HEADER    MEMBRANE PROTEIN                        08-JAN-18   6FFH              
TITLE     CRYSTAL STRUCTURE OF MGLUR5 IN COMPLEX WITH FENOBAM AT 2.65 A         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METABOTROPIC GLUTAMATE RECEPTOR 5,ENDOLYSIN;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: MGLUR5;                                                    
COMPND   5 SYNONYM: MGLUR5,LYSIS PROTEIN,LYSOZYME,MURAMIDASE;                   
COMPND   6 EC: 3.2.1.17;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: CHIMERIC CONSTRUCT OF HUMAN MGLU5 (GRM5) WITH A       
COMPND  10 BACTERIOPHAGE T4 LYSOZYME (P00720) INSERTION IN INTRACELLULAR LOOP 2 
COMPND  11 BETWEEN RESIDUES LYS678 AND LYS679.                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          
SOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            
SOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   5 GENE: GRM5, GPRC1E, MGLUR5;                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID                                
KEYWDS    7TM, RECEPTOR, GPCR, MEMBRANE-PROTEIN, SIGNALING PROTEIN, MEMBRANE    
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.CHRISTOPHER,Z.ORGOVAN,M.CONGREVE,A.S.DORE,J.C.ERREY,F.H.MARSHALL, 
AUTHOR   2 J.S.MASON,K.OKRASA,P.RUCKTOOA,M.J.SERRANO-VEGA,G.G.FERENCZY,         
AUTHOR   3 G.M.KESERU                                                           
REVDAT   4   24-APR-19 6FFH    1       SOURCE JRNL                              
REVDAT   3   28-MAR-18 6FFH    1       JRNL                                     
REVDAT   2   14-MAR-18 6FFH    1       COMPND JRNL                              
REVDAT   1   07-MAR-18 6FFH    0                                                
JRNL        AUTH   J.A.CHRISTOPHER,Z.ORGOVAN,M.CONGREVE,A.S.DORE,J.C.ERREY,     
JRNL        AUTH 2 F.H.MARSHALL,J.S.MASON,K.OKRASA,P.RUCKTOOA,M.J.SERRANO-VEGA, 
JRNL        AUTH 3 G.G.FERENCZY,G.M.KESERU                                      
JRNL        TITL   STRUCTURE-BASED OPTIMIZATION STRATEGIES FOR G                
JRNL        TITL 2 PROTEIN-COUPLED RECEPTOR (GPCR) ALLOSTERIC MODULATORS: A     
JRNL        TITL 3 CASE STUDY FROM ANALYSES OF NEW METABOTROPIC GLUTAMATE       
JRNL        TITL 4 RECEPTOR 5 (MGLU5) X-RAY STRUCTURES.                         
JRNL        REF    J.MED.CHEM.                   V.  62   207 2019              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   29455526                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B01722                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.12_2829                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 13073                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.245                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.370                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 702                             
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 34.4988 -  4.5288    0.85     2462   152  0.2169 0.2306        
REMARK   3     2  4.5288 -  3.5959    0.88     2485   127  0.2183 0.2225        
REMARK   3     3  3.5959 -  3.1417    0.87     2431   130  0.2577 0.3290        
REMARK   3     4  3.1417 -  2.8546    0.89     2478   153  0.2864 0.3008        
REMARK   3     5  2.8546 -  2.6501    0.90     2515   140  0.3245 0.3589        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.980           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.57                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           3418                                  
REMARK   3   ANGLE     :  0.443           4606                                  
REMARK   3   CHIRALITY :  0.036            531                                  
REMARK   3   PLANARITY :  0.003            563                                  
REMARK   3   DIHEDRAL  : 13.706           2055                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A): -25.2155  13.3972  39.8191              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1877 T22:   0.1919                                     
REMARK   3      T33:   0.3177 T12:  -0.0433                                     
REMARK   3      T13:  -0.0362 T23:  -0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5543 L22:   1.6790                                     
REMARK   3      L33:   1.7860 L12:  -0.1201                                     
REMARK   3      L13:  -0.3184 L23:  -0.5306                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0690 S12:   0.0647 S13:  -0.2065                       
REMARK   3      S21:  -0.0583 S22:  -0.0148 S23:   0.0432                       
REMARK   3      S31:  -0.0364 S32:  -0.1055 S33:  -0.0602                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A): -13.5996  29.8593   1.7566              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3182 T22:   0.4581                                     
REMARK   3      T33:   0.3298 T12:   0.0635                                     
REMARK   3      T13:   0.0088 T23:  -0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4280 L22:   1.2474                                     
REMARK   3      L33:   2.5885 L12:  -0.4018                                     
REMARK   3      L13:   0.6212 L23:   0.4220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3314 S12:  -0.6038 S13:   0.3497                       
REMARK   3      S21:   0.1200 S22:   0.0585 S23:   0.1434                       
REMARK   3      S31:  -0.3017 S32:  -0.4374 S33:   0.2366                       
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 6FFH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008050.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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) : 0.96862                            
REMARK 200  MONOCHROMATOR                  : SI                                 
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 0.2.17                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13189                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.8                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.15600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.89300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4OO9                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
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       71.60850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.73900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       71.60850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       21.73900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A   566                                                      
REMARK 465     ALA A   567                                                      
REMARK 465     CYS A  1681                                                      
REMARK 465     THR A  1682                                                      
REMARK 465     LYS A  1683                                                      
REMARK 465     LYS A  1684                                                      
REMARK 465     PRO A  1685                                                      
REMARK 465     ARG A  1686                                                      
REMARK 465     PHE A  1687                                                      
REMARK 465     MET A  1688                                                      
REMARK 465     SER A  1725                                                      
REMARK 465     ILE A  1726                                                      
REMARK 465     ARG A  1727                                                      
REMARK 465     VAL A  1833                                                      
REMARK 465     ARG A  1834                                                      
REMARK 465     SER A  1835                                                      
REMARK 465     ALA A  1836                                                      
REMARK 465     ALA A  1837                                                      
REMARK 465     ALA A  1838                                                      
REMARK 465     ALA A  1839                                                      
REMARK 465     HIS A  1840                                                      
REMARK 465     HIS A  1841                                                      
REMARK 465     HIS A  1842                                                      
REMARK 465     HIS A  1843                                                      
REMARK 465     HIS A  1844                                                      
REMARK 465     HIS A  1845                                                      
REMARK 465     HIS A  1846                                                      
REMARK 465     HIS A  1847                                                      
REMARK 465     HIS A  1848                                                      
REMARK 465     HIS A  1849                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A1721    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A1722    CG   OD1  OD2                                       
REMARK 470     TYR A1723    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PRO A1724    CG   CD                                             
REMARK 470     GLU A1728    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A 604       47.50    -89.71                                   
REMARK 500    PRO A 639       82.28    -65.13                                   
REMARK 500    ASP A1020     -166.56    -79.09                                   
REMARK 500    ARG A1154      -73.70    -68.12                                   
REMARK 500    HIS A1721      179.05     59.61                                   
REMARK 500    TYR A1723     -139.05   -103.59                                   
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 610     OLC A 4008                                                       
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 MES A 4005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D7W A 4006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 4007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 4008                
DBREF  6FFH A  569   678  UNP    P41594   GRM5_HUMAN     569    678             
DBREF  6FFH A 1002  1161  UNP    P00720   ENLYS_BPT4       2    161             
DBREF  6FFH A 1679  1836  UNP    P41594   GRM5_HUMAN     679    836             
SEQADV 6FFH ALA A  566  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH ALA A  567  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH SER A  568  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH ALA A  579  UNP  P41594    GLU   579 ENGINEERED MUTATION            
SEQADV 6FFH TYR A  667  UNP  P41594    ASN   667 ENGINEERED MUTATION            
SEQADV 6FFH ALA A  669  UNP  P41594    ILE   669 ENGINEERED MUTATION            
SEQADV 6FFH MET A  675  UNP  P41594    GLY   675 ENGINEERED MUTATION            
SEQADV 6FFH GLY A 1012  UNP  P00720    ARG    12 CONFLICT                       
SEQADV 6FFH THR A 1054  UNP  P00720    CYS    54 ENGINEERED MUTATION            
SEQADV 6FFH ALA A 1097  UNP  P00720    CYS    97 ENGINEERED MUTATION            
SEQADV 6FFH ARG A 1137  UNP  P00720    ILE   137 CONFLICT                       
SEQADV 6FFH ALA A 1742  UNP  P41594    THR   742 ENGINEERED MUTATION            
SEQADV 6FFH ALA A 1753  UNP  P41594    SER   753 ENGINEERED MUTATION            
SEQADV 6FFH ALA A 1837  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH ALA A 1838  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH ALA A 1839  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH HIS A 1840  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH HIS A 1841  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH HIS A 1842  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH HIS A 1843  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH HIS A 1844  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH HIS A 1845  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH HIS A 1846  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH HIS A 1847  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH HIS A 1848  UNP  P41594              EXPRESSION TAG                 
SEQADV 6FFH HIS A 1849  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 CYS          
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 6FFH YCM A  634  CYS  MODIFIED RESIDUE                                   
HET    YCM  A 634      10                                                       
HET    OLA  A4001      20                                                       
HET    OLA  A4002      15                                                       
HET    OLA  A4003      14                                                       
HET    OLA  A4004      13                                                       
HET    MES  A4005      12                                                       
HET    D7W  A4006      18                                                       
HET    OLA  A4007      20                                                       
HET    OLC  A4008      13                                                       
HETNAM     YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                                
HETNAM     OLA OLEIC ACID                                                       
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     D7W 1-(3-CHLOROPHENYL)-3-(3-METHYL-5-OXIDANYLIDENE-4~{H}-            
HETNAM   2 D7W  IMIDAZOL-2-YL)UREA                                              
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETSYN     YCM CYSTEINE-S-ACETAMIDE                                             
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   1  YCM    C5 H10 N2 O3 S                                               
FORMUL   2  OLA    5(C18 H34 O2)                                                
FORMUL   6  MES    C6 H13 N O4 S                                                
FORMUL   7  D7W    C11 H11 CL N4 O2                                             
FORMUL   9  OLC    C21 H40 O4                                                   
FORMUL  10  HOH   *13(H2 O)                                                     
HELIX    1 AA1 SER A  568  TRP A  575  1                                   8    
HELIX    2 AA2 PRO A  578  TYR A  604  1                                  27    
HELIX    3 AA3 THR A  607  SER A  613  1                                   7    
HELIX    4 AA4 SER A  614  CYS A  631  1                                  18    
HELIX    5 AA5 CYS A  631  ILE A  636  1                                   6    
HELIX    6 AA6 LYS A  640  LYS A  678  1                                  39    
HELIX    7 AA7 ILE A 1003  GLU A 1011  1                                   9    
HELIX    8 AA8 SER A 1038  GLY A 1051  1                                  14    
HELIX    9 AA9 THR A 1059  ARG A 1080  1                                  22    
HELIX   10 AB1 LEU A 1084  LEU A 1091  1                                   8    
HELIX   11 AB2 ASP A 1092  GLY A 1107  1                                  16    
HELIX   12 AB3 GLY A 1107  ALA A 1112  1                                   6    
HELIX   13 AB4 PHE A 1114  GLN A 1123  1                                  10    
HELIX   14 AB5 ARG A 1125  ALA A 1134  1                                  10    
HELIX   15 AB6 SER A 1136  THR A 1142  1                                   7    
HELIX   16 AB7 THR A 1142  GLY A 1156  1                                  15    
HELIX   17 AB8 ALA A 1690  GLU A 1715  1                                  26    
HELIX   18 AB9 THR A 1736  THR A 1761  1                                  26    
HELIX   19 AC1 PRO A 1765  GLY A 1794  1                                  30    
HELIX   20 AC2 TYR A 1797  PHE A 1818  1                                  22    
HELIX   21 AC3 PHE A 1818  LYS A 1828  1                                  11    
SHEET    1 AA1 3 ARG A1014  LYS A1019  0                                        
SHEET    2 AA1 3 TYR A1025  GLY A1028 -1  O  THR A1026   N  TYR A1018           
SHEET    3 AA1 3 HIS A1031  THR A1034 -1  O  LEU A1033   N  TYR A1025           
SSBOND   1 CYS A  644    CYS A 1733                          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  
SITE     1 AC1  4 ASN A1737  LEU A1744  LEU A1752  LEU A1786                    
SITE     1 AC2  3 CYS A 588  LEU A 589  OLA A4004                               
SITE     1 AC3  4 TYR A 645  VAL A1709  PHE A1712  OLC A4008                    
SITE     1 AC4  5 PRO A 569  CYS A 588  PHE A 633  ILE A 636                    
SITE     2 AC4  5 OLA A4002                                                     
SITE     1 AC5  7 TYR A1139  LYS A1147  TYR A1730  ASN A1796                    
SITE     2 AC5  7 TYR A1797  LYS A1798  ILE A1799                               
SITE     1 AC6 14 GLY A 624  ILE A 625  GLY A 628  SER A 654                    
SITE     2 AC6 14 PRO A 655  SER A 658  TYR A 659  LEU A1744                    
SITE     3 AC6 14 TRP A1785  PHE A1788  MET A1802  VAL A1806                    
SITE     4 AC6 14 SER A1809  ALA A1810                                          
SITE     1 AC7  3 LEU A1786  VAL A1789  PRO A1790                               
SITE     1 AC8  4 TYR A 645  LEU A 646  ILE A 649  OLA A4003                    
CRYST1  143.217   43.478   82.383  90.00  99.22  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      0.006982  0.000000  0.001133        0.00000                         
SCALE2      0.000000  0.023000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012297        0.00000                         
ATOM      1  N   SER A 568     -38.105   8.381  61.941  1.00 53.70           N  
ANISOU    1  N   SER A 568     5605   8014   6786   -372    984   1930       N  
ATOM      2  CA  SER A 568     -39.154   8.446  60.929  1.00 53.30           C  
ANISOU    2  CA  SER A 568     5428   7878   6947   -380   1004   1896       C  
ATOM      3  C   SER A 568     -39.375   9.876  60.440  1.00 52.33           C  
ANISOU    3  C   SER A 568     5371   7759   6752   -283   1025   1675       C  
ATOM      4  O   SER A 568     -39.666  10.769  61.237  1.00 52.70           O  
ANISOU    4  O   SER A 568     5479   7942   6603   -187   1145   1620       O  
ATOM      5  CB  SER A 568     -40.461   7.872  61.481  1.00 54.87           C  
ANISOU    5  CB  SER A 568     5460   8181   7207   -392   1153   2096       C  
ATOM      6  OG  SER A 568     -41.508   7.992  60.534  1.00 54.58           O  
ANISOU    6  OG  SER A 568     5285   8086   7367   -400   1165   2063       O  
ATOM      7  N   PRO A 569     -39.226  10.094  59.130  1.00 51.30           N  
ANISOU    7  N   PRO A 569     5235   7476   6781   -304    913   1550       N  
ATOM      8  CA  PRO A 569     -39.485  11.436  58.582  1.00 50.89           C  
ANISOU    8  CA  PRO A 569     5237   7412   6688   -208    933   1365       C  
ATOM      9  C   PRO A 569     -40.917  11.904  58.779  1.00 52.86           C  
ANISOU    9  C   PRO A 569     5367   7765   6951   -126   1086   1406       C  
ATOM     10  O   PRO A 569     -41.161  13.116  58.832  1.00 52.18           O  
ANISOU   10  O   PRO A 569     5346   7712   6768    -12   1158   1278       O  
ATOM     11  CB  PRO A 569     -39.143  11.278  57.093  1.00 48.78           C  
ANISOU   11  CB  PRO A 569     4952   6973   6609   -264    781   1279       C  
ATOM     12  CG  PRO A 569     -38.233  10.098  57.031  1.00 48.35           C  
ANISOU   12  CG  PRO A 569     4910   6836   6627   -371    672   1356       C  
ATOM     13  CD  PRO A 569     -38.699   9.170  58.112  1.00 49.92           C  
ANISOU   13  CD  PRO A 569     5025   7132   6810   -407    763   1562       C  
ATOM     14  N   VAL A 570     -41.874  10.979  58.886  1.00 55.58           N  
ANISOU   14  N   VAL A 570     5533   8157   7429   -179   1142   1586       N  
ATOM     15  CA  VAL A 570     -43.256  11.368  59.145  1.00 57.78           C  
ANISOU   15  CA  VAL A 570     5672   8555   7725   -100   1299   1648       C  
ATOM     16  C   VAL A 570     -43.408  11.903  60.565  1.00 60.71           C  
ANISOU   16  C   VAL A 570     6113   9102   7852      1   1477   1671       C  
ATOM     17  O   VAL A 570     -44.251  12.772  60.822  1.00 62.69           O  
ANISOU   17  O   VAL A 570     6329   9446   8045    124   1620   1630       O  
ATOM     18  CB  VAL A 570     -44.199  10.178  58.880  1.00 58.04           C  
ANISOU   18  CB  VAL A 570     5481   8590   7979   -206   1304   1841       C  
ATOM     19  CG1 VAL A 570     -45.653  10.585  59.071  1.00 58.67           C  
ANISOU   19  CG1 VAL A 570     5387   8803   8100   -126   1462   1914       C  
ATOM     20  CG2 VAL A 570     -43.977   9.626  57.479  1.00 56.49           C  
ANISOU   20  CG2 VAL A 570     5238   8221   8004   -313   1117   1789       C  
ATOM     21  N   GLN A 571     -42.599  11.406  61.505  1.00 60.36           N  
ANISOU   21  N   GLN A 571     6169   9112   7654    -42   1473   1734       N  
ATOM     22  CA  GLN A 571     -42.662  11.906  62.875  1.00 61.01           C  
ANISOU   22  CA  GLN A 571     6336   9380   7467     49   1632   1742       C  
ATOM     23  C   GLN A 571     -42.239  13.367  62.952  1.00 59.43           C  
ANISOU   23  C   GLN A 571     6314   9174   7091    166   1652   1495       C  
ATOM     24  O   GLN A 571     -42.870  14.166  63.652  1.00 60.66           O  
ANISOU   24  O   GLN A 571     6494   9455   7100    288   1822   1444       O  
ATOM     25  CB  GLN A 571     -41.791  11.048  63.793  1.00 61.84           C  
ANISOU   25  CB  GLN A 571     6511   9548   7436    -27   1595   1868       C  
ATOM     26  CG  GLN A 571     -42.342   9.659  64.065  1.00 64.09           C  
ANISOU   26  CG  GLN A 571     6625   9866   7859   -122   1633   2146       C  
ATOM     27  CD  GLN A 571     -41.447   8.850  64.984  1.00 66.13           C  
ANISOU   27  CD  GLN A 571     6959  10187   7981   -181   1596   2288       C  
ATOM     28  OE1 GLN A 571     -40.342   9.275  65.324  1.00 66.16           O  
ANISOU   28  OE1 GLN A 571     7133  10206   7797   -162   1515   2172       O  
ATOM     29  NE2 GLN A 571     -41.920   7.679  65.392  1.00 67.93           N  
ANISOU   29  NE2 GLN A 571     7051  10452   8309   -255   1653   2551       N  
ATOM     30  N   TYR A 572     -41.171  13.737  62.242  1.00 57.25           N  
ANISOU   30  N   TYR A 572     6167   8749   6837    130   1488   1337       N  
ATOM     31  CA  TYR A 572     -40.747  15.131  62.224  1.00 56.06           C  
ANISOU   31  CA  TYR A 572     6184   8560   6554    224   1498   1102       C  
ATOM     32  C   TYR A 572     -41.726  16.021  61.472  1.00 54.37           C  
ANISOU   32  C   TYR A 572     5903   8290   6466    333   1574   1022       C  
ATOM     33  O   TYR A 572     -41.775  17.227  61.738  1.00 55.40           O  
ANISOU   33  O   TYR A 572     6148   8420   6480    448   1659    858       O  
ATOM     34  CB  TYR A 572     -39.351  15.250  61.614  1.00 54.80           C  
ANISOU   34  CB  TYR A 572     6158   8255   6407    147   1305    977       C  
ATOM     35  CG  TYR A 572     -38.231  14.998  62.599  1.00 55.68           C  
ANISOU   35  CG  TYR A 572     6400   8448   6308     93   1251    974       C  
ATOM     36  CD1 TYR A 572     -38.030  13.737  63.144  1.00 56.32           C  
ANISOU   36  CD1 TYR A 572     6412   8607   6379     11   1224   1177       C  
ATOM     37  CD2 TYR A 572     -37.373  16.020  62.980  1.00 56.08           C  
ANISOU   37  CD2 TYR A 572     6636   8495   6176    119   1221    775       C  
ATOM     38  CE1 TYR A 572     -37.006  13.502  64.045  1.00 57.39           C  
ANISOU   38  CE1 TYR A 572     6655   8834   6316    -30   1165   1193       C  
ATOM     39  CE2 TYR A 572     -36.346  15.796  63.879  1.00 57.13           C  
ANISOU   39  CE2 TYR A 572     6875   8723   6109     63   1155    773       C  
ATOM     40  CZ  TYR A 572     -36.166  14.535  64.408  1.00 57.99           C  
ANISOU   40  CZ  TYR A 572     6907   8928   6200     -6   1125    988       C  
ATOM     41  OH  TYR A 572     -35.144  14.308  65.303  1.00 59.36           O  
ANISOU   41  OH  TYR A 572     7175   9211   6168    -53   1050   1004       O  
ATOM     42  N   LEU A 573     -42.506  15.458  60.546  1.00 51.91           N  
ANISOU   42  N   LEU A 573     5406   7928   6390    300   1541   1133       N  
ATOM     43  CA  LEU A 573     -43.502  16.251  59.834  1.00 51.08           C  
ANISOU   43  CA  LEU A 573     5210   7793   6407    409   1607   1087       C  
ATOM     44  C   LEU A 573     -44.614  16.705  60.771  1.00 54.31           C  
ANISOU   44  C   LEU A 573     5551   8364   6722    544   1837   1133       C  
ATOM     45  O   LEU A 573     -44.949  17.894  60.823  1.00 56.48           O  
ANISOU   45  O   LEU A 573     5889   8629   6943    690   1940   1002       O  
ATOM     46  CB  LEU A 573     -44.076  15.450  58.664  1.00 49.42           C  
ANISOU   46  CB  LEU A 573     4804   7517   6456    326   1503   1200       C  
ATOM     47  CG  LEU A 573     -45.235  16.110  57.914  1.00 50.45           C  
ANISOU   47  CG  LEU A 573     4793   7649   6726    432   1559   1198       C  
ATOM     48  CD1 LEU A 573     -44.810  17.451  57.334  1.00 50.12           C  
ANISOU   48  CD1 LEU A 573     4899   7494   6651    540   1531   1009       C  
ATOM     49  CD2 LEU A 573     -45.763  15.193  56.821  1.00 50.00           C  
ANISOU   49  CD2 LEU A 573     4541   7552   6906    323   1434   1310       C  
ATOM     50  N   ARG A 574     -45.202  15.769  61.523  1.00 54.89           N  
ANISOU   50  N   ARG A 574     5493   8583   6780    501   1931   1323       N  
ATOM     51  CA  ARG A 574     -46.243  16.139  62.475  1.00 56.60           C  
ANISOU   51  CA  ARG A 574     5637   8976   6892    630   2168   1380       C  
ATOM     52  C   ARG A 574     -45.692  16.934  63.650  1.00 56.71           C  
ANISOU   52  C   ARG A 574     5868   9074   6604    722   2279   1237       C  
ATOM     53  O   ARG A 574     -46.461  17.621  64.331  1.00 58.16           O  
ANISOU   53  O   ARG A 574     6043   9375   6680    870   2485   1206       O  
ATOM     54  CB  ARG A 574     -46.970  14.892  62.984  1.00 58.13           C  
ANISOU   54  CB  ARG A 574     5632   9308   7148    548   2243   1640       C  
ATOM     55  CG  ARG A 574     -46.057  13.815  63.546  1.00 57.89           C  
ANISOU   55  CG  ARG A 574     5669   9292   7033    403   2153   1744       C  
ATOM     56  CD  ARG A 574     -46.782  12.959  64.573  1.00 60.47           C  
ANISOU   56  CD  ARG A 574     5858   9808   7311    380   2315   1985       C  
ATOM     57  NE  ARG A 574     -46.996  13.679  65.826  1.00 63.12           N  
ANISOU   57  NE  ARG A 574     6290  10333   7361    519   2523   1940       N  
ATOM     58  CZ  ARG A 574     -47.761  13.241  66.820  1.00 66.25           C  
ANISOU   58  CZ  ARG A 574     6604  10894   7676    539   2677   2094       C  
ATOM     59  NH1 ARG A 574     -48.398  12.084  66.709  1.00 67.21           N  
ANISOU   59  NH1 ARG A 574     6554  10985   7997    422   2629   2296       N  
ATOM     60  NH2 ARG A 574     -47.895  13.963  67.925  1.00 68.58           N  
ANISOU   60  NH2 ARG A 574     7021  11336   7699    665   2837   2004       N  
ATOM     61  N   TRP A 575     -44.386  16.861  63.901  1.00 55.31           N  
ANISOU   61  N   TRP A 575     5881   8846   6289    639   2148   1144       N  
ATOM     62  CA  TRP A 575     -43.760  17.629  64.970  1.00 55.43           C  
ANISOU   62  CA  TRP A 575     6113   8940   6009    703   2221    983       C  
ATOM     63  C   TRP A 575     -43.438  19.060  64.564  1.00 54.26           C  
ANISOU   63  C   TRP A 575     6128   8651   5838    803   2214    719       C  
ATOM     64  O   TRP A 575     -42.976  19.835  65.409  1.00 56.59           O  
ANISOU   64  O   TRP A 575     6612   8991   5898    860   2278    549       O  
ATOM     65  CB  TRP A 575     -42.486  16.927  65.447  1.00 54.60           C  
ANISOU   65  CB  TRP A 575     6125   8856   5765    566   2072   1008       C  
ATOM     66  CG  TRP A 575     -42.750  15.760  66.348  1.00 56.11           C  
ANISOU   66  CG  TRP A 575     6217   9230   5873    507   2139   1250       C  
ATOM     67  CD1 TRP A 575     -43.861  15.550  67.111  1.00 58.20           C  
ANISOU   67  CD1 TRP A 575     6362   9677   6075    582   2351   1393       C  
ATOM     68  CD2 TRP A 575     -41.890  14.636  66.573  1.00 55.68           C  
ANISOU   68  CD2 TRP A 575     6168   9189   5800    367   2001   1395       C  
ATOM     69  NE1 TRP A 575     -43.745  14.369  67.802  1.00 59.07           N  
ANISOU   69  NE1 TRP A 575     6407   9913   6125    489   2353   1624       N  
ATOM     70  CE2 TRP A 575     -42.545  13.787  67.488  1.00 57.63           C  
ANISOU   70  CE2 TRP A 575     6301   9624   5972    360   2138   1631       C  
ATOM     71  CE3 TRP A 575     -40.631  14.266  66.092  1.00 54.19           C  
ANISOU   71  CE3 TRP A 575     6061   8871   5656    254   1783   1357       C  
ATOM     72  CZ2 TRP A 575     -41.983  12.592  67.931  1.00 58.45           C  
ANISOU   72  CZ2 TRP A 575     6379   9778   6052    247   2060   1836       C  
ATOM     73  CZ3 TRP A 575     -40.074  13.078  66.533  1.00 54.57           C  
ANISOU   73  CZ3 TRP A 575     6078   8973   5682    149   1707   1552       C  
ATOM     74  CH2 TRP A 575     -40.750  12.256  67.444  1.00 56.79           C  
ANISOU   74  CH2 TRP A 575     6253   9430   5894    147   1842   1792       C  
ATOM     75  N   GLY A 576     -43.664  19.428  63.306  1.00 50.79           N  
ANISOU   75  N   GLY A 576     5624   8042   5633    821   2136    683       N  
ATOM     76  CA  GLY A 576     -43.450  20.783  62.845  1.00 45.26           C  
ANISOU   76  CA  GLY A 576     5061   7191   4945    922   2141    464       C  
ATOM     77  C   GLY A 576     -42.227  21.005  61.981  1.00 53.55           C  
ANISOU   77  C   GLY A 576     6235   8050   6061    820   1927    348       C  
ATOM     78  O   GLY A 576     -41.857  22.163  61.754  1.00 52.59           O  
ANISOU   78  O   GLY A 576     6262   7798   5922    886   1929    157       O  
ATOM     79  N   ASP A 577     -41.588  19.945  61.491  1.00 52.27           N  
ANISOU   79  N   ASP A 577     6018   7862   5982    665   1753    457       N  
ATOM     80  CA  ASP A 577     -40.406  20.062  60.638  1.00 49.41           C  
ANISOU   80  CA  ASP A 577     5755   7332   5686    567   1557    364       C  
ATOM     81  C   ASP A 577     -40.618  19.236  59.377  1.00 46.96           C  
ANISOU   81  C   ASP A 577     5282   6945   5618    491   1432    496       C  
ATOM     82  O   ASP A 577     -40.441  18.005  59.400  1.00 44.57           O  
ANISOU   82  O   ASP A 577     4890   6688   5358    378   1355    639       O  
ATOM     83  CB  ASP A 577     -39.149  19.616  61.374  1.00 48.37           C  
ANISOU   83  CB  ASP A 577     5751   7247   5382    451   1457    334       C  
ATOM     84  CG  ASP A 577     -37.905  19.728  60.519  1.00 44.88           C  
ANISOU   84  CG  ASP A 577     5395   6645   5014    352   1265    246       C  
ATOM     85  OD1 ASP A 577     -37.692  20.796  59.906  1.00 44.05           O  
ANISOU   85  OD1 ASP A 577     5378   6399   4959    399   1251     97       O  
ATOM     86  OD2 ASP A 577     -37.132  18.749  60.470  1.00 43.53           O  
ANISOU   86  OD2 ASP A 577     5200   6486   4853    232   1136    335       O  
ATOM     87  N   PRO A 578     -40.987  19.865  58.264  1.00 47.58           N  
ANISOU   87  N   PRO A 578     5320   6903   5854    550   1405    452       N  
ATOM     88  CA  PRO A 578     -41.245  19.123  57.022  1.00 44.91           C  
ANISOU   88  CA  PRO A 578     4830   6506   5727    480   1282    560       C  
ATOM     89  C   PRO A 578     -40.040  18.962  56.105  1.00 42.05           C  
ANISOU   89  C   PRO A 578     4552   6006   5421    373   1095    497       C  
ATOM     90  O   PRO A 578     -40.226  18.584  54.945  1.00 40.69           O  
ANISOU   90  O   PRO A 578     4281   5771   5409    334    995    546       O  
ATOM     91  CB  PRO A 578     -42.316  19.991  56.345  1.00 45.01           C  
ANISOU   91  CB  PRO A 578     4757   6490   5857    619   1360    552       C  
ATOM     92  CG  PRO A 578     -42.099  21.396  56.898  1.00 46.54           C  
ANISOU   92  CG  PRO A 578     5127   6630   5925    746   1472    383       C  
ATOM     93  CD  PRO A 578     -41.154  21.314  58.073  1.00 48.11           C  
ANISOU   93  CD  PRO A 578     5491   6877   5913    685   1483    299       C  
ATOM     94  N   ALA A 579     -38.823  19.236  56.586  1.00 41.09           N  
ANISOU   94  N   ALA A 579     4601   5845   5165    324   1044    389       N  
ATOM     95  CA  ALA A 579     -37.651  19.110  55.721  1.00 39.12           C  
ANISOU   95  CA  ALA A 579     4419   5471   4973    229    879    334       C  
ATOM     96  C   ALA A 579     -37.293  17.658  55.427  1.00 39.28           C  
ANISOU   96  C   ALA A 579     4346   5507   5073    103    765    458       C  
ATOM     97  O   ALA A 579     -37.074  17.329  54.247  1.00 38.93           O  
ANISOU   97  O   ALA A 579     4254   5372   5166     55    655    467       O  
ATOM     98  CB  ALA A 579     -36.470  19.875  56.327  1.00 38.17           C  
ANISOU   98  CB  ALA A 579     4492   5310   4701    209    857    184       C  
ATOM     99  N   PRO A 580     -37.202  16.749  56.409  1.00 40.30           N  
ANISOU   99  N   PRO A 580     4447   5740   5125     49    786    556       N  
ATOM    100  CA  PRO A 580     -36.827  15.367  56.061  1.00 39.79           C  
ANISOU  100  CA  PRO A 580     4299   5654   5166    -66    678    675       C  
ATOM    101  C   PRO A 580     -37.839  14.671  55.168  1.00 39.60           C  
ANISOU  101  C   PRO A 580     4104   5607   5336    -86    664    773       C  
ATOM    102  O   PRO A 580     -37.445  13.943  54.249  1.00 37.83           O  
ANISOU  102  O   PRO A 580     3840   5293   5241   -167    545    789       O  
ATOM    103  CB  PRO A 580     -36.705  14.681  57.429  1.00 40.88           C  
ANISOU  103  CB  PRO A 580     4440   5920   5171    -96    733    781       C  
ATOM    104  CG  PRO A 580     -37.537  15.500  58.340  1.00 42.91           C  
ANISOU  104  CG  PRO A 580     4719   6295   5290     10    896    754       C  
ATOM    105  CD  PRO A 580     -37.365  16.906  57.866  1.00 42.14           C  
ANISOU  105  CD  PRO A 580     4733   6112   5167     88    905    568       C  
ATOM    106  N   ILE A 581     -39.137  14.876  55.405  1.00 41.49           N  
ANISOU  106  N   ILE A 581     4234   5930   5599    -17    782    834       N  
ATOM    107  CA  ILE A 581     -40.143  14.227  54.570  1.00 41.61           C  
ANISOU  107  CA  ILE A 581     4069   5939   5802    -48    757    928       C  
ATOM    108  C   ILE A 581     -40.116  14.792  53.154  1.00 39.47           C  
ANISOU  108  C   ILE A 581     3799   5568   5631    -27    662    833       C  
ATOM    109  O   ILE A 581     -40.415  14.079  52.188  1.00 38.73           O  
ANISOU  109  O   ILE A 581     3597   5433   5685    -97    567    872       O  
ATOM    110  CB  ILE A 581     -41.538  14.356  55.214  1.00 44.19           C  
ANISOU  110  CB  ILE A 581     4261   6399   6132     26    914   1028       C  
ATOM    111  CG1 ILE A 581     -42.572  13.537  54.438  1.00 43.40           C  
ANISOU  111  CG1 ILE A 581     3949   6305   6234    -35    875   1141       C  
ATOM    112  CG2 ILE A 581     -41.965  15.815  55.303  1.00 45.94           C  
ANISOU  112  CG2 ILE A 581     4540   6643   6273    182   1020    924       C  
ATOM    113  CD1 ILE A 581     -42.312  12.047  54.455  1.00 42.33           C  
ANISOU  113  CD1 ILE A 581     3748   6133   6201   -187    797   1252       C  
ATOM    114  N   ALA A 582     -39.740  16.064  52.998  1.00 38.79           N  
ANISOU  114  N   ALA A 582     3838   5439   5463     65    682    707       N  
ATOM    115  CA  ALA A 582     -39.697  16.666  51.669  1.00 37.92           C  
ANISOU  115  CA  ALA A 582     3734   5240   5435     94    601    637       C  
ATOM    116  C   ALA A 582     -38.511  16.150  50.863  1.00 37.08           C  
ANISOU  116  C   ALA A 582     3696   5031   5360     -8    451    586       C  
ATOM    117  O   ALA A 582     -38.630  15.912  49.655  1.00 36.81           O  
ANISOU  117  O   ALA A 582     3605   4953   5429    -38    356    581       O  
ATOM    118  CB  ALA A 582     -39.645  18.189  51.783  1.00 37.71           C  
ANISOU  118  CB  ALA A 582     3823   5178   5328    223    680    532       C  
ATOM    119  N   ALA A 583     -37.358  15.975  51.513  1.00 35.92           N  
ANISOU  119  N   ALA A 583     3670   4858   5121    -59    430    547       N  
ATOM    120  CA  ALA A 583     -36.187  15.461  50.812  1.00 33.88           C  
ANISOU  120  CA  ALA A 583     3467   4509   4898   -146    303    506       C  
ATOM    121  C   ALA A 583     -36.374  14.009  50.393  1.00 33.89           C  
ANISOU  121  C   ALA A 583     3354   4499   5024   -243    230    592       C  
ATOM    122  O   ALA A 583     -35.805  13.579  49.384  1.00 34.26           O  
ANISOU  122  O   ALA A 583     3407   4467   5144   -297    127    553       O  
ATOM    123  CB  ALA A 583     -34.945  15.606  51.691  1.00 33.69           C  
ANISOU  123  CB  ALA A 583     3575   4476   4750   -175    296    459       C  
ATOM    124  N   VAL A 584     -37.162  13.241  51.148  1.00 34.78           N  
ANISOU  124  N   VAL A 584     3363   4683   5167   -269    288    708       N  
ATOM    125  CA  VAL A 584     -37.409  11.849  50.785  1.00 35.35           C  
ANISOU  125  CA  VAL A 584     3325   4723   5382   -371    225    792       C  
ATOM    126  C   VAL A 584     -38.281  11.772  49.537  1.00 36.98           C  
ANISOU  126  C   VAL A 584     3421   4914   5715   -383    167    773       C  
ATOM    127  O   VAL A 584     -37.986  11.020  48.601  1.00 36.02           O  
ANISOU  127  O   VAL A 584     3279   4714   5693   -460     61    742       O  
ATOM    128  CB  VAL A 584     -38.043  11.091  51.966  1.00 35.51           C  
ANISOU  128  CB  VAL A 584     3261   4825   5407   -400    314    939       C  
ATOM    129  CG1 VAL A 584     -38.500   9.711  51.528  1.00 35.23           C  
ANISOU  129  CG1 VAL A 584     3096   4737   5554   -511    257   1029       C  
ATOM    130  CG2 VAL A 584     -37.053  10.982  53.115  1.00 36.17           C  
ANISOU  130  CG2 VAL A 584     3453   4933   5357   -402    342    966       C  
ATOM    131  N   VAL A 585     -39.365  12.553  49.504  1.00 38.56           N  
ANISOU  131  N   VAL A 585     3547   5195   5909   -302    234    790       N  
ATOM    132  CA  VAL A 585     -40.248  12.556  48.340  1.00 39.19           C  
ANISOU  132  CA  VAL A 585     3507   5287   6095   -306    169    784       C  
ATOM    133  C   VAL A 585     -39.497  13.035  47.104  1.00 39.02           C  
ANISOU  133  C   VAL A 585     3578   5191   6055   -294     65    667       C  
ATOM    134  O   VAL A 585     -39.667  12.489  46.006  1.00 40.19           O  
ANISOU  134  O   VAL A 585     3666   5316   6288   -356    -43    640       O  
ATOM    135  CB  VAL A 585     -41.496  13.415  48.621  1.00 40.01           C  
ANISOU  135  CB  VAL A 585     3510   5502   6191   -197    272    836       C  
ATOM    136  CG1 VAL A 585     -42.370  13.516  47.381  1.00 40.05           C  
ANISOU  136  CG1 VAL A 585     3384   5538   6294   -192    189    837       C  
ATOM    137  CG2 VAL A 585     -42.287  12.832  49.783  1.00 41.09           C  
ANISOU  137  CG2 VAL A 585     3534   5726   6350   -217    384    965       C  
ATOM    138  N   PHE A 586     -38.651  14.056  47.263  1.00 37.89           N  
ANISOU  138  N   PHE A 586     3583   5013   5799   -219     96    594       N  
ATOM    139  CA  PHE A 586     -37.806  14.515  46.164  1.00 37.01           C  
ANISOU  139  CA  PHE A 586     3567   4829   5665   -212     12    499       C  
ATOM    140  C   PHE A 586     -36.960  13.371  45.615  1.00 37.14           C  
ANISOU  140  C   PHE A 586     3603   4773   5734   -323    -91    465       C  
ATOM    141  O   PHE A 586     -36.878  13.168  44.399  1.00 38.11           O  
ANISOU  141  O   PHE A 586     3713   4873   5895   -350   -182    415       O  
ATOM    142  CB  PHE A 586     -36.919  15.667  46.647  1.00 36.34           C  
ANISOU  142  CB  PHE A 586     3639   4704   5466   -141     70    435       C  
ATOM    143  CG  PHE A 586     -36.303  16.489  45.539  1.00 36.32           C  
ANISOU  143  CG  PHE A 586     3718   4640   5440   -106     17    362       C  
ATOM    144  CD1 PHE A 586     -36.506  16.171  44.205  1.00 36.93           C  
ANISOU  144  CD1 PHE A 586     3740   4720   5573   -129    -77    354       C  
ATOM    145  CD2 PHE A 586     -35.513  17.587  45.843  1.00 36.30           C  
ANISOU  145  CD2 PHE A 586     3851   4582   5358    -55     63    302       C  
ATOM    146  CE1 PHE A 586     -35.933  16.929  43.200  1.00 36.90           C  
ANISOU  146  CE1 PHE A 586     3812   4675   5535    -93   -115    305       C  
ATOM    147  CE2 PHE A 586     -34.939  18.350  44.843  1.00 36.28           C  
ANISOU  147  CE2 PHE A 586     3921   4520   5345    -28     26    255       C  
ATOM    148  CZ  PHE A 586     -35.149  18.021  43.519  1.00 36.57           C  
ANISOU  148  CZ  PHE A 586     3899   4570   5427    -42    -59    265       C  
ATOM    149  N   ALA A 587     -36.329  12.605  46.507  1.00 36.44           N  
ANISOU  149  N   ALA A 587     3546   4653   5644   -381    -73    495       N  
ATOM    150  CA  ALA A 587     -35.481  11.505  46.063  1.00 35.61           C  
ANISOU  150  CA  ALA A 587     3462   4464   5604   -471   -156    468       C  
ATOM    151  C   ALA A 587     -36.300  10.401  45.406  1.00 34.74           C  
ANISOU  151  C   ALA A 587     3229   4341   5631   -553   -219    490       C  
ATOM    152  O   ALA A 587     -35.878   9.828  44.395  1.00 33.97           O  
ANISOU  152  O   ALA A 587     3145   4178   5586   -603   -306    417       O  
ATOM    153  CB  ALA A 587     -34.678  10.953  47.240  1.00 35.32           C  
ANISOU  153  CB  ALA A 587     3475   4403   5540   -501   -121    521       C  
ATOM    154  N   CYS A 588     -37.474  10.092  45.962  1.00 35.33           N  
ANISOU  154  N   CYS A 588     3179   4479   5765   -571   -174    584       N  
ATOM    155  CA  CYS A 588     -38.309   9.033  45.402  1.00 35.10           C  
ANISOU  155  CA  CYS A 588     3020   4436   5882   -670   -238    607       C  
ATOM    156  C   CYS A 588     -38.789   9.392  44.001  1.00 33.77           C  
ANISOU  156  C   CYS A 588     2810   4299   5723   -663   -331    522       C  
ATOM    157  O   CYS A 588     -38.725   8.569  43.081  1.00 33.42           O  
ANISOU  157  O   CYS A 588     2745   4198   5755   -749   -430    453       O  
ATOM    158  CB  CYS A 588     -39.495   8.757  46.325  1.00 36.59           C  
ANISOU  158  CB  CYS A 588     3069   4703   6132   -689   -158    741       C  
ATOM    159  SG  CYS A 588     -39.043   8.117  47.952  1.00 38.54           S  
ANISOU  159  SG  CYS A 588     3347   4932   6364   -711    -55    869       S  
ATOM    160  N   LEU A 589     -39.281  10.622  43.823  1.00 32.54           N  
ANISOU  160  N   LEU A 589     2645   4235   5485   -558   -298    526       N  
ATOM    161  CA  LEU A 589     -39.707  11.058  42.497  1.00 32.29           C  
ANISOU  161  CA  LEU A 589     2576   4252   5442   -537   -388    466       C  
ATOM    162  C   LEU A 589     -38.540  11.042  41.519  1.00 32.82           C  
ANISOU  162  C   LEU A 589     2774   4245   5451   -546   -463    349       C  
ATOM    163  O   LEU A 589     -38.701  10.665  40.352  1.00 32.95           O  
ANISOU  163  O   LEU A 589     2762   4274   5484   -593   -569    280       O  
ATOM    164  CB  LEU A 589     -40.326  12.454  42.575  1.00 30.77           C  
ANISOU  164  CB  LEU A 589     2363   4153   5176   -400   -324    510       C  
ATOM    165  CG  LEU A 589     -41.603  12.586  43.407  1.00 32.06           C  
ANISOU  165  CG  LEU A 589     2377   4412   5393   -367   -238    625       C  
ATOM    166  CD1 LEU A 589     -42.100  14.024  43.416  1.00 31.38           C  
ANISOU  166  CD1 LEU A 589     2289   4395   5241   -209   -166    656       C  
ATOM    167  CD2 LEU A 589     -42.674  11.650  42.880  1.00 34.32           C  
ANISOU  167  CD2 LEU A 589     2477   4757   5807   -470   -325    662       C  
ATOM    168  N   GLY A 590     -37.356  11.444  41.981  1.00 33.48           N  
ANISOU  168  N   GLY A 590     2998   4263   5460   -505   -410    324       N  
ATOM    169  CA  GLY A 590     -36.175  11.361  41.138  1.00 31.70           C  
ANISOU  169  CA  GLY A 590     2885   3970   5189   -515   -464    226       C  
ATOM    170  C   GLY A 590     -35.815   9.931  40.784  1.00 31.77           C  
ANISOU  170  C   GLY A 590     2883   3896   5291   -624   -531    171       C  
ATOM    171  O   GLY A 590     -35.483   9.632  39.634  1.00 32.37           O  
ANISOU  171  O   GLY A 590     2988   3954   5356   -649   -608     75       O  
ATOM    172  N   LEU A 591     -35.876   9.025  41.765  1.00 32.32           N  
ANISOU  172  N   LEU A 591     2915   3912   5453   -685   -497    233       N  
ATOM    173  CA  LEU A 591     -35.641   7.614  41.474  1.00 34.13           C  
ANISOU  173  CA  LEU A 591     3127   4037   5803   -788   -553    191       C  
ATOM    174  C   LEU A 591     -36.672   7.076  40.490  1.00 37.36           C  
ANISOU  174  C   LEU A 591     3435   4474   6285   -864   -647    136       C  
ATOM    175  O   LEU A 591     -36.344   6.260  39.620  1.00 38.91           O  
ANISOU  175  O   LEU A 591     3657   4596   6531   -928   -721     27       O  
ATOM    176  CB  LEU A 591     -35.661   6.795  42.764  1.00 34.66           C  
ANISOU  176  CB  LEU A 591     3159   4046   5965   -835   -493    302       C  
ATOM    177  CG  LEU A 591     -34.515   7.001  43.755  1.00 34.88           C  
ANISOU  177  CG  LEU A 591     3284   4041   5930   -784   -425    352       C  
ATOM    178  CD1 LEU A 591     -34.757   6.178  45.011  1.00 35.68           C  
ANISOU  178  CD1 LEU A 591     3331   4113   6113   -830   -369    488       C  
ATOM    179  CD2 LEU A 591     -33.177   6.646  43.124  1.00 34.74           C  
ANISOU  179  CD2 LEU A 591     3364   3925   5910   -780   -463    258       C  
ATOM    180  N   LEU A 592     -37.924   7.522  40.612  1.00 38.47           N  
ANISOU  180  N   LEU A 592     3456   4727   6435   -858   -646    205       N  
ATOM    181  CA  LEU A 592     -38.963   7.081  39.686  1.00 39.68           C  
ANISOU  181  CA  LEU A 592     3492   4933   6652   -937   -750    159       C  
ATOM    182  C   LEU A 592     -38.674   7.565  38.272  1.00 39.04           C  
ANISOU  182  C   LEU A 592     3471   4904   6458   -901   -840     37       C  
ATOM    183  O   LEU A 592     -38.679   6.776  37.320  1.00 39.83           O  
ANISOU  183  O   LEU A 592     3569   4972   6591   -986   -940    -80       O  
ATOM    184  CB  LEU A 592     -40.332   7.579  40.152  1.00 40.84           C  
ANISOU  184  CB  LEU A 592     3482   5209   6827   -918   -721    278       C  
ATOM    185  CG  LEU A 592     -41.024   6.800  41.269  1.00 41.42           C  
ANISOU  185  CG  LEU A 592     3438   5258   7041   -996   -659    399       C  
ATOM    186  CD1 LEU A 592     -42.311   7.496  41.677  1.00 42.03           C  
ANISOU  186  CD1 LEU A 592     3361   5487   7124   -946   -612    516       C  
ATOM    187  CD2 LEU A 592     -41.305   5.374  40.823  1.00 42.80           C  
ANISOU  187  CD2 LEU A 592     3608   5345   7309  -1126   -724    329       C  
ATOM    188  N   ALA A 593     -38.419   8.866  38.118  1.00 37.72           N  
ANISOU  188  N   ALA A 593     3362   4815   6154   -776   -801     61       N  
ATOM    189  CA  ALA A 593     -38.153   9.420  36.795  1.00 37.18           C  
ANISOU  189  CA  ALA A 593     3350   4811   5965   -732   -874    -25       C  
ATOM    190  C   ALA A 593     -36.882   8.833  36.193  1.00 37.50           C  
ANISOU  190  C   ALA A 593     3523   4751   5974   -760   -894   -151       C  
ATOM    191  O   ALA A 593     -36.821   8.576  34.985  1.00 39.08           O  
ANISOU  191  O   ALA A 593     3743   4987   6117   -787   -983   -260       O  
ATOM    192  CB  ALA A 593     -38.060  10.943  36.875  1.00 35.68           C  
ANISOU  192  CB  ALA A 593     3204   4695   5659   -590   -809     47       C  
ATOM    193  N   THR A 594     -35.853   8.618  37.018  1.00 36.29           N  
ANISOU  193  N   THR A 594     3456   4483   5850   -748   -811   -136       N  
ATOM    194  CA  THR A 594     -34.641   7.965  36.530  1.00 35.00           C  
ANISOU  194  CA  THR A 594     3399   4218   5681   -768   -819   -245       C  
ATOM    195  C   THR A 594     -34.933   6.535  36.092  1.00 35.79           C  
ANISOU  195  C   THR A 594     3460   4237   5900   -885   -893   -342       C  
ATOM    196  O   THR A 594     -34.365   6.049  35.106  1.00 35.25           O  
ANISOU  196  O   THR A 594     3459   4134   5802   -903   -938   -478       O  
ATOM    197  CB  THR A 594     -33.557   7.985  37.610  1.00 33.17           C  
ANISOU  197  CB  THR A 594     3239   3891   5472   -733   -723   -187       C  
ATOM    198  OG1 THR A 594     -33.371   9.325  38.079  1.00 32.30           O  
ANISOU  198  OG1 THR A 594     3164   3846   5261   -640   -658   -111       O  
ATOM    199  CG2 THR A 594     -32.236   7.473  37.057  1.00 32.38           C  
ANISOU  199  CG2 THR A 594     3238   3702   5362   -728   -720   -286       C  
ATOM    200  N   LEU A 595     -35.823   5.847  36.813  1.00 37.22           N  
ANISOU  200  N   LEU A 595     3536   4386   6222   -967   -900   -278       N  
ATOM    201  CA  LEU A 595     -36.217   4.498  36.422  1.00 39.24           C  
ANISOU  201  CA  LEU A 595     3749   4548   6612  -1094   -972   -368       C  
ATOM    202  C   LEU A 595     -37.008   4.511  35.120  1.00 41.28           C  
ANISOU  202  C   LEU A 595     3966   4918   6800  -1138  -1090   -480       C  
ATOM    203  O   LEU A 595     -36.825   3.636  34.266  1.00 42.60           O  
ANISOU  203  O   LEU A 595     4192   5030   6962  -1196  -1140   -625       O  
ATOM    204  CB  LEU A 595     -37.032   3.847  37.541  1.00 39.37           C  
ANISOU  204  CB  LEU A 595     3686   4529   6743  -1148   -915   -239       C  
ATOM    205  CG  LEU A 595     -37.585   2.444  37.281  1.00 40.90           C  
ANISOU  205  CG  LEU A 595     3868   4637   7034  -1257   -945   -299       C  
ATOM    206  CD1 LEU A 595     -36.454   1.452  37.068  1.00 40.51           C  
ANISOU  206  CD1 LEU A 595     3944   4414   7035  -1264   -923   -394       C  
ATOM    207  CD2 LEU A 595     -38.484   2.000  38.425  1.00 41.84           C  
ANISOU  207  CD2 LEU A 595     3890   4747   7262  -1305   -886   -147       C  
ATOM    208  N   PHE A 596     -37.890   5.498  34.951  1.00 41.36           N  
ANISOU  208  N   PHE A 596     3882   5095   6738  -1100  -1128   -410       N  
ATOM    209  CA  PHE A 596     -38.666   5.592  33.719  1.00 43.06           C  
ANISOU  209  CA  PHE A 596     4039   5446   6879  -1139  -1260   -498       C  
ATOM    210  C   PHE A 596     -37.773   5.915  32.527  1.00 42.99           C  
ANISOU  210  C   PHE A 596     4163   5475   6695  -1077  -1291   -628       C  
ATOM    211  O   PHE A 596     -37.918   5.315  31.456  1.00 43.61           O  
ANISOU  211  O   PHE A 596     4253   5580   6736  -1149  -1399   -782       O  
ATOM    212  CB  PHE A 596     -39.762   6.647  33.876  1.00 43.62           C  
ANISOU  212  CB  PHE A 596     3981   5693   6901  -1078  -1271   -360       C  
ATOM    213  CG  PHE A 596     -40.629   6.810  32.659  1.00 46.12           C  
ANISOU  213  CG  PHE A 596     4213   6177   7133  -1110  -1418   -421       C  
ATOM    214  CD1 PHE A 596     -41.719   5.980  32.452  1.00 48.56           C  
ANISOU  214  CD1 PHE A 596     4417   6530   7505  -1229  -1484   -450       C  
ATOM    215  CD2 PHE A 596     -40.361   7.800  31.726  1.00 46.24           C  
ANISOU  215  CD2 PHE A 596     4290   6322   6955  -1001  -1447   -433       C  
ATOM    216  CE1 PHE A 596     -42.522   6.128  31.335  1.00 50.49           C  
ANISOU  216  CE1 PHE A 596     4585   6952   7648  -1258  -1619   -504       C  
ATOM    217  CE2 PHE A 596     -41.159   7.953  30.605  1.00 48.43           C  
ANISOU  217  CE2 PHE A 596     4487   6777   7137  -1025  -1592   -474       C  
ATOM    218  CZ  PHE A 596     -42.242   7.116  30.410  1.00 50.44           C  
ANISOU  218  CZ  PHE A 596     4601   7080   7483  -1163  -1702   -517       C  
ATOM    219  N   VAL A 597     -36.838   6.853  32.698  1.00 42.28           N  
ANISOU  219  N   VAL A 597     4176   5392   6498   -950  -1196   -572       N  
ATOM    220  CA  VAL A 597     -35.978   7.267  31.592  1.00 41.63           C  
ANISOU  220  CA  VAL A 597     4212   5361   6245   -884  -1207   -666       C  
ATOM    221  C   VAL A 597     -35.085   6.116  31.142  1.00 42.08           C  
ANISOU  221  C   VAL A 597     4364   5285   6338   -941  -1210   -835       C  
ATOM    222  O   VAL A 597     -34.889   5.897  29.940  1.00 42.83           O  
ANISOU  222  O   VAL A 597     4515   5439   6320   -951  -1275   -978       O  
ATOM    223  CB  VAL A 597     -35.156   8.506  31.996  1.00 38.49           C  
ANISOU  223  CB  VAL A 597     3891   4976   5756   -751  -1094   -555       C  
ATOM    224  CG1 VAL A 597     -33.976   8.701  31.057  1.00 37.37           C  
ANISOU  224  CG1 VAL A 597     3880   4841   5479   -696  -1071   -646       C  
ATOM    225  CG2 VAL A 597     -36.040   9.744  32.003  1.00 37.62           C  
ANISOU  225  CG2 VAL A 597     3707   5011   5575   -675  -1104   -424       C  
ATOM    226  N   THR A 598     -34.542   5.357  32.097  1.00 40.48           N  
ANISOU  226  N   THR A 598     4183   4907   6293   -972  -1138   -820       N  
ATOM    227  CA  THR A 598     -33.639   4.263  31.749  1.00 39.70           C  
ANISOU  227  CA  THR A 598     4173   4658   6252  -1006  -1123   -967       C  
ATOM    228  C   THR A 598     -34.362   3.166  30.976  1.00 42.21           C  
ANISOU  228  C   THR A 598     4459   4945   6632  -1133  -1238  -1133       C  
ATOM    229  O   THR A 598     -33.830   2.643  29.988  1.00 44.04           O  
ANISOU  229  O   THR A 598     4779   5151   6802  -1141  -1264  -1313       O  
ATOM    230  CB  THR A 598     -32.996   3.694  33.014  1.00 37.51           C  
ANISOU  230  CB  THR A 598     3907   4203   6142  -1006  -1027   -883       C  
ATOM    231  OG1 THR A 598     -32.364   4.753  33.744  1.00 35.84           O  
ANISOU  231  OG1 THR A 598     3722   4034   5861   -902   -935   -742       O  
ATOM    232  CG2 THR A 598     -31.956   2.644  32.659  1.00 37.19           C  
ANISOU  232  CG2 THR A 598     3959   4001   6171  -1012   -996  -1020       C  
ATOM    233  N   VAL A 599     -35.575   2.806  31.405  1.00 42.73           N  
ANISOU  233  N   VAL A 599     4423   5032   6782  -1219  -1275  -1057       N  
ATOM    234  CA  VAL A 599     -36.329   1.762  30.713  1.00 44.77           C  
ANISOU  234  CA  VAL A 599     4676   5280   7056  -1334  -1350  -1173       C  
ATOM    235  C   VAL A 599     -36.672   2.194  29.294  1.00 46.46           C  
ANISOU  235  C   VAL A 599     4896   5675   7082  -1342  -1474  -1305       C  
ATOM    236  O   VAL A 599     -36.683   1.369  28.371  1.00 48.05           O  
ANISOU  236  O   VAL A 599     5166   5854   7238  -1409  -1529  -1474       O  
ATOM    237  CB  VAL A 599     -37.590   1.394  31.522  1.00 44.83           C  
ANISOU  237  CB  VAL A 599     4555   5294   7185  -1423  -1354  -1042       C  
ATOM    238  CG1 VAL A 599     -38.464   0.420  30.750  1.00 47.43           C  
ANISOU  238  CG1 VAL A 599     4864   5633   7526  -1559  -1448  -1161       C  
ATOM    239  CG2 VAL A 599     -37.196   0.797  32.862  1.00 44.48           C  
ANISOU  239  CG2 VAL A 599     4522   5071   7308  -1415  -1233   -923       C  
ATOM    240  N   VAL A 600     -36.940   3.485  29.090  1.00 46.43           N  
ANISOU  240  N   VAL A 600     4826   5855   6958  -1267  -1521  -1228       N  
ATOM    241  CA  VAL A 600     -37.216   3.984  27.745  1.00 48.31           C  
ANISOU  241  CA  VAL A 600     5070   6295   6992  -1253  -1641  -1331       C  
ATOM    242  C   VAL A 600     -36.004   3.788  26.843  1.00 49.71           C  
ANISOU  242  C   VAL A 600     5404   6442   7040  -1202  -1616  -1509       C  
ATOM    243  O   VAL A 600     -36.133   3.381  25.682  1.00 50.90           O  
ANISOU  243  O   VAL A 600     5609   6675   7054  -1243  -1697  -1669       O  
ATOM    244  CB  VAL A 600     -37.652   5.461  27.803  1.00 46.68           C  
ANISOU  244  CB  VAL A 600     4788   6280   6667  -1143  -1647  -1153       C  
ATOM    245  CG1 VAL A 600     -37.686   6.067  26.407  1.00 48.00           C  
ANISOU  245  CG1 VAL A 600     4996   6660   6582  -1090  -1734  -1217       C  
ATOM    246  CG2 VAL A 600     -39.014   5.583  28.466  1.00 46.92           C  
ANISOU  246  CG2 VAL A 600     4633   6372   6821  -1202  -1705  -1020       C  
ATOM    247  N   PHE A 601     -34.804   4.058  27.366  1.00 49.78           N  
ANISOU  247  N   PHE A 601     5509   6345   7062  -1099  -1468  -1448       N  
ATOM    248  CA  PHE A 601     -33.597   3.911  26.559  1.00 51.23           C  
ANISOU  248  CA  PHE A 601     5837   6508   7120  -1031  -1407  -1583       C  
ATOM    249  C   PHE A 601     -33.228   2.448  26.350  1.00 52.17           C  
ANISOU  249  C   PHE A 601     6020   6439   7363  -1116  -1412  -1795       C  
ATOM    250  O   PHE A 601     -32.568   2.114  25.360  1.00 53.50           O  
ANISOU  250  O   PHE A 601     6297   6623   7409  -1088  -1402  -1972       O  
ATOM    251  CB  PHE A 601     -32.439   4.669  27.206  1.00 50.85           C  
ANISOU  251  CB  PHE A 601     5848   6409   7062   -903  -1252  -1443       C  
ATOM    252  CG  PHE A 601     -32.564   6.162  27.104  1.00 51.77           C  
ANISOU  252  CG  PHE A 601     5945   6701   7023   -804  -1235  -1277       C  
ATOM    253  CD1 PHE A 601     -33.116   6.748  25.975  1.00 53.92           C  
ANISOU  253  CD1 PHE A 601     6210   7183   7094   -785  -1325  -1299       C  
ATOM    254  CD2 PHE A 601     -32.140   6.978  28.136  1.00 51.28           C  
ANISOU  254  CD2 PHE A 601     5874   6594   7018   -732  -1132  -1098       C  
ATOM    255  CE1 PHE A 601     -33.236   8.122  25.877  1.00 53.15           C  
ANISOU  255  CE1 PHE A 601     6095   7226   6872   -687  -1302  -1130       C  
ATOM    256  CE2 PHE A 601     -32.258   8.351  28.042  1.00 51.46           C  
ANISOU  256  CE2 PHE A 601     5887   6748   6918   -644  -1110   -953       C  
ATOM    257  CZ  PHE A 601     -32.808   8.924  26.911  1.00 51.93           C  
ANISOU  257  CZ  PHE A 601     5938   6997   6796   -617  -1190   -961       C  
ATOM    258  N   ILE A 602     -33.641   1.564  27.260  1.00 52.04           N  
ANISOU  258  N   ILE A 602     5958   6249   7565  -1200  -1392  -1742       N  
ATOM    259  CA  ILE A 602     -33.391   0.139  27.071  1.00 54.52           C  
ANISOU  259  CA  ILE A 602     6355   6377   7982  -1261  -1361  -1874       C  
ATOM    260  C   ILE A 602     -34.333  -0.435  26.020  1.00 59.34           C  
ANISOU  260  C   ILE A 602     6975   7072   8500  -1370  -1483  -2014       C  
ATOM    261  O   ILE A 602     -33.915  -1.198  25.141  1.00 62.86           O  
ANISOU  261  O   ILE A 602     7533   7462   8889  -1383  -1485  -2208       O  
ATOM    262  CB  ILE A 602     -33.515  -0.608  28.411  1.00 53.53           C  
ANISOU  262  CB  ILE A 602     6185   6053   8100  -1302  -1286  -1734       C  
ATOM    263  CG1 ILE A 602     -32.407  -0.173  29.371  1.00 51.14           C  
ANISOU  263  CG1 ILE A 602     5897   5660   7875  -1194  -1167  -1615       C  
ATOM    264  CG2 ILE A 602     -33.477  -2.114  28.193  1.00 55.63           C  
ANISOU  264  CG2 ILE A 602     6523   6129   8484  -1377  -1271  -1860       C  
ATOM    265  CD1 ILE A 602     -32.470  -0.855  30.720  1.00 50.82           C  
ANISOU  265  CD1 ILE A 602     5814   5451   8043  -1218  -1092  -1458       C  
ATOM    266  N   ILE A 603     -35.616  -0.078  26.089  1.00 60.56           N  
ANISOU  266  N   ILE A 603     7009   7365   8637  -1448  -1585  -1918       N  
ATOM    267  CA  ILE A 603     -36.593  -0.605  25.140  1.00 64.78           C  
ANISOU  267  CA  ILE A 603     7534   7991   9089  -1568  -1717  -2033       C  
ATOM    268  C   ILE A 603     -36.302  -0.090  23.735  1.00 67.93           C  
ANISOU  268  C   ILE A 603     8012   8580   9219  -1515  -1790  -2181       C  
ATOM    269  O   ILE A 603     -36.117  -0.870  22.792  1.00 70.02           O  
ANISOU  269  O   ILE A 603     8386   8815   9403  -1558  -1823  -2378       O  
ATOM    270  CB  ILE A 603     -38.022  -0.246  25.582  1.00 64.75           C  
ANISOU  270  CB  ILE A 603     7358   8113   9131  -1654  -1804  -1874       C  
ATOM    271  CG1 ILE A 603     -38.376  -0.965  26.885  1.00 64.11           C  
ANISOU  271  CG1 ILE A 603     7210   7850   9300  -1721  -1723  -1750       C  
ATOM    272  CG2 ILE A 603     -39.016  -0.593  24.492  1.00 68.65           C  
ANISOU  272  CG2 ILE A 603     7830   8747   9508  -1774  -1962  -1983       C  
ATOM    273  CD1 ILE A 603     -39.762  -0.646  27.395  1.00 63.77           C  
ANISOU  273  CD1 ILE A 603     6986   7933   9309  -1797  -1782  -1593       C  
ATOM    274  N   TYR A 604     -36.256   1.229  23.576  1.00 67.87           N  
ANISOU  274  N   TYR A 604     7954   8775   9060  -1415  -1813  -2086       N  
ATOM    275  CA  TYR A 604     -36.017   1.850  22.273  1.00 71.33           C  
ANISOU  275  CA  TYR A 604     8456   9432   9212  -1350  -1877  -2188       C  
ATOM    276  C   TYR A 604     -34.528   2.062  22.019  1.00 71.76           C  
ANISOU  276  C   TYR A 604     8640   9446   9179  -1222  -1752  -2282       C  
ATOM    277  O   TYR A 604     -34.095   3.134  21.601  1.00 70.60           O  
ANISOU  277  O   TYR A 604     8501   9482   8842  -1113  -1742  -2244       O  
ATOM    278  CB  TYR A 604     -36.781   3.166  22.181  1.00 71.59           C  
ANISOU  278  CB  TYR A 604     8363   9720   9119  -1300  -1966  -2020       C  
ATOM    279  CG  TYR A 604     -38.261   3.042  22.467  1.00 72.67           C  
ANISOU  279  CG  TYR A 604     8347   9913   9349  -1413  -2082  -1908       C  
ATOM    280  CD1 TYR A 604     -39.159   2.708  21.461  1.00 75.36           C  
ANISOU  280  CD1 TYR A 604     8673  10393   9567  -1506  -2234  -1983       C  
ATOM    281  CD2 TYR A 604     -38.762   3.263  23.744  1.00 71.20           C  
ANISOU  281  CD2 TYR A 604     8032   9652   9370  -1426  -2036  -1725       C  
ATOM    282  CE1 TYR A 604     -40.513   2.595  21.719  1.00 76.56           C  
ANISOU  282  CE1 TYR A 604     8671  10606   9812  -1616  -2343  -1875       C  
ATOM    283  CE2 TYR A 604     -40.114   3.153  24.012  1.00 72.39           C  
ANISOU  283  CE2 TYR A 604     8031   9873   9603  -1527  -2124  -1619       C  
ATOM    284  CZ  TYR A 604     -40.985   2.819  22.996  1.00 75.02           C  
ANISOU  284  CZ  TYR A 604     8338  10343   9822  -1625  -2280  -1692       C  
ATOM    285  OH  TYR A 604     -42.331   2.708  23.258  1.00 76.70           O  
ANISOU  285  OH  TYR A 604     8385  10637  10122  -1731  -2371  -1581       O  
ATOM    286  N   ARG A 605     -33.726   1.022  22.269  1.00 73.85           N  
ANISOU  286  N   ARG A 605     9002   9473   9584  -1231  -1648  -2396       N  
ATOM    287  CA  ARG A 605     -32.282   1.150  22.100  1.00 75.11           C  
ANISOU  287  CA  ARG A 605     9270   9580   9688  -1109  -1516  -2479       C  
ATOM    288  C   ARG A 605     -31.885   1.202  20.630  1.00 80.16           C  
ANISOU  288  C   ARG A 605    10026  10389  10042  -1061  -1532  -2660       C  
ATOM    289  O   ARG A 605     -30.842   1.775  20.293  1.00 79.02           O  
ANISOU  289  O   ARG A 605     9946  10319   9760   -940  -1436  -2687       O  
ATOM    290  CB  ARG A 605     -31.562  -0.006  22.798  1.00 75.10           C  
ANISOU  290  CB  ARG A 605     9327   9277   9930  -1118  -1398  -2529       C  
ATOM    291  CG  ARG A 605     -31.661  -1.336  22.064  1.00 78.06           C  
ANISOU  291  CG  ARG A 605     9804   9538  10317  -1191  -1415  -2731       C  
ATOM    292  CD  ARG A 605     -30.544  -2.286  22.468  1.00 78.58           C  
ANISOU  292  CD  ARG A 605     9956   9342  10560  -1136  -1268  -2802       C  
ATOM    293  NE  ARG A 605     -30.875  -3.063  23.658  1.00 78.18           N  
ANISOU  293  NE  ARG A 605     9845   9064  10795  -1206  -1244  -2682       N  
ATOM    294  CZ  ARG A 605     -31.404  -4.281  23.628  1.00 80.05           C  
ANISOU  294  CZ  ARG A 605    10111   9145  11159  -1312  -1275  -2759       C  
ATOM    295  NH1 ARG A 605     -31.663  -4.864  22.465  1.00 82.66           N  
ANISOU  295  NH1 ARG A 605    10534   9511  11362  -1367  -1339  -2968       N  
ATOM    296  NH2 ARG A 605     -31.674  -4.919  24.759  1.00 79.54           N  
ANISOU  296  NH2 ARG A 605     9986   8893  11342  -1366  -1242  -2625       N  
ATOM    297  N   ASP A 606     -32.693   0.618  19.745  1.00 85.82           N  
ANISOU  297  N   ASP A 606    10772  11177  10658  -1154  -1647  -2776       N  
ATOM    298  CA  ASP A 606     -32.375   0.536  18.326  1.00 90.02           C  
ANISOU  298  CA  ASP A 606    11427  11866  10911  -1118  -1664  -2953       C  
ATOM    299  C   ASP A 606     -33.017   1.658  17.517  1.00 93.33           C  
ANISOU  299  C   ASP A 606    11797  12616  11048  -1090  -1782  -2869       C  
ATOM    300  O   ASP A 606     -33.160   1.530  16.296  1.00 96.54           O  
ANISOU  300  O   ASP A 606    12285  13182  11215  -1095  -1844  -2991       O  
ATOM    301  CB  ASP A 606     -32.793  -0.826  17.769  1.00 92.72           C  
ANISOU  301  CB  ASP A 606    11851  12080  11298  -1235  -1721  -3147       C  
ATOM    302  CG  ASP A 606     -31.986  -1.969  18.356  1.00 90.90           C  
ANISOU  302  CG  ASP A 606    11695  11532  11310  -1231  -1586  -3243       C  
ATOM    303  OD1 ASP A 606     -30.800  -1.755  18.683  1.00 88.68           O  
ANISOU  303  OD1 ASP A 606    11455  11177  11063  -1106  -1434  -3233       O  
ATOM    304  OD2 ASP A 606     -32.538  -3.081  18.489  1.00 92.09           O  
ANISOU  304  OD2 ASP A 606    11861  11509  11619  -1353  -1632  -3319       O  
ATOM    305  N   THR A 607     -33.405   2.748  18.167  1.00 94.96           N  
ANISOU  305  N   THR A 607    11875  12929  11277  -1054  -1811  -2653       N  
ATOM    306  CA  THR A 607     -33.963   3.859  17.418  1.00100.91           C  
ANISOU  306  CA  THR A 607    12579  13995  11768  -1005  -1911  -2541       C  
ATOM    307  C   THR A 607     -32.881   4.886  17.101  1.00103.48           C  
ANISOU  307  C   THR A 607    12964  14462  11892   -844  -1791  -2472       C  
ATOM    308  O   THR A 607     -31.940   5.064  17.880  1.00101.54           O  
ANISOU  308  O   THR A 607    12749  14040  11792   -768  -1619  -2369       O  
ATOM    309  CB  THR A 607     -35.095   4.530  18.201  1.00101.52           C  
ANISOU  309  CB  THR A 607    12477  14129  11967  -1042  -2009  -2321       C  
ATOM    310  OG1 THR A 607     -34.629   4.890  19.507  1.00 99.94           O  
ANISOU  310  OG1 THR A 607    12223  13766  11985   -995  -1894  -2185       O  
ATOM    311  CG2 THR A 607     -36.283   3.586  18.330  1.00104.34           C  
ANISOU  311  CG2 THR A 607    12769  14393  12481  -1204  -2133  -2359       C  
ATOM    312  N   PRO A 608     -32.993   5.554  15.948  1.00107.60           N  
ANISOU  312  N   PRO A 608    13520  15270  12094   -784  -1846  -2455       N  
ATOM    313  CA  PRO A 608     -31.943   6.501  15.527  1.00107.69           C  
ANISOU  313  CA  PRO A 608    13614  15382  11923   -626  -1688  -2315       C  
ATOM    314  C   PRO A 608     -31.548   7.524  16.581  1.00104.63           C  
ANISOU  314  C   PRO A 608    13170  14886  11700   -536  -1557  -2020       C  
ATOM    315  O   PRO A 608     -30.389   7.957  16.602  1.00104.38           O  
ANISOU  315  O   PRO A 608    13211  14810  11638   -434  -1384  -1946       O  
ATOM    316  CB  PRO A 608     -32.565   7.189  14.303  1.00111.03           C  
ANISOU  316  CB  PRO A 608    14030  16150  12006   -595  -1816  -2270       C  
ATOM    317  CG  PRO A 608     -33.678   6.292  13.838  1.00113.65           C  
ANISOU  317  CG  PRO A 608    14340  16492  12349   -734  -1994  -2416       C  
ATOM    318  CD  PRO A 608     -33.905   5.204  14.846  1.00111.86           C  
ANISOU  318  CD  PRO A 608    14078  15961  12461   -856  -1997  -2528       C  
ATOM    319  N   VAL A 609     -32.471   7.928  17.456  1.00102.06           N  
ANISOU  319  N   VAL A 609    12713  14518  11546   -575  -1632  -1855       N  
ATOM    320  CA  VAL A 609     -32.153   8.952  18.447  1.00 99.22           C  
ANISOU  320  CA  VAL A 609    12309  14063  11326   -491  -1513  -1591       C  
ATOM    321  C   VAL A 609     -31.224   8.395  19.521  1.00 97.63           C  
ANISOU  321  C   VAL A 609    12142  13581  11373   -499  -1369  -1625       C  
ATOM    322  O   VAL A 609     -30.286   9.071  19.961  1.00 95.01           O  
ANISOU  322  O   VAL A 609    11843  13178  11079   -412  -1220  -1488       O  
ATOM    323  CB  VAL A 609     -33.449   9.529  19.047  1.00101.34           C  
ANISOU  323  CB  VAL A 609    12429  14380  11697   -518  -1627  -1418       C  
ATOM    324  CG1 VAL A 609     -34.401   8.408  19.436  1.00103.50           C  
ANISOU  324  CG1 VAL A 609    12618  14573  12134   -667  -1761  -1569       C  
ATOM    325  CG2 VAL A 609     -33.143  10.419  20.244  1.00 99.99           C  
ANISOU  325  CG2 VAL A 609    12221  14065  11706   -447  -1499  -1189       C  
ATOM    326  N   VAL A 610     -31.457   7.154  19.950  1.00 99.61           N  
ANISOU  326  N   VAL A 610    12381  13669  11799   -606  -1414  -1802       N  
ATOM    327  CA  VAL A 610     -30.606   6.562  20.976  1.00 98.16           C  
ANISOU  327  CA  VAL A 610    12223  13223  11852   -609  -1287  -1820       C  
ATOM    328  C   VAL A 610     -29.347   5.961  20.362  1.00 99.92           C  
ANISOU  328  C   VAL A 610    12571  13392  12002   -558  -1171  -1987       C  
ATOM    329  O   VAL A 610     -28.276   5.993  20.978  1.00 95.30           O  
ANISOU  329  O   VAL A 610    12014  12665  11530   -497  -1024  -1928       O  
ATOM    330  CB  VAL A 610     -31.392   5.512  21.779  1.00 96.03           C  
ANISOU  330  CB  VAL A 610    11880  12783  11826   -740  -1371  -1903       C  
ATOM    331  CG1 VAL A 610     -30.604   5.074  23.006  1.00 92.92           C  
ANISOU  331  CG1 VAL A 610    11491  12133  11681   -729  -1242  -1854       C  
ATOM    332  CG2 VAL A 610     -32.748   6.063  22.180  1.00 94.57           C  
ANISOU  332  CG2 VAL A 610    11558  12695  11681   -790  -1493  -1757       C  
ATOM    333  N   LYS A 611     -29.447   5.417  19.147  1.00110.22           N  
ANISOU  333  N   LYS A 611    13946  14818  13112   -580  -1233  -2198       N  
ATOM    334  CA  LYS A 611     -28.297   4.782  18.513  1.00118.62           C  
ANISOU  334  CA  LYS A 611    15132  15837  14102   -523  -1113  -2380       C  
ATOM    335  C   LYS A 611     -27.238   5.790  18.083  1.00127.75           C  
ANISOU  335  C   LYS A 611    16336  17116  15086   -385   -964  -2239       C  
ATOM    336  O   LYS A 611     -26.079   5.406  17.888  1.00130.64           O  
ANISOU  336  O   LYS A 611    16776  17409  15452   -316   -818  -2324       O  
ATOM    337  CB  LYS A 611     -28.757   3.962  17.306  1.00118.65           C  
ANISOU  337  CB  LYS A 611    15207  15953  13920   -587  -1224  -2661       C  
ATOM    338  CG  LYS A 611     -27.785   2.872  16.882  1.00119.04           C  
ANISOU  338  CG  LYS A 611    15377  15869  13983   -560  -1113  -2916       C  
ATOM    339  CD  LYS A 611     -28.010   2.471  15.433  1.00117.80           C  
ANISOU  339  CD  LYS A 611    15320  15907  13531   -577  -1189  -3171       C  
ATOM    340  CE  LYS A 611     -29.476   2.182  15.157  1.00113.48           C  
ANISOU  340  CE  LYS A 611    14725  15420  12972   -717  -1396  -3180       C  
ATOM    341  NZ  LYS A 611     -29.717   1.912  13.713  1.00111.50           N  
ANISOU  341  NZ  LYS A 611    14580  15351  12434   -726  -1456  -3321       N  
ATOM    342  N   SER A 612     -27.605   7.065  17.938  1.00135.02           N  
ANISOU  342  N   SER A 612    17211  18213  15876   -341   -991  -2019       N  
ATOM    343  CA  SER A 612     -26.660   8.079  17.482  1.00137.66           C  
ANISOU  343  CA  SER A 612    17586  18665  16051   -222   -853  -1868       C  
ATOM    344  C   SER A 612     -25.672   8.475  18.575  1.00136.61           C  
ANISOU  344  C   SER A 612    17426  18348  16131   -175   -700  -1710       C  
ATOM    345  O   SER A 612     -24.482   8.663  18.297  1.00137.21           O  
ANISOU  345  O   SER A 612    17549  18428  16155    -95   -548  -1690       O  
ATOM    346  CB  SER A 612     -27.413   9.312  16.980  1.00138.37           C  
ANISOU  346  CB  SER A 612    17637  18984  15952   -190   -933  -1672       C  
ATOM    347  OG  SER A 612     -28.232   9.003  15.867  1.00141.11           O  
ANISOU  347  OG  SER A 612    18007  19543  16064   -226  -1078  -1809       O  
ATOM    348  N   SER A 613     -26.137   8.611  19.816  1.00132.50           N  
ANISOU  348  N   SER A 613    16824  17678  15842   -223   -739  -1596       N  
ATOM    349  CA  SER A 613     -25.279   9.029  20.913  1.00127.85           C  
ANISOU  349  CA  SER A 613    16205  16932  15441   -190   -617  -1446       C  
ATOM    350  C   SER A 613     -24.624   7.813  21.568  1.00124.08           C  
ANISOU  350  C   SER A 613    15737  16239  15169   -215   -560  -1583       C  
ATOM    351  O   SER A 613     -24.874   6.662  21.200  1.00126.47           O  
ANISOU  351  O   SER A 613    16074  16491  15487   -259   -609  -1793       O  
ATOM    352  CB  SER A 613     -26.076   9.844  21.932  1.00127.46           C  
ANISOU  352  CB  SER A 613    16071  16843  15515   -218   -677  -1254       C  
ATOM    353  OG  SER A 613     -25.221  10.439  22.893  1.00126.10           O  
ANISOU  353  OG  SER A 613    15880  16552  15479   -184   -564  -1106       O  
ATOM    354  N   SER A 614     -23.768   8.072  22.555  1.00113.77           N  
ANISOU  354  N   SER A 614    14400  14801  14028   -186   -458  -1461       N  
ATOM    355  CA  SER A 614     -23.056   7.011  23.262  1.00104.85           C  
ANISOU  355  CA  SER A 614    13266  13470  13103   -192   -396  -1545       C  
ATOM    356  C   SER A 614     -24.008   6.343  24.246  1.00 95.87           C  
ANISOU  356  C   SER A 614    12076  12190  12160   -284   -501  -1560       C  
ATOM    357  O   SER A 614     -24.348   6.921  25.283  1.00 95.03           O  
ANISOU  357  O   SER A 614    11906  12042  12159   -309   -522  -1397       O  
ATOM    358  CB  SER A 614     -21.833   7.577  23.980  1.00103.28           C  
ANISOU  358  CB  SER A 614    13036  13208  12998   -134   -267  -1393       C  
ATOM    359  OG  SER A 614     -20.969   8.242  23.075  1.00104.66           O  
ANISOU  359  OG  SER A 614    13246  13518  13003    -57   -163  -1359       O  
ATOM    360  N   ARG A 615     -24.433   5.117  23.928  1.00 88.49           N  
ANISOU  360  N   ARG A 615    11169  11177  11277   -338   -559  -1757       N  
ATOM    361  CA  ARG A 615     -25.390   4.422  24.785  1.00 80.54           C  
ANISOU  361  CA  ARG A 615    10105  10035  10460   -439   -657  -1767       C  
ATOM    362  C   ARG A 615     -24.738   3.933  26.073  1.00 75.07           C  
ANISOU  362  C   ARG A 615     9376   9136  10012   -431   -584  -1684       C  
ATOM    363  O   ARG A 615     -25.358   3.977  27.142  1.00 72.40           O  
ANISOU  363  O   ARG A 615     8969   8727   9812   -488   -631  -1566       O  
ATOM    364  CB  ARG A 615     -26.023   3.254  24.031  1.00 78.81           C  
ANISOU  364  CB  ARG A 615     9928   9779  10236   -513   -745  -2009       C  
ATOM    365  CG  ARG A 615     -27.182   3.650  23.132  1.00 77.29           C  
ANISOU  365  CG  ARG A 615     9728   9788   9850   -569   -883  -2061       C  
ATOM    366  CD  ARG A 615     -27.769   2.438  22.431  1.00 76.74           C  
ANISOU  366  CD  ARG A 615     9700   9672   9786   -663   -980  -2321       C  
ATOM    367  NE  ARG A 615     -26.823   1.848  21.488  1.00 76.31           N  
ANISOU  367  NE  ARG A 615     9761   9607   9627   -599   -894  -2525       N  
ATOM    368  CZ  ARG A 615     -27.024   0.703  20.844  1.00 76.84           C  
ANISOU  368  CZ  ARG A 615     9896   9597   9703   -660   -941  -2791       C  
ATOM    369  NH1 ARG A 615     -28.140   0.014  21.043  1.00 77.10           N  
ANISOU  369  NH1 ARG A 615     9885   9553   9857   -803  -1083  -2880       N  
ATOM    370  NH2 ARG A 615     -26.107   0.245  20.003  1.00 77.56           N  
ANISOU  370  NH2 ARG A 615    10097   9685   9688   -582   -840  -2974       N  
ATOM    371  N   GLU A 616     -23.492   3.457  25.993  1.00 73.04           N  
ANISOU  371  N   GLU A 616     9157   8790   9804   -357   -467  -1735       N  
ATOM    372  CA  GLU A 616     -22.814   2.967  27.190  1.00 68.77           C  
ANISOU  372  CA  GLU A 616     8574   8068   9489   -340   -404  -1643       C  
ATOM    373  C   GLU A 616     -22.554   4.094  28.182  1.00 63.46           C  
ANISOU  373  C   GLU A 616     7839   7446   8829   -322   -380  -1411       C  
ATOM    374  O   GLU A 616     -22.643   3.889  29.398  1.00 61.33           O  
ANISOU  374  O   GLU A 616     7514   7066   8721   -352   -391  -1300       O  
ATOM    375  CB  GLU A 616     -21.505   2.275  26.811  1.00 69.33           C  
ANISOU  375  CB  GLU A 616     8685   8052   9603   -247   -281  -1739       C  
ATOM    376  CG  GLU A 616     -21.626   0.773  26.595  1.00 71.27           C  
ANISOU  376  CG  GLU A 616     8975   8112   9993   -270   -287  -1934       C  
ATOM    377  CD  GLU A 616     -22.300   0.414  25.284  1.00 72.94           C  
ANISOU  377  CD  GLU A 616     9267   8399  10047   -310   -349  -2166       C  
ATOM    378  OE1 GLU A 616     -22.371   1.282  24.388  1.00 72.65           O  
ANISOU  378  OE1 GLU A 616     9260   8576   9767   -285   -356  -2178       O  
ATOM    379  OE2 GLU A 616     -22.758  -0.740  25.149  1.00 74.16           O  
ANISOU  379  OE2 GLU A 616     9456   8399  10321   -370   -393  -2335       O  
ATOM    380  N   LEU A 617     -22.234   5.291  27.685  1.00 60.95           N  
ANISOU  380  N   LEU A 617     7532   7289   8337   -276   -346  -1337       N  
ATOM    381  CA  LEU A 617     -21.970   6.411  28.582  1.00 58.82           C  
ANISOU  381  CA  LEU A 617     7215   7055   8081   -266   -322  -1138       C  
ATOM    382  C   LEU A 617     -23.244   6.915  29.248  1.00 58.25           C  
ANISOU  382  C   LEU A 617     7103   7006   8023   -333   -418  -1048       C  
ATOM    383  O   LEU A 617     -23.189   7.427  30.372  1.00 57.96           O  
ANISOU  383  O   LEU A 617     7024   6935   8064   -343   -410   -908       O  
ATOM    384  CB  LEU A 617     -21.284   7.546  27.822  1.00 58.39           C  
ANISOU  384  CB  LEU A 617     7184   7145   7855   -205   -252  -1080       C  
ATOM    385  CG  LEU A 617     -19.822   7.315  27.432  1.00 60.59           C  
ANISOU  385  CG  LEU A 617     7472   7413   8136   -129   -128  -1108       C  
ATOM    386  CD1 LEU A 617     -19.285   8.500  26.646  1.00 61.08           C  
ANISOU  386  CD1 LEU A 617     7551   7629   8027    -83    -60  -1032       C  
ATOM    387  CD2 LEU A 617     -18.973   7.058  28.668  1.00 60.11           C  
ANISOU  387  CD2 LEU A 617     7348   7227   8264   -122    -86  -1012       C  
ATOM    388  N   CYS A 618     -24.392   6.782  28.580  1.00 59.01           N  
ANISOU  388  N   CYS A 618     7207   7171   8042   -377   -509  -1127       N  
ATOM    389  CA  CYS A 618     -25.644   7.242  29.174  1.00 57.61           C  
ANISOU  389  CA  CYS A 618     6974   7028   7886   -432   -594  -1037       C  
ATOM    390  C   CYS A 618     -26.013   6.414  30.398  1.00 52.93           C  
ANISOU  390  C   CYS A 618     6329   6286   7495   -493   -615  -1005       C  
ATOM    391  O   CYS A 618     -26.515   6.954  31.391  1.00 51.20           O  
ANISOU  391  O   CYS A 618     6059   6068   7326   -510   -626   -873       O  
ATOM    392  CB  CYS A 618     -26.767   7.199  28.138  1.00 62.50           C  
ANISOU  392  CB  CYS A 618     7595   7768   8383   -469   -697  -1129       C  
ATOM    393  SG  CYS A 618     -26.650   8.476  26.865  1.00 65.72           S  
ANISOU  393  SG  CYS A 618     8049   8392   8531   -394   -686  -1092       S  
ATOM    394  N   TYR A 619     -25.768   5.102  30.349  1.00 50.84           N  
ANISOU  394  N   TYR A 619     6078   5889   7350   -521   -613  -1121       N  
ATOM    395  CA  TYR A 619     -26.056   4.255  31.501  1.00 49.21           C  
ANISOU  395  CA  TYR A 619     5823   5531   7346   -576   -625  -1071       C  
ATOM    396  C   TYR A 619     -25.184   4.620  32.695  1.00 46.54           C  
ANISOU  396  C   TYR A 619     5462   5143   7078   -531   -551   -915       C  
ATOM    397  O   TYR A 619     -25.605   4.453  33.845  1.00 45.62           O  
ANISOU  397  O   TYR A 619     5293   4969   7071   -570   -563   -806       O  
ATOM    398  CB  TYR A 619     -25.866   2.785  31.130  1.00 51.03           C  
ANISOU  398  CB  TYR A 619     6083   5606   7702   -606   -627  -1227       C  
ATOM    399  CG  TYR A 619     -26.818   2.295  30.062  1.00 54.03           C  
ANISOU  399  CG  TYR A 619     6482   6023   8026   -677   -719  -1401       C  
ATOM    400  CD1 TYR A 619     -28.070   2.875  29.898  1.00 54.44           C  
ANISOU  400  CD1 TYR A 619     6482   6206   7996   -738   -816  -1368       C  
ATOM    401  CD2 TYR A 619     -26.464   1.252  29.216  1.00 56.54           C  
ANISOU  401  CD2 TYR A 619     6865   6246   8370   -682   -712  -1603       C  
ATOM    402  CE1 TYR A 619     -28.942   2.428  28.923  1.00 56.05           C  
ANISOU  402  CE1 TYR A 619     6690   6463   8143   -813   -919  -1526       C  
ATOM    403  CE2 TYR A 619     -27.329   0.800  28.239  1.00 58.36           C  
ANISOU  403  CE2 TYR A 619     7119   6519   8539   -759   -809  -1781       C  
ATOM    404  CZ  TYR A 619     -28.566   1.390  28.096  1.00 58.04           C  
ANISOU  404  CZ  TYR A 619     7016   6624   8411   -830   -920  -1738       C  
ATOM    405  OH  TYR A 619     -29.427   0.939  27.122  1.00 59.91           O  
ANISOU  405  OH  TYR A 619     7263   6920   8580   -917  -1034  -1915       O  
ATOM    406  N   ILE A 620     -23.971   5.117  32.444  1.00 44.75           N  
ANISOU  406  N   ILE A 620     5268   4951   6786   -454   -475   -900       N  
ATOM    407  CA  ILE A 620     -23.116   5.566  33.536  1.00 41.76           C  
ANISOU  407  CA  ILE A 620     4861   4549   6457   -421   -421   -757       C  
ATOM    408  C   ILE A 620     -23.610   6.896  34.090  1.00 39.91           C  
ANISOU  408  C   ILE A 620     4609   4421   6135   -432   -437   -636       C  
ATOM    409  O   ILE A 620     -23.525   7.144  35.299  1.00 40.57           O  
ANISOU  409  O   ILE A 620     4660   4480   6275   -443   -430   -520       O  
ATOM    410  CB  ILE A 620     -21.653   5.651  33.062  1.00 40.52           C  
ANISOU  410  CB  ILE A 620     4725   4398   6273   -345   -337   -780       C  
ATOM    411  CG1 ILE A 620     -21.186   4.287  32.548  1.00 40.79           C  
ANISOU  411  CG1 ILE A 620     4779   4311   6408   -318   -306   -908       C  
ATOM    412  CG2 ILE A 620     -20.747   6.137  34.185  1.00 38.97           C  
ANISOU  412  CG2 ILE A 620     4486   4194   6126   -324   -298   -634       C  
ATOM    413  CD1 ILE A 620     -19.759   4.275  32.049  1.00 40.61           C  
ANISOU  413  CD1 ILE A 620     4764   4297   6370   -230   -209   -933       C  
ATOM    414  N   ILE A 621     -24.140   7.768  33.229  1.00 38.38           N  
ANISOU  414  N   ILE A 621     4440   4344   5800   -423   -459   -660       N  
ATOM    415  CA  ILE A 621     -24.697   9.031  33.705  1.00 36.64           C  
ANISOU  415  CA  ILE A 621     4207   4203   5511   -422   -468   -550       C  
ATOM    416  C   ILE A 621     -25.964   8.783  34.514  1.00 36.22           C  
ANISOU  416  C   ILE A 621     4102   4132   5528   -475   -523   -505       C  
ATOM    417  O   ILE A 621     -26.158   9.373  35.584  1.00 35.05           O  
ANISOU  417  O   ILE A 621     3932   3987   5399   -477   -507   -401       O  
ATOM    418  CB  ILE A 621     -24.957   9.982  32.523  1.00 36.99           C  
ANISOU  418  CB  ILE A 621     4286   4372   5397   -388   -475   -568       C  
ATOM    419  CG1 ILE A 621     -23.649  10.305  31.798  1.00 37.53           C  
ANISOU  419  CG1 ILE A 621     4397   4467   5394   -337   -401   -588       C  
ATOM    420  CG2 ILE A 621     -25.635  11.258  33.005  1.00 35.75           C  
ANISOU  420  CG2 ILE A 621     4117   4275   5193   -377   -481   -455       C  
ATOM    421  CD1 ILE A 621     -23.820  11.220  30.603  1.00 37.67           C  
ANISOU  421  CD1 ILE A 621     4452   4612   5247   -299   -396   -585       C  
ATOM    422  N   LEU A 622     -26.844   7.909  34.020  1.00 37.46           N  
ANISOU  422  N   LEU A 622     4235   4275   5722   -522   -586   -588       N  
ATOM    423  CA  LEU A 622     -28.078   7.607  34.739  1.00 36.55           C  
ANISOU  423  CA  LEU A 622     4052   4148   5687   -580   -633   -539       C  
ATOM    424  C   LEU A 622     -27.804   6.899  36.059  1.00 34.44           C  
ANISOU  424  C   LEU A 622     3756   3768   5563   -607   -601   -463       C  
ATOM    425  O   LEU A 622     -28.557   7.077  37.023  1.00 35.13           O  
ANISOU  425  O   LEU A 622     3792   3868   5689   -632   -603   -365       O  
ATOM    426  CB  LEU A 622     -29.000   6.757  33.863  1.00 37.77           C  
ANISOU  426  CB  LEU A 622     4180   4308   5864   -643   -716   -654       C  
ATOM    427  CG  LEU A 622     -29.475   7.398  32.558  1.00 37.62           C  
ANISOU  427  CG  LEU A 622     4177   4431   5687   -623   -770   -719       C  
ATOM    428  CD1 LEU A 622     -30.235   6.390  31.710  1.00 38.81           C  
ANISOU  428  CD1 LEU A 622     4306   4580   5860   -700   -863   -860       C  
ATOM    429  CD2 LEU A 622     -30.333   8.620  32.843  1.00 36.90           C  
ANISOU  429  CD2 LEU A 622     4038   4454   5526   -592   -781   -597       C  
ATOM    430  N   ALA A 623     -26.740   6.093  36.123  1.00 35.39           N  
ANISOU  430  N   ALA A 623     3904   3786   5758   -595   -567   -497       N  
ATOM    431  CA  ALA A 623     -26.386   5.439  37.377  1.00 36.00           C  
ANISOU  431  CA  ALA A 623     3952   3765   5963   -609   -539   -402       C  
ATOM    432  C   ALA A 623     -25.868   6.439  38.401  1.00 36.25           C  
ANISOU  432  C   ALA A 623     3985   3857   5932   -572   -498   -279       C  
ATOM    433  O   ALA A 623     -26.112   6.277  39.602  1.00 36.72           O  
ANISOU  433  O   ALA A 623     4009   3899   6044   -592   -489   -172       O  
ATOM    434  CB  ALA A 623     -25.348   4.345  37.130  1.00 35.89           C  
ANISOU  434  CB  ALA A 623     3961   3624   6052   -588   -511   -462       C  
ATOM    435  N   GLY A 624     -25.149   7.469  37.953  1.00 36.30           N  
ANISOU  435  N   GLY A 624     4033   3934   5824   -523   -472   -293       N  
ATOM    436  CA  GLY A 624     -24.740   8.520  38.870  1.00 35.55           C  
ANISOU  436  CA  GLY A 624     3946   3892   5668   -503   -442   -199       C  
ATOM    437  C   GLY A 624     -25.927   9.290  39.414  1.00 34.47           C  
ANISOU  437  C   GLY A 624     3793   3821   5481   -516   -451   -144       C  
ATOM    438  O   GLY A 624     -26.028   9.529  40.620  1.00 32.94           O  
ANISOU  438  O   GLY A 624     3586   3638   5290   -524   -434    -60       O  
ATOM    439  N   ILE A 625     -26.850   9.674  38.528  1.00 35.26           N  
ANISOU  439  N   ILE A 625     3891   3975   5531   -513   -477   -190       N  
ATOM    440  CA  ILE A 625     -28.062  10.371  38.952  1.00 35.34           C  
ANISOU  440  CA  ILE A 625     3870   4049   5508   -511   -481   -135       C  
ATOM    441  C   ILE A 625     -28.865   9.508  39.917  1.00 36.11           C  
ANISOU  441  C   ILE A 625     3901   4117   5702   -560   -488    -77       C  
ATOM    442  O   ILE A 625     -29.416  10.005  40.907  1.00 36.08           O  
ANISOU  442  O   ILE A 625     3875   4152   5681   -551   -457      2       O  
ATOM    443  CB  ILE A 625     -28.898  10.780  37.725  1.00 34.99           C  
ANISOU  443  CB  ILE A 625     3816   4077   5403   -496   -522   -186       C  
ATOM    444  CG1 ILE A 625     -28.082  11.679  36.793  1.00 34.93           C  
ANISOU  444  CG1 ILE A 625     3876   4105   5291   -445   -502   -217       C  
ATOM    445  CG2 ILE A 625     -30.169  11.490  38.156  1.00 34.30           C  
ANISOU  445  CG2 ILE A 625     3679   4058   5297   -479   -521   -118       C  
ATOM    446  CD1 ILE A 625     -28.817  12.072  35.527  1.00 35.60           C  
ANISOU  446  CD1 ILE A 625     3955   4278   5295   -422   -547   -251       C  
ATOM    447  N   CYS A 626     -28.946   8.203  39.644  1.00 37.37           N  
ANISOU  447  N   CYS A 626     4030   4203   5967   -610   -522   -116       N  
ATOM    448  CA  CYS A 626     -29.638   7.294  40.552  1.00 39.85           C  
ANISOU  448  CA  CYS A 626     4276   4470   6393   -665   -522    -44       C  
ATOM    449  C   CYS A 626     -29.000   7.314  41.937  1.00 40.98           C  
ANISOU  449  C   CYS A 626     4430   4598   6541   -650   -471     65       C  
ATOM    450  O   CYS A 626     -29.692   7.466  42.951  1.00 41.18           O  
ANISOU  450  O   CYS A 626     4416   4667   6563   -660   -442    160       O  
ATOM    451  CB  CYS A 626     -29.634   5.880  39.973  1.00 41.90           C  
ANISOU  451  CB  CYS A 626     4518   4619   6784   -724   -562   -113       C  
ATOM    452  SG  CYS A 626     -30.265   4.611  41.088  1.00 44.78           S  
ANISOU  452  SG  CYS A 626     4805   4888   7322   -801   -553     -4       S  
ATOM    453  N   LEU A 627     -27.674   7.168  41.996  1.00 42.70           N  
ANISOU  453  N   LEU A 627     4696   4771   6758   -624   -459     54       N  
ATOM    454  CA  LEU A 627     -26.978   7.218  43.278  1.00 43.20           C  
ANISOU  454  CA  LEU A 627     4766   4842   6807   -611   -428    157       C  
ATOM    455  C   LEU A 627     -27.066   8.599  43.912  1.00 42.60           C  
ANISOU  455  C   LEU A 627     4722   4871   6595   -581   -399    186       C  
ATOM    456  O   LEU A 627     -26.940   8.729  45.136  1.00 42.97           O  
ANISOU  456  O   LEU A 627     4767   4956   6604   -581   -376    271       O  
ATOM    457  CB  LEU A 627     -25.517   6.809  43.094  1.00 44.14           C  
ANISOU  457  CB  LEU A 627     4912   4902   6959   -585   -430    139       C  
ATOM    458  CG  LEU A 627     -25.274   5.328  42.806  1.00 44.79           C  
ANISOU  458  CG  LEU A 627     4968   4855   7198   -601   -442    131       C  
ATOM    459  CD1 LEU A 627     -23.978   5.140  42.041  1.00 44.98           C  
ANISOU  459  CD1 LEU A 627     5019   4830   7239   -555   -435     59       C  
ATOM    460  CD2 LEU A 627     -25.246   4.539  44.106  1.00 46.25           C  
ANISOU  460  CD2 LEU A 627     5110   5001   7461   -617   -430    277       C  
ATOM    461  N   GLY A 628     -27.274   9.640  43.104  1.00 39.21           N  
ANISOU  461  N   GLY A 628     4326   4486   6087   -553   -399    115       N  
ATOM    462  CA  GLY A 628     -27.447  10.970  43.663  1.00 36.10           C  
ANISOU  462  CA  GLY A 628     3969   4163   5584   -521   -364    132       C  
ATOM    463  C   GLY A 628     -28.698  11.078  44.513  1.00 35.02           C  
ANISOU  463  C   GLY A 628     3791   4079   5438   -522   -332    196       C  
ATOM    464  O   GLY A 628     -28.666  11.607  45.627  1.00 35.49           O  
ANISOU  464  O   GLY A 628     3872   4183   5428   -508   -292    241       O  
ATOM    465  N   TYR A 629     -29.822  10.571  43.998  1.00 33.84           N  
ANISOU  465  N   TYR A 629     3574   3932   5353   -539   -349    198       N  
ATOM    466  CA  TYR A 629     -31.050  10.572  44.785  1.00 32.39           C  
ANISOU  466  CA  TYR A 629     3325   3803   5177   -541   -310    273       C  
ATOM    467  C   TYR A 629     -30.954   9.626  45.973  1.00 32.29           C  
ANISOU  467  C   TYR A 629     3281   3778   5211   -581   -287    371       C  
ATOM    468  O   TYR A 629     -31.577   9.873  47.011  1.00 32.82           O  
ANISOU  468  O   TYR A 629     3324   3912   5234   -568   -229    448       O  
ATOM    469  CB  TYR A 629     -32.245  10.199  43.909  1.00 30.73           C  
ANISOU  469  CB  TYR A 629     3031   3607   5040   -564   -346    257       C  
ATOM    470  CG  TYR A 629     -32.546  11.201  42.820  1.00 28.21           C  
ANISOU  470  CG  TYR A 629     2729   3330   4659   -513   -368    191       C  
ATOM    471  CD1 TYR A 629     -32.900  12.507  43.131  1.00 26.78           C  
ANISOU  471  CD1 TYR A 629     2573   3208   4393   -439   -313    210       C  
ATOM    472  CD2 TYR A 629     -32.489  10.838  41.482  1.00 27.51           C  
ANISOU  472  CD2 TYR A 629     2636   3224   4595   -535   -439    113       C  
ATOM    473  CE1 TYR A 629     -33.179  13.425  42.139  1.00 26.48           C  
ANISOU  473  CE1 TYR A 629     2549   3202   4310   -383   -330    175       C  
ATOM    474  CE2 TYR A 629     -32.767  11.748  40.484  1.00 27.16           C  
ANISOU  474  CE2 TYR A 629     2605   3235   4480   -484   -461     75       C  
ATOM    475  CZ  TYR A 629     -33.111  13.040  40.818  1.00 27.26           C  
ANISOU  475  CZ  TYR A 629     2637   3298   4423   -406   -406    117       C  
ATOM    476  OH  TYR A 629     -33.390  13.949  39.825  1.00 28.41           O  
ANISOU  476  OH  TYR A 629     2794   3491   4509   -347   -425    102       O  
ATOM    477  N   LEU A 630     -30.182   8.544  45.843  1.00 31.59           N  
ANISOU  477  N   LEU A 630     3192   3604   5208   -620   -324    378       N  
ATOM    478  CA  LEU A 630     -30.001   7.619  46.955  1.00 32.58           C  
ANISOU  478  CA  LEU A 630     3287   3708   5382   -650   -304    495       C  
ATOM    479  C   LEU A 630     -29.174   8.220  48.083  1.00 33.43           C  
ANISOU  479  C   LEU A 630     3452   3883   5365   -617   -276    544       C  
ATOM    480  O   LEU A 630     -29.197   7.689  49.199  1.00 33.31           O  
ANISOU  480  O   LEU A 630     3414   3898   5345   -630   -249    662       O  
ATOM    481  CB  LEU A 630     -29.342   6.328  46.466  1.00 32.58           C  
ANISOU  481  CB  LEU A 630     3275   3581   5523   -687   -347    490       C  
ATOM    482  CG  LEU A 630     -30.146   5.467  45.492  1.00 34.03           C  
ANISOU  482  CG  LEU A 630     3404   3682   5846   -743   -383    437       C  
ATOM    483  CD1 LEU A 630     -29.331   4.262  45.054  1.00 35.05           C  
ANISOU  483  CD1 LEU A 630     3543   3664   6109   -765   -413    412       C  
ATOM    484  CD2 LEU A 630     -31.457   5.030  46.123  1.00 34.75           C  
ANISOU  484  CD2 LEU A 630     3403   3798   6003   -795   -354    540       C  
ATOM    485  N   CYS A 631     -28.441   9.308  47.819  1.00 34.09           N  
ANISOU  485  N   CYS A 631     3610   3997   5348   -580   -284    459       N  
ATOM    486  CA  CYS A 631     -27.642   9.937  48.866  1.00 34.38           C  
ANISOU  486  CA  CYS A 631     3701   4100   5261   -564   -271    484       C  
ATOM    487  C   CYS A 631     -28.508  10.420  50.020  1.00 35.36           C  
ANISOU  487  C   CYS A 631     3826   4326   5285   -548   -207    540       C  
ATOM    488  O   CYS A 631     -28.072  10.395  51.176  1.00 35.61           O  
ANISOU  488  O   CYS A 631     3879   4426   5227   -551   -197    604       O  
ATOM    489  CB  CYS A 631     -26.837  11.105  48.296  1.00 33.37           C  
ANISOU  489  CB  CYS A 631     3646   3972   5061   -542   -288    375       C  
ATOM    490  SG  CYS A 631     -25.416  10.635  47.288  1.00 32.74           S  
ANISOU  490  SG  CYS A 631     3570   3809   5059   -552   -346    327       S  
ATOM    491  N   THR A 632     -29.735  10.858  49.731  1.00 36.27           N  
ANISOU  491  N   THR A 632     3913   4464   5404   -526   -162    521       N  
ATOM    492  CA  THR A 632     -30.617  11.350  50.781  1.00 38.75           C  
ANISOU  492  CA  THR A 632     4221   4877   5623   -496    -81    569       C  
ATOM    493  C   THR A 632     -31.131  10.239  51.686  1.00 40.63           C  
ANISOU  493  C   THR A 632     4384   5154   5899   -528    -49    715       C  
ATOM    494  O   THR A 632     -31.812  10.536  52.673  1.00 42.30           O  
ANISOU  494  O   THR A 632     4587   5466   6019   -502     31    772       O  
ATOM    495  CB  THR A 632     -31.806  12.095  50.173  1.00 39.70           C  
ANISOU  495  CB  THR A 632     4312   5014   5759   -451    -37    522       C  
ATOM    496  OG1 THR A 632     -32.861  11.167  49.895  1.00 40.64           O  
ANISOU  496  OG1 THR A 632     4314   5128   5999   -483    -32    598       O  
ATOM    497  CG2 THR A 632     -31.396  12.787  48.884  1.00 38.93           C  
ANISOU  497  CG2 THR A 632     4258   4849   5683   -432    -87    411       C  
ATOM    498  N   PHE A 633     -30.831   8.982  51.379  1.00 40.68           N  
ANISOU  498  N   PHE A 633     4339   5078   6039   -580    -98    780       N  
ATOM    499  CA  PHE A 633     -31.284   7.869  52.202  1.00 42.22           C  
ANISOU  499  CA  PHE A 633     4461   5287   6294   -616    -65    940       C  
ATOM    500  C   PHE A 633     -30.197   7.417  53.172  1.00 43.49           C  
ANISOU  500  C   PHE A 633     4659   5475   6391   -619    -85   1032       C  
ATOM    501  O   PHE A 633     -30.421   6.530  53.994  1.00 44.76           O  
ANISOU  501  O   PHE A 633     4770   5657   6581   -641    -55   1190       O  
ATOM    502  CB  PHE A 633     -31.733   6.699  51.325  1.00 41.52           C  
ANISOU  502  CB  PHE A 633     4289   5073   6414   -677   -101    964       C  
ATOM    503  CG  PHE A 633     -33.012   6.958  50.581  1.00 41.78           C  
ANISOU  503  CG  PHE A 633     4251   5113   6509   -688    -85    915       C  
ATOM    504  CD1 PHE A 633     -34.234   6.829  51.218  1.00 42.96           C  
ANISOU  504  CD1 PHE A 633     4311   5339   6672   -700    -10   1020       C  
ATOM    505  CD2 PHE A 633     -32.994   7.330  49.247  1.00 41.03           C  
ANISOU  505  CD2 PHE A 633     4171   4964   6454   -684   -145    776       C  
ATOM    506  CE1 PHE A 633     -35.413   7.066  50.539  1.00 43.21           C  
ANISOU  506  CE1 PHE A 633     4257   5392   6769   -709     -3    986       C  
ATOM    507  CE2 PHE A 633     -34.172   7.568  48.562  1.00 41.06           C  
ANISOU  507  CE2 PHE A 633     4100   4994   6508   -692   -145    742       C  
ATOM    508  CZ  PHE A 633     -35.382   7.436  49.209  1.00 42.37           C  
ANISOU  508  CZ  PHE A 633     4165   5236   6700   -705    -78    847       C  
HETATM  509  N   YCM A 634     -29.021   8.029  53.071  1.00 44.52           N  
ANISOU  509  N   YCM A 634     4867   5610   6437   -598   -138    946       N  
HETATM  510  CA  YCM A 634     -27.947   7.779  54.018  1.00 46.63           C  
ANISOU  510  CA  YCM A 634     5163   5934   6619   -597   -170   1026       C  
HETATM  511  CB  YCM A 634     -26.695   7.267  53.316  1.00 47.67           C  
ANISOU  511  CB  YCM A 634     5296   5962   6854   -604   -253   1000       C  
HETATM  512  SG  YCM A 634     -27.066   7.056  51.610  1.00 48.53           S  
ANISOU  512  SG  YCM A 634     5384   5918   7139   -616   -269    877       S  
HETATM  513  CD  YCM A 634     -26.627   5.357  51.461  1.00 51.59           C  
ANISOU  513  CD  YCM A 634     5707   6168   7725   -638   -299    992       C  
HETATM  514  CE  YCM A 634     -27.081   4.830  50.120  1.00 54.92           C  
ANISOU  514  CE  YCM A 634     6105   6452   8312   -661   -312    898       C  
HETATM  515  OZ1 YCM A 634     -28.263   4.616  49.902  1.00 56.32           O  
ANISOU  515  OZ1 YCM A 634     6240   6612   8549   -696   -285    901       O  
HETATM  516  NZ2 YCM A 634     -26.128   4.613  49.215  1.00 55.84           N  
ANISOU  516  NZ2 YCM A 634     6241   6478   8496   -644   -354    812       N  
HETATM  517  C   YCM A 634     -27.677   9.058  54.751  1.00 45.98           C  
ANISOU  517  C   YCM A 634     5164   5982   6324   -570   -155    950       C  
HETATM  518  O   YCM A 634     -26.979   9.057  55.788  1.00 46.85           O  
ANISOU  518  O   YCM A 634     5302   6192   6306   -571   -178   1013       O  
ATOM    519  N   LEU A 635     -28.210  10.157  54.228  1.00 45.14           N  
ANISOU  519  N   LEU A 635     5100   5873   6179   -547   -121    814       N  
ATOM    520  CA  LEU A 635     -28.182  11.435  54.924  1.00 45.38           C  
ANISOU  520  CA  LEU A 635     5217   6004   6022   -519    -86    725       C  
ATOM    521  C   LEU A 635     -29.371  11.503  55.877  1.00 49.82           C  
ANISOU  521  C   LEU A 635     5762   6676   6493   -488     19    794       C  
ATOM    522  O   LEU A 635     -29.270  12.026  56.987  1.00 51.21           O  
ANISOU  522  O   LEU A 635     5997   6974   6484   -471     54    788       O  
ATOM    523  CB  LEU A 635     -28.211  12.598  53.930  1.00 42.65           C  
ANISOU  523  CB  LEU A 635     4926   5587   5692   -496    -86    563       C  
ATOM    524  CG  LEU A 635     -26.949  12.806  53.088  1.00 41.95           C  
ANISOU  524  CG  LEU A 635     4868   5416   5655   -524   -173    484       C  
ATOM    525  CD1 LEU A 635     -27.211  13.766  51.940  1.00 41.69           C  
ANISOU  525  CD1 LEU A 635     4869   5304   5668   -499   -160    363       C  
ATOM    526  CD2 LEU A 635     -25.811  13.318  53.954  1.00 43.24           C  
ANISOU  526  CD2 LEU A 635     5095   5651   5682   -550   -220    452       C  
ATOM    527  N   ILE A 636     -30.500  10.963  55.423  1.00 52.87           N  
ANISOU  527  N   ILE A 636     6059   7024   7006   -484     70    857       N  
ATOM    528  CA  ILE A 636     -31.691  10.813  56.250  1.00 57.10           C  
ANISOU  528  CA  ILE A 636     6542   7661   7491   -459    179    955       C  
ATOM    529  C   ILE A 636     -31.836   9.338  56.597  1.00 62.98           C  
ANISOU  529  C   ILE A 636     7192   8396   8340   -509    175   1147       C  
ATOM    530  O   ILE A 636     -32.568   8.601  55.928  1.00 58.90           O  
ANISOU  530  O   ILE A 636     6580   7798   8003   -541    181   1202       O  
ATOM    531  CB  ILE A 636     -32.946  11.342  55.530  1.00 54.50           C  
ANISOU  531  CB  ILE A 636     6161   7307   7239   -420    245    900       C  
ATOM    532  CG1 ILE A 636     -32.699  12.745  54.970  1.00 52.96           C  
ANISOU  532  CG1 ILE A 636     6060   7078   6985   -369    238    721       C  
ATOM    533  CG2 ILE A 636     -34.145  11.342  56.465  1.00 55.06           C  
ANISOU  533  CG2 ILE A 636     6172   7504   7243   -383    375    997       C  
ATOM    534  CD1 ILE A 636     -32.451  13.795  56.026  1.00 54.02           C  
ANISOU  534  CD1 ILE A 636     6306   7309   6912   -322    297    645       C  
ATOM    535  N   ALA A 637     -31.131   8.890  57.635  1.00 73.83           N  
ANISOU  535  N   ALA A 637     8592   9851   9607   -520    160   1253       N  
ATOM    536  CA  ALA A 637     -31.103   7.474  57.968  1.00 83.66           C  
ANISOU  536  CA  ALA A 637     9756  11066  10964   -563    151   1452       C  
ATOM    537  C   ALA A 637     -30.920   7.303  59.469  1.00 86.99           C  
ANISOU  537  C   ALA A 637    10200  11660  11193   -547    194   1597       C  
ATOM    538  O   ALA A 637     -30.724   8.269  60.211  1.00 88.16           O  
ANISOU  538  O   ALA A 637    10433  11949  11114   -510    218   1518       O  
ATOM    539  CB  ALA A 637     -29.992   6.745  57.205  1.00 85.47           C  
ANISOU  539  CB  ALA A 637     9983  11148  11343   -596     36   1448       C  
ATOM    540  N   LYS A 638     -30.988   6.045  59.906  1.00 89.58           N  
ANISOU  540  N   LYS A 638    10453  11971  11613   -579    203   1812       N  
ATOM    541  CA  LYS A 638     -30.786   5.679  61.296  1.00 93.13           C  
ANISOU  541  CA  LYS A 638    10910  12585  11891   -565    238   1994       C  
ATOM    542  C   LYS A 638     -29.296   5.681  61.634  1.00 92.27           C  
ANISOU  542  C   LYS A 638    10865  12513  11682   -559    118   1993       C  
ATOM    543  O   LYS A 638     -28.457   5.407  60.771  1.00 91.56           O  
ANISOU  543  O   LYS A 638    10772  12277  11741   -575     20   1933       O  
ATOM    544  CB  LYS A 638     -31.379   4.301  61.572  1.00 97.27           C  
ANISOU  544  CB  LYS A 638    11323  13057  12578   -603    291   2246       C  
ATOM    545  CG  LYS A 638     -32.832   4.157  61.147  1.00 99.67           C  
ANISOU  545  CG  LYS A 638    11534  13312  13024   -630    394   2262       C  
ATOM    546  CD  LYS A 638     -33.348   2.751  61.403  1.00102.61           C  
ANISOU  546  CD  LYS A 638    11793  13609  13583   -687    441   2516       C  
ATOM    547  CE  LYS A 638     -34.782   2.594  60.926  1.00103.21           C  
ANISOU  547  CE  LYS A 638    11757  13637  13821   -732    530   2527       C  
ATOM    548  NZ  LYS A 638     -35.303   1.223  61.181  1.00105.39           N  
ANISOU  548  NZ  LYS A 638    11918  13825  14300   -807    577   2777       N  
ATOM    549  N   PRO A 639     -28.939   5.991  62.884  1.00 92.55           N  
ANISOU  549  N   PRO A 639    10953  12755  11456   -534    125   2057       N  
ATOM    550  CA  PRO A 639     -27.517   6.076  63.243  1.00 89.95           C  
ANISOU  550  CA  PRO A 639    10671  12489  11015   -534     -3   2051       C  
ATOM    551  C   PRO A 639     -26.786   4.745  63.146  1.00 84.11           C  
ANISOU  551  C   PRO A 639     9854  11650  10453   -544    -77   2256       C  
ATOM    552  O   PRO A 639     -26.606   4.047  64.149  1.00 83.06           O  
ANISOU  552  O   PRO A 639     9693  11634  10233   -531    -74   2481       O  
ATOM    553  CB  PRO A 639     -27.550   6.592  64.688  1.00 92.88           C  
ANISOU  553  CB  PRO A 639    11107  13127  11056   -510     33   2094       C  
ATOM    554  CG  PRO A 639     -28.904   6.227  65.193  1.00 95.89           C  
ANISOU  554  CG  PRO A 639    11441  13571  11424   -494    190   2232       C  
ATOM    555  CD  PRO A 639     -29.816   6.345  64.013  1.00 94.94           C  
ANISOU  555  CD  PRO A 639    11274  13262  11539   -505    249   2122       C  
ATOM    556  N   LYS A 640     -26.366   4.385  61.937  1.00 77.53           N  
ANISOU  556  N   LYS A 640     8988  10602   9866   -559   -136   2183       N  
ATOM    557  CA  LYS A 640     -25.496   3.243  61.708  1.00 70.85           C  
ANISOU  557  CA  LYS A 640     8081   9637   9202   -553   -210   2332       C  
ATOM    558  C   LYS A 640     -24.188   3.728  61.099  1.00 64.13           C  
ANISOU  558  C   LYS A 640     7258   8749   8360   -545   -329   2182       C  
ATOM    559  O   LYS A 640     -24.126   4.785  60.466  1.00 60.46           O  
ANISOU  559  O   LYS A 640     6850   8273   7850   -558   -344   1953       O  
ATOM    560  CB  LYS A 640     -26.157   2.198  60.798  1.00 66.88           C  
ANISOU  560  CB  LYS A 640     7506   8895   9010   -577   -163   2390       C  
ATOM    561  CG  LYS A 640     -27.268   1.409  61.472  1.00 66.20           C  
ANISOU  561  CG  LYS A 640     7361   8826   8965   -597    -56   2605       C  
ATOM    562  CD  LYS A 640     -27.686   0.207  60.637  1.00 64.97           C  
ANISOU  562  CD  LYS A 640     7129   8413   9141   -634    -34   2679       C  
ATOM    563  CE  LYS A 640     -28.682  -0.667  61.387  1.00 66.66           C  
ANISOU  563  CE  LYS A 640     7273   8638   9417   -666     69   2929       C  
ATOM    564  NZ  LYS A 640     -29.015  -1.911  60.638  1.00 67.23           N  
ANISOU  564  NZ  LYS A 640     7274   8440   9830   -717     81   3006       N  
ATOM    565  N   GLN A 641     -23.133   2.934  61.293  1.00 62.85           N  
ANISOU  565  N   GLN A 641     7045   8566   8268   -520   -409   2329       N  
ATOM    566  CA  GLN A 641     -21.793   3.405  60.956  1.00 60.48           C  
ANISOU  566  CA  GLN A 641     6752   8283   7944   -511   -524   2222       C  
ATOM    567  C   GLN A 641     -21.555   3.407  59.450  1.00 56.51           C  
ANISOU  567  C   GLN A 641     6240   7561   7669   -514   -532   2054       C  
ATOM    568  O   GLN A 641     -20.933   4.335  58.920  1.00 54.61           O  
ANISOU  568  O   GLN A 641     6035   7336   7378   -527   -582   1868       O  
ATOM    569  CB  GLN A 641     -20.743   2.551  61.667  1.00 62.76           C  
ANISOU  569  CB  GLN A 641     6973   8637   8236   -471   -606   2449       C  
ATOM    570  CG  GLN A 641     -19.328   3.116  61.608  1.00 62.54           C  
ANISOU  570  CG  GLN A 641     6934   8693   8136   -466   -733   2367       C  
ATOM    571  CD  GLN A 641     -19.114   4.295  62.545  1.00 63.30           C  
ANISOU  571  CD  GLN A 641     7097   9046   7909   -505   -788   2274       C  
ATOM    572  OE1 GLN A 641     -19.890   5.251  62.557  1.00 62.32           O  
ANISOU  572  OE1 GLN A 641     7060   8964   7655   -541   -729   2103       O  
ATOM    573  NE2 GLN A 641     -18.051   4.229  63.338  1.00 64.83           N  
ANISOU  573  NE2 GLN A 641     7247   9410   7974   -495   -904   2385       N  
ATOM    574  N   ILE A 642     -22.037   2.380  58.743  1.00 55.32           N  
ANISOU  574  N   ILE A 642     6044   7207   7767   -507   -481   2113       N  
ATOM    575  CA  ILE A 642     -21.793   2.289  57.307  1.00 54.37           C  
ANISOU  575  CA  ILE A 642     5919   6889   7849   -505   -488   1954       C  
ATOM    576  C   ILE A 642     -22.444   3.435  56.549  1.00 53.08           C  
ANISOU  576  C   ILE A 642     5820   6726   7621   -540   -457   1718       C  
ATOM    577  O   ILE A 642     -22.003   3.775  55.447  1.00 50.85           O  
ANISOU  577  O   ILE A 642     5552   6350   7420   -537   -481   1558       O  
ATOM    578  CB  ILE A 642     -22.276   0.931  56.756  1.00 55.72           C  
ANISOU  578  CB  ILE A 642     6040   6839   8293   -501   -440   2051       C  
ATOM    579  CG1 ILE A 642     -23.769   0.739  57.030  1.00 56.32           C  
ANISOU  579  CG1 ILE A 642     6115   6908   8377   -548   -353   2102       C  
ATOM    580  CG2 ILE A 642     -21.463  -0.206  57.353  1.00 58.21           C  
ANISOU  580  CG2 ILE A 642     6291   7117   8711   -449   -472   2284       C  
ATOM    581  CD1 ILE A 642     -24.342  -0.518  56.418  1.00 57.34           C  
ANISOU  581  CD1 ILE A 642     6196   6806   8786   -570   -310   2167       C  
ATOM    582  N   TYR A 643     -23.485   4.048  57.116  1.00 54.04           N  
ANISOU  582  N   TYR A 643     5979   6957   7598   -564   -398   1701       N  
ATOM    583  CA  TYR A 643     -24.132   5.168  56.441  1.00 52.75           C  
ANISOU  583  CA  TYR A 643     5872   6793   7378   -582   -365   1494       C  
ATOM    584  C   TYR A 643     -23.214   6.383  56.374  1.00 50.65           C  
ANISOU  584  C   TYR A 643     5667   6612   6967   -582   -424   1342       C  
ATOM    585  O   TYR A 643     -23.235   7.125  55.386  1.00 48.85           O  
ANISOU  585  O   TYR A 643     5474   6316   6771   -588   -423   1170       O  
ATOM    586  CB  TYR A 643     -25.447   5.512  57.138  1.00 53.48           C  
ANISOU  586  CB  TYR A 643     5978   6985   7356   -592   -276   1526       C  
ATOM    587  CG  TYR A 643     -26.575   4.563  56.802  1.00 53.02           C  
ANISOU  587  CG  TYR A 643     5853   6814   7478   -613   -209   1616       C  
ATOM    588  CD1 TYR A 643     -26.693   4.021  55.528  1.00 51.65           C  
ANISOU  588  CD1 TYR A 643     5648   6451   7525   -631   -225   1542       C  
ATOM    589  CD2 TYR A 643     -27.517   4.204  57.757  1.00 54.10           C  
ANISOU  589  CD2 TYR A 643     5955   7038   7561   -621   -129   1772       C  
ATOM    590  CE1 TYR A 643     -27.719   3.153  55.213  1.00 52.24           C  
ANISOU  590  CE1 TYR A 643     5659   6419   7772   -669   -177   1610       C  
ATOM    591  CE2 TYR A 643     -28.547   3.335  57.451  1.00 54.70           C  
ANISOU  591  CE2 TYR A 643     5956   7007   7819   -657    -70   1859       C  
ATOM    592  CZ  TYR A 643     -28.643   2.813  56.178  1.00 54.16           C  
ANISOU  592  CZ  TYR A 643     5857   6742   7978   -687   -101   1772       C  
ATOM    593  OH  TYR A 643     -29.666   1.948  55.869  1.00 56.03           O  
ANISOU  593  OH  TYR A 643     6018   6870   8403   -740    -55   1845       O  
ATOM    594  N   CYS A 644     -22.400   6.605  57.412  1.00 50.30           N  
ANISOU  594  N   CYS A 644     5633   6718   6761   -581   -481   1408       N  
ATOM    595  CA  CYS A 644     -21.375   7.642  57.320  1.00 48.72           C  
ANISOU  595  CA  CYS A 644     5474   6581   6455   -598   -554   1271       C  
ATOM    596  C   CYS A 644     -20.348   7.304  56.248  1.00 47.89           C  
ANISOU  596  C   CYS A 644     5320   6349   6527   -589   -608   1234       C  
ATOM    597  O   CYS A 644     -19.792   8.208  55.612  1.00 48.98           O  
ANISOU  597  O   CYS A 644     5489   6471   6650   -609   -636   1082       O  
ATOM    598  CB  CYS A 644     -20.687   7.843  58.674  1.00 48.29           C  
ANISOU  598  CB  CYS A 644     5428   6727   6192   -610   -621   1354       C  
ATOM    599  SG  CYS A 644     -21.694   8.667  59.939  1.00 48.63           S  
ANISOU  599  SG  CYS A 644     5561   6958   5958   -621   -555   1325       S  
ATOM    600  N   TYR A 645     -20.085   6.013  56.032  1.00 45.14           N  
ANISOU  600  N   TYR A 645     4896   5903   6351   -555   -614   1373       N  
ATOM    601  CA  TYR A 645     -19.229   5.607  54.923  1.00 43.22           C  
ANISOU  601  CA  TYR A 645     4608   5523   6289   -531   -640   1328       C  
ATOM    602  C   TYR A 645     -19.929   5.809  53.586  1.00 39.41           C  
ANISOU  602  C   TYR A 645     4159   4895   5919   -537   -581   1172       C  
ATOM    603  O   TYR A 645     -19.319   6.290  52.625  1.00 38.67           O  
ANISOU  603  O   TYR A 645     4074   4752   5868   -535   -595   1045       O  
ATOM    604  CB  TYR A 645     -18.811   4.146  55.083  1.00 45.71           C  
ANISOU  604  CB  TYR A 645     4842   5756   6771   -481   -650   1515       C  
ATOM    605  CG  TYR A 645     -17.599   3.933  55.959  1.00 47.62           C  
ANISOU  605  CG  TYR A 645     5021   6122   6951   -455   -736   1657       C  
ATOM    606  CD1 TYR A 645     -16.318   3.973  55.423  1.00 47.96           C  
ANISOU  606  CD1 TYR A 645     5007   6147   7070   -428   -791   1625       C  
ATOM    607  CD2 TYR A 645     -17.734   3.679  57.317  1.00 49.14           C  
ANISOU  607  CD2 TYR A 645     5202   6463   7006   -455   -761   1833       C  
ATOM    608  CE1 TYR A 645     -15.206   3.774  56.216  1.00 49.99           C  
ANISOU  608  CE1 TYR A 645     5185   6531   7277   -404   -880   1764       C  
ATOM    609  CE2 TYR A 645     -16.628   3.479  58.118  1.00 51.12           C  
ANISOU  609  CE2 TYR A 645     5386   6847   7188   -430   -854   1972       C  
ATOM    610  CZ  TYR A 645     -15.367   3.527  57.563  1.00 52.11           C  
ANISOU  610  CZ  TYR A 645     5445   6952   7403   -406   -919   1937       C  
ATOM    611  OH  TYR A 645     -14.261   3.329  58.357  1.00 55.69           O  
ANISOU  611  OH  TYR A 645     5813   7553   7794   -381  -1021   2085       O  
ATOM    612  N   LEU A 646     -21.212   5.446  53.507  1.00 36.82           N  
ANISOU  612  N   LEU A 646     3844   4509   5635   -547   -517   1187       N  
ATOM    613  CA  LEU A 646     -21.942   5.582  52.252  1.00 33.75           C  
ANISOU  613  CA  LEU A 646     3478   4002   5346   -556   -475   1048       C  
ATOM    614  C   LEU A 646     -22.211   7.042  51.910  1.00 33.07           C  
ANISOU  614  C   LEU A 646     3459   3982   5125   -573   -465    888       C  
ATOM    615  O   LEU A 646     -22.317   7.386  50.728  1.00 33.19           O  
ANISOU  615  O   LEU A 646     3493   3920   5199   -571   -454    762       O  
ATOM    616  CB  LEU A 646     -23.251   4.795  52.320  1.00 33.61           C  
ANISOU  616  CB  LEU A 646     3436   3917   5418   -573   -420   1117       C  
ATOM    617  CG  LEU A 646     -23.119   3.282  52.512  1.00 35.18           C  
ANISOU  617  CG  LEU A 646     3572   4000   5793   -563   -418   1273       C  
ATOM    618  CD1 LEU A 646     -24.486   2.624  52.603  1.00 36.04           C  
ANISOU  618  CD1 LEU A 646     3653   4047   5992   -602   -362   1338       C  
ATOM    619  CD2 LEU A 646     -22.293   2.660  51.396  1.00 35.41           C  
ANISOU  619  CD2 LEU A 646     3586   3874   5994   -533   -441   1202       C  
ATOM    620  N   GLN A 647     -22.325   7.909  52.918  1.00 32.81           N  
ANISOU  620  N   GLN A 647     3467   4087   4911   -587   -465    892       N  
ATOM    621  CA  GLN A 647     -22.472   9.337  52.655  1.00 32.07           C  
ANISOU  621  CA  GLN A 647     3446   4037   4704   -599   -452    740       C  
ATOM    622  C   GLN A 647     -21.281   9.869  51.869  1.00 31.84           C  
ANISOU  622  C   GLN A 647     3425   3973   4702   -606   -500    646       C  
ATOM    623  O   GLN A 647     -21.436  10.426  50.776  1.00 31.74           O  
ANISOU  623  O   GLN A 647     3438   3890   4732   -603   -478    535       O  
ATOM    624  CB  GLN A 647     -22.624  10.106  53.968  1.00 32.27           C  
ANISOU  624  CB  GLN A 647     3521   4211   4529   -612   -446    750       C  
ATOM    625  CG  GLN A 647     -24.016  10.079  54.570  1.00 32.50           C  
ANISOU  625  CG  GLN A 647     3561   4289   4500   -598   -366    794       C  
ATOM    626  CD  GLN A 647     -24.110  10.931  55.818  1.00 32.74           C  
ANISOU  626  CD  GLN A 647     3657   4471   4311   -602   -349    773       C  
ATOM    627  OE1 GLN A 647     -23.151  11.605  56.191  1.00 31.97           O  
ANISOU  627  OE1 GLN A 647     3603   4436   4107   -627   -409    709       O  
ATOM    628  NE2 GLN A 647     -25.267  10.909  56.469  1.00 33.26           N  
ANISOU  628  NE2 GLN A 647     3728   4603   4308   -580   -265    822       N  
ATOM    629  N   ARG A 648     -20.076   9.703  52.419  1.00 33.09           N  
ANISOU  629  N   ARG A 648     3550   4190   4833   -616   -565    704       N  
ATOM    630  CA  ARG A 648     -18.876  10.204  51.758  1.00 33.52           C  
ANISOU  630  CA  ARG A 648     3591   4227   4918   -630   -607    631       C  
ATOM    631  C   ARG A 648     -18.633   9.499  50.430  1.00 34.12           C  
ANISOU  631  C   ARG A 648     3625   4172   5168   -594   -585    611       C  
ATOM    632  O   ARG A 648     -18.057  10.090  49.509  1.00 33.21           O  
ANISOU  632  O   ARG A 648     3516   4023   5079   -599   -582    519       O  
ATOM    633  CB  ARG A 648     -17.669  10.043  52.685  1.00 34.14           C  
ANISOU  633  CB  ARG A 648     3617   4413   4941   -648   -690    718       C  
ATOM    634  CG  ARG A 648     -17.840  10.733  54.032  1.00 34.46           C  
ANISOU  634  CG  ARG A 648     3709   4603   4782   -689   -721    722       C  
ATOM    635  CD  ARG A 648     -16.817  10.257  55.054  1.00 36.17           C  
ANISOU  635  CD  ARG A 648     3857   4947   4938   -699   -814    848       C  
ATOM    636  NE  ARG A 648     -15.473  10.770  54.799  1.00 36.47           N  
ANISOU  636  NE  ARG A 648     3848   5018   4990   -739   -891    801       N  
ATOM    637  CZ  ARG A 648     -14.466  10.675  55.663  1.00 37.53           C  
ANISOU  637  CZ  ARG A 648     3918   5291   5051   -766   -993    882       C  
ATOM    638  NH1 ARG A 648     -14.653  10.089  56.837  1.00 38.52           N  
ANISOU  638  NH1 ARG A 648     4030   5537   5068   -750  -1029   1017       N  
ATOM    639  NH2 ARG A 648     -13.273  11.168  55.358  1.00 37.58           N  
ANISOU  639  NH2 ARG A 648     3865   5325   5088   -811  -1060    838       N  
ATOM    640  N   ILE A 649     -19.085   8.249  50.304  1.00 36.77           N  
ANISOU  640  N   ILE A 649     3920   4430   5620   -560   -564    692       N  
ATOM    641  CA  ILE A 649     -18.885   7.498  49.070  1.00 38.37           C  
ANISOU  641  CA  ILE A 649     4093   4503   5983   -525   -540    654       C  
ATOM    642  C   ILE A 649     -19.902   7.856  47.994  1.00 38.12           C  
ANISOU  642  C   ILE A 649     4112   4406   5967   -530   -494    533       C  
ATOM    643  O   ILE A 649     -19.613   7.678  46.806  1.00 39.21           O  
ANISOU  643  O   ILE A 649     4248   4468   6183   -509   -478    454       O  
ATOM    644  CB  ILE A 649     -18.912   5.987  49.361  1.00 40.15           C  
ANISOU  644  CB  ILE A 649     4260   4647   6347   -491   -538    782       C  
ATOM    645  CG1 ILE A 649     -17.711   5.304  48.718  1.00 41.72           C  
ANISOU  645  CG1 ILE A 649     4400   4772   6678   -439   -546    791       C  
ATOM    646  CG2 ILE A 649     -20.212   5.345  48.884  1.00 40.04           C  
ANISOU  646  CG2 ILE A 649     4264   4530   6421   -499   -493    759       C  
ATOM    647  CD1 ILE A 649     -17.288   4.046  49.430  1.00 44.74           C  
ANISOU  647  CD1 ILE A 649     4714   5112   7172   -395   -562    958       C  
ATOM    648  N   GLY A 650     -21.075   8.364  48.366  1.00 37.22           N  
ANISOU  648  N   GLY A 650     4039   4331   5773   -553   -471    519       N  
ATOM    649  CA  GLY A 650     -22.082   8.721  47.386  1.00 35.91           C  
ANISOU  649  CA  GLY A 650     3904   4121   5619   -553   -437    422       C  
ATOM    650  C   GLY A 650     -22.031  10.180  46.985  1.00 36.08           C  
ANISOU  650  C   GLY A 650     3985   4189   5536   -558   -427    324       C  
ATOM    651  O   GLY A 650     -22.188  10.509  45.807  1.00 36.34           O  
ANISOU  651  O   GLY A 650     4037   4181   5590   -545   -412    241       O  
ATOM    652  N   ILE A 651     -21.823  11.068  47.961  1.00 36.88           N  
ANISOU  652  N   ILE A 651     4120   4373   5520   -576   -433    335       N  
ATOM    653  CA  ILE A 651     -21.725  12.493  47.667  1.00 35.87           C  
ANISOU  653  CA  ILE A 651     4056   4265   5309   -585   -419    244       C  
ATOM    654  C   ILE A 651     -20.467  12.806  46.864  1.00 35.44           C  
ANISOU  654  C   ILE A 651     3993   4184   5288   -594   -438    201       C  
ATOM    655  O   ILE A 651     -20.368  13.878  46.256  1.00 35.89           O  
ANISOU  655  O   ILE A 651     4096   4227   5313   -600   -418    131       O  
ATOM    656  CB  ILE A 651     -21.794  13.290  48.987  1.00 35.67           C  
ANISOU  656  CB  ILE A 651     4076   4324   5152   -608   -420    248       C  
ATOM    657  CG1 ILE A 651     -23.079  12.935  49.739  1.00 35.77           C  
ANISOU  657  CG1 ILE A 651     4086   4375   5129   -589   -380    301       C  
ATOM    658  CG2 ILE A 651     -21.750  14.795  48.744  1.00 34.78           C  
ANISOU  658  CG2 ILE A 651     4040   4203   4972   -619   -398    147       C  
ATOM    659  CD1 ILE A 651     -23.283  13.719  51.018  1.00 36.21           C  
ANISOU  659  CD1 ILE A 651     4198   4524   5036   -599   -364    290       C  
ATOM    660  N   GLY A 652     -19.510  11.882  46.822  1.00 34.85           N  
ANISOU  660  N   GLY A 652     3855   4098   5288   -589   -468    252       N  
ATOM    661  CA  GLY A 652     -18.307  12.073  46.039  1.00 34.17           C  
ANISOU  661  CA  GLY A 652     3742   3995   5246   -590   -474    223       C  
ATOM    662  C   GLY A 652     -18.330  11.368  44.697  1.00 34.97           C  
ANISOU  662  C   GLY A 652     3822   4022   5442   -546   -441    188       C  
ATOM    663  O   GLY A 652     -17.940  11.955  43.685  1.00 35.78           O  
ANISOU  663  O   GLY A 652     3940   4113   5540   -540   -413    129       O  
ATOM    664  N   LEU A 653     -18.791  10.112  44.668  1.00 35.35           N  
ANISOU  664  N   LEU A 653     3841   4017   5573   -517   -440    220       N  
ATOM    665  CA  LEU A 653     -18.715   9.325  43.439  1.00 36.09           C  
ANISOU  665  CA  LEU A 653     3921   4035   5757   -477   -412    167       C  
ATOM    666  C   LEU A 653     -19.875   9.608  42.491  1.00 35.50           C  
ANISOU  666  C   LEU A 653     3897   3940   5652   -477   -392     83       C  
ATOM    667  O   LEU A 653     -19.668   9.707  41.277  1.00 34.93           O  
ANISOU  667  O   LEU A 653     3840   3853   5579   -454   -367      8       O  
ATOM    668  CB  LEU A 653     -18.665   7.830  43.760  1.00 37.44           C  
ANISOU  668  CB  LEU A 653     4042   4132   6052   -451   -420    227       C  
ATOM    669  CG  LEU A 653     -17.282   7.197  43.917  1.00 38.83           C  
ANISOU  669  CG  LEU A 653     4150   4292   6311   -412   -424    285       C  
ATOM    670  CD1 LEU A 653     -17.385   5.681  43.835  1.00 39.53           C  
ANISOU  670  CD1 LEU A 653     4206   4263   6550   -370   -412    318       C  
ATOM    671  CD2 LEU A 653     -16.319   7.733  42.867  1.00 38.76           C  
ANISOU  671  CD2 LEU A 653     4134   4302   6293   -388   -390    213       C  
ATOM    672  N   SER A 654     -21.097   9.722  43.015  1.00 35.44           N  
ANISOU  672  N   SER A 654     3907   3946   5614   -498   -401    101       N  
ATOM    673  CA  SER A 654     -22.254   9.874  42.135  1.00 34.96           C  
ANISOU  673  CA  SER A 654     3871   3877   5537   -495   -393     36       C  
ATOM    674  C   SER A 654     -22.184  11.112  41.243  1.00 34.82           C  
ANISOU  674  C   SER A 654     3899   3901   5430   -481   -374    -23       C  
ATOM    675  O   SER A 654     -22.651  11.028  40.094  1.00 34.87           O  
ANISOU  675  O   SER A 654     3917   3903   5428   -465   -373    -86       O  
ATOM    676  CB  SER A 654     -23.551   9.855  42.958  1.00 34.79           C  
ANISOU  676  CB  SER A 654     3839   3876   5502   -517   -399     84       C  
ATOM    677  OG  SER A 654     -23.669  10.976  43.813  1.00 34.18           O  
ANISOU  677  OG  SER A 654     3793   3867   5328   -521   -385    113       O  
ATOM    678  N   PRO A 655     -21.635  12.258  41.669  1.00 34.04           N  
ANISOU  678  N   PRO A 655     3830   3841   5264   -489   -361     -5       N  
ATOM    679  CA  PRO A 655     -21.392  13.319  40.678  1.00 33.86           C  
ANISOU  679  CA  PRO A 655     3847   3835   5184   -475   -335    -46       C  
ATOM    680  C   PRO A 655     -20.234  12.995  39.755  1.00 35.21           C  
ANISOU  680  C   PRO A 655     3999   3996   5382   -460   -316    -72       C  
ATOM    681  O   PRO A 655     -20.291  13.312  38.560  1.00 36.33           O  
ANISOU  681  O   PRO A 655     4164   4152   5486   -435   -291   -112       O  
ATOM    682  CB  PRO A 655     -21.107  14.554  41.543  1.00 33.40           C  
ANISOU  682  CB  PRO A 655     3824   3796   5070   -502   -326    -22       C  
ATOM    683  CG  PRO A 655     -20.592  14.004  42.816  1.00 33.23           C  
ANISOU  683  CG  PRO A 655     3770   3786   5070   -532   -355     23       C  
ATOM    684  CD  PRO A 655     -21.337  12.724  43.038  1.00 33.49           C  
ANISOU  684  CD  PRO A 655     3764   3802   5157   -518   -371     48       C  
ATOM    685  N   ALA A 656     -19.182  12.363  40.281  1.00 35.15           N  
ANISOU  685  N   ALA A 656     3945   3976   5435   -467   -322    -42       N  
ATOM    686  CA  ALA A 656     -18.043  11.993  39.448  1.00 34.87           C  
ANISOU  686  CA  ALA A 656     3876   3935   5437   -441   -291    -62       C  
ATOM    687  C   ALA A 656     -18.447  10.999  38.367  1.00 34.86           C  
ANISOU  687  C   ALA A 656     3880   3900   5466   -398   -275   -133       C  
ATOM    688  O   ALA A 656     -17.912  11.034  37.253  1.00 34.77           O  
ANISOU  688  O   ALA A 656     3874   3904   5432   -365   -231   -180       O  
ATOM    689  CB  ALA A 656     -16.924  11.417  40.315  1.00 34.65           C  
ANISOU  689  CB  ALA A 656     3779   3904   5482   -446   -307     -1       C  
ATOM    690  N   MET A 657     -19.388  10.103  38.674  1.00 35.12           N  
ANISOU  690  N   MET A 657     3911   3887   5545   -402   -308   -145       N  
ATOM    691  CA  MET A 657     -19.828   9.129  37.680  1.00 34.68           C  
ANISOU  691  CA  MET A 657     3866   3787   5524   -378   -305   -233       C  
ATOM    692  C   MET A 657     -20.538   9.806  36.517  1.00 33.48           C  
ANISOU  692  C   MET A 657     3762   3694   5264   -372   -302   -300       C  
ATOM    693  O   MET A 657     -20.313   9.455  35.353  1.00 33.93           O  
ANISOU  693  O   MET A 657     3839   3760   5294   -341   -279   -384       O  
ATOM    694  CB  MET A 657     -20.738   8.089  38.331  1.00 35.20           C  
ANISOU  694  CB  MET A 657     3912   3783   5678   -405   -345   -221       C  
ATOM    695  CG  MET A 657     -20.013   7.138  39.265  1.00 36.19           C  
ANISOU  695  CG  MET A 657     3989   3838   5923   -395   -344   -150       C  
ATOM    696  SD  MET A 657     -21.134   6.001  40.097  1.00 37.26           S  
ANISOU  696  SD  MET A 657     4101   3888   6169   -435   -381   -103       S  
ATOM    697  CE  MET A 657     -22.032   5.322  38.703  1.00 37.10           C  
ANISOU  697  CE  MET A 657     4111   3809   6175   -449   -392   -254       C  
ATOM    698  N   SER A 658     -21.395  10.784  36.809  1.00 32.14           N  
ANISOU  698  N   SER A 658     3613   3573   5027   -393   -323   -261       N  
ATOM    699  CA  SER A 658     -22.134  11.454  35.746  1.00 32.13           C  
ANISOU  699  CA  SER A 658     3647   3635   4925   -378   -329   -299       C  
ATOM    700  C   SER A 658     -21.242  12.418  34.976  1.00 32.92           C  
ANISOU  700  C   SER A 658     3776   3786   4945   -350   -275   -286       C  
ATOM    701  O   SER A 658     -21.291  12.468  33.742  1.00 34.30           O  
ANISOU  701  O   SER A 658     3977   4012   5043   -320   -261   -336       O  
ATOM    702  CB  SER A 658     -23.339  12.190  36.329  1.00 31.02           C  
ANISOU  702  CB  SER A 658     3509   3523   4756   -393   -358   -248       C  
ATOM    703  OG  SER A 658     -24.242  11.283  36.937  1.00 31.27           O  
ANISOU  703  OG  SER A 658     3503   3520   4860   -423   -400   -250       O  
ATOM    704  N   TYR A 659     -20.414  13.183  35.687  1.00 32.60           N  
ANISOU  704  N   TYR A 659     3730   3737   4919   -364   -246   -219       N  
ATOM    705  CA  TYR A 659     -19.627  14.227  35.044  1.00 33.06           C  
ANISOU  705  CA  TYR A 659     3809   3833   4918   -354   -192   -188       C  
ATOM    706  C   TYR A 659     -18.419  13.675  34.299  1.00 32.95           C  
ANISOU  706  C   TYR A 659     3769   3833   4917   -328   -139   -217       C  
ATOM    707  O   TYR A 659     -18.057  14.209  33.245  1.00 33.63           O  
ANISOU  707  O   TYR A 659     3876   3975   4929   -302    -87   -214       O  
ATOM    708  CB  TYR A 659     -19.187  15.259  36.084  1.00 34.09           C  
ANISOU  708  CB  TYR A 659     3942   3941   5070   -396   -186   -118       C  
ATOM    709  CG  TYR A 659     -20.338  16.036  36.686  1.00 34.82           C  
ANISOU  709  CG  TYR A 659     4072   4022   5134   -404   -212    -94       C  
ATOM    710  CD1 TYR A 659     -21.453  16.364  35.924  1.00 35.32           C  
ANISOU  710  CD1 TYR A 659     4165   4118   5138   -366   -220    -98       C  
ATOM    711  CD2 TYR A 659     -20.312  16.435  38.015  1.00 35.22           C  
ANISOU  711  CD2 TYR A 659     4126   4043   5214   -442   -228    -67       C  
ATOM    712  CE1 TYR A 659     -22.509  17.073  36.470  1.00 35.77           C  
ANISOU  712  CE1 TYR A 659     4244   4165   5181   -357   -233    -70       C  
ATOM    713  CE2 TYR A 659     -21.363  17.143  38.570  1.00 35.84           C  
ANISOU  713  CE2 TYR A 659     4241   4111   5266   -436   -235    -54       C  
ATOM    714  CZ  TYR A 659     -22.458  17.459  37.794  1.00 36.23           C  
ANISOU  714  CZ  TYR A 659     4310   4182   5274   -389   -233    -52       C  
ATOM    715  OH  TYR A 659     -23.503  18.163  38.349  1.00 36.95           O  
ANISOU  715  OH  TYR A 659     4426   4263   5351   -368   -229    -32       O  
ATOM    716  N   SER A 660     -17.780  12.622  34.814  1.00 32.57           N  
ANISOU  716  N   SER A 660     3671   3740   4962   -325   -142   -235       N  
ATOM    717  CA  SER A 660     -16.637  12.047  34.114  1.00 33.29           C  
ANISOU  717  CA  SER A 660     3729   3843   5079   -283    -79   -265       C  
ATOM    718  C   SER A 660     -17.053  11.199  32.920  1.00 33.44           C  
ANISOU  718  C   SER A 660     3782   3871   5051   -233    -62   -375       C  
ATOM    719  O   SER A 660     -16.263  11.042  31.983  1.00 34.30           O  
ANISOU  719  O   SER A 660     3887   4021   5126   -186     11   -411       O  
ATOM    720  CB  SER A 660     -15.784  11.208  35.067  1.00 33.75           C  
ANISOU  720  CB  SER A 660     3714   3845   5263   -281    -86   -235       C  
ATOM    721  OG  SER A 660     -16.472  10.035  35.458  1.00 34.05           O  
ANISOU  721  OG  SER A 660     3756   3812   5371   -273   -130   -276       O  
ATOM    722  N   ALA A 661     -18.265  10.639  32.937  1.00 32.81           N  
ANISOU  722  N   ALA A 661     3734   3763   4969   -247   -126   -433       N  
ATOM    723  CA  ALA A 661     -18.797  10.012  31.732  1.00 32.61           C  
ANISOU  723  CA  ALA A 661     3752   3765   4875   -219   -129   -553       C  
ATOM    724  C   ALA A 661     -19.225  11.057  30.713  1.00 32.67           C  
ANISOU  724  C   ALA A 661     3804   3887   4720   -207   -121   -543       C  
ATOM    725  O   ALA A 661     -19.127  10.821  29.504  1.00 33.90           O  
ANISOU  725  O   ALA A 661     3995   4110   4775   -169    -90   -624       O  
ATOM    726  CB  ALA A 661     -19.973   9.100  32.081  1.00 31.60           C  
ANISOU  726  CB  ALA A 661     3627   3571   4808   -255   -210   -614       C  
ATOM    727  N   LEU A 662     -19.691  12.216  31.184  1.00 31.44           N  
ANISOU  727  N   LEU A 662     3654   3758   4535   -234   -144   -442       N  
ATOM    728  CA  LEU A 662     -20.110  13.284  30.287  1.00 31.58           C  
ANISOU  728  CA  LEU A 662     3711   3874   4414   -214   -135   -401       C  
ATOM    729  C   LEU A 662     -18.923  14.044  29.708  1.00 32.83           C  
ANISOU  729  C   LEU A 662     3872   4080   4521   -189    -39   -339       C  
ATOM    730  O   LEU A 662     -19.036  14.621  28.620  1.00 34.28           O  
ANISOU  730  O   LEU A 662     4091   4359   4573   -156     -9   -319       O  
ATOM    731  CB  LEU A 662     -21.048  14.244  31.026  1.00 30.06           C  
ANISOU  731  CB  LEU A 662     3523   3670   4230   -240   -183   -313       C  
ATOM    732  CG  LEU A 662     -21.762  15.316  30.200  1.00 30.00           C  
ANISOU  732  CG  LEU A 662     3550   3749   4100   -210   -189   -253       C  
ATOM    733  CD1 LEU A 662     -22.475  14.685  29.018  1.00 30.87           C  
ANISOU  733  CD1 LEU A 662     3675   3954   4098   -184   -235   -339       C  
ATOM    734  CD2 LEU A 662     -22.744  16.101  31.059  1.00 28.60           C  
ANISOU  734  CD2 LEU A 662     3369   3538   3961   -221   -229   -180       C  
ATOM    735  N   VAL A 663     -17.782  14.056  30.403  1.00 32.85           N  
ANISOU  735  N   VAL A 663     3829   4029   4623   -206      9   -298       N  
ATOM    736  CA  VAL A 663     -16.622  14.763  29.871  1.00 33.36           C  
ANISOU  736  CA  VAL A 663     3877   4141   4657   -194    105   -230       C  
ATOM    737  C   VAL A 663     -15.992  13.975  28.731  1.00 35.51           C  
ANISOU  737  C   VAL A 663     4148   4479   4866   -132    178   -310       C  
ATOM    738  O   VAL A 663     -15.433  14.561  27.796  1.00 37.22           O  
ANISOU  738  O   VAL A 663     4372   4781   4988   -104    261   -265       O  
ATOM    739  CB  VAL A 663     -15.605  15.071  30.990  1.00 31.43           C  
ANISOU  739  CB  VAL A 663     3568   3833   4541   -242    121   -159       C  
ATOM    740  CG1 VAL A 663     -14.864  13.819  31.430  1.00 31.27           C  
ANISOU  740  CG1 VAL A 663     3485   3772   4626   -223    128   -214       C  
ATOM    741  CG2 VAL A 663     -14.628  16.140  30.533  1.00 31.26           C  
ANISOU  741  CG2 VAL A 663     3525   3854   4497   -257    207    -62       C  
ATOM    742  N   THR A 664     -16.082  12.643  28.771  1.00 35.90           N  
ANISOU  742  N   THR A 664     4191   4485   4964   -106    156   -429       N  
ATOM    743  CA  THR A 664     -15.620  11.848  27.641  1.00 38.37           C  
ANISOU  743  CA  THR A 664     4521   4852   5206    -39    228   -536       C  
ATOM    744  C   THR A 664     -16.563  11.980  26.452  1.00 39.55           C  
ANISOU  744  C   THR A 664     4749   5107   5170    -18    201   -602       C  
ATOM    745  O   THR A 664     -16.122  11.897  25.300  1.00 40.95           O  
ANISOU  745  O   THR A 664     4954   5386   5218     37    280   -650       O  
ATOM    746  CB  THR A 664     -15.479  10.383  28.049  1.00 39.68           C  
ANISOU  746  CB  THR A 664     4667   4913   5497    -17    213   -651       C  
ATOM    747  OG1 THR A 664     -16.773   9.843  28.350  1.00 40.38           O  
ANISOU  747  OG1 THR A 664     4795   4947   5603    -56    102   -722       O  
ATOM    748  CG2 THR A 664     -14.588  10.260  29.277  1.00 39.15           C  
ANISOU  748  CG2 THR A 664     4513   4759   5604    -33    223   -563       C  
ATOM    749  N   LYS A 665     -17.857  12.186  26.710  1.00 39.33           N  
ANISOU  749  N   LYS A 665     4751   5073   5119    -59     91   -602       N  
ATOM    750  CA  LYS A 665     -18.796  12.440  25.624  1.00 40.80           C  
ANISOU  750  CA  LYS A 665     4996   5381   5125    -43     48   -639       C  
ATOM    751  C   LYS A 665     -18.539  13.799  24.983  1.00 41.35           C  
ANISOU  751  C   LYS A 665     5081   5561   5068    -20    107   -497       C  
ATOM    752  O   LYS A 665     -18.548  13.925  23.753  1.00 41.81           O  
ANISOU  752  O   LYS A 665     5183   5756   4948     26    142   -518       O  
ATOM    753  CB  LYS A 665     -20.232  12.350  26.143  1.00 40.33           C  
ANISOU  753  CB  LYS A 665     4939   5290   5097    -91    -84   -653       C  
ATOM    754  CG  LYS A 665     -21.287  12.803  25.144  1.00 42.04           C  
ANISOU  754  CG  LYS A 665     5194   5647   5134    -78   -150   -655       C  
ATOM    755  CD  LYS A 665     -22.652  12.952  25.801  1.00 42.36           C  
ANISOU  755  CD  LYS A 665     5207   5660   5228   -123   -268   -625       C  
ATOM    756  CE  LYS A 665     -23.329  11.608  26.021  1.00 43.34           C  
ANISOU  756  CE  LYS A 665     5317   5722   5429   -170   -353   -777       C  
ATOM    757  NZ  LYS A 665     -23.812  11.017  24.742  1.00 45.61           N  
ANISOU  757  NZ  LYS A 665     5644   6127   5560   -165   -407   -918       N  
ATOM    758  N   THR A 666     -18.296  14.827  25.802  1.00 40.79           N  
ANISOU  758  N   THR A 666     4981   5431   5087    -52    123   -350       N  
ATOM    759  CA  THR A 666     -18.052  16.160  25.262  1.00 41.12           C  
ANISOU  759  CA  THR A 666     5038   5544   5041    -38    184   -201       C  
ATOM    760  C   THR A 666     -16.669  16.275  24.633  1.00 42.04           C  
ANISOU  760  C   THR A 666     5134   5716   5125    -10    320   -165       C  
ATOM    761  O   THR A 666     -16.485  17.050  23.688  1.00 42.47           O  
ANISOU  761  O   THR A 666     5213   5877   5048     21    387    -71       O  
ATOM    762  CB  THR A 666     -18.222  17.214  26.357  1.00 39.78           C  
ANISOU  762  CB  THR A 666     4852   5271   4991    -88    161    -76       C  
ATOM    763  OG1 THR A 666     -17.407  16.872  27.485  1.00 39.36           O  
ANISOU  763  OG1 THR A 666     4746   5107   5103   -133    175    -91       O  
ATOM    764  CG2 THR A 666     -19.678  17.302  26.790  1.00 38.41           C  
ANISOU  764  CG2 THR A 666     4697   5076   4822    -96     47    -86       C  
ATOM    765  N   TYR A 667     -15.688  15.523  25.139  1.00 42.52           N  
ANISOU  765  N   TYR A 667     5140   5710   5305    -15    368   -223       N  
ATOM    766  CA  TYR A 667     -14.357  15.552  24.538  1.00 43.84           C  
ANISOU  766  CA  TYR A 667     5266   5938   5452     19    507   -189       C  
ATOM    767  C   TYR A 667     -14.373  14.963  23.134  1.00 44.54           C  
ANISOU  767  C   TYR A 667     5406   6168   5350     98    566   -288       C  
ATOM    768  O   TYR A 667     -13.720  15.492  22.227  1.00 46.06           O  
ANISOU  768  O   TYR A 667     5598   6476   5429    134    680   -212       O  
ATOM    769  CB  TYR A 667     -13.360  14.803  25.422  1.00 44.80           C  
ANISOU  769  CB  TYR A 667     5304   5964   5754      8    536   -227       C  
ATOM    770  CG  TYR A 667     -11.979  14.676  24.817  1.00 47.39           C  
ANISOU  770  CG  TYR A 667     5567   6360   6077     55    684   -202       C  
ATOM    771  CD1 TYR A 667     -11.043  15.693  24.954  1.00 48.48           C  
ANISOU  771  CD1 TYR A 667     5636   6515   6268     14    762    -45       C  
ATOM    772  CD2 TYR A 667     -11.609  13.536  24.115  1.00 49.12           C  
ANISOU  772  CD2 TYR A 667     5792   6624   6249    140    752   -338       C  
ATOM    773  CE1 TYR A 667      -9.779  15.581  24.403  1.00 50.59           C  
ANISOU  773  CE1 TYR A 667     5825   6856   6541     55    905     -9       C  
ATOM    774  CE2 TYR A 667     -10.349  13.414  23.560  1.00 51.18           C  
ANISOU  774  CE2 TYR A 667     5985   6954   6507    197    903   -313       C  
ATOM    775  CZ  TYR A 667      -9.438  14.439  23.707  1.00 52.12           C  
ANISOU  775  CZ  TYR A 667     6019   7105   6679    154    980   -140       C  
ATOM    776  OH  TYR A 667      -8.181  14.319  23.158  1.00 54.29           O  
ANISOU  776  OH  TYR A 667     6207   7461   6960    209   1138   -103       O  
ATOM    777  N   ARG A 668     -15.103  13.864  22.936  1.00 43.91           N  
ANISOU  777  N   ARG A 668     5371   6082   5230    120    492   -461       N  
ATOM    778  CA  ARG A 668     -15.191  13.271  21.605  1.00 45.58           C  
ANISOU  778  CA  ARG A 668     5646   6430   5243    188    535   -587       C  
ATOM    779  C   ARG A 668     -15.923  14.195  20.639  1.00 45.78           C  
ANISOU  779  C   ARG A 668     5731   6614   5049    200    511   -503       C  
ATOM    780  O   ARG A 668     -15.562  14.280  19.459  1.00 47.78           O  
ANISOU  780  O   ARG A 668     6021   7026   5109    260    600   -509       O  
ATOM    781  CB  ARG A 668     -15.883  11.910  21.682  1.00 46.97           C  
ANISOU  781  CB  ARG A 668     5860   6541   5446    189    445   -801       C  
ATOM    782  CG  ARG A 668     -16.112  11.258  20.330  1.00 50.15           C  
ANISOU  782  CG  ARG A 668     6342   7079   5632    246    466   -969       C  
ATOM    783  CD  ARG A 668     -17.072  10.086  20.437  1.00 51.83           C  
ANISOU  783  CD  ARG A 668     6599   7216   5879    214    342  -1173       C  
ATOM    784  NE  ARG A 668     -17.511   9.621  19.125  1.00 55.19           N  
ANISOU  784  NE  ARG A 668     7112   7790   6067    248    327  -1340       N  
ATOM    785  CZ  ARG A 668     -18.448   8.698  18.936  1.00 57.05           C  
ANISOU  785  CZ  ARG A 668     7397   7997   6283    208    208  -1532       C  
ATOM    786  NH1 ARG A 668     -19.050   8.139  19.977  1.00 56.09           N  
ANISOU  786  NH1 ARG A 668     7241   7698   6374    138    105  -1564       N  
ATOM    787  NH2 ARG A 668     -18.787   8.335  17.705  1.00 59.44           N  
ANISOU  787  NH2 ARG A 668     7783   8453   6349    233    191  -1692       N  
ATOM    788  N   ALA A 669     -16.947  14.901  21.124  1.00 44.08           N  
ANISOU  788  N   ALA A 669     5523   6366   4858    153    396   -413       N  
ATOM    789  CA  ALA A 669     -17.679  15.836  20.276  1.00 44.62           C  
ANISOU  789  CA  ALA A 669     5637   6578   4737    174    367   -303       C  
ATOM    790  C   ALA A 669     -16.803  17.000  19.825  1.00 46.70           C  
ANISOU  790  C   ALA A 669     5887   6905   4951    195    500   -104       C  
ATOM    791  O   ALA A 669     -17.027  17.558  18.745  1.00 49.00           O  
ANISOU  791  O   ALA A 669     6221   7359   5036    241    528    -21       O  
ATOM    792  CB  ALA A 669     -18.912  16.355  21.013  1.00 41.92           C  
ANISOU  792  CB  ALA A 669     5290   6166   4470    130    229   -238       C  
ATOM    793  N   ALA A 670     -15.807  17.377  20.629  1.00 46.50           N  
ANISOU  793  N   ALA A 670     5799   6760   5109    158    581    -17       N  
ATOM    794  CA  ALA A 670     -14.927  18.478  20.254  1.00 48.07           C  
ANISOU  794  CA  ALA A 670     5972   7001   5292    158    711    176       C  
ATOM    795  C   ALA A 670     -13.862  18.031  19.262  1.00 48.44           C  
ANISOU  795  C   ALA A 670     6005   7182   5217    219    862    144       C  
ATOM    796  O   ALA A 670     -13.556  18.756  18.309  1.00 49.40           O  
ANISOU  796  O   ALA A 670     6142   7438   5189    252    961    280       O  
ATOM    797  CB  ALA A 670     -14.275  19.081  21.498  1.00 47.20           C  
ANISOU  797  CB  ALA A 670     5791   6717   5425     79    727    272       C  
ATOM    798  N   ARG A 671     -13.283  16.847  19.472  1.00 48.53           N  
ANISOU  798  N   ARG A 671     5986   7160   5295    240    892    -24       N  
ATOM    799  CA  ARG A 671     -12.308  16.325  18.521  1.00 50.87           C  
ANISOU  799  CA  ARG A 671     6270   7584   5475    315   1048    -78       C  
ATOM    800  C   ARG A 671     -12.951  16.055  17.167  1.00 51.78           C  
ANISOU  800  C   ARG A 671     6485   7896   5293    387   1046   -162       C  
ATOM    801  O   ARG A 671     -12.318  16.248  16.123  1.00 54.74           O  
ANISOU  801  O   ARG A 671     6869   8437   5494    449   1188   -113       O  
ATOM    802  CB  ARG A 671     -11.659  15.057  19.074  1.00 52.33           C  
ANISOU  802  CB  ARG A 671     6403   7669   5809    338   1072   -249       C  
ATOM    803  CG  ARG A 671     -10.609  15.312  20.144  1.00 52.31           C  
ANISOU  803  CG  ARG A 671     6278   7539   6057    287   1121   -145       C  
ATOM    804  CD  ARG A 671      -9.365  15.956  19.553  1.00 55.42           C  
ANISOU  804  CD  ARG A 671     6596   8038   6425    309   1304      4       C  
ATOM    805  NE  ARG A 671      -8.715  15.085  18.576  1.00 60.24           N  
ANISOU  805  NE  ARG A 671     7206   8771   6909    418   1445   -113       N  
ATOM    806  CZ  ARG A 671      -7.758  14.212  18.875  1.00 63.46           C  
ANISOU  806  CZ  ARG A 671     7527   9133   7451    468   1529   -193       C  
ATOM    807  NH1 ARG A 671      -7.333  14.093  20.125  1.00 62.72           N  
ANISOU  807  NH1 ARG A 671     7334   8885   7611    411   1473   -158       N  
ATOM    808  NH2 ARG A 671      -7.225  13.458  17.923  1.00 66.03           N  
ANISOU  808  NH2 ARG A 671     7866   9572   7652    581   1671   -309       N  
ATOM    809  N   ILE A 672     -14.208  15.606  17.164  1.00 49.62           N  
ANISOU  809  N   ILE A 672     6281   7620   4952    376    886   -287       N  
ATOM    810  CA  ILE A 672     -14.933  15.436  15.908  1.00 49.86           C  
ANISOU  810  CA  ILE A 672     6403   7852   4688    428    852   -363       C  
ATOM    811  C   ILE A 672     -15.141  16.785  15.231  1.00 51.08           C  
ANISOU  811  C   ILE A 672     6576   8149   4684    441    881   -120       C  
ATOM    812  O   ILE A 672     -14.987  16.917  14.010  1.00 54.55           O  
ANISOU  812  O   ILE A 672     7064   8801   4863    507    960    -96       O  
ATOM    813  CB  ILE A 672     -16.269  14.711  16.159  1.00 48.66           C  
ANISOU  813  CB  ILE A 672     6300   7657   4531    393    656   -535       C  
ATOM    814  CG1 ILE A 672     -16.021  13.242  16.508  1.00 48.46           C  
ANISOU  814  CG1 ILE A 672     6278   7516   4618    396    650   -790       C  
ATOM    815  CG2 ILE A 672     -17.186  14.834  14.952  1.00 49.66           C  
ANISOU  815  CG2 ILE A 672     6507   8007   4354    427    581   -564       C  
ATOM    816  CD1 ILE A 672     -17.261  12.502  16.958  1.00 48.10           C  
ANISOU  816  CD1 ILE A 672     6259   7385   4631    338    462   -945       C  
ATOM    817  N   LEU A 673     -15.488  17.810  16.014  1.00 48.94           N  
ANISOU  817  N   LEU A 673     6269   7760   4566    384    825     65       N  
ATOM    818  CA  LEU A 673     -15.669  19.145  15.453  1.00 50.82           C  
ANISOU  818  CA  LEU A 673     6521   8094   4694    399    859    317       C  
ATOM    819  C   LEU A 673     -14.347  19.723  14.962  1.00 54.90           C  
ANISOU  819  C   LEU A 673     6999   8673   5189    419   1064    474       C  
ATOM    820  O   LEU A 673     -14.304  20.386  13.919  1.00 58.01           O  
ANISOU  820  O   LEU A 673     7425   9242   5374    468   1140    628       O  
ATOM    821  CB  LEU A 673     -16.305  20.067  16.493  1.00 48.18           C  
ANISOU  821  CB  LEU A 673     6162   7584   4561    337    763    458       C  
ATOM    822  CG  LEU A 673     -16.502  21.526  16.077  1.00 49.65           C  
ANISOU  822  CG  LEU A 673     6361   7811   4693    351    801    735       C  
ATOM    823  CD1 LEU A 673     -17.388  21.614  14.844  1.00 52.24           C  
ANISOU  823  CD1 LEU A 673     6754   8372   4723    427    742    771       C  
ATOM    824  CD2 LEU A 673     -17.085  22.340  17.223  1.00 37.83           C  
ANISOU  824  CD2 LEU A 673     4844   6106   3423    294    716    833       C  
ATOM    825  N   ALA A 674     -13.260  19.483  15.699  1.00 56.07           N  
ANISOU  825  N   ALA A 674     7067   8688   5550    381   1156    452       N  
ATOM    826  CA  ALA A 674     -11.956  19.983  15.275  1.00 59.31           C  
ANISOU  826  CA  ALA A 674     7414   9157   5963    391   1354    602       C  
ATOM    827  C   ALA A 674     -11.486  19.310  13.992  1.00 61.39           C  
ANISOU  827  C   ALA A 674     7711   9650   5965    490   1482    512       C  
ATOM    828  O   ALA A 674     -10.812  19.945  13.172  1.00 62.80           O  
ANISOU  828  O   ALA A 674     7872   9969   6021    522   1640    683       O  
ATOM    829  CB  ALA A 674     -10.928  19.784  16.389  1.00 58.27           C  
ANISOU  829  CB  ALA A 674     7173   8847   6121    327   1403    585       C  
ATOM    830  N   MET A 675     -11.830  18.036  13.799  1.00 62.16           N  
ANISOU  830  N   MET A 675     7859   9785   5974    537   1424    246       N  
ATOM    831  CA  MET A 675     -11.488  17.339  12.567  1.00 67.40           C  
ANISOU  831  CA  MET A 675     8576  10665   6368    637   1537    120       C  
ATOM    832  C   MET A 675     -12.341  17.784  11.388  1.00 67.49           C  
ANISOU  832  C   MET A 675     8688  10909   6047    682   1494    181       C  
ATOM    833  O   MET A 675     -11.913  17.634  10.239  1.00 69.25           O  
ANISOU  833  O   MET A 675     8950  11355   6007    764   1626    168       O  
ATOM    834  CB  MET A 675     -11.621  15.829  12.767  1.00 71.93           C  
ANISOU  834  CB  MET A 675     9181  11176   6973    667   1482   -201       C  
ATOM    835  CG  MET A 675     -10.533  15.232  13.641  1.00 76.48           C  
ANISOU  835  CG  MET A 675     9653  11581   7824    662   1572   -260       C  
ATOM    836  SD  MET A 675     -11.027  13.671  14.394  1.00 81.51           S  
ANISOU  836  SD  MET A 675    10320  12034   8615    659   1438   -576       S  
ATOM    837  CE  MET A 675     -11.721  12.818  12.981  1.00 85.14           C  
ANISOU  837  CE  MET A 675    10929  12698   8721    739   1420   -826       C  
ATOM    838  N   SER A 676     -13.535  18.322  11.643  1.00 65.05           N  
ANISOU  838  N   SER A 676     8417  10566   5735    639   1315    252       N  
ATOM    839  CA  SER A 676     -14.348  18.867  10.564  1.00 67.09           C  
ANISOU  839  CA  SER A 676     8752  11052   5687    685   1263    354       C  
ATOM    840  C   SER A 676     -13.770  20.165  10.018  1.00 68.42           C  
ANISOU  840  C   SER A 676     8894  11317   5785    705   1413    681       C  
ATOM    841  O   SER A 676     -14.041  20.517   8.865  1.00 70.94           O  
ANISOU  841  O   SER A 676     9273  11882   5799    770   1442    781       O  
ATOM    842  CB  SER A 676     -15.781  19.094  11.050  1.00 66.83           C  
ANISOU  842  CB  SER A 676     8743  10948   5700    640   1032    356       C  
ATOM    843  OG  SER A 676     -16.579  19.673  10.033  1.00 70.14           O  
ANISOU  843  OG  SER A 676     9221  11594   5833    690    971    482       O  
ATOM    844  N   LYS A 677     -12.978  20.877  10.818  1.00 67.00           N  
ANISOU  844  N   LYS A 677     8625  10952   5880    644   1505    853       N  
ATOM    845  CA  LYS A 677     -12.360  22.127  10.403  1.00 68.48           C  
ANISOU  845  CA  LYS A 677     8777  11189   6055    642   1655   1172       C  
ATOM    846  C   LYS A 677     -10.948  21.947   9.863  1.00 70.58           C  
ANISOU  846  C   LYS A 677     8983  11559   6273    675   1894   1206       C  
ATOM    847  O   LYS A 677     -10.408  22.886   9.269  1.00 71.40           O  
ANISOU  847  O   LYS A 677     9061  11756   6310    683   2042   1471       O  
ATOM    848  CB  LYS A 677     -12.324  23.114  11.574  1.00 64.82           C  
ANISOU  848  CB  LYS A 677     8248  10454   5925    542   1617   1346       C  
ATOM    849  CG  LYS A 677     -13.687  23.471  12.142  1.00 61.91           C  
ANISOU  849  CG  LYS A 677     7927   9974   5621    518   1408   1352       C  
ATOM    850  CD  LYS A 677     -13.564  24.539  13.217  1.00 57.91           C  
ANISOU  850  CD  LYS A 677     7369   9208   5426    428   1400   1527       C  
ATOM    851  CE  LYS A 677     -14.926  24.953  13.748  1.00 55.64           C  
ANISOU  851  CE  LYS A 677     7126   8816   5200    423   1214   1545       C  
ATOM    852  NZ  LYS A 677     -14.814  26.078  14.718  1.00 54.27           N  
ANISOU  852  NZ  LYS A 677     6920   8390   5310    345   1222   1713       N  
ATOM    853  N   LYS A 678     -10.344  20.778  10.056  1.00 72.09           N  
ANISOU  853  N   LYS A 678     9147  11735   6510    699   1943    958       N  
ATOM    854  CA  LYS A 678      -8.962  20.530   9.652  1.00 75.11           C  
ANISOU  854  CA  LYS A 678     9451  12203   6884    739   2178    977       C  
ATOM    855  C   LYS A 678      -8.765  20.708   8.150  1.00 78.90           C  
ANISOU  855  C   LYS A 678     9988  12996   6992    839   2330   1068       C  
ATOM    856  O   LYS A 678      -7.684  21.080   7.695  1.00 82.03           O  
ANISOU  856  O   LYS A 678    10310  13488   7369    861   2549   1228       O  
ATOM    857  CB  LYS A 678      -8.535  19.119  10.069  1.00 75.60           C  
ANISOU  857  CB  LYS A 678     9489  12194   7040    773   2184    668       C  
ATOM    858  CG  LYS A 678      -7.057  18.817   9.860  1.00 79.59           C  
ANISOU  858  CG  LYS A 678     9885  12753   7604    819   2425    684       C  
ATOM    859  CD  LYS A 678      -6.184  19.591  10.838  1.00 80.38           C  
ANISOU  859  CD  LYS A 678     9830  12669   8042    715   2479    891       C  
ATOM    860  CE  LYS A 678      -4.711  19.252  10.660  1.00 82.88           C  
ANISOU  860  CE  LYS A 678    10009  13047   8432    761   2712    911       C  
ATOM    861  NZ  LYS A 678      -3.853  19.950  11.659  1.00 81.38           N  
ANISOU  861  NZ  LYS A 678     9655  12683   8582    643   2743   1097       N  
ATOM    862  N   ASN A1002     -11.484  19.479   7.500  1.00 46.35           N  
ANISOU  862  N   ASN A1002     5237   7582   4793    238   1077   1050       N  
ATOM    863  CA  ASN A1002     -11.169  19.240   6.098  1.00 44.16           C  
ANISOU  863  CA  ASN A1002     5027   7031   4720    145   1035   1024       C  
ATOM    864  C   ASN A1002     -11.380  20.501   5.266  1.00 40.91           C  
ANISOU  864  C   ASN A1002     4609   6564   4371    169    934    810       C  
ATOM    865  O   ASN A1002     -10.983  20.562   4.103  1.00 38.65           O  
ANISOU  865  O   ASN A1002     4380   6084   4221    112    881    767       O  
ATOM    866  CB  ASN A1002     -12.021  18.097   5.544  1.00 46.18           C  
ANISOU  866  CB  ASN A1002     5264   7188   5094     -1   1136   1154       C  
ATOM    867  CG  ASN A1002     -11.794  16.791   6.280  1.00 48.37           C  
ANISOU  867  CG  ASN A1002     5567   7463   5346    -40   1229   1394       C  
ATOM    868  OD1 ASN A1002     -10.655  16.394   6.526  1.00 49.47           O  
ANISOU  868  OD1 ASN A1002     5787   7532   5479     13   1197   1472       O  
ATOM    869  ND2 ASN A1002     -12.881  16.119   6.644  1.00 49.40           N  
ANISOU  869  ND2 ASN A1002     5626   7676   5468   -135   1343   1521       N  
ATOM    870  N   ILE A1003     -12.013  21.508   5.871  1.00 40.49           N  
ANISOU  870  N   ILE A1003     4485   6686   4212    262    906    678       N  
ATOM    871  CA  ILE A1003     -12.264  22.753   5.154  1.00 39.41           C  
ANISOU  871  CA  ILE A1003     4349   6480   4144    302    799    485       C  
ATOM    872  C   ILE A1003     -10.989  23.581   5.030  1.00 38.06           C  
ANISOU  872  C   ILE A1003     4260   6204   3996    355    674    391       C  
ATOM    873  O   ILE A1003     -10.802  24.288   4.033  1.00 38.01           O  
ANISOU  873  O   ILE A1003     4300   6038   4105    331    586    305       O  
ATOM    874  CB  ILE A1003     -13.393  23.546   5.838  1.00 41.40           C  
ANISOU  874  CB  ILE A1003     4494   6943   4292    403    803    356       C  
ATOM    875  CG1 ILE A1003     -13.689  24.839   5.074  1.00 41.42           C  
ANISOU  875  CG1 ILE A1003     4508   6843   4387    460    676    165       C  
ATOM    876  CG2 ILE A1003     -13.041  23.856   7.281  1.00 42.66           C  
ANISOU  876  CG2 ILE A1003     4622   7326   4262    528    804    319       C  
ATOM    877  CD1 ILE A1003     -14.776  25.680   5.700  1.00 43.62           C  
ANISOU  877  CD1 ILE A1003     4678   7315   4578    589    663      8       C  
ATOM    878  N   PHE A1004     -10.089  23.503   6.015  1.00 37.36           N  
ANISOU  878  N   PHE A1004     4186   6210   3798    421    662    415       N  
ATOM    879  CA  PHE A1004      -8.841  24.256   5.931  1.00 35.41           C  
ANISOU  879  CA  PHE A1004     3996   5876   3580    453    543    321       C  
ATOM    880  C   PHE A1004      -7.964  23.742   4.798  1.00 33.22           C  
ANISOU  880  C   PHE A1004     3789   5390   3442    348    533    404       C  
ATOM    881  O   PHE A1004      -7.340  24.534   4.082  1.00 31.51           O  
ANISOU  881  O   PHE A1004     3613   5044   3316    322    440    319       O  
ATOM    882  CB  PHE A1004      -8.094  24.194   7.264  1.00 36.01           C  
ANISOU  882  CB  PHE A1004     4055   6133   3495    550    530    325       C  
ATOM    883  CG  PHE A1004      -6.694  24.741   7.201  1.00 35.92           C  
ANISOU  883  CG  PHE A1004     4087   6042   3520    562    415    249       C  
ATOM    884  CD1 PHE A1004      -6.471  26.108   7.171  1.00 29.58           C  
ANISOU  884  CD1 PHE A1004     3288   5195   2758    600    287     48       C  
ATOM    885  CD2 PHE A1004      -5.601  23.889   7.175  1.00 29.14           C  
ANISOU  885  CD2 PHE A1004     3256   5149   2667    534    431    377       C  
ATOM    886  CE1 PHE A1004      -5.184  26.614   7.112  1.00 29.49           C  
ANISOU  886  CE1 PHE A1004     3301   5112   2793    584    183    -19       C  
ATOM    887  CE2 PHE A1004      -4.312  24.390   7.117  1.00 28.99           C  
ANISOU  887  CE2 PHE A1004     3251   5085   2681    537    329    302       C  
ATOM    888  CZ  PHE A1004      -4.104  25.755   7.086  1.00 29.17           C  
ANISOU  888  CZ  PHE A1004     3270   5071   2745    550    208    106       C  
ATOM    889  N   GLU A1005      -7.904  22.421   4.618  1.00 33.75           N  
ANISOU  889  N   GLU A1005     3870   5424   3531    287    629    570       N  
ATOM    890  CA  GLU A1005      -7.149  21.867   3.501  1.00 33.53           C  
ANISOU  890  CA  GLU A1005     3896   5213   3630    202    626    625       C  
ATOM    891  C   GLU A1005      -7.828  22.161   2.171  1.00 32.98           C  
ANISOU  891  C   GLU A1005     3837   5015   3678    119    615    572       C  
ATOM    892  O   GLU A1005      -7.162  22.190   1.130  1.00 31.67           O  
ANISOU  892  O   GLU A1005     3711   4722   3600     61    581    562       O  
ATOM    893  CB  GLU A1005      -6.969  20.359   3.679  1.00 34.63           C  
ANISOU  893  CB  GLU A1005     4051   5328   3778    174    721    798       C  
ATOM    894  CG  GLU A1005      -6.385  19.953   5.023  1.00 36.52           C  
ANISOU  894  CG  GLU A1005     4282   5710   3884    267    736    888       C  
ATOM    895  CD  GLU A1005      -5.043  20.603   5.304  1.00 37.04           C  
ANISOU  895  CD  GLU A1005     4355   5808   3910    336    634    808       C  
ATOM    896  OE1 GLU A1005      -4.255  20.790   4.353  1.00 36.33           O  
ANISOU  896  OE1 GLU A1005     4289   5588   3925    290    585    757       O  
ATOM    897  OE2 GLU A1005      -4.776  20.931   6.478  1.00 38.91           O  
ANISOU  897  OE2 GLU A1005     4562   6219   4003    432    604    790       O  
ATOM    898  N   MET A1006      -9.145  22.378   2.185  1.00 34.13           N  
ANISOU  898  N   MET A1006     3936   5217   3814    118    642    538       N  
ATOM    899  CA  MET A1006      -9.861  22.696   0.954  1.00 33.55           C  
ANISOU  899  CA  MET A1006     3864   5048   3838     56    618    486       C  
ATOM    900  C   MET A1006      -9.423  24.047   0.402  1.00 33.99           C  
ANISOU  900  C   MET A1006     3957   5027   3930     80    496    375       C  
ATOM    901  O   MET A1006      -9.098  24.171  -0.785  1.00 33.42           O  
ANISOU  901  O   MET A1006     3926   4836   3937     13    461    378       O  
ATOM    902  CB  MET A1006     -11.369  22.681   1.212  1.00 33.74           C  
ANISOU  902  CB  MET A1006     3806   5179   3834     65    666    464       C  
ATOM    903  CG  MET A1006     -12.224  22.862  -0.034  1.00 32.82           C  
ANISOU  903  CG  MET A1006     3674   4990   3808      7    641    417       C  
ATOM    904  SD  MET A1006     -13.972  23.075   0.361  1.00 34.02           S  
ANISOU  904  SD  MET A1006     3699   5307   3919     43    679    358       S  
ATOM    905  CE  MET A1006     -14.729  22.829  -1.243  1.00 33.25           C  
ANISOU  905  CE  MET A1006     3585   5113   3937    -54    656    338       C  
ATOM    906  N   LEU A1007      -9.400  25.072   1.253  1.00 35.48           N  
ANISOU  906  N   LEU A1007     4134   5285   4062    175    428    276       N  
ATOM    907  CA  LEU A1007      -9.034  26.408   0.803  1.00 37.65           C  
ANISOU  907  CA  LEU A1007     4451   5458   4397    192    302    174       C  
ATOM    908  C   LEU A1007      -7.528  26.618   0.727  1.00 39.64           C  
ANISOU  908  C   LEU A1007     4750   5637   4674    152    251    187       C  
ATOM    909  O   LEU A1007      -7.080  27.527   0.020  1.00 39.81           O  
ANISOU  909  O   LEU A1007     4815   5537   4776    112    162    151       O  
ATOM    910  CB  LEU A1007      -9.659  27.461   1.717  1.00 38.48           C  
ANISOU  910  CB  LEU A1007     4523   5645   4454    316    234     31       C  
ATOM    911  CG  LEU A1007     -11.149  27.706   1.479  1.00 39.30           C  
ANISOU  911  CG  LEU A1007     4573   5794   4565    365    243    -21       C  
ATOM    912  CD1 LEU A1007     -12.017  26.791   2.334  1.00 39.21           C  
ANISOU  912  CD1 LEU A1007     4468   5986   4445    393    367     19       C  
ATOM    913  CD2 LEU A1007     -11.475  29.163   1.727  1.00 41.25           C  
ANISOU  913  CD2 LEU A1007     4828   6003   4842    480    113   -187       C  
ATOM    914  N   ARG A1008      -6.738  25.809   1.438  1.00 41.88           N  
ANISOU  914  N   ARG A1008     5020   5999   4894    162    303    246       N  
ATOM    915  CA  ARG A1008      -5.290  25.872   1.271  1.00 43.37           C  
ANISOU  915  CA  ARG A1008     5230   6139   5109    120    262    261       C  
ATOM    916  C   ARG A1008      -4.890  25.502  -0.152  1.00 41.70           C  
ANISOU  916  C   ARG A1008     5047   5810   4985     12    285    333       C  
ATOM    917  O   ARG A1008      -3.920  26.048  -0.690  1.00 40.35           O  
ANISOU  917  O   ARG A1008     4889   5577   4864    -47    229    321       O  
ATOM    918  CB  ARG A1008      -4.608  24.946   2.278  1.00 46.00           C  
ANISOU  918  CB  ARG A1008     5535   6592   5350    172    313    323       C  
ATOM    919  CG  ARG A1008      -3.090  24.984   2.233  1.00 48.09           C  
ANISOU  919  CG  ARG A1008     5796   6845   5633    148    267    324       C  
ATOM    920  CD  ARG A1008      -2.482  23.871   3.072  1.00 51.07           C  
ANISOU  920  CD  ARG A1008     6149   7332   5925    213    320    413       C  
ATOM    921  NE  ARG A1008      -1.972  22.779   2.247  1.00 53.55           N  
ANISOU  921  NE  ARG A1008     6476   7570   6301    166    385    518       N  
ATOM    922  CZ  ARG A1008      -2.715  21.784   1.774  1.00 56.23           C  
ANISOU  922  CZ  ARG A1008     6840   7850   6676    140    475    607       C  
ATOM    923  NH1 ARG A1008      -4.013  21.736   2.038  1.00 57.44           N  
ANISOU  923  NH1 ARG A1008     6996   8024   6806    142    518    620       N  
ATOM    924  NH2 ARG A1008      -2.159  20.834   1.034  1.00 58.09           N  
ANISOU  924  NH2 ARG A1008     7086   8008   6976    111    518    668       N  
ATOM    925  N   ILE A1009      -5.639  24.594  -0.774  1.00 41.96           N  
ANISOU  925  N   ILE A1009     5082   5827   5036    -21    367    399       N  
ATOM    926  CA  ILE A1009      -5.409  24.193  -2.157  1.00 40.41           C  
ANISOU  926  CA  ILE A1009     4905   5546   4903   -110    390    443       C  
ATOM    927  C   ILE A1009      -6.090  25.148  -3.132  1.00 39.10           C  
ANISOU  927  C   ILE A1009     4763   5313   4782   -148    329    408       C  
ATOM    928  O   ILE A1009      -5.539  25.463  -4.190  1.00 39.68           O  
ANISOU  928  O   ILE A1009     4859   5330   4889   -219    302    430       O  
ATOM    929  CB  ILE A1009      -5.891  22.741  -2.356  1.00 39.89           C  
ANISOU  929  CB  ILE A1009     4829   5484   4845   -126    492    509       C  
ATOM    930  CG1 ILE A1009      -5.123  21.793  -1.427  1.00 40.07           C  
ANISOU  930  CG1 ILE A1009     4844   5550   4833    -78    541    571       C  
ATOM    931  CG2 ILE A1009      -5.754  22.311  -3.811  1.00 38.95           C  
ANISOU  931  CG2 ILE A1009     4724   5296   4779   -205    511    519       C  
ATOM    932  CD1 ILE A1009      -5.600  20.355  -1.491  1.00 40.94           C  
ANISOU  932  CD1 ILE A1009     4955   5625   4974    -95    633    649       C  
ATOM    933  N   ASP A1010      -7.291  25.629  -2.799  1.00 37.39           N  
ANISOU  933  N   ASP A1010     4534   5116   4557    -95    305    359       N  
ATOM    934  CA  ASP A1010      -8.025  26.493  -3.721  1.00 36.57           C  
ANISOU  934  CA  ASP A1010     4452   4948   4496   -108    237    334       C  
ATOM    935  C   ASP A1010      -7.557  27.941  -3.637  1.00 37.30           C  
ANISOU  935  C   ASP A1010     4586   4956   4629    -92    118    287       C  
ATOM    936  O   ASP A1010      -7.218  28.549  -4.657  1.00 37.25           O  
ANISOU  936  O   ASP A1010     4623   4861   4671   -158     63    329       O  
ATOM    937  CB  ASP A1010      -9.530  26.413  -3.443  1.00 35.88           C  
ANISOU  937  CB  ASP A1010     4318   4924   4393    -46    254    291       C  
ATOM    938  CG  ASP A1010     -10.173  25.176  -4.041  1.00 36.42           C  
ANISOU  938  CG  ASP A1010     4349   5028   4462   -104    345    338       C  
ATOM    939  OD1 ASP A1010      -9.492  24.454  -4.802  1.00 36.17           O  
ANISOU  939  OD1 ASP A1010     4340   4956   4447   -180    383    390       O  
ATOM    940  OD2 ASP A1010     -11.361  24.926  -3.749  1.00 37.08           O  
ANISOU  940  OD2 ASP A1010     4372   5185   4532    -75    377    311       O  
ATOM    941  N   GLU A1011      -7.537  28.510  -2.432  1.00 38.57           N  
ANISOU  941  N   GLU A1011     4735   5146   4773     -8     74    201       N  
ATOM    942  CA  GLU A1011      -7.313  29.942  -2.268  1.00 38.85           C  
ANISOU  942  CA  GLU A1011     4812   5078   4873     19    -56    124       C  
ATOM    943  C   GLU A1011      -5.842  30.304  -2.116  1.00 36.96           C  
ANISOU  943  C   GLU A1011     4591   4788   4665    -54    -98    131       C  
ATOM    944  O   GLU A1011      -5.413  31.354  -2.611  1.00 37.23           O  
ANISOU  944  O   GLU A1011     4674   4685   4789   -111   -195    131       O  
ATOM    945  CB  GLU A1011      -8.092  30.454  -1.054  1.00 40.77           C  
ANISOU  945  CB  GLU A1011     5023   5387   5081    160    -96    -15       C  
ATOM    946  CG  GLU A1011      -8.449  31.931  -1.102  1.00 42.90           C  
ANISOU  946  CG  GLU A1011     5337   5520   5441    223   -241   -118       C  
ATOM    947  CD  GLU A1011      -9.712  32.202  -1.895  1.00 43.41           C  
ANISOU  947  CD  GLU A1011     5407   5546   5542    271   -266   -107       C  
ATOM    948  OE1 GLU A1011      -9.636  32.287  -3.139  1.00 43.28           O  
ANISOU  948  OE1 GLU A1011     5438   5429   5578    184   -284      4       O  
ATOM    949  OE2 GLU A1011     -10.787  32.320  -1.272  1.00 43.87           O  
ANISOU  949  OE2 GLU A1011     5410   5698   5562    400   -268   -211       O  
ATOM    950  N   GLY A1012      -5.063  29.470  -1.447  1.00 35.07           N  
ANISOU  950  N   GLY A1012     4311   4655   4360    -56    -32    143       N  
ATOM    951  CA  GLY A1012      -3.664  29.745  -1.200  1.00 34.72           C  
ANISOU  951  CA  GLY A1012     4256   4600   4337   -116    -73    135       C  
ATOM    952  C   GLY A1012      -3.386  29.995   0.273  1.00 34.71           C  
ANISOU  952  C   GLY A1012     4220   4689   4280    -22   -118     15       C  
ATOM    953  O   GLY A1012      -4.286  30.086   1.108  1.00 35.16           O  
ANISOU  953  O   GLY A1012     4264   4817   4277     93   -122    -67       O  
ATOM    954  N   LEU A1013      -2.094  30.122   0.577  1.00 34.59           N  
ANISOU  954  N   LEU A1013     4175   4694   4273    -71   -155     -3       N  
ATOM    955  CA  LEU A1013      -1.644  30.222   1.960  1.00 34.38           C  
ANISOU  955  CA  LEU A1013     4102   4789   4171     16   -200   -116       C  
ATOM    956  C   LEU A1013      -0.239  30.807   1.993  1.00 34.22           C  
ANISOU  956  C   LEU A1013     4049   4738   4214    -75   -284   -159       C  
ATOM    957  O   LEU A1013       0.634  30.355   1.249  1.00 34.21           O  
ANISOU  957  O   LEU A1013     4022   4734   4241   -176   -239    -57       O  
ATOM    958  CB  LEU A1013      -1.668  28.843   2.624  1.00 33.33           C  
ANISOU  958  CB  LEU A1013     3927   4836   3901     96    -89    -42       C  
ATOM    959  CG  LEU A1013      -1.006  28.669   3.985  1.00 33.14           C  
ANISOU  959  CG  LEU A1013     3846   4983   3762    188   -120   -111       C  
ATOM    960  CD1 LEU A1013      -1.705  29.523   5.014  1.00 35.36           C  
ANISOU  960  CD1 LEU A1013     4123   5327   3986    297   -196   -277       C  
ATOM    961  CD2 LEU A1013      -1.048  27.207   4.380  1.00 31.81           C  
ANISOU  961  CD2 LEU A1013     3656   4951   3480    250     -3     23       C  
ATOM    962  N   ARG A1014      -0.024  31.805   2.851  1.00 34.21           N  
ANISOU  962  N   ARG A1014     4037   4725   4236    -41   -407   -324       N  
ATOM    963  CA  ARG A1014       1.292  32.402   3.057  1.00 35.57           C  
ANISOU  963  CA  ARG A1014     4161   4882   4473   -132   -501   -395       C  
ATOM    964  C   ARG A1014       1.659  32.312   4.531  1.00 37.16           C  
ANISOU  964  C   ARG A1014     4296   5272   4552    -11   -554   -541       C  
ATOM    965  O   ARG A1014       0.863  32.691   5.397  1.00 38.77           O  
ANISOU  965  O   ARG A1014     4514   5523   4693    118   -598   -676       O  
ATOM    966  CB  ARG A1014       1.330  33.863   2.600  1.00 35.74           C  
ANISOU  966  CB  ARG A1014     4233   4671   4674   -236   -632   -472       C  
ATOM    967  CG  ARG A1014       1.349  34.062   1.094  1.00 31.47           C  
ANISOU  967  CG  ARG A1014     3745   3963   4250   -389   -597   -303       C  
ATOM    968  CD  ARG A1014       2.636  34.731   0.634  1.00 32.64           C  
ANISOU  968  CD  ARG A1014     3854   4026   4523   -580   -662   -280       C  
ATOM    969  NE  ARG A1014       3.663  33.757   0.280  1.00 36.91           N  
ANISOU  969  NE  ARG A1014     4301   4731   4993   -649   -560   -172       N  
ATOM    970  CZ  ARG A1014       4.915  34.073  -0.036  1.00 37.79           C  
ANISOU  970  CZ  ARG A1014     4333   4850   5175   -809   -587   -149       C  
ATOM    971  NH1 ARG A1014       5.781  33.119  -0.350  1.00 32.41           N  
ANISOU  971  NH1 ARG A1014     3555   4341   4418   -838   -490    -65       N  
ATOM    972  NH2 ARG A1014       5.304  35.341  -0.035  1.00 34.74           N  
ANISOU  972  NH2 ARG A1014     3958   4297   4946   -939   -714   -213       N  
ATOM    973  N   LEU A1015       2.863  31.823   4.812  1.00 38.38           N  
ANISOU  973  N   LEU A1015     4366   5555   4661    -42   -552   -522       N  
ATOM    974  CA  LEU A1015       3.319  31.632   6.182  1.00 40.56           C  
ANISOU  974  CA  LEU A1015     4569   6045   4797     79   -604   -642       C  
ATOM    975  C   LEU A1015       4.020  32.857   6.754  1.00 45.96           C  
ANISOU  975  C   LEU A1015     5209   6694   5559     32   -774   -858       C  
ATOM    976  O   LEU A1015       4.564  32.780   7.859  1.00 47.79           O  
ANISOU  976  O   LEU A1015     5364   7121   5673    120   -839   -979       O  
ATOM    977  CB  LEU A1015       4.242  30.413   6.265  1.00 32.73           C  
ANISOU  977  CB  LEU A1015     3502   5225   3709    100   -528   -514       C  
ATOM    978  CG  LEU A1015       3.560  29.068   6.010  1.00 31.28           C  
ANISOU  978  CG  LEU A1015     3359   5092   3434    177   -374   -326       C  
ATOM    979  CD1 LEU A1015       4.518  27.915   6.253  1.00 31.33           C  
ANISOU  979  CD1 LEU A1015     3295   5254   3354    229   -326   -222       C  
ATOM    980  CD2 LEU A1015       2.313  28.922   6.871  1.00 33.98           C  
ANISOU  980  CD2 LEU A1015     3744   5519   3649    319   -343   -354       C  
ATOM    981  N   LYS A1016       4.019  33.977   6.035  1.00 47.96           N  
ANISOU  981  N   LYS A1016     5510   6704   6010   -107   -855   -907       N  
ATOM    982  CA  LYS A1016       4.576  35.220   6.546  1.00 49.94           C  
ANISOU  982  CA  LYS A1016     5733   6869   6374   -167  -1030  -1125       C  
ATOM    983  C   LYS A1016       3.659  36.374   6.167  1.00 47.37           C  
ANISOU  983  C   LYS A1016     5518   6270   6210   -187  -1111  -1206       C  
ATOM    984  O   LYS A1016       2.817  36.259   5.272  1.00 46.07           O  
ANISOU  984  O   LYS A1016     5439   5975   6090   -198  -1032  -1061       O  
ATOM    985  CB  LYS A1016       5.999  35.467   6.027  1.00 51.51           C  
ANISOU  985  CB  LYS A1016     5846   7030   6697   -370  -1073  -1090       C  
ATOM    986  CG  LYS A1016       6.105  35.603   4.519  1.00 53.25           C  
ANISOU  986  CG  LYS A1016     6112   7051   7070   -559  -1005   -887       C  
ATOM    987  CD  LYS A1016       7.545  35.841   4.095  1.00 57.54           C  
ANISOU  987  CD  LYS A1016     6541   7606   7716   -763  -1038   -857       C  
ATOM    988  CE  LYS A1016       7.665  35.932   2.585  1.00 58.42           C  
ANISOU  988  CE  LYS A1016     6688   7566   7945   -950   -954   -639       C  
ATOM    989  NZ  LYS A1016       6.844  37.044   2.036  1.00 60.29           N  
ANISOU  989  NZ  LYS A1016     7060   7501   8346  -1021  -1024   -630       N  
ATOM    990  N   ILE A1017       3.839  37.498   6.863  1.00 48.36           N  
ANISOU  990  N   ILE A1017     5639   6308   6428   -183  -1281  -1452       N  
ATOM    991  CA  ILE A1017       2.946  38.640   6.709  1.00 49.04           C  
ANISOU  991  CA  ILE A1017     5832   6132   6671   -157  -1385  -1573       C  
ATOM    992  C   ILE A1017       3.069  39.223   5.308  1.00 49.15           C  
ANISOU  992  C   ILE A1017     5924   5836   6913   -363  -1391  -1394       C  
ATOM    993  O   ILE A1017       4.174  39.379   4.769  1.00 49.45           O  
ANISOU  993  O   ILE A1017     5915   5815   7060   -569  -1406  -1306       O  
ATOM    994  CB  ILE A1017       3.249  39.700   7.782  1.00 51.81           C  
ANISOU  994  CB  ILE A1017     6154   6446   7085   -111  -1581  -1902       C  
ATOM    995  CG1 ILE A1017       3.019  39.127   9.181  1.00 52.50           C  
ANISOU  995  CG1 ILE A1017     6163   6880   6905    114  -1570  -2074       C  
ATOM    996  CG2 ILE A1017       2.396  40.946   7.573  1.00 53.35           C  
ANISOU  996  CG2 ILE A1017     6466   6324   7481    -80  -1708  -2038       C  
ATOM    997  CD1 ILE A1017       3.220  40.138  10.291  1.00 55.85           C  
ANISOU  997  CD1 ILE A1017     6554   7307   7359    191  -1766  -2436       C  
ATOM    998  N   TYR A1018       1.925  39.545   4.710  1.00 48.80           N  
ANISOU  998  N   TYR A1018     5991   5618   6933   -304  -1379  -1333       N  
ATOM    999  CA  TYR A1018       1.858  40.210   3.416  1.00 48.51           C  
ANISOU  999  CA  TYR A1018     6048   5282   7101   -469  -1402  -1162       C  
ATOM   1000  C   TYR A1018       0.743  41.248   3.484  1.00 49.48           C  
ANISOU 1000  C   TYR A1018     6284   5162   7353   -349  -1524  -1293       C  
ATOM   1001  O   TYR A1018       0.221  41.558   4.559  1.00 49.82           O  
ANISOU 1001  O   TYR A1018     6318   5266   7347   -163  -1604  -1549       O  
ATOM   1002  CB  TYR A1018       1.644  39.189   2.290  1.00 45.39           C  
ANISOU 1002  CB  TYR A1018     5662   4971   6614   -520  -1221   -870       C  
ATOM   1003  CG  TYR A1018       0.373  38.375   2.422  1.00 42.44           C  
ANISOU 1003  CG  TYR A1018     5311   4743   6073   -321  -1113   -845       C  
ATOM   1004  CD1 TYR A1018       0.327  37.251   3.237  1.00 40.80           C  
ANISOU 1004  CD1 TYR A1018     5022   4830   5651   -195  -1009   -875       C  
ATOM   1005  CD2 TYR A1018      -0.776  38.724   1.725  1.00 41.53           C  
ANISOU 1005  CD2 TYR A1018     5291   4471   6018   -263  -1117   -778       C  
ATOM   1006  CE1 TYR A1018      -0.828  36.503   3.359  1.00 39.25           C  
ANISOU 1006  CE1 TYR A1018     4836   4762   5315    -41   -906   -838       C  
ATOM   1007  CE2 TYR A1018      -1.938  37.979   1.840  1.00 39.83           C  
ANISOU 1007  CE2 TYR A1018     5074   4402   5657    -98  -1018   -761       C  
ATOM   1008  CZ  TYR A1018      -1.958  36.869   2.660  1.00 38.78           C  
ANISOU 1008  CZ  TYR A1018     4857   4556   5323      1   -909   -790       C  
ATOM   1009  OH  TYR A1018      -3.108  36.122   2.781  1.00 37.42           O  
ANISOU 1009  OH  TYR A1018     4674   4526   5018    139   -805   -760       O  
ATOM   1010  N   LYS A1019       0.378  41.795   2.329  1.00 50.11           N  
ANISOU 1010  N   LYS A1019     6468   4980   7592   -443  -1543  -1119       N  
ATOM   1011  CA  LYS A1019      -0.734  42.726   2.222  1.00 52.70           C  
ANISOU 1011  CA  LYS A1019     6910   5063   8050   -315  -1658  -1205       C  
ATOM   1012  C   LYS A1019      -1.736  42.209   1.199  1.00 53.90           C  
ANISOU 1012  C   LYS A1019     7118   5228   8134   -261  -1544   -980       C  
ATOM   1013  O   LYS A1019      -1.366  41.565   0.213  1.00 53.31           O  
ANISOU 1013  O   LYS A1019     7033   5211   8011   -405  -1423   -724       O  
ATOM   1014  CB  LYS A1019      -0.261  44.129   1.819  1.00 54.54           C  
ANISOU 1014  CB  LYS A1019     7235   4902   8585   -472  -1840  -1220       C  
ATOM   1015  CG  LYS A1019       0.564  44.848   2.875  1.00 56.79           C  
ANISOU 1015  CG  LYS A1019     7475   5124   8980   -511  -1995  -1501       C  
ATOM   1016  CD  LYS A1019       0.792  46.302   2.488  1.00 59.71           C  
ANISOU 1016  CD  LYS A1019     7957   5047   9684   -647  -2192  -1529       C  
ATOM   1017  CE  LYS A1019       1.623  47.031   3.529  1.00 62.17           C  
ANISOU 1017  CE  LYS A1019     8216   5281  10124   -700  -2360  -1835       C  
ATOM   1018  NZ  LYS A1019       1.774  48.478   3.209  1.00 65.52           N  
ANISOU 1018  NZ  LYS A1019     8762   5228  10906   -829  -2568  -1880       N  
ATOM   1019  N   ASP A1020      -3.012  42.494   1.442  1.00 55.78           N  
ANISOU 1019  N   ASP A1020     7402   5429   8363    -46  -1587  -1094       N  
ATOM   1020  CA  ASP A1020      -4.058  42.114   0.504  1.00 57.20           C  
ANISOU 1020  CA  ASP A1020     7626   5616   8492     18  -1506   -912       C  
ATOM   1021  C   ASP A1020      -4.079  43.114  -0.652  1.00 62.84           C  
ANISOU 1021  C   ASP A1020     8467   5983   9427    -96  -1614   -743       C  
ATOM   1022  O   ASP A1020      -3.158  43.915  -0.831  1.00 63.87           O  
ANISOU 1022  O   ASP A1020     8642   5885   9739   -271  -1716   -715       O  
ATOM   1023  CB  ASP A1020      -5.403  42.012   1.219  1.00 56.50           C  
ANISOU 1023  CB  ASP A1020     7511   5655   8301    291  -1506  -1098       C  
ATOM   1024  CG  ASP A1020      -5.748  43.260   2.005  1.00 60.30           C  
ANISOU 1024  CG  ASP A1020     8038   5941   8934    441  -1700  -1384       C  
ATOM   1025  OD1 ASP A1020      -4.998  44.255   1.918  1.00 62.46           O  
ANISOU 1025  OD1 ASP A1020     8382   5929   9421    322  -1848  -1425       O  
ATOM   1026  OD2 ASP A1020      -6.774  43.244   2.717  1.00 60.75           O  
ANISOU 1026  OD2 ASP A1020     8052   6131   8898    676  -1705  -1576       O  
ATOM   1027  N   THR A1021      -5.144  43.082  -1.455  1.00 67.00           N  
ANISOU 1027  N   THR A1021     9048   6469   9941     -4  -1596   -618       N  
ATOM   1028  CA  THR A1021      -5.219  43.953  -2.621  1.00 70.95           C  
ANISOU 1028  CA  THR A1021     9672   6664  10621   -100  -1693   -415       C  
ATOM   1029  C   THR A1021      -5.402  45.421  -2.256  1.00 77.49           C  
ANISOU 1029  C   THR A1021    10608   7130  11707    -29  -1919   -574       C  
ATOM   1030  O   THR A1021      -5.251  46.279  -3.133  1.00 78.08           O  
ANISOU 1030  O   THR A1021    10799   6899  11969   -140  -2022   -394       O  
ATOM   1031  CB  THR A1021      -6.359  43.508  -3.537  1.00 68.75           C  
ANISOU 1031  CB  THR A1021     9414   6467  10243      4  -1627   -256       C  
ATOM   1032  OG1 THR A1021      -6.230  44.158  -4.807  1.00 69.52           O  
ANISOU 1032  OG1 THR A1021     9622   6326  10465   -126  -1692      5       O  
ATOM   1033  CG2 THR A1021      -7.705  43.869  -2.926  1.00 68.86           C  
ANISOU 1033  CG2 THR A1021     9428   6470  10264    291  -1711   -473       C  
ATOM   1034  N   GLU A1022      -5.713  45.733  -0.996  1.00 83.29           N  
ANISOU 1034  N   GLU A1022    11305   7888  12453    156  -2000   -903       N  
ATOM   1035  CA  GLU A1022      -5.938  47.109  -0.566  1.00 91.65           C  
ANISOU 1035  CA  GLU A1022    12461   8599  13763    256  -2227  -1107       C  
ATOM   1036  C   GLU A1022      -4.971  47.541   0.532  1.00 91.63           C  
ANISOU 1036  C   GLU A1022    12420   8549  13846    191  -2317  -1367       C  
ATOM   1037  O   GLU A1022      -5.255  48.497   1.261  1.00 96.60           O  
ANISOU 1037  O   GLU A1022    13094   8976  14634    336  -2496  -1648       O  
ATOM   1038  CB  GLU A1022      -7.387  47.294  -0.111  1.00 96.00           C  
ANISOU 1038  CB  GLU A1022    13007   9197  14274    585  -2280  -1314       C  
ATOM   1039  CG  GLU A1022      -7.927  46.165   0.750  1.00 98.44           C  
ANISOU 1039  CG  GLU A1022    13161   9950  14290    746  -2118  -1465       C  
ATOM   1040  CD  GLU A1022      -9.411  46.309   1.027  1.00102.47           C  
ANISOU 1040  CD  GLU A1022    13644  10537  14751   1051  -2150  -1628       C  
ATOM   1041  OE1 GLU A1022      -9.955  47.410   0.799  1.00106.63           O  
ANISOU 1041  OE1 GLU A1022    14271  10756  15486   1178  -2330  -1704       O  
ATOM   1042  OE2 GLU A1022     -10.034  45.320   1.467  1.00102.17           O  
ANISOU 1042  OE2 GLU A1022    13481  10867  14472   1163  -1997  -1675       O  
ATOM   1043  N   GLY A1023      -3.837  46.857   0.669  1.00 88.12           N  
ANISOU 1043  N   GLY A1023    11886   8295  13299    -11  -2207  -1295       N  
ATOM   1044  CA  GLY A1023      -2.777  47.305   1.550  1.00 84.73           C  
ANISOU 1044  CA  GLY A1023    11415   7813  12965   -116  -2304  -1507       C  
ATOM   1045  C   GLY A1023      -2.933  46.958   3.013  1.00 85.44           C  
ANISOU 1045  C   GLY A1023    11394   8184  12886     86  -2304  -1854       C  
ATOM   1046  O   GLY A1023      -2.170  47.476   3.837  1.00 92.61           O  
ANISOU 1046  O   GLY A1023    12270   9036  13882     37  -2421  -2087       O  
ATOM   1047  N   TYR A1024      -3.886  46.103   3.370  1.00 77.44           N  
ANISOU 1047  N   TYR A1024    10316   7482  11626    302  -2177  -1895       N  
ATOM   1048  CA  TYR A1024      -4.078  45.698   4.756  1.00 71.99           C  
ANISOU 1048  CA  TYR A1024     9512   7107  10734    495  -2155  -2191       C  
ATOM   1049  C   TYR A1024      -3.200  44.494   5.069  1.00 66.81           C  
ANISOU 1049  C   TYR A1024     8736   6797   9852    379  -1990  -2088       C  
ATOM   1050  O   TYR A1024      -3.183  43.517   4.313  1.00 64.13           O  
ANISOU 1050  O   TYR A1024     8376   6596   9395    289  -1821  -1806       O  
ATOM   1051  CB  TYR A1024      -5.549  45.377   5.021  1.00 69.76           C  
ANISOU 1051  CB  TYR A1024     9204   7005  10297    775  -2093  -2274       C  
ATOM   1052  CG  TYR A1024      -6.447  46.590   4.949  1.00 71.31           C  
ANISOU 1052  CG  TYR A1024     9497   6896  10702    952  -2275  -2448       C  
ATOM   1053  CD1 TYR A1024      -6.008  47.826   5.405  1.00 74.07           C  
ANISOU 1053  CD1 TYR A1024     9912   6937  11292    956  -2496  -2699       C  
ATOM   1054  CD2 TYR A1024      -7.727  46.505   4.416  1.00 69.89           C  
ANISOU 1054  CD2 TYR A1024     9338   6726  10493   1119  -2236  -2370       C  
ATOM   1055  CE1 TYR A1024      -6.820  48.942   5.340  1.00 76.54           C  
ANISOU 1055  CE1 TYR A1024    10322   6942  11817   1135  -2676  -2867       C  
ATOM   1056  CE2 TYR A1024      -8.546  47.617   4.346  1.00 72.31           C  
ANISOU 1056  CE2 TYR A1024     9728   6751  10995   1305  -2414  -2532       C  
ATOM   1057  CZ  TYR A1024      -8.087  48.833   4.810  1.00 75.82           C  
ANISOU 1057  CZ  TYR A1024    10250   6874  11685   1319  -2634  -2779       C  
ATOM   1058  OH  TYR A1024      -8.895  49.945   4.745  1.00 79.66           O  
ANISOU 1058  OH  TYR A1024    10828   7053  12387   1521  -2823  -2950       O  
ATOM   1059  N   TYR A1025      -2.472  44.570   6.183  1.00 65.41           N  
ANISOU 1059  N   TYR A1025     8479   6758   9616    393  -2052  -2327       N  
ATOM   1060  CA  TYR A1025      -1.559  43.498   6.557  1.00 61.65           C  
ANISOU 1060  CA  TYR A1025     7887   6601   8936    300  -1923  -2243       C  
ATOM   1061  C   TYR A1025      -2.322  42.206   6.820  1.00 56.18           C  
ANISOU 1061  C   TYR A1025     7125   6273   7948    453  -1727  -2144       C  
ATOM   1062  O   TYR A1025      -3.323  42.193   7.543  1.00 46.44           O  
ANISOU 1062  O   TYR A1025     5866   5189   6588    682  -1722  -2315       O  
ATOM   1063  CB  TYR A1025      -0.743  43.901   7.784  1.00 64.90           C  
ANISOU 1063  CB  TYR A1025     8220   7110   9329    321  -2051  -2549       C  
ATOM   1064  CG  TYR A1025       0.359  44.883   7.463  1.00 52.53           C  
ANISOU 1064  CG  TYR A1025     6686   5228   8043     86  -2211  -2589       C  
ATOM   1065  CD1 TYR A1025       1.528  44.460   6.845  1.00 51.60           C  
ANISOU 1065  CD1 TYR A1025     6521   5127   7959   -171  -2145  -2362       C  
ATOM   1066  CD2 TYR A1025       0.231  46.231   7.770  1.00 55.66           C  
ANISOU 1066  CD2 TYR A1025     7156   5308   8684    118  -2431  -2855       C  
ATOM   1067  CE1 TYR A1025       2.539  45.349   6.542  1.00 57.14           C  
ANISOU 1067  CE1 TYR A1025     7234   5558   8919   -410  -2281  -2384       C  
ATOM   1068  CE2 TYR A1025       1.240  47.130   7.472  1.00 63.35           C  
ANISOU 1068  CE2 TYR A1025     8159   5973   9938   -124  -2580  -2879       C  
ATOM   1069  CZ  TYR A1025       2.392  46.682   6.859  1.00 61.70           C  
ANISOU 1069  CZ  TYR A1025     7888   5806   9747   -398  -2499  -2635       C  
ATOM   1070  OH  TYR A1025       3.403  47.566   6.557  1.00 64.89           O  
ANISOU 1070  OH  TYR A1025     8303   5922  10431   -662  -2636  -2645       O  
ATOM   1071  N   THR A1026      -1.834  41.118   6.227  1.00 51.08           N  
ANISOU 1071  N   THR A1026     6441   5769   7197    322  -1565  -1869       N  
ATOM   1072  CA  THR A1026      -2.548  39.851   6.182  1.00 46.48           C  
ANISOU 1072  CA  THR A1026     5815   5456   6388    417  -1374  -1712       C  
ATOM   1073  C   THR A1026      -1.547  38.711   6.291  1.00 45.66           C  
ANISOU 1073  C   THR A1026     5629   5582   6138    315  -1253  -1562       C  
ATOM   1074  O   THR A1026      -0.355  38.875   6.017  1.00 46.35           O  
ANISOU 1074  O   THR A1026     5698   5594   6320    142  -1296  -1517       O  
ATOM   1075  CB  THR A1026      -3.360  39.721   4.881  1.00 43.29           C  
ANISOU 1075  CB  THR A1026     5489   4897   6063    376  -1302  -1484       C  
ATOM   1076  OG1 THR A1026      -3.937  40.990   4.546  1.00 44.06           O  
ANISOU 1076  OG1 THR A1026     5681   4693   6368    421  -1455  -1588       O  
ATOM   1077  CG2 THR A1026      -4.476  38.702   5.030  1.00 40.73           C  
ANISOU 1077  CG2 THR A1026     5119   4820   5537    522  -1147  -1416       C  
ATOM   1078  N   ILE A1027      -2.044  37.543   6.699  1.00 45.03           N  
ANISOU 1078  N   ILE A1027     5493   5785   5833    424  -1102  -1482       N  
ATOM   1079  CA  ILE A1027      -1.212  36.352   6.828  1.00 44.65           C  
ANISOU 1079  CA  ILE A1027     5374   5950   5640    364   -985  -1329       C  
ATOM   1080  C   ILE A1027      -2.124  35.142   6.708  1.00 35.40           C  
ANISOU 1080  C   ILE A1027     4192   4952   4308    445   -809  -1160       C  
ATOM   1081  O   ILE A1027      -3.334  35.235   6.915  1.00 35.55           O  
ANISOU 1081  O   ILE A1027     4222   5009   4277    574   -784  -1216       O  
ATOM   1082  CB  ILE A1027      -0.437  36.348   8.171  1.00 46.54           C  
ANISOU 1082  CB  ILE A1027     5525   6409   5747    438  -1053  -1515       C  
ATOM   1083  CG1 ILE A1027       0.803  35.457   8.080  1.00 37.74           C  
ANISOU 1083  CG1 ILE A1027     4344   5423   4573    331   -991  -1365       C  
ATOM   1084  CG2 ILE A1027      -1.349  35.895   9.308  1.00 38.96           C  
ANISOU 1084  CG2 ILE A1027     4521   5731   4553    656   -998  -1614       C  
ATOM   1085  CD1 ILE A1027       1.716  35.561   9.287  1.00 39.39           C  
ANISOU 1085  CD1 ILE A1027     4459   5835   4671    386  -1086  -1546       C  
ATOM   1086  N   GLY A1028      -1.540  33.997   6.368  1.00 37.86           N  
ANISOU 1086  N   GLY A1028     4473   5366   4548    370   -689   -959       N  
ATOM   1087  CA  GLY A1028      -2.327  32.787   6.292  1.00 32.57           C  
ANISOU 1087  CA  GLY A1028     3792   4839   3744    429   -528   -799       C  
ATOM   1088  C   GLY A1028      -3.175  32.761   5.036  1.00 32.34           C  
ANISOU 1088  C   GLY A1028     3826   4639   3823    367   -473   -673       C  
ATOM   1089  O   GLY A1028      -2.742  33.167   3.950  1.00 31.03           O  
ANISOU 1089  O   GLY A1028     3708   4275   3808    232   -508   -598       O  
ATOM   1090  N   ILE A1029      -4.407  32.280   5.185  1.00 32.04           N  
ANISOU 1090  N   ILE A1029     3778   4698   3698    464   -387   -645       N  
ATOM   1091  CA  ILE A1029      -5.363  32.253   4.085  1.00 31.48           C  
ANISOU 1091  CA  ILE A1029     3750   4500   3710    429   -344   -551       C  
ATOM   1092  C   ILE A1029      -6.232  33.502   4.162  1.00 32.86           C  
ANISOU 1092  C   ILE A1029     3953   4567   3966    524   -459   -720       C  
ATOM   1093  O   ILE A1029      -7.419  33.428   4.497  1.00 34.26           O  
ANISOU 1093  O   ILE A1029     4095   4849   4075    644   -422   -775       O  
ATOM   1094  CB  ILE A1029      -6.217  30.973   4.123  1.00 31.06           C  
ANISOU 1094  CB  ILE A1029     3656   4609   3538    462   -187   -422       C  
ATOM   1095  CG1 ILE A1029      -5.339  29.743   4.358  1.00 30.21           C  
ANISOU 1095  CG1 ILE A1029     3522   4612   3344    411    -91   -283       C  
ATOM   1096  CG2 ILE A1029      -7.001  30.804   2.821  1.00 29.29           C  
ANISOU 1096  CG2 ILE A1029     3466   4258   3404    395   -145   -314       C  
ATOM   1097  CD1 ILE A1029      -6.090  28.441   4.230  1.00 29.59           C  
ANISOU 1097  CD1 ILE A1029     3420   4630   3193    408     58   -132       C  
ATOM   1098  N   GLY A1030      -5.643  34.657   3.866  1.00 32.37           N  
ANISOU 1098  N   GLY A1030     3948   4293   4059    471   -603   -805       N  
ATOM   1099  CA  GLY A1030      -6.404  35.893   3.850  1.00 33.83           C  
ANISOU 1099  CA  GLY A1030     4176   4321   4357    565   -733   -962       C  
ATOM   1100  C   GLY A1030      -6.951  36.316   5.194  1.00 61.01           C  
ANISOU 1100  C   GLY A1030     7563   7917   7702    759   -784  -1210       C  
ATOM   1101  O   GLY A1030      -8.009  36.952   5.252  1.00 59.61           O  
ANISOU 1101  O   GLY A1030     7390   7700   7560    894   -839  -1332       O  
ATOM   1102  N   HIS A1031      -6.260  35.984   6.282  1.00 63.32           N  
ANISOU 1102  N   HIS A1031     7795   8403   7860    790   -772  -1294       N  
ATOM   1103  CA  HIS A1031      -6.682  36.385   7.620  1.00 63.14           C  
ANISOU 1103  CA  HIS A1031     7709   8569   7711    978   -822  -1545       C  
ATOM   1104  C   HIS A1031      -6.123  37.773   7.911  1.00 62.76           C  
ANISOU 1104  C   HIS A1031     7705   8319   7820    995  -1026  -1787       C  
ATOM   1105  O   HIS A1031      -4.918  37.932   8.130  1.00 64.91           O  
ANISOU 1105  O   HIS A1031     7980   8553   8132    893  -1092  -1817       O  
ATOM   1106  CB  HIS A1031      -6.217  35.378   8.667  1.00 63.28           C  
ANISOU 1106  CB  HIS A1031     7642   8911   7492   1013   -722  -1514       C  
ATOM   1107  CG  HIS A1031      -6.617  35.737  10.064  1.00 66.36           C  
ANISOU 1107  CG  HIS A1031     7955   9549   7709   1209   -763  -1764       C  
ATOM   1108  ND1 HIS A1031      -7.905  35.587  10.530  1.00 67.11           N  
ANISOU 1108  ND1 HIS A1031     7986   9843   7669   1366   -688  -1825       N  
ATOM   1109  CD2 HIS A1031      -5.902  36.251  11.092  1.00 68.16           C  
ANISOU 1109  CD2 HIS A1031     8148   9881   7867   1277   -874  -1982       C  
ATOM   1110  CE1 HIS A1031      -7.965  35.986  11.788  1.00 69.67           C  
ANISOU 1110  CE1 HIS A1031     8242  10396   7835   1529   -742  -2067       C  
ATOM   1111  NE2 HIS A1031      -6.763  36.394  12.153  1.00 69.81           N  
ANISOU 1111  NE2 HIS A1031     8280  10358   7887   1481   -861  -2172       N  
ATOM   1112  N   LEU A1032      -6.999  38.774   7.913  1.00 58.61           N  
ANISOU 1112  N   LEU A1032     7211   7660   7398   1125  -1133  -1969       N  
ATOM   1113  CA  LEU A1032      -6.569  40.144   8.151  1.00 43.49           C  
ANISOU 1113  CA  LEU A1032     5353   5502   5670   1147  -1343  -2212       C  
ATOM   1114  C   LEU A1032      -6.117  40.308   9.596  1.00 55.47           C  
ANISOU 1114  C   LEU A1032     6789   7247   7038   1261  -1404  -2484       C  
ATOM   1115  O   LEU A1032      -6.823  39.915  10.530  1.00 45.77           O  
ANISOU 1115  O   LEU A1032     5471   6336   5583   1443  -1333  -2599       O  
ATOM   1116  CB  LEU A1032      -7.704  41.117   7.828  1.00 44.91           C  
ANISOU 1116  CB  LEU A1032     5585   5484   5995   1294  -1445  -2346       C  
ATOM   1117  CG  LEU A1032      -7.383  42.613   7.774  1.00 48.04           C  
ANISOU 1117  CG  LEU A1032     6077   5518   6659   1303  -1679  -2558       C  
ATOM   1118  CD1 LEU A1032      -8.236  43.293   6.717  1.00 48.50           C  
ANISOU 1118  CD1 LEU A1032     6232   5273   6921   1338  -1749  -2480       C  
ATOM   1119  CD2 LEU A1032      -7.600  43.276   9.126  1.00 51.15           C  
ANISOU 1119  CD2 LEU A1032     6412   6039   6985   1520  -1795  -2953       C  
ATOM   1120  N   LEU A1033      -4.931  40.889   9.777  1.00 56.39           N  
ANISOU 1120  N   LEU A1033     6929   7223   7273   1148  -1536  -2585       N  
ATOM   1121  CA  LEU A1033      -4.386  41.136  11.105  1.00 59.84           C  
ANISOU 1121  CA  LEU A1033     7289   7865   7582   1245  -1624  -2866       C  
ATOM   1122  C   LEU A1033      -4.744  42.523  11.625  1.00 63.12           C  
ANISOU 1122  C   LEU A1033     7736   8107   8140   1391  -1831  -3239       C  
ATOM   1123  O   LEU A1033      -5.151  42.664  12.783  1.00 64.06           O  
ANISOU 1123  O   LEU A1033     7776   8487   8077   1601  -1862  -3515       O  
ATOM   1124  CB  LEU A1033      -2.865  40.963  11.089  1.00 59.68           C  
ANISOU 1124  CB  LEU A1033     7251   7820   7604   1044  -1662  -2798       C  
ATOM   1125  CG  LEU A1033      -2.341  39.557  10.793  1.00 55.27           C  
ANISOU 1125  CG  LEU A1033     6645   7470   6885    933  -1476  -2481       C  
ATOM   1126  CD1 LEU A1033      -0.833  39.585  10.611  1.00 54.98           C  
ANISOU 1126  CD1 LEU A1033     6586   7361   6943    733  -1538  -2433       C  
ATOM   1127  CD2 LEU A1033      -2.731  38.597  11.906  1.00 54.31           C  
ANISOU 1127  CD2 LEU A1033     6424   7782   6430   1107  -1358  -2500       C  
ATOM   1128  N   THR A1034      -4.606  43.548  10.788  1.00 63.75           N  
ANISOU 1128  N   THR A1034     7929   7751   8541   1288  -1975  -3251       N  
ATOM   1129  CA  THR A1034      -4.909  44.914  11.189  1.00 67.60           C  
ANISOU 1129  CA  THR A1034     8466   8000   9218   1420  -2192  -3602       C  
ATOM   1130  C   THR A1034      -5.071  45.768   9.941  1.00 68.72           C  
ANISOU 1130  C   THR A1034     8755   7652   9703   1306  -2293  -3472       C  
ATOM   1131  O   THR A1034      -4.673  45.377   8.841  1.00 65.84           O  
ANISOU 1131  O   THR A1034     8444   7149   9425   1090  -2211  -3132       O  
ATOM   1132  CB  THR A1034      -3.815  45.494  12.093  1.00 70.19           C  
ANISOU 1132  CB  THR A1034     8755   8329   9583   1377  -2356  -3890       C  
ATOM   1133  OG1 THR A1034      -4.132  46.853  12.419  1.00 73.91           O  
ANISOU 1133  OG1 THR A1034     9283   8526  10272   1500  -2572  -4228       O  
ATOM   1134  CG2 THR A1034      -2.467  45.451  11.391  1.00 69.84           C  
ANISOU 1134  CG2 THR A1034     8742   8084   9709   1062  -2377  -3678       C  
ATOM   1135  N   LYS A1035      -5.667  46.945  10.130  1.00 72.52           N  
ANISOU 1135  N   LYS A1035     9301   7880  10373   1464  -2476  -3747       N  
ATOM   1136  CA  LYS A1035      -5.792  47.936   9.070  1.00 72.99           C  
ANISOU 1136  CA  LYS A1035     9514   7435  10784   1378  -2615  -3654       C  
ATOM   1137  C   LYS A1035      -4.871  49.130   9.284  1.00 75.08           C  
ANISOU 1137  C   LYS A1035     9835   7365  11326   1252  -2824  -3818       C  
ATOM   1138  O   LYS A1035      -4.995  50.134   8.575  1.00 76.78           O  
ANISOU 1138  O   LYS A1035    10166   7179  11828   1193  -2937  -3725       O  
ATOM   1139  CB  LYS A1035      -7.244  48.401   8.944  1.00 74.17           C  
ANISOU 1139  CB  LYS A1035     9699   7509  10973   1650  -2657  -3764       C  
ATOM   1140  CG  LYS A1035      -8.194  47.318   8.457  1.00 71.20           C  
ANISOU 1140  CG  LYS A1035     9263   7419  10371   1718  -2435  -3504       C  
ATOM   1141  CD  LYS A1035      -9.563  47.885   8.124  1.00 72.63           C  
ANISOU 1141  CD  LYS A1035     9481   7475  10642   1958  -2498  -3583       C  
ATOM   1142  CE  LYS A1035     -10.454  46.828   7.493  1.00 69.89           C  
ANISOU 1142  CE  LYS A1035     9071   7380  10103   1982  -2288  -3304       C  
ATOM   1143  NZ  LYS A1035     -11.765  47.389   7.070  1.00 71.38           N  
ANISOU 1143  NZ  LYS A1035     9285   7449  10389   2208  -2358  -3364       N  
ATOM   1144  N   SER A1036      -3.951  49.045  10.243  1.00 76.64           N  
ANISOU 1144  N   SER A1036     9933   7767  11420   1199  -2843  -3986       N  
ATOM   1145  CA  SER A1036      -2.991  50.112  10.485  1.00 80.69           C  
ANISOU 1145  CA  SER A1036    10464   8029  12168   1049  -2996  -4083       C  
ATOM   1146  C   SER A1036      -1.808  49.983   9.528  1.00 65.66           C  
ANISOU 1146  C   SER A1036     8612   5899  10437    692  -2992  -3811       C  
ATOM   1147  O   SER A1036      -1.365  48.869   9.235  1.00 67.04           O  
ANISOU 1147  O   SER A1036     8738   6276  10456    572  -2875  -3656       O  
ATOM   1148  CB  SER A1036      -2.494  50.069  11.930  1.00 84.64           C  
ANISOU 1148  CB  SER A1036    10819   8866  12473   1149  -3018  -4379       C  
ATOM   1149  OG  SER A1036      -1.424  50.975  12.135  1.00 89.84           O  
ANISOU 1149  OG  SER A1036    11484   9302  13350    972  -3156  -4467       O  
ATOM   1150  N   PRO A1037      -1.279  51.103   9.025  1.00 68.25           N  
ANISOU 1150  N   PRO A1037     9027   5825  11079    513  -3114  -3741       N  
ATOM   1151  CA  PRO A1037      -0.109  51.031   8.135  1.00 75.80           C  
ANISOU 1151  CA  PRO A1037    10009   6602  12191    155  -3095  -3465       C  
ATOM   1152  C   PRO A1037       1.157  50.546   8.824  1.00 78.29           C  
ANISOU 1152  C   PRO A1037    10183   7178  12388      5  -3076  -3561       C  
ATOM   1153  O   PRO A1037       2.145  50.267   8.132  1.00 78.55           O  
ANISOU 1153  O   PRO A1037    10195   7154  12496   -285  -3032  -3333       O  
ATOM   1154  CB  PRO A1037       0.052  52.478   7.645  1.00 71.27           C  
ANISOU 1154  CB  PRO A1037     9552   5571  11957     39  -3234  -3409       C  
ATOM   1155  CG  PRO A1037      -1.272  53.130   7.907  1.00 72.89           C  
ANISOU 1155  CG  PRO A1037     9823   5675  12195    347  -3311  -3571       C  
ATOM   1156  CD  PRO A1037      -1.804  52.472   9.139  1.00 71.97           C  
ANISOU 1156  CD  PRO A1037     9579   5986  11779    628  -3266  -3876       C  
ATOM   1157  N   SER A1038       1.160  50.434  10.150  1.00 80.82           N  
ANISOU 1157  N   SER A1038    10391   7803  12512    196  -3102  -3878       N  
ATOM   1158  CA  SER A1038       2.347  50.021  10.887  1.00 78.93           C  
ANISOU 1158  CA  SER A1038    10009   7835  12146     83  -3098  -3982       C  
ATOM   1159  C   SER A1038       2.547  48.517  10.754  1.00 75.07           C  
ANISOU 1159  C   SER A1038     9432   7709  11383     60  -2946  -3833       C  
ATOM   1160  O   SER A1038       1.658  47.732  11.103  1.00 72.59           O  
ANISOU 1160  O   SER A1038     9097   7669  10814    290  -2856  -3878       O  
ATOM   1161  CB  SER A1038       2.223  50.416  12.357  1.00 80.71           C  
ANISOU 1161  CB  SER A1038    10146   8285  12233    317  -3176  -4355       C  
ATOM   1162  OG  SER A1038       3.321  49.929  13.109  1.00 80.27           O  
ANISOU 1162  OG  SER A1038     9945   8536  12017    236  -3167  -4447       O  
ATOM   1163  N   LEU A1039       3.717  48.115  10.251  1.00 72.43           N  
ANISOU 1163  N   LEU A1039     9033   7390  11096   -218  -2914  -3653       N  
ATOM   1164  CA  LEU A1039       4.049  46.696  10.205  1.00 67.13           C  
ANISOU 1164  CA  LEU A1039     8254   7109  10144   -229  -2741  -3468       C  
ATOM   1165  C   LEU A1039       4.251  46.129  11.605  1.00 66.81           C  
ANISOU 1165  C   LEU A1039     8073   7513   9797    -35  -2747  -3729       C  
ATOM   1166  O   LEU A1039       3.954  44.953  11.846  1.00 63.96           O  
ANISOU 1166  O   LEU A1039     7655   7519   9128    101  -2569  -3584       O  
ATOM   1167  CB  LEU A1039       5.296  46.477   9.347  1.00 65.43           C  
ANISOU 1167  CB  LEU A1039     7982   6830  10049   -557  -2689  -3198       C  
ATOM   1168  CG  LEU A1039       5.883  45.064   9.271  1.00 62.99           C  
ANISOU 1168  CG  LEU A1039     7546   6924   9464   -581  -2489  -2965       C  
ATOM   1169  CD1 LEU A1039       4.836  44.054   8.829  1.00 59.68           C  
ANISOU 1169  CD1 LEU A1039     7185   6657   8835   -415  -2282  -2720       C  
ATOM   1170  CD2 LEU A1039       7.085  45.033   8.337  1.00 63.40           C  
ANISOU 1170  CD2 LEU A1039     7538   6880   9672   -906  -2453  -2725       C  
ATOM   1171  N   ASN A1040       4.745  46.948  12.538  1.00 69.64           N  
ANISOU 1171  N   ASN A1040     8381   7869  10208     -9  -2886  -4013       N  
ATOM   1172  CA  ASN A1040       4.873  46.503  13.921  1.00 69.62           C  
ANISOU 1172  CA  ASN A1040     8252   8305   9896    201  -2877  -4231       C  
ATOM   1173  C   ASN A1040       3.513  46.249  14.556  1.00 67.87           C  
ANISOU 1173  C   ASN A1040     8059   8284   9446    528  -2816  -4348       C  
ATOM   1174  O   ASN A1040       3.399  45.412  15.458  1.00 63.99           O  
ANISOU 1174  O   ASN A1040     7467   8230   8616    708  -2734  -4400       O  
ATOM   1175  CB  ASN A1040       5.654  47.534  14.736  1.00 74.12           C  
ANISOU 1175  CB  ASN A1040     8767   8807  10587    158  -3023  -4481       C  
ATOM   1176  CG  ASN A1040       7.113  47.609  14.336  1.00 74.47           C  
ANISOU 1176  CG  ASN A1040     8734   8780  10780   -153  -3063  -4379       C  
ATOM   1177  OD1 ASN A1040       7.945  46.857  14.843  1.00 73.54           O  
ANISOU 1177  OD1 ASN A1040     8474   9007  10461   -168  -3029  -4378       O  
ATOM   1178  ND2 ASN A1040       7.432  48.520  13.424  1.00 75.62           N  
ANISOU 1178  ND2 ASN A1040     8968   8492  11273   -399  -3129  -4277       N  
ATOM   1179  N   ALA A1041       2.476  46.959  14.105  1.00 66.92           N  
ANISOU 1179  N   ALA A1041     8065   7865   9497    611  -2847  -4372       N  
ATOM   1180  CA  ALA A1041       1.133  46.713  14.617  1.00 65.59           C  
ANISOU 1180  CA  ALA A1041     7905   7898   9119    914  -2775  -4466       C  
ATOM   1181  C   ALA A1041       0.609  45.349  14.187  1.00 62.05           C  
ANISOU 1181  C   ALA A1041     7451   7704   8422    959  -2601  -4245       C  
ATOM   1182  O   ALA A1041      -0.152  44.718  14.929  1.00 61.79           O  
ANISOU 1182  O   ALA A1041     7358   8035   8085   1191  -2495  -4296       O  
ATOM   1183  CB  ALA A1041       0.181  47.816  14.154  1.00 66.66           C  
ANISOU 1183  CB  ALA A1041     8166   7646   9516    991  -2859  -4530       C  
ATOM   1184  N   ALA A1042       0.998  44.881  12.999  1.00 59.39           N  
ANISOU 1184  N   ALA A1042     7160   7201   8203    734  -2496  -3879       N  
ATOM   1185  CA  ALA A1042       0.552  43.572  12.535  1.00 56.15           C  
ANISOU 1185  CA  ALA A1042     6737   7022   7577    758  -2252  -3527       C  
ATOM   1186  C   ALA A1042       1.196  42.454  13.347  1.00 55.69           C  
ANISOU 1186  C   ALA A1042     6545   7410   7204    798  -2151  -3477       C  
ATOM   1187  O   ALA A1042       0.519  41.510  13.770  1.00 54.06           O  
ANISOU 1187  O   ALA A1042     6299   7522   6718    961  -1997  -3380       O  
ATOM   1188  CB  ALA A1042       0.862  43.408  11.047  1.00 53.27           C  
ANISOU 1188  CB  ALA A1042     6450   6373   7419    511  -2172  -3164       C  
ATOM   1189  N   LYS A1043       2.509  42.547  13.579  1.00 57.37           N  
ANISOU 1189  N   LYS A1043     6682   7652   7462    648  -2241  -3535       N  
ATOM   1190  CA  LYS A1043       3.193  41.536  14.379  1.00 57.71           C  
ANISOU 1190  CA  LYS A1043     6596   8117   7212    701  -2171  -3496       C  
ATOM   1191  C   LYS A1043       2.713  41.539  15.825  1.00 59.69           C  
ANISOU 1191  C   LYS A1043     6777   8723   7180    971  -2220  -3790       C  
ATOM   1192  O   LYS A1043       2.771  40.502  16.495  1.00 58.16           O  
ANISOU 1192  O   LYS A1043     6503   8924   6672   1087  -2108  -3689       O  
ATOM   1193  CB  LYS A1043       4.705  41.750  14.315  1.00 58.95           C  
ANISOU 1193  CB  LYS A1043     6671   8233   7496    488  -2279  -3527       C  
ATOM   1194  CG  LYS A1043       5.365  41.099  13.107  1.00 56.85           C  
ANISOU 1194  CG  LYS A1043     6408   7854   7337    262  -2150  -3155       C  
ATOM   1195  CD  LYS A1043       6.788  41.594  12.904  1.00 58.03           C  
ANISOU 1195  CD  LYS A1043     6473   7899   7679     21  -2275  -3213       C  
ATOM   1196  CE  LYS A1043       6.806  43.045  12.453  1.00 60.12           C  
ANISOU 1196  CE  LYS A1043     6818   7728   8298   -139  -2448  -3378       C  
ATOM   1197  NZ  LYS A1043       8.169  43.474  12.036  1.00 61.65           N  
ANISOU 1197  NZ  LYS A1043     6925   7793   8707   -428  -2538  -3364       N  
ATOM   1198  N   SER A1044       2.240  42.683  16.324  1.00 63.30           N  
ANISOU 1198  N   SER A1044     7263   9051   7735   1079  -2387  -4152       N  
ATOM   1199  CA  SER A1044       1.673  42.719  17.668  1.00 65.64           C  
ANISOU 1199  CA  SER A1044     7485   9680   7776   1345  -2358  -4334       C  
ATOM   1200  C   SER A1044       0.386  41.905  17.737  1.00 64.51           C  
ANISOU 1200  C   SER A1044     7355   9776   7380   1533  -2186  -4210       C  
ATOM   1201  O   SER A1044       0.244  41.021  18.588  1.00 63.54           O  
ANISOU 1201  O   SER A1044     7142  10076   6923   1673  -2066  -4134       O  
ATOM   1202  CB  SER A1044       1.422  44.165  18.099  1.00 69.34           C  
ANISOU 1202  CB  SER A1044     7976   9908   8463   1413  -2510  -4633       C  
ATOM   1203  OG  SER A1044       2.635  44.893  18.179  1.00 71.61           O  
ANISOU 1203  OG  SER A1044     8237  10013   8958   1239  -2660  -4750       O  
ATOM   1204  N   GLU A1045      -0.563  42.187  16.838  1.00 64.78           N  
ANISOU 1204  N   GLU A1045     7496   9540   7576   1532  -2164  -4161       N  
ATOM   1205  CA  GLU A1045      -1.810  41.429  16.814  1.00 65.07           C  
ANISOU 1205  CA  GLU A1045     7533   9779   7412   1682  -1968  -3987       C  
ATOM   1206  C   GLU A1045      -1.572  39.964  16.473  1.00 63.80           C  
ANISOU 1206  C   GLU A1045     7345   9816   7080   1590  -1753  -3571       C  
ATOM   1207  O   GLU A1045      -2.299  39.089  16.957  1.00 63.12           O  
ANISOU 1207  O   GLU A1045     7208  10058   6717   1725  -1593  -3452       O  
ATOM   1208  CB  GLU A1045      -2.789  42.051  15.816  1.00 65.37           C  
ANISOU 1208  CB  GLU A1045     7682   9449   7708   1676  -1972  -3948       C  
ATOM   1209  CG  GLU A1045      -3.439  43.346  16.287  1.00 69.39           C  
ANISOU 1209  CG  GLU A1045     8208   9816   8342   1849  -2138  -4324       C  
ATOM   1210  CD  GLU A1045      -4.585  43.113  17.255  1.00 71.44           C  
ANISOU 1210  CD  GLU A1045     8361  10453   8330   2115  -2026  -4403       C  
ATOM   1211  OE1 GLU A1045      -4.900  41.938  17.539  1.00 70.16           O  
ANISOU 1211  OE1 GLU A1045     8134  10661   7864   2165  -1843  -4222       O  
ATOM   1212  OE2 GLU A1045      -5.176  44.106  17.729  1.00 74.34           O  
ANISOU 1212  OE2 GLU A1045     8702  10748   8795   2266  -2122  -4631       O  
ATOM   1213  N   LEU A1046      -0.565  39.677  15.644  1.00 63.83           N  
ANISOU 1213  N   LEU A1046     7379   9626   7248   1361  -1746  -3349       N  
ATOM   1214  CA  LEU A1046      -0.275  38.293  15.285  1.00 64.05           C  
ANISOU 1214  CA  LEU A1046     7385   9812   7138   1283  -1557  -2976       C  
ATOM   1215  C   LEU A1046       0.189  37.492  16.495  1.00 66.33           C  
ANISOU 1215  C   LEU A1046     7564  10546   7093   1405  -1522  -2990       C  
ATOM   1216  O   LEU A1046      -0.261  36.360  16.707  1.00 65.19           O  
ANISOU 1216  O   LEU A1046     7396  10648   6724   1476  -1348  -2755       O  
ATOM   1217  CB  LEU A1046       0.776  38.247  14.177  1.00 62.93           C  
ANISOU 1217  CB  LEU A1046     7281   9391   7240   1028  -1571  -2781       C  
ATOM   1218  CG  LEU A1046       1.263  36.854  13.772  1.00 46.24           C  
ANISOU 1218  CG  LEU A1046     5140   7418   5012    949  -1401  -2431       C  
ATOM   1219  CD1 LEU A1046       0.096  35.990  13.323  1.00 44.24           C  
ANISOU 1219  CD1 LEU A1046     4935   7204   4671   1008  -1208  -2189       C  
ATOM   1220  CD2 LEU A1046       2.316  36.953  12.680  1.00 45.29           C  
ANISOU 1220  CD2 LEU A1046     5038   7039   5131    708  -1426  -2286       C  
ATOM   1221  N   ASP A1047       1.087  38.063  17.301  1.00 69.84           N  
ANISOU 1221  N   ASP A1047     7939  11095   7502   1426  -1692  -3257       N  
ATOM   1222  CA  ASP A1047       1.541  37.375  18.505  1.00 70.42           C  
ANISOU 1222  CA  ASP A1047     7904  11617   7238   1561  -1681  -3285       C  
ATOM   1223  C   ASP A1047       0.410  37.230  19.516  1.00 70.46           C  
ANISOU 1223  C   ASP A1047     7871  11963   6940   1808  -1614  -3398       C  
ATOM   1224  O   ASP A1047       0.306  36.202  20.195  1.00 67.89           O  
ANISOU 1224  O   ASP A1047     7486  11986   6323   1907  -1480  -3203       O  
ATOM   1225  CB  ASP A1047       2.724  38.122  19.119  1.00 72.33           C  
ANISOU 1225  CB  ASP A1047     8068  11898   7518   1529  -1899  -3585       C  
ATOM   1226  CG  ASP A1047       3.933  38.146  18.205  1.00 70.45           C  
ANISOU 1226  CG  ASP A1047     7830  11396   7540   1278  -1948  -3451       C  
ATOM   1227  OD1 ASP A1047       3.838  37.607  17.082  1.00 67.87           O  
ANISOU 1227  OD1 ASP A1047     7572  10859   7355   1141  -1812  -3134       O  
ATOM   1228  OD2 ASP A1047       4.977  38.701  18.607  1.00 72.20           O  
ANISOU 1228  OD2 ASP A1047     7974  11637   7821   1215  -2118  -3665       O  
ATOM   1229  N   LYS A1048      -0.449  38.246  19.627  1.00 74.40           N  
ANISOU 1229  N   LYS A1048     8392  12318   7556   1895  -1671  -3639       N  
ATOM   1230  CA  LYS A1048      -1.595  38.161  20.524  1.00 77.56           C  
ANISOU 1230  CA  LYS A1048     8729  12993   7747   2107  -1563  -3676       C  
ATOM   1231  C   LYS A1048      -2.610  37.122  20.065  1.00 74.30           C  
ANISOU 1231  C   LYS A1048     8346  12702   7182   2130  -1354  -3390       C  
ATOM   1232  O   LYS A1048      -3.379  36.620  20.891  1.00 75.85           O  
ANISOU 1232  O   LYS A1048     8459  13217   7142   2269  -1220  -3305       O  
ATOM   1233  CB  LYS A1048      -2.267  39.530  20.650  1.00 80.81           C  
ANISOU 1233  CB  LYS A1048     9150  13197   8357   2198  -1684  -3997       C  
ATOM   1234  CG  LYS A1048      -1.384  40.597  21.279  1.00 86.05           C  
ANISOU 1234  CG  LYS A1048     9772  13764   9161   2196  -1881  -4294       C  
ATOM   1235  CD  LYS A1048      -1.974  41.989  21.107  1.00 90.16           C  
ANISOU 1235  CD  LYS A1048    10336  13967   9953   2250  -2021  -4578       C  
ATOM   1236  CE  LYS A1048      -3.300  42.131  21.835  1.00 92.55           C  
ANISOU 1236  CE  LYS A1048    10561  14508  10096   2487  -1948  -4673       C  
ATOM   1237  NZ  LYS A1048      -3.847  43.512  21.720  1.00 94.64           N  
ANISOU 1237  NZ  LYS A1048    10860  14470  10628   2563  -2102  -4956       N  
ATOM   1238  N   ALA A1049      -2.627  36.788  18.774  1.00 69.95           N  
ANISOU 1238  N   ALA A1049     7894  11853   6833   1962  -1294  -3162       N  
ATOM   1239  CA  ALA A1049      -3.547  35.789  18.251  1.00 64.98           C  
ANISOU 1239  CA  ALA A1049     7285  11261   6143   1942  -1075  -2830       C  
ATOM   1240  C   ALA A1049      -2.970  34.380  18.266  1.00 64.65           C  
ANISOU 1240  C   ALA A1049     7229  11385   5952   1865   -934  -2468       C  
ATOM   1241  O   ALA A1049      -3.739  33.412  18.295  1.00 49.03           O  
ANISOU 1241  O   ALA A1049     5237   9567   3825   1892   -750  -2220       O  
ATOM   1242  CB  ALA A1049      -3.961  36.149  16.821  1.00 49.32           C  
ANISOU 1242  CB  ALA A1049     5406   8837   4498   1798  -1065  -2726       C  
ATOM   1243  N   ILE A1050      -1.649  34.243  18.248  1.00 64.69           N  
ANISOU 1243  N   ILE A1050     7230  11349   6002   1772  -1019  -2435       N  
ATOM   1244  CA  ILE A1050      -0.993  32.939  18.240  1.00 61.01           C  
ANISOU 1244  CA  ILE A1050     6752  11012   5419   1718   -908  -2107       C  
ATOM   1245  C   ILE A1050      -0.535  32.536  19.635  1.00 60.11           C  
ANISOU 1245  C   ILE A1050     6543  11336   4961   1874   -936  -2156       C  
ATOM   1246  O   ILE A1050      -0.752  31.403  20.065  1.00 59.31           O  
ANISOU 1246  O   ILE A1050     6421  11479   4633   1932   -793  -1890       O  
ATOM   1247  CB  ILE A1050       0.184  32.941  17.239  1.00 57.44           C  
ANISOU 1247  CB  ILE A1050     6339  10254   5230   1521   -971  -2010       C  
ATOM   1248  CG1 ILE A1050      -0.321  33.239  15.826  1.00 54.48           C  
ANISOU 1248  CG1 ILE A1050     6061   9483   5158   1370   -927  -1918       C  
ATOM   1249  CG2 ILE A1050       0.925  31.614  17.277  1.00 55.93           C  
ANISOU 1249  CG2 ILE A1050     6128  10202   4922   1495   -876  -1705       C  
ATOM   1250  CD1 ILE A1050      -1.422  32.313  15.368  1.00 52.52           C  
ANISOU 1250  CD1 ILE A1050     5851   9242   4862   1375   -729  -1652       C  
ATOM   1251  N   GLY A1051       0.100  33.453  20.359  1.00 61.49           N  
ANISOU 1251  N   GLY A1051     6658  11613   5093   1943  -1124  -2492       N  
ATOM   1252  CA  GLY A1051       0.564  33.187  21.704  1.00 63.48           C  
ANISOU 1252  CA  GLY A1051     6805  12206   5109   2074  -1135  -2513       C  
ATOM   1253  C   GLY A1051       2.065  33.095  21.875  1.00 64.30           C  
ANISOU 1253  C   GLY A1051     6862  12331   5237   2017  -1257  -2528       C  
ATOM   1254  O   GLY A1051       2.521  32.685  22.949  1.00 66.82           O  
ANISOU 1254  O   GLY A1051     7096  12930   5364   2123  -1246  -2483       O  
ATOM   1255  N   ARG A1052       2.847  33.459  20.862  1.00 62.72           N  
ANISOU 1255  N   ARG A1052     6702  11857   5272   1852  -1373  -2586       N  
ATOM   1256  CA  ARG A1052       4.298  33.424  20.959  1.00 64.88           C  
ANISOU 1256  CA  ARG A1052     6906  12147   5598   1780  -1490  -2610       C  
ATOM   1257  C   ARG A1052       4.875  34.553  20.119  1.00 65.37           C  
ANISOU 1257  C   ARG A1052     6983  11863   5990   1598  -1660  -2847       C  
ATOM   1258  O   ARG A1052       4.173  35.192  19.331  1.00 63.98           O  
ANISOU 1258  O   ARG A1052     6897  11365   6048   1512  -1641  -2890       O  
ATOM   1259  CB  ARG A1052       4.863  32.074  20.501  1.00 63.25           C  
ANISOU 1259  CB  ARG A1052     6706  11998   5329   1738  -1386  -2237       C  
ATOM   1260  CG  ARG A1052       4.633  31.781  19.025  1.00 61.33           C  
ANISOU 1260  CG  ARG A1052     6561  11357   5383   1553  -1264  -2000       C  
ATOM   1261  CD  ARG A1052       5.403  30.552  18.568  1.00 59.98           C  
ANISOU 1261  CD  ARG A1052     6384  11189   5217   1506  -1175  -1673       C  
ATOM   1262  NE  ARG A1052       5.092  30.192  17.185  1.00 57.33           N  
ANISOU 1262  NE  ARG A1052     6139  10512   5130   1349  -1047  -1454       N  
ATOM   1263  CZ  ARG A1052       5.736  30.665  16.123  1.00 45.35           C  
ANISOU 1263  CZ  ARG A1052     4628   8709   3894   1165  -1094  -1483       C  
ATOM   1264  NH1 ARG A1052       6.734  31.525  16.275  1.00 46.78           N  
ANISOU 1264  NH1 ARG A1052     4726   8881   4166   1096  -1264  -1715       N  
ATOM   1265  NH2 ARG A1052       5.383  30.278  14.905  1.00 43.07           N  
ANISOU 1265  NH2 ARG A1052     4421   8156   3789   1042   -970  -1281       N  
ATOM   1266  N   ASN A1053       6.171  34.794  20.296  1.00 68.24           N  
ANISOU 1266  N   ASN A1053     7261  12237   6430   1521  -1785  -2941       N  
ATOM   1267  CA  ASN A1053       6.892  35.761  19.473  1.00 69.75           C  
ANISOU 1267  CA  ASN A1053     7448  12103   6952   1307  -1938  -3115       C  
ATOM   1268  C   ASN A1053       7.150  35.117  18.117  1.00 64.14           C  
ANISOU 1268  C   ASN A1053     6794  11125   6451   1124  -1799  -2770       C  
ATOM   1269  O   ASN A1053       8.061  34.301  17.963  1.00 63.58           O  
ANISOU 1269  O   ASN A1053     6656  11162   6339   1087  -1765  -2582       O  
ATOM   1270  CB  ASN A1053       8.189  36.187  20.150  1.00 76.63           C  
ANISOU 1270  CB  ASN A1053     8198  13060   7856   1271  -2067  -3281       C  
ATOM   1271  CG  ASN A1053       8.930  37.254  19.368  1.00 82.20           C  
ANISOU 1271  CG  ASN A1053     8892  13422   8920   1026  -2216  -3453       C  
ATOM   1272  OD1 ASN A1053       8.355  37.922  18.508  1.00 84.32           O  
ANISOU 1272  OD1 ASN A1053     9253  13362   9421    908  -2242  -3505       O  
ATOM   1273  ND2 ASN A1053      10.213  37.422  19.666  1.00 85.80           N  
ANISOU 1273  ND2 ASN A1053     9230  13944   9427    943  -2310  -3527       N  
ATOM   1274  N   THR A1054       6.337  35.480  17.127  1.00 60.25           N  
ANISOU 1274  N   THR A1054     6420  10295   6178   1023  -1724  -2693       N  
ATOM   1275  CA  THR A1054       6.411  34.859  15.811  1.00 57.56           C  
ANISOU 1275  CA  THR A1054     6140   9720   6010    867  -1580  -2372       C  
ATOM   1276  C   THR A1054       7.434  35.509  14.894  1.00 57.18           C  
ANISOU 1276  C   THR A1054     6063   9403   6259    622  -1668  -2400       C  
ATOM   1277  O   THR A1054       7.900  34.856  13.952  1.00 47.40           O  
ANISOU 1277  O   THR A1054     4824   8074   5111    501  -1564  -2148       O  
ATOM   1278  CB  THR A1054       5.040  34.902  15.128  1.00 57.29           C  
ANISOU 1278  CB  THR A1054     6238   9475   6054    874  -1457  -2261       C  
ATOM   1279  OG1 THR A1054       4.623  36.265  14.982  1.00 59.55           O  
ANISOU 1279  OG1 THR A1054     6576   9514   6538    828  -1586  -2519       O  
ATOM   1280  CG2 THR A1054       4.008  34.151  15.953  1.00 59.03           C  
ANISOU 1280  CG2 THR A1054     6471   9976   5983   1089  -1341  -2191       C  
ATOM   1281  N   ASN A1055       7.789  36.771  15.144  1.00 59.44           N  
ANISOU 1281  N   ASN A1055     6321   9563   6700    544  -1856  -2703       N  
ATOM   1282  CA  ASN A1055       8.661  37.546  14.259  1.00 59.40           C  
ANISOU 1282  CA  ASN A1055     6294   9270   7006    282  -1943  -2730       C  
ATOM   1283  C   ASN A1055       8.081  37.649  12.849  1.00 56.20           C  
ANISOU 1283  C   ASN A1055     6017   8516   6822    134  -1828  -2501       C  
ATOM   1284  O   ASN A1055       8.819  37.778  11.869  1.00 56.40           O  
ANISOU 1284  O   ASN A1055     6020   8366   7045    -85  -1814  -2370       O  
ATOM   1285  CB  ASN A1055      10.080  36.965  14.215  1.00 59.35           C  
ANISOU 1285  CB  ASN A1055     6137   9441   6973    188  -1955  -2644       C  
ATOM   1286  CG  ASN A1055      10.710  36.854  15.592  1.00 59.77           C  
ANISOU 1286  CG  ASN A1055     6052   9861   6797    339  -2083  -2865       C  
ATOM   1287  OD1 ASN A1055      11.284  37.814  16.106  1.00 62.38           O  
ANISOU 1287  OD1 ASN A1055     6303  10181   7215    275  -2275  -3166       O  
ATOM   1288  ND2 ASN A1055      10.613  35.673  16.194  1.00 58.42           N  
ANISOU 1288  ND2 ASN A1055     5852  10013   6330    540  -1985  -2712       N  
ATOM   1289  N   GLY A1056       6.753  37.591  12.736  1.00 52.45           N  
ANISOU 1289  N   GLY A1056     5664   7963   6302    255  -1743  -2451       N  
ATOM   1290  CA  GLY A1056       6.073  37.737  11.467  1.00 46.79           C  
ANISOU 1290  CA  GLY A1056     5069   6937   5772    145  -1650  -2257       C  
ATOM   1291  C   GLY A1056       5.889  36.465  10.668  1.00 47.61           C  
ANISOU 1291  C   GLY A1056     5196   7101   5793    136  -1443  -1916       C  
ATOM   1292  O   GLY A1056       5.337  36.526   9.561  1.00 45.90           O  
ANISOU 1292  O   GLY A1056     5074   6654   5714     45  -1364  -1750       O  
ATOM   1293  N   VAL A1057       6.327  35.318  11.183  1.00 43.47           N  
ANISOU 1293  N   VAL A1057     4592   6874   5053    234  -1363  -1810       N  
ATOM   1294  CA  VAL A1057       6.242  34.045  10.477  1.00 43.26           C  
ANISOU 1294  CA  VAL A1057     4582   6894   4959    233  -1180  -1506       C  
ATOM   1295  C   VAL A1057       5.438  33.069  11.324  1.00 42.99           C  
ANISOU 1295  C   VAL A1057     4563   7108   4663    451  -1081  -1437       C  
ATOM   1296  O   VAL A1057       5.662  32.959  12.535  1.00 44.27           O  
ANISOU 1296  O   VAL A1057     4657   7531   4634    592  -1144  -1564       O  
ATOM   1297  CB  VAL A1057       7.637  33.474  10.162  1.00 41.19           C  
ANISOU 1297  CB  VAL A1057     4208   6729   4714    133  -1170  -1403       C  
ATOM   1298  CG1 VAL A1057       7.515  32.214   9.315  1.00 39.01           C  
ANISOU 1298  CG1 VAL A1057     3962   6458   4402    134   -989  -1113       C  
ATOM   1299  CG2 VAL A1057       8.492  34.518   9.462  1.00 42.24           C  
ANISOU 1299  CG2 VAL A1057     4300   6656   5093   -100  -1273  -1484       C  
ATOM   1300  N   ILE A1058       4.508  32.360  10.687  1.00 40.93           N  
ANISOU 1300  N   ILE A1058     4385   6775   4389    471   -927  -1231       N  
ATOM   1301  CA  ILE A1058       3.683  31.377  11.378  1.00 40.08           C  
ANISOU 1301  CA  ILE A1058     4293   6879   4057    643   -814  -1124       C  
ATOM   1302  C   ILE A1058       3.876  30.010  10.735  1.00 38.48           C  
ANISOU 1302  C   ILE A1058     4101   6686   3833    619   -664   -837       C  
ATOM   1303  O   ILE A1058       4.694  29.849   9.822  1.00 38.28           O  
ANISOU 1303  O   ILE A1058     4059   6540   3945    490   -653   -750       O  
ATOM   1304  CB  ILE A1058       2.198  31.782  11.365  1.00 39.40           C  
ANISOU 1304  CB  ILE A1058     4285   6717   3968    707   -773  -1173       C  
ATOM   1305  CG1 ILE A1058       1.689  31.909   9.926  1.00 37.61           C  
ANISOU 1305  CG1 ILE A1058     4143   6195   3951    569   -707  -1044       C  
ATOM   1306  CG2 ILE A1058       1.994  33.080  12.125  1.00 40.74           C  
ANISOU 1306  CG2 ILE A1058     4441   6894   4146    772   -929  -1486       C  
ATOM   1307  CD1 ILE A1058       0.217  32.248   9.825  1.00 37.20           C  
ANISOU 1307  CD1 ILE A1058     4154   6075   3903    638   -667  -1081       C  
ATOM   1308  N   THR A1059       3.126  29.021  11.209  1.00 37.78           N  
ANISOU 1308  N   THR A1059     4036   6741   3575    742   -548   -693       N  
ATOM   1309  CA  THR A1059       3.153  27.670  10.671  1.00 36.95           C  
ANISOU 1309  CA  THR A1059     3957   6622   3461    734   -409   -429       C  
ATOM   1310  C   THR A1059       1.791  27.329  10.079  1.00 37.11           C  
ANISOU 1310  C   THR A1059     4061   6521   3519    714   -283   -314       C  
ATOM   1311  O   THR A1059       0.831  28.097  10.182  1.00 38.01           O  
ANISOU 1311  O   THR A1059     4202   6597   3642    729   -300   -431       O  
ATOM   1312  CB  THR A1059       3.531  26.650  11.752  1.00 38.08           C  
ANISOU 1312  CB  THR A1059     4055   7030   3385    883   -384   -320       C  
ATOM   1313  OG1 THR A1059       2.510  26.617  12.756  1.00 39.43           O  
ANISOU 1313  OG1 THR A1059     4236   7380   3365   1008   -349   -337       O  
ATOM   1314  CG2 THR A1059       4.855  27.025  12.400  1.00 39.36           C  
ANISOU 1314  CG2 THR A1059     4115   7346   3492    918   -526   -456       C  
ATOM   1315  N   LYS A1060       1.715  26.153   9.451  1.00 36.37           N  
ANISOU 1315  N   LYS A1060     4000   6366   3454    687   -162    -94       N  
ATOM   1316  CA  LYS A1060       0.453  25.713   8.863  1.00 36.03           C  
ANISOU 1316  CA  LYS A1060     4022   6216   3451    656    -42     17       C  
ATOM   1317  C   LYS A1060      -0.613  25.517   9.935  1.00 37.69           C  
ANISOU 1317  C   LYS A1060     4226   6613   3482    772     10     29       C  
ATOM   1318  O   LYS A1060      -1.787  25.840   9.720  1.00 36.77           O  
ANISOU 1318  O   LYS A1060     4132   6452   3388    760     53     -4       O  
ATOM   1319  CB  LYS A1060       0.664  24.423   8.070  1.00 34.91           C  
ANISOU 1319  CB  LYS A1060     3910   5977   3376    609     64    228       C  
ATOM   1320  CG  LYS A1060      -0.594  23.900   7.394  1.00 34.19           C  
ANISOU 1320  CG  LYS A1060     3877   5771   3342    559    180    334       C  
ATOM   1321  CD  LYS A1060      -0.326  22.613   6.629  1.00 34.05           C  
ANISOU 1321  CD  LYS A1060     3889   5645   3402    518    270    511       C  
ATOM   1322  CE  LYS A1060       0.111  21.489   7.556  1.00 36.47           C  
ANISOU 1322  CE  LYS A1060     4185   6080   3592    625    305    659       C  
ATOM   1323  NZ  LYS A1060      -0.930  21.158   8.569  1.00 38.46           N  
ANISOU 1323  NZ  LYS A1060     4443   6473   3699    692    370    741       N  
ATOM   1324  N   ASP A1061      -0.220  24.995  11.100  1.00 40.49           N  
ANISOU 1324  N   ASP A1061     4539   7201   3645    890      6     78       N  
ATOM   1325  CA  ASP A1061      -1.178  24.797  12.182  1.00 42.12           C  
ANISOU 1325  CA  ASP A1061     4725   7632   3647    999     65    104       C  
ATOM   1326  C   ASP A1061      -1.574  26.117  12.832  1.00 42.57           C  
ANISOU 1326  C   ASP A1061     4740   7802   3630   1067    -32   -166       C  
ATOM   1327  O   ASP A1061      -2.676  26.229  13.381  1.00 42.41           O  
ANISOU 1327  O   ASP A1061     4701   7923   3490   1135     26   -194       O  
ATOM   1328  CB  ASP A1061      -0.604  23.837  13.224  1.00 44.21           C  
ANISOU 1328  CB  ASP A1061     4962   8126   3712   1110     87    261       C  
ATOM   1329  CG  ASP A1061      -0.350  22.450  12.664  1.00 44.11           C  
ANISOU 1329  CG  ASP A1061     4998   7984   3777   1066    184    533       C  
ATOM   1330  OD1 ASP A1061      -0.536  22.253  11.444  1.00 42.99           O  
ANISOU 1330  OD1 ASP A1061     4904   7590   3840    947    231    573       O  
ATOM   1331  OD2 ASP A1061       0.033  21.554  13.446  1.00 45.74           O  
ANISOU 1331  OD2 ASP A1061     5199   8342   3840   1160    208    704       O  
ATOM   1332  N   GLU A1062      -0.696  27.120  12.786  1.00 43.15           N  
ANISOU 1332  N   GLU A1062     4794   7820   3782   1050   -181   -374       N  
ATOM   1333  CA  GLU A1062      -1.050  28.436  13.300  1.00 45.20           C  
ANISOU 1333  CA  GLU A1062     5027   8129   4018   1110   -293   -660       C  
ATOM   1334  C   GLU A1062      -1.883  29.227  12.301  1.00 45.52           C  
ANISOU 1334  C   GLU A1062     5121   7912   4263   1028   -299   -744       C  
ATOM   1335  O   GLU A1062      -2.721  30.041  12.709  1.00 46.85           O  
ANISOU 1335  O   GLU A1062     5276   8129   4396   1109   -338   -928       O  
ATOM   1336  CB  GLU A1062       0.213  29.212  13.674  1.00 46.44           C  
ANISOU 1336  CB  GLU A1062     5138   8311   4197   1110   -464   -858       C  
ATOM   1337  CG  GLU A1062       0.981  28.598  14.831  1.00 48.21           C  
ANISOU 1337  CG  GLU A1062     5292   8841   4184   1229   -488   -822       C  
ATOM   1338  CD  GLU A1062       2.327  29.255  15.065  1.00 49.16           C  
ANISOU 1338  CD  GLU A1062     5351   8980   4349   1206   -658  -1005       C  
ATOM   1339  OE1 GLU A1062       2.749  30.069  14.218  1.00 48.26           O  
ANISOU 1339  OE1 GLU A1062     5253   8612   4472   1068   -738  -1118       O  
ATOM   1340  OE2 GLU A1062       2.963  28.956  16.098  1.00 50.83           O  
ANISOU 1340  OE2 GLU A1062     5490   9468   4354   1320   -713  -1030       O  
ATOM   1341  N   ALA A1063      -1.670  29.015  10.999  1.00 44.46           N  
ANISOU 1341  N   ALA A1063     5043   7517   4333    882   -266   -617       N  
ATOM   1342  CA  ALA A1063      -2.548  29.636  10.015  1.00 44.58           C  
ANISOU 1342  CA  ALA A1063     5112   7307   4519    815   -261   -654       C  
ATOM   1343  C   ALA A1063      -3.925  28.988  10.021  1.00 44.75           C  
ANISOU 1343  C   ALA A1063     5133   7407   4463    861   -123   -542       C  
ATOM   1344  O   ALA A1063      -4.910  29.623   9.629  1.00 44.47           O  
ANISOU 1344  O   ALA A1063     5113   7282   4501    871   -133   -629       O  
ATOM   1345  CB  ALA A1063      -1.924  29.555   8.618  1.00 43.03           C  
ANISOU 1345  CB  ALA A1063     4967   6853   4531    648   -260   -541       C  
ATOM   1346  N   GLU A1064      -4.008  27.726  10.448  1.00 45.42           N  
ANISOU 1346  N   GLU A1064     5197   7652   4409    884      0   -345       N  
ATOM   1347  CA  GLU A1064      -5.302  27.073  10.605  1.00 46.93           C  
ANISOU 1347  CA  GLU A1064     5368   7949   4516    913    136   -234       C  
ATOM   1348  C   GLU A1064      -6.060  27.629  11.805  1.00 50.62           C  
ANISOU 1348  C   GLU A1064     5764   8680   4791   1063    125   -393       C  
ATOM   1349  O   GLU A1064      -7.292  27.734  11.772  1.00 50.36           O  
ANISOU 1349  O   GLU A1064     5698   8700   4737   1092    191   -416       O  
ATOM   1350  CB  GLU A1064      -5.107  25.564  10.743  1.00 46.55           C  
ANISOU 1350  CB  GLU A1064     5325   7969   4393    883    263     37       C  
ATOM   1351  CG  GLU A1064      -6.393  24.794  10.951  1.00 47.38           C  
ANISOU 1351  CG  GLU A1064     5400   8183   4418    883    411    179       C  
ATOM   1352  CD  GLU A1064      -6.157  23.314  11.146  1.00 48.27           C  
ANISOU 1352  CD  GLU A1064     5531   8331   4479    848    523    455       C  
ATOM   1353  OE1 GLU A1064      -5.010  22.857  10.954  1.00 48.16           O  
ANISOU 1353  OE1 GLU A1064     5557   8228   4512    831    485    532       O  
ATOM   1354  OE2 GLU A1064      -7.124  22.607  11.494  1.00 49.46           O  
ANISOU 1354  OE2 GLU A1064     5649   8594   4549    837    647    597       O  
ATOM   1355  N   LYS A1065      -5.342  27.975  12.878  1.00 54.76           N  
ANISOU 1355  N   LYS A1065     6249   9394   5161   1166     42   -515       N  
ATOM   1356  CA  LYS A1065      -5.986  28.584  14.038  1.00 56.10           C  
ANISOU 1356  CA  LYS A1065     6344   9841   5130   1324     18   -707       C  
ATOM   1357  C   LYS A1065      -6.635  29.911  13.668  1.00 54.86           C  
ANISOU 1357  C   LYS A1065     6191   9546   5108   1361    -81   -974       C  
ATOM   1358  O   LYS A1065      -7.748  30.215  14.114  1.00 55.40           O  
ANISOU 1358  O   LYS A1065     6198   9774   5076   1467    -41  -1080       O  
ATOM   1359  CB  LYS A1065      -4.966  28.774  15.159  1.00 59.03           C  
ANISOU 1359  CB  LYS A1065     6675  10430   5323   1424    -80   -817       C  
ATOM   1360  CG  LYS A1065      -5.537  29.382  16.429  1.00 63.35           C  
ANISOU 1360  CG  LYS A1065     7136  11307   5628   1605   -110  -1039       C  
ATOM   1361  CD  LYS A1065      -4.466  29.510  17.499  1.00 66.37           C  
ANISOU 1361  CD  LYS A1065     7476  11920   5823   1701   -217  -1147       C  
ATOM   1362  CE  LYS A1065      -5.036  30.064  18.794  1.00 69.78           C  
ANISOU 1362  CE  LYS A1065     7812  12722   5978   1895   -243  -1380       C  
ATOM   1363  NZ  LYS A1065      -3.996  30.167  19.855  1.00 73.02           N  
ANISOU 1363  NZ  LYS A1065     8173  13388   6182   1996   -357  -1494       N  
ATOM   1364  N   LEU A1066      -5.957  30.712  12.844  1.00 53.95           N  
ANISOU 1364  N   LEU A1066     6143   9133   5223   1278   -211  -1079       N  
ATOM   1365  CA  LEU A1066      -6.552  31.955  12.369  1.00 54.50           C  
ANISOU 1365  CA  LEU A1066     6239   9012   5457   1306   -316  -1297       C  
ATOM   1366  C   LEU A1066      -7.652  31.697  11.348  1.00 51.66           C  
ANISOU 1366  C   LEU A1066     5902   8512   5214   1248   -221  -1168       C  
ATOM   1367  O   LEU A1066      -8.573  32.511  11.212  1.00 38.21           O  
ANISOU 1367  O   LEU A1066     4188   6759   3572   1329   -268  -1329       O  
ATOM   1368  CB  LEU A1066      -5.471  32.852  11.768  1.00 54.00           C  
ANISOU 1368  CB  LEU A1066     6243   8661   5612   1209   -479  -1407       C  
ATOM   1369  CG  LEU A1066      -4.328  33.250  12.702  1.00 40.10           C  
ANISOU 1369  CG  LEU A1066     4448   7017   3771   1250   -603  -1574       C  
ATOM   1370  CD1 LEU A1066      -3.250  34.005  11.940  1.00 39.79           C  
ANISOU 1370  CD1 LEU A1066     4466   6676   3977   1103   -741  -1630       C  
ATOM   1371  CD2 LEU A1066      -4.850  34.083  13.861  1.00 42.56           C  
ANISOU 1371  CD2 LEU A1066     4700   7529   3943   1441   -689  -1881       C  
ATOM   1372  N   PHE A1067      -7.577  30.576  10.624  1.00 47.81           N  
ANISOU 1372  N   PHE A1067     5441   7962   4764   1119    -98   -895       N  
ATOM   1373  CA  PHE A1067      -8.579  30.282   9.605  1.00 43.77           C  
ANISOU 1373  CA  PHE A1067     4944   7324   4363   1052    -17   -780       C  
ATOM   1374  C   PHE A1067      -9.901  29.842  10.219  1.00 43.34           C  
ANISOU 1374  C   PHE A1067     4794   7524   4149   1143    105   -764       C  
ATOM   1375  O   PHE A1067     -10.966  30.135   9.663  1.00 41.71           O  
ANISOU 1375  O   PHE A1067     4565   7264   4019   1157    120   -802       O  
ATOM   1376  CB  PHE A1067      -8.057  29.210   8.648  1.00 40.01           C  
ANISOU 1376  CB  PHE A1067     4520   6704   3976    890     67   -524       C  
ATOM   1377  CG  PHE A1067      -9.040  28.819   7.582  1.00 36.17           C  
ANISOU 1377  CG  PHE A1067     4043   6104   3595    813    146   -413       C  
ATOM   1378  CD1 PHE A1067      -9.340  29.688   6.547  1.00 33.98           C  
ANISOU 1378  CD1 PHE A1067     3813   5605   3490    782     59   -489       C  
ATOM   1379  CD2 PHE A1067      -9.658  27.581   7.611  1.00 34.22           C  
ANISOU 1379  CD2 PHE A1067     3756   5970   3277    769    299   -229       C  
ATOM   1380  CE1 PHE A1067     -10.243  29.332   5.564  1.00 32.10           C  
ANISOU 1380  CE1 PHE A1067     3574   5289   3333    721    119   -397       C  
ATOM   1381  CE2 PHE A1067     -10.560  27.219   6.630  1.00 32.32           C  
ANISOU 1381  CE2 PHE A1067     3511   5634   3136    692    360   -149       C  
ATOM   1382  CZ  PHE A1067     -10.853  28.095   5.606  1.00 31.41           C  
ANISOU 1382  CZ  PHE A1067     3434   5326   3173    675    269   -240       C  
ATOM   1383  N   ASN A1068      -9.858  29.138  11.354  1.00 44.63           N  
ANISOU 1383  N   ASN A1068     4891   7980   4085   1203    193   -697       N  
ATOM   1384  CA  ASN A1068     -11.092  28.732  12.019  1.00 45.85           C  
ANISOU 1384  CA  ASN A1068     4936   8416   4068   1277    321   -671       C  
ATOM   1385  C   ASN A1068     -11.905  29.936  12.473  1.00 47.08           C  
ANISOU 1385  C   ASN A1068     5023   8684   4183   1445    242   -966       C  
ATOM   1386  O   ASN A1068     -13.138  29.870  12.526  1.00 46.85           O  
ANISOU 1386  O   ASN A1068     4900   8800   4102   1493    327   -982       O  
ATOM   1387  CB  ASN A1068     -10.777  27.823  13.209  1.00 47.88           C  
ANISOU 1387  CB  ASN A1068     5143   8979   4072   1313    420   -529       C  
ATOM   1388  CG  ASN A1068     -10.191  26.488  12.788  1.00 47.09           C  
ANISOU 1388  CG  ASN A1068     5103   8772   4016   1166    514   -218       C  
ATOM   1389  OD1 ASN A1068     -10.385  26.041  11.657  1.00 46.21           O  
ANISOU 1389  OD1 ASN A1068     5041   8423   4094   1034    553    -95       O  
ATOM   1390  ND2 ASN A1068      -9.476  25.841  13.700  1.00 47.75           N  
ANISOU 1390  ND2 ASN A1068     5182   9037   3924   1201    544    -96       N  
ATOM   1391  N   GLN A1069     -11.235  31.042  12.806  1.00 48.69           N  
ANISOU 1391  N   GLN A1069     5262   8820   4418   1538     76  -1214       N  
ATOM   1392  CA  GLN A1069     -11.953  32.254  13.181  1.00 51.18           C  
ANISOU 1392  CA  GLN A1069     5524   9192   4728   1713    -24  -1526       C  
ATOM   1393  C   GLN A1069     -12.626  32.889  11.971  1.00 50.37           C  
ANISOU 1393  C   GLN A1069     5468   8795   4876   1686    -86  -1570       C  
ATOM   1394  O   GLN A1069     -13.723  33.449  12.084  1.00 51.39           O  
ANISOU 1394  O   GLN A1069     5521   9012   4992   1821    -95  -1732       O  
ATOM   1395  CB  GLN A1069     -10.997  33.244  13.848  1.00 53.53           C  
ANISOU 1395  CB  GLN A1069     5856   9464   5018   1806   -201  -1788       C  
ATOM   1396  CG  GLN A1069     -10.256  32.678  15.049  1.00 55.44           C  
ANISOU 1396  CG  GLN A1069     6050  10014   5000   1848   -165  -1758       C  
ATOM   1397  CD  GLN A1069      -9.281  33.670  15.653  1.00 57.56           C  
ANISOU 1397  CD  GLN A1069     6343  10253   5275   1928   -356  -2040       C  
ATOM   1398  OE1 GLN A1069      -9.173  34.808  15.196  1.00 58.61           O  
ANISOU 1398  OE1 GLN A1069     6533  10112   5623   1945   -516  -2260       O  
ATOM   1399  NE2 GLN A1069      -8.565  33.242  16.686  1.00 58.26           N  
ANISOU 1399  NE2 GLN A1069     6386  10617   5131   1975   -348  -2032       N  
ATOM   1400  N   ASP A1070     -11.983  32.809  10.803  1.00 49.24           N  
ANISOU 1400  N   ASP A1070     5441   8319   4948   1522   -129  -1426       N  
ATOM   1401  CA  ASP A1070     -12.582  33.349   9.588  1.00 49.81           C  
ANISOU 1401  CA  ASP A1070     5564   8123   5240   1490   -188  -1430       C  
ATOM   1402  C   ASP A1070     -13.776  32.519   9.134  1.00 51.18           C  
ANISOU 1402  C   ASP A1070     5658   8411   5378   1455    -38  -1274       C  
ATOM   1403  O   ASP A1070     -14.713  33.061   8.538  1.00 52.67           O  
ANISOU 1403  O   ASP A1070     5823   8519   5668   1515    -79  -1352       O  
ATOM   1404  CB  ASP A1070     -11.533  33.429   8.479  1.00 47.68           C  
ANISOU 1404  CB  ASP A1070     5427   7513   5175   1317   -261  -1301       C  
ATOM   1405  CG  ASP A1070     -10.402  34.383   8.816  1.00 48.61           C  
ANISOU 1405  CG  ASP A1070     5614   7488   5369   1329   -425  -1468       C  
ATOM   1406  OD1 ASP A1070     -10.546  35.156   9.786  1.00 50.66           O  
ANISOU 1406  OD1 ASP A1070     5831   7859   5557   1488   -511  -1722       O  
ATOM   1407  OD2 ASP A1070      -9.368  34.356   8.116  1.00 47.72           O  
ANISOU 1407  OD2 ASP A1070     5586   7161   5385   1176   -467  -1355       O  
ATOM   1408  N   VAL A1071     -13.762  31.212   9.401  1.00 52.11           N  
ANISOU 1408  N   VAL A1071     5728   8706   5363   1358    128  -1055       N  
ATOM   1409  CA  VAL A1071     -14.905  30.375   9.052  1.00 54.99           C  
ANISOU 1409  CA  VAL A1071     6003   9190   5700   1305    273   -912       C  
ATOM   1410  C   VAL A1071     -16.077  30.661   9.982  1.00 60.30           C  
ANISOU 1410  C   VAL A1071     6518  10187   6206   1471    326  -1068       C  
ATOM   1411  O   VAL A1071     -17.227  30.762   9.539  1.00 60.34           O  
ANISOU 1411  O   VAL A1071     6437  10233   6255   1501    356  -1101       O  
ATOM   1412  CB  VAL A1071     -14.509  28.888   9.078  1.00 54.75           C  
ANISOU 1412  CB  VAL A1071     5980   9219   5604   1143    426   -628       C  
ATOM   1413  CG1 VAL A1071     -15.703  28.012   8.728  1.00 55.62           C  
ANISOU 1413  CG1 VAL A1071     5991   9436   5706   1065    571   -488       C  
ATOM   1414  CG2 VAL A1071     -13.367  28.633   8.116  1.00 53.73           C  
ANISOU 1414  CG2 VAL A1071     5990   8788   5637   1001    372   -504       C  
ATOM   1415  N   ASP A1072     -15.807  30.799  11.284  1.00 64.74           N  
ANISOU 1415  N   ASP A1072     7027  11010   6563   1589    338  -1174       N  
ATOM   1416  CA  ASP A1072     -16.868  31.139  12.227  1.00 69.50           C  
ANISOU 1416  CA  ASP A1072     7466  11961   6981   1766    388  -1349       C  
ATOM   1417  C   ASP A1072     -17.504  32.479  11.879  1.00 70.52           C  
ANISOU 1417  C   ASP A1072     7581  11974   7241   1935    238  -1640       C  
ATOM   1418  O   ASP A1072     -18.723  32.648  12.003  1.00 72.80           O  
ANISOU 1418  O   ASP A1072     7727  12460   7475   2043    289  -1739       O  
ATOM   1419  CB  ASP A1072     -16.319  31.161  13.654  1.00 72.98           C  
ANISOU 1419  CB  ASP A1072     7864  12699   7165   1876    401  -1436       C  
ATOM   1420  CG  ASP A1072     -15.937  29.781  14.154  1.00 74.63           C  
ANISOU 1420  CG  ASP A1072     8061  13090   7208   1743    567  -1130       C  
ATOM   1421  OD1 ASP A1072     -16.051  28.813  13.374  1.00 73.79           O  
ANISOU 1421  OD1 ASP A1072     7986  12843   7208   1560    664   -864       O  
ATOM   1422  OD2 ASP A1072     -15.527  29.665  15.328  1.00 76.30           O  
ANISOU 1422  OD2 ASP A1072     8231  13580   7180   1829    591  -1157       O  
ATOM   1423  N   ALA A1073     -16.693  33.443  11.438  1.00 68.46           N  
ANISOU 1423  N   ALA A1073     7462  11390   7162   1960     50  -1776       N  
ATOM   1424  CA  ALA A1073     -17.239  34.727  11.016  1.00 67.02           C  
ANISOU 1424  CA  ALA A1073     7293  11029   7142   2115   -112  -2027       C  
ATOM   1425  C   ALA A1073     -17.994  34.609   9.699  1.00 65.96           C  
ANISOU 1425  C   ALA A1073     7169  10703   7189   2038   -105  -1898       C  
ATOM   1426  O   ALA A1073     -18.945  35.363   9.462  1.00 65.85           O  
ANISOU 1426  O   ALA A1073     7095  10678   7245   2193   -178  -2068       O  
ATOM   1427  CB  ALA A1073     -16.120  35.762  10.896  1.00 66.08           C  
ANISOU 1427  CB  ALA A1073     7330  10593   7186   2132   -317  -2178       C  
ATOM   1428  N   ALA A1074     -17.592  33.674   8.836  1.00 65.92           N  
ANISOU 1428  N   ALA A1074     7234  10556   7256   1814    -27  -1613       N  
ATOM   1429  CA  ALA A1074     -18.281  33.503   7.561  1.00 66.35           C  
ANISOU 1429  CA  ALA A1074     7293  10453   7463   1735    -23  -1494       C  
ATOM   1430  C   ALA A1074     -19.623  32.807   7.746  1.00 63.02           C  
ANISOU 1430  C   ALA A1074     6682  10340   6924   1756    129  -1455       C  
ATOM   1431  O   ALA A1074     -20.605  33.157   7.081  1.00 63.71           O  
ANISOU 1431  O   ALA A1074     6706  10403   7100   1820     90  -1512       O  
ATOM   1432  CB  ALA A1074     -17.399  32.722   6.587  1.00 66.02           C  
ANISOU 1432  CB  ALA A1074     7378  10182   7526   1499     10  -1233       C  
ATOM   1433  N   VAL A1075     -19.685  31.818   8.641  1.00 59.06           N  
ANISOU 1433  N   VAL A1075     6081  10136   6222   1697    301  -1347       N  
ATOM   1434  CA  VAL A1075     -20.945  31.127   8.902  1.00 58.41           C  
ANISOU 1434  CA  VAL A1075     5801  10369   6022   1690    460  -1295       C  
ATOM   1435  C   VAL A1075     -21.958  32.083   9.520  1.00 59.55           C  
ANISOU 1435  C   VAL A1075     5793  10747   6087   1943    415  -1579       C  
ATOM   1436  O   VAL A1075     -23.150  32.046   9.190  1.00 60.84           O  
ANISOU 1436  O   VAL A1075     5805  11046   6264   1982    457  -1614       O  
ATOM   1437  CB  VAL A1075     -20.705  29.895   9.796  1.00 58.41           C  
ANISOU 1437  CB  VAL A1075     5743  10625   5825   1567    650  -1092       C  
ATOM   1438  CG1 VAL A1075     -22.028  29.260  10.202  1.00 59.65           C  
ANISOU 1438  CG1 VAL A1075     5677  11139   5850   1554    821  -1042       C  
ATOM   1439  CG2 VAL A1075     -19.829  28.881   9.076  1.00 55.81           C  
ANISOU 1439  CG2 VAL A1075     5554  10052   5601   1332    693   -817       C  
ATOM   1440  N   ARG A1076     -21.502  32.957  10.421  1.00 60.17           N  
ANISOU 1440  N   ARG A1076     5897  10883   6083   2125    321  -1807       N  
ATOM   1441  CA  ARG A1076     -22.403  33.939  11.015  1.00 61.78           C  
ANISOU 1441  CA  ARG A1076     5978  11266   6228   2371    246  -2099       C  
ATOM   1442  C   ARG A1076     -22.950  34.893   9.961  1.00 61.38           C  
ANISOU 1442  C   ARG A1076     5949  10965   6406   2503     91  -2253       C  
ATOM   1443  O   ARG A1076     -24.122  35.285  10.016  1.00 64.48           O  
ANISOU 1443  O   ARG A1076     6227  11478   6794   2601     59  -2356       O  
ATOM   1444  CB  ARG A1076     -21.685  34.712  12.123  1.00 63.89           C  
ANISOU 1444  CB  ARG A1076     6308  11568   6400   2503    134  -2304       C  
ATOM   1445  CG  ARG A1076     -21.644  33.982  13.455  1.00 65.96           C  
ANISOU 1445  CG  ARG A1076     6486  12182   6394   2441    259  -2199       C  
ATOM   1446  CD  ARG A1076     -21.047  34.853  14.549  1.00 68.97           C  
ANISOU 1446  CD  ARG A1076     6899  12624   6683   2595    123  -2438       C  
ATOM   1447  NE  ARG A1076     -19.591  34.918  14.467  1.00 68.23           N  
ANISOU 1447  NE  ARG A1076     6963  12329   6634   2555     61  -2438       N  
ATOM   1448  CZ  ARG A1076     -18.773  34.099  15.120  1.00 68.48           C  
ANISOU 1448  CZ  ARG A1076     7014  12503   6501   2450    152  -2268       C  
ATOM   1449  NH1 ARG A1076     -19.269  33.152  15.906  1.00 70.07           N  
ANISOU 1449  NH1 ARG A1076     7101  13025   6498   2372    306  -2068       N  
ATOM   1450  NH2 ARG A1076     -17.460  34.226  14.990  1.00 66.99           N  
ANISOU 1450  NH2 ARG A1076     6963  12131   6359   2421     80  -2292       N  
ATOM   1451  N   GLY A1077     -22.119  35.276   8.990  1.00 57.79           N  
ANISOU 1451  N   GLY A1077     5704  10078   6174   2412    -53  -2178       N  
ATOM   1452  CA  GLY A1077     -22.604  36.111   7.906  1.00 57.96           C  
ANISOU 1452  CA  GLY A1077     5779   9824   6418   2496   -212  -2248       C  
ATOM   1453  C   GLY A1077     -23.588  35.397   7.002  1.00 58.50           C  
ANISOU 1453  C   GLY A1077     5739   9967   6520   2398   -121  -2082       C  
ATOM   1454  O   GLY A1077     -24.493  36.026   6.446  1.00 61.04           O  
ANISOU 1454  O   GLY A1077     5998  10253   6940   2544   -217  -2196       O  
ATOM   1455  N   ILE A1078     -23.431  34.081   6.842  1.00 56.63           N  
ANISOU 1455  N   ILE A1078     5477   9829   6210   2156     52  -1822       N  
ATOM   1456  CA  ILE A1078     -24.370  33.317   6.027  1.00 56.47           C  
ANISOU 1456  CA  ILE A1078     5339   9894   6222   2041    142  -1678       C  
ATOM   1457  C   ILE A1078     -25.701  33.162   6.755  1.00 60.65           C  
ANISOU 1457  C   ILE A1078     5598  10848   6600   2164    256  -1801       C  
ATOM   1458  O   ILE A1078     -26.774  33.335   6.165  1.00 60.74           O  
ANISOU 1458  O   ILE A1078     5478  10929   6670   2233    228  -1860       O  
ATOM   1459  CB  ILE A1078     -23.759  31.954   5.649  1.00 52.43           C  
ANISOU 1459  CB  ILE A1078     4890   9328   5702   1746    282  -1381       C  
ATOM   1460  CG1 ILE A1078     -22.600  32.141   4.665  1.00 49.39           C  
ANISOU 1460  CG1 ILE A1078     4744   8539   5483   1632    163  -1268       C  
ATOM   1461  CG2 ILE A1078     -24.814  31.032   5.057  1.00 52.14           C  
ANISOU 1461  CG2 ILE A1078     4696   9444   5672   1616    398  -1259       C  
ATOM   1462  CD1 ILE A1078     -21.950  30.841   4.230  1.00 46.43           C  
ANISOU 1462  CD1 ILE A1078     4436   8092   5113   1368    284  -1005       C  
ATOM   1463  N   LEU A1079     -25.652  32.846   8.052  1.00 63.90           N  
ANISOU 1463  N   LEU A1079     5922  11556   6803   2184    378  -1832       N  
ATOM   1464  CA  LEU A1079     -26.862  32.765   8.862  1.00 67.99           C  
ANISOU 1464  CA  LEU A1079     6271  12388   7175   2212    440  -1884       C  
ATOM   1465  C   LEU A1079     -27.562  34.111   9.008  1.00 72.61           C  
ANISOU 1465  C   LEU A1079     6826  12965   7798   2474    264  -2172       C  
ATOM   1466  O   LEU A1079     -28.775  34.139   9.234  1.00 74.00           O  
ANISOU 1466  O   LEU A1079     6842  13365   7909   2515    290  -2230       O  
ATOM   1467  CB  LEU A1079     -26.531  32.197  10.239  1.00 67.35           C  
ANISOU 1467  CB  LEU A1079     6170  12551   6871   2141    561  -1805       C  
ATOM   1468  CG  LEU A1079     -26.035  30.752  10.257  1.00 64.15           C  
ANISOU 1468  CG  LEU A1079     5782  12179   6411   1874    744  -1491       C  
ATOM   1469  CD1 LEU A1079     -25.594  30.344  11.656  1.00 64.83           C  
ANISOU 1469  CD1 LEU A1079     5874  12476   6283   1844    825  -1418       C  
ATOM   1470  CD2 LEU A1079     -27.117  29.814   9.740  1.00 63.64           C  
ANISOU 1470  CD2 LEU A1079     5577  12221   6384   1695    867  -1325       C  
ATOM   1471  N   ARG A1080     -26.836  35.221   8.882  1.00 75.67           N  
ANISOU 1471  N   ARG A1080     7364  13089   8299   2645     82  -2353       N  
ATOM   1472  CA  ARG A1080     -27.434  36.549   8.874  1.00 79.60           C  
ANISOU 1472  CA  ARG A1080     7866  13499   8881   2889   -111  -2616       C  
ATOM   1473  C   ARG A1080     -27.880  36.978   7.482  1.00 77.53           C  
ANISOU 1473  C   ARG A1080     7634  12985   8838   2947   -233  -2612       C  
ATOM   1474  O   ARG A1080     -28.186  38.157   7.280  1.00 79.90           O  
ANISOU 1474  O   ARG A1080     7991  13112   9257   3149   -425  -2803       O  
ATOM   1475  CB  ARG A1080     -26.455  37.582   9.443  1.00 83.04           C  
ANISOU 1475  CB  ARG A1080     8460  13734   9357   3033   -271  -2813       C  
ATOM   1476  CG  ARG A1080     -26.741  38.014  10.877  1.00 88.80           C  
ANISOU 1476  CG  ARG A1080     9106  14736   9895   3152   -283  -3005       C  
ATOM   1477  CD  ARG A1080     -25.757  37.400  11.866  1.00 90.79           C  
ANISOU 1477  CD  ARG A1080     9389  15134   9973   3044   -179  -2925       C  
ATOM   1478  NE  ARG A1080     -25.913  35.953  11.986  1.00 92.61           N  
ANISOU 1478  NE  ARG A1080     9523  15609  10055   2823     54  -2640       N  
ATOM   1479  CZ  ARG A1080     -25.301  35.211  12.904  1.00 94.79           C  
ANISOU 1479  CZ  ARG A1080     9795  16076  10146   2714    173  -2514       C  
ATOM   1480  NH1 ARG A1080     -25.499  33.901  12.943  1.00 94.64           N  
ANISOU 1480  NH1 ARG A1080     9703  16230  10025   2504    372  -2234       N  
ATOM   1481  NH2 ARG A1080     -24.492  35.782  13.787  1.00 96.98           N  
ANISOU 1481  NH2 ARG A1080    10141  16357  10348   2812     83  -2665       N  
ATOM   1482  N   ASN A1081     -27.921  36.054   6.523  1.00 73.42           N  
ANISOU 1482  N   ASN A1081     7081  12439   8377   2774   -137  -2393       N  
ATOM   1483  CA  ASN A1081     -28.305  36.346   5.149  1.00 71.57           C  
ANISOU 1483  CA  ASN A1081     6867  11992   8335   2814   -255  -2358       C  
ATOM   1484  C   ASN A1081     -29.563  35.562   4.807  1.00 72.05           C  
ANISOU 1484  C   ASN A1081     6721  12320   8335   2712   -140  -2269       C  
ATOM   1485  O   ASN A1081     -29.595  34.337   4.960  1.00 72.09           O  
ANISOU 1485  O   ASN A1081     6632  12516   8242   2488     53  -2091       O  
ATOM   1486  CB  ASN A1081     -27.176  35.994   4.177  1.00 68.71           C  
ANISOU 1486  CB  ASN A1081     6703  11296   8109   2633   -286  -2144       C  
ATOM   1487  CG  ASN A1081     -27.464  36.443   2.761  1.00 69.62           C  
ANISOU 1487  CG  ASN A1081     6900  11143   8409   2652   -446  -2079       C  
ATOM   1488  OD1 ASN A1081     -28.119  35.737   1.995  1.00 69.75           O  
ANISOU 1488  OD1 ASN A1081     6814  11258   8429   2536   -386  -1953       O  
ATOM   1489  ND2 ASN A1081     -26.971  37.623   2.403  1.00 70.73           N  
ANISOU 1489  ND2 ASN A1081     7227  10942   8706   2793   -656  -2159       N  
ATOM   1490  N   ALA A1082     -30.595  36.267   4.337  1.00 72.84           N  
ANISOU 1490  N   ALA A1082     6757  12418   8502   2868   -265  -2390       N  
ATOM   1491  CA  ALA A1082     -31.882  35.622   4.100  1.00 73.00           C  
ANISOU 1491  CA  ALA A1082     6564  12713   8459   2788   -171  -2344       C  
ATOM   1492  C   ALA A1082     -31.842  34.673   2.908  1.00 69.92           C  
ANISOU 1492  C   ALA A1082     6142  12268   8158   2587   -116  -2135       C  
ATOM   1493  O   ALA A1082     -32.635  33.726   2.848  1.00 70.67           O  
ANISOU 1493  O   ALA A1082     6064  12601   8185   2418     22  -2043       O  
ATOM   1494  CB  ALA A1082     -32.968  36.679   3.898  1.00 75.45           C  
ANISOU 1494  CB  ALA A1082     6816  13037   8814   3026   -332  -2541       C  
ATOM   1495  N   LYS A1083     -30.938  34.903   1.956  1.00 66.69           N  
ANISOU 1495  N   LYS A1083     5893  11547   7901   2594   -229  -2060       N  
ATOM   1496  CA  LYS A1083     -30.885  34.085   0.751  1.00 63.94           C  
ANISOU 1496  CA  LYS A1083     5548  11117   7629   2391   -210  -1863       C  
ATOM   1497  C   LYS A1083     -30.043  32.828   0.922  1.00 60.81           C  
ANISOU 1497  C   LYS A1083     5232  10697   7177   2069    -30  -1641       C  
ATOM   1498  O   LYS A1083     -30.331  31.808   0.286  1.00 59.41           O  
ANISOU 1498  O   LYS A1083     4985  10577   7011   1851     57  -1496       O  
ATOM   1499  CB  LYS A1083     -30.337  34.905  -0.420  1.00 62.82           C  
ANISOU 1499  CB  LYS A1083     5644  10574   7650   2451   -430  -1808       C  
ATOM   1500  CG  LYS A1083     -31.152  36.145  -0.744  1.00 65.43           C  
ANISOU 1500  CG  LYS A1083     5924  10872   8065   2773   -634  -1994       C  
ATOM   1501  CD  LYS A1083     -30.477  36.979  -1.819  1.00 65.10           C  
ANISOU 1501  CD  LYS A1083     6147  10407   8180   2816   -848  -1898       C  
ATOM   1502  CE  LYS A1083     -31.261  38.246  -2.112  1.00 68.20           C  
ANISOU 1502  CE  LYS A1083     6509  10731   8674   3155  -1067  -2067       C  
ATOM   1503  NZ  LYS A1083     -30.561  39.111  -3.102  1.00 68.01           N  
ANISOU 1503  NZ  LYS A1083     6759  10276   8805   3191  -1276  -1944       N  
ATOM   1504  N   LEU A1084     -29.011  32.877   1.764  1.00 59.66           N  
ANISOU 1504  N   LEU A1084     5227  10465   6977   2044     16  -1621       N  
ATOM   1505  CA  LEU A1084     -28.114  31.746   1.954  1.00 56.40           C  
ANISOU 1505  CA  LEU A1084     4908  10004   6517   1770    166  -1410       C  
ATOM   1506  C   LEU A1084     -28.444  30.909   3.182  1.00 55.43           C  
ANISOU 1506  C   LEU A1084     4608  10231   6223   1695    380  -1388       C  
ATOM   1507  O   LEU A1084     -27.936  29.789   3.299  1.00 53.82           O  
ANISOU 1507  O   LEU A1084     4443  10019   5985   1456    520  -1190       O  
ATOM   1508  CB  LEU A1084     -26.664  32.235   2.061  1.00 55.80           C  
ANISOU 1508  CB  LEU A1084     5101   9615   6486   1766     82  -1371       C  
ATOM   1509  CG  LEU A1084     -26.155  33.125   0.924  1.00 55.51           C  
ANISOU 1509  CG  LEU A1084     5264   9213   6614   1821   -124  -1361       C  
ATOM   1510  CD1 LEU A1084     -24.744  33.615   1.212  1.00 54.84           C  
ANISOU 1510  CD1 LEU A1084     5408   8863   6567   1806   -190  -1337       C  
ATOM   1511  CD2 LEU A1084     -26.208  32.385  -0.403  1.00 53.83           C  
ANISOU 1511  CD2 LEU A1084     5084   8895   6474   1626   -118  -1180       C  
ATOM   1512  N   LYS A1085     -29.280  31.419   4.093  1.00 56.61           N  
ANISOU 1512  N   LYS A1085     4561  10689   6260   1898    409  -1582       N  
ATOM   1513  CA  LYS A1085     -29.551  30.680   5.326  1.00 58.61           C  
ANISOU 1513  CA  LYS A1085     4731  11207   6331   1776    585  -1507       C  
ATOM   1514  C   LYS A1085     -30.330  29.393   5.078  1.00 61.45           C  
ANISOU 1514  C   LYS A1085     4948  11718   6682   1516    739  -1323       C  
ATOM   1515  O   LYS A1085     -29.939  28.348   5.629  1.00 62.12           O  
ANISOU 1515  O   LYS A1085     5052  11857   6694   1310    895  -1130       O  
ATOM   1516  CB  LYS A1085     -30.262  31.588   6.334  1.00 59.85           C  
ANISOU 1516  CB  LYS A1085     4819  11552   6371   1990    527  -1719       C  
ATOM   1517  CG  LYS A1085     -30.334  31.017   7.738  1.00 60.75           C  
ANISOU 1517  CG  LYS A1085     4872  11933   6278   1908    677  -1654       C  
ATOM   1518  CD  LYS A1085     -31.089  31.948   8.667  1.00 63.94           C  
ANISOU 1518  CD  LYS A1085     5186  12548   6562   2130    608  -1885       C  
ATOM   1519  CE  LYS A1085     -31.057  31.438  10.095  1.00 65.75           C  
ANISOU 1519  CE  LYS A1085     5359  13053   6570   2066    741  -1818       C  
ATOM   1520  NZ  LYS A1085     -31.562  30.041  10.189  1.00 66.14           N  
ANISOU 1520  NZ  LYS A1085     5297  13265   6570   1795    936  -1561       N  
ATOM   1521  N   PRO A1086     -31.420  29.378   4.296  1.00 64.44           N  
ANISOU 1521  N   PRO A1086     5190  12156   7138   1508    698  -1366       N  
ATOM   1522  CA  PRO A1086     -32.136  28.104   4.104  1.00 65.77           C  
ANISOU 1522  CA  PRO A1086     5226  12451   7314   1238    843  -1199       C  
ATOM   1523  C   PRO A1086     -31.308  27.044   3.397  1.00 63.42           C  
ANISOU 1523  C   PRO A1086     5019  11964   7113    989    914   -990       C  
ATOM   1524  O   PRO A1086     -31.382  25.864   3.761  1.00 63.13           O  
ANISOU 1524  O   PRO A1086     4955  11978   7054    746   1067   -806       O  
ATOM   1525  CB  PRO A1086     -33.363  28.513   3.275  1.00 67.53           C  
ANISOU 1525  CB  PRO A1086     5297  12750   7612   1322    740  -1330       C  
ATOM   1526  CG  PRO A1086     -33.529  29.969   3.529  1.00 68.79           C  
ANISOU 1526  CG  PRO A1086     5485  12908   7745   1647    581  -1562       C  
ATOM   1527  CD  PRO A1086     -32.139  30.496   3.659  1.00 66.10           C  
ANISOU 1527  CD  PRO A1086     5354  12334   7426   1744    517  -1570       C  
ATOM   1528  N   VAL A1087     -30.517  27.432   2.395  1.00 61.83           N  
ANISOU 1528  N   VAL A1087     4934  11530   7027   1044    799  -1010       N  
ATOM   1529  CA  VAL A1087     -29.716  26.456   1.664  1.00 62.17           C  
ANISOU 1529  CA  VAL A1087     5149  11304   7170    787    824   -807       C  
ATOM   1530  C   VAL A1087     -28.619  25.886   2.557  1.00 62.57           C  
ANISOU 1530  C   VAL A1087     5344  11286   7144    686    938   -654       C  
ATOM   1531  O   VAL A1087     -28.270  24.704   2.456  1.00 61.70           O  
ANISOU 1531  O   VAL A1087     5276  11097   7071    446   1047   -465       O  
ATOM   1532  CB  VAL A1087     -29.135  27.093   0.388  1.00 60.60           C  
ANISOU 1532  CB  VAL A1087     5154  10770   7103    847    626   -834       C  
ATOM   1533  CG1 VAL A1087     -28.628  26.019  -0.564  1.00 58.86           C  
ANISOU 1533  CG1 VAL A1087     5042  10340   6983    588    652   -666       C  
ATOM   1534  CG2 VAL A1087     -30.180  27.969  -0.287  1.00 62.71           C  
ANISOU 1534  CG2 VAL A1087     5289  11123   7414   1033    483  -1005       C  
ATOM   1535  N   TYR A1088     -28.066  26.712   3.448  1.00 65.26           N  
ANISOU 1535  N   TYR A1088     5760  11655   7383    875    904   -743       N  
ATOM   1536  CA  TYR A1088     -27.005  26.248   4.337  1.00 66.76           C  
ANISOU 1536  CA  TYR A1088     6078  11806   7482    805    994   -611       C  
ATOM   1537  C   TYR A1088     -27.516  25.230   5.349  1.00 69.71           C  
ANISOU 1537  C   TYR A1088     6298  12464   7726    666   1200   -474       C  
ATOM   1538  O   TYR A1088     -26.768  24.333   5.754  1.00 69.23           O  
ANISOU 1538  O   TYR A1088     6337  12330   7637    510   1296   -275       O  
ATOM   1539  CB  TYR A1088     -26.368  27.441   5.053  1.00 68.52           C  
ANISOU 1539  CB  TYR A1088     6400  12011   7625   1048    891   -773       C  
ATOM   1540  CG  TYR A1088     -25.273  27.072   6.030  1.00 69.39           C  
ANISOU 1540  CG  TYR A1088     6627  12117   7619   1007    964   -665       C  
ATOM   1541  CD1 TYR A1088     -23.966  26.889   5.600  1.00 68.39           C  
ANISOU 1541  CD1 TYR A1088     6733  11674   7578    918    903   -554       C  
ATOM   1542  CD2 TYR A1088     -25.546  26.916   7.382  1.00 72.25           C  
ANISOU 1542  CD2 TYR A1088     6859  12819   7775   1066   1093   -675       C  
ATOM   1543  CE1 TYR A1088     -22.961  26.554   6.489  1.00 69.01           C  
ANISOU 1543  CE1 TYR A1088     6907  11764   7549    894    957   -460       C  
ATOM   1544  CE2 TYR A1088     -24.550  26.581   8.279  1.00 73.05           C  
ANISOU 1544  CE2 TYR A1088     7071  12926   7758   1038   1143   -568       C  
ATOM   1545  CZ  TYR A1088     -23.259  26.402   7.827  1.00 71.56           C  
ANISOU 1545  CZ  TYR A1088     7104  12422   7664    959   1075   -466       C  
ATOM   1546  OH  TYR A1088     -22.265  26.069   8.718  1.00 72.51           O  
ANISOU 1546  OH  TYR A1088     7316  12574   7661    948   1120   -368       O  
ATOM   1547  N   ASP A1089     -28.780  25.348   5.765  1.00 72.78           N  
ANISOU 1547  N   ASP A1089     6521  13070   8061    700   1221   -551       N  
ATOM   1548  CA  ASP A1089     -29.318  24.435   6.768  1.00 74.42           C  
ANISOU 1548  CA  ASP A1089     6655  13455   8168    551   1368   -400       C  
ATOM   1549  C   ASP A1089     -29.602  23.054   6.190  1.00 73.08           C  
ANISOU 1549  C   ASP A1089     6459  13183   8124    255   1471   -190       C  
ATOM   1550  O   ASP A1089     -29.515  22.054   6.912  1.00 74.39           O  
ANISOU 1550  O   ASP A1089     6648  13369   8249     90   1597      9       O  
ATOM   1551  CB  ASP A1089     -30.590  25.023   7.379  1.00 78.50           C  
ANISOU 1551  CB  ASP A1089     6988  14255   8582    683   1359   -558       C  
ATOM   1552  CG  ASP A1089     -30.360  26.386   8.001  1.00 79.68           C  
ANISOU 1552  CG  ASP A1089     7167  14488   8618    980   1244   -788       C  
ATOM   1553  OD1 ASP A1089     -29.210  26.872   7.958  1.00 79.30           O  
ANISOU 1553  OD1 ASP A1089     7280  14273   8578   1076   1172   -825       O  
ATOM   1554  OD2 ASP A1089     -31.327  26.971   8.532  1.00 82.56           O  
ANISOU 1554  OD2 ASP A1089     7393  15082   8892   1116   1221   -942       O  
ATOM   1555  N   SER A1090     -29.940  22.974   4.902  1.00 69.54           N  
ANISOU 1555  N   SER A1090     5966  12619   7836    189   1410   -237       N  
ATOM   1556  CA  SER A1090     -30.312  21.696   4.307  1.00 70.43           C  
ANISOU 1556  CA  SER A1090     6042  12633   8086    -90   1488    -79       C  
ATOM   1557  C   SER A1090     -29.100  20.848   3.944  1.00 66.12           C  
ANISOU 1557  C   SER A1090     5682  11814   7628   -251   1521    101       C  
ATOM   1558  O   SER A1090     -29.191  19.615   3.941  1.00 46.99           O  
ANISOU 1558  O   SER A1090     3274   9288   5292   -485   1615    277       O  
ATOM   1559  CB  SER A1090     -31.173  21.930   3.065  1.00 74.27           C  
ANISOU 1559  CB  SER A1090     6398  13122   8698    -96   1394   -218       C  
ATOM   1560  OG  SER A1090     -30.472  22.698   2.103  1.00 76.75           O  
ANISOU 1560  OG  SER A1090     6799  13292   9071     35   1257   -328       O  
ATOM   1561  N   LEU A1091     -27.969  21.478   3.645  1.00 62.28           N  
ANISOU 1561  N   LEU A1091     5336  11197   7129   -128   1442     57       N  
ATOM   1562  CA  LEU A1091     -26.794  20.757   3.180  1.00 58.98           C  
ANISOU 1562  CA  LEU A1091     5112  10495   6802   -262   1445    207       C  
ATOM   1563  C   LEU A1091     -26.079  20.063   4.334  1.00 57.98           C  
ANISOU 1563  C   LEU A1091     5084  10363   6582   -322   1558    404       C  
ATOM   1564  O   LEU A1091     -26.143  20.496   5.488  1.00 58.43           O  
ANISOU 1564  O   LEU A1091     5124  10598   6478   -194   1586    386       O  
ATOM   1565  CB  LEU A1091     -25.832  21.709   2.469  1.00 55.18           C  
ANISOU 1565  CB  LEU A1091     4838   9762   6366   -102   1264     92       C  
ATOM   1566  CG  LEU A1091     -26.367  22.368   1.196  1.00 51.92           C  
ANISOU 1566  CG  LEU A1091     4399   9270   6058    -40   1116    -68       C  
ATOM   1567  CD1 LEU A1091     -25.394  23.416   0.683  1.00 49.38           C  
ANISOU 1567  CD1 LEU A1091     4280   8725   5758    123    950   -153       C  
ATOM   1568  CD2 LEU A1091     -26.638  21.321   0.130  1.00 50.47           C  
ANISOU 1568  CD2 LEU A1091     4199   8953   6024   -262   1128     -1       C  
ATOM   1569  N   ASP A1092     -25.390  18.971   4.003  1.00 55.44           N  
ANISOU 1569  N   ASP A1092     4886   9808   6370   -505   1601    584       N  
ATOM   1570  CA  ASP A1092     -24.590  18.228   4.964  1.00 55.44           C  
ANISOU 1570  CA  ASP A1092     5022   9730   6312   -554   1677    783       C  
ATOM   1571  C   ASP A1092     -23.295  18.983   5.262  1.00 53.97           C  
ANISOU 1571  C   ASP A1092     4974   9512   6019   -379   1613    755       C  
ATOM   1572  O   ASP A1092     -23.069  20.097   4.784  1.00 52.83           O  
ANISOU 1572  O   ASP A1092     4880   9314   5880   -216   1475    560       O  
ATOM   1573  CB  ASP A1092     -24.307  16.821   4.439  1.00 56.65           C  
ANISOU 1573  CB  ASP A1092     5264   9615   6646   -788   1724    962       C  
ATOM   1574  CG  ASP A1092     -23.889  16.813   2.979  1.00 56.55           C  
ANISOU 1574  CG  ASP A1092     5315   9375   6795   -839   1628    882       C  
ATOM   1575  OD1 ASP A1092     -24.633  17.364   2.140  1.00 57.11           O  
ANISOU 1575  OD1 ASP A1092     5291   9489   6920   -813   1550    707       O  
ATOM   1576  OD2 ASP A1092     -22.814  16.258   2.669  1.00 56.19           O  
ANISOU 1576  OD2 ASP A1092     5454   9062   6832   -878   1596    968       O  
ATOM   1577  N   ALA A1093     -22.421  18.363   6.061  1.00 53.86           N  
ANISOU 1577  N   ALA A1093     5092   9424   5950   -400   1658    927       N  
ATOM   1578  CA  ALA A1093     -21.192  19.037   6.472  1.00 52.16           C  
ANISOU 1578  CA  ALA A1093     5006   9184   5627   -234   1589    894       C  
ATOM   1579  C   ALA A1093     -20.255  19.268   5.292  1.00 49.12           C  
ANISOU 1579  C   ALA A1093     4796   8464   5403   -224   1446    815       C  
ATOM   1580  O   ALA A1093     -19.614  20.322   5.199  1.00 47.21           O  
ANISOU 1580  O   ALA A1093     4633   8177   5127    -69   1326    667       O  
ATOM   1581  CB  ALA A1093     -20.487  18.229   7.562  1.00 53.19           C  
ANISOU 1581  CB  ALA A1093     5234   9309   5668   -260   1653   1100       C  
ATOM   1582  N   VAL A1094     -20.165  18.301   4.378  1.00 48.20           N  
ANISOU 1582  N   VAL A1094     4735   8116   5463   -393   1457    905       N  
ATOM   1583  CA  VAL A1094     -19.234  18.423   3.260  1.00 44.49           C  
ANISOU 1583  CA  VAL A1094     4420   7360   5123   -388   1338    841       C  
ATOM   1584  C   VAL A1094     -19.698  19.506   2.293  1.00 42.32           C  
ANISOU 1584  C   VAL A1094     4113   7073   4893   -310   1218    631       C  
ATOM   1585  O   VAL A1094     -18.913  20.366   1.875  1.00 41.25           O  
ANISOU 1585  O   VAL A1094     4086   6828   4762   -203   1101    533       O  
ATOM   1586  CB  VAL A1094     -19.066  17.069   2.550  1.00 43.94           C  
ANISOU 1586  CB  VAL A1094     4408   7063   5225   -575   1380    967       C  
ATOM   1587  CG1 VAL A1094     -18.116  17.207   1.372  1.00 41.07           C  
ANISOU 1587  CG1 VAL A1094     4186   6448   4971   -558   1265    884       C  
ATOM   1588  CG2 VAL A1094     -18.563  16.018   3.528  1.00 44.89           C  
ANISOU 1588  CG2 VAL A1094     4577   7166   5312   -635   1485   1197       C  
ATOM   1589  N   ARG A1095     -20.979  19.485   1.923  1.00 42.51           N  
ANISOU 1589  N   ARG A1095     3985   7213   4955   -366   1242    568       N  
ATOM   1590  CA  ARG A1095     -21.485  20.466   0.971  1.00 41.50           C  
ANISOU 1590  CA  ARG A1095     3822   7076   4868   -282   1120    385       C  
ATOM   1591  C   ARG A1095     -21.573  21.866   1.565  1.00 42.49           C  
ANISOU 1591  C   ARG A1095     3923   7345   4877    -66   1046    244       C  
ATOM   1592  O   ARG A1095     -21.589  22.843   0.809  1.00 41.98           O  
ANISOU 1592  O   ARG A1095     3895   7203   4853     37    913    111       O  
ATOM   1593  CB  ARG A1095     -22.850  20.031   0.441  1.00 41.61           C  
ANISOU 1593  CB  ARG A1095     3660   7197   4951   -392   1157    349       C  
ATOM   1594  CG  ARG A1095     -22.784  18.839  -0.495  1.00 40.92           C  
ANISOU 1594  CG  ARG A1095     3610   6919   5019   -594   1177    421       C  
ATOM   1595  CD  ARG A1095     -24.132  18.560  -1.123  1.00 42.08           C  
ANISOU 1595  CD  ARG A1095     3573   7176   5239   -697   1184    345       C  
ATOM   1596  NE  ARG A1095     -24.072  17.464  -2.084  1.00 41.57           N  
ANISOU 1596  NE  ARG A1095     3544   6921   5331   -885   1183    374       N  
ATOM   1597  CZ  ARG A1095     -24.234  16.184  -1.766  1.00 42.01           C  
ANISOU 1597  CZ  ARG A1095     3568   6918   5476  -1081   1296    506       C  
ATOM   1598  NH1 ARG A1095     -24.463  15.836  -0.507  1.00 42.97           N  
ANISOU 1598  NH1 ARG A1095     3621   7177   5528  -1121   1429    651       N  
ATOM   1599  NH2 ARG A1095     -24.164  15.252  -2.706  1.00 41.51           N  
ANISOU 1599  NH2 ARG A1095     3544   6660   5570  -1236   1274    494       N  
ATOM   1600  N   ARG A1096     -21.634  21.989   2.893  1.00 44.40           N  
ANISOU 1600  N   ARG A1096     4105   7792   4974      9   1124    268       N  
ATOM   1601  CA  ARG A1096     -21.559  23.312   3.503  1.00 44.98           C  
ANISOU 1601  CA  ARG A1096     4172   7976   4940    226   1041    106       C  
ATOM   1602  C   ARG A1096     -20.189  23.940   3.291  1.00 44.07           C  
ANISOU 1602  C   ARG A1096     4253   7638   4854    300    922     76       C  
ATOM   1603  O   ARG A1096     -20.083  25.163   3.142  1.00 44.11           O  
ANISOU 1603  O   ARG A1096     4294   7600   4865    450    793    -83       O  
ATOM   1604  CB  ARG A1096     -21.884  23.231   4.994  1.00 46.11           C  
ANISOU 1604  CB  ARG A1096     4201   8421   4897    290   1157    131       C  
ATOM   1605  CG  ARG A1096     -23.371  23.159   5.306  1.00 47.66           C  
ANISOU 1605  CG  ARG A1096     4162   8911   5035    289   1248     83       C  
ATOM   1606  CD  ARG A1096     -23.618  23.034   6.799  1.00 49.67           C  
ANISOU 1606  CD  ARG A1096     4301   9496   5076    346   1377    125       C  
ATOM   1607  NE  ARG A1096     -25.039  22.902   7.107  1.00 52.49           N  
ANISOU 1607  NE  ARG A1096     4455  10098   5392    322   1450     90       N  
ATOM   1608  CZ  ARG A1096     -25.532  22.829   8.339  1.00 56.05           C  
ANISOU 1608  CZ  ARG A1096     4838  10770   5690    358   1512    110       C  
ATOM   1609  NH1 ARG A1096     -24.718  22.878   9.384  1.00 57.62           N  
ANISOU 1609  NH1 ARG A1096     5127  11024   5741    429   1523    161       N  
ATOM   1610  NH2 ARG A1096     -26.839  22.709   8.526  1.00 58.24           N  
ANISOU 1610  NH2 ARG A1096     4946  11230   5951    323   1559     76       N  
ATOM   1611  N   ALA A1097     -19.134  23.122   3.264  1.00 43.36           N  
ANISOU 1611  N   ALA A1097     4286   7398   4792    193    958    225       N  
ATOM   1612  CA  ALA A1097     -17.795  23.643   3.014  1.00 42.42           C  
ANISOU 1612  CA  ALA A1097     4331   7083   4704    242    853    203       C  
ATOM   1613  C   ALA A1097     -17.666  24.177   1.594  1.00 40.95           C  
ANISOU 1613  C   ALA A1097     4218   6685   4654    225    733    136       C  
ATOM   1614  O   ALA A1097     -17.011  25.201   1.367  1.00 39.95           O  
ANISOU 1614  O   ALA A1097     4181   6448   4549    312    613     49       O  
ATOM   1615  CB  ALA A1097     -16.753  22.556   3.276  1.00 42.13           C  
ANISOU 1615  CB  ALA A1097     4386   6956   4667    141    922    378       C  
ATOM   1616  N   ALA A1098     -18.280  23.494   0.625  1.00 41.49           N  
ANISOU 1616  N   ALA A1098     4249   6703   4814    105    761    178       N  
ATOM   1617  CA  ALA A1098     -18.264  23.978  -0.751  1.00 40.79           C  
ANISOU 1617  CA  ALA A1098     4216   6457   4824     95    650    121       C  
ATOM   1618  C   ALA A1098     -19.008  25.299  -0.890  1.00 42.83           C  
ANISOU 1618  C   ALA A1098     4425   6773   5075    247    539    -28       C  
ATOM   1619  O   ALA A1098     -18.618  26.145  -1.702  1.00 41.74           O  
ANISOU 1619  O   ALA A1098     4379   6488   4993    295    414    -71       O  
ATOM   1620  CB  ALA A1098     -18.864  22.929  -1.686  1.00 40.30           C  
ANISOU 1620  CB  ALA A1098     4103   6366   4844    -56    701    173       C  
ATOM   1621  N   LEU A1099     -20.077  25.494  -0.115  1.00 46.70           N  
ANISOU 1621  N   LEU A1099     4767   7479   5498    328    581   -102       N  
ATOM   1622  CA  LEU A1099     -20.771  26.777  -0.133  1.00 47.01           C  
ANISOU 1622  CA  LEU A1099     4755   7573   5533    507    468   -263       C  
ATOM   1623  C   LEU A1099     -19.916  27.869   0.495  1.00 45.77           C  
ANISOU 1623  C   LEU A1099     4705   7335   5349    647    374   -346       C  
ATOM   1624  O   LEU A1099     -19.868  28.996  -0.012  1.00 46.82           O  
ANISOU 1624  O   LEU A1099     4903   7339   5549    757    227   -438       O  
ATOM   1625  CB  LEU A1099     -22.112  26.659   0.591  1.00 49.79           C  
ANISOU 1625  CB  LEU A1099     4899   8210   5809    566    548   -336       C  
ATOM   1626  CG  LEU A1099     -23.040  27.875   0.524  1.00 51.24           C  
ANISOU 1626  CG  LEU A1099     4994   8480   5996    770    433   -521       C  
ATOM   1627  CD1 LEU A1099     -23.444  28.163  -0.913  1.00 50.85           C  
ANISOU 1627  CD1 LEU A1099     4965   8297   6058    761    317   -532       C  
ATOM   1628  CD2 LEU A1099     -24.267  27.661   1.396  1.00 52.86           C  
ANISOU 1628  CD2 LEU A1099     4969   9015   6101    826    539   -593       C  
ATOM   1629  N   ILE A1100     -19.231  27.551   1.597  1.00 44.65           N  
ANISOU 1629  N   ILE A1100     4584   7265   5116    644    448   -312       N  
ATOM   1630  CA  ILE A1100     -18.329  28.512   2.222  1.00 43.33           C  
ANISOU 1630  CA  ILE A1100     4513   7025   4926    759    354   -404       C  
ATOM   1631  C   ILE A1100     -17.139  28.802   1.315  1.00 40.99           C  
ANISOU 1631  C   ILE A1100     4386   6450   4740    684    258   -343       C  
ATOM   1632  O   ILE A1100     -16.627  29.929   1.292  1.00 40.56           O  
ANISOU 1632  O   ILE A1100     4415   6259   4736    772    127   -439       O  
ATOM   1633  CB  ILE A1100     -17.886  27.995   3.605  1.00 43.54           C  
ANISOU 1633  CB  ILE A1100     4507   7231   4805    769    458   -372       C  
ATOM   1634  CG1 ILE A1100     -19.097  27.836   4.529  1.00 45.62           C  
ANISOU 1634  CG1 ILE A1100     4588   7808   4937    850    557   -435       C  
ATOM   1635  CG2 ILE A1100     -16.863  28.928   4.233  1.00 43.81           C  
ANISOU 1635  CG2 ILE A1100     4636   7192   4817    873    352   -482       C  
ATOM   1636  CD1 ILE A1100     -18.782  27.158   5.846  1.00 35.16           C  
ANISOU 1636  CD1 ILE A1100     3218   6701   3440    842    682   -359       C  
ATOM   1637  N   ASN A1101     -16.684  27.803   0.552  1.00 39.42           N  
ANISOU 1637  N   ASN A1101     4234   6161   4584    520    322   -189       N  
ATOM   1638  CA  ASN A1101     -15.606  28.029  -0.407  1.00 38.01           C  
ANISOU 1638  CA  ASN A1101     4192   5755   4493    443    246   -128       C  
ATOM   1639  C   ASN A1101     -15.990  29.105  -1.417  1.00 37.81           C  
ANISOU 1639  C   ASN A1101     4207   5600   4558    500    107   -187       C  
ATOM   1640  O   ASN A1101     -15.168  29.960  -1.769  1.00 36.16           O  
ANISOU 1640  O   ASN A1101     4107   5221   4412    508      1   -194       O  
ATOM   1641  CB  ASN A1101     -15.259  26.715  -1.114  1.00 36.42           C  
ANISOU 1641  CB  ASN A1101     4010   5513   4317    279    341     18       C  
ATOM   1642  CG  ASN A1101     -13.952  26.786  -1.893  1.00 34.44           C  
ANISOU 1642  CG  ASN A1101     3881   5081   4122    201    293     84       C  
ATOM   1643  OD1 ASN A1101     -13.689  27.750  -2.610  1.00 34.34           O  
ANISOU 1643  OD1 ASN A1101     3935   4947   4166    221    182     56       O  
ATOM   1644  ND2 ASN A1101     -13.129  25.753  -1.755  1.00 32.90           N  
ANISOU 1644  ND2 ASN A1101     3713   4875   3914    113    377    179       N  
ATOM   1645  N   MET A1102     -17.241  29.087  -1.883  1.00 39.26           N  
ANISOU 1645  N   MET A1102     4299   5867   4753    536    103   -223       N  
ATOM   1646  CA  MET A1102     -17.696  30.108  -2.821  1.00 40.90           C  
ANISOU 1646  CA  MET A1102     4540   5963   5036    614    -39   -268       C  
ATOM   1647  C   MET A1102     -17.826  31.471  -2.153  1.00 43.81           C  
ANISOU 1647  C   MET A1102     4929   6287   5430    796   -160   -413       C  
ATOM   1648  O   MET A1102     -17.589  32.499  -2.798  1.00 44.80           O  
ANISOU 1648  O   MET A1102     5152   6223   5646    846   -302   -420       O  
ATOM   1649  CB  MET A1102     -19.030  29.692  -3.442  1.00 41.22           C  
ANISOU 1649  CB  MET A1102     4457   6133   5074    618    -18   -281       C  
ATOM   1650  CG  MET A1102     -18.980  28.379  -4.206  1.00 40.45           C  
ANISOU 1650  CG  MET A1102     4340   6058   4972    438     81   -168       C  
ATOM   1651  SD  MET A1102     -20.576  27.943  -4.922  1.00 41.96           S  
ANISOU 1651  SD  MET A1102     4364   6410   5167    435     86   -212       S  
ATOM   1652  CE  MET A1102     -20.871  29.361  -5.976  1.00 42.86           C  
ANISOU 1652  CE  MET A1102     4544   6409   5332    578   -115   -251       C  
ATOM   1653  N   VAL A1103     -18.199  31.500  -0.872  1.00 43.68           N  
ANISOU 1653  N   VAL A1103     4821   6440   5336    899   -110   -529       N  
ATOM   1654  CA  VAL A1103     -18.339  32.771  -0.167  1.00 45.08           C  
ANISOU 1654  CA  VAL A1103     5008   6585   5535   1090   -230   -707       C  
ATOM   1655  C   VAL A1103     -16.978  33.434   0.020  1.00 44.87           C  
ANISOU 1655  C   VAL A1103     5132   6348   5568   1062   -316   -710       C  
ATOM   1656  O   VAL A1103     -16.854  34.661  -0.057  1.00 46.88           O  
ANISOU 1656  O   VAL A1103     5463   6426   5924   1168   -471   -809       O  
ATOM   1657  CB  VAL A1103     -19.062  32.556   1.177  1.00 46.87           C  
ANISOU 1657  CB  VAL A1103     5081   7097   5631   1207   -140   -840       C  
ATOM   1658  CG1 VAL A1103     -19.151  33.857   1.958  1.00 48.81           C  
ANISOU 1658  CG1 VAL A1103     5335   7319   5893   1421   -268  -1063       C  
ATOM   1659  CG2 VAL A1103     -20.453  31.983   0.947  1.00 47.22           C  
ANISOU 1659  CG2 VAL A1103     4955   7355   5631   1222    -59   -841       C  
ATOM   1660  N   PHE A1104     -15.932  32.637   0.250  1.00 42.76           N  
ANISOU 1660  N   PHE A1104     4906   6087   5253    918   -225   -601       N  
ATOM   1661  CA  PHE A1104     -14.606  33.209   0.462  1.00 42.08           C  
ANISOU 1661  CA  PHE A1104     4936   5832   5219    878   -302   -609       C  
ATOM   1662  C   PHE A1104     -14.013  33.760  -0.829  1.00 42.06           C  
ANISOU 1662  C   PHE A1104     5058   5569   5352    782   -402   -501       C  
ATOM   1663  O   PHE A1104     -13.205  34.695  -0.789  1.00 43.31           O  
ANISOU 1663  O   PHE A1104     5310   5543   5603    778   -517   -539       O  
ATOM   1664  CB  PHE A1104     -13.675  32.164   1.075  1.00 40.68           C  
ANISOU 1664  CB  PHE A1104     4750   5760   4944    767   -179   -521       C  
ATOM   1665  CG  PHE A1104     -13.700  32.144   2.576  1.00 42.29           C  
ANISOU 1665  CG  PHE A1104     4882   6163   5022    876   -143   -647       C  
ATOM   1666  CD1 PHE A1104     -13.511  33.310   3.299  1.00 44.28           C  
ANISOU 1666  CD1 PHE A1104     5156   6374   5296   1009   -269   -843       C  
ATOM   1667  CD2 PHE A1104     -13.928  30.965   3.264  1.00 42.42           C  
ANISOU 1667  CD2 PHE A1104     4811   6411   4897    847     13   -571       C  
ATOM   1668  CE1 PHE A1104     -13.537  33.296   4.678  1.00 46.45           C  
ANISOU 1668  CE1 PHE A1104     5356   6866   5428   1121   -238   -976       C  
ATOM   1669  CE2 PHE A1104     -13.953  30.945   4.642  1.00 44.46           C  
ANISOU 1669  CE2 PHE A1104     5000   6885   5009    951     50   -669       C  
ATOM   1670  CZ  PHE A1104     -13.759  32.112   5.351  1.00 46.43           C  
ANISOU 1670  CZ  PHE A1104     5261   7123   5256   1093    -74   -880       C  
ATOM   1671  N   GLN A1105     -14.403  33.204  -1.978  1.00 41.43           N  
ANISOU 1671  N   GLN A1105     4976   5481   5284    697   -362   -367       N  
ATOM   1672  CA  GLN A1105     -13.916  33.657  -3.277  1.00 41.19           C  
ANISOU 1672  CA  GLN A1105     5052   5250   5347    605   -444   -243       C  
ATOM   1673  C   GLN A1105     -14.695  34.848  -3.820  1.00 42.91           C  
ANISOU 1673  C   GLN A1105     5309   5334   5662    730   -598   -288       C  
ATOM   1674  O   GLN A1105     -14.093  35.791  -4.343  1.00 42.78           O  
ANISOU 1674  O   GLN A1105     5408   5095   5752    703   -718   -236       O  
ATOM   1675  CB  GLN A1105     -13.974  32.518  -4.294  1.00 39.55           C  
ANISOU 1675  CB  GLN A1105     4822   5115   5090    471   -340    -95       C  
ATOM   1676  CG  GLN A1105     -13.452  32.905  -5.670  1.00 39.12           C  
ANISOU 1676  CG  GLN A1105     4865   4907   5093    374   -408     43       C  
ATOM   1677  CD  GLN A1105     -13.494  31.754  -6.651  1.00 37.66           C  
ANISOU 1677  CD  GLN A1105     4649   4817   4844    255   -308    152       C  
ATOM   1678  OE1 GLN A1105     -13.869  30.638  -6.298  1.00 36.84           O  
ANISOU 1678  OE1 GLN A1105     4459   4860   4678    232   -192    129       O  
ATOM   1679  NE2 GLN A1105     -13.107  32.020  -7.893  1.00 37.81           N  
ANISOU 1679  NE2 GLN A1105     4737   4752   4876    177   -356    272       N  
ATOM   1680  N   MET A1106     -16.024  34.828  -3.714  1.00 45.25           N  
ANISOU 1680  N   MET A1106     5506   5759   5928    867   -602   -376       N  
ATOM   1681  CA  MET A1106     -16.861  35.830  -4.357  1.00 48.07           C  
ANISOU 1681  CA  MET A1106     5888   6006   6372   1002   -750   -405       C  
ATOM   1682  C   MET A1106     -17.606  36.736  -3.389  1.00 51.15           C  
ANISOU 1682  C   MET A1106     6228   6407   6798   1230   -842   -622       C  
ATOM   1683  O   MET A1106     -18.097  37.787  -3.813  1.00 52.55           O  
ANISOU 1683  O   MET A1106     6456   6428   7082   1366   -999   -660       O  
ATOM   1684  CB  MET A1106     -17.892  35.154  -5.273  1.00 47.99           C  
ANISOU 1684  CB  MET A1106     5789   6141   6305    995   -708   -337       C  
ATOM   1685  CG  MET A1106     -17.303  34.200  -6.299  1.00 46.76           C  
ANISOU 1685  CG  MET A1106     5666   6001   6102    791   -621   -157       C  
ATOM   1686  SD  MET A1106     -18.328  32.730  -6.514  1.00 46.21           S  
ANISOU 1686  SD  MET A1106     5427   6206   5926    736   -476   -162       S  
ATOM   1687  CE  MET A1106     -19.955  33.408  -6.204  1.00 47.69           C  
ANISOU 1687  CE  MET A1106     5483   6511   6127    966   -563   -320       C  
ATOM   1688  N   GLY A1107     -17.712  36.363  -2.119  1.00 52.25           N  
ANISOU 1688  N   GLY A1107     6271   6733   6849   1286   -753   -764       N  
ATOM   1689  CA  GLY A1107     -18.475  37.135  -1.162  1.00 55.75           C  
ANISOU 1689  CA  GLY A1107     6641   7244   7297   1517   -824   -997       C  
ATOM   1690  C   GLY A1107     -19.904  36.638  -1.024  1.00 58.58           C  
ANISOU 1690  C   GLY A1107     6814   7881   7562   1628   -750  -1070       C  
ATOM   1691  O   GLY A1107     -20.427  35.905  -1.863  1.00 58.40           O  
ANISOU 1691  O   GLY A1107     6735   7946   7509   1542   -687   -944       O  
ATOM   1692  N   GLU A1108     -20.542  37.057   0.072  1.00 61.93           N  
ANISOU 1692  N   GLU A1108     7130   8462   7936   1825   -760  -1293       N  
ATOM   1693  CA  GLU A1108     -21.908  36.620   0.344  1.00 64.10           C  
ANISOU 1693  CA  GLU A1108     7198   9044   8112   1935   -678  -1380       C  
ATOM   1694  C   GLU A1108     -22.873  37.115  -0.724  1.00 65.80           C  
ANISOU 1694  C   GLU A1108     7389   9191   8421   2042   -797  -1371       C  
ATOM   1695  O   GLU A1108     -23.752  36.369  -1.172  1.00 64.37           O  
ANISOU 1695  O   GLU A1108     7067   9210   8179   2001   -714  -1315       O  
ATOM   1696  CB  GLU A1108     -22.347  37.101   1.726  1.00 66.29           C  
ANISOU 1696  CB  GLU A1108     7363   9518   8308   2146   -675  -1638       C  
ATOM   1697  CG  GLU A1108     -21.504  36.564   2.867  1.00 65.64           C  
ANISOU 1697  CG  GLU A1108     7279   9566   8094   2061   -555  -1650       C  
ATOM   1698  CD  GLU A1108     -21.936  37.107   4.213  1.00 68.05           C  
ANISOU 1698  CD  GLU A1108     7470  10091   8295   2285   -562  -1923       C  
ATOM   1699  OE1 GLU A1108     -23.013  37.736   4.283  1.00 70.07           O  
ANISOU 1699  OE1 GLU A1108     7614  10441   8568   2503   -629  -2102       O  
ATOM   1700  OE2 GLU A1108     -21.195  36.910   5.198  1.00 67.93           O  
ANISOU 1700  OE2 GLU A1108     7469  10170   8172   2256   -504  -1967       O  
ATOM   1701  N   THR A1109     -22.727  38.373  -1.147  1.00 69.04           N  
ANISOU 1701  N   THR A1109     7932   9315   8985   2178   -999  -1423       N  
ATOM   1702  CA  THR A1109     -23.611  38.916  -2.171  1.00 69.96           C  
ANISOU 1702  CA  THR A1109     8037   9354   9189   2303  -1134  -1399       C  
ATOM   1703  C   THR A1109     -23.364  38.290  -3.538  1.00 68.26           C  
ANISOU 1703  C   THR A1109     7890   9066   8979   2098  -1112  -1139       C  
ATOM   1704  O   THR A1109     -24.262  38.313  -4.387  1.00 70.30           O  
ANISOU 1704  O   THR A1109     8081   9382   9246   2166  -1171  -1102       O  
ATOM   1705  CB  THR A1109     -23.458  40.437  -2.253  1.00 72.01           C  
ANISOU 1705  CB  THR A1109     8444   9289   9628   2501  -1366  -1499       C  
ATOM   1706  OG1 THR A1109     -24.431  40.969  -3.160  1.00 72.59           O  
ANISOU 1706  OG1 THR A1109     8491   9315   9776   2662  -1504  -1482       O  
ATOM   1707  CG2 THR A1109     -22.065  40.815  -2.736  1.00 71.57           C  
ANISOU 1707  CG2 THR A1109     8624   8886   9684   2323  -1433  -1330       C  
ATOM   1708  N   GLY A1110     -22.174  37.730  -3.769  1.00 63.82           N  
ANISOU 1708  N   GLY A1110     7448   8398   8402   1859  -1032   -972       N  
ATOM   1709  CA  GLY A1110     -21.910  37.057  -5.028  1.00 60.07           C  
ANISOU 1709  CA  GLY A1110     7024   7892   7909   1668   -997   -749       C  
ATOM   1710  C   GLY A1110     -22.461  35.650  -5.084  1.00 58.16           C  
ANISOU 1710  C   GLY A1110     6618   7940   7540   1543   -820   -716       C  
ATOM   1711  O   GLY A1110     -22.888  35.194  -6.149  1.00 59.25           O  
ANISOU 1711  O   GLY A1110     6724   8130   7659   1475   -823   -614       O  
ATOM   1712  N   VAL A1111     -22.463  34.944  -3.951  1.00 55.87           N  
ANISOU 1712  N   VAL A1111     6222   7842   7162   1507   -669   -797       N  
ATOM   1713  CA  VAL A1111     -23.055  33.612  -3.908  1.00 52.92           C  
ANISOU 1713  CA  VAL A1111     5688   7729   6690   1381   -502   -762       C  
ATOM   1714  C   VAL A1111     -24.574  33.699  -3.990  1.00 53.07           C  
ANISOU 1714  C   VAL A1111     5509   7966   6689   1527   -526   -879       C  
ATOM   1715  O   VAL A1111     -25.228  32.799  -4.533  1.00 52.54           O  
ANISOU 1715  O   VAL A1111     5319   8059   6584   1421   -452   -829       O  
ATOM   1716  CB  VAL A1111     -22.588  32.868  -2.642  1.00 51.29           C  
ANISOU 1716  CB  VAL A1111     5437   7659   6393   1301   -337   -783       C  
ATOM   1717  CG1 VAL A1111     -23.209  31.481  -2.567  1.00 50.66           C  
ANISOU 1717  CG1 VAL A1111     5197   7819   6232   1156   -165   -725       C  
ATOM   1718  CG2 VAL A1111     -21.072  32.772  -2.622  1.00 49.30           C  
ANISOU 1718  CG2 VAL A1111     5366   7204   6163   1166   -325   -672       C  
ATOM   1719  N   ALA A1112     -25.161  34.782  -3.474  1.00 53.64           N  
ANISOU 1719  N   ALA A1112     5537   8049   6793   1775   -637  -1050       N  
ATOM   1720  CA  ALA A1112     -26.602  34.984  -3.562  1.00 54.17           C  
ANISOU 1720  CA  ALA A1112     5403   8332   6848   1946   -678  -1178       C  
ATOM   1721  C   ALA A1112     -27.084  35.190  -4.992  1.00 54.02           C  
ANISOU 1721  C   ALA A1112     5403   8236   6888   1964   -809  -1093       C  
ATOM   1722  O   ALA A1112     -28.293  35.117  -5.236  1.00 55.10           O  
ANISOU 1722  O   ALA A1112     5350   8584   7004   2066   -831  -1175       O  
ATOM   1723  CB  ALA A1112     -27.018  36.177  -2.701  1.00 55.85           C  
ANISOU 1723  CB  ALA A1112     5580   8548   7091   2237   -786  -1400       C  
ATOM   1724  N   GLY A1113     -26.176  35.452  -5.935  1.00 52.79           N  
ANISOU 1724  N   GLY A1113     5458   7806   6792   1871   -896   -929       N  
ATOM   1725  CA  GLY A1113     -26.566  35.597  -7.325  1.00 52.30           C  
ANISOU 1725  CA  GLY A1113     5420   7696   6755   1878  -1015   -825       C  
ATOM   1726  C   GLY A1113     -26.960  34.298  -7.995  1.00 50.23           C  
ANISOU 1726  C   GLY A1113     5034   7639   6413   1683   -900   -755       C  
ATOM   1727  O   GLY A1113     -27.708  34.324  -8.978  1.00 50.85           O  
ANISOU 1727  O   GLY A1113     5044   7796   6482   1730   -992   -736       O  
ATOM   1728  N   PHE A1114     -26.477  33.163  -7.488  1.00 48.00           N  
ANISOU 1728  N   PHE A1114     4723   7440   6077   1471   -713   -719       N  
ATOM   1729  CA  PHE A1114     -26.842  31.852  -8.027  1.00 47.21           C  
ANISOU 1729  CA  PHE A1114     4503   7510   5923   1273   -600   -672       C  
ATOM   1730  C   PHE A1114     -28.216  31.425  -7.504  1.00 48.69           C  
ANISOU 1730  C   PHE A1114     4418   8006   6078   1326   -534   -812       C  
ATOM   1731  O   PHE A1114     -28.381  30.383  -6.873  1.00 49.24           O  
ANISOU 1731  O   PHE A1114     4367   8232   6111   1173   -363   -819       O  
ATOM   1732  CB  PHE A1114     -25.781  30.817  -7.677  1.00 45.96           C  
ANISOU 1732  CB  PHE A1114     4429   7290   5742   1039   -437   -573       C  
ATOM   1733  CG  PHE A1114     -24.455  31.055  -8.337  1.00 45.49           C  
ANISOU 1733  CG  PHE A1114     4602   6978   5706    956   -485   -433       C  
ATOM   1734  CD1 PHE A1114     -24.242  30.668  -9.648  1.00 45.41           C  
ANISOU 1734  CD1 PHE A1114     4646   6928   5679    847   -522   -334       C  
ATOM   1735  CD2 PHE A1114     -23.416  31.652  -7.643  1.00 45.62           C  
ANISOU 1735  CD2 PHE A1114     4766   6818   5750    983   -490   -410       C  
ATOM   1736  CE1 PHE A1114     -23.021  30.879 -10.257  1.00 45.06           C  
ANISOU 1736  CE1 PHE A1114     4795   6688   5640    766   -553   -203       C  
ATOM   1737  CE2 PHE A1114     -22.192  31.866  -8.249  1.00 44.84           C  
ANISOU 1737  CE2 PHE A1114     4857   6506   5672    891   -526   -278       C  
ATOM   1738  CZ  PHE A1114     -21.994  31.479  -9.556  1.00 44.61           C  
ANISOU 1738  CZ  PHE A1114     4876   6455   5621    782   -551   -169       C  
ATOM   1739  N   THR A1115     -29.216  32.263  -7.793  1.00 50.06           N  
ANISOU 1739  N   THR A1115     4487   8265   6269   1547   -675   -915       N  
ATOM   1740  CA  THR A1115     -30.556  32.037  -7.259  1.00 51.81           C  
ANISOU 1740  CA  THR A1115     4424   8802   6458   1631   -626  -1068       C  
ATOM   1741  C   THR A1115     -31.104  30.680  -7.682  1.00 51.98           C  
ANISOU 1741  C   THR A1115     4275   9024   6449   1397   -506  -1041       C  
ATOM   1742  O   THR A1115     -31.713  29.968  -6.874  1.00 52.36           O  
ANISOU 1742  O   THR A1115     4122   9306   6465   1316   -356  -1102       O  
ATOM   1743  CB  THR A1115     -31.497  33.154  -7.714  1.00 54.17           C  
ANISOU 1743  CB  THR A1115     4646   9146   6789   1918   -824  -1177       C  
ATOM   1744  OG1 THR A1115     -30.979  34.421  -7.293  1.00 55.03           O  
ANISOU 1744  OG1 THR A1115     4924   9029   6955   2132   -944  -1211       O  
ATOM   1745  CG2 THR A1115     -32.882  32.959  -7.120  1.00 56.40           C  
ANISOU 1745  CG2 THR A1115     4608   9787   7034   2019   -769  -1352       C  
ATOM   1746  N   ASN A1116     -30.884  30.298  -8.939  1.00 51.94           N  
ANISOU 1746  N   ASN A1116     4347   8935   6453   1279   -571   -949       N  
ATOM   1747  CA  ASN A1116     -31.449  29.049  -9.439  1.00 52.09           C  
ANISOU 1747  CA  ASN A1116     4202   9128   6461   1065   -486   -954       C  
ATOM   1748  C   ASN A1116     -30.695  27.841  -8.896  1.00 49.43           C  
ANISOU 1748  C   ASN A1116     3918   8733   6131    798   -290   -868       C  
ATOM   1749  O   ASN A1116     -31.309  26.859  -8.466  1.00 49.83           O  
ANISOU 1749  O   ASN A1116     3781   8965   6188    642   -155   -900       O  
ATOM   1750  CB  ASN A1116     -31.439  29.052 -10.967  1.00 52.90           C  
ANISOU 1750  CB  ASN A1116     4369   9176   6555   1043   -630   -906       C  
ATOM   1751  CG  ASN A1116     -32.239  27.911 -11.557  1.00 53.06           C  
ANISOU 1751  CG  ASN A1116     4185   9402   6571    860   -585   -965       C  
ATOM   1752  OD1 ASN A1116     -33.131  27.362 -10.909  1.00 53.91           O  
ANISOU 1752  OD1 ASN A1116     4056   9732   6695    800   -485  -1059       O  
ATOM   1753  ND2 ASN A1116     -31.924  27.546 -12.792  1.00 52.61           N  
ANISOU 1753  ND2 ASN A1116     4212   9285   6491    764   -658   -916       N  
ATOM   1754  N   SER A1117     -29.360  27.897  -8.908  1.00 47.09           N  
ANISOU 1754  N   SER A1117     3870   8183   5840    740   -274   -750       N  
ATOM   1755  CA  SER A1117     -28.563  26.755  -8.468  1.00 46.74           C  
ANISOU 1755  CA  SER A1117     3891   8062   5806    508   -106   -660       C  
ATOM   1756  C   SER A1117     -28.731  26.495  -6.977  1.00 48.46           C  
ANISOU 1756  C   SER A1117     4011   8398   6003    498     47   -678       C  
ATOM   1757  O   SER A1117     -28.811  25.337  -6.551  1.00 48.84           O  
ANISOU 1757  O   SER A1117     3979   8515   6063    301    199   -633       O  
ATOM   1758  CB  SER A1117     -27.090  26.980  -8.810  1.00 45.30           C  
ANISOU 1758  CB  SER A1117     3978   7607   5626    478   -135   -542       C  
ATOM   1759  OG  SER A1117     -26.891  26.998 -10.212  1.00 46.10           O  
ANISOU 1759  OG  SER A1117     4159   7634   5723    447   -245   -506       O  
ATOM   1760  N   LEU A1118     -28.774  27.556  -6.167  1.00 50.22           N  
ANISOU 1760  N   LEU A1118     4243   8646   6194    709      6   -742       N  
ATOM   1761  CA  LEU A1118     -28.985  27.379  -4.733  1.00 52.12           C  
ANISOU 1761  CA  LEU A1118     4374   9050   6381    723    147   -773       C  
ATOM   1762  C   LEU A1118     -30.330  26.721  -4.455  1.00 55.44           C  
ANISOU 1762  C   LEU A1118     4502   9780   6783    657    244   -840       C  
ATOM   1763  O   LEU A1118     -30.454  25.909  -3.531  1.00 55.56           O  
ANISOU 1763  O   LEU A1118     4417   9932   6762    524    417   -791       O  
ATOM   1764  CB  LEU A1118     -28.887  28.725  -4.017  1.00 51.85           C  
ANISOU 1764  CB  LEU A1118     4386   9001   6314    990     60   -877       C  
ATOM   1765  CG  LEU A1118     -27.524  29.418  -4.031  1.00 49.29           C  
ANISOU 1765  CG  LEU A1118     4334   8380   6013   1042    -21   -817       C  
ATOM   1766  CD1 LEU A1118     -27.635  30.808  -3.427  1.00 49.63           C  
ANISOU 1766  CD1 LEU A1118     4399   8403   6054   1316   -137   -958       C  
ATOM   1767  CD2 LEU A1118     -26.483  28.588  -3.297  1.00 47.40           C  
ANISOU 1767  CD2 LEU A1118     4193   8076   5739    870    128   -702       C  
ATOM   1768  N   ARG A1119     -31.349  27.060  -5.247  1.00 58.84           N  
ANISOU 1768  N   ARG A1119     4784  10334   7238    744    132   -942       N  
ATOM   1769  CA  ARG A1119     -32.641  26.397  -5.115  1.00 62.01           C  
ANISOU 1769  CA  ARG A1119     4885  11040   7635    657    215  -1011       C  
ATOM   1770  C   ARG A1119     -32.548  24.922  -5.484  1.00 60.20           C  
ANISOU 1770  C   ARG A1119     4631  10780   7464    334    333   -905       C  
ATOM   1771  O   ARG A1119     -33.239  24.087  -4.890  1.00 60.60           O  
ANISOU 1771  O   ARG A1119     4476  11036   7515    177    481   -896       O  
ATOM   1772  CB  ARG A1119     -33.678  27.106  -5.987  1.00 66.01           C  
ANISOU 1772  CB  ARG A1119     5246  11677   8158    833     45  -1148       C  
ATOM   1773  CG  ARG A1119     -35.083  26.540  -5.891  1.00 70.36           C  
ANISOU 1773  CG  ARG A1119     5452  12574   8707    761    112  -1245       C  
ATOM   1774  CD  ARG A1119     -36.012  27.238  -6.871  1.00 75.00           C  
ANISOU 1774  CD  ARG A1119     5910  13278   9310    947    -82  -1376       C  
ATOM   1775  NE  ARG A1119     -35.503  27.171  -8.239  1.00 77.69           N  
ANISOU 1775  NE  ARG A1119     6429  13398   9690    893   -223  -1313       N  
ATOM   1776  CZ  ARG A1119     -35.810  26.210  -9.105  1.00 81.30           C  
ANISOU 1776  CZ  ARG A1119     6804  13902  10186    677   -220  -1306       C  
ATOM   1777  NH1 ARG A1119     -35.298  26.228 -10.328  1.00 81.47           N  
ANISOU 1777  NH1 ARG A1119     6994  13747  10215    655   -351  -1260       N  
ATOM   1778  NH2 ARG A1119     -36.631  25.231  -8.748  1.00 83.66           N  
ANISOU 1778  NH2 ARG A1119     6845  14430  10513    477    -87  -1350       N  
ATOM   1779  N   MET A1120     -31.697  24.582  -6.456  1.00 58.07           N  
ANISOU 1779  N   MET A1120     4564  10255   7246    229    270   -828       N  
ATOM   1780  CA  MET A1120     -31.511  23.182  -6.820  1.00 56.85           C  
ANISOU 1780  CA  MET A1120     4408  10030   7162    -63    368   -748       C  
ATOM   1781  C   MET A1120     -30.767  22.422  -5.729  1.00 54.80           C  
ANISOU 1781  C   MET A1120     4232   9689   6900   -206    547   -611       C  
ATOM   1782  O   MET A1120     -31.099  21.268  -5.432  1.00 55.80           O  
ANISOU 1782  O   MET A1120     4249   9870   7081   -432    680   -552       O  
ATOM   1783  CB  MET A1120     -30.760  23.082  -8.147  1.00 56.41           C  
ANISOU 1783  CB  MET A1120     4545   9747   7142   -104    249   -724       C  
ATOM   1784  CG  MET A1120     -31.498  23.686  -9.328  1.00 57.67           C  
ANISOU 1784  CG  MET A1120     4622   9999   7289     15     69   -836       C  
ATOM   1785  SD  MET A1120     -30.452  23.815 -10.790  1.00 56.36           S  
ANISOU 1785  SD  MET A1120     4710   9592   7113     12    -70   -784       S  
ATOM   1786  CE  MET A1120     -31.657  24.285 -12.027  1.00 58.14           C  
ANISOU 1786  CE  MET A1120     4762  10022   7306    126   -260   -916       C  
ATOM   1787  N   LEU A1121     -29.755  23.051  -5.126  1.00 51.96           N  
ANISOU 1787  N   LEU A1121     4065   9193   6484    -80    546   -553       N  
ATOM   1788  CA  LEU A1121     -28.999  22.394  -4.064  1.00 50.99           C  
ANISOU 1788  CA  LEU A1121     4026   9008   6339   -188    700   -418       C  
ATOM   1789  C   LEU A1121     -29.869  22.145  -2.840  1.00 53.16           C  
ANISOU 1789  C   LEU A1121     4080   9567   6550   -211    848   -413       C  
ATOM   1790  O   LEU A1121     -29.722  21.120  -2.163  1.00 54.73           O  
ANISOU 1790  O   LEU A1121     4259   9777   6757   -396   1004   -279       O  
ATOM   1791  CB  LEU A1121     -27.779  23.237  -3.691  1.00 48.46           C  
ANISOU 1791  CB  LEU A1121     3935   8514   5964    -31    647   -385       C  
ATOM   1792  CG  LEU A1121     -26.632  23.285  -4.700  1.00 47.14           C  
ANISOU 1792  CG  LEU A1121     4003   8060   5848    -56    549   -336       C  
ATOM   1793  CD1 LEU A1121     -25.594  24.310  -4.275  1.00 46.12           C  
ANISOU 1793  CD1 LEU A1121     4056   7798   5668    109    485   -326       C  
ATOM   1794  CD2 LEU A1121     -25.997  21.912  -4.843  1.00 46.59           C  
ANISOU 1794  CD2 LEU A1121     4007   7851   5843   -287    652   -216       C  
ATOM   1795  N   GLN A1122     -30.780  23.074  -2.538  1.00 53.87           N  
ANISOU 1795  N   GLN A1122     4001   9896   6573    -17    802   -552       N  
ATOM   1796  CA  GLN A1122     -31.669  22.895  -1.394  1.00 55.07           C  
ANISOU 1796  CA  GLN A1122     3913  10372   6640    -25    949   -563       C  
ATOM   1797  C   GLN A1122     -32.609  21.714  -1.603  1.00 55.68           C  
ANISOU 1797  C   GLN A1122     3812  10549   6795   -284   1045   -510       C  
ATOM   1798  O   GLN A1122     -32.897  20.969  -0.659  1.00 56.62           O  
ANISOU 1798  O   GLN A1122     3903  10725   6886   -420   1188   -389       O  
ATOM   1799  CB  GLN A1122     -32.463  24.177  -1.144  1.00 57.57           C  
ANISOU 1799  CB  GLN A1122     4083  10914   6877    264    858   -756       C  
ATOM   1800  CG  GLN A1122     -33.453  24.079   0.006  1.00 61.19           C  
ANISOU 1800  CG  GLN A1122     4400  11615   7236    271    965   -769       C  
ATOM   1801  CD  GLN A1122     -34.175  25.386   0.267  1.00 63.82           C  
ANISOU 1801  CD  GLN A1122     4648  12110   7493    572    853   -972       C  
ATOM   1802  OE1 GLN A1122     -33.748  26.446  -0.190  1.00 63.55           O  
ANISOU 1802  OE1 GLN A1122     4694  11976   7477    802    701  -1088       O  
ATOM   1803  NE2 GLN A1122     -35.277  25.316   1.004  1.00 67.41           N  
ANISOU 1803  NE2 GLN A1122     4942  12804   7869    575    921  -1013       N  
ATOM   1804  N   GLN A1123     -33.094  21.526  -2.829  1.00 54.83           N  
ANISOU 1804  N   GLN A1123     3627  10415   6790   -353    946   -590       N  
ATOM   1805  CA  GLN A1123     -33.953  20.398  -3.164  1.00 55.74           C  
ANISOU 1805  CA  GLN A1123     3625  10546   7008   -604    999   -556       C  
ATOM   1806  C   GLN A1123     -33.170  19.120  -3.430  1.00 54.91           C  
ANISOU 1806  C   GLN A1123     3649  10195   7020   -876   1076   -407       C  
ATOM   1807  O   GLN A1123     -33.757  18.136  -3.896  1.00 56.56           O  
ANISOU 1807  O   GLN A1123     3782  10357   7350  -1092   1096   -394       O  
ATOM   1808  CB  GLN A1123     -34.818  20.739  -4.379  1.00 56.77           C  
ANISOU 1808  CB  GLN A1123     3620  10760   7191   -551    843   -725       C  
ATOM   1809  CG  GLN A1123     -35.655  21.995  -4.210  1.00 58.51           C  
ANISOU 1809  CG  GLN A1123     3718  11199   7313   -266    745   -879       C  
ATOM   1810  CD  GLN A1123     -36.540  22.268  -5.408  1.00 60.24           C  
ANISOU 1810  CD  GLN A1123     3809  11502   7578   -211    584  -1027       C  
ATOM   1811  OE1 GLN A1123     -36.669  21.432  -6.302  1.00 60.50           O  
ANISOU 1811  OE1 GLN A1123     3817  11461   7708   -410    558  -1026       O  
ATOM   1812  NE2 GLN A1123     -37.156  23.444  -5.434  1.00 61.70           N  
ANISOU 1812  NE2 GLN A1123     3921  11832   7691     68    466  -1162       N  
ATOM   1813  N   LYS A1124     -31.864  19.125  -3.154  1.00 52.26           N  
ANISOU 1813  N   LYS A1124     3515   9682   6657   -858   1108   -303       N  
ATOM   1814  CA  LYS A1124     -31.000  17.954  -3.309  1.00 51.24           C  
ANISOU 1814  CA  LYS A1124     3558   9274   6635  -1077   1170   -155       C  
ATOM   1815  C   LYS A1124     -30.952  17.466  -4.755  1.00 50.84           C  
ANISOU 1815  C   LYS A1124     3559   9038   6719  -1186   1053   -240       C  
ATOM   1816  O   LYS A1124     -30.806  16.269  -5.015  1.00 45.11           O  
ANISOU 1816  O   LYS A1124     2861   8154   6126  -1421   1108   -173       O  
ATOM   1817  CB  LYS A1124     -31.423  16.823  -2.367  1.00 52.78           C  
ANISOU 1817  CB  LYS A1124     3698   9478   6879  -1282   1336      9       C  
ATOM   1818  CG  LYS A1124     -31.426  17.226  -0.899  1.00 53.14           C  
ANISOU 1818  CG  LYS A1124     3746   9673   6771  -1159   1440    103       C  
ATOM   1819  CD  LYS A1124     -31.626  16.027   0.010  1.00 54.88           C  
ANISOU 1819  CD  LYS A1124     3974   9835   7043  -1358   1594    304       C  
ATOM   1820  CE  LYS A1124     -31.732  16.456   1.464  1.00 55.59           C  
ANISOU 1820  CE  LYS A1124     4049  10123   6952  -1230   1690    377       C  
ATOM   1821  NZ  LYS A1124     -30.545  17.245   1.894  1.00 53.11           N  
ANISOU 1821  NZ  LYS A1124     3899   9779   6502  -1036   1658    383       N  
ATOM   1822  N   ARG A1125     -31.069  18.393  -5.705  1.00 50.41           N  
ANISOU 1822  N   ARG A1125     3523   9003   6628  -1010    885   -389       N  
ATOM   1823  CA  ARG A1125     -30.920  18.087  -7.126  1.00 51.20           C  
ANISOU 1823  CA  ARG A1125     3688   8956   6809  -1072    757   -478       C  
ATOM   1824  C   ARG A1125     -29.484  18.420  -7.519  1.00 49.88           C  
ANISOU 1824  C   ARG A1125     3817   8525   6609   -970    691   -425       C  
ATOM   1825  O   ARG A1125     -29.194  19.447  -8.135  1.00 48.37           O  
ANISOU 1825  O   ARG A1125     3716   8316   6344   -779    556   -485       O  
ATOM   1826  CB  ARG A1125     -31.943  18.861  -7.951  1.00 52.76           C  
ANISOU 1826  CB  ARG A1125     3716   9361   6971   -944    612   -651       C  
ATOM   1827  CG  ARG A1125     -33.381  18.432  -7.703  1.00 55.51           C  
ANISOU 1827  CG  ARG A1125     3741   9987   7364  -1067    671   -725       C  
ATOM   1828  CD  ARG A1125     -34.339  19.606  -7.811  1.00 57.15           C  
ANISOU 1828  CD  ARG A1125     3767  10469   7479   -831    564   -862       C  
ATOM   1829  NE  ARG A1125     -34.246  20.281  -9.101  1.00 57.77           N  
ANISOU 1829  NE  ARG A1125     3927  10494   7529   -678    360   -968       N  
ATOM   1830  CZ  ARG A1125     -34.931  21.375  -9.418  1.00 59.81           C  
ANISOU 1830  CZ  ARG A1125     4078  10933   7713   -438    224  -1079       C  
ATOM   1831  NH1 ARG A1125     -34.787  21.927 -10.615  1.00 60.07           N  
ANISOU 1831  NH1 ARG A1125     4204  10906   7715   -312     39  -1139       N  
ATOM   1832  NH2 ARG A1125     -35.759  21.919  -8.537  1.00 61.26           N  
ANISOU 1832  NH2 ARG A1125     4061  11367   7849   -315    272  -1128       N  
ATOM   1833  N   TRP A1126     -28.571  17.519  -7.149  1.00 50.37           N  
ANISOU 1833  N   TRP A1126     4026   8379   6733  -1105    788   -299       N  
ATOM   1834  CA  TRP A1126     -27.145  17.792  -7.299  1.00 49.14           C  
ANISOU 1834  CA  TRP A1126     4131   8000   6541  -1013    752   -233       C  
ATOM   1835  C   TRP A1126     -26.735  17.822  -8.766  1.00 48.86           C  
ANISOU 1835  C   TRP A1126     4195   7846   6525  -1002    618   -328       C  
ATOM   1836  O   TRP A1126     -25.995  18.715  -9.196  1.00 48.35           O  
ANISOU 1836  O   TRP A1126     4273   7719   6380   -845    526   -331       O  
ATOM   1837  CB  TRP A1126     -26.331  16.747  -6.538  1.00 50.01           C  
ANISOU 1837  CB  TRP A1126     4352   7935   6715  -1151    885    -79       C  
ATOM   1838  CG  TRP A1126     -26.911  16.367  -5.207  1.00 51.86           C  
ANISOU 1838  CG  TRP A1126     4456   8307   6940  -1228   1034     33       C  
ATOM   1839  CD1 TRP A1126     -27.359  15.134  -4.832  1.00 53.47           C  
ANISOU 1839  CD1 TRP A1126     4570   8487   7259  -1457   1151    122       C  
ATOM   1840  CD2 TRP A1126     -27.108  17.226  -4.077  1.00 52.16           C  
ANISOU 1840  CD2 TRP A1126     4436   8542   6841  -1078   1085     71       C  
ATOM   1841  NE1 TRP A1126     -27.818  15.170  -3.538  1.00 54.58           N  
ANISOU 1841  NE1 TRP A1126     4597   8815   7326  -1467   1281    237       N  
ATOM   1842  CE2 TRP A1126     -27.676  16.443  -3.052  1.00 53.86           C  
ANISOU 1842  CE2 TRP A1126     4519   8875   7070  -1227   1243    194       C  
ATOM   1843  CE3 TRP A1126     -26.859  18.579  -3.831  1.00 51.79           C  
ANISOU 1843  CE3 TRP A1126     4436   8577   6664   -835   1008      9       C  
ATOM   1844  CZ2 TRP A1126     -27.996  16.967  -1.802  1.00 54.96           C  
ANISOU 1844  CZ2 TRP A1126     4564   9250   7070  -1129   1333    247       C  
ATOM   1845  CZ3 TRP A1126     -27.182  19.099  -2.592  1.00 52.77           C  
ANISOU 1845  CZ3 TRP A1126     4471   8908   6672   -732   1085     37       C  
ATOM   1846  CH2 TRP A1126     -27.744  18.295  -1.592  1.00 54.37           C  
ANISOU 1846  CH2 TRP A1126     4533   9262   6863   -873   1250    151       C  
ATOM   1847  N   ASP A1127     -27.196  16.844  -9.548  1.00 49.31           N  
ANISOU 1847  N   ASP A1127     4173   7878   6687  -1175    605   -408       N  
ATOM   1848  CA  ASP A1127     -26.816  16.781 -10.956  1.00 48.89           C  
ANISOU 1848  CA  ASP A1127     4201   7743   6630  -1167    482   -513       C  
ATOM   1849  C   ASP A1127     -27.304  18.009 -11.715  1.00 49.44           C  
ANISOU 1849  C   ASP A1127     4224   7980   6583   -984    334   -602       C  
ATOM   1850  O   ASP A1127     -26.597  18.532 -12.584  1.00 49.04           O  
ANISOU 1850  O   ASP A1127     4312   7866   6456   -883    235   -613       O  
ATOM   1851  CB  ASP A1127     -27.366  15.504 -11.586  1.00 50.95           C  
ANISOU 1851  CB  ASP A1127     4359   7969   7030  -1386    488   -616       C  
ATOM   1852  CG  ASP A1127     -26.867  14.252 -10.894  1.00 52.41           C  
ANISOU 1852  CG  ASP A1127     4611   7946   7358  -1566    621   -514       C  
ATOM   1853  OD1 ASP A1127     -25.644  14.147 -10.665  1.00 51.42           O  
ANISOU 1853  OD1 ASP A1127     4682   7635   7219  -1517    655   -419       O  
ATOM   1854  OD2 ASP A1127     -27.697  13.378 -10.570  1.00 54.87           O  
ANISOU 1854  OD2 ASP A1127     4772   8278   7798  -1758    688   -521       O  
ATOM   1855  N   GLU A1128     -28.509  18.484 -11.397  1.00 51.02           N  
ANISOU 1855  N   GLU A1128     4222   8399   6763   -934    315   -657       N  
ATOM   1856  CA  GLU A1128     -29.028  19.683 -12.046  1.00 51.07           C  
ANISOU 1856  CA  GLU A1128     4180   8557   6667   -734    163   -732       C  
ATOM   1857  C   GLU A1128     -28.245  20.920 -11.628  1.00 47.86           C  
ANISOU 1857  C   GLU A1128     3941   8075   6168   -522    128   -639       C  
ATOM   1858  O   GLU A1128     -28.042  21.836 -12.435  1.00 46.32           O  
ANISOU 1858  O   GLU A1128     3829   7874   5896   -371    -10   -650       O  
ATOM   1859  CB  GLU A1128     -30.510  19.854 -11.719  1.00 54.90           C  
ANISOU 1859  CB  GLU A1128     4390   9306   7163   -719    157   -823       C  
ATOM   1860  CG  GLU A1128     -31.406  18.773 -12.296  1.00 57.89           C  
ANISOU 1860  CG  GLU A1128     4575   9784   7637   -928    158   -940       C  
ATOM   1861  CD  GLU A1128     -32.827  18.871 -11.785  1.00 61.15           C  
ANISOU 1861  CD  GLU A1128     4691  10475   8069   -938    182  -1016       C  
ATOM   1862  OE1 GLU A1128     -33.224  18.022 -10.960  1.00 62.61           O  
ANISOU 1862  OE1 GLU A1128     4750  10693   8345  -1129    330   -977       O  
ATOM   1863  OE2 GLU A1128     -33.542  19.807 -12.200  1.00 62.51           O  
ANISOU 1863  OE2 GLU A1128     4751  10838   8163   -751     54  -1106       O  
ATOM   1864  N   ALA A1129     -27.798  20.964 -10.371  1.00 46.87           N  
ANISOU 1864  N   ALA A1129     3868   7893   6050   -512    246   -544       N  
ATOM   1865  CA  ALA A1129     -27.058  22.124  -9.887  1.00 44.87           C  
ANISOU 1865  CA  ALA A1129     3764   7562   5724   -322    209   -479       C  
ATOM   1866  C   ALA A1129     -25.676  22.205 -10.521  1.00 43.56           C  
ANISOU 1866  C   ALA A1129     3833   7179   5539   -325    170   -404       C  
ATOM   1867  O   ALA A1129     -25.207  23.296 -10.862  1.00 43.49           O  
ANISOU 1867  O   ALA A1129     3941   7112   5473   -174     66   -379       O  
ATOM   1868  CB  ALA A1129     -26.948  22.078  -8.364  1.00 44.50           C  
ANISOU 1868  CB  ALA A1129     3695   7542   5672   -316    344   -415       C  
ATOM   1869  N   ALA A1130     -25.008  21.061 -10.690  1.00 43.09           N  
ANISOU 1869  N   ALA A1130     3842   6997   5534   -495    252   -368       N  
ATOM   1870  CA  ALA A1130     -23.677  21.068 -11.289  1.00 42.62           C  
ANISOU 1870  CA  ALA A1130     3982   6763   5451   -498    227   -309       C  
ATOM   1871  C   ALA A1130     -23.732  21.482 -12.753  1.00 44.08           C  
ANISOU 1871  C   ALA A1130     4192   6982   5573   -451     89   -364       C  
ATOM   1872  O   ALA A1130     -22.851  22.206 -13.232  1.00 43.87           O  
ANISOU 1872  O   ALA A1130     4313   6875   5481   -370     26   -301       O  
ATOM   1873  CB  ALA A1130     -23.031  19.693 -11.148  1.00 41.60           C  
ANISOU 1873  CB  ALA A1130     3902   6503   5402   -670    339   -279       C  
ATOM   1874  N   VAL A1131     -24.754  21.024 -13.480  1.00 45.84           N  
ANISOU 1874  N   VAL A1131     4268   7339   5810   -509     40   -477       N  
ATOM   1875  CA  VAL A1131     -24.913  21.417 -14.877  1.00 45.43           C  
ANISOU 1875  CA  VAL A1131     4224   7365   5674   -453   -100   -532       C  
ATOM   1876  C   VAL A1131     -25.162  22.915 -14.983  1.00 45.30           C  
ANISOU 1876  C   VAL A1131     4234   7405   5575   -247   -222   -483       C  
ATOM   1877  O   VAL A1131     -24.585  23.599 -15.838  1.00 44.53           O  
ANISOU 1877  O   VAL A1131     4257   7273   5389   -168   -317   -422       O  
ATOM   1878  CB  VAL A1131     -26.047  20.606 -15.532  1.00 45.97           C  
ANISOU 1878  CB  VAL A1131     4103   7587   5776   -556   -136   -684       C  
ATOM   1879  CG1 VAL A1131     -26.512  21.278 -16.815  1.00 46.51           C  
ANISOU 1879  CG1 VAL A1131     4139   7805   5728   -446   -305   -741       C  
ATOM   1880  CG2 VAL A1131     -25.591  19.182 -15.806  1.00 45.33           C  
ANISOU 1880  CG2 VAL A1131     4044   7402   5778   -750    -55   -743       C  
ATOM   1881  N   ASN A1132     -26.016  23.450 -14.108  1.00 46.18           N  
ANISOU 1881  N   ASN A1132     4230   7601   5716   -154   -222   -504       N  
ATOM   1882  CA  ASN A1132     -26.332  24.873 -14.153  1.00 46.46           C  
ANISOU 1882  CA  ASN A1132     4285   7669   5699     62   -350   -478       C  
ATOM   1883  C   ASN A1132     -25.133  25.721 -13.745  1.00 44.05           C  
ANISOU 1883  C   ASN A1132     4190   7167   5381    140   -351   -352       C  
ATOM   1884  O   ASN A1132     -24.930  26.818 -14.281  1.00 44.02           O  
ANISOU 1884  O   ASN A1132     4284   7111   5332    277   -479   -289       O  
ATOM   1885  CB  ASN A1132     -27.535  25.163 -13.254  1.00 48.51           C  
ANISOU 1885  CB  ASN A1132     4353   8084   5996    151   -340   -561       C  
ATOM   1886  CG  ASN A1132     -28.279  26.417 -13.662  1.00 50.57           C  
ANISOU 1886  CG  ASN A1132     4568   8432   6213    380   -510   -591       C  
ATOM   1887  OD1 ASN A1132     -28.818  26.500 -14.766  1.00 52.67           O  
ANISOU 1887  OD1 ASN A1132     4777   8805   6430    415   -632   -628       O  
ATOM   1888  ND2 ASN A1132     -28.330  27.396 -12.766  1.00 50.54           N  
ANISOU 1888  ND2 ASN A1132     4587   8389   6227    549   -529   -584       N  
ATOM   1889  N   LEU A1133     -24.322  25.229 -12.805  1.00 41.94           N  
ANISOU 1889  N   LEU A1133     3992   6785   5158     51   -216   -307       N  
ATOM   1890  CA  LEU A1133     -23.166  25.995 -12.350  1.00 40.84           C  
ANISOU 1890  CA  LEU A1133     4032   6472   5013    112   -218   -205       C  
ATOM   1891  C   LEU A1133     -22.049  26.005 -13.386  1.00 41.02           C  
ANISOU 1891  C   LEU A1133     4212   6386   4989     54   -252   -115       C  
ATOM   1892  O   LEU A1133     -21.273  26.966 -13.448  1.00 41.68           O  
ANISOU 1892  O   LEU A1133     4433   6347   5056    125   -311    -23       O  
ATOM   1893  CB  LEU A1133     -22.654  25.438 -11.022  1.00 39.62           C  
ANISOU 1893  CB  LEU A1133     3888   6262   4903     44    -71   -187       C  
ATOM   1894  CG  LEU A1133     -23.496  25.755  -9.784  1.00 40.60           C  
ANISOU 1894  CG  LEU A1133     3887   6495   5044    137    -33   -250       C  
ATOM   1895  CD1 LEU A1133     -23.038  24.924  -8.598  1.00 39.99           C  
ANISOU 1895  CD1 LEU A1133     3806   6402   4985     37    127   -214       C  
ATOM   1896  CD2 LEU A1133     -23.428  27.236  -9.456  1.00 41.17           C  
ANISOU 1896  CD2 LEU A1133     4027   6511   5106    337   -145   -257       C  
ATOM   1897  N   ALA A1134     -21.950  24.958 -14.206  1.00 40.46           N  
ANISOU 1897  N   ALA A1134     4116   6361   4896    -77   -215   -147       N  
ATOM   1898  CA  ALA A1134     -20.926  24.901 -15.242  1.00 39.04           C  
ANISOU 1898  CA  ALA A1134     4061   6125   4647   -128   -238    -80       C  
ATOM   1899  C   ALA A1134     -21.183  25.875 -16.384  1.00 39.78           C  
ANISOU 1899  C   ALA A1134     4187   6281   4645    -26   -390    -30       C  
ATOM   1900  O   ALA A1134     -20.332  25.993 -17.275  1.00 38.70           O  
ANISOU 1900  O   ALA A1134     4154   6124   4426    -59   -412     50       O  
ATOM   1901  CB  ALA A1134     -20.811  23.477 -15.787  1.00 38.65           C  
ANISOU 1901  CB  ALA A1134     3965   6118   4603   -278   -163   -163       C  
ATOM   1902  N   LYS A1135     -22.324  26.566 -16.387  1.00 40.85           N  
ANISOU 1902  N   LYS A1135     4235   6505   4782    101   -494    -66       N  
ATOM   1903  CA  LYS A1135     -22.623  27.586 -17.380  1.00 41.01           C  
ANISOU 1903  CA  LYS A1135     4294   6571   4718    225   -655      5       C  
ATOM   1904  C   LYS A1135     -22.301  28.995 -16.901  1.00 41.53           C  
ANISOU 1904  C   LYS A1135     4479   6478   4824    363   -734    121       C  
ATOM   1905  O   LYS A1135     -22.370  29.935 -17.699  1.00 43.96           O  
ANISOU 1905  O   LYS A1135     4855   6772   5075    464   -871    225       O  
ATOM   1906  CB  LYS A1135     -24.105  27.525 -17.775  1.00 41.22           C  
ANISOU 1906  CB  LYS A1135     4143   6796   4725    304   -749   -111       C  
ATOM   1907  CG  LYS A1135     -24.604  26.146 -18.167  1.00 40.16           C  
ANISOU 1907  CG  LYS A1135     3864   6814   4581    160   -686   -257       C  
ATOM   1908  CD  LYS A1135     -26.118  26.146 -18.298  1.00 41.35           C  
ANISOU 1908  CD  LYS A1135     3809   7164   4737    235   -772   -385       C  
ATOM   1909  CE  LYS A1135     -26.660  24.752 -18.558  1.00 41.76           C  
ANISOU 1909  CE  LYS A1135     3703   7347   4815     67   -707   -545       C  
ATOM   1910  NZ  LYS A1135     -28.148  24.734 -18.512  1.00 43.89           N  
ANISOU 1910  NZ  LYS A1135     3743   7823   5111    121   -776   -677       N  
ATOM   1911  N   SER A1136     -21.950  29.162 -15.629  1.00 39.50           N  
ANISOU 1911  N   SER A1136     4249   6097   4663    372   -659    106       N  
ATOM   1912  CA  SER A1136     -21.802  30.482 -15.040  1.00 40.03           C  
ANISOU 1912  CA  SER A1136     4406   6010   4792    514   -745    164       C  
ATOM   1913  C   SER A1136     -20.507  31.147 -15.494  1.00 39.05           C  
ANISOU 1913  C   SER A1136     4472   5710   4654    468   -775    334       C  
ATOM   1914  O   SER A1136     -19.569  30.496 -15.963  1.00 32.78           O  
ANISOU 1914  O   SER A1136     3732   4918   3805    321   -692    393       O  
ATOM   1915  CB  SER A1136     -21.830  30.393 -13.515  1.00 40.26           C  
ANISOU 1915  CB  SER A1136     4392   5997   4908    536   -652     71       C  
ATOM   1916  OG  SER A1136     -20.822  29.517 -13.041  1.00 39.84           O  
ANISOU 1916  OG  SER A1136     4382   5895   4859    378   -505     90       O  
ATOM   1917  N   ARG A1137     -20.472  32.474 -15.349  1.00 40.58           N  
ANISOU 1917  N   ARG A1137     4762   5749   4908    599   -900    407       N  
ATOM   1918  CA  ARG A1137     -19.240  33.217 -15.588  1.00 42.47           C  
ANISOU 1918  CA  ARG A1137     5175   5794   5167    541   -929    572       C  
ATOM   1919  C   ARG A1137     -18.178  32.873 -14.551  1.00 42.63           C  
ANISOU 1919  C   ARG A1137     5236   5715   5247    434   -801    542       C  
ATOM   1920  O   ARG A1137     -16.978  32.966 -14.836  1.00 42.71           O  
ANISOU 1920  O   ARG A1137     5349   5634   5245    315   -766    661       O  
ATOM   1921  CB  ARG A1137     -19.534  34.719 -15.588  1.00 45.17           C  
ANISOU 1921  CB  ARG A1137     5610   5958   5594    706  -1104    646       C  
ATOM   1922  CG  ARG A1137     -18.333  35.609 -15.868  1.00 46.71           C  
ANISOU 1922  CG  ARG A1137     5985   5929   5835    634  -1151    835       C  
ATOM   1923  CD  ARG A1137     -18.738  37.076 -15.908  1.00 49.94           C  
ANISOU 1923  CD  ARG A1137     6490   6130   6353    804  -1343    908       C  
ATOM   1924  NE  ARG A1137     -19.603  37.372 -17.047  1.00 52.96           N  
ANISOU 1924  NE  ARG A1137     6861   6608   6655    911  -1470   1004       N  
ATOM   1925  CZ  ARG A1137     -19.179  37.907 -18.188  1.00 55.58           C  
ANISOU 1925  CZ  ARG A1137     7308   6887   6923    866  -1550   1242       C  
ATOM   1926  NH1 ARG A1137     -20.036  38.140 -19.172  1.00 57.80           N  
ANISOU 1926  NH1 ARG A1137     7566   7282   7112    983  -1673   1322       N  
ATOM   1927  NH2 ARG A1137     -17.898  38.214 -18.343  1.00 56.00           N  
ANISOU 1927  NH2 ARG A1137     7489   6791   6996    702  -1507   1408       N  
ATOM   1928  N   TRP A1138     -18.602  32.470 -13.350  1.00 42.22           N  
ANISOU 1928  N   TRP A1138     5093   5702   5248    474   -730    389       N  
ATOM   1929  CA  TRP A1138     -17.660  32.025 -12.330  1.00 41.29           C  
ANISOU 1929  CA  TRP A1138     4997   5526   5163    383   -608    357       C  
ATOM   1930  C   TRP A1138     -16.907  30.778 -12.777  1.00 41.32           C  
ANISOU 1930  C   TRP A1138     4991   5611   5096    209   -475    394       C  
ATOM   1931  O   TRP A1138     -15.725  30.607 -12.455  1.00 40.31           O  
ANISOU 1931  O   TRP A1138     4929   5406   4979    115   -407    441       O  
ATOM   1932  CB  TRP A1138     -18.407  31.775 -11.018  1.00 40.32           C  
ANISOU 1932  CB  TRP A1138     4762   5479   5078    470   -556    198       C  
ATOM   1933  CG  TRP A1138     -17.682  30.912 -10.027  1.00 38.02           C  
ANISOU 1933  CG  TRP A1138     4454   5208   4782    371   -408    164       C  
ATOM   1934  CD1 TRP A1138     -16.514  31.202  -9.384  1.00 37.41           C  
ANISOU 1934  CD1 TRP A1138     4470   5008   4738    329   -385    194       C  
ATOM   1935  CD2 TRP A1138     -18.098  29.628  -9.544  1.00 36.77           C  
ANISOU 1935  CD2 TRP A1138     4179   5203   4591    303   -272     99       C  
ATOM   1936  NE1 TRP A1138     -16.169  30.172  -8.542  1.00 36.05           N  
ANISOU 1936  NE1 TRP A1138     4246   4913   4539    257   -247    158       N  
ATOM   1937  CE2 TRP A1138     -17.126  29.194  -8.620  1.00 35.60           C  
ANISOU 1937  CE2 TRP A1138     4067   5012   4446    237   -173    110       C  
ATOM   1938  CE3 TRP A1138     -19.194  28.800  -9.808  1.00 36.50           C  
ANISOU 1938  CE3 TRP A1138     4006   5332   4529    285   -228     39       C  
ATOM   1939  CZ2 TRP A1138     -17.217  27.971  -7.960  1.00 34.72           C  
ANISOU 1939  CZ2 TRP A1138     3877   5003   4313    162    -35     85       C  
ATOM   1940  CZ3 TRP A1138     -19.282  27.586  -9.151  1.00 35.55           C  
ANISOU 1940  CZ3 TRP A1138     3804   5302   4402    189    -86      8       C  
ATOM   1941  CH2 TRP A1138     -18.299  27.183  -8.238  1.00 34.91           C  
ANISOU 1941  CH2 TRP A1138     3777   5161   4325    132     10     42       C  
ATOM   1942  N   TYR A1139     -17.572  29.897 -13.529  1.00 42.79           N  
ANISOU 1942  N   TYR A1139     5089   5955   5215    171   -446    358       N  
ATOM   1943  CA  TYR A1139     -16.908  28.685 -13.998  1.00 43.15           C  
ANISOU 1943  CA  TYR A1139     5124   6067   5205     23   -332    365       C  
ATOM   1944  C   TYR A1139     -15.898  28.994 -15.095  1.00 43.61           C  
ANISOU 1944  C   TYR A1139     5284   6093   5192    -48   -359    498       C  
ATOM   1945  O   TYR A1139     -14.816  28.398 -15.133  1.00 43.16           O  
ANISOU 1945  O   TYR A1139     5261   6024   5116   -154   -266    525       O  
ATOM   1946  CB  TYR A1139     -17.938  27.671 -14.496  1.00 44.23           C  
ANISOU 1946  CB  TYR A1139     5132   6370   5304     -3   -306    263       C  
ATOM   1947  CG  TYR A1139     -17.322  26.471 -15.186  1.00 43.93           C  
ANISOU 1947  CG  TYR A1139     5089   6387   5214   -139   -216    248       C  
ATOM   1948  CD1 TYR A1139     -16.836  25.396 -14.452  1.00 43.02           C  
ANISOU 1948  CD1 TYR A1139     4955   6240   5151   -227    -86    200       C  
ATOM   1949  CD2 TYR A1139     -17.224  26.414 -16.572  1.00 44.61           C  
ANISOU 1949  CD2 TYR A1139     5190   6564   5195   -167   -268    279       C  
ATOM   1950  CE1 TYR A1139     -16.270  24.300 -15.078  1.00 42.79           C  
ANISOU 1950  CE1 TYR A1139     4925   6241   5093   -330    -16    167       C  
ATOM   1951  CE2 TYR A1139     -16.659  25.323 -17.206  1.00 44.33           C  
ANISOU 1951  CE2 TYR A1139     5145   6589   5110   -273   -191    233       C  
ATOM   1952  CZ  TYR A1139     -16.185  24.269 -16.454  1.00 43.51           C  
ANISOU 1952  CZ  TYR A1139     5024   6425   5081   -350    -68    169       C  
ATOM   1953  OH  TYR A1139     -15.623  23.181 -17.081  1.00 43.81           O  
ANISOU 1953  OH  TYR A1139     5055   6503   5087   -436     -3    105       O  
ATOM   1954  N   ASN A1140     -16.229  29.918 -15.997  1.00 44.45           N  
ANISOU 1954  N   ASN A1140     5436   6201   5253     15   -484    590       N  
ATOM   1955  CA  ASN A1140     -15.368  30.179 -17.143  1.00 44.76           C  
ANISOU 1955  CA  ASN A1140     5556   6255   5195    -61   -502    738       C  
ATOM   1956  C   ASN A1140     -14.163  31.048 -16.804  1.00 44.98           C  
ANISOU 1956  C   ASN A1140     5701   6110   5280   -109   -507    869       C  
ATOM   1957  O   ASN A1140     -13.186  31.045 -17.561  1.00 45.67           O  
ANISOU 1957  O   ASN A1140     5837   6227   5289   -212   -473    986       O  
ATOM   1958  CB  ASN A1140     -16.177  30.827 -18.267  1.00 46.78           C  
ANISOU 1958  CB  ASN A1140     5818   6591   5366     22   -639    817       C  
ATOM   1959  CG  ASN A1140     -17.249  29.906 -18.813  1.00 47.58           C  
ANISOU 1959  CG  ASN A1140     5790   6897   5391     45   -640    681       C  
ATOM   1960  OD1 ASN A1140     -16.982  29.064 -19.671  1.00 47.90           O  
ANISOU 1960  OD1 ASN A1140     5797   7083   5318    -40   -588    656       O  
ATOM   1961  ND2 ASN A1140     -18.471  30.057 -18.314  1.00 47.93           N  
ANISOU 1961  ND2 ASN A1140     5748   6964   5499    159   -701    578       N  
ATOM   1962  N   GLN A1141     -14.201  31.784 -15.693  1.00 44.53           N  
ANISOU 1962  N   GLN A1141     5677   5890   5351    -42   -547    842       N  
ATOM   1963  CA  GLN A1141     -13.070  32.625 -15.316  1.00 44.04           C  
ANISOU 1963  CA  GLN A1141     5717   5652   5363   -100   -563    944       C  
ATOM   1964  C   GLN A1141     -12.045  31.881 -14.468  1.00 42.16           C  
ANISOU 1964  C   GLN A1141     5456   5413   5151   -194   -432    878       C  
ATOM   1965  O   GLN A1141     -10.838  32.077 -14.647  1.00 43.54           O  
ANISOU 1965  O   GLN A1141     5680   5541   5322   -304   -399    975       O  
ATOM   1966  CB  GLN A1141     -13.560  33.870 -14.573  1.00 45.36           C  
ANISOU 1966  CB  GLN A1141     5939   5631   5664     28   -692    927       C  
ATOM   1967  CG  GLN A1141     -14.261  34.880 -15.467  1.00 47.74           C  
ANISOU 1967  CG  GLN A1141     6301   5874   5964    121   -848   1046       C  
ATOM   1968  CD  GLN A1141     -14.541  36.193 -14.761  1.00 49.38           C  
ANISOU 1968  CD  GLN A1141     6585   5847   6332    247   -989   1033       C  
ATOM   1969  OE1 GLN A1141     -14.550  36.261 -13.532  1.00 48.88           O  
ANISOU 1969  OE1 GLN A1141     6496   5715   6361    301   -971    881       O  
ATOM   1970  NE2 GLN A1141     -14.764  37.246 -15.539  1.00 51.44           N  
ANISOU 1970  NE2 GLN A1141     6941   5983   6622    301  -1134   1192       N  
ATOM   1971  N   THR A1142     -12.496  31.035 -13.544  1.00 39.70           N  
ANISOU 1971  N   THR A1142     5064   5159   4861   -154   -357    728       N  
ATOM   1972  CA  THR A1142     -11.612  30.213 -12.717  1.00 37.76           C  
ANISOU 1972  CA  THR A1142     4793   4925   4629   -224   -237    672       C  
ATOM   1973  C   THR A1142     -12.058  28.760 -12.818  1.00 35.71           C  
ANISOU 1973  C   THR A1142     4443   4809   4316   -247   -132    584       C  
ATOM   1974  O   THR A1142     -12.592  28.191 -11.859  1.00 34.14           O  
ANISOU 1974  O   THR A1142     4184   4634   4153   -207    -81    487       O  
ATOM   1975  CB  THR A1142     -11.616  30.682 -11.261  1.00 39.00           C  
ANISOU 1975  CB  THR A1142     4953   4986   4878   -152   -254    590       C  
ATOM   1976  OG1 THR A1142     -12.947  30.598 -10.736  1.00 39.79           O  
ANISOU 1976  OG1 THR A1142     4985   5141   4992    -34   -275    483       O  
ATOM   1977  CG2 THR A1142     -11.119  32.117 -11.157  1.00 40.84           C  
ANISOU 1977  CG2 THR A1142     5281   5045   5193   -139   -371    656       C  
ATOM   1978  N   PRO A1143     -11.845  28.125 -13.975  1.00 35.82           N  
ANISOU 1978  N   PRO A1143     4444   4921   4244   -317    -98    615       N  
ATOM   1979  CA  PRO A1143     -12.383  26.769 -14.165  1.00 34.75           C  
ANISOU 1979  CA  PRO A1143     4227   4897   4081   -340    -20    511       C  
ATOM   1980  C   PRO A1143     -11.679  25.711 -13.340  1.00 32.39           C  
ANISOU 1980  C   PRO A1143     3906   4578   3822   -387     98    459       C  
ATOM   1981  O   PRO A1143     -12.308  24.707 -12.984  1.00 31.86           O  
ANISOU 1981  O   PRO A1143     3776   4546   3786   -392    156    373       O  
ATOM   1982  CB  PRO A1143     -12.201  26.528 -15.670  1.00 36.07           C  
ANISOU 1982  CB  PRO A1143     4395   5176   4135   -392    -32    546       C  
ATOM   1983  CG  PRO A1143     -11.050  27.394 -16.046  1.00 36.85           C  
ANISOU 1983  CG  PRO A1143     4572   5230   4199   -437    -52    686       C  
ATOM   1984  CD  PRO A1143     -11.149  28.618 -15.177  1.00 37.09           C  
ANISOU 1984  CD  PRO A1143     4660   5108   4325   -380   -131    741       C  
ATOM   1985  N   ASN A1144     -10.397  25.896 -13.022  1.00 31.89           N  
ANISOU 1985  N   ASN A1144     3890   4460   3767   -425    131    515       N  
ATOM   1986  CA  ASN A1144      -9.687  24.874 -12.261  1.00 31.89           C  
ANISOU 1986  CA  ASN A1144     3869   4447   3800   -450    231    475       C  
ATOM   1987  C   ASN A1144     -10.200  24.778 -10.829  1.00 32.74           C  
ANISOU 1987  C   ASN A1144     3955   4511   3973   -392    251    435       C  
ATOM   1988  O   ASN A1144     -10.242  23.681 -10.261  1.00 33.10           O  
ANISOU 1988  O   ASN A1144     3966   4565   4045   -402    332    397       O  
ATOM   1989  CB  ASN A1144      -8.185  25.150 -12.277  1.00 31.47           C  
ANISOU 1989  CB  ASN A1144     3851   4373   3733   -495    253    539       C  
ATOM   1990  CG  ASN A1144      -7.377  23.972 -11.777  1.00 31.77           C  
ANISOU 1990  CG  ASN A1144     3862   4419   3790   -508    349    498       C  
ATOM   1991  OD1 ASN A1144      -7.182  23.805 -10.573  1.00 32.19           O  
ANISOU 1991  OD1 ASN A1144     3913   4426   3893   -472    373    488       O  
ATOM   1992  ND2 ASN A1144      -6.907  23.140 -12.700  1.00 32.22           N  
ANISOU 1992  ND2 ASN A1144     3897   4543   3802   -544    400    469       N  
ATOM   1993  N   ARG A1145     -10.599  25.904 -10.236  1.00 33.08           N  
ANISOU 1993  N   ARG A1145     4018   4512   4040   -328    176    443       N  
ATOM   1994  CA  ARG A1145     -11.165  25.925  -8.891  1.00 33.28           C  
ANISOU 1994  CA  ARG A1145     4010   4537   4100   -258    191    391       C  
ATOM   1995  C   ARG A1145     -12.656  25.619  -8.880  1.00 34.58           C  
ANISOU 1995  C   ARG A1145     4097   4774   4266   -220    193    331       C  
ATOM   1996  O   ARG A1145     -13.127  24.868  -8.017  1.00 35.32           O  
ANISOU 1996  O   ARG A1145     4131   4917   4371   -214    267    299       O  
ATOM   1997  CB  ARG A1145     -10.925  27.282  -8.233  1.00 33.60           C  
ANISOU 1997  CB  ARG A1145     4095   4505   4167   -192    102    390       C  
ATOM   1998  CG  ARG A1145     -11.501  27.388  -6.831  1.00 34.25           C  
ANISOU 1998  CG  ARG A1145     4134   4622   4257   -101    114    315       C  
ATOM   1999  CD  ARG A1145     -11.183  28.729  -6.201  1.00 35.41           C  
ANISOU 1999  CD  ARG A1145     4329   4687   4440    -29     13    279       C  
ATOM   2000  NE  ARG A1145     -11.721  28.841  -4.850  1.00 35.60           N  
ANISOU 2000  NE  ARG A1145     4302   4780   4446     74     25    185       N  
ATOM   2001  CZ  ARG A1145     -11.579  29.916  -4.083  1.00 36.44           C  
ANISOU 2001  CZ  ARG A1145     4432   4834   4578    160    -61    106       C  
ATOM   2002  NH1 ARG A1145     -10.915  30.970  -4.536  1.00 36.70           N  
ANISOU 2002  NH1 ARG A1145     4548   4714   4681    140   -169    125       N  
ATOM   2003  NH2 ARG A1145     -12.100  29.939  -2.864  1.00 37.34           N  
ANISOU 2003  NH2 ARG A1145     4486   5052   4648    263    -41      6       N  
ATOM   2004  N   ALA A1146     -13.411  26.194  -9.818  1.00 35.75           N  
ANISOU 2004  N   ALA A1146     4238   4942   4401   -196    111    325       N  
ATOM   2005  CA  ALA A1146     -14.852  25.968  -9.851  1.00 37.16           C  
ANISOU 2005  CA  ALA A1146     4323   5213   4584   -156    101    256       C  
ATOM   2006  C   ALA A1146     -15.185  24.500 -10.076  1.00 37.42           C  
ANISOU 2006  C   ALA A1146     4286   5309   4622   -248    198    222       C  
ATOM   2007  O   ALA A1146     -16.197  24.009  -9.565  1.00 37.57           O  
ANISOU 2007  O   ALA A1146     4208   5402   4664   -245    238    170       O  
ATOM   2008  CB  ALA A1146     -15.492  26.834 -10.936  1.00 37.76           C  
ANISOU 2008  CB  ALA A1146     4407   5305   4636   -105    -19    265       C  
ATOM   2009  N   LYS A1147     -14.339  23.781 -10.816  1.00 37.48           N  
ANISOU 2009  N   LYS A1147     4336   5290   4617   -331    237    246       N  
ATOM   2010  CA  LYS A1147     -14.598  22.372 -11.092  1.00 37.26           C  
ANISOU 2010  CA  LYS A1147     4253   5285   4617   -417    314    195       C  
ATOM   2011  C   LYS A1147     -14.520  21.525  -9.827  1.00 35.08           C  
ANISOU 2011  C   LYS A1147     3954   4974   4400   -441    416    210       C  
ATOM   2012  O   LYS A1147     -15.268  20.549  -9.689  1.00 35.64           O  
ANISOU 2012  O   LYS A1147     3954   5066   4523   -503    471    174       O  
ATOM   2013  CB  LYS A1147     -13.618  21.859 -12.141  1.00 39.02           C  
ANISOU 2013  CB  LYS A1147     4528   5490   4809   -475    326    196       C  
ATOM   2014  CG  LYS A1147     -14.183  20.773 -13.030  1.00 42.59           C  
ANISOU 2014  CG  LYS A1147     4921   5987   5274   -543    341    101       C  
ATOM   2015  CD  LYS A1147     -13.347  20.594 -14.286  1.00 47.29           C  
ANISOU 2015  CD  LYS A1147     5557   6615   5795   -568    326     80       C  
ATOM   2016  CE  LYS A1147     -14.087  19.750 -15.310  1.00 51.81           C  
ANISOU 2016  CE  LYS A1147     6063   7263   6360   -618    307    -47       C  
ATOM   2017  NZ  LYS A1147     -15.444  20.299 -15.577  1.00 53.14           N  
ANISOU 2017  NZ  LYS A1147     6158   7526   6507   -594    226    -77       N  
ATOM   2018  N   ARG A1148     -13.635  21.878  -8.894  1.00 32.88           N  
ANISOU 2018  N   ARG A1148     3732   4648   4114   -399    438    269       N  
ATOM   2019  CA  ARG A1148     -13.536  21.110  -7.656  1.00 31.89           C  
ANISOU 2019  CA  ARG A1148     3589   4510   4019   -409    529    305       C  
ATOM   2020  C   ARG A1148     -14.696  21.418  -6.718  1.00 31.78           C  
ANISOU 2020  C   ARG A1148     3490   4589   3995   -366    543    290       C  
ATOM   2021  O   ARG A1148     -15.221  20.516  -6.055  1.00 32.44           O  
ANISOU 2021  O   ARG A1148     3514   4704   4108   -415    628    315       O  
ATOM   2022  CB  ARG A1148     -12.201  21.388  -6.965  1.00 30.82           C  
ANISOU 2022  CB  ARG A1148     3527   4323   3859   -368    538    363       C  
ATOM   2023  CG  ARG A1148     -10.991  20.824  -7.697  1.00 30.42           C  
ANISOU 2023  CG  ARG A1148     3532   4205   3819   -410    554    378       C  
ATOM   2024  CD  ARG A1148      -9.708  21.048  -6.907  1.00 29.87           C  
ANISOU 2024  CD  ARG A1148     3510   4110   3729   -369    562    430       C  
ATOM   2025  NE  ARG A1148      -9.379  22.465  -6.792  1.00 29.58           N  
ANISOU 2025  NE  ARG A1148     3500   4084   3655   -325    481    428       N  
ATOM   2026  CZ  ARG A1148      -8.571  23.113  -7.625  1.00 22.25           C  
ANISOU 2026  CZ  ARG A1148     2609   3133   2711   -349    431    439       C  
ATOM   2027  NH1 ARG A1148      -8.003  22.468  -8.634  1.00 22.23           N  
ANISOU 2027  NH1 ARG A1148     2612   3131   2704   -402    460    440       N  
ATOM   2028  NH2 ARG A1148      -8.330  24.405  -7.448  1.00 22.34           N  
ANISOU 2028  NH2 ARG A1148     2649   3124   2714   -322    352    446       N  
ATOM   2029  N   VAL A1149     -15.106  22.687  -6.644  1.00 31.25           N  
ANISOU 2029  N   VAL A1149     3414   4569   3891   -274    460    252       N  
ATOM   2030  CA  VAL A1149     -16.247  23.051  -5.808  1.00 31.10           C  
ANISOU 2030  CA  VAL A1149     3297   4667   3853   -209    468    210       C  
ATOM   2031  C   VAL A1149     -17.524  22.427  -6.354  1.00 31.34           C  
ANISOU 2031  C   VAL A1149     3211   4781   3915   -272    489    165       C  
ATOM   2032  O   VAL A1149     -18.383  21.963  -5.594  1.00 33.19           O  
ANISOU 2032  O   VAL A1149     3338   5122   4152   -293    563    162       O  
ATOM   2033  CB  VAL A1149     -16.368  24.583  -5.703  1.00 30.94           C  
ANISOU 2033  CB  VAL A1149     3300   4652   3805    -76    355    156       C  
ATOM   2034  CG1 VAL A1149     -17.545  24.966  -4.816  1.00 31.39           C  
ANISOU 2034  CG1 VAL A1149     3240   4853   3833     17    364     85       C  
ATOM   2035  CG2 VAL A1149     -15.077  25.183  -5.174  1.00 30.59           C  
ANISOU 2035  CG2 VAL A1149     3361   4517   3745    -37    327    187       C  
ATOM   2036  N   ILE A1150     -17.666  22.403  -7.680  1.00 30.22           N  
ANISOU 2036  N   ILE A1150     3080   4611   3792   -310    425    131       N  
ATOM   2037  CA  ILE A1150     -18.838  21.791  -8.295  1.00 27.36           C  
ANISOU 2037  CA  ILE A1150     2600   4335   3463   -378    429     68       C  
ATOM   2038  C   ILE A1150     -18.856  20.290  -8.038  1.00 34.88           C  
ANISOU 2038  C   ILE A1150     3516   5251   4484   -521    543     94       C  
ATOM   2039  O   ILE A1150     -19.905  19.714  -7.725  1.00 35.83           O  
ANISOU 2039  O   ILE A1150     3509   5459   4645   -588    595     71       O  
ATOM   2040  CB  ILE A1150     -18.869  22.116  -9.799  1.00 27.41           C  
ANISOU 2040  CB  ILE A1150     2632   4333   3448   -376    324     24       C  
ATOM   2041  CG1 ILE A1150     -19.299  23.568 -10.014  1.00 28.65           C  
ANISOU 2041  CG1 ILE A1150     2792   4538   3557   -233    202      6       C  
ATOM   2042  CG2 ILE A1150     -19.782  21.156 -10.542  1.00 28.39           C  
ANISOU 2042  CG2 ILE A1150     2647   4526   3613   -480    333    -55       C  
ATOM   2043  CD1 ILE A1150     -19.093  24.059 -11.424  1.00 27.84           C  
ANISOU 2043  CD1 ILE A1150     2748   4420   3409   -217     93     12       C  
ATOM   2044  N   THR A1151     -17.699  19.635  -8.155  1.00 34.44           N  
ANISOU 2044  N   THR A1151     3567   5063   4453   -571    581    146       N  
ATOM   2045  CA  THR A1151     -17.640  18.196  -7.919  1.00 35.97           C  
ANISOU 2045  CA  THR A1151     3749   5180   4737   -694    677    177       C  
ATOM   2046  C   THR A1151     -18.014  17.857  -6.480  1.00 38.58           C  
ANISOU 2046  C   THR A1151     4026   5558   5076   -710    776    268       C  
ATOM   2047  O   THR A1151     -18.643  16.824  -6.220  1.00 39.23           O  
ANISOU 2047  O   THR A1151     4036   5630   5238   -830    851    295       O  
ATOM   2048  CB  THR A1151     -16.245  17.670  -8.254  1.00 34.44           C  
ANISOU 2048  CB  THR A1151     3681   4841   4564   -704    688    209       C  
ATOM   2049  OG1 THR A1151     -15.916  18.026  -9.603  1.00 34.40           O  
ANISOU 2049  OG1 THR A1151     3713   4836   4524   -690    606    130       O  
ATOM   2050  CG2 THR A1151     -16.195  16.155  -8.109  1.00 34.55           C  
ANISOU 2050  CG2 THR A1151     3695   4738   4695   -819    768    232       C  
ATOM   2051  N   THR A1152     -17.644  18.722  -5.532  1.00 39.84           N  
ANISOU 2051  N   THR A1152     4214   5774   5148   -597    776    315       N  
ATOM   2052  CA  THR A1152     -18.034  18.505  -4.143  1.00 41.64           C  
ANISOU 2052  CA  THR A1152     4380   6099   5343   -594    870    396       C  
ATOM   2053  C   THR A1152     -19.546  18.596  -3.977  1.00 44.33           C  
ANISOU 2053  C   THR A1152     4552   6611   5681   -624    894    347       C  
ATOM   2054  O   THR A1152     -20.144  17.817  -3.226  1.00 45.47           O  
ANISOU 2054  O   THR A1152     4608   6824   5846   -715   1000    423       O  
ATOM   2055  CB  THR A1152     -17.331  19.516  -3.237  1.00 40.63           C  
ANISOU 2055  CB  THR A1152     4310   6020   5108   -450    845    415       C  
ATOM   2056  OG1 THR A1152     -15.916  19.458  -3.461  1.00 41.36           O  
ANISOU 2056  OG1 THR A1152     4539   5970   5207   -431    816    452       O  
ATOM   2057  CG2 THR A1152     -17.617  19.211  -1.775  1.00 40.12           C  
ANISOU 2057  CG2 THR A1152     4185   6082   4977   -439    947    504       C  
ATOM   2058  N   PHE A1153     -20.183  19.542  -4.673  1.00 45.42           N  
ANISOU 2058  N   PHE A1153     4635   6828   5794   -549    797    229       N  
ATOM   2059  CA  PHE A1153     -21.639  19.629  -4.644  1.00 48.11           C  
ANISOU 2059  CA  PHE A1153     4794   7348   6137   -567    807    161       C  
ATOM   2060  C   PHE A1153     -22.287  18.373  -5.212  1.00 52.19           C  
ANISOU 2060  C   PHE A1153     5225   7838   6765   -757    857    160       C  
ATOM   2061  O   PHE A1153     -23.367  17.973  -4.761  1.00 54.55           O  
ANISOU 2061  O   PHE A1153     5361   8281   7085   -837    928    162       O  
ATOM   2062  CB  PHE A1153     -22.106  20.861  -5.422  1.00 46.68           C  
ANISOU 2062  CB  PHE A1153     4587   7230   5919   -432    669     38       C  
ATOM   2063  CG  PHE A1153     -21.990  22.148  -4.655  1.00 46.72           C  
ANISOU 2063  CG  PHE A1153     4612   7305   5836   -245    622      7       C  
ATOM   2064  CD1 PHE A1153     -22.385  22.219  -3.329  1.00 47.67           C  
ANISOU 2064  CD1 PHE A1153     4642   7580   5891   -199    709     21       C  
ATOM   2065  CD2 PHE A1153     -21.486  23.288  -5.261  1.00 46.08           C  
ANISOU 2065  CD2 PHE A1153     4637   7134   5737   -119    488    -38       C  
ATOM   2066  CE1 PHE A1153     -22.283  23.403  -2.622  1.00 47.88           C  
ANISOU 2066  CE1 PHE A1153     4682   7670   5838    -15    655    -43       C  
ATOM   2067  CE2 PHE A1153     -21.380  24.475  -4.558  1.00 46.39           C  
ANISOU 2067  CE2 PHE A1153     4700   7203   5722     50    431    -85       C  
ATOM   2068  CZ  PHE A1153     -21.779  24.531  -3.237  1.00 47.33           C  
ANISOU 2068  CZ  PHE A1153     4727   7476   5779    109    511   -104       C  
ATOM   2069  N   ARG A1154     -21.646  17.740  -6.194  1.00 54.32           N  
ANISOU 2069  N   ARG A1154     5594   7934   7111   -835    822    145       N  
ATOM   2070  CA  ARG A1154     -22.183  16.543  -6.829  1.00 57.22           C  
ANISOU 2070  CA  ARG A1154     5894   8244   7603  -1014    848    111       C  
ATOM   2071  C   ARG A1154     -22.193  15.359  -5.872  1.00 56.29           C  
ANISOU 2071  C   ARG A1154     5761   8058   7570  -1156    984    245       C  
ATOM   2072  O   ARG A1154     -23.252  14.955  -5.382  1.00 58.00           O  
ANISOU 2072  O   ARG A1154     5821   8393   7824  -1262   1056    269       O  
ATOM   2073  CB  ARG A1154     -21.372  16.197  -8.082  1.00 59.40           C  
ANISOU 2073  CB  ARG A1154     6290   8357   7923  -1034    773     42       C  
ATOM   2074  CG  ARG A1154     -21.801  16.950  -9.324  1.00 61.24           C  
ANISOU 2074  CG  ARG A1154     6486   8681   8102   -970    644    -94       C  
ATOM   2075  CD  ARG A1154     -22.977  16.266  -9.999  1.00 65.16           C  
ANISOU 2075  CD  ARG A1154     6826   9252   8680  -1101    623   -209       C  
ATOM   2076  NE  ARG A1154     -22.545  15.175 -10.868  1.00 68.11           N  
ANISOU 2076  NE  ARG A1154     7255   9473   9149  -1219    613   -278       N  
ATOM   2077  CZ  ARG A1154     -22.368  15.294 -12.181  1.00 69.46           C  
ANISOU 2077  CZ  ARG A1154     7455   9657   9281  -1192    509   -402       C  
ATOM   2078  NH1 ARG A1154     -22.593  16.456 -12.779  1.00 68.83           N  
ANISOU 2078  NH1 ARG A1154     7360   9721   9071  -1059    406   -440       N  
ATOM   2079  NH2 ARG A1154     -21.971  14.250 -12.896  1.00 70.94           N  
ANISOU 2079  NH2 ARG A1154     7685   9714   9554  -1290    503   -488       N  
ATOM   2080  N   THR A1155     -21.012  14.799  -5.603  1.00 53.49           N  
ANISOU 2080  N   THR A1155     5561   7519   7245  -1159   1018    342       N  
ATOM   2081  CA  THR A1155     -20.904  13.599  -4.779  1.00 53.84           C  
ANISOU 2081  CA  THR A1155     5619   7455   7382  -1288   1133    494       C  
ATOM   2082  C   THR A1155     -21.144  13.875  -3.300  1.00 53.86           C  
ANISOU 2082  C   THR A1155     5567   7616   7281  -1250   1233    642       C  
ATOM   2083  O   THR A1155     -21.558  12.969  -2.567  1.00 56.33           O  
ANISOU 2083  O   THR A1155     5827   7922   7655  -1384   1340    781       O  
ATOM   2084  CB  THR A1155     -19.525  12.963  -4.952  1.00 53.14           C  
ANISOU 2084  CB  THR A1155     5711   7127   7351  -1268   1125    547       C  
ATOM   2085  OG1 THR A1155     -18.513  13.936  -4.671  1.00 50.96           O  
ANISOU 2085  OG1 THR A1155     5537   6887   6939  -1091   1085    563       O  
ATOM   2086  CG2 THR A1155     -19.344  12.444  -6.371  1.00 53.44           C  
ANISOU 2086  CG2 THR A1155     5787   7019   7498  -1325   1045    395       C  
ATOM   2087  N   GLY A1156     -20.890  15.096  -2.838  1.00 51.36           N  
ANISOU 2087  N   GLY A1156     5264   7444   6807  -1072   1198    616       N  
ATOM   2088  CA  GLY A1156     -20.922  15.344  -1.412  1.00 50.88           C  
ANISOU 2088  CA  GLY A1156     5169   7539   6624  -1012   1286    739       C  
ATOM   2089  C   GLY A1156     -19.734  14.781  -0.673  1.00 50.08           C  
ANISOU 2089  C   GLY A1156     5213   7308   6508   -992   1333    901       C  
ATOM   2090  O   GLY A1156     -19.813  14.573   0.540  1.00 51.93           O  
ANISOU 2090  O   GLY A1156     5416   7659   6657   -990   1428   1046       O  
ATOM   2091  N   THR A1157     -18.636  14.523  -1.375  1.00 47.83           N  
ANISOU 2091  N   THR A1157     5076   6805   6291   -970   1268    879       N  
ATOM   2092  CA  THR A1157     -17.418  13.961  -0.812  1.00 47.19           C  
ANISOU 2092  CA  THR A1157     5131   6588   6210   -933   1293   1014       C  
ATOM   2093  C   THR A1157     -16.253  14.910  -1.077  1.00 45.37           C  
ANISOU 2093  C   THR A1157     5007   6335   5898   -773   1197    930       C  
ATOM   2094  O   THR A1157     -16.425  16.010  -1.606  1.00 44.13           O  
ANISOU 2094  O   THR A1157     4826   6257   5686   -697   1118    792       O  
ATOM   2095  CB  THR A1157     -17.128  12.576  -1.401  1.00 47.46           C  
ANISOU 2095  CB  THR A1157     5234   6366   6432  -1065   1309   1065       C  
ATOM   2096  OG1 THR A1157     -16.578  12.724  -2.715  1.00 46.32           O  
ANISOU 2096  OG1 THR A1157     5155   6093   6351  -1037   1211    903       O  
ATOM   2097  CG2 THR A1157     -18.407  11.753  -1.488  1.00 49.80           C  
ANISOU 2097  CG2 THR A1157     5410   6662   6850  -1257   1377   1096       C  
ATOM   2098  N   TRP A1158     -15.053  14.462  -0.712  1.00 45.58           N  
ANISOU 2098  N   TRP A1158     5148   6246   5926   -724   1200   1024       N  
ATOM   2099  CA  TRP A1158     -13.829  15.234  -0.890  1.00 43.63           C  
ANISOU 2099  CA  TRP A1158     4990   5975   5612   -593   1119    962       C  
ATOM   2100  C   TRP A1158     -12.940  14.653  -1.986  1.00 42.65           C  
ANISOU 2100  C   TRP A1158     4953   5650   5600   -615   1073    912       C  
ATOM   2101  O   TRP A1158     -11.718  14.813  -1.947  1.00 41.53           O  
ANISOU 2101  O   TRP A1158     4888   5463   5428   -528   1036    917       O  
ATOM   2102  CB  TRP A1158     -13.054  15.315   0.424  1.00 43.64           C  
ANISOU 2102  CB  TRP A1158     5031   6053   5498   -494   1145   1084       C  
ATOM   2103  CG  TRP A1158     -13.805  15.964   1.546  1.00 43.48           C  
ANISOU 2103  CG  TRP A1158     4922   6266   5332   -446   1187   1111       C  
ATOM   2104  CD1 TRP A1158     -14.538  15.339   2.513  1.00 44.47           C  
ANISOU 2104  CD1 TRP A1158     4980   6503   5414   -501   1292   1256       C  
ATOM   2105  CD2 TRP A1158     -13.885  17.367   1.825  1.00 42.44           C  
ANISOU 2105  CD2 TRP A1158     4755   6293   5079   -329   1123    984       C  
ATOM   2106  NE1 TRP A1158     -15.074  16.267   3.375  1.00 44.39           N  
ANISOU 2106  NE1 TRP A1158     4882   6742   5240   -414   1305   1213       N  
ATOM   2107  CE2 TRP A1158     -14.688  17.519   2.974  1.00 43.43           C  
ANISOU 2107  CE2 TRP A1158     4783   6639   5078   -301   1195   1035       C  
ATOM   2108  CE3 TRP A1158     -13.359  18.509   1.214  1.00 40.92           C  
ANISOU 2108  CE3 TRP A1158     4602   6071   4876   -248   1012    836       C  
ATOM   2109  CZ2 TRP A1158     -14.977  18.768   3.523  1.00 43.54           C  
ANISOU 2109  CZ2 TRP A1158     4740   6840   4962   -176   1150    911       C  
ATOM   2110  CZ3 TRP A1158     -13.646  19.747   1.760  1.00 41.03           C  
ANISOU 2110  CZ3 TRP A1158     4571   6237   4782   -138    962    732       C  
ATOM   2111  CH2 TRP A1158     -14.447  19.866   2.903  1.00 42.32           C  
ANISOU 2111  CH2 TRP A1158     4639   6615   4827    -93   1028    754       C  
ATOM   2112  N   ASP A1159     -13.539  13.977  -2.970  1.00 43.16           N  
ANISOU 2112  N   ASP A1159     4995   5613   5791   -726   1074    846       N  
ATOM   2113  CA  ASP A1159     -12.742  13.299  -3.989  1.00 43.45           C  
ANISOU 2113  CA  ASP A1159     5106   5474   5931   -739   1037    779       C  
ATOM   2114  C   ASP A1159     -11.974  14.283  -4.862  1.00 42.45           C  
ANISOU 2114  C   ASP A1159     5011   5390   5729   -656    954    658       C  
ATOM   2115  O   ASP A1159     -10.879  13.961  -5.337  1.00 42.40           O  
ANISOU 2115  O   ASP A1159     5070   5293   5748   -614    931    632       O  
ATOM   2116  CB  ASP A1159     -13.635  12.412  -4.854  1.00 45.49           C  
ANISOU 2116  CB  ASP A1159     5320   5631   6333   -878   1046    704       C  
ATOM   2117  CG  ASP A1159     -14.247  11.268  -4.074  1.00 48.05           C  
ANISOU 2117  CG  ASP A1159     5624   5864   6770   -990   1130    843       C  
ATOM   2118  OD1 ASP A1159     -14.058  11.222  -2.840  1.00 48.73           O  
ANISOU 2118  OD1 ASP A1159     5724   5996   6794   -953   1189   1013       O  
ATOM   2119  OD2 ASP A1159     -14.916  10.414  -4.693  1.00 49.83           O  
ANISOU 2119  OD2 ASP A1159     5816   5974   7143  -1122   1136    787       O  
ATOM   2120  N   ALA A1160     -12.520  15.480  -5.082  1.00 42.08           N  
ANISOU 2120  N   ALA A1160     4916   5480   5594   -629    907    591       N  
ATOM   2121  CA  ALA A1160     -11.849  16.468  -5.917  1.00 41.98           C  
ANISOU 2121  CA  ALA A1160     4936   5499   5515   -568    827    507       C  
ATOM   2122  C   ALA A1160     -10.590  17.034  -5.272  1.00 42.91           C  
ANISOU 2122  C   ALA A1160     5112   5630   5561   -473    810    560       C  
ATOM   2123  O   ALA A1160      -9.818  17.713  -5.957  1.00 42.59           O  
ANISOU 2123  O   ALA A1160     5103   5598   5483   -442    754    511       O  
ATOM   2124  CB  ALA A1160     -12.811  17.607  -6.258  1.00 41.16           C  
ANISOU 2124  CB  ALA A1160     4773   5513   5351   -555    770    440       C  
ATOM   2125  N   TYR A1161     -10.363  16.772  -3.988  1.00 44.71           N  
ANISOU 2125  N   TYR A1161     5347   5875   5764   -433    856    662       N  
ATOM   2126  CA  TYR A1161      -9.201  17.275  -3.273  1.00 45.27           C  
ANISOU 2126  CA  TYR A1161     5458   5980   5763   -341    833    701       C  
ATOM   2127  C   TYR A1161      -8.391  16.110  -2.724  1.00 50.01           C  
ANISOU 2127  C   TYR A1161     6098   6497   6404   -318    880    799       C  
ATOM   2128  O   TYR A1161      -8.931  15.033  -2.451  1.00 50.66           O  
ANISOU 2128  O   TYR A1161     6181   6509   6560   -369    941    874       O  
ATOM   2129  CB  TYR A1161      -9.617  18.212  -2.130  1.00 41.72           C  
ANISOU 2129  CB  TYR A1161     4975   5667   5212   -278    822    719       C  
ATOM   2130  CG  TYR A1161     -10.453  19.388  -2.584  1.00 38.67           C  
ANISOU 2130  CG  TYR A1161     4549   5346   4797   -274    764    620       C  
ATOM   2131  CD1 TYR A1161     -11.837  19.294  -2.665  1.00 37.68           C  
ANISOU 2131  CD1 TYR A1161     4354   5275   4688   -316    792    599       C  
ATOM   2132  CD2 TYR A1161      -9.858  20.592  -2.936  1.00 36.89           C  
ANISOU 2132  CD2 TYR A1161     4354   5124   4540   -229    676    554       C  
ATOM   2133  CE1 TYR A1161     -12.604  20.366  -3.083  1.00 36.31           C  
ANISOU 2133  CE1 TYR A1161     4142   5162   4492   -288    726    507       C  
ATOM   2134  CE2 TYR A1161     -10.617  21.670  -3.354  1.00 35.73           C  
ANISOU 2134  CE2 TYR A1161     4185   5009   4383   -211    609    477       C  
ATOM   2135  CZ  TYR A1161     -11.989  21.552  -3.426  1.00 35.18           C  
ANISOU 2135  CZ  TYR A1161     4046   4997   4322   -228    632    451       C  
ATOM   2136  OH  TYR A1161     -12.744  22.625  -3.842  1.00 34.07           O  
ANISOU 2136  OH  TYR A1161     3881   4890   4174   -186    554    373       O  
ATOM   2137  N   LYS A1679      -7.083  16.332  -2.573  1.00 54.29           N  
ANISOU 2137  N   LYS A1679     6672   7044   6910   -243    845    802       N  
ATOM   2138  CA  LYS A1679      -6.218  15.301  -2.007  1.00 60.31           C  
ANISOU 2138  CA  LYS A1679     7470   7739   7704   -189    873    895       C  
ATOM   2139  C   LYS A1679      -6.654  14.941  -0.592  1.00 65.97           C  
ANISOU 2139  C   LYS A1679     8184   8512   8369   -160    921   1038       C  
ATOM   2140  O   LYS A1679      -6.813  13.760  -0.263  1.00 66.21           O  
ANISOU 2140  O   LYS A1679     8243   8443   8473   -178    974   1152       O  
ATOM   2141  CB  LYS A1679      -4.762  15.769  -2.029  1.00 59.57           C  
ANISOU 2141  CB  LYS A1679     7384   7688   7562   -106    820    861       C  
ATOM   2142  CG  LYS A1679      -4.118  15.712  -3.407  1.00 58.99           C  
ANISOU 2142  CG  LYS A1679     7310   7561   7543   -130    797    755       C  
ATOM   2143  CD  LYS A1679      -2.750  16.374  -3.414  1.00 58.16           C  
ANISOU 2143  CD  LYS A1679     7183   7537   7379    -72    749    722       C  
ATOM   2144  CE  LYS A1679      -2.872  17.883  -3.277  1.00 57.42           C  
ANISOU 2144  CE  LYS A1679     7068   7545   7205    -98    695    683       C  
ATOM   2145  NZ  LYS A1679      -3.623  18.479  -4.417  1.00 56.66           N  
ANISOU 2145  NZ  LYS A1679     6971   7434   7123   -184    681    615       N  
ATOM   2146  N   ILE A1680      -6.850  15.952   0.254  1.00 71.44           N  
ANISOU 2146  N   ILE A1680     8844   9366   8936   -115    902   1035       N  
ATOM   2147  CA  ILE A1680      -7.404  15.808   1.603  1.00 74.54           C  
ANISOU 2147  CA  ILE A1680     9214   9876   9234    -85    951   1153       C  
ATOM   2148  C   ILE A1680      -6.745  14.680   2.393  1.00 74.92           C  
ANISOU 2148  C   ILE A1680     9304   9878   9283    -33    986   1322       C  
ATOM   2149  O   ILE A1680      -6.840  14.628   3.620  1.00 75.39           O  
ANISOU 2149  O   ILE A1680     9351  10071   9224     22   1015   1439       O  
ATOM   2150  CB  ILE A1680      -8.938  15.609   1.544  1.00 77.88           C  
ANISOU 2150  CB  ILE A1680     9585  10320   9685   -185   1018   1172       C  
ATOM   2151  CG1 ILE A1680      -9.614  16.338   2.707  1.00 79.86           C  
ANISOU 2151  CG1 ILE A1680     9772  10789   9782   -136   1040   1190       C  
ATOM   2152  CG2 ILE A1680      -9.306  14.131   1.566  1.00 79.66           C  
ANISOU 2152  CG2 ILE A1680     9834  10408  10025   -268   1096   1315       C  
ATOM   2153  CD1 ILE A1680      -9.441  17.840   2.665  1.00 79.20           C  
ANISOU 2153  CD1 ILE A1680     9665  10810   9616    -60    952   1026       C  
ATOM   2154  N   SER A1689     -12.494   5.986  20.105  1.00 65.58           N  
ANISOU 2154  N   SER A1689     8261   8632   8024    556    894  -1647       N  
ATOM   2155  CA  SER A1689     -13.022   4.626  20.118  1.00 66.58           C  
ANISOU 2155  CA  SER A1689     8458   8607   8235    560    838  -1879       C  
ATOM   2156  C   SER A1689     -14.134   4.473  21.153  1.00 64.29           C  
ANISOU 2156  C   SER A1689     8161   8174   8092    443    652  -1849       C  
ATOM   2157  O   SER A1689     -14.226   5.257  22.097  1.00 61.84           O  
ANISOU 2157  O   SER A1689     7776   7846   7874    383    593  -1648       O  
ATOM   2158  CB  SER A1689     -11.902   3.622  20.394  1.00 66.84           C  
ANISOU 2158  CB  SER A1689     8439   8493   8463    666    973  -1945       C  
ATOM   2159  OG  SER A1689     -12.409   2.302  20.470  1.00 67.71           O  
ANISOU 2159  OG  SER A1689     8620   8420   8687    666    922  -2160       O  
ATOM   2160  N   ALA A1690     -14.979   3.456  20.968  1.00 65.51           N  
ANISOU 2160  N   ALA A1690     8394   8227   8268    408    565  -2054       N  
ATOM   2161  CA  ALA A1690     -16.089   3.239  21.890  1.00 64.15           C  
ANISOU 2161  CA  ALA A1690     8210   7928   8235    294    397  -2029       C  
ATOM   2162  C   ALA A1690     -15.598   2.687  23.222  1.00 64.57           C  
ANISOU 2162  C   ALA A1690     8178   7768   8586    298    410  -1933       C  
ATOM   2163  O   ALA A1690     -15.938   3.214  24.288  1.00 62.12           O  
ANISOU 2163  O   ALA A1690     7801   7422   8377    229    329  -1759       O  
ATOM   2164  CB  ALA A1690     -17.118   2.298  21.262  1.00 65.09           C  
ANISOU 2164  CB  ALA A1690     8429   8002   8301    240    300  -2277       C  
ATOM   2165  N   CYS A1691     -14.797   1.620  23.181  1.00 65.51           N  
ANISOU 2165  N   CYS A1691     8300   7749   8843    386    513  -2044       N  
ATOM   2166  CA  CYS A1691     -14.244   1.058  24.407  1.00 64.95           C  
ANISOU 2166  CA  CYS A1691     8141   7487   9051    407    530  -1935       C  
ATOM   2167  C   CYS A1691     -13.215   1.977  25.049  1.00 61.51           C  
ANISOU 2167  C   CYS A1691     7586   7130   8653    444    596  -1699       C  
ATOM   2168  O   CYS A1691     -12.947   1.845  26.248  1.00 59.93           O  
ANISOU 2168  O   CYS A1691     7301   6822   8648    430    565  -1555       O  
ATOM   2169  CB  CYS A1691     -13.620  -0.309  24.123  1.00 70.23           C  
ANISOU 2169  CB  CYS A1691     8840   7982   9863    511    634  -2109       C  
ATOM   2170  SG  CYS A1691     -14.777  -1.526  23.455  1.00 75.17           S  
ANISOU 2170  SG  CYS A1691     9608   8466  10488    450    552  -2413       S  
ATOM   2171  N   ALA A1692     -12.637   2.904  24.282  1.00 60.30           N  
ANISOU 2171  N   ALA A1692     7425   7171   8317    485    683  -1651       N  
ATOM   2172  CA  ALA A1692     -11.679   3.844  24.852  1.00 58.44           C  
ANISOU 2172  CA  ALA A1692     7071   7012   8120    498    739  -1430       C  
ATOM   2173  C   ALA A1692     -12.366   4.888  25.723  1.00 54.53           C  
ANISOU 2173  C   ALA A1692     6549   6552   7619    379    609  -1260       C  
ATOM   2174  O   ALA A1692     -11.751   5.418  26.654  1.00 53.66           O  
ANISOU 2174  O   ALA A1692     6338   6434   7615    359    608  -1085       O  
ATOM   2175  CB  ALA A1692     -10.883   4.519  23.736  1.00 59.98           C  
ANISOU 2175  CB  ALA A1692     7263   7396   8130    568    881  -1423       C  
ATOM   2176  N   GLN A1693     -13.635   5.192  25.437  1.00 52.07           N  
ANISOU 2176  N   GLN A1693     6319   6281   7182    300    499  -1312       N  
ATOM   2177  CA  GLN A1693     -14.396   6.131  26.252  1.00 46.42           C  
ANISOU 2177  CA  GLN A1693     5584   5587   6465    199    382  -1166       C  
ATOM   2178  C   GLN A1693     -14.801   5.532  27.590  1.00 41.48           C  
ANISOU 2178  C   GLN A1693     4918   4798   6043    148    291  -1121       C  
ATOM   2179  O   GLN A1693     -14.894   6.257  28.587  1.00 39.09           O  
ANISOU 2179  O   GLN A1693     4565   4497   5791     91    237   -967       O  
ATOM   2180  CB  GLN A1693     -15.639   6.596  25.493  1.00 47.06           C  
ANISOU 2180  CB  GLN A1693     5752   5773   6357    147    297  -1228       C  
ATOM   2181  CG  GLN A1693     -15.326   7.382  24.232  1.00 48.89           C  
ANISOU 2181  CG  GLN A1693     6022   6192   6361    192    377  -1228       C  
ATOM   2182  CD  GLN A1693     -16.563   7.705  23.417  1.00 50.15           C  
ANISOU 2182  CD  GLN A1693     6262   6466   6325    152    283  -1294       C  
ATOM   2183  OE1 GLN A1693     -17.052   6.873  22.653  1.00 51.46           O  
ANISOU 2183  OE1 GLN A1693     6498   6644   6411    161    255  -1482       O  
ATOM   2184  NE2 GLN A1693     -17.073   8.920  23.574  1.00 49.45           N  
ANISOU 2184  NE2 GLN A1693     6163   6462   6164    108    230  -1140       N  
ATOM   2185  N   LEU A1694     -15.044   4.221  27.635  1.00 40.42           N  
ANISOU 2185  N   LEU A1694     4812   4521   6025    165    278  -1252       N  
ATOM   2186  CA  LEU A1694     -15.415   3.587  28.895  1.00 38.73           C  
ANISOU 2186  CA  LEU A1694     4558   4151   6009    119    202  -1191       C  
ATOM   2187  C   LEU A1694     -14.211   3.450  29.818  1.00 39.42           C  
ANISOU 2187  C   LEU A1694     4543   4181   6255    173    260  -1053       C  
ATOM   2188  O   LEU A1694     -14.341   3.589  31.039  1.00 39.47           O  
ANISOU 2188  O   LEU A1694     4493   4141   6361    125    194   -915       O  
ATOM   2189  CB  LEU A1694     -16.050   2.222  28.632  1.00 39.43           C  
ANISOU 2189  CB  LEU A1694     4706   4086   6190    114    172  -1365       C  
ATOM   2190  CG  LEU A1694     -17.383   2.238  27.882  1.00 39.49           C  
ANISOU 2190  CG  LEU A1694     4797   4143   6063     36     79  -1501       C  
ATOM   2191  CD1 LEU A1694     -17.900   0.824  27.651  1.00 41.08           C  
ANISOU 2191  CD1 LEU A1694     5053   4171   6386     17     52  -1686       C  
ATOM   2192  CD2 LEU A1694     -18.408   3.070  28.636  1.00 37.68           C  
ANISOU 2192  CD2 LEU A1694     4539   3971   5806    -64    -35  -1367       C  
ATOM   2193  N   VAL A1695     -13.032   3.181  29.254  1.00 40.33           N  
ANISOU 2193  N   VAL A1695     4626   4311   6386    277    384  -1085       N  
ATOM   2194  CA  VAL A1695     -11.830   3.049  30.073  1.00 40.59           C  
ANISOU 2194  CA  VAL A1695     4541   4309   6571    335    436   -946       C  
ATOM   2195  C   VAL A1695     -11.445   4.396  30.674  1.00 39.90           C  
ANISOU 2195  C   VAL A1695     4381   4354   6425    276    408   -767       C  
ATOM   2196  O   VAL A1695     -11.135   4.496  31.867  1.00 40.00           O  
ANISOU 2196  O   VAL A1695     4312   4337   6548    247    356   -625       O  
ATOM   2197  CB  VAL A1695     -10.680   2.449  29.245  1.00 33.00           C  
ANISOU 2197  CB  VAL A1695     3552   3344   5644    470    588  -1026       C  
ATOM   2198  CG1 VAL A1695      -9.371   2.541  30.009  1.00 37.74           C  
ANISOU 2198  CG1 VAL A1695     4002   3956   6381    529    640   -857       C  
ATOM   2199  CG2 VAL A1695     -10.986   1.003  28.892  1.00 34.62           C  
ANISOU 2199  CG2 VAL A1695     3826   3371   5958    531    614  -1203       C  
ATOM   2200  N   ILE A1696     -11.463   5.451  29.858  1.00 39.96           N  
ANISOU 2200  N   ILE A1696     4420   4507   6255    254    441   -770       N  
ATOM   2201  CA  ILE A1696     -11.105   6.777  30.350  1.00 39.65           C  
ANISOU 2201  CA  ILE A1696     4322   4572   6169    190    422   -612       C  
ATOM   2202  C   ILE A1696     -12.100   7.244  31.406  1.00 40.42           C  
ANISOU 2202  C   ILE A1696     4444   4637   6277     86    288   -542       C  
ATOM   2203  O   ILE A1696     -11.712   7.816  32.432  1.00 38.74           O  
ANISOU 2203  O   ILE A1696     4163   4436   6120     37    247   -412       O  
ATOM   2204  CB  ILE A1696     -11.004   7.767  29.176  1.00 38.15           C  
ANISOU 2204  CB  ILE A1696     4173   4528   5795    192    493   -625       C  
ATOM   2205  CG1 ILE A1696      -9.810   7.406  28.294  1.00 39.96           C  
ANISOU 2205  CG1 ILE A1696     4352   4811   6021    298    646   -661       C  
ATOM   2206  CG2 ILE A1696     -10.877   9.194  29.681  1.00 36.40           C  
ANISOU 2206  CG2 ILE A1696     3915   4381   5534    106    459   -472       C  
ATOM   2207  CD1 ILE A1696      -9.694   8.251  27.056  1.00 40.94           C  
ANISOU 2207  CD1 ILE A1696     4518   5086   5951    311    733   -670       C  
ATOM   2208  N   ALA A1697     -13.394   7.002  31.183  1.00 43.18           N  
ANISOU 2208  N   ALA A1697     4885   4952   6568     50    219   -631       N  
ATOM   2209  CA  ALA A1697     -14.385   7.336  32.202  1.00 44.60           C  
ANISOU 2209  CA  ALA A1697     5079   5100   6766    -35    107   -566       C  
ATOM   2210  C   ALA A1697     -14.163   6.517  33.467  1.00 47.39           C  
ANISOU 2210  C   ALA A1697     5371   5345   7291    -38     66   -499       C  
ATOM   2211  O   ALA A1697     -14.286   7.036  34.582  1.00 45.25           O  
ANISOU 2211  O   ALA A1697     5067   5083   7042    -95      5   -386       O  
ATOM   2212  CB  ALA A1697     -15.796   7.117  31.659  1.00 44.56           C  
ANISOU 2212  CB  ALA A1697     5162   5086   6683    -69     45   -673       C  
ATOM   2213  N   PHE A1698     -13.824   5.235  33.310  1.00 53.05           N  
ANISOU 2213  N   PHE A1698     6075   5957   8126     29    104   -564       N  
ATOM   2214  CA  PHE A1698     -13.536   4.389  34.465  1.00 55.48           C  
ANISOU 2214  CA  PHE A1698     6318   6156   8605     42     74   -478       C  
ATOM   2215  C   PHE A1698     -12.316   4.889  35.230  1.00 52.16           C  
ANISOU 2215  C   PHE A1698     5789   5801   8228     58     88   -330       C  
ATOM   2216  O   PHE A1698     -12.296   4.864  36.466  1.00 51.85           O  
ANISOU 2216  O   PHE A1698     5700   5747   8253     23     21   -209       O  
ATOM   2217  CB  PHE A1698     -13.340   2.944  34.004  1.00 62.77           C  
ANISOU 2217  CB  PHE A1698     7253   6936   9659    124    128   -582       C  
ATOM   2218  CG  PHE A1698     -12.657   2.064  35.012  1.00 69.29           C  
ANISOU 2218  CG  PHE A1698     7994   7656  10676    176    129   -469       C  
ATOM   2219  CD1 PHE A1698     -13.377   1.468  36.034  1.00 70.89           C  
ANISOU 2219  CD1 PHE A1698     8198   7757  10981    129     52   -397       C  
ATOM   2220  CD2 PHE A1698     -11.295   1.815  34.924  1.00 72.25           C  
ANISOU 2220  CD2 PHE A1698     8280   8040  11133    278    212   -422       C  
ATOM   2221  CE1 PHE A1698     -12.751   0.652  36.957  1.00 73.52           C  
ANISOU 2221  CE1 PHE A1698     8451   7998  11484    184     53   -271       C  
ATOM   2222  CE2 PHE A1698     -10.662   1.002  35.844  1.00 74.32           C  
ANISOU 2222  CE2 PHE A1698     8453   8212  11574    337    208   -301       C  
ATOM   2223  CZ  PHE A1698     -11.390   0.418  36.862  1.00 75.19           C  
ANISOU 2223  CZ  PHE A1698     8573   8221  11776    291    126   -222       C  
ATOM   2224  N   ILE A1699     -11.286   5.344  34.512  1.00 48.95           N  
ANISOU 2224  N   ILE A1699     5339   5478   7783    106    173   -334       N  
ATOM   2225  CA  ILE A1699     -10.096   5.878  35.171  1.00 44.88           C  
ANISOU 2225  CA  ILE A1699     4703   5038   7312    106    180   -196       C  
ATOM   2226  C   ILE A1699     -10.435   7.157  35.927  1.00 41.19           C  
ANISOU 2226  C   ILE A1699     4243   4655   6754     -8     97   -111       C  
ATOM   2227  O   ILE A1699      -9.988   7.364  37.062  1.00 40.99           O  
ANISOU 2227  O   ILE A1699     4142   4654   6779    -46     35      5       O  
ATOM   2228  CB  ILE A1699      -8.973   6.105  34.140  1.00 44.79           C  
ANISOU 2228  CB  ILE A1699     4635   5103   7281    177    303   -219       C  
ATOM   2229  CG1 ILE A1699      -8.387   4.767  33.679  1.00 46.37           C  
ANISOU 2229  CG1 ILE A1699     4802   5211   7607    310    393   -283       C  
ATOM   2230  CG2 ILE A1699      -7.885   6.996  34.712  1.00 44.88           C  
ANISOU 2230  CG2 ILE A1699     4521   5220   7310    138    298    -77       C  
ATOM   2231  CD1 ILE A1699      -7.248   4.903  32.685  1.00 47.54           C  
ANISOU 2231  CD1 ILE A1699     4882   5441   7738    398    534   -304       C  
ATOM   2232  N   LEU A1700     -11.244   8.026  35.318  1.00 38.17           N  
ANISOU 2232  N   LEU A1700     3952   4316   6234    -61     93   -169       N  
ATOM   2233  CA  LEU A1700     -11.613   9.279  35.965  1.00 35.38           C  
ANISOU 2233  CA  LEU A1700     3620   4022   5803   -160     28   -103       C  
ATOM   2234  C   LEU A1700     -12.508   9.070  37.180  1.00 32.69           C  
ANISOU 2234  C   LEU A1700     3305   3633   5483   -210    -71    -67       C  
ATOM   2235  O   LEU A1700     -12.576   9.955  38.039  1.00 31.09           O  
ANISOU 2235  O   LEU A1700     3099   3473   5241   -283   -126     -2       O  
ATOM   2236  CB  LEU A1700     -12.302  10.205  34.961  1.00 34.23           C  
ANISOU 2236  CB  LEU A1700     3564   3924   5516   -184     56   -161       C  
ATOM   2237  CG  LEU A1700     -11.404  10.784  33.868  1.00 33.50           C  
ANISOU 2237  CG  LEU A1700     3446   3911   5371   -155    157   -159       C  
ATOM   2238  CD1 LEU A1700     -12.215  11.618  32.891  1.00 32.70           C  
ANISOU 2238  CD1 LEU A1700     3442   3859   5125   -170    176   -200       C  
ATOM   2239  CD2 LEU A1700     -10.283  11.613  34.479  1.00 33.15           C  
ANISOU 2239  CD2 LEU A1700     3305   3918   5374   -208    162    -47       C  
ATOM   2240  N   ILE A1701     -13.194   7.929  37.273  1.00 32.35           N  
ANISOU 2240  N   ILE A1701     3289   3500   5502   -177    -90   -109       N  
ATOM   2241  CA  ILE A1701     -14.000   7.644  38.457  1.00 31.46           C  
ANISOU 2241  CA  ILE A1701     3188   3347   5417   -222   -170    -54       C  
ATOM   2242  C   ILE A1701     -13.136   7.057  39.568  1.00 32.12           C  
ANISOU 2242  C   ILE A1701     3177   3419   5606   -203   -200     62       C  
ATOM   2243  O   ILE A1701     -13.325   7.370  40.748  1.00 31.69           O  
ANISOU 2243  O   ILE A1701     3110   3402   5530   -256   -267    148       O  
ATOM   2244  CB  ILE A1701     -15.173   6.713  38.093  1.00 30.50           C  
ANISOU 2244  CB  ILE A1701     3129   3132   5327   -212   -180   -135       C  
ATOM   2245  CG1 ILE A1701     -16.119   7.405  37.112  1.00 29.84           C  
ANISOU 2245  CG1 ILE A1701     3128   3091   5120   -239   -176   -231       C  
ATOM   2246  CG2 ILE A1701     -15.943   6.300  39.336  1.00 29.40           C  
ANISOU 2246  CG2 ILE A1701     2986   2952   5234   -254   -247    -56       C  
ATOM   2247  CD1 ILE A1701     -17.286   6.546  36.676  1.00 30.27           C  
ANISOU 2247  CD1 ILE A1701     3232   3071   5200   -245   -199   -322       C  
ATOM   2248  N   CYS A1702     -12.168   6.208  39.211  1.00 33.06           N  
ANISOU 2248  N   CYS A1702     3228   3499   5835   -121   -148     69       N  
ATOM   2249  CA  CYS A1702     -11.297   5.610  40.219  1.00 33.78           C  
ANISOU 2249  CA  CYS A1702     3214   3586   6034    -87   -178    198       C  
ATOM   2250  C   CYS A1702     -10.444   6.657  40.921  1.00 33.18           C  
ANISOU 2250  C   CYS A1702     3064   3643   5902   -144   -224    290       C  
ATOM   2251  O   CYS A1702     -10.054   6.463  42.079  1.00 32.78           O  
ANISOU 2251  O   CYS A1702     2942   3629   5883   -157   -293    409       O  
ATOM   2252  CB  CYS A1702     -10.408   4.545  39.580  1.00 36.00           C  
ANISOU 2252  CB  CYS A1702     3431   3793   6455     30    -98    183       C  
ATOM   2253  SG  CYS A1702     -11.307   3.090  39.009  1.00 37.92           S  
ANISOU 2253  SG  CYS A1702     3756   3846   6806     91    -59     77       S  
ATOM   2254  N   ILE A1703     -10.137   7.764  40.242  1.00 32.82           N  
ANISOU 2254  N   ILE A1703     3029   3671   5769   -185   -190    241       N  
ATOM   2255  CA  ILE A1703      -9.373   8.833  40.878  1.00 32.92           C  
ANISOU 2255  CA  ILE A1703     2978   3795   5736   -262   -238    312       C  
ATOM   2256  C   ILE A1703     -10.176   9.455  42.012  1.00 33.16           C  
ANISOU 2256  C   ILE A1703     3071   3855   5676   -354   -332    336       C  
ATOM   2257  O   ILE A1703      -9.649   9.701  43.104  1.00 34.33           O  
ANISOU 2257  O   ILE A1703     3155   4074   5813   -402   -409    420       O  
ATOM   2258  CB  ILE A1703      -8.951   9.885  39.836  1.00 31.92           C  
ANISOU 2258  CB  ILE A1703     2858   3718   5551   -291   -169    260       C  
ATOM   2259  CG1 ILE A1703      -7.910   9.300  38.880  1.00 32.73           C  
ANISOU 2259  CG1 ILE A1703     2870   3825   5739   -196    -69    257       C  
ATOM   2260  CG2 ILE A1703      -8.416  11.133  40.523  1.00 31.29           C  
ANISOU 2260  CG2 ILE A1703     2740   3727   5422   -402   -228    312       C  
ATOM   2261  CD1 ILE A1703      -7.375  10.296  37.880  1.00 33.02           C  
ANISOU 2261  CD1 ILE A1703     2896   3927   5721   -223     12    233       C  
ATOM   2262  N   GLN A1704     -11.465   9.711  41.774  1.00 32.01           N  
ANISOU 2262  N   GLN A1704     3045   3663   5455   -376   -327    262       N  
ATOM   2263  CA  GLN A1704     -12.318  10.230  42.837  1.00 31.78           C  
ANISOU 2263  CA  GLN A1704     3077   3659   5341   -446   -396    280       C  
ATOM   2264  C   GLN A1704     -12.464   9.217  43.965  1.00 32.62           C  
ANISOU 2264  C   GLN A1704     3146   3756   5493   -424   -452    372       C  
ATOM   2265  O   GLN A1704     -12.424   9.583  45.145  1.00 32.51           O  
ANISOU 2265  O   GLN A1704     3122   3814   5416   -477   -522    433       O  
ATOM   2266  CB  GLN A1704     -13.687  10.612  42.276  1.00 31.07           C  
ANISOU 2266  CB  GLN A1704     3102   3523   5179   -456   -369    194       C  
ATOM   2267  CG  GLN A1704     -14.692  11.090  43.321  1.00 30.64           C  
ANISOU 2267  CG  GLN A1704     3110   3490   5042   -509   -419    207       C  
ATOM   2268  CD  GLN A1704     -14.372  12.469  43.871  1.00 31.08           C  
ANISOU 2268  CD  GLN A1704     3188   3610   5010   -585   -447    201       C  
ATOM   2269  OE1 GLN A1704     -13.322  12.686  44.476  1.00 32.67           O  
ANISOU 2269  OE1 GLN A1704     3325   3871   5219   -622   -489    247       O  
ATOM   2270  NE2 GLN A1704     -15.283  13.411  43.662  1.00 30.19           N  
ANISOU 2270  NE2 GLN A1704     3166   3483   4822   -609   -427    142       N  
ATOM   2271  N   LEU A1705     -12.633   7.938  43.621  1.00 33.52           N  
ANISOU 2271  N   LEU A1705     3242   3779   5715   -348   -420    382       N  
ATOM   2272  CA  LEU A1705     -12.715   6.904  44.648  1.00 34.47           C  
ANISOU 2272  CA  LEU A1705     3321   3876   5901   -320   -463    495       C  
ATOM   2273  C   LEU A1705     -11.415   6.811  45.435  1.00 35.15           C  
ANISOU 2273  C   LEU A1705     3288   4047   6019   -308   -515    616       C  
ATOM   2274  O   LEU A1705     -11.433   6.612  46.656  1.00 36.06           O  
ANISOU 2274  O   LEU A1705     3376   4221   6103   -327   -585    726       O  
ATOM   2275  CB  LEU A1705     -13.058   5.556  44.014  1.00 35.60           C  
ANISOU 2275  CB  LEU A1705     3469   3875   6182   -242   -411    475       C  
ATOM   2276  CG  LEU A1705     -13.071   4.349  44.955  1.00 36.26           C  
ANISOU 2276  CG  LEU A1705     3504   3901   6373   -200   -439    610       C  
ATOM   2277  CD1 LEU A1705     -14.145   4.501  46.024  1.00 35.49           C  
ANISOU 2277  CD1 LEU A1705     3456   3839   6190   -266   -489    672       C  
ATOM   2278  CD2 LEU A1705     -13.263   3.058  44.175  1.00 37.12           C  
ANISOU 2278  CD2 LEU A1705     3622   3838   6645   -124   -376    567       C  
ATOM   2279  N   GLY A1706     -10.276   6.958  44.755  1.00 34.39           N  
ANISOU 2279  N   GLY A1706     3112   3974   5979   -275   -481    604       N  
ATOM   2280  CA  GLY A1706      -9.004   6.962  45.458  1.00 34.15           C  
ANISOU 2280  CA  GLY A1706     2947   4045   5982   -271   -539    721       C  
ATOM   2281  C   GLY A1706      -8.897   8.100  46.454  1.00 34.27           C  
ANISOU 2281  C   GLY A1706     2967   4198   5858   -386   -634    742       C  
ATOM   2282  O   GLY A1706      -8.312   7.946  47.530  1.00 36.10           O  
ANISOU 2282  O   GLY A1706     3115   4527   6074   -401   -723    858       O  
ATOM   2283  N   ILE A1707      -9.461   9.260  46.109  1.00 32.26           N  
ANISOU 2283  N   ILE A1707     2811   3950   5496   -467   -619    629       N  
ATOM   2284  CA  ILE A1707      -9.496  10.378  47.046  1.00 31.27           C  
ANISOU 2284  CA  ILE A1707     2718   3928   5237   -580   -700    619       C  
ATOM   2285  C   ILE A1707     -10.368  10.036  48.247  1.00 31.62           C  
ANISOU 2285  C   ILE A1707     2819   3999   5196   -590   -758    670       C  
ATOM   2286  O   ILE A1707     -10.020  10.346  49.394  1.00 32.45           O  
ANISOU 2286  O   ILE A1707     2895   4221   5213   -647   -851    726       O  
ATOM   2287  CB  ILE A1707      -9.986  11.653  46.334  1.00 29.22           C  
ANISOU 2287  CB  ILE A1707     2560   3636   4904   -647   -653    490       C  
ATOM   2288  CG1 ILE A1707      -9.038  12.027  45.194  1.00 28.37           C  
ANISOU 2288  CG1 ILE A1707     2386   3521   4870   -642   -591    464       C  
ATOM   2289  CG2 ILE A1707     -10.116  12.803  47.321  1.00 29.39           C  
ANISOU 2289  CG2 ILE A1707     2635   3734   4797   -759   -728    457       C  
ATOM   2290  CD1 ILE A1707      -9.507  13.209  44.380  1.00 26.84           C  
ANISOU 2290  CD1 ILE A1707     2292   3286   4619   -695   -533    363       C  
ATOM   2291  N   ILE A1708     -11.507   9.382  48.008  1.00 30.54           N  
ANISOU 2291  N   ILE A1708     2758   3765   5080   -540   -705    655       N  
ATOM   2292  CA  ILE A1708     -12.426   9.062  49.095  1.00 30.35           C  
ANISOU 2292  CA  ILE A1708     2785   3768   4978   -550   -740    712       C  
ATOM   2293  C   ILE A1708     -11.819   8.018  50.026  1.00 31.67           C  
ANISOU 2293  C   ILE A1708     2853   3987   5192   -504   -799    879       C  
ATOM   2294  O   ILE A1708     -11.917   8.130  51.254  1.00 32.60           O  
ANISOU 2294  O   ILE A1708     2974   4217   5196   -540   -870    955       O  
ATOM   2295  CB  ILE A1708     -13.780   8.599  48.526  1.00 29.48           C  
ANISOU 2295  CB  ILE A1708     2761   3540   4902   -516   -666    661       C  
ATOM   2296  CG1 ILE A1708     -14.395   9.698  47.656  1.00 28.04           C  
ANISOU 2296  CG1 ILE A1708     2669   3326   4659   -554   -618    516       C  
ATOM   2297  CG2 ILE A1708     -14.729   8.209  49.650  1.00 29.29           C  
ANISOU 2297  CG2 ILE A1708     2773   3547   4810   -525   -688    740       C  
ATOM   2298  CD1 ILE A1708     -15.634   9.262  46.899  1.00 26.96           C  
ANISOU 2298  CD1 ILE A1708     2595   3086   4563   -521   -556    459       C  
ATOM   2299  N   VAL A1709     -11.183   6.989  49.461  1.00 31.79           N  
ANISOU 2299  N   VAL A1709     2782   3925   5371   -417   -769    943       N  
ATOM   2300  CA  VAL A1709     -10.561   5.957  50.286  1.00 32.49           C  
ANISOU 2300  CA  VAL A1709     2767   4049   5529   -356   -820   1122       C  
ATOM   2301  C   VAL A1709      -9.381   6.530  51.060  1.00 32.79           C  
ANISOU 2301  C   VAL A1709     2703   4263   5491   -400   -925   1192       C  
ATOM   2302  O   VAL A1709      -9.140   6.161  52.216  1.00 34.23           O  
ANISOU 2302  O   VAL A1709     2833   4554   5619   -396  -1008   1337       O  
ATOM   2303  CB  VAL A1709     -10.144   4.759  49.413  1.00 33.39           C  
ANISOU 2303  CB  VAL A1709     2817   4016   5855   -240   -749   1157       C  
ATOM   2304  CG1 VAL A1709      -9.425   3.711  50.247  1.00 30.10           C  
ANISOU 2304  CG1 VAL A1709     2282   3624   5531   -161   -798   1362       C  
ATOM   2305  CG2 VAL A1709     -11.360   4.153  48.734  1.00 33.45           C  
ANISOU 2305  CG2 VAL A1709     2926   3852   5930   -216   -664   1079       C  
ATOM   2306  N   ALA A1710      -8.630   7.445  50.441  1.00 32.35           N  
ANISOU 2306  N   ALA A1710     2614   4248   5429   -449   -925   1097       N  
ATOM   2307  CA  ALA A1710      -7.514   8.072  51.141  1.00 29.86           C  
ANISOU 2307  CA  ALA A1710     2194   4103   5048   -515  -1034   1147       C  
ATOM   2308  C   ALA A1710      -8.002   8.901  52.321  1.00 36.62           C  
ANISOU 2308  C   ALA A1710     3131   5086   5695   -623  -1125   1121       C  
ATOM   2309  O   ALA A1710      -7.361   8.927  53.378  1.00 31.44           O  
ANISOU 2309  O   ALA A1710     2398   4590   4957   -658  -1242   1218       O  
ATOM   2310  CB  ALA A1710      -6.702   8.935  50.177  1.00 29.63           C  
ANISOU 2310  CB  ALA A1710     2118   4075   5067   -561  -1003   1046       C  
ATOM   2311  N   LEU A1711      -9.137   9.587  52.162  1.00 34.61           N  
ANISOU 2311  N   LEU A1711     3031   4772   5346   -672  -1072    989       N  
ATOM   2312  CA  LEU A1711      -9.679  10.370  53.265  1.00 34.03           C  
ANISOU 2312  CA  LEU A1711     3048   4808   5072   -761  -1137    947       C  
ATOM   2313  C   LEU A1711     -10.332   9.495  54.326  1.00 34.66           C  
ANISOU 2313  C   LEU A1711     3146   4942   5080   -713  -1160   1079       C  
ATOM   2314  O   LEU A1711     -10.436   9.921  55.481  1.00 35.98           O  
ANISOU 2314  O   LEU A1711     3348   5256   5067   -772  -1238   1092       O  
ATOM   2315  CB  LEU A1711     -10.677  11.404  52.739  1.00 32.26           C  
ANISOU 2315  CB  LEU A1711     2975   4499   4785   -811  -1060    772       C  
ATOM   2316  CG  LEU A1711     -10.069  12.598  51.999  1.00 30.77           C  
ANISOU 2316  CG  LEU A1711     2790   4286   4615   -891  -1053    644       C  
ATOM   2317  CD1 LEU A1711     -11.151  13.404  51.304  1.00 29.19           C  
ANISOU 2317  CD1 LEU A1711     2731   3971   4389   -904   -959    504       C  
ATOM   2318  CD2 LEU A1711      -9.284  13.476  52.960  1.00 31.79           C  
ANISOU 2318  CD2 LEU A1711     2892   4561   4625  -1008  -1173    616       C  
ATOM   2319  N   PHE A1712     -10.781   8.292  53.959  1.00 34.04           N  
ANISOU 2319  N   PHE A1712     3050   4748   5136   -612  -1092   1175       N  
ATOM   2320  CA  PHE A1712     -11.229   7.331  54.962  1.00 34.93           C  
ANISOU 2320  CA  PHE A1712     3152   4906   5212   -563  -1113   1344       C  
ATOM   2321  C   PHE A1712     -10.093   6.962  55.908  1.00 38.79           C  
ANISOU 2321  C   PHE A1712     3514   5561   5665   -552  -1235   1511       C  
ATOM   2322  O   PHE A1712     -10.306   6.782  57.113  1.00 40.19           O  
ANISOU 2322  O   PHE A1712     3700   5876   5694   -563  -1297   1624       O  
ATOM   2323  CB  PHE A1712     -11.778   6.076  54.280  1.00 33.68           C  
ANISOU 2323  CB  PHE A1712     2987   4562   5248   -465  -1018   1413       C  
ATOM   2324  CG  PHE A1712     -13.174   6.229  53.748  1.00 32.48           C  
ANISOU 2324  CG  PHE A1712     2956   4289   5095   -479   -921   1299       C  
ATOM   2325  CD1 PHE A1712     -14.083   7.071  54.367  1.00 32.21           C  
ANISOU 2325  CD1 PHE A1712     3024   4336   4879   -545   -917   1229       C  
ATOM   2326  CD2 PHE A1712     -13.580   5.522  52.628  1.00 32.15           C  
ANISOU 2326  CD2 PHE A1712     2923   4060   5233   -424   -834   1258       C  
ATOM   2327  CE1 PHE A1712     -15.372   7.207  53.878  1.00 30.93           C  
ANISOU 2327  CE1 PHE A1712     2952   4074   4725   -551   -830   1139       C  
ATOM   2328  CE2 PHE A1712     -14.865   5.654  52.134  1.00 30.91           C  
ANISOU 2328  CE2 PHE A1712     2861   3809   5074   -444   -760   1159       C  
ATOM   2329  CZ  PHE A1712     -15.762   6.497  52.760  1.00 30.16           C  
ANISOU 2329  CZ  PHE A1712     2850   3802   4808   -505   -758   1108       C  
ATOM   2330  N   ILE A1713      -8.877   6.849  55.375  1.00 40.23           N  
ANISOU 2330  N   ILE A1713     3568   5744   5972   -527  -1268   1536       N  
ATOM   2331  CA  ILE A1713      -7.727   6.474  56.188  1.00 42.91           C  
ANISOU 2331  CA  ILE A1713     3758   6247   6298   -507  -1390   1707       C  
ATOM   2332  C   ILE A1713      -7.234   7.651  57.022  1.00 43.78           C  
ANISOU 2332  C   ILE A1713     3868   6570   6195   -639  -1520   1637       C  
ATOM   2333  O   ILE A1713      -6.787   7.465  58.159  1.00 45.40           O  
ANISOU 2333  O   ILE A1713     4008   6966   6277   -651  -1642   1772       O  
ATOM   2334  CB  ILE A1713      -6.618   5.916  55.280  1.00 43.75           C  
ANISOU 2334  CB  ILE A1713     3714   6277   6631   -424  -1366   1761       C  
ATOM   2335  CG1 ILE A1713      -7.175   4.783  54.418  1.00 43.33           C  
ANISOU 2335  CG1 ILE A1713     3687   5994   6783   -300  -1232   1791       C  
ATOM   2336  CG2 ILE A1713      -5.442   5.432  56.101  1.00 45.52           C  
ANISOU 2336  CG2 ILE A1713     3760   6671   6865   -385  -1493   1964       C  
ATOM   2337  CD1 ILE A1713      -6.242   4.331  53.323  1.00 43.60           C  
ANISOU 2337  CD1 ILE A1713     3607   5925   7035   -211  -1170   1789       C  
ATOM   2338  N   MET A1714      -7.308   8.871  56.488  1.00 43.18           N  
ANISOU 2338  N   MET A1714     3867   6467   6071   -741  -1500   1428       N  
ATOM   2339  CA  MET A1714      -6.884  10.042  57.249  1.00 45.88           C  
ANISOU 2339  CA  MET A1714     4226   6982   6223   -880  -1619   1332       C  
ATOM   2340  C   MET A1714      -7.914  10.418  58.307  1.00 46.74           C  
ANISOU 2340  C   MET A1714     4485   7177   6097   -927  -1635   1286       C  
ATOM   2341  O   MET A1714      -7.567  10.646  59.472  1.00 47.89           O  
ANISOU 2341  O   MET A1714     4614   7528   6055   -986  -1762   1327       O  
ATOM   2342  CB  MET A1714      -6.639  11.223  56.309  1.00 46.11           C  
ANISOU 2342  CB  MET A1714     4291   6927   6302   -974  -1579   1133       C  
ATOM   2343  CG  MET A1714      -5.516  11.007  55.314  1.00 48.34           C  
ANISOU 2343  CG  MET A1714     4415   7160   6791   -943  -1562   1172       C  
ATOM   2344  SD  MET A1714      -5.592  12.154  53.925  1.00 49.46           S  
ANISOU 2344  SD  MET A1714     4629   7144   7020  -1012  -1451    968       S  
ATOM   2345  CE  MET A1714      -5.642  13.722  54.786  1.00 50.92           C  
ANISOU 2345  CE  MET A1714     4916   7433   7000  -1201  -1554    804       C  
ATOM   2346  N   GLU A1715      -9.185  10.486  57.917  1.00 45.89           N  
ANISOU 2346  N   GLU A1715     4521   6928   5989   -898  -1506   1201       N  
ATOM   2347  CA  GLU A1715     -10.268  10.923  58.797  1.00 46.65           C  
ANISOU 2347  CA  GLU A1715     4763   7088   5872   -931  -1488   1139       C  
ATOM   2348  C   GLU A1715     -11.351   9.854  58.792  1.00 46.65           C  
ANISOU 2348  C   GLU A1715     4799   6997   5928   -825  -1384   1261       C  
ATOM   2349  O   GLU A1715     -12.290   9.906  57.984  1.00 45.85           O  
ANISOU 2349  O   GLU A1715     4777   6730   5915   -797  -1262   1175       O  
ATOM   2350  CB  GLU A1715     -10.816  12.279  58.355  1.00 45.78           C  
ANISOU 2350  CB  GLU A1715     4791   6897   5706  -1015  -1430    898       C  
ATOM   2351  CG  GLU A1715      -9.755  13.367  58.273  1.00 46.22           C  
ANISOU 2351  CG  GLU A1715     4813   7009   5740  -1136  -1525    772       C  
ATOM   2352  CD  GLU A1715     -10.231  14.602  57.535  1.00 45.19           C  
ANISOU 2352  CD  GLU A1715     4805   6737   5628  -1199  -1444    558       C  
ATOM   2353  OE1 GLU A1715     -11.171  14.488  56.719  1.00 43.25           O  
ANISOU 2353  OE1 GLU A1715     4630   6333   5472  -1130  -1313    526       O  
ATOM   2354  OE2 GLU A1715      -9.663  15.689  57.774  1.00 46.08           O  
ANISOU 2354  OE2 GLU A1715     4941   6896   5670  -1320  -1515    427       O  
ATOM   2355  N   PRO A1716     -11.253   8.866  59.678  1.00 48.30           N  
ANISOU 2355  N   PRO A1716     4944   7315   6094   -768  -1431   1471       N  
ATOM   2356  CA  PRO A1716     -12.214   7.754  59.675  1.00 48.32           C  
ANISOU 2356  CA  PRO A1716     4964   7215   6181   -675  -1332   1611       C  
ATOM   2357  C   PRO A1716     -13.622   8.242  59.960  1.00 48.00           C  
ANISOU 2357  C   PRO A1716     5069   7161   6007   -700  -1237   1513       C  
ATOM   2358  O   PRO A1716     -13.825   9.113  60.819  1.00 48.98           O  
ANISOU 2358  O   PRO A1716     5274   7440   5898   -764  -1274   1427       O  
ATOM   2359  CB  PRO A1716     -11.701   6.842  60.801  1.00 50.37           C  
ANISOU 2359  CB  PRO A1716     5130   7639   6371   -629  -1423   1864       C  
ATOM   2360  CG  PRO A1716     -10.254   7.203  60.955  1.00 51.16           C  
ANISOU 2360  CG  PRO A1716     5115   7874   6449   -668  -1566   1871       C  
ATOM   2361  CD  PRO A1716     -10.184   8.673  60.673  1.00 50.36           C  
ANISOU 2361  CD  PRO A1716     5097   7793   6245   -787  -1584   1608       C  
ATOM   2362  N   PRO A1717     -14.621   7.716  59.251  1.00 47.03           N  
ANISOU 2362  N   PRO A1717     4980   6859   6028   -650  -1114   1514       N  
ATOM   2363  CA  PRO A1717     -16.004   8.122  59.523  1.00 46.88           C  
ANISOU 2363  CA  PRO A1717     5076   6835   5899   -663  -1018   1441       C  
ATOM   2364  C   PRO A1717     -16.433   7.711  60.924  1.00 49.28           C  
ANISOU 2364  C   PRO A1717     5394   7316   6015   -651  -1028   1602       C  
ATOM   2365  O   PRO A1717     -15.991   6.693  61.460  1.00 50.13           O  
ANISOU 2365  O   PRO A1717     5415   7478   6153   -606  -1074   1821       O  
ATOM   2366  CB  PRO A1717     -16.812   7.378  58.451  1.00 45.08           C  
ANISOU 2366  CB  PRO A1717     4842   6388   5900   -612   -909   1451       C  
ATOM   2367  CG  PRO A1717     -15.825   7.041  57.389  1.00 44.42           C  
ANISOU 2367  CG  PRO A1717     4679   6181   6018   -588   -938   1433       C  
ATOM   2368  CD  PRO A1717     -14.526   6.813  58.093  1.00 45.78           C  
ANISOU 2368  CD  PRO A1717     4759   6494   6142   -584  -1057   1556       C  
ATOM   2369  N   ASP A1718     -17.303   8.524  61.519  1.00 50.79           N  
ANISOU 2369  N   ASP A1718     5692   7598   6008   -684   -977   1498       N  
ATOM   2370  CA  ASP A1718     -17.793   8.261  62.865  1.00 53.52           C  
ANISOU 2370  CA  ASP A1718     6064   8133   6138   -672   -968   1633       C  
ATOM   2371  C   ASP A1718     -19.080   9.043  63.077  1.00 53.38           C  
ANISOU 2371  C   ASP A1718     6163   8130   5990   -682   -849   1496       C  
ATOM   2372  O   ASP A1718     -19.235  10.155  62.568  1.00 52.11           O  
ANISOU 2372  O   ASP A1718     6079   7911   5811   -717   -827   1270       O  
ATOM   2373  CB  ASP A1718     -16.750   8.640  63.927  1.00 55.62           C  
ANISOU 2373  CB  ASP A1718     6319   8639   6173   -714  -1111   1657       C  
ATOM   2374  CG  ASP A1718     -16.976   7.931  65.250  1.00 57.74           C  
ANISOU 2374  CG  ASP A1718     6573   9111   6255   -681  -1123   1884       C  
ATOM   2375  OD1 ASP A1718     -16.882   6.687  65.276  1.00 58.38           O  
ANISOU 2375  OD1 ASP A1718     6558   9146   6476   -618  -1118   2130       O  
ATOM   2376  OD2 ASP A1718     -17.241   8.614  66.262  1.00 59.29           O  
ANISOU 2376  OD2 ASP A1718     6856   9510   6163   -714  -1133   1818       O  
ATOM   2377  N   ILE A1719     -20.000   8.447  63.828  1.00 55.55           N  
ANISOU 2377  N   ILE A1719     6442   8480   6184   -645   -766   1649       N  
ATOM   2378  CA  ILE A1719     -21.268   9.095  64.143  1.00 58.52           C  
ANISOU 2378  CA  ILE A1719     6909   8892   6432   -638   -639   1549       C  
ATOM   2379  C   ILE A1719     -21.018  10.170  65.193  1.00 63.73           C  
ANISOU 2379  C   ILE A1719     7672   9771   6774   -674   -680   1416       C  
ATOM   2380  O   ILE A1719     -20.472   9.889  66.266  1.00 65.29           O  
ANISOU 2380  O   ILE A1719     7858  10174   6776   -681   -759   1536       O  
ATOM   2381  CB  ILE A1719     -22.306   8.074  64.628  1.00 59.66           C  
ANISOU 2381  CB  ILE A1719     7011   9058   6600   -592   -528   1771       C  
ATOM   2382  CG1 ILE A1719     -22.501   6.972  63.581  1.00 59.13           C  
ANISOU 2382  CG1 ILE A1719     6848   8758   6862   -571   -499   1885       C  
ATOM   2383  CG2 ILE A1719     -23.627   8.763  64.937  1.00 60.75           C  
ANISOU 2383  CG2 ILE A1719     7226   9245   6612   -577   -385   1671       C  
ATOM   2384  CD1 ILE A1719     -23.437   5.863  64.024  1.00 60.13           C  
ANISOU 2384  CD1 ILE A1719     6916   8878   7052   -543   -400   2124       C  
ATOM   2385  N   MET A1720     -21.408  11.405  64.882  1.00 66.30           N  
ANISOU 2385  N   MET A1720     8098  10047   7045   -696   -631   1166       N  
ATOM   2386  CA  MET A1720     -21.209  12.511  65.810  1.00 70.45           C  
ANISOU 2386  CA  MET A1720     8739  10747   7282   -735   -662    997       C  
ATOM   2387  C   MET A1720     -21.982  12.253  67.099  1.00 75.48           C  
ANISOU 2387  C   MET A1720     9415  11598   7666   -694   -581   1106       C  
ATOM   2388  O   MET A1720     -23.083  11.697  67.074  1.00 74.82           O  
ANISOU 2388  O   MET A1720     9303  11479   7646   -634   -443   1226       O  
ATOM   2389  CB  MET A1720     -21.668  13.821  65.169  1.00 69.38           C  
ANISOU 2389  CB  MET A1720     8707  10477   7177   -748   -592    723       C  
ATOM   2390  CG  MET A1720     -20.865  15.047  65.571  1.00 70.35           C  
ANISOU 2390  CG  MET A1720     8930  10670   7127   -826   -686    496       C  
ATOM   2391  SD  MET A1720     -19.296  15.162  64.688  1.00 69.12           S  
ANISOU 2391  SD  MET A1720     8698  10410   7153   -913   -859    454       S  
ATOM   2392  CE  MET A1720     -18.790  16.832  65.093  1.00 69.67           C  
ANISOU 2392  CE  MET A1720     8912  10515   7044  -1014   -919    143       C  
ATOM   2393  N   HIS A1721     -21.386  12.640  68.231  1.00 80.74           N  
ANISOU 2393  N   HIS A1721    10140  12497   8039   -731   -669   1070       N  
ATOM   2394  CA  HIS A1721     -21.980  12.455  69.552  1.00 86.54           C  
ANISOU 2394  CA  HIS A1721    10922  13477   8480   -695   -601   1168       C  
ATOM   2395  C   HIS A1721     -22.259  10.991  69.889  1.00 89.62           C  
ANISOU 2395  C   HIS A1721    11196  13926   8928   -640   -568   1515       C  
ATOM   2396  O   HIS A1721     -21.974  10.087  69.095  1.00 88.57           O  
ANISOU 2396  O   HIS A1721    10948  13628   9076   -631   -602   1669       O  
ATOM   2397  CB  HIS A1721     -23.270  13.279  69.675  1.00 86.83           C  
ANISOU 2397  CB  HIS A1721    11069  13495   8428   -648   -415   1001       C  
ATOM   2398  N   ASP A1722     -22.784  10.757  71.092  1.00 94.19           N  
ANISOU 2398  N   ASP A1722    11808  14741   9238   -605   -500   1638       N  
ATOM   2399  CA  ASP A1722     -23.247   9.452  71.569  1.00 96.73           C  
ANISOU 2399  CA  ASP A1722    12034  15133   9584   -551   -434   1979       C  
ATOM   2400  C   ASP A1722     -24.662   9.726  72.054  1.00100.21           C  
ANISOU 2400  C   ASP A1722    12535  15648   9893   -499   -224   1960       C  
ATOM   2401  O   ASP A1722     -24.902   9.985  73.237  1.00101.77           O  
ANISOU 2401  O   ASP A1722    12806  16108   9753   -479   -179   1975       O  
ATOM   2402  CB  ASP A1722     -22.355   8.891  72.666  1.00 98.88           C  
ANISOU 2402  CB  ASP A1722    12277  15669   9624   -558   -568   2183       C  
ATOM   2403  N   TYR A1723     -25.597   9.658  71.119  1.00102.28           N  
ANISOU 2403  N   TYR A1723    12758  15683  10419   -474    -95   1929       N  
ATOM   2404  CA  TYR A1723     -26.877  10.324  71.257  1.00101.66           C  
ANISOU 2404  CA  TYR A1723    12741  15623  10263   -427     95   1807       C  
ATOM   2405  C   TYR A1723     -27.988   9.354  71.613  1.00101.88           C  
ANISOU 2405  C   TYR A1723    12676  15694  10338   -379    258   2080       C  
ATOM   2406  O   TYR A1723     -27.792   8.450  72.430  1.00103.70           O  
ANISOU 2406  O   TYR A1723    12858  16082  10461   -373    243   2349       O  
ATOM   2407  CB  TYR A1723     -27.198  11.070  69.964  1.00 98.41           C  
ANISOU 2407  CB  TYR A1723    12344  14947  10099   -433    124   1570       C  
ATOM   2408  N   PRO A1724     -29.152   9.537  71.002  1.00102.00           N  
ANISOU 2408  N   PRO A1724    12661  15574  10522   -347    411   2026       N  
ATOM   2409  CA  PRO A1724     -30.336   8.762  71.349  1.00103.60           C  
ANISOU 2409  CA  PRO A1724    12770  15825  10770   -310    585   2262       C  
ATOM   2410  C   PRO A1724     -31.163   8.392  70.120  1.00102.17           C  
ANISOU 2410  C   PRO A1724    12477  15379  10962   -319    651   2278       C  
ATOM   2411  O   PRO A1724     -30.708   7.665  69.238  1.00101.51           O  
ANISOU 2411  O   PRO A1724    12318  15094  11157   -364    549   2350       O  
ATOM   2412  CB  PRO A1724     -31.191   9.535  72.338  1.00104.95           C  
ANISOU 2412  CB  PRO A1724    13022  16222  10632   -245    756   2180       C  
ATOM   2413  N   GLU A1728     -32.331   9.614  66.155  1.00 90.25           N  
ANISOU 2413  N   GLU A1728    10880  13179  10230   -336    648   1782       N  
ATOM   2414  CA  GLU A1728     -32.887  10.771  65.465  1.00 89.31           C  
ANISOU 2414  CA  GLU A1728    10805  12978  10150   -294    702   1546       C  
ATOM   2415  C   GLU A1728     -32.898  10.559  63.953  1.00 87.90           C  
ANISOU 2415  C   GLU A1728    10557  12556  10283   -329    626   1493       C  
ATOM   2416  O   GLU A1728     -32.127   9.758  63.426  1.00 89.23           O  
ANISOU 2416  O   GLU A1728    10689  12613  10602   -388    505   1565       O  
ATOM   2417  CB  GLU A1728     -32.103  12.025  65.816  1.00 88.56           C  
ANISOU 2417  CB  GLU A1728    10872  12945   9833   -275    649   1306       C  
ATOM   2418  N   VAL A1729     -33.783  11.285  63.265  1.00 83.31           N  
ANISOU 2418  N   VAL A1729     9959  11902   9792   -285    702   1367       N  
ATOM   2419  CA  VAL A1729     -33.862  11.183  61.809  1.00 77.57           C  
ANISOU 2419  CA  VAL A1729     9174  10971   9330   -314    632   1305       C  
ATOM   2420  C   VAL A1729     -32.564  11.658  61.170  1.00 72.15           C  
ANISOU 2420  C   VAL A1729     8581  10177   8654   -344    485   1149       C  
ATOM   2421  O   VAL A1729     -32.029  11.014  60.258  1.00 70.03           O  
ANISOU 2421  O   VAL A1729     8268   9768   8571   -396    381   1173       O  
ATOM   2422  CB  VAL A1729     -35.077  11.973  61.288  1.00 77.72           C  
ANISOU 2422  CB  VAL A1729     9153  10964   9412   -247    742   1211       C  
ATOM   2423  CG1 VAL A1729     -34.883  12.355  59.834  1.00 75.99           C  
ANISOU 2423  CG1 VAL A1729     8932  10562   9379   -259    650   1077       C  
ATOM   2424  CG2 VAL A1729     -36.341  11.154  61.452  1.00 79.21           C  
ANISOU 2424  CG2 VAL A1729     9186  11201   9709   -249    853   1399       C  
ATOM   2425  N   TYR A1730     -32.035  12.781  61.641  1.00 68.82           N  
ANISOU 2425  N   TYR A1730     8291   9819   8039   -316    479    983       N  
ATOM   2426  CA  TYR A1730     -30.795  13.323  61.110  1.00 63.98           C  
ANISOU 2426  CA  TYR A1730     7762   9115   7431   -354    347    837       C  
ATOM   2427  C   TYR A1730     -29.607  12.514  61.614  1.00 61.60           C  
ANISOU 2427  C   TYR A1730     7458   8868   7078   -414    229    945       C  
ATOM   2428  O   TYR A1730     -29.485  12.253  62.815  1.00 63.23           O  
ANISOU 2428  O   TYR A1730     7685   9244   7094   -413    248   1037       O  
ATOM   2429  CB  TYR A1730     -30.643  14.790  61.507  1.00 63.33           C  
ANISOU 2429  CB  TYR A1730     7819   9073   7170   -316    381    625       C  
ATOM   2430  CG  TYR A1730     -31.651  15.706  60.856  1.00 61.09           C  
ANISOU 2430  CG  TYR A1730     7543   8702   6964   -243    484    508       C  
ATOM   2431  CD1 TYR A1730     -32.944  15.816  61.353  1.00 61.87           C  
ANISOU 2431  CD1 TYR A1730     7603   8889   7017   -165    642    554       C  
ATOM   2432  CD2 TYR A1730     -31.310  16.465  59.746  1.00 58.66           C  
ANISOU 2432  CD2 TYR A1730     7274   8234   6780   -246    430    369       C  
ATOM   2433  CE1 TYR A1730     -33.868  16.657  60.760  1.00 61.63           C  
ANISOU 2433  CE1 TYR A1730     7565   8784   7068    -84    735    461       C  
ATOM   2434  CE2 TYR A1730     -32.226  17.307  59.147  1.00 58.61           C  
ANISOU 2434  CE2 TYR A1730     7269   8150   6848   -168    521    283       C  
ATOM   2435  CZ  TYR A1730     -33.504  17.401  59.657  1.00 60.24           C  
ANISOU 2435  CZ  TYR A1730     7431   8443   7014    -84    670    329       C  
ATOM   2436  OH  TYR A1730     -34.418  18.240  59.061  1.00 60.40           O  
ANISOU 2436  OH  TYR A1730     7440   8392   7119      7    760    258       O  
ATOM   2437  N   LEU A1731     -28.733  12.119  60.693  1.00 57.44           N  
ANISOU 2437  N   LEU A1731     6902   8207   6715   -460    111    939       N  
ATOM   2438  CA  LEU A1731     -27.515  11.385  61.016  1.00 55.88           C  
ANISOU 2438  CA  LEU A1731     6687   8040   6503   -507     -8   1038       C  
ATOM   2439  C   LEU A1731     -26.329  12.325  60.839  1.00 55.58           C  
ANISOU 2439  C   LEU A1731     6735   7990   6392   -539   -111    865       C  
ATOM   2440  O   LEU A1731     -25.977  12.684  59.710  1.00 54.43           O  
ANISOU 2440  O   LEU A1731     6590   7697   6393   -553   -153    757       O  
ATOM   2441  CB  LEU A1731     -27.373  10.145  60.139  1.00 53.38           C  
ANISOU 2441  CB  LEU A1731     6264   7578   6440   -529    -54   1168       C  
ATOM   2442  CG  LEU A1731     -26.044   9.401  60.276  1.00 53.62           C  
ANISOU 2442  CG  LEU A1731     6266   7607   6500   -559   -176   1265       C  
ATOM   2443  CD1 LEU A1731     -25.810   8.969  61.714  1.00 55.63           C  
ANISOU 2443  CD1 LEU A1731     6521   8054   6562   -555   -182   1427       C  
ATOM   2444  CD2 LEU A1731     -26.013   8.208  59.347  1.00 52.84           C  
ANISOU 2444  CD2 LEU A1731     6073   7337   6668   -569   -199   1369       C  
ATOM   2445  N   ILE A1732     -25.720  12.720  61.953  1.00 56.23           N  
ANISOU 2445  N   ILE A1732     6885   8236   6245   -556   -153    841       N  
ATOM   2446  CA  ILE A1732     -24.577  13.624  61.958  1.00 54.57           C  
ANISOU 2446  CA  ILE A1732     6749   8035   5949   -606   -258    679       C  
ATOM   2447  C   ILE A1732     -23.310  12.780  62.008  1.00 52.61           C  
ANISOU 2447  C   ILE A1732     6428   7815   5747   -650   -398    805       C  
ATOM   2448  O   ILE A1732     -23.122  11.985  62.937  1.00 52.25           O  
ANISOU 2448  O   ILE A1732     6343   7911   5597   -646   -426    976       O  
ATOM   2449  CB  ILE A1732     -24.634  14.596  63.148  1.00 56.07           C  
ANISOU 2449  CB  ILE A1732     7058   8393   5854   -610   -234    555       C  
ATOM   2450  CG1 ILE A1732     -26.083  14.871  63.557  1.00 56.60           C  
ANISOU 2450  CG1 ILE A1732     7159   8503   5843   -536    -64    543       C  
ATOM   2451  CG2 ILE A1732     -23.924  15.900  62.807  1.00 55.64           C  
ANISOU 2451  CG2 ILE A1732     7101   8268   5773   -660   -294    316       C  
ATOM   2452  CD1 ILE A1732     -26.837  15.771  62.609  1.00 55.17           C  
ANISOU 2452  CD1 ILE A1732     7014   8156   5793   -495     25    387       C  
ATOM   2453  N   CYS A1733     -22.443  12.946  61.015  1.00 51.13           N  
ANISOU 2453  N   CYS A1733     6215   7497   5714   -684   -479    733       N  
ATOM   2454  CA  CYS A1733     -21.157  12.268  60.969  1.00 49.71           C  
ANISOU 2454  CA  CYS A1733     5958   7336   5595   -716   -607    834       C  
ATOM   2455  C   CYS A1733     -20.040  13.259  61.276  1.00 48.61           C  
ANISOU 2455  C   CYS A1733     5868   7271   5329   -787   -716    690       C  
ATOM   2456  O   CYS A1733     -20.255  14.471  61.361  1.00 49.25           O  
ANISOU 2456  O   CYS A1733     6054   7349   5310   -815   -689    497       O  
ATOM   2457  CB  CYS A1733     -20.931  11.609  59.601  1.00 47.93           C  
ANISOU 2457  CB  CYS A1733     5649   6917   5647   -701   -613    872       C  
ATOM   2458  SG  CYS A1733     -22.222  10.441  59.096  1.00 47.59           S  
ANISOU 2458  SG  CYS A1733     5542   6756   5782   -643   -502   1013       S  
ATOM   2459  N   ASN A1734     -18.829  12.727  61.443  1.00 47.93           N  
ANISOU 2459  N   ASN A1734     5700   7248   5262   -817   -842    787       N  
ATOM   2460  CA  ASN A1734     -17.657  13.542  61.744  1.00 49.05           C  
ANISOU 2460  CA  ASN A1734     5859   7475   5302   -900   -967    673       C  
ATOM   2461  C   ASN A1734     -16.924  14.003  60.489  1.00 49.67           C  
ANISOU 2461  C   ASN A1734     5905   7391   5579   -937   -998    568       C  
ATOM   2462  O   ASN A1734     -15.701  14.197  60.526  1.00 51.63           O  
ANISOU 2462  O   ASN A1734     6095   7691   5828  -1001  -1118    555       O  
ATOM   2463  CB  ASN A1734     -16.708  12.773  62.662  1.00 49.57           C  
ANISOU 2463  CB  ASN A1734     5837   7728   5270   -914  -1097    847       C  
ATOM   2464  CG  ASN A1734     -16.157  11.524  62.011  1.00 49.81           C  
ANISOU 2464  CG  ASN A1734     5725   7672   5529   -862  -1125   1042       C  
ATOM   2465  OD1 ASN A1734     -16.777  10.951  61.115  1.00 48.70           O  
ANISOU 2465  OD1 ASN A1734     5561   7357   5586   -805  -1029   1084       O  
ATOM   2466  ND2 ASN A1734     -14.983  11.094  62.457  1.00 51.40           N  
ANISOU 2466  ND2 ASN A1734     5827   7996   5707   -880  -1259   1160       N  
ATOM   2467  N   THR A1735     -17.637  14.183  59.380  1.00 48.39           N  
ANISOU 2467  N   THR A1735     5767   7043   5576   -900   -894    502       N  
ATOM   2468  CA  THR A1735     -17.005  14.624  58.145  1.00 47.55           C  
ANISOU 2468  CA  THR A1735     5633   6790   5643   -928   -907    414       C  
ATOM   2469  C   THR A1735     -16.537  16.069  58.281  1.00 47.83           C  
ANISOU 2469  C   THR A1735     5754   6832   5588  -1018   -945    220       C  
ATOM   2470  O   THR A1735     -17.319  16.956  58.636  1.00 46.75           O  
ANISOU 2470  O   THR A1735     5736   6686   5339  -1022   -881     89       O  
ATOM   2471  CB  THR A1735     -17.977  14.491  56.973  1.00 45.92           C  
ANISOU 2471  CB  THR A1735     5442   6408   5599   -864   -789    393       C  
ATOM   2472  OG1 THR A1735     -18.552  13.179  56.974  1.00 46.72           O  
ANISOU 2472  OG1 THR A1735     5477   6498   5776   -796   -751    558       O  
ATOM   2473  CG2 THR A1735     -17.253  14.714  55.653  1.00 45.02           C  
ANISOU 2473  CG2 THR A1735     5284   6162   5660   -881   -801    342       C  
ATOM   2474  N   THR A1736     -15.258  16.302  58.003  1.00 49.00           N  
ANISOU 2474  N   THR A1736     5835   6988   5794  -1089  -1045    202       N  
ATOM   2475  CA  THR A1736     -14.673  17.627  58.115  1.00 50.56           C  
ANISOU 2475  CA  THR A1736     6098   7181   5933  -1197  -1096     25       C  
ATOM   2476  C   THR A1736     -14.794  18.374  56.788  1.00 49.02           C  
ANISOU 2476  C   THR A1736     5934   6785   5905  -1201  -1017    -73       C  
ATOM   2477  O   THR A1736     -15.413  17.903  55.830  1.00 49.05           O  
ANISOU 2477  O   THR A1736     5920   6675   6042  -1117   -926    -19       O  
ATOM   2478  CB  THR A1736     -13.212  17.530  58.552  1.00 52.57           C  
ANISOU 2478  CB  THR A1736     6247   7565   6164  -1288  -1252     66       C  
ATOM   2479  OG1 THR A1736     -12.471  16.780  57.580  1.00 52.08           O  
ANISOU 2479  OG1 THR A1736     6043   7440   6306  -1255  -1264    188       O  
ATOM   2480  CG2 THR A1736     -13.104  16.842  59.907  1.00 54.35           C  
ANISOU 2480  CG2 THR A1736     6444   8009   6198  -1280  -1339    176       C  
ATOM   2481  N   ASN A1737     -14.195  19.566  56.733  1.00 47.79           N  
ANISOU 2481  N   ASN A1737     5827   6588   5741  -1305  -1054   -219       N  
ATOM   2482  CA  ASN A1737     -14.173  20.315  55.482  1.00 44.76           C  
ANISOU 2482  CA  ASN A1737     5467   6022   5519  -1316   -984   -290       C  
ATOM   2483  C   ASN A1737     -13.338  19.599  54.431  1.00 44.54           C  
ANISOU 2483  C   ASN A1737     5295   5959   5668  -1299  -1000   -170       C  
ATOM   2484  O   ASN A1737     -13.706  19.574  53.250  1.00 43.58           O  
ANISOU 2484  O   ASN A1737     5173   5708   5676  -1240   -910   -155       O  
ATOM   2485  CB  ASN A1737     -13.639  21.727  55.719  1.00 45.08           C  
ANISOU 2485  CB  ASN A1737     5587   6016   5526  -1444  -1024   -460       C  
ATOM   2486  CG  ASN A1737     -14.546  22.547  56.608  1.00 46.86           C  
ANISOU 2486  CG  ASN A1737     5975   6237   5591  -1445   -979   -609       C  
ATOM   2487  OD1 ASN A1737     -15.731  22.247  56.747  1.00 46.33           O  
ANISOU 2487  OD1 ASN A1737     5967   6164   5473  -1335   -884   -589       O  
ATOM   2488  ND2 ASN A1737     -13.995  23.593  57.213  1.00 49.71           N  
ANISOU 2488  ND2 ASN A1737     6409   6600   5879  -1571  -1045   -767       N  
ATOM   2489  N   LEU A1738     -12.213  19.006  54.839  1.00 45.84           N  
ANISOU 2489  N   LEU A1738     5334   6249   5833  -1344  -1113    -82       N  
ATOM   2490  CA  LEU A1738     -11.374  18.291  53.885  1.00 44.15           C  
ANISOU 2490  CA  LEU A1738     4976   6009   5789  -1314  -1117     31       C  
ATOM   2491  C   LEU A1738     -12.078  17.058  53.333  1.00 41.58           C  
ANISOU 2491  C   LEU A1738     4619   5638   5540  -1177  -1039    147       C  
ATOM   2492  O   LEU A1738     -11.867  16.697  52.170  1.00 40.80           O  
ANISOU 2492  O   LEU A1738     4463   5449   5590  -1128   -981    185       O  
ATOM   2493  CB  LEU A1738     -10.046  17.904  54.535  1.00 45.32           C  
ANISOU 2493  CB  LEU A1738     4983   6314   5924  -1380  -1257    112       C  
ATOM   2494  CG  LEU A1738      -9.007  17.273  53.603  1.00 42.38           C  
ANISOU 2494  CG  LEU A1738     4445   5925   5733  -1352  -1259    222       C  
ATOM   2495  CD1 LEU A1738      -8.726  18.190  52.422  1.00 40.60           C  
ANISOU 2495  CD1 LEU A1738     4233   5565   5629  -1400  -1187    139       C  
ATOM   2496  CD2 LEU A1738      -7.725  16.955  54.358  1.00 43.37           C  
ANISOU 2496  CD2 LEU A1738     4417   6222   5838  -1414  -1406    310       C  
ATOM   2497  N   GLY A1739     -12.918  16.406  54.140  1.00 39.88           N  
ANISOU 2497  N   GLY A1739     4443   5484   5227  -1118  -1032    201       N  
ATOM   2498  CA  GLY A1739     -13.715  15.299  53.641  1.00 38.14           C  
ANISOU 2498  CA  GLY A1739     4203   5199   5088  -1005   -955    297       C  
ATOM   2499  C   GLY A1739     -14.762  15.710  52.628  1.00 37.19           C  
ANISOU 2499  C   GLY A1739     4169   4934   5029   -961   -839    217       C  
ATOM   2500  O   GLY A1739     -15.252  14.862  51.875  1.00 37.03           O  
ANISOU 2500  O   GLY A1739     4119   4840   5112   -883   -781    275       O  
ATOM   2501  N   VAL A1740     -15.110  16.992  52.590  1.00 35.86           N  
ANISOU 2501  N   VAL A1740     4104   4721   4802  -1009   -809     84       N  
ATOM   2502  CA  VAL A1740     -16.082  17.519  51.642  1.00 33.37           C  
ANISOU 2502  CA  VAL A1740     3864   4277   4539   -964   -706     16       C  
ATOM   2503  C   VAL A1740     -15.399  18.230  50.482  1.00 32.28           C  
ANISOU 2503  C   VAL A1740     3714   4046   4507   -998   -686    -31       C  
ATOM   2504  O   VAL A1740     -15.709  17.972  49.319  1.00 31.20           O  
ANISOU 2504  O   VAL A1740     3562   3828   4465   -940   -623    -12       O  
ATOM   2505  CB  VAL A1740     -17.076  18.457  52.364  1.00 33.61           C  
ANISOU 2505  CB  VAL A1740     4021   4305   4443   -968   -663    -84       C  
ATOM   2506  CG1 VAL A1740     -18.008  19.123  51.361  1.00 32.40           C  
ANISOU 2506  CG1 VAL A1740     3936   4021   4354   -917   -563   -143       C  
ATOM   2507  CG2 VAL A1740     -17.867  17.689  53.410  1.00 33.74           C  
ANISOU 2507  CG2 VAL A1740     4044   4422   4355   -922   -658    -19       C  
ATOM   2508  N   VAL A1741     -14.447  19.119  50.783  1.00 33.31           N  
ANISOU 2508  N   VAL A1741     3846   4193   4618  -1100   -742    -91       N  
ATOM   2509  CA  VAL A1741     -13.879  19.989  49.756  1.00 33.59           C  
ANISOU 2509  CA  VAL A1741     3881   4133   4750  -1145   -709   -134       C  
ATOM   2510  C   VAL A1741     -13.051  19.189  48.757  1.00 34.44           C  
ANISOU 2510  C   VAL A1741     3863   4242   4981  -1115   -703    -41       C  
ATOM   2511  O   VAL A1741     -13.107  19.440  47.547  1.00 34.94           O  
ANISOU 2511  O   VAL A1741     3930   4220   5124  -1085   -629    -41       O  
ATOM   2512  CB  VAL A1741     -13.052  21.113  50.406  1.00 34.72           C  
ANISOU 2512  CB  VAL A1741     4049   4287   4854  -1280   -775   -223       C  
ATOM   2513  CG1 VAL A1741     -12.312  21.915  49.345  1.00 34.83           C  
ANISOU 2513  CG1 VAL A1741     4038   4205   4990  -1340   -742   -236       C  
ATOM   2514  CG2 VAL A1741     -13.949  22.024  51.224  1.00 34.90           C  
ANISOU 2514  CG2 VAL A1741     4221   4277   4762  -1297   -754   -344       C  
ATOM   2515  N   ALA A1742     -12.274  18.218  49.237  1.00 35.77           N  
ANISOU 2515  N   ALA A1742     3918   4512   5162  -1113   -774     44       N  
ATOM   2516  CA  ALA A1742     -11.389  17.476  48.340  1.00 37.27           C  
ANISOU 2516  CA  ALA A1742     3982   4703   5475  -1075   -760    126       C  
ATOM   2517  C   ALA A1742     -12.146  16.720  47.254  1.00 34.98           C  
ANISOU 2517  C   ALA A1742     3708   4335   5248   -961   -667    149       C  
ATOM   2518  O   ALA A1742     -11.771  16.848  46.076  1.00 34.23           O  
ANISOU 2518  O   ALA A1742     3584   4190   5232   -942   -606    147       O  
ATOM   2519  CB  ALA A1742     -10.482  16.550  49.158  1.00 39.17           C  
ANISOU 2519  CB  ALA A1742     4095   5065   5721  -1077   -854    224       C  
ATOM   2520  N   PRO A1743     -13.191  15.936  47.547  1.00 34.85           N  
ANISOU 2520  N   PRO A1743     3733   4310   5201   -889   -653    169       N  
ATOM   2521  CA  PRO A1743     -13.984  15.378  46.440  1.00 34.14           C  
ANISOU 2521  CA  PRO A1743     3667   4139   5168   -803   -573    164       C  
ATOM   2522  C   PRO A1743     -14.837  16.421  45.739  1.00 32.84           C  
ANISOU 2522  C   PRO A1743     3604   3903   4970   -805   -510     85       C  
ATOM   2523  O   PRO A1743     -15.143  16.256  44.552  1.00 30.90           O  
ANISOU 2523  O   PRO A1743     3366   3606   4769   -753   -450     74       O  
ATOM   2524  CB  PRO A1743     -14.843  14.306  47.126  1.00 33.92           C  
ANISOU 2524  CB  PRO A1743     3643   4124   5122   -750   -587    215       C  
ATOM   2525  CG  PRO A1743     -14.971  14.779  48.520  1.00 33.98           C  
ANISOU 2525  CG  PRO A1743     3685   4209   5015   -805   -644    215       C  
ATOM   2526  CD  PRO A1743     -13.662  15.432  48.852  1.00 35.30           C  
ANISOU 2526  CD  PRO A1743     3803   4437   5172   -886   -707    208       C  
ATOM   2527  N   LEU A1744     -15.228  17.492  46.435  1.00 34.43           N  
ANISOU 2527  N   LEU A1744     3887   4103   5091   -858   -520     30       N  
ATOM   2528  CA  LEU A1744     -15.981  18.564  45.789  1.00 35.31           C  
ANISOU 2528  CA  LEU A1744     4092   4136   5187   -850   -457    -32       C  
ATOM   2529  C   LEU A1744     -15.131  19.279  44.748  1.00 35.00           C  
ANISOU 2529  C   LEU A1744     4035   4053   5211   -883   -423    -35       C  
ATOM   2530  O   LEU A1744     -15.612  19.602  43.655  1.00 34.74           O  
ANISOU 2530  O   LEU A1744     4038   3965   5198   -838   -358    -38       O  
ATOM   2531  CB  LEU A1744     -16.484  19.557  46.838  1.00 37.80           C  
ANISOU 2531  CB  LEU A1744     4501   4446   5416   -894   -467    -98       C  
ATOM   2532  CG  LEU A1744     -17.434  20.671  46.396  1.00 38.20           C  
ANISOU 2532  CG  LEU A1744     4656   4405   5454   -866   -396   -155       C  
ATOM   2533  CD1 LEU A1744     -18.805  20.104  46.096  1.00 36.51           C  
ANISOU 2533  CD1 LEU A1744     4457   4189   5228   -768   -353   -133       C  
ATOM   2534  CD2 LEU A1744     -17.527  21.758  47.457  1.00 39.93           C  
ANISOU 2534  CD2 LEU A1744     4965   4605   5603   -925   -406   -241       C  
ATOM   2535  N   GLY A1745     -13.863  19.540  45.073  1.00 34.48           N  
ANISOU 2535  N   GLY A1745     3906   4021   5174   -966   -468    -25       N  
ATOM   2536  CA  GLY A1745     -12.987  20.204  44.122  1.00 34.66           C  
ANISOU 2536  CA  GLY A1745     3895   4008   5265  -1008   -428    -11       C  
ATOM   2537  C   GLY A1745     -12.711  19.360  42.894  1.00 35.75           C  
ANISOU 2537  C   GLY A1745     3963   4160   5461   -930   -373     43       C  
ATOM   2538  O   GLY A1745     -12.668  19.877  41.774  1.00 37.62           O  
ANISOU 2538  O   GLY A1745     4217   4355   5720   -915   -301     52       O  
ATOM   2539  N   TYR A1746     -12.522  18.051  43.082  1.00 35.18           N  
ANISOU 2539  N   TYR A1746     3816   4142   5410   -875   -400     80       N  
ATOM   2540  CA  TYR A1746     -12.301  17.172  41.939  1.00 35.02           C  
ANISOU 2540  CA  TYR A1746     3741   4124   5442   -792   -342    107       C  
ATOM   2541  C   TYR A1746     -13.536  17.109  41.050  1.00 34.78           C  
ANISOU 2541  C   TYR A1746     3799   4045   5372   -720   -286     71       C  
ATOM   2542  O   TYR A1746     -13.424  17.122  39.818  1.00 34.27           O  
ANISOU 2542  O   TYR A1746     3733   3974   5314   -679   -220     70       O  
ATOM   2543  CB  TYR A1746     -11.908  15.773  42.410  1.00 34.41           C  
ANISOU 2543  CB  TYR A1746     3574   4088   5412   -743   -380    151       C  
ATOM   2544  CG  TYR A1746     -11.754  14.783  41.278  1.00 33.76           C  
ANISOU 2544  CG  TYR A1746     3451   3989   5388   -649   -314    155       C  
ATOM   2545  CD1 TYR A1746     -10.586  14.733  40.528  1.00 33.75           C  
ANISOU 2545  CD1 TYR A1746     3359   4016   5446   -636   -263    183       C  
ATOM   2546  CD2 TYR A1746     -12.778  13.902  40.954  1.00 32.99           C  
ANISOU 2546  CD2 TYR A1746     3404   3848   5284   -577   -299    122       C  
ATOM   2547  CE1 TYR A1746     -10.441  13.833  39.490  1.00 33.61           C  
ANISOU 2547  CE1 TYR A1746     3314   3985   5469   -541   -190    168       C  
ATOM   2548  CE2 TYR A1746     -12.643  12.999  39.916  1.00 32.85           C  
ANISOU 2548  CE2 TYR A1746     3362   3807   5313   -497   -240    100       C  
ATOM   2549  CZ  TYR A1746     -11.472  12.968  39.189  1.00 33.33           C  
ANISOU 2549  CZ  TYR A1746     3345   3898   5421   -473   -182    117       C  
ATOM   2550  OH  TYR A1746     -11.333  12.069  38.155  1.00 33.42           O  
ANISOU 2550  OH  TYR A1746     3342   3888   5466   -385   -113     77       O  
ATOM   2551  N   ASN A1747     -14.723  17.032  41.658  1.00 34.89           N  
ANISOU 2551  N   ASN A1747     3882   4039   5335   -704   -313     44       N  
ATOM   2552  CA  ASN A1747     -15.955  17.085  40.877  1.00 34.31           C  
ANISOU 2552  CA  ASN A1747     3878   3932   5224   -645   -274     15       C  
ATOM   2553  C   ASN A1747     -16.077  18.413  40.142  1.00 33.02           C  
ANISOU 2553  C   ASN A1747     3777   3736   5034   -659   -224      9       C  
ATOM   2554  O   ASN A1747     -16.565  18.461  39.007  1.00 31.44           O  
ANISOU 2554  O   ASN A1747     3602   3532   4810   -606   -180      8       O  
ATOM   2555  CB  ASN A1747     -17.166  16.861  41.785  1.00 35.25           C  
ANISOU 2555  CB  ASN A1747     4043   4046   5306   -632   -308      1       C  
ATOM   2556  CG  ASN A1747     -17.246  15.441  42.315  1.00 37.25           C  
ANISOU 2556  CG  ASN A1747     4240   4318   5595   -606   -344     25       C  
ATOM   2557  OD1 ASN A1747     -16.939  14.483  41.606  1.00 38.30           O  
ANISOU 2557  OD1 ASN A1747     4327   4443   5783   -566   -331     28       O  
ATOM   2558  ND2 ASN A1747     -17.661  15.301  43.570  1.00 38.78           N  
ANISOU 2558  ND2 ASN A1747     4443   4534   5759   -627   -383     44       N  
ATOM   2559  N   GLY A1748     -15.634  19.503  40.774  1.00 34.07           N  
ANISOU 2559  N   GLY A1748     3935   3842   5168   -734   -234      7       N  
ATOM   2560  CA  GLY A1748     -15.656  20.793  40.106  1.00 33.42           C  
ANISOU 2560  CA  GLY A1748     3911   3704   5085   -753   -180     17       C  
ATOM   2561  C   GLY A1748     -14.768  20.826  38.878  1.00 32.78           C  
ANISOU 2561  C   GLY A1748     3778   3642   5033   -748   -122     64       C  
ATOM   2562  O   GLY A1748     -15.140  21.390  37.847  1.00 34.21           O  
ANISOU 2562  O   GLY A1748     4003   3804   5191   -711    -64     93       O  
ATOM   2563  N   LEU A1749     -13.585  20.213  38.969  1.00 31.48           N  
ANISOU 2563  N   LEU A1749     3515   3528   4917   -779   -134     84       N  
ATOM   2564  CA  LEU A1749     -12.711  20.120  37.804  1.00 30.80           C  
ANISOU 2564  CA  LEU A1749     3367   3478   4857   -761    -64    130       C  
ATOM   2565  C   LEU A1749     -13.387  19.365  36.665  1.00 30.38           C  
ANISOU 2565  C   LEU A1749     3337   3457   4748   -654    -19    117       C  
ATOM   2566  O   LEU A1749     -13.239  19.732  35.494  1.00 30.42           O  
ANISOU 2566  O   LEU A1749     3353   3483   4723   -625     55    151       O  
ATOM   2567  CB  LEU A1749     -11.392  19.447  38.187  1.00 30.68           C  
ANISOU 2567  CB  LEU A1749     3224   3520   4912   -794    -84    154       C  
ATOM   2568  CG  LEU A1749     -10.425  20.254  39.055  1.00 32.03           C  
ANISOU 2568  CG  LEU A1749     3343   3686   5140   -918   -129    175       C  
ATOM   2569  CD1 LEU A1749      -9.174  19.443  39.368  1.00 32.93           C  
ANISOU 2569  CD1 LEU A1749     3307   3879   5324   -930   -156    214       C  
ATOM   2570  CD2 LEU A1749     -10.059  21.564  38.374  1.00 32.78           C  
ANISOU 2570  CD2 LEU A1749     3462   3733   5260   -984    -62    214       C  
ATOM   2571  N   LEU A1750     -14.133  18.305  36.989  1.00 30.89           N  
ANISOU 2571  N   LEU A1750     3409   3530   4796   -601    -64     70       N  
ATOM   2572  CA  LEU A1750     -14.898  17.599  35.967  1.00 30.68           C  
ANISOU 2572  CA  LEU A1750     3413   3528   4716   -516    -40     35       C  
ATOM   2573  C   LEU A1750     -15.974  18.490  35.361  1.00 30.62           C  
ANISOU 2573  C   LEU A1750     3492   3509   4633   -493    -24     44       C  
ATOM   2574  O   LEU A1750     -16.312  18.343  34.181  1.00 29.47           O  
ANISOU 2574  O   LEU A1750     3368   3408   4422   -436     12     39       O  
ATOM   2575  CB  LEU A1750     -15.530  16.339  36.560  1.00 29.45           C  
ANISOU 2575  CB  LEU A1750     3246   3363   4581   -484    -98    -14       C  
ATOM   2576  CG  LEU A1750     -14.578  15.247  37.050  1.00 28.17           C  
ANISOU 2576  CG  LEU A1750     2996   3206   4501   -478   -111    -11       C  
ATOM   2577  CD1 LEU A1750     -15.355  14.132  37.730  1.00 26.79           C  
ANISOU 2577  CD1 LEU A1750     2824   3000   4356   -455   -167    -38       C  
ATOM   2578  CD2 LEU A1750     -13.755  14.702  35.895  1.00 28.59           C  
ANISOU 2578  CD2 LEU A1750     3005   3292   4565   -423    -38    -24       C  
ATOM   2579  N   ILE A1751     -16.520  19.417  36.150  1.00 31.72           N  
ANISOU 2579  N   ILE A1751     3681   3594   4777   -531    -50     58       N  
ATOM   2580  CA  ILE A1751     -17.550  20.315  35.640  1.00 32.67           C  
ANISOU 2580  CA  ILE A1751     3876   3695   4844   -496    -32     82       C  
ATOM   2581  C   ILE A1751     -16.937  21.375  34.732  1.00 35.52           C  
ANISOU 2581  C   ILE A1751     4254   4046   5196   -507     40    155       C  
ATOM   2582  O   ILE A1751     -17.509  21.727  33.693  1.00 35.53           O  
ANISOU 2582  O   ILE A1751     4292   4077   5131   -449     73    195       O  
ATOM   2583  CB  ILE A1751     -18.330  20.941  36.810  1.00 31.60           C  
ANISOU 2583  CB  ILE A1751     3789   3494   4725   -518    -67     67       C  
ATOM   2584  CG1 ILE A1751     -19.148  19.870  37.531  1.00 30.41           C  
ANISOU 2584  CG1 ILE A1751     3619   3368   4568   -494   -125     18       C  
ATOM   2585  CG2 ILE A1751     -19.238  22.058  36.325  1.00 31.39           C  
ANISOU 2585  CG2 ILE A1751     3832   3427   4667   -475    -34    108       C  
ATOM   2586  CD1 ILE A1751     -19.835  20.378  38.768  1.00 30.17           C  
ANISOU 2586  CD1 ILE A1751     3629   3294   4541   -511   -147      0       C  
ATOM   2587  N   LEU A1752     -15.764  21.897  35.102  1.00 38.59           N  
ANISOU 2587  N   LEU A1752     4610   4402   5651   -586     64    183       N  
ATOM   2588  CA  LEU A1752     -15.089  22.870  34.247  1.00 41.23           C  
ANISOU 2588  CA  LEU A1752     4948   4723   5995   -610    142    268       C  
ATOM   2589  C   LEU A1752     -14.729  22.265  32.895  1.00 42.09           C  
ANISOU 2589  C   LEU A1752     5020   4935   6037   -547    203    297       C  
ATOM   2590  O   LEU A1752     -14.923  22.899  31.852  1.00 42.58           O  
ANISOU 2590  O   LEU A1752     5119   5019   6041   -510    263    372       O  
ATOM   2591  CB  LEU A1752     -13.834  23.408  34.936  1.00 42.25           C  
ANISOU 2591  CB  LEU A1752     5025   4805   6222   -724    147    285       C  
ATOM   2592  CG  LEU A1752     -13.965  24.685  35.769  1.00 43.37           C  
ANISOU 2592  CG  LEU A1752     5231   4823   6424   -805    133    285       C  
ATOM   2593  CD1 LEU A1752     -14.540  24.391  37.139  1.00 42.98           C  
ANISOU 2593  CD1 LEU A1752     5211   4747   6373   -821     47    191       C  
ATOM   2594  CD2 LEU A1752     -12.619  25.380  35.891  1.00 46.03           C  
ANISOU 2594  CD2 LEU A1752     5510   5124   6856   -925    160    329       C  
ATOM   2595  N   ALA A1753     -14.203  21.038  32.894  1.00 43.30           N  
ANISOU 2595  N   ALA A1753     5105   5153   6194   -527    192    242       N  
ATOM   2596  CA  ALA A1753     -13.831  20.395  31.638  1.00 44.67           C  
ANISOU 2596  CA  ALA A1753     5251   5424   6297   -460    258    245       C  
ATOM   2597  C   ALA A1753     -15.059  20.080  30.792  1.00 42.58           C  
ANISOU 2597  C   ALA A1753     5055   5211   5912   -376    241    211       C  
ATOM   2598  O   ALA A1753     -15.030  20.237  29.565  1.00 43.51           O  
ANISOU 2598  O   ALA A1753     5192   5410   5930   -326    304    249       O  
ATOM   2599  CB  ALA A1753     -13.024  19.128  31.916  1.00 44.46           C  
ANISOU 2599  CB  ALA A1753     5138   5432   6323   -447    254    183       C  
ATOM   2600  N   CYS A1754     -16.145  19.631  31.425  1.00 40.37           N  
ANISOU 2600  N   CYS A1754     4807   4900   5632   -361    156    146       N  
ATOM   2601  CA  CYS A1754     -17.386  19.400  30.693  1.00 39.78           C  
ANISOU 2601  CA  CYS A1754     4783   4879   5453   -296    122    118       C  
ATOM   2602  C   CYS A1754     -17.884  20.684  30.045  1.00 38.22           C  
ANISOU 2602  C   CYS A1754     4640   4690   5192   -274    153    222       C  
ATOM   2603  O   CYS A1754     -18.231  20.702  28.858  1.00 37.88           O  
ANISOU 2603  O   CYS A1754     4621   4743   5029   -215    173    247       O  
ATOM   2604  CB  CYS A1754     -18.454  18.831  31.627  1.00 41.00           C  
ANISOU 2604  CB  CYS A1754     4943   4989   5644   -299     31     51       C  
ATOM   2605  SG  CYS A1754     -18.368  17.058  31.922  1.00 42.58           S  
ANISOU 2605  SG  CYS A1754     5098   5196   5887   -292    -14    -67       S  
ATOM   2606  N   THR A1755     -17.921  21.774  30.814  1.00 36.71           N  
ANISOU 2606  N   THR A1755     4471   4399   5078   -317    157    285       N  
ATOM   2607  CA  THR A1755     -18.440  23.035  30.295  1.00 36.90           C  
ANISOU 2607  CA  THR A1755     4551   4400   5070   -288    190    395       C  
ATOM   2608  C   THR A1755     -17.559  23.578  29.176  1.00 38.27           C  
ANISOU 2608  C   THR A1755     4721   4624   5195   -285    285    498       C  
ATOM   2609  O   THR A1755     -18.060  24.197  28.230  1.00 40.36           O  
ANISOU 2609  O   THR A1755     5024   4937   5373   -226    314    594       O  
ATOM   2610  CB  THR A1755     -18.561  24.054  31.428  1.00 36.09           C  
ANISOU 2610  CB  THR A1755     4481   4152   5079   -340    185    418       C  
ATOM   2611  OG1 THR A1755     -19.187  23.437  32.561  1.00 34.68           O  
ANISOU 2611  OG1 THR A1755     4295   3945   4938   -349    111    320       O  
ATOM   2612  CG2 THR A1755     -19.398  25.243  30.989  1.00 36.50           C  
ANISOU 2612  CG2 THR A1755     4595   4159   5114   -285    211    523       C  
ATOM   2613  N   PHE A1756     -16.247  23.348  29.263  1.00 36.90           N  
ANISOU 2613  N   PHE A1756     4492   4453   5076   -343    338    493       N  
ATOM   2614  CA  PHE A1756     -15.335  23.841  28.236  1.00 37.87           C  
ANISOU 2614  CA  PHE A1756     4596   4632   5160   -344    444    600       C  
ATOM   2615  C   PHE A1756     -15.630  23.200  26.885  1.00 40.15           C  
ANISOU 2615  C   PHE A1756     4896   5082   5275   -251    470    595       C  
ATOM   2616  O   PHE A1756     -15.749  23.893  25.868  1.00 41.37           O  
ANISOU 2616  O   PHE A1756     5085   5300   5335   -210    530    714       O  
ATOM   2617  CB  PHE A1756     -13.889  23.582  28.658  1.00 36.59           C  
ANISOU 2617  CB  PHE A1756     4347   4455   5099   -422    490    588       C  
ATOM   2618  CG  PHE A1756     -12.874  23.994  27.630  1.00 37.34           C  
ANISOU 2618  CG  PHE A1756     4401   4621   5164   -427    614    702       C  
ATOM   2619  CD1 PHE A1756     -12.558  25.330  27.447  1.00 38.00           C  
ANISOU 2619  CD1 PHE A1756     4501   4632   5304   -482    679    847       C  
ATOM   2620  CD2 PHE A1756     -12.228  23.044  26.854  1.00 37.39           C  
ANISOU 2620  CD2 PHE A1756     4354   4761   5093   -375    674    665       C  
ATOM   2621  CE1 PHE A1756     -11.623  25.713  26.504  1.00 39.22           C  
ANISOU 2621  CE1 PHE A1756     4610   4856   5435   -492    803    971       C  
ATOM   2622  CE2 PHE A1756     -11.291  23.420  25.910  1.00 38.65           C  
ANISOU 2622  CE2 PHE A1756     4469   5001   5216   -374    804    777       C  
ATOM   2623  CZ  PHE A1756     -10.988  24.757  25.735  1.00 39.72           C  
ANISOU 2623  CZ  PHE A1756     4612   5074   5406   -436    868    938       C  
ATOM   2624  N   TYR A1757     -15.758  21.872  26.857  1.00 40.88           N  
ANISOU 2624  N   TYR A1757     4967   5243   5322   -218    426    457       N  
ATOM   2625  CA  TYR A1757     -16.040  21.183  25.603  1.00 41.94           C  
ANISOU 2625  CA  TYR A1757     5122   5531   5283   -137    442    415       C  
ATOM   2626  C   TYR A1757     -17.504  21.300  25.198  1.00 41.64           C  
ANISOU 2626  C   TYR A1757     5144   5542   5135    -82    357    414       C  
ATOM   2627  O   TYR A1757     -17.815  21.239  24.003  1.00 41.88           O  
ANISOU 2627  O   TYR A1757     5205   5714   4994    -19    372    435       O  
ATOM   2628  CB  TYR A1757     -15.638  19.711  25.707  1.00 41.74           C  
ANISOU 2628  CB  TYR A1757     5057   5536   5266   -123    430    256       C  
ATOM   2629  CG  TYR A1757     -14.152  19.493  25.886  1.00 42.02           C  
ANISOU 2629  CG  TYR A1757     5014   5560   5391   -152    523    267       C  
ATOM   2630  CD1 TYR A1757     -13.256  19.823  24.878  1.00 42.87           C  
ANISOU 2630  CD1 TYR A1757     5099   5765   5423   -127    650    348       C  
ATOM   2631  CD2 TYR A1757     -13.644  18.950  27.060  1.00 41.63           C  
ANISOU 2631  CD2 TYR A1757     4904   5415   5499   -201    486    210       C  
ATOM   2632  CE1 TYR A1757     -11.898  19.626  25.034  1.00 43.55           C  
ANISOU 2632  CE1 TYR A1757     5094   5851   5602   -151    740    368       C  
ATOM   2633  CE2 TYR A1757     -12.286  18.747  27.225  1.00 42.30           C  
ANISOU 2633  CE2 TYR A1757     4898   5503   5672   -223    563    232       C  
ATOM   2634  CZ  TYR A1757     -11.418  19.087  26.209  1.00 43.77           C  
ANISOU 2634  CZ  TYR A1757     5053   5784   5795   -198    691    309       C  
ATOM   2635  OH  TYR A1757     -10.065  18.889  26.366  1.00 45.36           O  
ANISOU 2635  OH  TYR A1757     5143   5999   6094   -217    773    340       O  
ATOM   2636  N   ALA A1758     -18.413  21.464  26.163  1.00 41.60           N  
ANISOU 2636  N   ALA A1758     5149   5439   5216   -102    267    392       N  
ATOM   2637  CA  ALA A1758     -19.818  21.654  25.817  1.00 42.90           C  
ANISOU 2637  CA  ALA A1758     5349   5656   5295    -47    188    409       C  
ATOM   2638  C   ALA A1758     -20.037  22.993  25.126  1.00 45.61           C  
ANISOU 2638  C   ALA A1758     5730   6021   5580     -6    236    590       C  
ATOM   2639  O   ALA A1758     -20.772  23.075  24.135  1.00 47.86           O  
ANISOU 2639  O   ALA A1758     6036   6435   5713     62    206    637       O  
ATOM   2640  CB  ALA A1758     -20.693  21.544  27.065  1.00 41.25           C  
ANISOU 2640  CB  ALA A1758     5131   5339   5203    -72    101    355       C  
ATOM   2641  N   PHE A1759     -19.405  24.055  25.634  1.00 45.00           N  
ANISOU 2641  N   PHE A1759     5660   5815   5623    -50    306    697       N  
ATOM   2642  CA  PHE A1759     -19.509  25.359  24.986  1.00 46.34           C  
ANISOU 2642  CA  PHE A1759     5867   5975   5764    -14    368    886       C  
ATOM   2643  C   PHE A1759     -18.826  25.363  23.624  1.00 48.49           C  
ANISOU 2643  C   PHE A1759     6141   6400   5885     18    454    972       C  
ATOM   2644  O   PHE A1759     -19.297  26.028  22.696  1.00 50.06           O  
ANISOU 2644  O   PHE A1759     6372   6681   5970     86    472   1116       O  
ATOM   2645  CB  PHE A1759     -18.918  26.441  25.893  1.00 46.10           C  
ANISOU 2645  CB  PHE A1759     5848   5747   5920    -88    425    959       C  
ATOM   2646  CG  PHE A1759     -18.869  27.804  25.261  1.00 48.24           C  
ANISOU 2646  CG  PHE A1759     6160   5971   6199    -63    505   1163       C  
ATOM   2647  CD1 PHE A1759     -19.988  28.619  25.256  1.00 49.39           C  
ANISOU 2647  CD1 PHE A1759     6349   6060   6356      9    475   1258       C  
ATOM   2648  CD2 PHE A1759     -17.702  28.270  24.676  1.00 49.60           C  
ANISOU 2648  CD2 PHE A1759     6317   6150   6378   -108    618   1274       C  
ATOM   2649  CE1 PHE A1759     -19.946  29.870  24.674  1.00 51.54           C  
ANISOU 2649  CE1 PHE A1759     6661   6271   6650     41    554   1462       C  
ATOM   2650  CE2 PHE A1759     -17.655  29.519  24.092  1.00 51.65           C  
ANISOU 2650  CE2 PHE A1759     6614   6353   6658    -89    699   1481       C  
ATOM   2651  CZ  PHE A1759     -18.778  30.321  24.092  1.00 52.76           C  
ANISOU 2651  CZ  PHE A1759     6809   6425   6814    -13    666   1576       C  
ATOM   2652  N   LYS A1760     -17.726  24.621  23.486  1.00 49.25           N  
ANISOU 2652  N   LYS A1760     6197   6544   5971    -20    511    894       N  
ATOM   2653  CA  LYS A1760     -17.013  24.528  22.217  1.00 49.94           C  
ANISOU 2653  CA  LYS A1760     6280   6789   5904     17    611    959       C  
ATOM   2654  C   LYS A1760     -17.839  23.845  21.136  1.00 48.74           C  
ANISOU 2654  C   LYS A1760     6162   6838   5520    106    554    903       C  
ATOM   2655  O   LYS A1760     -17.608  24.092  19.948  1.00 50.71           O  
ANISOU 2655  O   LYS A1760     6432   7241   5596    158    626   1003       O  
ATOM   2656  CB  LYS A1760     -15.699  23.779  22.422  1.00 50.59           C  
ANISOU 2656  CB  LYS A1760     6301   6875   6047    -32    684    868       C  
ATOM   2657  CG  LYS A1760     -14.647  24.024  21.358  1.00 53.15           C  
ANISOU 2657  CG  LYS A1760     6602   7319   6275    -16    832    978       C  
ATOM   2658  CD  LYS A1760     -13.323  23.381  21.749  1.00 55.44           C  
ANISOU 2658  CD  LYS A1760     6806   7588   6669    -65    907    902       C  
ATOM   2659  CE  LYS A1760     -12.229  23.684  20.737  1.00 59.24           C  
ANISOU 2659  CE  LYS A1760     7248   8190   7072    -50   1073   1027       C  
ATOM   2660  NZ  LYS A1760     -10.930  23.079  21.150  1.00 59.93           N  
ANISOU 2660  NZ  LYS A1760     7230   8261   7280    -91   1148    965       N  
ATOM   2661  N   THR A1761     -18.801  23.005  21.520  1.00 45.80           N  
ANISOU 2661  N   THR A1761     5793   6473   5136    118    426    749       N  
ATOM   2662  CA  THR A1761     -19.629  22.270  20.570  1.00 46.04           C  
ANISOU 2662  CA  THR A1761     5848   6688   4957    181    349    666       C  
ATOM   2663  C   THR A1761     -21.099  22.649  20.684  1.00 45.15           C  
ANISOU 2663  C   THR A1761     5746   6584   4825    216    224    710       C  
ATOM   2664  O   THR A1761     -21.960  21.906  20.207  1.00 45.72           O  
ANISOU 2664  O   THR A1761     5821   6784   4768    244    119    606       O  
ATOM   2665  CB  THR A1761     -19.469  20.760  20.764  1.00 46.33           C  
ANISOU 2665  CB  THR A1761     5868   6742   4993    160    307    428       C  
ATOM   2666  OG1 THR A1761     -19.814  20.408  22.110  1.00 44.74           O  
ANISOU 2666  OG1 THR A1761     5636   6373   4989    104    231    342       O  
ATOM   2667  CG2 THR A1761     -18.041  20.332  20.485  1.00 47.36           C  
ANISOU 2667  CG2 THR A1761     5979   6891   5123    152    439    388       C  
ATOM   2668  N   ARG A1762     -21.403  23.798  21.295  1.00 43.59           N  
ANISOU 2668  N   ARG A1762     5550   6252   4758    216    233    861       N  
ATOM   2669  CA  ARG A1762     -22.787  24.167  21.577  1.00 42.77           C  
ANISOU 2669  CA  ARG A1762     5441   6135   4674    258    125    903       C  
ATOM   2670  C   ARG A1762     -23.631  24.327  20.317  1.00 44.77           C  
ANISOU 2670  C   ARG A1762     5704   6600   4706    345     66    994       C  
ATOM   2671  O   ARG A1762     -24.863  24.275  20.401  1.00 45.63           O  
ANISOU 2671  O   ARG A1762     5787   6753   4799    382    -50    990       O  
ATOM   2672  CB  ARG A1762     -22.822  25.463  22.388  1.00 41.51           C  
ANISOU 2672  CB  ARG A1762     5293   5781   4696    254    175   1051       C  
ATOM   2673  CG  ARG A1762     -22.396  26.689  21.601  1.00 42.27           C  
ANISOU 2673  CG  ARG A1762     5425   5885   4752    295    277   1280       C  
ATOM   2674  CD  ARG A1762     -22.193  27.889  22.507  1.00 41.49           C  
ANISOU 2674  CD  ARG A1762     5347   5548   4869    267    342   1389       C  
ATOM   2675  NE  ARG A1762     -21.830  29.080  21.746  1.00 43.26           N  
ANISOU 2675  NE  ARG A1762     5605   5756   5075    303    443   1624       N  
ATOM   2676  CZ  ARG A1762     -20.605  29.335  21.297  1.00 44.13           C  
ANISOU 2676  CZ  ARG A1762     5720   5868   5179    252    560   1699       C  
ATOM   2677  NH1 ARG A1762     -20.367  30.445  20.612  1.00 46.49           N  
ANISOU 2677  NH1 ARG A1762     6048   6146   5471    284    653   1933       N  
ATOM   2678  NH2 ARG A1762     -19.618  28.481  21.531  1.00 42.69           N  
ANISOU 2678  NH2 ARG A1762     5506   5709   5006    172    590   1552       N  
ATOM   2679  N   ASN A1763     -23.007  24.523  19.157  1.00 45.57           N  
ANISOU 2679  N   ASN A1763     5836   6848   4631    379    142   1082       N  
ATOM   2680  CA  ASN A1763     -23.733  24.694  17.907  1.00 47.77           C  
ANISOU 2680  CA  ASN A1763     6127   7355   4668    463     84   1180       C  
ATOM   2681  C   ASN A1763     -23.696  23.455  17.023  1.00 49.85           C  
ANISOU 2681  C   ASN A1763     6402   7833   4706    461     32    994       C  
ATOM   2682  O   ASN A1763     -24.217  23.494  15.904  1.00 51.88           O  
ANISOU 2682  O   ASN A1763     6674   8315   4723    523    -22   1052       O  
ATOM   2683  CB  ASN A1763     -23.182  25.898  17.136  1.00 49.18           C  
ANISOU 2683  CB  ASN A1763     6339   7570   4778    515    207   1442       C  
ATOM   2684  CG  ASN A1763     -23.332  27.199  17.903  1.00 48.99           C  
ANISOU 2684  CG  ASN A1763     6316   7324   4975    524    253   1629       C  
ATOM   2685  OD1 ASN A1763     -24.294  27.387  18.648  1.00 48.07           O  
ANISOU 2685  OD1 ASN A1763     6176   7108   4982    541    166   1616       O  
ATOM   2686  ND2 ASN A1763     -22.377  28.104  17.725  1.00 49.95           N  
ANISOU 2686  ND2 ASN A1763     6463   7360   5155    510    398   1801       N  
ATOM   2687  N   VAL A1764     -23.095  22.365  17.491  1.00 49.40           N  
ANISOU 2687  N   VAL A1764     6340   7712   4716    394     47    773       N  
ATOM   2688  CA  VAL A1764     -23.065  21.111  16.742  1.00 50.85           C  
ANISOU 2688  CA  VAL A1764     6544   8061   4714    390      2    562       C  
ATOM   2689  C   VAL A1764     -24.480  20.546  16.693  1.00 52.75           C  
ANISOU 2689  C   VAL A1764     6760   8388   4897    387   -187    457       C  
ATOM   2690  O   VAL A1764     -25.090  20.314  17.747  1.00 50.86           O  
ANISOU 2690  O   VAL A1764     6474   8000   4851    342   -263    397       O  
ATOM   2691  CB  VAL A1764     -22.079  20.110  17.365  1.00 48.22           C  
ANISOU 2691  CB  VAL A1764     6207   7601   4513    329     70    366       C  
ATOM   2692  CG1 VAL A1764     -22.180  18.760  16.672  1.00 48.74           C  
ANISOU 2692  CG1 VAL A1764     6301   7802   4417    326     16    123       C  
ATOM   2693  CG2 VAL A1764     -20.659  20.648  17.280  1.00 47.86           C  
ANISOU 2693  CG2 VAL A1764     6167   7510   4508    331    253    476       C  
ATOM   2694  N   PRO A1765     -25.038  20.306  15.507  1.00 57.03           N  
ANISOU 2694  N   PRO A1765     7322   9175   5171    428   -267    435       N  
ATOM   2695  CA  PRO A1765     -26.448  19.915  15.399  1.00 59.47           C  
ANISOU 2695  CA  PRO A1765     7588   9587   5422    419   -460    367       C  
ATOM   2696  C   PRO A1765     -26.710  18.417  15.354  1.00 61.66           C  
ANISOU 2696  C   PRO A1765     7867   9894   5667    346   -559     65       C  
ATOM   2697  O   PRO A1765     -27.863  18.023  15.146  1.00 62.14           O  
ANISOU 2697  O   PRO A1765     7885  10062   5663    324   -727     -4       O  
ATOM   2698  CB  PRO A1765     -26.859  20.570  14.071  1.00 61.07           C  
ANISOU 2698  CB  PRO A1765     7809  10060   5334    503   -498    529       C  
ATOM   2699  CG  PRO A1765     -25.564  20.680  13.265  1.00 61.55           C  
ANISOU 2699  CG  PRO A1765     7947  10204   5236    536   -330    559       C  
ATOM   2700  CD  PRO A1765     -24.400  20.396  14.185  1.00 59.22           C  
ANISOU 2700  CD  PRO A1765     7659   9668   5173    482   -186    476       C  
ATOM   2701  N   ALA A1766     -25.694  17.581  15.545  1.00 63.21           N  
ANISOU 2701  N   ALA A1766     8105   9993   5918    308   -462   -109       N  
ATOM   2702  CA  ALA A1766     -25.887  16.141  15.453  1.00 65.66           C  
ANISOU 2702  CA  ALA A1766     8430  10308   6209    243   -542   -399       C  
ATOM   2703  C   ALA A1766     -26.801  15.643  16.567  1.00 66.05           C  
ANISOU 2703  C   ALA A1766     8406  10198   6492    166   -664   -475       C  
ATOM   2704  O   ALA A1766     -26.853  16.210  17.662  1.00 64.25           O  
ANISOU 2704  O   ALA A1766     8130   9799   6485    159   -633   -348       O  
ATOM   2705  CB  ALA A1766     -24.541  15.418  15.516  1.00 65.57           C  
ANISOU 2705  CB  ALA A1766     8471  10198   6245    238   -391   -543       C  
ATOM   2706  N   ASN A1767     -27.539  14.571  16.265  1.00 69.01           N  
ANISOU 2706  N   ASN A1767     8774  10636   6811    104   -802   -686       N  
ATOM   2707  CA  ASN A1767     -28.399  13.887  17.232  1.00 70.19           C  
ANISOU 2707  CA  ASN A1767     8851  10644   7176     16   -915   -782       C  
ATOM   2708  C   ASN A1767     -29.494  14.813  17.764  1.00 69.77           C  
ANISOU 2708  C   ASN A1767     8702  10602   7204     31  -1001   -579       C  
ATOM   2709  O   ASN A1767     -29.676  14.967  18.974  1.00 68.64           O  
ANISOU 2709  O   ASN A1767     8504  10277   7300      7   -981   -516       O  
ATOM   2710  CB  ASN A1767     -27.573  13.299  18.379  1.00 71.44           C  
ANISOU 2710  CB  ASN A1767     9014  10539   7592    -24   -809   -857       C  
ATOM   2711  CG  ASN A1767     -26.399  12.474  17.888  1.00 75.67           C  
ANISOU 2711  CG  ASN A1767     9634  11050   8068    -14   -700  -1032       C  
ATOM   2712  OD1 ASN A1767     -26.046  12.513  16.709  1.00 78.45           O  
ANISOU 2712  OD1 ASN A1767    10051  11581   8176     34   -670  -1076       O  
ATOM   2713  ND2 ASN A1767     -25.784  11.724  18.795  1.00 75.92           N  
ANISOU 2713  ND2 ASN A1767     9662  10867   8319    -50   -635  -1124       N  
ATOM   2714  N   PHE A1768     -30.232  15.426  16.837  1.00 71.20           N  
ANISOU 2714  N   PHE A1768     8863  11012   7179     79  -1095   -473       N  
ATOM   2715  CA  PHE A1768     -31.355  16.308  17.163  1.00 71.56           C  
ANISOU 2715  CA  PHE A1768     8808  11100   7280    115  -1183   -274       C  
ATOM   2716  C   PHE A1768     -30.927  17.428  18.108  1.00 70.38           C  
ANISOU 2716  C   PHE A1768     8653  10772   7315    177  -1046    -60       C  
ATOM   2717  O   PHE A1768     -31.550  17.673  19.144  1.00 69.61           O  
ANISOU 2717  O   PHE A1768     8482  10547   7421    166  -1066      5       O  
ATOM   2718  CB  PHE A1768     -32.525  15.517  17.753  1.00 71.42           C  
ANISOU 2718  CB  PHE A1768     8687  11049   7401     22  -1335   -388       C  
ATOM   2719  CG  PHE A1768     -33.320  14.749  16.735  1.00 74.43           C  
ANISOU 2719  CG  PHE A1768     9043  11649   7588    -37  -1515   -543       C  
ATOM   2720  CD1 PHE A1768     -34.092  15.412  15.794  1.00 76.91           C  
ANISOU 2720  CD1 PHE A1768     9310  12223   7688     22  -1630   -412       C  
ATOM   2721  CD2 PHE A1768     -33.310  13.363  16.728  1.00 75.18           C  
ANISOU 2721  CD2 PHE A1768     9159  11689   7719   -154  -1576   -819       C  
ATOM   2722  CE1 PHE A1768     -34.829  14.708  14.856  1.00 79.20           C  
ANISOU 2722  CE1 PHE A1768     9573  12735   7785    -43  -1813   -563       C  
ATOM   2723  CE2 PHE A1768     -34.046  12.653  15.794  1.00 77.73           C  
ANISOU 2723  CE2 PHE A1768     9463  12207   7865   -225  -1750   -984       C  
ATOM   2724  CZ  PHE A1768     -34.807  13.327  14.857  1.00 79.66           C  
ANISOU 2724  CZ  PHE A1768     9658  12730   7878   -173  -1875   -861       C  
ATOM   2725  N   ASN A1769     -29.845  18.115  17.736  1.00 70.48           N  
ANISOU 2725  N   ASN A1769     8746  10778   7254    239   -902     45       N  
ATOM   2726  CA  ASN A1769     -29.305  19.221  18.529  1.00 68.47           C  
ANISOU 2726  CA  ASN A1769     8501  10351   7165    286   -767    237       C  
ATOM   2727  C   ASN A1769     -29.003  18.778  19.959  1.00 64.31           C  
ANISOU 2727  C   ASN A1769     7954   9575   6905    217   -719    145       C  
ATOM   2728  O   ASN A1769     -29.315  19.473  20.928  1.00 63.41           O  
ANISOU 2728  O   ASN A1769     7804   9325   6966    233   -693    259       O  
ATOM   2729  CB  ASN A1769     -30.251  20.424  18.517  1.00 70.28           C  
ANISOU 2729  CB  ASN A1769     8672  10629   7401    370   -811    474       C  
ATOM   2730  CG  ASN A1769     -30.070  21.295  17.291  1.00 73.84           C  
ANISOU 2730  CG  ASN A1769     9164  11264   7627    462   -783    657       C  
ATOM   2731  OD1 ASN A1769     -29.340  20.940  16.367  1.00 75.62           O  
ANISOU 2731  OD1 ASN A1769     9457  11616   7658    460   -743    594       O  
ATOM   2732  ND2 ASN A1769     -30.737  22.444  17.277  1.00 75.75           N  
ANISOU 2732  ND2 ASN A1769     9366  11523   7894    552   -795    894       N  
ATOM   2733  N   GLU A1770     -28.390  17.598  20.087  1.00 61.52           N  
ANISOU 2733  N   GLU A1770     7630   9166   6580    147   -704    -64       N  
ATOM   2734  CA  GLU A1770     -28.065  17.069  21.408  1.00 57.87           C  
ANISOU 2734  CA  GLU A1770     7148   8484   6355     83   -664   -145       C  
ATOM   2735  C   GLU A1770     -27.111  17.988  22.162  1.00 55.26           C  
ANISOU 2735  C   GLU A1770     6844   8000   6152    107   -523    -12       C  
ATOM   2736  O   GLU A1770     -27.228  18.139  23.383  1.00 54.34           O  
ANISOU 2736  O   GLU A1770     6696   7725   6227     80   -508     12       O  
ATOM   2737  CB  GLU A1770     -27.469  15.666  21.276  1.00 58.19           C  
ANISOU 2737  CB  GLU A1770     7221   8492   6396     21   -661   -375       C  
ATOM   2738  CG  GLU A1770     -26.984  15.076  22.592  1.00 57.60           C  
ANISOU 2738  CG  GLU A1770     7128   8198   6558    -36   -611   -441       C  
ATOM   2739  CD  GLU A1770     -26.203  13.791  22.412  1.00 59.01           C  
ANISOU 2739  CD  GLU A1770     7345   8325   6750    -73   -579   -640       C  
ATOM   2740  OE1 GLU A1770     -26.163  13.269  21.279  1.00 60.98           O  
ANISOU 2740  OE1 GLU A1770     7638   8706   6825    -64   -605   -760       O  
ATOM   2741  OE2 GLU A1770     -25.626  13.304  23.407  1.00 58.19           O  
ANISOU 2741  OE2 GLU A1770     7230   8052   6828   -107   -527   -677       O  
ATOM   2742  N   ALA A1771     -26.186  18.632  21.448  1.00 54.22           N  
ANISOU 2742  N   ALA A1771     6767   7921   5914    153   -419     79       N  
ATOM   2743  CA  ALA A1771     -25.185  19.489  22.074  1.00 51.01           C  
ANISOU 2743  CA  ALA A1771     6381   7370   5629    158   -286    197       C  
ATOM   2744  C   ALA A1771     -25.774  20.760  22.670  1.00 48.49           C  
ANISOU 2744  C   ALA A1771     6045   6970   5410    193   -282    379       C  
ATOM   2745  O   ALA A1771     -25.177  21.327  23.592  1.00 47.52           O  
ANISOU 2745  O   ALA A1771     5930   6681   5443    170   -203    433       O  
ATOM   2746  CB  ALA A1771     -24.109  19.849  21.060  1.00 52.22           C  
ANISOU 2746  CB  ALA A1771     6585   7616   5640    194   -174    260       C  
ATOM   2747  N   LYS A1772     -26.922  21.226  22.172  1.00 48.02           N  
ANISOU 2747  N   LYS A1772     5960   7022   5265    252   -366    473       N  
ATOM   2748  CA  LYS A1772     -27.523  22.429  22.741  1.00 46.71           C  
ANISOU 2748  CA  LYS A1772     5776   6765   5207    303   -352    644       C  
ATOM   2749  C   LYS A1772     -28.006  22.178  24.163  1.00 43.64           C  
ANISOU 2749  C   LYS A1772     5345   6219   5017    261   -378    571       C  
ATOM   2750  O   LYS A1772     -27.879  23.050  25.032  1.00 42.14           O  
ANISOU 2750  O   LYS A1772     5169   5872   4968    272   -310    654       O  
ATOM   2751  CB  LYS A1772     -28.678  22.913  21.863  1.00 48.86           C  
ANISOU 2751  CB  LYS A1772     6013   7207   5345    389   -442    769       C  
ATOM   2752  CG  LYS A1772     -29.315  24.219  22.324  1.00 49.95           C  
ANISOU 2752  CG  LYS A1772     6133   7249   5595    469   -415    964       C  
ATOM   2753  CD  LYS A1772     -30.638  24.478  21.612  1.00 52.60           C  
ANISOU 2753  CD  LYS A1772     6401   7762   5823    556   -531   1073       C  
ATOM   2754  CE  LYS A1772     -30.460  24.511  20.103  1.00 54.90           C  
ANISOU 2754  CE  LYS A1772     6718   8279   5861    598   -560   1146       C  
ATOM   2755  NZ  LYS A1772     -31.745  24.781  19.402  1.00 56.48           N  
ANISOU 2755  NZ  LYS A1772     6841   8673   5945    683   -689   1265       N  
ATOM   2756  N   TYR A1773     -28.552  20.988  24.421  1.00 42.40           N  
ANISOU 2756  N   TYR A1773     5140   6099   4871    208   -472    414       N  
ATOM   2757  CA  TYR A1773     -29.064  20.670  25.748  1.00 40.45           C  
ANISOU 2757  CA  TYR A1773     4845   5725   4797    167   -494    356       C  
ATOM   2758  C   TYR A1773     -27.946  20.346  26.730  1.00 38.00           C  
ANISOU 2758  C   TYR A1773     4573   5254   4613    100   -411    278       C  
ATOM   2759  O   TYR A1773     -28.120  20.532  27.940  1.00 37.35           O  
ANISOU 2759  O   TYR A1773     4474   5045   4670     81   -390    280       O  
ATOM   2760  CB  TYR A1773     -30.049  19.502  25.667  1.00 41.23           C  
ANISOU 2760  CB  TYR A1773     4872   5916   4879    124   -621    233       C  
ATOM   2761  CG  TYR A1773     -31.245  19.775  24.784  1.00 42.44           C  
ANISOU 2761  CG  TYR A1773     4964   6246   4915    181   -726    307       C  
ATOM   2762  CD1 TYR A1773     -32.405  20.334  25.303  1.00 42.59           C  
ANISOU 2762  CD1 TYR A1773     4903   6263   5016    230   -765    409       C  
ATOM   2763  CD2 TYR A1773     -31.211  19.477  23.428  1.00 44.14           C  
ANISOU 2763  CD2 TYR A1773     5198   6644   4931    191   -787    279       C  
ATOM   2764  CE1 TYR A1773     -33.499  20.587  24.496  1.00 44.82           C  
ANISOU 2764  CE1 TYR A1773     5111   6721   5198    287   -870    492       C  
ATOM   2765  CE2 TYR A1773     -32.299  19.728  22.613  1.00 45.86           C  
ANISOU 2765  CE2 TYR A1773     5352   7046   5027    241   -900    355       C  
ATOM   2766  CZ  TYR A1773     -33.440  20.282  23.151  1.00 46.50           C  
ANISOU 2766  CZ  TYR A1773     5339   7121   5205    289   -945    467       C  
ATOM   2767  OH  TYR A1773     -34.521  20.529  22.337  1.00 49.07           O  
ANISOU 2767  OH  TYR A1773     5583   7644   5416    344  -1065    556       O  
ATOM   2768  N   ILE A1774     -26.803  19.864  26.238  1.00 36.63           N  
ANISOU 2768  N   ILE A1774     4441   5093   4384     68   -362    211       N  
ATOM   2769  CA  ILE A1774     -25.681  19.572  27.124  1.00 34.39           C  
ANISOU 2769  CA  ILE A1774     4176   4674   4218     10   -290    153       C  
ATOM   2770  C   ILE A1774     -25.021  20.862  27.590  1.00 35.55           C  
ANISOU 2770  C   ILE A1774     4358   4712   4435     21   -194    279       C  
ATOM   2771  O   ILE A1774     -24.613  20.982  28.751  1.00 34.86           O  
ANISOU 2771  O   ILE A1774     4272   4494   4479    -24   -163    261       O  
ATOM   2772  CB  ILE A1774     -24.673  18.642  26.425  1.00 33.74           C  
ANISOU 2772  CB  ILE A1774     4114   4642   4065    -14   -260     47       C  
ATOM   2773  CG1 ILE A1774     -25.376  17.383  25.913  1.00 33.60           C  
ANISOU 2773  CG1 ILE A1774     4072   4713   3980    -31   -357    -97       C  
ATOM   2774  CG2 ILE A1774     -23.536  18.273  27.376  1.00 33.09           C  
ANISOU 2774  CG2 ILE A1774     4029   4429   4117    -68   -195     -2       C  
ATOM   2775  CD1 ILE A1774     -24.468  16.436  25.163  1.00 33.51           C  
ANISOU 2775  CD1 ILE A1774     4090   4747   3894    -41   -322   -223       C  
ATOM   2776  N   ALA A1775     -24.905  21.846  26.695  1.00 37.62           N  
ANISOU 2776  N   ALA A1775     4653   5028   4612     75   -150    409       N  
ATOM   2777  CA  ALA A1775     -24.295  23.118  27.070  1.00 38.83           C  
ANISOU 2777  CA  ALA A1775     4845   5060   4849     76    -57    532       C  
ATOM   2778  C   ALA A1775     -25.141  23.852  28.102  1.00 39.37           C  
ANISOU 2778  C   ALA A1775     4913   5011   5037     96    -71    575       C  
ATOM   2779  O   ALA A1775     -24.603  24.466  29.030  1.00 38.08           O  
ANISOU 2779  O   ALA A1775     4776   4698   4993     57    -14    584       O  
ATOM   2780  CB  ALA A1775     -24.084  23.985  25.830  1.00 40.39           C  
ANISOU 2780  CB  ALA A1775     5076   5340   4932    135     -4    683       C  
ATOM   2781  N   PHE A1776     -26.468  23.799  27.959  1.00 41.61           N  
ANISOU 2781  N   PHE A1776     5160   5365   5286    157   -145    595       N  
ATOM   2782  CA  PHE A1776     -27.337  24.444  28.937  1.00 42.25           C  
ANISOU 2782  CA  PHE A1776     5231   5345   5479    193   -146    631       C  
ATOM   2783  C   PHE A1776     -27.281  23.741  30.287  1.00 40.80           C  
ANISOU 2783  C   PHE A1776     5027   5076   5398    123   -159    502       C  
ATOM   2784  O   PHE A1776     -27.447  24.389  31.327  1.00 40.24           O  
ANISOU 2784  O   PHE A1776     4977   4881   5429    127   -118    511       O  
ATOM   2785  CB  PHE A1776     -28.774  24.486  28.420  1.00 44.04           C  
ANISOU 2785  CB  PHE A1776     5397   5689   5646    279   -224    693       C  
ATOM   2786  CG  PHE A1776     -29.733  25.167  29.354  1.00 44.98           C  
ANISOU 2786  CG  PHE A1776     5495   5716   5879    337   -210    739       C  
ATOM   2787  CD1 PHE A1776     -29.840  26.548  29.370  1.00 46.34           C  
ANISOU 2787  CD1 PHE A1776     5712   5785   6110    417   -136    876       C  
ATOM   2788  CD2 PHE A1776     -30.531  24.427  30.213  1.00 44.93           C  
ANISOU 2788  CD2 PHE A1776     5423   5721   5929    317   -261    650       C  
ATOM   2789  CE1 PHE A1776     -30.721  27.179  30.228  1.00 47.27           C  
ANISOU 2789  CE1 PHE A1776     5815   5812   6334    485   -109    906       C  
ATOM   2790  CE2 PHE A1776     -31.414  25.052  31.074  1.00 45.61           C  
ANISOU 2790  CE2 PHE A1776     5484   5734   6111    381   -232    691       C  
ATOM   2791  CZ  PHE A1776     -31.510  26.429  31.081  1.00 46.86           C  
ANISOU 2791  CZ  PHE A1776     5693   5790   6322    470   -154    812       C  
ATOM   2792  N   THR A1777     -27.054  22.426  30.292  1.00 40.36           N  
ANISOU 2792  N   THR A1777     4937   5083   5315     62   -211    383       N  
ATOM   2793  CA  THR A1777     -26.940  21.704  31.555  1.00 40.34           C  
ANISOU 2793  CA  THR A1777     4915   5006   5407     -2   -221    282       C  
ATOM   2794  C   THR A1777     -25.702  22.138  32.327  1.00 41.43           C  
ANISOU 2794  C   THR A1777     5102   5022   5617    -59   -149    272       C  
ATOM   2795  O   THR A1777     -25.750  22.292  33.553  1.00 42.71           O  
ANISOU 2795  O   THR A1777     5272   5097   5860    -86   -136    243       O  
ATOM   2796  CB  THR A1777     -26.907  20.198  31.302  1.00 40.14           C  
ANISOU 2796  CB  THR A1777     4845   5055   5351    -51   -286    170       C  
ATOM   2797  OG1 THR A1777     -28.049  19.820  30.525  1.00 40.22           O  
ANISOU 2797  OG1 THR A1777     4806   5185   5290    -15   -366    169       O  
ATOM   2798  CG2 THR A1777     -26.927  19.436  32.619  1.00 39.88           C  
ANISOU 2798  CG2 THR A1777     4784   4949   5419   -109   -299     96       C  
ATOM   2799  N   MET A1778     -24.584  22.346  31.627  1.00 41.56           N  
ANISOU 2799  N   MET A1778     5148   5044   5600    -80   -103    296       N  
ATOM   2800  CA  MET A1778     -23.358  22.750  32.306  1.00 41.49           C  
ANISOU 2800  CA  MET A1778     5166   4931   5665   -146    -45    290       C  
ATOM   2801  C   MET A1778     -23.415  24.203  32.758  1.00 43.28           C  
ANISOU 2801  C   MET A1778     5448   5039   5956   -136     10    367       C  
ATOM   2802  O   MET A1778     -22.760  24.567  33.741  1.00 43.60           O  
ANISOU 2802  O   MET A1778     5512   4978   6077   -200     35    334       O  
ATOM   2803  CB  MET A1778     -22.151  22.517  31.398  1.00 40.96           C  
ANISOU 2803  CB  MET A1778     5096   4914   5554   -172     -3    300       C  
ATOM   2804  CG  MET A1778     -21.970  21.068  30.965  1.00 40.53           C  
ANISOU 2804  CG  MET A1778     4999   4954   5448   -178    -42    204       C  
ATOM   2805  SD  MET A1778     -22.181  19.876  32.307  1.00 39.41           S  
ANISOU 2805  SD  MET A1778     4814   4764   5394   -226   -105     91       S  
ATOM   2806  CE  MET A1778     -20.961  20.444  33.491  1.00 39.45           C  
ANISOU 2806  CE  MET A1778     4825   4662   5504   -300    -61    106       C  
ATOM   2807  N   TYR A1779     -24.184  25.044  32.060  1.00 45.21           N  
ANISOU 2807  N   TYR A1779     5715   5293   6170    -55     26    468       N  
ATOM   2808  CA  TYR A1779     -24.369  26.421  32.509  1.00 46.32           C  
ANISOU 2808  CA  TYR A1779     5914   5295   6391    -30     85    538       C  
ATOM   2809  C   TYR A1779     -25.048  26.457  33.872  1.00 44.93           C  
ANISOU 2809  C   TYR A1779     5744   5043   6284    -29     71    461       C  
ATOM   2810  O   TYR A1779     -24.593  27.150  34.790  1.00 45.92           O  
ANISOU 2810  O   TYR A1779     5922   5035   6489    -76    113    428       O  
ATOM   2811  CB  TYR A1779     -25.189  27.210  31.486  1.00 48.87           C  
ANISOU 2811  CB  TYR A1779     6248   5651   6671     78    100    678       C  
ATOM   2812  CG  TYR A1779     -24.561  27.323  30.113  1.00 50.48           C  
ANISOU 2812  CG  TYR A1779     6455   5941   6785     87    126    776       C  
ATOM   2813  CD1 TYR A1779     -23.189  27.199  29.938  1.00 50.95           C  
ANISOU 2813  CD1 TYR A1779     6523   5985   6850      1    173    761       C  
ATOM   2814  CD2 TYR A1779     -25.346  27.557  28.990  1.00 51.89           C  
ANISOU 2814  CD2 TYR A1779     6620   6231   6864    186    106    892       C  
ATOM   2815  CE1 TYR A1779     -22.616  27.302  28.681  1.00 52.16           C  
ANISOU 2815  CE1 TYR A1779     6677   6231   6912     15    213    856       C  
ATOM   2816  CE2 TYR A1779     -24.783  27.661  27.731  1.00 52.54           C  
ANISOU 2816  CE2 TYR A1779     6710   6413   6839    199    135    987       C  
ATOM   2817  CZ  TYR A1779     -23.418  27.533  27.582  1.00 53.06           C  
ANISOU 2817  CZ  TYR A1779     6790   6460   6911    114    196    968       C  
ATOM   2818  OH  TYR A1779     -22.852  27.637  26.332  1.00 54.98           O  
ANISOU 2818  OH  TYR A1779     7037   6813   7038    132    242   1068       O  
ATOM   2819  N   THR A1780     -26.143  25.708  34.021  1.00 43.12           N  
ANISOU 2819  N   THR A1780     5459   4903   6021     19     14    429       N  
ATOM   2820  CA  THR A1780     -26.849  25.665  35.298  1.00 41.65           C  
ANISOU 2820  CA  THR A1780     5269   4669   5887     27     12    366       C  
ATOM   2821  C   THR A1780     -26.027  24.943  36.359  1.00 40.31           C  
ANISOU 2821  C   THR A1780     5099   4477   5738    -75     -3    258       C  
ATOM   2822  O   THR A1780     -26.023  25.347  37.529  1.00 40.97           O  
ANISOU 2822  O   THR A1780     5221   4479   5865    -97     24    208       O  
ATOM   2823  CB  THR A1780     -28.208  24.989  35.118  1.00 41.33           C  
ANISOU 2823  CB  THR A1780     5148   4743   5812     95    -44    376       C  
ATOM   2824  OG1 THR A1780     -28.922  25.632  34.057  1.00 42.40           O  
ANISOU 2824  OG1 THR A1780     5270   4924   5916    192    -45    490       O  
ATOM   2825  CG2 THR A1780     -29.028  25.082  36.397  1.00 41.76           C  
ANISOU 2825  CG2 THR A1780     5192   4755   5919    120    -23    335       C  
ATOM   2826  N   THR A1781     -25.322  23.878  35.969  1.00 38.83           N  
ANISOU 2826  N   THR A1781     4872   4366   5517   -133    -46    222       N  
ATOM   2827  CA  THR A1781     -24.528  23.119  36.931  1.00 37.89           C  
ANISOU 2827  CA  THR A1781     4739   4236   5422   -219    -67    141       C  
ATOM   2828  C   THR A1781     -23.439  23.983  37.555  1.00 37.55           C  
ANISOU 2828  C   THR A1781     4753   4091   5425   -287    -26    127       C  
ATOM   2829  O   THR A1781     -23.181  23.893  38.762  1.00 36.97           O  
ANISOU 2829  O   THR A1781     4690   3984   5372   -339    -36     66       O  
ATOM   2830  CB  THR A1781     -23.918  21.892  36.252  1.00 37.01           C  
ANISOU 2830  CB  THR A1781     4575   4208   5280   -251   -106    115       C  
ATOM   2831  OG1 THR A1781     -24.966  21.045  35.760  1.00 36.83           O  
ANISOU 2831  OG1 THR A1781     4502   4271   5221   -207   -156    105       O  
ATOM   2832  CG2 THR A1781     -23.061  21.111  37.232  1.00 35.75           C  
ANISOU 2832  CG2 THR A1781     4391   4035   5157   -327   -127     55       C  
ATOM   2833  N   CYS A1782     -22.793  24.832  36.753  1.00 37.73           N  
ANISOU 2833  N   CYS A1782     4808   4067   5461   -295     18    187       N  
ATOM   2834  CA  CYS A1782     -21.769  25.723  37.290  1.00 37.72           C  
ANISOU 2834  CA  CYS A1782     4853   3957   5520   -376     54    175       C  
ATOM   2835  C   CYS A1782     -22.359  26.682  38.315  1.00 38.66           C  
ANISOU 2835  C   CYS A1782     5045   3963   5680   -364     80    136       C  
ATOM   2836  O   CYS A1782     -21.800  26.868  39.401  1.00 38.62           O  
ANISOU 2836  O   CYS A1782     5068   3906   5700   -443     70     59       O  
ATOM   2837  CB  CYS A1782     -21.097  26.496  36.157  1.00 37.18           C  
ANISOU 2837  CB  CYS A1782     4802   3855   5469   -382    108    268       C  
ATOM   2838  SG  CYS A1782     -20.005  25.496  35.130  1.00 35.78           S  
ANISOU 2838  SG  CYS A1782     4548   3801   5246   -415    101    292       S  
ATOM   2839  N   ILE A1783     -23.497  27.298  37.987  1.00 39.01           N  
ANISOU 2839  N   ILE A1783     5119   3975   5727   -260    115    187       N  
ATOM   2840  CA  ILE A1783     -24.119  28.248  38.905  1.00 39.31           C  
ANISOU 2840  CA  ILE A1783     5231   3896   5810   -227    159    146       C  
ATOM   2841  C   ILE A1783     -24.588  27.539  40.168  1.00 37.79           C  
ANISOU 2841  C   ILE A1783     5021   3758   5579   -235    128     48       C  
ATOM   2842  O   ILE A1783     -24.449  28.061  41.281  1.00 38.71           O  
ANISOU 2842  O   ILE A1783     5201   3797   5709   -273    149    -37       O  
ATOM   2843  CB  ILE A1783     -25.276  28.985  38.209  1.00 40.69           C  
ANISOU 2843  CB  ILE A1783     5421   4037   6003    -92    206    241       C  
ATOM   2844  CG1 ILE A1783     -24.787  29.652  36.922  1.00 40.98           C  
ANISOU 2844  CG1 ILE A1783     5473   4035   6063    -82    238    363       C  
ATOM   2845  CG2 ILE A1783     -25.889  30.015  39.145  1.00 41.89           C  
ANISOU 2845  CG2 ILE A1783     5653   4048   6214    -42    271    193       C  
ATOM   2846  CD1 ILE A1783     -25.886  30.315  36.125  1.00 41.64           C  
ANISOU 2846  CD1 ILE A1783     5559   4107   6155     60    273    486       C  
ATOM   2847  N   ILE A1784     -25.149  26.338  40.015  1.00 36.07           N  
ANISOU 2847  N   ILE A1784     4719   3675   5309   -206     78     59       N  
ATOM   2848  CA  ILE A1784     -25.623  25.579  41.170  1.00 34.80           C  
ANISOU 2848  CA  ILE A1784     4533   3576   5115   -214     55     -7       C  
ATOM   2849  C   ILE A1784     -24.456  25.203  42.074  1.00 34.10           C  
ANISOU 2849  C   ILE A1784     4456   3490   5012   -329     19    -79       C  
ATOM   2850  O   ILE A1784     -24.522  25.352  43.300  1.00 34.86           O  
ANISOU 2850  O   ILE A1784     4590   3574   5082   -354     26   -149       O  
ATOM   2851  CB  ILE A1784     -26.404  24.336  40.709  1.00 33.69           C  
ANISOU 2851  CB  ILE A1784     4294   3564   4944   -174      7     30       C  
ATOM   2852  CG1 ILE A1784     -27.797  24.731  40.223  1.00 33.60           C  
ANISOU 2852  CG1 ILE A1784     4256   3569   4939    -58     34     91       C  
ATOM   2853  CG2 ILE A1784     -26.493  23.307  41.827  1.00 33.66           C  
ANISOU 2853  CG2 ILE A1784     4250   3624   4913   -217    -25    -19       C  
ATOM   2854  CD1 ILE A1784     -28.646  23.556  39.822  1.00 33.20           C  
ANISOU 2854  CD1 ILE A1784     4102   3644   4868    -35    -22    118       C  
ATOM   2855  N   TRP A1785     -23.367  24.713  41.481  1.00 32.88           N  
ANISOU 2855  N   TRP A1785     4263   3364   4867   -397    -20    -60       N  
ATOM   2856  CA  TRP A1785     -22.224  24.288  42.280  1.00 31.30           C  
ANISOU 2856  CA  TRP A1785     4048   3184   4659   -501    -64   -110       C  
ATOM   2857  C   TRP A1785     -21.465  25.480  42.853  1.00 32.58           C  
ANISOU 2857  C   TRP A1785     4287   3241   4849   -576    -45   -164       C  
ATOM   2858  O   TRP A1785     -20.930  25.401  43.966  1.00 32.60           O  
ANISOU 2858  O   TRP A1785     4302   3260   4823   -651    -82   -232       O  
ATOM   2859  CB  TRP A1785     -21.302  23.406  41.441  1.00 29.77           C  
ANISOU 2859  CB  TRP A1785     3780   3052   4480   -536    -99    -70       C  
ATOM   2860  CG  TRP A1785     -21.783  21.991  41.345  1.00 28.31           C  
ANISOU 2860  CG  TRP A1785     3523   2962   4273   -500   -139    -58       C  
ATOM   2861  CD1 TRP A1785     -22.946  21.557  40.781  1.00 27.52           C  
ANISOU 2861  CD1 TRP A1785     3400   2899   4158   -423   -136    -33       C  
ATOM   2862  CD2 TRP A1785     -21.113  20.822  41.834  1.00 28.03           C  
ANISOU 2862  CD2 TRP A1785     3423   2985   4241   -544   -189    -67       C  
ATOM   2863  NE1 TRP A1785     -23.042  20.190  40.886  1.00 27.16           N  
ANISOU 2863  NE1 TRP A1785     3287   2919   4113   -428   -180    -37       N  
ATOM   2864  CE2 TRP A1785     -21.928  19.715  41.527  1.00 27.41           C  
ANISOU 2864  CE2 TRP A1785     3296   2958   4159   -494   -208    -51       C  
ATOM   2865  CE3 TRP A1785     -19.900  20.604  42.495  1.00 27.60           C  
ANISOU 2865  CE3 TRP A1785     3341   2945   4199   -621   -224    -79       C  
ATOM   2866  CZ2 TRP A1785     -21.572  18.409  41.862  1.00 27.09           C  
ANISOU 2866  CZ2 TRP A1785     3193   2960   4139   -514   -249    -47       C  
ATOM   2867  CZ3 TRP A1785     -19.548  19.307  42.825  1.00 26.97           C  
ANISOU 2867  CZ3 TRP A1785     3190   2926   4131   -628   -269    -62       C  
ATOM   2868  CH2 TRP A1785     -20.381  18.227  42.510  1.00 26.84           C  
ANISOU 2868  CH2 TRP A1785     3138   2937   4122   -572   -275    -46       C  
ATOM   2869  N   LEU A1786     -21.400  26.591  42.115  1.00 34.00           N  
ANISOU 2869  N   LEU A1786     4520   3314   5084   -564      9   -132       N  
ATOM   2870  CA  LEU A1786     -20.747  27.783  42.648  1.00 35.74           C  
ANISOU 2870  CA  LEU A1786     4821   3407   5353   -645     31   -191       C  
ATOM   2871  C   LEU A1786     -21.532  28.355  43.820  1.00 37.61           C  
ANISOU 2871  C   LEU A1786     5145   3586   5560   -616     58   -288       C  
ATOM   2872  O   LEU A1786     -20.955  28.709  44.854  1.00 38.44           O  
ANISOU 2872  O   LEU A1786     5298   3660   5648   -707     32   -390       O  
ATOM   2873  CB  LEU A1786     -20.578  28.832  41.550  1.00 35.77           C  
ANISOU 2873  CB  LEU A1786     4863   3292   5437   -631     94   -114       C  
ATOM   2874  CG  LEU A1786     -19.391  28.630  40.609  1.00 34.98           C  
ANISOU 2874  CG  LEU A1786     4697   3223   5372   -703     84    -39       C  
ATOM   2875  CD1 LEU A1786     -19.361  29.729  39.562  1.00 36.03           C  
ANISOU 2875  CD1 LEU A1786     4873   3238   5577   -680    160     58       C  
ATOM   2876  CD2 LEU A1786     -18.090  28.594  41.397  1.00 34.68           C  
ANISOU 2876  CD2 LEU A1786     4633   3186   5358   -852     32   -107       C  
ATOM   2877  N   ALA A1787     -22.856  28.446  43.678  1.00 38.15           N  
ANISOU 2877  N   ALA A1787     5228   3651   5615   -486    109   -261       N  
ATOM   2878  CA  ALA A1787     -23.690  28.957  44.758  1.00 40.26           C  
ANISOU 2878  CA  ALA A1787     5571   3875   5852   -436    155   -350       C  
ATOM   2879  C   ALA A1787     -23.698  28.033  45.967  1.00 39.26           C  
ANISOU 2879  C   ALA A1787     5416   3878   5622   -473    106   -418       C  
ATOM   2880  O   ALA A1787     -23.998  28.486  47.077  1.00 40.26           O  
ANISOU 2880  O   ALA A1787     5619   3981   5699   -471    135   -520       O  
ATOM   2881  CB  ALA A1787     -25.118  29.176  44.256  1.00 40.40           C  
ANISOU 2881  CB  ALA A1787     5581   3881   5888   -278    223   -282       C  
ATOM   2882  N   PHE A1788     -23.365  26.754  45.780  1.00 37.98           N  
ANISOU 2882  N   PHE A1788     5152   3850   5427   -503     36   -362       N  
ATOM   2883  CA  PHE A1788     -23.404  25.805  46.888  1.00 38.42           C  
ANISOU 2883  CA  PHE A1788     5174   4031   5392   -530     -8   -394       C  
ATOM   2884  C   PHE A1788     -22.339  26.109  47.934  1.00 39.29           C  
ANISOU 2884  C   PHE A1788     5333   4143   5454   -649    -58   -490       C  
ATOM   2885  O   PHE A1788     -22.577  25.929  49.134  1.00 40.00           O  
ANISOU 2885  O   PHE A1788     5451   4301   5444   -657    -65   -552       O  
ATOM   2886  CB  PHE A1788     -23.236  24.381  46.360  1.00 38.33           C  
ANISOU 2886  CB  PHE A1788     5047   4133   5385   -533    -67   -305       C  
ATOM   2887  CG  PHE A1788     -22.976  23.360  47.434  1.00 38.56           C  
ANISOU 2887  CG  PHE A1788     5032   4278   5341   -577   -123   -312       C  
ATOM   2888  CD1 PHE A1788     -24.027  22.788  48.133  1.00 38.26           C  
ANISOU 2888  CD1 PHE A1788     4976   4315   5247   -517    -97   -295       C  
ATOM   2889  CD2 PHE A1788     -21.680  22.964  47.737  1.00 38.75           C  
ANISOU 2889  CD2 PHE A1788     5024   4343   5357   -675   -198   -316       C  
ATOM   2890  CE1 PHE A1788     -23.791  21.842  49.116  1.00 37.62           C  
ANISOU 2890  CE1 PHE A1788     4855   4342   5096   -554   -143   -277       C  
ATOM   2891  CE2 PHE A1788     -21.438  22.021  48.721  1.00 37.87           C  
ANISOU 2891  CE2 PHE A1788     4868   4343   5178   -706   -252   -299       C  
ATOM   2892  CZ  PHE A1788     -22.494  21.458  49.410  1.00 37.45           C  
ANISOU 2892  CZ  PHE A1788     4808   4358   5063   -645   -223   -275       C  
ATOM   2893  N   VAL A1789     -21.161  26.551  47.504  1.00 38.83           N  
ANISOU 2893  N   VAL A1789     5276   4024   5455   -746    -95   -499       N  
ATOM   2894  CA  VAL A1789     -20.023  26.725  48.406  1.00 40.16           C  
ANISOU 2894  CA  VAL A1789     5461   4216   5584   -879   -168   -579       C  
ATOM   2895  C   VAL A1789     -20.351  27.728  49.512  1.00 41.20           C  
ANISOU 2895  C   VAL A1789     5720   4283   5651   -898   -137   -723       C  
ATOM   2896  O   VAL A1789     -20.198  27.388  50.694  1.00 41.84           O  
ANISOU 2896  O   VAL A1789     5814   4470   5614   -941   -187   -789       O  
ATOM   2897  CB  VAL A1789     -18.754  27.132  47.636  1.00 41.26           C  
ANISOU 2897  CB  VAL A1789     5565   4292   5822   -982   -200   -553       C  
ATOM   2898  CG1 VAL A1789     -17.588  27.289  48.593  1.00 42.73           C  
ANISOU 2898  CG1 VAL A1789     5747   4519   5971  -1129   -291   -634       C  
ATOM   2899  CG2 VAL A1789     -18.429  26.105  46.561  1.00 39.84           C  
ANISOU 2899  CG2 VAL A1789     5265   4185   5689   -951   -217   -426       C  
ATOM   2900  N   PRO A1790     -20.806  28.952  49.213  1.00 41.21           N  
ANISOU 2900  N   PRO A1790     5822   4116   5720   -862    -54   -777       N  
ATOM   2901  CA  PRO A1790     -21.132  29.865  50.319  1.00 42.37           C  
ANISOU 2901  CA  PRO A1790     6102   4194   5804   -872    -16   -936       C  
ATOM   2902  C   PRO A1790     -22.401  29.482  51.057  1.00 42.33           C  
ANISOU 2902  C   PRO A1790     6118   4276   5689   -746     47   -955       C  
ATOM   2903  O   PRO A1790     -22.508  29.750  52.261  1.00 44.17           O  
ANISOU 2903  O   PRO A1790     6433   4545   5804   -767     52  -1085       O  
ATOM   2904  CB  PRO A1790     -21.266  31.225  49.623  1.00 43.40           C  
ANISOU 2904  CB  PRO A1790     6325   4095   6071   -854     68   -963       C  
ATOM   2905  CG  PRO A1790     -21.724  30.884  48.261  1.00 42.20           C  
ANISOU 2905  CG  PRO A1790     6091   3936   6008   -754    106   -794       C  
ATOM   2906  CD  PRO A1790     -21.027  29.602  47.906  1.00 40.94           C  
ANISOU 2906  CD  PRO A1790     5795   3942   5817   -807     14   -697       C  
ATOM   2907  N   ILE A1791     -23.363  28.856  50.376  1.00 40.48           N  
ANISOU 2907  N   ILE A1791     5809   4089   5485   -620     94   -830       N  
ATOM   2908  CA  ILE A1791     -24.617  28.487  51.026  1.00 40.39           C  
ANISOU 2908  CA  ILE A1791     5795   4163   5387   -501    163   -829       C  
ATOM   2909  C   ILE A1791     -24.389  27.365  52.032  1.00 40.46           C  
ANISOU 2909  C   ILE A1791     5751   4366   5256   -550     95   -822       C  
ATOM   2910  O   ILE A1791     -24.894  27.414  53.160  1.00 43.20           O  
ANISOU 2910  O   ILE A1791     6151   4784   5478   -520    136   -897       O  
ATOM   2911  CB  ILE A1791     -25.670  28.098  49.971  1.00 39.42           C  
ANISOU 2911  CB  ILE A1791     5588   4046   5346   -372    215   -691       C  
ATOM   2912  CG1 ILE A1791     -26.141  29.337  49.205  1.00 40.38           C  
ANISOU 2912  CG1 ILE A1791     5776   3985   5583   -290    302   -694       C  
ATOM   2913  CG2 ILE A1791     -26.847  27.382  50.618  1.00 38.98           C  
ANISOU 2913  CG2 ILE A1791     5482   4121   5210   -275    265   -657       C  
ATOM   2914  CD1 ILE A1791     -27.092  29.030  48.062  1.00 39.64           C  
ANISOU 2914  CD1 ILE A1791     5589   3907   5564   -170    333   -549       C  
ATOM   2915  N   TYR A1792     -23.617  26.346  51.651  1.00 38.06           N  
ANISOU 2915  N   TYR A1792     5342   4150   4969   -619     -2   -726       N  
ATOM   2916  CA  TYR A1792     -23.450  25.175  52.508  1.00 37.56           C  
ANISOU 2916  CA  TYR A1792     5213   4264   4794   -649    -64   -681       C  
ATOM   2917  C   TYR A1792     -22.561  25.484  53.707  1.00 40.56           C  
ANISOU 2917  C   TYR A1792     5658   4704   5047   -757   -131   -794       C  
ATOM   2918  O   TYR A1792     -22.974  25.320  54.861  1.00 41.58           O  
ANISOU 2918  O   TYR A1792     5826   4943   5028   -739   -113   -837       O  
ATOM   2919  CB  TYR A1792     -22.875  24.013  51.700  1.00 34.88           C  
ANISOU 2919  CB  TYR A1792     4745   3979   4531   -677   -140   -548       C  
ATOM   2920  CG  TYR A1792     -22.545  22.790  52.528  1.00 34.66           C  
ANISOU 2920  CG  TYR A1792     4644   4109   4415   -711   -209   -481       C  
ATOM   2921  CD1 TYR A1792     -23.544  21.921  52.948  1.00 34.43           C  
ANISOU 2921  CD1 TYR A1792     4569   4172   4339   -638   -169   -403       C  
ATOM   2922  CD2 TYR A1792     -21.233  22.499  52.881  1.00 34.59           C  
ANISOU 2922  CD2 TYR A1792     4602   4159   4380   -816   -315   -481       C  
ATOM   2923  CE1 TYR A1792     -23.247  20.802  53.701  1.00 34.33           C  
ANISOU 2923  CE1 TYR A1792     4493   4294   4258   -665   -226   -320       C  
ATOM   2924  CE2 TYR A1792     -20.927  21.382  53.634  1.00 34.37           C  
ANISOU 2924  CE2 TYR A1792     4504   4276   4278   -835   -380   -398       C  
ATOM   2925  CZ  TYR A1792     -21.938  20.538  54.040  1.00 34.43           C  
ANISOU 2925  CZ  TYR A1792     4480   4361   4242   -758   -332   -315       C  
ATOM   2926  OH  TYR A1792     -21.640  19.424  54.789  1.00 34.62           O  
ANISOU 2926  OH  TYR A1792     4435   4517   4203   -773   -390   -212       O  
ATOM   2927  N   PHE A1793     -21.326  25.925  53.453  1.00 42.31           N  
ANISOU 2927  N   PHE A1793     5886   4870   5320   -875   -211   -838       N  
ATOM   2928  CA  PHE A1793     -20.364  26.128  54.529  1.00 44.54           C  
ANISOU 2928  CA  PHE A1793     6206   5231   5485   -999   -304   -938       C  
ATOM   2929  C   PHE A1793     -20.757  27.250  55.480  1.00 46.79           C  
ANISOU 2929  C   PHE A1793     6647   5466   5664  -1005   -251  -1124       C  
ATOM   2930  O   PHE A1793     -20.168  27.354  56.561  1.00 47.43           O  
ANISOU 2930  O   PHE A1793     6772   5648   5601  -1097   -327  -1223       O  
ATOM   2931  CB  PHE A1793     -18.975  26.397  53.946  1.00 44.47           C  
ANISOU 2931  CB  PHE A1793     6150   5167   5580  -1129   -398   -937       C  
ATOM   2932  CG  PHE A1793     -18.351  25.193  53.306  1.00 42.61           C  
ANISOU 2932  CG  PHE A1793     5760   5019   5411  -1135   -465   -775       C  
ATOM   2933  CD1 PHE A1793     -17.701  24.244  54.078  1.00 42.37           C  
ANISOU 2933  CD1 PHE A1793     5648   5161   5289  -1182   -567   -719       C  
ATOM   2934  CD2 PHE A1793     -18.421  25.002  51.934  1.00 41.63           C  
ANISOU 2934  CD2 PHE A1793     5574   4807   5438  -1085   -422   -678       C  
ATOM   2935  CE1 PHE A1793     -17.129  23.131  53.496  1.00 41.71           C  
ANISOU 2935  CE1 PHE A1793     5426   5139   5283  -1173   -617   -573       C  
ATOM   2936  CE2 PHE A1793     -17.849  23.889  51.343  1.00 40.48           C  
ANISOU 2936  CE2 PHE A1793     5296   4732   5351  -1082   -471   -549       C  
ATOM   2937  CZ  PHE A1793     -17.203  22.952  52.126  1.00 40.88           C  
ANISOU 2937  CZ  PHE A1793     5268   4934   5330  -1123   -565   -498       C  
ATOM   2938  N   GLY A1794     -21.725  28.083  55.113  1.00 48.48           N  
ANISOU 2938  N   GLY A1794     6946   5533   5941   -906   -125  -1177       N  
ATOM   2939  CA  GLY A1794     -22.273  29.081  56.005  1.00 49.21           C  
ANISOU 2939  CA  GLY A1794     7191   5568   5939   -878    -46  -1356       C  
ATOM   2940  C   GLY A1794     -23.619  28.725  56.595  1.00 47.85           C  
ANISOU 2940  C   GLY A1794     7032   5490   5659   -730     67  -1337       C  
ATOM   2941  O   GLY A1794     -24.274  29.598  57.176  1.00 49.64           O  
ANISOU 2941  O   GLY A1794     7383   5649   5828   -667    170  -1478       O  
ATOM   2942  N   SER A1795     -24.050  27.473  56.475  1.00 45.11           N  
ANISOU 2942  N   SER A1795     6558   5290   5291   -672     58  -1167       N  
ATOM   2943  CA  SER A1795     -25.370  27.046  56.907  1.00 43.37           C  
ANISOU 2943  CA  SER A1795     6318   5161   4998   -535    171  -1114       C  
ATOM   2944  C   SER A1795     -25.298  26.272  58.218  1.00 42.92           C  
ANISOU 2944  C   SER A1795     6254   5326   4727   -563    136  -1106       C  
ATOM   2945  O   SER A1795     -24.289  25.638  58.537  1.00 42.75           O  
ANISOU 2945  O   SER A1795     6185   5412   4644   -671      6  -1065       O  
ATOM   2946  CB  SER A1795     -26.034  26.177  55.836  1.00 40.53           C  
ANISOU 2946  CB  SER A1795     5819   4804   4777   -454    192   -923       C  
ATOM   2947  OG  SER A1795     -27.184  25.527  56.344  1.00 41.26           O  
ANISOU 2947  OG  SER A1795     5859   5020   4798   -351    277   -845       O  
ATOM   2948  N   ASN A1796     -26.390  26.338  58.976  1.00 43.16           N  
ANISOU 2948  N   ASN A1796     6323   5431   4643   -455    260  -1132       N  
ATOM   2949  CA  ASN A1796     -26.570  25.544  60.181  1.00 43.28           C  
ANISOU 2949  CA  ASN A1796     6322   5673   4448   -453    259  -1088       C  
ATOM   2950  C   ASN A1796     -27.527  24.380  59.962  1.00 42.11           C  
ANISOU 2950  C   ASN A1796     6031   5623   4345   -364    317   -878       C  
ATOM   2951  O   ASN A1796     -27.918  23.716  60.927  1.00 42.24           O  
ANISOU 2951  O   ASN A1796     6025   5822   4203   -339    352   -812       O  
ATOM   2952  CB  ASN A1796     -27.063  26.432  61.324  1.00 44.66           C  
ANISOU 2952  CB  ASN A1796     6648   5888   4433   -404    366  -1276       C  
ATOM   2953  CG  ASN A1796     -26.104  27.564  61.633  1.00 45.33           C  
ANISOU 2953  CG  ASN A1796     6883   5873   4470   -512    299  -1505       C  
ATOM   2954  OD1 ASN A1796     -24.886  27.388  61.600  1.00 44.54           O  
ANISOU 2954  OD1 ASN A1796     6763   5795   4364   -655    140  -1510       O  
ATOM   2955  ND2 ASN A1796     -26.649  28.737  61.926  1.00 46.72           N  
ANISOU 2955  ND2 ASN A1796     7201   5928   4621   -444    421  -1696       N  
ATOM   2956  N   TYR A1797     -27.914  24.127  58.711  1.00 41.34           N  
ANISOU 2956  N   TYR A1797     5838   5411   4457   -321    328   -771       N  
ATOM   2957  CA  TYR A1797     -28.747  22.987  58.336  1.00 39.71           C  
ANISOU 2957  CA  TYR A1797     5485   5275   4328   -262    361   -578       C  
ATOM   2958  C   TYR A1797     -28.076  22.258  57.171  1.00 37.37           C  
ANISOU 2958  C   TYR A1797     5088   4911   4202   -327    245   -468       C  
ATOM   2959  O   TYR A1797     -28.622  22.127  56.076  1.00 35.93           O  
ANISOU 2959  O   TYR A1797     4832   4639   4179   -278    267   -402       O  
ATOM   2960  CB  TYR A1797     -30.161  23.439  57.981  1.00 39.75           C  
ANISOU 2960  CB  TYR A1797     5469   5225   4409   -124    511   -570       C  
ATOM   2961  CG  TYR A1797     -30.784  24.342  59.022  1.00 41.50           C  
ANISOU 2961  CG  TYR A1797     5805   5483   4480    -42    646   -706       C  
ATOM   2962  CD1 TYR A1797     -31.388  23.815  60.155  1.00 42.51           C  
ANISOU 2962  CD1 TYR A1797     5915   5798   4440     -1    726   -659       C  
ATOM   2963  CD2 TYR A1797     -30.764  25.723  58.872  1.00 42.09           C  
ANISOU 2963  CD2 TYR A1797     6010   5402   4582     -2    703   -882       C  
ATOM   2964  CE1 TYR A1797     -31.956  24.636  61.110  1.00 44.88           C  
ANISOU 2964  CE1 TYR A1797     6325   6142   4587     83    863   -795       C  
ATOM   2965  CE2 TYR A1797     -31.331  26.553  59.823  1.00 44.39           C  
ANISOU 2965  CE2 TYR A1797     6415   5711   4738     82    837  -1026       C  
ATOM   2966  CZ  TYR A1797     -31.926  26.003  60.939  1.00 46.45           C  
ANISOU 2966  CZ  TYR A1797     6658   6174   4817    127    918   -988       C  
ATOM   2967  OH  TYR A1797     -32.492  26.823  61.889  1.00 50.27           O  
ANISOU 2967  OH  TYR A1797     7261   6688   5153    219   1065  -1143       O  
ATOM   2968  N   LYS A1798     -26.859  21.772  57.429  1.00 37.25           N  
ANISOU 2968  N   LYS A1798     5064   4948   4141   -434    118   -452       N  
ATOM   2969  CA  LYS A1798     -26.009  21.259  56.361  1.00 35.80           C  
ANISOU 2969  CA  LYS A1798     4804   4690   4109   -496     13   -383       C  
ATOM   2970  C   LYS A1798     -26.552  19.972  55.753  1.00 36.16           C  
ANISOU 2970  C   LYS A1798     4714   4758   4267   -463     12   -211       C  
ATOM   2971  O   LYS A1798     -26.360  19.731  54.556  1.00 36.16           O  
ANISOU 2971  O   LYS A1798     4657   4661   4419   -469    -24   -173       O  
ATOM   2972  CB  LYS A1798     -24.590  21.038  56.886  1.00 35.88           C  
ANISOU 2972  CB  LYS A1798     4823   4767   4043   -609   -116   -399       C  
ATOM   2973  CG  LYS A1798     -23.865  22.322  57.255  1.00 36.90           C  
ANISOU 2973  CG  LYS A1798     5076   4845   4099   -676   -145   -581       C  
ATOM   2974  CD  LYS A1798     -22.377  22.084  57.441  1.00 37.93           C  
ANISOU 2974  CD  LYS A1798     5177   5028   4208   -799   -292   -580       C  
ATOM   2975  CE  LYS A1798     -21.633  23.391  57.654  1.00 40.32           C  
ANISOU 2975  CE  LYS A1798     5590   5256   4474   -888   -329   -766       C  
ATOM   2976  NZ  LYS A1798     -20.160  23.186  57.713  1.00 41.80           N  
ANISOU 2976  NZ  LYS A1798     5722   5494   4666  -1015   -479   -755       N  
ATOM   2977  N   ILE A1799     -27.225  19.138  56.548  1.00 37.35           N  
ANISOU 2977  N   ILE A1799     4814   5032   4344   -433     54   -109       N  
ATOM   2978  CA  ILE A1799     -27.729  17.868  56.027  1.00 37.48           C  
ANISOU 2978  CA  ILE A1799     4702   5056   4483   -419     50     51       C  
ATOM   2979  C   ILE A1799     -28.797  18.112  54.970  1.00 38.22           C  
ANISOU 2979  C   ILE A1799     4752   5056   4714   -351    117     52       C  
ATOM   2980  O   ILE A1799     -28.746  17.552  53.869  1.00 36.38           O  
ANISOU 2980  O   ILE A1799     4446   4749   4627   -364     70    103       O  
ATOM   2981  CB  ILE A1799     -28.260  16.988  57.172  1.00 38.11           C  
ANISOU 2981  CB  ILE A1799     4736   5285   4458   -407     92    174       C  
ATOM   2982  CG1 ILE A1799     -27.107  16.485  58.038  1.00 38.49           C  
ANISOU 2982  CG1 ILE A1799     4799   5434   4392   -477     -3    218       C  
ATOM   2983  CG2 ILE A1799     -29.061  15.816  56.620  1.00 38.03           C  
ANISOU 2983  CG2 ILE A1799     4597   5256   4598   -391    114    327       C  
ATOM   2984  CD1 ILE A1799     -27.533  15.488  59.085  1.00 39.42           C  
ANISOU 2984  CD1 ILE A1799     4863   5699   4417   -467     30    377       C  
ATOM   2985  N   ILE A1800     -29.778  18.959  55.289  1.00 41.46           N  
ANISOU 2985  N   ILE A1800     5204   5477   5074   -272    228     -7       N  
ATOM   2986  CA  ILE A1800     -30.893  19.185  54.375  1.00 42.77           C  
ANISOU 2986  CA  ILE A1800     5309   5580   5363   -196    292     15       C  
ATOM   2987  C   ILE A1800     -30.439  19.973  53.153  1.00 43.67           C  
ANISOU 2987  C   ILE A1800     5463   5553   5578   -195    248    -62       C  
ATOM   2988  O   ILE A1800     -30.871  19.699  52.026  1.00 42.09           O  
ANISOU 2988  O   ILE A1800     5186   5301   5504   -175    229    -10       O  
ATOM   2989  CB  ILE A1800     -32.050  19.883  55.112  1.00 44.03           C  
ANISOU 2989  CB  ILE A1800     5491   5794   5443    -95    434    -17       C  
ATOM   2990  CG1 ILE A1800     -32.703  18.913  56.097  1.00 44.74           C  
ANISOU 2990  CG1 ILE A1800     5503   6034   5461    -91    490    104       C  
ATOM   2991  CG2 ILE A1800     -33.084  20.405  54.130  1.00 43.54           C  
ANISOU 2991  CG2 ILE A1800     5375   5659   5510     -4    492    -10       C  
ATOM   2992  CD1 ILE A1800     -33.236  17.654  55.445  1.00 43.47           C  
ANISOU 2992  CD1 ILE A1800     5189   5881   5448   -119    455    259       C  
ATOM   2993  N   THR A1801     -29.559  20.960  53.348  1.00 46.49           N  
ANISOU 2993  N   THR A1801     5939   5849   5877   -223    230   -183       N  
ATOM   2994  CA  THR A1801     -29.030  21.692  52.202  1.00 46.84           C  
ANISOU 2994  CA  THR A1801     6019   5758   6020   -233    193   -235       C  
ATOM   2995  C   THR A1801     -28.200  20.788  51.300  1.00 46.55           C  
ANISOU 2995  C   THR A1801     5911   5705   6071   -305     86   -167       C  
ATOM   2996  O   THR A1801     -28.126  21.023  50.089  1.00 48.53           O  
ANISOU 2996  O   THR A1801     6144   5873   6420   -293     66   -160       O  
ATOM   2997  CB  THR A1801     -28.194  22.886  52.665  1.00 47.95           C  
ANISOU 2997  CB  THR A1801     6296   5828   6094   -270    193   -375       C  
ATOM   2998  OG1 THR A1801     -27.124  22.430  53.500  1.00 50.47           O  
ANISOU 2998  OG1 THR A1801     6635   6227   6316   -370    111   -394       O  
ATOM   2999  CG2 THR A1801     -29.053  23.876  53.440  1.00 47.15           C  
ANISOU 2999  CG2 THR A1801     6281   5715   5920   -183    313   -466       C  
ATOM   3000  N   MET A1802     -27.574  19.753  51.865  1.00 45.02           N  
ANISOU 3000  N   MET A1802     5676   5592   5839   -371     22   -113       N  
ATOM   3001  CA  MET A1802     -26.853  18.791  51.039  1.00 42.02           C  
ANISOU 3001  CA  MET A1802     5222   5191   5553   -423    -64    -48       C  
ATOM   3002  C   MET A1802     -27.817  17.890  50.279  1.00 39.73           C  
ANISOU 3002  C   MET A1802     4831   4902   5363   -385    -53     39       C  
ATOM   3003  O   MET A1802     -27.576  17.558  49.112  1.00 39.35           O  
ANISOU 3003  O   MET A1802     4744   4797   5410   -395    -96     51       O  
ATOM   3004  CB  MET A1802     -25.910  17.957  51.907  1.00 42.16           C  
ANISOU 3004  CB  MET A1802     5220   5287   5513   -491   -132     -3       C  
ATOM   3005  CG  MET A1802     -25.125  16.901  51.144  1.00 42.26           C  
ANISOU 3005  CG  MET A1802     5154   5272   5630   -530   -209     65       C  
ATOM   3006  SD  MET A1802     -23.849  17.593  50.075  1.00 42.59           S  
ANISOU 3006  SD  MET A1802     5225   5224   5735   -572   -260     -8       S  
ATOM   3007  CE  MET A1802     -22.711  18.251  51.291  1.00 44.21           C  
ANISOU 3007  CE  MET A1802     5492   5487   5819   -646   -310    -67       C  
ATOM   3008  N   CYS A1803     -28.915  17.487  50.924  1.00 38.92           N  
ANISOU 3008  N   CYS A1803     4682   4869   5237   -347      6     97       N  
ATOM   3009  CA  CYS A1803     -29.896  16.623  50.273  1.00 36.94           C  
ANISOU 3009  CA  CYS A1803     4324   4623   5090   -329     11    178       C  
ATOM   3010  C   CYS A1803     -30.497  17.297  49.047  1.00 35.68           C  
ANISOU 3010  C   CYS A1803     4153   4405   5000   -276     22    143       C  
ATOM   3011  O   CYS A1803     -30.587  16.692  47.973  1.00 34.97           O  
ANISOU 3011  O   CYS A1803     4002   4284   5001   -292    -31    166       O  
ATOM   3012  CB  CYS A1803     -30.997  16.240  51.263  1.00 36.57           C  
ANISOU 3012  CB  CYS A1803     4223   4670   5004   -299     87    252       C  
ATOM   3013  SG  CYS A1803     -30.531  14.981  52.465  1.00 35.78           S  
ANISOU 3013  SG  CYS A1803     4091   4651   4855   -362     66    360       S  
ATOM   3014  N   PHE A1804     -30.919  18.555  49.192  1.00 35.73           N  
ANISOU 3014  N   PHE A1804     4222   4394   4962   -208     90     87       N  
ATOM   3015  CA  PHE A1804     -31.545  19.257  48.078  1.00 35.04           C  
ANISOU 3015  CA  PHE A1804     4120   4257   4938   -142    105     78       C  
ATOM   3016  C   PHE A1804     -30.533  19.590  46.988  1.00 32.68           C  
ANISOU 3016  C   PHE A1804     3868   3875   4672   -174     40     38       C  
ATOM   3017  O   PHE A1804     -30.868  19.570  45.799  1.00 32.30           O  
ANISOU 3017  O   PHE A1804     3777   3812   4685   -150     11     62       O  
ATOM   3018  CB  PHE A1804     -32.236  20.524  48.580  1.00 38.02           C  
ANISOU 3018  CB  PHE A1804     4554   4620   5273    -47    208     36       C  
ATOM   3019  CG  PHE A1804     -33.460  20.257  49.413  1.00 40.35           C  
ANISOU 3019  CG  PHE A1804     4776   5006   5546     10    291     88       C  
ATOM   3020  CD1 PHE A1804     -34.232  19.128  49.191  1.00 40.78           C  
ANISOU 3020  CD1 PHE A1804     4694   5134   5666    -10    268    186       C  
ATOM   3021  CD2 PHE A1804     -33.838  21.132  50.418  1.00 41.91           C  
ANISOU 3021  CD2 PHE A1804     5044   5217   5665     81    400     36       C  
ATOM   3022  CE1 PHE A1804     -35.359  18.879  49.953  1.00 42.03           C  
ANISOU 3022  CE1 PHE A1804     4770   5384   5815     36    353    249       C  
ATOM   3023  CE2 PHE A1804     -34.964  20.888  51.184  1.00 43.26           C  
ANISOU 3023  CE2 PHE A1804     5140   5486   5810    141    493     91       C  
ATOM   3024  CZ  PHE A1804     -35.724  19.760  50.952  1.00 43.12           C  
ANISOU 3024  CZ  PHE A1804     4972   5550   5864    117    471    207       C  
ATOM   3025  N   SER A1805     -29.290  19.894  47.369  1.00 31.15           N  
ANISOU 3025  N   SER A1805     3757   3643   4434   -231     16    -18       N  
ATOM   3026  CA  SER A1805     -28.276  20.238  46.376  1.00 29.51           C  
ANISOU 3026  CA  SER A1805     3585   3365   4261   -265    -31    -45       C  
ATOM   3027  C   SER A1805     -27.965  19.051  45.472  1.00 28.04           C  
ANISOU 3027  C   SER A1805     3322   3200   4134   -304   -102     -2       C  
ATOM   3028  O   SER A1805     -27.906  19.188  44.245  1.00 28.32           O  
ANISOU 3028  O   SER A1805     3346   3207   4206   -288   -122      2       O  
ATOM   3029  CB  SER A1805     -27.008  20.737  47.070  1.00 29.82           C  
ANISOU 3029  CB  SER A1805     3706   3372   4250   -333    -47   -108       C  
ATOM   3030  OG  SER A1805     -27.245  21.963  47.740  1.00 31.38           O  
ANISOU 3030  OG  SER A1805     3996   3526   4401   -301     18   -175       O  
ATOM   3031  N   VAL A1806     -27.766  17.871  46.065  1.00 27.77           N  
ANISOU 3031  N   VAL A1806     3236   3210   4104   -351   -136     30       N  
ATOM   3032  CA  VAL A1806     -27.485  16.678  45.271  1.00 26.90           C  
ANISOU 3032  CA  VAL A1806     3060   3098   4062   -384   -194     57       C  
ATOM   3033  C   VAL A1806     -28.678  16.326  44.390  1.00 27.20           C  
ANISOU 3033  C   VAL A1806     3030   3152   4150   -349   -199     79       C  
ATOM   3034  O   VAL A1806     -28.518  15.966  43.218  1.00 27.07           O  
ANISOU 3034  O   VAL A1806     2993   3120   4171   -355   -241     63       O  
ATOM   3035  CB  VAL A1806     -27.094  15.505  46.189  1.00 26.31           C  
ANISOU 3035  CB  VAL A1806     2946   3053   3999   -433   -221    103       C  
ATOM   3036  CG1 VAL A1806     -26.856  14.247  45.371  1.00 25.88           C  
ANISOU 3036  CG1 VAL A1806     2830   2969   4036   -459   -271    120       C  
ATOM   3037  CG2 VAL A1806     -25.857  15.857  47.001  1.00 25.78           C  
ANISOU 3037  CG2 VAL A1806     2932   2991   3873   -471   -236     84       C  
ATOM   3038  N   SER A1807     -29.892  16.431  44.936  1.00 27.68           N  
ANISOU 3038  N   SER A1807     3051   3257   4207   -312   -157    115       N  
ATOM   3039  CA  SER A1807     -31.080  16.105  44.153  1.00 27.43           C  
ANISOU 3039  CA  SER A1807     2935   3259   4229   -287   -172    143       C  
ATOM   3040  C   SER A1807     -31.326  17.136  43.057  1.00 28.38           C  
ANISOU 3040  C   SER A1807     3080   3370   4335   -225   -172    123       C  
ATOM   3041  O   SER A1807     -31.767  16.784  41.957  1.00 29.58           O  
ANISOU 3041  O   SER A1807     3178   3546   4515   -223   -224    127       O  
ATOM   3042  CB  SER A1807     -32.298  15.989  45.069  1.00 26.64           C  
ANISOU 3042  CB  SER A1807     2767   3219   4134   -261   -117    201       C  
ATOM   3043  OG  SER A1807     -32.182  14.871  45.933  1.00 25.65           O  
ANISOU 3043  OG  SER A1807     2604   3110   4033   -322   -122    246       O  
ATOM   3044  N   LEU A1808     -31.049  18.413  43.334  1.00 27.77           N  
ANISOU 3044  N   LEU A1808     3086   3255   4211   -176   -117    104       N  
ATOM   3045  CA  LEU A1808     -31.237  19.444  42.318  1.00 29.04           C  
ANISOU 3045  CA  LEU A1808     3275   3393   4366   -110   -109    108       C  
ATOM   3046  C   LEU A1808     -30.235  19.281  41.184  1.00 31.07           C  
ANISOU 3046  C   LEU A1808     3562   3625   4618   -148   -163     86       C  
ATOM   3047  O   LEU A1808     -30.602  19.339  40.004  1.00 31.89           O  
ANISOU 3047  O   LEU A1808     3636   3761   4720   -118   -197    107       O  
ATOM   3048  CB  LEU A1808     -31.117  20.835  42.942  1.00 28.51           C  
ANISOU 3048  CB  LEU A1808     3300   3261   4272    -55    -28     89       C  
ATOM   3049  CG  LEU A1808     -31.318  22.014  41.987  1.00 29.82           C  
ANISOU 3049  CG  LEU A1808     3503   3380   4449     23     -5    115       C  
ATOM   3050  CD1 LEU A1808     -32.729  22.009  41.420  1.00 30.61           C  
ANISOU 3050  CD1 LEU A1808     3503   3551   4576    109     -8    185       C  
ATOM   3051  CD2 LEU A1808     -31.018  23.334  42.679  1.00 30.39           C  
ANISOU 3051  CD2 LEU A1808     3683   3350   4513     61     78     77       C  
ATOM   3052  N   SER A1809     -28.961  19.076  41.524  1.00 32.65           N  
ANISOU 3052  N   SER A1809     3814   3782   4808   -212   -170     49       N  
ATOM   3053  CA  SER A1809     -27.942  18.891  40.495  1.00 32.39           C  
ANISOU 3053  CA  SER A1809     3801   3734   4773   -244   -205     30       C  
ATOM   3054  C   SER A1809     -28.194  17.621  39.692  1.00 32.76           C  
ANISOU 3054  C   SER A1809     3778   3829   4841   -266   -267     21       C  
ATOM   3055  O   SER A1809     -27.922  17.575  38.487  1.00 32.89           O  
ANISOU 3055  O   SER A1809     3798   3864   4835   -258   -291      9       O  
ATOM   3056  CB  SER A1809     -26.555  18.861  41.135  1.00 31.61           C  
ANISOU 3056  CB  SER A1809     3748   3592   4672   -307   -201      0       C  
ATOM   3057  OG  SER A1809     -25.547  18.627  40.166  1.00 31.61           O  
ANISOU 3057  OG  SER A1809     3750   3583   4675   -332   -221    -11       O  
ATOM   3058  N   ALA A1810     -28.718  16.579  40.342  1.00 33.04           N  
ANISOU 3058  N   ALA A1810     3752   3885   4917   -298   -289     24       N  
ATOM   3059  CA  ALA A1810     -29.064  15.362  39.615  1.00 33.51           C  
ANISOU 3059  CA  ALA A1810     3748   3969   5015   -330   -348      2       C  
ATOM   3060  C   ALA A1810     -30.278  15.581  38.721  1.00 34.85           C  
ANISOU 3060  C   ALA A1810     3866   4204   5170   -291   -380     16       C  
ATOM   3061  O   ALA A1810     -30.351  15.030  37.616  1.00 35.63           O  
ANISOU 3061  O   ALA A1810     3944   4335   5260   -306   -436    -24       O  
ATOM   3062  CB  ALA A1810     -29.316  14.217  40.595  1.00 32.47           C  
ANISOU 3062  CB  ALA A1810     3563   3824   4950   -381   -358     19       C  
ATOM   3063  N   THR A1811     -31.238  16.390  39.178  1.00 34.75           N  
ANISOU 3063  N   THR A1811     3831   4222   5152   -237   -345     69       N  
ATOM   3064  CA  THR A1811     -32.434  16.642  38.382  1.00 35.48           C  
ANISOU 3064  CA  THR A1811     3855   4391   5237   -191   -380    101       C  
ATOM   3065  C   THR A1811     -32.126  17.504  37.165  1.00 35.82           C  
ANISOU 3065  C   THR A1811     3946   4454   5209   -137   -392    108       C  
ATOM   3066  O   THR A1811     -32.753  17.335  36.112  1.00 36.35           O  
ANISOU 3066  O   THR A1811     3962   4602   5248   -123   -457    114       O  
ATOM   3067  CB  THR A1811     -33.510  17.302  39.248  1.00 35.53           C  
ANISOU 3067  CB  THR A1811     3813   4421   5264   -130   -323    166       C  
ATOM   3068  OG1 THR A1811     -33.763  16.486  40.399  1.00 35.39           O  
ANISOU 3068  OG1 THR A1811     3750   4398   5298   -181   -302    173       O  
ATOM   3069  CG2 THR A1811     -34.805  17.469  38.468  1.00 36.16           C  
ANISOU 3069  CG2 THR A1811     3792   4596   5352    -80   -367    215       C  
ATOM   3070  N   VAL A1812     -31.162  18.420  37.284  1.00 35.12           N  
ANISOU 3070  N   VAL A1812     3954   4299   5092   -113   -333    113       N  
ATOM   3071  CA  VAL A1812     -30.790  19.266  36.152  1.00 34.86           C  
ANISOU 3071  CA  VAL A1812     3970   4278   4998    -66   -331    141       C  
ATOM   3072  C   VAL A1812     -30.263  18.414  35.004  1.00 35.03           C  
ANISOU 3072  C   VAL A1812     3988   4351   4970   -108   -392     90       C  
ATOM   3073  O   VAL A1812     -30.695  18.554  33.854  1.00 36.03           O  
ANISOU 3073  O   VAL A1812     4096   4563   5031    -73   -436    111       O  
ATOM   3074  CB  VAL A1812     -29.762  20.326  36.588  1.00 34.28           C  
ANISOU 3074  CB  VAL A1812     3996   4104   4925    -57   -253    153       C  
ATOM   3075  CG1 VAL A1812     -29.173  21.027  35.373  1.00 35.01           C  
ANISOU 3075  CG1 VAL A1812     4138   4203   4962    -27   -244    192       C  
ATOM   3076  CG2 VAL A1812     -30.408  21.334  37.522  1.00 34.02           C  
ANISOU 3076  CG2 VAL A1812     3981   4019   4927      4   -188    190       C  
ATOM   3077  N   ALA A1813     -29.323  17.513  35.301  1.00 34.27           N  
ANISOU 3077  N   ALA A1813     3911   4212   4900   -178   -394     20       N  
ATOM   3078  CA  ALA A1813     -28.767  16.658  34.258  1.00 33.98           C  
ANISOU 3078  CA  ALA A1813     3877   4211   4822   -209   -435    -47       C  
ATOM   3079  C   ALA A1813     -29.809  15.697  33.702  1.00 34.98           C  
ANISOU 3079  C   ALA A1813     3932   4413   4948   -233   -522    -92       C  
ATOM   3080  O   ALA A1813     -29.781  15.377  32.508  1.00 35.41           O  
ANISOU 3080  O   ALA A1813     3991   4539   4926   -232   -568   -140       O  
ATOM   3081  CB  ALA A1813     -27.565  15.884  34.798  1.00 32.70           C  
ANISOU 3081  CB  ALA A1813     3739   3974   4711   -265   -411   -102       C  
ATOM   3082  N   LEU A1814     -30.736  15.236  34.542  1.00 35.15           N  
ANISOU 3082  N   LEU A1814     3882   4425   5047   -260   -544    -81       N  
ATOM   3083  CA  LEU A1814     -31.757  14.303  34.082  1.00 35.44           C  
ANISOU 3083  CA  LEU A1814     3835   4525   5104   -303   -632   -123       C  
ATOM   3084  C   LEU A1814     -32.864  15.003  33.303  1.00 37.16           C  
ANISOU 3084  C   LEU A1814     3999   4864   5257   -248   -683    -68       C  
ATOM   3085  O   LEU A1814     -33.414  14.421  32.361  1.00 38.26           O  
ANISOU 3085  O   LEU A1814     4091   5090   5355   -279   -775   -120       O  
ATOM   3086  CB  LEU A1814     -32.346  13.546  35.273  1.00 34.23           C  
ANISOU 3086  CB  LEU A1814     3613   4322   5070   -357   -629   -110       C  
ATOM   3087  CG  LEU A1814     -33.377  12.464  34.950  1.00 34.37           C  
ANISOU 3087  CG  LEU A1814     3532   4381   5147   -429   -718   -153       C  
ATOM   3088  CD1 LEU A1814     -32.751  11.351  34.122  1.00 34.45           C  
ANISOU 3088  CD1 LEU A1814     3578   4354   5156   -493   -770   -279       C  
ATOM   3089  CD2 LEU A1814     -33.987  11.913  36.226  1.00 34.30           C  
ANISOU 3089  CD2 LEU A1814     3448   4325   5258   -475   -692   -100       C  
ATOM   3090  N   GLY A1815     -33.195  16.244  33.666  1.00 38.05           N  
ANISOU 3090  N   GLY A1815     4115   4983   5359   -165   -628     35       N  
ATOM   3091  CA  GLY A1815     -34.284  16.936  33.000  1.00 40.46           C  
ANISOU 3091  CA  GLY A1815     4354   5402   5618    -96   -673    113       C  
ATOM   3092  C   GLY A1815     -33.888  17.633  31.717  1.00 42.76           C  
ANISOU 3092  C   GLY A1815     4702   5761   5783    -38   -690    141       C  
ATOM   3093  O   GLY A1815     -34.707  17.756  30.801  1.00 44.20           O  
ANISOU 3093  O   GLY A1815     4822   6075   5897     -6   -771    177       O  
ATOM   3094  N   CYS A1816     -32.642  18.094  31.622  1.00 43.95           N  
ANISOU 3094  N   CYS A1816     4963   5839   5898    -27   -618    136       N  
ATOM   3095  CA  CYS A1816     -32.209  18.847  30.452  1.00 46.24           C  
ANISOU 3095  CA  CYS A1816     5310   6191   6070     31   -613    188       C  
ATOM   3096  C   CYS A1816     -31.616  17.969  29.360  1.00 48.09           C  
ANISOU 3096  C   CYS A1816     5572   6500   6199    -18   -665     88       C  
ATOM   3097  O   CYS A1816     -31.753  18.294  28.175  1.00 48.55           O  
ANISOU 3097  O   CYS A1816     5638   6680   6127     25   -704    123       O  
ATOM   3098  CB  CYS A1816     -31.184  19.909  30.858  1.00 45.62           C  
ANISOU 3098  CB  CYS A1816     5326   5995   6012     66   -499    248       C  
ATOM   3099  SG  CYS A1816     -31.770  21.077  32.103  1.00 45.65           S  
ANISOU 3099  SG  CYS A1816     5328   5892   6126    134   -420    341       S  
ATOM   3100  N   MET A1817     -30.962  16.866  29.723  1.00 49.80           N  
ANISOU 3100  N   MET A1817     5806   6649   6466    -99   -662    -34       N  
ATOM   3101  CA  MET A1817     -30.270  16.026  28.752  1.00 52.15           C  
ANISOU 3101  CA  MET A1817     6144   6993   6676   -136   -688   -147       C  
ATOM   3102  C   MET A1817     -31.090  14.830  28.291  1.00 53.45           C  
ANISOU 3102  C   MET A1817     6249   7230   6830   -200   -803   -264       C  
ATOM   3103  O   MET A1817     -31.000  14.442  27.122  1.00 56.25           O  
ANISOU 3103  O   MET A1817     6628   7689   7055   -206   -854   -343       O  
ATOM   3104  CB  MET A1817     -28.942  15.526  29.329  1.00 51.90           C  
ANISOU 3104  CB  MET A1817     6168   6836   6715   -175   -608   -212       C  
ATOM   3105  CG  MET A1817     -27.926  16.621  29.585  1.00 52.83           C  
ANISOU 3105  CG  MET A1817     6347   6894   6832   -134   -503   -120       C  
ATOM   3106  SD  MET A1817     -26.264  15.970  29.838  1.00 53.62           S  
ANISOU 3106  SD  MET A1817     6492   6901   6979   -174   -426   -196       S  
ATOM   3107  CE  MET A1817     -26.541  14.829  31.190  1.00 52.93           C  
ANISOU 3107  CE  MET A1817     6355   6706   7049   -241   -459   -262       C  
ATOM   3108  N   PHE A1818     -31.887  14.231  29.171  1.00 51.16           N  
ANISOU 3108  N   PHE A1818     5881   6889   6668   -254   -843   -281       N  
ATOM   3109  CA  PHE A1818     -32.584  12.990  28.854  1.00 50.03           C  
ANISOU 3109  CA  PHE A1818     5679   6779   6552   -341   -948   -402       C  
ATOM   3110  C   PHE A1818     -34.073  13.165  28.606  1.00 50.66           C  
ANISOU 3110  C   PHE A1818     5643   6985   6619   -346  -1054   -351       C  
ATOM   3111  O   PHE A1818     -34.626  12.490  27.735  1.00 52.89           O  
ANISOU 3111  O   PHE A1818     5888   7367   6839   -401  -1167   -446       O  
ATOM   3112  CB  PHE A1818     -32.375  11.970  29.976  1.00 48.15           C  
ANISOU 3112  CB  PHE A1818     5423   6386   6485   -418   -920   -457       C  
ATOM   3113  CG  PHE A1818     -30.937  11.599  30.190  1.00 47.48           C  
ANISOU 3113  CG  PHE A1818     5430   6186   6425   -417   -833   -513       C  
ATOM   3114  CD1 PHE A1818     -30.264  10.815  29.266  1.00 48.62           C  
ANISOU 3114  CD1 PHE A1818     5632   6331   6510   -437   -845   -651       C  
ATOM   3115  CD2 PHE A1818     -30.256  12.032  31.313  1.00 46.08           C  
ANISOU 3115  CD2 PHE A1818     5276   5907   6326   -394   -740   -432       C  
ATOM   3116  CE1 PHE A1818     -28.941  10.470  29.460  1.00 48.04           C  
ANISOU 3116  CE1 PHE A1818     5625   6156   6470   -424   -759   -692       C  
ATOM   3117  CE2 PHE A1818     -28.934  11.691  31.511  1.00 45.77           C  
ANISOU 3117  CE2 PHE A1818     5300   5777   6315   -393   -670   -472       C  
ATOM   3118  CZ  PHE A1818     -28.276  10.908  30.584  1.00 46.42           C  
ANISOU 3118  CZ  PHE A1818     5427   5858   6353   -403   -676   -594       C  
ATOM   3119  N   VAL A1819     -34.741  14.049  29.352  1.00 49.13           N  
ANISOU 3119  N   VAL A1819     5387   6794   6484   -289  -1021   -208       N  
ATOM   3120  CA  VAL A1819     -36.169  14.279  29.126  1.00 49.87           C  
ANISOU 3120  CA  VAL A1819     5351   7020   6577   -277  -1114   -139       C  
ATOM   3121  C   VAL A1819     -36.463  14.724  27.694  1.00 51.31           C  
ANISOU 3121  C   VAL A1819     5531   7384   6581   -230  -1205   -123       C  
ATOM   3122  O   VAL A1819     -37.403  14.190  27.089  1.00 52.60           O  
ANISOU 3122  O   VAL A1819     5597   7677   6712   -284  -1338   -168       O  
ATOM   3123  CB  VAL A1819     -36.721  15.256  30.180  1.00 49.00           C  
ANISOU 3123  CB  VAL A1819     5186   6872   6558   -197  -1034     13       C  
ATOM   3124  CG1 VAL A1819     -38.114  15.724  29.794  1.00 51.04           C  
ANISOU 3124  CG1 VAL A1819     5306   7285   6801   -148  -1118    113       C  
ATOM   3125  CG2 VAL A1819     -36.743  14.598  31.550  1.00 48.31           C  
ANISOU 3125  CG2 VAL A1819     5071   6655   6629   -261   -976     -8       C  
ATOM   3126  N   PRO A1820     -35.721  15.671  27.102  1.00 50.86           N  
ANISOU 3126  N   PRO A1820     5569   7353   6401   -138  -1145    -56       N  
ATOM   3127  CA  PRO A1820     -35.991  16.005  25.692  1.00 52.48           C  
ANISOU 3127  CA  PRO A1820     5774   7752   6415    -95  -1235    -33       C  
ATOM   3128  C   PRO A1820     -35.804  14.835  24.743  1.00 53.89           C  
ANISOU 3128  C   PRO A1820     5980   8011   6485   -190  -1334   -221       C  
ATOM   3129  O   PRO A1820     -36.502  14.760  23.723  1.00 54.90           O  
ANISOU 3129  O   PRO A1820     6056   8329   6473   -195  -1463   -235       O  
ATOM   3130  CB  PRO A1820     -34.988  17.131  25.403  1.00 52.00           C  
ANISOU 3130  CB  PRO A1820     5828   7659   6270      7  -1118     74       C  
ATOM   3131  CG  PRO A1820     -34.723  17.742  26.730  1.00 50.33           C  
ANISOU 3131  CG  PRO A1820     5631   7268   6223     40   -995    153       C  
ATOM   3132  CD  PRO A1820     -34.732  16.593  27.690  1.00 49.35           C  
ANISOU 3132  CD  PRO A1820     5477   7034   6240    -66   -999     27       C  
ATOM   3133  N   LYS A1821     -34.882  13.916  25.041  1.00 54.38           N  
ANISOU 3133  N   LYS A1821     6121   7936   6604   -263  -1280   -370       N  
ATOM   3134  CA  LYS A1821     -34.697  12.757  24.176  1.00 54.91           C  
ANISOU 3134  CA  LYS A1821     6225   8054   6585   -349  -1362   -572       C  
ATOM   3135  C   LYS A1821     -35.800  11.724  24.364  1.00 52.42           C  
ANISOU 3135  C   LYS A1821     5797   7749   6370   -469  -1494   -673       C  
ATOM   3136  O   LYS A1821     -36.151  11.022  23.409  1.00 53.98           O  
ANISOU 3136  O   LYS A1821     5989   8060   6462   -538  -1616   -817       O  
ATOM   3137  CB  LYS A1821     -33.326  12.121  24.422  1.00 54.27           C  
ANISOU 3137  CB  LYS A1821     6260   7811   6548   -371  -1249   -689       C  
ATOM   3138  CG  LYS A1821     -32.163  12.949  23.894  1.00 54.22           C  
ANISOU 3138  CG  LYS A1821     6362   7830   6410   -275  -1136   -625       C  
ATOM   3139  CD  LYS A1821     -30.886  12.128  23.769  1.00 54.06           C  
ANISOU 3139  CD  LYS A1821     6440   7706   6396   -298  -1051   -774       C  
ATOM   3140  CE  LYS A1821     -30.367  11.680  25.125  1.00 52.01           C  
ANISOU 3140  CE  LYS A1821     6173   7229   6360   -333   -970   -776       C  
ATOM   3141  NZ  LYS A1821     -29.080  10.935  25.009  1.00 51.85           N  
ANISOU 3141  NZ  LYS A1821     6234   7109   6357   -337   -881   -898       N  
ATOM   3142  N   VAL A1822     -36.356  11.617  25.572  1.00 49.57           N  
ANISOU 3142  N   VAL A1822     5346   7277   6211   -502  -1471   -604       N  
ATOM   3143  CA  VAL A1822     -37.476  10.707  25.786  1.00 50.06           C  
ANISOU 3143  CA  VAL A1822     5280   7354   6387   -622  -1590   -671       C  
ATOM   3144  C   VAL A1822     -38.740  11.255  25.135  1.00 51.47           C  
ANISOU 3144  C   VAL A1822     5327   7755   6476   -603  -1726   -583       C  
ATOM   3145  O   VAL A1822     -39.575  10.487  24.638  1.00 52.43           O  
ANISOU 3145  O   VAL A1822     5357   7969   6594   -712  -1875   -685       O  
ATOM   3146  CB  VAL A1822     -37.671  10.451  27.292  1.00 48.48           C  
ANISOU 3146  CB  VAL A1822     5018   6983   6419   -656  -1509   -601       C  
ATOM   3147  CG1 VAL A1822     -38.874   9.554  27.537  1.00 51.23           C  
ANISOU 3147  CG1 VAL A1822     5216   7347   6900   -785  -1622   -643       C  
ATOM   3148  CG2 VAL A1822     -36.419   9.829  27.886  1.00 47.36           C  
ANISOU 3148  CG2 VAL A1822     4997   6638   6360   -676  -1394   -682       C  
ATOM   3149  N   TYR A1823     -38.897  12.581  25.108  1.00 50.73           N  
ANISOU 3149  N   TYR A1823     5216   7748   6313   -465  -1681   -394       N  
ATOM   3150  CA  TYR A1823     -40.080  13.178  24.497  1.00 52.24           C  
ANISOU 3150  CA  TYR A1823     5271   8156   6423   -422  -1805   -281       C  
ATOM   3151  C   TYR A1823     -40.152  12.870  23.006  1.00 54.56           C  
ANISOU 3151  C   TYR A1823     5590   8651   6490   -456  -1952   -390       C  
ATOM   3152  O   TYR A1823     -41.226  12.555  22.481  1.00 54.45           O  
ANISOU 3152  O   TYR A1823     5442   8806   6439   -520  -2120   -411       O  
ATOM   3153  CB  TYR A1823     -40.085  14.688  24.736  1.00 49.93           C  
ANISOU 3153  CB  TYR A1823     4980   7885   6107   -251  -1706    -54       C  
ATOM   3154  CG  TYR A1823     -41.210  15.421  24.039  1.00 49.68           C  
ANISOU 3154  CG  TYR A1823     4813   8080   5985   -174  -1823     92       C  
ATOM   3155  CD1 TYR A1823     -42.504  15.389  24.544  1.00 49.49           C  
ANISOU 3155  CD1 TYR A1823     4593   8118   6091   -188  -1890    174       C  
ATOM   3156  CD2 TYR A1823     -40.977  16.153  22.882  1.00 49.29           C  
ANISOU 3156  CD2 TYR A1823     4821   8189   5720    -80  -1861    165       C  
ATOM   3157  CE1 TYR A1823     -43.534  16.059  23.913  1.00 50.82           C  
ANISOU 3157  CE1 TYR A1823     4621   8503   6187   -108  -2000    322       C  
ATOM   3158  CE2 TYR A1823     -42.000  16.826  22.244  1.00 50.65           C  
ANISOU 3158  CE2 TYR A1823     4862   8577   5808      1  -1974    320       C  
ATOM   3159  CZ  TYR A1823     -43.277  16.776  22.763  1.00 51.78           C  
ANISOU 3159  CZ  TYR A1823     4805   8779   6092    -11  -2046    397       C  
ATOM   3160  OH  TYR A1823     -44.299  17.445  22.132  1.00 54.16           O  
ANISOU 3160  OH  TYR A1823     4958   9303   6318     79  -2162    564       O  
ATOM   3161  N   ILE A1824     -39.017  12.951  22.307  1.00 56.22           N  
ANISOU 3161  N   ILE A1824     5965   8856   6539   -417  -1893   -462       N  
ATOM   3162  CA  ILE A1824     -39.012  12.679  20.873  1.00 60.01           C  
ANISOU 3162  CA  ILE A1824     6487   9542   6772   -440  -2018   -573       C  
ATOM   3163  C   ILE A1824     -39.325  11.213  20.596  1.00 61.81           C  
ANISOU 3163  C   ILE A1824     6695   9760   7028   -614  -2145   -827       C  
ATOM   3164  O   ILE A1824     -39.967  10.889  19.590  1.00 64.92           O  
ANISOU 3164  O   ILE A1824     7043  10361   7263   -673  -2317   -917       O  
ATOM   3165  CB  ILE A1824     -37.663  13.103  20.262  1.00 60.44           C  
ANISOU 3165  CB  ILE A1824     6722   9585   6656   -353  -1895   -583       C  
ATOM   3166  CG1 ILE A1824     -37.444  14.605  20.457  1.00 60.64           C  
ANISOU 3166  CG1 ILE A1824     6758   9619   6662   -193  -1783   -322       C  
ATOM   3167  CG2 ILE A1824     -37.601  12.752  18.784  1.00 63.28           C  
ANISOU 3167  CG2 ILE A1824     7140  10167   6737   -375  -2010   -714       C  
ATOM   3168  CD1 ILE A1824     -36.177  15.126  19.819  1.00 60.89           C  
ANISOU 3168  CD1 ILE A1824     6947   9656   6532   -111  -1662   -297       C  
ATOM   3169  N   ILE A1825     -38.903  10.309  21.481  1.00 58.34           N  
ANISOU 3169  N   ILE A1825     6290   9084   6793   -703  -2069   -945       N  
ATOM   3170  CA  ILE A1825     -39.152   8.886  21.265  1.00 56.68           C  
ANISOU 3170  CA  ILE A1825     6072   8821   6643   -872  -2175  -1190       C  
ATOM   3171  C   ILE A1825     -40.642   8.581  21.350  1.00 57.25           C  
ANISOU 3171  C   ILE A1825     5948   8999   6805   -980  -2348  -1169       C  
ATOM   3172  O   ILE A1825     -41.229   8.006  20.425  1.00 60.80           O  
ANISOU 3172  O   ILE A1825     6411   9524   7166  -1063  -2476  -1262       O  
ATOM   3173  CB  ILE A1825     -38.352   8.041  22.272  1.00 53.25           C  
ANISOU 3173  CB  ILE A1825     5712   8092   6429   -926  -2042  -1280       C  
ATOM   3174  CG1 ILE A1825     -36.854   8.194  22.025  1.00 51.88           C  
ANISOU 3174  CG1 ILE A1825     5721   7833   6156   -833  -1891  -1329       C  
ATOM   3175  CG2 ILE A1825     -38.765   6.579  22.188  1.00 53.91           C  
ANISOU 3175  CG2 ILE A1825     5769   8085   6628  -1107  -2149  -1508       C  
ATOM   3176  CD1 ILE A1825     -36.003   7.396  22.977  1.00 51.11           C  
ANISOU 3176  CD1 ILE A1825     5690   7462   6267   -869  -1763  -1401       C  
ATOM   3177  N   LEU A1826     -41.277   8.961  22.460  1.00 54.39           N  
ANISOU 3177  N   LEU A1826     5452   8572   6643   -962  -2302   -992       N  
ATOM   3178  CA  LEU A1826     -42.659   8.561  22.696  1.00 55.71           C  
ANISOU 3178  CA  LEU A1826     5449   8765   6953  -1062  -2416   -938       C  
ATOM   3179  C   LEU A1826     -43.650   9.461  21.967  1.00 58.17           C  
ANISOU 3179  C   LEU A1826     5650   9318   7135   -975  -2531   -788       C  
ATOM   3180  O   LEU A1826     -44.628   8.969  21.394  1.00 60.68           O  
ANISOU 3180  O   LEU A1826     5895   9697   7463  -1056  -2677   -828       O  
ATOM   3181  CB  LEU A1826     -42.953   8.557  24.197  1.00 52.98           C  
ANISOU 3181  CB  LEU A1826     4987   8274   6868  -1076  -2315   -822       C  
ATOM   3182  CG  LEU A1826     -42.115   7.612  25.061  1.00 51.15           C  
ANISOU 3182  CG  LEU A1826     4853   7773   6808  -1154  -2195   -935       C  
ATOM   3183  CD1 LEU A1826     -42.592   7.647  26.504  1.00 40.71           C  
ANISOU 3183  CD1 LEU A1826     3414   6330   5724  -1160  -2097   -784       C  
ATOM   3184  CD2 LEU A1826     -42.156   6.194  24.512  1.00 52.93           C  
ANISOU 3184  CD2 LEU A1826     5163   7904   7045  -1325  -2250  -1120       C  
ATOM   3185  N   ALA A1827     -43.419  10.773  21.972  1.00 58.43           N  
ANISOU 3185  N   ALA A1827     5668   9477   7055   -807  -2467   -606       N  
ATOM   3186  CA  ALA A1827     -44.403  11.708  21.439  1.00 61.70           C  
ANISOU 3186  CA  ALA A1827     5968  10089   7386   -699  -2547   -421       C  
ATOM   3187  C   ALA A1827     -44.237  11.980  19.951  1.00 65.35           C  
ANISOU 3187  C   ALA A1827     6524  10743   7564   -654  -2646   -456       C  
ATOM   3188  O   ALA A1827     -45.223  12.305  19.280  1.00 67.05           O  
ANISOU 3188  O   ALA A1827     6646  11116   7714   -622  -2765   -371       O  
ATOM   3189  CB  ALA A1827     -44.345  13.032  22.206  1.00 59.76           C  
ANISOU 3189  CB  ALA A1827     5662   9860   7185   -530  -2421   -170       C  
ATOM   3190  N   LYS A1828     -43.022  11.858  19.413  1.00 67.63           N  
ANISOU 3190  N   LYS A1828     6991  11029   7677   -645  -2594   -577       N  
ATOM   3191  CA  LYS A1828     -42.749  12.129  18.002  1.00 72.12           C  
ANISOU 3191  CA  LYS A1828     7666  11785   7953   -594  -2661   -606       C  
ATOM   3192  C   LYS A1828     -42.122  10.899  17.351  1.00 76.05           C  
ANISOU 3192  C   LYS A1828     8314  12220   8361   -725  -2694   -895       C  
ATOM   3193  O   LYS A1828     -40.928  10.898  17.019  1.00 74.31           O  
ANISOU 3193  O   LYS A1828     8249  11988   7999   -686  -2599   -988       O  
ATOM   3194  CB  LYS A1828     -41.841  13.348  17.845  1.00 70.48           C  
ANISOU 3194  CB  LYS A1828     7537  11658   7584   -420  -2542   -440       C  
ATOM   3195  CG  LYS A1828     -42.421  14.626  18.430  1.00 69.01           C  
ANISOU 3195  CG  LYS A1828     7223  11509   7489   -273  -2494   -142       C  
ATOM   3196  CD  LYS A1828     -43.777  14.945  17.818  1.00 71.18           C  
ANISOU 3196  CD  LYS A1828     7368  11937   7739   -244  -2632    -24       C  
ATOM   3197  CE  LYS A1828     -44.403  16.174  18.458  1.00 70.11           C  
ANISOU 3197  CE  LYS A1828     7106  11806   7726    -86  -2565    261       C  
ATOM   3198  NZ  LYS A1828     -45.727  16.494  17.855  1.00 72.51           N  
ANISOU 3198  NZ  LYS A1828     7275  12263   8013    -48  -2693    374       N  
ATOM   3199  N   PRO A1829     -42.905   9.838  17.137  1.00 82.14           N  
ANISOU 3199  N   PRO A1829     9046  12945   9219   -878  -2823  -1041       N  
ATOM   3200  CA  PRO A1829     -42.327   8.623  16.543  1.00 84.37           C  
ANISOU 3200  CA  PRO A1829     9484  13138   9436  -1002  -2843  -1317       C  
ATOM   3201  C   PRO A1829     -41.943   8.791  15.084  1.00 86.80           C  
ANISOU 3201  C   PRO A1829     9923  13644   9414   -952  -2893  -1393       C  
ATOM   3202  O   PRO A1829     -41.028   8.102  14.615  1.00 87.42           O  
ANISOU 3202  O   PRO A1829    10167  13657   9390   -989  -2836  -1601       O  
ATOM   3203  CB  PRO A1829     -43.441   7.578  16.713  1.00 87.37           C  
ANISOU 3203  CB  PRO A1829     9766  13427  10004  -1176  -2981  -1404       C  
ATOM   3204  CG  PRO A1829     -44.426   8.189  17.679  1.00 87.06           C  
ANISOU 3204  CG  PRO A1829     9515  13390  10175  -1139  -2992  -1182       C  
ATOM   3205  CD  PRO A1829     -44.330   9.661  17.458  1.00 85.54           C  
ANISOU 3205  CD  PRO A1829     9289  13387   9824   -944  -2947   -962       C  
ATOM   3206  N   GLU A1830     -42.612   9.682  14.349  1.00 89.20           N  
ANISOU 3206  N   GLU A1830    10157  14184   9549   -863  -2988  -1225       N  
ATOM   3207  CA  GLU A1830     -42.291   9.865  12.938  1.00 93.08           C  
ANISOU 3207  CA  GLU A1830    10771  14880   9714   -814  -3035  -1277       C  
ATOM   3208  C   GLU A1830     -41.069  10.748  12.734  1.00 95.19           C  
ANISOU 3208  C   GLU A1830    11156  15211   9800   -658  -2870  -1184       C  
ATOM   3209  O   GLU A1830     -40.334  10.560  11.758  1.00 96.92           O  
ANISOU 3209  O   GLU A1830    11529  15519   9777   -638  -2840  -1304       O  
ATOM   3210  CB  GLU A1830     -43.491  10.451  12.192  1.00 93.91           C  
ANISOU 3210  CB  GLU A1830    10756  15214   9711   -778  -3203  -1123       C  
ATOM   3211  CG  GLU A1830     -44.613   9.455  11.958  1.00 95.98           C  
ANISOU 3211  CG  GLU A1830    10937  15465  10068   -944  -3396  -1264       C  
ATOM   3212  CD  GLU A1830     -44.163   8.246  11.160  1.00 97.86           C  
ANISOU 3212  CD  GLU A1830    11343  15659  10180  -1076  -3445  -1567       C  
ATOM   3213  OE1 GLU A1830     -43.254   8.386  10.313  1.00 98.44           O  
ANISOU 3213  OE1 GLU A1830    11581  15829   9992  -1010  -3378  -1640       O  
ATOM   3214  OE2 GLU A1830     -44.716   7.150  11.385  1.00 99.13           O  
ANISOU 3214  OE2 GLU A1830    11473  15683  10509  -1244  -3542  -1729       O  
ATOM   3215  N   ARG A1831     -40.839  11.713  13.628  1.00 95.68           N  
ANISOU 3215  N   ARG A1831    11149  15231   9974   -546  -2758   -969       N  
ATOM   3216  CA  ARG A1831     -39.625  12.518  13.545  1.00 97.25           C  
ANISOU 3216  CA  ARG A1831    11457  15464  10030   -410  -2596   -876       C  
ATOM   3217  C   ARG A1831     -38.379  11.661  13.710  1.00 99.42           C  
ANISOU 3217  C   ARG A1831    11881  15585  10308   -464  -2477  -1120       C  
ATOM   3218  O   ARG A1831     -37.350  11.930  13.080  1.00 98.56           O  
ANISOU 3218  O   ARG A1831    11907  15552   9991   -385  -2374  -1141       O  
ATOM   3219  CB  ARG A1831     -39.649  13.618  14.604  1.00 93.39           C  
ANISOU 3219  CB  ARG A1831    10865  14920   9700   -297  -2504   -613       C  
ATOM   3220  CG  ARG A1831     -40.705  14.686  14.383  1.00 93.66           C  
ANISOU 3220  CG  ARG A1831    10769  15100   9719   -193  -2578   -336       C  
ATOM   3221  CD  ARG A1831     -40.071  15.990  13.927  1.00 91.90           C  
ANISOU 3221  CD  ARG A1831    10612  14986   9321    -15  -2472    -96       C  
ATOM   3222  NE  ARG A1831     -40.856  17.149  14.341  1.00 91.10           N  
ANISOU 3222  NE  ARG A1831    10379  14902   9333    110  -2467    202       N  
ATOM   3223  CZ  ARG A1831     -40.754  17.730  15.533  1.00 88.44           C  
ANISOU 3223  CZ  ARG A1831     9980  14414   9209    173  -2362    341       C  
ATOM   3224  NH1 ARG A1831     -39.901  17.257  16.432  1.00 85.57           N  
ANISOU 3224  NH1 ARG A1831     9703  13797   9011    114  -2222    209       N  
ATOM   3225  NH2 ARG A1831     -41.507  18.781  15.828  1.00 88.56           N  
ANISOU 3225  NH2 ARG A1831     9887  14434   9328    298  -2348    601       N  
ATOM   3226  N   ASN A1832     -38.454  10.629  14.543  1.00103.01           N  
ANISOU 3226  N   ASN A1832    12314  15820  11006   -592  -2478  -1295       N  
ATOM   3227  CA  ASN A1832     -37.323   9.746  14.782  1.00104.01           C  
ANISOU 3227  CA  ASN A1832    12573  15763  11182   -640  -2360  -1526       C  
ATOM   3228  C   ASN A1832     -37.292   8.597  13.779  1.00107.82           C  
ANISOU 3228  C   ASN A1832    13175  16244  11548   -738  -2423  -1789       C  
ATOM   3229  O   ASN A1832     -36.402   8.525  12.930  1.00109.01           O  
ANISOU 3229  O   ASN A1832    13471  16469  11479   -684  -2348  -1893       O  
ATOM   3230  CB  ASN A1832     -37.372   9.200  16.209  1.00102.33           C  
ANISOU 3230  CB  ASN A1832    12285  15288  11309   -719  -2314  -1564       C  
ATOM   3231  CG  ASN A1832     -36.342   8.121  16.451  1.00101.87           C  
ANISOU 3231  CG  ASN A1832    12355  15007  11345   -777  -2206  -1808       C  
ATOM   3232  OD1 ASN A1832     -36.673   7.015  16.878  1.00102.53           O  
ANISOU 3232  OD1 ASN A1832    12430  14893  11633   -906  -2236  -1945       O  
ATOM   3233  ND2 ASN A1832     -35.085   8.430  16.163  1.00100.63           N  
ANISOU 3233  ND2 ASN A1832    12338  14820  11076   -670  -2040  -1804       N  
TER    3234      ASN A1832                                                      
HETATM 3235  C1  OLA A4001     -14.410  25.965  54.016  1.00 57.40           C  
ANISOU 3235  C1  OLA A4001     7501   6988   7320  -1564   -791   -881       C  
HETATM 3236  O1  OLA A4001     -14.927  26.824  54.764  1.00 58.65           O  
ANISOU 3236  O1  OLA A4001     7801   7100   7384  -1583   -765  -1034       O  
HETATM 3237  O2  OLA A4001     -13.713  25.023  54.448  1.00 57.48           O  
ANISOU 3237  O2  OLA A4001     7395   7165   7279  -1593   -893   -794       O  
HETATM 3238  C2  OLA A4001     -14.638  26.073  52.526  1.00 55.49           C  
ANISOU 3238  C2  OLA A4001     7231   6599   7255  -1497   -694   -796       C  
HETATM 3239  C3  OLA A4001     -13.294  26.212  51.819  1.00 55.44           C  
ANISOU 3239  C3  OLA A4001     7114   6571   7381  -1608   -751   -745       C  
HETATM 3240  C4  OLA A4001     -13.462  26.638  50.364  1.00 54.51           C  
ANISOU 3240  C4  OLA A4001     6995   6296   7420  -1560   -645   -684       C  
HETATM 3241  C5  OLA A4001     -13.885  25.466  49.486  1.00 52.69           C  
ANISOU 3241  C5  OLA A4001     6679   6119   7223  -1424   -597   -539       C  
HETATM 3242  C6  OLA A4001     -13.956  25.855  48.012  1.00 52.15           C  
ANISOU 3242  C6  OLA A4001     6603   5927   7284  -1382   -503   -474       C  
HETATM 3243  C7  OLA A4001     -13.984  24.592  47.160  1.00 51.10           C  
ANISOU 3243  C7  OLA A4001     6362   5874   7181  -1283   -485   -347       C  
HETATM 3244  C8  OLA A4001     -14.439  24.830  45.725  1.00 50.65           C  
ANISOU 3244  C8  OLA A4001     6319   5725   7200  -1204   -385   -286       C  
HETATM 3245  C9  OLA A4001     -14.717  23.467  45.137  1.00 49.71           C  
ANISOU 3245  C9  OLA A4001     6119   5693   7075  -1099   -376   -201       C  
HETATM 3246  C10 OLA A4001     -15.697  23.236  44.266  1.00 49.06           C  
ANISOU 3246  C10 OLA A4001     6066   5582   6994   -991   -310   -167       C  
HETATM 3247  C11 OLA A4001     -16.610  24.319  43.741  1.00 49.31           C  
ANISOU 3247  C11 OLA A4001     6201   5500   7034   -946   -235   -185       C  
HETATM 3248  C12 OLA A4001     -17.179  23.806  42.423  1.00 48.71           C  
ANISOU 3248  C12 OLA A4001     6098   5439   6969   -844   -184   -112       C  
HETATM 3249  C13 OLA A4001     -17.377  24.901  41.383  1.00 49.52           C  
ANISOU 3249  C13 OLA A4001     6256   5446   7113   -821   -110    -73       C  
HETATM 3250  C14 OLA A4001     -17.540  24.261  40.009  1.00 49.47           C  
ANISOU 3250  C14 OLA A4001     6201   5496   7099   -743    -78      1       C  
HETATM 3251  C15 OLA A4001     -17.993  25.264  38.955  1.00 51.10           C  
ANISOU 3251  C15 OLA A4001     6464   5632   7320   -694     -6     63       C  
HETATM 3252  C16 OLA A4001     -16.966  26.374  38.765  1.00 53.18           C  
ANISOU 3252  C16 OLA A4001     6745   5805   7658   -786     33     95       C  
HETATM 3253  C17 OLA A4001     -17.169  27.080  37.428  1.00 54.10           C  
ANISOU 3253  C17 OLA A4001     6889   5883   7785   -732    110    199       C  
HETATM 3254  C18 OLA A4001     -16.050  28.062  37.155  1.00 55.28           C  
ANISOU 3254  C18 OLA A4001     7036   5945   8021   -834    157    252       C  
HETATM 3255  C1  OLA A4002     -42.550   5.546  55.666  1.00 79.48           C  
ANISOU 3255  C1  OLA A4002     8057  10640  11504   -784    702   1951       C  
HETATM 3256  O1  OLA A4002     -43.498   4.732  55.712  1.00 81.05           O  
ANISOU 3256  O1  OLA A4002     8112  10831  11852   -862    728   2068       O  
HETATM 3257  O2  OLA A4002     -41.846   5.826  56.660  1.00 79.47           O  
ANISOU 3257  O2  OLA A4002     8176  10707  11313   -718    764   1982       O  
HETATM 3258  C2  OLA A4002     -42.241   6.220  54.350  1.00 77.61           C  
ANISOU 3258  C2  OLA A4002     7878  10322  11287   -757    576   1739       C  
HETATM 3259  C3  OLA A4002     -42.258   7.733  54.537  1.00 76.57           C  
ANISOU 3259  C3  OLA A4002     7829  10304  10958   -604    642   1627       C  
HETATM 3260  C4  OLA A4002     -42.053   8.465  53.216  1.00 74.48           C  
ANISOU 3260  C4  OLA A4002     7611   9970  10718   -571    529   1444       C  
HETATM 3261  C5  OLA A4002     -43.146   8.115  52.213  1.00 74.62           C  
ANISOU 3261  C5  OLA A4002     7449   9978  10924   -634    470   1456       C  
HETATM 3262  C6  OLA A4002     -43.018   8.965  50.954  1.00 72.90           C  
ANISOU 3262  C6  OLA A4002     7276   9728  10696   -580    369   1293       C  
HETATM 3263  C7  OLA A4002     -43.663   8.273  49.759  1.00 72.85           C  
ANISOU 3263  C7  OLA A4002     7131   9676  10875   -688    244   1276       C  
HETATM 3264  C8  OLA A4002     -43.438   9.066  48.478  1.00 71.31           C  
ANISOU 3264  C8  OLA A4002     6990   9458  10645   -635    136   1125       C  
HETATM 3265  C9  OLA A4002     -42.757   8.180  47.463  1.00 70.54           C  
ANISOU 3265  C9  OLA A4002     6940   9228  10636   -751    -16   1032       C  
HETATM 3266  C10 OLA A4002     -43.272   8.005  46.248  1.00 70.98           C  
ANISOU 3266  C10 OLA A4002     6910   9284  10777   -805   -136    967       C  
HETATM 3267  C11 OLA A4002     -44.552   8.693  45.832  1.00 71.84           C  
ANISOU 3267  C11 OLA A4002     6857   9533  10906   -751   -135   1002       C  
HETATM 3268  C12 OLA A4002     -44.529   8.923  44.325  1.00 71.26           C  
ANISOU 3268  C12 OLA A4002     6788   9459  10829   -761   -288    879       C  
HETATM 3269  C13 OLA A4002     -45.792   9.635  43.853  1.00 72.39           C  
ANISOU 3269  C13 OLA A4002     6759   9755  10990   -697   -303    929       C  
HETATM 3270  C1  OLA A4003     -10.846   3.364  57.769  1.00 71.34           C  
ANISOU 3270  C1  OLA A4003     7524   9641   9943   -312  -1219   2143       C  
HETATM 3271  O1  OLA A4003     -12.015   3.353  58.211  1.00 71.14           O  
ANISOU 3271  O1  OLA A4003     7599   9610   9822   -339  -1167   2145       O  
HETATM 3272  O2  OLA A4003      -9.850   3.608  58.484  1.00 72.95           O  
ANISOU 3272  O2  OLA A4003     7637  10035  10045   -325  -1340   2228       O  
HETATM 3273  C2  OLA A4003     -10.626   3.066  56.305  1.00 69.52           C  
ANISOU 3273  C2  OLA A4003     7272   9190   9951   -262  -1132   2032       C  
HETATM 3274  C3  OLA A4003     -11.252   1.718  55.969  1.00 69.25           C  
ANISOU 3274  C3  OLA A4003     7244   8945  10124   -172  -1038   2140       C  
HETATM 3275  C4  OLA A4003     -10.493   1.019  54.847  1.00 69.08           C  
ANISOU 3275  C4  OLA A4003     7144   8746  10357    -78   -986   2121       C  
HETATM 3276  C5  OLA A4003     -10.445   1.866  53.580  1.00 67.50           C  
ANISOU 3276  C5  OLA A4003     6992   8481  10173   -119   -933   1869       C  
HETATM 3277  C6  OLA A4003     -11.318   1.273  52.478  1.00 66.77           C  
ANISOU 3277  C6  OLA A4003     6980   8151  10240    -90   -815   1756       C  
HETATM 3278  C7  OLA A4003     -12.801   1.458  52.779  1.00 66.19           C  
ANISOU 3278  C7  OLA A4003     7025   8055  10068   -164   -783   1712       C  
HETATM 3279  C8  OLA A4003     -13.664   0.700  51.777  1.00 65.82           C  
ANISOU 3279  C8  OLA A4003     7037   7777  10194   -141   -685   1624       C  
HETATM 3280  C9  OLA A4003     -14.444   1.681  50.935  1.00 64.36           C  
ANISOU 3280  C9  OLA A4003     6949   7586   9917   -215   -648   1401       C  
HETATM 3281  C10 OLA A4003     -14.185   1.799  49.636  1.00 64.03           C  
ANISOU 3281  C10 OLA A4003     6922   7448   9957   -194   -600   1241       C  
HETATM 3282  C11 OLA A4003     -13.107   0.954  48.999  1.00 65.36           C  
ANISOU 3282  C11 OLA A4003     7012   7510  10311    -92   -570   1265       C  
HETATM 3283  C12 OLA A4003     -13.612   0.382  47.679  1.00 65.21           C  
ANISOU 3283  C12 OLA A4003     7051   7296  10428    -66   -485   1110       C  
HETATM 3284  C1  OLA A4004     -35.505   7.217  57.298  1.00 77.75           C  
ANISOU 3284  C1  OLA A4004     8701  10344  10498   -576    426   1574       C  
HETATM 3285  O1  OLA A4004     -34.757   8.064  57.831  1.00 77.57           O  
ANISOU 3285  O1  OLA A4004     8795  10399  10278   -522    421   1490       O  
HETATM 3286  O2  OLA A4004     -36.380   6.587  57.930  1.00 79.22           O  
ANISOU 3286  O2  OLA A4004     8786  10592  10722   -600    516   1741       O  
HETATM 3287  C2  OLA A4004     -35.343   6.947  55.822  1.00 76.43           C  
ANISOU 3287  C2  OLA A4004     8509  10004  10527   -622    318   1465       C  
HETATM 3288  C3  OLA A4004     -36.553   6.163  55.334  1.00 77.25           C  
ANISOU 3288  C3  OLA A4004     8462  10057  10833   -686    343   1548       C  
HETATM 3289  C4  OLA A4004     -36.875   6.506  53.886  1.00 76.17           C  
ANISOU 3289  C4  OLA A4004     8299   9830  10811   -698    268   1392       C  
HETATM 3290  C5  OLA A4004     -38.267   6.002  53.531  1.00 77.29           C  
ANISOU 3290  C5  OLA A4004     8278   9975  11116   -756    299   1464       C  
HETATM 3291  C6  OLA A4004     -38.481   6.017  52.024  1.00 76.73           C  
ANISOU 3291  C6  OLA A4004     8174   9806  11175   -793    192   1324       C  
HETATM 3292  C7  OLA A4004     -39.878   5.525  51.667  1.00 78.43           C  
ANISOU 3292  C7  OLA A4004     8210  10037  11551   -864    205   1391       C  
HETATM 3293  C8  OLA A4004     -40.079   5.523  50.157  1.00 78.03           C  
ANISOU 3293  C8  OLA A4004     8129   9910  11608   -906     82   1246       C  
HETATM 3294  C9  OLA A4004     -39.336   4.365  49.534  1.00 77.95           C  
ANISOU 3294  C9  OLA A4004     8158   9723  11738  -1005    -20   1204       C  
HETATM 3295  C10 OLA A4004     -39.821   3.768  48.448  1.00 78.57           C  
ANISOU 3295  C10 OLA A4004     8190   9725  11939  -1079   -114   1114       C  
HETATM 3296  C11 OLA A4004     -41.112   4.248  47.825  1.00 79.32           C  
ANISOU 3296  C11 OLA A4004     8165   9925  12049  -1081   -134   1080       C  
HETATM 3297  O1  MES A4005     -32.797  19.753  63.285  1.00 75.73           O  
ANISOU 3297  O1  MES A4005     9815  10737   8222     -5    847    -59       O  
HETATM 3298  C2  MES A4005     -31.967  18.595  63.228  1.00 75.00           C  
ANISOU 3298  C2  MES A4005     9650  10684   8161   -108    704     94       C  
HETATM 3299  C3  MES A4005     -30.507  18.938  63.505  1.00 74.95           C  
ANISOU 3299  C3  MES A4005     9753  10681   8044   -204    552    -22       C  
HETATM 3300  N4  MES A4005     -30.140  20.078  62.676  1.00 73.76           N  
ANISOU 3300  N4  MES A4005     9686  10344   7997   -209    520   -216       N  
HETATM 3301  C5  MES A4005     -31.009  21.246  62.622  1.00 74.64           C  
ANISOU 3301  C5  MES A4005     9875  10379   8105   -108    663   -369       C  
HETATM 3302  C6  MES A4005     -32.413  20.738  62.330  1.00 74.49           C  
ANISOU 3302  C6  MES A4005     9726  10381   8196     -7    798   -221       C  
HETATM 3303  C7  MES A4005     -28.724  20.303  62.431  1.00 72.79           C  
ANISOU 3303  C7  MES A4005     9616  10161   7880   -319    355   -299       C  
HETATM 3304  C8  MES A4005     -28.293  19.206  61.467  1.00 70.30           C  
ANISOU 3304  C8  MES A4005     9164   9779   7769   -369    251   -128       C  
HETATM 3305  S   MES A4005     -27.034  19.753  60.532  1.00 68.70           S  
ANISOU 3305  S   MES A4005     8995   9420   7687   -455    114   -236       S  
HETATM 3306  O1S MES A4005     -27.539  20.017  59.167  1.00 67.54           O  
ANISOU 3306  O1S MES A4005     8806   9094   7762   -411    153   -242       O  
HETATM 3307  O2S MES A4005     -25.982  18.714  60.461  1.00 68.32           O  
ANISOU 3307  O2S MES A4005     8864   9420   7675   -535    -25   -107       O  
HETATM 3308  O3S MES A4005     -26.476  20.999  61.103  1.00 69.71           O  
ANISOU 3308  O3S MES A4005     9271   9542   7674   -492     98   -449       O  
HETATM 3309  C13 D7W A4006     -24.730  14.989  40.542  1.00 52.04           C  
HETATM 3310  C15 D7W A4006     -26.068  13.231  39.465  1.00 53.07           C  
HETATM 3311  C17 D7W A4006     -25.329  13.015  41.805  1.00 52.04           C  
HETATM 3312  C01 D7W A4006     -21.801  18.265  47.081  1.00 46.98           C  
HETATM 3313  C03 D7W A4006     -22.977  20.307  46.033  1.00 47.00           C  
HETATM 3314  C04 D7W A4006     -23.881  20.515  44.816  1.00 47.33           C  
HETATM 3315  C07 D7W A4006     -23.338  18.247  44.898  1.00 47.60           C  
HETATM 3316  C09 D7W A4006     -23.967  16.210  43.378  1.00 50.47           C  
HETATM 3317  C12 D7W A4006     -24.672  14.271  41.769  1.00 51.65           C  
HETATM 3318  C14 D7W A4006     -25.418  14.466  39.434  1.00 53.04           C  
HETATM 3319  C16 D7W A4006     -26.013  12.512  40.675  1.00 52.79           C  
HETATM 3320  N02 D7W A4006     -22.661  18.849  46.038  1.00 47.00           N  
HETATM 3321  N06 D7W A4006     -24.035  19.205  44.198  1.00 47.22           N  
HETATM 3322  N08 D7W A4006     -23.273  16.819  44.549  1.00 48.87           N  
HETATM 3323  N11 D7W A4006     -23.944  14.806  42.973  1.00 51.31           N  
HETATM 3324  O05 D7W A4006     -24.358  21.582  44.465  1.00 47.63           O  
HETATM 3325  O10 D7W A4006     -24.624  16.967  42.688  1.00 51.14           O  
HETATM 3326 CL1  D7W A4006     -25.470  15.418  37.894  1.00 54.39          CL  
HETATM 3327  C1  OLA A4007     -18.844  30.888  53.892  1.00 66.09           C  
HETATM 3328  O1  OLA A4007     -18.040  30.580  54.799  1.00 66.53           O  
HETATM 3329  O2  OLA A4007     -19.991  31.332  54.117  1.00 66.50           O  
HETATM 3330  C2  OLA A4007     -18.416  30.716  52.456  1.00 64.83           C  
HETATM 3331  C3  OLA A4007     -16.959  30.279  52.368  1.00 63.65           C  
HETATM 3332  C4  OLA A4007     -16.577  30.062  50.909  1.00 62.93           C  
HETATM 3333  C5  OLA A4007     -15.085  30.265  50.683  1.00 62.36           C  
HETATM 3334  C6  OLA A4007     -14.844  30.933  49.334  1.00 61.71           C  
HETATM 3335  C7  OLA A4007     -15.376  30.078  48.189  1.00 61.10           C  
HETATM 3336  C8  OLA A4007     -16.153  30.921  47.182  1.00 60.49           C  
HETATM 3337  C9  OLA A4007     -16.335  30.132  45.905  1.00 59.47           C  
HETATM 3338  C10 OLA A4007     -17.436  30.247  45.166  1.00 58.35           C  
HETATM 3339  C11 OLA A4007     -18.555  31.178  45.569  1.00 57.55           C  
HETATM 3340  C12 OLA A4007     -18.959  32.015  44.361  1.00 57.01           C  
HETATM 3341  C13 OLA A4007     -20.468  32.221  44.306  1.00 56.36           C  
HETATM 3342  C14 OLA A4007     -20.886  32.654  42.906  1.00 55.82           C  
HETATM 3343  C15 OLA A4007     -22.394  32.564  42.705  1.00 55.20           C  
HETATM 3344  C16 OLA A4007     -22.725  32.676  41.222  1.00 54.84           C  
HETATM 3345  C17 OLA A4007     -24.111  33.269  41.001  1.00 54.66           C  
HETATM 3346  C18 OLA A4007     -24.308  33.652  39.550  1.00 54.56           C  
HETATM 3347  C24 OLC A4008     -17.916   0.656  54.659  1.00 71.85           C  
HETATM 3348  C6  OLC A4008     -17.114   1.397  44.582  1.00 68.32           C  
HETATM 3349  C5  OLC A4008     -17.327   0.547  45.829  1.00 68.46           C  
HETATM 3350  C4  OLC A4008     -17.066   1.365  47.087  1.00 68.62           C  
HETATM 3351  C3  OLC A4008     -17.257   0.540  48.355  1.00 68.66           C  
HETATM 3352  C2  OLC A4008     -18.664  -0.036  48.446  1.00 69.00           C  
HETATM 3353  C21 OLC A4008     -18.643   0.509  52.274  1.00 71.04           C  
HETATM 3354  C1  OLC A4008     -19.145   0.030  49.877  1.00 69.53           C  
HETATM 3355  C22 OLC A4008     -17.679  -0.036  53.322  1.00 71.81           C  
HETATM 3356  O19 OLC A4008     -20.338   0.003  50.132  1.00 69.17           O  
HETATM 3357  O25 OLC A4008     -16.987   0.151  55.624  1.00 71.77           O  
HETATM 3358  O23 OLC A4008     -17.902  -1.441  53.480  1.00 72.35           O  
HETATM 3359  O20 OLC A4008     -18.192   0.141  50.971  1.00 70.44           O  
HETATM 3360  O   HOH A4101      -9.489  17.600  -8.412  1.00 30.69           O  
HETATM 3361  O   HOH A4102     -16.756  12.219  49.753  1.00 26.84           O  
HETATM 3362  O   HOH A4103     -26.222  18.405  36.816  1.00 21.83           O  
HETATM 3363  O   HOH A4104     -25.049  17.640  18.862  1.00 26.91           O  
HETATM 3364  O   HOH A4105       4.582  26.971  16.660  1.00 20.81           O  
HETATM 3365  O   HOH A4106      -5.663  31.620   7.420  1.00 41.16           O  
HETATM 3366  O   HOH A4107     -14.997  16.899  -3.978  1.00 42.96           O  
HETATM 3367  O   HOH A4108     -15.353  28.796  -4.796  1.00 30.54           O  
HETATM 3368  O   HOH A4109     -13.578  10.059  52.434  1.00 37.03           O  
HETATM 3369  O   HOH A4110     -18.867  37.461  13.455  1.00 31.02           O  
HETATM 3370  O   HOH A4111     -14.008  12.191  59.182  1.00 35.20           O  
HETATM 3371  O   HOH A4112     -10.865  35.301  -2.590  1.00 59.78           O  
HETATM 3372  O   HOH A4113     -17.987  16.142  48.381  1.00 46.24           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 2458                                                                
CONECT 2458  599                                                                
CONECT 3235 3236 3237 3238                                                      
CONECT 3236 3235                                                                
CONECT 3237 3235                                                                
CONECT 3238 3235 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 3249                                                           
CONECT 3249 3248 3250                                                           
CONECT 3250 3249 3251                                                           
CONECT 3251 3250 3252                                                           
CONECT 3252 3251 3253                                                           
CONECT 3253 3252 3254                                                           
CONECT 3254 3253                                                                
CONECT 3255 3256 3257 3258                                                      
CONECT 3256 3255                                                                
CONECT 3257 3255                                                                
CONECT 3258 3255 3259                                                           
CONECT 3259 3258 3260                                                           
CONECT 3260 3259 3261                                                           
CONECT 3261 3260 3262                                                           
CONECT 3262 3261 3263                                                           
CONECT 3263 3262 3264                                                           
CONECT 3264 3263 3265                                                           
CONECT 3265 3264 3266                                                           
CONECT 3266 3265 3267                                                           
CONECT 3267 3266 3268                                                           
CONECT 3268 3267 3269                                                           
CONECT 3269 3268                                                                
CONECT 3270 3271 3272 3273                                                      
CONECT 3271 3270                                                                
CONECT 3272 3270                                                                
CONECT 3273 3270 3274                                                           
CONECT 3274 3273 3275                                                           
CONECT 3275 3274 3276                                                           
CONECT 3276 3275 3277                                                           
CONECT 3277 3276 3278                                                           
CONECT 3278 3277 3279                                                           
CONECT 3279 3278 3280                                                           
CONECT 3280 3279 3281                                                           
CONECT 3281 3280 3282                                                           
CONECT 3282 3281 3283                                                           
CONECT 3283 3282                                                                
CONECT 3284 3285 3286 3287                                                      
CONECT 3285 3284                                                                
CONECT 3286 3284                                                                
CONECT 3287 3284 3288                                                           
CONECT 3288 3287 3289                                                           
CONECT 3289 3288 3290                                                           
CONECT 3290 3289 3291                                                           
CONECT 3291 3290 3292                                                           
CONECT 3292 3291 3293                                                           
CONECT 3293 3292 3294                                                           
CONECT 3294 3293 3295                                                           
CONECT 3295 3294 3296                                                           
CONECT 3296 3295                                                                
CONECT 3297 3298 3302                                                           
CONECT 3298 3297 3299                                                           
CONECT 3299 3298 3300                                                           
CONECT 3300 3299 3301 3303                                                      
CONECT 3301 3300 3302                                                           
CONECT 3302 3297 3301                                                           
CONECT 3303 3300 3304                                                           
CONECT 3304 3303 3305                                                           
CONECT 3305 3304 3306 3307 3308                                                 
CONECT 3306 3305                                                                
CONECT 3307 3305                                                                
CONECT 3308 3305                                                                
CONECT 3309 3317 3318                                                           
CONECT 3310 3318 3319                                                           
CONECT 3311 3317 3319                                                           
CONECT 3312 3320                                                                
CONECT 3313 3314 3320                                                           
CONECT 3314 3313 3321 3324                                                      
CONECT 3315 3320 3321 3322                                                      
CONECT 3316 3322 3323 3325                                                      
CONECT 3317 3309 3311 3323                                                      
CONECT 3318 3309 3310 3326                                                      
CONECT 3319 3310 3311                                                           
CONECT 3320 3312 3313 3315                                                      
CONECT 3321 3314 3315                                                           
CONECT 3322 3315 3316                                                           
CONECT 3323 3316 3317                                                           
CONECT 3324 3314                                                                
CONECT 3325 3316                                                                
CONECT 3326 3318                                                                
CONECT 3327 3328 3329 3330                                                      
CONECT 3328 3327                                                                
CONECT 3329 3327                                                                
CONECT 3330 3327 3331                                                           
CONECT 3331 3330 3332                                                           
CONECT 3332 3331 3333                                                           
CONECT 3333 3332 3334                                                           
CONECT 3334 3333 3335                                                           
CONECT 3335 3334 3336                                                           
CONECT 3336 3335 3337                                                           
CONECT 3337 3336 3338                                                           
CONECT 3338 3337 3339                                                           
CONECT 3339 3338 3340                                                           
CONECT 3340 3339 3341                                                           
CONECT 3341 3340 3342                                                           
CONECT 3342 3341 3343                                                           
CONECT 3343 3342 3344                                                           
CONECT 3344 3343 3345                                                           
CONECT 3345 3344 3346                                                           
CONECT 3346 3345                                                                
CONECT 3347 3355 3357                                                           
CONECT 3348 3349                                                                
CONECT 3349 3348 3350                                                           
CONECT 3350 3349 3351                                                           
CONECT 3351 3350 3352                                                           
CONECT 3352 3351 3354                                                           
CONECT 3353 3355 3359                                                           
CONECT 3354 3352 3356 3359                                                      
CONECT 3355 3347 3353 3358                                                      
CONECT 3356 3354                                                                
CONECT 3357 3347                                                                
CONECT 3358 3355                                                                
CONECT 3359 3353 3354                                                           
MASTER      341    0    9   21    3    0   13    6 3371    1  139   35          
END