25           C  
ANISOU 1784  CG  MET A1120     4285   7558   4211    -71    192     22       C  
ATOM   1785  SD  MET A1120     -30.219   1.501 -11.037  1.00 54.40           S  
ANISOU 1785  SD  MET A1120     5935   8909   5825   -162    199     15       S  
ATOM   1786  CE  MET A1120     -31.420   2.089 -12.228  1.00 58.61           C  
ANISOU 1786  CE  MET A1120     6443   9524   6300   -166    158     36       C  
ATOM   1787  N   LEU A1121     -29.581   0.723  -5.336  1.00 40.42           N  
ANISOU 1787  N   LEU A1121     4019   7305   4034     91    233    -36       N  
ATOM   1788  CA  LEU A1121     -28.821   0.108  -4.255  1.00 39.59           C  
ANISOU 1788  CA  LEU A1121     3927   7150   3964     87    256    -44       C  
ATOM   1789  C   LEU A1121     -29.698  -0.134  -3.033  1.00 41.27           C  
ANISOU 1789  C   LEU A1121     4092   7452   4139    137    228    -38       C  
ATOM   1790  O   LEU A1121     -29.574  -1.160  -2.364  1.00 41.61           O  
ANISOU 1790  O   LEU A1121     4148   7465   4198     83    242    -26       O  
ATOM   1791  CB  LEU A1121     -27.624   0.980  -3.872  1.00 38.08           C  
ANISOU 1791  CB  LEU A1121     3793   6838   3837    165    237    -84       C  
ATOM   1792  CG  LEU A1121     -26.437   0.985  -4.836  1.00 34.88           C  
ANISOU 1792  CG  LEU A1121     3475   6268   3510     99    249    -91       C  
ATOM   1793  CD1 LEU A1121     -25.385   1.985  -4.383  1.00 34.05           C  
ANISOU 1793  CD1 LEU A1121     3423   6053   3459    187    217   -133       C  
ATOM   1794  CD2 LEU A1121     -25.841  -0.407  -4.947  1.00 32.41           C  
ANISOU 1794  CD2 LEU A1121     3182   5906   3227    -24    310    -64       C  
ATOM   1795  N   GLN A1122     -30.582   0.816  -2.748  1.00 43.43           N  
ANISOU 1795  N   GLN A1122     4314   7829   4359    241    190    -48       N  
ATOM   1796  CA  GLN A1122     -31.477   0.710  -1.602  1.00 44.96           C  
ANISOU 1796  CA  GLN A1122     4462   8110   4510    294    162    -44       C  
ATOM   1797  C   GLN A1122     -32.458  -0.444  -1.778  1.00 43.93           C  
ANISOU 1797  C   GLN A1122     4307   8036   4347    195    162     -8       C  
ATOM   1798  O   GLN A1122     -32.803  -1.130  -0.817  1.00 43.02           O  
ANISOU 1798  O   GLN A1122     4180   7945   4220    183    158     -4       O  
ATOM   1799  CB  GLN A1122     -32.236   2.020  -1.389  1.00 47.72           C  
ANISOU 1799  CB  GLN A1122     4771   8551   4809    427    121    -60       C  
ATOM   1800  CG  GLN A1122     -33.137   2.023  -0.164  1.00 50.29           C  
ANISOU 1800  CG  GLN A1122     5060   8962   5087    487     94    -57       C  
ATOM   1801  CD  GLN A1122     -33.739   3.386   0.112  1.00 52.75           C  
ANISOU 1801  CD  GLN A1122     5353   9336   5352    625     58    -74       C  
ATOM   1802  OE1 GLN A1122     -33.478   4.350  -0.608  1.00 53.58           O  
ANISOU 1802  OE1 GLN A1122     5472   9420   5465    684     48    -90       O  
ATOM   1803  NE2 GLN A1122     -34.548   3.474   1.160  1.00 54.42           N  
ANISOU 1803  NE2 GLN A1122     5543   9619   5516    679     39    -72       N  
ATOM   1804  N   GLN A1123     -32.896  -0.658  -3.014  1.00 44.38           N  
ANISOU 1804  N   GLN A1123     4361   8111   4391    123    166     15       N  
ATOM   1805  CA  GLN A1123     -33.807  -1.752  -3.326  1.00 43.76           C  
ANISOU 1805  CA  GLN A1123     4267   8074   4285     23    163     48       C  
ATOM   1806  C   GLN A1123     -33.030  -3.039  -3.585  1.00 42.49           C  
ANISOU 1806  C   GLN A1123     4175   7789   4179    -99    201     60       C  
ATOM   1807  O   GLN A1123     -33.579  -4.016  -4.097  1.00 41.83           O  
ANISOU 1807  O   GLN A1123     4103   7705   4087   -195    205     84       O  
ATOM   1808  CB  GLN A1123     -34.676  -1.400  -4.535  1.00 44.48           C  
ANISOU 1808  CB  GLN A1123     4326   8239   4336      1    146     70       C  
ATOM   1809  CG  GLN A1123     -35.528  -0.150  -4.351  1.00 46.44           C  
ANISOU 1809  CG  GLN A1123     4508   8614   4524    127    108     62       C  
ATOM   1810  CD  GLN A1123     -36.339   0.195  -5.590  1.00 49.17           C  
ANISOU 1810  CD  GLN A1123     4820   9033   4830    104     92     85       C  
ATOM   1811  OE1 GLN A1123     -36.391  -0.578  -6.547  1.00 48.45           O  
ANISOU 1811  OE1 GLN A1123     4753   8904   4752    -16    106    111       O  
ATOM   1812  NE2 GLN A1123     -36.974   1.362  -5.576  1.00 50.43           N  
ANISOU 1812  NE2 GLN A1123     4932   9291   4939    221     61     77       N  
ATOM   1813  N   LYS A1124     -31.745  -3.018  -3.235  1.00 41.52           N  
ANISOU 1813  N   LYS A1124     4102   7559   4114    -89    229     41       N  
ATOM   1814  CA  LYS A1124     -30.866  -4.181  -3.343  1.00 40.22           C  
ANISOU 1814  CA  LYS A1124     4009   7267   4006   -185    267     50       C  
ATOM   1815  C   LYS A1124     -30.747  -4.722  -4.770  1.00 38.68           C  
ANISOU 1815  C   LYS A1124     3864   6999   3833   -293    288     73       C  
ATOM   1816  O   LYS A1124     -30.525  -5.916  -4.977  1.00 36.75           O  
ANISOU 1816  O   LYS A1124     3676   6671   3618   -381    311     88       O  
ATOM   1817  CB  LYS A1124     -31.302  -5.279  -2.368  1.00 42.59           C  
ANISOU 1817  CB  LYS A1124     4306   7582   4294   -214    266     56       C  
ATOM   1818  CG  LYS A1124     -31.356  -4.815  -0.918  1.00 45.42           C  
ANISOU 1818  CG  LYS A1124     4625   7999   4635   -116    248     33       C  
ATOM   1819  CD  LYS A1124     -31.770  -5.936   0.021  1.00 48.26           C  
ANISOU 1819  CD  LYS A1124     4985   8369   4982   -152    249     37       C  
ATOM   1820  CE  LYS A1124     -31.932  -5.427   1.446  1.00 50.31           C  
ANISOU 1820  CE  LYS A1124     5205   8691   5220    -56    227     15       C  
ATOM   1821  NZ  LYS A1124     -30.691  -4.774   1.949  1.00 50.54           N  
ANISOU 1821  NZ  LYS A1124     5260   8648   5295      6    240     -7       N  
ATOM   1822  N   ARG A1125     -30.892  -3.832  -5.747  1.00 38.80           N  
ANISOU 1822  N   ARG A1125     3866   7040   3835   -280    279     74       N  
ATOM   1823  CA  ARG A1125     -30.722  -4.190  -7.150  1.00 40.08           C  
ANISOU 1823  CA  ARG A1125     4082   7125   4021   -378    297     94       C  
ATOM   1824  C   ARG A1125     -29.301  -3.860  -7.590  1.00 40.16           C  
ANISOU 1824  C   ARG A1125     4154   7008   4096   -389    331     79       C  
ATOM   1825  O   ARG A1125     -29.060  -2.843  -8.242  1.00 40.16           O  
ANISOU 1825  O   ARG A1125     4150   7015   4094   -360    328     66       O  
ATOM   1826  CB  ARG A1125     -31.735  -3.440  -8.017  1.00 43.05           C  
ANISOU 1826  CB  ARG A1125     4410   7605   4344   -367    267    106       C  
ATOM   1827  CG  ARG A1125     -33.177  -3.853  -7.776  1.00 45.92           C  
ANISOU 1827  CG  ARG A1125     4711   8092   4644   -373    233    126       C  
ATOM   1828  CD  ARG A1125     -34.125  -2.672  -7.921  1.00 49.92           C  
ANISOU 1828  CD  ARG A1125     5136   8744   5087   -287    196    125       C  
ATOM   1829  NE  ARG A1125     -34.038  -2.043  -9.235  1.00 52.76           N  
ANISOU 1829  NE  ARG A1125     5512   9088   5446   -312    197    133       N  
ATOM   1830  CZ  ARG A1125     -34.718  -0.957  -9.589  1.00 55.27           C  
ANISOU 1830  CZ  ARG A1125     5772   9516   5713   -237    169    132       C  
ATOM   1831  NH1 ARG A1125     -34.578  -0.452 -10.808  1.00 55.81           N  
ANISOU 1831  NH1 ARG A1125     5865   9559   5781   -269    173    138       N  
ATOM   1832  NH2 ARG A1125     -35.538  -0.375  -8.725  1.00 56.21           N  
ANISOU 1832  NH2 ARG A1125     5812   9765   5779   -128    137    124       N  
ATOM   1833  N   TRP A1126     -28.365  -4.732  -7.228  1.00 38.72           N  
ANISOU 1833  N   TRP A1126     4030   6710   3970   -431    363     79       N  
ATOM   1834  CA  TRP A1126     -26.944  -4.473  -7.427  1.00 37.83           C  
ANISOU 1834  CA  TRP A1126     3971   6480   3923   -435    396     63       C  
ATOM   1835  C   TRP A1126     -26.534  -4.440  -8.899  1.00 38.74           C  
ANISOU 1835  C   TRP A1126     4148   6500   4073   -514    414     74       C  
ATOM   1836  O   TRP A1126     -25.781  -3.559  -9.318  1.00 39.13           O  
ANISOU 1836  O   TRP A1126     4209   6512   4145   -496    424     54       O  
ATOM   1837  CB  TRP A1126     -26.105  -5.510  -6.678  1.00 37.78           C  
ANISOU 1837  CB  TRP A1126     4011   6377   3967   -458    425     66       C  
ATOM   1838  CG  TRP A1126     -26.664  -5.913  -5.341  1.00 36.20           C  
ANISOU 1838  CG  TRP A1126     3768   6256   3733   -412    408     62       C  
ATOM   1839  CD1 TRP A1126     -27.021  -7.171  -4.950  1.00 34.70           C  
ANISOU 1839  CD1 TRP A1126     3601   6046   3539   -458    415     78       C  
ATOM   1840  CD2 TRP A1126     -26.931  -5.053  -4.217  1.00 35.56           C  
ANISOU 1840  CD2 TRP A1126     3617   6278   3615   -306    381     39       C  
ATOM   1841  NE1 TRP A1126     -27.488  -7.150  -3.657  1.00 34.52           N  
ANISOU 1841  NE1 TRP A1126     3526   6110   3481   -398    395     67       N  
ATOM   1842  CE2 TRP A1126     -27.444  -5.872  -3.191  1.00 34.69           C  
ANISOU 1842  CE2 TRP A1126     3492   6205   3483   -305    373     44       C  
ATOM   1843  CE3 TRP A1126     -26.783  -3.685  -3.993  1.00 36.13           C  
ANISOU 1843  CE3 TRP A1126     3646   6408   3673   -208    361     10       C  
ATOM   1844  CZ2 TRP A1126     -27.810  -5.349  -1.947  1.00 34.60           C  
ANISOU 1844  CZ2 TRP A1126     3424   6285   3439   -213    346     25       C  
ATOM   1845  CZ3 TRP A1126     -27.151  -3.175  -2.758  1.00 35.07           C  
ANISOU 1845  CZ3 TRP A1126     3459   6358   3506   -108    333     -9       C  
ATOM   1846  CH2 TRP A1126     -27.657  -4.005  -1.752  1.00 34.53           C  
ANISOU 1846  CH2 TRP A1126     3377   6324   3419   -115    326      0       C  
ATOM   1847  N   ASP A1127     -27.024  -5.402  -9.675  1.00 37.80           N  
ANISOU 1847  N   ASP A1127     4071   6335   3957   -599    417    102       N  
ATOM   1848  CA  ASP A1127     -26.646  -5.517 -11.083  1.00 36.06           C  
ANISOU 1848  CA  ASP A1127     3921   6005   3776   -676    433    114       C  
ATOM   1849  C   ASP A1127     -27.097  -4.305 -11.898  1.00 37.00           C  
ANISOU 1849  C   ASP A1127     4006   6194   3857   -665    411    108       C  
ATOM   1850  O   ASP A1127     -26.400  -3.871 -12.815  1.00 38.51           O  
ANISOU 1850  O   ASP A1127     4247   6297   4086   -701    426    101       O  
ATOM   1851  CB  ASP A1127     -27.200  -6.808 -11.693  1.00 34.25           C  
ANISOU 1851  CB  ASP A1127     3741   5720   3550   -751    435    141       C  
ATOM   1852  CG  ASP A1127     -26.654  -8.055 -11.019  1.00 33.72           C  
ANISOU 1852  CG  ASP A1127     3721   5569   3524   -758    461    145       C  
ATOM   1853  OD1 ASP A1127     -25.501  -8.436 -11.311  1.00 34.57           O  
ANISOU 1853  OD1 ASP A1127     3897   5537   3701   -773    493    145       O  
ATOM   1854  OD2 ASP A1127     -27.380  -8.660 -10.202  1.00 33.29           O  
ANISOU 1854  OD2 ASP A1127     3632   5587   3430   -746    450    149       O  
ATOM   1855  N   GLU A1128     -28.259  -3.761 -11.556  1.00 36.66           N  
ANISOU 1855  N   GLU A1128     3879   6310   3739   -611    375    109       N  
ATOM   1856  CA  GLU A1128     -28.770  -2.572 -12.227  1.00 37.75           C  
ANISOU 1856  CA  GLU A1128     3978   6535   3831   -579    353    103       C  
ATOM   1857  C   GLU A1128     -28.014  -1.328 -11.783  1.00 35.10           C  
ANISOU 1857  C   GLU A1128     3626   6209   3501   -478    352     61       C  
ATOM   1858  O   GLU A1128     -27.843  -0.386 -12.555  1.00 36.55           O  
ANISOU 1858  O   GLU A1128     3852   6325   3711   -448    314     39       O  
ATOM   1859  CB  GLU A1128     -30.265  -2.398 -11.956  1.00 44.10           C  
ANISOU 1859  CB  GLU A1128     4696   7506   4555   -536    311    118       C  
ATOM   1860  CG  GLU A1128     -31.128  -3.463 -12.597  1.00 47.99           C  
ANISOU 1860  CG  GLU A1128     5206   7992   5035   -632    301    153       C  
ATOM   1861  CD  GLU A1128     -32.599  -3.279 -12.299  1.00 52.63           C  
ANISOU 1861  CD  GLU A1128     5701   8751   5544   -592    260    168       C  
ATOM   1862  OE1 GLU A1128     -33.401  -4.144 -12.708  1.00 55.55           O  
ANISOU 1862  OE1 GLU A1128     6075   9134   5896   -664    248    193       O  
ATOM   1863  OE2 GLU A1128     -32.954  -2.270 -11.657  1.00 54.10           O  
ANISOU 1863  OE2 GLU A1128     5813   9056   5686   -482    238    152       O  
ATOM   1864  N   ALA A1129     -27.566  -1.332 -10.533  1.00 33.64           N  
ANISOU 1864  N   ALA A1129     3421   6031   3331   -404    354     40       N  
ATOM   1865  CA  ALA A1129     -26.803  -0.214  -9.993  1.00 31.62           C  
ANISOU 1865  CA  ALA A1129     3191   5698   3124   -285    312     -9       C  
ATOM   1866  C   ALA A1129     -25.434  -0.109 -10.658  1.00 31.50           C  
ANISOU 1866  C   ALA A1129     3272   5499   3199   -330    326    -28       C  
ATOM   1867  O   ALA A1129     -24.977   0.986 -10.982  1.00 31.96           O  
ANISOU 1867  O   ALA A1129     3375   5477   3291   -266    285    -65       O  
ATOM   1868  CB  ALA A1129     -26.654  -0.353  -8.488  1.00 30.13           C  
ANISOU 1868  CB  ALA A1129     2959   5561   2928   -209    314    -22       C  
ATOM   1869  N   ALA A1130     -24.789  -1.253 -10.863  1.00 31.40           N  
ANISOU 1869  N   ALA A1130     3292   5418   3220   -440    387     -3       N  
ATOM   1870  CA  ALA A1130     -23.458  -1.293 -11.461  1.00 31.08           C  
ANISOU 1870  CA  ALA A1130     3338   5204   3266   -490    410    -17       C  
ATOM   1871  C   ALA A1130     -23.478  -0.797 -12.899  1.00 30.85           C  
ANISOU 1871  C   ALA A1130     3367   5099   3255   -541    395    -21       C  
ATOM   1872  O   ALA A1130     -22.598  -0.043 -13.319  1.00 29.02           O  
ANISOU 1872  O   ALA A1130     3199   4742   3084   -516    375    -56       O  
ATOM   1873  CB  ALA A1130     -22.899  -2.697 -11.403  1.00 30.86           C  
ANISOU 1873  CB  ALA A1130     3330   5133   3261   -598    483     17       C  
ATOM   1874  N   VAL A1131     -24.484  -1.235 -13.650  1.00 32.49           N  
ANISOU 1874  N   VAL A1131     3553   5383   3408   -616    406     16       N  
ATOM   1875  CA  VAL A1131     -24.661  -0.807 -15.031  1.00 31.14           C  
ANISOU 1875  CA  VAL A1131     3433   5154   3246   -670    390     18       C  
ATOM   1876  C   VAL A1131     -24.899   0.697 -15.098  1.00 30.44           C  
ANISOU 1876  C   VAL A1131     3345   5071   3151   -549    316    -27       C  
ATOM   1877  O   VAL A1131     -24.332   1.393 -15.941  1.00 30.24           O  
ANISOU 1877  O   VAL A1131     3392   4928   3171   -554    296    -55       O  
ATOM   1878  CB  VAL A1131     -25.842  -1.543 -15.694  1.00 32.02           C  
ANISOU 1878  CB  VAL A1131     3509   5372   3286   -767    411     70       C  
ATOM   1879  CG1 VAL A1131     -26.194  -0.902 -17.027  1.00 32.03           C  
ANISOU 1879  CG1 VAL A1131     3551   5332   3285   -801    380     68       C  
ATOM   1880  CG2 VAL A1131     -25.517  -3.020 -15.871  1.00 30.53           C  
ANISOU 1880  CG2 VAL A1131     3382   5068   3151   -845    439     98       C  
ATOM   1881  N   ASN A1132     -25.733   1.192 -14.192  1.00 32.32           N  
ANISOU 1881  N   ASN A1132     3507   5445   3330   -440    278    -34       N  
ATOM   1882  CA  ASN A1132     -26.069   2.609 -14.148  1.00 36.39           C  
ANISOU 1882  CA  ASN A1132     4020   5982   3826   -315    210    -72       C  
ATOM   1883  C   ASN A1132     -24.879   3.475 -13.728  1.00 34.36           C  
ANISOU 1883  C   ASN A1132     3822   5601   3631   -235    188   -125       C  
ATOM   1884  O   ASN A1132     -24.705   4.586 -14.229  1.00 34.18           O  
ANISOU 1884  O   ASN A1132     3850   5517   3620   -179    144   -162       O  
ATOM   1885  CB  ASN A1132     -27.270   2.834 -13.223  1.00 41.51           C  
ANISOU 1885  CB  ASN A1132     4569   6810   4394   -221    182    -61       C  
ATOM   1886  CG  ASN A1132     -27.880   4.210 -13.381  1.00 45.55           C  
ANISOU 1886  CG  ASN A1132     5074   7363   4870   -103    116    -89       C  
ATOM   1887  OD1 ASN A1132     -28.398   4.786 -12.424  1.00 49.13           O  
ANISOU 1887  OD1 ASN A1132     5473   7912   5281     15     87   -102       O  
ATOM   1888  ND2 ASN A1132     -27.817   4.748 -14.590  1.00 44.76           N  
ANISOU 1888  ND2 ASN A1132     5035   7187   4786   -133     95    -99       N  
ATOM   1889  N   LEU A1133     -24.057   2.958 -12.819  1.00 32.32           N  
ANISOU 1889  N   LEU A1133     3563   5307   3411   -233    219   -130       N  
ATOM   1890  CA  LEU A1133     -22.870   3.676 -12.363  1.00 29.97           C  
ANISOU 1890  CA  LEU A1133     3319   4896   3172   -168    202   -176       C  
ATOM   1891  C   LEU A1133     -21.776   3.713 -13.429  1.00 25.96           C  
ANISOU 1891  C   LEU A1133     2906   4218   2738   -247    219   -193       C  
ATOM   1892  O   LEU A1133     -20.998   4.664 -13.498  1.00 25.50           O  
ANISOU 1892  O   LEU A1133     2907   4063   2717   -193    189   -239       O  
ATOM   1893  CB  LEU A1133     -22.329   3.060 -11.070  1.00 29.67           C  
ANISOU 1893  CB  LEU A1133     3248   4875   3151   -146    229   -172       C  
ATOM   1894  CG  LEU A1133     -23.151   3.312  -9.804  1.00 29.53           C  
ANISOU 1894  CG  LEU A1133     3150   4999   3070    -41    204   -171       C  
ATOM   1895  CD1 LEU A1133     -22.619   2.498  -8.634  1.00 27.38           C  
ANISOU 1895  CD1 LEU A1133     2849   4737   2817    -44    239   -161       C  
ATOM   1896  CD2 LEU A1133     -23.163   4.791  -9.462  1.00 30.77           C  
ANISOU 1896  CD2 LEU A1133     3325   5152   3213     91    144   -216       C  
ATOM   1897  N   ALA A1134     -21.729   2.680 -14.264  1.00 23.33           N  
ANISOU 1897  N   ALA A1134     2592   3848   2425   -378    269   -157       N  
ATOM   1898  CA  ALA A1134     -20.698   2.566 -15.293  1.00 21.84           C  
ANISOU 1898  CA  ALA A1134     2492   3497   2309   -466    294   -168       C  
ATOM   1899  C   ALA A1134     -20.928   3.511 -16.472  1.00 25.23           C  
ANISOU 1899  C   ALA A1134     2979   3871   2736   -468    254   -193       C  
ATOM   1900  O   ALA A1134     -20.138   3.540 -17.415  1.00 27.08           O  
ANISOU 1900  O   ALA A1134     3293   3968   3028   -539    270   -207       O  
ATOM   1901  CB  ALA A1134     -20.590   1.126 -15.779  1.00 18.07           C  
ANISOU 1901  CB  ALA A1134     2022   2997   1849   -606    366   -117       C  
ATOM   1902  N   LYS A1135     -22.010   4.280 -16.418  1.00 26.27           N  
ANISOU 1902  N   LYS A1135     3071   4110   2801   -388    203   -199       N  
ATOM   1903  CA  LYS A1135     -22.318   5.241 -17.471  1.00 26.32           C  
ANISOU 1903  CA  LYS A1135     3129   4075   2796   -377    159   -224       C  
ATOM   1904  C   LYS A1135     -21.994   6.661 -17.025  1.00 26.88           C  
ANISOU 1904  C   LYS A1135     3231   4118   2864   -243    102   -282       C  
ATOM   1905  O   LYS A1135     -21.930   7.580 -17.842  1.00 28.59           O  
ANISOU 1905  O   LYS A1135     3513   4267   3083   -226     66   -316       O  
ATOM   1906  CB  LYS A1135     -23.796   5.160 -17.854  1.00 27.35           C  
ANISOU 1906  CB  LYS A1135     3198   4345   2848   -382    140   -187       C  
ATOM   1907  CG  LYS A1135     -24.263   3.782 -18.274  1.00 28.11           C  
ANISOU 1907  CG  LYS A1135     3262   4487   2930   -515    195   -126       C  
ATOM   1908  CD  LYS A1135     -25.761   3.777 -18.515  1.00 28.39           C  
ANISOU 1908  CD  LYS A1135     3227   4679   2881   -509    171    -90       C  
ATOM   1909  CE  LYS A1135     -26.260   2.387 -18.864  1.00 30.66           C  
ANISOU 1909  CE  LYS A1135     3483   5023   3144   -646    227    -28       C  
ATOM   1910  NZ  LYS A1135     -27.736   2.368 -19.070  1.00 33.05           N  
ANISOU 1910  NZ  LYS A1135     3711   5488   3360   -643    203      9       N  
ATOM   1911  N   SER A1136     -21.790   6.830 -15.722  1.00 25.12           N  
ANISOU 1911  N   SER A1136     2967   3945   2632   -152     95   -294       N  
ATOM   1912  CA  SER A1136     -21.600   8.151 -15.134  1.00 25.48           C  
ANISOU 1912  CA  SER A1136     3036   3983   2660    -18     43   -344       C  
ATOM   1913  C   SER A1136     -20.315   8.827 -15.597  1.00 26.09           C  
ANISOU 1913  C   SER A1136     3218   3894   2800    -27     35   -396       C  
ATOM   1914  O   SER A1136     -19.394   8.172 -16.086  1.00 23.44           O  
ANISOU 1914  O   SER A1136     2926   3450   2532   -128     75   -393       O  
ATOM   1915  CB  SER A1136     -21.614   8.060 -13.606  1.00 26.27           C  
ANISOU 1915  CB  SER A1136     3072   4169   2740     67     44   -340       C  
ATOM   1916  OG  SER A1136     -20.556   7.244 -13.133  1.00 25.75           O  
ANISOU 1916  OG  SER A1136     3013   4034   2736     10     88   -334       O  
ATOM   1917  N   ARG A1137     -20.266  10.147 -15.440  1.00 28.81           N  
ANISOU 1917  N   ARG A1137     3607   4222   3119     79    -16   -443       N  
ATOM   1918  CA  ARG A1137     -19.062  10.909 -15.731  1.00 32.72           C  
ANISOU 1918  CA  ARG A1137     4202   4571   3661     83    -28   -498       C  
ATOM   1919  C   ARG A1137     -17.973  10.523 -14.736  1.00 34.69           C  
ANISOU 1919  C   ARG A1137     4444   4779   3959     84     -1   -504       C  
ATOM   1920  O   ARG A1137     -16.785  10.541 -15.055  1.00 34.23           O  
ANISOU 1920  O   ARG A1137     4451   4590   3963     33     14   -531       O  
ATOM   1921  CB  ARG A1137     -19.349  12.410 -15.650  1.00 37.16           C  
ANISOU 1921  CB  ARG A1137     4811   5139   4169    205    -87   -546       C  
ATOM   1922  CG  ARG A1137     -18.177  13.292 -16.051  1.00 44.48           C  
ANISOU 1922  CG  ARG A1137     5851   5916   5133    207   -103   -607       C  
ATOM   1923  CD  ARG A1137     -18.546  14.766 -15.992  1.00 50.52           C  
ANISOU 1923  CD  ARG A1137     6670   6693   5834    327   -160   -652       C  
ATOM   1924  NE  ARG A1137     -19.602  15.102 -16.942  1.00 54.63           N  
ANISOU 1924  NE  ARG A1137     7196   7253   6309    333   -186   -645       N  
ATOM   1925  CZ  ARG A1137     -19.386  15.472 -18.201  1.00 56.06           C  
ANISOU 1925  CZ  ARG A1137     7462   7332   6507    277   -198   -673       C  
ATOM   1926  NH1 ARG A1137     -20.410  15.758 -18.994  1.00 57.37           N  
ANISOU 1926  NH1 ARG A1137     7626   7545   6628    287   -224   -662       N  
ATOM   1927  NH2 ARG A1137     -18.146  15.556 -18.667  1.00 54.76           N  
ANISOU 1927  NH2 ARG A1137     7383   7018   6405    209   -183   -713       N  
ATOM   1928  N   TRP A1138     -18.401  10.164 -13.529  1.00 35.08           N  
ANISOU 1928  N   TRP A1138     4411   4941   3977    141      4   -477       N  
ATOM   1929  CA  TRP A1138     -17.502   9.718 -12.472  1.00 32.63           C  
ANISOU 1929  CA  TRP A1138     4081   4611   3705    146     28   -475       C  
ATOM   1930  C   TRP A1138     -16.729   8.470 -12.886  1.00 31.15           C  
ANISOU 1930  C   TRP A1138     3897   4349   3591     19     86   -448       C  
ATOM   1931  O   TRP A1138     -15.533   8.355 -12.620  1.00 32.50           O  
ANISOU 1931  O   TRP A1138     4100   4427   3819     -3    104   -464       O  
ATOM   1932  CB  TRP A1138     -18.299   9.460 -11.191  1.00 33.89           C  
ANISOU 1932  CB  TRP A1138     4149   4915   3812    221     25   -447       C  
ATOM   1933  CG  TRP A1138     -17.593   8.616 -10.175  1.00 31.57           C  
ANISOU 1933  CG  TRP A1138     3817   4621   3556    201     60   -429       C  
ATOM   1934  CD1 TRP A1138     -16.463   8.938  -9.483  1.00 30.55           C  
ANISOU 1934  CD1 TRP A1138     3722   4421   3466    229     57   -455       C  
ATOM   1935  CD2 TRP A1138     -17.991   7.315  -9.716  1.00 30.37           C  
ANISOU 1935  CD2 TRP A1138     3588   4548   3404    148    102   -379       C  
ATOM   1936  NE1 TRP A1138     -16.124   7.914  -8.631  1.00 30.45           N  
ANISOU 1936  NE1 TRP A1138     3655   4435   3478    200     93   -424       N  
ATOM   1937  CE2 TRP A1138     -17.043   6.911  -8.754  1.00 29.87           C  
ANISOU 1937  CE2 TRP A1138     3517   4451   3381    151    123   -379       C  
ATOM   1938  CE3 TRP A1138     -19.048   6.459 -10.030  1.00 30.23           C  
ANISOU 1938  CE3 TRP A1138     3510   4626   3351     97    125   -335       C  
ATOM   1939  CZ2 TRP A1138     -17.128   5.679  -8.102  1.00 28.88           C  
ANISOU 1939  CZ2 TRP A1138     3328   4381   3262    108    165   -337       C  
ATOM   1940  CZ3 TRP A1138     -19.128   5.239  -9.382  1.00 30.99           C  
ANISOU 1940  CZ3 TRP A1138     3547   4779   3451     50    169   -295       C  
ATOM   1941  CH2 TRP A1138     -18.173   4.861  -8.429  1.00 30.89           C  
ANISOU 1941  CH2 TRP A1138     3531   4727   3480     58    189   -297       C  
ATOM   1942  N   TYR A1139     -17.414   7.540 -13.543  1.00 30.45           N  
ANISOU 1942  N   TYR A1139     3774   4300   3496    -65    118   -404       N  
ATOM   1943  CA  TYR A1139     -16.765   6.333 -14.038  1.00 31.05           C  
ANISOU 1943  CA  TYR A1139     3860   4303   3634   -190    178   -374       C  
ATOM   1944  C   TYR A1139     -15.818   6.647 -15.190  1.00 32.56           C  
ANISOU 1944  C   TYR A1139     4148   4336   3887   -258    185   -406       C  
ATOM   1945  O   TYR A1139     -14.736   6.074 -15.284  1.00 32.17           O  
ANISOU 1945  O   TYR A1139     4129   4190   3906   -323    225   -404       O  
ATOM   1946  CB  TYR A1139     -17.801   5.295 -14.480  1.00 31.00           C  
ANISOU 1946  CB  TYR A1139     3802   4383   3595   -267    210   -319       C  
ATOM   1947  CG  TYR A1139     -17.205   4.113 -15.219  1.00 31.28           C  
ANISOU 1947  CG  TYR A1139     3866   4332   3687   -404    275   -287       C  
ATOM   1948  CD1 TYR A1139     -16.686   3.024 -14.529  1.00 31.37           C  
ANISOU 1948  CD1 TYR A1139     3845   4345   3727   -443    327   -256       C  
ATOM   1949  CD2 TYR A1139     -17.163   4.086 -16.609  1.00 31.69           C  
ANISOU 1949  CD2 TYR A1139     3981   4297   3762   -494    287   -286       C  
ATOM   1950  CE1 TYR A1139     -16.141   1.944 -15.203  1.00 31.38           C  
ANISOU 1950  CE1 TYR A1139     3879   4267   3778   -564    390   -224       C  
ATOM   1951  CE2 TYR A1139     -16.620   3.014 -17.289  1.00 31.26           C  
ANISOU 1951  CE2 TYR A1139     3959   4159   3758   -620    350   -255       C  
ATOM   1952  CZ  TYR A1139     -16.112   1.946 -16.583  1.00 31.81           C  
ANISOU 1952  CZ  TYR A1139     3998   4235   3855   -653    403   -224       C  
ATOM   1953  OH  TYR A1139     -15.573   0.877 -17.263  1.00 32.39           O  
ANISOU 1953  OH  TYR A1139     4108   4223   3975   -775    470   -190       O  
ATOM   1954  N   ASN A1140     -16.231   7.556 -16.068  1.00 34.15           N  
ANISOU 1954  N   ASN A1140     4400   4512   4065   -242    146   -435       N  
ATOM   1955  CA  ASN A1140     -15.433   7.895 -17.243  1.00 36.27           C  
ANISOU 1955  CA  ASN A1140     4765   4631   4386   -311    150   -468       C  
ATOM   1956  C   ASN A1140     -14.268   8.835 -16.944  1.00 38.89           C  
ANISOU 1956  C   ASN A1140     5162   4864   4752   -259    126   -527       C  
ATOM   1957  O   ASN A1140     -13.375   9.011 -17.774  1.00 39.60           O  
ANISOU 1957  O   ASN A1140     5330   4819   4896   -321    137   -556       O  
ATOM   1958  CB  ASN A1140     -16.318   8.481 -18.346  1.00 36.94           C  
ANISOU 1958  CB  ASN A1140     4884   4721   4431   -321    117   -477       C  
ATOM   1959  CG  ASN A1140     -17.223   7.442 -18.979  1.00 37.81           C  
ANISOU 1959  CG  ASN A1140     4951   4890   4522   -413    150   -418       C  
ATOM   1960  OD1 ASN A1140     -16.786   6.657 -19.819  1.00 36.83           O  
ANISOU 1960  OD1 ASN A1140     4865   4680   4449   -533    197   -398       O  
ATOM   1961  ND2 ASN A1140     -18.490   7.434 -18.580  1.00 38.35           N  
ANISOU 1961  ND2 ASN A1140     4945   5109   4518   -360    128   -389       N  
ATOM   1962  N   GLN A1141     -14.276   9.434 -15.757  1.00 39.24           N  
ANISOU 1962  N   GLN A1141     5174   4973   4761   -148     94   -543       N  
ATOM   1963  CA  GLN A1141     -13.235  10.382 -15.380  1.00 39.61           C  
ANISOU 1963  CA  GLN A1141     5282   4940   4827    -95     69   -598       C  
ATOM   1964  C   GLN A1141     -12.133   9.700 -14.572  1.00 38.64           C  
ANISOU 1964  C   GLN A1141     5137   4783   4763   -119    105   -586       C  
ATOM   1965  O   GLN A1141     -10.948   9.962 -14.777  1.00 40.49           O  
ANISOU 1965  O   GLN A1141     5431   4905   5051   -147    111   -619       O  
ATOM   1966  CB  GLN A1141     -13.835  11.551 -14.597  1.00 41.24           C  
ANISOU 1966  CB  GLN A1141     5483   5228   4958     40     12   -625       C  
ATOM   1967  CG  GLN A1141     -13.219  12.899 -14.927  1.00 42.08           C  
ANISOU 1967  CG  GLN A1141     5691   5243   5056     85    -28   -692       C  
ATOM   1968  CD  GLN A1141     -13.959  14.052 -14.279  1.00 43.93           C  
ANISOU 1968  CD  GLN A1141     5927   5559   5205    217    -80   -714       C  
ATOM   1969  OE1 GLN A1141     -14.827  13.849 -13.430  1.00 44.30           O  
ANISOU 1969  OE1 GLN A1141     5895   5732   5205    280    -86   -681       O  
ATOM   1970  NE2 GLN A1141     -13.622  15.271 -14.681  1.00 45.58           N  
ANISOU 1970  NE2 GLN A1141     6232   5696   5391    258   -117   -772       N  
ATOM   1971  N   THR A1142     -12.531   8.827 -13.651  1.00 34.63           N  
ANISOU 1971  N   THR A1142     4541   4374   4243   -107    128   -539       N  
ATOM   1972  CA  THR A1142     -11.580   8.037 -12.874  1.00 28.88           C  
ANISOU 1972  CA  THR A1142     3783   3622   3567   -133    166   -520       C  
ATOM   1973  C   THR A1142     -11.949   6.557 -12.937  1.00 24.81           C  
ANISOU 1973  C   THR A1142     3207   3150   3068   -213    223   -459       C  
ATOM   1974  O   THR A1142     -12.431   5.993 -11.955  1.00 21.31           O  
ANISOU 1974  O   THR A1142     2691   2810   2597   -180    232   -426       O  
ATOM   1975  CB  THR A1142     -11.542   8.483 -11.401  1.00 29.78           C  
ANISOU 1975  CB  THR A1142     3856   3813   3647    -27    137   -527       C  
ATOM   1976  OG1 THR A1142     -12.839   8.320 -10.814  1.00 30.56           O  
ANISOU 1976  OG1 THR A1142     3883   4052   3678     28    125   -498       O  
ATOM   1977  CG2 THR A1142     -11.123   9.942 -11.294  1.00 30.54           C  
ANISOU 1977  CG2 THR A1142     4019   3863   3721     49     85   -587       C  
ATOM   1978  N   PRO A1143     -11.710   5.920 -14.095  1.00 25.79           N  
ANISOU 1978  N   PRO A1143     3369   3192   3237   -322    263   -444       N  
ATOM   1979  CA  PRO A1143     -12.170   4.552 -14.363  1.00 26.35           C  
ANISOU 1979  CA  PRO A1143     3399   3299   3313   -409    320   -385       C  
ATOM   1980  C   PRO A1143     -11.534   3.494 -13.468  1.00 26.87           C  
ANISOU 1980  C   PRO A1143     3420   3374   3414   -427    367   -351       C  
ATOM   1981  O   PRO A1143     -12.218   2.553 -13.069  1.00 27.49           O  
ANISOU 1981  O   PRO A1143     3440   3543   3462   -448    396   -305       O  
ATOM   1982  CB  PRO A1143     -11.767   4.327 -15.823  1.00 25.54           C  
ANISOU 1982  CB  PRO A1143     3370   3073   3260   -518    351   -388       C  
ATOM   1983  CG  PRO A1143     -10.635   5.257 -16.048  1.00 25.76           C  
ANISOU 1983  CG  PRO A1143     3468   2983   3334   -498    327   -444       C  
ATOM   1984  CD  PRO A1143     -10.937   6.469 -15.222  1.00 24.94           C  
ANISOU 1984  CD  PRO A1143     3354   2946   3177   -373    261   -484       C  
ATOM   1985  N   ASN A1144     -10.251   3.646 -13.159  1.00 27.27           N  
ANISOU 1985  N   ASN A1144     3500   3338   3525   -421    374   -373       N  
ATOM   1986  CA  ASN A1144      -9.543   2.651 -12.362  1.00 27.18           C  
ANISOU 1986  CA  ASN A1144     3451   3324   3552   -439    418   -341       C  
ATOM   1987  C   ASN A1144     -10.109   2.490 -10.950  1.00 27.04           C  
ANISOU 1987  C   ASN A1144     3355   3436   3483   -359    401   -323       C  
ATOM   1988  O   ASN A1144     -10.331   1.371 -10.488  1.00 27.47           O  
ANISOU 1988  O   ASN A1144     3362   3542   3532   -390    443   -279       O  
ATOM   1989  CB  ASN A1144      -8.047   2.969 -12.301  1.00 26.77           C  
ANISOU 1989  CB  ASN A1144     3442   3158   3572   -441    422   -370       C  
ATOM   1990  CG  ASN A1144      -7.245   1.861 -11.647  1.00 28.16           C  
ANISOU 1990  CG  ASN A1144     3585   3320   3795   -470    475   -333       C  
ATOM   1991  OD1 ASN A1144      -7.059   1.848 -10.430  1.00 30.67           O  
ANISOU 1991  OD1 ASN A1144     3854   3696   4101   -405    460   -329       O  
ATOM   1992  ND2 ASN A1144      -6.770   0.921 -12.455  1.00 27.27           N  
ANISOU 1992  ND2 ASN A1144     3499   3127   3734   -568    538   -304       N  
ATOM   1993  N   ARG A1145     -10.346   3.609 -10.271  1.00 26.12           N  
ANISOU 1993  N   ARG A1145     3231   3368   3327   -258    340   -359       N  
ATOM   1994  CA  ARG A1145     -10.892   3.573  -8.918  1.00 26.78           C  
ANISOU 1994  CA  ARG A1145     3245   3569   3360   -177    320   -347       C  
ATOM   1995  C   ARG A1145     -12.376   3.227  -8.914  1.00 27.16           C  
ANISOU 1995  C   ARG A1145     3241   3740   3337   -172    319   -319       C  
ATOM   1996  O   ARG A1145     -12.825   2.401  -8.121  1.00 26.89           O  
ANISOU 1996  O   ARG A1145     3146   3792   3277   -169    341   -284       O  
ATOM   1997  CB  ARG A1145     -10.667   4.909  -8.207  1.00 27.44           C  
ANISOU 1997  CB  ARG A1145     3345   3660   3419    -73    259   -393       C  
ATOM   1998  CG  ARG A1145     -11.360   5.012  -6.856  1.00 28.70           C  
ANISOU 1998  CG  ARG A1145     3440   3942   3521     15    235   -383       C  
ATOM   1999  CD  ARG A1145     -11.061   6.342  -6.189  1.00 30.07           C  
ANISOU 1999  CD  ARG A1145     3642   4112   3671    113    179   -427       C  
ATOM   2000  NE  ARG A1145     -11.815   6.518  -4.951  1.00 29.10           N  
ANISOU 2000  NE  ARG A1145     3464   4105   3489    198    155   -418       N  
ATOM   2001  CZ  ARG A1145     -11.690   7.568  -4.146  1.00 29.61           C  
ANISOU 2001  CZ  ARG A1145     3545   4184   3521    288    111   -448       C  
ATOM   2002  NH1 ARG A1145     -10.834   8.537  -4.446  1.00 32.26           N  
ANISOU 2002  NH1 ARG A1145     3952   4429   3875    303     86   -489       N  
ATOM   2003  NH2 ARG A1145     -12.416   7.648  -3.041  1.00 27.94           N  
ANISOU 2003  NH2 ARG A1145     3283   4077   3257    361     95   -437       N  
ATOM   2004  N   ALA A1146     -13.129   3.865  -9.806  1.00 29.29           N  
ANISOU 2004  N   ALA A1146     3536   4020   3573   -171    293   -334       N  
ATOM   2005  CA  ALA A1146     -14.573   3.659  -9.895  1.00 30.30           C  
ANISOU 2005  CA  ALA A1146     3615   4269   3630   -164    287   -308       C  
ATOM   2006  C   ALA A1146     -14.937   2.197 -10.134  1.00 30.19           C  
ANISOU 2006  C   ALA A1146     3566   4288   3616   -261    348   -254       C  
ATOM   2007  O   ALA A1146     -15.928   1.703  -9.600  1.00 29.35           O  
ANISOU 2007  O   ALA A1146     3396   4304   3452   -248    353   -225       O  
ATOM   2008  CB  ALA A1146     -15.167   4.537 -10.987  1.00 29.87           C  
ANISOU 2008  CB  ALA A1146     3601   4198   3549   -160    252   -332       C  
ATOM   2009  N   LYS A1147     -14.125   1.510 -10.932  1.00 29.70           N  
ANISOU 2009  N   LYS A1147     3551   4118   3616   -359    396   -240       N  
ATOM   2010  CA  LYS A1147     -14.379   0.114 -11.272  1.00 29.52           C  
ANISOU 2010  CA  LYS A1147     3512   4110   3593   -461    461   -188       C  
ATOM   2011  C   LYS A1147     -14.357  -0.783 -10.035  1.00 29.64           C  
ANISOU 2011  C   LYS A1147     3469   4198   3595   -444    489   -159       C  
ATOM   2012  O   LYS A1147     -15.099  -1.762  -9.954  1.00 30.56           O  
ANISOU 2012  O   LYS A1147     3549   4392   3670   -493    525   -118       O  
ATOM   2013  CB  LYS A1147     -13.366  -0.373 -12.308  1.00 30.10           C  
ANISOU 2013  CB  LYS A1147     3656   4039   3741   -562    509   -182       C  
ATOM   2014  CG  LYS A1147     -13.812  -1.593 -13.094  1.00 34.89           C  
ANISOU 2014  CG  LYS A1147     4271   4647   4338   -680    572   -130       C  
ATOM   2015  CD  LYS A1147     -12.881  -1.863 -14.269  1.00 39.43           C  
ANISOU 2015  CD  LYS A1147     4925   5070   4985   -776    615   -129       C  
ATOM   2016  CE  LYS A1147     -13.388  -3.013 -15.131  1.00 41.69           C  
ANISOU 2016  CE  LYS A1147     5240   5348   5255   -805    608    -73       C  
ATOM   2017  NZ  LYS A1147     -14.724  -2.728 -15.728  1.00 42.25           N  
ANISOU 2017  NZ  LYS A1147     5295   5498   5261   -839    595    -66       N  
ATOM   2018  N   ARG A1148     -13.512  -0.440  -9.068  1.00 29.30           N  
ANISOU 2018  N   ARG A1148     3419   4129   3583   -376    471   -182       N  
ATOM   2019  CA  ARG A1148     -13.413  -1.216  -7.836  1.00 27.36           C  
ANISOU 2019  CA  ARG A1148     3122   3945   3328   -354    493   -158       C  
ATOM   2020  C   ARG A1148     -14.568  -0.925  -6.880  1.00 26.63           C  
ANISOU 2020  C   ARG A1148     2963   3998   3157   -275    456   -160       C  
ATOM   2021  O   ARG A1148     -15.093  -1.835  -6.238  1.00 27.92           O  
ANISOU 2021  O   ARG A1148     3079   4246   3284   -290    484   -129       O  
ATOM   2022  CB  ARG A1148     -12.073  -0.964  -7.140  1.00 25.54           C  
ANISOU 2022  CB  ARG A1148     2908   3636   3160   -314    486   -179       C  
ATOM   2023  CG  ARG A1148     -10.874  -1.534  -7.880  1.00 23.39           C  
ANISOU 2023  CG  ARG A1148     2689   3232   2968   -395    536   -169       C  
ATOM   2024  CD  ARG A1148      -9.602  -1.384  -7.062  1.00 23.27           C  
ANISOU 2024  CD  ARG A1148     2677   3158   3008   -353    530   -183       C  
ATOM   2025  NE  ARG A1148      -9.230   0.016  -6.880  1.00 24.57           N  
ANISOU 2025  NE  ARG A1148     2862   3296   3179   -277    467   -233       N  
ATOM   2026  CZ  ARG A1148      -8.383   0.671  -7.668  1.00 25.60           C  
ANISOU 2026  CZ  ARG A1148     3052   3316   3360   -296    458   -264       C  
ATOM   2027  NH1 ARG A1148      -7.815   0.053  -8.695  1.00 23.49           N  
ANISOU 2027  NH1 ARG A1148     2826   2953   3146   -387    508   -249       N  
ATOM   2028  NH2 ARG A1148      -8.102   1.945  -7.428  1.00 26.46           N  
ANISOU 2028  NH2 ARG A1148     3183   3408   3461   -225    400   -310       N  
ATOM   2029  N   VAL A1149     -14.955   0.343  -6.784  1.00 23.87           N  
ANISOU 2029  N   VAL A1149     2613   3676   2779   -190    394   -196       N  
ATOM   2030  CA  VAL A1149     -16.059   0.739  -5.917  1.00 24.54           C  
ANISOU 2030  CA  VAL A1149     2639   3897   2791   -107    358   -199       C  
ATOM   2031  C   VAL A1149     -17.371   0.126  -6.402  1.00 23.85           C  
ANISOU 2031  C   VAL A1149     2512   3910   2641   -156    376   -167       C  
ATOM   2032  O   VAL A1149     -18.143  -0.416  -5.611  1.00 22.72           O  
ANISOU 2032  O   VAL A1149     2307   3879   2444   -140    385   -146       O  
ATOM   2033  CB  VAL A1149     -16.202   2.272  -5.850  1.00 26.12           C  
ANISOU 2033  CB  VAL A1149     2858   4096   2970     -7    292   -244       C  
ATOM   2034  CG1 VAL A1149     -17.355   2.661  -4.935  1.00 25.65           C  
ANISOU 2034  CG1 VAL A1149     2736   4176   2834     82    259   -244       C  
ATOM   2035  CG2 VAL A1149     -14.904   2.902  -5.374  1.00 25.76           C  
ANISOU 2035  CG2 VAL A1149     2855   3953   2979     35    274   -276       C  
ATOM   2036  N   ILE A1150     -17.604   0.214  -7.709  1.00 23.58           N  
ANISOU 2036  N   ILE A1150     2513   3835   2610   -218    382   -162       N  
ATOM   2037  CA  ILE A1150     -18.779  -0.371  -8.347  1.00 22.28           C  
ANISOU 2037  CA  ILE A1150     2320   3756   2389   -280    401   -128       C  
ATOM   2038  C   ILE A1150     -18.863  -1.873  -8.090  1.00 22.62           C  
ANISOU 2038  C   ILE A1150     2339   3834   2423   -366    466    -83       C  
ATOM   2039  O   ILE A1150     -19.928  -2.402  -7.770  1.00 23.75           O  
ANISOU 2039  O   ILE A1150     2425   4100   2497   -377    475    -57       O  
ATOM   2040  CB  ILE A1150     -18.763  -0.112  -9.869  1.00 21.62           C  
ANISOU 2040  CB  ILE A1150     2294   3594   2326   -350    403   -130       C  
ATOM   2041  CG1 ILE A1150     -19.008   1.369 -10.161  1.00 23.16           C  
ANISOU 2041  CG1 ILE A1150     2509   3783   2508   -262    336   -173       C  
ATOM   2042  CG2 ILE A1150     -19.801  -0.965 -10.579  1.00 20.10           C  
ANISOU 2042  CG2 ILE A1150     2079   3476   2083   -441    435    -86       C  
ATOM   2043  CD1 ILE A1150     -18.832   1.738 -11.617  1.00 23.45           C  
ANISOU 2043  CD1 ILE A1150     2613   3723   2572   -324    333   -183       C  
ATOM   2044  N   THR A1151     -17.727  -2.550  -8.222  1.00 21.58           N  
ANISOU 2044  N   THR A1151     2250   3592   2356   -427    511    -73       N  
ATOM   2045  CA  THR A1151     -17.652  -3.991  -8.004  1.00 21.44           C  
ANISOU 2045  CA  THR A1151     2225   3589   2333   -509    578    -31       C  
ATOM   2046  C   THR A1151     -18.007  -4.349  -6.562  1.00 23.88           C  
ANISOU 2046  C   THR A1151     2470   4003   2600   -449    574    -27       C  
ATOM   2047  O   THR A1151     -18.580  -5.406  -6.296  1.00 24.16           O  
ANISOU 2047  O   THR A1151     2501   4072   2607   -483    592      7       O  
ATOM   2048  CB  THR A1151     -16.245  -4.521  -8.330  1.00 19.36           C  
ANISOU 2048  CB  THR A1151     2022   3180   2154   -566    624    -25       C  
ATOM   2049  OG1 THR A1151     -15.852  -4.058  -9.627  1.00 22.91           O  
ANISOU 2049  OG1 THR A1151     2533   3523   2647   -614    623    -36       O  
ATOM   2050  CG2 THR A1151     -16.217  -6.043  -8.306  1.00 16.12           C  
ANISOU 2050  CG2 THR A1151     1648   2719   1760   -607    651     26       C  
ATOM   2051  N   THR A1152     -17.670  -3.459  -5.635  1.00 25.50           N  
ANISOU 2051  N   THR A1152     2657   4213   2819   -342    525    -62       N  
ATOM   2052  CA  THR A1152     -17.955  -3.679  -4.222  1.00 27.69           C  
ANISOU 2052  CA  THR A1152     2880   4581   3061   -279    517    -62       C  
ATOM   2053  C   THR A1152     -19.458  -3.579  -3.960  1.00 30.44           C  
ANISOU 2053  C   THR A1152     3166   5082   3320   -252    496    -56       C  
ATOM   2054  O   THR A1152     -20.000  -4.279  -3.105  1.00 29.48           O  
ANISOU 2054  O   THR A1152     2998   5053   3150   -251    514    -40       O  
ATOM   2055  CB  THR A1152     -17.179  -2.684  -3.332  1.00 27.11           C  
ANISOU 2055  CB  THR A1152     2810   4467   3025   -175    469   -101       C  
ATOM   2056  OG1 THR A1152     -15.773  -2.812  -3.584  1.00 26.81           O  
ANISOU 2056  OG1 THR A1152     2825   4293   3068   -205    489   -105       O  
ATOM   2057  CG2 THR A1152     -17.446  -2.952  -1.863  1.00 26.82           C  
ANISOU 2057  CG2 THR A1152     2721   4517   2953   -116    462   -100       C  
ATOM   2058  N   PHE A1153     -20.127  -2.713  -4.714  1.00 33.29           N  
ANISOU 2058  N   PHE A1153     3526   5468   3656   -229    459    -68       N  
ATOM   2059  CA  PHE A1153     -21.579  -2.598  -4.653  1.00 35.36           C  
ANISOU 2059  CA  PHE A1153     3727   5874   3833   -208    440    -58       C  
ATOM   2060  C   PHE A1153     -22.241  -3.858  -5.197  1.00 39.32           C  
ANISOU 2060  C   PHE A1153     4231   6403   4304   -318    480    -14       C  
ATOM   2061  O   PHE A1153     -23.294  -4.277  -4.714  1.00 41.92           O  
ANISOU 2061  O   PHE A1153     4529   6812   4584   -308    458      0       O  
ATOM   2062  CB  PHE A1153     -22.053  -1.384  -5.451  1.00 34.03           C  
ANISOU 2062  CB  PHE A1153     3570   5708   3653   -161    389    -80       C  
ATOM   2063  CG  PHE A1153     -21.869  -0.078  -4.737  1.00 33.37           C  
ANISOU 2063  CG  PHE A1153     3484   5621   3574    -31    330   -121       C  
ATOM   2064  CD1 PHE A1153     -22.109   0.024  -3.376  1.00 33.09           C  
ANISOU 2064  CD1 PHE A1153     3401   5662   3510     49    316   -130       C  
ATOM   2065  CD2 PHE A1153     -21.455   1.050  -5.427  1.00 32.00           C  
ANISOU 2065  CD2 PHE A1153     3363   5365   3432      8    292   -152       C  
ATOM   2066  CE1 PHE A1153     -21.943   1.227  -2.716  1.00 32.65           C  
ANISOU 2066  CE1 PHE A1153     3351   5600   3455    165    265   -165       C  
ATOM   2067  CE2 PHE A1153     -21.285   2.255  -4.773  1.00 32.59           C  
ANISOU 2067  CE2 PHE A1153     3444   5434   3503    124    242   -189       C  
ATOM   2068  CZ  PHE A1153     -21.529   2.344  -3.415  1.00 33.30           C  
ANISOU 2068  CZ  PHE A1153     3489   5601   3564    203    229   -194       C  
ATOM   2069  N   ARG A1154     -21.614  -4.455  -6.206  1.00 40.01           N  
ANISOU 2069  N   ARG A1154     4389   6370   4444   -411    512      4       N  
ATOM   2070  CA  ARG A1154     -22.133  -5.659  -6.850  1.00 42.18           C  
ANISOU 2070  CA  ARG A1154     4712   6592   4722   -495    522     42       C  
ATOM   2071  C   ARG A1154     -22.185  -6.856  -5.910  1.00 42.41           C  
ANISOU 2071  C   ARG A1154     4753   6607   4755   -499    531     57       C  
ATOM   2072  O   ARG A1154     -23.261  -7.358  -5.585  1.00 42.57           O  
ANISOU 2072  O   ARG A1154     4749   6700   4725   -501    511     68       O  
ATOM   2073  CB  ARG A1154     -21.280  -6.016  -8.070  1.00 43.40           C  
ANISOU 2073  CB  ARG A1154     4950   6597   4944   -572    552     54       C  
ATOM   2074  CG  ARG A1154     -21.672  -5.291  -9.338  1.00 45.95           C  
ANISOU 2074  CG  ARG A1154     5282   6924   5253   -607    540     52       C  
ATOM   2075  CD  ARG A1154     -22.801  -6.011 -10.053  1.00 49.77           C  
ANISOU 2075  CD  ARG A1154     5781   7425   5703   -657    525     81       C  
ATOM   2076  NE  ARG A1154     -22.315  -7.134 -10.849  1.00 52.49           N  
ANISOU 2076  NE  ARG A1154     6213   7624   6107   -718    548    105       N  
ATOM   2077  CZ  ARG A1154     -22.025  -7.059 -12.145  1.00 54.68           C  
ANISOU 2077  CZ  ARG A1154     6548   7806   6421   -765    552    111       C  
ATOM   2078  NH1 ARG A1154     -22.173  -5.912 -12.794  1.00 55.29           N  
ANISOU 2078  NH1 ARG A1154     6610   7916   6481   -774    538     94       N  
ATOM   2079  NH2 ARG A1154     -21.588  -8.130 -12.793  1.00 55.08           N  
ANISOU 2079  NH2 ARG A1154     6670   7734   6524   -793    568    133       N  
ATOM   2080  N   THR A1155     -21.013  -7.308  -5.481  1.00 42.38           N  
ANISOU 2080  N   THR A1155     4785   6508   4809   -499    561     57       N  
ATOM   2081  CA  THR A1155     -20.895  -8.535  -4.704  1.00 44.13           C  
ANISOU 2081  CA  THR A1155     5032   6694   5041   -507    577     74       C  
ATOM   2082  C   THR A1155     -21.125  -8.315  -3.212  1.00 44.96           C  
ANISOU 2082  C   THR A1155     5077   6895   5111   -439    558     56       C  
ATOM   2083  O   THR A1155     -21.622  -9.200  -2.515  1.00 47.05           O  
ANISOU 2083  O   THR A1155     5343   7183   5352   -444    556     65       O  
ATOM   2084  CB  THR A1155     -19.508  -9.173  -4.896  1.00 44.20           C  
ANISOU 2084  CB  THR A1155     5105   6559   5129   -530    617     87       C  
ATOM   2085  OG1 THR A1155     -18.495  -8.227  -4.533  1.00 44.23           O  
ANISOU 2085  OG1 THR A1155     5085   6554   5165   -493    622     62       O  
ATOM   2086  CG2 THR A1155     -19.308  -9.587  -6.346  1.00 43.80           C  
ANISOU 2086  CG2 THR A1155     5121   6402   5118   -588    631    109       C  
ATOM   2087  N   GLY A1156     -20.762  -7.134  -2.726  1.00 42.50           N  
ANISOU 2087  N   GLY A1156     4716   6637   4796   -372    542     27       N  
ATOM   2088  CA  GLY A1156     -20.815  -6.859  -1.304  1.00 40.53           C  
ANISOU 2088  CA  GLY A1156     4417   6461   4523   -295    522      8       C  
ATOM   2089  C   GLY A1156     -19.632  -7.503  -0.608  1.00 39.39           C  
ANISOU 2089  C   GLY A1156     4303   6231   4431   -299    552     12       C  
ATOM   2090  O   GLY A1156     -19.691  -7.824   0.579  1.00 39.07           O  
ANISOU 2090  O   GLY A1156     4243   6226   4377   -263    544      7       O  
ATOM   2091  N   THR A1157     -18.556  -7.701  -1.365  1.00 38.95           N  
ANISOU 2091  N   THR A1157     4297   6062   4439   -343    586     21       N  
ATOM   2092  CA  THR A1157     -17.328  -8.288  -0.843  1.00 37.47           C  
ANISOU 2092  CA  THR A1157     4140   5788   4310   -347    617     28       C  
ATOM   2093  C   THR A1157     -16.141  -7.381  -1.138  1.00 37.38           C  
ANISOU 2093  C   THR A1157     4124   5728   4351   -330    627      7       C  
ATOM   2094  O   THR A1157     -16.299  -6.311  -1.724  1.00 38.97           O  
ANISOU 2094  O   THR A1157     4302   5964   4542   -313    611    -16       O  
ATOM   2095  CB  THR A1157     -17.046  -9.667  -1.468  1.00 35.45           C  
ANISOU 2095  CB  THR A1157     3959   5419   4090   -415    653     66       C  
ATOM   2096  OG1 THR A1157     -16.711  -9.507  -2.853  1.00 33.05           O  
ANISOU 2096  OG1 THR A1157     3699   5036   3825   -461    667     77       O  
ATOM   2097  CG2 THR A1157     -18.257 -10.580  -1.340  1.00 34.78           C  
ANISOU 2097  CG2 THR A1157     3883   5377   3953   -437    643     81       C  
ATOM   2098  N   TRP A1158     -14.950  -7.816  -0.738  1.00 36.90           N  
ANISOU 2098  N   TRP A1158     4084   5589   4347   -334    655     14       N  
ATOM   2099  CA  TRP A1158     -13.738  -7.043  -0.979  1.00 37.58           C  
ANISOU 2099  CA  TRP A1158     4170   5618   4492   -323    664     -9       C  
ATOM   2100  C   TRP A1158     -12.878  -7.683  -2.061  1.00 37.91           C  
ANISOU 2100  C   TRP A1158     4282   5520   4600   -397    704     18       C  
ATOM   2101  O   TRP A1158     -11.654  -7.587  -2.019  1.00 38.25           O  
ANISOU 2101  O   TRP A1158     4340   5486   4707   -401    724     10       O  
ATOM   2102  CB  TRP A1158     -12.919  -6.912   0.305  1.00 37.72           C  
ANISOU 2102  CB  TRP A1158     4171   5620   4540   -254    643    -22       C  
ATOM   2103  CG  TRP A1158     -13.669  -6.311   1.446  1.00 38.68           C  
ANISOU 2103  CG  TRP A1158     4242   5845   4608   -168    592    -44       C  
ATOM   2104  CD1 TRP A1158     -14.350  -6.980   2.421  1.00 39.43           C  
ANISOU 2104  CD1 TRP A1158     4299   6037   4648   -159    603    -33       C  
ATOM   2105  CD2 TRP A1158     -13.814  -4.917   1.741  1.00 38.73           C  
ANISOU 2105  CD2 TRP A1158     4237   5867   4610    -80    524    -81       C  
ATOM   2106  NE1 TRP A1158     -14.910  -6.090   3.304  1.00 40.35           N  
ANISOU 2106  NE1 TRP A1158     4378   6226   4728    -71    547    -60       N  
ATOM   2107  CE2 TRP A1158     -14.596  -4.815   2.907  1.00 39.56           C  
ANISOU 2107  CE2 TRP A1158     4295   6078   4658    -19    499    -89       C  
ATOM   2108  CE3 TRP A1158     -13.358  -3.744   1.129  1.00 37.14           C  
ANISOU 2108  CE3 TRP A1158     4067   5598   4445    -47    485   -109       C  
ATOM   2109  CZ2 TRP A1158     -14.934  -3.590   3.476  1.00 38.84           C  
ANISOU 2109  CZ2 TRP A1158     4187   6026   4544     74    438   -120       C  
ATOM   2110  CZ3 TRP A1158     -13.695  -2.528   1.695  1.00 37.14           C  
ANISOU 2110  CZ3 TRP A1158     4053   5638   4419     46    424   -142       C  
ATOM   2111  CH2 TRP A1158     -14.474  -2.460   2.856  1.00 37.91           C  
ANISOU 2111  CH2 TRP A1158     4104   5840   4459    106    402   -145       C  
ATOM   2112  N   ASP A1159     -13.517  -8.336  -3.025  1.00 38.64           N  
ANISOU 2112  N   ASP A1159     4423   5576   4683   -446    707     49       N  
ATOM   2113  CA  ASP A1159     -12.792  -9.031  -4.085  1.00 40.51           C  
ANISOU 2113  CA  ASP A1159     4731   5682   4980   -493    726     84       C  
ATOM   2114  C   ASP A1159     -11.970  -8.080  -4.953  1.00 37.22           C  
ANISOU 2114  C   ASP A1159     4333   5193   4614   -515    727     57       C  
ATOM   2115  O   ASP A1159     -10.908  -8.449  -5.450  1.00 38.30           O  
ANISOU 2115  O   ASP A1159     4518   5223   4813   -532    734     74       O  
ATOM   2116  CB  ASP A1159     -13.755  -9.842  -4.957  1.00 45.75           C  
ANISOU 2116  CB  ASP A1159     5432   6334   5616   -526    719    117       C  
ATOM   2117  CG  ASP A1159     -14.373 -11.009  -4.211  1.00 48.31           C  
ANISOU 2117  CG  ASP A1159     5758   6691   5906   -514    725    141       C  
ATOM   2118  OD1 ASP A1159     -14.452 -10.944  -2.966  1.00 48.48           O  
ANISOU 2118  OD1 ASP A1159     5740   6778   5903   -480    725    125       O  
ATOM   2119  OD2 ASP A1159     -14.781 -11.990  -4.869  1.00 48.72           O  
ANISOU 2119  OD2 ASP A1159     5851   6705   5957   -536    726    172       O  
ATOM   2120  N   ALA A1160     -12.460  -6.857  -5.125  1.00 35.23           N  
ANISOU 2120  N   ALA A1160     4046   5007   4333   -508    715     11       N  
ATOM   2121  CA  ALA A1160     -11.770  -5.871  -5.951  1.00 35.66           C  
ANISOU 2121  CA  ALA A1160     4132   4977   4440   -518    706    -23       C  
ATOM   2122  C   ALA A1160     -10.472  -5.389  -5.309  1.00 38.23           C  
ANISOU 2122  C   ALA A1160     4465   5228   4833   -460    685    -47       C  
ATOM   2123  O   ALA A1160      -9.586  -4.872  -5.989  1.00 38.37           O  
ANISOU 2123  O   ALA A1160     4527   5140   4913   -471    680    -66       O  
ATOM   2124  CB  ALA A1160     -12.684  -4.693  -6.247  1.00 34.90           C  
ANISOU 2124  CB  ALA A1160     4022   4939   4301   -468    643    -55       C  
ATOM   2125  N   TYR A1161     -10.364  -5.560  -3.996  1.00 39.50           N  
ANISOU 2125  N   TYR A1161     4583   5445   4980   -399    672    -46       N  
ATOM   2126  CA  TYR A1161      -9.190  -5.115  -3.258  1.00 38.94           C  
ANISOU 2126  CA  TYR A1161     4513   5318   4965   -342    648    -65       C  
ATOM   2127  C   TYR A1161      -8.416  -6.317  -2.740  1.00 45.53           C  
ANISOU 2127  C   TYR A1161     5345   6122   5833   -374    703    -30       C  
ATOM   2128  O   TYR A1161      -9.001  -7.357  -2.450  1.00 45.62           O  
ANISOU 2128  O   TYR A1161     5339   6193   5801   -408    744      3       O  
ATOM   2129  CB  TYR A1161      -9.609  -4.220  -2.090  1.00 32.78           C  
ANISOU 2129  CB  TYR A1161     3691   4621   4145   -240    582    -94       C  
ATOM   2130  CG  TYR A1161     -10.387  -2.997  -2.513  1.00 28.09           C  
ANISOU 2130  CG  TYR A1161     3100   4061   3513   -197    527   -129       C  
ATOM   2131  CD1 TYR A1161      -9.739  -1.798  -2.772  1.00 26.23           C  
ANISOU 2131  CD1 TYR A1161     2898   3758   3311   -155    482   -168       C  
ATOM   2132  CD2 TYR A1161     -11.768  -3.042  -2.661  1.00 26.93           C  
ANISOU 2132  CD2 TYR A1161     2924   4015   3292   -198    520   -122       C  
ATOM   2133  CE1 TYR A1161     -10.441  -0.677  -3.162  1.00 24.98           C  
ANISOU 2133  CE1 TYR A1161     2749   3627   3113   -112    433   -199       C  
ATOM   2134  CE2 TYR A1161     -12.481  -1.925  -3.054  1.00 25.49           C  
ANISOU 2134  CE2 TYR A1161     2745   3866   3075   -152    470   -151       C  
ATOM   2135  CZ  TYR A1161     -11.811  -0.745  -3.303  1.00 24.63           C  
ANISOU 2135  CZ  TYR A1161     2674   3683   2999   -108    427   -190       C  
ATOM   2136  OH  TYR A1161     -12.508   0.376  -3.692  1.00 22.99           O  
ANISOU 2136  OH  TYR A1161     2477   3506   2754    -59    379   -220       O  
ATOM   2137  N   LYS A1162      -7.098  -6.182  -2.630  1.00 51.68           N  
ANISOU 2137  N   LYS A1162     6143   6810   6685   -363    706    -35       N  
ATOM   2138  CA  LYS A1162      -6.292  -7.257  -2.066  1.00 57.67           C  
ANISOU 2138  CA  LYS A1162     6896   7539   7475   -381    755     -1       C  
ATOM   2139  C   LYS A1162      -6.609  -7.404  -0.585  1.00 60.23           C  
ANISOU 2139  C   LYS A1162     7170   7957   7759   -316    728      0       C  
ATOM   2140  O   LYS A1162      -6.517  -8.499  -0.032  1.00 61.67           O  
ANISOU 2140  O   LYS A1162     7341   8158   7932   -336    772     32       O  
ATOM   2141  CB  LYS A1162      -4.799  -7.003  -2.279  1.00 61.26           C  
ANISOU 2141  CB  LYS A1162     7376   7880   8018   -380    759     -8       C  
ATOM   2142  CG  LYS A1162      -4.356  -7.123  -3.730  1.00 64.46           C  
ANISOU 2142  CG  LYS A1162     7842   8183   8465   -449    786     -1       C  
ATOM   2143  CD  LYS A1162      -2.847  -6.981  -3.873  1.00 66.82           C  
ANISOU 2143  CD  LYS A1162     8166   8377   8844   -442    785     -6       C  
ATOM   2144  CE  LYS A1162      -2.362  -5.617  -3.398  1.00 68.37           C  
ANISOU 2144  CE  LYS A1162     8342   8565   9070   -384    736    -53       C  
ATOM   2145  NZ  LYS A1162      -3.014  -4.491  -4.126  1.00 68.45           N  
ANISOU 2145  NZ  LYS A1162     8378   8578   9053   -377    690    -94       N  
ATOM   2146  N   ILE A 680      -6.985  -6.284   0.032  1.00 61.35           N  
ANISOU 2146  N   ILE A 680     7286   8151   7873   -240    659    -36       N  
ATOM   2147  CA  ILE A 680      -7.493  -6.226   1.406  1.00 63.14           C  
ANISOU 2147  CA  ILE A 680     7466   8473   8051   -175    625    -41       C  
ATOM   2148  C   ILE A 680      -6.803  -7.173   2.390  1.00 64.13           C  
ANISOU 2148  C   ILE A 680     7576   8594   8197   -171    654    -14       C  
ATOM   2149  O   ILE A 680      -6.378  -6.760   3.468  1.00 64.62           O  
ANISOU 2149  O   ILE A 680     7616   8671   8267   -108    615    -27       O  
ATOM   2150  CB  ILE A 680      -9.025  -6.453   1.453  1.00 62.39           C  
ANISOU 2150  CB  ILE A 680     7345   8489   7870   -180    626    -38       C  
ATOM   2151  CG1 ILE A 680      -9.608  -5.910   2.759  1.00 62.20           C  
ANISOU 2151  CG1 ILE A 680     7277   8558   7797    -97    574    -57       C  
ATOM   2152  CG2 ILE A 680      -9.372  -7.924   1.262  1.00 62.43           C  
ANISOU 2152  CG2 ILE A 680     7354   8516   7852   -256    697      4       C  
ATOM   2153  CD1 ILE A 680      -9.620  -4.399   2.833  1.00 61.88           C  
ANISOU 2153  CD1 ILE A 680     7239   8516   7756    -25    505    -98       C  
ATOM   2154  N   SER A 689     -12.942 -15.741  19.691  1.00 50.35           N  
ANISOU 2154  N   SER A 689     5679   7628   5823     46    599    -27       N  
ATOM   2155  CA  SER A 689     -13.250 -17.152  19.891  1.00 53.21           C  
ANISOU 2155  CA  SER A 689     6097   7961   6159     -7    630    -18       C  
ATOM   2156  C   SER A 689     -14.159 -17.345  21.096  1.00 56.38           C  
ANISOU 2156  C   SER A 689     6496   8423   6504      3    604    -44       C  
ATOM   2157  O   SER A 689     -14.014 -16.660  22.107  1.00 58.18           O  
ANISOU 2157  O   SER A 689     6685   8695   6724     54    574    -62       O  
ATOM   2158  CB  SER A 689     -11.968 -17.964  20.072  1.00 53.57           C  
ANISOU 2158  CB  SER A 689     6170   7939   6244    -16    670      7       C  
ATOM   2159  OG  SER A 689     -12.266 -19.333  20.287  1.00 54.10           O  
ANISOU 2159  OG  SER A 689     6299   7972   6283    -62    700     14       O  
ATOM   2160  N   ALA A 690     -15.090 -18.287  20.986  1.00 56.70           N  
ANISOU 2160  N   ALA A 690     7563   6678   7304    183    207    -27       N  
ATOM   2161  CA  ALA A 690     -16.085 -18.508  22.030  1.00 55.07           C  
ANISOU 2161  CA  ALA A 690     7364   6429   7130    128    186    -44       C  
ATOM   2162  C   ALA A 690     -15.504 -19.207  23.256  1.00 54.06           C  
ANISOU 2162  C   ALA A 690     7239   6259   7041    112    191    -21       C  
ATOM   2163  O   ALA A 690     -15.782 -18.816  24.390  1.00 53.19           O  
ANISOU 2163  O   ALA A 690     7119   6134   6956     69    183      2       O  
ATOM   2164  CB  ALA A 690     -17.263 -19.293  21.478  1.00 54.82           C  
ANISOU 2164  CB  ALA A 690     7359   6375   7093    124    166   -109       C  
HETATM 2165  N   YCM A 691     -14.704 -20.244  23.023  1.00 53.80           N  
ANISOU 2165  N   YCM A 691     7222   6209   7012    148    203    -27       N  
HETATM 2166  CA  YCM A 691     -14.082 -20.981  24.101  1.00 51.80           C  
ANISOU 2166  CA  YCM A 691     6972   5916   6793    138    208     -5       C  
HETATM 2167  CB  YCM A 691     -13.430 -22.288  23.641  1.00 51.71           C  
ANISOU 2167  CB  YCM A 691     6983   5880   6784    182    217    -27       C  
HETATM 2168  SG  YCM A 691     -12.236 -23.009  24.733  1.00114.88           S  
ANISOU 2168  SG  YCM A 691    14982  13849  14820    187    231     15       S  
HETATM 2169  CD  YCM A 691     -13.102 -24.273  25.609  1.00 80.68           C  
ANISOU 2169  CD  YCM A 691    10677   9446  10531    150    212    -15       C  
HETATM 2170  CE  YCM A 691     -13.053 -24.134  27.117  1.00 79.93           C  
ANISOU 2170  CE  YCM A 691    10570   9331  10469    107    210     28       C  
HETATM 2171  OZ1 YCM A 691     -12.062 -24.537  27.766  1.00 79.79           O  
ANISOU 2171  OZ1 YCM A 691    10548   9299  10468    119    221     62       O  
HETATM 2172  NZ2 YCM A 691     -14.117 -23.564  27.763  1.00 79.14           N  
ANISOU 2172  NZ2 YCM A 691    10463   9231  10377     57    195     28       N  
HETATM 2173  C   YCM A 691     -13.100 -20.132  24.905  1.00 49.91           C  
ANISOU 2173  C   YCM A 691     6703   5696   6563    130    220     59       C  
HETATM 2174  O   YCM A 691     -12.917 -20.256  26.119  1.00 49.93           O  
ANISOU 2174  O   YCM A 691     6701   5673   6595    102    217     85       O  
ATOM   2175  N   ALA A 692     -12.452 -19.225  24.183  1.00 47.89           N  
ANISOU 2175  N   ALA A 692     6426   5489   6283    158    233     86       N  
ATOM   2176  CA  ALA A 692     -11.499 -18.296  24.775  1.00 44.83           C  
ANISOU 2176  CA  ALA A 692     6006   5122   5905    153    242    146       C  
ATOM   2177  C   ALA A 692     -12.195 -17.304  25.700  1.00 42.96           C  
ANISOU 2177  C   ALA A 692     5755   4884   5684    101    223    161       C  
ATOM   2178  O   ALA A 692     -11.670 -16.952  26.756  1.00 42.53           O  
ANISOU 2178  O   ALA A 692     5685   4822   5653     81    220    199       O  
ATOM   2179  CB  ALA A 692     -10.745 -17.560  23.684  1.00 44.17           C  
ANISOU 2179  CB  ALA A 692     5901   5090   5792    193    259    172       C  
ATOM   2180  N   GLN A 693     -13.379 -16.855  25.294  1.00 41.91           N  
ANISOU 2180  N   GLN A 693     5627   4760   5536     81    209    129       N  
ATOM   2181  CA  GLN A 693     -14.153 -15.895  26.075  1.00 39.49           C  
ANISOU 2181  CA  GLN A 693     5308   4454   5241     36    191    137       C  
ATOM   2182  C   GLN A 693     -14.594 -16.476  27.417  1.00 34.50           C  
ANISOU 2182  C   GLN A 693     4687   3783   4638     -1    180    132       C  
ATOM   2183  O   GLN A 693     -14.612 -15.776  28.429  1.00 30.27           O  
ANISOU 2183  O   GLN A 693     4137   3248   4118    -30    171    158       O  
ATOM   2184  CB  GLN A 693     -15.373 -15.422  25.284  1.00 41.03           C  
ANISOU 2184  CB  GLN A 693     5509   4667   5415     27    179    101       C  
ATOM   2185  CG  GLN A 693     -15.047 -14.494  24.127  1.00 43.61           C  
ANISOU 2185  CG  GLN A 693     5817   5040   5712     56    187    116       C  
ATOM   2186  CD  GLN A 693     -16.254 -14.210  23.255  1.00 46.85           C  
ANISOU 2186  CD  GLN A 693     6236   5466   6097     52    175     76       C  
ATOM   2187  OE1 GLN A 693     -16.411 -14.795  22.182  1.00 49.55           O  
ANISOU 2187  OE1 GLN A 693     6595   5819   6414     84    180     43       O  
ATOM   2188  NE2 GLN A 693     -17.116 -13.310  23.711  1.00 46.00           N  
ANISOU 2188  NE2 GLN A 693     6119   5363   5998     16    157     76       N  
ATOM   2189  N   LEU A 694     -14.950 -17.756  27.417  1.00 33.73           N  
ANISOU 2189  N   LEU A 694     4616   3652   4549      1    181    100       N  
ATOM   2190  CA  LEU A 694     -15.371 -18.430  28.639  1.00 34.08           C  
ANISOU 2190  CA  LEU A 694     4670   3657   4620    -32    173     99       C  
ATOM   2191  C   LEU A 694     -14.208 -18.574  29.615  1.00 32.77           C  
ANISOU 2191  C   LEU A 694     4495   3482   4474    -27    182    144       C  
ATOM   2192  O   LEU A 694     -14.371 -18.388  30.821  1.00 31.85           O  
ANISOU 2192  O   LEU A 694     4372   3356   4374    -57    174    164       O  
ATOM   2193  CB  LEU A 694     -15.971 -19.798  28.315  1.00 36.25           C  
ANISOU 2193  CB  LEU A 694     4974   3895   4905    -29    171     56       C  
ATOM   2194  CG  LEU A 694     -17.178 -19.759  27.376  1.00 39.27           C  
ANISOU 2194  CG  LEU A 694     5367   4283   5271    -35    158      7       C  
ATOM   2195  CD1 LEU A 694     -17.802 -21.138  27.231  1.00 40.31           C  
ANISOU 2195  CD1 LEU A 694     5524   4369   5421    -39    151    -34       C  
ATOM   2196  CD2 LEU A 694     -18.202 -18.748  27.869  1.00 40.09           C  
ANISOU 2196  CD2 LEU A 694     5456   4403   5373    -75    145      9       C  
ATOM   2197  N   VAL A 695     -13.035 -18.904  29.083  1.00 31.35           N  
ANISOU 2197  N   VAL A 695     4312   3309   4290     13    198    161       N  
ATOM   2198  CA  VAL A 695     -11.829 -19.024  29.890  1.00 29.84           C  
ANISOU 2198  CA  VAL A 695     4109   3112   4116     22    206    205       C  
ATOM   2199  C   VAL A 695     -11.441 -17.675  30.495  1.00 29.33           C  
ANISOU 2199  C   VAL A 695     4014   3075   4053      6    198    245       C  
ATOM   2200  O   VAL A 695     -11.123 -17.587  31.681  1.00 28.14           O  
ANISOU 2200  O   VAL A 695     3856   2915   3921    -13    191    271       O  
ATOM   2201  CB  VAL A 695     -10.655 -19.582  29.059  1.00 30.41           C  
ANISOU 2201  CB  VAL A 695     4182   3191   4181     73    226    215       C  
ATOM   2202  CG1 VAL A 695      -9.360 -19.540  29.857  1.00 32.09           C  
ANISOU 2202  CG1 VAL A 695     4376   3404   4412     83    233    265       C  
ATOM   2203  CG2 VAL A 695     -10.961 -21.000  28.604  1.00 29.75           C  
ANISOU 2203  CG2 VAL A 695     4130   3073   4101     91    230    174       C  
ATOM   2204  N   ILE A 696     -11.479 -16.628  29.676  1.00 29.13           N  
ANISOU 2204  N   ILE A 696     3972   3084   4010     13    197    248       N  
ATOM   2205  CA  ILE A 696     -11.153 -15.280  30.132  1.00 29.18           C  
ANISOU 2205  CA  ILE A 696     3949   3114   4022     -3    186    283       C  
ATOM   2206  C   ILE A 696     -12.150 -14.792  31.181  1.00 30.84           C  
ANISOU 2206  C   ILE A 696     4162   3316   4242    -46    164    272       C  
ATOM   2207  O   ILE A 696     -11.767 -14.169  32.173  1.00 32.81           O  
ANISOU 2207  O   ILE A 696     4395   3567   4505    -62    151    300       O  
ATOM   2208  CB  ILE A 696     -11.093 -14.288  28.952  1.00 27.95           C  
ANISOU 2208  CB  ILE A 696     3775   2996   3847     14    189    289       C  
ATOM   2209  CG1 ILE A 696      -9.915 -14.636  28.040  1.00 29.65           C  
ANISOU 2209  CG1 ILE A 696     3982   3228   4054     61    213    311       C  
ATOM   2210  CG2 ILE A 696     -10.965 -12.855  29.453  1.00 25.79           C  
ANISOU 2210  CG2 ILE A 696     3473   2740   3587     -8    172    320       C  
ATOM   2211  CD1 ILE A 696      -9.895 -13.870  26.742  1.00 31.25           C  
ANISOU 2211  CD1 ILE A 696     4169   3470   4232     84    222    317       C  
ATOM   2212  N   ALA A 697     -13.427 -15.087  30.960  1.00 29.08           N  
ANISOU 2212  N   ALA A 697     3957   3083   4008    -63    159    231       N  
ATOM   2213  CA  ALA A 697     -14.462 -14.756  31.931  1.00 26.06           C  
ANISOU 2213  CA  ALA A 697     3577   2693   3631   -101    142    219       C  
ATOM   2214  C   ALA A 697     -14.219 -15.513  33.232  1.00 24.59           C  
ANISOU 2214  C   ALA A 697     3398   2481   3463   -114    141    234       C  
ATOM   2215  O   ALA A 697     -14.321 -14.945  34.317  1.00 22.97           O  
ANISOU 2215  O   ALA A 697     3184   2281   3265   -135    128    249       O  
ATOM   2216  CB  ALA A 697     -15.836 -15.081  31.373  1.00 25.52           C  
ANISOU 2216  CB  ALA A 697     3526   2620   3552   -115    138    174       C  
ATOM   2217  N   PHE A 698     -13.888 -16.795  33.105  1.00 26.21           N  
ANISOU 2217  N   PHE A 698     3621   2661   3676    -98    155    229       N  
ATOM   2218  CA  PHE A 698     -13.568 -17.649  34.247  1.00 30.90           C  
ANISOU 2218  CA  PHE A 698     4223   3229   4288   -106    157    247       C  
ATOM   2219  C   PHE A 698     -12.392 -17.104  35.058  1.00 30.64           C  
ANISOU 2219  C   PHE A 698     4170   3208   4264    -98    153    291       C  
ATOM   2220  O   PHE A 698     -12.414 -17.123  36.289  1.00 29.95           O  
ANISOU 2220  O   PHE A 698     4081   3115   4185   -116    144    308       O  
ATOM   2221  CB  PHE A 698     -13.274 -19.074  33.762  1.00 36.24           C  
ANISOU 2221  CB  PHE A 698     4921   3874   4974    -84    172    235       C  
ATOM   2222  CG  PHE A 698     -12.508 -19.916  34.746  1.00 41.10           C  
ANISOU 2222  CG  PHE A 698     5541   4467   5610    -79    177    264       C  
ATOM   2223  CD1 PHE A 698     -13.163 -20.583  35.768  1.00 42.69           C  
ANISOU 2223  CD1 PHE A 698     5753   4642   5825   -105    173    265       C  
ATOM   2224  CD2 PHE A 698     -11.133 -20.060  34.631  1.00 42.11           C  
ANISOU 2224  CD2 PHE A 698     5660   4597   5742    -47    187    293       C  
ATOM   2225  CE1 PHE A 698     -12.460 -21.366  36.666  1.00 43.72           C  
ANISOU 2225  CE1 PHE A 698     5887   4751   5973    -99    178    295       C  
ATOM   2226  CE2 PHE A 698     -10.424 -20.837  35.526  1.00 43.25           C  
ANISOU 2226  CE2 PHE A 698     5808   4721   5905    -41    191    321       C  
ATOM   2227  CZ  PHE A 698     -11.088 -21.492  36.545  1.00 44.36           C  
ANISOU 2227  CZ  PHE A 698     5960   4835   6058    -67    187    322       C  
ATOM   2228  N   ILE A 699     -11.370 -16.620  34.358  1.00 29.74           N  
ANISOU 2228  N   ILE A 699     4040   3112   4147    -72    159    310       N  
ATOM   2229  CA  ILE A 699     -10.188 -16.058  35.003  1.00 28.35           C  
ANISOU 2229  CA  ILE A 699     3841   2948   3983    -64    153    353       C  
ATOM   2230  C   ILE A 699     -10.525 -14.819  35.830  1.00 29.26           C  
ANISOU 2230  C   ILE A 699     3939   3080   4100    -91    129    361       C  
ATOM   2231  O   ILE A 699     -10.099 -14.694  36.980  1.00 30.60           O  
ANISOU 2231  O   ILE A 699     4101   3246   4279    -99    116    382       O  
ATOM   2232  CB  ILE A 699      -9.099 -15.704  33.969  1.00 26.70           C  
ANISOU 2232  CB  ILE A 699     3613   2759   3774    -32    165    374       C  
ATOM   2233  CG1 ILE A 699      -8.495 -16.979  33.377  1.00 27.33           C  
ANISOU 2233  CG1 ILE A 699     3708   2822   3853      2    188    371       C  
ATOM   2234  CG2 ILE A 699      -8.010 -14.856  34.605  1.00 26.26           C  
ANISOU 2234  CG2 ILE A 699     3527   2716   3733    -30    153    418       C  
ATOM   2235  CD1 ILE A 699      -7.516 -16.728  32.249  1.00 27.68           C  
ANISOU 2235  CD1 ILE A 699     3735   2891   3891     39    205    390       C  
ATOM   2236  N   LEU A 700     -11.301 -13.912  35.243  1.00 27.13           N  
ANISOU 2236  N   LEU A 700     3664   2827   3819   -102    121    341       N  
ATOM   2237  CA  LEU A 700     -11.662 -12.664  35.910  1.00 25.91           C  
ANISOU 2237  CA  LEU A 700     3493   2686   3665   -125     96    344       C  
ATOM   2238  C   LEU A 700     -12.548 -12.899  37.131  1.00 26.52           C  
ANISOU 2238  C   LEU A 700     3583   2754   3739   -150     85    330       C  
ATOM   2239  O   LEU A 700     -12.547 -12.103  38.069  1.00 27.40           O  
ANISOU 2239  O   LEU A 700     3683   2875   3853   -162     63    338       O  
ATOM   2240  CB  LEU A 700     -12.354 -11.713  34.934  1.00 25.80           C  
ANISOU 2240  CB  LEU A 700     3472   2691   3640   -129     91    326       C  
ATOM   2241  CG  LEU A 700     -11.549 -11.257  33.715  1.00 26.76           C  
ANISOU 2241  CG  LEU A 700     3575   2829   3762   -104    101    346       C  
ATOM   2242  CD1 LEU A 700     -12.410 -10.403  32.800  1.00 25.93           C  
ANISOU 2242  CD1 LEU A 700     3466   2742   3643   -110     96    326       C  
ATOM   2243  CD2 LEU A 700     -10.300 -10.498  34.139  1.00 27.33           C  
ANISOU 2243  CD2 LEU A 700     3618   2909   3857    -98     89    389       C  
ATOM   2244  N   ILE A 701     -13.303 -13.993  37.114  1.00 24.85           N  
ANISOU 2244  N   ILE A 701     3394   2525   3521   -156     99    308       N  
ATOM   2245  CA  ILE A 701     -14.153 -14.345  38.245  1.00 24.72           C  
ANISOU 2245  CA  ILE A 701     3389   2502   3503   -179     93    300       C  
ATOM   2246  C   ILE A 701     -13.313 -14.937  39.372  1.00 27.41           C  
ANISOU 2246  C   ILE A 701     3731   2832   3853   -173     93    331       C  
ATOM   2247  O   ILE A 701     -13.552 -14.662  40.548  1.00 29.43           O  
ANISOU 2247  O   ILE A 701     3983   3095   4104   -185     80    338       O  
ATOM   2248  CB  ILE A 701     -15.264 -15.337  37.841  1.00 23.29           C  
ANISOU 2248  CB  ILE A 701     3229   2302   3318   -190    106    270       C  
ATOM   2249  CG1 ILE A 701     -16.190 -14.702  36.802  1.00 22.68           C  
ANISOU 2249  CG1 ILE A 701     3151   2238   3229   -197    103    238       C  
ATOM   2250  CG2 ILE A 701     -16.065 -15.778  39.060  1.00 20.16           C  
ANISOU 2250  CG2 ILE A 701     2839   1898   2921   -212    104    271       C  
ATOM   2251  CD1 ILE A 701     -17.247 -15.639  36.265  1.00 22.68           C  
ANISOU 2251  CD1 ILE A 701     3169   2220   3229   -207    112    206       C  
ATOM   2252  N   CYS A 702     -12.320 -15.740  39.005  1.00 26.18           N  
ANISOU 2252  N   CYS A 702     3578   2660   3708   -150    108    348       N  
ATOM   2253  CA  CYS A 702     -11.435 -16.352  39.991  1.00 24.83           C  
ANISOU 2253  CA  CYS A 702     3406   2479   3547   -141    108    380       C  
ATOM   2254  C   CYS A 702     -10.550 -15.323  40.688  1.00 23.91           C  
ANISOU 2254  C   CYS A 702     3266   2383   3434   -137     87    406       C  
ATOM   2255  O   CYS A 702     -10.109 -15.541  41.815  1.00 23.87           O  
ANISOU 2255  O   CYS A 702     3260   2377   3432   -137     79    427       O  
ATOM   2256  CB  CYS A 702     -10.578 -17.446  39.351  1.00 24.44           C  
ANISOU 2256  CB  CYS A 702     3366   2409   3511   -115    129    391       C  
ATOM   2257  SG  CYS A 702     -11.495 -18.936  38.910  1.00 58.86           S  
ANISOU 2257  SG  CYS A 702     7755   6733   7875   -120    148    363       S  
ATOM   2258  N   ILE A 703     -10.291 -14.205  40.017  1.00 23.74           N  
ANISOU 2258  N   ILE A 703     3227   2379   3414   -135     76    404       N  
ATOM   2259  CA  ILE A 703      -9.516 -13.125  40.621  1.00 24.86           C  
ANISOU 2259  CA  ILE A 703     3344   2536   3564   -134     51    426       C  
ATOM   2260  C   ILE A 703     -10.285 -12.513  41.787  1.00 24.75           C  
ANISOU 2260  C   ILE A 703     3332   2534   3539   -154     27    413       C  
ATOM   2261  O   ILE A 703      -9.717 -12.243  42.845  1.00 26.55           O  
ANISOU 2261  O   ILE A 703     3550   2767   3769   -152      7    430       O  
ATOM   2262  CB  ILE A 703      -9.155 -12.032  39.594  1.00 23.01           C  
ANISOU 2262  CB  ILE A 703     3088   2316   3338   -128     44    430       C  
ATOM   2263  CG1 ILE A 703      -8.184 -12.583  38.549  1.00 23.72           C  
ANISOU 2263  CG1 ILE A 703     3172   2403   3439   -102     68    450       C  
ATOM   2264  CG2 ILE A 703      -8.539 -10.827  40.285  1.00 20.63           C  
ANISOU 2264  CG2 ILE A 703     2760   2026   3051   -133     11    448       C  
ATOM   2265  CD1 ILE A 703      -7.737 -11.559  37.527  1.00 24.20           C  
ANISOU 2265  CD1 ILE A 703     3208   2481   3508    -94     65    462       C  
ATOM   2266  N   GLN A 704     -11.582 -12.310  41.591  1.00 23.90           N  
ANISOU 2266  N   GLN A 704     3235   2430   3416   -171     29    382       N  
ATOM   2267  CA  GLN A 704     -12.441 -11.794  42.648  1.00 24.72           C  
ANISOU 2267  CA  GLN A 704     3340   2546   3504   -187     10    367       C  
ATOM   2268  C   GLN A 704     -12.564 -12.811  43.778  1.00 24.47           C  
ANISOU 2268  C   GLN A 704     3324   2511   3465   -188     18    378       C  
ATOM   2269  O   GLN A 704     -12.646 -12.443  44.949  1.00 24.62           O  
ANISOU 2269  O   GLN A 704     3340   2544   3472   -190      0    382       O  
ATOM   2270  CB  GLN A 704     -13.827 -11.448  42.096  1.00 26.07           C  
ANISOU 2270  CB  GLN A 704     3519   2725   3663   -203     14    332       C  
ATOM   2271  CG  GLN A 704     -14.803 -10.898  43.132  1.00 26.16           C  
ANISOU 2271  CG  GLN A 704     3531   2753   3656   -217     -3    315       C  
ATOM   2272  CD  GLN A 704     -14.422  -9.515  43.630  1.00 25.24           C  
ANISOU 2272  CD  GLN A 704     3397   2652   3542   -214    -37    314       C  
ATOM   2273  OE1 GLN A 704     -13.437  -9.346  44.349  1.00 24.96           O  
ANISOU 2273  OE1 GLN A 704     3351   2617   3513   -204    -54    335       O  
ATOM   2274  NE2 GLN A 704     -15.206  -8.515  43.244  1.00 23.48           N  
ANISOU 2274  NE2 GLN A 704     3167   2440   3315   -223    -51    289       N  
ATOM   2275  N   LEU A 705     -12.570 -14.090  43.416  1.00 24.64           N  
ANISOU 2275  N   LEU A 705     3360   2510   3491   -184     45    384       N  
ATOM   2276  CA  LEU A 705     -12.660 -15.164  44.398  1.00 29.05           C  
ANISOU 2276  CA  LEU A 705     3931   3060   4046   -185     55    401       C  
ATOM   2277  C   LEU A 705     -11.397 -15.240  45.249  1.00 31.15           C  
ANISOU 2277  C   LEU A 705     4189   3329   4318   -168     44    434       C  
ATOM   2278  O   LEU A 705     -11.465 -15.483  46.454  1.00 32.80           O  
ANISOU 2278  O   LEU A 705     4401   3547   4516   -169     38    448       O  
ATOM   2279  CB  LEU A 705     -12.906 -16.507  43.709  1.00 30.91           C  
ANISOU 2279  CB  LEU A 705     4186   3266   4294   -185     83    399       C  
ATOM   2280  CG  LEU A 705     -13.027 -17.717  44.639  1.00 31.79           C  
ANISOU 2280  CG  LEU A 705     4310   3362   4408   -187     96    420       C  
ATOM   2281  CD1 LEU A 705     -14.135 -17.500  45.656  1.00 31.34           C  
ANISOU 2281  CD1 LEU A 705     4253   3323   4331   -206     91    415       C  
ATOM   2282  CD2 LEU A 705     -13.272 -18.989  43.843  1.00 32.71           C  
ANISOU 2282  CD2 LEU A 705     4444   3443   4543   -187    119    413       C  
ATOM   2283  N   GLY A 706     -10.248 -15.032  44.614  1.00 29.54           N  
ANISOU 2283  N   GLY A 706     3972   3119   4131   -152     42    449       N  
ATOM   2284  CA  GLY A 706      -8.978 -15.024  45.314  1.00 28.25           C  
ANISOU 2284  CA  GLY A 706     3797   2960   3978   -135     29    481       C  
ATOM   2285  C   GLY A 706      -8.922 -13.901  46.330  1.00 28.04           C  
ANISOU 2285  C   GLY A 706     3757   2958   3941   -140     -6    479       C  
ATOM   2286  O   GLY A 706      -8.370 -14.061  47.419  1.00 27.53           O  
ANISOU 2286  O   GLY A 706     3689   2899   3871   -131    -20    499       O  
ATOM   2287  N   ILE A 707      -9.502 -12.762  45.965  1.00 26.67           N  
ANISOU 2287  N   ILE A 707     3575   2797   3763   -151    -22    454       N  
ATOM   2288  CA  ILE A 707      -9.598 -11.616  46.862  1.00 25.44           C  
ANISOU 2288  CA  ILE A 707     3407   2661   3598   -155    -58    444       C  
ATOM   2289  C   ILE A 707     -10.475 -11.953  48.061  1.00 25.84           C  
ANISOU 2289  C   ILE A 707     3473   2727   3619   -160    -59    436       C  
ATOM   2290  O   ILE A 707     -10.128 -11.654  49.204  1.00 25.71           O  
ANISOU 2290  O   ILE A 707     3452   2727   3591   -151    -83    443       O  
ATOM   2291  CB  ILE A 707     -10.187 -10.388  46.138  1.00 22.86           C  
ANISOU 2291  CB  ILE A 707     3070   2341   3274   -166    -73    417       C  
ATOM   2292  CG1 ILE A 707      -9.263  -9.947  45.002  1.00 20.87           C  
ANISOU 2292  CG1 ILE A 707     2799   2079   3051   -160    -73    432       C  
ATOM   2293  CG2 ILE A 707     -10.416  -9.243  47.115  1.00 23.09           C  
ANISOU 2293  CG2 ILE A 707     3091   2389   3293   -169   -112    400       C  
ATOM   2294  CD1 ILE A 707      -9.784  -8.767  44.214  1.00 20.84           C  
ANISOU 2294  CD1 ILE A 707     2784   2080   3053   -170    -86    411       C  
ATOM   2295  N   ILE A 708     -11.612 -12.586  47.790  1.00 25.33           N  
ANISOU 2295  N   ILE A 708     3425   2658   3542   -172    -33    422       N  
ATOM   2296  CA  ILE A 708     -12.557 -12.943  48.838  1.00 25.28           C  
ANISOU 2296  CA  ILE A 708     3429   2667   3507   -178    -28    418       C  
ATOM   2297  C   ILE A 708     -11.972 -13.988  49.783  1.00 25.43           C  
ANISOU 2297  C   ILE A 708     3456   2685   3523   -166    -20    452       C  
ATOM   2298  O   ILE A 708     -12.062 -13.852  51.003  1.00 22.99           O  
ANISOU 2298  O   ILE A 708     3147   2399   3190   -159    -33    459       O  
ATOM   2299  CB  ILE A 708     -13.877 -13.463  48.242  1.00 22.53           C  
ANISOU 2299  CB  ILE A 708     3094   2312   3155   -196     -1    399       C  
ATOM   2300  CG1 ILE A 708     -14.598 -12.341  47.498  1.00 24.48           C  
ANISOU 2300  CG1 ILE A 708     3333   2567   3399   -207    -13    364       C  
ATOM   2301  CG2 ILE A 708     -14.773 -14.026  49.332  1.00 19.49           C  
ANISOU 2301  CG2 ILE A 708     2717   1942   2745   -201      9    405       C  
ATOM   2302  CD1 ILE A 708     -15.911 -12.767  46.876  1.00 25.11           C  
ANISOU 2302  CD1 ILE A 708     3423   2642   3476   -225      9    343       C  
ATOM   2303  N   VAL A 709     -11.369 -15.025  49.211  1.00 25.31           N  
ANISOU 2303  N   VAL A 709     3447   2642   3529   -161      3    473       N  
ATOM   2304  CA  VAL A 709     -10.758 -16.088  50.002  1.00 26.24           C  
ANISOU 2304  CA  VAL A 709     3571   2753   3647   -149     13    508       C  
ATOM   2305  C   VAL A 709      -9.621 -15.544  50.866  1.00 26.27           C  
ANISOU 2305  C   VAL A 709     3561   2774   3648   -130    -17    526       C  
ATOM   2306  O   VAL A 709      -9.473 -15.926  52.028  1.00 26.76           O  
ANISOU 2306  O   VAL A 709     3626   2850   3691   -121    -22    547       O  
ATOM   2307  CB  VAL A 709     -10.244 -17.233  49.102  1.00 27.19           C  
ANISOU 2307  CB  VAL A 709     3699   2836   3795   -144     40    524       C  
ATOM   2308  CG1 VAL A 709      -9.336 -18.170  49.880  1.00 29.11           C  
ANISOU 2308  CG1 VAL A 709     3946   3071   4044   -126     44    563       C  
ATOM   2309  CG2 VAL A 709     -11.413 -17.998  48.500  1.00 26.26           C  
ANISOU 2309  CG2 VAL A 709     3597   2699   3680   -161     67    508       C  
ATOM   2310  N   ALA A 710      -8.831 -14.639  50.297  1.00 24.70           N  
ANISOU 2310  N   ALA A 710     3345   2574   3465   -125    -38    519       N  
ATOM   2311  CA  ALA A 710      -7.744 -14.006  51.034  1.00 25.36           C  
ANISOU 2311  CA  ALA A 710     3412   2672   3552   -110    -72    533       C  
ATOM   2312  C   ALA A 710      -8.281 -13.240  52.236  1.00 27.57           C  
ANISOU 2312  C   ALA A 710     3692   2983   3799   -109   -101    517       C  
ATOM   2313  O   ALA A 710      -7.712 -13.296  53.326  1.00 29.07           O  
ANISOU 2313  O   ALA A 710     3880   3190   3977    -94   -121    533       O  
ATOM   2314  CB  ALA A 710      -6.954 -13.077  50.124  1.00 23.04           C  
ANISOU 2314  CB  ALA A 710     3098   2371   3287   -110    -90    529       C  
ATOM   2315  N   LEU A 711      -9.385 -12.530  52.034  1.00 25.89           N  
ANISOU 2315  N   LEU A 711     3482   2782   3573   -123   -105    484       N  
ATOM   2316  CA  LEU A 711      -9.979 -11.738  53.103  1.00 25.29           C  
ANISOU 2316  CA  LEU A 711     3406   2737   3464   -119   -132    462       C  
ATOM   2317  C   LEU A 711     -10.706 -12.604  54.130  1.00 26.30           C  
ANISOU 2317  C   LEU A 711     3550   2886   3558   -114   -112    475       C  
ATOM   2318  O   LEU A 711     -11.019 -12.141  55.223  1.00 26.84           O  
ANISOU 2318  O   LEU A 711     3619   2987   3593   -103   -133    466       O  
ATOM   2319  CB  LEU A 711     -10.910 -10.670  52.532  1.00 23.10           C  
ANISOU 2319  CB  LEU A 711     3125   2465   3185   -133   -142    423       C  
ATOM   2320  CG  LEU A 711     -10.208  -9.475  51.886  1.00 22.74           C  
ANISOU 2320  CG  LEU A 711     3061   2410   3170   -134   -174    410       C  
ATOM   2321  CD1 LEU A 711     -11.217  -8.575  51.197  1.00 21.46           C  
ANISOU 2321  CD1 LEU A 711     2898   2249   3008   -148   -178    375       C  
ATOM   2322  CD2 LEU A 711      -9.414  -8.695  52.926  1.00 23.99           C  
ANISOU 2322  CD2 LEU A 711     3207   2583   3325   -118   -222    408       C  
ATOM   2323  N   PHE A 712     -10.978 -13.856  53.774  1.00 26.84           N  
ANISOU 2323  N   PHE A 712     3629   2934   3633   -122    -73    498       N  
ATOM   2324  CA  PHE A 712     -11.530 -14.811  54.728  1.00 28.32           C  
ANISOU 2324  CA  PHE A 712     3829   3137   3795   -118    -52    521       C  
ATOM   2325  C   PHE A 712     -10.427 -15.225  55.688  1.00 33.09           C  
ANISOU 2325  C   PHE A 712     4430   3749   4393    -96    -65    555       C  
ATOM   2326  O   PHE A 712     -10.673 -15.518  56.858  1.00 35.05           O  
ANISOU 2326  O   PHE A 712     4683   4027   4609    -83    -66    572       O  
ATOM   2327  CB  PHE A 712     -12.066 -16.051  54.014  1.00 27.75           C  
ANISOU 2327  CB  PHE A 712     3768   3033   3742   -134    -10    536       C  
ATOM   2328  CG  PHE A 712     -13.450 -15.887  53.458  1.00 28.77           C  
ANISOU 2328  CG  PHE A 712     3902   3164   3868   -156      7    509       C  
ATOM   2329  CD1 PHE A 712     -14.328 -14.962  53.998  1.00 29.60           C  
ANISOU 2329  CD1 PHE A 712     4002   3304   3942   -157     -8    483       C  
ATOM   2330  CD2 PHE A 712     -13.876 -16.669  52.397  1.00 28.12           C  
ANISOU 2330  CD2 PHE A 712     3826   3046   3811   -173     35    507       C  
ATOM   2331  CE1 PHE A 712     -15.602 -14.817  53.485  1.00 29.92           C  
ANISOU 2331  CE1 PHE A 712     4043   3345   3978   -177      7    459       C  
ATOM   2332  CE2 PHE A 712     -15.147 -16.528  51.881  1.00 27.95           C  
ANISOU 2332  CE2 PHE A 712     3807   3025   3787   -194     47    481       C  
ATOM   2333  CZ  PHE A 712     -16.012 -15.601  52.425  1.00 28.75           C  
ANISOU 2333  CZ  PHE A 712     3902   3163   3858   -196     34    459       C  
ATOM   2334  N   ILE A 713      -9.204 -15.248  55.172  1.00 33.24           N  
ANISOU 2334  N   ILE A 713     4441   3746   4443    -89    -75    567       N  
ATOM   2335  CA  ILE A 713      -8.039 -15.655  55.941  1.00 31.92           C  
ANISOU 2335  CA  ILE A 713     4270   3583   4276    -67    -89    600       C  
ATOM   2336  C   ILE A 713      -7.501 -14.495  56.772  1.00 33.02           C  
ANISOU 2336  C   ILE A 713     4395   3752   4398    -52   -137    585       C  
ATOM   2337  O   ILE A 713      -7.169 -14.664  57.945  1.00 36.68           O  
ANISOU 2337  O   ILE A 713     4860   4241   4835    -32   -153    602       O  
ATOM   2338  CB  ILE A 713      -6.932 -16.182  55.013  1.00 31.53           C  
ANISOU 2338  CB  ILE A 713     4214   3498   4269    -64    -79    620       C  
ATOM   2339  CG1 ILE A 713      -7.450 -17.369  54.197  1.00 31.16           C  
ANISOU 2339  CG1 ILE A 713     4182   3418   4239    -76    -34    631       C  
ATOM   2340  CG2 ILE A 713      -5.704 -16.571  55.813  1.00 30.50           C  
ANISOU 2340  CG2 ILE A 713     4077   3373   4141    -41    -94    655       C  
ATOM   2341  CD1 ILE A 713      -6.528 -17.795  53.077  1.00 31.58           C  
ANISOU 2341  CD1 ILE A 713     4230   3437   4332    -72    -21    641       C  
ATOM   2342  N   MET A 714      -7.420 -13.318  56.158  1.00 30.62           N  
ANISOU 2342  N   MET A 714     4079   3444   4110    -60   -163    552       N  
ATOM   2343  CA  MET A 714      -6.948 -12.122  56.849  1.00 29.55           C  
ANISOU 2343  CA  MET A 714     3930   3331   3966    -47   -215    532       C  
ATOM   2344  C   MET A 714      -7.908 -11.726  57.963  1.00 30.76           C  
ANISOU 2344  C   MET A 714     4094   3525   4070    -38   -228    510       C  
ATOM   2345  O   MET A 714      -7.491 -11.426  59.082  1.00 30.32           O  
ANISOU 2345  O   MET A 714     4035   3497   3988    -16   -261    509       O  
ATOM   2346  CB  MET A 714      -6.801 -10.953  55.870  1.00 26.36           C  
ANISOU 2346  CB  MET A 714     3511   2911   3595    -61   -237    503       C  
ATOM   2347  CG  MET A 714      -5.769 -11.166  54.779  1.00 25.44           C  
ANISOU 2347  CG  MET A 714     3380   2761   3525    -66   -227    526       C  
ATOM   2348  SD  MET A 714      -5.874  -9.928  53.470  1.00 40.91           S  
ANISOU 2348  SD  MET A 714     5322   4702   5520    -85   -240    499       S  
ATOM   2349  CE  MET A 714      -5.526  -8.427  54.382  1.00 42.24           C  
ANISOU 2349  CE  MET A 714     5474   4889   5688    -77   -308    472       C  
ATOM   2350  N   GLU A 715      -9.197 -11.723  57.643  1.00 32.72           N  
ANISOU 2350  N   GLU A 715     4352   3778   4303    -52   -202    490       N  
ATOM   2351  CA  GLU A 715     -10.224 -11.302  58.586  1.00 36.05           C  
ANISOU 2351  CA  GLU A 715     4781   4240   4677    -43   -210    468       C  
ATOM   2352  C   GLU A 715     -11.371 -12.307  58.625  1.00 37.61           C  
ANISOU 2352  C   GLU A 715     4992   4444   4853    -53   -161    485       C  
ATOM   2353  O   GLU A 715     -12.350 -12.161  57.894  1.00 36.47           O  
ANISOU 2353  O   GLU A 715     4850   4291   4715    -73   -142    465       O  
ATOM   2354  CB  GLU A 715     -10.757  -9.925  58.193  1.00 37.79           C  
ANISOU 2354  CB  GLU A 715     4995   4463   4900    -50   -239    419       C  
ATOM   2355  CG  GLU A 715      -9.694  -8.842  58.127  1.00 40.62           C  
ANISOU 2355  CG  GLU A 715     5337   4811   5285    -43   -291    402       C  
ATOM   2356  CD  GLU A 715     -10.134  -7.650  57.305  1.00 44.60           C  
ANISOU 2356  CD  GLU A 715     5833   5302   5812    -57   -310    363       C  
ATOM   2357  OE1 GLU A 715     -11.150  -7.766  56.589  1.00 44.76           O  
ANISOU 2357  OE1 GLU A 715     5860   5316   5832    -75   -278    352       O  
ATOM   2358  OE2 GLU A 715      -9.465  -6.597  57.373  1.00 47.66           O  
ANISOU 2358  OE2 GLU A 715     6206   5683   6220    -52   -357    344       O  
ATOM   2359  N   PRO A 716     -11.252 -13.331  59.486  1.00 39.35           N  
ANISOU 2359  N   PRO A 716     5219   4679   5052    -40   -143    524       N  
ATOM   2360  CA  PRO A 716     -12.249 -14.403  59.583  1.00 40.34           C  
ANISOU 2360  CA  PRO A 716     5355   4808   5166    -51    -97    549       C  
ATOM   2361  C   PRO A 716     -13.639 -13.865  59.894  1.00 42.33           C  
ANISOU 2361  C   PRO A 716     5608   5093   5382    -54    -90    522       C  
ATOM   2362  O   PRO A 716     -13.808 -13.162  60.890  1.00 43.52           O  
ANISOU 2362  O   PRO A 716     5757   5288   5491    -31   -116    505       O  
ATOM   2363  CB  PRO A 716     -11.745 -15.243  60.759  1.00 40.00           C  
ANISOU 2363  CB  PRO A 716     5316   4787   5096    -28    -92    593       C  
ATOM   2364  CG  PRO A 716     -10.290 -14.959  60.835  1.00 39.64           C  
ANISOU 2364  CG  PRO A 716     5263   4730   5068    -12   -127    598       C  
ATOM   2365  CD  PRO A 716     -10.140 -13.526  60.431  1.00 39.65           C  
ANISOU 2365  CD  PRO A 716     5254   4732   5078    -14   -167    548       C  
ATOM   2366  N   PRO A 717     -14.626 -14.192  59.047  1.00 43.68           N  
ANISOU 2366  N   PRO A 717     5781   5245   5570    -80    -58    516       N  
ATOM   2367  CA  PRO A 717     -16.002 -13.730  59.252  1.00 45.73           C  
ANISOU 2367  CA  PRO A 717     6039   5536   5801    -85    -49    492       C  
ATOM   2368  C   PRO A 717     -16.625 -14.360  60.490  1.00 48.73           C  
ANISOU 2368  C   PRO A 717     6420   5958   6136    -70    -29    524       C  
ATOM   2369  O   PRO A 717     -16.493 -15.564  60.708  1.00 49.24           O  
ANISOU 2369  O   PRO A 717     6488   6011   6209    -74      0    571       O  
ATOM   2370  CB  PRO A 717     -16.724 -14.207  57.988  1.00 45.09           C  
ANISOU 2370  CB  PRO A 717     5960   5416   5756   -119    -18    487       C  
ATOM   2371  CG  PRO A 717     -15.925 -15.355  57.508  1.00 44.49           C  
ANISOU 2371  CG  PRO A 717     5889   5297   5716   -127      1    523       C  
ATOM   2372  CD  PRO A 717     -14.501 -15.047  57.856  1.00 43.67           C  
ANISOU 2372  CD  PRO A 717     5784   5193   5616   -105    -30    530       C  
ATOM   2373  N   ASP A 718     -17.290 -13.541  61.295  1.00 51.87           N  
ANISOU 2373  N   ASP A 718     6814   6406   6487    -51    -43    500       N  
ATOM   2374  CA  ASP A 718     -17.914 -14.010  62.524  1.00 54.82           C  
ANISOU 2374  CA  ASP A 718     7187   6831   6811    -31    -24    530       C  
ATOM   2375  C   ASP A 718     -19.212 -13.248  62.773  1.00 54.41           C  
ANISOU 2375  C   ASP A 718     7128   6821   6723    -26    -21    498       C  
ATOM   2376  O   ASP A 718     -19.347 -12.089  62.381  1.00 53.37           O  
ANISOU 2376  O   ASP A 718     6995   6689   6593    -24    -51    446       O  
ATOM   2377  CB  ASP A 718     -16.948 -13.844  63.703  1.00 58.01           C  
ANISOU 2377  CB  ASP A 718     7593   7269   7178      7    -54    542       C  
ATOM   2378  CG  ASP A 718     -17.544 -14.303  65.022  1.00 61.90           C  
ANISOU 2378  CG  ASP A 718     8084   7821   7612     33    -35    576       C  
ATOM   2379  OD1 ASP A 718     -18.544 -15.052  65.000  1.00 63.51           O  
ANISOU 2379  OD1 ASP A 718     8283   8031   7815     17      9    606       O  
ATOM   2380  OD2 ASP A 718     -17.008 -13.919  66.084  1.00 63.10           O  
ANISOU 2380  OD2 ASP A 718     8239   8017   7721     70    -63    573       O  
ATOM   2381  N   ILE A 719     -20.170 -13.907  63.417  1.00 55.66           N  
ANISOU 2381  N   ILE A 719     7281   7014   6853    -24     15    531       N  
ATOM   2382  CA  ILE A 719     -21.437 -13.268  63.752  1.00 56.84           C  
ANISOU 2382  CA  ILE A 719     7422   7210   6965    -15     22    507       C  
ATOM   2383  C   ILE A 719     -21.240 -12.189  64.813  1.00 59.44           C  
ANISOU 2383  C   ILE A 719     7752   7595   7236     30    -17    474       C  
ATOM   2384  O   ILE A 719     -20.753 -12.463  65.910  1.00 59.38           O  
ANISOU 2384  O   ILE A 719     7748   7625   7189     61    -23    500       O  
ATOM   2385  CB  ILE A 719     -22.476 -14.286  64.251  1.00 56.09           C  
ANISOU 2385  CB  ILE A 719     7317   7142   6853    -23     71    558       C  
ATOM   2386  CG1 ILE A 719     -22.694 -15.381  63.205  1.00 55.96           C  
ANISOU 2386  CG1 ILE A 719     7299   7064   6898    -68    105    588       C  
ATOM   2387  CG2 ILE A 719     -23.786 -13.587  64.574  1.00 56.07           C  
ANISOU 2387  CG2 ILE A 719     7302   7189   6811    -12     80    533       C  
ATOM   2388  CD1 ILE A 719     -23.754 -16.390  63.588  1.00 55.89           C  
ANISOU 2388  CD1 ILE A 719     7277   7073   6885    -81    152    640       C  
ATOM   2389  N   MET A 720     -21.622 -10.962  64.476  1.00 61.66           N  
ANISOU 2389  N   MET A 720     8032   7882   7513     35    -45    415       N  
ATOM   2390  CA  MET A 720     -21.465  -9.835  65.384  1.00 63.93           C  
ANISOU 2390  CA  MET A 720     8322   8217   7750     78    -87    373       C  
ATOM   2391  C   MET A 720     -22.509  -9.883  66.496  1.00 65.64           C  
ANISOU 2391  C   MET A 720     8532   8508   7900    109    -65    384       C  
ATOM   2392  O   MET A 720     -23.690 -10.125  66.242  1.00 66.02           O  
ANISOU 2392  O   MET A 720     8570   8569   7947     94    -28    393       O  
ATOM   2393  CB  MET A 720     -21.574  -8.515  64.618  1.00 64.75           C  
ANISOU 2393  CB  MET A 720     8426   8298   7877     72   -125    307       C  
ATOM   2394  CG  MET A 720     -20.960  -7.326  65.336  1.00 65.54           C  
ANISOU 2394  CG  MET A 720     8532   8423   7949    112   -183    259       C  
ATOM   2395  SD  MET A 720     -19.170  -7.478  65.510  1.00100.35           S  
ANISOU 2395  SD  MET A 720    12947  12800  12381    118   -222    273       S  
ATOM   2396  CE  MET A 720     -18.780  -5.951  66.361  1.00 36.16           C  
ANISOU 2396  CE  MET A 720     4821   4702   4217    164   -295    207       C  
ATOM   2397  N   VAL A 729     -34.005 -11.751  62.467  1.00 37.41           N  
ANISOU 2397  N   VAL A 729     4799   4982   4435   -103    235    446       N  
ATOM   2398  CA  VAL A 729     -34.135 -11.566  61.025  1.00 38.51           C  
ANISOU 2398  CA  VAL A 729     4941   5059   4631   -143    222    410       C  
ATOM   2399  C   VAL A 729     -32.878 -10.944  60.417  1.00 38.08           C  
ANISOU 2399  C   VAL A 729     4915   4958   4594   -139    179    367       C  
ATOM   2400  O   VAL A 729     -32.325 -11.466  59.448  1.00 36.90           O  
ANISOU 2400  O   VAL A 729     4778   4746   4498   -172    176    370       O  
ATOM   2401  CB  VAL A 729     -35.374 -10.718  60.677  1.00 37.71           C  
ANISOU 2401  CB  VAL A 729     4821   4985   4521   -141    222    372       C  
ATOM   2402  CG1 VAL A 729     -35.305 -10.231  59.244  1.00 35.60           C  
ANISOU 2402  CG1 VAL A 729     4563   4660   4303   -171    198    324       C  
ATOM   2403  CG2 VAL A 729     -36.637 -11.525  60.906  1.00 38.28           C  
ANISOU 2403  CG2 VAL A 729     4862   5085   4598   -160    268    419       C  
ATOM   2404  N   TYR A 730     -32.429  -9.832  60.989  1.00 38.18           N  
ANISOU 2404  N   TYR A 730     4938   5002   4565    -98    146    327       N  
ATOM   2405  CA  TYR A 730     -31.189  -9.210  60.551  1.00 38.47           C  
ANISOU 2405  CA  TYR A 730     4998   4999   4619    -93    103    291       C  
ATOM   2406  C   TYR A 730     -30.009 -10.066  60.985  1.00 41.57           C  
ANISOU 2406  C   TYR A 730     5404   5373   5016    -91    104    332       C  
ATOM   2407  O   TYR A 730     -29.922 -10.468  62.145  1.00 43.76           O  
ANISOU 2407  O   TYR A 730     5680   5695   5253    -65    117    366       O  
ATOM   2408  CB  TYR A 730     -31.045  -7.811  61.147  1.00 37.02           C  
ANISOU 2408  CB  TYR A 730     4820   4853   4392    -48     64    239       C  
ATOM   2409  CG  TYR A 730     -31.996  -6.784  60.581  1.00 36.60           C  
ANISOU 2409  CG  TYR A 730     4758   4808   4342    -48     52    190       C  
ATOM   2410  CD1 TYR A 730     -33.160  -6.440  61.258  1.00 37.21           C  
ANISOU 2410  CD1 TYR A 730     4817   4947   4375    -23     68    184       C  
ATOM   2411  CD2 TYR A 730     -31.726  -6.151  59.376  1.00 36.24           C  
ANISOU 2411  CD2 TYR A 730     4719   4710   4341    -70     26    152       C  
ATOM   2412  CE1 TYR A 730     -34.030  -5.497  60.747  1.00 37.41           C  
ANISOU 2412  CE1 TYR A 730     4833   4979   4403    -21     57    139       C  
ATOM   2413  CE2 TYR A 730     -32.588  -5.207  58.857  1.00 37.16           C  
ANISOU 2413  CE2 TYR A 730     4826   4833   4459    -68     14    109       C  
ATOM   2414  CZ  TYR A 730     -33.739  -4.883  59.546  1.00 38.20           C  
ANISOU 2414  CZ  TYR A 730     4941   5024   4549    -44     30    102       C  
ATOM   2415  OH  TYR A 730     -34.601  -3.943  59.031  1.00 38.68           O  
ANISOU 2415  OH  TYR A 730     4992   5091   4614    -41     18     59       O  
ATOM   2416  N   LEU A 731     -29.104 -10.349  60.055  1.00 41.04           N  
ANISOU 2416  N   LEU A 731     5351   5243   4998   -117     92    330       N  
ATOM   2417  CA  LEU A 731     -27.889 -11.080  60.388  1.00 41.05           C  
ANISOU 2417  CA  LEU A 731     5366   5223   5008   -113     89    364       C  
ATOM   2418  C   LEU A 731     -26.677 -10.167  60.300  1.00 40.15           C  
ANISOU 2418  C   LEU A 731     5268   5092   4895    -94     42    327       C  
ATOM   2419  O   LEU A 731     -26.131  -9.943  59.221  1.00 37.26           O  
ANISOU 2419  O   LEU A 731     4909   4675   4573   -115     26    306       O  
ATOM   2420  CB  LEU A 731     -27.702 -12.287  59.471  1.00 41.38           C  
ANISOU 2420  CB  LEU A 731     5411   5206   5106   -154    114    398       C  
ATOM   2421  CG  LEU A 731     -26.403 -13.064  59.691  1.00 41.76           C  
ANISOU 2421  CG  LEU A 731     5473   5226   5168   -152    111    432       C  
ATOM   2422  CD1 LEU A 731     -26.236 -13.452  61.153  1.00 42.26           C  
ANISOU 2422  CD1 LEU A 731     5534   5340   5183   -120    121    472       C  
ATOM   2423  CD2 LEU A 731     -26.375 -14.289  58.811  1.00 41.61           C  
ANISOU 2423  CD2 LEU A 731     5455   5150   5203   -190    137    463       C  
ATOM   2424  N   ILE A 732     -26.259  -9.641  61.445  1.00 42.09           N  
ANISOU 2424  N   ILE A 732     5517   5382   5092    -53     19    320       N  
ATOM   2425  CA  ILE A 732     -25.125  -8.733  61.489  1.00 43.87           C  
ANISOU 2425  CA  ILE A 732     5755   5595   5320    -33    -30    284       C  
ATOM   2426  C   ILE A 732     -23.820  -9.518  61.569  1.00 45.65           C  
ANISOU 2426  C   ILE A 732     5990   5790   5566    -37    -33    320       C  
ATOM   2427  O   ILE A 732     -23.603 -10.278  62.511  1.00 46.66           O  
ANISOU 2427  O   ILE A 732     6119   5945   5665    -21    -18    362       O  
ATOM   2428  CB  ILE A 732     -25.209  -7.792  62.704  1.00 44.41           C  
ANISOU 2428  CB  ILE A 732     5823   5723   5327     15    -59    255       C  
ATOM   2429  CG1 ILE A 732     -26.646  -7.301  62.912  1.00 46.11           C  
ANISOU 2429  CG1 ILE A 732     6025   5983   5510     26    -44    233       C  
ATOM   2430  CG2 ILE A 732     -24.239  -6.631  62.545  1.00 42.92           C  
ANISOU 2430  CG2 ILE A 732     5644   5513   5152     30   -117    207       C  
ATOM   2431  CD1 ILE A 732     -27.155  -6.389  61.822  1.00 45.73           C  
ANISOU 2431  CD1 ILE A 732     5974   5905   5496      7    -60    185       C  
ATOM   2432  N   CYS A 733     -22.957  -9.339  60.576  1.00 45.27           N  
ANISOU 2432  N   CYS A 733     5948   5687   5566    -57    -53    307       N  
ATOM   2433  CA  CYS A 733     -21.645  -9.975  60.591  1.00 44.87           C  
ANISOU 2433  CA  CYS A 733     5905   5606   5537    -58    -60    337       C  
ATOM   2434  C   CYS A 733     -20.559  -8.953  60.910  1.00 43.01           C  
ANISOU 2434  C   CYS A 733     5673   5370   5297    -33   -113    306       C  
ATOM   2435  O   CYS A 733     -20.816  -7.750  60.927  1.00 43.52           O  
ANISOU 2435  O   CYS A 733     5736   5449   5352    -20   -145    259       O  
ATOM   2436  CB  CYS A 733     -21.356 -10.665  59.256  1.00 44.81           C  
ANISOU 2436  CB  CYS A 733     5900   5538   5589    -96    -40    352       C  
ATOM   2437  SG  CYS A 733     -22.344 -12.149  58.947  1.00 49.41           S  
ANISOU 2437  SG  CYS A 733     6479   6108   6186   -126     18    397       S  
ATOM   2438  N   ASN A 734     -19.346  -9.434  61.159  1.00 40.83           N  
ANISOU 2438  N   ASN A 734     5403   5079   5033    -27   -124    333       N  
ATOM   2439  CA  ASN A 734     -18.247  -8.561  61.558  1.00 39.45           C  
ANISOU 2439  CA  ASN A 734     5229   4904   4856     -4   -176    308       C  
ATOM   2440  C   ASN A 734     -17.404  -8.064  60.387  1.00 39.74           C  
ANISOU 2440  C   ASN A 734     5262   4886   4950    -25   -199    292       C  
ATOM   2441  O   ASN A 734     -16.246  -7.688  60.566  1.00 39.19           O  
ANISOU 2441  O   ASN A 734     5191   4804   4894    -13   -236    289       O  
ATOM   2442  CB  ASN A 734     -17.349  -9.272  62.570  1.00 37.64           C  
ANISOU 2442  CB  ASN A 734     5004   4693   4604     19   -180    346       C  
ATOM   2443  CG  ASN A 734     -16.653 -10.483  61.980  1.00 35.81           C  
ANISOU 2443  CG  ASN A 734     4775   4419   4413     -4   -151    395       C  
ATOM   2444  OD1 ASN A 734     -17.087 -11.030  60.965  1.00 35.58           O  
ANISOU 2444  OD1 ASN A 734     4745   4355   4419    -35   -118    405       O  
ATOM   2445  ND2 ASN A 734     -15.571 -10.911  62.617  1.00 34.98           N  
ANISOU 2445  ND2 ASN A 734     4671   4316   4302     14   -165    422       N  
ATOM   2446  N   THR A 735     -17.988  -8.064  59.192  1.00 40.90           N  
ANISOU 2446  N   THR A 735     5407   5003   5131    -55   -178    283       N  
ATOM   2447  CA  THR A 735     -17.276  -7.637  57.991  1.00 40.84           C  
ANISOU 2447  CA  THR A 735     5394   4946   5175    -75   -194    273       C  
ATOM   2448  C   THR A 735     -16.886  -6.162  58.053  1.00 40.08           C  
ANISOU 2448  C   THR A 735     5292   4850   5087    -61   -248    229       C  
ATOM   2449  O   THR A 735     -17.744  -5.282  58.114  1.00 41.27           O  
ANISOU 2449  O   THR A 735     5441   5018   5221    -56   -262    192       O  
ATOM   2450  CB  THR A 735     -18.109  -7.893  56.722  1.00 41.12           C  
ANISOU 2450  CB  THR A 735     5429   4955   5238   -106   -161    269       C  
ATOM   2451  OG1 THR A 735     -18.422  -9.288  56.629  1.00 42.39           O  
ANISOU 2451  OG1 THR A 735     5597   5110   5401   -120   -114    308       O  
ATOM   2452  CG2 THR A 735     -17.337  -7.468  55.482  1.00 40.14           C  
ANISOU 2452  CG2 THR A 735     5300   4787   5164   -122   -175    262       C  
ATOM   2453  N   THR A 736     -15.582  -5.902  58.035  1.00 38.24           N  
ANISOU 2453  N   THR A 736     5054   4596   4880    -56   -280    236       N  
ATOM   2454  CA  THR A 736     -15.065  -4.541  58.126  1.00 38.74           C  
ANISOU 2454  CA  THR A 736     5109   4653   4958    -45   -337    199       C  
ATOM   2455  C   THR A 736     -15.139  -3.820  56.784  1.00 40.41           C  
ANISOU 2455  C   THR A 736     5310   4826   5217    -69   -342    183       C  
ATOM   2456  O   THR A 736     -15.725  -4.326  55.827  1.00 39.20           O  
ANISOU 2456  O   THR A 736     5160   4658   5077    -92   -303    194       O  
ATOM   2457  CB  THR A 736     -13.600  -4.528  58.604  1.00 37.41           C  
ANISOU 2457  CB  THR A 736     4933   4474   4805    -32   -372    216       C  
ATOM   2458  OG1 THR A 736     -12.761  -5.109  57.598  1.00 38.14           O  
ANISOU 2458  OG1 THR A 736     5020   4527   4945    -54   -353    250       O  
ATOM   2459  CG2 THR A 736     -13.452  -5.312  59.901  1.00 34.71           C  
ANISOU 2459  CG2 THR A 736     4601   4170   4416     -6   -365    237       C  
ATOM   2460  N   ASN A 737     -14.538  -2.635  56.726  1.00 43.25           N  
ANISOU 2460  N   ASN A 737     5659   5171   5603    -63   -394    157       N  
ATOM   2461  CA  ASN A 737     -14.489  -1.854  55.495  1.00 44.69           C  
ANISOU 2461  CA  ASN A 737     5830   5318   5834    -84   -404    146       C  
ATOM   2462  C   ASN A 737     -13.667  -2.549  54.415  1.00 43.84           C  
ANISOU 2462  C   ASN A 737     5715   5175   5766   -106   -377    187       C  
ATOM   2463  O   ASN A 737     -14.102  -2.660  53.269  1.00 43.83           O  
ANISOU 2463  O   ASN A 737     5712   5157   5785   -126   -349    192       O  
ATOM   2464  CB  ASN A 737     -13.918  -0.458  55.760  1.00 45.44           C  
ANISOU 2464  CB  ASN A 737     5913   5400   5953    -73   -468    115       C  
ATOM   2465  CG  ASN A 737     -14.799   0.372  56.674  1.00 47.04           C  
ANISOU 2465  CG  ASN A 737     6122   5633   6117    -50   -498     67       C  
ATOM   2466  OD1 ASN A 737     -16.025   0.260  56.646  1.00 46.73           O  
ANISOU 2466  OD1 ASN A 737     6092   5616   6046    -49   -470     52       O  
ATOM   2467  ND2 ASN A 737     -14.174   1.214  57.490  1.00 48.10           N  
ANISOU 2467  ND2 ASN A 737     6252   5769   6255    -28   -556     42       N  
ATOM   2468  N   LEU A 738     -12.482  -3.019  54.793  1.00 41.26           N  
ANISOU 2468  N   LEU A 738     5383   4842   5451    -99   -386    216       N  
ATOM   2469  CA  LEU A 738     -11.570  -3.670  53.854  1.00 40.12           C  
ANISOU 2469  CA  LEU A 738     5230   4668   5345   -113   -363    255       C  
ATOM   2470  C   LEU A 738     -12.182  -4.938  53.259  1.00 35.94           C  
ANISOU 2470  C   LEU A 738     4715   4138   4804   -126   -303    277       C  
ATOM   2471  O   LEU A 738     -11.875  -5.315  52.128  1.00 34.74           O  
ANISOU 2471  O   LEU A 738     4558   3960   4681   -140   -278    297       O  
ATOM   2472  CB  LEU A 738     -10.235  -3.988  54.536  1.00 41.49           C  
ANISOU 2472  CB  LEU A 738     5397   4840   5528   -100   -385    282       C  
ATOM   2473  CG  LEU A 738      -9.102  -4.503  53.645  1.00 42.30           C  
ANISOU 2473  CG  LEU A 738     5486   4914   5674   -110   -369    322       C  
ATOM   2474  CD1 LEU A 738      -8.791  -3.505  52.539  1.00 42.27           C  
ANISOU 2474  CD1 LEU A 738     5461   4882   5718   -124   -387    318       C  
ATOM   2475  CD2 LEU A 738      -7.858  -4.798  54.472  1.00 42.92           C  
ANISOU 2475  CD2 LEU A 738     5555   4994   5757    -94   -394    346       C  
ATOM   2476  N   GLY A 739     -13.054  -5.587  54.024  1.00 32.81           N  
ANISOU 2476  N   GLY A 739     4335   3769   4364   -119   -281    274       N  
ATOM   2477  CA  GLY A 739     -13.759  -6.761  53.544  1.00 29.49           C  
ANISOU 2477  CA  GLY A 739     3927   3345   3934   -133   -228    292       C  
ATOM   2478  C   GLY A 739     -14.788  -6.404  52.487  1.00 26.37           C  
ANISOU 2478  C   GLY A 739     3531   2940   3547   -151   -211    269       C  
ATOM   2479  O   GLY A 739     -15.255  -7.267  51.745  1.00 24.00           O  
ANISOU 2479  O   GLY A 739     3238   2628   3252   -166   -172    281       O  
ATOM   2480  N   VAL A 740     -15.142  -5.124  52.422  1.00 24.67           N  
ANISOU 2480  N   VAL A 740     3308   2730   3335   -150   -244    235       N  
ATOM   2481  CA  VAL A 740     -16.101  -4.638  51.437  1.00 23.89           C  
ANISOU 2481  CA  VAL A 740     3208   2625   3245   -165   -233    212       C  
ATOM   2482  C   VAL A 740     -15.401  -3.855  50.329  1.00 23.91           C  
ANISOU 2482  C   VAL A 740     3195   2598   3291   -174   -251    213       C  
ATOM   2483  O   VAL A 740     -15.692  -4.047  49.150  1.00 23.08           O  
ANISOU 2483  O   VAL A 740     3089   2477   3202   -189   -227    217       O  
ATOM   2484  CB  VAL A 740     -17.174  -3.737  52.085  1.00 23.16           C  
ANISOU 2484  CB  VAL A 740     3116   2560   3123   -156   -253    173       C  
ATOM   2485  CG1 VAL A 740     -18.158  -3.247  51.036  1.00 22.69           C  
ANISOU 2485  CG1 VAL A 740     3054   2493   3074   -172   -243    151       C  
ATOM   2486  CG2 VAL A 740     -17.901  -4.483  53.193  1.00 23.42           C  
ANISOU 2486  CG2 VAL A 740     3161   2628   3110   -145   -233    176       C  
ATOM   2487  N   VAL A 741     -14.474  -2.983  50.718  1.00 24.50           N  
ANISOU 2487  N   VAL A 741     3258   2666   3385   -164   -295    211       N  
ATOM   2488  CA  VAL A 741     -13.777  -2.102  49.780  1.00 24.81           C  
ANISOU 2488  CA  VAL A 741     3278   2679   3470   -172   -317    215       C  
ATOM   2489  C   VAL A 741     -13.061  -2.850  48.655  1.00 25.46           C  
ANISOU 2489  C   VAL A 741     3355   2739   3579   -182   -285    252       C  
ATOM   2490  O   VAL A 741     -13.205  -2.501  47.482  1.00 25.76           O  
ANISOU 2490  O   VAL A 741     3385   2764   3639   -193   -275    254       O  
ATOM   2491  CB  VAL A 741     -12.763  -1.184  50.508  1.00 23.59           C  
ANISOU 2491  CB  VAL A 741     3108   2518   3337   -160   -372    212       C  
ATOM   2492  CG1 VAL A 741     -11.875  -0.462  49.508  1.00 20.98           C  
ANISOU 2492  CG1 VAL A 741     2753   2157   3060   -170   -390    231       C  
ATOM   2493  CG2 VAL A 741     -13.491  -0.184  51.392  1.00 24.31           C  
ANISOU 2493  CG2 VAL A 741     3204   2627   3408   -147   -411    168       C  
ATOM   2494  N   ALA A 742     -12.301  -3.880  49.014  1.00 25.86           N  
ANISOU 2494  N   ALA A 742     3410   2790   3627   -175   -268    281       N  
ATOM   2495  CA  ALA A 742     -11.512  -4.628  48.033  1.00 27.37           C  
ANISOU 2495  CA  ALA A 742     3596   2962   3842   -179   -239    315       C  
ATOM   2496  C   ALA A 742     -12.339  -5.292  46.919  1.00 29.00           C  
ANISOU 2496  C   ALA A 742     3815   3164   4041   -191   -195    312       C  
ATOM   2497  O   ALA A 742     -12.043  -5.095  45.741  1.00 28.58           O  
ANISOU 2497  O   ALA A 742     3750   3097   4011   -195   -186    323       O  
ATOM   2498  CB  ALA A 742     -10.584  -5.639  48.724  1.00 26.39           C  
ANISOU 2498  CB  ALA A 742     3476   2838   3714   -168   -231    345       C  
ATOM   2499  N   PRO A 743     -13.377  -6.074  47.274  1.00 31.88           N  
ANISOU 2499  N   PRO A 743     4199   3539   4374   -195   -170    300       N  
ATOM   2500  CA  PRO A 743     -14.187  -6.610  46.174  1.00 32.22           C  
ANISOU 2500  CA  PRO A 743     4252   3576   4415   -206   -135    292       C  
ATOM   2501  C   PRO A 743     -15.041  -5.538  45.490  1.00 30.37           C  
ANISOU 2501  C   PRO A 743     4011   3346   4183   -215   -147    264       C  
ATOM   2502  O   PRO A 743     -15.456  -5.732  44.348  1.00 32.58           O  
ANISOU 2502  O   PRO A 743     4293   3618   4468   -223   -125    260       O  
ATOM   2503  CB  PRO A 743     -15.081  -7.640  46.870  1.00 33.79           C  
ANISOU 2503  CB  PRO A 743     4469   3785   4583   -210   -110    288       C  
ATOM   2504  CG  PRO A 743     -15.183  -7.157  48.269  1.00 34.08           C  
ANISOU 2504  CG  PRO A 743     4506   3845   4600   -200   -137    280       C  
ATOM   2505  CD  PRO A 743     -13.835  -6.581  48.582  1.00 33.93           C  
ANISOU 2505  CD  PRO A 743     4472   3820   4601   -188   -169    295       C  
ATOM   2506  N   LEU A 744     -15.298  -4.430  46.179  1.00 27.26           N  
ANISOU 2506  N   LEU A 744     3610   2964   3785   -212   -182    243       N  
ATOM   2507  CA  LEU A 744     -16.036  -3.317  45.589  1.00 26.19           C  
ANISOU 2507  CA  LEU A 744     3466   2829   3655   -219   -198    218       C  
ATOM   2508  C   LEU A 744     -15.176  -2.600  44.557  1.00 26.82           C  
ANISOU 2508  C   LEU A 744     3527   2890   3773   -220   -210    235       C  
ATOM   2509  O   LEU A 744     -15.675  -2.124  43.538  1.00 27.25           O  
ANISOU 2509  O   LEU A 744     3576   2941   3835   -227   -205    227       O  
ATOM   2510  CB  LEU A 744     -16.476  -2.326  46.669  1.00 23.73           C  
ANISOU 2510  CB  LEU A 744     3152   2532   3330   -211   -235    189       C  
ATOM   2511  CG  LEU A 744     -17.320  -1.128  46.225  1.00 23.24           C  
ANISOU 2511  CG  LEU A 744     3083   2472   3274   -215   -255    159       C  
ATOM   2512  CD1 LEU A 744     -18.635  -1.588  45.616  1.00 22.18           C  
ANISOU 2512  CD1 LEU A 744     2959   2348   3119   -226   -222    143       C  
ATOM   2513  CD2 LEU A 744     -17.571  -0.189  47.395  1.00 22.34           C  
ANISOU 2513  CD2 LEU A 744     2967   2372   3148   -202   -296    130       C  
ATOM   2514  N   GLY A 745     -13.879  -2.523  44.836  1.00 25.54           N  
ANISOU 2514  N   GLY A 745     3352   2718   3633   -213   -227    261       N  
ATOM   2515  CA  GLY A 745     -12.943  -1.875  43.940  1.00 23.70           C  
ANISOU 2515  CA  GLY A 745     3096   2469   3440   -213   -238    286       C  
ATOM   2516  C   GLY A 745     -12.710  -2.690  42.685  1.00 22.99           C  
ANISOU 2516  C   GLY A 745     3008   2375   3354   -214   -197    309       C  
ATOM   2517  O   GLY A 745     -12.630  -2.141  41.586  1.00 23.35           O  
ANISOU 2517  O   GLY A 745     3040   2415   3417   -216   -194    318       O  
ATOM   2518  N   TYR A 746     -12.600  -4.006  42.848  1.00 21.83           N  
ANISOU 2518  N   TYR A 746     2877   2229   3189   -209   -166    318       N  
ATOM   2519  CA  TYR A 746     -12.391  -4.894  41.710  1.00 23.91           C  
ANISOU 2519  CA  TYR A 746     3146   2487   3453   -206   -127    334       C  
ATOM   2520  C   TYR A 746     -13.610  -4.909  40.793  1.00 28.46           C  
ANISOU 2520  C   TYR A 746     3733   3069   4013   -214   -108    309       C  
ATOM   2521  O   TYR A 746     -13.473  -4.889  39.570  1.00 27.95           O  
ANISOU 2521  O   TYR A 746     3663   3003   3955   -210    -92    318       O  
ATOM   2522  CB  TYR A 746     -12.047  -6.315  42.162  1.00 22.37           C  
ANISOU 2522  CB  TYR A 746     2967   2288   3246   -199   -102    347       C  
ATOM   2523  CG  TYR A 746     -11.866  -7.280  41.009  1.00 22.10           C  
ANISOU 2523  CG  TYR A 746     2940   2246   3211   -192    -64    358       C  
ATOM   2524  CD1 TYR A 746     -10.732  -7.230  40.207  1.00 23.72           C  
ANISOU 2524  CD1 TYR A 746     3128   2447   3438   -178    -57    389       C  
ATOM   2525  CD2 TYR A 746     -12.830  -8.237  40.718  1.00 23.07           C  
ANISOU 2525  CD2 TYR A 746     3087   2367   3313   -197    -37    338       C  
ATOM   2526  CE1 TYR A 746     -10.564  -8.107  39.146  1.00 23.75           C  
ANISOU 2526  CE1 TYR A 746     3140   2447   3437   -166    -23    395       C  
ATOM   2527  CE2 TYR A 746     -12.670  -9.118  39.661  1.00 25.49           C  
ANISOU 2527  CE2 TYR A 746     3401   2664   3619   -187     -7    342       C  
ATOM   2528  CZ  TYR A 746     -11.534  -9.048  38.879  1.00 25.35           C  
ANISOU 2528  CZ  TYR A 746     3368   2645   3618   -170      0    370       C  
ATOM   2529  OH  TYR A 746     -11.375  -9.922  37.829  1.00 26.59           O  
ANISOU 2529  OH  TYR A 746     3535   2797   3772   -156     30    371       O  
ATOM   2530  N   ASN A 747     -14.799  -4.947  41.390  1.00 29.63           N  
ANISOU 2530  N   ASN A 747     3896   3225   4137   -223   -110    278       N  
ATOM   2531  CA  ASN A 747     -16.038  -4.854  40.625  1.00 30.58           C  
ANISOU 2531  CA  ASN A 747     4024   3351   4243   -233    -98    251       C  
ATOM   2532  C   ASN A 747     -16.142  -3.511  39.914  1.00 31.48           C  
ANISOU 2532  C   ASN A 747     4121   3468   4373   -234   -119    247       C  
ATOM   2533  O   ASN A 747     -16.707  -3.417  38.826  1.00 32.15           O  
ANISOU 2533  O   ASN A 747     4206   3556   4453   -236   -106    238       O  
ATOM   2534  CB  ASN A 747     -17.257  -5.060  41.529  1.00 29.82           C  
ANISOU 2534  CB  ASN A 747     3942   3267   4121   -242    -98    222       C  
ATOM   2535  CG  ASN A 747     -17.421  -6.501  41.971  1.00 29.02           C  
ANISOU 2535  CG  ASN A 747     3860   3163   4006   -244    -70    227       C  
ATOM   2536  OD1 ASN A 747     -17.025  -7.428  41.266  1.00 29.02           O  
ANISOU 2536  OD1 ASN A 747     3866   3149   4011   -240    -46    240       O  
ATOM   2537  ND2 ASN A 747     -18.013  -6.696  43.143  1.00 29.14           N  
ANISOU 2537  ND2 ASN A 747     3881   3189   4002   -247    -74    218       N  
ATOM   2538  N   GLY A 748     -15.590  -2.476  40.540  1.00 31.60           N  
ANISOU 2538  N   GLY A 748     4119   3480   4407   -232   -154    253       N  
ATOM   2539  CA  GLY A 748     -15.579  -1.147  39.959  1.00 30.48           C  
ANISOU 2539  CA  GLY A 748     3957   3335   4287   -234   -179    254       C  
ATOM   2540  C   GLY A 748     -14.762  -1.110  38.685  1.00 29.92           C  
ANISOU 2540  C   GLY A 748     3871   3259   4238   -228   -164    288       C  
ATOM   2541  O   GLY A 748     -15.116  -0.418  37.730  1.00 30.80           O  
ANISOU 2541  O   GLY A 748     3973   3374   4357   -229   -165    288       O  
ATOM   2542  N   LEU A 749     -13.664  -1.861  38.670  1.00 27.20           N  
ANISOU 2542  N   LEU A 749     3524   2910   3902   -219   -149    318       N  
ATOM   2543  CA  LEU A 749     -12.810  -1.943  37.490  1.00 24.00           C  
ANISOU 2543  CA  LEU A 749     3102   2504   3511   -209   -130    353       C  
ATOM   2544  C   LEU A 749     -13.516  -2.690  36.363  1.00 22.33           C  
ANISOU 2544  C   LEU A 749     2907   2303   3274   -204    -94    340       C  
ATOM   2545  O   LEU A 749     -13.448  -2.283  35.203  1.00 22.92           O  
ANISOU 2545  O   LEU A 749     2970   2385   3353   -198    -84    354       O  
ATOM   2546  CB  LEU A 749     -11.483  -2.625  37.828  1.00 22.54           C  
ANISOU 2546  CB  LEU A 749     2910   2313   3341   -198   -123    386       C  
ATOM   2547  CG  LEU A 749     -10.582  -1.891  38.824  1.00 22.77           C  
ANISOU 2547  CG  LEU A 749     2919   2332   3401   -201   -161    403       C  
ATOM   2548  CD1 LEU A 749      -9.361  -2.731  39.175  1.00 20.30           C  
ANISOU 2548  CD1 LEU A 749     2601   2016   3098   -189   -150    434       C  
ATOM   2549  CD2 LEU A 749     -10.167  -0.536  38.271  1.00 23.46           C  
ANISOU 2549  CD2 LEU A 749     2975   2414   3526   -205   -187    425       C  
ATOM   2550  N   LEU A 750     -14.189  -3.783  36.714  1.00 19.44           N  
ANISOU 2550  N   LEU A 750     2567   1937   2881   -207    -74    315       N  
ATOM   2551  CA  LEU A 750     -14.975  -4.546  35.752  1.00 21.77           C  
ANISOU 2551  CA  LEU A 750     2881   2239   3152   -204    -45    296       C  
ATOM   2552  C   LEU A 750     -16.057  -3.673  35.122  1.00 23.43           C  
ANISOU 2552  C   LEU A 750     3088   2459   3354   -212    -54    273       C  
ATOM   2553  O   LEU A 750     -16.312  -3.751  33.922  1.00 23.36           O  
ANISOU 2553  O   LEU A 750     3080   2459   3336   -204    -38    271       O  
ATOM   2554  CB  LEU A 750     -15.613  -5.763  36.424  1.00 22.51           C  
ANISOU 2554  CB  LEU A 750     3001   2326   3226   -211    -30    272       C  
ATOM   2555  CG  LEU A 750     -14.672  -6.872  36.892  1.00 23.98           C  
ANISOU 2555  CG  LEU A 750     3194   2501   3416   -201    -14    293       C  
ATOM   2556  CD1 LEU A 750     -15.458  -7.990  37.559  1.00 24.37           C  
ANISOU 2556  CD1 LEU A 750     3267   2542   3448   -210     -1    271       C  
ATOM   2557  CD2 LEU A 750     -13.859  -7.408  35.727  1.00 24.74           C  
ANISOU 2557  CD2 LEU A 750     3288   2597   3516   -180     10    313       C  
ATOM   2558  N   ILE A 751     -16.687  -2.841  35.943  1.00 24.49           N  
ANISOU 2558  N   ILE A 751     3219   2593   3492   -225    -82    255       N  
ATOM   2559  CA  ILE A 751     -17.701  -1.909  35.467  1.00 25.31           C  
ANISOU 2559  CA  ILE A 751     3319   2706   3592   -232    -95    234       C  
ATOM   2560  C   ILE A 751     -17.073  -0.836  34.582  1.00 27.81           C  
ANISOU 2560  C   ILE A 751     3610   3024   3932   -225   -106    263       C  
ATOM   2561  O   ILE A 751     -17.602  -0.500  33.521  1.00 27.35           O  
ANISOU 2561  O   ILE A 751     3549   2977   3867   -222    -99    259       O  
ATOM   2562  CB  ILE A 751     -18.441  -1.245  36.648  1.00 21.32           C  
ANISOU 2562  CB  ILE A 751     2815   2201   3085   -244   -123    208       C  
ATOM   2563  CG1 ILE A 751     -19.283  -2.279  37.396  1.00 19.08           C  
ANISOU 2563  CG1 ILE A 751     2553   1921   2775   -251   -108    181       C  
ATOM   2564  CG2 ILE A 751     -19.319  -0.104  36.165  1.00 19.93           C  
ANISOU 2564  CG2 ILE A 751     2630   2032   2912   -248   -141    190       C  
ATOM   2565  CD1 ILE A 751     -19.794  -1.792  38.733  1.00 19.64           C  
ANISOU 2565  CD1 ILE A 751     2625   1997   2840   -257   -132    161       C  
ATOM   2566  N   LEU A 752     -15.933  -0.312  35.022  1.00 32.27           N  
ANISOU 2566  N   LEU A 752     4156   3578   4527   -222   -125    294       N  
ATOM   2567  CA  LEU A 752     -15.234   0.746  34.299  1.00 34.84           C  
ANISOU 2567  CA  LEU A 752     4453   3903   4884   -217   -138    329       C  
ATOM   2568  C   LEU A 752     -14.724   0.261  32.945  1.00 34.41           C  
ANISOU 2568  C   LEU A 752     4393   3861   4821   -201   -105    357       C  
ATOM   2569  O   LEU A 752     -14.721   1.011  31.968  1.00 35.67           O  
ANISOU 2569  O   LEU A 752     4534   4029   4989   -196   -105    377       O  
ATOM   2570  CB  LEU A 752     -14.075   1.288  35.139  1.00 35.83           C  
ANISOU 2570  CB  LEU A 752     4557   4011   5045   -219   -166    356       C  
ATOM   2571  CG  LEU A 752     -13.318   2.493  34.581  1.00 37.18           C  
ANISOU 2571  CG  LEU A 752     4693   4175   5259   -218   -188    396       C  
ATOM   2572  CD1 LEU A 752     -14.268   3.651  34.331  1.00 37.51           C  
ANISOU 2572  CD1 LEU A 752     4729   4213   5308   -226   -212    378       C  
ATOM   2573  CD2 LEU A 752     -12.206   2.908  35.531  1.00 37.78           C  
ANISOU 2573  CD2 LEU A 752     4750   4232   5374   -222   -219    418       C  
ATOM   2574  N   ALA A 753     -14.296  -0.996  32.891  1.00 32.19           N  
ANISOU 2574  N   ALA A 753     4126   3582   4523   -191    -76    360       N  
ATOM   2575  CA  ALA A 753     -13.818  -1.584  31.646  1.00 30.31           C  
ANISOU 2575  CA  ALA A 753     3885   3359   4271   -170    -43    382       C  
ATOM   2576  C   ALA A 753     -14.974  -1.858  30.690  1.00 31.59           C  
ANISOU 2576  C   ALA A 753     4065   3536   4400   -166    -26    350       C  
ATOM   2577  O   ALA A 753     -14.861  -1.619  29.489  1.00 33.23           O  
ANISOU 2577  O   ALA A 753     4263   3762   4600   -151    -12    368       O  
ATOM   2578  CB  ALA A 753     -13.039  -2.860  31.922  1.00 29.28           C  
ANISOU 2578  CB  ALA A 753     3767   3224   4135   -158    -20    390       C  
ATOM   2579  N   CYS A 754     -16.081  -2.362  31.231  1.00 30.11           N  
ANISOU 2579  N   CYS A 754     3904   3345   4194   -180    -28    306       N  
ATOM   2580  CA  CYS A 754     -17.274  -2.635  30.434  1.00 28.86           C  
ANISOU 2580  CA  CYS A 754     3760   3198   4006   -180    -17    272       C  
ATOM   2581  C   CYS A 754     -17.794  -1.374  29.761  1.00 29.49           C  
ANISOU 2581  C   CYS A 754     3824   3291   4090   -181    -33    276       C  
ATOM   2582  O   CYS A 754     -18.069  -1.370  28.562  1.00 30.44           O  
ANISOU 2582  O   CYS A 754     3945   3430   4193   -168    -19    276       O  
ATOM   2583  CB  CYS A 754     -18.383  -3.230  31.300  1.00 28.25           C  
ANISOU 2583  CB  CYS A 754     3707   3112   3915   -199    -22    228       C  
ATOM   2584  SG  CYS A 754     -18.224  -4.983  31.672  1.00 56.59           S  
ANISOU 2584  SG  CYS A 754     7323   6689   7492   -196      4    215       S  
ATOM   2585  N   THR A 755     -17.933  -0.310  30.547  1.00 29.93           N  
ANISOU 2585  N   THR A 755     3866   3336   4169   -196    -64    278       N  
ATOM   2586  CA  THR A 755     -18.438   0.967  30.053  1.00 30.64           C  
ANISOU 2586  CA  THR A 755     3940   3433   4270   -199    -84    282       C  
ATOM   2587  C   THR A 755     -17.565   1.504  28.924  1.00 31.75           C  
ANISOU 2587  C   THR A 755     4056   3585   4423   -182    -75    329       C  
ATOM   2588  O   THR A 755     -18.071   2.053  27.944  1.00 32.31           O  
ANISOU 2588  O   THR A 755     4120   3672   4484   -175    -73    333       O  
ATOM   2589  CB  THR A 755     -18.506   2.017  31.182  1.00 29.51           C  
ANISOU 2589  CB  THR A 755     3785   3271   4156   -215   -121    278       C  
ATOM   2590  OG1 THR A 755     -19.338   1.531  32.243  1.00 29.06           O  
ANISOU 2590  OG1 THR A 755     3749   3209   4083   -228   -127    236       O  
ATOM   2591  CG2 THR A 755     -19.071   3.331  30.663  1.00 29.16           C  
ANISOU 2591  CG2 THR A 755     3725   3230   4126   -217   -143    281       C  
ATOM   2592  N   PHE A 756     -16.255   1.332  29.069  1.00 31.09           N  
ANISOU 2592  N   PHE A 756     3958   3495   4360   -174    -69    368       N  
ATOM   2593  CA  PHE A 756     -15.296   1.785  28.069  1.00 31.26           C  
ANISOU 2593  CA  PHE A 756     3952   3530   4395   -156    -57    421       C  
ATOM   2594  C   PHE A 756     -15.573   1.152  26.708  1.00 31.92           C  
ANISOU 2594  C   PHE A 756     4045   3643   4438   -133    -24    419       C  
ATOM   2595  O   PHE A 756     -15.628   1.847  25.694  1.00 33.11           O  
ANISOU 2595  O   PHE A 756     4180   3813   4587   -121    -20    444       O  
ATOM   2596  CB  PHE A 756     -13.868   1.469  28.522  1.00 32.47           C  
ANISOU 2596  CB  PHE A 756     4090   3673   4573   -151    -52    460       C  
ATOM   2597  CG  PHE A 756     -12.806   1.987  27.592  1.00 34.67           C  
ANISOU 2597  CG  PHE A 756     4335   3967   4872   -134    -41    521       C  
ATOM   2598  CD1 PHE A 756     -12.359   3.294  27.691  1.00 36.29           C  
ANISOU 2598  CD1 PHE A 756     4506   4160   5123   -144    -69    560       C  
ATOM   2599  CD2 PHE A 756     -12.249   1.165  26.625  1.00 37.02           C  
ANISOU 2599  CD2 PHE A 756     4633   4290   5143   -106     -3    541       C  
ATOM   2600  CE1 PHE A 756     -11.380   3.774  26.840  1.00 38.45           C  
ANISOU 2600  CE1 PHE A 756     4744   4447   5418   -130    -57    623       C  
ATOM   2601  CE2 PHE A 756     -11.270   1.639  25.770  1.00 39.05           C  
ANISOU 2601  CE2 PHE A 756     4857   4566   5417    -87     11    602       C  
ATOM   2602  CZ  PHE A 756     -10.835   2.945  25.878  1.00 39.53           C  
ANISOU 2602  CZ  PHE A 756     4880   4614   5525   -101    -16    646       C  
ATOM   2603  N   TYR A 757     -15.754  -0.164  26.692  1.00 31.47           N  
ANISOU 2603  N   TYR A 757     4016   3590   4350   -125     -1    389       N  
ATOM   2604  CA  TYR A 757     -16.007  -0.881  25.446  1.00 32.92           C  
ANISOU 2604  CA  TYR A 757     4213   3801   4495    -99     28    379       C  
ATOM   2605  C   TYR A 757     -17.453  -0.740  24.982  1.00 35.74           C  
ANISOU 2605  C   TYR A 757     4587   4168   4825   -106     21    336       C  
ATOM   2606  O   TYR A 757     -17.723  -0.702  23.782  1.00 38.62           O  
ANISOU 2606  O   TYR A 757     4951   4560   5163    -85     34    338       O  
ATOM   2607  CB  TYR A 757     -15.635  -2.360  25.580  1.00 32.48           C  
ANISOU 2607  CB  TYR A 757     4181   3740   4420    -87     52    361       C  
ATOM   2608  CG  TYR A 757     -14.162  -2.600  25.817  1.00 33.88           C  
ANISOU 2608  CG  TYR A 757     4341   3914   4618    -74     64    405       C  
ATOM   2609  CD1 TYR A 757     -13.224  -2.300  24.838  1.00 34.44           C  
ANISOU 2609  CD1 TYR A 757     4388   4010   4689    -46     82    453       C  
ATOM   2610  CD2 TYR A 757     -13.708  -3.132  27.017  1.00 34.99           C  
ANISOU 2610  CD2 TYR A 757     4488   4028   4777    -87     58    401       C  
ATOM   2611  CE1 TYR A 757     -11.876  -2.518  25.048  1.00 35.77           C  
ANISOU 2611  CE1 TYR A 757     4537   4176   4878    -33     94    496       C  
ATOM   2612  CE2 TYR A 757     -12.359  -3.354  27.237  1.00 35.96           C  
ANISOU 2612  CE2 TYR A 757     4594   4148   4920    -74     67    442       C  
ATOM   2613  CZ  TYR A 757     -11.448  -3.044  26.247  1.00 36.49           C  
ANISOU 2613  CZ  TYR A 757     4636   4239   4989    -48     85    489       C  
ATOM   2614  OH  TYR A 757     -10.106  -3.261  26.456  1.00 36.64           O  
ANISOU 2614  OH  TYR A 757     4635   4258   5030    -35     95    532       O  
ATOM   2615  N   ALA A 758     -18.380  -0.663  25.933  1.00 36.47           N  
ANISOU 2615  N   ALA A 758     4692   4241   4924   -132      0    298       N  
ATOM   2616  CA  ALA A 758     -19.797  -0.529  25.608  1.00 36.92           C  
ANISOU 2616  CA  ALA A 758     4762   4306   4959   -141     -8    257       C  
ATOM   2617  C   ALA A 758     -20.089   0.814  24.947  1.00 37.68           C  
ANISOU 2617  C   ALA A 758     4837   4417   5064   -138    -23    278       C  
ATOM   2618  O   ALA A 758     -20.907   0.900  24.031  1.00 38.95           O  
ANISOU 2618  O   ALA A 758     5003   4600   5199   -129    -20    261       O  
ATOM   2619  CB  ALA A 758     -20.652  -0.707  26.853  1.00 37.22           C  
ANISOU 2619  CB  ALA A 758     4815   4324   5004   -168    -25    218       C  
ATOM   2620  N   PHE A 759     -19.418   1.860  25.420  1.00 36.44           N  
ANISOU 2620  N   PHE A 759     4654   4247   4944   -146    -42    315       N  
ATOM   2621  CA  PHE A 759     -19.563   3.191  24.843  1.00 36.40           C  
ANISOU 2621  CA  PHE A 759     4625   4250   4956   -144    -58    343       C  
ATOM   2622  C   PHE A 759     -18.919   3.237  23.464  1.00 34.95           C  
ANISOU 2622  C   PHE A 759     4426   4096   4757   -115    -34    386       C  
ATOM   2623  O   PHE A 759     -19.335   4.001  22.595  1.00 33.99           O  
ANISOU 2623  O   PHE A 759     4291   3993   4629   -106    -38    401       O  
ATOM   2624  CB  PHE A 759     -18.929   4.242  25.759  1.00 38.64           C  
ANISOU 2624  CB  PHE A 759     4885   4507   5290   -160    -88    372       C  
ATOM   2625  CG  PHE A 759     -18.933   5.632  25.186  1.00 40.66           C  
ANISOU 2625  CG  PHE A 759     5113   4765   5573   -158   -106    408       C  
ATOM   2626  CD1 PHE A 759     -20.066   6.424  25.267  1.00 40.95           C  
ANISOU 2626  CD1 PHE A 759     5152   4797   5612   -169   -130    381       C  
ATOM   2627  CD2 PHE A 759     -17.801   6.150  24.576  1.00 41.95           C  
ANISOU 2627  CD2 PHE A 759     5246   4933   5761   -146   -100    471       C  
ATOM   2628  CE1 PHE A 759     -20.074   7.703  24.744  1.00 42.01           C  
ANISOU 2628  CE1 PHE A 759     5260   4929   5773   -167   -149    415       C  
ATOM   2629  CE2 PHE A 759     -17.803   7.429  24.051  1.00 42.46           C  
ANISOU 2629  CE2 PHE A 759     5282   4996   5854   -146   -118    509       C  
ATOM   2630  CZ  PHE A 759     -18.941   8.206  24.136  1.00 43.09           C  
ANISOU 2630  CZ  PHE A 759     5366   5068   5937   -156   -143    480       C  
ATOM   2631  N   LYS A 760     -17.897   2.410  23.275  1.00 35.01           N  
ANISOU 2631  N   LYS A 760     4434   4110   4757    -98     -9    407       N  
ATOM   2632  CA  LYS A 760     -17.183   2.338  22.009  1.00 36.19           C  
ANISOU 2632  CA  LYS A 760     4569   4293   4888    -66     18    449       C  
ATOM   2633  C   LYS A 760     -18.051   1.688  20.934  1.00 35.35           C  
ANISOU 2633  C   LYS A 760     4485   4218   4728    -44     36    413       C  
ATOM   2634  O   LYS A 760     -17.960   2.030  19.755  1.00 34.93           O  
ANISOU 2634  O   LYS A 760     4420   4199   4654    -18     49    441       O  
ATOM   2635  CB  LYS A 760     -15.883   1.549  22.192  1.00 38.42           C  
ANISOU 2635  CB  LYS A 760     4848   4575   5177    -52     41    476       C  
ATOM   2636  CG  LYS A 760     -14.994   1.486  20.963  1.00 42.60           C  
ANISOU 2636  CG  LYS A 760     5357   5140   5688    -14     71    525       C  
ATOM   2637  CD  LYS A 760     -13.706   0.731  21.265  1.00 46.32           C  
ANISOU 2637  CD  LYS A 760     5822   5607   6169     -1     91    551       C  
ATOM   2638  CE  LYS A 760     -12.796   0.662  20.046  1.00 47.64           C  
ANISOU 2638  CE  LYS A 760     5968   5817   6317     39    124    603       C  
ATOM   2639  NZ  LYS A 760     -11.544  -0.093  20.332  1.00 47.24           N  
ANISOU 2639  NZ  LYS A 760     5910   5763   6275     55    145    628       N  
ATOM   2640  N   THR A 761     -18.903   0.758  21.356  1.00 35.31           N  
ANISOU 2640  N   THR A 761     4512   4201   4702    -55     34    353       N  
ATOM   2641  CA  THR A 761     -19.724  -0.014  20.430  1.00 36.52           C  
ANISOU 2641  CA  THR A 761     4689   4378   4807    -37     47    312       C  
ATOM   2642  C   THR A 761     -21.208   0.322  20.550  1.00 37.45           C  
ANISOU 2642  C   THR A 761     4819   4493   4919    -57     24    267       C  
ATOM   2643  O   THR A 761     -22.063  -0.473  20.165  1.00 36.50           O  
ANISOU 2643  O   THR A 761     4722   4381   4766    -53     27    219       O  
ATOM   2644  CB  THR A 761     -19.540  -1.525  20.665  1.00 35.66           C  
ANISOU 2644  CB  THR A 761     4608   4260   4681    -30     64    277       C  
ATOM   2645  OG1 THR A 761     -19.925  -1.852  22.007  1.00 33.37           O  
ANISOU 2645  OG1 THR A 761     4331   3933   4414    -63     49    247       O  
ATOM   2646  CG2 THR A 761     -18.089  -1.920  20.455  1.00 36.67           C  
ANISOU 2646  CG2 THR A 761     4725   4395   4812     -4     88    319       C  
ATOM   2647  N   ARG A 762     -21.506   1.508  21.071  1.00 38.12           N  
ANISOU 2647  N   ARG A 762     4885   4565   5034    -78      0    282       N  
ATOM   2648  CA  ARG A 762     -22.881   1.898  21.367  1.00 38.50           C  
ANISOU 2648  CA  ARG A 762     4942   4608   5081    -99    -23    241       C  
ATOM   2649  C   ARG A 762     -23.771   1.986  20.129  1.00 40.99           C  
ANISOU 2649  C   ARG A 762     5260   4955   5358    -81    -21    224       C  
ATOM   2650  O   ARG A 762     -24.978   1.761  20.210  1.00 41.17           O  
ANISOU 2650  O   ARG A 762     5299   4978   5367    -93    -33    176       O  
ATOM   2651  CB  ARG A 762     -22.902   3.231  22.115  1.00 37.46           C  
ANISOU 2651  CB  ARG A 762     4787   4455   4990   -119    -51    263       C  
ATOM   2652  CG  ARG A 762     -22.380   4.395  21.302  1.00 37.69           C  
ANISOU 2652  CG  ARG A 762     4787   4500   5034   -104    -54    319       C  
ATOM   2653  CD  ARG A 762     -22.268   5.643  22.149  1.00 37.86           C  
ANISOU 2653  CD  ARG A 762     4787   4492   5105   -125    -85    339       C  
ATOM   2654  NE  ARG A 762     -21.795   6.779  21.367  1.00 39.18           N  
ANISOU 2654  NE  ARG A 762     4924   4669   5293   -113    -90    396       N  
ATOM   2655  CZ  ARG A 762     -20.518   7.012  21.089  1.00 41.00           C  
ANISOU 2655  CZ  ARG A 762     5132   4902   5545   -102    -79    455       C  
ATOM   2656  NH1 ARG A 762     -20.179   8.072  20.369  1.00 42.62           N  
ANISOU 2656  NH1 ARG A 762     5307   5116   5772    -93    -84    510       N  
ATOM   2657  NH2 ARG A 762     -19.578   6.186  21.528  1.00 41.54           N  
ANISOU 2657  NH2 ARG A 762     5204   4963   5616   -101    -62    462       N  
ATOM   2658  N   ASN A 763     -23.176   2.311  18.986  1.00 42.32           N  
ANISOU 2658  N   ASN A 763     5415   5155   5510    -51     -6    264       N  
ATOM   2659  CA  ASN A 763     -23.942   2.487  17.756  1.00 42.80           C  
ANISOU 2659  CA  ASN A 763     5478   5252   5533    -29     -5    253       C  
ATOM   2660  C   ASN A 763     -23.985   1.238  16.879  1.00 43.45           C  
ANISOU 2660  C   ASN A 763     5583   5359   5566     -1     15    222       C  
ATOM   2661  O   ASN A 763     -24.697   1.199  15.876  1.00 44.04           O  
ANISOU 2661  O   ASN A 763     5664   5465   5604     19     14    202       O  
ATOM   2662  CB  ASN A 763     -23.404   3.677  16.961  1.00 42.78           C  
ANISOU 2662  CB  ASN A 763     5444   5273   5538    -10     -4    317       C  
ATOM   2663  CG  ASN A 763     -23.586   4.990  17.693  1.00 42.49           C  
ANISOU 2663  CG  ASN A 763     5386   5210   5550    -37    -31    340       C  
ATOM   2664  OD1 ASN A 763     -24.625   5.230  18.308  1.00 40.91           O  
ANISOU 2664  OD1 ASN A 763     5194   4992   5359    -60    -54    300       O  
ATOM   2665  ND2 ASN A 763     -22.571   5.844  17.640  1.00 43.26           N  
ANISOU 2665  ND2 ASN A 763     5453   5302   5680    -33    -30    405       N  
ATOM   2666  N   VAL A 764     -23.221   0.221  17.265  1.00 43.47           N  
ANISOU 2666  N   VAL A 764     5599   5348   5570      3     32    216       N  
ATOM   2667  CA  VAL A 764     -23.190  -1.042  16.535  1.00 43.89           C  
ANISOU 2667  CA  VAL A 764     5676   5418   5582     31     50    182       C  
ATOM   2668  C   VAL A 764     -24.571  -1.699  16.507  1.00 45.86           C  
ANISOU 2668  C   VAL A 764     5951   5662   5812     17     34    113       C  
ATOM   2669  O   VAL A 764     -25.187  -1.897  17.556  1.00 43.23           O  
ANISOU 2669  O   VAL A 764     5625   5295   5505    -19     19     84       O  
ATOM   2670  CB  VAL A 764     -22.162  -2.010  17.149  1.00 42.41           C  
ANISOU 2670  CB  VAL A 764     5498   5208   5406     33     68    187       C  
ATOM   2671  CG1 VAL A 764     -22.221  -3.364  16.459  1.00 42.55           C  
ANISOU 2671  CG1 VAL A 764     5544   5238   5386     61     82    144       C  
ATOM   2672  CG2 VAL A 764     -20.763  -1.417  17.062  1.00 41.16           C  
ANISOU 2672  CG2 VAL A 764     5312   5060   5266     49     85    256       C  
ATOM   2673  N   PRO A 765     -25.062  -2.035  15.300  1.00 49.99           N  
ANISOU 2673  N   PRO A 765     6484   6219   6290     47     36     88       N  
ATOM   2674  CA  PRO A 765     -26.422  -2.553  15.120  1.00 51.82           C  
ANISOU 2674  CA  PRO A 765     6736   6449   6505     35     16     24       C  
ATOM   2675  C   PRO A 765     -26.523  -4.079  15.124  1.00 52.63           C  
ANISOU 2675  C   PRO A 765     6868   6534   6595     40     20    -28       C  
ATOM   2676  O   PRO A 765     -27.616  -4.606  14.918  1.00 52.86           O  
ANISOU 2676  O   PRO A 765     6913   6560   6613     31      3    -82       O  
ATOM   2677  CB  PRO A 765     -26.812  -2.007  13.743  1.00 52.59           C  
ANISOU 2677  CB  PRO A 765     6827   6596   6561     69     14     30       C  
ATOM   2678  CG  PRO A 765     -25.492  -1.784  13.014  1.00 52.70           C  
ANISOU 2678  CG  PRO A 765     6828   6641   6556    110     41     85       C  
ATOM   2679  CD  PRO A 765     -24.361  -1.925  14.009  1.00 51.37           C  
ANISOU 2679  CD  PRO A 765     6652   6440   6427     95     56    119       C  
ATOM   2680  N   ALA A 766     -25.412  -4.772  15.352  1.00 53.49           N  
ANISOU 2680  N   ALA A 766     6984   6631   6709     53     41    -13       N  
ATOM   2681  CA  ALA A 766     -25.425  -6.230  15.397  1.00 55.66           C  
ANISOU 2681  CA  ALA A 766     7287   6885   6978     59     44    -60       C  
ATOM   2682  C   ALA A 766     -26.334  -6.716  16.521  1.00 60.10           C  
ANISOU 2682  C   ALA A 766     7858   7402   7573     11     26    -97       C  
ATOM   2683  O   ALA A 766     -26.465  -6.050  17.548  1.00 62.02           O  
ANISOU 2683  O   ALA A 766     8087   7627   7850    -23     20    -76       O  
ATOM   2684  CB  ALA A 766     -24.017  -6.771  15.579  1.00 54.21           C  
ANISOU 2684  CB  ALA A 766     7104   6693   6799     80     70    -29       C  
ATOM   2685  N   ASN A 767     -26.969  -7.866  16.310  1.00 62.78           N  
ANISOU 2685  N   ASN A 767     8222   7727   7906     10     17   -153       N  
ATOM   2686  CA  ASN A 767     -27.854  -8.464  17.307  1.00 65.45           C  
ANISOU 2686  CA  ASN A 767     8568   8024   8276    -34      1   -188       C  
ATOM   2687  C   ASN A 767     -29.034  -7.588  17.718  1.00 66.31           C  
ANISOU 2687  C   ASN A 767     8662   8135   8398    -67    -19   -193       C  
ATOM   2688  O   ASN A 767     -29.293  -7.413  18.908  1.00 66.77           O  
ANISOU 2688  O   ASN A 767     8713   8168   8490   -104    -22   -185       O  
ATOM   2689  CB  ASN A 767     -27.064  -8.883  18.547  1.00 67.80           C  
ANISOU 2689  CB  ASN A 767     8868   8285   8610    -54     15   -163       C  
ATOM   2690  CG  ASN A 767     -26.482 -10.269  18.423  1.00 70.38           C  
ANISOU 2690  CG  ASN A 767     9218   8589   8936    -36     25   -185       C  
ATOM   2691  OD1 ASN A 767     -26.919 -11.196  19.104  1.00 71.64           O  
ANISOU 2691  OD1 ASN A 767     9390   8710   9120    -62     18   -213       O  
ATOM   2692  ND2 ASN A 767     -25.498 -10.425  17.544  1.00 70.31           N  
ANISOU 2692  ND2 ASN A 767     9213   8603   8899      9     42   -171       N  
ATOM   2693  N   PHE A 768     -29.747  -7.053  16.730  1.00 66.81           N  
ANISOU 2693  N   PHE A 768     8720   8232   8432    -53    -32   -208       N  
ATOM   2694  CA  PHE A 768     -30.980  -6.310  16.974  1.00 67.35           C  
ANISOU 2694  CA  PHE A 768     8775   8306   8510    -81    -53   -221       C  
ATOM   2695  C   PHE A 768     -30.734  -5.094  17.863  1.00 66.01           C  
ANISOU 2695  C   PHE A 768     8583   8134   8366   -100    -50   -175       C  
ATOM   2696  O   PHE A 768     -31.440  -4.892  18.852  1.00 65.53           O  
ANISOU 2696  O   PHE A 768     8515   8053   8332   -135    -61   -182       O  
ATOM   2697  CB  PHE A 768     -32.041  -7.215  17.618  1.00 69.44           C  
ANISOU 2697  CB  PHE A 768     9048   8537   8798   -116    -68   -268       C  
ATOM   2698  CG  PHE A 768     -32.305  -8.491  16.859  1.00 71.39           C  
ANISOU 2698  CG  PHE A 768     9319   8778   9031   -102    -76   -318       C  
ATOM   2699  CD1 PHE A 768     -33.438  -8.622  16.072  1.00 71.96           C  
ANISOU 2699  CD1 PHE A 768     9392   8864   9085   -100   -101   -362       C  
ATOM   2700  CD2 PHE A 768     -31.428  -9.564  16.943  1.00 72.08           C  
ANISOU 2700  CD2 PHE A 768     9425   8841   9122    -89    -62   -322       C  
ATOM   2701  CE1 PHE A 768     -33.684  -9.796  15.376  1.00 72.89           C  
ANISOU 2701  CE1 PHE A 768     9531   8972   9192    -87   -113   -412       C  
ATOM   2702  CE2 PHE A 768     -31.664 -10.732  16.246  1.00 72.79           C  
ANISOU 2702  CE2 PHE A 768     9537   8920   9201    -73    -73   -371       C  
ATOM   2703  CZ  PHE A 768     -32.795 -10.852  15.466  1.00 73.11           C  
ANISOU 2703  CZ  PHE A 768     9579   8973   9225    -73   -100   -418       C  
ATOM   2704  N   ASN A 769     -29.728  -4.298  17.506  1.00 65.37           N  
ANISOU 2704  N   ASN A 769     8489   8072   8276    -76    -37   -126       N  
ATOM   2705  CA  ASN A 769     -29.324  -3.128  18.291  1.00 63.42           C  
ANISOU 2705  CA  ASN A 769     8221   7820   8057    -90    -37    -80       C  
ATOM   2706  C   ASN A 769     -29.020  -3.439  19.755  1.00 60.74           C  
ANISOU 2706  C   ASN A 769     7883   7442   7754   -121    -34    -75       C  
ATOM   2707  O   ASN A 769     -29.326  -2.646  20.647  1.00 60.67           O  
ANISOU 2707  O   ASN A 769     7860   7422   7769   -145    -45    -63       O  
ATOM   2708  CB  ASN A 769     -30.364  -2.011  18.183  1.00 63.77           C  
ANISOU 2708  CB  ASN A 769     8248   7879   8102   -102    -58    -83       C  
ATOM   2709  CG  ASN A 769     -30.146  -1.131  16.972  1.00 65.10           C  
ANISOU 2709  CG  ASN A 769     8404   8087   8245    -69    -57    -54       C  
ATOM   2710  OD1 ASN A 769     -29.236  -1.364  16.178  1.00 65.71           O  
ANISOU 2710  OD1 ASN A 769     8484   8183   8299    -37    -39    -32       O  
ATOM   2711  ND2 ASN A 769     -30.984  -0.113  16.823  1.00 65.73           N  
ANISOU 2711  ND2 ASN A 769     8469   8180   8326    -76    -75    -52       N  
ATOM   2712  N   GLU A 770     -28.401  -4.593  19.981  1.00 57.76           N  
ANISOU 2712  N   GLU A 770     7523   7045   7379   -117    -19    -83       N  
ATOM   2713  CA  GLU A 770     -28.117  -5.098  21.320  1.00 55.57           C  
ANISOU 2713  CA  GLU A 770     7250   6732   7132   -144    -15    -80       C  
ATOM   2714  C   GLU A 770     -27.274  -4.146  22.165  1.00 56.14           C  
ANISOU 2714  C   GLU A 770     7303   6797   7228   -151    -13    -33       C  
ATOM   2715  O   GLU A 770     -27.556  -3.933  23.344  1.00 57.69           O  
ANISOU 2715  O   GLU A 770     7496   6975   7450   -178    -21    -33       O  
ATOM   2716  CB  GLU A 770     -27.403  -6.447  21.211  1.00 55.37           C  
ANISOU 2716  CB  GLU A 770     7245   6691   7103   -130      1    -91       C  
ATOM   2717  CG  GLU A 770     -26.910  -7.023  22.526  1.00 56.82           C  
ANISOU 2717  CG  GLU A 770     7433   6839   7316   -152      9    -80       C  
ATOM   2718  CD  GLU A 770     -25.975  -8.204  22.326  1.00 59.14           C  
ANISOU 2718  CD  GLU A 770     7745   7119   7608   -131     26    -80       C  
ATOM   2719  OE1 GLU A 770     -25.460  -8.372  21.200  1.00 60.40           O  
ANISOU 2719  OE1 GLU A 770     7909   7299   7741    -96     35    -80       O  
ATOM   2720  OE2 GLU A 770     -25.754  -8.964  23.292  1.00 59.14           O  
ANISOU 2720  OE2 GLU A 770     7753   7087   7629   -148     31    -81       O  
ATOM   2721  N   ALA A 771     -26.243  -3.576  21.551  1.00 55.33           N  
ANISOU 2721  N   ALA A 771     7190   6713   7120   -125     -3      7       N  
ATOM   2722  CA  ALA A 771     -25.238  -2.805  22.277  1.00 53.77           C  
ANISOU 2722  CA  ALA A 771     6975   6506   6950   -129     -2     55       C  
ATOM   2723  C   ALA A 771     -25.767  -1.499  22.869  1.00 51.87           C  
ANISOU 2723  C   ALA A 771     6715   6263   6730   -149    -24     65       C  
ATOM   2724  O   ALA A 771     -25.225  -0.997  23.855  1.00 52.73           O  
ANISOU 2724  O   ALA A 771     6813   6353   6867   -162    -31     88       O  
ATOM   2725  CB  ALA A 771     -24.040  -2.538  21.387  1.00 53.46           C  
ANISOU 2725  CB  ALA A 771     6924   6487   6901    -95     15     98       C  
ATOM   2726  N   LYS A 772     -26.815  -0.949  22.262  1.00 48.05           N  
ANISOU 2726  N   LYS A 772     6227   5797   6233   -149    -37     46       N  
ATOM   2727  CA  LYS A 772     -27.439   0.269  22.769  1.00 45.03           C  
ANISOU 2727  CA  LYS A 772     5828   5412   5868   -165    -59     51       C  
ATOM   2728  C   LYS A 772     -27.988   0.034  24.171  1.00 41.34           C  
ANISOU 2728  C   LYS A 772     5367   4920   5421   -195    -69     26       C  
ATOM   2729  O   LYS A 772     -27.881   0.893  25.048  1.00 40.56           O  
ANISOU 2729  O   LYS A 772     5255   4809   5347   -206    -84     39       O  
ATOM   2730  CB  LYS A 772     -28.568   0.724  21.842  1.00 47.42           C  
ANISOU 2730  CB  LYS A 772     6127   5739   6150   -159    -71     30       C  
ATOM   2731  CG  LYS A 772     -29.228   2.027  22.270  1.00 50.36           C  
ANISOU 2731  CG  LYS A 772     6482   6110   6542   -172    -94     34       C  
ATOM   2732  CD  LYS A 772     -30.581   2.221  21.598  1.00 52.30           C  
ANISOU 2732  CD  LYS A 772     6727   6376   6767   -171   -106      2       C  
ATOM   2733  CE  LYS A 772     -30.468   2.151  20.082  1.00 53.32           C  
ANISOU 2733  CE  LYS A 772     6858   6538   6865   -142    -98     11       C  
ATOM   2734  NZ  LYS A 772     -31.791   2.306  19.415  1.00 53.28           N  
ANISOU 2734  NZ  LYS A 772     6852   6553   6837   -141   -112    -22       N  
ATOM   2735  N   TYR A 773     -28.576  -1.141  24.372  1.00 38.46           N  
ANISOU 2735  N   TYR A 773     5020   4549   5045   -205    -61    -11       N  
ATOM   2736  CA  TYR A 773     -29.119  -1.521  25.668  1.00 37.65           C  
ANISOU 2736  CA  TYR A 773     4923   4427   4957   -231    -66    -32       C  
ATOM   2737  C   TYR A 773     -28.000  -1.838  26.654  1.00 35.73           C  
ANISOU 2737  C   TYR A 773     4682   4163   4732   -235    -57     -7       C  
ATOM   2738  O   TYR A 773     -28.124  -1.579  27.851  1.00 35.38           O  
ANISOU 2738  O   TYR A 773     4634   4106   4703   -251    -66     -7       O  
ATOM   2739  CB  TYR A 773     -30.052  -2.725  25.522  1.00 38.52           C  
ANISOU 2739  CB  TYR A 773     5048   4534   5054   -243    -60    -73       C  
ATOM   2740  CG  TYR A 773     -31.249  -2.469  24.634  1.00 40.66           C  
ANISOU 2740  CG  TYR A 773     5315   4825   5307   -241    -72   -101       C  
ATOM   2741  CD1 TYR A 773     -32.430  -1.956  25.157  1.00 41.90           C  
ANISOU 2741  CD1 TYR A 773     5462   4987   5470   -260    -87   -121       C  
ATOM   2742  CD2 TYR A 773     -31.199  -2.738  23.272  1.00 39.95           C  
ANISOU 2742  CD2 TYR A 773     5231   4753   5193   -219    -68   -108       C  
ATOM   2743  CE1 TYR A 773     -33.526  -1.719  24.348  1.00 42.23           C  
ANISOU 2743  CE1 TYR A 773     5499   5049   5498   -259    -99   -146       C  
ATOM   2744  CE2 TYR A 773     -32.289  -2.505  22.456  1.00 40.56           C  
ANISOU 2744  CE2 TYR A 773     5306   4852   5254   -217    -82   -135       C  
ATOM   2745  CZ  TYR A 773     -33.450  -1.995  22.998  1.00 41.65           C  
ANISOU 2745  CZ  TYR A 773     5433   4992   5402   -238    -97   -153       C  
ATOM   2746  OH  TYR A 773     -34.539  -1.762  22.190  1.00 41.27           O  
ANISOU 2746  OH  TYR A 773     5378   4965   5337   -235   -111   -179       O  
ATOM   2747  N   ILE A 774     -26.909  -2.400  26.143  1.00 33.20           N  
ANISOU 2747  N   ILE A 774     4368   3840   4408   -217    -41     14       N  
ATOM   2748  CA  ILE A 774     -25.753  -2.730  26.968  1.00 30.80           C  
ANISOU 2748  CA  ILE A 774     4064   3517   4120   -217    -32     40       C  
ATOM   2749  C   ILE A 774     -25.088  -1.470  27.514  1.00 31.68           C  
ANISOU 2749  C   ILE A 774     4156   3626   4256   -218    -48     74       C  
ATOM   2750  O   ILE A 774     -24.711  -1.411  28.685  1.00 33.13           O  
ANISOU 2750  O   ILE A 774     4338   3793   4457   -229    -54     82       O  
ATOM   2751  CB  ILE A 774     -24.715  -3.552  26.180  1.00 28.61           C  
ANISOU 2751  CB  ILE A 774     3795   3241   3833   -194    -11     56       C  
ATOM   2752  CG1 ILE A 774     -25.350  -4.838  25.647  1.00 27.75           C  
ANISOU 2752  CG1 ILE A 774     3709   3131   3705   -192      0     18       C  
ATOM   2753  CG2 ILE A 774     -23.502  -3.867  27.050  1.00 25.57           C  
ANISOU 2753  CG2 ILE A 774     3410   2838   3468   -193     -3     85       C  
ATOM   2754  CD1 ILE A 774     -24.373  -5.760  24.953  1.00 25.73           C  
ANISOU 2754  CD1 ILE A 774     3465   2874   3438   -166     21     27       C  
ATOM   2755  N   ALA A 775     -24.951  -0.461  26.659  1.00 30.53           N  
ANISOU 2755  N   ALA A 775     3995   3496   4111   -205    -55     95       N  
ATOM   2756  CA  ALA A 775     -24.337   0.800  27.056  1.00 29.07           C  
ANISOU 2756  CA  ALA A 775     3788   3304   3954   -205    -73    128       C  
ATOM   2757  C   ALA A 775     -25.168   1.517  28.116  1.00 31.11           C  
ANISOU 2757  C   ALA A 775     4042   3552   4225   -225    -98    106       C  
ATOM   2758  O   ALA A 775     -24.622   2.081  29.065  1.00 31.98           O  
ANISOU 2758  O   ALA A 775     4144   3647   4361   -231   -114    121       O  
ATOM   2759  CB  ALA A 775     -24.127   1.697  25.845  1.00 26.52           C  
ANISOU 2759  CB  ALA A 775     3448   3000   3630   -188    -75    157       C  
ATOM   2760  N   PHE A 776     -26.487   1.488  27.952  1.00 31.90           N  
ANISOU 2760  N   PHE A 776     4149   3664   4309   -232   -103     70       N  
ATOM   2761  CA  PHE A 776     -27.391   2.142  28.893  1.00 32.49           C  
ANISOU 2761  CA  PHE A 776     4219   3734   4392   -247   -124     47       C  
ATOM   2762  C   PHE A 776     -27.280   1.539  30.291  1.00 29.85           C  
ANISOU 2762  C   PHE A 776     3894   3386   4063   -260   -123     36       C  
ATOM   2763  O   PHE A 776     -27.303   2.258  31.291  1.00 29.63           O  
ANISOU 2763  O   PHE A 776     3859   3350   4049   -265   -143     34       O  
ATOM   2764  CB  PHE A 776     -28.837   2.062  28.401  1.00 35.17           C  
ANISOU 2764  CB  PHE A 776     4562   4091   4711   -252   -126     11       C  
ATOM   2765  CG  PHE A 776     -29.811   2.807  29.267  1.00 38.18           C  
ANISOU 2765  CG  PHE A 776     4936   4472   5099   -262   -146    -12       C  
ATOM   2766  CD1 PHE A 776     -29.929   4.183  29.169  1.00 40.02           C  
ANISOU 2766  CD1 PHE A 776     5153   4706   5349   -256   -170     -3       C  
ATOM   2767  CD2 PHE A 776     -30.608   2.133  30.179  1.00 39.80           C  
ANISOU 2767  CD2 PHE A 776     5149   4677   5294   -277   -142    -41       C  
ATOM   2768  CE1 PHE A 776     -30.822   4.875  29.964  1.00 41.73           C  
ANISOU 2768  CE1 PHE A 776     5363   4923   5570   -261   -190    -27       C  
ATOM   2769  CE2 PHE A 776     -31.504   2.820  30.978  1.00 41.78           C  
ANISOU 2769  CE2 PHE A 776     5392   4934   5549   -282   -159    -62       C  
ATOM   2770  CZ  PHE A 776     -31.611   4.193  30.869  1.00 42.74           C  
ANISOU 2770  CZ  PHE A 776     5499   5055   5684   -273   -183    -57       C  
ATOM   2771  N   THR A 777     -27.163   0.217  30.349  1.00 27.43           N  
ANISOU 2771  N   THR A 777     3604   3076   3743   -263   -100     28       N  
ATOM   2772  CA  THR A 777     -26.994  -0.489  31.611  1.00 27.52           C  
ANISOU 2772  CA  THR A 777     3624   3075   3757   -274    -95     23       C  
ATOM   2773  C   THR A 777     -25.718  -0.041  32.316  1.00 30.82           C  
ANISOU 2773  C   THR A 777     4034   3479   4196   -269   -105     54       C  
ATOM   2774  O   THR A 777     -25.713   0.192  33.526  1.00 32.60           O  
ANISOU 2774  O   THR A 777     4259   3699   4428   -275   -118     49       O  
ATOM   2775  CB  THR A 777     -26.937  -2.011  31.392  1.00 26.81           C  
ANISOU 2775  CB  THR A 777     3552   2980   3655   -277    -70     16       C  
ATOM   2776  OG1 THR A 777     -28.182  -2.459  30.844  1.00 26.57           O  
ANISOU 2776  OG1 THR A 777     3527   2959   3609   -285    -65    -16       O  
ATOM   2777  CG2 THR A 777     -26.679  -2.734  32.705  1.00 29.49           C  
ANISOU 2777  CG2 THR A 777     3900   3307   3999   -287    -64     18       C  
ATOM   2778  N   MET A 778     -24.640   0.090  31.550  1.00 30.96           N  
ANISOU 2778  N   MET A 778     4046   3493   4223   -255   -100     85       N  
ATOM   2779  CA  MET A 778     -23.356   0.474  32.118  1.00 30.07           C  
ANISOU 2779  CA  MET A 778     3924   3368   4135   -250   -109    118       C  
ATOM   2780  C   MET A 778     -23.323   1.932  32.562  1.00 33.11           C  
ANISOU 2780  C   MET A 778     4290   3747   4544   -252   -143    124       C  
ATOM   2781  O   MET A 778     -22.540   2.300  33.435  1.00 35.95           O  
ANISOU 2781  O   MET A 778     4643   4094   4925   -252   -160    139       O  
ATOM   2782  CB  MET A 778     -22.212   0.177  31.145  1.00 27.76           C  
ANISOU 2782  CB  MET A 778     3625   3075   3846   -235    -92    153       C  
ATOM   2783  CG  MET A 778     -22.071  -1.296  30.797  1.00 27.37           C  
ANISOU 2783  CG  MET A 778     3595   3027   3777   -230    -62    146       C  
ATOM   2784  SD  MET A 778     -22.251  -2.389  32.225  1.00 30.98           S  
ANISOU 2784  SD  MET A 778     4070   3469   4230   -244    -56    127       S  
ATOM   2785  CE  MET A 778     -20.935  -1.807  33.294  1.00 56.41           C  
ANISOU 2785  CE  MET A 778     7278   6677   7480   -242    -74    161       C  
ATOM   2786  N   TYR A 779     -24.174   2.760  31.966  1.00 34.53           N  
ANISOU 2786  N   TYR A 779     4463   3937   4722   -251   -154    112       N  
ATOM   2787  CA  TYR A 779     -24.279   4.155  32.381  1.00 35.96           C  
ANISOU 2787  CA  TYR A 779     4627   4108   4927   -252   -189    113       C  
ATOM   2788  C   TYR A 779     -24.884   4.250  33.777  1.00 35.66           C  
ANISOU 2788  C   TYR A 779     4597   4068   4886   -259   -205     81       C  
ATOM   2789  O   TYR A 779     -24.363   4.950  34.646  1.00 35.66           O  
ANISOU 2789  O   TYR A 779     4588   4053   4907   -258   -232     85       O  
ATOM   2790  CB  TYR A 779     -25.130   4.953  31.394  1.00 36.94           C  
ANISOU 2790  CB  TYR A 779     4743   4245   5049   -248   -196    107       C  
ATOM   2791  CG  TYR A 779     -24.524   5.088  30.018  1.00 38.95           C  
ANISOU 2791  CG  TYR A 779     4987   4507   5307   -237   -183    143       C  
ATOM   2792  CD1 TYR A 779     -23.148   5.060  29.836  1.00 39.63           C  
ANISOU 2792  CD1 TYR A 779     5061   4583   5413   -230   -178    186       C  
ATOM   2793  CD2 TYR A 779     -25.331   5.243  28.898  1.00 39.89           C  
ANISOU 2793  CD2 TYR A 779     5104   4644   5407   -231   -176    136       C  
ATOM   2794  CE1 TYR A 779     -22.592   5.185  28.577  1.00 41.60           C  
ANISOU 2794  CE1 TYR A 779     5299   4845   5663   -216   -163    223       C  
ATOM   2795  CE2 TYR A 779     -24.786   5.367  27.636  1.00 40.44           C  
ANISOU 2795  CE2 TYR A 779     5164   4726   5475   -216   -163    171       C  
ATOM   2796  CZ  TYR A 779     -23.416   5.337  27.481  1.00 42.60           C  
ANISOU 2796  CZ  TYR A 779     5426   4992   5767   -209   -155    215       C  
ATOM   2797  OH  TYR A 779     -22.871   5.460  26.225  1.00 43.84           O  
ANISOU 2797  OH  TYR A 779     5571   5167   5920   -191   -139    253       O  
ATOM   2798  N   THR A 780     -25.988   3.537  33.983  1.00 34.28           N  
ANISOU 2798  N   THR A 780     4436   3908   4683   -266   -190     49       N  
ATOM   2799  CA  THR A 780     -26.690   3.548  35.260  1.00 33.35           C  
ANISOU 2799  CA  THR A 780     4324   3795   4554   -270   -200     19       C  
ATOM   2800  C   THR A 780     -25.865   2.877  36.352  1.00 30.56           C  
ANISOU 2800  C   THR A 780     3978   3433   4200   -271   -196     29       C  
ATOM   2801  O   THR A 780     -25.793   3.367  37.479  1.00 29.11           O  
ANISOU 2801  O   THR A 780     3793   3247   4021   -267   -218     19       O  
ATOM   2802  CB  THR A 780     -28.054   2.837  35.160  1.00 33.78           C  
ANISOU 2802  CB  THR A 780     4387   3868   4580   -279   -181    -11       C  
ATOM   2803  OG1 THR A 780     -28.830   3.427  34.109  1.00 35.32           O  
ANISOU 2803  OG1 THR A 780     4575   4072   4774   -277   -186    -20       O  
ATOM   2804  CG2 THR A 780     -28.815   2.953  36.471  1.00 32.98           C  
ANISOU 2804  CG2 THR A 780     4287   3777   4467   -280   -191    -37       C  
ATOM   2805  N   THR A 781     -25.244   1.754  36.004  1.00 29.07           N  
ANISOU 2805  N   THR A 781     3799   3241   4007   -273   -170     47       N  
ATOM   2806  CA  THR A 781     -24.434   0.984  36.944  1.00 28.32           C  
ANISOU 2806  CA  THR A 781     3711   3138   3910   -274   -163     60       C  
ATOM   2807  C   THR A 781     -23.273   1.803  37.509  1.00 29.11           C  
ANISOU 2807  C   THR A 781     3799   3224   4037   -266   -190     81       C  
ATOM   2808  O   THR A 781     -22.902   1.651  38.675  1.00 31.41           O  
ANISOU 2808  O   THR A 781     4094   3513   4327   -264   -200     79       O  
ATOM   2809  CB  THR A 781     -23.884  -0.296  36.285  1.00 26.44           C  
ANISOU 2809  CB  THR A 781     3484   2895   3666   -274   -130     78       C  
ATOM   2810  OG1 THR A 781     -24.975  -1.105  35.830  1.00 26.60           O  
ANISOU 2810  OG1 THR A 781     3515   2925   3666   -283   -109     55       O  
ATOM   2811  CG2 THR A 781     -23.053  -1.093  37.272  1.00 24.65           C  
ANISOU 2811  CG2 THR A 781     3265   2660   3440   -273   -124     93       C  
ATOM   2812  N   CYS A 782     -22.705   2.673  36.681  1.00 26.50           N  
ANISOU 2812  N   CYS A 782     3454   2884   3732   -261   -204    101       N  
ATOM   2813  CA  CYS A 782     -21.648   3.566  37.137  1.00 24.87           C  
ANISOU 2813  CA  CYS A 782     3232   2660   3559   -257   -235    122       C  
ATOM   2814  C   CYS A 782     -22.198   4.563  38.148  1.00 26.99           C  
ANISOU 2814  C   CYS A 782     3496   2926   3831   -254   -272     93       C  
ATOM   2815  O   CYS A 782     -21.564   4.840  39.165  1.00 29.10           O  
ANISOU 2815  O   CYS A 782     3761   3185   4111   -250   -297     93       O  
ATOM   2816  CB  CYS A 782     -21.002   4.296  35.960  1.00 22.23           C  
ANISOU 2816  CB  CYS A 782     2877   2316   3252   -253   -241    155       C  
ATOM   2817  SG  CYS A 782     -19.931   3.253  34.948  1.00 29.60           S  
ANISOU 2817  SG  CYS A 782     3810   3252   4184   -248   -203    196       S  
ATOM   2818  N   ILE A 783     -23.384   5.094  37.866  1.00 27.32           N  
ANISOU 2818  N   ILE A 783     3539   2978   3863   -255   -277     66       N  
ATOM   2819  CA  ILE A 783     -24.061   5.985  38.800  1.00 25.86           C  
ANISOU 2819  CA  ILE A 783     3353   2796   3678   -249   -309     33       C  
ATOM   2820  C   ILE A 783     -24.401   5.234  40.082  1.00 25.00           C  
ANISOU 2820  C   ILE A 783     3259   2703   3538   -247   -301     11       C  
ATOM   2821  O   ILE A 783     -24.185   5.739  41.183  1.00 26.10           O  
ANISOU 2821  O   ILE A 783     3398   2840   3680   -237   -330     -4       O  
ATOM   2822  CB  ILE A 783     -25.349   6.570  38.194  1.00 23.89           C  
ANISOU 2822  CB  ILE A 783     3100   2557   3419   -249   -311      9       C  
ATOM   2823  CG1 ILE A 783     -25.029   7.344  36.913  1.00 24.36           C  
ANISOU 2823  CG1 ILE A 783     3145   2604   3509   -249   -319     35       C  
ATOM   2824  CG2 ILE A 783     -26.052   7.468  39.201  1.00 21.27           C  
ANISOU 2824  CG2 ILE A 783     2768   2229   3085   -239   -343    -28       C  
ATOM   2825  CD1 ILE A 783     -26.251   7.893  36.210  1.00 25.46           C  
ANISOU 2825  CD1 ILE A 783     3280   2754   3639   -248   -320     15       C  
ATOM   2826  N   ILE A 784     -24.925   4.021  39.927  1.00 23.62           N  
ANISOU 2826  N   ILE A 784     3096   2544   3333   -254   -263      9       N  
ATOM   2827  CA  ILE A 784     -25.265   3.165  41.061  1.00 22.44           C  
ANISOU 2827  CA  ILE A 784     2960   2411   3155   -253   -249     -4       C  
ATOM   2828  C   ILE A 784     -24.046   2.874  41.932  1.00 22.79           C  
ANISOU 2828  C   ILE A 784     3008   2446   3207   -247   -259     15       C  
ATOM   2829  O   ILE A 784     -24.106   2.991  43.156  1.00 23.00           O  
ANISOU 2829  O   ILE A 784     3038   2483   3219   -238   -274      0       O  
ATOM   2830  CB  ILE A 784     -25.900   1.841  40.590  1.00 21.92           C  
ANISOU 2830  CB  ILE A 784     2905   2356   3066   -266   -207     -1       C  
ATOM   2831  CG1 ILE A 784     -27.310   2.099  40.048  1.00 22.78           C  
ANISOU 2831  CG1 ILE A 784     3011   2481   3163   -271   -201    -27       C  
ATOM   2832  CG2 ILE A 784     -25.943   0.828  41.724  1.00 20.66           C  
ANISOU 2832  CG2 ILE A 784     2757   2209   2884   -266   -190      0       C  
ATOM   2833  CD1 ILE A 784     -28.023   0.856  39.564  1.00 21.77           C  
ANISOU 2833  CD1 ILE A 784     2892   2362   3018   -284   -165    -29       C  
ATOM   2834  N   TRP A 785     -22.941   2.507  41.291  1.00 21.83           N  
ANISOU 2834  N   TRP A 785     2883   2307   3106   -251   -250     48       N  
ATOM   2835  CA  TRP A 785     -21.697   2.232  41.998  1.00 19.98           C  
ANISOU 2835  CA  TRP A 785     2648   2063   2883   -246   -259     70       C  
ATOM   2836  C   TRP A 785     -21.174   3.484  42.697  1.00 21.76           C  
ANISOU 2836  C   TRP A 785     2861   2277   3131   -236   -308     62       C  
ATOM   2837  O   TRP A 785     -20.804   3.441  43.872  1.00 20.60           O  
ANISOU 2837  O   TRP A 785     2719   2134   2976   -227   -325     55       O  
ATOM   2838  CB  TRP A 785     -20.642   1.696  41.030  1.00 18.23           C  
ANISOU 2838  CB  TRP A 785     2421   1824   2680   -250   -240    108       C  
ATOM   2839  CG  TRP A 785     -19.416   1.169  41.707  1.00 16.52           C  
ANISOU 2839  CG  TRP A 785     2204   1600   2472   -245   -243    132       C  
ATOM   2840  CD1 TRP A 785     -19.167  -0.127  42.057  1.00 15.49           C  
ANISOU 2840  CD1 TRP A 785     2087   1474   2324   -246   -214    144       C  
ATOM   2841  CD2 TRP A 785     -18.268   1.920  42.118  1.00 16.90           C  
ANISOU 2841  CD2 TRP A 785     2238   1633   2552   -239   -277    149       C  
ATOM   2842  NE1 TRP A 785     -17.936  -0.228  42.658  1.00 16.98           N  
ANISOU 2842  NE1 TRP A 785     2271   1653   2528   -239   -228    167       N  
ATOM   2843  CE2 TRP A 785     -17.363   1.020  42.708  1.00 17.70           C  
ANISOU 2843  CE2 TRP A 785     2344   1733   2650   -235   -267    170       C  
ATOM   2844  CE3 TRP A 785     -17.917   3.274  42.042  1.00 18.47           C  
ANISOU 2844  CE3 TRP A 785     2417   1816   2785   -237   -318    149       C  
ATOM   2845  CZ2 TRP A 785     -16.132   1.419  43.222  1.00 19.70           C  
ANISOU 2845  CZ2 TRP A 785     2583   1972   2930   -229   -296    190       C  
ATOM   2846  CZ3 TRP A 785     -16.694   3.672  42.552  1.00 20.16           C  
ANISOU 2846  CZ3 TRP A 785     2617   2014   3029   -233   -349    169       C  
ATOM   2847  CH2 TRP A 785     -15.816   2.748  43.135  1.00 20.12           C  
ANISOU 2847  CH2 TRP A 785     2616   2010   3018   -229   -337    188       C  
ATOM   2848  N   LEU A 786     -21.141   4.594  41.966  1.00 24.57           N  
ANISOU 2848  N   LEU A 786     3201   2617   3516   -237   -331     63       N  
ATOM   2849  CA  LEU A 786     -20.651   5.857  42.509  1.00 26.85           C  
ANISOU 2849  CA  LEU A 786     3477   2888   3835   -229   -381     55       C  
ATOM   2850  C   LEU A 786     -21.507   6.326  43.678  1.00 29.24           C  
ANISOU 2850  C   LEU A 786     3788   3206   4114   -216   -405     10       C  
ATOM   2851  O   LEU A 786     -20.986   6.819  44.676  1.00 30.53           O  
ANISOU 2851  O   LEU A 786     3951   3364   4286   -204   -442     -2       O  
ATOM   2852  CB  LEU A 786     -20.598   6.938  41.426  1.00 25.96           C  
ANISOU 2852  CB  LEU A 786     3346   2755   3761   -234   -399     67       C  
ATOM   2853  CG  LEU A 786     -19.420   6.885  40.451  1.00 26.43           C  
ANISOU 2853  CG  LEU A 786     3388   2797   3856   -241   -391    116       C  
ATOM   2854  CD1 LEU A 786     -19.542   7.972  39.393  1.00 26.81           C  
ANISOU 2854  CD1 LEU A 786     3418   2831   3939   -244   -406    130       C  
ATOM   2855  CD2 LEU A 786     -18.099   7.007  41.199  1.00 26.69           C  
ANISOU 2855  CD2 LEU A 786     3411   2812   3917   -238   -418    135       C  
ATOM   2856  N   ALA A 787     -22.819   6.167  43.550  1.00 29.47           N  
ANISOU 2856  N   ALA A 787     3827   3258   4114   -216   -385    -15       N  
ATOM   2857  CA  ALA A 787     -23.740   6.561  44.609  1.00 30.24           C  
ANISOU 2857  CA  ALA A 787     3931   3376   4183   -200   -402    -56       C  
ATOM   2858  C   ALA A 787     -23.633   5.621  45.804  1.00 30.32           C  
ANISOU 2858  C   ALA A 787     3955   3410   4157   -192   -388    -59       C  
ATOM   2859  O   ALA A 787     -23.878   6.021  46.939  1.00 29.97           O  
ANISOU 2859  O   ALA A 787     3914   3380   4092   -173   -412    -87       O  
ATOM   2860  CB  ALA A 787     -25.171   6.596  44.088  1.00 29.54           C  
ANISOU 2860  CB  ALA A 787     3844   3306   4073   -203   -381    -78       C  
ATOM   2861  N   PHE A 788     -23.263   4.372  45.541  1.00 31.56           N  
ANISOU 2861  N   PHE A 788     4118   3569   4304   -204   -350    -29       N  
ATOM   2862  CA  PHE A 788     -23.170   3.359  46.587  1.00 32.35           C  
ANISOU 2862  CA  PHE A 788     4230   3690   4370   -198   -331    -25       C  
ATOM   2863  C   PHE A 788     -22.153   3.719  47.667  1.00 34.43           C  
ANISOU 2863  C   PHE A 788     4493   3949   4639   -182   -368    -25       C  
ATOM   2864  O   PHE A 788     -22.389   3.479  48.850  1.00 36.44           O  
ANISOU 2864  O   PHE A 788     4757   4230   4860   -166   -371    -40       O  
ATOM   2865  CB  PHE A 788     -22.827   1.992  45.984  1.00 32.22           C  
ANISOU 2865  CB  PHE A 788     4221   3670   4353   -215   -287     10       C  
ATOM   2866  CG  PHE A 788     -22.590   0.918  47.010  1.00 34.25           C  
ANISOU 2866  CG  PHE A 788     4489   3942   4581   -210   -269     22       C  
ATOM   2867  CD1 PHE A 788     -23.649   0.197  47.534  1.00 35.43           C  
ANISOU 2867  CD1 PHE A 788     4647   4120   4695   -210   -241     14       C  
ATOM   2868  CD2 PHE A 788     -21.305   0.627  47.446  1.00 36.32           C  
ANISOU 2868  CD2 PHE A 788     4751   4193   4856   -205   -279     46       C  
ATOM   2869  CE1 PHE A 788     -23.434  -0.792  48.478  1.00 37.40           C  
ANISOU 2869  CE1 PHE A 788     4905   4385   4921   -205   -223     31       C  
ATOM   2870  CE2 PHE A 788     -21.084  -0.359  48.391  1.00 37.53           C  
ANISOU 2870  CE2 PHE A 788     4914   4362   4983   -198   -263     60       C  
ATOM   2871  CZ  PHE A 788     -22.149  -1.070  48.906  1.00 38.11           C  
ANISOU 2871  CZ  PHE A 788     4997   4463   5021   -198   -234     54       C  
ATOM   2872  N   VAL A 789     -21.024   4.290  47.257  1.00 33.82           N  
ANISOU 2872  N   VAL A 789     4405   3842   4604   -186   -395     -8       N  
ATOM   2873  CA  VAL A 789     -19.932   4.575  48.187  1.00 33.51           C  
ANISOU 2873  CA  VAL A 789     4362   3794   4576   -173   -432     -5       C  
ATOM   2874  C   VAL A 789     -20.300   5.535  49.333  1.00 33.69           C  
ANISOU 2874  C   VAL A 789     4387   3829   4585   -149   -478    -49       C  
ATOM   2875  O   VAL A 789     -20.151   5.172  50.501  1.00 34.06           O  
ANISOU 2875  O   VAL A 789     4443   3898   4600   -132   -485    -58       O  
ATOM   2876  CB  VAL A 789     -18.639   5.033  47.454  1.00 17.12           C  
ANISOU 2876  CB  VAL A 789     2269   1682   2556   -183   -454     26       C  
ATOM   2877  CG1 VAL A 789     -17.568   5.436  48.457  1.00 14.69           C  
ANISOU 2877  CG1 VAL A 789     1955   1364   2263   -171   -499     24       C  
ATOM   2878  CG2 VAL A 789     -18.132   3.931  46.531  1.00 16.29           C  
ANISOU 2878  CG2 VAL A 789     2163   1570   2456   -199   -408     69       C  
ATOM   2879  N   PRO A 790     -20.791   6.750  49.019  1.00 33.03           N  
ANISOU 2879  N   PRO A 790     4295   3732   4522   -145   -509    -76       N  
ATOM   2880  CA  PRO A 790     -21.101   7.633  50.150  1.00 34.31           C  
ANISOU 2880  CA  PRO A 790     4462   3906   4670   -118   -555   -122       C  
ATOM   2881  C   PRO A 790     -22.344   7.187  50.920  1.00 35.96           C  
ANISOU 2881  C   PRO A 790     4685   4161   4818   -101   -530   -149       C  
ATOM   2882  O   PRO A 790     -22.424   7.409  52.129  1.00 37.93           O  
ANISOU 2882  O   PRO A 790     4941   4433   5036    -74   -554   -178       O  
ATOM   2883  CB  PRO A 790     -21.349   8.986  49.477  1.00 32.53           C  
ANISOU 2883  CB  PRO A 790     4223   3650   4486   -120   -592   -141       C  
ATOM   2884  CG  PRO A 790     -21.825   8.641  48.116  1.00 30.58           C  
ANISOU 2884  CG  PRO A 790     3972   3398   4250   -144   -549   -115       C  
ATOM   2885  CD  PRO A 790     -21.083   7.396  47.726  1.00 30.97           C  
ANISOU 2885  CD  PRO A 790     4023   3448   4297   -161   -508    -70       C  
ATOM   2886  N   ILE A 791     -23.292   6.561  50.228  1.00 34.50           N  
ANISOU 2886  N   ILE A 791     4502   3991   4614   -116   -482   -140       N  
ATOM   2887  CA  ILE A 791     -24.532   6.113  50.853  1.00 31.90           C  
ANISOU 2887  CA  ILE A 791     4182   3706   4233   -103   -454   -160       C  
ATOM   2888  C   ILE A 791     -24.302   4.967  51.836  1.00 31.44           C  
ANISOU 2888  C   ILE A 791     4134   3678   4134    -95   -428   -142       C  
ATOM   2889  O   ILE A 791     -24.675   5.062  53.004  1.00 33.19           O  
ANISOU 2889  O   ILE A 791     4362   3934   4315    -68   -438   -165       O  
ATOM   2890  CB  ILE A 791     -25.578   5.686  49.800  1.00 27.75           C  
ANISOU 2890  CB  ILE A 791     3653   3185   3704   -124   -410   -151       C  
ATOM   2891  CG1 ILE A 791     -26.065   6.903  49.014  1.00 26.57           C  
ANISOU 2891  CG1 ILE A 791     3495   3017   3585   -124   -436   -175       C  
ATOM   2892  CG2 ILE A 791     -26.755   4.989  50.464  1.00 27.42           C  
ANISOU 2892  CG2 ILE A 791     3617   3189   3610   -115   -375   -161       C  
ATOM   2893  CD1 ILE A 791     -27.020   6.563  47.889  1.00 26.53           C  
ANISOU 2893  CD1 ILE A 791     3485   3015   3580   -144   -399   -167       C  
ATOM   2894  N   TYR A 792     -23.683   3.891  51.361  1.00 29.83           N  
ANISOU 2894  N   TYR A 792     3933   3462   3941   -117   -395   -100       N  
ATOM   2895  CA  TYR A 792     -23.461   2.709  52.188  1.00 30.35           C  
ANISOU 2895  CA  TYR A 792     4008   3553   3973   -112   -367    -77       C  
ATOM   2896  C   TYR A 792     -22.541   2.968  53.383  1.00 34.61           C  
ANISOU 2896  C   TYR A 792     4551   4100   4500    -87   -405    -83       C  
ATOM   2897  O   TYR A 792     -22.816   2.508  54.492  1.00 38.03           O  
ANISOU 2897  O   TYR A 792     4991   4570   4887    -67   -396    -86       O  
ATOM   2898  CB  TYR A 792     -22.915   1.550  51.349  1.00 27.20           C  
ANISOU 2898  CB  TYR A 792     3610   3132   3593   -140   -328    -32       C  
ATOM   2899  CG  TYR A 792     -22.569   0.324  52.163  1.00 26.12           C  
ANISOU 2899  CG  TYR A 792     3482   3014   3428   -136   -302     -4       C  
ATOM   2900  CD1 TYR A 792     -23.561  -0.545  52.600  1.00 26.80           C  
ANISOU 2900  CD1 TYR A 792     3574   3133   3477   -136   -263      3       C  
ATOM   2901  CD2 TYR A 792     -21.252   0.035  52.496  1.00 24.99           C  
ANISOU 2901  CD2 TYR A 792     3340   2856   3299   -132   -317     20       C  
ATOM   2902  CE1 TYR A 792     -23.250  -1.666  53.347  1.00 26.89           C  
ANISOU 2902  CE1 TYR A 792     3592   3160   3466   -132   -239     34       C  
ATOM   2903  CE2 TYR A 792     -20.932  -1.083  53.243  1.00 24.78           C  
ANISOU 2903  CE2 TYR A 792     3322   2846   3248   -127   -293     48       C  
ATOM   2904  CZ  TYR A 792     -21.934  -1.930  53.666  1.00 26.26           C  
ANISOU 2904  CZ  TYR A 792     3515   3063   3398   -127   -254     55       C  
ATOM   2905  OH  TYR A 792     -21.619  -3.045  54.410  1.00 26.94           O  
ANISOU 2905  OH  TYR A 792     3609   3166   3463   -122   -231     88       O  
ATOM   2906  N   PHE A 793     -21.454   3.699  53.160  1.00 33.25           N  
ANISOU 2906  N   PHE A 793     4371   3893   4369    -88   -447    -84       N  
ATOM   2907  CA  PHE A 793     -20.464   3.920  54.212  1.00 33.10           C  
ANISOU 2907  CA  PHE A 793     4353   3876   4345    -67   -487    -89       C  
ATOM   2908  C   PHE A 793     -20.876   4.991  55.222  1.00 35.72           C  
ANISOU 2908  C   PHE A 793     4689   4230   4655    -33   -534   -141       C  
ATOM   2909  O   PHE A 793     -20.254   5.134  56.275  1.00 39.74           O  
ANISOU 2909  O   PHE A 793     5202   4751   5147     -9   -568   -153       O  
ATOM   2910  CB  PHE A 793     -19.088   4.232  53.615  1.00 30.43           C  
ANISOU 2910  CB  PHE A 793     4003   3493   4064    -82   -515    -67       C  
ATOM   2911  CG  PHE A 793     -18.415   3.037  52.998  1.00 26.73           C  
ANISOU 2911  CG  PHE A 793     3534   3012   3608   -104   -473    -16       C  
ATOM   2912  CD1 PHE A 793     -17.939   2.010  53.795  1.00 23.52           C  
ANISOU 2912  CD1 PHE A 793     3137   2626   3174    -95   -456      7       C  
ATOM   2913  CD2 PHE A 793     -18.261   2.939  51.624  1.00 26.71           C  
ANISOU 2913  CD2 PHE A 793     3523   2980   3645   -130   -451      8       C  
ATOM   2914  CE1 PHE A 793     -17.324   0.906  53.236  1.00 23.43           C  
ANISOU 2914  CE1 PHE A 793     3126   2601   3177   -113   -419     52       C  
ATOM   2915  CE2 PHE A 793     -17.645   1.836  51.056  1.00 24.34           C  
ANISOU 2915  CE2 PHE A 793     3223   2670   3354   -146   -414     51       C  
ATOM   2916  CZ  PHE A 793     -17.176   0.819  51.864  1.00 24.36           C  
ANISOU 2916  CZ  PHE A 793     3235   2688   3332   -138   -398     72       C  
ATOM   2917  N   GLY A 794     -21.928   5.736  54.902  1.00 34.54           N  
ANISOU 2917  N   GLY A 794     4538   4084   4503    -29   -538   -173       N  
ATOM   2918  CA  GLY A 794     -22.454   6.730  55.818  1.00 35.60           C  
ANISOU 2918  CA  GLY A 794     4675   4240   4611      7   -580   -226       C  
ATOM   2919  C   GLY A 794     -23.766   6.279  56.431  1.00 36.55           C  
ANISOU 2919  C   GLY A 794     4803   4416   4669     26   -543   -239       C  
ATOM   2920  O   GLY A 794     -24.415   7.029  57.162  1.00 38.94           O  
ANISOU 2920  O   GLY A 794     5108   4744   4941     59   -568   -284       O  
ATOM   2921  N   SER A 795     -24.149   5.040  56.137  1.00 33.73           N  
ANISOU 2921  N   SER A 795     4447   4075   4293      6   -483   -200       N  
ATOM   2922  CA  SER A 795     -25.452   4.521  56.534  1.00 31.62           C  
ANISOU 2922  CA  SER A 795     4182   3857   3975     16   -441   -203       C  
ATOM   2923  C   SER A 795     -25.434   3.790  57.870  1.00 30.43           C  
ANISOU 2923  C   SER A 795     4040   3756   3767     43   -427   -193       C  
ATOM   2924  O   SER A 795     -24.464   3.114  58.213  1.00 28.41           O  
ANISOU 2924  O   SER A 795     3789   3495   3512     40   -425   -163       O  
ATOM   2925  CB  SER A 795     -25.998   3.586  55.457  1.00 31.15           C  
ANISOU 2925  CB  SER A 795     4118   3787   3930    -22   -385   -167       C  
ATOM   2926  OG  SER A 795     -27.202   2.974  55.883  1.00 32.83           O  
ANISOU 2926  OG  SER A 795     4330   4046   4098    -15   -344   -163       O  
ATOM   2927  N   ASN A 796     -26.524   3.929  58.616  1.00 31.29           N  
ANISOU 2927  N   ASN A 796     4148   3915   3824     72   -415   -215       N  
ATOM   2928  CA  ASN A 796     -26.721   3.169  59.842  1.00 31.63           C  
ANISOU 2928  CA  ASN A 796     4196   4014   3806     98   -392   -200       C  
ATOM   2929  C   ASN A 796     -27.680   2.015  59.608  1.00 29.95           C  
ANISOU 2929  C   ASN A 796     3976   3827   3575     77   -325   -159       C  
ATOM   2930  O   ASN A 796     -28.156   1.383  60.550  1.00 29.90           O  
ANISOU 2930  O   ASN A 796     3970   3873   3518     98   -297   -142       O  
ATOM   2931  CB  ASN A 796     -27.245   4.070  60.956  1.00 32.97           C  
ANISOU 2931  CB  ASN A 796     4369   4232   3927    151   -424   -250       C  
ATOM   2932  CG  ASN A 796     -26.192   5.022  61.468  1.00 35.77           C  
ANISOU 2932  CG  ASN A 796     4732   4567   4292    177   -493   -288       C  
ATOM   2933  OD1 ASN A 796     -25.031   4.647  61.636  1.00 35.30           O  
ANISOU 2933  OD1 ASN A 796     4677   4487   4249    169   -508   -265       O  
ATOM   2934  ND2 ASN A 796     -26.586   6.265  61.709  1.00 38.31           N  
ANISOU 2934  ND2 ASN A 796     5054   4892   4610    208   -537   -346       N  
ATOM   2935  N   TYR A 797     -27.967   1.754  58.339  1.00 27.91           N  
ANISOU 2935  N   TYR A 797     3712   3531   3361     36   -302   -144       N  
ATOM   2936  CA  TYR A 797     -28.825   0.645  57.953  1.00 26.68           C  
ANISOU 2936  CA  TYR A 797     3549   3389   3200     10   -243   -106       C  
ATOM   2937  C   TYR A 797     -28.182  -0.059  56.768  1.00 27.15           C  
ANISOU 2937  C   TYR A 797     3610   3394   3312    -34   -226    -73       C  
ATOM   2938  O   TYR A 797     -28.713  -0.047  55.660  1.00 24.86           O  
ANISOU 2938  O   TYR A 797     3314   3080   3052    -62   -212    -74       O  
ATOM   2939  CB  TYR A 797     -30.217   1.154  57.583  1.00 24.69           C  
ANISOU 2939  CB  TYR A 797     3285   3156   2940     11   -230   -132       C  
ATOM   2940  CG  TYR A 797     -30.834   2.040  58.641  1.00 24.71           C  
ANISOU 2940  CG  TYR A 797     3286   3210   2894     59   -252   -173       C  
ATOM   2941  CD1 TYR A 797     -31.511   1.494  59.723  1.00 25.07           C  
ANISOU 2941  CD1 TYR A 797     3327   3318   2882     85   -222   -158       C  
ATOM   2942  CD2 TYR A 797     -30.735   3.424  58.559  1.00 23.96           C  
ANISOU 2942  CD2 TYR A 797     3193   3100   2810     81   -304   -225       C  
ATOM   2943  CE1 TYR A 797     -32.074   2.300  60.695  1.00 25.40           C  
ANISOU 2943  CE1 TYR A 797     3366   3410   2874    134   -241   -197       C  
ATOM   2944  CE2 TYR A 797     -31.295   4.239  59.525  1.00 23.32           C  
ANISOU 2944  CE2 TYR A 797     3112   3065   2684    129   -326   -268       C  
ATOM   2945  CZ  TYR A 797     -31.963   3.671  60.591  1.00 24.04           C  
ANISOU 2945  CZ  TYR A 797     3199   3222   2713    157   -294   -254       C  
ATOM   2946  OH  TYR A 797     -32.522   4.475  61.558  1.00 23.09           O  
ANISOU 2946  OH  TYR A 797     3078   3151   2543    210   -315   -298       O  
ATOM   2947  N   LYS A 798     -27.029  -0.672  57.017  1.00 28.75           N  
ANISOU 2947  N   LYS A 798     3821   3580   3523    -38   -229    -44       N  
ATOM   2948  CA  LYS A 798     -26.186  -1.208  55.953  1.00 27.71           C  
ANISOU 2948  CA  LYS A 798     3692   3395   3440    -72   -222    -17       C  
ATOM   2949  C   LYS A 798     -26.753  -2.437  55.246  1.00 26.77           C  
ANISOU 2949  C   LYS A 798     3571   3268   3334   -105   -170     19       C  
ATOM   2950  O   LYS A 798     -26.682  -2.540  54.022  1.00 25.48           O  
ANISOU 2950  O   LYS A 798     3406   3066   3211   -133   -162     23       O  
ATOM   2951  CB  LYS A 798     -24.784  -1.510  56.487  1.00 28.10           C  
ANISOU 2951  CB  LYS A 798     3749   3433   3494    -63   -241      4       C  
ATOM   2952  CG  LYS A 798     -23.966  -0.272  56.811  1.00 29.10           C  
ANISOU 2952  CG  LYS A 798     3878   3549   3631    -41   -300    -31       C  
ATOM   2953  CD  LYS A 798     -22.505  -0.621  57.038  1.00 31.19           C  
ANISOU 2953  CD  LYS A 798     4146   3791   3914    -40   -318     -6       C  
ATOM   2954  CE  LYS A 798     -21.652   0.630  57.170  1.00 32.78           C  
ANISOU 2954  CE  LYS A 798     4345   3972   4138    -25   -380    -39       C  
ATOM   2955  NZ  LYS A 798     -20.198   0.308  57.242  1.00 35.58           N  
ANISOU 2955  NZ  LYS A 798     4699   4300   4518    -29   -398    -12       N  
ATOM   2956  N   ILE A 799     -27.301  -3.370  56.016  1.00 26.57           N  
ANISOU 2956  N   ILE A 799     3544   3277   3276   -101   -135     46       N  
ATOM   2957  CA  ILE A 799     -27.826  -4.609  55.451  1.00 27.14           C  
ANISOU 2957  CA  ILE A 799     3612   3337   3363   -133    -88     82       C  
ATOM   2958  C   ILE A 799     -28.949  -4.362  54.445  1.00 28.53           C  
ANISOU 2958  C   ILE A 799     3778   3505   3557   -155    -75     63       C  
ATOM   2959  O   ILE A 799     -28.938  -4.915  53.345  1.00 27.65           O  
ANISOU 2959  O   ILE A 799     3667   3356   3481   -185    -59     74       O  
ATOM   2960  CB  ILE A 799     -28.307  -5.569  56.553  1.00 25.84           C  
ANISOU 2960  CB  ILE A 799     3444   3214   3160   -123    -55    117       C  
ATOM   2961  CG1 ILE A 799     -27.106  -6.112  57.326  1.00 27.03           C  
ANISOU 2961  CG1 ILE A 799     3606   3364   3302   -109    -61    146       C  
ATOM   2962  CG2 ILE A 799     -29.114  -6.715  55.961  1.00 25.34           C  
ANISOU 2962  CG2 ILE A 799     3374   3139   3117   -157    -10    149       C  
ATOM   2963  CD1 ILE A 799     -27.455  -7.191  58.316  1.00 27.48           C  
ANISOU 2963  CD1 ILE A 799     3659   3455   3326   -102    -26    191       C  
ATOM   2964  N   ILE A 800     -29.905  -3.520  54.819  1.00 29.21           N  
ANISOU 2964  N   ILE A 800     3855   3627   3616   -136    -84     32       N  
ATOM   2965  CA  ILE A 800     -31.032  -3.218  53.946  1.00 28.30           C  
ANISOU 2965  CA  ILE A 800     3729   3509   3515   -153    -73     12       C  
ATOM   2966  C   ILE A 800     -30.589  -2.421  52.714  1.00 30.22           C  
ANISOU 2966  C   ILE A 800     3975   3708   3798   -166   -101    -13       C  
ATOM   2967  O   ILE A 800     -31.096  -2.637  51.611  1.00 32.24           O  
ANISOU 2967  O   ILE A 800     4227   3943   4081   -192    -87    -14       O  
ATOM   2968  CB  ILE A 800     -32.153  -2.475  54.708  1.00 26.99           C  
ANISOU 2968  CB  ILE A 800     3550   3395   3308   -125    -76    -14       C  
ATOM   2969  CG1 ILE A 800     -32.693  -3.351  55.841  1.00 29.74           C  
ANISOU 2969  CG1 ILE A 800     3891   3791   3616   -114    -41     19       C  
ATOM   2970  CG2 ILE A 800     -33.283  -2.086  53.773  1.00 25.60           C  
ANISOU 2970  CG2 ILE A 800     3361   3216   3149   -142    -69    -36       C  
ATOM   2971  CD1 ILE A 800     -33.338  -4.645  55.372  1.00 29.14           C  
ANISOU 2971  CD1 ILE A 800     3805   3707   3561   -150      4     59       C  
ATOM   2972  N   THR A 801     -29.631  -1.517  52.898  1.00 29.46           N  
ANISOU 2972  N   THR A 801     3887   3599   3708   -147   -142    -32       N  
ATOM   2973  CA  THR A 801     -29.107  -0.734  51.781  1.00 31.32           C  
ANISOU 2973  CA  THR A 801     4123   3793   3984   -158   -169    -50       C  
ATOM   2974  C   THR A 801     -28.248  -1.583  50.841  1.00 27.65           C  
ANISOU 2974  C   THR A 801     3664   3286   3554   -186   -153    -18       C  
ATOM   2975  O   THR A 801     -28.042  -1.221  49.683  1.00 27.42           O  
ANISOU 2975  O   THR A 801     3634   3226   3557   -201   -161    -24       O  
ATOM   2976  CB  THR A 801     -28.296   0.491  52.255  1.00 35.65           C  
ANISOU 2976  CB  THR A 801     4674   4335   4534   -132   -220    -77       C  
ATOM   2977  OG1 THR A 801     -27.300   0.073  53.195  1.00 40.36           O  
ANISOU 2977  OG1 THR A 801     5279   4937   5117   -118   -227    -58       O  
ATOM   2978  CG2 THR A 801     -29.207   1.521  52.911  1.00 35.83           C  
ANISOU 2978  CG2 THR A 801     4692   4393   4529   -103   -240   -117       C  
ATOM   2979  N   MET A 802     -27.750  -2.709  51.343  1.00 23.88           N  
ANISOU 2979  N   MET A 802     3193   2810   3069   -190   -131     16       N  
ATOM   2980  CA  MET A 802     -26.985  -3.638  50.519  1.00 21.38           C  
ANISOU 2980  CA  MET A 802     2884   2457   2784   -213   -113     45       C  
ATOM   2981  C   MET A 802     -27.927  -4.543  49.728  1.00 23.30           C  
ANISOU 2981  C   MET A 802     3124   2692   3035   -239    -76     55       C  
ATOM   2982  O   MET A 802     -27.632  -4.925  48.594  1.00 22.01           O  
ANISOU 2982  O   MET A 802     2964   2496   2902   -258    -68     62       O  
ATOM   2983  CB  MET A 802     -26.040  -4.480  51.381  1.00 19.05           C  
ANISOU 2983  CB  MET A 802     2597   2162   2479   -205   -106     78       C  
ATOM   2984  CG  MET A 802     -25.172  -5.445  50.587  1.00 20.97           C  
ANISOU 2984  CG  MET A 802     2848   2367   2754   -223    -89    108       C  
ATOM   2985  SD  MET A 802     -23.963  -4.624  49.524  1.00 28.04           S  
ANISOU 2985  SD  MET A 802     3742   3223   3688   -225   -120    100       S  
ATOM   2986  CE  MET A 802     -22.751  -4.099  50.735  1.00 58.69           C  
ANISOU 2986  CE  MET A 802     7625   7115   7561   -198   -156    105       C  
ATOM   2987  N   CYS A 803     -29.060  -4.881  50.337  1.00 23.96           N  
ANISOU 2987  N   CYS A 803     3201   2809   3095   -239    -55     56       N  
ATOM   2988  CA  CYS A 803     -30.083  -5.680  49.674  1.00 26.63           C  
ANISOU 2988  CA  CYS A 803     3532   3143   3443   -265    -24     63       C  
ATOM   2989  C   CYS A 803     -30.647  -4.947  48.465  1.00 28.39           C  
ANISOU 2989  C   CYS A 803     3749   3352   3685   -276    -35     33       C  
ATOM   2990  O   CYS A 803     -30.738  -5.507  47.372  1.00 29.19           O  
ANISOU 2990  O   CYS A 803     3852   3426   3812   -298    -23     37       O  
ATOM   2991  CB  CYS A 803     -31.220  -6.011  50.643  1.00 27.67           C  
ANISOU 2991  CB  CYS A 803     3651   3317   3544   -261     -2     71       C  
ATOM   2992  SG  CYS A 803     -30.797  -7.202  51.929  1.00 26.20           S  
ANISOU 2992  SG  CYS A 803     3469   3147   3337   -254     22    118       S  
ATOM   2993  N   PHE A 804     -31.026  -3.690  48.670  1.00 29.02           N  
ANISOU 2993  N   PHE A 804     3823   3453   3752   -258    -60      2       N  
ATOM   2994  CA  PHE A 804     -31.627  -2.889  47.613  1.00 32.57           C  
ANISOU 2994  CA  PHE A 804     4265   3894   4217   -265    -73    -26       C  
ATOM   2995  C   PHE A 804     -30.632  -2.578  46.501  1.00 30.18           C  
ANISOU 2995  C   PHE A 804     3970   3552   3946   -271    -89    -26       C  
ATOM   2996  O   PHE A 804     -30.978  -2.622  45.322  1.00 29.10           O  
ANISOU 2996  O   PHE A 804     3831   3399   3827   -287    -84    -33       O  
ATOM   2997  CB  PHE A 804     -32.207  -1.593  48.186  1.00 37.39           C  
ANISOU 2997  CB  PHE A 804     4867   4534   4806   -240    -98    -59       C  
ATOM   2998  CG  PHE A 804     -33.389  -1.803  49.093  1.00 41.90           C  
ANISOU 2998  CG  PHE A 804     5426   5150   5345   -231    -79    -61       C  
ATOM   2999  CD1 PHE A 804     -34.106  -2.990  49.060  1.00 42.70           C  
ANISOU 2999  CD1 PHE A 804     5521   5259   5445   -253    -41    -37       C  
ATOM   3000  CD2 PHE A 804     -33.787  -0.811  49.975  1.00 44.36           C  
ANISOU 3000  CD2 PHE A 804     5731   5495   5627   -200    -99    -87       C  
ATOM   3001  CE1 PHE A 804     -35.194  -3.184  49.894  1.00 43.25           C  
ANISOU 3001  CE1 PHE A 804     5575   5372   5486   -246    -22    -33       C  
ATOM   3002  CE2 PHE A 804     -34.875  -0.999  50.809  1.00 45.06           C  
ANISOU 3002  CE2 PHE A 804     5807   5631   5683   -189    -78    -87       C  
ATOM   3003  CZ  PHE A 804     -35.579  -2.187  50.769  1.00 43.83           C  
ANISOU 3003  CZ  PHE A 804     5642   5485   5527   -212    -38    -58       C  
ATOM   3004  N   SER A 805     -29.397  -2.271  46.884  1.00 29.66           N  
ANISOU 3004  N   SER A 805     3912   3474   3885   -258   -110    -18       N  
ATOM   3005  CA  SER A 805     -28.353  -1.923  45.926  1.00 27.78           C  
ANISOU 3005  CA  SER A 805     3677   3201   3677   -262   -126    -12       C  
ATOM   3006  C   SER A 805     -28.059  -3.068  44.961  1.00 23.85           C  
ANISOU 3006  C   SER A 805     3187   2679   3198   -282    -98     10       C  
ATOM   3007  O   SER A 805     -28.015  -2.873  43.746  1.00 22.42           O  
ANISOU 3007  O   SER A 805     3004   2479   3035   -291    -99      6       O  
ATOM   3008  CB  SER A 805     -27.073  -1.516  46.660  1.00 28.40           C  
ANISOU 3008  CB  SER A 805     3760   3272   3759   -244   -151     -3       C  
ATOM   3009  OG  SER A 805     -26.074  -1.097  45.748  1.00 29.14           O  
ANISOU 3009  OG  SER A 805     3853   3336   3885   -248   -167      6       O  
ATOM   3010  N   VAL A 806     -27.862  -4.262  45.510  1.00 22.60           N  
ANISOU 3010  N   VAL A 806     3035   2519   3032   -288    -74     34       N  
ATOM   3011  CA  VAL A 806     -27.568  -5.437  44.699  1.00 22.19           C  
ANISOU 3011  CA  VAL A 806     2991   2441   2997   -305    -49     53       C  
ATOM   3012  C   VAL A 806     -28.769  -5.827  43.841  1.00 23.79           C  
ANISOU 3012  C   VAL A 806     3189   2644   3204   -323    -32     38       C  
ATOM   3013  O   VAL A 806     -28.618  -6.185  42.674  1.00 25.92           O  
ANISOU 3013  O   VAL A 806     3464   2892   3492   -333    -26     37       O  
ATOM   3014  CB  VAL A 806     -27.129  -6.631  45.574  1.00 20.70           C  
ANISOU 3014  CB  VAL A 806     2810   2251   2803   -306    -29     83       C  
ATOM   3015  CG1 VAL A 806     -26.974  -7.887  44.733  1.00 20.65           C  
ANISOU 3015  CG1 VAL A 806     2814   2216   2818   -322     -5     98       C  
ATOM   3016  CG2 VAL A 806     -25.826  -6.309  46.287  1.00 19.85           C  
ANISOU 3016  CG2 VAL A 806     2707   2141   2695   -287    -48     98       C  
ATOM   3017  N   SER A 807     -29.962  -5.741  44.419  1.00 23.51           N  
ANISOU 3017  N   SER A 807     3145   2636   3152   -327    -26     27       N  
ATOM   3018  CA  SER A 807     -31.184  -6.086  43.701  1.00 22.05           C  
ANISOU 3018  CA  SER A 807     2953   2453   2972   -345    -12     13       C  
ATOM   3019  C   SER A 807     -31.532  -5.059  42.625  1.00 24.04           C  
ANISOU 3019  C   SER A 807     3199   2704   3230   -344    -31    -15       C  
ATOM   3020  O   SER A 807     -32.193  -5.388  41.642  1.00 24.82           O  
ANISOU 3020  O   SER A 807     3296   2796   3340   -359    -23    -26       O  
ATOM   3021  CB  SER A 807     -32.357  -6.250  44.671  1.00 19.86           C  
ANISOU 3021  CB  SER A 807     2663   2209   2675   -348      0     13       C  
ATOM   3022  OG  SER A 807     -32.210  -7.417  45.458  1.00 18.33           O  
ANISOU 3022  OG  SER A 807     2473   2014   2479   -355     23     43       O  
ATOM   3023  N   LEU A 808     -31.090  -3.820  42.816  1.00 24.82           N  
ANISOU 3023  N   LEU A 808     3295   2810   3325   -325    -57    -25       N  
ATOM   3024  CA  LEU A 808     -31.349  -2.763  41.842  1.00 25.16           C  
ANISOU 3024  CA  LEU A 808     3332   2851   3377   -322    -77    -47       C  
ATOM   3025  C   LEU A 808     -30.502  -2.948  40.590  1.00 27.05           C  
ANISOU 3025  C   LEU A 808     3578   3062   3636   -326    -76    -37       C  
ATOM   3026  O   LEU A 808     -31.030  -3.060  39.485  1.00 29.41           O  
ANISOU 3026  O   LEU A 808     3876   3357   3941   -335    -71    -48       O  
ATOM   3027  CB  LEU A 808     -31.089  -1.381  42.446  1.00 24.03           C  
ANISOU 3027  CB  LEU A 808     3183   2719   3228   -301   -108    -60       C  
ATOM   3028  CG  LEU A 808     -31.321  -0.188  41.516  1.00 24.27           C  
ANISOU 3028  CG  LEU A 808     3206   2745   3272   -296   -130    -78       C  
ATOM   3029  CD1 LEU A 808     -32.756  -0.176  41.009  1.00 25.48           C  
ANISOU 3029  CD1 LEU A 808     3350   2916   3418   -305   -121    -99       C  
ATOM   3030  CD2 LEU A 808     -30.989   1.124  42.212  1.00 24.10           C  
ANISOU 3030  CD2 LEU A 808     3178   2727   3250   -275   -165    -91       C  
ATOM   3031  N   SER A 809     -29.186  -2.986  40.770  1.00 28.32           N  
ANISOU 3031  N   SER A 809     3746   3207   3806   -317    -82    -16       N  
ATOM   3032  CA  SER A 809     -28.263  -3.121  39.646  1.00 30.75           C  
ANISOU 3032  CA  SER A 809     4059   3492   4132   -316    -80     -3       C  
ATOM   3033  C   SER A 809     -28.399  -4.464  38.926  1.00 28.01           C  
ANISOU 3033  C   SER A 809     3723   3133   3788   -329    -54      2       C  
ATOM   3034  O   SER A 809     -28.023  -4.590  37.759  1.00 25.45           O  
ANISOU 3034  O   SER A 809     3402   2795   3472   -327    -50      4       O  
ATOM   3035  CB  SER A 809     -26.821  -2.900  40.110  1.00 34.27           C  
ANISOU 3035  CB  SER A 809     4508   3926   4589   -304    -92     21       C  
ATOM   3036  OG  SER A 809     -26.575  -3.585  41.322  1.00 36.13           O  
ANISOU 3036  OG  SER A 809     4748   4164   4813   -303    -84     32       O  
ATOM   3037  N   ALA A 810     -28.935  -5.461  39.623  1.00 27.38           N  
ANISOU 3037  N   ALA A 810     3647   3055   3701   -340    -36      4       N  
ATOM   3038  CA  ALA A 810     -29.233  -6.750  39.008  1.00 27.03           C  
ANISOU 3038  CA  ALA A 810     3612   2995   3664   -354    -14      5       C  
ATOM   3039  C   ALA A 810     -30.496  -6.650  38.157  1.00 26.88           C  
ANISOU 3039  C   ALA A 810     3586   2984   3644   -366    -14    -22       C  
ATOM   3040  O   ALA A 810     -30.599  -7.278  37.102  1.00 26.33           O  
ANISOU 3040  O   ALA A 810     3523   2899   3581   -371     -7    -30       O  
ATOM   3041  CB  ALA A 810     -29.397  -7.822  40.071  1.00 25.01           C  
ANISOU 3041  CB  ALA A 810     3360   2736   3407   -364      4     21       C  
ATOM   3042  N   THR A 811     -31.452  -5.856  38.628  1.00 25.00           N  
ANISOU 3042  N   THR A 811     3334   2770   3394   -367    -24    -37       N  
ATOM   3043  CA  THR A 811     -32.713  -5.661  37.924  1.00 25.43           C  
ANISOU 3043  CA  THR A 811     3379   2836   3447   -378    -26    -62       C  
ATOM   3044  C   THR A 811     -32.491  -4.853  36.650  1.00 27.95           C  
ANISOU 3044  C   THR A 811     3698   3153   3769   -368    -41    -74       C  
ATOM   3045  O   THR A 811     -33.083  -5.140  35.608  1.00 28.19           O  
ANISOU 3045  O   THR A 811     3729   3182   3802   -374    -40    -90       O  
ATOM   3046  CB  THR A 811     -33.751  -4.946  38.817  1.00 22.46           C  
ANISOU 3046  CB  THR A 811     2987   2490   3058   -377    -32    -74       C  
ATOM   3047  OG1 THR A 811     -33.981  -5.721  40.000  1.00 18.86           O  
ANISOU 3047  OG1 THR A 811     2529   2041   2596   -385    -16    -58       O  
ATOM   3048  CG2 THR A 811     -35.066  -4.761  38.076  1.00 23.85           C  
ANISOU 3048  CG2 THR A 811     3150   2679   3234   -388    -35    -98       C  
ATOM   3049  N   VAL A 812     -31.626  -3.848  36.742  1.00 27.56           N  
ANISOU 3049  N   VAL A 812     3648   3105   3721   -351    -57    -65       N  
ATOM   3050  CA  VAL A 812     -31.302  -2.998  35.604  1.00 27.73           C  
ANISOU 3050  CA  VAL A 812     3666   3124   3746   -339    -71    -68       C  
ATOM   3051  C   VAL A 812     -30.656  -3.803  34.479  1.00 30.03           C  
ANISOU 3051  C   VAL A 812     3969   3400   4042   -337    -58    -60       C  
ATOM   3052  O   VAL A 812     -31.006  -3.646  33.307  1.00 31.53           O  
ANISOU 3052  O   VAL A 812     4157   3594   4228   -334    -60    -72       O  
ATOM   3053  CB  VAL A 812     -30.364  -1.846  36.016  1.00 28.76           C  
ANISOU 3053  CB  VAL A 812     3791   3254   3884   -324    -91    -53       C  
ATOM   3054  CG1 VAL A 812     -29.875  -1.086  34.792  1.00 29.79           C  
ANISOU 3054  CG1 VAL A 812     3917   3380   4023   -313   -101    -46       C  
ATOM   3055  CG2 VAL A 812     -31.069  -0.910  36.989  1.00 27.52           C  
ANISOU 3055  CG2 VAL A 812     3623   3113   3720   -320   -108    -68       C  
ATOM   3056  N   ALA A 813     -29.719  -4.672  34.841  1.00 29.42           N  
ANISOU 3056  N   ALA A 813     3903   3306   3971   -336    -44    -40       N  
ATOM   3057  CA  ALA A 813     -29.049  -5.520  33.862  1.00 29.19           C  
ANISOU 3057  CA  ALA A 813     3885   3260   3944   -330    -31    -34       C  
ATOM   3058  C   ALA A 813     -30.031  -6.509  33.245  1.00 29.17           C  
ANISOU 3058  C   ALA A 813     3890   3254   3939   -343    -22    -58       C  
ATOM   3059  O   ALA A 813     -29.889  -6.904  32.087  1.00 29.00           O  
ANISOU 3059  O   ALA A 813     3876   3227   3915   -336    -18    -67       O  
ATOM   3060  CB  ALA A 813     -27.884  -6.256  34.504  1.00 26.41           C  
ANISOU 3060  CB  ALA A 813     3543   2890   3600   -326    -20     -9       C  
ATOM   3061  N   LEU A 814     -31.030  -6.901  34.027  1.00 27.74           N  
ANISOU 3061  N   LEU A 814     3705   3076   3759   -362    -18    -69       N  
ATOM   3062  CA  LEU A 814     -32.041  -7.844  33.568  1.00 26.97           C  
ANISOU 3062  CA  LEU A 814     3610   2972   3666   -379    -12    -91       C  
ATOM   3063  C   LEU A 814     -33.100  -7.145  32.719  1.00 27.09           C  
ANISOU 3063  C   LEU A 814     3614   3007   3672   -381    -26   -118       C  
ATOM   3064  O   LEU A 814     -33.604  -7.712  31.750  1.00 25.97           O  
ANISOU 3064  O   LEU A 814     3477   2860   3532   -385    -27   -139       O  
ATOM   3065  CB  LEU A 814     -32.702  -8.534  34.763  1.00 25.31           C  
ANISOU 3065  CB  LEU A 814     3395   2760   3463   -399     -2    -85       C  
ATOM   3066  CG  LEU A 814     -33.674  -9.671  34.447  1.00 24.88           C  
ANISOU 3066  CG  LEU A 814     3340   2691   3422   -421      4   -102       C  
ATOM   3067  CD1 LEU A 814     -32.949 -10.824  33.770  1.00 24.66           C  
ANISOU 3067  CD1 LEU A 814     3332   2632   3407   -418     11   -102       C  
ATOM   3068  CD2 LEU A 814     -34.374 -10.142  35.712  1.00 24.60           C  
ANISOU 3068  CD2 LEU A 814     3294   2660   3394   -441     15    -89       C  
ATOM   3069  N   GLY A 815     -33.426  -5.911  33.087  1.00 27.45           N  
ANISOU 3069  N   GLY A 815     3645   3073   3710   -376    -38   -118       N  
ATOM   3070  CA  GLY A 815     -34.485  -5.174  32.425  1.00 29.33           C  
ANISOU 3070  CA  GLY A 815     3871   3332   3942   -377    -52   -141       C  
ATOM   3071  C   GLY A 815     -34.085  -4.586  31.087  1.00 32.29           C  
ANISOU 3071  C   GLY A 815     4248   3711   4308   -359    -61   -145       C  
ATOM   3072  O   GLY A 815     -34.908  -4.479  30.178  1.00 36.26           O  
ANISOU 3072  O   GLY A 815     4746   4225   4805   -360    -69   -167       O  
ATOM   3073  N   CYS A 816     -32.820  -4.204  30.960  1.00 30.41           N  
ANISOU 3073  N   CYS A 816     4016   3467   4072   -342    -61   -121       N  
ATOM   3074  CA  CYS A 816     -32.356  -3.529  29.755  1.00 30.14           C  
ANISOU 3074  CA  CYS A 816     3981   3441   4030   -322    -68   -116       C  
ATOM   3075  C   CYS A 816     -31.754  -4.486  28.731  1.00 33.80           C  
ANISOU 3075  C   CYS A 816     4460   3896   4488   -311    -56   -116       C  
ATOM   3076  O   CYS A 816     -31.955  -4.322  27.530  1.00 38.22           O  
ANISOU 3076  O   CYS A 816     5020   4468   5033   -298    -60   -127       O  
ATOM   3077  CB  CYS A 816     -31.345  -2.436  30.107  1.00 28.47           C  
ANISOU 3077  CB  CYS A 816     3762   3230   3826   -308    -76    -86       C  
ATOM   3078  SG  CYS A 816     -31.999  -1.120  31.159  1.00 67.02           S  
ANISOU 3078  SG  CYS A 816     8627   8123   8715   -313    -97    -91       S  
ATOM   3079  N   MET A 817     -31.020  -5.486  29.204  1.00 32.51           N  
ANISOU 3079  N   MET A 817     4309   3712   4332   -313    -41   -106       N  
ATOM   3080  CA  MET A 817     -30.310  -6.385  28.301  1.00 30.65           C  
ANISOU 3080  CA  MET A 817     4089   3466   4090   -298    -29   -106       C  
ATOM   3081  C   MET A 817     -31.144  -7.578  27.837  1.00 31.19           C  
ANISOU 3081  C   MET A 817     4169   3524   4158   -309    -27   -140       C  
ATOM   3082  O   MET A 817     -31.071  -7.977  26.676  1.00 34.13           O  
ANISOU 3082  O   MET A 817     4551   3900   4518   -293    -27   -156       O  
ATOM   3083  CB  MET A 817     -29.008  -6.873  28.940  1.00 28.54           C  
ANISOU 3083  CB  MET A 817     3830   3181   3834   -291    -16    -77       C  
ATOM   3084  CG  MET A 817     -28.020  -5.762  29.236  1.00 28.32           C  
ANISOU 3084  CG  MET A 817     3790   3160   3810   -279    -20    -43       C  
ATOM   3085  SD  MET A 817     -26.377  -6.387  29.630  1.00 34.22           S  
ANISOU 3085  SD  MET A 817     4545   3888   4568   -265     -4     -9       S  
ATOM   3086  CE  MET A 817     -26.718  -7.355  31.097  1.00 39.49           C  
ANISOU 3086  CE  MET A 817     5221   4534   5248   -289      1    -14       C  
ATOM   3087  N   PHE A 818     -31.938  -8.143  28.741  1.00 28.49           N  
ANISOU 3087  N   PHE A 818     3825   3170   3830   -335    -27   -150       N  
ATOM   3088  CA  PHE A 818     -32.651  -9.382  28.444  1.00 29.31           C  
ANISOU 3088  CA  PHE A 818     3938   3256   3942   -349    -26   -178       C  
ATOM   3089  C   PHE A 818     -34.118  -9.185  28.064  1.00 29.87           C  
ANISOU 3089  C   PHE A 818     3997   3341   4012   -365    -41   -208       C  
ATOM   3090  O   PHE A 818     -34.621  -9.854  27.162  1.00 27.47           O  
ANISOU 3090  O   PHE A 818     3700   3031   3707   -365    -48   -238       O  
ATOM   3091  CB  PHE A 818     -32.525 -10.357  29.614  1.00 30.22           C  
ANISOU 3091  CB  PHE A 818     4058   3345   4080   -368    -14   -164       C  
ATOM   3092  CG  PHE A 818     -31.109 -10.724  29.935  1.00 32.33           C  
ANISOU 3092  CG  PHE A 818     4338   3596   4350   -353      0   -137       C  
ATOM   3093  CD1 PHE A 818     -30.512 -11.819  29.335  1.00 34.03           C  
ANISOU 3093  CD1 PHE A 818     4571   3787   4570   -341      7   -144       C  
ATOM   3094  CD2 PHE A 818     -30.367  -9.966  30.825  1.00 32.87           C  
ANISOU 3094  CD2 PHE A 818     4399   3673   4417   -347      4   -105       C  
ATOM   3095  CE1 PHE A 818     -29.205 -12.155  29.623  1.00 35.30           C  
ANISOU 3095  CE1 PHE A 818     4743   3935   4735   -325     20   -117       C  
ATOM   3096  CE2 PHE A 818     -29.061 -10.296  31.117  1.00 32.68           C  
ANISOU 3096  CE2 PHE A 818     4384   3635   4397   -333     15    -79       C  
ATOM   3097  CZ  PHE A 818     -28.479 -11.393  30.515  1.00 34.54           C  
ANISOU 3097  CZ  PHE A 818     4637   3848   4638   -322     24    -84       C  
ATOM   3098  N   VAL A 819     -34.798  -8.273  28.752  1.00 32.10           N  
ANISOU 3098  N   VAL A 819     4261   3642   4294   -376    -46   -203       N  
ATOM   3099  CA  VAL A 819     -36.217  -8.014  28.495  1.00 35.76           C  
ANISOU 3099  CA  VAL A 819     4709   4122   4757   -391    -60   -229       C  
ATOM   3100  C   VAL A 819     -36.557  -7.609  27.046  1.00 38.20           C  
ANISOU 3100  C   VAL A 819     5019   4448   5048   -375    -75   -253       C  
ATOM   3101  O   VAL A 819     -37.494  -8.158  26.463  1.00 38.12           O  
ANISOU 3101  O   VAL A 819     5006   4437   5040   -386    -86   -283       O  
ATOM   3102  CB  VAL A 819     -36.820  -7.009  29.514  1.00 27.90           C  
ANISOU 3102  CB  VAL A 819     3694   3147   3762   -401    -63   -218       C  
ATOM   3103  CG1 VAL A 819     -38.214  -6.576  29.088  1.00 29.26           C  
ANISOU 3103  CG1 VAL A 819     3848   3340   3930   -410    -78   -244       C  
ATOM   3104  CG2 VAL A 819     -36.849  -7.620  30.907  1.00 27.12           C  
ANISOU 3104  CG2 VAL A 819     3592   3035   3678   -419    -49   -201       C  
ATOM   3105  N   PRO A 820     -35.802  -6.659  26.454  1.00 38.87           N  
ANISOU 3105  N   PRO A 820     5104   4549   5114   -349    -77   -239       N  
ATOM   3106  CA  PRO A 820     -36.110  -6.317  25.059  1.00 39.66           C  
ANISOU 3106  CA  PRO A 820     5206   4670   5194   -330    -90   -258       C  
ATOM   3107  C   PRO A 820     -35.914  -7.485  24.092  1.00 42.47           C  
ANISOU 3107  C   PRO A 820     5581   5013   5543   -320    -90   -282       C  
ATOM   3108  O   PRO A 820     -36.500  -7.481  23.010  1.00 43.93           O  
ANISOU 3108  O   PRO A 820     5766   5213   5712   -310   -104   -309       O  
ATOM   3109  CB  PRO A 820     -35.106  -5.204  24.743  1.00 38.00           C  
ANISOU 3109  CB  PRO A 820     4993   4475   4970   -304    -87   -227       C  
ATOM   3110  CG  PRO A 820     -34.786  -4.606  26.059  1.00 37.87           C  
ANISOU 3110  CG  PRO A 820     4967   4452   4970   -315    -83   -201       C  
ATOM   3111  CD  PRO A 820     -34.779  -5.758  27.014  1.00 38.28           C  
ANISOU 3111  CD  PRO A 820     5027   4479   5039   -336    -71   -204       C  
ATOM   3112  N   LYS A 821     -35.103  -8.466  24.475  1.00 42.52           N  
ANISOU 3112  N   LYS A 821     5602   4991   5561   -321    -75   -274       N  
ATOM   3113  CA  LYS A 821     -34.898  -9.645  23.641  1.00 42.59           C  
ANISOU 3113  CA  LYS A 821     5631   4984   5567   -310    -77   -300       C  
ATOM   3114  C   LYS A 821     -35.991 -10.681  23.884  1.00 40.09           C  
ANISOU 3114  C   LYS A 821     5315   4645   5275   -340    -87   -332       C  
ATOM   3115  O   LYS A 821     -36.346 -11.443  22.986  1.00 41.93           O  
ANISOU 3115  O   LYS A 821     5558   4870   5505   -334   -101   -367       O  
ATOM   3116  CB  LYS A 821     -33.517 -10.259  23.887  1.00 46.22           C  
ANISOU 3116  CB  LYS A 821     6108   5423   6030   -294    -58   -277       C  
ATOM   3117  CG  LYS A 821     -32.356  -9.309  23.627  1.00 48.56           C  
ANISOU 3117  CG  LYS A 821     6402   5741   6308   -265    -47   -242       C  
ATOM   3118  CD  LYS A 821     -31.073 -10.070  23.328  1.00 50.22           C  
ANISOU 3118  CD  LYS A 821     6630   5937   6514   -240    -31   -231       C  
ATOM   3119  CE  LYS A 821     -30.703 -11.007  24.465  1.00 51.49           C  
ANISOU 3119  CE  LYS A 821     6799   6062   6704   -259    -20   -220       C  
ATOM   3120  NZ  LYS A 821     -29.482 -11.804  24.155  1.00 52.74           N  
ANISOU 3120  NZ  LYS A 821     6975   6205   6860   -233     -5   -211       N  
ATOM   3121  N   VAL A 822     -36.518 -10.705  25.104  1.00 37.20           N  
ANISOU 3121  N   VAL A 822     4935   4268   4933   -371    -83   -318       N  
ATOM   3122  CA  VAL A 822     -37.626 -11.589  25.445  1.00 36.25           C  
ANISOU 3122  CA  VAL A 822     4806   4127   4840   -403    -91   -340       C  
ATOM   3123  C   VAL A 822     -38.916 -11.061  24.823  1.00 37.72           C  
ANISOU 3123  C   VAL A 822     4976   4338   5019   -411   -113   -368       C  
ATOM   3124  O   VAL A 822     -39.751 -11.831  24.347  1.00 38.37           O  
ANISOU 3124  O   VAL A 822     5057   4408   5116   -425   -129   -401       O  
ATOM   3125  CB  VAL A 822     -37.798 -11.719  26.976  1.00 34.43           C  
ANISOU 3125  CB  VAL A 822     4563   3885   4634   -431    -77   -310       C  
ATOM   3126  CG1 VAL A 822     -39.070 -12.486  27.315  1.00 34.42           C  
ANISOU 3126  CG1 VAL A 822     4546   3869   4662   -466    -85   -327       C  
ATOM   3127  CG2 VAL A 822     -36.585 -12.396  27.593  1.00 32.58           C  
ANISOU 3127  CG2 VAL A 822     4346   3624   4409   -425    -58   -284       C  
ATOM   3128  N   TYR A 823     -39.064  -9.740  24.825  1.00 39.10           N  
ANISOU 3128  N   TYR A 823     5136   4547   5174   -401   -114   -355       N  
ATOM   3129  CA  TYR A 823     -40.221  -9.091  24.222  1.00 41.74           C  
ANISOU 3129  CA  TYR A 823     5453   4908   5498   -404   -134   -378       C  
ATOM   3130  C   TYR A 823     -40.341  -9.447  22.742  1.00 42.60           C  
ANISOU 3130  C   TYR A 823     5575   5023   5589   -384   -153   -414       C  
ATOM   3131  O   TYR A 823     -41.385  -9.920  22.292  1.00 42.62           O  
ANISOU 3131  O   TYR A 823     5570   5024   5602   -399   -173   -448       O  
ATOM   3132  CB  TYR A 823     -40.136  -7.573  24.397  1.00 44.61           C  
ANISOU 3132  CB  TYR A 823     5802   5303   5843   -390   -133   -356       C  
ATOM   3133  CG  TYR A 823     -41.248  -6.817  23.707  1.00 48.69           C  
ANISOU 3133  CG  TYR A 823     6302   5850   6347   -388   -153   -378       C  
ATOM   3134  CD1 TYR A 823     -42.519  -6.753  24.264  1.00 50.97           C  
ANISOU 3134  CD1 TYR A 823     6567   6146   6653   -414   -161   -388       C  
ATOM   3135  CD2 TYR A 823     -41.028  -6.168  22.499  1.00 50.62           C  
ANISOU 3135  CD2 TYR A 823     6551   6118   6563   -358   -164   -384       C  
ATOM   3136  CE1 TYR A 823     -43.540  -6.065  23.636  1.00 53.13           C  
ANISOU 3136  CE1 TYR A 823     6824   6447   6917   -411   -180   -407       C  
ATOM   3137  CE2 TYR A 823     -42.043  -5.477  21.864  1.00 52.68           C  
ANISOU 3137  CE2 TYR A 823     6796   6407   6813   -355   -184   -402       C  
ATOM   3138  CZ  TYR A 823     -43.296  -5.429  22.437  1.00 54.21           C  
ANISOU 3138  CZ  TYR A 823     6968   6605   7025   -382   -193   -415       C  
ATOM   3139  OH  TYR A 823     -44.309  -4.742  21.808  1.00 56.46           O  
ANISOU 3139  OH  TYR A 823     7235   6918   7299   -378   -213   -433       O  
ATOM   3140  N   ILE A 824     -39.264  -9.222  21.996  1.00 42.18           N  
ANISOU 3140  N   ILE A 824     5539   4978   5509   -350   -147   -406       N  
ATOM   3141  CA  ILE A 824     -39.221  -9.555  20.575  1.00 41.02           C  
ANISOU 3141  CA  ILE A 824     5407   4842   5337   -323   -162   -438       C  
ATOM   3142  C   ILE A 824     -39.524 -11.034  20.339  1.00 41.26           C  
ANISOU 3142  C   ILE A 824     5451   4837   5388   -335   -173   -476       C  
ATOM   3143  O   ILE A 824     -40.225 -11.393  19.397  1.00 41.40           O  
ANISOU 3143  O   ILE A 824     5471   4861   5399   -330   -198   -517       O  
ATOM   3144  CB  ILE A 824     -37.848  -9.191  19.959  1.00 39.04           C  
ANISOU 3144  CB  ILE A 824     5172   4605   5057   -282   -147   -416       C  
ATOM   3145  CG1 ILE A 824     -37.677  -7.672  19.902  1.00 38.69           C  
ANISOU 3145  CG1 ILE A 824     5112   4596   4993   -268   -143   -383       C  
ATOM   3146  CG2 ILE A 824     -37.696  -9.786  18.568  1.00 38.34           C  
ANISOU 3146  CG2 ILE A 824     5101   4525   4939   -251   -159   -451       C  
ATOM   3147  CD1 ILE A 824     -36.408  -7.221  19.208  1.00 38.99           C  
ANISOU 3147  CD1 ILE A 824     5159   4651   5002   -229   -129   -356       C  
ATOM   3148  N   ILE A 825     -39.020 -11.887  21.221  1.00 42.06           N  
ANISOU 3148  N   ILE A 825     5561   4903   5519   -351   -158   -462       N  
ATOM   3149  CA  ILE A 825     -39.134 -13.328  21.038  1.00 42.54           C  
ANISOU 3149  CA  ILE A 825     5636   4923   5604   -361   -169   -493       C  
ATOM   3150  C   ILE A 825     -40.531 -13.875  21.355  1.00 42.34           C  
ANISOU 3150  C   ILE A 825     5593   4880   5615   -402   -189   -517       C  
ATOM   3151  O   ILE A 825     -40.920 -14.926  20.844  1.00 44.71           O  
ANISOU 3151  O   ILE A 825     5902   5152   5934   -408   -209   -555       O  
ATOM   3152  CB  ILE A 825     -38.062 -14.069  21.866  1.00 44.56           C  
ANISOU 3152  CB  ILE A 825     5908   5144   5880   -363   -145   -466       C  
ATOM   3153  CG1 ILE A 825     -37.422 -15.186  21.051  1.00 47.35           C  
ANISOU 3153  CG1 ILE A 825     6288   5471   6231   -339   -152   -496       C  
ATOM   3154  CG2 ILE A 825     -38.641 -14.620  23.156  1.00 44.42           C  
ANISOU 3154  CG2 ILE A 825     5875   5096   5906   -407   -139   -450       C  
ATOM   3155  CD1 ILE A 825     -36.290 -15.845  21.778  1.00 47.91           C  
ANISOU 3155  CD1 ILE A 825     6374   5510   6318   -335   -129   -468       C  
ATOM   3156  N   LEU A 826     -41.286 -13.159  22.184  1.00 38.92           N  
ANISOU 3156  N   LEU A 826     5132   4463   5192   -428   -184   -496       N  
ATOM   3157  CA  LEU A 826     -42.601 -13.634  22.611  1.00 36.24           C  
ANISOU 3157  CA  LEU A 826     4770   4110   4890   -468   -199   -510       C  
ATOM   3158  C   LEU A 826     -43.752 -12.830  22.002  1.00 34.88           C  
ANISOU 3158  C   LEU A 826     4576   3974   4704   -469   -221   -532       C  
ATOM   3159  O   LEU A 826     -44.807 -13.379  21.690  1.00 32.48           O  
ANISOU 3159  O   LEU A 826     4259   3660   4423   -491   -245   -562       O  
ATOM   3160  CB  LEU A 826     -42.710 -13.636  24.142  1.00 35.46           C  
ANISOU 3160  CB  LEU A 826     4654   4001   4819   -498   -175   -468       C  
ATOM   3161  CG  LEU A 826     -41.880 -14.667  24.916  1.00 33.70           C  
ANISOU 3161  CG  LEU A 826     4446   3736   4622   -507   -157   -446       C  
ATOM   3162  CD1 LEU A 826     -42.182 -14.609  26.409  1.00 32.00           C  
ANISOU 3162  CD1 LEU A 826     4210   3519   4430   -536   -136   -405       C  
ATOM   3163  CD2 LEU A 826     -42.114 -16.070  24.377  1.00 33.67           C  
ANISOU 3163  CD2 LEU A 826     4454   3687   4650   -519   -176   -480       C  
ATOM   3164  N   ALA A 827     -43.541 -11.531  21.836  1.00 35.50           N  
ANISOU 3164  N   ALA A 827     4649   4092   4746   -447   -214   -515       N  
ATOM   3165  CA  ALA A 827     -44.588 -10.653  21.347  1.00 37.01           C  
ANISOU 3165  CA  ALA A 827     4818   4319   4924   -447   -233   -530       C  
ATOM   3166  C   ALA A 827     -44.470 -10.463  19.835  1.00 38.69           C  
ANISOU 3166  C   ALA A 827     5047   4554   5101   -412   -254   -562       C  
ATOM   3167  O   ALA A 827     -45.471 -10.233  19.148  1.00 41.93           O  
ANISOU 3167  O   ALA A 827     5443   4984   5505   -413   -280   -591       O  
ATOM   3168  CB  ALA A 827     -44.556  -9.307  22.093  1.00 37.38           C  
ANISOU 3168  CB  ALA A 827     4849   4396   4958   -443   -216   -493       C  
ATOM   3169  N   LYS A 828     -43.246 -10.581  19.312  1.00 38.32           N  
ANISOU 3169  N   LYS A 828     5027   4505   5028   -379   -243   -557       N  
ATOM   3170  CA  LYS A 828     -42.983 -10.343  17.877  1.00 38.51           C  
ANISOU 3170  CA  LYS A 828     5066   4556   5010   -338   -259   -581       C  
ATOM   3171  C   LYS A 828     -42.180 -11.447  17.162  1.00 39.70           C  
ANISOU 3171  C   LYS A 828     5248   4685   5152   -315   -262   -607       C  
ATOM   3172  O   LYS A 828     -41.047 -11.198  16.715  1.00 38.73           O  
ANISOU 3172  O   LYS A 828     5142   4575   4997   -278   -246   -590       O  
ATOM   3173  CB  LYS A 828     -42.293  -8.979  17.694  1.00 38.65           C  
ANISOU 3173  CB  LYS A 828     5081   4611   4992   -308   -242   -544       C  
ATOM   3174  CG  LYS A 828     -42.963  -7.875  18.466  1.00 38.92           C  
ANISOU 3174  CG  LYS A 828     5088   4663   5036   -328   -239   -518       C  
ATOM   3175  CD  LYS A 828     -44.024  -7.166  17.662  1.00 39.48           C  
ANISOU 3175  CD  LYS A 828     5141   4769   5089   -321   -264   -539       C  
ATOM   3176  CE  LYS A 828     -44.612  -6.050  18.505  1.00 40.28           C  
ANISOU 3176  CE  LYS A 828     5217   4886   5202   -337   -259   -513       C  
ATOM   3177  NZ  LYS A 828     -45.609  -5.301  17.713  1.00 42.43           N  
ANISOU 3177  NZ  LYS A 828     5472   5194   5457   -328   -283   -531       N  
ATOM   3178  N   PRO A 829     -42.774 -12.659  17.033  1.00 43.10           N  
ANISOU 3178  N   PRO A 829     5683   5081   5611   -335   -284   -648       N  
ATOM   3179  CA  PRO A 829     -41.942 -13.716  16.453  1.00 44.87           C  
ANISOU 3179  CA  PRO A 829     5938   5280   5830   -310   -287   -673       C  
ATOM   3180  C   PRO A 829     -41.677 -13.547  14.974  1.00 47.76           C  
ANISOU 3180  C   PRO A 829     6322   5681   6145   -260   -303   -705       C  
ATOM   3181  O   PRO A 829     -40.781 -14.176  14.427  1.00 47.78           O  
ANISOU 3181  O   PRO A 829     6351   5674   6128   -228   -299   -719       O  
ATOM   3182  CB  PRO A 829     -42.766 -14.982  16.704  1.00 44.09           C  
ANISOU 3182  CB  PRO A 829     5837   5133   5782   -346   -311   -709       C  
ATOM   3183  CG  PRO A 829     -43.663 -14.660  17.830  1.00 44.33           C  
ANISOU 3183  CG  PRO A 829     5836   5159   5851   -394   -305   -683       C  
ATOM   3184  CD  PRO A 829     -44.044 -13.213  17.545  1.00 43.80           C  
ANISOU 3184  CD  PRO A 829     5750   5146   5746   -380   -304   -668       C  
ATOM   3185  N   GLU A 830     -42.476 -12.715  14.330  1.00 51.85           N  
ANISOU 3185  N   GLU A 830     6824   6239   6637   -253   -321   -716       N  
ATOM   3186  CA  GLU A 830     -42.269 -12.410  12.930  1.00 56.92           C  
ANISOU 3186  CA  GLU A 830     7480   6923   7224   -203   -335   -740       C  
ATOM   3187  C   GLU A 830     -41.036 -11.515  12.774  1.00 60.76           C  
ANISOU 3187  C   GLU A 830     7973   7442   7670   -165   -301   -691       C  
ATOM   3188  O   GLU A 830     -40.300 -11.626  11.798  1.00 60.61           O  
ANISOU 3188  O   GLU A 830     7975   7447   7608   -118   -299   -701       O  
ATOM   3189  CB  GLU A 830     -43.508 -11.719  12.362  1.00 57.09           C  
ANISOU 3189  CB  GLU A 830     7480   6979   7231   -208   -364   -760       C  
ATOM   3190  CG  GLU A 830     -44.756 -12.595  12.312  1.00 57.04           C  
ANISOU 3190  CG  GLU A 830     7465   6945   7263   -242   -403   -812       C  
ATOM   3191  CD  GLU A 830     -44.631 -13.757  11.340  1.00 57.85           C  
ANISOU 3191  CD  GLU A 830     7594   7030   7355   -217   -432   -872       C  
ATOM   3192  OE1 GLU A 830     -43.676 -13.779  10.532  1.00 59.92           O  
ANISOU 3192  OE1 GLU A 830     7882   7314   7571   -166   -423   -877       O  
ATOM   3193  OE2 GLU A 830     -45.498 -14.653  11.391  1.00 56.71           O  
ANISOU 3193  OE2 GLU A 830     7444   6850   7252   -247   -464   -914       O  
ATOM   3194  N   ARG A 831     -40.816 -10.634  13.750  1.00 64.07           N  
ANISOU 3194  N   ARG A 831     8375   7864   8105   -186   -276   -638       N  
ATOM   3195  CA  ARG A 831     -39.645  -9.753  13.764  1.00 66.32           C  
ANISOU 3195  CA  ARG A 831     8662   8174   8363   -157   -245   -587       C  
ATOM   3196  C   ARG A 831     -38.380 -10.594  13.904  1.00 66.88           C  
ANISOU 3196  C   ARG A 831     8757   8220   8436   -139   -223   -578       C  
ATOM   3197  O   ARG A 831     -37.314 -10.264  13.374  1.00 67.58           O  
ANISOU 3197  O   ARG A 831     8855   8332   8490    -99   -204   -554       O  
ATOM   3198  CB  ARG A 831     -39.728  -8.757  14.924  1.00 67.94           C  
ANISOU 3198  CB  ARG A 831     8843   8377   8593   -187   -228   -539       C  
ATOM   3199  CG  ARG A 831     -40.765  -7.644  14.761  1.00 70.33           C  
ANISOU 3199  CG  ARG A 831     9121   8712   8888   -195   -243   -535       C  
ATOM   3200  CD  ARG A 831     -40.604  -6.913  13.434  1.00 73.03           C  
ANISOU 3200  CD  ARG A 831     9465   9102   9179   -150   -251   -534       C  
ATOM   3201  NE  ARG A 831     -41.172  -5.565  13.459  1.00 74.74           N  
ANISOU 3201  NE  ARG A 831     9657   9348   9390   -152   -255   -508       N  
ATOM   3202  CZ  ARG A 831     -41.309  -4.792  12.384  1.00 75.81           C  
ANISOU 3202  CZ  ARG A 831     9788   9528   9487   -119   -265   -504       C  
ATOM   3203  NH1 ARG A 831     -40.932  -5.235  11.192  1.00 76.06           N  
ANISOU 3203  NH1 ARG A 831     9839   9584   9478    -79   -271   -524       N  
ATOM   3204  NH2 ARG A 831     -41.830  -3.577  12.498  1.00 75.93           N  
ANISOU 3204  NH2 ARG A 831     9782   9566   9504   -123   -270   -479       N  
ATOM   3205  N   ASN A 832     -38.518 -11.686  14.640  1.00 66.28           N  
ANISOU 3205  N   ASN A 832     8688   8094   8401   -170   -226   -597       N  
ATOM   3206  CA  ASN A 832     -37.437 -12.632  14.825  1.00 65.53           C  
ANISOU 3206  CA  ASN A 832     8616   7969   8314   -156   -209   -594       C  
ATOM   3207  C   ASN A 832     -36.968 -13.236  13.496  1.00 64.79           C  
ANISOU 3207  C   ASN A 832     8548   7891   8180   -105   -219   -632       C  
ATOM   3208  O   ASN A 832     -36.298 -14.270  13.464  1.00 63.98           O  
ANISOU 3208  O   ASN A 832     8466   7758   8084    -92   -215   -649       O  
ATOM   3209  CB  ASN A 832     -37.891 -13.723  15.782  1.00 66.43           C  
ANISOU 3209  CB  ASN A 832     8732   8027   8483   -200   -216   -611       C  
ATOM   3210  CG  ASN A 832     -36.755 -14.579  16.260  1.00 67.40           C  
ANISOU 3210  CG  ASN A 832     8874   8115   8622   -192   -195   -597       C  
ATOM   3211  OD1 ASN A 832     -35.626 -14.111  16.395  1.00 66.53           O  
ANISOU 3211  OD1 ASN A 832     8767   8019   8493   -169   -167   -556       O  
ATOM   3212  ND2 ASN A 832     -37.038 -15.847  16.503  1.00 69.13           N  
ANISOU 3212  ND2 ASN A 832     9103   8284   8877   -212   -209   -629       N  
TER    3213      ASN A 832                                                      
HETATM 3214  C1  OLA A4001     -14.665   4.086  53.862  1.00 61.85           C  
HETATM 3215  O1  OLA A4001     -15.668   4.406  54.500  1.00 62.31           O  
HETATM 3216  O2  OLA A4001     -13.752   3.448  54.387  1.00 62.97           O  
HETATM 3217  C2  OLA A4001     -14.548   4.478  52.418  1.00 59.91           C  
HETATM 3218  C3  OLA A4001     -13.457   3.690  51.710  1.00 58.72           C  
HETATM 3219  C4  OLA A4001     -13.309   4.026  50.229  1.00 57.71           C  
HETATM 3220  C5  OLA A4001     -13.729   2.849  49.370  1.00 56.22           C  
HETATM 3221  C6  OLA A4001     -13.815   3.188  47.893  1.00 54.85           C  
HETATM 3222  C7  OLA A4001     -13.288   2.024  47.078  1.00 53.13           C  
HETATM 3223  C8  OLA A4001     -12.554   2.460  45.828  1.00 51.66           C  
HETATM 3224  C9  OLA A4001     -11.721   1.300  45.364  1.00 49.68           C  
HETATM 3225  C10 OLA A4001     -11.136   1.258  44.181  1.00 47.61           C  
HETATM 3226  C11 OLA A4001     -11.262   2.378  43.200  1.00 47.10           C  
HETATM 3227  C12 OLA A4001     -11.682   1.843  41.844  1.00 46.63           C  
HETATM 3228  C13 OLA A4001     -12.340   2.952  41.066  1.00 45.48           C  
HETATM 3229  C14 OLA A4001     -13.447   2.438  40.198  1.00 44.20           C  
HETATM 3230  C15 OLA A4001     -14.364   3.595  39.865  1.00 43.84           C  
HETATM 3231  C16 OLA A4001     -15.111   3.413  38.562  1.00 43.51           C  
HETATM 3232  C17 OLA A4001     -16.545   2.991  38.788  1.00 41.18           C  
HETATM 3233  C18 OLA A4001     -17.464   3.764  37.906  1.00 39.65           C  
HETATM 3234  C1  OLA A4002     -42.100 -15.116  55.631  1.00 68.31           C  
HETATM 3235  O1  OLA A4002     -42.074 -16.181  56.248  1.00 68.95           O  
HETATM 3236  O2  OLA A4002     -41.994 -14.036  56.212  1.00 68.48           O  
HETATM 3237  C2  OLA A4002     -42.257 -15.132  54.139  1.00 66.39           C  
HETATM 3238  C3  OLA A4002     -43.253 -14.095  53.650  1.00 64.18           C  
HETATM 3239  C4  OLA A4002     -42.852 -13.434  52.335  1.00 61.91           C  
HETATM 3240  C5  OLA A4002     -43.164 -14.334  51.157  1.00 61.14           C  
HETATM 3241  C6  OLA A4002     -43.866 -13.601  50.028  1.00 59.57           C  
HETATM 3242  C7  OLA A4002     -43.117 -13.834  48.731  1.00 57.70           C  
HETATM 3243  C8  OLA A4002     -43.859 -13.322  47.515  1.00 56.88           C  
HETATM 3244  C9  OLA A4002     -43.501 -14.237  46.381  1.00 56.66           C  
HETATM 3245  C10 OLA A4002     -44.183 -14.301  45.252  1.00 56.06           C  
HETATM 3246  C11 OLA A4002     -45.118 -13.219  44.821  1.00 56.05           C  
HETATM 3247  C12 OLA A4002     -45.435 -13.375  43.344  1.00 56.26           C  
HETATM 3248  C13 OLA A4002     -46.490 -12.371  42.959  1.00 55.56           C  
HETATM 3249  C1  OLA A4003     -11.035 -20.277  55.962  1.00 62.41           C  
HETATM 3250  O1  OLA A4003     -10.784 -21.341  56.526  1.00 62.74           O  
HETATM 3251  O2  OLA A4003     -11.177 -19.232  56.599  1.00 61.30           O  
HETATM 3252  C2  OLA A4003     -11.177 -20.251  54.468  1.00 62.80           C  
HETATM 3253  C3  OLA A4003      -9.834 -20.407  53.770  1.00 63.90           C  
HETATM 3254  C4  OLA A4003      -9.942 -20.913  52.334  1.00 64.51           C  
HETATM 3255  C5  OLA A4003      -8.567 -21.246  51.784  1.00 64.75           C  
HETATM 3256  C6  OLA A4003      -8.615 -22.217  50.619  1.00 64.70           C  
HETATM 3257  C7  OLA A4003      -7.556 -21.839  49.602  1.00 65.77           C  
HETATM 3258  C8  OLA A4003      -8.150 -21.328  48.306  1.00 67.13           C  
HETATM 3259  C9  OLA A4003      -7.056 -21.298  47.277  1.00 67.90           C  
HETATM 3260  C10 OLA A4003      -7.113 -20.567  46.177  1.00 68.30           C  
HETATM 3261  C11 OLA A4003      -8.167 -19.528  45.964  1.00 68.51           C  
HETATM 3262  C12 OLA A4003      -8.554 -19.460  44.498  1.00 68.39           C  
HETATM 3263  C1  OLA A4004     -35.673 -15.097  57.567  1.00 70.43           C  
HETATM 3264  O1  OLA A4004     -36.467 -15.899  58.057  1.00 70.67           O  
HETATM 3265  O2  OLA A4004     -34.830 -14.529  58.260  1.00 70.59           O  
HETATM 3266  C2  OLA A4004     -35.728 -14.807  56.096  1.00 69.71           C  
HETATM 3267  C3  OLA A4004     -36.356 -15.963  55.335  1.00 68.73           C  
HETATM 3268  C4  OLA A4004     -36.593 -15.685  53.855  1.00 68.36           C  
HETATM 3269  C5  OLA A4004     -38.071 -15.782  53.535  1.00 68.43           C  
HETATM 3270  C6  OLA A4004     -38.339 -16.261  52.121  1.00 69.03           C  
HETATM 3271  C7  OLA A4004     -39.823 -16.153  51.835  1.00 69.92           C  
HETATM 3272  C8  OLA A4004     -40.189 -16.398  50.387  1.00 70.58           C  
HETATM 3273  C9  OLA A4004     -39.778 -17.799  50.041  1.00 70.83           C  
HETATM 3274  C10 OLA A4004     -40.339 -18.488  49.066  1.00 70.68           C  
HETATM 3275  C11 OLA A4004     -41.520 -17.962  48.315  1.00 70.24           C  
HETATM 3276  C1  2U8 A4005     -24.942  -6.788  40.839  1.00 25.78           C  
HETATM 3277  N1  2U8 A4005     -20.796  -4.351  45.504  1.00 38.89           N  
HETATM 3278  O1  2U8 A4005     -24.983  -2.980  43.763  1.00 29.11           O  
HETATM 3279  C2  2U8 A4005     -25.145  -8.081  41.352  1.00 24.28           C  
HETATM 3280  O2  2U8 A4005     -18.766  -5.390  45.075  1.00 38.91           O  
HETATM 3281  C3  2U8 A4005     -25.150  -6.538  39.467  1.00 24.22           C  
HETATM 3282  O3  2U8 A4005     -19.514  -5.179  47.189  1.00 38.22           O  
HETATM 3283  C4  2U8 A4005     -24.502  -5.688  41.696  1.00 30.10           C  
HETATM 3284  C5  2U8 A4005     -25.556  -9.119  40.514  1.00 24.83           C  
HETATM 3285  C6  2U8 A4005     -25.770  -8.881  39.145  1.00 26.41           C  
HETATM 3286  C7  2U8 A4005     -25.569  -7.587  38.612  1.00 25.53           C  
HETATM 3287  C8  2U8 A4005     -25.793  -7.315  37.147  1.00 23.97           C  
HETATM 3288  C9  2U8 A4005     -24.194  -4.764  42.440  1.00 31.31           C  
HETATM 3289  C10 2U8 A4005     -23.827  -3.601  43.276  1.00 30.79           C  
HETATM 3290  C11 2U8 A4005     -23.077  -2.506  42.466  1.00 42.60           C  
HETATM 3291  C12 2U8 A4005     -21.692  -2.942  41.942  1.00 42.50           C  
HETATM 3292  C13 2U8 A4005     -20.769  -3.554  43.001  1.00 40.66           C  
HETATM 3293  C14 2U8 A4005     -21.402  -4.344  44.173  1.00 38.93           C  
HETATM 3294  C15 2U8 A4005     -22.923  -4.161  44.413  1.00 37.01           C  
HETATM 3295  C16 2U8 A4005     -23.006  -3.423  45.759  1.00 37.01           C  
HETATM 3296  C17 2U8 A4005     -21.670  -3.680  46.464  1.00 36.76           C  
HETATM 3297  C18 2U8 A4005     -19.561  -4.900  45.877  1.00 38.89           C  
HETATM 3298  C19 2U8 A4005     -18.397  -5.879  47.715  1.00 36.91           C  
HETATM 3299  O1  MES A4006     -32.505  -2.537  63.358  1.00 50.10           O  
HETATM 3300  C2  MES A4006     -31.754  -3.731  63.123  1.00 50.82           C  
HETATM 3301  C3  MES A4006     -30.310  -3.427  62.719  1.00 51.17           C  
HETATM 3302  N4  MES A4006     -30.203  -2.326  61.767  1.00 50.79           N  
HETATM 3303  C5  MES A4006     -30.980  -1.151  62.208  1.00 50.48           C  
HETATM 3304  C6  MES A4006     -32.437  -1.564  62.336  1.00 49.91           C  
HETATM 3305  C7  MES A4006     -28.794  -1.929  61.674  1.00 50.95           C  
HETATM 3306  C8  MES A4006     -27.862  -3.072  61.323  1.00 51.36           C  
HETATM 3307  S   MES A4006     -26.994  -2.741  59.968  1.00 39.21           S  
HETATM 3308  O1S MES A4006     -27.824  -3.031  58.830  1.00 40.56           O  
HETATM 3309  O2S MES A4006     -26.618  -1.351  59.872  1.00 38.68           O  
HETATM 3310  O3S MES A4006     -25.838  -3.591  59.957  1.00 40.83           O  
HETATM 3311  O   HOH A4101     -18.165 -11.128  58.490  1.00 49.05           O  
HETATM 3312  O   HOH A4102     -20.999   9.550  53.993  1.00 31.52           O  
HETATM 3313  O   HOH A4103     -17.294   0.638  10.641  1.00 26.83           O  
HETATM 3314  O   HOH A4104     -20.218   3.108  18.179  1.00 34.47           O  
HETATM 3315  O   HOH A4105      -6.161  -2.321 -10.345  1.00 29.80           O  
HETATM 3316  O   HOH A4106      -7.300   6.549  -8.765  1.00 19.91           O  
HETATM 3317  O   HOH A4107      -1.416   3.728  -1.663  1.00 14.84           O  
HETATM 3318  O   HOH A4108      -6.291  -4.116  -5.059  1.00 32.35           O  
HETATM 3319  O   HOH A4109     -36.197 -24.203  61.565  1.00 64.06           O  
HETATM 3320  O   HOH A4110     -23.680   8.952  19.501  1.00 45.00           O  
HETATM 3321  O   HOH A4111     -25.120   7.052  24.171  1.00 29.77           O  
HETATM 3322  O   HOH A4112     -14.905  -6.880   7.171  1.00 56.36           O  
HETATM 3323  O   HOH A4113     -15.354 -10.265  50.539  1.00 44.14           O  
HETATM 3324  O   HOH A4114     -21.399  -5.818  56.324  1.00 47.75           O  
HETATM 3325  O   HOH A4115       8.086  18.019   2.503  1.00 33.42           O  
HETATM 3326  O   HOH A4116     -10.101  16.485   7.592  1.00 29.52           O  
HETATM 3327  O   HOH A4117     -23.866  17.606   3.109  1.00 39.16           O  
HETATM 3328  O   HOH A4118     -23.174  11.308 -15.043  1.00 21.58           O  
HETATM 3329  O   HOH A4119     -13.901 -11.790  52.129  1.00 19.50           O  
HETATM 3330  O   HOH A4120      10.286  11.680  16.740  1.00 29.23           O  
HETATM 3331  O   HOH A4121       4.408   4.790  16.818  1.00 25.59           O  
HETATM 3332  O   HOH A4122      -5.484   9.225   7.696  1.00 23.35           O  
HETATM 3333  O   HOH A4123     -14.229  13.156   7.110  1.00 37.69           O  
HETATM 3334  O   HOH A4124     -26.093  16.087  -0.627  1.00 50.10           O  
HETATM 3335  O   HOH A4125     -23.289   0.514 -17.953  1.00 17.66           O  
HETATM 3336  O   HOH A4126     -26.249  -3.174  36.239  1.00 25.55           O  
HETATM 3337  O   HOH A4127     -44.562 -10.315  14.984  1.00 33.11           O  
HETATM 3338  O   HOH A4128     -28.474 -24.108  56.635  1.00 27.73           O  
HETATM 3339  O   HOH A4129     -27.599 -22.996  53.689  1.00 35.69           O  
HETATM 3340  O   HOH A4130       5.431  15.601  -0.338  1.00 37.22           O  
HETATM 3341  O   HOH A4131     -40.619  -6.698  57.581  1.00 22.39           O  
HETATM 3342  O   HOH A4132       6.537  17.195  16.961  1.00 50.22           O  
HETATM 3343  O   HOH A4133       3.024   2.522  15.161  1.00 30.00           O  
HETATM 3344  O   HOH A4134      -0.970  -3.642   9.214  1.00 49.78           O  
HETATM 3345  O   HOH A4135     -14.296   5.504  12.171  1.00 47.12           O  
HETATM 3346  O   HOH A4136      -8.070  10.935   7.951  1.00 29.06           O  
HETATM 3347  O   HOH A4137      -8.205   7.911  -6.612  1.00 30.59           O  
HETATM 3348  O   HOH A4138     -15.070   6.495  -4.743  1.00 24.71           O  
HETATM 3349  O   HOH A4139     -24.149  12.349 -12.035  1.00 50.51           O  
HETATM 3350  O   HOH A4140     -25.320  -4.166  18.931  1.00 17.84           O  
HETATM 3351  O   HOH A4141      -3.387  -0.330  10.000  1.00 57.85           O  
HETATM 3352  O   HOH A4142      -5.483  10.859  -3.040  1.00 49.21           O  
HETATM 3353  O   HOH A4143       0.000   5.845   0.000  0.50 34.00           O  
HETATM 3354  O   HOH A4144      -1.209   2.522  -4.263  1.00 29.09           O  
HETATM 3355  O   HOH A4145     -28.161  -5.605   2.130  1.00 35.84           O  
HETATM 3356  O   HOH A4146     -20.174  -7.154   5.803  1.00 46.23           O  
CONECT  500  509                                                                
CONECT  509  500  510                                                           
CONECT  510  509  511  517                                                      
CONECT  511  510  512                                                           
CONECT  512  511  513                                                           
CONECT  513  512  514                                                           
CONECT  514  513  515  516                                                      
CONECT  515  514                                                                
CONECT  516  514                                                                
CONECT  517  510  518  519                                                      
CONECT  518  517                                                                
CONECT  519  517                                                                
CONECT  599 2437                                                                
CONECT 2162 2165                                                                
CONECT 2165 2162 2166                                                           
CONECT 2166 2165 2167 2173                                                      
CONECT 2167 2166 2168                                                           
CONECT 2168 2167 2169                                                           
CONECT 2169 2168 2170                                                           
CONECT 2170 2169 2171 2172                                                      
CONECT 2171 2170                                                                
CONECT 2172 2170                                                                
CONECT 2173 2166 2174 2175                                                      
CONECT 2174 2173                                                                
CONECT 2175 2173                                                                
CONECT 2437  599                                                                
CONECT 3214 3215 3216 3217                                                      
CONECT 3215 3214                                                                
CONECT 3216 3214                                                                
CONECT 3217 3214 3218                                                           
CONECT 3218 3217 3219                                                           
CONECT 3219 3218 3220                                                           
CONECT 3220 3219 3221                                                           
CONECT 3221 3220 3222                                                           
CONECT 3222 3221 3223                                                           
CONECT 3223 3222 3224                                                           
CONECT 3224 3223 3225                                                           
CONECT 3225 3224 3226                                                           
CONECT 3226 3225 3227                                                           
CONECT 3227 3226 3228                                                           
CONECT 3228 3227 3229                                                           
CONECT 3229 3228 3230                                                           
CONECT 3230 3229 3231                                                           
CONECT 3231 3230 3232                                                           
CONECT 3232 3231 3233                                                           
CONECT 3233 3232                                                                
CONECT 3234 3235 3236 3237                                                      
CONECT 3235 3234                                                                
CONECT 3236 3234                                                                
CONECT 3237 3234 3238                                                           
CONECT 3238 3237 3239                                                           
CONECT 3239 3238 3240                                                           
CONECT 3240 3239 3241                                                           
CONECT 3241 3240 3242                                                           
CONECT 3242 3241 3243                                                           
CONECT 3243 3242 3244                                                           
CONECT 3244 3243 3245                                                           
CONECT 3245 3244 3246                                                           
CONECT 3246 3245 3247                                                           
CONECT 3247 3246 3248                                                           
CONECT 3248 3247                                                                
CONECT 3249 3250 3251 3252                                                      
CONECT 3250 3249                                                                
CONECT 3251 3249                                                                
CONECT 3252 3249 3253                                                           
CONECT 3253 3252 3254                                                           
CONECT 3254 3253 3255                                                           
CONECT 3255 3254 3256                                                           
CONECT 3256 3255 3257                                                           
CONECT 3257 3256 3258                                                           
CONECT 3258 3257 3259                                                           
CONECT 3259 3258 3260                                                           
CONECT 3260 3259 3261                                                           
CONECT 3261 3260 3262                                                           
CONECT 3262 3261                                                                
CONECT 3263 3264 3265 3266                                                      
CONECT 3264 3263                                                                
CONECT 3265 3263                                                                
CONECT 3266 3263 3267                                                           
CONECT 3267 3266 3268                                                           
CONECT 3268 3267 3269                                                           
CONECT 3269 3268 3270                                                           
CONECT 3270 3269 3271                                                           
CONECT 3271 3270 3272                                                           
CONECT 3272 3271 3273                                                           
CONECT 3273 3272 3274                                                           
CONECT 3274 3273 3275                                                           
CONECT 3275 3274                                                                
CONECT 3276 3279 3281 3283                                                      
CONECT 3277 3293 3296 3297                                                      
CONECT 3278 3289                                                                
CONECT 3279 3276 3284                                                           
CONECT 3280 3297                                                                
CONECT 3281 3276 3286                                                           
CONECT 3282 3297 3298                                                           
CONECT 3283 3276 3288                                                           
CONECT 3284 3279 3285                                                           
CONECT 3285 3284 3286                                                           
CONECT 3286 3281 3285 3287                                                      
CONECT 3287 3286                                                                
CONECT 3288 3283 3289                                                           
CONECT 3289 3278 3288 3290 3294                                                 
CONECT 3290 3289 3291                                                           
CONECT 3291 3290 3292                                                           
CONECT 3292 3291 3293                                                           
CONECT 3293 3277 3292 3294                                                      
CONECT 3294 3289 3293 3295                                                      
CONECT 3295 3294 3296                                                           
CONECT 3296 3277 3295                                                           
CONECT 3297 3277 3280 3282                                                      
CONECT 3298 3282                                                                
CONECT 3299 3300 3304                                                           
CONECT 3300 3299 3301                                                           
CONECT 3301 3300 3302                                                           
CONECT 3302 3301 3303 3305                                                      
CONECT 3303 3302 3304                                                           
CONECT 3304 3299 3303                                                           
CONECT 3305 3302 3306                                                           
CONECT 3306 3305 3307                                                           
CONECT 3307 3306 3308 3309 3310                                                 
CONECT 3308 3307                                                                
CONECT 3309 3307                                                                
CONECT 3310 3307                                                                
MASTER      355    0    8   20    3    0   11    6 3355    1  123   35          
END