HEADER    SIGNALING PROTEIN                       02-SEP-19   6KUX              
TITLE     CRYSTAL STRUCTURES OF THE ALPHA2A ADRENERGIC RECEPTOR IN COMPLEX WITH 
TITLE    2 AN ANTAGONIST RSC.                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA2A ADRENERGIC RECEPTOR;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    ALPHA2A ADRENERGIC RECEPTOR, ANTAGONIST, GPCR, SIGNALING PROTEIN      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.QU,Q.T.ZHOU,D.WU,S.W.ZHAO                                           
REVDAT   2   25-NOV-20 6KUX    1       SOURCE                                   
REVDAT   1   04-DEC-19 6KUX    0                                                
JRNL        AUTH   L.QU,Q.T.ZHOU,D.WU,S.W.ZHAO                                  
JRNL        TITL   CRYSTAL STRUCTURES OF THE ALPHA2A ADRENERGIC RECEPTOR IN     
JRNL        TITL 2 COMPLEX WITH AN ANTAGONIST RSC.                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 18724                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.252                           
REMARK   3   R VALUE            (WORKING SET) : 0.251                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.630                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 867                             
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  2.8691 -  2.7000    0.73     2332   109  0.2511 0.2669        
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)     : 0.530            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.410           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3043                                  
REMARK   3   ANGLE     :  0.526           4135                                  
REMARK   3   CHIRALITY :  0.039            487                                  
REMARK   3   PLANARITY :  0.003            508                                  
REMARK   3   DIHEDRAL  : 15.642           1802                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 29 THROUGH 227 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3629  -4.9629 -33.3038              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7608 T22:   1.4739                                     
REMARK   3      T33:   0.7221 T12:  -0.1829                                     
REMARK   3      T13:   0.1812 T23:  -0.5117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8863 L22:   0.2759                                     
REMARK   3      L33:   6.0010 L12:   0.6215                                     
REMARK   3      L13:   1.0899 L23:   1.5225                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0278 S12:  -0.9694 S13:   0.1075                       
REMARK   3      S21:   0.1897 S22:   0.5563 S23:   0.0659                       
REMARK   3      S31:  -1.1464 S32:   1.7109 S33:  -0.2238                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1001 THROUGH 1106 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -11.3049 -34.3860 -70.0184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3097 T22:   0.3075                                     
REMARK   3      T33:   0.7441 T12:  -0.0049                                     
REMARK   3      T13:  -0.0075 T23:  -0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7589 L22:   7.9903                                     
REMARK   3      L33:   3.9272 L12:   2.1212                                     
REMARK   3      L13:   0.9562 L23:  -0.1052                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0268 S12:   0.0133 S13:  -0.1415                       
REMARK   3      S21:   0.1850 S22:   0.0838 S23:   0.1786                       
REMARK   3      S31:   0.2116 S32:  -0.2315 S33:  -0.1369                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 365 THROUGH 443 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0879 -15.3426 -35.5685              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7587 T22:   1.6924                                     
REMARK   3      T33:   0.8347 T12:   0.3365                                     
REMARK   3      T13:   0.0247 T23:  -0.4292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6540 L22:   0.5670                                     
REMARK   3      L33:   2.6944 L12:   0.1350                                     
REMARK   3      L13:   3.7781 L23:   0.1679                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1833 S12:  -0.0066 S13:  -0.1816                       
REMARK   3      S21:   0.8070 S22:   0.3430 S23:  -0.5368                       
REMARK   3      S31:   1.5169 S32:   2.9610 S33:   0.0528                       
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 6KUX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE DEPOSITION ID IS D_1300012402.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-SEP-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18743                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY                : 8.100                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48700                            
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: 2Y02                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE TRIBASIC DIHYDRATE   
REMARK 280  PH 5.0, 290MM AMMONIUM CHLORIDE, 30% PEG400, 7% GLYCEROL,           
REMARK 280  LIPIDIC CUBIC PHASE, TEMPERATURE 293K                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      142.15500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      142.15500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       35.58500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.89500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       35.58500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.89500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      142.15500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       35.58500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       35.89500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      142.15500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       35.58500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       35.89500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 100 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 20600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     ALA A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     TYR A    28                                                      
REMARK 465     LYS A   174                                                      
REMARK 465     LYS A   175                                                      
REMARK 465     GLY A   176                                                      
REMARK 465     GLY A   177                                                      
REMARK 465     GLY A   178                                                      
REMARK 465     GLY A   179                                                      
REMARK 465     GLY A   180                                                      
REMARK 465     PRO A   181                                                      
REMARK 465     GLN A   182                                                      
REMARK 465     GLY A   444                                                      
REMARK 465     ASP A   445                                                      
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     LEU A  30    CG   CD1  CD2                                       
REMARK 470     GLN A  31    CG   CD   OE1  NE2                                  
REMARK 470     LEU A  34    CG   CD1  CD2                                       
REMARK 470     MET A  44    CG   SD   CE                                        
REMARK 470     ARG A  62    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A  98    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TRP A  99    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A  99    CZ3  CH2                                            
REMARK 470     TYR A 100    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TRP A 105    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 105    CZ3  CH2                                            
REMARK 470     GLU A 107    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 110    CG   CD1  CD2                                       
REMARK 470     ARG A 145    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 151    CG   CD   CE   NZ                                   
REMARK 470     ILE A 172    CG1  CG2  CD1                                       
REMARK 470     GLU A 173    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 189    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 192    CG   OD1  OD2                                       
REMARK 470     LYS A 194    CG   CD   CE   NZ                                   
REMARK 470     GLU A 369    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     ARG A 405    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 409    CG   CD   CE   NZ                                   
REMARK 470     LYS A 439    CG   CD   CE   NZ                                   
REMARK 470     LEU A 441    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  86      -58.02   -132.18                                   
REMARK 500    ARG A 145       36.25    -88.90                                   
REMARK 500    LEU A 169       -4.07     73.30                                   
REMARK 500    ILE A 172     -155.14   -138.48                                   
REMARK 500    CYS A 188       74.31    -69.81                                   
REMARK 500    LEU A1048       34.43    -95.24                                   
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 1207                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E3F A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 1208                
DBREF  6KUX A   20   445  PDB    6KUX     6KUX            20    445             
SEQRES   1 A  395  GLY GLY GLY ALA ARG ALA THR PRO TYR SER LEU GLN VAL          
SEQRES   2 A  395  THR LEU THR LEU VAL CYS LEU ALA GLY LEU LEU MET LEU          
SEQRES   3 A  395  LEU THR VAL PHE GLY ASN VAL LEU VAL ILE ILE ALA VAL          
SEQRES   4 A  395  PHE THR SER ARG ALA LEU LYS ALA PRO GLN ASN LEU PHE          
SEQRES   5 A  395  LEU VAL SER LEU ALA SER ALA ASP ILE LEU VAL ALA THR          
SEQRES   6 A  395  LEU VAL ILE PRO PHE SER LEU ALA ASN GLU VAL MET GLY          
SEQRES   7 A  395  TYR TRP TYR PHE GLY LYS ALA TRP CYS GLU ILE TYR LEU          
SEQRES   8 A  395  ALA LEU ASP VAL LEU PHE CYS THR SER SER ALA TRP HIS          
SEQRES   9 A  395  LEU CYS ALA ILE SER LEU ASP ARG TYR TRP SER ILE THR          
SEQRES  10 A  395  GLN ALA ILE GLU TYR ASN LEU LYS ARG THR PRO ARG ARG          
SEQRES  11 A  395  ILE LYS ALA ILE ILE ILE THR VAL TRP VAL ILE SER ALA          
SEQRES  12 A  395  VAL ILE SER PHE PRO PRO LEU ILE SER ILE GLU LYS LYS          
SEQRES  13 A  395  GLY GLY GLY GLY GLY PRO GLN PRO ALA GLU PRO ARG CYS          
SEQRES  14 A  395  GLU ILE ASN ASP GLN LYS TRP TYR VAL ILE SER SER CYS          
SEQRES  15 A  395  ILE GLY SER PHE PHE ALA PRO CYS LEU ILE MET ILE LEU          
SEQRES  16 A  395  VAL TYR VAL ARG ILE TYR GLN ILE ALA LYS ARG ARG THR          
SEQRES  17 A  395  ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN          
SEQRES  18 A  395  LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL          
SEQRES  19 A  395  LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP          
SEQRES  20 A  395  ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER          
SEQRES  21 A  395  PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE          
SEQRES  22 A  395  ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU          
SEQRES  23 A  395  ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA          
SEQRES  24 A  395  GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS          
SEQRES  25 A  395  TYR LEU ARG GLN ASN ARG GLU LYS ARG PHE THR PHE VAL          
SEQRES  26 A  395  LEU ALA VAL VAL ILE GLY VAL PHE VAL VAL CYS TRP PHE          
SEQRES  27 A  395  PRO PHE PHE PHE THR TYR THR LEU THR ALA VAL GLY CYS          
SEQRES  28 A  395  SER VAL PRO ARG THR LEU PHE LYS PHE PHE PHE TRP PHE          
SEQRES  29 A  395  GLY TYR CYS ASN SER SER LEU ASN PRO VAL ILE TYR THR          
SEQRES  30 A  395  ILE PHE ASN HIS ASP PHE ARG ARG ALA PHE LYS LYS ILE          
SEQRES  31 A  395  LEU CYS ARG GLY ASP                                          
HET    E3F  A1201      25                                                       
HET    PEG  A1202       7                                                       
HET    PEG  A1203       7                                                       
HET    PEG  A1204       7                                                       
HET    PEG  A1205       7                                                       
HET    PEG  A1206       7                                                       
HET    OLA  A1207       6                                                       
HET    FLC  A1208      13                                                       
HETNAM     E3F (8~{A}~{R},12~{A}~{S},13~{A}~{S})-12-ETHYLSULFONYL-3-            
HETNAM   2 E3F  METHOXY-5,6,8,8~{A},9,10,11,12~{A},13,13~{A}-                   
HETNAM   3 E3F  DECAHYDROISOQUINOLINO[2,1-G][1,6]NAPHTHYRIDINE                  
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     OLA OLEIC ACID                                                       
HETNAM     FLC CITRATE ANION                                                    
FORMUL   2  E3F    C19 H28 N2 O3 S                                              
FORMUL   3  PEG    5(C4 H10 O3)                                                 
FORMUL   8  OLA    C18 H34 O2                                                   
FORMUL   9  FLC    C6 H5 O7 3-                                                  
HELIX    1 AA1 THR A   33  SER A   61  1                                  29    
HELIX    2 AA2 ALA A   66  GLN A   68  5                                   3    
HELIX    3 AA3 ASN A   69  LEU A   85  1                                  17    
HELIX    4 AA4 VAL A   86  MET A   96  1                                  11    
HELIX    5 AA5 GLY A  102  GLN A  137  1                                  36    
HELIX    6 AA6 GLN A  137  LYS A  144  1                                   8    
HELIX    7 AA7 THR A  146  PHE A  166  1                                  21    
HELIX    8 AA8 TYR A  196  PHE A  205  1                                  10    
HELIX    9 AA9 PHE A  205  LYS A 1019  1                                  42    
HELIX   10 AB1 ASN A 1022  LYS A 1042  1                                  21    
HELIX   11 AB2 SER A 1055  ASN A 1080  1                                  26    
HELIX   12 AB3 LYS A 1083  GLN A 1103  1                                  21    
HELIX   13 AB4 LYS A 1104  ARG A  365  5                                   4    
HELIX   14 AB5 ASN A  367  THR A  397  1                                  31    
HELIX   15 AB6 ALA A  398  GLY A  400  5                                   3    
HELIX   16 AB7 PRO A  404  CYS A  417  1                                  14    
HELIX   17 AB8 CYS A  417  ASN A  430  1                                  14    
HELIX   18 AB9 ASN A  430  ARG A  443  1                                  14    
SSBOND   1 CYS A  106    CYS A  188                          1555   1555  2.03  
SITE     1 AC1  8 TYR A 109  ASP A 113  GLU A 189  ILE A 190                    
SITE     2 AC1  8 PHE A 390  PHE A 391  PHE A 408  TYR A 416                    
SITE     1 AC2  3 ILE A 164  SER A 199  ILE A 202                               
SITE     1 AC3  1 ASP A1005                                                     
SITE     1 AC4  4 THR A1009  LYS A1032  ALA A1035  PEG A1205                    
SITE     1 AC5  5 ASP A1005  ASN A1006  THR A1009  ALA A1036                    
SITE     2 AC5  5 PEG A1204                                                     
SITE     1 AC6  3 TYR A 220  LYS A 370  THR A 373                               
SITE     1 AC7  2 GLN A 137  LYS A 144                                          
SITE     1 AC8  5 ARG A 368  LYS A1047  LYS A1051  PRO A1056                    
SITE     2 AC8  5 GLU A1057                                                     
CRYST1   71.170   71.790  284.310  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014051  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013930  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003517        0.00000                         
ATOM      1  N   SER A  29      13.830 -14.629  -7.818  1.00209.82           N  
ANISOU    1  N   SER A  29    22795  43057  13869   2584  -1067  -4442       N  
ATOM      2  CA  SER A  29      12.480 -15.139  -7.605  1.00206.18           C  
ANISOU    2  CA  SER A  29    22791  42154  13393   2730  -1115  -3946       C  
ATOM      3  C   SER A  29      12.329 -16.540  -8.186  1.00201.60           C  
ANISOU    3  C   SER A  29    22430  41394  12774   3376  -1481  -3556       C  
ATOM      4  O   SER A  29      11.448 -17.299  -7.782  1.00206.65           O  
ANISOU    4  O   SER A  29    23372  41852  13294   3651  -1641  -3021       O  
ATOM      5  CB  SER A  29      11.446 -14.198  -8.225  1.00200.46           C  
ANISOU    5  CB  SER A  29    22464  40694  13009   2211   -803  -4069       C  
ATOM      6  OG  SER A  29      11.557 -12.892  -7.684  1.00210.34           O  
ANISOU    6  OG  SER A  29    23567  42038  14313   1652   -505  -4415       O  
ATOM      7  N   LEU A  30      13.193 -16.878  -9.138  1.00188.57           N  
ANISOU    7  N   LEU A  30    20628  39784  11237   3610  -1627  -3816       N  
ATOM      8  CA  LEU A  30      13.175 -18.176  -9.791  1.00185.31           C  
ANISOU    8  CA  LEU A  30    20404  39176  10828   4261  -2010  -3524       C  
ATOM      9  C   LEU A  30      14.457 -18.935  -9.476  1.00196.71           C  
ANISOU    9  C   LEU A  30    21425  41286  12031   4811  -2324  -3592       C  
ATOM     10  O   LEU A  30      15.489 -18.343  -9.145  1.00197.80           O  
ANISOU   10  O   LEU A  30    21081  42007  12069   4619  -2194  -3999       O  
ATOM     11  CB  LEU A  30      13.009 -18.034 -11.310  1.00180.42           C  
ANISOU   11  CB  LEU A  30    19995  37979  10579   4145  -1946  -3781       C  
ATOM     12  N   GLN A  31      14.377 -20.264  -9.580  1.00202.95           N  
ANISOU   12  N   GLN A  31    22413  41955  12745   5516  -2757  -3171       N  
ATOM     13  CA  GLN A  31      15.551 -21.100  -9.347  1.00207.01           C  
ANISOU   13  CA  GLN A  31    22577  43016  13059   6143  -3103  -3213       C  
ATOM     14  C   GLN A  31      16.647 -20.792 -10.359  1.00202.19           C  
ANISOU   14  C   GLN A  31    21581  42636  12606   6117  -3041  -3852       C  
ATOM     15  O   GLN A  31      17.820 -20.641  -9.997  1.00203.36           O  
ANISOU   15  O   GLN A  31    21208  43487  12574   6200  -3034  -4186       O  
ATOM     16  CB  GLN A  31      15.159 -22.577  -9.396  1.00203.37           C  
ANISOU   16  CB  GLN A  31    22503  42169  12600   6900  -3612  -2607       C  
ATOM     17  N   VAL A  32      16.284 -20.697 -11.634  1.00203.05           N  
ANISOU   17  N   VAL A  32    21920  42183  13047   5988  -2986  -4024       N  
ATOM     18  CA  VAL A  32      17.203 -20.260 -12.676  1.00206.98           C  
ANISOU   18  CA  VAL A  32    22070  42839  13736   5817  -2862  -4621       C  
ATOM     19  C   VAL A  32      16.596 -19.047 -13.364  1.00216.15           C  
ANISOU   19  C   VAL A  32    23411  43513  15204   5003  -2431  -4859       C  
ATOM     20  O   VAL A  32      15.374 -18.930 -13.487  1.00203.65           O  
ANISOU   20  O   VAL A  32    22314  41306  13755   4807  -2338  -4568       O  
ATOM     21  CB  VAL A  32      17.514 -21.385 -13.689  1.00199.84           C  
ANISOU   21  CB  VAL A  32    21226  41733  12970   6501  -3251  -4643       C  
ATOM     22  CG1 VAL A  32      16.329 -21.646 -14.617  1.00189.45           C  
ANISOU   22  CG1 VAL A  32    20479  39544  11960   6479  -3298  -4407       C  
ATOM     23  CG2 VAL A  32      18.774 -21.054 -14.485  1.00201.52           C  
ANISOU   23  CG2 VAL A  32    20905  42394  13269   6420  -3158  -5269       C  
ATOM     24  N   THR A  33      17.451 -18.129 -13.780  1.00232.68           N  
ANISOU   24  N   THR A  33    25119  45882  17406   4522  -2173  -5363       N  
ATOM     25  CA  THR A  33      16.996 -16.861 -14.339  1.00232.31           C  
ANISOU   25  CA  THR A  33    25244  45370  17652   3711  -1772  -5576       C  
ATOM     26  C   THR A  33      17.607 -16.554 -15.698  1.00219.49           C  
ANISOU   26  C   THR A  33    23464  43625  16307   3485  -1691  -5974       C  
ATOM     27  O   THR A  33      16.911 -16.025 -16.570  1.00222.65           O  
ANISOU   27  O   THR A  33    24211  43374  17010   3075  -1500  -6000       O  
ATOM     28  CB  THR A  33      17.308 -15.724 -13.343  1.00241.59           C  
ANISOU   28  CB  THR A  33    26180  46911  18703   3143  -1484  -5732       C  
ATOM     29  OG1 THR A  33      16.520 -15.896 -12.157  1.00248.96           O  
ANISOU   29  OG1 THR A  33    27318  47852  19421   3255  -1508  -5344       O  
ATOM     30  CG2 THR A  33      17.001 -14.363 -13.953  1.00235.08           C  
ANISOU   30  CG2 THR A  33    25537  45596  18188   2331  -1109  -5978       C  
ATOM     31  N   LEU A  34      18.883 -16.888 -15.908  1.00195.92           N  
ANISOU   31  N   LEU A  34    19954  41268  13219   3753  -1831  -6277       N  
ATOM     32  CA  LEU A  34      19.536 -16.576 -17.176  1.00190.91           C  
ANISOU   32  CA  LEU A  34    19106  40605  12826   3504  -1744  -6655       C  
ATOM     33  C   LEU A  34      18.864 -17.277 -18.349  1.00207.94           C  
ANISOU   33  C   LEU A  34    21625  42141  15240   3795  -1895  -6555       C  
ATOM     34  O   LEU A  34      18.913 -16.778 -19.479  1.00201.05           O  
ANISOU   34  O   LEU A  34    20781  40963  14645   3392  -1732  -6771       O  
ATOM     35  CB  LEU A  34      21.015 -16.956 -17.111  1.00191.47           C  
ANISOU   35  CB  LEU A  34    18507  41545  12699   3842  -1893  -6983       C  
ATOM     36  N   THR A  35      18.232 -18.429 -18.107  1.00227.43           N  
ANISOU   36  N   THR A  35    24386  44410  17619   4486  -2220  -6211       N  
ATOM     37  CA  THR A  35      17.565 -19.145 -19.190  1.00229.13           C  
ANISOU   37  CA  THR A  35    24956  44023  18078   4801  -2398  -6112       C  
ATOM     38  C   THR A  35      16.345 -18.380 -19.689  1.00222.87           C  
ANISOU   38  C   THR A  35    24672  42450  17559   4204  -2101  -5976       C  
ATOM     39  O   THR A  35      16.109 -18.296 -20.900  1.00220.18           O  
ANISOU   39  O   THR A  35    24467  41679  17511   4043  -2038  -6114       O  
ATOM     40  CB  THR A  35      17.157 -20.543 -18.726  1.00231.11           C  
ANISOU   40  CB  THR A  35    25452  44195  18163   5682  -2861  -5715       C  
ATOM     41  OG1 THR A  35      16.155 -20.432 -17.708  1.00229.75           O  
ANISOU   41  OG1 THR A  35    25664  43784  17848   5581  -2811  -5255       O  
ATOM     42  CG2 THR A  35      18.358 -21.288 -18.164  1.00235.42           C  
ANISOU   42  CG2 THR A  35    25526  45488  18435   6316  -3164  -5833       C  
ATOM     43  N   LEU A  36      15.564 -17.809 -18.770  1.00221.45           N  
ANISOU   43  N   LEU A  36    24762  42094  17286   3882  -1912  -5715       N  
ATOM     44  CA  LEU A  36      14.338 -17.124 -19.164  1.00211.47           C  
ANISOU   44  CA  LEU A  36    23995  40089  16264   3390  -1639  -5575       C  
ATOM     45  C   LEU A  36      14.635 -15.811 -19.879  1.00202.91           C  
ANISOU   45  C   LEU A  36    22840  38826  15429   2610  -1273  -5917       C  
ATOM     46  O   LEU A  36      13.956 -15.464 -20.852  1.00202.08           O  
ANISOU   46  O   LEU A  36    23062  38105  15613   2323  -1126  -5927       O  
ATOM     47  CB  LEU A  36      13.457 -16.884 -17.938  1.00206.31           C  
ANISOU   47  CB  LEU A  36    23606  39353  15428   3292  -1543  -5223       C  
ATOM     48  CG  LEU A  36      12.379 -17.929 -17.632  1.00197.35           C  
ANISOU   48  CG  LEU A  36    22887  37903  14196   3829  -1799  -4719       C  
ATOM     49  CD1 LEU A  36      12.948 -19.341 -17.617  1.00197.84           C  
ANISOU   49  CD1 LEU A  36    22814  38264  14092   4664  -2292  -4573       C  
ATOM     50  CD2 LEU A  36      11.696 -17.614 -16.309  1.00194.84           C  
ANISOU   50  CD2 LEU A  36    22710  37664  13656   3673  -1679  -4394       C  
ATOM     51  N   VAL A  37      15.641 -15.066 -19.413  1.00189.09           N  
ANISOU   51  N   VAL A  37    20684  37601  13562   2264  -1137  -6178       N  
ATOM     52  CA  VAL A  37      15.959 -13.794 -20.054  1.00173.93           C  
ANISOU   52  CA  VAL A  37    18735  35502  11849   1521   -825  -6455       C  
ATOM     53  C   VAL A  37      16.596 -14.022 -21.421  1.00180.63           C  
ANISOU   53  C   VAL A  37    19388  36355  12886   1530   -885  -6699       C  
ATOM     54  O   VAL A  37      16.399 -13.224 -22.346  1.00178.28           O  
ANISOU   54  O   VAL A  37    19280  35622  12837   1007   -671  -6800       O  
ATOM     55  CB  VAL A  37      16.854 -12.936 -19.137  1.00169.30           C  
ANISOU   55  CB  VAL A  37    17773  35488  11065   1149   -680  -6656       C  
ATOM     56  CG1 VAL A  37      18.173 -13.637 -18.852  1.00176.35           C  
ANISOU   56  CG1 VAL A  37    18047  37243  11716   1575   -906  -6846       C  
ATOM     57  CG2 VAL A  37      17.092 -11.562 -19.750  1.00167.86           C  
ANISOU   57  CG2 VAL A  37    17647  35056  11076    370   -375  -6894       C  
ATOM     58  N   CYS A  38      17.355 -15.110 -21.580  1.00184.59           N  
ANISOU   58  N   CYS A  38    19514  37351  13269   2142  -1184  -6794       N  
ATOM     59  CA  CYS A  38      17.873 -15.455 -22.900  1.00182.09           C  
ANISOU   59  CA  CYS A  38    19007  37040  13140   2226  -1264  -7024       C  
ATOM     60  C   CYS A  38      16.748 -15.899 -23.826  1.00171.00           C  
ANISOU   60  C   CYS A  38    18089  34881  12004   2366  -1314  -6843       C  
ATOM     61  O   CYS A  38      16.790 -15.635 -25.034  1.00176.59           O  
ANISOU   61  O   CYS A  38    18820  35318  12956   2090  -1219  -6992       O  
ATOM     62  CB  CYS A  38      18.936 -16.547 -22.784  1.00191.51           C  
ANISOU   62  CB  CYS A  38    19676  38955  14134   2931  -1593  -7196       C  
ATOM     63  SG  CYS A  38      20.530 -15.981 -22.146  1.00198.85           S  
ANISOU   63  SG  CYS A  38    19883  40872  14800   2708  -1504  -7541       S  
ATOM     64  N   LEU A  39      15.739 -16.578 -23.278  1.00162.19           N  
ANISOU   64  N   LEU A  39    17356  33441  10829   2791  -1466  -6510       N  
ATOM     65  CA  LEU A  39      14.562 -16.930 -24.066  1.00161.36           C  
ANISOU   65  CA  LEU A  39    17740  32602  10968   2889  -1489  -6321       C  
ATOM     66  C   LEU A  39      13.849 -15.676 -24.555  1.00158.28           C  
ANISOU   66  C   LEU A  39    17696  31625  10819   2118  -1102  -6310       C  
ATOM     67  O   LEU A  39      13.496 -15.566 -25.736  1.00154.09           O  
ANISOU   67  O   LEU A  39    17337  30648  10560   1942  -1030  -6372       O  
ATOM     68  CB  LEU A  39      13.620 -17.803 -23.230  1.00155.93           C  
ANISOU   68  CB  LEU A  39    17400  31728  10118   3443  -1715  -5922       C  
ATOM     69  CG  LEU A  39      12.657 -18.806 -23.886  1.00153.88           C  
ANISOU   69  CG  LEU A  39    17544  30919  10004   3945  -1959  -5703       C  
ATOM     70  CD1 LEU A  39      11.695 -18.151 -24.875  1.00157.55           C  
ANISOU   70  CD1 LEU A  39    18384  30675  10803   3452  -1673  -5706       C  
ATOM     71  CD2 LEU A  39      13.415 -19.951 -24.547  1.00156.09           C  
ANISOU   71  CD2 LEU A  39    17561  31437  10307   4613  -2358  -5883       C  
ATOM     72  N   ALA A  40      13.635 -14.711 -23.656  1.00152.03           N  
ANISOU   72  N   ALA A  40    17014  30823   9928   1674   -864  -6239       N  
ATOM     73  CA  ALA A  40      12.922 -13.494 -24.028  1.00148.44           C  
ANISOU   73  CA  ALA A  40    16936  29779   9686   1009   -529  -6223       C  
ATOM     74  C   ALA A  40      13.722 -12.660 -25.022  1.00152.29           C  
ANISOU   74  C   ALA A  40    17240  30296  10327    486   -371  -6509       C  
ATOM     75  O   ALA A  40      13.150 -12.071 -25.946  1.00162.77           O  
ANISOU   75  O   ALA A  40    18888  31057  11899    122   -203  -6497       O  
ATOM     76  CB  ALA A  40      12.593 -12.676 -22.780  1.00160.22           C  
ANISOU   76  CB  ALA A  40    18553  31299  11024    717   -346  -6122       C  
ATOM     77  N   GLY A  41      15.043 -12.591 -24.845  1.00161.29           N  
ANISOU   77  N   GLY A  41    17858  32117  11309    443   -423  -6755       N  
ATOM     78  CA  GLY A  41      15.870 -11.900 -25.821  1.00180.17           C  
ANISOU   78  CA  GLY A  41    20025  34623  13807    -28   -296  -7013       C  
ATOM     79  C   GLY A  41      15.864 -12.591 -27.171  1.00193.02           C  
ANISOU   79  C   GLY A  41    21616  36086  15637    186   -417  -7072       C  
ATOM     80  O   GLY A  41      15.874 -11.933 -28.216  1.00188.64           O  
ANISOU   80  O   GLY A  41    21160  35250  15264   -267   -260  -7149       O  
ATOM     81  N   LEU A  42      15.854 -13.926 -27.167  1.00195.78           N  
ANISOU   81  N   LEU A  42    21825  36616  15946    897   -714  -7038       N  
ATOM     82  CA  LEU A  42      15.668 -14.680 -28.403  1.00192.90           C  
ANISOU   82  CA  LEU A  42    21477  36022  15795   1176   -855  -7086       C  
ATOM     83  C   LEU A  42      14.343 -14.321 -29.065  1.00190.54           C  
ANISOU   83  C   LEU A  42    21764  34873  15760    919   -698  -6879       C  
ATOM     84  O   LEU A  42      14.275 -14.142 -30.287  1.00197.03           O  
ANISOU   84  O   LEU A  42    22634  35430  16799    689   -628  -6958       O  
ATOM     85  CB  LEU A  42      15.752 -16.181 -28.101  1.00195.82           C  
ANISOU   85  CB  LEU A  42    21685  36661  16059   2061  -1239  -7063       C  
ATOM     86  CG  LEU A  42      15.328 -17.294 -29.074  1.00196.10           C  
ANISOU   86  CG  LEU A  42    21818  36402  16290   2601  -1491  -7069       C  
ATOM     87  CD1 LEU A  42      13.818 -17.557 -29.037  1.00191.57           C  
ANISOU   87  CD1 LEU A  42    21858  35080  15849   2737  -1496  -6747       C  
ATOM     88  CD2 LEU A  42      15.804 -17.028 -30.498  1.00192.46           C  
ANISOU   88  CD2 LEU A  42    21141  35931  16052   2283  -1395  -7317       C  
ATOM     89  N   LEU A  43      13.278 -14.208 -28.269  1.00174.84           N  
ANISOU   89  N   LEU A  43    20203  32485  13743    959   -636  -6614       N  
ATOM     90  CA  LEU A  43      11.968 -13.866 -28.813  1.00166.25           C  
ANISOU   90  CA  LEU A  43    19658  30619  12890    752   -478  -6422       C  
ATOM     91  C   LEU A  43      11.945 -12.440 -29.348  1.00164.92           C  
ANISOU   91  C   LEU A  43    19672  30139  12851     -1   -166  -6483       C  
ATOM     92  O   LEU A  43      11.373 -12.180 -30.414  1.00161.29           O  
ANISOU   92  O   LEU A  43    19474  29183  12626   -210    -69  -6450       O  
ATOM     93  CB  LEU A  43      10.899 -14.071 -27.738  1.00164.19           C  
ANISOU   93  CB  LEU A  43    19750  30107  12526    984   -479  -6136       C  
ATOM     94  CG  LEU A  43       9.439 -13.692 -27.990  1.00161.15           C  
ANISOU   94  CG  LEU A  43    19921  28977  12334    811   -298  -5919       C  
ATOM     95  CD1 LEU A  43       8.985 -14.111 -29.374  1.00158.02           C  
ANISOU   95  CD1 LEU A  43    19666  28157  12219    896   -339  -5945       C  
ATOM     96  CD2 LEU A  43       8.562 -14.339 -26.927  1.00155.02           C  
ANISOU   96  CD2 LEU A  43    19354  28154  11393   1243   -400  -5638       C  
ATOM     97  N   MET A  44      12.569 -11.504 -28.630  1.00167.39           N  
ANISOU   97  N   MET A  44    19854  30742  13005   -394    -23  -6571       N  
ATOM     98  CA  MET A  44      12.597 -10.119 -29.089  1.00172.06           C  
ANISOU   98  CA  MET A  44    20637  31048  13689  -1075    236  -6633       C  
ATOM     99  C   MET A  44      13.426  -9.975 -30.360  1.00180.96           C  
ANISOU   99  C   MET A  44    21495  32354  14908  -1327    240  -6824       C  
ATOM    100  O   MET A  44      13.076  -9.192 -31.251  1.00176.15           O  
ANISOU  100  O   MET A  44    21157  31312  14459  -1751    397  -6801       O  
ATOM    101  CB  MET A  44      13.140  -9.211 -27.988  1.00172.53           C  
ANISOU  101  CB  MET A  44    20584  31426  13545  -1400    359  -6717       C  
ATOM    102  N   LEU A  45      14.529 -10.720 -30.462  1.00190.18           N  
ANISOU  102  N   LEU A  45    22112  34186  15959  -1057     65  -7016       N  
ATOM    103  CA  LEU A  45      15.343 -10.666 -31.673  1.00191.54           C  
ANISOU  103  CA  LEU A  45    21966  34610  16201  -1267     67  -7212       C  
ATOM    104  C   LEU A  45      14.578 -11.209 -32.874  1.00178.98           C  
ANISOU  104  C   LEU A  45    20607  32530  14865  -1100     11  -7123       C  
ATOM    105  O   LEU A  45      14.645 -10.639 -33.969  1.00179.33           O  
ANISOU  105  O   LEU A  45    20702  32402  15033  -1509    132  -7163       O  
ATOM    106  CB  LEU A  45      16.644 -11.442 -31.468  1.00201.73           C  
ANISOU  106  CB  LEU A  45    22585  36753  17310   -923   -124  -7458       C  
ATOM    107  CG  LEU A  45      17.536 -11.593 -32.703  1.00207.38           C  
ANISOU  107  CG  LEU A  45    22876  37842  18079  -1036   -148  -7690       C  
ATOM    108  CD1 LEU A  45      17.977 -10.234 -33.228  1.00207.25           C  
ANISOU  108  CD1 LEU A  45    22867  37835  18045  -1834    119  -7765       C  
ATOM    109  CD2 LEU A  45      18.738 -12.472 -32.397  1.00212.02           C  
ANISOU  109  CD2 LEU A  45    22791  39286  18482   -572   -359  -7947       C  
ATOM    110  N   LEU A  46      13.842 -12.309 -32.686  1.00166.07           N  
ANISOU  110  N   LEU A  46    19112  30686  13302   -505   -176  -7000       N  
ATOM    111  CA  LEU A  46      13.045 -12.866 -33.775  1.00159.09           C  
ANISOU  111  CA  LEU A  46    18452  29324  12669   -323   -233  -6925       C  
ATOM    112  C   LEU A  46      11.978 -11.883 -34.238  1.00146.79           C  
ANISOU  112  C   LEU A  46    17449  27039  11285   -795      9  -6736       C  
ATOM    113  O   LEU A  46      11.740 -11.734 -35.443  1.00137.65           O  
ANISOU  113  O   LEU A  46    16384  25604  10312   -989     63  -6741       O  
ATOM    114  CB  LEU A  46      12.402 -14.182 -33.336  1.00162.18           C  
ANISOU  114  CB  LEU A  46    18927  29613  13081    407   -484  -6823       C  
ATOM    115  CG  LEU A  46      13.027 -15.476 -33.861  1.00157.72           C  
ANISOU  115  CG  LEU A  46    17945  29438  12541   1007   -792  -7017       C  
ATOM    116  CD1 LEU A  46      14.508 -15.527 -33.537  1.00160.24           C  
ANISOU  116  CD1 LEU A  46    17665  30579  12642   1054   -878  -7275       C  
ATOM    117  CD2 LEU A  46      12.305 -16.688 -33.288  1.00156.86           C  
ANISOU  117  CD2 LEU A  46    18021  29156  12424   1747  -1065  -6882       C  
ATOM    118  N   THR A  47      11.325 -11.202 -33.293  1.00142.57           N  
ANISOU  118  N   THR A  47    17274  26207  10688   -962    149  -6576       N  
ATOM    119  CA  THR A  47      10.281 -10.247 -33.653  1.00143.03           C  
ANISOU  119  CA  THR A  47    17863  25576  10904  -1347    364  -6413       C  
ATOM    120  C   THR A  47      10.859  -9.061 -34.417  1.00153.87           C  
ANISOU  120  C   THR A  47    19216  26958  12291  -1976    529  -6513       C  
ATOM    121  O   THR A  47      10.364  -8.697 -35.491  1.00162.45           O  
ANISOU  121  O   THR A  47    20537  27632  13552  -2203    610  -6451       O  
ATOM    122  CB  THR A  47       9.548  -9.763 -32.402  1.00140.61           C  
ANISOU  122  CB  THR A  47    17886  25030  10509  -1360    469  -6263       C  
ATOM    123  OG1 THR A  47       8.919 -10.873 -31.752  1.00150.25           O  
ANISOU  123  OG1 THR A  47    19148  26241  11701   -793    320  -6137       O  
ATOM    124  CG2 THR A  47       8.495  -8.732 -32.772  1.00138.20           C  
ANISOU  124  CG2 THR A  47    18109  24031  10368  -1719    677  -6128       C  
ATOM    125  N   VAL A  48      11.915  -8.450 -33.876  1.00146.87           N  
ANISOU  125  N   VAL A  48    18035  26564  11204  -2269    580  -6667       N  
ATOM    126  CA  VAL A  48      12.516  -7.284 -34.518  1.00141.86           C  
ANISOU  126  CA  VAL A  48    17369  25988  10543  -2904    743  -6769       C  
ATOM    127  C   VAL A  48      13.060  -7.653 -35.892  1.00135.30           C  
ANISOU  127  C   VAL A  48    16250  25367   9792  -2971    690  -6871       C  
ATOM    128  O   VAL A  48      12.815  -6.957 -36.883  1.00134.38           O  
ANISOU  128  O   VAL A  48    16341  24942   9776  -3374    809  -6825       O  
ATOM    129  CB  VAL A  48      13.613  -6.682 -33.621  1.00139.40           C  
ANISOU  129  CB  VAL A  48    16731  26249   9985  -3180    800  -6945       C  
ATOM    130  CG1 VAL A  48      14.396  -5.620 -34.380  1.00142.18           C  
ANISOU  130  CG1 VAL A  48    16963  26779  10280  -3843    955  -7080       C  
ATOM    131  CG2 VAL A  48      13.004  -6.095 -32.358  1.00139.03           C  
ANISOU  131  CG2 VAL A  48    17012  25941   9871  -3210    887  -6850       C  
ATOM    132  N   PHE A  49      13.797  -8.764 -35.971  1.00148.59           N  
ANISOU  132  N   PHE A  49    17439  27594  11424  -2559    503  -7018       N  
ATOM    133  CA  PHE A  49      14.430  -9.154 -37.228  1.00152.39           C  
ANISOU  133  CA  PHE A  49    17559  28379  11962  -2597    447  -7162       C  
ATOM    134  C   PHE A  49      13.391  -9.466 -38.297  1.00147.45           C  
ANISOU  134  C   PHE A  49    17269  27165  11589  -2494    434  -7011       C  
ATOM    135  O   PHE A  49      13.499  -9.005 -39.439  1.00149.31           O  
ANISOU  135  O   PHE A  49    17499  27341  11892  -2864    525  -7027       O  
ATOM    136  CB  PHE A  49      15.346 -10.357 -36.996  1.00159.15           C  
ANISOU  136  CB  PHE A  49    17825  29922  12722  -2069    222  -7371       C  
ATOM    137  CG  PHE A  49      16.254 -10.663 -38.150  1.00157.93           C  
ANISOU  137  CG  PHE A  49    17174  30255  12575  -2136    181  -7588       C  
ATOM    138  CD1 PHE A  49      17.293  -9.807 -38.471  1.00160.84           C  
ANISOU  138  CD1 PHE A  49    17218  31106  12788  -2694    335  -7749       C  
ATOM    139  CD2 PHE A  49      16.083 -11.814 -38.903  1.00149.44           C  
ANISOU  139  CD2 PHE A  49    15936  29188  11655  -1642     -8  -7649       C  
ATOM    140  CE1 PHE A  49      18.137 -10.083 -39.528  1.00166.25           C  
ANISOU  140  CE1 PHE A  49    17411  32297  13459  -2767    316  -7957       C  
ATOM    141  CE2 PHE A  49      16.925 -12.097 -39.962  1.00150.97           C  
ANISOU  141  CE2 PHE A  49    15640  29868  11853  -1688    -40  -7872       C  
ATOM    142  CZ  PHE A  49      17.953 -11.230 -40.275  1.00155.50           C  
ANISOU  142  CZ  PHE A  49    15877  30948  12257  -2253    129  -8021       C  
ATOM    143  N   GLY A  50      12.370 -10.248 -37.943  1.00140.18           N  
ANISOU  143  N   GLY A  50    16633  25830  10798  -2006    328  -6864       N  
ATOM    144  CA  GLY A  50      11.375 -10.635 -38.928  1.00136.70           C  
ANISOU  144  CA  GLY A  50    16476  24863  10602  -1874    310  -6742       C  
ATOM    145  C   GLY A  50      10.526  -9.470 -39.399  1.00135.76           C  
ANISOU  145  C   GLY A  50    16867  24134  10584  -2363    522  -6559       C  
ATOM    146  O   GLY A  50      10.253  -9.335 -40.596  1.00125.04           O  
ANISOU  146  O   GLY A  50    15583  22563   9362  -2543    563  -6527       O  
ATOM    147  N   ASN A  51      10.109  -8.606 -38.472  1.00137.75           N  
ANISOU  147  N   ASN A  51    17461  24114  10763  -2569    652  -6449       N  
ATOM    148  CA  ASN A  51       9.214  -7.512 -38.839  1.00133.46           C  
ANISOU  148  CA  ASN A  51    17429  22955  10324  -2958    831  -6285       C  
ATOM    149  C   ASN A  51       9.952  -6.405 -39.584  1.00141.62           C  
ANISOU  149  C   ASN A  51    18385  24150  11273  -3597    962  -6362       C  
ATOM    150  O   ASN A  51       9.397  -5.800 -40.509  1.00145.67           O  
ANISOU  150  O   ASN A  51    19192  24258  11900  -3892   1057  -6256       O  
ATOM    151  CB  ASN A  51       8.522  -6.959 -37.595  1.00136.93           C  
ANISOU  151  CB  ASN A  51    18239  23071  10720  -2940    919  -6173       C  
ATOM    152  CG  ASN A  51       7.476  -7.906 -37.040  1.00141.77           C  
ANISOU  152  CG  ASN A  51    19046  23387  11435  -2392    839  -6039       C  
ATOM    153  OD1 ASN A  51       6.314  -7.870 -37.444  1.00124.45           O  
ANISOU  153  OD1 ASN A  51    17233  20626   9426  -2323    896  -5885       O  
ATOM    154  ND2 ASN A  51       7.884  -8.758 -36.107  1.00152.66           N  
ANISOU  154  ND2 ASN A  51    20153  25171  12680  -2008    709  -6099       N  
ATOM    155  N   VAL A  52      11.199  -6.117 -39.200  1.00144.71           N  
ANISOU  155  N   VAL A  52    18380  25148  11454  -3834    976  -6546       N  
ATOM    156  CA  VAL A  52      11.966  -5.127 -39.950  1.00142.98           C  
ANISOU  156  CA  VAL A  52    18048  25150  11129  -4477   1112  -6632       C  
ATOM    157  C   VAL A  52      12.309  -5.666 -41.331  1.00143.34           C  
ANISOU  157  C   VAL A  52    17798  25423  11242  -4486   1057  -6688       C  
ATOM    158  O   VAL A  52      12.483  -4.895 -42.282  1.00151.77           O  
ANISOU  158  O   VAL A  52    18925  26460  12282  -5003   1180  -6671       O  
ATOM    159  CB  VAL A  52      13.230  -4.699 -39.179  1.00152.30           C  
ANISOU  159  CB  VAL A  52    18841  26969  12055  -4748   1158  -6833       C  
ATOM    160  CG1 VAL A  52      14.337  -5.739 -39.316  1.00147.43           C  
ANISOU  160  CG1 VAL A  52    17555  27112  11350  -4452   1013  -7043       C  
ATOM    161  CG2 VAL A  52      13.711  -3.340 -39.665  1.00160.02           C  
ANISOU  161  CG2 VAL A  52    19911  27980  12908  -5522   1360  -6872       C  
ATOM    162  N   LEU A  53      12.405  -6.991 -41.468  1.00134.19           N  
ANISOU  162  N   LEU A  53    16322  24502  10163  -3926    872  -6760       N  
ATOM    163  CA  LEU A  53      12.613  -7.584 -42.783  1.00130.76           C  
ANISOU  163  CA  LEU A  53    15612  24249   9821  -3871    808  -6826       C  
ATOM    164  C   LEU A  53      11.353  -7.478 -43.630  1.00126.69           C  
ANISOU  164  C   LEU A  53    15566  23045   9524  -3880    846  -6614       C  
ATOM    165  O   LEU A  53      11.430  -7.282 -44.848  1.00126.92           O  
ANISOU  165  O   LEU A  53    15526  23106   9590  -4154    895  -6612       O  
ATOM    166  CB  LEU A  53      13.048  -9.042 -42.634  1.00131.18           C  
ANISOU  166  CB  LEU A  53    15206  24730   9907  -3233    585  -6991       C  
ATOM    167  CG  LEU A  53      14.300  -9.478 -43.397  1.00141.03           C  
ANISOU  167  CG  LEU A  53    15791  26732  11063  -3265    527  -7252       C  
ATOM    168  CD1 LEU A  53      15.389  -8.424 -43.282  1.00139.35           C  
ANISOU  168  CD1 LEU A  53    15331  27013  10604  -3878    696  -7370       C  
ATOM    169  CD2 LEU A  53      14.798 -10.817 -42.873  1.00145.64           C  
ANISOU  169  CD2 LEU A  53    15938  27759  11640  -2588    290  -7442       C  
ATOM    170  N   VAL A  54      10.183  -7.599 -42.998  1.00143.62           N  
ANISOU  170  N   VAL A  54    18172  24597  11802  -3589    834  -6437       N  
ATOM    171  CA  VAL A  54       8.922  -7.422 -43.715  1.00157.10           C  
ANISOU  171  CA  VAL A  54    20338  25639  13713  -3600    887  -6236       C  
ATOM    172  C   VAL A  54       8.788  -5.983 -44.199  1.00148.70           C  
ANISOU  172  C   VAL A  54    19601  24307  12593  -4249   1077  -6132       C  
ATOM    173  O   VAL A  54       8.407  -5.729 -45.348  1.00157.64           O  
ANISOU  173  O   VAL A  54    20863  25224  13809  -4469   1126  -6046       O  
ATOM    174  CB  VAL A  54       7.736  -7.830 -42.822  1.00162.13           C  
ANISOU  174  CB  VAL A  54    21363  25757  14481  -3163    857  -6088       C  
ATOM    175  CG1 VAL A  54       6.421  -7.386 -43.443  1.00161.06           C  
ANISOU  175  CG1 VAL A  54    21734  24924  14539  -3252    954  -5880       C  
ATOM    176  CG2 VAL A  54       7.734  -9.333 -42.594  1.00161.59           C  
ANISOU  176  CG2 VAL A  54    21019  25889  14487  -2537    662  -6174       C  
ATOM    177  N   ILE A  55       9.109  -5.021 -43.331  1.00125.30           N  
ANISOU  177  N   ILE A  55    16777  21359   9475  -4575   1184  -6144       N  
ATOM    178  CA  ILE A  55       8.965  -3.611 -43.687  1.00124.21           C  
ANISOU  178  CA  ILE A  55    17005  20919   9269  -5205   1363  -6053       C  
ATOM    179  C   ILE A  55       9.902  -3.251 -44.833  1.00127.35           C  
ANISOU  179  C   ILE A  55    17105  21751   9534  -5712   1425  -6139       C  
ATOM    180  O   ILE A  55       9.508  -2.582 -45.796  1.00128.30           O  
ANISOU  180  O   ILE A  55    17507  21569   9672  -6098   1520  -6013       O  
ATOM    181  CB  ILE A  55       9.210  -2.720 -42.456  1.00126.50           C  
ANISOU  181  CB  ILE A  55    17462  21188   9413  -5437   1456  -6094       C  
ATOM    182  CG1 ILE A  55       8.132  -2.962 -41.398  1.00125.66           C  
ANISOU  182  CG1 ILE A  55    17700  20609   9437  -4978   1421  -5986       C  
ATOM    183  CG2 ILE A  55       9.248  -1.253 -42.855  1.00132.11           C  
ANISOU  183  CG2 ILE A  55    18532  21643  10021  -6145   1637  -6038       C  
ATOM    184  CD1 ILE A  55       8.307  -2.130 -40.148  1.00125.62           C  
ANISOU  184  CD1 ILE A  55    17846  20588   9296  -5163   1507  -6040       C  
ATOM    185  N   ILE A  56      11.160  -3.690 -44.746  1.00130.45           N  
ANISOU  185  N   ILE A  56    16912  22880   9773  -5722   1377  -6354       N  
ATOM    186  CA  ILE A  56      12.120  -3.404 -45.809  1.00133.89           C  
ANISOU  186  CA  ILE A  56    16990  23823  10059  -6203   1451  -6458       C  
ATOM    187  C   ILE A  56      11.698  -4.083 -47.106  1.00131.64           C  
ANISOU  187  C   ILE A  56    16619  23471   9926  -6025   1382  -6402       C  
ATOM    188  O   ILE A  56      11.778  -3.489 -48.188  1.00132.99           O  
ANISOU  188  O   ILE A  56    16846  23654  10031  -6510   1490  -6342       O  
ATOM    189  CB  ILE A  56      13.538  -3.826 -45.378  1.00137.82           C  
ANISOU  189  CB  ILE A  56    16829  25166  10371  -6177   1412  -6725       C  
ATOM    190  CG1 ILE A  56      14.073  -2.877 -44.303  1.00151.42           C  
ANISOU  190  CG1 ILE A  56    18627  27009  11895  -6557   1532  -6788       C  
ATOM    191  CG2 ILE A  56      14.479  -3.863 -46.573  1.00141.05           C  
ANISOU  191  CG2 ILE A  56    16761  26177  10656  -6528   1465  -6858       C  
ATOM    192  CD1 ILE A  56      14.219  -1.444 -44.772  1.00153.81           C  
ANISOU  192  CD1 ILE A  56    19236  27168  12038  -7383   1753  -6719       C  
ATOM    193  N   ALA A  57      11.225  -5.329 -47.019  1.00128.41           N  
ANISOU  193  N   ALA A  57    16090  22990   9712  -5348   1206  -6420       N  
ATOM    194  CA  ALA A  57      10.829  -6.053 -48.223  1.00126.40           C  
ANISOU  194  CA  ALA A  57    15721  22692   9613  -5146   1131  -6398       C  
ATOM    195  C   ALA A  57       9.643  -5.387 -48.911  1.00134.89           C  
ANISOU  195  C   ALA A  57    17364  23083  10806  -5375   1224  -6147       C  
ATOM    196  O   ALA A  57       9.547  -5.394 -50.144  1.00129.83           O  
ANISOU  196  O   ALA A  57    16655  22484  10189  -5561   1248  -6111       O  
ATOM    197  CB  ALA A  57      10.501  -7.505 -47.879  1.00123.76           C  
ANISOU  197  CB  ALA A  57    15202  22357   9463  -4384    926  -6472       C  
ATOM    198  N   VAL A  58       8.732  -4.801 -48.132  1.00136.24           N  
ANISOU  198  N   VAL A  58    18083  22640  11041  -5359   1279  -5979       N  
ATOM    199  CA  VAL A  58       7.553  -4.171 -48.720  1.00134.25           C  
ANISOU  199  CA  VAL A  58    18388  21716  10906  -5529   1362  -5745       C  
ATOM    200  C   VAL A  58       7.920  -2.842 -49.370  1.00151.17           C  
ANISOU  200  C   VAL A  58    20734  23853  12850  -6295   1531  -5671       C  
ATOM    201  O   VAL A  58       7.427  -2.509 -50.455  1.00143.25           O  
ANISOU  201  O   VAL A  58    19947  22609  11870  -6543   1581  -5531       O  
ATOM    202  CB  VAL A  58       6.454  -3.999 -47.654  1.00131.11           C  
ANISOU  202  CB  VAL A  58    18488  20684  10645  -5231   1372  -5608       C  
ATOM    203  CG1 VAL A  58       5.337  -3.108 -48.175  1.00137.79           C  
ANISOU  203  CG1 VAL A  58    19938  20840  11577  -5480   1482  -5375       C  
ATOM    204  CG2 VAL A  58       5.899  -5.352 -47.245  1.00126.48           C  
ANISOU  204  CG2 VAL A  58    17769  20036  10254  -4518   1223  -5635       C  
ATOM    205  N   PHE A  59       8.800  -2.071 -48.732  1.00170.22           N  
ANISOU  205  N   PHE A  59    23088  26542  15046  -6706   1623  -5762       N  
ATOM    206  CA  PHE A  59       9.101  -0.720 -49.186  1.00188.85           C  
ANISOU  206  CA  PHE A  59    25739  28823  17191  -7482   1799  -5680       C  
ATOM    207  C   PHE A  59      10.186  -0.653 -50.254  1.00199.29           C  
ANISOU  207  C   PHE A  59    26611  30804  18304  -7956   1861  -5779       C  
ATOM    208  O   PHE A  59      10.292   0.371 -50.938  1.00203.23           O  
ANISOU  208  O   PHE A  59    27392  31206  18620  -8624   2006  -5664       O  
ATOM    209  CB  PHE A  59       9.518   0.155 -47.998  1.00199.09           C  
ANISOU  209  CB  PHE A  59    27215  30091  18337  -7763   1892  -5740       C  
ATOM    210  CG  PHE A  59       8.489   1.177 -47.607  1.00205.62           C  
ANISOU  210  CG  PHE A  59    28795  30116  19216  -7927   1976  -5548       C  
ATOM    211  CD1 PHE A  59       8.275   2.297 -48.393  1.00211.38           C  
ANISOU  211  CD1 PHE A  59    30005  30495  19814  -8549   2106  -5385       C  
ATOM    212  CD2 PHE A  59       7.740   1.023 -46.451  1.00200.20           C  
ANISOU  212  CD2 PHE A  59    28347  29028  18690  -7458   1925  -5531       C  
ATOM    213  CE1 PHE A  59       7.331   3.242 -48.039  1.00209.54           C  
ANISOU  213  CE1 PHE A  59    30498  29490  19628  -8662   2167  -5216       C  
ATOM    214  CE2 PHE A  59       6.794   1.965 -46.091  1.00196.27           C  
ANISOU  214  CE2 PHE A  59    28523  27803  18249  -7573   2000  -5377       C  
ATOM    215  CZ  PHE A  59       6.590   3.076 -46.886  1.00203.09           C  
ANISOU  215  CZ  PHE A  59    29879  28287  18998  -8155   2114  -5225       C  
ATOM    216  N   THR A  60      10.991  -1.702 -50.421  1.00195.03           N  
ANISOU  216  N   THR A  60    25399  30932  17772  -7641   1759  -5988       N  
ATOM    217  CA  THR A  60      12.116  -1.645 -51.347  1.00186.38           C  
ANISOU  217  CA  THR A  60    23802  30551  16462  -8082   1835  -6119       C  
ATOM    218  C   THR A  60      11.813  -2.225 -52.721  1.00183.54           C  
ANISOU  218  C   THR A  60    23271  30274  16190  -7990   1788  -6074       C  
ATOM    219  O   THR A  60      12.560  -1.948 -53.667  1.00186.94           O  
ANISOU  219  O   THR A  60    23403  31206  16420  -8475   1890  -6126       O  
ATOM    220  CB  THR A  60      13.330  -2.379 -50.764  1.00192.54           C  
ANISOU  220  CB  THR A  60    23888  32107  17161  -7836   1768  -6412       C  
ATOM    221  OG1 THR A  60      12.930  -3.671 -50.290  1.00195.76           O  
ANISOU  221  OG1 THR A  60    24118  32450  17812  -7007   1558  -6485       O  
ATOM    222  CG2 THR A  60      13.933  -1.581 -49.619  1.00197.18           C  
ANISOU  222  CG2 THR A  60    24550  32805  17566  -8156   1868  -6483       C  
ATOM    223  N   SER A  61      10.749  -3.010 -52.858  1.00178.57           N  
ANISOU  223  N   SER A  61    22811  29198  15841  -7405   1650  -5986       N  
ATOM    224  CA  SER A  61      10.459  -3.656 -54.130  1.00178.93           C  
ANISOU  224  CA  SER A  61    22652  29350  15984  -7269   1595  -5973       C  
ATOM    225  C   SER A  61      10.036  -2.630 -55.173  1.00205.13           C  
ANISOU  225  C   SER A  61    26374  32396  19170  -7905   1738  -5746       C  
ATOM    226  O   SER A  61       9.357  -1.647 -54.865  1.00202.03           O  
ANISOU  226  O   SER A  61    26623  31396  18743  -8198   1821  -5534       O  
ATOM    227  CB  SER A  61       9.368  -4.708 -53.951  1.00158.79           C  
ANISOU  227  CB  SER A  61    20227  26350  13757  -6520   1426  -5932       C  
ATOM    228  OG  SER A  61       8.154  -4.112 -53.533  1.00151.62           O  
ANISOU  228  OG  SER A  61    20005  24644  12960  -6506   1463  -5692       O  
ATOM    229  N   ARG A  62      10.444  -2.867 -56.420  1.00235.82           N  
ANISOU  229  N   ARG A  62    29891  36743  22968  -8115   1765  -5793       N  
ATOM    230  CA  ARG A  62      10.162  -1.945 -57.522  1.00249.31           C  
ANISOU  230  CA  ARG A  62    31928  38302  24496  -8762   1898  -5577       C  
ATOM    231  C   ARG A  62       8.787  -2.279 -58.086  1.00252.16           C  
ANISOU  231  C   ARG A  62    32662  38054  25094  -8416   1810  -5389       C  
ATOM    232  O   ARG A  62       8.654  -3.041 -59.040  1.00255.87           O  
ANISOU  232  O   ARG A  62    32797  38768  25654  -8195   1746  -5444       O  
ATOM    233  CB  ARG A  62      11.243  -2.033 -58.594  1.00246.66           C  
ANISOU  233  CB  ARG A  62    30997  38795  23927  -9172   1985  -5713       C  
ATOM    234  N   ALA A  63       7.754  -1.690 -57.482  1.00244.36           N  
ANISOU  234  N   ALA A  63    32365  36278  24203  -8367   1816  -5180       N  
ATOM    235  CA  ALA A  63       6.370  -1.848 -57.922  1.00233.92           C  
ANISOU  235  CA  ALA A  63    31476  34317  23087  -8078   1758  -4983       C  
ATOM    236  C   ALA A  63       5.888  -3.289 -57.790  1.00227.54           C  
ANISOU  236  C   ALA A  63    30325  33529  22602  -7263   1595  -5123       C  
ATOM    237  O   ALA A  63       4.980  -3.712 -58.511  1.00236.44           O  
ANISOU  237  O   ALA A  63    31559  34393  23885  -7026   1545  -5032       O  
ATOM    238  CB  ALA A  63       6.176  -1.354 -59.363  1.00234.35           C  
ANISOU  238  CB  ALA A  63    31662  34412  22970  -8580   1826  -4812       C  
ATOM    239  N   LEU A  64       6.496  -4.055 -56.881  1.00211.56           N  
ANISOU  239  N   LEU A  64    27903  31819  20663  -6847   1509  -5345       N  
ATOM    240  CA  LEU A  64       6.033  -5.403 -56.584  1.00190.25           C  
ANISOU  240  CA  LEU A  64    24969  29066  18250  -6086   1347  -5467       C  
ATOM    241  C   LEU A  64       5.024  -5.444 -55.446  1.00162.59           C  
ANISOU  241  C   LEU A  64    21943  24898  14937  -5688   1316  -5355       C  
ATOM    242  O   LEU A  64       4.271  -6.419 -55.341  1.00155.87           O  
ANISOU  242  O   LEU A  64    21074  23818  14331  -5125   1212  -5376       O  
ATOM    243  CB  LEU A  64       7.217  -6.314 -56.238  1.00191.61           C  
ANISOU  243  CB  LEU A  64    24470  29933  18400  -5809   1249  -5765       C  
ATOM    244  CG  LEU A  64       7.930  -7.048 -57.373  1.00192.38           C  
ANISOU  244  CG  LEU A  64    23939  30686  18471  -5785   1204  -5958       C  
ATOM    245  CD1 LEU A  64       8.748  -6.095 -58.230  1.00198.34           C  
ANISOU  245  CD1 LEU A  64    24551  31889  18922  -6529   1367  -5933       C  
ATOM    246  CD2 LEU A  64       8.808  -8.153 -56.812  1.00193.42           C  
ANISOU  246  CD2 LEU A  64    23501  31332  18659  -5301   1065  -6253       C  
ATOM    247  N   LYS A  65       4.989  -4.419 -54.598  1.00125.88           N  
ANISOU  247  N   LYS A  65    17710  19943  10177  -5976   1413  -5246       N  
ATOM    248  CA  LYS A  65       4.063  -4.356 -53.477  1.00122.64           C  
ANISOU  248  CA  LYS A  65    17741  18931   9926  -5632   1407  -5145       C  
ATOM    249  C   LYS A  65       3.107  -3.184 -53.651  1.00130.53           C  
ANISOU  249  C   LYS A  65    19437  19251  10908  -5964   1527  -4882       C  
ATOM    250  O   LYS A  65       3.521  -2.075 -54.009  1.00114.44           O  
ANISOU  250  O   LYS A  65    17618  17219   8644  -6579   1633  -4800       O  
ATOM    251  CB  LYS A  65       4.816  -4.239 -52.147  1.00117.89           C  
ANISOU  251  CB  LYS A  65    17020  18543   9228  -5589   1402  -5272       C  
ATOM    252  CG  LYS A  65       5.715  -5.428 -51.852  1.00123.62           C  
ANISOU  252  CG  LYS A  65    17112  19890   9968  -5195   1265  -5524       C  
ATOM    253  CD  LYS A  65       4.953  -6.736 -51.996  1.00109.56           C  
ANISOU  253  CD  LYS A  65    15229  17951   8449  -4551   1128  -5551       C  
ATOM    254  CE  LYS A  65       5.890  -7.932 -51.987  1.00110.66           C  
ANISOU  254  CE  LYS A  65    14741  18711   8592  -4194    977  -5810       C  
ATOM    255  NZ  LYS A  65       6.635  -8.045 -50.706  1.00117.89           N  
ANISOU  255  NZ  LYS A  65    15500  19896   9398  -4053    934  -5932       N  
ATOM    256  N   ALA A  66       1.822  -3.439 -53.391  1.00130.83           N  
ANISOU  256  N   ALA A  66    19840  18692  11178  -5553   1511  -4749       N  
ATOM    257  CA  ALA A  66       0.729  -2.506 -53.597  1.00117.41           C  
ANISOU  257  CA  ALA A  66    18812  16284   9513  -5715   1599  -4497       C  
ATOM    258  C   ALA A  66       0.476  -1.681 -52.339  1.00124.93           C  
ANISOU  258  C   ALA A  66    20201  16811  10455  -5736   1663  -4435       C  
ATOM    259  O   ALA A  66       0.931  -2.041 -51.248  1.00131.98           O  
ANISOU  259  O   ALA A  66    20862  17925  11360  -5514   1633  -4578       O  
ATOM    260  CB  ALA A  66      -0.532  -3.271 -53.987  1.00120.73           C  
ANISOU  260  CB  ALA A  66    19347  16321  10203  -5222   1557  -4402       C  
ATOM    261  N   PRO A  67      -0.231  -0.551 -52.461  1.00131.06           N  
ANISOU  261  N   PRO A  67    21622  16978  11196  -5995   1744  -4228       N  
ATOM    262  CA  PRO A  67      -0.617   0.202 -51.255  1.00136.94           C  
ANISOU  262  CA  PRO A  67    22798  17263  11971  -5931   1795  -4180       C  
ATOM    263  C   PRO A  67      -1.463  -0.598 -50.283  1.00128.80           C  
ANISOU  263  C   PRO A  67    21728  16006  11205  -5258   1756  -4193       C  
ATOM    264  O   PRO A  67      -1.510  -0.247 -49.099  1.00124.27           O  
ANISOU  264  O   PRO A  67    21294  15285  10639  -5153   1783  -4231       O  
ATOM    265  CB  PRO A  67      -1.401   1.392 -51.824  1.00135.54           C  
ANISOU  265  CB  PRO A  67    23336  16416  11747  -6219   1852  -3937       C  
ATOM    266  CG  PRO A  67      -0.864   1.564 -53.200  1.00130.66           C  
ANISOU  266  CG  PRO A  67    22627  16090  10927  -6713   1857  -3891       C  
ATOM    267  CD  PRO A  67      -0.571   0.182 -53.695  1.00112.81           C  
ANISOU  267  CD  PRO A  67    19684  14408   8770  -6405   1782  -4039       C  
ATOM    268  N   GLN A  68      -2.138  -1.656 -50.740  1.00142.87           N  
ANISOU  268  N   GLN A  68    23325  17766  13191  -4821   1701  -4166       N  
ATOM    269  CA  GLN A  68      -2.923  -2.482 -49.831  1.00143.15           C  
ANISOU  269  CA  GLN A  68    23318  17614  13459  -4219   1675  -4166       C  
ATOM    270  C   GLN A  68      -2.045  -3.264 -48.863  1.00130.79           C  
ANISOU  270  C   GLN A  68    21281  16575  11838  -4037   1614  -4379       C  
ATOM    271  O   GLN A  68      -2.553  -3.782 -47.863  1.00131.43           O  
ANISOU  271  O   GLN A  68    21372  16523  12042  -3619   1605  -4379       O  
ATOM    272  CB  GLN A  68      -3.816  -3.431 -50.630  1.00135.88           C  
ANISOU  272  CB  GLN A  68    22321  16549  12759  -3848   1642  -4088       C  
ATOM    273  CG  GLN A  68      -4.758  -2.717 -51.587  1.00129.07           C  
ANISOU  273  CG  GLN A  68    21921  15172  11946  -3964   1690  -3867       C  
ATOM    274  CD  GLN A  68      -5.769  -3.652 -52.219  1.00129.51           C  
ANISOU  274  CD  GLN A  68    21912  15053  12244  -3543   1670  -3788       C  
ATOM    275  OE1 GLN A  68      -5.552  -4.861 -52.293  1.00134.33           O  
ANISOU  275  OE1 GLN A  68    22081  16008  12951  -3287   1613  -3926       O  
ATOM    276  NE2 GLN A  68      -6.890  -3.097 -52.665  1.00124.56           N  
ANISOU  276  NE2 GLN A  68    21731  13877  11718  -3451   1710  -3572       N  
ATOM    277  N   ASN A  69      -0.745  -3.353 -49.133  1.00105.26           N  
ANISOU  277  N   ASN A  69    17639  13947   8408  -4335   1571  -4551       N  
ATOM    278  CA  ASN A  69       0.211  -3.957 -48.214  1.00104.32           C  
ANISOU  278  CA  ASN A  69    17090  14353   8193  -4187   1501  -4754       C  
ATOM    279  C   ASN A  69       0.789  -2.956 -47.220  1.00112.35           C  
ANISOU  279  C   ASN A  69    18248  15410   9028  -4490   1567  -4800       C  
ATOM    280  O   ASN A  69       1.665  -3.325 -46.430  1.00112.29           O  
ANISOU  280  O   ASN A  69    17892  15869   8905  -4415   1515  -4967       O  
ATOM    281  CB  ASN A  69       1.346  -4.623 -48.999  1.00105.58           C  
ANISOU  281  CB  ASN A  69    16685  15186   8244  -4291   1410  -4931       C  
ATOM    282  CG  ASN A  69       0.890  -5.866 -49.744  1.00134.82           C  
ANISOU  282  CG  ASN A  69    20151  18936  12138  -3885   1315  -4958       C  
ATOM    283  OD1 ASN A  69      -0.307  -6.141 -49.839  1.00138.17           O  
ANISOU  283  OD1 ASN A  69    20858  18869  12770  -3603   1339  -4821       O  
ATOM    284  ND2 ASN A  69       1.843  -6.623 -50.278  1.00151.87           N  
ANISOU  284  ND2 ASN A  69    21780  21687  14234  -3848   1210  -5145       N  
ATOM    285  N   LEU A  70       0.322  -1.703 -47.239  1.00121.23           N  
ANISOU  285  N   LEU A  70    19890  16052  10121  -4818   1672  -4664       N  
ATOM    286  CA  LEU A  70       0.773  -0.729 -46.249  1.00132.72           C  
ANISOU  286  CA  LEU A  70    21522  17484  11423  -5093   1739  -4723       C  
ATOM    287  C   LEU A  70       0.378  -1.146 -44.839  1.00129.53           C  
ANISOU  287  C   LEU A  70    21096  17020  11101  -4638   1718  -4772       C  
ATOM    288  O   LEU A  70       1.102  -0.855 -43.878  1.00127.94           O  
ANISOU  288  O   LEU A  70    20762  17103  10746  -4750   1729  -4909       O  
ATOM    289  CB  LEU A  70       0.210   0.653 -46.573  1.00141.26           C  
ANISOU  289  CB  LEU A  70    23234  17964  12474  -5472   1838  -4563       C  
ATOM    290  CG  LEU A  70       1.202   1.727 -47.011  1.00140.87           C  
ANISOU  290  CG  LEU A  70    23281  18088  12156  -6185   1910  -4600       C  
ATOM    291  CD1 LEU A  70       1.993   1.262 -48.219  1.00155.89           C  
ANISOU  291  CD1 LEU A  70    24779  20507  13946  -6451   1882  -4638       C  
ATOM    292  CD2 LEU A  70       0.468   3.024 -47.314  1.00142.43           C  
ANISOU  292  CD2 LEU A  70    24205  17574  12337  -6476   1984  -4412       C  
ATOM    293  N   PHE A  71      -0.760  -1.830 -44.697  1.00132.05           N  
ANISOU  293  N   PHE A  71    21534  16996  11644  -4141   1696  -4658       N  
ATOM    294  CA  PHE A  71      -1.151  -2.348 -43.390  1.00122.39           C  
ANISOU  294  CA  PHE A  71    20261  15768  10473  -3712   1681  -4690       C  
ATOM    295  C   PHE A  71      -0.123  -3.336 -42.860  1.00125.37           C  
ANISOU  295  C   PHE A  71    20106  16810  10719  -3553   1583  -4874       C  
ATOM    296  O   PHE A  71       0.089  -3.424 -41.642  1.00133.26           O  
ANISOU  296  O   PHE A  71    21023  17987  11625  -3406   1577  -4952       O  
ATOM    297  CB  PHE A  71      -2.518  -3.025 -43.463  1.00113.30           C  
ANISOU  297  CB  PHE A  71    19291  14183   9576  -3235   1685  -4525       C  
ATOM    298  CG  PHE A  71      -3.600  -2.158 -44.030  1.00113.96           C  
ANISOU  298  CG  PHE A  71    19874  13621   9804  -3293   1758  -4331       C  
ATOM    299  CD1 PHE A  71      -4.206  -1.184 -43.254  1.00106.89           C  
ANISOU  299  CD1 PHE A  71    19365  12325   8925  -3286   1823  -4277       C  
ATOM    300  CD2 PHE A  71      -4.026  -2.333 -45.337  1.00111.60           C  
ANISOU  300  CD2 PHE A  71    19650  13132   9621  -3320   1748  -4211       C  
ATOM    301  CE1 PHE A  71      -5.211  -0.393 -43.777  1.00102.40           C  
ANISOU  301  CE1 PHE A  71    19258  11162   8488  -3275   1864  -4102       C  
ATOM    302  CE2 PHE A  71      -5.033  -1.544 -45.860  1.00116.07           C  
ANISOU  302  CE2 PHE A  71    20684  13114  10305  -3332   1798  -4021       C  
ATOM    303  CZ  PHE A  71      -5.623  -0.575 -45.079  1.00108.17           C  
ANISOU  303  CZ  PHE A  71    20073  11704   9322  -3292   1848  -3963       C  
ATOM    304  N   LEU A  72       0.536  -4.076 -43.755  1.00109.67           N  
ANISOU  304  N   LEU A  72    17747  15211   8710  -3567   1498  -4951       N  
ATOM    305  CA  LEU A  72       1.482  -5.092 -43.311  1.00107.28           C  
ANISOU  305  CA  LEU A  72    16945  15520   8296  -3341   1379  -5126       C  
ATOM    306  C   LEU A  72       2.681  -4.478 -42.603  1.00132.18           C  
ANISOU  306  C   LEU A  72    19898  19122  11202  -3647   1388  -5277       C  
ATOM    307  O   LEU A  72       3.284  -5.124 -41.739  1.00130.00           O  
ANISOU  307  O   LEU A  72    19317  19262  10816  -3407   1308  -5396       O  
ATOM    308  CB  LEU A  72       1.952  -5.940 -44.491  1.00103.43           C  
ANISOU  308  CB  LEU A  72    16097  15352   7849  -3289   1278  -5201       C  
ATOM    309  CG  LEU A  72       0.888  -6.701 -45.281  1.00107.22           C  
ANISOU  309  CG  LEU A  72    16692  15472   8575  -2982   1258  -5094       C  
ATOM    310  CD1 LEU A  72       1.550  -7.773 -46.134  1.00100.15           C  
ANISOU  310  CD1 LEU A  72    15327  15029   7697  -2830   1121  -5246       C  
ATOM    311  CD2 LEU A  72      -0.155  -7.305 -44.355  1.00 97.61           C  
ANISOU  311  CD2 LEU A  72    15688  13903   7497  -2530   1273  -5003       C  
ATOM    312  N   VAL A  73       3.049  -3.245 -42.956  1.00145.94           N  
ANISOU  312  N   VAL A  73    21818  20791  12843  -4189   1488  -5273       N  
ATOM    313  CA  VAL A  73       4.166  -2.602 -42.271  1.00151.76           C  
ANISOU  313  CA  VAL A  73    22378  21936  13345  -4526   1521  -5424       C  
ATOM    314  C   VAL A  73       3.702  -1.957 -40.969  1.00134.86           C  
ANISOU  314  C   VAL A  73    20541  19519  11180  -4479   1589  -5410       C  
ATOM    315  O   VAL A  73       4.484  -1.848 -40.017  1.00137.65           O  
ANISOU  315  O   VAL A  73    20677  20263  11362  -4531   1583  -5550       O  
ATOM    316  CB  VAL A  73       4.861  -1.582 -43.193  1.00160.82           C  
ANISOU  316  CB  VAL A  73    23570  23176  14360  -5183   1611  -5444       C  
ATOM    317  CG1 VAL A  73       4.926  -2.110 -44.618  1.00164.98           C  
ANISOU  317  CG1 VAL A  73    23913  23821  14952  -5218   1564  -5406       C  
ATOM    318  CG2 VAL A  73       4.172  -0.220 -43.144  1.00155.31           C  
ANISOU  318  CG2 VAL A  73    23480  21860  13672  -5547   1746  -5320       C  
ATOM    319  N   SER A  74       2.437  -1.531 -40.898  1.00115.25           N  
ANISOU  319  N   SER A  74    18539  16387   8863  -4366   1654  -5253       N  
ATOM    320  CA  SER A  74       1.907  -0.989 -39.652  1.00112.85           C  
ANISOU  320  CA  SER A  74    18498  15829   8550  -4259   1712  -5255       C  
ATOM    321  C   SER A  74       1.743  -2.090 -38.616  1.00116.70           C  
ANISOU  321  C   SER A  74    18735  16573   9033  -3732   1635  -5283       C  
ATOM    322  O   SER A  74       2.142  -1.931 -37.456  1.00119.14           O  
ANISOU  322  O   SER A  74    18937  17138   9191  -3707   1641  -5387       O  
ATOM    323  CB  SER A  74       0.575  -0.283 -39.907  1.00115.48           C  
ANISOU  323  CB  SER A  74    19392  15413   9073  -4228   1791  -5083       C  
ATOM    324  OG  SER A  74       0.029   0.220 -38.700  1.00127.65           O  
ANISOU  324  OG  SER A  74    21159  16731  10612  -4086   1840  -5107       O  
ATOM    325  N   LEU A  75       1.148  -3.216 -39.020  1.00116.74           N  
ANISOU  325  N   LEU A  75    18658  16511   9186  -3326   1568  -5187       N  
ATOM    326  CA  LEU A  75       1.100  -4.381 -38.146  1.00107.23           C  
ANISOU  326  CA  LEU A  75    17214  15590   7940  -2861   1488  -5209       C  
ATOM    327  C   LEU A  75       2.501  -4.838 -37.765  1.00111.49           C  
ANISOU  327  C   LEU A  75    17276  16831   8255  -2890   1387  -5386       C  
ATOM    328  O   LEU A  75       2.720  -5.293 -36.636  1.00115.58           O  
ANISOU  328  O   LEU A  75    17636  17643   8636  -2651   1345  -5434       O  
ATOM    329  CB  LEU A  75       0.332  -5.514 -38.826  1.00103.30           C  
ANISOU  329  CB  LEU A  75    16716  14900   7635  -2491   1437  -5098       C  
ATOM    330  CG  LEU A  75       0.174  -6.830 -38.060  1.00109.46           C  
ANISOU  330  CG  LEU A  75    17306  15911   8375  -2018   1358  -5104       C  
ATOM    331  CD1 LEU A  75      -0.733  -6.650 -36.852  1.00122.52           C  
ANISOU  331  CD1 LEU A  75    19222  17321  10009  -1836   1450  -5004       C  
ATOM    332  CD2 LEU A  75      -0.355  -7.921 -38.980  1.00 99.54           C  
ANISOU  332  CD2 LEU A  75    16013  14499   7310  -1747   1303  -5049       C  
ATOM    333  N   ALA A  76       3.462  -4.707 -38.683  1.00110.75           N  
ANISOU  333  N   ALA A  76    16938  17035   8108  -3187   1351  -5481       N  
ATOM    334  CA  ALA A  76       4.843  -5.060 -38.372  1.00116.24           C  
ANISOU  334  CA  ALA A  76    17153  18417   8596  -3234   1263  -5661       C  
ATOM    335  C   ALA A  76       5.477  -4.039 -37.435  1.00122.58           C  
ANISOU  335  C   ALA A  76    17961  19408   9206  -3572   1346  -5762       C  
ATOM    336  O   ALA A  76       6.155  -4.406 -36.467  1.00118.76           O  
ANISOU  336  O   ALA A  76    17188  19381   8555  -3425   1289  -5865       O  
ATOM    337  CB  ALA A  76       5.659  -5.186 -39.658  1.00114.70           C  
ANISOU  337  CB  ALA A  76    16671  18513   8399  -3473   1219  -5743       C  
ATOM    338  N   SER A  77       5.273  -2.746 -37.709  1.00131.90           N  
ANISOU  338  N   SER A  77    19474  20241  10401  -4032   1480  -5739       N  
ATOM    339  CA  SER A  77       5.822  -1.714 -36.836  1.00138.11           C  
ANISOU  339  CA  SER A  77    20304  21159  11013  -4385   1570  -5856       C  
ATOM    340  C   SER A  77       5.240  -1.805 -35.432  1.00139.94           C  
ANISOU  340  C   SER A  77    20652  21301  11216  -4058   1574  -5843       C  
ATOM    341  O   SER A  77       5.895  -1.412 -34.461  1.00147.87           O  
ANISOU  341  O   SER A  77    21511  22634  12039  -4190   1599  -5975       O  
ATOM    342  CB  SER A  77       5.568  -0.326 -37.426  1.00145.67           C  
ANISOU  342  CB  SER A  77    21685  21664  12001  -4925   1708  -5823       C  
ATOM    343  OG  SER A  77       4.182  -0.038 -37.481  1.00161.39           O  
ANISOU  343  OG  SER A  77    24166  22965  14189  -4747   1752  -5661       O  
ATOM    344  N   ALA A  78       4.015  -2.319 -35.304  1.00132.05           N  
ANISOU  344  N   ALA A  78    19898  19892  10383  -3648   1561  -5688       N  
ATOM    345  CA  ALA A  78       3.444  -2.545 -33.981  1.00124.31           C  
ANISOU  345  CA  ALA A  78    18982  18898   9352  -3317   1567  -5664       C  
ATOM    346  C   ALA A  78       4.120  -3.719 -33.283  1.00126.50           C  
ANISOU  346  C   ALA A  78    18824  19773   9467  -2976   1445  -5711       C  
ATOM    347  O   ALA A  78       4.350  -3.675 -32.068  1.00132.61           O  
ANISOU  347  O   ALA A  78    19491  20823  10072  -2892   1448  -5768       O  
ATOM    348  CB  ALA A  78       1.937  -2.775 -34.092  1.00118.36           C  
ANISOU  348  CB  ALA A  78    18591  17568   8810  -3005   1606  -5483       C  
ATOM    349  N   ASP A  79       4.454  -4.772 -34.037  1.00124.33           N  
ANISOU  349  N   ASP A  79    18293  19713   9234  -2771   1328  -5695       N  
ATOM    350  CA  ASP A  79       5.119  -5.928 -33.444  1.00132.99           C  
ANISOU  350  CA  ASP A  79    18984  21366  10180  -2420   1186  -5746       C  
ATOM    351  C   ASP A  79       6.503  -5.560 -32.926  1.00133.27           C  
ANISOU  351  C   ASP A  79    18648  21998   9989  -2665   1165  -5932       C  
ATOM    352  O   ASP A  79       6.904  -5.998 -31.840  1.00128.56           O  
ANISOU  352  O   ASP A  79    17822  21809   9214  -2451   1102  -5972       O  
ATOM    353  CB  ASP A  79       5.212  -7.067 -34.461  1.00143.93           C  
ANISOU  353  CB  ASP A  79    20174  22835  11677  -2158   1055  -5732       C  
ATOM    354  CG  ASP A  79       3.857  -7.650 -34.812  1.00164.10           C  
ANISOU  354  CG  ASP A  79    23039  24877  14436  -1855   1068  -5562       C  
ATOM    355  OD1 ASP A  79       3.075  -7.938 -33.883  1.00159.64           O  
ANISOU  355  OD1 ASP A  79    22632  24186  13836  -1596   1096  -5459       O  
ATOM    356  OD2 ASP A  79       3.569  -7.813 -36.016  1.00168.15           O  
ANISOU  356  OD2 ASP A  79    23619  25136  15133  -1894   1062  -5533       O  
ATOM    357  N   ILE A  80       7.257  -4.769 -33.695  1.00123.20           N  
ANISOU  357  N   ILE A  80    17292  20812   8705  -3129   1220  -6045       N  
ATOM    358  CA  ILE A  80       8.549  -4.290 -33.212  1.00127.44           C  
ANISOU  358  CA  ILE A  80    17483  21913   9026  -3434   1234  -6237       C  
ATOM    359  C   ILE A  80       8.362  -3.438 -31.964  1.00143.92           C  
ANISOU  359  C   ILE A  80    19746  23938  10997  -3575   1337  -6270       C  
ATOM    360  O   ILE A  80       9.120  -3.554 -30.993  1.00152.72           O  
ANISOU  360  O   ILE A  80    20551  25560  11914  -3537   1306  -6383       O  
ATOM    361  CB  ILE A  80       9.288  -3.516 -34.321  1.00129.44           C  
ANISOU  361  CB  ILE A  80    17657  22244   9279  -3975   1308  -6339       C  
ATOM    362  CG1 ILE A  80       9.764  -4.470 -35.412  1.00134.76           C  
ANISOU  362  CG1 ILE A  80    17998  23192  10013  -3812   1187  -6366       C  
ATOM    363  CG2 ILE A  80      10.463  -2.739 -33.743  1.00134.13           C  
ANISOU  363  CG2 ILE A  80    17982  23334   9648  -4399   1380  -6538       C  
ATOM    364  CD1 ILE A  80      10.491  -3.782 -36.549  1.00137.83           C  
ANISOU  364  CD1 ILE A  80    18268  23723  10377  -4350   1266  -6455       C  
ATOM    365  N   LEU A  81       7.335  -2.585 -31.962  1.00135.50           N  
ANISOU  365  N   LEU A  81    19166  22262  10055  -3718   1456  -6183       N  
ATOM    366  CA  LEU A  81       7.067  -1.746 -30.799  1.00129.36           C  
ANISOU  366  CA  LEU A  81    18574  21391   9184  -3831   1551  -6237       C  
ATOM    367  C   LEU A  81       6.690  -2.574 -29.576  1.00128.56           C  
ANISOU  367  C   LEU A  81    18364  21494   8989  -3348   1485  -6171       C  
ATOM    368  O   LEU A  81       6.892  -2.126 -28.443  1.00130.92           O  
ANISOU  368  O   LEU A  81    18609  22003   9132  -3411   1529  -6261       O  
ATOM    369  CB  LEU A  81       5.962  -0.740 -31.125  1.00131.20           C  
ANISOU  369  CB  LEU A  81    19357  20903   9590  -4016   1671  -6165       C  
ATOM    370  CG  LEU A  81       6.395   0.691 -31.455  1.00133.51           C  
ANISOU  370  CG  LEU A  81    19849  21031   9845  -4637   1795  -6298       C  
ATOM    371  CD1 LEU A  81       7.435   0.711 -32.565  1.00139.32           C  
ANISOU  371  CD1 LEU A  81    20340  22058  10536  -5008   1788  -6356       C  
ATOM    372  CD2 LEU A  81       5.189   1.537 -31.834  1.00129.98           C  
ANISOU  372  CD2 LEU A  81    19977  19820   9589  -4722   1882  -6204       C  
ATOM    373  N   VAL A  82       6.146  -3.780 -29.778  1.00137.93           N  
ANISOU  373  N   VAL A  82    19515  22640  10252  -2886   1382  -6015       N  
ATOM    374  CA  VAL A  82       5.784  -4.643 -28.653  1.00137.45           C  
ANISOU  374  CA  VAL A  82    19352  22803  10071  -2447   1317  -5924       C  
ATOM    375  C   VAL A  82       6.951  -5.499 -28.181  1.00133.48           C  
ANISOU  375  C   VAL A  82    18338  23018   9360  -2271   1172  -6006       C  
ATOM    376  O   VAL A  82       6.888  -6.064 -27.078  1.00128.44           O  
ANISOU  376  O   VAL A  82    17560  22684   8557  -1976   1114  -5950       O  
ATOM    377  CB  VAL A  82       4.580  -5.540 -29.015  1.00129.13           C  
ANISOU  377  CB  VAL A  82    18522  21368   9174  -2049   1284  -5715       C  
ATOM    378  CG1 VAL A  82       5.036  -6.918 -29.474  1.00124.12           C  
ANISOU  378  CG1 VAL A  82    17574  21066   8521  -1710   1108  -5683       C  
ATOM    379  CG2 VAL A  82       3.622  -5.656 -27.839  1.00125.34           C  
ANISOU  379  CG2 VAL A  82    18207  20802   8615  -1801   1336  -5597       C  
ATOM    380  N   ALA A  83       8.021  -5.596 -28.969  1.00129.15           N  
ANISOU  380  N   ALA A  83    17486  22785   8801  -2440   1109  -6139       N  
ATOM    381  CA  ALA A  83       9.211  -6.354 -28.607  1.00132.03           C  
ANISOU  381  CA  ALA A  83    17324  23866   8976  -2268    963  -6255       C  
ATOM    382  C   ALA A  83      10.267  -5.524 -27.892  1.00142.82           C  
ANISOU  382  C   ALA A  83    18425  25697  10145  -2627   1029  -6453       C  
ATOM    383  O   ALA A  83      11.038  -6.076 -27.099  1.00148.07           O  
ANISOU  383  O   ALA A  83    18688  26962  10610  -2424    925  -6527       O  
ATOM    384  CB  ALA A  83       9.837  -6.988 -29.855  1.00131.89           C  
ANISOU  384  CB  ALA A  83    17050  24014   9047  -2220    852  -6324       C  
ATOM    385  N   THR A  84      10.337  -4.219 -28.154  1.00149.49           N  
ANISOU  385  N   THR A  84    19473  26297  11028  -3154   1194  -6548       N  
ATOM    386  CA  THR A  84      11.342  -3.376 -27.523  1.00164.86           C  
ANISOU  386  CA  THR A  84    21174  28680  12785  -3550   1273  -6759       C  
ATOM    387  C   THR A  84      10.784  -2.524 -26.397  1.00164.03           C  
ANISOU  387  C   THR A  84    21334  28375  12617  -3674   1391  -6770       C  
ATOM    388  O   THR A  84      11.565  -1.964 -25.618  1.00162.07           O  
ANISOU  388  O   THR A  84    20852  28543  12185  -3926   1444  -6947       O  
ATOM    389  CB  THR A  84      12.005  -2.452 -28.554  1.00173.02           C  
ANISOU  389  CB  THR A  84    22198  29688  13855  -4130   1379  -6900       C  
ATOM    390  OG1 THR A  84      12.972  -1.623 -27.896  1.00192.69           O  
ANISOU  390  OG1 THR A  84    24449  32620  16146  -4547   1472  -7116       O  
ATOM    391  CG2 THR A  84      10.968  -1.560 -29.226  1.00157.30           C  
ANISOU  391  CG2 THR A  84    20782  26923  12060  -4390   1504  -6798       C  
ATOM    392  N   LEU A  85       9.459  -2.424 -26.286  1.00157.74           N  
ANISOU  392  N   LEU A  85    20989  26983  11961  -3495   1436  -6605       N  
ATOM    393  CA  LEU A  85       8.835  -1.504 -25.348  1.00140.27           C  
ANISOU  393  CA  LEU A  85    19061  24522   9715  -3626   1557  -6642       C  
ATOM    394  C   LEU A  85       7.764  -2.165 -24.489  1.00141.46           C  
ANISOU  394  C   LEU A  85    19349  24540   9859  -3149   1522  -6460       C  
ATOM    395  O   LEU A  85       7.103  -1.467 -23.712  1.00138.50           O  
ANISOU  395  O   LEU A  85    19211  23947   9466  -3200   1619  -6486       O  
ATOM    396  CB  LEU A  85       8.219  -0.320 -26.112  1.00139.57           C  
ANISOU  396  CB  LEU A  85    19450  23776   9806  -4009   1691  -6669       C  
ATOM    397  CG  LEU A  85       8.862   1.062 -25.944  1.00143.71           C  
ANISOU  397  CG  LEU A  85    20031  24334  10238  -4598   1822  -6902       C  
ATOM    398  CD1 LEU A  85      10.379   0.982 -25.977  1.00147.36           C  
ANISOU  398  CD1 LEU A  85    19988  25489  10514  -4875   1802  -7073       C  
ATOM    399  CD2 LEU A  85       8.357   2.032 -27.011  1.00143.08           C  
ANISOU  399  CD2 LEU A  85    20416  23610  10339  -4965   1919  -6892       C  
ATOM    400  N   VAL A  86       7.561  -3.478 -24.605  1.00162.34           N  
ANISOU  400  N   VAL A  86    21851  27325  12506  -2698   1389  -6285       N  
ATOM    401  CA  VAL A  86       6.487  -4.139 -23.870  1.00172.38           C  
ANISOU  401  CA  VAL A  86    23266  28475  13756  -2283   1368  -6085       C  
ATOM    402  C   VAL A  86       6.994  -5.397 -23.174  1.00180.40           C  
ANISOU  402  C   VAL A  86    23878  30102  14564  -1888   1202  -5998       C  
ATOM    403  O   VAL A  86       6.884  -5.524 -21.949  1.00187.30           O  
ANISOU  403  O   VAL A  86    24637  31280  15247  -1745   1196  -5956       O  
ATOM    404  CB  VAL A  86       5.306  -4.468 -24.800  1.00167.77           C  
ANISOU  404  CB  VAL A  86    23054  27278  13412  -2108   1385  -5905       C  
ATOM    405  CG1 VAL A  86       4.282  -5.308 -24.064  1.00150.42           C  
ANISOU  405  CG1 VAL A  86    20937  25058  11157  -1684   1359  -5688       C  
ATOM    406  CG2 VAL A  86       4.663  -3.191 -25.319  1.00174.04           C  
ANISOU  406  CG2 VAL A  86    24270  27464  14395  -2441   1535  -5973       C  
ATOM    407  N   ILE A  87       7.546  -6.335 -23.939  1.00178.00           N  
ANISOU  407  N   ILE A  87    23347  29998  14286  -1693   1053  -5974       N  
ATOM    408  CA  ILE A  87       7.963  -7.624 -23.385  1.00171.74           C  
ANISOU  408  CA  ILE A  87    22198  29752  13303  -1239    853  -5883       C  
ATOM    409  C   ILE A  87       9.184  -7.510 -22.468  1.00168.93           C  
ANISOU  409  C   ILE A  87    21390  30103  12693  -1305    797  -6045       C  
ATOM    410  O   ILE A  87       9.281  -8.303 -21.519  1.00181.08           O  
ANISOU  410  O   ILE A  87    22704  32080  14018   -942    665  -5937       O  
ATOM    411  CB  ILE A  87       8.186  -8.660 -24.506  1.00174.18           C  
ANISOU  411  CB  ILE A  87    22394  30064  13724   -965    687  -5849       C  
ATOM    412  CG1 ILE A  87       8.563 -10.030 -23.930  1.00174.47           C  
ANISOU  412  CG1 ILE A  87    22093  30643  13553   -414    436  -5751       C  
ATOM    413  CG2 ILE A  87       9.225  -8.206 -25.510  1.00169.32           C  
ANISOU  413  CG2 ILE A  87    21579  29558  13194  -1296    699  -6075       C  
ATOM    414  CD1 ILE A  87       7.498 -10.640 -23.047  1.00168.13           C  
ANISOU  414  CD1 ILE A  87    21481  29763  12637    -54    393  -5470       C  
ATOM    415  N   PRO A  88      10.129  -6.571 -22.655  1.00154.86           N  
ANISOU  415  N   PRO A  88    19445  28497  10899  -1747    886  -6292       N  
ATOM    416  CA  PRO A  88      11.237  -6.514 -21.684  1.00162.41           C  
ANISOU  416  CA  PRO A  88    19940  30171  11597  -1786    838  -6448       C  
ATOM    417  C   PRO A  88      10.791  -6.095 -20.295  1.00167.30           C  
ANISOU  417  C   PRO A  88    20622  30885  12059  -1796    917  -6405       C  
ATOM    418  O   PRO A  88      11.297  -6.632 -19.301  1.00161.37           O  
ANISOU  418  O   PRO A  88    19516  30730  11067  -1557    807  -6393       O  
ATOM    419  CB  PRO A  88      12.204  -5.493 -22.305  1.00160.67           C  
ANISOU  419  CB  PRO A  88    19586  30045  11415  -2328    950  -6717       C  
ATOM    420  CG  PRO A  88      11.827  -5.423 -23.734  1.00148.53           C  
ANISOU  420  CG  PRO A  88    18322  27984  10130  -2444    979  -6676       C  
ATOM    421  CD  PRO A  88      10.348  -5.585 -23.730  1.00143.20           C  
ANISOU  421  CD  PRO A  88    18134  26672   9603  -2226   1016  -6440       C  
ATOM    422  N   PHE A  89       9.857  -5.145 -20.194  1.00166.35           N  
ANISOU  422  N   PHE A  89    20928  30216  12060  -2047   1095  -6392       N  
ATOM    423  CA  PHE A  89       9.365  -4.735 -18.882  1.00172.99           C  
ANISOU  423  CA  PHE A  89    21820  31148  12759  -2044   1173  -6370       C  
ATOM    424  C   PHE A  89       8.626  -5.874 -18.191  1.00182.25           C  
ANISOU  424  C   PHE A  89    22978  32456  13814  -1536   1055  -6082       C  
ATOM    425  O   PHE A  89       8.775  -6.078 -16.981  1.00199.71           O  
ANISOU  425  O   PHE A  89    24952  35140  15789  -1402   1014  -6045       O  
ATOM    426  CB  PHE A  89       8.455  -3.513 -19.012  1.00175.01           C  
ANISOU  426  CB  PHE A  89    22548  30765  13185  -2362   1370  -6435       C  
ATOM    427  CG  PHE A  89       9.187  -2.228 -19.289  1.00176.27           C  
ANISOU  427  CG  PHE A  89    22716  30885  13374  -2901   1492  -6725       C  
ATOM    428  CD1 PHE A  89      10.570  -2.197 -19.363  1.00179.19           C  
ANISOU  428  CD1 PHE A  89    22658  31808  13616  -3110   1448  -6909       C  
ATOM    429  CD2 PHE A  89       8.484  -1.049 -19.475  1.00170.99           C  
ANISOU  429  CD2 PHE A  89    22477  29645  12848  -3200   1646  -6818       C  
ATOM    430  CE1 PHE A  89      11.238  -1.013 -19.619  1.00179.90           C  
ANISOU  430  CE1 PHE A  89    22754  31890  13711  -3651   1573  -7167       C  
ATOM    431  CE2 PHE A  89       9.146   0.138 -19.729  1.00172.73           C  
ANISOU  431  CE2 PHE A  89    22733  29825  13073  -3718   1753  -7075       C  
ATOM    432  CZ  PHE A  89      10.524   0.156 -19.802  1.00178.43           C  
ANISOU  432  CZ  PHE A  89    23029  31108  13656  -3967   1725  -7243       C  
ATOM    433  N   SER A  90       7.819  -6.625 -18.945  1.00171.71           N  
ANISOU  433  N   SER A  90    21887  30732  12625  -1262    996  -5868       N  
ATOM    434  CA  SER A  90       7.119  -7.770 -18.369  1.00168.68           C  
ANISOU  434  CA  SER A  90    21494  30490  12106   -787    869  -5566       C  
ATOM    435  C   SER A  90       8.098  -8.859 -17.953  1.00165.03           C  
ANISOU  435  C   SER A  90    20577  30727  11400   -429    628  -5512       C  
ATOM    436  O   SER A  90       7.892  -9.532 -16.937  1.00158.99           O  
ANISOU  436  O   SER A  90    19679  30336  10394   -113    519  -5304       O  
ATOM    437  CB  SER A  90       6.101  -8.322 -19.367  1.00168.67           C  
ANISOU  437  CB  SER A  90    21839  29931  12317   -596    857  -5374       C  
ATOM    438  OG  SER A  90       5.184  -7.321 -19.770  1.00170.87           O  
ANISOU  438  OG  SER A  90    22532  29574  12817   -885   1067  -5427       O  
ATOM    439  N   LEU A  91       9.161  -9.054 -18.737  1.00163.49           N  
ANISOU  439  N   LEU A  91    20131  30737  11251   -454    531  -5690       N  
ATOM    440  CA  LEU A  91      10.206  -9.996 -18.354  1.00170.92           C  
ANISOU  440  CA  LEU A  91    20602  32384  11957    -95    293  -5698       C  
ATOM    441  C   LEU A  91      10.832  -9.596 -17.024  1.00184.61           C  
ANISOU  441  C   LEU A  91    22014  34705  13424   -193    316  -5788       C  
ATOM    442  O   LEU A  91      11.020 -10.435 -16.137  1.00181.13           O  
ANISOU  442  O   LEU A  91    21333  34771  12719    209    136  -5623       O  
ATOM    443  CB  LEU A  91      11.263 -10.077 -19.459  1.00163.38           C  
ANISOU  443  CB  LEU A  91    19403  31561  11113   -174    222  -5936       C  
ATOM    444  CG  LEU A  91      12.476 -11.011 -19.338  1.00164.66           C  
ANISOU  444  CG  LEU A  91    19040  32448  11073    213    -33  -6024       C  
ATOM    445  CD1 LEU A  91      13.652 -10.339 -18.630  1.00173.67           C  
ANISOU  445  CD1 LEU A  91    19749  34208  12032    -68     28  -6283       C  
ATOM    446  CD2 LEU A  91      12.110 -12.323 -18.651  1.00171.30           C  
ANISOU  446  CD2 LEU A  91    19845  33543  11698    874   -295  -5724       C  
ATOM    447  N   ALA A  92      11.160  -8.312 -16.869  1.00195.77           N  
ANISOU  447  N   ALA A  92    23427  36065  14893   -716    525  -6042       N  
ATOM    448  CA  ALA A  92      11.759  -7.845 -15.624  1.00198.69           C  
ANISOU  448  CA  ALA A  92    23479  36991  15021   -850    562  -6167       C  
ATOM    449  C   ALA A  92      10.805  -8.030 -14.451  1.00184.98           C  
ANISOU  449  C   ALA A  92    21873  35277  13132   -659    575  -5925       C  
ATOM    450  O   ALA A  92      11.200  -8.512 -13.385  1.00194.09           O  
ANISOU  450  O   ALA A  92    22698  37044  14005   -424    459  -5848       O  
ATOM    451  CB  ALA A  92      12.174  -6.381 -15.760  1.00203.33           C  
ANISOU  451  CB  ALA A  92    24107  37438  15712  -1463    784  -6484       C  
ATOM    452  N   ASN A  93       9.533  -7.667 -14.636  1.00166.02           N  
ANISOU  452  N   ASN A  93    19936  32242  10904   -747    713  -5796       N  
ATOM    453  CA  ASN A  93       8.538  -7.845 -13.583  1.00169.40           C  
ANISOU  453  CA  ASN A  93    20483  32692  11191   -580    738  -5558       C  
ATOM    454  C   ASN A  93       8.315  -9.312 -13.236  1.00166.67           C  
ANISOU  454  C   ASN A  93    20025  32664  10636    -26    499  -5185       C  
ATOM    455  O   ASN A  93       7.819  -9.608 -12.143  1.00166.91           O  
ANISOU  455  O   ASN A  93    20006  32965  10446    137    470  -4963       O  
ATOM    456  CB  ASN A  93       7.217  -7.196 -14.001  1.00167.76           C  
ANISOU  456  CB  ASN A  93    20779  31738  11225   -757    929  -5514       C  
ATOM    457  CG  ASN A  93       7.195  -5.699 -13.753  1.00169.35           C  
ANISOU  457  CG  ASN A  93    21105  31720  11521  -1228   1148  -5821       C  
ATOM    458  OD1 ASN A  93       8.239  -5.063 -13.624  1.00179.51           O  
ANISOU  458  OD1 ASN A  93    22151  33298  12757  -1508   1177  -6095       O  
ATOM    459  ND2 ASN A  93       5.996  -5.129 -13.678  1.00158.46           N  
ANISOU  459  ND2 ASN A  93    20098  29844  10267  -1305   1296  -5784       N  
ATOM    460  N   GLU A  94       8.676 -10.231 -14.132  1.00155.11           N  
ANISOU  460  N   GLU A  94    18525  31190   9222    274    312  -5106       N  
ATOM    461  CA  GLU A  94       8.509 -11.659 -13.892  1.00155.81           C  
ANISOU  461  CA  GLU A  94    18551  31548   9103    851     38  -4740       C  
ATOM    462  C   GLU A  94       9.677 -12.274 -13.133  1.00166.45           C  
ANISOU  462  C   GLU A  94    19418  33686  10138   1147   -185  -4747       C  
ATOM    463  O   GLU A  94       9.476 -13.239 -12.384  1.00164.44           O  
ANISOU  463  O   GLU A  94    19106  33759   9614   1584   -396  -4394       O  
ATOM    464  CB  GLU A  94       8.314 -12.397 -15.221  1.00152.69           C  
ANISOU  464  CB  GLU A  94    18355  30757   8906   1101    -91  -4665       C  
ATOM    465  CG  GLU A  94       8.057 -13.897 -15.097  1.00156.15           C  
ANISOU  465  CG  GLU A  94    18818  31367   9146   1744   -415  -4258       C  
ATOM    466  CD  GLU A  94       6.965 -14.230 -14.100  1.00164.02           C  
ANISOU  466  CD  GLU A  94    20012  32361   9946   1885   -420  -3825       C  
ATOM    467  OE1 GLU A  94       7.190 -15.105 -13.235  1.00163.56           O  
ANISOU  467  OE1 GLU A  94    19798  32773   9573   2284   -667  -3512       O  
ATOM    468  OE2 GLU A  94       5.888 -13.604 -14.168  1.00162.79           O  
ANISOU  468  OE2 GLU A  94    20161  31744   9946   1594   -181  -3786       O  
ATOM    469  N   VAL A  95      10.886 -11.746 -13.296  1.00185.56           N  
ANISOU  469  N   VAL A  95    21495  36435  12572    927   -152  -5116       N  
ATOM    470  CA  VAL A  95      12.077 -12.327 -12.677  1.00199.85           C  
ANISOU  470  CA  VAL A  95    22807  39032  14095   1231   -363  -5169       C  
ATOM    471  C   VAL A  95      12.507 -11.555 -11.434  1.00214.59           C  
ANISOU  471  C   VAL A  95    24382  41390  15762    950   -235  -5315       C  
ATOM    472  O   VAL A  95      12.752 -12.148 -10.383  1.00217.13           O  
ANISOU  472  O   VAL A  95    24451  42280  15769   1271   -390  -5131       O  
ATOM    473  CB  VAL A  95      13.231 -12.435 -13.701  1.00193.68           C  
ANISOU  473  CB  VAL A  95    21749  38414  13425   1248   -448  -5480       C  
ATOM    474  CG1 VAL A  95      12.912 -13.490 -14.752  1.00185.86           C  
ANISOU  474  CG1 VAL A  95    20960  37098  12559   1689   -661  -5313       C  
ATOM    475  CG2 VAL A  95      13.520 -11.095 -14.363  1.00189.11           C  
ANISOU  475  CG2 VAL A  95    21215  37532  13106    584   -167  -5848       C  
ATOM    476  N   MET A  96      12.604 -10.230 -11.526  1.00221.06           N  
ANISOU  476  N   MET A  96    25243  41999  16751    364     34  -5633       N  
ATOM    477  CA  MET A  96      13.072  -9.418 -10.412  1.00223.12           C  
ANISOU  477  CA  MET A  96    25216  42719  16840     69    154  -5826       C  
ATOM    478  C   MET A  96      11.932  -8.885  -9.554  1.00229.90           C  
ANISOU  478  C   MET A  96    26346  43324  17680    -96    313  -5687       C  
ATOM    479  O   MET A  96      12.176  -8.089  -8.641  1.00248.31           O  
ANISOU  479  O   MET A  96    28486  45961  19899   -378    435  -5873       O  
ATOM    480  CB  MET A  96      13.929  -8.252 -10.924  1.00220.41           C  
ANISOU  480  CB  MET A  96    24738  42357  16652   -473    331  -6263       C  
ATOM    481  CG  MET A  96      13.136  -7.052 -11.415  1.00213.27           C  
ANISOU  481  CG  MET A  96    24295  40706  16033   -973    590  -6389       C  
ATOM    482  SD  MET A  96      14.174  -5.612 -11.724  1.00212.87           S  
ANISOU  482  SD  MET A  96    24077  40735  16070  -1635    785  -6862       S  
ATOM    483  CE  MET A  96      12.933  -4.382 -12.113  1.00206.61           C  
ANISOU  483  CE  MET A  96    23926  39013  15562  -2054   1038  -6905       C  
ATOM    484  N   GLY A  97      10.702  -9.320  -9.812  1.00221.81           N  
ANISOU  484  N   GLY A  97    25734  41791  16754     81    310  -5378       N  
ATOM    485  CA  GLY A  97       9.546  -8.785  -9.129  1.00223.07           C  
ANISOU  485  CA  GLY A  97    26154  41678  16924    -81    475  -5270       C  
ATOM    486  C   GLY A  97       9.003  -7.558  -9.834  1.00226.23           C  
ANISOU  486  C   GLY A  97    26926  41380  17652   -537    727  -5527       C  
ATOM    487  O   GLY A  97       9.646  -6.946 -10.687  1.00214.59           O  
ANISOU  487  O   GLY A  97    25469  39703  16363   -816    795  -5811       O  
ATOM    488  N   TYR A  98       7.781  -7.183  -9.461  1.00238.82           N  
ANISOU  488  N   TYR A  98    28822  42616  19302   -606    862  -5417       N  
ATOM    489  CA  TYR A  98       7.103  -6.062 -10.111  1.00243.37           C  
ANISOU  489  CA  TYR A  98    29803  42490  20177   -957   1081  -5627       C  
ATOM    490  C   TYR A  98       7.645  -4.728  -9.591  1.00242.39           C  
ANISOU  490  C   TYR A  98    29563  42486  20048  -1388   1237  -6024       C  
ATOM    491  O   TYR A  98       6.931  -3.902  -9.026  1.00253.78           O  
ANISOU  491  O   TYR A  98    31167  43744  21513  -1561   1386  -6132       O  
ATOM    492  CB  TYR A  98       5.596  -6.167  -9.914  1.00245.16           C  
ANISOU  492  CB  TYR A  98    30365  42329  20457   -833   1159  -5386       C  
ATOM    493  N   TRP A  99       8.947  -4.524  -9.802  1.00226.45           N  
ANISOU  493  N   TRP A  99    27247  40805  17989  -1560   1196  -6256       N  
ATOM    494  CA  TRP A  99       9.614  -3.296  -9.372  1.00214.95           C  
ANISOU  494  CA  TRP A  99    25649  39517  16506  -1998   1332  -6638       C  
ATOM    495  C   TRP A  99       9.499  -2.260 -10.485  1.00189.29           C  
ANISOU  495  C   TRP A  99    22790  35584  13547  -2377   1480  -6861       C  
ATOM    496  O   TRP A  99      10.442  -1.982 -11.229  1.00185.03           O  
ANISOU  496  O   TRP A  99    22150  35077  13074  -2614   1478  -7041       O  
ATOM    497  CB  TRP A  99      11.066  -3.570  -9.003  1.00221.69           C  
ANISOU  497  CB  TRP A  99    25955  41131  17144  -2017   1223  -6776       C  
ATOM    498  N   TYR A 100       8.310  -1.675 -10.588  1.00166.08           N  
ANISOU  498  N   TYR A 100    20292  32043  10768  -2429   1605  -6845       N  
ATOM    499  CA  TYR A 100       8.085  -0.602 -11.546  1.00164.18           C  
ANISOU  499  CA  TYR A 100    20463  31135  10782  -2770   1740  -7049       C  
ATOM    500  C   TYR A 100       8.751   0.675 -11.056  1.00168.37           C  
ANISOU  500  C   TYR A 100    20904  31824  11244  -3226   1861  -7431       C  
ATOM    501  O   TYR A 100       8.572   1.073  -9.901  1.00171.14           O  
ANISOU  501  O   TYR A 100    21125  32462  11440  -3258   1914  -7544       O  
ATOM    502  CB  TYR A 100       6.589  -0.370 -11.740  1.00160.94           C  
ANISOU  502  CB  TYR A 100    20533  30075  10543  -2638   1823  -6931       C  
ATOM    503  N   PHE A 101       9.515   1.326 -11.931  1.00170.10           N  
ANISOU  503  N   PHE A 101    21185  31876  11569  -3599   1909  -7632       N  
ATOM    504  CA  PHE A 101      10.244   2.530 -11.539  1.00186.92           C  
ANISOU  504  CA  PHE A 101    23225  34178  13618  -4084   2028  -8000       C  
ATOM    505  C   PHE A 101       9.390   3.740 -11.897  1.00186.40           C  
ANISOU  505  C   PHE A 101    23714  33374  13735  -4331   2170  -8161       C  
ATOM    506  O   PHE A 101       9.422   4.247 -13.022  1.00178.05           O  
ANISOU  506  O   PHE A 101    22975  31816  12860  -4575   2213  -8210       O  
ATOM    507  CB  PHE A 101      11.612   2.579 -12.204  1.00191.10           C  
ANISOU  507  CB  PHE A 101    23466  35030  14114  -4392   2007  -8138       C  
ATOM    508  CG  PHE A 101      12.633   1.679 -11.564  1.00189.29           C  
ANISOU  508  CG  PHE A 101    22614  35660  13647  -4209   1880  -8103       C  
ATOM    509  CD1 PHE A 101      12.244   0.587 -10.805  1.00184.80           C  
ANISOU  509  CD1 PHE A 101    21844  35423  12950  -3709   1750  -7846       C  
ATOM    510  CD2 PHE A 101      13.987   1.921 -11.725  1.00191.95           C  
ANISOU  510  CD2 PHE A 101    22559  36500  13872  -4536   1888  -8325       C  
ATOM    511  CE1 PHE A 101      13.180  -0.244 -10.218  1.00191.81           C  
ANISOU  511  CE1 PHE A 101    22171  37103  13604  -3505   1613  -7810       C  
ATOM    512  CE2 PHE A 101      14.930   1.097 -11.140  1.00195.37           C  
ANISOU  512  CE2 PHE A 101    22401  37749  14081  -4329   1760  -8311       C  
ATOM    513  CZ  PHE A 101      14.526   0.012 -10.386  1.00197.91           C  
ANISOU  513  CZ  PHE A 101    22548  38371  14278  -3796   1614  -8053       C  
ATOM    514  N   GLY A 102       8.619   4.209 -10.923  1.00190.12           N  
ANISOU  514  N   GLY A 102    24294  33797  14146  -4257   2234  -8250       N  
ATOM    515  CA  GLY A 102       7.723   5.339 -11.100  1.00189.55           C  
ANISOU  515  CA  GLY A 102    24739  33056  14224  -4409   2348  -8428       C  
ATOM    516  C   GLY A 102       6.319   4.910 -11.464  1.00177.38           C  
ANISOU  516  C   GLY A 102    23565  30977  12855  -4008   2323  -8179       C  
ATOM    517  O   GLY A 102       6.082   3.828 -11.997  1.00169.55           O  
ANISOU  517  O   GLY A 102    22534  29960  11928  -3700   2231  -7863       O  
ATOM    518  N   LYS A 103       5.361   5.784 -11.151  1.00170.69           N  
ANISOU  518  N   LYS A 103    23072  29707  12075  -4004   2406  -8344       N  
ATOM    519  CA  LYS A 103       3.982   5.516 -11.538  1.00166.87           C  
ANISOU  519  CA  LYS A 103    22949  28692  11762  -3646   2396  -8151       C  
ATOM    520  C   LYS A 103       3.805   5.660 -13.042  1.00170.35           C  
ANISOU  520  C   LYS A 103    23788  28473  12465  -3722   2383  -8066       C  
ATOM    521  O   LYS A 103       2.993   4.947 -13.646  1.00181.19           O  
ANISOU  521  O   LYS A 103    25320  29548  13976  -3405   2339  -7796       O  
ATOM    522  CB  LYS A 103       3.026   6.447 -10.795  1.00169.08           C  
ANISOU  522  CB  LYS A 103    23477  28730  12036  -3596   2477  -8390       C  
ATOM    523  CG  LYS A 103       1.625   5.884 -10.635  1.00166.06           C  
ANISOU  523  CG  LYS A 103    23229  28155  11711  -3144   2465  -8171       C  
ATOM    524  CD  LYS A 103       0.571   6.983 -10.555  1.00167.42           C  
ANISOU  524  CD  LYS A 103    23834  27782  11997  -3094   2530  -8429       C  
ATOM    525  CE  LYS A 103       0.914   8.014  -9.500  1.00172.86           C  
ANISOU  525  CE  LYS A 103    24438  28715  12526  -3326   2593  -8826       C  
ATOM    526  NZ  LYS A 103      -0.102   9.100  -9.441  1.00174.65           N  
ANISOU  526  NZ  LYS A 103    25108  28388  12864  -3237   2632  -9108       N  
ATOM    527  N   ALA A 104       4.570   6.556 -13.667  1.00169.44           N  
ANISOU  527  N   ALA A 104    23821  28151  12408  -4165   2423  -8285       N  
ATOM    528  CA  ALA A 104       4.517   6.680 -15.120  1.00167.36           C  
ANISOU  528  CA  ALA A 104    23890  27324  12374  -4287   2406  -8190       C  
ATOM    529  C   ALA A 104       4.988   5.407 -15.808  1.00168.47           C  
ANISOU  529  C   ALA A 104    23759  27717  12537  -4126   2313  -7885       C  
ATOM    530  O   ALA A 104       4.626   5.153 -16.963  1.00158.84           O  
ANISOU  530  O   ALA A 104    22782  26053  11517  -4062   2281  -7718       O  
ATOM    531  CB  ALA A 104       5.354   7.870 -15.584  1.00172.26           C  
ANISOU  531  CB  ALA A 104    24680  27764  13009  -4859   2476  -8473       C  
ATOM    532  N   TRP A 105       5.790   4.600 -15.123  1.00187.31           N  
ANISOU  532  N   TRP A 105    25640  30812  14717  -4045   2259  -7819       N  
ATOM    533  CA  TRP A 105       6.215   3.320 -15.665  1.00186.78           C  
ANISOU  533  CA  TRP A 105    25302  31016  14651  -3821   2146  -7547       C  
ATOM    534  C   TRP A 105       5.000   2.459 -16.000  1.00180.52           C  
ANISOU  534  C   TRP A 105    24717  29882  13991  -3365   2097  -7242       C  
ATOM    535  O   TRP A 105       4.736   2.194 -17.174  1.00178.72           O  
ANISOU  535  O   TRP A 105    24707  29238  13959  -3322   2068  -7105       O  
ATOM    536  CB  TRP A 105       7.133   2.606 -14.672  1.00195.26           C  
ANISOU  536  CB  TRP A 105    25810  32920  15462  -3734   2078  -7535       C  
ATOM    537  N   CYS A 106       4.233   2.059 -14.979  1.00184.07           N  
ANISOU  537  N   CYS A 106    25094  30514  14329  -3052   2098  -7141       N  
ATOM    538  CA  CYS A 106       3.041   1.248 -15.222  1.00184.92           C  
ANISOU  538  CA  CYS A 106    25379  30346  14536  -2651   2071  -6854       C  
ATOM    539  C   CYS A 106       2.049   1.957 -16.134  1.00182.14           C  
ANISOU  539  C   CYS A 106    25540  29216  14448  -2675   2138  -6894       C  
ATOM    540  O   CYS A 106       1.317   1.300 -16.886  1.00189.82           O  
ANISOU  540  O   CYS A 106    26683  29868  15571  -2434   2109  -6665       O  
ATOM    541  CB  CYS A 106       2.360   0.882 -13.904  1.00194.69           C  
ANISOU  541  CB  CYS A 106    26450  31938  15584  -2387   2084  -6766       C  
ATOM    542  SG  CYS A 106       3.325  -0.136 -12.773  1.00217.30           S  
ANISOU  542  SG  CYS A 106    28708  35732  18122  -2265   1974  -6641       S  
ATOM    543  N   GLU A 107       1.999   3.285 -16.074  1.00168.12           N  
ANISOU  543  N   GLU A 107    24016  27133  12727  -2955   2219  -7189       N  
ATOM    544  CA  GLU A 107       1.060   4.053 -16.881  1.00166.76           C  
ANISOU  544  CA  GLU A 107    24342  26220  12799  -2963   2263  -7251       C  
ATOM    545  C   GLU A 107       1.290   3.823 -18.370  1.00164.04           C  
ANISOU  545  C   GLU A 107    24160  25504  12665  -3067   2220  -7117       C  
ATOM    546  O   GLU A 107       0.427   3.265 -19.056  1.00171.42           O  
ANISOU  546  O   GLU A 107    25270  26098  13764  -2801   2198  -6904       O  
ATOM    547  CB  GLU A 107       1.167   5.544 -16.558  1.00170.53           C  
ANISOU  547  CB  GLU A 107    25058  26461  13276  -3282   2334  -7616       C  
ATOM    548  N   ILE A 108       2.451   4.243 -18.877  1.00150.17           N  
ANISOU  548  N   ILE A 108    22324  23841  10893  -3471   2216  -7242       N  
ATOM    549  CA  ILE A 108       2.737   4.084 -20.300  1.00148.55           C  
ANISOU  549  CA  ILE A 108    22243  23330  10867  -3619   2182  -7128       C  
ATOM    550  C   ILE A 108       2.933   2.615 -20.654  1.00153.36           C  
ANISOU  550  C   ILE A 108    22556  24252  11463  -3322   2087  -6850       C  
ATOM    551  O   ILE A 108       2.701   2.211 -21.801  1.00146.47           O  
ANISOU  551  O   ILE A 108    21818  23064  10771  -3267   2051  -6694       O  
ATOM    552  CB  ILE A 108       3.960   4.933 -20.700  1.00155.49           C  
ANISOU  552  CB  ILE A 108    23083  24301  11696  -4172   2218  -7341       C  
ATOM    553  CG1 ILE A 108       5.221   4.455 -19.972  1.00156.29           C  
ANISOU  553  CG1 ILE A 108    22650  25186  11546  -4274   2190  -7406       C  
ATOM    554  CG2 ILE A 108       3.709   6.403 -20.402  1.00162.04           C  
ANISOU  554  CG2 ILE A 108    24274  24749  12544  -4475   2307  -7618       C  
ATOM    555  CD1 ILE A 108       6.137   3.579 -20.809  1.00149.58           C  
ANISOU  555  CD1 ILE A 108    21490  24650  10691  -4308   2109  -7273       C  
ATOM    556  N   TYR A 109       3.362   1.797 -19.690  1.00162.93           N  
ANISOU  556  N   TYR A 109    23367  26082  12459  -3127   2039  -6788       N  
ATOM    557  CA  TYR A 109       3.593   0.379 -19.959  1.00162.24           C  
ANISOU  557  CA  TYR A 109    23005  26303  12335  -2828   1929  -6538       C  
ATOM    558  C   TYR A 109       2.282  -0.339 -20.262  1.00159.39           C  
ANISOU  558  C   TYR A 109    22870  25582  12108  -2440   1920  -6287       C  
ATOM    559  O   TYR A 109       2.142  -0.987 -21.305  1.00159.35           O  
ANISOU  559  O   TYR A 109    22933  25362  12252  -2331   1867  -6130       O  
ATOM    560  CB  TYR A 109       4.318  -0.254 -18.768  1.00178.99           C  
ANISOU  560  CB  TYR A 109    24665  29165  14178  -2708   1869  -6532       C  
ATOM    561  CG  TYR A 109       4.272  -1.760 -18.684  1.00180.26           C  
ANISOU  561  CG  TYR A 109    24580  29653  14256  -2300   1742  -6255       C  
ATOM    562  CD1 TYR A 109       5.037  -2.549 -19.530  1.00165.98           C  
ANISOU  562  CD1 TYR A 109    22577  28009  12477  -2248   1627  -6184       C  
ATOM    563  CD2 TYR A 109       3.481  -2.391 -17.733  1.00189.27           C  
ANISOU  563  CD2 TYR A 109    25670  30975  15268  -1972   1730  -6073       C  
ATOM    564  CE1 TYR A 109       5.002  -3.925 -19.444  1.00167.51           C  
ANISOU  564  CE1 TYR A 109    22565  28498  12584  -1853   1490  -5951       C  
ATOM    565  CE2 TYR A 109       3.442  -3.766 -17.638  1.00182.92           C  
ANISOU  565  CE2 TYR A 109    24662  30479  14362  -1614   1601  -5806       C  
ATOM    566  CZ  TYR A 109       4.203  -4.528 -18.496  1.00173.78           C  
ANISOU  566  CZ  TYR A 109    23342  29443  13242  -1542   1473  -5753       C  
ATOM    567  OH  TYR A 109       4.171  -5.899 -18.410  1.00177.19           O  
ANISOU  567  OH  TYR A 109    23588  30176  13561  -1153   1317  -5502       O  
ATOM    568  N   LEU A 110       1.300  -0.218 -19.369  1.00165.66           N  
ANISOU  568  N   LEU A 110    23769  26328  12847  -2242   1979  -6260       N  
ATOM    569  CA  LEU A 110       0.004  -0.844 -19.613  1.00163.67           C  
ANISOU  569  CA  LEU A 110    23716  25766  12704  -1904   1993  -6034       C  
ATOM    570  C   LEU A 110      -0.728  -0.182 -20.776  1.00162.52           C  
ANISOU  570  C   LEU A 110    23994  24903  12853  -1980   2043  -6069       C  
ATOM    571  O   LEU A 110      -1.475  -0.851 -21.503  1.00177.15           O  
ANISOU  571  O   LEU A 110    25979  26474  14854  -1765   2032  -5869       O  
ATOM    572  CB  LEU A 110      -0.853  -0.795 -18.349  1.00156.21           C  
ANISOU  572  CB  LEU A 110    22744  25002  11608  -1708   2053  -6017       C  
ATOM    573  N   ALA A 111      -0.509   1.118 -20.982  1.00136.58           N  
ANISOU  573  N   ALA A 111    20923  21318   9651  -2295   2093  -6317       N  
ATOM    574  CA  ALA A 111      -1.203   1.817 -22.062  1.00135.63           C  
ANISOU  574  CA  ALA A 111    21217  20508   9807  -2373   2124  -6342       C  
ATOM    575  C   ALA A 111      -0.760   1.303 -23.428  1.00132.54           C  
ANISOU  575  C   ALA A 111    20829  19959   9573  -2471   2068  -6200       C  
ATOM    576  O   ALA A 111      -1.588   0.919 -24.265  1.00129.98           O  
ANISOU  576  O   ALA A 111    20696  19241   9449  -2292   2066  -6034       O  
ATOM    577  CB  ALA A 111      -0.968   3.324 -21.955  1.00135.03           C  
ANISOU  577  CB  ALA A 111    21383  20165   9758  -2721   2176  -6637       C  
ATOM    578  N   LEU A 112       0.553   1.278 -23.667  1.00130.47           N  
ANISOU  578  N   LEU A 112    20327  20032   9213  -2755   2025  -6273       N  
ATOM    579  CA  LEU A 112       1.054   0.814 -24.957  1.00129.29           C  
ANISOU  579  CA  LEU A 112    20137  19801   9188  -2862   1967  -6169       C  
ATOM    580  C   LEU A 112       0.885  -0.691 -25.120  1.00131.41           C  
ANISOU  580  C   LEU A 112    20185  20301   9443  -2479   1885  -5936       C  
ATOM    581  O   LEU A 112       0.713  -1.176 -26.244  1.00135.45           O  
ANISOU  581  O   LEU A 112    20770  20571  10126  -2430   1848  -5811       O  
ATOM    582  CB  LEU A 112       2.524   1.201 -25.128  1.00136.99           C  
ANISOU  582  CB  LEU A 112    20871  21142  10037  -3275   1949  -6333       C  
ATOM    583  CG  LEU A 112       2.838   2.698 -25.137  1.00135.11           C  
ANISOU  583  CG  LEU A 112    20870  20667   9798  -3749   2038  -6566       C  
ATOM    584  CD1 LEU A 112       4.305   2.941 -25.464  1.00137.96           C  
ANISOU  584  CD1 LEU A 112    20958  21432  10028  -4187   2033  -6700       C  
ATOM    585  CD2 LEU A 112       1.937   3.431 -26.119  1.00137.96           C  
ANISOU  585  CD2 LEU A 112    21723  20285  10410  -3847   2082  -6523       C  
ATOM    586  N   ASP A 113       0.929  -1.442 -24.018  1.00127.19           N  
ANISOU  586  N   ASP A 113    19390  20234   8701  -2219   1853  -5873       N  
ATOM    587  CA  ASP A 113       0.776  -2.891 -24.105  1.00136.17           C  
ANISOU  587  CA  ASP A 113    20342  21602   9796  -1865   1765  -5650       C  
ATOM    588  C   ASP A 113      -0.632  -3.273 -24.545  1.00139.29           C  
ANISOU  588  C   ASP A 113    21027  21527  10370  -1610   1814  -5467       C  
ATOM    589  O   ASP A 113      -0.814  -4.255 -25.275  1.00146.56           O  
ANISOU  589  O   ASP A 113    21922  22391  11374  -1427   1755  -5309       O  
ATOM    590  CB  ASP A 113       1.133  -3.529 -22.761  1.00142.49           C  
ANISOU  590  CB  ASP A 113    20811  23023  10308  -1675   1714  -5607       C  
ATOM    591  CG  ASP A 113       0.483  -4.877 -22.559  1.00145.75           C  
ANISOU  591  CG  ASP A 113    21143  23582  10652  -1272   1648  -5342       C  
ATOM    592  OD1 ASP A 113      -0.659  -4.914 -22.057  1.00149.69           O  
ANISOU  592  OD1 ASP A 113    21808  23923  11144  -1107   1726  -5228       O  
ATOM    593  OD2 ASP A 113       1.114  -5.898 -22.904  1.00145.35           O  
ANISOU  593  OD2 ASP A 113    20852  23830  10544  -1116   1511  -5256       O  
ATOM    594  N   VAL A 114      -1.639  -2.510 -24.118  1.00121.32           N  
ANISOU  594  N   VAL A 114    19016  18925   8154  -1590   1920  -5505       N  
ATOM    595  CA  VAL A 114      -2.995  -2.742 -24.604  1.00120.76           C  
ANISOU  595  CA  VAL A 114    19222  18385   8275  -1376   1982  -5353       C  
ATOM    596  C   VAL A 114      -3.194  -2.107 -25.976  1.00133.39           C  
ANISOU  596  C   VAL A 114    21114  19391  10177  -1554   1997  -5382       C  
ATOM    597  O   VAL A 114      -3.923  -2.649 -26.816  1.00133.29           O  
ANISOU  597  O   VAL A 114    21250  19040  10355  -1403   2007  -5215       O  
ATOM    598  CB  VAL A 114      -4.021  -2.219 -23.583  1.00128.87           C  
ANISOU  598  CB  VAL A 114    20375  19354   9236  -1241   2077  -5393       C  
ATOM    599  CG1 VAL A 114      -5.441  -2.380 -24.108  1.00128.66           C  
ANISOU  599  CG1 VAL A 114    20623  18845   9415  -1028   2150  -5250       C  
ATOM    600  CG2 VAL A 114      -3.861  -2.944 -22.255  1.00135.56           C  
ANISOU  600  CG2 VAL A 114    20907  20830   9768  -1077   2058  -5312       C  
ATOM    601  N   LEU A 115      -2.545  -0.967 -26.232  1.00139.35           N  
ANISOU  601  N   LEU A 115    21961  20017  10970  -1898   2002  -5578       N  
ATOM    602  CA  LEU A 115      -2.703  -0.288 -27.514  1.00131.43           C  
ANISOU  602  CA  LEU A 115    21247  18469  10222  -2112   2014  -5583       C  
ATOM    603  C   LEU A 115      -2.209  -1.151 -28.669  1.00126.59           C  
ANISOU  603  C   LEU A 115    20504  17897   9698  -2133   1944  -5452       C  
ATOM    604  O   LEU A 115      -2.857  -1.224 -29.719  1.00138.28           O  
ANISOU  604  O   LEU A 115    22201  18928  11412  -2092   1955  -5327       O  
ATOM    605  CB  LEU A 115      -1.961   1.049 -27.493  1.00126.98           C  
ANISOU  605  CB  LEU A 115    20795  17833   9618  -2537   2036  -5812       C  
ATOM    606  CG  LEU A 115      -1.740   1.741 -28.840  1.00132.68           C  
ANISOU  606  CG  LEU A 115    21768  18120  10523  -2875   2039  -5809       C  
ATOM    607  CD1 LEU A 115      -3.064   2.124 -29.482  1.00131.94           C  
ANISOU  607  CD1 LEU A 115    22084  17354  10693  -2716   2075  -5694       C  
ATOM    608  CD2 LEU A 115      -0.845   2.960 -28.674  1.00147.73           C  
ANISOU  608  CD2 LEU A 115    23752  20060  12318  -3349   2071  -6034       C  
ATOM    609  N   PHE A 116      -1.064  -1.813 -28.493  1.00118.19           N  
ANISOU  609  N   PHE A 116    19073  17382   8451  -2176   1863  -5488       N  
ATOM    610  CA  PHE A 116      -0.494  -2.604 -29.579  1.00131.60           C  
ANISOU  610  CA  PHE A 116    20609  19176  10219  -2187   1779  -5417       C  
ATOM    611  C   PHE A 116      -1.357  -3.820 -29.896  1.00131.49           C  
ANISOU  611  C   PHE A 116    20618  19035  10308  -1804   1757  -5213       C  
ATOM    612  O   PHE A 116      -1.519  -4.183 -31.066  1.00115.30           O  
ANISOU  612  O   PHE A 116    18634  16731   8442  -1800   1731  -5133       O  
ATOM    613  CB  PHE A 116       0.932  -3.028 -29.226  1.00136.77           C  
ANISOU  613  CB  PHE A 116    20838  20484  10643  -2274   1685  -5527       C  
ATOM    614  CG  PHE A 116       1.883  -1.875 -29.064  1.00137.32           C  
ANISOU  614  CG  PHE A 116    20864  20697  10612  -2715   1721  -5731       C  
ATOM    615  CD1 PHE A 116       1.644  -0.669 -29.702  1.00137.18           C  
ANISOU  615  CD1 PHE A 116    21179  20209  10732  -3067   1805  -5793       C  
ATOM    616  CD2 PHE A 116       3.015  -1.998 -28.276  1.00133.87           C  
ANISOU  616  CD2 PHE A 116    20064  20866   9935  -2794   1675  -5858       C  
ATOM    617  CE1 PHE A 116       2.514   0.394 -29.556  1.00140.18           C  
ANISOU  617  CE1 PHE A 116    21549  20713  11001  -3518   1852  -5983       C  
ATOM    618  CE2 PHE A 116       3.889  -0.938 -28.125  1.00142.55           C  
ANISOU  618  CE2 PHE A 116    21116  22110  10935  -3236   1728  -6057       C  
ATOM    619  CZ  PHE A 116       3.637   0.259 -28.765  1.00141.44           C  
ANISOU  619  CZ  PHE A 116    21328  21490  10922  -3614   1821  -6121       C  
ATOM    620  N   CYS A 117      -1.918  -4.461 -28.867  1.00124.70           N  
ANISOU  620  N   CYS A 117    19704  18361   9315  -1506   1774  -5126       N  
ATOM    621  CA  CYS A 117      -2.801  -5.599 -29.105  1.00125.45           C  
ANISOU  621  CA  CYS A 117    19864  18317   9484  -1189   1779  -4926       C  
ATOM    622  C   CYS A 117      -4.104  -5.157 -29.759  1.00127.36           C  
ANISOU  622  C   CYS A 117    20507  17877  10007  -1148   1888  -4808       C  
ATOM    623  O   CYS A 117      -4.600  -5.821 -30.677  1.00124.60           O  
ANISOU  623  O   CYS A 117    20183  17208   9950   -966   1832  -4577       O  
ATOM    624  CB  CYS A 117      -3.079  -6.332 -27.794  1.00121.25           C  
ANISOU  624  CB  CYS A 117    19134  18150   8784   -887   1740  -4763       C  
ATOM    625  SG  CYS A 117      -4.116  -7.800 -27.969  1.00148.70           S  
ANISOU  625  SG  CYS A 117    22530  21344  12626   -377   1604  -4224       S  
ATOM    626  N   THR A 118      -4.666  -4.032 -29.306  1.00113.98           N  
ANISOU  626  N   THR A 118    19019  15933   8354  -1227   1970  -4877       N  
ATOM    627  CA  THR A 118      -5.886  -3.515 -29.915  1.00114.81           C  
ANISOU  627  CA  THR A 118    19479  15414   8731  -1149   2045  -4779       C  
ATOM    628  C   THR A 118      -5.636  -3.069 -31.350  1.00118.65           C  
ANISOU  628  C   THR A 118    20101  15530   9450  -1366   2010  -4775       C  
ATOM    629  O   THR A 118      -6.459  -3.322 -32.238  1.00116.77           O  
ANISOU  629  O   THR A 118    20051  14870   9446  -1230   2027  -4610       O  
ATOM    630  CB  THR A 118      -6.437  -2.357 -29.084  1.00121.29           C  
ANISOU  630  CB  THR A 118    20460  16101   9521  -1172   2113  -4911       C  
ATOM    631  OG1 THR A 118      -6.597  -2.776 -27.724  1.00123.88           O  
ANISOU  631  OG1 THR A 118    20614  16863   9593   -998   2146  -4921       O  
ATOM    632  CG2 THR A 118      -7.782  -1.900 -29.629  1.00123.20           C  
ANISOU  632  CG2 THR A 118    21034  15748  10029  -1005   2170  -4808       C  
ATOM    633  N   SER A 119      -4.505  -2.404 -31.596  1.00107.04           N  
ANISOU  633  N   SER A 119    18535  14234   7902  -1716   1964  -4943       N  
ATOM    634  CA  SER A 119      -4.197  -1.951 -32.949  1.00106.15           C  
ANISOU  634  CA  SER A 119    18545  13833   7954  -1981   1939  -4930       C  
ATOM    635  C   SER A 119      -3.956  -3.130 -33.883  1.00103.67           C  
ANISOU  635  C   SER A 119    18046  13631   7713  -1873   1872  -4820       C  
ATOM    636  O   SER A 119      -4.320  -3.078 -35.064  1.00102.12           O  
ANISOU  636  O   SER A 119    18005  13075   7720  -1922   1871  -4718       O  
ATOM    637  CB  SER A 119      -2.982  -1.024 -32.930  1.00109.39           C  
ANISOU  637  CB  SER A 119    18881  14465   8215  -2419   1921  -5127       C  
ATOM    638  OG  SER A 119      -2.729  -0.491 -34.218  1.00114.75           O  
ANISOU  638  OG  SER A 119    19718  14867   9016  -2727   1916  -5099       O  
ATOM    639  N   SER A 120      -3.351  -4.206 -33.370  1.00104.50           N  
ANISOU  639  N   SER A 120    17823  14238   7645  -1713   1807  -4847       N  
ATOM    640  CA  SER A 120      -3.136  -5.394 -34.190  1.00104.59           C  
ANISOU  640  CA  SER A 120    17662  14360   7719  -1566   1730  -4781       C  
ATOM    641  C   SER A 120      -4.462  -6.038 -34.575  1.00 99.97           C  
ANISOU  641  C   SER A 120    17273  13307   7406  -1233   1759  -4517       C  
ATOM    642  O   SER A 120      -4.655  -6.446 -35.727  1.00 96.80           O  
ANISOU  642  O   SER A 120    16866  12679   7235  -1187   1712  -4409       O  
ATOM    643  CB  SER A 120      -2.249  -6.396 -33.447  1.00109.64           C  
ANISOU  643  CB  SER A 120    17920  15633   8107  -1414   1631  -4867       C  
ATOM    644  OG  SER A 120      -0.967  -5.852 -33.189  1.00115.59           O  
ANISOU  644  OG  SER A 120    18415  16826   8677  -1672   1569  -5049       O  
ATOM    645  N   ALA A 121      -5.391  -6.131 -33.623  1.00107.31           N  
ANISOU  645  N   ALA A 121    18271  14115   8387   -963   1796  -4344       N  
ATOM    646  CA  ALA A 121      -6.685  -6.742 -33.908  1.00 95.97           C  
ANISOU  646  CA  ALA A 121    16904  12282   7277   -614   1783  -4013       C  
ATOM    647  C   ALA A 121      -7.481  -5.906 -34.904  1.00102.68           C  
ANISOU  647  C   ALA A 121    18120  12586   8308   -721   1878  -4016       C  
ATOM    648  O   ALA A 121      -8.059  -6.437 -35.860  1.00 98.74           O  
ANISOU  648  O   ALA A 121    17624  11811   8083   -571   1840  -3825       O  
ATOM    649  CB  ALA A 121      -7.469  -6.932 -32.611  1.00103.05           C  
ANISOU  649  CB  ALA A 121    17777  13257   8121   -361   1813  -3858       C  
ATOM    650  N   TRP A 122      -7.514  -4.588 -34.700  1.00 97.58           N  
ANISOU  650  N   TRP A 122    17797  11772   7506   -976   1990  -4238       N  
ATOM    651  CA  TRP A 122      -8.274  -3.730 -35.603  1.00 97.57           C  
ANISOU  651  CA  TRP A 122    18082  11250   7738  -1025   2017  -4167       C  
ATOM    652  C   TRP A 122      -7.602  -3.602 -36.964  1.00109.05           C  
ANISOU  652  C   TRP A 122    19514  12636   9283  -1299   1960  -4179       C  
ATOM    653  O   TRP A 122      -8.289  -3.402 -37.972  1.00116.14           O  
ANISOU  653  O   TRP A 122    20599  13138  10392  -1260   1964  -4045       O  
ATOM    654  CB  TRP A 122      -8.486  -2.353 -34.976  1.00101.17           C  
ANISOU  654  CB  TRP A 122    18739  11551   8149  -1149   2057  -4290       C  
ATOM    655  CG  TRP A 122      -9.647  -2.312 -34.032  1.00116.66           C  
ANISOU  655  CG  TRP A 122    20796  13411  10118   -817   2120  -4241       C  
ATOM    656  CD1 TRP A 122      -9.598  -2.249 -32.671  1.00125.21           C  
ANISOU  656  CD1 TRP A 122    21776  14813  10987   -749   2158  -4359       C  
ATOM    657  CD2 TRP A 122     -11.036  -2.344 -34.382  1.00115.43           C  
ANISOU  657  CD2 TRP A 122    20815  12871  10172   -505   2152  -4071       C  
ATOM    658  NE1 TRP A 122     -10.870  -2.233 -32.151  1.00124.43           N  
ANISOU  658  NE1 TRP A 122    21779  14561  10938   -427   2216  -4282       N  
ATOM    659  CE2 TRP A 122     -11.771  -2.289 -33.182  1.00105.15           C  
ANISOU  659  CE2 TRP A 122    19499  11694   8759   -264   2210  -4108       C  
ATOM    660  CE3 TRP A 122     -11.730  -2.409 -35.595  1.00115.72           C  
ANISOU  660  CE3 TRP A 122    20988  12520  10462   -404   2133  -3897       C  
ATOM    661  CZ2 TRP A 122     -13.163  -2.301 -33.157  1.00 97.78           C  
ANISOU  661  CZ2 TRP A 122    18666  10530   7954     73   2249  -3989       C  
ATOM    662  CZ3 TRP A 122     -13.112  -2.419 -35.569  1.00103.54           C  
ANISOU  662  CZ3 TRP A 122    19545  10736   9059    -59   2166  -3769       C  
ATOM    663  CH2 TRP A 122     -13.814  -2.365 -34.359  1.00100.13           C  
ANISOU  663  CH2 TRP A 122    19081  10454   8508    176   2223  -3822       C  
ATOM    664  N   HIS A 123      -6.272  -3.711 -37.022  1.00105.64           N  
ANISOU  664  N   HIS A 123    18833  12631   8675  -1573   1902  -4339       N  
ATOM    665  CA  HIS A 123      -5.605  -3.747 -38.320  1.00 97.17           C  
ANISOU  665  CA  HIS A 123    17675  11593   7651  -1824   1847  -4358       C  
ATOM    666  C   HIS A 123      -5.989  -4.999 -39.095  1.00102.22           C  
ANISOU  666  C   HIS A 123    18203  12189   8446  -1561   1810  -4238       C  
ATOM    667  O   HIS A 123      -6.235  -4.936 -40.305  1.00104.55           O  
ANISOU  667  O   HIS A 123    18578  12247   8900  -1634   1799  -4158       O  
ATOM    668  CB  HIS A 123      -4.088  -3.669 -38.148  1.00103.10           C  
ANISOU  668  CB  HIS A 123    18114  12897   8162  -2136   1786  -4566       C  
ATOM    669  CG  HIS A 123      -3.556  -2.271 -38.101  1.00121.11           C  
ANISOU  669  CG  HIS A 123    20555  15120  10340  -2559   1821  -4670       C  
ATOM    670  ND1 HIS A 123      -3.654  -1.474 -36.981  1.00127.47           N  
ANISOU  670  ND1 HIS A 123    21497  15891  11047  -2599   1872  -4755       N  
ATOM    671  CD2 HIS A 123      -2.923  -1.526 -39.038  1.00120.00           C  
ANISOU  671  CD2 HIS A 123    20482  14946  10167  -2984   1820  -4707       C  
ATOM    672  CE1 HIS A 123      -3.103  -0.299 -37.230  1.00129.97           C  
ANISOU  672  CE1 HIS A 123    21979  16117  11288  -3027   1899  -4844       C  
ATOM    673  NE2 HIS A 123      -2.652  -0.305 -38.471  1.00126.98           N  
ANISOU  673  NE2 HIS A 123    21573  15735  10937  -3282   1874  -4803       N  
ATOM    674  N   LEU A 124      -6.048  -6.145 -38.413  1.00102.45           N  
ANISOU  674  N   LEU A 124    17996  12449   8480  -1232   1760  -4172       N  
ATOM    675  CA  LEU A 124      -6.496  -7.371 -39.064  1.00 99.26           C  
ANISOU  675  CA  LEU A 124    17370  11970   8372   -903   1659  -3944       C  
ATOM    676  C   LEU A 124      -7.945  -7.254 -39.519  1.00107.31           C  
ANISOU  676  C   LEU A 124    18641  12463   9667   -700   1720  -3706       C  
ATOM    677  O   LEU A 124      -8.315  -7.771 -40.580  1.00 86.91           O  
ANISOU  677  O   LEU A 124    16002   9709   7312   -608   1679  -3589       O  
ATOM    678  CB  LEU A 124      -6.329  -8.559 -38.118  1.00 93.13           C  
ANISOU  678  CB  LEU A 124    16270  11501   7613   -564   1544  -3823       C  
ATOM    679  CG  LEU A 124      -5.050  -9.389 -38.238  1.00113.61           C  
ANISOU  679  CG  LEU A 124    18477  14588  10100   -554   1392  -3968       C  
ATOM    680  CD1 LEU A 124      -3.815  -8.540 -37.999  1.00120.83           C  
ANISOU  680  CD1 LEU A 124    19349  15923  10639   -953   1432  -4313       C  
ATOM    681  CD2 LEU A 124      -5.092 -10.557 -37.271  1.00128.08           C  
ANISOU  681  CD2 LEU A 124    20076  16607  11982   -164   1259  -3779       C  
ATOM    682  N   CYS A 125      -8.781  -6.579 -38.726  1.00109.17           N  
ANISOU  682  N   CYS A 125    19131  12479   9871   -617   1816  -3659       N  
ATOM    683  CA  CYS A 125     -10.174  -6.387 -39.114  1.00101.99           C  
ANISOU  683  CA  CYS A 125    18445  11124   9182   -406   1874  -3470       C  
ATOM    684  C   CYS A 125     -10.283  -5.484 -40.336  1.00103.46           C  
ANISOU  684  C   CYS A 125    18929  10974   9405   -636   1916  -3535       C  
ATOM    685  O   CYS A 125     -11.071  -5.759 -41.250  1.00 89.39           O  
ANISOU  685  O   CYS A 125    17181   8936   7848   -487   1908  -3372       O  
ATOM    686  CB  CYS A 125     -10.968  -5.811 -37.942  1.00 93.47           C  
ANISOU  686  CB  CYS A 125    17542   9959   8015   -258   1958  -3464       C  
ATOM    687  SG  CYS A 125     -12.748  -5.716 -38.221  1.00118.01           S  
ANISOU  687  SG  CYS A 125    20834  12648  11355     80   2017  -3251       S  
ATOM    688  N   ALA A 126      -9.495  -4.406 -40.373  1.00 99.78           N  
ANISOU  688  N   ALA A 126    18607  10544   8760  -1007   1930  -3717       N  
ATOM    689  CA  ALA A 126      -9.498  -3.529 -41.538  1.00 90.59           C  
ANISOU  689  CA  ALA A 126    17635   9113   7672  -1256   1917  -3678       C  
ATOM    690  C   ALA A 126      -8.916  -4.221 -42.764  1.00 99.28           C  
ANISOU  690  C   ALA A 126    18544  10369   8810  -1395   1865  -3685       C  
ATOM    691  O   ALA A 126      -9.351  -3.953 -43.889  1.00103.00           O  
ANISOU  691  O   ALA A 126    19152  10581   9404  -1446   1860  -3574       O  
ATOM    692  CB  ALA A 126      -8.725  -2.246 -41.239  1.00 93.74           C  
ANISOU  692  CB  ALA A 126    18188   9539   7891  -1647   1923  -3822       C  
ATOM    693  N   ILE A 127      -7.931  -5.101 -42.571  1.00100.34           N  
ANISOU  693  N   ILE A 127    18350  10952   8823  -1445   1817  -3829       N  
ATOM    694  CA  ILE A 127      -7.382  -5.859 -43.692  1.00 88.21           C  
ANISOU  694  CA  ILE A 127    16575   9620   7320  -1528   1753  -3880       C  
ATOM    695  C   ILE A 127      -8.441  -6.787 -44.272  1.00100.28           C  
ANISOU  695  C   ILE A 127    17995  10921   9187  -1135   1715  -3638       C  
ATOM    696  O   ILE A 127      -8.622  -6.861 -45.492  1.00 98.94           O  
ANISOU  696  O   ILE A 127    17820  10647   9126  -1202   1699  -3593       O  
ATOM    697  CB  ILE A 127      -6.125  -6.632 -43.256  1.00 89.72           C  
ANISOU  697  CB  ILE A 127    16346  10392   7350  -1570   1664  -4069       C  
ATOM    698  CG1 ILE A 127      -4.943  -5.681 -43.069  1.00 91.94           C  
ANISOU  698  CG1 ILE A 127    16579  10997   7358  -2017   1662  -4263       C  
ATOM    699  CG2 ILE A 127      -5.781  -7.713 -44.269  1.00 87.84           C  
ANISOU  699  CG2 ILE A 127    15742  10376   7260  -1461   1550  -4074       C  
ATOM    700  CD1 ILE A 127      -3.674  -6.371 -42.620  1.00110.96           C  
ANISOU  700  CD1 ILE A 127    18559  14036   9564  -2043   1570  -4482       C  
ATOM    701  N   SER A 128      -9.159  -7.506 -43.402  1.00109.74           N  
ANISOU  701  N   SER A 128    19094  12066  10538   -747   1699  -3475       N  
ATOM    702  CA  SER A 128     -10.219  -8.396 -43.865  1.00 93.15           C  
ANISOU  702  CA  SER A 128    16892   9756   8746   -405   1669  -3243       C  
ATOM    703  C   SER A 128     -11.291  -7.628 -44.626  1.00 97.42           C  
ANISOU  703  C   SER A 128    17749   9879   9386   -400   1752  -3133       C  
ATOM    704  O   SER A 128     -11.806  -8.111 -45.641  1.00 80.18           O  
ANISOU  704  O   SER A 128    15481   7583   7399   -300   1727  -3027       O  
ATOM    705  CB  SER A 128     -10.832  -9.141 -42.680  1.00 84.64           C  
ANISOU  705  CB  SER A 128    15708   8697   7755    -67   1652  -3077       C  
ATOM    706  OG  SER A 128     -11.517  -8.250 -41.817  1.00112.29           O  
ANISOU  706  OG  SER A 128    19489  12024  11153    -34   1757  -3051       O  
ATOM    707  N   LEU A 129     -11.640  -6.429 -44.153  1.00 94.76           N  
ANISOU  707  N   LEU A 129    17780   9312   8912   -488   1839  -3170       N  
ATOM    708  CA  LEU A 129     -12.586  -5.594 -44.887  1.00 89.53           C  
ANISOU  708  CA  LEU A 129    17458   8244   8317   -462   1893  -3083       C  
ATOM    709  C   LEU A 129     -12.003  -5.151 -46.223  1.00105.64           C  
ANISOU  709  C   LEU A 129    19553  10269  10317   -796   1860  -3121       C  
ATOM    710  O   LEU A 129     -12.729  -5.024 -47.217  1.00117.49           O  
ANISOU  710  O   LEU A 129    21149  11545  11948   -722   1858  -2987       O  
ATOM    711  CB  LEU A 129     -12.979  -4.380 -44.046  1.00 85.10           C  
ANISOU  711  CB  LEU A 129    17167   7497   7670   -461   1928  -3084       C  
ATOM    712  CG  LEU A 129     -13.803  -4.653 -42.787  1.00101.50           C  
ANISOU  712  CG  LEU A 129    19220   9581   9764   -119   1974  -3044       C  
ATOM    713  CD1 LEU A 129     -14.059  -3.367 -42.014  1.00114.23           C  
ANISOU  713  CD1 LEU A 129    21072  11050  11280   -144   1993  -3105       C  
ATOM    714  CD2 LEU A 129     -15.113  -5.332 -43.149  1.00 93.57           C  
ANISOU  714  CD2 LEU A 129    18152   8431   8969    246   1992  -2855       C  
ATOM    715  N   ASP A 130     -10.689  -4.909 -46.265  1.00 92.96           N  
ANISOU  715  N   ASP A 130    17865   8948   8507  -1177   1834  -3302       N  
ATOM    716  CA  ASP A 130     -10.048  -4.528 -47.519  1.00 85.89           C  
ANISOU  716  CA  ASP A 130    16987   8123   7526  -1549   1806  -3346       C  
ATOM    717  C   ASP A 130     -10.132  -5.653 -48.543  1.00 83.82           C  
ANISOU  717  C   ASP A 130    16430   8009   7410  -1428   1764  -3330       C  
ATOM    718  O   ASP A 130     -10.416  -5.411 -49.723  1.00 83.72           O  
ANISOU  718  O   ASP A 130    16504   7873   7432  -1538   1761  -3256       O  
ATOM    719  CB  ASP A 130      -8.592  -4.138 -47.270  1.00 89.82           C  
ANISOU  719  CB  ASP A 130    17362   9004   7760  -1983   1784  -3552       C  
ATOM    720  CG  ASP A 130      -7.789  -4.047 -48.549  1.00102.72           C  
ANISOU  720  CG  ASP A 130    18881  10873   9275  -2376   1749  -3625       C  
ATOM    721  OD1 ASP A 130      -8.014  -3.096 -49.326  1.00111.35           O  
ANISOU  721  OD1 ASP A 130    20291  11698  10318  -2626   1769  -3518       O  
ATOM    722  OD2 ASP A 130      -6.933  -4.927 -48.779  1.00 92.76           O  
ANISOU  722  OD2 ASP A 130    17212  10081   7953  -2428   1694  -3793       O  
ATOM    723  N   ARG A 131      -9.897  -6.893 -48.110  1.00 92.45           N  
ANISOU  723  N   ARG A 131    17111   9390   8626  -1180   1701  -3355       N  
ATOM    724  CA  ARG A 131      -9.981  -8.015 -49.041  1.00 85.01           C  
ANISOU  724  CA  ARG A 131    15815   8598   7889  -1024   1625  -3322       C  
ATOM    725  C   ARG A 131     -11.421  -8.261 -49.476  1.00 95.34           C  
ANISOU  725  C   ARG A 131    17213   9552   9461   -709   1654  -3088       C  
ATOM    726  O   ARG A 131     -11.677  -8.581 -50.643  1.00 78.88           O  
ANISOU  726  O   ARG A 131    15012   7471   7489   -713   1631  -3053       O  
ATOM    727  CB  ARG A 131      -9.392  -9.281 -48.416  1.00 94.40           C  
ANISOU  727  CB  ARG A 131    16595  10117   9155   -805   1523  -3403       C  
ATOM    728  CG  ARG A 131      -8.123  -9.068 -47.603  1.00111.62           C  
ANISOU  728  CG  ARG A 131    18681  12667  11063  -1013   1496  -3622       C  
ATOM    729  CD  ARG A 131      -7.036  -8.356 -48.392  1.00114.87           C  
ANISOU  729  CD  ARG A 131    19079  13370  11196  -1497   1504  -3851       C  
ATOM    730  NE  ARG A 131      -6.506  -9.178 -49.474  1.00 99.71           N  
ANISOU  730  NE  ARG A 131    16780  11774   9333  -1510   1408  -3977       N  
ATOM    731  CZ  ARG A 131      -5.439  -8.860 -50.200  1.00101.39           C  
ANISOU  731  CZ  ARG A 131    16839  12394   9289  -1909   1390  -4213       C  
ATOM    732  NH1 ARG A 131      -5.027  -9.669 -51.166  1.00 85.42           N  
ANISOU  732  NH1 ARG A 131    14436  10695   7326  -1872   1296  -4351       N  
ATOM    733  NH2 ARG A 131      -4.781  -7.734 -49.960  1.00121.84           N  
ANISOU  733  NH2 ARG A 131    19642  15093  11560  -2356   1460  -4320       N  
ATOM    734  N   TYR A 132     -12.373  -8.112 -48.552  1.00 91.72           N  
ANISOU  734  N   TYR A 132    16934   8836   9079   -442   1708  -2945       N  
ATOM    735  CA  TYR A 132     -13.777  -8.330 -48.889  1.00 87.93           C  
ANISOU  735  CA  TYR A 132    16512   8083   8813   -141   1742  -2744       C  
ATOM    736  C   TYR A 132     -14.259  -7.328 -49.928  1.00 98.44           C  
ANISOU  736  C   TYR A 132    18142   9166  10095   -266   1782  -2691       C  
ATOM    737  O   TYR A 132     -14.961  -7.696 -50.878  1.00 80.50           O  
ANISOU  737  O   TYR A 132    15778   6832   7976   -141   1775  -2588       O  
ATOM    738  CB  TYR A 132     -14.637  -8.248 -47.628  1.00 98.08           C  
ANISOU  738  CB  TYR A 132    17922   9221  10125    132   1795  -2638       C  
ATOM    739  CG  TYR A 132     -16.125  -8.263 -47.895  1.00103.69           C  
ANISOU  739  CG  TYR A 132    18714   9693  10990    422   1844  -2463       C  
ATOM    740  CD1 TYR A 132     -16.786  -9.451 -48.179  1.00 87.37           C  
ANISOU  740  CD1 TYR A 132    16360   7687   9150    639   1819  -2342       C  
ATOM    741  CD2 TYR A 132     -16.870  -7.091 -47.858  1.00 94.94           C  
ANISOU  741  CD2 TYR A 132    17971   8308   9793    483   1907  -2437       C  
ATOM    742  CE1 TYR A 132     -18.146  -9.471 -48.423  1.00 82.82           C  
ANISOU  742  CE1 TYR A 132    15824   6961   8684    880   1870  -2203       C  
ATOM    743  CE2 TYR A 132     -18.231  -7.101 -48.101  1.00113.86           C  
ANISOU  743  CE2 TYR A 132    20398  10558  12306    777   1941  -2299       C  
ATOM    744  CZ  TYR A 132     -18.864  -8.294 -48.383  1.00112.11           C  
ANISOU  744  CZ  TYR A 132    19860  10454  12282    962   1933  -2190       C  
ATOM    745  OH  TYR A 132     -20.219  -8.310 -48.625  1.00115.99           O  
ANISOU  745  OH  TYR A 132    20357  10858  12856   1232   1977  -2078       O  
ATOM    746  N   TRP A 133     -13.891  -6.055 -49.767  1.00 96.71           N  
ANISOU  746  N   TRP A 133    18297   8794   9655   -518   1817  -2757       N  
ATOM    747  CA  TRP A 133     -14.329  -5.034 -50.712  1.00 88.60           C  
ANISOU  747  CA  TRP A 133    17624   7477   8563   -639   1832  -2678       C  
ATOM    748  C   TRP A 133     -13.615  -5.174 -52.051  1.00 98.67           C  
ANISOU  748  C   TRP A 133    18752   8960   9779   -962   1788  -2716       C  
ATOM    749  O   TRP A 133     -14.214  -4.937 -53.106  1.00 89.79           O  
ANISOU  749  O   TRP A 133    17725   7694   8696   -942   1780  -2593       O  
ATOM    750  CB  TRP A 133     -14.105  -3.645 -50.117  1.00 83.76           C  
ANISOU  750  CB  TRP A 133    17378   6666   7782   -824   1834  -2676       C  
ATOM    751  CG  TRP A 133     -15.177  -3.236 -49.155  1.00 86.34           C  
ANISOU  751  CG  TRP A 133    17831   6775   8201   -455   1849  -2570       C  
ATOM    752  CD1 TRP A 133     -16.489  -3.611 -49.185  1.00 82.83           C  
ANISOU  752  CD1 TRP A 133    17309   6229   7935    -36   1858  -2427       C  
ATOM    753  CD2 TRP A 133     -15.030  -2.383 -48.014  1.00 92.43           C  
ANISOU  753  CD2 TRP A 133    18787   7464   8867   -483   1856  -2630       C  
ATOM    754  NE1 TRP A 133     -17.169  -3.039 -48.138  1.00 93.23           N  
ANISOU  754  NE1 TRP A 133    18741   7432   9249    199   1867  -2404       N  
ATOM    755  CE2 TRP A 133     -16.295  -2.281 -47.403  1.00100.27           C  
ANISOU  755  CE2 TRP A 133    19804   8318   9978    -59   1865  -2532       C  
ATOM    756  CE3 TRP A 133     -13.952  -1.693 -47.450  1.00105.19           C  
ANISOU  756  CE3 TRP A 133    20531   9146  10290   -838   1856  -2778       C  
ATOM    757  CZ2 TRP A 133     -16.513  -1.518 -46.258  1.00117.45           C  
ANISOU  757  CZ2 TRP A 133    22129  10411  12086     37   1870  -2595       C  
ATOM    758  CZ3 TRP A 133     -14.169  -0.936 -46.313  1.00131.03           C  
ANISOU  758  CZ3 TRP A 133    23965  12306  13512   -746   1866  -2827       C  
ATOM    759  CH2 TRP A 133     -15.440  -0.855 -45.729  1.00135.04           C  
ANISOU  759  CH2 TRP A 133    24497  12669  14144   -304   1871  -2744       C  
ATOM    760  N   SER A 134     -12.336  -5.560 -52.031  1.00105.06           N  
ANISOU  760  N   SER A 134    19301  10150  10466  -1253   1754  -2900       N  
ATOM    761  CA  SER A 134     -11.615  -5.774 -53.282  1.00109.14           C  
ANISOU  761  CA  SER A 134    19605  10962  10901  -1560   1710  -2977       C  
ATOM    762  C   SER A 134     -12.179  -6.960 -54.055  1.00104.24           C  
ANISOU  762  C   SER A 134    18597  10473  10537  -1274   1670  -2922       C  
ATOM    763  O   SER A 134     -12.039  -7.022 -55.282  1.00119.20           O  
ANISOU  763  O   SER A 134    20372  12520  12398  -1448   1645  -2931       O  
ATOM    764  CB  SER A 134     -10.125  -5.979 -53.007  1.00111.19           C  
ANISOU  764  CB  SER A 134    19617  11678  10954  -1894   1677  -3231       C  
ATOM    765  OG  SER A 134      -9.899  -7.174 -52.279  1.00116.72           O  
ANISOU  765  OG  SER A 134    19922  12621  11806  -1595   1628  -3321       O  
ATOM    766  N   ILE A 135     -12.821  -7.900 -53.361  1.00103.66           N  
ANISOU  766  N   ILE A 135    18330  10351  10704   -865   1663  -2867       N  
ATOM    767  CA  ILE A 135     -13.423  -9.049 -54.030  1.00 91.00           C  
ANISOU  767  CA  ILE A 135    16390   8828   9359   -603   1625  -2821       C  
ATOM    768  C   ILE A 135     -14.818  -8.707 -54.539  1.00 80.47           C  
ANISOU  768  C   ILE A 135    15253   7184   8137   -394   1678  -2611       C  
ATOM    769  O   ILE A 135     -15.169  -9.012 -55.685  1.00 87.25           O  
ANISOU  769  O   ILE A 135    15961   8117   9073   -388   1663  -2581       O  
ATOM    770  CB  ILE A 135     -13.452 -10.262 -53.081  1.00 82.20           C  
ANISOU  770  CB  ILE A 135    14997   7795   8439   -302   1579  -2843       C  
ATOM    771  CG1 ILE A 135     -12.041 -10.812 -52.863  1.00 78.99           C  
ANISOU  771  CG1 ILE A 135    14304   7771   7939   -452   1489  -3076       C  
ATOM    772  CG2 ILE A 135     -14.374 -11.347 -53.619  1.00 73.07           C  
ANISOU  772  CG2 ILE A 135    13598   6595   7571    -14   1555  -2753       C  
ATOM    773  CD1 ILE A 135     -11.980 -11.960 -51.875  1.00 94.28           C  
ANISOU  773  CD1 ILE A 135    16019   9761  10043   -152   1415  -3076       C  
ATOM    774  N   THR A 136     -15.629  -8.060 -53.699  1.00 94.00           N  
ANISOU  774  N   THR A 136    17285   8587   9843   -205   1737  -2485       N  
ATOM    775  CA  THR A 136     -17.017  -7.788 -54.060  1.00 86.73           C  
ANISOU  775  CA  THR A 136    16517   7419   9019     65   1778  -2309       C  
ATOM    776  C   THR A 136     -17.108  -6.766 -55.187  1.00 95.01           C  
ANISOU  776  C   THR A 136    17842   8338   9921   -124   1772  -2243       C  
ATOM    777  O   THR A 136     -17.812  -6.983 -56.180  1.00106.38           O  
ANISOU  777  O   THR A 136    19183   9795  11442    -14   1766  -2152       O  
ATOM    778  CB  THR A 136     -17.791  -7.304 -52.833  1.00103.17           C  
ANISOU  778  CB  THR A 136    18851   9258  11092    322   1831  -2238       C  
ATOM    779  OG1 THR A 136     -17.723  -8.294 -51.799  1.00119.04           O  
ANISOU  779  OG1 THR A 136    20601  11415  13216    472   1831  -2265       O  
ATOM    780  CG2 THR A 136     -19.248  -7.047 -53.187  1.00121.95           C  
ANISOU  780  CG2 THR A 136    21343  11447  13546    640   1865  -2091       C  
ATOM    781  N   GLN A 137     -16.406  -5.645 -55.051  1.00 90.37           N  
ANISOU  781  N   GLN A 137    17614   7619   9103   -427   1768  -2278       N  
ATOM    782  CA  GLN A 137     -16.452  -4.551 -56.019  1.00101.16           C  
ANISOU  782  CA  GLN A 137    19340   8798  10299   -646   1747  -2179       C  
ATOM    783  C   GLN A 137     -15.030  -4.305 -56.512  1.00101.53           C  
ANISOU  783  C   GLN A 137    19354   9096  10125  -1187   1719  -2306       C  
ATOM    784  O   GLN A 137     -14.287  -3.512 -55.931  1.00113.91           O  
ANISOU  784  O   GLN A 137    21207  10572  11501  -1475   1725  -2382       O  
ATOM    785  CB  GLN A 137     -17.064  -3.303 -55.389  1.00111.44           C  
ANISOU  785  CB  GLN A 137    21193   9638  11510   -514   1757  -2092       C  
ATOM    786  CG  GLN A 137     -18.443  -3.541 -54.793  1.00119.85           C  
ANISOU  786  CG  GLN A 137    22243  10543  12751     26   1788  -2013       C  
ATOM    787  CD  GLN A 137     -18.622  -2.868 -53.448  1.00121.46           C  
ANISOU  787  CD  GLN A 137    22618  10598  12933    166   1785  -2015       C  
ATOM    788  OE1 GLN A 137     -18.033  -1.821 -53.181  1.00135.76           O  
ANISOU  788  OE1 GLN A 137    24761  12235  14585    -81   1754  -2034       O  
ATOM    789  NE2 GLN A 137     -19.433  -3.472 -52.587  1.00108.88           N  
ANISOU  789  NE2 GLN A 137    20766   9114  11491    534   1811  -1995       N  
ATOM    790  N   ALA A 138     -14.656  -4.989 -57.594  1.00 94.51           N  
ANISOU  790  N   ALA A 138    18100   8563   9248  -1339   1689  -2352       N  
ATOM    791  CA  ALA A 138     -13.283  -4.921 -58.085  1.00100.68           C  
ANISOU  791  CA  ALA A 138    18738   9713   9803  -1846   1662  -2515       C  
ATOM    792  C   ALA A 138     -12.945  -3.527 -58.602  1.00108.37           C  
ANISOU  792  C   ALA A 138    20206  10491  10480  -2287   1654  -2412       C  
ATOM    793  O   ALA A 138     -12.046  -2.860 -58.080  1.00108.05           O  
ANISOU  793  O   ALA A 138    20381  10451  10221  -2656   1663  -2512       O  
ATOM    794  CB  ALA A 138     -13.064  -5.971 -59.177  1.00103.70           C  
ANISOU  794  CB  ALA A 138    18598  10540  10263  -1868   1625  -2611       C  
ATOM    795  N   ILE A 139     -13.667  -3.068 -59.627  1.00106.00           N  
ANISOU  795  N   ILE A 139    20106  10015  10154  -2267   1630  -2203       N  
ATOM    796  CA  ILE A 139     -13.311  -1.817 -60.296  1.00113.06           C  
ANISOU  796  CA  ILE A 139    21473  10733  10751  -2729   1598  -2069       C  
ATOM    797  C   ILE A 139     -13.470  -0.636 -59.346  1.00111.92           C  
ANISOU  797  C   ILE A 139    21957  10040  10529  -2740   1601  -2000       C  
ATOM    798  O   ILE A 139     -12.573   0.207 -59.219  1.00101.91           O  
ANISOU  798  O   ILE A 139    21003   8718   8999  -3245   1595  -2045       O  
ATOM    799  CB  ILE A 139     -14.157  -1.631 -61.568  1.00117.48           C  
ANISOU  799  CB  ILE A 139    22114  11214  11310  -2632   1556  -1832       C  
ATOM    800  CG1 ILE A 139     -14.197  -2.926 -62.381  1.00 88.90           C  
ANISOU  800  CG1 ILE A 139    17834   8117   7827  -2513   1560  -1937       C  
ATOM    801  CG2 ILE A 139     -13.609  -0.487 -62.407  1.00132.43           C  
ANISOU  801  CG2 ILE A 139    24438  13020  12860  -3198   1506  -1682       C  
ATOM    802  CD1 ILE A 139     -12.845  -3.377 -62.884  1.00 89.45           C  
ANISOU  802  CD1 ILE A 139    17501   8778   7706  -3005   1554  -2166       C  
ATOM    803  N   GLU A 140     -14.614  -0.559 -58.663  1.00118.61           N  
ANISOU  803  N   GLU A 140    22982  10495  11587  -2194   1609  -1913       N  
ATOM    804  CA  GLU A 140     -14.912   0.601 -57.827  1.00107.29           C  
ANISOU  804  CA  GLU A 140    22159   8513  10092  -2130   1596  -1864       C  
ATOM    805  C   GLU A 140     -13.915   0.732 -56.681  1.00103.68           C  
ANISOU  805  C   GLU A 140    21718   8137   9537  -2396   1642  -2092       C  
ATOM    806  O   GLU A 140     -13.335   1.803 -56.468  1.00109.01           O  
ANISOU  806  O   GLU A 140    22862   8562   9997  -2790   1624  -2108       O  
ATOM    807  CB  GLU A 140     -16.340   0.499 -57.293  1.00125.18           C  
ANISOU  807  CB  GLU A 140    24492  10474  12595  -1450   1599  -1782       C  
ATOM    808  CG  GLU A 140     -17.407   0.510 -58.375  1.00141.05           C  
ANISOU  808  CG  GLU A 140    26532  12389  14673  -1157   1548  -1563       C  
ATOM    809  CD  GLU A 140     -18.699  -0.140 -57.923  1.00157.11           C  
ANISOU  809  CD  GLU A 140    28324  14415  16955   -508   1579  -1552       C  
ATOM    810  OE1 GLU A 140     -18.641  -1.268 -57.388  1.00152.42           O  
ANISOU  810  OE1 GLU A 140    27234  14154  16524   -373   1646  -1683       O  
ATOM    811  OE2 GLU A 140     -19.770   0.478 -58.096  1.00158.42           O  
ANISOU  811  OE2 GLU A 140    28802  14253  17137   -137   1529  -1413       O  
ATOM    812  N   TYR A 141     -13.700  -0.352 -55.933  1.00112.69           N  
ANISOU  812  N   TYR A 141    22357   9634  10827  -2195   1693  -2264       N  
ATOM    813  CA  TYR A 141     -12.801  -0.289 -54.785  1.00117.58           C  
ANISOU  813  CA  TYR A 141    22926  10393  11355  -2387   1729  -2467       C  
ATOM    814  C   TYR A 141     -11.347  -0.128 -55.212  1.00113.51           C  
ANISOU  814  C   TYR A 141    22327  10248  10553  -3046   1728  -2621       C  
ATOM    815  O   TYR A 141     -10.553   0.473 -54.478  1.00115.25           O  
ANISOU  815  O   TYR A 141    22629  10526  10634  -3333   1736  -2700       O  
ATOM    816  CB  TYR A 141     -12.968  -1.536 -53.917  1.00 99.25           C  
ANISOU  816  CB  TYR A 141    20104   8355   9251  -1989   1764  -2581       C  
ATOM    817  CG  TYR A 141     -12.108  -1.540 -52.674  1.00103.03           C  
ANISOU  817  CG  TYR A 141    20433   9051   9664  -2107   1780  -2739       C  
ATOM    818  CD1 TYR A 141     -12.497  -0.846 -51.536  1.00118.65           C  
ANISOU  818  CD1 TYR A 141    22628  10777  11678  -1921   1787  -2696       C  
ATOM    819  CD2 TYR A 141     -10.907  -2.236 -52.640  1.00 89.15           C  
ANISOU  819  CD2 TYR A 141    18287   7794   7792  -2387   1779  -2949       C  
ATOM    820  CE1 TYR A 141     -11.716  -0.846 -50.398  1.00122.03           C  
ANISOU  820  CE1 TYR A 141    22919  11421  12024  -2036   1806  -2854       C  
ATOM    821  CE2 TYR A 141     -10.119  -2.242 -51.506  1.00 99.63           C  
ANISOU  821  CE2 TYR A 141    19466   9347   9040  -2475   1786  -3096       C  
ATOM    822  CZ  TYR A 141     -10.528  -1.545 -50.388  1.00117.14           C  
ANISOU  822  CZ  TYR A 141    21934  11286  11289  -2313   1806  -3046       C  
ATOM    823  OH  TYR A 141      -9.747  -1.547 -49.256  1.00124.51           O  
ANISOU  823  OH  TYR A 141    22717  12467  12123  -2408   1817  -3205       O  
ATOM    824  N   ASN A 142     -10.979  -0.655 -56.384  1.00101.92           N  
ANISOU  824  N   ASN A 142    20541   9154   9030  -3259   1703  -2612       N  
ATOM    825  CA  ASN A 142      -9.630  -0.435 -56.896  1.00101.91           C  
ANISOU  825  CA  ASN A 142    20434   9575   8712  -3915   1698  -2759       C  
ATOM    826  C   ASN A 142      -9.382   1.038 -57.197  1.00127.26           C  
ANISOU  826  C   ASN A 142    24301  12413  11639  -4430   1683  -2640       C  
ATOM    827  O   ASN A 142      -8.239   1.503 -57.110  1.00136.34           O  
ANISOU  827  O   ASN A 142    25431  13843  12530  -4979   1695  -2741       O  
ATOM    828  CB  ASN A 142      -9.392  -1.280 -58.150  1.00103.29           C  
ANISOU  828  CB  ASN A 142    20115  10247   8882  -4004   1667  -2776       C  
ATOM    829  CG  ASN A 142      -8.000  -1.097 -58.724  1.00130.78           C  
ANISOU  829  CG  ASN A 142    23420  14270  12001  -4688   1662  -2957       C  
ATOM    830  OD1 ASN A 142      -7.043  -1.728 -58.275  1.00144.34           O  
ANISOU  830  OD1 ASN A 142    24707  16493  13641  -4793   1669  -3238       O  
ATOM    831  ND2 ASN A 142      -7.882  -0.237 -59.730  1.00130.67           N  
ANISOU  831  ND2 ASN A 142    23729  14182  11739  -5158   1642  -2795       N  
ATOM    832  N   LEU A 143     -10.430   1.786 -57.552  1.00130.25           N  
ANISOU  832  N   LEU A 143    25187  12206  12098  -4222   1643  -2373       N  
ATOM    833  CA  LEU A 143     -10.259   3.217 -57.781  1.00106.15           C  
ANISOU  833  CA  LEU A 143    22831   8699   8803  -4665   1602  -2229       C  
ATOM    834  C   LEU A 143     -10.144   3.982 -56.469  1.00107.91           C  
ANISOU  834  C   LEU A 143    23272   8663   9067  -4574   1617  -2242       C  
ATOM    835  O   LEU A 143      -9.493   5.032 -56.422  1.00135.98           O  
ANISOU  835  O   LEU A 143    27193  12085  12389  -5060   1602  -2193       O  
ATOM    836  CB  LEU A 143     -11.421   3.762 -58.613  1.00107.26           C  
ANISOU  836  CB  LEU A 143    23402   8326   9026  -4395   1523  -1910       C  
ATOM    837  CG  LEU A 143     -11.552   3.205 -60.034  1.00116.52           C  
ANISOU  837  CG  LEU A 143    24238   9863  10169  -4462   1492  -1759       C  
ATOM    838  CD1 LEU A 143     -12.729   3.836 -60.762  1.00118.34           C  
ANISOU  838  CD1 LEU A 143    24923   9578  10462  -4157   1402  -1429       C  
ATOM    839  CD2 LEU A 143     -10.263   3.405 -60.817  1.00129.55           C  
ANISOU  839  CD2 LEU A 143    25793  11976  11454  -5266   1493  -1816       C  
ATOM    840  N   LYS A 144     -10.764   3.478 -55.402  1.00105.15           N  
ANISOU  840  N   LYS A 144    22695   8266   8990  -3983   1645  -2311       N  
ATOM    841  CA  LYS A 144     -10.681   4.084 -54.082  1.00119.61           C  
ANISOU  841  CA  LYS A 144    24651   9936  10861  -3867   1660  -2370       C  
ATOM    842  C   LYS A 144      -9.558   3.502 -53.230  1.00116.08           C  
ANISOU  842  C   LYS A 144    23734  10023  10347  -4085   1726  -2631       C  
ATOM    843  O   LYS A 144      -9.438   3.864 -52.056  1.00113.14           O  
ANISOU  843  O   LYS A 144    23394   9591  10004  -3988   1746  -2717       O  
ATOM    844  CB  LYS A 144     -12.018   3.939 -53.348  1.00128.53           C  
ANISOU  844  CB  LYS A 144    25782  10766  12286  -3123   1642  -2295       C  
ATOM    845  CG  LYS A 144     -13.067   4.957 -53.760  1.00147.97           C  
ANISOU  845  CG  LYS A 144    28774  12663  14784  -2867   1551  -2058       C  
ATOM    846  CD  LYS A 144     -14.262   4.918 -52.821  1.00151.74           C  
ANISOU  846  CD  LYS A 144    29174  12969  15509  -2173   1534  -2043       C  
ATOM    847  CE  LYS A 144     -15.251   6.032 -53.125  1.00154.34           C  
ANISOU  847  CE  LYS A 144    29996  12793  15853  -1886   1418  -1852       C  
ATOM    848  NZ  LYS A 144     -16.391   6.031 -52.166  1.00150.82           N  
ANISOU  848  NZ  LYS A 144    29419  12270  15615  -1238   1396  -1884       N  
ATOM    849  N   ARG A 145      -8.736   2.616 -53.790  1.00121.98           N  
ANISOU  849  N   ARG A 145    24020  11327  10998  -4353   1747  -2769       N  
ATOM    850  CA  ARG A 145      -7.619   2.012 -53.062  1.00109.36           C  
ANISOU  850  CA  ARG A 145    21916  10309   9328  -4517   1783  -3015       C  
ATOM    851  C   ARG A 145      -6.344   2.834 -53.174  1.00115.90           C  
ANISOU  851  C   ARG A 145    22826  11378   9833  -5220   1804  -3090       C  
ATOM    852  O   ARG A 145      -5.244   2.280 -53.244  1.00130.55           O  
ANISOU  852  O   ARG A 145    24184  13866  11555  -5498   1817  -3273       O  
ATOM    853  CB  ARG A 145      -7.391   0.589 -53.561  1.00100.02           C  
ANISOU  853  CB  ARG A 145    20124   9654   8225  -4358   1771  -3142       C  
ATOM    854  N   THR A 146      -6.464   4.159 -53.188  1.00111.86           N  
ANISOU  854  N   THR A 146    22922  10389   9191  -5498   1800  -2947       N  
ATOM    855  CA  THR A 146      -5.296   5.015 -53.300  1.00115.71           C  
ANISOU  855  CA  THR A 146    23543  11069   9354  -6209   1832  -2993       C  
ATOM    856  C   THR A 146      -4.453   4.938 -52.028  1.00118.04           C  
ANISOU  856  C   THR A 146    23516  11715   9617  -6262   1885  -3226       C  
ATOM    857  O   THR A 146      -4.969   4.631 -50.950  1.00126.31           O  
ANISOU  857  O   THR A 146    24476  12638  10878  -5762   1885  -3297       O  
ATOM    858  CB  THR A 146      -5.718   6.460 -53.554  1.00125.59           C  
ANISOU  858  CB  THR A 146    25579  11652  10487  -6436   1797  -2768       C  
ATOM    859  OG1 THR A 146      -6.542   6.915 -52.472  1.00139.48           O  
ANISOU  859  OG1 THR A 146    27615  12921  12459  -5939   1779  -2752       O  
ATOM    860  CG2 THR A 146      -6.498   6.565 -54.855  1.00129.87           C  
ANISOU  860  CG2 THR A 146    26445  11871  11029  -6400   1725  -2522       C  
ATOM    861  N   PRO A 147      -3.146   5.201 -52.130  1.00119.16           N  
ANISOU  861  N   PRO A 147    23452  12344   9478  -6868   1931  -3348       N  
ATOM    862  CA  PRO A 147      -2.312   5.220 -50.916  1.00120.15           C  
ANISOU  862  CA  PRO A 147    23291  12811   9551  -6938   1978  -3571       C  
ATOM    863  C   PRO A 147      -2.774   6.236 -49.887  1.00132.82           C  
ANISOU  863  C   PRO A 147    25408  13857  11200  -6839   1994  -3547       C  
ATOM    864  O   PRO A 147      -2.559   6.029 -48.686  1.00127.16           O  
ANISOU  864  O   PRO A 147    24453  13312  10551  -6625   2015  -3724       O  
ATOM    865  CB  PRO A 147      -0.916   5.561 -51.457  1.00123.97           C  
ANISOU  865  CB  PRO A 147    23564  13847   9693  -7680   2032  -3652       C  
ATOM    866  CG  PRO A 147      -0.946   5.137 -52.886  1.00125.83           C  
ANISOU  866  CG  PRO A 147    23671  14275   9863  -7843   2001  -3542       C  
ATOM    867  CD  PRO A 147      -2.349   5.378 -53.355  1.00123.48           C  
ANISOU  867  CD  PRO A 147    23929  13247   9741  -7496   1944  -3301       C  
ATOM    868  N   ARG A 148      -3.406   7.329 -50.322  1.00177.07           N  
ANISOU  868  N   ARG A 148    31705  18810  16762  -6962   1968  -3336       N  
ATOM    869  CA  ARG A 148      -3.933   8.307 -49.376  1.00193.31           C  
ANISOU  869  CA  ARG A 148    34241  20318  18891  -6785   1957  -3326       C  
ATOM    870  C   ARG A 148      -5.071   7.715 -48.555  1.00194.22           C  
ANISOU  870  C   ARG A 148    34234  20213  19348  -5990   1921  -3347       C  
ATOM    871  O   ARG A 148      -5.170   7.966 -47.347  1.00212.66           O  
ANISOU  871  O   ARG A 148    36566  22481  21756  -5779   1936  -3486       O  
ATOM    872  CB  ARG A 148      -4.399   9.556 -50.124  1.00200.22           C  
ANISOU  872  CB  ARG A 148    35873  20545  19656  -7014   1897  -3081       C  
ATOM    873  CG  ARG A 148      -4.695  10.747 -49.228  1.00205.38           C  
ANISOU  873  CG  ARG A 148    37031  20677  20325  -6949   1870  -3103       C  
ATOM    874  CD  ARG A 148      -5.076  11.970 -50.048  1.00209.41           C  
ANISOU  874  CD  ARG A 148    38288  20570  20707  -7172   1775  -2853       C  
ATOM    875  NE  ARG A 148      -6.389  11.828 -50.671  1.00206.81           N  
ANISOU  875  NE  ARG A 148    38170  19802  20605  -6600   1663  -2631       N  
ATOM    876  CZ  ARG A 148      -6.915  12.711 -51.513  1.00203.81           C  
ANISOU  876  CZ  ARG A 148    38387  18897  20157  -6644   1543  -2380       C  
ATOM    877  NH1 ARG A 148      -8.118  12.501 -52.031  1.00203.21           N  
ANISOU  877  NH1 ARG A 148    38419  18496  20297  -6073   1443  -2198       N  
ATOM    878  NH2 ARG A 148      -6.238  13.803 -51.841  1.00204.75           N  
ANISOU  878  NH2 ARG A 148    38984  18834  19976  -7257   1516  -2309       N  
ATOM    879  N   ARG A 149      -5.938   6.926 -49.192  1.00165.16           N  
ANISOU  879  N   ARG A 149    30437  16454  15863  -5562   1878  -3216       N  
ATOM    880  CA  ARG A 149      -7.033   6.292 -48.466  1.00150.03           C  
ANISOU  880  CA  ARG A 149    28365  14390  14249  -4832   1856  -3219       C  
ATOM    881  C   ARG A 149      -6.514   5.231 -47.504  1.00144.22           C  
ANISOU  881  C   ARG A 149    27018  14218  13561  -4662   1898  -3442       C  
ATOM    882  O   ARG A 149      -7.037   5.081 -46.394  1.00144.41           O  
ANISOU  882  O   ARG A 149    26965  14177  13728  -4244   1902  -3516       O  
ATOM    883  CB  ARG A 149      -8.031   5.683 -49.451  1.00140.50           C  
ANISOU  883  CB  ARG A 149    27158  13007  13217  -4463   1809  -3024       C  
ATOM    884  CG  ARG A 149      -9.447   5.556 -48.918  1.00143.42           C  
ANISOU  884  CG  ARG A 149    27605  13019  13870  -3750   1773  -2936       C  
ATOM    885  CD  ARG A 149     -10.426   6.271 -49.837  1.00154.09           C  
ANISOU  885  CD  ARG A 149    29440  13835  15273  -3589   1694  -2687       C  
ATOM    886  NE  ARG A 149     -11.809   6.152 -49.385  1.00164.28           N  
ANISOU  886  NE  ARG A 149    30735  14866  16820  -2892   1654  -2611       N  
ATOM    887  CZ  ARG A 149     -12.843   6.724 -49.993  1.00167.34           C  
ANISOU  887  CZ  ARG A 149    31470  14827  17285  -2596   1568  -2414       C  
ATOM    888  NH1 ARG A 149     -14.069   6.564 -49.515  1.00162.07           N  
ANISOU  888  NH1 ARG A 149    30713  14034  16831  -1966   1536  -2380       N  
ATOM    889  NH2 ARG A 149     -12.650   7.459 -51.081  1.00163.26           N  
ANISOU  889  NH2 ARG A 149    31375  14045  16610  -2936   1507  -2253       N  
ATOM    890  N   ILE A 150      -5.478   4.494 -47.910  1.00135.66           N  
ANISOU  890  N   ILE A 150    25482  13719  12343  -4970   1917  -3553       N  
ATOM    891  CA  ILE A 150      -4.911   3.465 -47.044  1.00128.33           C  
ANISOU  891  CA  ILE A 150    23969  13352  11439  -4785   1927  -3756       C  
ATOM    892  C   ILE A 150      -4.232   4.098 -45.836  1.00123.33           C  
ANISOU  892  C   ILE A 150    23343  12847  10669  -4981   1964  -3935       C  
ATOM    893  O   ILE A 150      -4.378   3.619 -44.705  1.00125.37           O  
ANISOU  893  O   ILE A 150    23368  13258  11007  -4629   1964  -4049       O  
ATOM    894  CB  ILE A 150      -3.940   2.575 -47.841  1.00133.41           C  
ANISOU  894  CB  ILE A 150    24103  14618  11969  -5029   1909  -3845       C  
ATOM    895  CG1 ILE A 150      -4.641   1.983 -49.066  1.00136.88           C  
ANISOU  895  CG1 ILE A 150    24542  14928  12537  -4849   1874  -3689       C  
ATOM    896  CG2 ILE A 150      -3.378   1.473 -46.958  1.00129.34           C  
ANISOU  896  CG2 ILE A 150    23000  14664  11479  -4762   1885  -4042       C  
ATOM    897  CD1 ILE A 150      -5.869   1.165 -48.733  1.00138.99           C  
ANISOU  897  CD1 ILE A 150    24762  14948  13100  -4177   1852  -3607       C  
ATOM    898  N   LYS A 151      -3.482   5.181 -46.053  1.00119.51           N  
ANISOU  898  N   LYS A 151    23136  12315   9959  -5563   2000  -3959       N  
ATOM    899  CA  LYS A 151      -2.822   5.858 -44.941  1.00120.36           C  
ANISOU  899  CA  LYS A 151    23269  12536   9927  -5787   2043  -4142       C  
ATOM    900  C   LYS A 151      -3.841   6.465 -43.984  1.00132.15           C  
ANISOU  900  C   LYS A 151    25133  13501  11579  -5393   2033  -4132       C  
ATOM    901  O   LYS A 151      -3.623   6.490 -42.767  1.00135.59           O  
ANISOU  901  O   LYS A 151    25407  14116  11993  -5282   2053  -4314       O  
ATOM    902  CB  LYS A 151      -1.872   6.932 -45.469  1.00125.38           C  
ANISOU  902  CB  LYS A 151    24173  13186  10278  -6527   2093  -4147       C  
ATOM    903  N   ALA A 152      -4.961   6.957 -44.517  1.00145.35           N  
ANISOU  903  N   ALA A 152    27271  14555  13399  -5156   1993  -3929       N  
ATOM    904  CA  ALA A 152      -6.013   7.493 -43.659  1.00152.09           C  
ANISOU  904  CA  ALA A 152    28417  14950  14422  -4706   1965  -3929       C  
ATOM    905  C   ALA A 152      -6.658   6.392 -42.828  1.00145.48           C  
ANISOU  905  C   ALA A 152    27163  14341  13774  -4109   1962  -3986       C  
ATOM    906  O   ALA A 152      -7.020   6.614 -41.666  1.00142.84           O  
ANISOU  906  O   ALA A 152    26826  13961  13487  -3845   1968  -4114       O  
ATOM    907  CB  ALA A 152      -7.062   8.218 -44.502  1.00147.53           C  
ANISOU  907  CB  ALA A 152    28378  13718  13957  -4536   1898  -3691       C  
ATOM    908  N   ILE A 153      -6.813   5.199 -43.407  1.00138.48           N  
ANISOU  908  N   ILE A 153    25926  13709  12979  -3903   1953  -3898       N  
ATOM    909  CA  ILE A 153      -7.364   4.076 -42.654  1.00128.80           C  
ANISOU  909  CA  ILE A 153    24317  12720  11903  -3382   1953  -3931       C  
ATOM    910  C   ILE A 153      -6.418   3.676 -41.530  1.00128.70           C  
ANISOU  910  C   ILE A 153    23919  13241  11739  -3484   1979  -4161       C  
ATOM    911  O   ILE A 153      -6.848   3.419 -40.398  1.00124.94           O  
ANISOU  911  O   ILE A 153    23324  12842  11308  -3145   1988  -4241       O  
ATOM    912  CB  ILE A 153      -7.661   2.892 -43.595  1.00124.61           C  
ANISOU  912  CB  ILE A 153    23519  12332  11496  -3180   1931  -3793       C  
ATOM    913  CG1 ILE A 153      -8.819   3.227 -44.535  1.00120.09           C  
ANISOU  913  CG1 ILE A 153    23297  11241  11091  -2957   1901  -3561       C  
ATOM    914  CG2 ILE A 153      -7.977   1.635 -42.796  1.00121.09           C  
ANISOU  914  CG2 ILE A 153    22659  12199  11152  -2737   1934  -3836       C  
ATOM    915  CD1 ILE A 153     -10.146   3.413 -43.830  1.00109.41           C  
ANISOU  915  CD1 ILE A 153    22088   9561   9924  -2419   1890  -3496       C  
ATOM    916  N   ILE A 154      -5.114   3.633 -41.818  1.00118.19           N  
ANISOU  916  N   ILE A 154    22373  12326  10207  -3953   1987  -4272       N  
ATOM    917  CA  ILE A 154      -4.137   3.247 -40.804  1.00120.08           C  
ANISOU  917  CA  ILE A 154    22208  13133  10283  -4040   1996  -4488       C  
ATOM    918  C   ILE A 154      -4.131   4.251 -39.658  1.00122.19           C  
ANISOU  918  C   ILE A 154    22698  13260  10469  -4114   2032  -4634       C  
ATOM    919  O   ILE A 154      -4.113   3.872 -38.479  1.00123.75           O  
ANISOU  919  O   ILE A 154    22657  13733  10631  -3874   2035  -4763       O  
ATOM    920  CB  ILE A 154      -2.739   3.102 -41.436  1.00113.15           C  
ANISOU  920  CB  ILE A 154    21034  12757   9201  -4531   1991  -4580       C  
ATOM    921  CG1 ILE A 154      -2.734   1.968 -42.462  1.00109.94           C  
ANISOU  921  CG1 ILE A 154    20325  12570   8878  -4388   1939  -4486       C  
ATOM    922  CG2 ILE A 154      -1.691   2.847 -40.366  1.00118.01           C  
ANISOU  922  CG2 ILE A 154    21244  13966   9631  -4619   1989  -4804       C  
ATOM    923  CD1 ILE A 154      -1.394   1.763 -43.138  1.00124.49           C  
ANISOU  923  CD1 ILE A 154    21809  14966  10525  -4819   1922  -4591       C  
ATOM    924  N   ILE A 155      -4.149   5.546 -39.981  1.00127.38           N  
ANISOU  924  N   ILE A 155    23830  13487  11082  -4447   2054  -4618       N  
ATOM    925  CA  ILE A 155      -4.172   6.563 -38.933  1.00132.74           C  
ANISOU  925  CA  ILE A 155    24750  13988  11696  -4514   2078  -4780       C  
ATOM    926  C   ILE A 155      -5.462   6.494 -38.126  1.00126.89           C  
ANISOU  926  C   ILE A 155    24107  12962  11144  -3925   2058  -4771       C  
ATOM    927  O   ILE A 155      -5.445   6.658 -36.900  1.00121.84           O  
ANISOU  927  O   ILE A 155    23365  12483  10444  -3801   2073  -4960       O  
ATOM    928  CB  ILE A 155      -4.003   7.969 -39.541  1.00 30.00           C  
ATOM    929  CG1 ILE A 155      -2.611   8.120 -40.157  1.00 30.00           C  
ATOM    930  CG2 ILE A 155      -4.243   9.037 -38.486  1.00 30.00           C  
ATOM    931  CD1 ILE A 155      -2.450   9.363 -41.002  1.00 30.00           C  
ATOM    932  N   THR A 156      -6.591   6.248 -38.794  1.00137.24           N  
ANISOU  932  N   THR A 156    25584  13894  12666  -3557   2023  -4561       N  
ATOM    933  CA  THR A 156      -7.859   6.138 -38.081  1.00136.11           C  
ANISOU  933  CA  THR A 156    25481  13541  12693  -2990   2007  -4548       C  
ATOM    934  C   THR A 156      -7.866   4.930 -37.152  1.00134.12           C  
ANISOU  934  C   THR A 156    24742  13800  12417  -2685   2031  -4618       C  
ATOM    935  O   THR A 156      -8.345   5.019 -36.016  1.00138.09           O  
ANISOU  935  O   THR A 156    25190  14368  12910  -2413   2044  -4744       O  
ATOM    936  CB  THR A 156      -9.017   6.062 -39.077  1.00135.99           C  
ANISOU  936  CB  THR A 156    25690  13085  12894  -2670   1964  -4295       C  
ATOM    937  OG1 THR A 156      -9.066   7.269 -39.849  1.00148.11           O  
ANISOU  937  OG1 THR A 156    27729  14122  14424  -2921   1925  -4219       O  
ATOM    938  CG2 THR A 156     -10.342   5.883 -38.350  1.00128.23           C  
ANISOU  938  CG2 THR A 156    24676  11973  12072  -2079   1951  -4288       C  
ATOM    939  N   VAL A 157      -7.327   3.797 -37.611  1.00123.10           N  
ANISOU  939  N   VAL A 157    22993  12785  10993  -2726   2030  -4545       N  
ATOM    940  CA  VAL A 157      -7.270   2.606 -36.767  1.00114.24           C  
ANISOU  940  CA  VAL A 157    21444  12139   9823  -2445   2038  -4587       C  
ATOM    941  C   VAL A 157      -6.385   2.854 -35.552  1.00116.99           C  
ANISOU  941  C   VAL A 157    21603  12907   9941  -2623   2056  -4829       C  
ATOM    942  O   VAL A 157      -6.723   2.460 -34.430  1.00122.24           O  
ANISOU  942  O   VAL A 157    22098  13798  10548  -2338   2073  -4899       O  
ATOM    943  CB  VAL A 157      -6.791   1.391 -37.583  1.00106.96           C  
ANISOU  943  CB  VAL A 157    20207  11516   8915  -2457   2009  -4481       C  
ATOM    944  CG1 VAL A 157      -6.502   0.216 -36.665  1.00111.56           C  
ANISOU  944  CG1 VAL A 157    20380  12612   9394  -2224   2002  -4539       C  
ATOM    945  CG2 VAL A 157      -7.835   1.005 -38.616  1.00109.19           C  
ANISOU  945  CG2 VAL A 157    20633  11419   9435  -2195   1997  -4248       C  
ATOM    946  N   TRP A 158      -5.244   3.520 -35.752  1.00113.90           N  
ANISOU  946  N   TRP A 158    21230  12652   9394  -3111   2057  -4955       N  
ATOM    947  CA  TRP A 158      -4.371   3.839 -34.627  1.00120.04           C  
ANISOU  947  CA  TRP A 158    21824  13838   9947  -3303   2075  -5191       C  
ATOM    948  C   TRP A 158      -5.049   4.791 -33.649  1.00125.11           C  
ANISOU  948  C   TRP A 158    22735  14202  10599  -3172   2102  -5326       C  
ATOM    949  O   TRP A 158      -4.881   4.663 -32.430  1.00131.59           O  
ANISOU  949  O   TRP A 158    23341  15379  11279  -3058   2115  -5488       O  
ATOM    950  CB  TRP A 158      -3.058   4.441 -35.129  1.00126.58           C  
ANISOU  950  CB  TRP A 158    22637  14848  10610  -3887   2084  -5290       C  
ATOM    951  CG  TRP A 158      -2.024   3.421 -35.487  1.00121.67           C  
ANISOU  951  CG  TRP A 158    21540  14815   9873  -3992   2046  -5288       C  
ATOM    952  CD1 TRP A 158      -1.582   3.102 -36.738  1.00117.19           C  
ANISOU  952  CD1 TRP A 158    20900  14299   9330  -4203   2023  -5186       C  
ATOM    953  CD2 TRP A 158      -1.301   2.580 -34.580  1.00124.46           C  
ANISOU  953  CD2 TRP A 158    21416  15814  10060  -3858   2012  -5403       C  
ATOM    954  NE1 TRP A 158      -0.627   2.117 -36.666  1.00116.40           N  
ANISOU  954  NE1 TRP A 158    20288  14837   9103  -4186   1969  -5253       N  
ATOM    955  CE2 TRP A 158      -0.437   1.778 -35.352  1.00117.28           C  
ANISOU  955  CE2 TRP A 158    20159  15306   9095  -3966   1957  -5374       C  
ATOM    956  CE3 TRP A 158      -1.300   2.427 -33.190  1.00119.05           C  
ANISOU  956  CE3 TRP A 158    20560  15424   9251  -3644   2016  -5525       C  
ATOM    957  CZ2 TRP A 158       0.419   0.839 -34.781  1.00116.71           C  
ANISOU  957  CZ2 TRP A 158    19596  15884   8862  -3833   1892  -5460       C  
ATOM    958  CZ3 TRP A 158      -0.450   1.495 -32.625  1.00125.15           C  
ANISOU  958  CZ3 TRP A 158    20859  16845   9846  -3542   1962  -5585       C  
ATOM    959  CH2 TRP A 158       0.398   0.712 -33.419  1.00127.91           C  
ANISOU  959  CH2 TRP A 158    20890  17552  10158  -3622   1894  -5551       C  
ATOM    960  N   VAL A 159      -5.819   5.752 -34.162  1.00136.63           N  
ANISOU  960  N   VAL A 159    24657  15045  12211  -3167   2098  -5271       N  
ATOM    961  CA  VAL A 159      -6.489   6.710 -33.288  1.00141.90           C  
ANISOU  961  CA  VAL A 159    25585  15429  12902  -3008   2101  -5432       C  
ATOM    962  C   VAL A 159      -7.575   6.018 -32.471  1.00144.76           C  
ANISOU  962  C   VAL A 159    25764  15902  13336  -2446   2105  -5418       C  
ATOM    963  O   VAL A 159      -7.643   6.172 -31.246  1.00142.78           O  
ANISOU  963  O   VAL A 159    25387  15897  12966  -2319   2123  -5620       O  
ATOM    964  CB  VAL A 159      -7.058   7.883 -34.106  1.00139.68           C  
ANISOU  964  CB  VAL A 159    25855  14449  12769  -3093   2069  -5360       C  
ATOM    965  CG1 VAL A 159      -8.060   8.670 -33.277  1.00138.55           C  
ANISOU  965  CG1 VAL A 159    25942  13991  12712  -2748   2043  -5513       C  
ATOM    966  CG2 VAL A 159      -5.934   8.793 -34.575  1.00141.78           C  
ANISOU  966  CG2 VAL A 159    26350  14633  12889  -3717   2084  -5430       C  
ATOM    967  N   ILE A 160      -8.437   5.243 -33.134  1.00141.41           N  
ANISOU  967  N   ILE A 160    25313  15329  13089  -2120   2094  -5181       N  
ATOM    968  CA  ILE A 160      -9.514   4.571 -32.413  1.00139.24           C  
ANISOU  968  CA  ILE A 160    24872  15169  12863  -1620   2113  -5146       C  
ATOM    969  C   ILE A 160      -8.959   3.490 -31.494  1.00143.37           C  
ANISOU  969  C   ILE A 160    24958  16333  13184  -1571   2146  -5190       C  
ATOM    970  O   ILE A 160      -9.558   3.185 -30.457  1.00149.48           O  
ANISOU  970  O   ILE A 160    25585  17333  13876  -1275   2178  -5253       O  
ATOM    971  CB  ILE A 160     -10.558   4.000 -33.393  1.00135.01           C  
ANISOU  971  CB  ILE A 160    24411  14326  12559  -1310   2098  -4871       C  
ATOM    972  CG1 ILE A 160      -9.952   2.891 -34.255  1.00138.23           C  
ANISOU  972  CG1 ILE A 160    24602  14941  12979  -1437   2096  -4685       C  
ATOM    973  CG2 ILE A 160     -11.132   5.107 -34.265  1.00133.16           C  
ANISOU  973  CG2 ILE A 160    24613  13482  12498  -1322   2049  -4813       C  
ATOM    974  CD1 ILE A 160     -10.928   2.281 -35.239  1.00136.68           C  
ANISOU  974  CD1 ILE A 160    24457  14471  13006  -1150   2082  -4425       C  
ATOM    975  N   SER A 161      -7.813   2.900 -31.843  1.00137.47           N  
ANISOU  975  N   SER A 161    23985  15919  12328  -1850   2132  -5160       N  
ATOM    976  CA  SER A 161      -7.189   1.933 -30.945  1.00136.81           C  
ANISOU  976  CA  SER A 161    23495  16459  12026  -1795   2139  -5205       C  
ATOM    977  C   SER A 161      -6.673   2.612 -29.684  1.00147.09           C  
ANISOU  977  C   SER A 161    24718  18065  13105  -1920   2156  -5467       C  
ATOM    978  O   SER A 161      -6.783   2.058 -28.584  1.00164.88           O  
ANISOU  978  O   SER A 161    26727  20734  15186  -1711   2176  -5509       O  
ATOM    979  CB  SER A 161      -6.056   1.197 -31.660  1.00139.89           C  
ANISOU  979  CB  SER A 161    23643  17153  12355  -2030   2095  -5142       C  
ATOM    980  OG  SER A 161      -6.531   0.529 -32.816  1.00145.96           O  
ANISOU  980  OG  SER A 161    24467  17665  13324  -1904   2077  -4921       O  
ATOM    981  N   ALA A 162      -6.110   3.815 -29.823  1.00140.58           N  
ANISOU  981  N   ALA A 162    24109  17042  12263  -2275   2150  -5638       N  
ATOM    982  CA  ALA A 162      -5.664   4.561 -28.653  1.00147.86           C  
ANISOU  982  CA  ALA A 162    24989  18201  12988  -2405   2168  -5908       C  
ATOM    983  C   ALA A 162      -6.839   5.027 -27.805  1.00156.35           C  
ANISOU  983  C   ALA A 162    26209  19096  14101  -2057   2189  -6020       C  
ATOM    984  O   ALA A 162      -6.705   5.166 -26.585  1.00165.81           O  
ANISOU  984  O   ALA A 162    27241  20658  15103  -1997   2207  -6211       O  
ATOM    985  CB  ALA A 162      -4.812   5.755 -29.083  1.00153.65           C  
ANISOU  985  CB  ALA A 162    25967  18715  13698  -2903   2166  -6057       C  
ATOM    986  N   VAL A 163      -7.992   5.272 -28.430  1.00160.45           N  
ANISOU  986  N   VAL A 163    27011  19095  14859  -1812   2181  -5910       N  
ATOM    987  CA  VAL A 163      -9.174   5.682 -27.680  1.00157.56           C  
ANISOU  987  CA  VAL A 163    26739  18595  14532  -1438   2191  -6032       C  
ATOM    988  C   VAL A 163      -9.764   4.496 -26.928  1.00159.09           C  
ANISOU  988  C   VAL A 163    26592  19243  14610  -1078   2237  -5929       C  
ATOM    989  O   VAL A 163     -10.104   4.598 -25.743  1.00163.07           O  
ANISOU  989  O   VAL A 163    26955  20059  14944   -899   2264  -6104       O  
ATOM    990  CB  VAL A 163     -10.208   6.325 -28.622  1.00153.35           C  
ANISOU  990  CB  VAL A 163    26591  17391  14283  -1267   2155  -5939       C  
ATOM    991  CG1 VAL A 163     -11.521   6.561 -27.892  1.00144.25           C  
ANISOU  991  CG1 VAL A 163    25451  16185  13173   -810   2158  -6059       C  
ATOM    992  CG2 VAL A 163      -9.668   7.632 -29.185  1.00154.01           C  
ANISOU  992  CG2 VAL A 163    27068  17017  14432  -1630   2110  -6054       C  
ATOM    993  N   ILE A 164      -9.890   3.352 -27.604  1.00157.26           N  
ANISOU  993  N   ILE A 164    26235  19066  14452   -981   2247  -5642       N  
ATOM    994  CA  ILE A 164     -10.450   2.168 -26.961  1.00158.19           C  
ANISOU  994  CA  ILE A 164    26077  19579  14447   -677   2298  -5501       C  
ATOM    995  C   ILE A 164      -9.533   1.682 -25.844  1.00146.64           C  
ANISOU  995  C   ILE A 164    24284  18772  12660   -786   2311  -5589       C  
ATOM    996  O   ILE A 164      -9.998   1.266 -24.776  1.00145.43           O  
ANISOU  996  O   ILE A 164    23944  19005  12306   -573   2359  -5605       O  
ATOM    997  CB  ILE A 164     -10.711   1.067 -28.007  1.00173.19           C  
ANISOU  997  CB  ILE A 164    27959  21339  16507   -576   2298  -5179       C  
ATOM    998  CG1 ILE A 164     -11.771   1.524 -29.015  1.00176.05           C  
ANISOU  998  CG1 ILE A 164    28616  21101  17172   -404   2282  -5070       C  
ATOM    999  CG2 ILE A 164     -11.132  -0.231 -27.336  1.00179.24           C  
ANISOU  999  CG2 ILE A 164    28477  22519  17107   -324   2354  -5007       C  
ATOM   1000  CD1 ILE A 164     -13.068   1.986 -28.388  1.00184.34           C  
ANISOU 1000  CD1 ILE A 164    29736  22059  18246    -59   2313  -5162       C  
ATOM   1001  N   SER A 165      -8.217   1.740 -26.063  1.00140.82           N  
ANISOU 1001  N   SER A 165    23453  18208  11844  -1121   2266  -5642       N  
ATOM   1002  CA  SER A 165      -7.284   1.255 -25.051  1.00144.06           C  
ANISOU 1002  CA  SER A 165    23523  19265  11948  -1204   2258  -5704       C  
ATOM   1003  C   SER A 165      -7.248   2.163 -23.828  1.00153.96           C  
ANISOU 1003  C   SER A 165    24759  20719  13019  -1230   2280  -5980       C  
ATOM   1004  O   SER A 165      -7.008   1.686 -22.712  1.00154.87           O  
ANISOU 1004  O   SER A 165    24595  21382  12867  -1149   2295  -5992       O  
ATOM   1005  CB  SER A 165      -5.883   1.118 -25.647  1.00148.97           C  
ANISOU 1005  CB  SER A 165    24018  20047  12535  -1540   2197  -5705       C  
ATOM   1006  OG  SER A 165      -5.895   0.282 -26.790  1.00162.33           O  
ANISOU 1006  OG  SER A 165    25713  21576  14388  -1504   2168  -5482       O  
ATOM   1007  N   PHE A 166      -7.481   3.455 -24.011  1.00157.29           N  
ANISOU 1007  N   PHE A 166    25483  20707  13574  -1339   2275  -6194       N  
ATOM   1008  CA  PHE A 166      -7.446   4.397 -22.897  1.00168.85           C  
ANISOU 1008  CA  PHE A 166    26965  22312  14880  -1366   2287  -6498       C  
ATOM   1009  C   PHE A 166      -8.640   4.176 -21.977  1.00171.13           C  
ANISOU 1009  C   PHE A 166    27173  22775  15075   -960   2330  -6525       C  
ATOM   1010  O   PHE A 166      -9.788   4.293 -22.426  1.00175.13           O  
ANISOU 1010  O   PHE A 166    27860  22908  15773   -704   2339  -6483       O  
ATOM   1011  CB  PHE A 166      -7.432   5.831 -23.418  1.00171.23           C  
ANISOU 1011  CB  PHE A 166    27661  22039  15361  -1580   2258  -6718       C  
ATOM   1012  CG  PHE A 166      -7.682   6.863 -22.357  1.00174.77           C  
ANISOU 1012  CG  PHE A 166    28197  22510  15697  -1527   2259  -7059       C  
ATOM   1013  CD1 PHE A 166      -6.745   7.097 -21.364  1.00182.30           C  
ANISOU 1013  CD1 PHE A 166    28955  23921  16391  -1742   2274  -7247       C  
ATOM   1014  CD2 PHE A 166      -8.857   7.595 -22.349  1.00175.81           C  
ANISOU 1014  CD2 PHE A 166    28591  22224  15985  -1243   2238  -7205       C  
ATOM   1015  CE1 PHE A 166      -6.974   8.046 -20.385  1.00194.94           C  
ANISOU 1015  CE1 PHE A 166    30643  25542  17885  -1692   2274  -7577       C  
ATOM   1016  CE2 PHE A 166      -9.092   8.546 -21.374  1.00192.31           C  
ANISOU 1016  CE2 PHE A 166    30757  24342  17970  -1162   2221  -7557       C  
ATOM   1017  CZ  PHE A 166      -8.149   8.771 -20.391  1.00197.02           C  
ANISOU 1017  CZ  PHE A 166    31181  25376  18301  -1393   2242  -7743       C  
ATOM   1018  N   PRO A 167      -8.427   3.861 -20.703  1.00162.32           N  
ANISOU 1018  N   PRO A 167    25776  22239  13660   -896   2361  -6584       N  
ATOM   1019  CA  PRO A 167      -9.549   3.610 -19.798  1.00153.86           C  
ANISOU 1019  CA  PRO A 167    24601  21406  12452   -541   2415  -6592       C  
ATOM   1020  C   PRO A 167     -10.097   4.909 -19.235  1.00161.29           C  
ANISOU 1020  C   PRO A 167    25742  22143  13400   -442   2404  -6955       C  
ATOM   1021  O   PRO A 167      -9.436   5.956 -19.309  1.00163.77           O  
ANISOU 1021  O   PRO A 167    26240  22219  13768   -691   2360  -7206       O  
ATOM   1022  CB  PRO A 167      -8.917   2.749 -18.697  1.00143.41           C  
ANISOU 1022  CB  PRO A 167    22890  20803  10795   -586   2446  -6470       C  
ATOM   1023  CG  PRO A 167      -7.508   3.234 -18.639  1.00148.72           C  
ANISOU 1023  CG  PRO A 167    23514  21582  11413   -951   2401  -6615       C  
ATOM   1024  CD  PRO A 167      -7.127   3.612 -20.054  1.00153.82           C  
ANISOU 1024  CD  PRO A 167    24423  21678  12342  -1154   2351  -6606       C  
ATOM   1025  N   PRO A 168     -11.306   4.887 -18.667  1.00181.74           N  
ANISOU 1025  N   PRO A 168    28305  24825  15924    -84   2443  -7007       N  
ATOM   1026  CA  PRO A 168     -11.865   6.108 -18.046  1.00196.98           C  
ANISOU 1026  CA  PRO A 168    30411  26599  17832     73   2415  -7391       C  
ATOM   1027  C   PRO A 168     -11.276   6.383 -16.667  1.00193.42           C  
ANISOU 1027  C   PRO A 168    29787  26637  17067    -53   2457  -7569       C  
ATOM   1028  O   PRO A 168     -11.936   6.263 -15.628  1.00186.07           O  
ANISOU 1028  O   PRO A 168    28703  26073  15923    145   2527  -7617       O  
ATOM   1029  CB  PRO A 168     -13.364   5.794 -18.001  1.00196.86           C  
ANISOU 1029  CB  PRO A 168    30372  26589  17836    510   2449  -7341       C  
ATOM   1030  CG  PRO A 168     -13.425   4.313 -17.873  1.00188.83           C  
ANISOU 1030  CG  PRO A 168    29061  26019  16665    519   2542  -6938       C  
ATOM   1031  CD  PRO A 168     -12.283   3.783 -18.693  1.00177.73           C  
ANISOU 1031  CD  PRO A 168    27633  24522  15374    195   2508  -6725       C  
ATOM   1032  N   LEU A 169      -9.995   6.754 -16.657  1.00192.32           N  
ANISOU 1032  N   LEU A 169    29642  26530  16900   -434   2428  -7660       N  
ATOM   1033  CA  LEU A 169      -9.223   7.211 -15.502  1.00196.28           C  
ANISOU 1033  CA  LEU A 169    29986  27436  17157   -644   2456  -7880       C  
ATOM   1034  C   LEU A 169      -8.857   6.098 -14.525  1.00191.47           C  
ANISOU 1034  C   LEU A 169    28900  27587  16262   -681   2529  -7645       C  
ATOM   1035  O   LEU A 169      -8.144   6.365 -13.551  1.00195.57           O  
ANISOU 1035  O   LEU A 169    29208  28522  16578   -873   2550  -7800       O  
ATOM   1036  CB  LEU A 169      -9.934   8.329 -14.723  1.00198.56           C  
ANISOU 1036  CB  LEU A 169    30458  27598  17389   -457   2451  -8270       C  
ATOM   1037  CG  LEU A 169     -10.429   9.534 -15.529  1.00197.01           C  
ANISOU 1037  CG  LEU A 169    30732  26655  17469   -348   2341  -8552       C  
ATOM   1038  CD1 LEU A 169     -10.951  10.635 -14.613  1.00201.12           C  
ANISOU 1038  CD1 LEU A 169    31420  27109  17887   -165   2317  -8975       C  
ATOM   1039  CD2 LEU A 169      -9.337  10.066 -16.448  1.00196.57           C  
ANISOU 1039  CD2 LEU A 169    30876  26213  17599   -778   2282  -8587       C  
ATOM   1040  N   ILE A 170      -9.316   4.867 -14.738  1.00179.38           N  
ANISOU 1040  N   ILE A 170    27179  26265  14711   -513   2557  -7280       N  
ATOM   1041  CA  ILE A 170      -8.926   3.741 -13.887  1.00176.51           C  
ANISOU 1041  CA  ILE A 170    26359  26615  14093   -556   2588  -7018       C  
ATOM   1042  C   ILE A 170      -7.675   3.149 -14.529  1.00186.07           C  
ANISOU 1042  C   ILE A 170    27472  27889  15337   -799   2527  -6836       C  
ATOM   1043  O   ILE A 170      -7.740   2.267 -15.387  1.00190.35           O  
ANISOU 1043  O   ILE A 170    28026  28311  15986   -734   2502  -6550       O  
ATOM   1044  CB  ILE A 170     -10.050   2.720 -13.729  1.00172.99           C  
ANISOU 1044  CB  ILE A 170    25752  26394  13584   -278   2636  -6720       C  
ATOM   1045  CG1 ILE A 170     -11.317   3.402 -13.209  1.00172.20           C  
ANISOU 1045  CG1 ILE A 170    25750  26209  13469    -38   2696  -6938       C  
ATOM   1046  CG2 ILE A 170      -9.641   1.629 -12.767  1.00179.45           C  
ANISOU 1046  CG2 ILE A 170    26094  27967  14123   -329   2631  -6447       C  
ATOM   1047  CD1 ILE A 170     -12.443   3.452 -14.213  1.00164.25           C  
ANISOU 1047  CD1 ILE A 170    25048  24668  12691    224   2708  -6895       C  
ATOM   1048  N   SER A 171      -6.514   3.652 -14.111  1.00184.17           N  
ANISOU 1048  N   SER A 171    27121  27857  14997  -1087   2504  -7022       N  
ATOM   1049  CA  SER A 171      -5.277   3.348 -14.822  1.00186.13           C  
ANISOU 1049  CA  SER A 171    27309  28114  15296  -1343   2443  -6931       C  
ATOM   1050  C   SER A 171      -4.793   1.934 -14.521  1.00174.08           C  
ANISOU 1050  C   SER A 171    25386  27157  13598  -1281   2403  -6590       C  
ATOM   1051  O   SER A 171      -4.759   1.076 -15.410  1.00138.65           O  
ANISOU 1051  O   SER A 171    20919  22544   9217  -1208   2359  -6332       O  
ATOM   1052  CB  SER A 171      -4.210   4.382 -14.463  1.00187.05           C  
ANISOU 1052  CB  SER A 171    27420  28301  15349  -1690   2439  -7258       C  
ATOM   1053  OG  SER A 171      -4.653   5.687 -14.789  1.00186.76           O  
ANISOU 1053  OG  SER A 171    27790  27696  15474  -1746   2452  -7568       O  
ATOM   1054  N   ILE A 172      -4.419   1.670 -13.271  1.00183.53           N  
ANISOU 1054  N   ILE A 172    26217  28989  14527  -1299   2403  -6588       N  
ATOM   1055  CA  ILE A 172      -3.817   0.391 -12.913  1.00176.96           C  
ANISOU 1055  CA  ILE A 172    24999  28728  13509  -1241   2328  -6279       C  
ATOM   1056  C   ILE A 172      -4.380  -0.094 -11.586  1.00167.87           C  
ANISOU 1056  C   ILE A 172    23539  28146  12099  -1078   2342  -6152       C  
ATOM   1057  O   ILE A 172      -5.496   0.275 -11.201  1.00174.80           O  
ANISOU 1057  O   ILE A 172    24517  28919  12980   -945   2418  -6219       O  
ATOM   1058  CB  ILE A 172      -2.284   0.507 -12.848  1.00178.10           C  
ANISOU 1058  CB  ILE A 172    24926  29174  13571  -1508   2265  -6394       C  
ATOM   1059  N   GLU A 173      -3.609  -0.926 -10.890  1.00147.99           N  
ANISOU 1059  N   GLU A 173    20626  26255   9347  -1078   2257  -5966       N  
ATOM   1060  CA  GLU A 173      -4.003  -1.507  -9.607  1.00159.35           C  
ANISOU 1060  CA  GLU A 173    21722  28319  10506   -945   2240  -5787       C  
ATOM   1061  C   GLU A 173      -5.326  -2.261  -9.710  1.00159.40           C  
ANISOU 1061  C   GLU A 173    21798  28256  10512   -693   2258  -5472       C  
ATOM   1062  O   GLU A 173      -5.393  -3.456  -9.421  1.00153.90           O  
ANISOU 1062  O   GLU A 173    20886  27952   9638   -547   2167  -5081       O  
ATOM   1063  CB  GLU A 173      -4.096  -0.425  -8.526  1.00162.30           C  
ANISOU 1063  CB  GLU A 173    21996  28902  10770  -1071   2322  -6137       C  
ATOM   1064  N   PRO A 183       2.188   4.854  -5.211  1.00219.58           N  
ANISOU 1064  N   PRO A 183    28275  37700  17456  -2911   2468  -8277       N  
ATOM   1065  CA  PRO A 183       3.383   4.986  -6.046  1.00217.96           C  
ANISOU 1065  CA  PRO A 183    28084  37406  17327  -3191   2442  -8339       C  
ATOM   1066  C   PRO A 183       4.651   4.520  -5.337  1.00232.63           C  
ANISOU 1066  C   PRO A 183    29382  40064  18943  -3315   2380  -8334       C  
ATOM   1067  O   PRO A 183       5.738   4.597  -5.911  1.00221.69           O  
ANISOU 1067  O   PRO A 183    27913  38738  17580  -3557   2359  -8405       O  
ATOM   1068  CB  PRO A 183       3.444   6.494  -6.342  1.00213.74           C  
ANISOU 1068  CB  PRO A 183    27923  36373  16914  -3529   2546  -8771       C  
ATOM   1069  CG  PRO A 183       2.147   7.088  -5.789  1.00217.99           C  
ANISOU 1069  CG  PRO A 183    28705  36643  17478  -3341   2610  -8922       C  
ATOM   1070  CD  PRO A 183       1.238   5.947  -5.461  1.00215.49           C  
ANISOU 1070  CD  PRO A 183    28227  36545  17105  -2926   2560  -8547       C  
ATOM   1071  N   ALA A 184       4.509   4.045  -4.099  1.00251.27           N  
ANISOU 1071  N   ALA A 184    31342  43064  21064  -3150   2348  -8253       N  
ATOM   1072  CA  ALA A 184       5.659   3.523  -3.367  1.00257.68           C  
ANISOU 1072  CA  ALA A 184    31597  44683  21628  -3209   2269  -8225       C  
ATOM   1073  C   ALA A 184       6.148   2.219  -3.985  1.00262.66           C  
ANISOU 1073  C   ALA A 184    32073  45476  22249  -2980   2121  -7842       C  
ATOM   1074  O   ALA A 184       7.290   2.125  -4.450  1.00274.31           O  
ANISOU 1074  O   ALA A 184    33379  47128  23717  -3141   2074  -7903       O  
ATOM   1075  CB  ALA A 184       5.298   3.327  -1.893  1.00251.33           C  
ANISOU 1075  CB  ALA A 184    30414  44518  20561  -3074   2260  -8211       C  
ATOM   1076  N   GLU A 185       5.292   1.200  -3.999  1.00252.93           N  
ANISOU 1076  N   GLU A 185    30891  44206  21005  -2605   2044  -7453       N  
ATOM   1077  CA  GLU A 185       5.574  -0.073  -4.662  1.00238.56           C  
ANISOU 1077  CA  GLU A 185    29005  42447  19189  -2340   1897  -7077       C  
ATOM   1078  C   GLU A 185       4.384  -0.439  -5.542  1.00226.18           C  
ANISOU 1078  C   GLU A 185    27886  40215  17839  -2125   1912  -6831       C  
ATOM   1079  O   GLU A 185       3.656  -1.398  -5.260  1.00224.94           O  
ANISOU 1079  O   GLU A 185    27688  40190  17589  -1813   1841  -6476       O  
ATOM   1080  CB  GLU A 185       5.864  -1.173  -3.640  1.00233.04           C  
ANISOU 1080  CB  GLU A 185    27830  42538  18176  -2071   1751  -6794       C  
ATOM   1081  CG  GLU A 185       6.454  -2.445  -4.233  1.00215.39           C  
ANISOU 1081  CG  GLU A 185    25467  40478  15896  -1801   1570  -6468       C  
ATOM   1082  CD  GLU A 185       6.440  -3.604  -3.255  1.00209.23           C  
ANISOU 1082  CD  GLU A 185    24326  40375  14797  -1462   1411  -6107       C  
ATOM   1083  OE1 GLU A 185       5.615  -3.584  -2.317  1.00210.61           O  
ANISOU 1083  OE1 GLU A 185    24451  40737  14834  -1401   1450  -6006       O  
ATOM   1084  OE2 GLU A 185       7.255  -4.536  -3.423  1.00200.23           O  
ANISOU 1084  OE2 GLU A 185    22951  39598  13531  -1249   1239  -5922       O  
ATOM   1085  N   PRO A 186       4.151   0.316  -6.624  1.00213.11           N  
ANISOU 1085  N   PRO A 186    26662  37848  16464  -2297   2002  -7004       N  
ATOM   1086  CA  PRO A 186       2.986   0.036  -7.470  1.00211.21           C  
ANISOU 1086  CA  PRO A 186    26839  36976  16434  -2095   2025  -6796       C  
ATOM   1087  C   PRO A 186       3.269  -1.027  -8.519  1.00209.24           C  
ANISOU 1087  C   PRO A 186    26633  36591  16278  -1917   1907  -6499       C  
ATOM   1088  O   PRO A 186       3.797  -0.725  -9.594  1.00204.56           O  
ANISOU 1088  O   PRO A 186    26217  35636  15872  -2084   1912  -6611       O  
ATOM   1089  CB  PRO A 186       2.692   1.398  -8.108  1.00207.07           C  
ANISOU 1089  CB  PRO A 186    26744  35790  16145  -2361   2159  -7140       C  
ATOM   1090  CG  PRO A 186       4.040   2.044  -8.217  1.00207.08           C  
ANISOU 1090  CG  PRO A 186    26590  35977  16116  -2723   2166  -7425       C  
ATOM   1091  CD  PRO A 186       4.899   1.497  -7.094  1.00207.32           C  
ANISOU 1091  CD  PRO A 186    26059  36865  15849  -2697   2089  -7392       C  
ATOM   1092  N   ARG A 187       2.925  -2.277  -8.216  1.00212.10           N  
ANISOU 1092  N   ARG A 187    26831  37259  16497  -1586   1794  -6118       N  
ATOM   1093  CA  ARG A 187       3.107  -3.353  -9.180  1.00213.52           C  
ANISOU 1093  CA  ARG A 187    27062  37314  16751  -1374   1668  -5835       C  
ATOM   1094  C   ARG A 187       2.248  -3.107 -10.414  1.00208.22           C  
ANISOU 1094  C   ARG A 187    26870  35856  16390  -1376   1748  -5818       C  
ATOM   1095  O   ARG A 187       1.056  -2.804 -10.304  1.00216.83           O  
ANISOU 1095  O   ARG A 187    28207  36623  17556  -1315   1847  -5786       O  
ATOM   1096  CB  ARG A 187       2.754  -4.701  -8.546  1.00215.89           C  
ANISOU 1096  CB  ARG A 187    27149  38067  16813  -1010   1526  -5408       C  
ATOM   1097  CG  ARG A 187       1.414  -4.736  -7.831  1.00221.83           C  
ANISOU 1097  CG  ARG A 187    27997  38795  17492   -896   1601  -5237       C  
ATOM   1098  CD  ARG A 187       0.900  -6.162  -7.689  1.00229.35           C  
ANISOU 1098  CD  ARG A 187    28888  39979  18277   -549   1455  -4730       C  
ATOM   1099  NE  ARG A 187       1.876  -7.046  -7.059  1.00240.27           N  
ANISOU 1099  NE  ARG A 187    29887  42034  19371   -381   1260  -4537       N  
ATOM   1100  CZ  ARG A 187       1.668  -8.337  -6.818  1.00244.00           C  
ANISOU 1100  CZ  ARG A 187    30277  42799  19632    -60   1082  -4068       C  
ATOM   1101  NH1 ARG A 187       0.514  -8.899  -7.154  1.00240.65           N  
ANISOU 1101  NH1 ARG A 187    30113  42066  19256     90   1087  -3737       N  
ATOM   1102  NH2 ARG A 187       2.612  -9.067  -6.241  1.00249.49           N  
ANISOU 1102  NH2 ARG A 187    30636  44101  20057    118    889  -3914       N  
ATOM   1103  N   CYS A 188       2.858  -3.228 -11.595  1.00183.15           N  
ANISOU 1103  N   CYS A 188    23801  32400  13387  -1442   1702  -5850       N  
ATOM   1104  CA  CYS A 188       2.139  -3.019 -12.852  1.00147.57           C  
ANISOU 1104  CA  CYS A 188    19727  27166   9177  -1451   1764  -5832       C  
ATOM   1105  C   CYS A 188       1.156  -4.169 -13.050  1.00144.64           C  
ANISOU 1105  C   CYS A 188    19444  26711   8800  -1097   1704  -5450       C  
ATOM   1106  O   CYS A 188       1.354  -5.076 -13.862  1.00142.43           O  
ANISOU 1106  O   CYS A 188    19170  26370   8578   -933   1594  -5258       O  
ATOM   1107  CB  CYS A 188       3.098  -2.901 -14.031  1.00146.60           C  
ANISOU 1107  CB  CYS A 188    19641  26846   9214  -1629   1720  -5953       C  
ATOM   1108  SG  CYS A 188       4.243  -1.510 -13.957  1.00183.20           S  
ANISOU 1108  SG  CYS A 188    24200  31556  13854  -2112   1800  -6384       S  
ATOM   1109  N   GLU A 189       0.075  -4.127 -12.276  1.00144.94           N  
ANISOU 1109  N   GLU A 189    19536  26779   8756   -984   1775  -5347       N  
ATOM   1110  CA  GLU A 189      -1.043  -5.049 -12.414  1.00142.49           C  
ANISOU 1110  CA  GLU A 189    19337  26367   8437   -701   1751  -4993       C  
ATOM   1111  C   GLU A 189      -2.274  -4.232 -12.772  1.00148.37           C  
ANISOU 1111  C   GLU A 189    20446  26536   9393   -747   1915  -5116       C  
ATOM   1112  O   GLU A 189      -2.735  -3.415 -11.967  1.00167.71           O  
ANISOU 1112  O   GLU A 189    22896  29038  11787   -827   2017  -5300       O  
ATOM   1113  CB  GLU A 189      -1.274  -5.845 -11.128  1.00144.98           C  
ANISOU 1113  CB  GLU A 189    19341  27322   8423   -511   1672  -4706       C  
ATOM   1114  N   ILE A 190      -2.795  -4.443 -13.982  1.00137.05           N  
ANISOU 1114  N   ILE A 190    19307  24571   8195   -679   1932  -5034       N  
ATOM   1115  CA  ILE A 190      -3.906  -3.629 -14.454  1.00135.45           C  
ANISOU 1115  CA  ILE A 190    19462  23790   8212   -700   2073  -5174       C  
ATOM   1116  C   ILE A 190      -5.132  -3.860 -13.576  1.00146.93           C  
ANISOU 1116  C   ILE A 190    20858  25445   9524   -522   2133  -5017       C  
ATOM   1117  O   ILE A 190      -5.284  -4.892 -12.911  1.00150.59           O  
ANISOU 1117  O   ILE A 190    21068  26395   9754   -363   2055  -4690       O  
ATOM   1118  CB  ILE A 190      -4.219  -3.921 -15.931  1.00137.62           C  
ANISOU 1118  CB  ILE A 190    20026  23505   8757   -649   2069  -5090       C  
ATOM   1119  CG1 ILE A 190      -5.122  -5.148 -16.071  1.00133.78           C  
ANISOU 1119  CG1 ILE A 190    19515  23099   8215   -375   2034  -4709       C  
ATOM   1120  CG2 ILE A 190      -2.930  -4.129 -16.711  1.00134.43           C  
ANISOU 1120  CG2 ILE A 190    19553  23103   8422   -780   1967  -5142       C  
ATOM   1121  CD1 ILE A 190      -5.459  -5.497 -17.510  1.00125.54           C  
ANISOU 1121  CD1 ILE A 190    18729  21537   7432   -321   2033  -4635       C  
ATOM   1122  N   ASN A 191      -6.011  -2.863 -13.558  1.00161.05           N  
ANISOU 1122  N   ASN A 191    22878  26875  11440   -543   2258  -5248       N  
ATOM   1123  CA  ASN A 191      -7.230  -2.953 -12.771  1.00177.20           C  
ANISOU 1123  CA  ASN A 191    24854  29109  13364   -384   2325  -5153       C  
ATOM   1124  C   ASN A 191      -8.144  -4.035 -13.334  1.00169.09           C  
ANISOU 1124  C   ASN A 191    23876  28005  12364   -176   2311  -4778       C  
ATOM   1125  O   ASN A 191      -8.129  -4.336 -14.530  1.00156.37           O  
ANISOU 1125  O   ASN A 191    22479  25975  10960   -147   2294  -4709       O  
ATOM   1126  CB  ASN A 191      -7.956  -1.609 -12.752  1.00188.72           C  
ANISOU 1126  CB  ASN A 191    26572  30164  14971   -409   2443  -5526       C  
ATOM   1127  CG  ASN A 191      -9.087  -1.574 -11.743  1.00205.70           C  
ANISOU 1127  CG  ASN A 191    28568  32629  16959   -264   2508  -5504       C  
ATOM   1128  OD1 ASN A 191     -10.203  -2.010 -12.027  1.00209.93           O  
ANISOU 1128  OD1 ASN A 191    29165  33063  17537    -85   2546  -5325       O  
ATOM   1129  ND2 ASN A 191      -8.806  -1.045 -10.558  1.00214.37           N  
ANISOU 1129  ND2 ASN A 191    29439  34147  17865   -352   2521  -5697       N  
ATOM   1130  N   ASP A 192      -8.950  -4.624 -12.451  1.00169.28           N  
ANISOU 1130  N   ASP A 192    23686  28466  12168    -48   2315  -4528       N  
ATOM   1131  CA  ASP A 192      -9.839  -5.726 -12.811  1.00160.32           C  
ANISOU 1131  CA  ASP A 192    22551  27366  10996    131   2290  -4114       C  
ATOM   1132  C   ASP A 192     -11.254  -5.433 -12.313  1.00162.75           C  
ANISOU 1132  C   ASP A 192    22841  27734  11263    223   2401  -4124       C  
ATOM   1133  O   ASP A 192     -11.819  -6.163 -11.499  1.00167.97           O  
ANISOU 1133  O   ASP A 192    23260  28885  11675    281   2373  -3798       O  
ATOM   1134  CB  ASP A 192      -9.321  -7.050 -12.251  1.00160.77           C  
ANISOU 1134  CB  ASP A 192    22333  27990  10763    199   2132  -3655       C  
ATOM   1135  N   GLN A 193     -11.833  -4.343 -12.810  1.00162.54           N  
ANISOU 1135  N   GLN A 193    23072  27210  11475    238   2514  -4494       N  
ATOM   1136  CA  GLN A 193     -13.228  -4.050 -12.516  1.00167.28           C  
ANISOU 1136  CA  GLN A 193    23664  27825  12068    373   2609  -4542       C  
ATOM   1137  C   GLN A 193     -14.127  -5.059 -13.219  1.00147.74           C  
ANISOU 1137  C   GLN A 193    21225  25282   9629    518   2608  -4163       C  
ATOM   1138  O   GLN A 193     -13.837  -5.503 -14.334  1.00133.33           O  
ANISOU 1138  O   GLN A 193    19596  22962   8100    540   2544  -3978       O  
ATOM   1139  CB  GLN A 193     -13.586  -2.629 -12.953  1.00180.12           C  
ANISOU 1139  CB  GLN A 193    25599  28891  13946    406   2697  -5029       C  
ATOM   1140  CG  GLN A 193     -15.006  -2.212 -12.591  1.00191.27           C  
ANISOU 1140  CG  GLN A 193    26978  30350  15345    587   2781  -5147       C  
ATOM   1141  CD  GLN A 193     -15.441  -0.934 -13.281  1.00190.59           C  
ANISOU 1141  CD  GLN A 193    27276  29604  15537    692   2837  -5570       C  
ATOM   1142  OE1 GLN A 193     -14.612  -0.148 -13.739  1.00193.08           O  
ANISOU 1142  OE1 GLN A 193    27866  29489  16008    584   2814  -5820       O  
ATOM   1143  NE2 GLN A 193     -16.750  -0.724 -13.364  1.00184.50           N  
ANISOU 1143  NE2 GLN A 193    26526  28759  14818    909   2894  -5635       N  
ATOM   1144  N   LYS A 194     -15.226  -5.424 -12.556  1.00160.12           N  
ANISOU 1144  N   LYS A 194    22588  27230  11022    600   2644  -3972       N  
ATOM   1145  CA  LYS A 194     -16.129  -6.426 -13.112  1.00164.26           C  
ANISOU 1145  CA  LYS A 194    23122  27593  11697    698   2608  -3496       C  
ATOM   1146  C   LYS A 194     -16.787  -5.950 -14.401  1.00173.73           C  
ANISOU 1146  C   LYS A 194    24636  28045  13328    832   2658  -3646       C  
ATOM   1147  O   LYS A 194     -17.152  -6.775 -15.247  1.00173.55           O  
ANISOU 1147  O   LYS A 194    24704  27635  13602    883   2592  -3249       O  
ATOM   1148  CB  LYS A 194     -17.195  -6.800 -12.082  1.00162.21           C  
ANISOU 1148  CB  LYS A 194    22558  27983  11092    705   2657  -3316       C  
ATOM   1149  N   TRP A 195     -16.943  -4.638 -14.577  1.00187.47           N  
ANISOU 1149  N   TRP A 195    26560  29561  15108    895   2763  -4211       N  
ATOM   1150  CA  TRP A 195     -17.610  -4.091 -15.753  1.00188.76           C  
ANISOU 1150  CA  TRP A 195    27039  29033  15647   1050   2801  -4369       C  
ATOM   1151  C   TRP A 195     -16.683  -3.256 -16.629  1.00180.38           C  
ANISOU 1151  C   TRP A 195    26335  27371  14830    972   2792  -4689       C  
ATOM   1152  O   TRP A 195     -17.158  -2.594 -17.559  1.00184.54           O  
ANISOU 1152  O   TRP A 195    27166  27315  15635   1091   2821  -4882       O  
ATOM   1153  CB  TRP A 195     -18.831  -3.269 -15.336  1.00195.19           C  
ANISOU 1153  CB  TRP A 195    27813  30024  16326   1245   2912  -4734       C  
ATOM   1154  CG  TRP A 195     -20.040  -4.116 -15.081  1.00200.30           C  
ANISOU 1154  CG  TRP A 195    28198  31025  16881   1338   2925  -4375       C  
ATOM   1155  CD1 TRP A 195     -20.157  -5.120 -14.166  1.00201.55           C  
ANISOU 1155  CD1 TRP A 195    28008  31833  16739   1210   2898  -3976       C  
ATOM   1156  CD2 TRP A 195     -21.304  -4.034 -15.751  1.00208.89           C  
ANISOU 1156  CD2 TRP A 195    29351  31865  18155   1553   2966  -4378       C  
ATOM   1157  NE1 TRP A 195     -21.414  -5.671 -14.224  1.00207.07           N  
ANISOU 1157  NE1 TRP A 195    28556  32703  17420   1288   2927  -3730       N  
ATOM   1158  CE2 TRP A 195     -22.138  -5.021 -15.188  1.00212.55           C  
ANISOU 1158  CE2 TRP A 195    29477  32878  18405   1509   2973  -3986       C  
ATOM   1159  CE3 TRP A 195     -21.812  -3.223 -16.770  1.00211.93           C  
ANISOU 1159  CE3 TRP A 195    30047  31633  18844   1773   2990  -4666       C  
ATOM   1160  CZ2 TRP A 195     -23.451  -5.218 -15.611  1.00216.49           C  
ANISOU 1160  CZ2 TRP A 195    29910  33371  18976   1662   3016  -3906       C  
ATOM   1161  CZ3 TRP A 195     -23.117  -3.421 -17.188  1.00213.76           C  
ANISOU 1161  CZ3 TRP A 195    30211  31853  19154   1974   3021  -4580       C  
ATOM   1162  CH2 TRP A 195     -23.921  -4.410 -16.609  1.00214.58           C  
ANISOU 1162  CH2 TRP A 195    29944  32553  19032   1911   3040  -4218       C  
ATOM   1163  N   TYR A 196     -15.380  -3.263 -16.356  1.00162.37           N  
ANISOU 1163  N   TYR A 196    24020  25245  12427    764   2747  -4749       N  
ATOM   1164  CA  TYR A 196     -14.394  -2.698 -17.269  1.00141.97           C  
ANISOU 1164  CA  TYR A 196    21741  22142  10059    618   2724  -4963       C  
ATOM   1165  C   TYR A 196     -13.648  -3.762 -18.059  1.00135.12           C  
ANISOU 1165  C   TYR A 196    20854  21083   9404    547   2601  -4537       C  
ATOM   1166  O   TYR A 196     -13.257  -3.511 -19.204  1.00152.88           O  
ANISOU 1166  O   TYR A 196    23370  22778  11941    486   2577  -4594       O  
ATOM   1167  CB  TYR A 196     -13.381  -1.838 -16.503  1.00158.11           C  
ANISOU 1167  CB  TYR A 196    23763  24352  11959    434   2711  -5279       C  
ATOM   1168  CG  TYR A 196     -12.160  -1.463 -17.314  1.00159.09           C  
ANISOU 1168  CG  TYR A 196    24096  24088  12262    230   2649  -5395       C  
ATOM   1169  CD1 TYR A 196     -12.222  -0.471 -18.283  1.00157.14           C  
ANISOU 1169  CD1 TYR A 196    24221  23172  12313    223   2640  -5634       C  
ATOM   1170  CD2 TYR A 196     -10.946  -2.111 -17.116  1.00165.15           C  
ANISOU 1170  CD2 TYR A 196    24656  25195  12897     55   2571  -5248       C  
ATOM   1171  CE1 TYR A 196     -11.109  -0.129 -19.029  1.00160.37           C  
ANISOU 1171  CE1 TYR A 196    24764  23287  12881     -4   2565  -5708       C  
ATOM   1172  CE2 TYR A 196      -9.828  -1.776 -17.857  1.00164.66           C  
ANISOU 1172  CE2 TYR A 196    24731  24848  12986   -143   2508  -5357       C  
ATOM   1173  CZ  TYR A 196      -9.915  -0.784 -18.811  1.00162.01           C  
ANISOU 1173  CZ  TYR A 196    24745  23872  12942   -194   2511  -5579       C  
ATOM   1174  OH  TYR A 196      -8.804  -0.448 -19.551  1.00161.79           O  
ANISOU 1174  OH  TYR A 196    24807  23615  13049   -433   2440  -5663       O  
ATOM   1175  N   VAL A 197     -13.445  -4.942 -17.467  1.00129.99           N  
ANISOU 1175  N   VAL A 197    19899  20885   8606    559   2510  -4118       N  
ATOM   1176  CA  VAL A 197     -12.807  -6.045 -18.179  1.00125.26           C  
ANISOU 1176  CA  VAL A 197    19275  20103   8215    552   2366  -3712       C  
ATOM   1177  C   VAL A 197     -13.611  -6.417 -19.417  1.00120.77           C  
ANISOU 1177  C   VAL A 197    18903  18923   8063    681   2351  -3481       C  
ATOM   1178  O   VAL A 197     -13.050  -6.650 -20.495  1.00115.47           O  
ANISOU 1178  O   VAL A 197    18374  17832   7667    648   2281  -3418       O  
ATOM   1179  CB  VAL A 197     -12.633  -7.250 -17.235  1.00127.66           C  
ANISOU 1179  CB  VAL A 197    19257  20969   8279    586   2253  -3275       C  
ATOM   1180  CG1 VAL A 197     -12.316  -8.510 -18.026  1.00143.43           C  
ANISOU 1180  CG1 VAL A 197    21264  22683  10550    659   2086  -2810       C  
ATOM   1181  CG2 VAL A 197     -11.549  -6.968 -16.209  1.00130.61           C  
ANISOU 1181  CG2 VAL A 197    19429  21937   8260    453   2238  -3491       C  
ATOM   1182  N   ILE A 198     -14.937  -6.469 -19.283  1.00124.87           N  
ANISOU 1182  N   ILE A 198    19404  19430   8609    824   2417  -3376       N  
ATOM   1183  CA  ILE A 198     -15.791  -6.856 -20.403  1.00128.96           C  
ANISOU 1183  CA  ILE A 198    20072  19437   9491    949   2408  -3156       C  
ATOM   1184  C   ILE A 198     -15.690  -5.830 -21.525  1.00139.01           C  
ANISOU 1184  C   ILE A 198    21681  20112  11023    947   2460  -3500       C  
ATOM   1185  O   ILE A 198     -15.564  -6.182 -22.704  1.00138.17           O  
ANISOU 1185  O   ILE A 198    21719  19543  11237    955   2404  -3348       O  
ATOM   1186  CB  ILE A 198     -17.244  -7.032 -19.929  1.00128.01           C  
ANISOU 1186  CB  ILE A 198    19824  19538   9278   1084   2481  -3030       C  
ATOM   1187  CG1 ILE A 198     -17.288  -7.870 -18.651  1.00137.95           C  
ANISOU 1187  CG1 ILE A 198    20760  21464  10192   1022   2441  -2728       C  
ATOM   1188  CG2 ILE A 198     -18.084  -7.681 -21.015  1.00137.88           C  
ANISOU 1188  CG2 ILE A 198    21163  20354  10871   1188   2456  -2733       C  
ATOM   1189  CD1 ILE A 198     -18.660  -7.943 -18.019  1.00141.80           C  
ANISOU 1189  CD1 ILE A 198    21071  22316  10491   1095   2528  -2658       C  
ATOM   1190  N   SER A 199     -15.740  -4.544 -21.173  1.00132.12           N  
ANISOU 1190  N   SER A 199    20952  19239  10011    930   2559  -3968       N  
ATOM   1191  CA  SER A 199     -15.690  -3.492 -22.183  1.00130.56           C  
ANISOU 1191  CA  SER A 199    21129  18442  10035    915   2596  -4285       C  
ATOM   1192  C   SER A 199     -14.359  -3.504 -22.926  1.00128.51           C  
ANISOU 1192  C   SER A 199    20994  17944   9889    682   2529  -4311       C  
ATOM   1193  O   SER A 199     -14.321  -3.402 -24.157  1.00123.76           O  
ANISOU 1193  O   SER A 199    20623  16825   9576    664   2504  -4273       O  
ATOM   1194  CB  SER A 199     -15.934  -2.130 -21.531  1.00145.51           C  
ANISOU 1194  CB  SER A 199    23172  20384  11732    937   2692  -4795       C  
ATOM   1195  OG  SER A 199     -15.809  -1.081 -22.474  1.00149.41           O  
ANISOU 1195  OG  SER A 199    24086  20256  12426    898   2706  -5086       O  
ATOM   1196  N   SER A 200     -13.254  -3.638 -22.190  1.00143.39           N  
ANISOU 1196  N   SER A 200    22702  20258  11524    497   2499  -4383       N  
ATOM   1197  CA  SER A 200     -11.939  -3.626 -22.823  1.00158.94           C  
ANISOU 1197  CA  SER A 200    24736  22113  13541    262   2438  -4457       C  
ATOM   1198  C   SER A 200     -11.738  -4.845 -23.715  1.00145.10           C  
ANISOU 1198  C   SER A 200    22883  20203  12045    329   2318  -4045       C  
ATOM   1199  O   SER A 200     -11.139  -4.742 -24.792  1.00138.22           O  
ANISOU 1199  O   SER A 200    22161  18996  11359    204   2281  -4094       O  
ATOM   1200  CB  SER A 200     -10.845  -3.557 -21.758  1.00179.13           C  
ANISOU 1200  CB  SER A 200    27068  25259  15732     79   2427  -4634       C  
ATOM   1201  OG  SER A 200      -9.557  -3.605 -22.346  1.00201.22           O  
ANISOU 1201  OG  SER A 200    29874  28042  18540   -149   2364  -4718       O  
ATOM   1202  N   CYS A 201     -12.232  -6.009 -23.286  1.00121.73           N  
ANISOU 1202  N   CYS A 201    19679  17484   9088    510   2250  -3644       N  
ATOM   1203  CA  CYS A 201     -12.022  -7.230 -24.059  1.00106.58           C  
ANISOU 1203  CA  CYS A 201    17674  15409   7414    587   2116  -3265       C  
ATOM   1204  C   CYS A 201     -12.816  -7.208 -25.358  1.00108.63           C  
ANISOU 1204  C   CYS A 201    18150  15084   8042    673   2138  -3180       C  
ATOM   1205  O   CYS A 201     -12.266  -7.461 -26.436  1.00115.08           O  
ANISOU 1205  O   CYS A 201    19036  15611   9077    618   2071  -3150       O  
ATOM   1206  CB  CYS A 201     -12.386  -8.454 -23.219  1.00117.79           C  
ANISOU 1206  CB  CYS A 201    18830  17194   8733    731   2027  -2845       C  
ATOM   1207  SG  CYS A 201     -11.168  -8.855 -21.947  1.00145.99           S  
ANISOU 1207  SG  CYS A 201    22114  21447  11907    661   1928  -2830       S  
ATOM   1208  N   ILE A 202     -14.115  -6.905 -25.282  1.00112.15           N  
ANISOU 1208  N   ILE A 202    18677  15395   8540    814   2229  -3158       N  
ATOM   1209  CA  ILE A 202     -14.923  -6.834 -26.493  1.00118.16           C  
ANISOU 1209  CA  ILE A 202    19631  15643   9624    915   2252  -3093       C  
ATOM   1210  C   ILE A 202     -14.615  -5.598 -27.322  1.00122.60           C  
ANISOU 1210  C   ILE A 202    20516  15793  10273    801   2308  -3447       C  
ATOM   1211  O   ILE A 202     -15.074  -5.502 -28.463  1.00124.88           O  
ANISOU 1211  O   ILE A 202    20981  15644  10824    858   2309  -3398       O  
ATOM   1212  CB  ILE A 202     -16.433  -6.875 -26.174  1.00114.89           C  
ANISOU 1212  CB  ILE A 202    19180  15264   9209   1116   2327  -2984       C  
ATOM   1213  CG1 ILE A 202     -16.945  -5.490 -25.767  1.00126.41           C  
ANISOU 1213  CG1 ILE A 202    20814  16698  10517   1170   2445  -3388       C  
ATOM   1214  CG2 ILE A 202     -16.726  -7.909 -25.096  1.00103.33           C  
ANISOU 1214  CG2 ILE A 202    17412  14290   7556   1154   2288  -2667       C  
ATOM   1215  CD1 ILE A 202     -17.959  -4.910 -26.740  1.00122.27           C  
ANISOU 1215  CD1 ILE A 202    20527  15712  10218   1341   2492  -3473       C  
ATOM   1216  N   GLY A 203     -13.852  -4.652 -26.782  1.00115.76           N  
ANISOU 1216  N   GLY A 203    19743  15058   9182    623   2351  -3795       N  
ATOM   1217  CA  GLY A 203     -13.477  -3.472 -27.534  1.00111.21           C  
ANISOU 1217  CA  GLY A 203    19516  14072   8665    453   2392  -4116       C  
ATOM   1218  C   GLY A 203     -12.158  -3.645 -28.256  1.00115.91           C  
ANISOU 1218  C   GLY A 203    20112  14632   9296    183   2324  -4145       C  
ATOM   1219  O   GLY A 203     -11.862  -2.923 -29.213  1.00107.77           O  
ANISOU 1219  O   GLY A 203    19365  13213   8371     10   2336  -4303       O  
ATOM   1220  N   SER A 204     -11.357  -4.611 -27.805  1.00118.79           N  
ANISOU 1220  N   SER A 204    20155  15426   9555    150   2241  -3991       N  
ATOM   1221  CA  SER A 204     -10.042  -4.871 -28.373  1.00128.82           C  
ANISOU 1221  CA  SER A 204    21344  16795  10809    -72   2162  -4049       C  
ATOM   1222  C   SER A 204      -9.999  -6.177 -29.157  1.00135.47           C  
ANISOU 1222  C   SER A 204    21999  17576  11896     78   2038  -3709       C  
ATOM   1223  O   SER A 204      -9.619  -6.182 -30.330  1.00154.06           O  
ANISOU 1223  O   SER A 204    24439  19675  14423    -29   2004  -3735       O  
ATOM   1224  CB  SER A 204      -8.984  -4.886 -27.260  1.00129.78           C  
ANISOU 1224  CB  SER A 204    21232  17496  10581   -214   2141  -4211       C  
ATOM   1225  OG  SER A 204      -8.879  -3.619 -26.634  1.00124.45           O  
ANISOU 1225  OG  SER A 204    20743  16864   9679   -407   2255  -4587       O  
ATOM   1226  N   PHE A 205     -10.381  -7.293 -28.537  1.00111.49           N  
ANISOU 1226  N   PHE A 205    18720  14768   8872    312   1963  -3393       N  
ATOM   1227  CA  PHE A 205     -10.234  -8.596 -29.174  1.00104.75           C  
ANISOU 1227  CA  PHE A 205    17698  13861   8241    456   1820  -3089       C  
ATOM   1228  C   PHE A 205     -11.526  -9.082 -29.819  1.00111.83           C  
ANISOU 1228  C   PHE A 205    18680  14372   9441    647   1834  -2816       C  
ATOM   1229  O   PHE A 205     -11.545  -9.392 -31.014  1.00114.60           O  
ANISOU 1229  O   PHE A 205    19082  14411  10052    657   1791  -2758       O  
ATOM   1230  CB  PHE A 205      -9.743  -9.623 -28.149  1.00 99.36           C  
ANISOU 1230  CB  PHE A 205    16727  13639   7388    580   1692  -2882       C  
ATOM   1231  CG  PHE A 205      -9.602 -11.020 -28.697  1.00114.24           C  
ANISOU 1231  CG  PHE A 205    18468  15436   9503    764   1515  -2568       C  
ATOM   1232  CD1 PHE A 205      -8.439 -11.413 -29.337  1.00 99.66           C  
ANISOU 1232  CD1 PHE A 205    16500  13673   7693    736   1385  -2674       C  
ATOM   1233  CD2 PHE A 205     -10.628 -11.943 -28.559  1.00120.92           C  
ANISOU 1233  CD2 PHE A 205    19295  16134  10514    958   1471  -2187       C  
ATOM   1234  CE1 PHE A 205      -8.305 -12.695 -29.838  1.00101.59           C  
ANISOU 1234  CE1 PHE A 205    16624  13817   8160    941   1204  -2424       C  
ATOM   1235  CE2 PHE A 205     -10.500 -13.225 -29.060  1.00115.09           C  
ANISOU 1235  CE2 PHE A 205    18466  15263  10001   1118   1296  -1913       C  
ATOM   1236  CZ  PHE A 205      -9.336 -13.602 -29.700  1.00111.61           C  
ANISOU 1236  CZ  PHE A 205    17919  14869   9618   1133   1156  -2039       C  
ATOM   1237  N   PHE A 206     -12.613  -9.136 -29.047  1.00 96.42           N  
ANISOU 1237  N   PHE A 206    16719  12483   7432    783   1898  -2668       N  
ATOM   1238  CA  PHE A 206     -13.785  -9.903 -29.456  1.00 97.47           C  
ANISOU 1238  CA  PHE A 206    16840  12391   7802    960   1889  -2355       C  
ATOM   1239  C   PHE A 206     -14.488  -9.280 -30.658  1.00 96.59           C  
ANISOU 1239  C   PHE A 206    16953  11821   7928    973   1969  -2456       C  
ATOM   1240  O   PHE A 206     -14.811  -9.979 -31.625  1.00 98.96           O  
ANISOU 1240  O   PHE A 206    17240  11865   8497   1043   1916  -2273       O  
ATOM   1241  CB  PHE A 206     -14.742 -10.053 -28.274  1.00110.09           C  
ANISOU 1241  CB  PHE A 206    18343  14269   9217   1058   1946  -2202       C  
ATOM   1242  CG  PHE A 206     -14.253 -11.011 -27.223  1.00128.34           C  
ANISOU 1242  CG  PHE A 206    20428  16994  11343   1075   1833  -1959       C  
ATOM   1243  CD1 PHE A 206     -13.435 -10.578 -26.191  1.00141.74           C  
ANISOU 1243  CD1 PHE A 206    22032  19106  12716    989   1835  -2135       C  
ATOM   1244  CD2 PHE A 206     -14.602 -12.349 -27.277  1.00123.95           C  
ANISOU 1244  CD2 PHE A 206    19766  16401  10929   1170   1714  -1551       C  
ATOM   1245  CE1 PHE A 206     -12.982 -11.465 -25.227  1.00138.03           C  
ANISOU 1245  CE1 PHE A 206    21357  19034  12056   1024   1715  -1889       C  
ATOM   1246  CE2 PHE A 206     -14.153 -13.240 -26.318  1.00126.05           C  
ANISOU 1246  CE2 PHE A 206    19868  17007  11019   1196   1584  -1293       C  
ATOM   1247  CZ  PHE A 206     -13.342 -12.797 -25.291  1.00127.99           C  
ANISOU 1247  CZ  PHE A 206    20011  17690  10930   1136   1581  -1453       C  
ATOM   1248  N   ALA A 207     -14.745  -7.967 -30.619  1.00 93.90           N  
ANISOU 1248  N   ALA A 207    16830  11362   7488    918   2087  -2749       N  
ATOM   1249  CA  ALA A 207     -15.454  -7.345 -31.738  1.00 96.25           C  
ANISOU 1249  CA  ALA A 207    17365  11214   7991    964   2145  -2823       C  
ATOM   1250  C   ALA A 207     -14.650  -7.393 -33.032  1.00104.97           C  
ANISOU 1250  C   ALA A 207    18549  12057   9277    817   2083  -2864       C  
ATOM   1251  O   ALA A 207     -15.217  -7.791 -34.065  1.00103.62           O  
ANISOU 1251  O   ALA A 207    18402  11616   9355    904   2065  -2718       O  
ATOM   1252  CB  ALA A 207     -15.868  -5.915 -31.378  1.00 94.43           C  
ANISOU 1252  CB  ALA A 207    17392  10876   7611    966   2255  -3134       C  
ATOM   1253  N   PRO A 208     -13.364  -7.014 -33.070  1.00104.66           N  
ANISOU 1253  N   PRO A 208    18531  12125   9109    580   2052  -3070       N  
ATOM   1254  CA  PRO A 208     -12.626  -7.156 -34.337  1.00101.34           C  
ANISOU 1254  CA  PRO A 208    18134  11532   8839    427   1990  -3104       C  
ATOM   1255  C   PRO A 208     -12.522  -8.595 -34.807  1.00105.63           C  
ANISOU 1255  C   PRO A 208    18411  12139   9584    560   1868  -2844       C  
ATOM   1256  O   PRO A 208     -12.698  -8.863 -36.002  1.00103.53           O  
ANISOU 1256  O   PRO A 208    18170  11622   9544    568   1840  -2782       O  
ATOM   1257  CB  PRO A 208     -11.249  -6.560 -34.011  1.00104.33           C  
ANISOU 1257  CB  PRO A 208    18517  12158   8966    133   1982  -3385       C  
ATOM   1258  CG  PRO A 208     -11.489  -5.658 -32.862  1.00 99.57           C  
ANISOU 1258  CG  PRO A 208    18042  11661   8127    109   2076  -3560       C  
ATOM   1259  CD  PRO A 208     -12.543  -6.340 -32.047  1.00 95.80           C  
ANISOU 1259  CD  PRO A 208    17415  11305   7682    410   2083  -3319       C  
ATOM   1260  N   CYS A 209     -12.246  -9.532 -33.896  1.00106.19           N  
ANISOU 1260  N   CYS A 209    18240  12530   9577    668   1785  -2689       N  
ATOM   1261  CA  CYS A 209     -12.125 -10.932 -34.291  1.00 99.37           C  
ANISOU 1261  CA  CYS A 209    17164  11677   8914    813   1642  -2445       C  
ATOM   1262  C   CYS A 209     -13.443 -11.472 -34.832  1.00108.15           C  
ANISOU 1262  C   CYS A 209    18313  12491  10289    979   1665  -2197       C  
ATOM   1263  O   CYS A 209     -13.459 -12.191 -35.836  1.00105.37           O  
ANISOU 1263  O   CYS A 209    17898  11954  10182   1029   1588  -2106       O  
ATOM   1264  CB  CYS A 209     -11.643 -11.776 -33.111  1.00110.33           C  
ANISOU 1264  CB  CYS A 209    18341  13434  10146    912   1532  -2298       C  
ATOM   1265  SG  CYS A 209      -9.905 -11.530 -32.684  1.00148.45           S  
ANISOU 1265  SG  CYS A 209    23021  18693  14692    757   1450  -2576       S  
ATOM   1266  N   LEU A 210     -14.560 -11.135 -34.182  1.00 95.89           N  
ANISOU 1266  N   LEU A 210    16838  10926   8671   1063   1771  -2112       N  
ATOM   1267  CA  LEU A 210     -15.857 -11.591 -34.675  1.00 94.19           C  
ANISOU 1267  CA  LEU A 210    16633  10492   8664   1201   1806  -1904       C  
ATOM   1268  C   LEU A 210     -16.155 -11.017 -36.054  1.00 94.41           C  
ANISOU 1268  C   LEU A 210    16816  10177   8879   1175   1856  -2026       C  
ATOM   1269  O   LEU A 210     -16.629 -11.733 -36.943  1.00102.14           O  
ANISOU 1269  O   LEU A 210    17734  10976  10098   1243   1818  -1880       O  
ATOM   1270  CB  LEU A 210     -16.962 -11.217 -33.687  1.00 93.50           C  
ANISOU 1270  CB  LEU A 210    16568  10546   8413   1289   1917  -1849       C  
ATOM   1271  CG  LEU A 210     -18.396 -11.482 -34.156  1.00 98.48           C  
ANISOU 1271  CG  LEU A 210    17198  11021   9197   1417   1980  -1692       C  
ATOM   1272  CD1 LEU A 210     -19.175 -12.265 -33.111  1.00114.28           C  
ANISOU 1272  CD1 LEU A 210    19035  13301  11086   1469   1984  -1431       C  
ATOM   1273  CD2 LEU A 210     -19.103 -10.174 -34.485  1.00106.47           C  
ANISOU 1273  CD2 LEU A 210    18413  11877  10164   1482   2106  -1926       C  
ATOM   1274  N   ILE A 211     -15.875  -9.727 -36.254  1.00 84.69           N  
ANISOU 1274  N   ILE A 211    15798   8847   7531   1063   1933  -2290       N  
ATOM   1275  CA  ILE A 211     -16.158  -9.102 -37.542  1.00 86.82           C  
ANISOU 1275  CA  ILE A 211    16255   8787   7947   1028   1970  -2381       C  
ATOM   1276  C   ILE A 211     -15.264  -9.683 -38.631  1.00 90.52           C  
ANISOU 1276  C   ILE A 211    16618   9207   8567    906   1872  -2388       C  
ATOM   1277  O   ILE A 211     -15.732  -9.998 -39.731  1.00102.66           O  
ANISOU 1277  O   ILE A 211    18146  10546  10314    954   1860  -2309       O  
ATOM   1278  CB  ILE A 211     -16.011  -7.572 -37.439  1.00 95.60           C  
ANISOU 1278  CB  ILE A 211    17674   9767   8884    914   2053  -2648       C  
ATOM   1279  CG1 ILE A 211     -17.074  -6.995 -36.499  1.00 88.61           C  
ANISOU 1279  CG1 ILE A 211    16882   8911   7875   1100   2143  -2677       C  
ATOM   1280  CG2 ILE A 211     -16.116  -6.930 -38.815  1.00 85.24           C  
ANISOU 1280  CG2 ILE A 211    16584   8106   7697    837   2063  -2715       C  
ATOM   1281  CD1 ILE A 211     -16.990  -5.492 -36.322  1.00 94.57           C  
ANISOU 1281  CD1 ILE A 211    17975   9488   8471   1028   2206  -2961       C  
ATOM   1282  N   MET A 212     -13.968  -9.846 -38.344  1.00 92.20           N  
ANISOU 1282  N   MET A 212    16722   9650   8658    755   1798  -2503       N  
ATOM   1283  CA  MET A 212     -13.054 -10.367 -39.356  1.00 82.10           C  
ANISOU 1283  CA  MET A 212    15306   8400   7487    649   1698  -2564       C  
ATOM   1284  C   MET A 212     -13.334 -11.833 -39.667  1.00 91.09           C  
ANISOU 1284  C   MET A 212    16210   9530   8870    845   1586  -2345       C  
ATOM   1285  O   MET A 212     -13.128 -12.273 -40.804  1.00100.56           O  
ANISOU 1285  O   MET A 212    17322  10640  10246    827   1525  -2369       O  
ATOM   1286  CB  MET A 212     -11.602 -10.179 -38.911  1.00 90.60           C  
ANISOU 1286  CB  MET A 212    16289   9799   8335    457   1641  -2774       C  
ATOM   1287  CG  MET A 212     -11.158 -11.091 -37.780  1.00115.56           C  
ANISOU 1287  CG  MET A 212    19222  13275  11412    598   1542  -2675       C  
ATOM   1288  SD  MET A 212      -9.458 -10.795 -37.261  1.00128.90           S  
ANISOU 1288  SD  MET A 212    20769  15418  12789    388   1478  -2960       S  
ATOM   1289  CE  MET A 212      -9.582  -9.131 -36.618  1.00114.76           C  
ANISOU 1289  CE  MET A 212    19282  13593  10728    140   1656  -3172       C  
ATOM   1290  N   ILE A 213     -13.808 -12.599 -38.681  1.00 88.98           N  
ANISOU 1290  N   ILE A 213    15846   9353   8607   1014   1551  -2133       N  
ATOM   1291  CA  ILE A 213     -14.219 -13.973 -38.950  1.00 93.88           C  
ANISOU 1291  CA  ILE A 213    16309   9891   9471   1179   1443  -1899       C  
ATOM   1292  C   ILE A 213     -15.488 -13.990 -39.792  1.00 99.46           C  
ANISOU 1292  C   ILE A 213    17084  10323  10381   1238   1526  -1793       C  
ATOM   1293  O   ILE A 213     -15.596 -14.751 -40.761  1.00 87.20           O  
ANISOU 1293  O   ILE A 213    15435   8633   9064   1280   1457  -1746       O  
ATOM   1294  CB  ILE A 213     -14.398 -14.752 -37.633  1.00 96.57           C  
ANISOU 1294  CB  ILE A 213    16567  10398   9728   1296   1380  -1667       C  
ATOM   1295  CG1 ILE A 213     -13.039 -15.045 -36.995  1.00111.96           C  
ANISOU 1295  CG1 ILE A 213    18390  12634  11516   1290   1245  -1754       C  
ATOM   1296  CG2 ILE A 213     -15.164 -16.045 -37.873  1.00 82.17           C  
ANISOU 1296  CG2 ILE A 213    14664   8402   8154   1427   1297  -1386       C  
ATOM   1297  CD1 ILE A 213     -13.132 -15.624 -35.598  1.00115.71           C  
ANISOU 1297  CD1 ILE A 213    18809  13314  11840   1385   1184  -1526       C  
ATOM   1298  N   LEU A 214     -16.466 -13.148 -39.445  1.00 93.17           N  
ANISOU 1298  N   LEU A 214    16442   9472   9487   1257   1670  -1780       N  
ATOM   1299  CA  LEU A 214     -17.676 -13.040 -40.251  1.00 86.82           C  
ANISOU 1299  CA  LEU A 214    15694   8459   8836   1333   1751  -1712       C  
ATOM   1300  C   LEU A 214     -17.386 -12.543 -41.659  1.00 95.85           C  
ANISOU 1300  C   LEU A 214    16909   9424  10086   1248   1756  -1868       C  
ATOM   1301  O   LEU A 214     -18.180 -12.800 -42.571  1.00111.22           O  
ANISOU 1301  O   LEU A 214    18828  11222  12207   1313   1778  -1800       O  
ATOM   1302  CB  LEU A 214     -18.686 -12.112 -39.569  1.00 96.24           C  
ANISOU 1302  CB  LEU A 214    17031   9674   9862   1409   1887  -1726       C  
ATOM   1303  CG  LEU A 214     -19.756 -12.746 -38.676  1.00101.88           C  
ANISOU 1303  CG  LEU A 214    17634  10538  10540   1522   1922  -1509       C  
ATOM   1304  CD1 LEU A 214     -19.142 -13.618 -37.592  1.00113.37           C  
ANISOU 1304  CD1 LEU A 214    18957  12209  11911   1484   1829  -1359       C  
ATOM   1305  CD2 LEU A 214     -20.632 -11.663 -38.063  1.00106.76           C  
ANISOU 1305  CD2 LEU A 214    18375  11230  10957   1617   2053  -1612       C  
ATOM   1306  N   VAL A 215     -16.271 -11.842 -41.858  1.00 87.13           N  
ANISOU 1306  N   VAL A 215    15884   8365   8857   1078   1738  -2075       N  
ATOM   1307  CA  VAL A 215     -15.899 -11.395 -43.194  1.00 87.33           C  
ANISOU 1307  CA  VAL A 215    15969   8268   8945    943   1734  -2209       C  
ATOM   1308  C   VAL A 215     -15.274 -12.535 -43.987  1.00 92.28           C  
ANISOU 1308  C   VAL A 215    16338   8970   9756    935   1608  -2210       C  
ATOM   1309  O   VAL A 215     -15.624 -12.766 -45.150  1.00 93.99           O  
ANISOU 1309  O   VAL A 215    16502   9071  10137    940   1602  -2204       O  
ATOM   1310  CB  VAL A 215     -14.956 -10.181 -43.105  1.00 80.76           C  
ANISOU 1310  CB  VAL A 215    15332   7475   7878    704   1767  -2433       C  
ATOM   1311  CG1 VAL A 215     -14.230  -9.966 -44.425  1.00 83.22           C  
ANISOU 1311  CG1 VAL A 215    15634   7770   8215    491   1729  -2564       C  
ATOM   1312  CG2 VAL A 215     -15.738  -8.934 -42.728  1.00 86.31           C  
ANISOU 1312  CG2 VAL A 215    16351   7987   8455    733   1881  -2464       C  
ATOM   1313  N   TYR A 216     -14.354 -13.278 -43.367  1.00 82.01           N  
ANISOU 1313  N   TYR A 216    14863   7875   8422    948   1495  -2232       N  
ATOM   1314  CA  TYR A 216     -13.632 -14.316 -44.093  1.00 76.42           C  
ANISOU 1314  CA  TYR A 216    13912   7251   7872    975   1350  -2292       C  
ATOM   1315  C   TYR A 216     -14.478 -15.554 -44.357  1.00 89.83           C  
ANISOU 1315  C   TYR A 216    15491   8789   9853   1171   1287  -2093       C  
ATOM   1316  O   TYR A 216     -14.163 -16.312 -45.281  1.00101.84           O  
ANISOU 1316  O   TYR A 216    16841  10298  11554   1203   1185  -2166       O  
ATOM   1317  CB  TYR A 216     -12.359 -14.703 -43.340  1.00 77.93           C  
ANISOU 1317  CB  TYR A 216    13958   7726   7923    973   1225  -2398       C  
ATOM   1318  CG  TYR A 216     -11.106 -14.138 -43.970  1.00 78.50           C  
ANISOU 1318  CG  TYR A 216    13957   8033   7835    752   1199  -2694       C  
ATOM   1319  CD1 TYR A 216     -10.599 -14.675 -45.145  1.00 78.16           C  
ANISOU 1319  CD1 TYR A 216    13713   8066   7916    733   1105  -2838       C  
ATOM   1320  CD2 TYR A 216     -10.442 -13.059 -43.402  1.00 94.17           C  
ANISOU 1320  CD2 TYR A 216    16063  10193   9523    535   1271  -2848       C  
ATOM   1321  CE1 TYR A 216      -9.460 -14.161 -45.733  1.00 79.57           C  
ANISOU 1321  CE1 TYR A 216    13793   8531   7908    494   1086  -3118       C  
ATOM   1322  CE2 TYR A 216      -9.300 -12.539 -43.982  1.00 90.50           C  
ANISOU 1322  CE2 TYR A 216    15526   9983   8879    272   1254  -3120       C  
ATOM   1323  CZ  TYR A 216      -8.814 -13.095 -45.147  1.00 80.22           C  
ANISOU 1323  CZ  TYR A 216    14003   8793   7683    247   1163  -3249       C  
ATOM   1324  OH  TYR A 216      -7.678 -12.583 -45.732  1.00104.63           O  
ANISOU 1324  OH  TYR A 216    16991  12208  10557    -49   1150  -3529       O  
ATOM   1325  N   VAL A 217     -15.537 -15.786 -43.578  1.00 96.89           N  
ANISOU 1325  N   VAL A 217    16458   9581  10773   1281   1344  -1862       N  
ATOM   1326  CA  VAL A 217     -16.437 -16.889 -43.899  1.00 96.46           C  
ANISOU 1326  CA  VAL A 217    16314   9366  10969   1401   1303  -1674       C  
ATOM   1327  C   VAL A 217     -17.247 -16.561 -45.148  1.00 89.60           C  
ANISOU 1327  C   VAL A 217    15459   8356  10227   1372   1396  -1717       C  
ATOM   1328  O   VAL A 217     -17.567 -17.448 -45.947  1.00111.15           O  
ANISOU 1328  O   VAL A 217    18059  10987  13187   1418   1337  -1688       O  
ATOM   1329  CB  VAL A 217     -17.343 -17.228 -42.699  1.00 86.95           C  
ANISOU 1329  CB  VAL A 217    15166   8159   9712   1473   1343  -1412       C  
ATOM   1330  CG1 VAL A 217     -16.512 -17.744 -41.533  1.00 87.80           C  
ANISOU 1330  CG1 VAL A 217    15239   8415   9707   1515   1219  -1336       C  
ATOM   1331  CG2 VAL A 217     -18.169 -16.022 -42.282  1.00100.73           C  
ANISOU 1331  CG2 VAL A 217    17070   9939  11264   1447   1525  -1416       C  
ATOM   1332  N   ARG A 218     -17.580 -15.282 -45.343  1.00 88.72           N  
ANISOU 1332  N   ARG A 218    15517   8229   9963   1304   1531  -1793       N  
ATOM   1333  CA  ARG A 218     -18.227 -14.869 -46.584  1.00 93.84           C  
ANISOU 1333  CA  ARG A 218    16192   8766  10697   1285   1602  -1838       C  
ATOM   1334  C   ARG A 218     -17.251 -14.925 -47.751  1.00 95.58           C  
ANISOU 1334  C   ARG A 218    16304   9038  10973   1161   1525  -2029       C  
ATOM   1335  O   ARG A 218     -17.640 -15.248 -48.879  1.00100.81           O  
ANISOU 1335  O   ARG A 218    16863   9653  11789   1166   1521  -2050       O  
ATOM   1336  CB  ARG A 218     -18.809 -13.463 -46.430  1.00 94.41           C  
ANISOU 1336  CB  ARG A 218    16517   8774  10582   1279   1736  -1861       C  
ATOM   1337  CG  ARG A 218     -20.315 -13.434 -46.209  1.00110.94           C  
ANISOU 1337  CG  ARG A 218    18641  10814  12699   1444   1833  -1714       C  
ATOM   1338  CD  ARG A 218     -21.073 -13.445 -47.531  1.00124.59           C  
ANISOU 1338  CD  ARG A 218    20319  12460  14559   1486   1864  -1712       C  
ATOM   1339  NE  ARG A 218     -20.989 -12.157 -48.215  1.00148.17           N  
ANISOU 1339  NE  ARG A 218    23528  15347  17424   1444   1908  -1821       N  
ATOM   1340  CZ  ARG A 218     -21.583 -11.882 -49.373  1.00140.78           C  
ANISOU 1340  CZ  ARG A 218    22601  14347  16541   1482   1933  -1822       C  
ATOM   1341  NH1 ARG A 218     -22.308 -12.808 -49.986  1.00134.78           N  
ANISOU 1341  NH1 ARG A 218    21611  13641  15957   1556   1932  -1751       N  
ATOM   1342  NH2 ARG A 218     -21.451 -10.680 -49.918  1.00125.82           N  
ANISOU 1342  NH2 ARG A 218    20960  12331  14516   1433   1953  -1890       N  
ATOM   1343  N   ILE A 219     -15.977 -14.612 -47.497  1.00 96.68           N  
ANISOU 1343  N   ILE A 219    16441   9328  10965   1035   1466  -2187       N  
ATOM   1344  CA  ILE A 219     -14.955 -14.753 -48.531  1.00 89.13           C  
ANISOU 1344  CA  ILE A 219    15326   8516  10023    901   1383  -2396       C  
ATOM   1345  C   ILE A 219     -14.825 -16.212 -48.946  1.00 93.60           C  
ANISOU 1345  C   ILE A 219    15617   9104  10843   1043   1243  -2408       C  
ATOM   1346  O   ILE A 219     -14.732 -16.531 -50.140  1.00102.74           O  
ANISOU 1346  O   ILE A 219    16618  10301  12118   1007   1206  -2528       O  
ATOM   1347  CB  ILE A 219     -13.612 -14.184 -48.033  1.00 87.45           C  
ANISOU 1347  CB  ILE A 219    15132   8530   9566    729   1347  -2578       C  
ATOM   1348  CG1 ILE A 219     -13.729 -12.680 -47.779  1.00 92.65           C  
ANISOU 1348  CG1 ILE A 219    16102   9115   9986    548   1480  -2596       C  
ATOM   1349  CG2 ILE A 219     -12.501 -14.476 -49.030  1.00 76.13           C  
ANISOU 1349  CG2 ILE A 219    13465   7341   8119    594   1247  -2820       C  
ATOM   1350  CD1 ILE A 219     -12.468 -12.055 -47.219  1.00104.68           C  
ANISOU 1350  CD1 ILE A 219    17662  10867  11243    330   1463  -2782       C  
ATOM   1351  N   TYR A 220     -14.828 -17.123 -47.967  1.00 88.07           N  
ANISOU 1351  N   TYR A 220    14867   8371  10224   1205   1154  -2285       N  
ATOM   1352  CA  TYR A 220     -14.730 -18.546 -48.275  1.00 78.37           C  
ANISOU 1352  CA  TYR A 220    13437   7088   9253   1359    995  -2285       C  
ATOM   1353  C   TYR A 220     -15.952 -19.026 -49.051  1.00 75.59           C  
ANISOU 1353  C   TYR A 220    13058   6536   9129   1401   1048  -2176       C  
ATOM   1354  O   TYR A 220     -15.825 -19.787 -50.020  1.00 77.13           O  
ANISOU 1354  O   TYR A 220    13070   6717   9519   1438    959  -2301       O  
ATOM   1355  CB  TYR A 220     -14.557 -19.348 -46.983  1.00 82.23           C  
ANISOU 1355  CB  TYR A 220    13946   7539   9757   1510    881  -2120       C  
ATOM   1356  CG  TYR A 220     -14.568 -20.849 -47.175  1.00104.84           C  
ANISOU 1356  CG  TYR A 220    16682  10251  12902   1685    696  -2075       C  
ATOM   1357  CD1 TYR A 220     -13.415 -21.532 -47.542  1.00120.21           C  
ANISOU 1357  CD1 TYR A 220    18442  12314  14918   1798    497  -2300       C  
ATOM   1358  CD2 TYR A 220     -15.729 -21.585 -46.976  1.00116.02           C  
ANISOU 1358  CD2 TYR A 220    18168  11413  14501   1734    712  -1823       C  
ATOM   1359  CE1 TYR A 220     -13.420 -22.905 -47.714  1.00119.10           C  
ANISOU 1359  CE1 TYR A 220    18222  11981  15051   1989    303  -2277       C  
ATOM   1360  CE2 TYR A 220     -15.745 -22.958 -47.146  1.00123.11           C  
ANISOU 1360  CE2 TYR A 220    18999  12113  15663   1866    532  -1778       C  
ATOM   1361  CZ  TYR A 220     -14.588 -23.613 -47.514  1.00118.97           C  
ANISOU 1361  CZ  TYR A 220    18324  11649  15232   2010    320  -2006       C  
ATOM   1362  OH  TYR A 220     -14.600 -24.978 -47.683  1.00127.45           O  
ANISOU 1362  OH  TYR A 220    19366  12474  16584   2172    117  -1980       O  
ATOM   1363  N   GLN A 221     -17.145 -18.586 -48.643  1.00 79.32           N  
ANISOU 1363  N   GLN A 221    13687   6889   9562   1400   1193  -1971       N  
ATOM   1364  CA  GLN A 221     -18.362 -19.010 -49.331  1.00 82.23           C  
ANISOU 1364  CA  GLN A 221    14008   7126  10110   1430   1255  -1876       C  
ATOM   1365  C   GLN A 221     -18.400 -18.498 -50.767  1.00 86.73           C  
ANISOU 1365  C   GLN A 221    14500   7756  10696   1349   1307  -2047       C  
ATOM   1366  O   GLN A 221     -18.827 -19.216 -51.679  1.00 97.42           O  
ANISOU 1366  O   GLN A 221    15695   9071  12248   1370   1279  -2089       O  
ATOM   1367  CB  GLN A 221     -19.597 -18.536 -48.565  1.00 86.53           C  
ANISOU 1367  CB  GLN A 221    14707   7621  10551   1455   1402  -1659       C  
ATOM   1368  CG  GLN A 221     -19.849 -19.279 -47.265  1.00107.90           C  
ANISOU 1368  CG  GLN A 221    17451  10287  13260   1507   1356  -1443       C  
ATOM   1369  CD  GLN A 221     -21.070 -18.760 -46.527  1.00119.12           C  
ANISOU 1369  CD  GLN A 221    18978  11749  14535   1518   1509  -1268       C  
ATOM   1370  OE1 GLN A 221     -21.498 -17.622 -46.729  1.00116.39           O  
ANISOU 1370  OE1 GLN A 221    18725  11457  14041   1528   1637  -1334       O  
ATOM   1371  NE2 GLN A 221     -21.641 -19.597 -45.670  1.00116.76           N  
ANISOU 1371  NE2 GLN A 221    18667  11431  14263   1517   1485  -1050       N  
ATOM   1372  N   ILE A 222     -17.954 -17.260 -50.989  1.00 82.80           N  
ANISOU 1372  N   ILE A 222    14123   7355   9983   1235   1379  -2144       N  
ATOM   1373  CA  ILE A 222     -17.956 -16.701 -52.338  1.00 92.52           C  
ANISOU 1373  CA  ILE A 222    15309   8657  11189   1127   1421  -2273       C  
ATOM   1374  C   ILE A 222     -16.984 -17.457 -53.232  1.00101.74           C  
ANISOU 1374  C   ILE A 222    16209   9981  12467   1076   1288  -2500       C  
ATOM   1375  O   ILE A 222     -17.292 -17.761 -54.392  1.00103.12           O  
ANISOU 1375  O   ILE A 222    16223  10203  12754   1056   1286  -2583       O  
ATOM   1376  CB  ILE A 222     -17.630 -15.196 -52.292  1.00 81.93           C  
ANISOU 1376  CB  ILE A 222    14213   7343   9574    981   1508  -2304       C  
ATOM   1377  CG1 ILE A 222     -18.811 -14.406 -51.726  1.00 92.87           C  
ANISOU 1377  CG1 ILE A 222    15845   8568  10874   1083   1635  -2124       C  
ATOM   1378  CG2 ILE A 222     -17.242 -14.687 -53.676  1.00 84.97           C  
ANISOU 1378  CG2 ILE A 222    14547   7846   9894    805   1509  -2445       C  
ATOM   1379  CD1 ILE A 222     -18.574 -12.916 -51.676  1.00 73.64           C  
ANISOU 1379  CD1 ILE A 222    13709   6079   8192    965   1702  -2156       C  
ATOM   1380  N   ALA A 223     -15.798 -17.775 -52.706  1.00 90.99           N  
ANISOU 1380  N   ALA A 223    14773   8741  11058   1070   1170  -2626       N  
ATOM   1381  CA  ALA A 223     -14.802 -18.498 -53.488  1.00 91.27           C  
ANISOU 1381  CA  ALA A 223    14527   8979  11174   1062   1025  -2890       C  
ATOM   1382  C   ALA A 223     -15.296 -19.886 -53.873  1.00104.71           C  
ANISOU 1382  C   ALA A 223    16044  10545  13195   1241    923  -2897       C  
ATOM   1383  O   ALA A 223     -15.110 -20.323 -55.015  1.00113.81           O  
ANISOU 1383  O   ALA A 223    16968  11821  14453   1224    868  -3101       O  
ATOM   1384  CB  ALA A 223     -13.496 -18.592 -52.703  1.00 83.14           C  
ANISOU 1384  CB  ALA A 223    13447   8131  10012   1072    908  -3023       C  
ATOM   1385  N   LYS A 224     -15.932 -20.593 -52.935  1.00106.32           N  
ANISOU 1385  N   LYS A 224    16349  10504  13542   1390    896  -2681       N  
ATOM   1386  CA  LYS A 224     -16.400 -21.946 -53.221  1.00103.59           C  
ANISOU 1386  CA  LYS A 224    15881   9977  13503   1524    788  -2673       C  
ATOM   1387  C   LYS A 224     -17.588 -21.936 -54.175  1.00 97.17           C  
ANISOU 1387  C   LYS A 224    15018   9106  12798   1461    909  -2632       C  
ATOM   1388  O   LYS A 224     -17.694 -22.803 -55.050  1.00107.10           O  
ANISOU 1388  O   LYS A 224    16083  10342  14270   1499    831  -2783       O  
ATOM   1389  CB  LYS A 224     -16.758 -22.665 -51.922  1.00111.10           C  
ANISOU 1389  CB  LYS A 224    16987  10686  14539   1642    724  -2417       C  
ATOM   1390  CG  LYS A 224     -15.550 -23.076 -51.097  1.00114.11           C  
ANISOU 1390  CG  LYS A 224    17362  11118  14876   1769    541  -2478       C  
ATOM   1391  CD  LYS A 224     -14.501 -23.738 -51.977  1.00128.01           C  
ANISOU 1391  CD  LYS A 224    18870  13013  16755   1872    354  -2822       C  
ATOM   1392  CE  LYS A 224     -13.325 -24.251 -51.164  1.00136.35           C  
ANISOU 1392  CE  LYS A 224    19898  14139  17771   2059    143  -2899       C  
ATOM   1393  NZ  LYS A 224     -13.707 -25.395 -50.292  1.00149.20           N  
ANISOU 1393  NZ  LYS A 224    21673  15417  19600   2238     -5  -2655       N  
ATOM   1394  N   ARG A 225     -18.499 -20.971 -54.017  1.00 89.55           N  
ANISOU 1394  N   ARG A 225    14216   8129  11681   1386   1093  -2451       N  
ATOM   1395  CA  ARG A 225     -19.606 -20.848 -54.959  1.00 95.08           C  
ANISOU 1395  CA  ARG A 225    14850   8837  12437   1346   1208  -2426       C  
ATOM   1396  C   ARG A 225     -19.108 -20.509 -56.358  1.00 96.65           C  
ANISOU 1396  C   ARG A 225    14866   9257  12598   1252   1200  -2669       C  
ATOM   1397  O   ARG A 225     -19.727 -20.907 -57.353  1.00102.89           O  
ANISOU 1397  O   ARG A 225    15488  10093  13512   1241   1223  -2740       O  
ATOM   1398  CB  ARG A 225     -20.597 -19.784 -54.480  1.00110.75           C  
ANISOU 1398  CB  ARG A 225    17049  10799  14233   1335   1383  -2212       C  
ATOM   1399  CG  ARG A 225     -21.812 -19.611 -55.381  1.00134.32           C  
ANISOU 1399  CG  ARG A 225    19961  13831  17242   1334   1498  -2177       C  
ATOM   1400  CD  ARG A 225     -22.713 -18.484 -54.899  1.00152.66           C  
ANISOU 1400  CD  ARG A 225    22496  16154  19355   1383   1646  -2005       C  
ATOM   1401  NE  ARG A 225     -23.851 -18.278 -55.791  1.00157.65           N  
ANISOU 1401  NE  ARG A 225    23041  16877  19980   1419   1742  -1986       N  
ATOM   1402  CZ  ARG A 225     -25.025 -18.886 -55.657  1.00149.66           C  
ANISOU 1402  CZ  ARG A 225    21933  15880  19051   1470   1802  -1891       C  
ATOM   1403  NH1 ARG A 225     -26.004 -18.639 -56.517  1.00139.14           N  
ANISOU 1403  NH1 ARG A 225    20497  14688  17682   1512   1886  -1900       N  
ATOM   1404  NH2 ARG A 225     -25.222 -19.742 -54.663  1.00143.26           N  
ANISOU 1404  NH2 ARG A 225    21127  14969  18336   1460   1774  -1780       N  
ATOM   1405  N   ARG A 226     -17.990 -19.785 -56.457  1.00105.16           N  
ANISOU 1405  N   ARG A 226    15959  10511  13485   1156   1171  -2805       N  
ATOM   1406  CA  ARG A 226     -17.484 -19.389 -57.765  1.00 93.50           C  
ANISOU 1406  CA  ARG A 226    14310   9299  11918   1014   1169  -3021       C  
ATOM   1407  C   ARG A 226     -16.779 -20.541 -58.471  1.00 90.99           C  
ANISOU 1407  C   ARG A 226    13662   9124  11787   1065   1010  -3312       C  
ATOM   1408  O   ARG A 226     -16.803 -20.614 -59.705  1.00106.19           O  
ANISOU 1408  O   ARG A 226    15368  11253  13725    987   1012  -3486       O  
ATOM   1409  CB  ARG A 226     -16.543 -18.195 -57.612  1.00 96.42           C  
ANISOU 1409  CB  ARG A 226    14821   9830  11985    835   1197  -3064       C  
ATOM   1410  CG  ARG A 226     -16.114 -17.550 -58.917  1.00107.90           C  
ANISOU 1410  CG  ARG A 226    16158  11570  13269    616   1220  -3222       C  
ATOM   1411  CD  ARG A 226     -15.745 -16.095 -58.696  1.00114.58           C  
ANISOU 1411  CD  ARG A 226    17294  12441  13800    401   1303  -3132       C  
ATOM   1412  NE  ARG A 226     -16.865 -15.351 -58.124  1.00130.07           N  
ANISOU 1412  NE  ARG A 226    19587  14107  15728    490   1423  -2853       N  
ATOM   1413  CZ  ARG A 226     -16.837 -14.056 -57.828  1.00150.22           C  
ANISOU 1413  CZ  ARG A 226    22469  16564  18044    362   1498  -2740       C  
ATOM   1414  NH1 ARG A 226     -17.909 -13.471 -57.311  1.00148.66           N  
ANISOU 1414  NH1 ARG A 226    22542  16109  17833    507   1588  -2526       N  
ATOM   1415  NH2 ARG A 226     -15.740 -13.343 -58.048  1.00155.76           N  
ANISOU 1415  NH2 ARG A 226    23232  17439  18512     82   1477  -2858       N  
ATOM   1416  N   THR A 227     -16.166 -21.451 -57.716  1.00 82.76           N  
ANISOU 1416  N   THR A 227    12579   7984  10884   1215    859  -3377       N  
ATOM   1417  CA  THR A 227     -15.438 -22.579 -58.282  1.00 77.47           C  
ANISOU 1417  CA  THR A 227    11617   7417  10401   1327    673  -3684       C  
ATOM   1418  C   THR A 227     -16.216 -23.886 -58.213  1.00 73.48           C  
ANISOU 1418  C   THR A 227    11082   6599  10237   1494    593  -3637       C  
ATOM   1419  O   THR A 227     -15.665 -24.934 -58.560  1.00 86.76           O  
ANISOU 1419  O   THR A 227    12568   8279  12117   1635    410  -3890       O  
ATOM   1420  CB  THR A 227     -14.092 -22.749 -57.566  1.00 94.68           C  
ANISOU 1420  CB  THR A 227    13761   9720  12495   1415    517  -3833       C  
ATOM   1421  OG1 THR A 227     -13.305 -23.732 -58.248  1.00130.54           O  
ANISOU 1421  OG1 THR A 227    17988  14428  17183   1552    323  -4194       O  
ATOM   1422  CG2 THR A 227     -14.315 -23.193 -56.127  1.00 81.31           C  
ANISOU 1422  CG2 THR A 227    12306   7695  10891   1578    464  -3574       C  
ATOM   1423  N   ALA A1001     -17.479 -23.852 -57.780  1.00 89.57           N  
ANISOU 1423  N   ALA A1001    10502   9834  13696    481   3128  -2893       N  
ATOM   1424  CA  ALA A1001     -18.217 -25.092 -57.560  1.00 71.40           C  
ANISOU 1424  CA  ALA A1001     8101   7845  11185    326   3373  -2658       C  
ATOM   1425  C   ALA A1001     -18.464 -25.839 -58.864  1.00 78.01           C  
ANISOU 1425  C   ALA A1001     8564   8656  12422    375   3075  -2212       C  
ATOM   1426  O   ALA A1001     -18.264 -27.057 -58.934  1.00 90.14           O  
ANISOU 1426  O   ALA A1001    10187  10375  13687    178   2933  -1886       O  
ATOM   1427  CB  ALA A1001     -19.538 -24.794 -56.853  1.00 77.31           C  
ANISOU 1427  CB  ALA A1001     8639   8690  12045    393   4043  -2991       C  
ATOM   1428  N   ASP A1002     -18.887 -25.124 -59.911  1.00 90.51           N  
ANISOU 1428  N   ASP A1002     9753   9993  14643    623   2949  -2189       N  
ATOM   1429  CA  ASP A1002     -19.237 -25.781 -61.168  1.00 66.59           C  
ANISOU 1429  CA  ASP A1002     6384   6959  11958    649   2670  -1802       C  
ATOM   1430  C   ASP A1002     -18.026 -26.444 -61.814  1.00 64.60           C  
ANISOU 1430  C   ASP A1002     6371   6724  11451    517   2184  -1499       C  
ATOM   1431  O   ASP A1002     -18.125 -27.571 -62.313  1.00 61.08           O  
ANISOU 1431  O   ASP A1002     5855   6405  10948    394   2047  -1213       O  
ATOM   1432  CB  ASP A1002     -19.879 -24.774 -62.121  1.00 67.37           C  
ANISOU 1432  CB  ASP A1002     6063   6783  12751    927   2574  -1818       C  
ATOM   1433  CG  ASP A1002     -21.297 -24.417 -61.718  1.00 89.79           C  
ANISOU 1433  CG  ASP A1002     8491   9615  16009   1082   3041  -2040       C  
ATOM   1434  OD1 ASP A1002     -21.746 -24.888 -60.651  1.00100.85           O  
ANISOU 1434  OD1 ASP A1002     9964  11247  17106    953   3506  -2219       O  
ATOM   1435  OD2 ASP A1002     -21.965 -23.675 -62.468  1.00113.46           O  
ANISOU 1435  OD2 ASP A1002    11200  12425  19483   1248   2838  -1945       O  
ATOM   1436  N   LEU A1003     -16.876 -25.766 -61.823  1.00 76.40           N  
ANISOU 1436  N   LEU A1003     8123   8072  12833    536   1934  -1577       N  
ATOM   1437  CA  LEU A1003     -15.688 -26.360 -62.429  1.00 52.05           C  
ANISOU 1437  CA  LEU A1003     5206   5003   9566    426   1522  -1320       C  
ATOM   1438  C   LEU A1003     -15.183 -27.542 -61.611  1.00 61.14           C  
ANISOU 1438  C   LEU A1003     6648   6370  10214    207   1514  -1222       C  
ATOM   1439  O   LEU A1003     -14.719 -28.542 -62.173  1.00 54.91           O  
ANISOU 1439  O   LEU A1003     5864   5633   9366    123   1275   -957       O  
ATOM   1440  CB  LEU A1003     -14.589 -25.310 -62.586  1.00 51.41           C  
ANISOU 1440  CB  LEU A1003     5280   4714   9541    475   1280  -1423       C  
ATOM   1441  CG  LEU A1003     -13.379 -25.751 -63.414  1.00 47.72           C  
ANISOU 1441  CG  LEU A1003     4876   4241   9015    392    895  -1169       C  
ATOM   1442  CD1 LEU A1003     -13.814 -26.132 -64.818  1.00 48.80           C  
ANISOU 1442  CD1 LEU A1003     4739   4376   9427    446    769   -903       C  
ATOM   1443  CD2 LEU A1003     -12.322 -24.662 -63.459  1.00 59.01           C  
ANISOU 1443  CD2 LEU A1003     6426   5467  10527    400    697  -1275       C  
ATOM   1444  N   GLU A1004     -15.265 -27.445 -60.281  1.00 61.02           N  
ANISOU 1444  N   GLU A1004     6893   6467   9826    108   1766  -1434       N  
ATOM   1445  CA  GLU A1004     -14.898 -28.573 -59.431  1.00 55.75           C  
ANISOU 1445  CA  GLU A1004     6524   6000   8658   -124   1742  -1282       C  
ATOM   1446  C   GLU A1004     -15.842 -29.751 -59.632  1.00 74.37           C  
ANISOU 1446  C   GLU A1004     8697   8493  11067   -216   1908  -1038       C  
ATOM   1447  O   GLU A1004     -15.423 -30.908 -59.511  1.00 92.29           O  
ANISOU 1447  O   GLU A1004    11119  10831  13117   -377   1727   -770       O  
ATOM   1448  CB  GLU A1004     -14.885 -28.145 -57.961  1.00 60.63           C  
ANISOU 1448  CB  GLU A1004     7502   6740   8793   -248   1996  -1564       C  
ATOM   1449  CG  GLU A1004     -13.705 -27.263 -57.577  1.00 78.44           C  
ANISOU 1449  CG  GLU A1004    10044   8879  10882   -254   1718  -1769       C  
ATOM   1450  CD  GLU A1004     -13.783 -26.771 -56.144  1.00103.91           C  
ANISOU 1450  CD  GLU A1004    13660  12231  13589   -394   1977  -2115       C  
ATOM   1451  OE1 GLU A1004     -14.910 -26.604 -55.632  1.00108.62           O  
ANISOU 1451  OE1 GLU A1004    14206  12939  14127   -383   2495  -2331       O  
ATOM   1452  OE2 GLU A1004     -12.717 -26.558 -55.527  1.00119.49           O  
ANISOU 1452  OE2 GLU A1004    15987  14203  15210   -528   1666  -2184       O  
ATOM   1453  N   ASP A1005     -17.111 -29.478 -59.944  1.00 81.70           N  
ANISOU 1453  N   ASP A1005     9272   9427  12341   -117   2226  -1120       N  
ATOM   1454  CA  ASP A1005     -18.050 -30.552 -60.251  1.00 85.27           C  
ANISOU 1454  CA  ASP A1005     9483   9983  12932   -223   2350   -888       C  
ATOM   1455  C   ASP A1005     -17.650 -31.272 -61.533  1.00 85.17           C  
ANISOU 1455  C   ASP A1005     9340   9865  13157   -208   1928   -614       C  
ATOM   1456  O   ASP A1005     -17.603 -32.508 -61.577  1.00 93.46           O  
ANISOU 1456  O   ASP A1005    10454  10960  14095   -377   1826   -374       O  
ATOM   1457  CB  ASP A1005     -19.468 -29.991 -60.368  1.00108.30           C  
ANISOU 1457  CB  ASP A1005    11970  12913  16265   -100   2741  -1049       C  
ATOM   1458  CG  ASP A1005     -20.011 -29.490 -59.044  1.00141.63           C  
ANISOU 1458  CG  ASP A1005    16301  17275  20235   -144   3282  -1355       C  
ATOM   1459  OD1 ASP A1005     -19.562 -29.990 -57.992  1.00150.92           O  
ANISOU 1459  OD1 ASP A1005    17896  18620  20826   -371   3386  -1336       O  
ATOM   1460  OD2 ASP A1005     -20.884 -28.596 -59.053  1.00149.54           O  
ANISOU 1460  OD2 ASP A1005    16979  18216  21625     46   3602  -1618       O  
ATOM   1461  N   ASN A1006     -17.359 -30.510 -62.591  1.00 71.45           N  
ANISOU 1461  N   ASN A1006     7438   7973  11738    -19   1689   -651       N  
ATOM   1462  CA  ASN A1006     -16.940 -31.114 -63.852  1.00 54.38           C  
ANISOU 1462  CA  ASN A1006     5192   5738   9734    -19   1328   -441       C  
ATOM   1463  C   ASN A1006     -15.640 -31.890 -63.687  1.00 59.53           C  
ANISOU 1463  C   ASN A1006     6155   6379  10086   -120   1078   -328       C  
ATOM   1464  O   ASN A1006     -15.471 -32.968 -64.270  1.00 86.87           O  
ANISOU 1464  O   ASN A1006     9605   9821  13579   -200    904   -157       O  
ATOM   1465  CB  ASN A1006     -16.785 -30.035 -64.923  1.00 49.20           C  
ANISOU 1465  CB  ASN A1006     4366   4940   9386    166   1140   -484       C  
ATOM   1466  CG  ASN A1006     -18.067 -29.262 -65.164  1.00 63.74           C  
ANISOU 1466  CG  ASN A1006     5852   6739  11627    302   1312   -558       C  
ATOM   1467  OD1 ASN A1006     -19.152 -29.840 -65.214  1.00 65.07           O  
ANISOU 1467  OD1 ASN A1006     5767   6991  11964    246   1447   -491       O  
ATOM   1468  ND2 ASN A1006     -17.949 -27.946 -65.306  1.00 66.74           N  
ANISOU 1468  ND2 ASN A1006     6182   6957  12218    480   1292   -690       N  
ATOM   1469  N   TRP A1007     -14.709 -31.356 -62.893  1.00 62.74           N  
ANISOU 1469  N   TRP A1007     6824   6774  10239   -115   1036   -438       N  
ATOM   1470  CA  TRP A1007     -13.439 -32.040 -62.672  1.00 44.76           C  
ANISOU 1470  CA  TRP A1007     4789   4471   7747   -193    758   -319       C  
ATOM   1471  C   TRP A1007     -13.643 -33.350 -61.921  1.00 58.79           C  
ANISOU 1471  C   TRP A1007     6726   6321   9291   -377    790   -128       C  
ATOM   1472  O   TRP A1007     -12.999 -34.358 -62.233  1.00 66.61           O  
ANISOU 1472  O   TRP A1007     7768   7230  10310   -419    545     52       O  
ATOM   1473  CB  TRP A1007     -12.482 -31.125 -61.908  1.00 45.64           C  
ANISOU 1473  CB  TRP A1007     5125   4559   7655   -179    667   -478       C  
ATOM   1474  CG  TRP A1007     -11.070 -31.612 -61.885  1.00 44.59           C  
ANISOU 1474  CG  TRP A1007     5134   4370   7440   -217    314   -360       C  
ATOM   1475  CD1 TRP A1007     -10.472 -32.353 -60.908  1.00 63.18           C  
ANISOU 1475  CD1 TRP A1007     7745   6766   9497   -350    153   -235       C  
ATOM   1476  CD2 TRP A1007     -10.073 -31.389 -62.888  1.00 65.70           C  
ANISOU 1476  CD2 TRP A1007     7669   6930  10364   -125     76   -340       C  
ATOM   1477  NE1 TRP A1007      -9.162 -32.605 -61.241  1.00 67.43           N  
ANISOU 1477  NE1 TRP A1007     8264   7201  10155   -314   -195   -148       N  
ATOM   1478  CE2 TRP A1007      -8.893 -32.024 -62.452  1.00 69.53           C  
ANISOU 1478  CE2 TRP A1007     8280   7384  10754   -181   -207   -230       C  
ATOM   1479  CE3 TRP A1007     -10.063 -30.714 -64.112  1.00 67.26           C  
ANISOU 1479  CE3 TRP A1007     7647   7056  10853    -15     78   -382       C  
ATOM   1480  CZ2 TRP A1007      -7.716 -32.004 -63.197  1.00 59.31           C  
ANISOU 1480  CZ2 TRP A1007     6846   5996   9693   -116   -431   -204       C  
ATOM   1481  CZ3 TRP A1007      -8.894 -30.695 -64.851  1.00 63.13           C  
ANISOU 1481  CZ3 TRP A1007     7045   6465  10477     13   -126   -339       C  
ATOM   1482  CH2 TRP A1007      -7.737 -31.336 -64.391  1.00 57.80           C  
ANISOU 1482  CH2 TRP A1007     6447   5767   9747    -29   -350   -272       C  
ATOM   1483  N   GLU A1008     -14.540 -33.355 -60.933  1.00 58.53           N  
ANISOU 1483  N   GLU A1008     6770   6424   9045   -493   1111   -162       N  
ATOM   1484  CA  GLU A1008     -14.788 -34.578 -60.181  1.00 60.65           C  
ANISOU 1484  CA  GLU A1008     7215   6762   9068   -715   1161     75       C  
ATOM   1485  C   GLU A1008     -15.533 -35.609 -61.019  1.00 56.16           C  
ANISOU 1485  C   GLU A1008     6399   6126   8813   -770   1161    255       C  
ATOM   1486  O   GLU A1008     -15.336 -36.815 -60.833  1.00 62.83           O  
ANISOU 1486  O   GLU A1008     7375   6901   9598   -920   1020    503       O  
ATOM   1487  CB  GLU A1008     -15.564 -34.263 -58.903  1.00 69.58           C  
ANISOU 1487  CB  GLU A1008     8504   8094   9839   -863   1573    -20       C  
ATOM   1488  CG  GLU A1008     -15.374 -35.288 -57.799  1.00 97.85           C  
ANISOU 1488  CG  GLU A1008    12446  11766  12968  -1139   1551    250       C  
ATOM   1489  CD  GLU A1008     -13.915 -35.648 -57.589  1.00124.97           C  
ANISOU 1489  CD  GLU A1008    16169  15086  16228  -1145   1049    409       C  
ATOM   1490  OE1 GLU A1008     -13.501 -36.738 -58.037  1.00127.92           O  
ANISOU 1490  OE1 GLU A1008    16518  15295  16790  -1169    753    683       O  
ATOM   1491  OE2 GLU A1008     -13.179 -34.836 -56.988  1.00136.23           O  
ANISOU 1491  OE2 GLU A1008    17821  16563  17376  -1123    936    242       O  
ATOM   1492  N   THR A1009     -16.387 -35.158 -61.943  1.00 68.09           N  
ANISOU 1492  N   THR A1009     7560   7633  10680   -661   1278    144       N  
ATOM   1493  CA  THR A1009     -17.039 -36.089 -62.858  1.00 75.92           C  
ANISOU 1493  CA  THR A1009     8319   8552  11975   -729   1201    283       C  
ATOM   1494  C   THR A1009     -16.020 -36.739 -63.783  1.00 60.15           C  
ANISOU 1494  C   THR A1009     6393   6381  10079   -673    816    351       C  
ATOM   1495  O   THR A1009     -16.077 -37.950 -64.035  1.00 56.58           O  
ANISOU 1495  O   THR A1009     5964   5816   9718   -797    695    504       O  
ATOM   1496  CB  THR A1009     -18.118 -35.368 -63.667  1.00 65.59           C  
ANISOU 1496  CB  THR A1009     6616   7280  11024   -622   1327    160       C  
ATOM   1497  OG1 THR A1009     -19.242 -35.084 -62.822  1.00 94.84           O  
ANISOU 1497  OG1 THR A1009    10171  11130  14736   -696   1743    107       O  
ATOM   1498  CG2 THR A1009     -18.576 -36.226 -64.844  1.00 60.31           C  
ANISOU 1498  CG2 THR A1009     5737   6525  10653   -689   1117    270       C  
ATOM   1499  N   LEU A1010     -15.073 -35.949 -64.293  1.00 48.76           N  
ANISOU 1499  N   LEU A1010     4980   4899   8649   -495    646    223       N  
ATOM   1500  CA  LEU A1010     -14.008 -36.508 -65.122  1.00 42.22           C  
ANISOU 1500  CA  LEU A1010     4201   3929   7911   -435    354    246       C  
ATOM   1501  C   LEU A1010     -13.185 -37.541 -64.357  1.00 71.97           C  
ANISOU 1501  C   LEU A1010     8207   7588  11552   -516    199    405       C  
ATOM   1502  O   LEU A1010     -12.812 -38.581 -64.911  1.00 48.26           O  
ANISOU 1502  O   LEU A1010     5205   4419   8715   -527     28    469       O  
ATOM   1503  CB  LEU A1010     -13.104 -35.391 -65.644  1.00 40.23           C  
ANISOU 1503  CB  LEU A1010     3929   3679   7679   -268    255    104       C  
ATOM   1504  CG  LEU A1010     -13.707 -34.420 -66.660  1.00 60.32           C  
ANISOU 1504  CG  LEU A1010     6255   6266  10396   -177    302      8       C  
ATOM   1505  CD1 LEU A1010     -12.723 -33.304 -66.986  1.00 44.64           C  
ANISOU 1505  CD1 LEU A1010     4294   4255   8410    -57    214    -83       C  
ATOM   1506  CD2 LEU A1010     -14.120 -35.164 -67.921  1.00 50.90           C  
ANISOU 1506  CD2 LEU A1010     4934   5043   9363   -221    193     41       C  
ATOM   1507  N   ASN A1011     -12.902 -37.277 -63.079  1.00 69.59           N  
ANISOU 1507  N   ASN A1011     8120   7361  10960   -577    238    466       N  
ATOM   1508  CA  ASN A1011     -12.087 -38.192 -62.281  1.00 82.45           C  
ANISOU 1508  CA  ASN A1011     9992   8879  12455   -661     14    676       C  
ATOM   1509  C   ASN A1011     -12.828 -39.502 -62.012  1.00 61.02           C  
ANISOU 1509  C   ASN A1011     7334   6074   9778   -855     54    916       C  
ATOM   1510  O   ASN A1011     -12.262 -40.590 -62.161  1.00 56.53           O  
ANISOU 1510  O   ASN A1011     6826   5274   9377   -866   -194   1076       O  
ATOM   1511  CB  ASN A1011     -11.674 -37.526 -60.964  1.00 64.16           C  
ANISOU 1511  CB  ASN A1011     7938   6701   9740   -725     12    687       C  
ATOM   1512  CG  ASN A1011     -10.270 -36.909 -61.016  1.00 64.19           C  
ANISOU 1512  CG  ASN A1011     7973   6651   9766   -585   -280    593       C  
ATOM   1513  OD1 ASN A1011      -9.472 -37.191 -61.912  1.00 64.17           O  
ANISOU 1513  OD1 ASN A1011     7808   6497  10077   -448   -479    573       O  
ATOM   1514  ND2 ASN A1011      -9.962 -36.078 -60.026  1.00 83.82           N  
ANISOU 1514  ND2 ASN A1011    10666   9264  11918   -640   -291    517       N  
ATOM   1515  N   ASP A1012     -14.096 -39.418 -61.601  1.00 72.52           N  
ANISOU 1515  N   ASP A1012     8746   7683  11126  -1013    377    946       N  
ATOM   1516  CA  ASP A1012     -14.871 -40.622 -61.305  1.00 76.96           C  
ANISOU 1516  CA  ASP A1012     9342   8162  11737  -1251    447   1199       C  
ATOM   1517  C   ASP A1012     -15.010 -41.513 -62.541  1.00 62.84           C  
ANISOU 1517  C   ASP A1012     7359   6135  10381  -1223    280   1184       C  
ATOM   1518  O   ASP A1012     -14.876 -42.737 -62.450  1.00 71.65           O  
ANISOU 1518  O   ASP A1012     8583   7010  11629  -1345    113   1397       O  
ATOM   1519  CB  ASP A1012     -16.247 -40.225 -60.752  1.00 73.77           C  
ANISOU 1519  CB  ASP A1012     8829   7998  11201  -1418    890   1184       C  
ATOM   1520  CG  ASP A1012     -16.160 -39.444 -59.434  1.00 95.13           C  
ANISOU 1520  CG  ASP A1012    11790  10943  13413  -1484   1113   1155       C  
ATOM   1521  OD1 ASP A1012     -15.135 -39.553 -58.720  1.00104.04           O  
ANISOU 1521  OD1 ASP A1012    13250  12040  14239  -1504    869   1273       O  
ATOM   1522  OD2 ASP A1012     -17.129 -38.733 -59.095  1.00 99.04           O  
ANISOU 1522  OD2 ASP A1012    12148  11652  13831  -1523   1527    999       O  
ATOM   1523  N   ASN A1013     -15.270 -40.921 -63.710  1.00 55.36           N  
ANISOU 1523  N   ASN A1013     6153   5232   9651  -1076    303    934       N  
ATOM   1524  CA  ASN A1013     -15.417 -41.716 -64.928  1.00 49.07           C  
ANISOU 1524  CA  ASN A1013     5217   4241   9188  -1076    143    865       C  
ATOM   1525  C   ASN A1013     -14.077 -42.275 -65.403  1.00 48.13           C  
ANISOU 1525  C   ASN A1013     5217   3883   9189   -925   -143    814       C  
ATOM   1526  O   ASN A1013     -14.039 -43.352 -65.999  1.00 64.44           O  
ANISOU 1526  O   ASN A1013     7282   5695  11506   -971   -284    807       O  
ATOM   1527  CB  ASN A1013     -16.079 -40.872 -66.030  1.00 49.49           C  
ANISOU 1527  CB  ASN A1013     4995   4441   9367   -990    212    643       C  
ATOM   1528  CG  ASN A1013     -17.596 -40.785 -65.893  1.00 66.11           C  
ANISOU 1528  CG  ASN A1013     6863   6679  11575  -1159    432    697       C  
ATOM   1529  OD1 ASN A1013     -18.284 -41.808 -65.911  1.00 82.80           O  
ANISOU 1529  OD1 ASN A1013     8924   8680  13856  -1374    424    821       O  
ATOM   1530  ND2 ASN A1013     -18.122 -39.570 -65.800  1.00 87.35           N  
ANISOU 1530  ND2 ASN A1013     9376   9580  14233  -1060    621    597       N  
ATOM   1531  N   LEU A1014     -12.972 -41.574 -65.129  1.00 51.89           N  
ANISOU 1531  N   LEU A1014     5774   4412   9529   -750   -224    758       N  
ATOM   1532  CA  LEU A1014     -11.640 -42.127 -65.383  1.00 46.76           C  
ANISOU 1532  CA  LEU A1014     5185   3533   9047   -602   -475    735       C  
ATOM   1533  C   LEU A1014     -11.363 -43.339 -64.492  1.00 65.43           C  
ANISOU 1533  C   LEU A1014     7739   5638  11484   -705   -661   1027       C  
ATOM   1534  O   LEU A1014     -10.805 -44.342 -64.951  1.00 80.02           O  
ANISOU 1534  O   LEU A1014     9580   7170  13654   -636   -847   1017       O  
ATOM   1535  CB  LEU A1014     -10.567 -41.044 -65.179  1.00 45.15           C  
ANISOU 1535  CB  LEU A1014     4981   3461   8713   -430   -530    642       C  
ATOM   1536  CG  LEU A1014     -10.354 -40.064 -66.337  1.00 64.19           C  
ANISOU 1536  CG  LEU A1014     7211   6005  11173   -291   -440    374       C  
ATOM   1537  CD1 LEU A1014      -9.380 -38.931 -65.979  1.00 52.38           C  
ANISOU 1537  CD1 LEU A1014     5715   4624   9563   -178   -486    319       C  
ATOM   1538  CD2 LEU A1014      -9.883 -40.809 -67.569  1.00 42.43           C  
ANISOU 1538  CD2 LEU A1014     4359   3076   8686   -208   -502    209       C  
ATOM   1539  N   LYS A1015     -11.745 -43.269 -63.215  1.00 52.01           N  
ANISOU 1539  N   LYS A1015     6224   4052   9486   -877   -611   1290       N  
ATOM   1540  CA  LYS A1015     -11.606 -44.430 -62.339  1.00 55.84           C  
ANISOU 1540  CA  LYS A1015     6927   4292   9996  -1031   -804   1649       C  
ATOM   1541  C   LYS A1015     -12.538 -45.562 -62.760  1.00 79.41           C  
ANISOU 1541  C   LYS A1015     9869   7049  13254  -1212   -752   1739       C  
ATOM   1542  O   LYS A1015     -12.187 -46.739 -62.598  1.00 60.57           O  
ANISOU 1542  O   LYS A1015     7595   4293  11126  -1258   -993   1952       O  
ATOM   1543  CB  LYS A1015     -11.859 -44.028 -60.880  1.00 59.37           C  
ANISOU 1543  CB  LYS A1015     7633   4975   9950  -1227   -722   1910       C  
ATOM   1544  CG  LYS A1015     -10.589 -43.800 -60.057  1.00 83.94           C  
ANISOU 1544  CG  LYS A1015    10943   8071  12878  -1140  -1049   2048       C  
ATOM   1545  CD  LYS A1015     -10.890 -43.207 -58.677  1.00106.84           C  
ANISOU 1545  CD  LYS A1015    14145  11278  15171  -1357   -933   2216       C  
ATOM   1546  CE  LYS A1015     -11.260 -41.735 -58.753  1.00104.24           C  
ANISOU 1546  CE  LYS A1015    13720  11299  14588  -1289   -606   1858       C  
ATOM   1547  NZ  LYS A1015     -11.388 -41.177 -57.382  1.00115.65           N  
ANISOU 1547  NZ  LYS A1015    15500  13018  15425  -1489   -505   1952       N  
ATOM   1548  N   VAL A1016     -13.721 -45.236 -63.288  1.00 66.63           N  
ANISOU 1548  N   VAL A1016     8072   5612  11630  -1323   -475   1590       N  
ATOM   1549  CA  VAL A1016     -14.624 -46.275 -63.783  1.00 66.05           C  
ANISOU 1549  CA  VAL A1016     7920   5319  11856  -1522   -458   1641       C  
ATOM   1550  C   VAL A1016     -13.973 -47.046 -64.927  1.00 67.12           C  
ANISOU 1550  C   VAL A1016     8002   5099  12403  -1363   -697   1418       C  
ATOM   1551  O   VAL A1016     -13.955 -48.285 -64.932  1.00 66.08           O  
ANISOU 1551  O   VAL A1016     7959   4572  12577  -1467   -868   1552       O  
ATOM   1552  CB  VAL A1016     -15.977 -45.661 -64.189  1.00 68.16           C  
ANISOU 1552  CB  VAL A1016     7940   5873  12086  -1651   -162   1505       C  
ATOM   1553  CG1 VAL A1016     -16.738 -46.584 -65.126  1.00 59.05           C  
ANISOU 1553  CG1 VAL A1016     6638   4492  11308  -1806   -233   1427       C  
ATOM   1554  CG2 VAL A1016     -16.822 -45.351 -62.951  1.00 60.10           C  
ANISOU 1554  CG2 VAL A1016     6967   5108  10761  -1885    139   1757       C  
ATOM   1555  N   ILE A1017     -13.380 -46.320 -65.882  1.00 54.98           N  
ANISOU 1555  N   ILE A1017     6334   3677  10877  -1114   -698   1070       N  
ATOM   1556  CA  ILE A1017     -12.674 -46.956 -66.993  1.00 57.57           C  
ANISOU 1556  CA  ILE A1017     6621   3718  11535   -952   -849    790       C  
ATOM   1557  C   ILE A1017     -11.467 -47.741 -66.485  1.00 61.50           C  
ANISOU 1557  C   ILE A1017     7239   3853  12276   -803  -1091    927       C  
ATOM   1558  O   ILE A1017     -11.121 -48.799 -67.032  1.00 77.88           O  
ANISOU 1558  O   ILE A1017     9320   5638  14633   -724  -1205    788       O  
ATOM   1559  CB  ILE A1017     -12.262 -45.894 -68.040  1.00 51.75           C  
ANISOU 1559  CB  ILE A1017     5740   3246  10676   -752   -749    434       C  
ATOM   1560  CG1 ILE A1017     -13.491 -45.148 -68.574  1.00 61.88           C  
ANISOU 1560  CG1 ILE A1017     6889   4841  11783   -889   -586    345       C  
ATOM   1561  CG2 ILE A1017     -11.495 -46.519 -69.196  1.00 52.57           C  
ANISOU 1561  CG2 ILE A1017     5817   3102  11054   -599   -825    101       C  
ATOM   1562  CD1 ILE A1017     -13.161 -43.939 -69.481  1.00 65.48           C  
ANISOU 1562  CD1 ILE A1017     7236   5579  12065   -727   -508     97       C  
ATOM   1563  N   GLU A1018     -10.812 -47.243 -65.432  1.00 63.80           N  
ANISOU 1563  N   GLU A1018     7619   4261  12361   -737  -1172   1168       N  
ATOM   1564  CA  GLU A1018      -9.660 -47.942 -64.866  1.00 81.47           C  
ANISOU 1564  CA  GLU A1018     9941   6158  14855   -595  -1479   1360       C  
ATOM   1565  C   GLU A1018     -10.034 -49.340 -64.384  1.00 88.16           C  
ANISOU 1565  C   GLU A1018    10937   6732  15828   -748  -1618   1623       C  
ATOM   1566  O   GLU A1018      -9.305 -50.309 -64.627  1.00 67.40           O  
ANISOU 1566  O   GLU A1018     8275   3842  13494   -581  -1795   1553       O  
ATOM   1567  CB  GLU A1018      -9.070 -47.129 -63.712  1.00 91.58           C  
ANISOU 1567  CB  GLU A1018    11327   7684  15786   -573  -1583   1606       C  
ATOM   1568  CG  GLU A1018      -7.761 -47.685 -63.176  1.00109.06           C  
ANISOU 1568  CG  GLU A1018    13570   9585  18283   -399  -1973   1805       C  
ATOM   1569  CD  GLU A1018      -7.318 -46.979 -61.911  1.00119.81           C  
ANISOU 1569  CD  GLU A1018    15101  11189  19234   -462  -2146   2096       C  
ATOM   1570  OE1 GLU A1018      -8.152 -46.277 -61.300  1.00109.91           O  
ANISOU 1570  OE1 GLU A1018    14004  10294  17461   -680  -1929   2178       O  
ATOM   1571  OE2 GLU A1018      -6.142 -47.125 -61.519  1.00124.21           O  
ANISOU 1571  OE2 GLU A1018    15624  11576  19996   -298  -2502   2226       O  
ATOM   1572  N   LYS A1019     -11.159 -49.462 -63.684  1.00 79.53           N  
ANISOU 1572  N   LYS A1019     9988   5699  14530  -1076  -1516   1931       N  
ATOM   1573  CA  LYS A1019     -11.623 -50.741 -63.160  1.00 81.95           C  
ANISOU 1573  CA  LYS A1019    10450   5767  14919  -1272  -1617   2222       C  
ATOM   1574  C   LYS A1019     -12.736 -51.355 -64.004  1.00100.27           C  
ANISOU 1574  C   LYS A1019    12678   8022  17399  -1439  -1451   2023       C  
ATOM   1575  O   LYS A1019     -13.398 -52.299 -63.552  1.00 96.63           O  
ANISOU 1575  O   LYS A1019    12334   7400  16983  -1677  -1472   2277       O  
ATOM   1576  CB  LYS A1019     -12.099 -50.591 -61.711  1.00100.07           C  
ANISOU 1576  CB  LYS A1019    12994   8189  16838  -1579  -1601   2748       C  
ATOM   1577  CG  LYS A1019     -11.030 -50.088 -60.746  1.00118.64           C  
ANISOU 1577  CG  LYS A1019    15511  10601  18965  -1474  -1851   3003       C  
ATOM   1578  CD  LYS A1019     -11.236 -50.666 -59.351  1.00137.45           C  
ANISOU 1578  CD  LYS A1019    18228  12966  21030  -1763  -1981   3564       C  
ATOM   1579  CE  LYS A1019     -11.143 -52.185 -59.359  1.00128.34           C  
ANISOU 1579  CE  LYS A1019    17117  11436  20211  -1760  -2192   3701       C  
ATOM   1580  NZ  LYS A1019     -11.314 -52.757 -57.992  1.00115.10           N  
ANISOU 1580  NZ  LYS A1019    15780   9746  18205  -2051  -2331   4273       N  
ATOM   1581  N   ALA A1020     -12.957 -50.846 -65.213  1.00111.34           N  
ANISOU 1581  N   ALA A1020    13883   9548  18872  -1339  -1310   1587       N  
ATOM   1582  CA  ALA A1020     -13.971 -51.411 -66.089  1.00 92.42           C  
ANISOU 1582  CA  ALA A1020    11403   7100  16611  -1504  -1223   1376       C  
ATOM   1583  C   ALA A1020     -13.539 -52.785 -66.595  1.00 82.76           C  
ANISOU 1583  C   ALA A1020    10246   5481  15719  -1409  -1406   1233       C  
ATOM   1584  O   ALA A1020     -12.359 -53.150 -66.564  1.00 82.21           O  
ANISOU 1584  O   ALA A1020    10204   5216  15818  -1145  -1562   1183       O  
ATOM   1585  CB  ALA A1020     -14.248 -50.481 -67.270  1.00 76.82           C  
ANISOU 1585  CB  ALA A1020     9234   5373  14580  -1430  -1083    966       C  
ATOM   1586  N   ASP A1021     -14.523 -53.557 -67.066  1.00114.28           N  
ANISOU 1586  N   ASP A1021    14236   9349  19836  -1634  -1386   1159       N  
ATOM   1587  CA  ASP A1021     -14.280 -54.896 -67.581  1.00 96.10           C  
ANISOU 1587  CA  ASP A1021    12008   6638  17866  -1590  -1539   1000       C  
ATOM   1588  C   ASP A1021     -15.011 -55.194 -68.883  1.00 85.09           C  
ANISOU 1588  C   ASP A1021    10550   5218  16561  -1699  -1498    583       C  
ATOM   1589  O   ASP A1021     -14.852 -56.295 -69.418  1.00 84.10           O  
ANISOU 1589  O   ASP A1021    10504   4741  16710  -1678  -1607    387       O  
ATOM   1590  CB  ASP A1021     -14.668 -55.955 -66.532  1.00 84.60           C  
ANISOU 1590  CB  ASP A1021    10709   4910  16526  -1815  -1648   1452       C  
ATOM   1591  CG  ASP A1021     -15.953 -55.607 -65.799  1.00 99.74           C  
ANISOU 1591  CG  ASP A1021    12619   7075  18203  -2194  -1476   1790       C  
ATOM   1592  OD1 ASP A1021     -16.166 -54.414 -65.497  1.00 90.50           O  
ANISOU 1592  OD1 ASP A1021    11362   6286  16738  -2216  -1304   1853       O  
ATOM   1593  OD2 ASP A1021     -16.749 -56.528 -65.514  1.00112.14           O  
ANISOU 1593  OD2 ASP A1021    14255   8456  19899  -2476  -1488   1989       O  
ATOM   1594  N   ASN A1022     -15.801 -54.259 -69.406  1.00 76.86           N  
ANISOU 1594  N   ASN A1022     9373   4526  15303  -1823  -1369    444       N  
ATOM   1595  CA  ASN A1022     -16.486 -54.469 -70.673  1.00 77.79           C  
ANISOU 1595  CA  ASN A1022     9445   4654  15458  -1949  -1391     58       C  
ATOM   1596  C   ASN A1022     -16.579 -53.141 -71.412  1.00 73.27           C  
ANISOU 1596  C   ASN A1022     8730   4477  14632  -1883  -1296   -177       C  
ATOM   1597  O   ASN A1022     -16.288 -52.075 -70.863  1.00 69.54           O  
ANISOU 1597  O   ASN A1022     8173   4261  13986  -1773  -1188    -14       O  
ATOM   1598  CB  ASN A1022     -17.871 -55.099 -70.469  1.00 81.19           C  
ANISOU 1598  CB  ASN A1022     9838   5039  15973  -2332  -1418    244       C  
ATOM   1599  CG  ASN A1022     -18.696 -54.382 -69.419  1.00 81.57           C  
ANISOU 1599  CG  ASN A1022     9747   5393  15853  -2528  -1261    662       C  
ATOM   1600  OD1 ASN A1022     -18.703 -53.154 -69.348  1.00 75.60           O  
ANISOU 1600  OD1 ASN A1022     8854   4990  14881  -2446  -1135    669       O  
ATOM   1601  ND2 ASN A1022     -19.397 -55.150 -68.595  1.00104.18           N  
ANISOU 1601  ND2 ASN A1022    12645   8117  18820  -2801  -1240   1004       N  
ATOM   1602  N   ALA A1023     -16.999 -53.222 -72.677  1.00 74.20           N  
ANISOU 1602  N   ALA A1023     8841   4630  14720  -1971  -1356   -561       N  
ATOM   1603  CA  ALA A1023     -17.015 -52.040 -73.532  1.00 70.80           C  
ANISOU 1603  CA  ALA A1023     8311   4543  14046  -1919  -1314   -803       C  
ATOM   1604  C   ALA A1023     -18.141 -51.082 -73.165  1.00 77.21           C  
ANISOU 1604  C   ALA A1023     8891   5715  14731  -2104  -1273   -541       C  
ATOM   1605  O   ALA A1023     -18.038 -49.879 -73.429  1.00 65.31           O  
ANISOU 1605  O   ALA A1023     7266   4506  13044  -2012  -1215   -587       O  
ATOM   1606  CB  ALA A1023     -17.131 -52.458 -74.998  1.00 73.38           C  
ANISOU 1606  CB  ALA A1023     8751   4807  14324  -2001  -1425  -1285       C  
ATOM   1607  N   ALA A1024     -19.219 -51.588 -72.561  1.00 86.13           N  
ANISOU 1607  N   ALA A1024     9928   6819  15978  -2362  -1283   -270       N  
ATOM   1608  CA  ALA A1024     -20.350 -50.727 -72.231  1.00 70.19           C  
ANISOU 1608  CA  ALA A1024     7629   5150  13890  -2523  -1201    -50       C  
ATOM   1609  C   ALA A1024     -19.994 -49.739 -71.127  1.00 67.78           C  
ANISOU 1609  C   ALA A1024     7244   5042  13468  -2381   -978    230       C  
ATOM   1610  O   ALA A1024     -20.408 -48.575 -71.172  1.00 96.13           O  
ANISOU 1610  O   ALA A1024    10614   8958  16952  -2349   -887    258       O  
ATOM   1611  CB  ALA A1024     -21.554 -51.577 -71.828  1.00 75.19           C  
ANISOU 1611  CB  ALA A1024     8162   5703  14702  -2842  -1216    154       C  
ATOM   1612  N   GLN A1025     -19.225 -50.180 -70.129  1.00 67.02           N  
ANISOU 1612  N   GLN A1025     7329   4744  13392  -2298   -910    441       N  
ATOM   1613  CA  GLN A1025     -18.868 -49.292 -69.026  1.00 65.31           C  
ANISOU 1613  CA  GLN A1025     7087   4702  13025  -2207   -719    706       C  
ATOM   1614  C   GLN A1025     -17.947 -48.172 -69.494  1.00 75.67           C  
ANISOU 1614  C   GLN A1025     8384   6162  14206  -1929   -709    496       C  
ATOM   1615  O   GLN A1025     -18.161 -46.999 -69.163  1.00 83.87           O  
ANISOU 1615  O   GLN A1025     9278   7517  15073  -1872   -548    566       O  
ATOM   1616  CB  GLN A1025     -18.214 -50.086 -67.895  1.00 66.55           C  
ANISOU 1616  CB  GLN A1025     7486   4597  13204  -2207   -731   1005       C  
ATOM   1617  CG  GLN A1025     -19.166 -50.983 -67.123  1.00 83.54           C  
ANISOU 1617  CG  GLN A1025     9657   6655  15427  -2529   -669   1321       C  
ATOM   1618  CD  GLN A1025     -18.485 -51.679 -65.959  1.00 86.34           C  
ANISOU 1618  CD  GLN A1025    10284   6770  15749  -2544   -714   1675       C  
ATOM   1619  OE1 GLN A1025     -17.551 -51.143 -65.362  1.00 71.45           O  
ANISOU 1619  OE1 GLN A1025     8518   4919  13711  -2365   -723   1790       O  
ATOM   1620  NE2 GLN A1025     -18.947 -52.881 -65.634  1.00 80.87           N  
ANISOU 1620  NE2 GLN A1025     9697   5825  15204  -2768   -774   1867       N  
ATOM   1621  N   VAL A1026     -16.916 -48.514 -70.270  1.00 66.54           N  
ANISOU 1621  N   VAL A1026     7375   4817  13090  -1729   -843    215       N  
ATOM   1622  CA  VAL A1026     -15.962 -47.502 -70.714  1.00 73.92           C  
ANISOU 1622  CA  VAL A1026     8304   5913  13867  -1466   -802     19       C  
ATOM   1623  C   VAL A1026     -16.615 -46.542 -71.702  1.00 58.52           C  
ANISOU 1623  C   VAL A1026     6195   4314  11726  -1486   -784   -165       C  
ATOM   1624  O   VAL A1026     -16.362 -45.332 -71.667  1.00 65.26           O  
ANISOU 1624  O   VAL A1026     6980   5475  12341  -1324   -679   -152       O  
ATOM   1625  CB  VAL A1026     -14.704 -48.171 -71.303  1.00 57.33           C  
ANISOU 1625  CB  VAL A1026     6359   3522  11900  -1257   -893   -252       C  
ATOM   1626  CG1 VAL A1026     -15.084 -49.254 -72.291  1.00 70.14           C  
ANISOU 1626  CG1 VAL A1026     8059   4953  13637  -1370  -1003   -525       C  
ATOM   1627  CG2 VAL A1026     -13.802 -47.136 -71.964  1.00 57.66           C  
ANISOU 1627  CG2 VAL A1026     6372   3817  11720  -1010   -803   -487       C  
ATOM   1628  N   LYS A1027     -17.477 -47.056 -72.584  1.00 68.45           N  
ANISOU 1628  N   LYS A1027     7396   5512  13101  -1702   -928   -320       N  
ATOM   1629  CA  LYS A1027     -18.174 -46.179 -73.520  1.00 68.36           C  
ANISOU 1629  CA  LYS A1027     7232   5825  12918  -1749   -995   -434       C  
ATOM   1630  C   LYS A1027     -19.079 -45.199 -72.785  1.00 64.66           C  
ANISOU 1630  C   LYS A1027     6496   5646  12426  -1775   -868   -152       C  
ATOM   1631  O   LYS A1027     -19.129 -44.011 -73.127  1.00 67.57           O  
ANISOU 1631  O   LYS A1027     6758   6299  12616  -1641   -843   -163       O  
ATOM   1632  CB  LYS A1027     -18.986 -47.001 -74.519  1.00 64.22           C  
ANISOU 1632  CB  LYS A1027     6701   5168  12533  -2023  -1239   -634       C  
ATOM   1633  CG  LYS A1027     -19.762 -46.146 -75.511  1.00 60.23           C  
ANISOU 1633  CG  LYS A1027     6041   4990  11852  -2102  -1403   -702       C  
ATOM   1634  CD  LYS A1027     -20.848 -46.935 -76.222  1.00 79.87           C  
ANISOU 1634  CD  LYS A1027     8483   7420  14445  -2401  -1665   -796       C  
ATOM   1635  CE  LYS A1027     -21.667 -46.028 -77.129  1.00 81.80           C  
ANISOU 1635  CE  LYS A1027     8535   7981  14565  -2497  -1910   -794       C  
ATOM   1636  NZ  LYS A1027     -22.835 -46.732 -77.728  1.00102.95           N  
ANISOU 1636  NZ  LYS A1027    11142  10663  17313  -2776  -2175   -832       N  
ATOM   1637  N   ASP A1028     -19.807 -45.679 -71.775  1.00 62.96           N  
ANISOU 1637  N   ASP A1028     6167   5347  12409  -1952   -764    101       N  
ATOM   1638  CA  ASP A1028     -20.674 -44.793 -71.006  1.00 56.92           C  
ANISOU 1638  CA  ASP A1028     5128   4853  11645  -1971   -559    320       C  
ATOM   1639  C   ASP A1028     -19.862 -43.737 -70.269  1.00 64.26           C  
ANISOU 1639  C   ASP A1028     6147   5959  12311  -1696   -348    375       C  
ATOM   1640  O   ASP A1028     -20.220 -42.554 -70.273  1.00 66.78           O  
ANISOU 1640  O   ASP A1028     6280   6531  12563  -1577   -251    377       O  
ATOM   1641  CB  ASP A1028     -21.517 -45.607 -70.025  1.00 66.50           C  
ANISOU 1641  CB  ASP A1028     6257   5976  13035  -2224   -415    571       C  
ATOM   1642  CG  ASP A1028     -22.478 -44.748 -69.225  1.00 95.37           C  
ANISOU 1642  CG  ASP A1028     9599   9920  16717  -2257   -124    747       C  
ATOM   1643  OD1 ASP A1028     -23.380 -44.134 -69.834  1.00 81.96           O  
ANISOU 1643  OD1 ASP A1028     7604   8425  15112  -2240   -181    678       O  
ATOM   1644  OD2 ASP A1028     -22.335 -44.692 -67.985  1.00115.38           O  
ANISOU 1644  OD2 ASP A1028    12196  12477  19165  -2293    162    948       O  
ATOM   1645  N   ALA A1029     -18.755 -44.145 -69.642  1.00 57.14           N  
ANISOU 1645  N   ALA A1029     5519   4895  11296  -1595   -313    417       N  
ATOM   1646  CA  ALA A1029     -17.925 -43.191 -68.914  1.00 57.69           C  
ANISOU 1646  CA  ALA A1029     5688   5115  11116  -1369   -168    459       C  
ATOM   1647  C   ALA A1029     -17.314 -42.160 -69.853  1.00 51.93           C  
ANISOU 1647  C   ALA A1029     4941   4534  10255  -1145   -238    248       C  
ATOM   1648  O   ALA A1029     -17.196 -40.981 -69.499  1.00 58.29           O  
ANISOU 1648  O   ALA A1029     5691   5536  10921  -1003   -114    263       O  
ATOM   1649  CB  ALA A1029     -16.833 -43.926 -68.140  1.00 50.77           C  
ANISOU 1649  CB  ALA A1029     5086   4012  10193  -1322   -212    568       C  
ATOM   1650  N   LEU A1030     -16.920 -42.583 -71.056  1.00 47.70           N  
ANISOU 1650  N   LEU A1030     4471   3899   9752  -1132   -420     43       N  
ATOM   1651  CA  LEU A1030     -16.363 -41.642 -72.022  1.00 52.48           C  
ANISOU 1651  CA  LEU A1030     5083   4666  10190   -974   -466   -123       C  
ATOM   1652  C   LEU A1030     -17.413 -40.645 -72.493  1.00 53.57           C  
ANISOU 1652  C   LEU A1030     4997   5035  10322  -1008   -499    -75       C  
ATOM   1653  O   LEU A1030     -17.102 -39.469 -72.720  1.00 72.58           O  
ANISOU 1653  O   LEU A1030     7375   7598  12604   -860   -471    -76       O  
ATOM   1654  CB  LEU A1030     -15.770 -42.398 -73.210  1.00 56.37           C  
ANISOU 1654  CB  LEU A1030     5724   5025  10668   -993   -603   -379       C  
ATOM   1655  CG  LEU A1030     -14.460 -43.144 -72.966  1.00 52.05           C  
ANISOU 1655  CG  LEU A1030     5351   4239  10186   -863   -567   -483       C  
ATOM   1656  CD1 LEU A1030     -14.139 -44.040 -74.148  1.00 49.10           C  
ANISOU 1656  CD1 LEU A1030     5099   3702   9855   -910   -651   -800       C  
ATOM   1657  CD2 LEU A1030     -13.328 -42.164 -72.713  1.00 44.54           C  
ANISOU 1657  CD2 LEU A1030     4411   3418   9093   -640   -459   -474       C  
ATOM   1658  N   THR A1031     -18.663 -41.093 -72.648  1.00 50.97           N  
ANISOU 1658  N   THR A1031     4483   4702  10180  -1207   -584    -17       N  
ATOM   1659  CA  THR A1031     -19.724 -40.174 -73.052  1.00 58.82           C  
ANISOU 1659  CA  THR A1031     5195   5888  11267  -1223   -658     56       C  
ATOM   1660  C   THR A1031     -19.997 -39.144 -71.963  1.00 56.63           C  
ANISOU 1660  C   THR A1031     4747   5725  11044  -1079   -400    190       C  
ATOM   1661  O   THR A1031     -20.172 -37.953 -72.252  1.00 71.01           O  
ANISOU 1661  O   THR A1031     6435   7670  12877   -936   -422    209       O  
ATOM   1662  CB  THR A1031     -20.999 -40.948 -73.388  1.00 55.31           C  
ANISOU 1662  CB  THR A1031     4530   5402  11082  -1486   -823     92       C  
ATOM   1663  OG1 THR A1031     -20.720 -41.925 -74.400  1.00 56.70           O  
ANISOU 1663  OG1 THR A1031     4913   5445  11184  -1635  -1068    -94       O  
ATOM   1664  CG2 THR A1031     -22.070 -40.001 -73.906  1.00 68.25           C  
ANISOU 1664  CG2 THR A1031     5826   7223  12884  -1482   -972    181       C  
ATOM   1665  N   LYS A1032     -20.040 -39.586 -70.702  1.00 48.73           N  
ANISOU 1665  N   LYS A1032     3774   4672  10069  -1126   -155    280       N  
ATOM   1666  CA  LYS A1032     -20.214 -38.643 -69.600  1.00 56.68           C  
ANISOU 1666  CA  LYS A1032     4688   5798  11051  -1004    138    342       C  
ATOM   1667  C   LYS A1032     -19.006 -37.725 -69.461  1.00 52.41           C  
ANISOU 1667  C   LYS A1032     4363   5279  10270   -776    162    263       C  
ATOM   1668  O   LYS A1032     -19.147 -36.562 -69.058  1.00 68.00           O  
ANISOU 1668  O   LYS A1032     6240   7345  12253   -630    306    239       O  
ATOM   1669  CB  LYS A1032     -20.471 -39.387 -68.287  1.00 50.37           C  
ANISOU 1669  CB  LYS A1032     3945   4967  10227  -1160    398    469       C  
ATOM   1670  CG  LYS A1032     -21.903 -39.879 -68.115  1.00 67.93           C  
ANISOU 1670  CG  LYS A1032     5837   7227  12745  -1387    511    575       C  
ATOM   1671  CD  LYS A1032     -21.961 -41.394 -67.953  1.00 72.69           C  
ANISOU 1671  CD  LYS A1032     6572   7643  13403  -1661    440    697       C  
ATOM   1672  CE  LYS A1032     -21.519 -41.843 -66.569  1.00 77.13           C  
ANISOU 1672  CE  LYS A1032     7399   8173  13736  -1744    688    862       C  
ATOM   1673  NZ  LYS A1032     -22.562 -41.580 -65.540  1.00 70.72           N  
ANISOU 1673  NZ  LYS A1032     6363   7546  12961  -1887   1098    981       N  
ATOM   1674  N   MET A1033     -17.815 -38.221 -69.793  1.00 61.71           N  
ANISOU 1674  N   MET A1033     5808   6353  11284   -743     29    203       N  
ATOM   1675  CA  MET A1033     -16.637 -37.359 -69.770  1.00 41.80           C  
ANISOU 1675  CA  MET A1033     3439   3854   8589   -555     30    133       C  
ATOM   1676  C   MET A1033     -16.703 -36.304 -70.867  1.00 65.43           C  
ANISOU 1676  C   MET A1033     6326   6932  11603   -459    -88     84       C  
ATOM   1677  O   MET A1033     -16.250 -35.167 -70.674  1.00 70.16           O  
ANISOU 1677  O   MET A1033     6938   7568  12153   -318    -33     70       O  
ATOM   1678  CB  MET A1033     -15.362 -38.189 -69.915  1.00 47.18           C  
ANISOU 1678  CB  MET A1033     4352   4397   9175   -537    -72     78       C  
ATOM   1679  CG  MET A1033     -14.960 -38.933 -68.659  1.00 62.72           C  
ANISOU 1679  CG  MET A1033     6476   6258  11096   -581     -8    186       C  
ATOM   1680  SD  MET A1033     -13.407 -39.828 -68.843  1.00 86.22           S  
ANISOU 1680  SD  MET A1033     9643   9020  14095   -498   -172    129       S  
ATOM   1681  CE  MET A1033     -12.288 -38.463 -69.134  1.00 78.57           C  
ANISOU 1681  CE  MET A1033     8664   8177  13011   -304   -166     17       C  
ATOM   1682  N   ARG A1034     -17.259 -36.665 -72.026  1.00 62.69           N  
ANISOU 1682  N   ARG A1034     5898   6602  11318   -559   -281     72       N  
ATOM   1683  CA  ARG A1034     -17.395 -35.702 -73.113  1.00 42.33           C  
ANISOU 1683  CA  ARG A1034     3251   4113   8720   -509   -447     91       C  
ATOM   1684  C   ARG A1034     -18.314 -34.557 -72.708  1.00 51.08           C  
ANISOU 1684  C   ARG A1034     4095   5263  10050   -407   -393    193       C  
ATOM   1685  O   ARG A1034     -18.027 -33.386 -72.990  1.00 61.11           O  
ANISOU 1685  O   ARG A1034     5358   6540  11319   -278   -433    233       O  
ATOM   1686  CB  ARG A1034     -17.920 -36.400 -74.369  1.00 49.53           C  
ANISOU 1686  CB  ARG A1034     4158   5053   9607   -683   -705     61       C  
ATOM   1687  CG  ARG A1034     -17.215 -35.984 -75.648  1.00 44.17           C  
ANISOU 1687  CG  ARG A1034     3659   4455   8669   -690   -860     17       C  
ATOM   1688  CD  ARG A1034     -17.923 -36.530 -76.878  1.00 46.92           C  
ANISOU 1688  CD  ARG A1034     4022   4870   8937   -893  -1155    -13       C  
ATOM   1689  NE  ARG A1034     -18.873 -35.571 -77.434  1.00 85.00           N  
ANISOU 1689  NE  ARG A1034     8646   9791  13858   -905  -1407    188       N  
ATOM   1690  CZ  ARG A1034     -18.602 -34.758 -78.450  1.00 74.62           C  
ANISOU 1690  CZ  ARG A1034     7453   8585  12316   -919  -1590    287       C  
ATOM   1691  NH1 ARG A1034     -17.409 -34.793 -79.027  1.00 64.45           N  
ANISOU 1691  NH1 ARG A1034     6471   7352  10665   -941  -1485    173       N  
ATOM   1692  NH2 ARG A1034     -19.524 -33.915 -78.894  1.00 78.67           N  
ANISOU 1692  NH2 ARG A1034     7764   9143  12986   -920  -1877    519       N  
ATOM   1693  N   ALA A1035     -19.422 -34.878 -72.038  1.00 72.17           N  
ANISOU 1693  N   ALA A1035     6530   7941  12952   -465   -283    233       N  
ATOM   1694  CA  ALA A1035     -20.322 -33.838 -71.549  1.00 49.46           C  
ANISOU 1694  CA  ALA A1035     3351   5084  10358   -338   -159    278       C  
ATOM   1695  C   ALA A1035     -19.663 -33.006 -70.455  1.00 61.68           C  
ANISOU 1695  C   ALA A1035     5023   6600  11811   -172    120    192       C  
ATOM   1696  O   ALA A1035     -19.849 -31.784 -70.395  1.00 72.33           O  
ANISOU 1696  O   ALA A1035     6245   7906  13329     -2    154    177       O  
ATOM   1697  CB  ALA A1035     -21.618 -34.465 -71.038  1.00 49.68           C  
ANISOU 1697  CB  ALA A1035     3063   5146  10666   -462    -32    318       C  
ATOM   1698  N   ALA A1036     -18.887 -33.650 -69.582  1.00 53.67           N  
ANISOU 1698  N   ALA A1036     4266   5581  10544   -227    284    135       N  
ATOM   1699  CA  ALA A1036     -18.221 -32.914 -68.513  1.00 58.76           C  
ANISOU 1699  CA  ALA A1036     5072   6210  11043   -113    495     39       C  
ATOM   1700  C   ALA A1036     -17.134 -31.999 -69.064  1.00 61.24           C  
ANISOU 1700  C   ALA A1036     5535   6460  11272     11    338      5       C  
ATOM   1701  O   ALA A1036     -16.979 -30.863 -68.602  1.00 60.51           O  
ANISOU 1701  O   ALA A1036     5443   6314  11232    142    435    -76       O  
ATOM   1702  CB  ALA A1036     -17.637 -33.884 -67.488  1.00 43.41           C  
ANISOU 1702  CB  ALA A1036     3383   4280   8833   -232    619     43       C  
ATOM   1703  N   ALA A1037     -16.376 -32.475 -70.055  1.00 59.90           N  
ANISOU 1703  N   ALA A1037     5491   6286  10983    -43    121     49       N  
ATOM   1704  CA  ALA A1037     -15.306 -31.661 -70.623  1.00 55.17           C  
ANISOU 1704  CA  ALA A1037     5015   5648  10301     30     13     41       C  
ATOM   1705  C   ALA A1037     -15.861 -30.451 -71.363  1.00 57.92           C  
ANISOU 1705  C   ALA A1037     5205   5959  10845    114    -98    124       C  
ATOM   1706  O   ALA A1037     -15.305 -29.351 -71.267  1.00 58.52           O  
ANISOU 1706  O   ALA A1037     5329   5945  10960    206    -94    116       O  
ATOM   1707  CB  ALA A1037     -14.436 -32.507 -71.553  1.00 63.87           C  
ANISOU 1707  CB  ALA A1037     6259   6775  11233    -58   -121     40       C  
ATOM   1708  N   LEU A1038     -16.953 -30.635 -72.111  1.00 51.91           N  
ANISOU 1708  N   LEU A1038     4247   5236  10240     72   -241    226       N  
ATOM   1709  CA  LEU A1038     -17.568 -29.506 -72.802  1.00 43.62           C  
ANISOU 1709  CA  LEU A1038     3022   4121   9430    160   -414    362       C  
ATOM   1710  C   LEU A1038     -18.156 -28.505 -71.820  1.00 54.50           C  
ANISOU 1710  C   LEU A1038     4209   5370  11129    344   -226    288       C  
ATOM   1711  O   LEU A1038     -18.150 -27.298 -72.088  1.00 73.20           O  
ANISOU 1711  O   LEU A1038     6521   7589  13704    470   -319    356       O  
ATOM   1712  CB  LEU A1038     -18.645 -30.000 -73.771  1.00 45.68           C  
ANISOU 1712  CB  LEU A1038     3093   4460   9805     58   -673    498       C  
ATOM   1713  CG  LEU A1038     -18.152 -30.718 -75.032  1.00 55.00           C  
ANISOU 1713  CG  LEU A1038     4488   5755  10654   -130   -908    550       C  
ATOM   1714  CD1 LEU A1038     -19.312 -31.137 -75.926  1.00 48.95           C  
ANISOU 1714  CD1 LEU A1038     3542   5062   9996   -257  -1221    670       C  
ATOM   1715  CD2 LEU A1038     -17.178 -29.837 -75.795  1.00 52.16           C  
ANISOU 1715  CD2 LEU A1038     4336   5383  10098   -122  -1004    652       C  
ATOM   1716  N   ASP A1039     -18.663 -28.982 -70.681  1.00 62.20           N  
ANISOU 1716  N   ASP A1039     5098   6386  12150    352     57    143       N  
ATOM   1717  CA  ASP A1039     -19.168 -28.073 -69.661  1.00 56.25           C  
ANISOU 1717  CA  ASP A1039     4196   5529  11647    520    324     -8       C  
ATOM   1718  C   ASP A1039     -18.029 -27.319 -68.987  1.00 46.69           C  
ANISOU 1718  C   ASP A1039     3270   4217  10254    584    429   -158       C  
ATOM   1719  O   ASP A1039     -18.130 -26.109 -68.759  1.00 62.64           O  
ANISOU 1719  O   ASP A1039     5223   6052  12523    745    478   -247       O  
ATOM   1720  CB  ASP A1039     -19.989 -28.853 -68.636  1.00 64.18           C  
ANISOU 1720  CB  ASP A1039     5066   6652  12666    457    649   -118       C  
ATOM   1721  CG  ASP A1039     -20.857 -27.957 -67.778  1.00 85.66           C  
ANISOU 1721  CG  ASP A1039     7531   9294  15722    632    970   -299       C  
ATOM   1722  OD1 ASP A1039     -20.335 -26.972 -67.215  1.00121.41           O  
ANISOU 1722  OD1 ASP A1039    12207  13691  20234    764   1093   -477       O  
ATOM   1723  OD2 ASP A1039     -22.070 -28.232 -67.674  1.00 85.79           O  
ANISOU 1723  OD2 ASP A1039     7195   9369  16032    628   1107   -287       O  
ATOM   1724  N   ALA A1040     -16.939 -28.016 -68.659  1.00 55.00           N  
ANISOU 1724  N   ALA A1040     4621   5356  10919    459    437   -192       N  
ATOM   1725  CA  ALA A1040     -15.808 -27.352 -68.020  1.00 52.45           C  
ANISOU 1725  CA  ALA A1040     4545   4947  10436    486    477   -324       C  
ATOM   1726  C   ALA A1040     -15.117 -26.380 -68.966  1.00 52.12           C  
ANISOU 1726  C   ALA A1040     4533   4758  10511    528    248   -219       C  
ATOM   1727  O   ALA A1040     -14.486 -25.420 -68.510  1.00 76.81           O  
ANISOU 1727  O   ALA A1040     7770   7733  13679    579    269   -332       O  
ATOM   1728  CB  ALA A1040     -14.813 -28.390 -67.505  1.00 41.48           C  
ANISOU 1728  CB  ALA A1040     3410   3675   8675    347    474   -339       C  
ATOM   1729  N   GLN A1041     -15.225 -26.608 -70.278  1.00 62.87           N  
ANISOU 1729  N   GLN A1041     5821   6163  11906    476     26      0       N  
ATOM   1730  CA  GLN A1041     -14.602 -25.706 -71.241  1.00 51.93           C  
ANISOU 1730  CA  GLN A1041     4487   4663  10582    469   -176    157       C  
ATOM   1731  C   GLN A1041     -15.212 -24.312 -71.179  1.00 45.41           C  
ANISOU 1731  C   GLN A1041     3518   3580  10156    629   -213    178       C  
ATOM   1732  O   GLN A1041     -14.507 -23.316 -71.376  1.00 97.50           O  
ANISOU 1732  O   GLN A1041    10211   9993  16842    634   -297    229       O  
ATOM   1733  CB  GLN A1041     -14.729 -26.282 -72.652  1.00 42.41           C  
ANISOU 1733  CB  GLN A1041     3269   3594   9250    348   -392    381       C  
ATOM   1734  CG  GLN A1041     -14.034 -25.469 -73.730  1.00 43.15           C  
ANISOU 1734  CG  GLN A1041     3464   3627   9303    276   -573    591       C  
ATOM   1735  CD  GLN A1041     -14.322 -25.988 -75.126  1.00 56.99           C  
ANISOU 1735  CD  GLN A1041     5245   5546  10862    133   -785    798       C  
ATOM   1736  OE1 GLN A1041     -15.465 -26.299 -75.462  1.00 58.97           O  
ANISOU 1736  OE1 GLN A1041     5343   5841  11222    146   -932    877       O  
ATOM   1737  NE2 GLN A1041     -13.282 -26.092 -75.944  1.00 55.59           N  
ANISOU 1737  NE2 GLN A1041     5259   5474  10388    -23   -795    872       N  
ATOM   1738  N   LYS A1042     -16.511 -24.220 -70.899  1.00 79.02           N  
ANISOU 1738  N   LYS A1042     7518   7793  14714    762   -144    138       N  
ATOM   1739  CA  LYS A1042     -17.198 -22.940 -70.794  1.00 79.36           C  
ANISOU 1739  CA  LYS A1042     7375   7551  15227    956   -163    125       C  
ATOM   1740  C   LYS A1042     -16.980 -22.251 -69.452  1.00 75.56           C  
ANISOU 1740  C   LYS A1042     6998   6930  14782   1045    130   -223       C  
ATOM   1741  O   LYS A1042     -17.540 -21.171 -69.233  1.00 86.90           O  
ANISOU 1741  O   LYS A1042     8354   8172  16493   1153    162   -305       O  
ATOM   1742  CB  LYS A1042     -18.698 -23.130 -71.032  1.00 69.18           C  
ANISOU 1742  CB  LYS A1042     5792   6327  14167   1002   -190    195       C  
ATOM   1743  CG  LYS A1042     -19.068 -23.410 -72.478  1.00 70.91           C  
ANISOU 1743  CG  LYS A1042     5912   6614  14418    916   -583    554       C  
ATOM   1744  CD  LYS A1042     -20.557 -23.681 -72.619  1.00 90.81           C  
ANISOU 1744  CD  LYS A1042     8132   9193  17179    940   -628    600       C  
ATOM   1745  CE  LYS A1042     -21.003 -23.574 -74.068  1.00101.94           C  
ANISOU 1745  CE  LYS A1042     9459  10601  18670    866  -1101    969       C  
ATOM   1746  NZ  LYS A1042     -20.219 -24.466 -74.965  1.00127.59           N  
ANISOU 1746  NZ  LYS A1042    12864  14051  21562    689  -1331   1142       N  
ATOM   1747  N   ALA A1043     -16.193 -22.836 -68.557  1.00 53.31           N  
ANISOU 1747  N   ALA A1043     4395   4232  11630    965    318   -431       N  
ATOM   1748  CA  ALA A1043     -15.938 -22.233 -67.259  1.00 58.89           C  
ANISOU 1748  CA  ALA A1043     5244   4817  12313   1025    567   -786       C  
ATOM   1749  C   ALA A1043     -14.680 -21.369 -67.304  1.00 56.94           C  
ANISOU 1749  C   ALA A1043     5232   4369  12034    964    402   -808       C  
ATOM   1750  O   ALA A1043     -13.883 -21.426 -68.243  1.00 56.39           O  
ANISOU 1750  O   ALA A1043     5226   4316  11883    845    156   -546       O  
ATOM   1751  CB  ALA A1043     -15.808 -23.313 -66.184  1.00 50.75           C  
ANISOU 1751  CB  ALA A1043     4379   4067  10837    901    809   -960       C  
ATOM   1752  N   THR A1044     -14.513 -20.551 -66.266  1.00 55.82           N  
ANISOU 1752  N   THR A1044     5218   4035  11957   1024    562  -1148       N  
ATOM   1753  CA  THR A1044     -13.335 -19.709 -66.118  1.00 59.56           C  
ANISOU 1753  CA  THR A1044     5913   4293  12426    936    409  -1225       C  
ATOM   1754  C   THR A1044     -12.502 -20.224 -64.954  1.00 53.63           C  
ANISOU 1754  C   THR A1044     5448   3729  11199    778    493  -1475       C  
ATOM   1755  O   THR A1044     -12.974 -20.198 -63.807  1.00 69.30           O  
ANISOU 1755  O   THR A1044     7536   5751  13045    819    755  -1815       O  
ATOM   1756  CB  THR A1044     -13.730 -18.251 -65.888  1.00 66.20           C  
ANISOU 1756  CB  THR A1044     6733   4848  13573   1041    428  -1380       C  
ATOM   1757  OG1 THR A1044     -14.600 -17.818 -66.942  1.00 94.34           O  
ANISOU 1757  OG1 THR A1044    10044   8351  17451   1132    293  -1076       O  
ATOM   1758  CG2 THR A1044     -12.496 -17.362 -65.864  1.00 59.30           C  
ANISOU 1758  CG2 THR A1044     6064   3754  12714    907    227  -1406       C  
ATOM   1759  N   PRO A1045     -11.282 -20.697 -65.192  1.00 51.24           N  
ANISOU 1759  N   PRO A1045     5273   3554  10642    591    281  -1317       N  
ATOM   1760  CA  PRO A1045     -10.487 -21.297 -64.113  1.00 50.76           C  
ANISOU 1760  CA  PRO A1045     5460   3679  10149    439    276  -1489       C  
ATOM   1761  C   PRO A1045     -10.080 -20.256 -63.086  1.00 64.57           C  
ANISOU 1761  C   PRO A1045     7429   5208  11897    402    279  -1857       C  
ATOM   1762  O   PRO A1045     -10.064 -19.051 -63.383  1.00 72.96           O  
ANISOU 1762  O   PRO A1045     8450   5927  13346    464    225  -1938       O  
ATOM   1763  CB  PRO A1045      -9.265 -21.865 -64.851  1.00 47.88           C  
ANISOU 1763  CB  PRO A1045     5073   3424   9694    291     17  -1210       C  
ATOM   1764  CG  PRO A1045      -9.163 -21.044 -66.092  1.00 82.36           C  
ANISOU 1764  CG  PRO A1045     9280   7583  14431    317    -96   -993       C  
ATOM   1765  CD  PRO A1045     -10.574 -20.717 -66.483  1.00 74.32           C  
ANISOU 1765  CD  PRO A1045     8104   6466  13669    505     41   -964       C  
ATOM   1766  N   PRO A1046      -9.750 -20.681 -61.862  1.00 57.76           N  
ANISOU 1766  N   PRO A1046     6831   4517  10599    280    317  -2085       N  
ATOM   1767  CA  PRO A1046      -9.422 -19.697 -60.815  1.00 59.67           C  
ANISOU 1767  CA  PRO A1046     7336   4565  10769    216    318  -2501       C  
ATOM   1768  C   PRO A1046      -8.195 -18.857 -61.126  1.00 62.11           C  
ANISOU 1768  C   PRO A1046     7674   4616  11307     87    -25  -2479       C  
ATOM   1769  O   PRO A1046      -8.162 -17.671 -60.776  1.00 63.69           O  
ANISOU 1769  O   PRO A1046     7980   4486  11733     95    -27  -2785       O  
ATOM   1770  CB  PRO A1046      -9.212 -20.574 -59.571  1.00 60.80           C  
ANISOU 1770  CB  PRO A1046     7783   5029  10289     53    349  -2634       C  
ATOM   1771  CG  PRO A1046      -9.959 -21.838 -59.862  1.00 58.14           C  
ANISOU 1771  CG  PRO A1046     7302   4985   9805    107    525  -2360       C  
ATOM   1772  CD  PRO A1046      -9.807 -22.054 -61.335  1.00 55.48           C  
ANISOU 1772  CD  PRO A1046     6640   4587   9855    191    369  -1983       C  
ATOM   1773  N   LYS A1047      -7.180 -19.436 -61.773  1.00 57.13           N  
ANISOU 1773  N   LYS A1047     6933   4108  10664    -39   -295  -2144       N  
ATOM   1774  CA  LYS A1047      -5.975 -18.671 -62.083  1.00 68.30           C  
ANISOU 1774  CA  LYS A1047     8320   5301  12330   -197   -593  -2098       C  
ATOM   1775  C   LYS A1047      -6.255 -17.601 -63.131  1.00 59.44           C  
ANISOU 1775  C   LYS A1047     7017   3829  11738   -111   -568  -1972       C  
ATOM   1776  O   LYS A1047      -5.693 -16.500 -63.068  1.00 61.33           O  
ANISOU 1776  O   LYS A1047     7307   3733  12263   -213   -721  -2091       O  
ATOM   1777  CB  LYS A1047      -4.862 -19.606 -62.556  1.00 55.26           C  
ANISOU 1777  CB  LYS A1047     6527   3883  10586   -332   -820  -1778       C  
ATOM   1778  CG  LYS A1047      -3.525 -18.915 -62.779  1.00 56.74           C  
ANISOU 1778  CG  LYS A1047     6633   3888  11037   -535  -1113  -1730       C  
ATOM   1779  CD  LYS A1047      -2.463 -19.901 -63.238  1.00 76.02           C  
ANISOU 1779  CD  LYS A1047     8865   6569  13449   -632  -1279  -1444       C  
ATOM   1780  CE  LYS A1047      -1.149 -19.199 -63.548  1.00 82.26           C  
ANISOU 1780  CE  LYS A1047     9488   7190  14577   -846  -1523  -1375       C  
ATOM   1781  NZ  LYS A1047      -0.574 -18.521 -62.353  1.00 94.38           N  
ANISOU 1781  NZ  LYS A1047    11228   8569  16061  -1024  -1806  -1686       N  
ATOM   1782  N   LEU A1048      -7.119 -17.904 -64.100  1.00 56.36           N  
ANISOU 1782  N   LEU A1048     6427   3496  11494     55   -417  -1708       N  
ATOM   1783  CA  LEU A1048      -7.485 -16.965 -65.154  1.00 58.33           C  
ANISOU 1783  CA  LEU A1048     6517   3465  12182    135   -437  -1492       C  
ATOM   1784  C   LEU A1048      -8.764 -16.202 -64.834  1.00 60.30           C  
ANISOU 1784  C   LEU A1048     6760   3559  12591    359   -243  -1685       C  
ATOM   1785  O   LEU A1048      -9.544 -15.891 -65.744  1.00 71.46           O  
ANISOU 1785  O   LEU A1048     7986   4929  14236    488   -227  -1424       O  
ATOM   1786  CB  LEU A1048      -7.619 -17.703 -66.487  1.00 54.01           C  
ANISOU 1786  CB  LEU A1048     5764   3104  11653    148   -451  -1054       C  
ATOM   1787  CG  LEU A1048      -6.476 -18.661 -66.830  1.00 59.05           C  
ANISOU 1787  CG  LEU A1048     6362   4051  12022    -36   -550   -862       C  
ATOM   1788  CD1 LEU A1048      -6.663 -19.255 -68.219  1.00 79.80           C  
ANISOU 1788  CD1 LEU A1048     8828   6864  14631    -33   -523   -482       C  
ATOM   1789  CD2 LEU A1048      -5.128 -17.965 -66.710  1.00 54.55           C  
ANISOU 1789  CD2 LEU A1048     5813   3311  11601   -257   -742   -878       C  
ATOM   1790  N   GLU A1049      -8.997 -15.893 -63.558  1.00 63.24           N  
ANISOU 1790  N   GLU A1049     7334   3853  12843    394   -104  -2147       N  
ATOM   1791  CA  GLU A1049     -10.235 -15.241 -63.151  1.00 66.80           C  
ANISOU 1791  CA  GLU A1049     7751   4179  13450    618    149  -2384       C  
ATOM   1792  C   GLU A1049     -10.321 -13.800 -63.638  1.00 81.81           C  
ANISOU 1792  C   GLU A1049     9588   5746  15752    672     32  -2297       C  
ATOM   1793  O   GLU A1049     -11.429 -13.272 -63.781  1.00 81.00           O  
ANISOU 1793  O   GLU A1049     9332   5526  15919    882    173  -2321       O  
ATOM   1794  CB  GLU A1049     -10.367 -15.306 -61.627  1.00 87.59           C  
ANISOU 1794  CB  GLU A1049    10665   6840  15773    603    373  -2944       C  
ATOM   1795  CG  GLU A1049     -11.702 -14.840 -61.072  1.00124.50           C  
ANISOU 1795  CG  GLU A1049    15288  11462  20555    836    739  -3245       C  
ATOM   1796  CD  GLU A1049     -11.942 -15.336 -59.659  1.00138.91           C  
ANISOU 1796  CD  GLU A1049    17389  13467  21922    792   1059  -3754       C  
ATOM   1797  OE1 GLU A1049     -12.022 -16.568 -59.468  1.00130.09           O  
ANISOU 1797  OE1 GLU A1049    16288  12640  20499    730   1177  -3723       O  
ATOM   1798  OE2 GLU A1049     -12.038 -14.496 -58.740  1.00146.12           O  
ANISOU 1798  OE2 GLU A1049    18532  14236  22752    798   1198  -4190       O  
ATOM   1799  N   ASP A1050      -9.188 -13.160 -63.911  1.00 96.04           N  
ANISOU 1799  N   ASP A1050    11476   7382  17634    478   -229  -2181       N  
ATOM   1800  CA  ASP A1050      -9.149 -11.781 -64.381  1.00 96.94           C  
ANISOU 1800  CA  ASP A1050    11551   7142  18138    492   -361  -2075       C  
ATOM   1801  C   ASP A1050      -8.448 -11.678 -65.731  1.00 77.79           C  
ANISOU 1801  C   ASP A1050     8982   4714  15859    339   -607  -1541       C  
ATOM   1802  O   ASP A1050      -7.645 -10.773 -65.967  1.00 75.41           O  
ANISOU 1802  O   ASP A1050     8734   4181  15738    182   -785  -1446       O  
ATOM   1803  CB  ASP A1050      -8.474 -10.878 -63.351  1.00112.44           C  
ANISOU 1803  CB  ASP A1050    13784   8851  20086    373   -414  -2483       C  
ATOM   1804  CG  ASP A1050      -9.243 -10.808 -62.046  1.00136.75           C  
ANISOU 1804  CG  ASP A1050    17049  11907  23002    519   -130  -3044       C  
ATOM   1805  OD1 ASP A1050     -10.490 -10.770 -62.095  1.00150.64           O  
ANISOU 1805  OD1 ASP A1050    18652  13663  24922    775    110  -3096       O  
ATOM   1806  OD2 ASP A1050      -8.604 -10.797 -60.973  1.00131.45           O  
ANISOU 1806  OD2 ASP A1050    16678  11239  22028    361   -148  -3434       O  
ATOM   1807  N   LYS A1051      -8.749 -12.603 -66.639  1.00 76.97           N  
ANISOU 1807  N   LYS A1051     8709   4868  15668    366   -602  -1193       N  
ATOM   1808  CA  LYS A1051      -8.129 -12.637 -67.954  1.00 67.52           C  
ANISOU 1808  CA  LYS A1051     7408   3717  14530    206   -783   -699       C  
ATOM   1809  C   LYS A1051      -9.184 -12.520 -69.046  1.00 68.92           C  
ANISOU 1809  C   LYS A1051     7413   3876  14898    347   -823   -347       C  
ATOM   1810  O   LYS A1051     -10.357 -12.848 -68.848  1.00 74.23           O  
ANISOU 1810  O   LYS A1051     7983   4616  15604    560   -702   -452       O  
ATOM   1811  CB  LYS A1051      -7.310 -13.919 -68.150  1.00 64.44           C  
ANISOU 1811  CB  LYS A1051     7007   3659  13819     49   -779   -588       C  
ATOM   1812  CG  LYS A1051      -5.814 -13.678 -68.236  1.00 63.36           C  
ANISOU 1812  CG  LYS A1051     6908   3500  13666   -229   -917   -507       C  
ATOM   1813  CD  LYS A1051      -5.341 -12.796 -67.093  1.00 74.51           C  
ANISOU 1813  CD  LYS A1051     8481   4677  15151   -290   -981   -882       C  
ATOM   1814  CE  LYS A1051      -3.862 -12.478 -67.211  1.00 87.75           C  
ANISOU 1814  CE  LYS A1051    10145   6328  16868   -583  -1148   -778       C  
ATOM   1815  NZ  LYS A1051      -3.509 -11.904 -68.539  1.00 90.41           N  
ANISOU 1815  NZ  LYS A1051    10358   6582  17411   -712  -1205   -314       N  
ATOM   1816  N   SER A1052      -8.745 -12.050 -70.208  1.00 80.33           N  
ANISOU 1816  N   SER A1052     8824   5237  16463    200  -1006     88       N  
ATOM   1817  CA  SER A1052      -9.604 -11.830 -71.359  1.00 76.88           C  
ANISOU 1817  CA  SER A1052     8266   4757  16190    274  -1136    491       C  
ATOM   1818  C   SER A1052      -9.737 -13.102 -72.183  1.00 70.58           C  
ANISOU 1818  C   SER A1052     7409   4306  15104    224  -1128    760       C  
ATOM   1819  O   SER A1052      -8.901 -14.006 -72.094  1.00 62.97           O  
ANISOU 1819  O   SER A1052     6497   3570  13858     85  -1037    719       O  
ATOM   1820  CB  SER A1052      -9.036 -10.705 -72.224  1.00 74.22           C  
ANISOU 1820  CB  SER A1052     7976   4157  16066    101  -1344    860       C  
ATOM   1821  OG  SER A1052      -8.883  -9.512 -71.476  1.00108.71           O  
ANISOU 1821  OG  SER A1052    12409   8164  20732    138  -1366    604       O  
ATOM   1822  N   PRO A1053     -10.795 -13.213 -72.992  1.00 84.65           N  
ANISOU 1822  N   PRO A1053     9074   6121  16969    332  -1241   1030       N  
ATOM   1823  CA  PRO A1053     -10.906 -14.382 -73.878  1.00 83.84           C  
ANISOU 1823  CA  PRO A1053     8951   6322  16584    257  -1274   1308       C  
ATOM   1824  C   PRO A1053      -9.813 -14.441 -74.929  1.00 81.74           C  
ANISOU 1824  C   PRO A1053     8814   6126  16116    -44  -1356   1702       C  
ATOM   1825  O   PRO A1053      -9.440 -15.541 -75.354  1.00103.37           O  
ANISOU 1825  O   PRO A1053    11590   9128  18560   -165  -1278   1797       O  
ATOM   1826  CB  PRO A1053     -12.294 -14.211 -74.515  1.00 90.93           C  
ANISOU 1826  CB  PRO A1053     9696   7183  17672    413  -1456   1527       C  
ATOM   1827  CG  PRO A1053     -13.038 -13.322 -73.574  1.00 90.57           C  
ANISOU 1827  CG  PRO A1053     9538   6883  17992    635  -1385   1200       C  
ATOM   1828  CD  PRO A1053     -12.011 -12.385 -73.021  1.00 88.76           C  
ANISOU 1828  CD  PRO A1053     9459   6413  17855    540  -1342   1042       C  
ATOM   1829  N   ASP A1054      -9.292 -13.295 -75.366  1.00 73.36           N  
ANISOU 1829  N   ASP A1054     7827   4838  15208   -189  -1481   1934       N  
ATOM   1830  CA  ASP A1054      -8.171 -13.276 -76.296  1.00 92.26           C  
ANISOU 1830  CA  ASP A1054    10342   7324  17387   -523  -1484   2295       C  
ATOM   1831  C   ASP A1054      -6.828 -13.464 -75.604  1.00 81.28           C  
ANISOU 1831  C   ASP A1054     8968   5994  15921   -683  -1283   2030       C  
ATOM   1832  O   ASP A1054      -5.793 -13.429 -76.279  1.00 96.65           O  
ANISOU 1832  O   ASP A1054    10962   8041  17720   -981  -1219   2277       O  
ATOM   1833  CB  ASP A1054      -8.161 -11.968 -77.093  1.00114.49           C  
ANISOU 1833  CB  ASP A1054    13231   9883  20386   -644  -1701   2694       C  
ATOM   1834  CG  ASP A1054      -8.234 -10.742 -76.205  1.00123.71           C  
ANISOU 1834  CG  ASP A1054    14363  10665  21976   -504  -1752   2429       C  
ATOM   1835  OD1 ASP A1054      -9.162 -10.666 -75.374  1.00131.12           O  
ANISOU 1835  OD1 ASP A1054    15193  11493  23132   -213  -1738   2090       O  
ATOM   1836  OD2 ASP A1054      -7.362  -9.858 -76.334  1.00125.74           O  
ANISOU 1836  OD2 ASP A1054    14701  10733  22344   -704  -1782   2552       O  
ATOM   1837  N   SER A1055      -6.817 -13.654 -74.289  1.00 64.62           N  
ANISOU 1837  N   SER A1055     6813   3850  13890   -516  -1184   1542       N  
ATOM   1838  CA  SER A1055      -5.569 -13.918 -73.592  1.00 63.21           C  
ANISOU 1838  CA  SER A1055     6633   3753  13630   -669  -1064   1294       C  
ATOM   1839  C   SER A1055      -5.028 -15.286 -74.000  1.00 75.31           C  
ANISOU 1839  C   SER A1055     8112   5638  14865   -798   -912   1353       C  
ATOM   1840  O   SER A1055      -5.805 -16.221 -74.222  1.00 80.39           O  
ANISOU 1840  O   SER A1055     8741   6442  15364   -677   -872   1365       O  
ATOM   1841  CB  SER A1055      -5.773 -13.863 -72.078  1.00 62.51           C  
ANISOU 1841  CB  SER A1055     6562   3571  13619   -480  -1028    777       C  
ATOM   1842  OG  SER A1055      -4.568 -14.140 -71.387  1.00 87.63           O  
ANISOU 1842  OG  SER A1055     9744   6839  16713   -639   -990    560       O  
ATOM   1843  N   PRO A1056      -3.707 -15.432 -74.118  1.00 84.29           N  
ANISOU 1843  N   PRO A1056     9190   6900  15935  -1048   -817   1379       N  
ATOM   1844  CA  PRO A1056      -3.152 -16.726 -74.548  1.00 68.15           C  
ANISOU 1844  CA  PRO A1056     7048   5238  13607  -1155   -629   1393       C  
ATOM   1845  C   PRO A1056      -3.442 -17.861 -73.584  1.00 53.66           C  
ANISOU 1845  C   PRO A1056     5185   3621  11582   -925   -579   1005       C  
ATOM   1846  O   PRO A1056      -3.562 -19.014 -74.017  1.00 74.05           O  
ANISOU 1846  O   PRO A1056     7740   6554  13844   -878   -451    997       O  
ATOM   1847  CB  PRO A1056      -1.646 -16.442 -74.648  1.00 65.74           C  
ANISOU 1847  CB  PRO A1056     6615   4977  13388  -1435   -541   1436       C  
ATOM   1848  CG  PRO A1056      -1.547 -14.956 -74.789  1.00 63.34           C  
ANISOU 1848  CG  PRO A1056     6405   4368  13293  -1524   -681   1610       C  
ATOM   1849  CD  PRO A1056      -2.668 -14.400 -73.978  1.00 63.19           C  
ANISOU 1849  CD  PRO A1056     6506   4066  13436  -1241   -864   1406       C  
ATOM   1850  N   GLU A1057      -3.560 -17.573 -72.287  1.00 53.43           N  
ANISOU 1850  N   GLU A1057     5191   3386  11724   -802   -677    682       N  
ATOM   1851  CA  GLU A1057      -3.859 -18.629 -71.325  1.00 50.60           C  
ANISOU 1851  CA  GLU A1057     4848   3234  11143   -622   -636    363       C  
ATOM   1852  C   GLU A1057      -5.304 -19.093 -71.444  1.00 56.29           C  
ANISOU 1852  C   GLU A1057     5623   4033  11731   -395   -590    360       C  
ATOM   1853  O   GLU A1057      -5.584 -20.294 -71.352  1.00 71.73           O  
ANISOU 1853  O   GLU A1057     7562   6276  13416   -309   -504    280       O  
ATOM   1854  CB  GLU A1057      -3.566 -18.144 -69.909  1.00 51.70           C  
ANISOU 1854  CB  GLU A1057     5062   3161  11421   -604   -750     23       C  
ATOM   1855  CG  GLU A1057      -2.146 -18.390 -69.445  1.00 83.06           C  
ANISOU 1855  CG  GLU A1057     8936   7220  15404   -788   -830    -70       C  
ATOM   1856  CD  GLU A1057      -1.737 -17.437 -68.347  1.00 86.08           C  
ANISOU 1856  CD  GLU A1057     9422   7337  15946   -858  -1012   -327       C  
ATOM   1857  OE1 GLU A1057      -1.952 -16.220 -68.521  1.00 65.93           O  
ANISOU 1857  OE1 GLU A1057     6943   4543  13563   -870  -1044   -279       O  
ATOM   1858  OE2 GLU A1057      -1.218 -17.901 -67.310  1.00 85.76           O  
ANISOU 1858  OE2 GLU A1057     9414   7367  15806   -894  -1140   -570       O  
ATOM   1859  N   MET A1058      -6.237 -18.157 -71.637  1.00 52.66           N  
ANISOU 1859  N   MET A1058     5201   3291  11517   -297   -664    453       N  
ATOM   1860  CA  MET A1058      -7.628 -18.541 -71.850  1.00 67.87           C  
ANISOU 1860  CA  MET A1058     7103   5284  13402    -92   -645    486       C  
ATOM   1861  C   MET A1058      -7.779 -19.340 -73.138  1.00 60.03           C  
ANISOU 1861  C   MET A1058     6078   4596  12134   -172   -638    783       C  
ATOM   1862  O   MET A1058      -8.551 -20.305 -73.194  1.00 72.93           O  
ANISOU 1862  O   MET A1058     7679   6454  13577    -66   -592    731       O  
ATOM   1863  CB  MET A1058      -8.519 -17.301 -71.878  1.00 63.80           C  
ANISOU 1863  CB  MET A1058     6575   4369  13298     43   -757    550       C  
ATOM   1864  CG  MET A1058     -10.002 -17.603 -71.744  1.00 75.21           C  
ANISOU 1864  CG  MET A1058     7919   5863  14795    290   -724    484       C  
ATOM   1865  SD  MET A1058     -10.432 -18.193 -70.096  1.00 84.61           S  
ANISOU 1865  SD  MET A1058     9128   7148  15873    456   -489    -36       S  
ATOM   1866  CE  MET A1058     -10.044 -16.746 -69.113  1.00 77.22           C  
ANISOU 1866  CE  MET A1058     8307   5906  15127    456   -488   -331       C  
ATOM   1867  N   LYS A1059      -7.048 -18.949 -74.186  1.00 50.69           N  
ANISOU 1867  N   LYS A1059     4921   3428  10911   -389   -672   1087       N  
ATOM   1868  CA  LYS A1059      -7.033 -19.737 -75.413  1.00 50.28           C  
ANISOU 1868  CA  LYS A1059     4892   3707  10504   -512   -625   1313       C  
ATOM   1869  C   LYS A1059      -6.441 -21.118 -75.168  1.00 53.80           C  
ANISOU 1869  C   LYS A1059     5299   4488  10655   -518   -440   1070       C  
ATOM   1870  O   LYS A1059      -6.918 -22.115 -75.723  1.00 74.78           O  
ANISOU 1870  O   LYS A1059     7976   7398  13039   -498   -399   1072       O  
ATOM   1871  CB  LYS A1059      -6.246 -19.006 -76.499  1.00 53.28           C  
ANISOU 1871  CB  LYS A1059     5331   4058  10853   -787   -632   1670       C  
ATOM   1872  CG  LYS A1059      -6.905 -17.738 -77.008  1.00 56.82           C  
ANISOU 1872  CG  LYS A1059     5847   4169  11575   -804   -870   2024       C  
ATOM   1873  CD  LYS A1059      -5.997 -17.007 -77.984  1.00 79.89           C  
ANISOU 1873  CD  LYS A1059     8852   7057  14447  -1133   -853   2409       C  
ATOM   1874  CE  LYS A1059      -6.744 -15.905 -78.714  1.00 90.73           C  
ANISOU 1874  CE  LYS A1059    10328   8117  16026  -1172  -1145   2869       C  
ATOM   1875  NZ  LYS A1059      -7.837 -16.457 -79.563  1.00 93.56           N  
ANISOU 1875  NZ  LYS A1059    10756   8698  16093  -1111  -1311   3073       N  
ATOM   1876  N   ASP A1060      -5.399 -21.195 -74.337  1.00 65.37           N  
ANISOU 1876  N   ASP A1060     6703   5927  12205   -551   -363    861       N  
ATOM   1877  CA  ASP A1060      -4.803 -22.487 -74.014  1.00 71.07           C  
ANISOU 1877  CA  ASP A1060     7361   6903  12741   -526   -236    649       C  
ATOM   1878  C   ASP A1060      -5.762 -23.348 -73.201  1.00 47.42           C  
ANISOU 1878  C   ASP A1060     4399   3962   9656   -324   -261    447       C  
ATOM   1879  O   ASP A1060      -5.814 -24.570 -73.381  1.00 56.52           O  
ANISOU 1879  O   ASP A1060     5538   5324  10611   -291   -184    371       O  
ATOM   1880  CB  ASP A1060      -3.489 -22.282 -73.262  1.00 48.04           C  
ANISOU 1880  CB  ASP A1060     4339   3915   9998   -609   -232    514       C  
ATOM   1881  CG  ASP A1060      -2.805 -23.588 -72.923  1.00 61.41           C  
ANISOU 1881  CG  ASP A1060     5928   5819  11586   -563   -152    333       C  
ATOM   1882  OD1 ASP A1060      -2.684 -24.445 -73.823  1.00 84.69           O  
ANISOU 1882  OD1 ASP A1060     8837   8983  14357   -585      5    368       O  
ATOM   1883  OD2 ASP A1060      -2.381 -23.757 -71.761  1.00 81.98           O  
ANISOU 1883  OD2 ASP A1060     8503   8357  14287   -510   -263    153       O  
ATOM   1884  N   PHE A1061      -6.529 -22.727 -72.303  1.00 56.72           N  
ANISOU 1884  N   PHE A1061     5618   4937  10995   -198   -341    347       N  
ATOM   1885  CA  PHE A1061      -7.528 -23.466 -71.536  1.00 48.04           C  
ANISOU 1885  CA  PHE A1061     4540   3903   9810    -38   -311    180       C  
ATOM   1886  C   PHE A1061      -8.608 -24.030 -72.452  1.00 52.99           C  
ANISOU 1886  C   PHE A1061     5135   4664  10334      2   -314    324       C  
ATOM   1887  O   PHE A1061      -8.974 -25.207 -72.350  1.00 61.33           O  
ANISOU 1887  O   PHE A1061     6184   5895  11221     33   -261    245       O  
ATOM   1888  CB  PHE A1061      -8.135 -22.551 -70.471  1.00 42.44           C  
ANISOU 1888  CB  PHE A1061     3871   2954   9302     77   -328     13       C  
ATOM   1889  CG  PHE A1061      -9.104 -23.239 -69.551  1.00 41.75           C  
ANISOU 1889  CG  PHE A1061     3799   2951   9112    208   -226   -174       C  
ATOM   1890  CD1 PHE A1061      -8.651 -23.916 -68.431  1.00 45.25           C  
ANISOU 1890  CD1 PHE A1061     4340   3495   9358    187   -184   -367       C  
ATOM   1891  CD2 PHE A1061     -10.468 -23.195 -69.795  1.00 42.40           C  
ANISOU 1891  CD2 PHE A1061     3786   3015   9311    332   -183   -129       C  
ATOM   1892  CE1 PHE A1061      -9.539 -24.545 -67.577  1.00 41.04           C  
ANISOU 1892  CE1 PHE A1061     3847   3056   8690    261    -58   -501       C  
ATOM   1893  CE2 PHE A1061     -11.362 -23.823 -68.945  1.00 42.33           C  
ANISOU 1893  CE2 PHE A1061     3757   3099   9228    420    -37   -292       C  
ATOM   1894  CZ  PHE A1061     -10.895 -24.498 -67.833  1.00 41.65           C  
ANISOU 1894  CZ  PHE A1061     3808   3127   8892    371     49   -473       C  
ATOM   1895  N   ARG A1062      -9.124 -23.199 -73.361  1.00 44.62           N  
ANISOU 1895  N   ARG A1062     4060   3503   9389    -20   -418    556       N  
ATOM   1896  CA  ARG A1062     -10.144 -23.653 -74.302  1.00 47.38           C  
ANISOU 1896  CA  ARG A1062     4382   3982   9640    -15   -504    722       C  
ATOM   1897  C   ARG A1062      -9.599 -24.736 -75.225  1.00 60.35           C  
ANISOU 1897  C   ARG A1062     6090   5906  10933   -163   -446    753       C  
ATOM   1898  O   ARG A1062     -10.245 -25.769 -75.439  1.00 60.27           O  
ANISOU 1898  O   ARG A1062     6072   6054  10775   -149   -453    693       O  
ATOM   1899  CB  ARG A1062     -10.661 -22.467 -75.119  1.00 56.17           C  
ANISOU 1899  CB  ARG A1062     5483   4908  10949    -30   -698   1024       C  
ATOM   1900  CG  ARG A1062     -12.006 -21.913 -74.673  1.00 57.63           C  
ANISOU 1900  CG  ARG A1062     5522   4882  11492    178   -804   1020       C  
ATOM   1901  CD  ARG A1062     -12.013 -21.540 -73.201  1.00 52.48           C  
ANISOU 1901  CD  ARG A1062     4830   4041  11070    336   -640    696       C  
ATOM   1902  NE  ARG A1062     -12.750 -20.302 -72.960  1.00 85.76           N  
ANISOU 1902  NE  ARG A1062     8938   7898  15747    503   -725    722       N  
ATOM   1903  CZ  ARG A1062     -13.237 -19.940 -71.778  1.00 79.03           C  
ANISOU 1903  CZ  ARG A1062     8017   6872  15140    685   -567    412       C  
ATOM   1904  NH1 ARG A1062     -13.082 -20.728 -70.723  1.00 77.27           N  
ANISOU 1904  NH1 ARG A1062     7850   6832  14678    689   -341    102       N  
ATOM   1905  NH2 ARG A1062     -13.890 -18.792 -71.653  1.00 77.65           N  
ANISOU 1905  NH2 ARG A1062     7754   6455  15293    798   -615    396       N  
ATOM   1906  N   HIS A1063      -8.408 -24.513 -75.788  1.00 57.72           N  
ANISOU 1906  N   HIS A1063     5812   5627  10490   -318   -366    824       N  
ATOM   1907  CA  HIS A1063      -7.833 -25.487 -76.709  1.00 62.87           C  
ANISOU 1907  CA  HIS A1063     6522   6542  10824   -452   -242    798       C  
ATOM   1908  C   HIS A1063      -7.489 -26.793 -76.005  1.00 66.30           C  
ANISOU 1908  C   HIS A1063     6908   7065  11220   -364   -118    509       C  
ATOM   1909  O   HIS A1063      -7.553 -27.862 -76.621  1.00 52.15           O  
ANISOU 1909  O   HIS A1063     5159   5440   9215   -404    -53    418       O  
ATOM   1910  CB  HIS A1063      -6.592 -24.903 -77.385  1.00 61.48           C  
ANISOU 1910  CB  HIS A1063     6367   6407  10587   -642   -112    922       C  
ATOM   1911  CG  HIS A1063      -5.964 -25.816 -78.393  1.00 80.44           C  
ANISOU 1911  CG  HIS A1063     8820   9085  12657   -784     93    854       C  
ATOM   1912  ND1 HIS A1063      -6.618 -26.229 -79.534  1.00 73.87           N  
ANISOU 1912  ND1 HIS A1063     8149   8445  11474   -895     50    944       N  
ATOM   1913  CD2 HIS A1063      -4.740 -26.392 -78.432  1.00 81.58           C  
ANISOU 1913  CD2 HIS A1063     8870   9341  12785   -830    349    673       C  
ATOM   1914  CE1 HIS A1063      -5.824 -27.022 -80.231  1.00 79.02           C  
ANISOU 1914  CE1 HIS A1063     8839   9318  11867  -1008    311    784       C  
ATOM   1915  NE2 HIS A1063      -4.679 -27.137 -79.584  1.00 81.69           N  
ANISOU 1915  NE2 HIS A1063     8996   9603  12439   -954    513    619       N  
ATOM   1916  N   GLY A1064      -7.128 -26.729 -74.721  1.00 58.86           N  
ANISOU 1916  N   GLY A1064     5899   5992  10474   -256   -109    364       N  
ATOM   1917  CA  GLY A1064      -6.831 -27.949 -73.989  1.00 38.96           C  
ANISOU 1917  CA  GLY A1064     3349   3520   7933   -178    -52    158       C  
ATOM   1918  C   GLY A1064      -8.036 -28.860 -73.861  1.00 49.42           C  
ANISOU 1918  C   GLY A1064     4709   4891   9176   -112    -94    110       C  
ATOM   1919  O   GLY A1064      -7.921 -30.081 -73.995  1.00 56.28           O  
ANISOU 1919  O   GLY A1064     5590   5833   9961   -111    -47      0       O  
ATOM   1920  N   PHE A1065      -9.210 -28.279 -73.605  1.00 49.37           N  
ANISOU 1920  N   PHE A1065     4693   4816   9251    -58   -180    187       N  
ATOM   1921  CA  PHE A1065     -10.427 -29.080 -73.541  1.00 37.03           C  
ANISOU 1921  CA  PHE A1065     3105   3303   7662    -26   -215    165       C  
ATOM   1922  C   PHE A1065     -10.888 -29.510 -74.928  1.00 42.78           C  
ANISOU 1922  C   PHE A1065     3864   4162   8230   -134   -300    253       C  
ATOM   1923  O   PHE A1065     -11.547 -30.547 -75.066  1.00 42.08           O  
ANISOU 1923  O   PHE A1065     3771   4135   8082   -163   -330    188       O  
ATOM   1924  CB  PHE A1065     -11.529 -28.306 -72.816  1.00 37.60           C  
ANISOU 1924  CB  PHE A1065     3089   3264   7934     77   -242    194       C  
ATOM   1925  CG  PHE A1065     -11.488 -28.458 -71.322  1.00 38.39           C  
ANISOU 1925  CG  PHE A1065     3208   3306   8074    151   -126     36       C  
ATOM   1926  CD1 PHE A1065     -11.996 -29.596 -70.722  1.00 59.84           C  
ANISOU 1926  CD1 PHE A1065     5927   6092  10719    139    -59    -29       C  
ATOM   1927  CD2 PHE A1065     -10.940 -27.470 -70.518  1.00 59.64           C  
ANISOU 1927  CD2 PHE A1065     5945   5870  10846    197    -95    -40       C  
ATOM   1928  CE1 PHE A1065     -11.963 -29.750 -69.349  1.00 59.81           C  
ANISOU 1928  CE1 PHE A1065     5991   6065  10668    164     47   -135       C  
ATOM   1929  CE2 PHE A1065     -10.903 -27.621 -69.140  1.00 58.76           C  
ANISOU 1929  CE2 PHE A1065     5909   5739  10677    228     -3   -197       C  
ATOM   1930  CZ  PHE A1065     -11.416 -28.762 -68.558  1.00 60.53           C  
ANISOU 1930  CZ  PHE A1065     6157   6068  10775    207     74   -228       C  
ATOM   1931  N   ASP A1066     -10.557 -28.731 -75.960  1.00 40.75           N  
ANISOU 1931  N   ASP A1066     3661   3946   7877   -227   -352    408       N  
ATOM   1932  CA  ASP A1066     -10.791 -29.177 -77.330  1.00 47.53           C  
ANISOU 1932  CA  ASP A1066     4622   4974   8463   -379   -429    473       C  
ATOM   1933  C   ASP A1066      -9.999 -30.444 -77.626  1.00 57.22           C  
ANISOU 1933  C   ASP A1066     5930   6314   9499   -437   -259    237       C  
ATOM   1934  O   ASP A1066     -10.523 -31.399 -78.212  1.00 73.89           O  
ANISOU 1934  O   ASP A1066     8110   8514  11450   -512   -313    138       O  
ATOM   1935  CB  ASP A1066     -10.417 -28.068 -78.314  1.00 58.08           C  
ANISOU 1935  CB  ASP A1066     6047   6344   9675   -505   -488    719       C  
ATOM   1936  CG  ASP A1066     -11.367 -26.888 -78.256  1.00 83.62           C  
ANISOU 1936  CG  ASP A1066     9205   9421  13147   -443   -725    981       C  
ATOM   1937  OD1 ASP A1066     -12.582 -27.105 -78.062  1.00 84.41           O  
ANISOU 1937  OD1 ASP A1066     9191   9487  13392   -362   -890    998       O  
ATOM   1938  OD2 ASP A1066     -10.897 -25.740 -78.406  1.00 94.35           O  
ANISOU 1938  OD2 ASP A1066    10589  10663  14597   -475   -747   1171       O  
ATOM   1939  N   ILE A1067      -8.726 -30.468 -77.224  1.00 43.83           N  
ANISOU 1939  N   ILE A1067     4202   4587   7864   -399    -67    127       N  
ATOM   1940  CA  ILE A1067      -7.900 -31.656 -77.416  1.00 57.60           C  
ANISOU 1940  CA  ILE A1067     5960   6380   9543   -402    108   -117       C  
ATOM   1941  C   ILE A1067      -8.443 -32.819 -76.596  1.00 60.15           C  
ANISOU 1941  C   ILE A1067     6256   6597  10001   -302     48   -259       C  
ATOM   1942  O   ILE A1067      -8.467 -33.967 -77.057  1.00 61.34           O  
ANISOU 1942  O   ILE A1067     6468   6761  10077   -333     90   -441       O  
ATOM   1943  CB  ILE A1067      -6.432 -31.346 -77.066  1.00 49.84           C  
ANISOU 1943  CB  ILE A1067     4866   5363   8706   -365    286   -171       C  
ATOM   1944  CG1 ILE A1067      -5.838 -30.373 -78.087  1.00 50.19           C  
ANISOU 1944  CG1 ILE A1067     4947   5536   8588   -528    403    -29       C  
ATOM   1945  CG2 ILE A1067      -5.609 -32.623 -76.990  1.00 47.97           C  
ANISOU 1945  CG2 ILE A1067     4565   5103   8558   -294    441   -434       C  
ATOM   1946  CD1 ILE A1067      -4.377 -30.061 -77.857  1.00 77.94           C  
ANISOU 1946  CD1 ILE A1067     8294   9032  12287   -533    599    -78       C  
ATOM   1947  N   LEU A1068      -8.901 -32.540 -75.372  1.00 54.68           N  
ANISOU 1947  N   LEU A1068     5492   5785   9498   -201    -37   -183       N  
ATOM   1948  CA  LEU A1068      -9.433 -33.601 -74.523  1.00 46.81           C  
ANISOU 1948  CA  LEU A1068     4488   4694   8605   -149    -77   -258       C  
ATOM   1949  C   LEU A1068     -10.684 -34.222 -75.132  1.00 44.65           C  
ANISOU 1949  C   LEU A1068     4245   4464   8256   -242   -179   -259       C  
ATOM   1950  O   LEU A1068     -10.863 -35.445 -75.087  1.00 72.44           O  
ANISOU 1950  O   LEU A1068     7799   7916  11808   -270   -187   -378       O  
ATOM   1951  CB  LEU A1068      -9.732 -33.055 -73.126  1.00 43.59           C  
ANISOU 1951  CB  LEU A1068     4034   4201   8329    -66   -105   -176       C  
ATOM   1952  CG  LEU A1068     -10.266 -34.064 -72.108  1.00 47.44           C  
ANISOU 1952  CG  LEU A1068     4539   4609   8878    -52   -118   -194       C  
ATOM   1953  CD1 LEU A1068      -9.258 -35.181 -71.887  1.00104.87           C  
ANISOU 1953  CD1 LEU A1068    11851  11785  16211    -21   -117   -285       C  
ATOM   1954  CD2 LEU A1068     -10.608 -33.377 -70.792  1.00 42.43           C  
ANISOU 1954  CD2 LEU A1068     3901   3946   8273     -4    -93   -135       C  
ATOM   1955  N   VAL A1069     -11.560 -33.396 -75.707  1.00 55.85           N  
ANISOU 1955  N   VAL A1069     5637   5965   9617   -298   -295   -114       N  
ATOM   1956  CA  VAL A1069     -12.761 -33.917 -76.354  1.00 55.28           C  
ANISOU 1956  CA  VAL A1069     5558   5947   9500   -409   -459    -96       C  
ATOM   1957  C   VAL A1069     -12.392 -34.740 -77.583  1.00 68.59           C  
ANISOU 1957  C   VAL A1069     7410   7721  10932   -547   -468   -260       C  
ATOM   1958  O   VAL A1069     -13.007 -35.776 -77.861  1.00 62.71           O  
ANISOU 1958  O   VAL A1069     6700   6952  10175   -644   -559   -379       O  
ATOM   1959  CB  VAL A1069     -13.717 -32.760 -76.703  1.00 51.98           C  
ANISOU 1959  CB  VAL A1069     5037   5576   9137   -417   -636    130       C  
ATOM   1960  CG1 VAL A1069     -14.838 -33.239 -77.608  1.00 43.42           C  
ANISOU 1960  CG1 VAL A1069     3935   4575   7988   -566   -882    171       C  
ATOM   1961  CG2 VAL A1069     -14.286 -32.149 -75.433  1.00 40.08           C  
ANISOU 1961  CG2 VAL A1069     3348   3957   7922   -272   -578    201       C  
ATOM   1962  N   GLY A1070     -11.377 -34.300 -78.330  1.00 48.90           N  
ANISOU 1962  N   GLY A1070     5024   5327   8230   -579   -349   -293       N  
ATOM   1963  CA  GLY A1070     -10.929 -35.075 -79.476  1.00 45.18           C  
ANISOU 1963  CA  GLY A1070     4731   4960   7475   -711   -271   -515       C  
ATOM   1964  C   GLY A1070     -10.373 -36.429 -79.082  1.00 63.89           C  
ANISOU 1964  C   GLY A1070     7105   7174   9996   -638   -123   -810       C  
ATOM   1965  O   GLY A1070     -10.632 -37.435 -79.747  1.00 59.77           O  
ANISOU 1965  O   GLY A1070     6710   6640   9361   -742   -149  -1038       O  
ATOM   1966  N   GLN A1071      -9.603 -36.476 -77.991  1.00 59.01           N  
ANISOU 1966  N   GLN A1071     6358   6408   9656   -465     -3   -809       N  
ATOM   1967  CA  GLN A1071      -9.082 -37.752 -77.512  1.00 43.54           C  
ANISOU 1967  CA  GLN A1071     4380   4243   7919   -372     76  -1025       C  
ATOM   1968  C   GLN A1071     -10.192 -38.635 -76.957  1.00 62.76           C  
ANISOU 1968  C   GLN A1071     6824   6523  10499   -414   -102   -998       C  
ATOM   1969  O   GLN A1071     -10.106 -39.866 -77.049  1.00 95.06           O  
ANISOU 1969  O   GLN A1071    10973  10433  14713   -422    -96  -1203       O  
ATOM   1970  CB  GLN A1071      -8.004 -37.517 -76.454  1.00 42.07           C  
ANISOU 1970  CB  GLN A1071     4051   3945   7990   -196    165   -966       C  
ATOM   1971  CG  GLN A1071      -6.719 -36.917 -77.006  1.00 44.89           C  
ANISOU 1971  CG  GLN A1071     4340   4411   8305   -166    377  -1041       C  
ATOM   1972  CD  GLN A1071      -5.693 -36.634 -75.926  1.00 60.64           C  
ANISOU 1972  CD  GLN A1071     6156   6293  10592    -16    388   -965       C  
ATOM   1973  OE1 GLN A1071      -6.040 -36.423 -74.764  1.00 82.92           O  
ANISOU 1973  OE1 GLN A1071     8957   9024  13524     35    220   -792       O  
ATOM   1974  NE2 GLN A1071      -4.421 -36.630 -76.305  1.00 68.08           N  
ANISOU 1974  NE2 GLN A1071     6961   7253  11652     37    588  -1103       N  
ATOM   1975  N   ILE A1072     -11.234 -38.032 -76.381  1.00 56.67           N  
ANISOU 1975  N   ILE A1072     5978   5798   9756   -447   -241   -758       N  
ATOM   1976  CA  ILE A1072     -12.383 -38.812 -75.931  1.00 55.89           C  
ANISOU 1976  CA  ILE A1072     5848   5590   9800   -535   -376   -712       C  
ATOM   1977  C   ILE A1072     -13.101 -39.434 -77.123  1.00 59.86           C  
ANISOU 1977  C   ILE A1072     6444   6133  10165   -724   -516   -864       C  
ATOM   1978  O   ILE A1072     -13.547 -40.587 -77.067  1.00 49.57           O  
ANISOU 1978  O   ILE A1072     5175   4658   9000   -817   -590   -977       O  
ATOM   1979  CB  ILE A1072     -13.327 -37.935 -75.085  1.00 41.90           C  
ANISOU 1979  CB  ILE A1072     3923   3884   8112   -520   -425   -456       C  
ATOM   1980  CG1 ILE A1072     -12.716 -37.673 -73.706  1.00 43.91           C  
ANISOU 1980  CG1 ILE A1072     4147   4057   8480   -380   -305   -362       C  
ATOM   1981  CG2 ILE A1072     -14.696 -38.581 -74.949  1.00 42.74           C  
ANISOU 1981  CG2 ILE A1072     3939   3948   8353   -665   -549   -398       C  
ATOM   1982  CD1 ILE A1072     -13.580 -36.808 -72.810  1.00 66.95           C  
ANISOU 1982  CD1 ILE A1072     6940   7038  11458   -357   -277   -187       C  
ATOM   1983  N   ASP A1073     -13.212 -38.687 -78.225  1.00 73.77           N  
ANISOU 1983  N   ASP A1073     8274   8113  11642   -810   -582   -858       N  
ATOM   1984  CA  ASP A1073     -13.831 -39.232 -79.429  1.00 60.15           C  
ANISOU 1984  CA  ASP A1073     6692   6463   9697  -1025   -760  -1015       C  
ATOM   1985  C   ASP A1073     -13.030 -40.404 -79.981  1.00 51.47           C  
ANISOU 1985  C   ASP A1073     5786   5240   8530  -1051   -614  -1403       C  
ATOM   1986  O   ASP A1073     -13.606 -41.403 -80.429  1.00 81.54           O  
ANISOU 1986  O   ASP A1073     9696   8944  12344  -1209   -753  -1605       O  
ATOM   1987  CB  ASP A1073     -13.978 -38.138 -80.487  1.00 71.71           C  
ANISOU 1987  CB  ASP A1073     8240   8199  10808  -1126   -877   -882       C  
ATOM   1988  CG  ASP A1073     -15.082 -37.154 -80.158  1.00100.81           C  
ANISOU 1988  CG  ASP A1073    11715  11948  14639  -1121  -1112   -533       C  
ATOM   1989  OD1 ASP A1073     -16.091 -37.573 -79.551  1.00 89.52           O  
ANISOU 1989  OD1 ASP A1073    10100  10416  13496  -1145  -1243   -469       O  
ATOM   1990  OD2 ASP A1073     -14.944 -35.964 -80.509  1.00113.24           O  
ANISOU 1990  OD2 ASP A1073    13291  13655  16080  -1095  -1154   -322       O  
ATOM   1991  N   ASP A1074     -11.699 -40.299 -79.960  1.00 61.87           N  
ANISOU 1991  N   ASP A1074     7132   6546   9830   -897   -332  -1533       N  
ATOM   1992  CA  ASP A1074     -10.863 -41.410 -80.403  1.00 73.99           C  
ANISOU 1992  CA  ASP A1074     8789   7919  11403   -865   -141  -1937       C  
ATOM   1993  C   ASP A1074     -11.019 -42.616 -79.486  1.00 60.69           C  
ANISOU 1993  C   ASP A1074     7038   5861  10159   -788   -204  -2000       C  
ATOM   1994  O   ASP A1074     -11.074 -43.759 -79.955  1.00 65.66           O  
ANISOU 1994  O   ASP A1074     7798   6286  10864   -858   -215  -2323       O  
ATOM   1995  CB  ASP A1074      -9.399 -40.973 -80.471  1.00 68.57           C  
ANISOU 1995  CB  ASP A1074     8048   7296  10709   -697    187  -2029       C  
ATOM   1996  CG  ASP A1074      -9.140 -39.960 -81.569  1.00 85.89           C  
ANISOU 1996  CG  ASP A1074    10362   9841  12429   -831    299  -2002       C  
ATOM   1997  OD1 ASP A1074     -10.086 -39.627 -82.313  1.00 96.53           O  
ANISOU 1997  OD1 ASP A1074    11866  11378  13435  -1045     79  -1908       O  
ATOM   1998  OD2 ASP A1074      -7.986 -39.497 -81.690  1.00111.43           O  
ANISOU 1998  OD2 ASP A1074    13526  13162  15650   -740    589  -2046       O  
ATOM   1999  N   ALA A1075     -11.092 -42.381 -78.173  1.00 50.59           N  
ANISOU 1999  N   ALA A1075     5586   4476   9162   -664   -250  -1695       N  
ATOM   2000  CA  ALA A1075     -11.288 -43.482 -77.238  1.00 51.00           C  
ANISOU 2000  CA  ALA A1075     5603   4181   9595   -631   -333  -1662       C  
ATOM   2001  C   ALA A1075     -12.657 -44.126 -77.410  1.00 58.49           C  
ANISOU 2001  C   ALA A1075     6594   5051  10577   -870   -554  -1647       C  
ATOM   2002  O   ALA A1075     -12.797 -45.341 -77.226  1.00 72.77           O  
ANISOU 2002  O   ALA A1075     8460   6531  12657   -923   -621  -1770       O  
ATOM   2003  CB  ALA A1075     -11.103 -42.992 -75.802  1.00 55.67           C  
ANISOU 2003  CB  ALA A1075     6051   4741  10361   -496   -333  -1316       C  
ATOM   2004  N   LEU A1076     -13.673 -43.335 -77.761  1.00 52.00           N  
ANISOU 2004  N   LEU A1076     5719   4497   9542  -1020   -693  -1485       N  
ATOM   2005  CA  LEU A1076     -14.987 -43.901 -78.046  1.00 54.19           C  
ANISOU 2005  CA  LEU A1076     5982   4727   9882  -1271   -936  -1480       C  
ATOM   2006  C   LEU A1076     -14.962 -44.732 -79.322  1.00 87.88           C  
ANISOU 2006  C   LEU A1076    10477   8925  13987  -1437  -1025  -1886       C  
ATOM   2007  O   LEU A1076     -15.646 -45.758 -79.414  1.00 91.70           O  
ANISOU 2007  O   LEU A1076    10999   9180  14661  -1625  -1196  -2007       O  
ATOM   2008  CB  LEU A1076     -16.027 -42.786 -78.149  1.00 58.63           C  
ANISOU 2008  CB  LEU A1076     6375   5584  10319  -1358  -1089  -1205       C  
ATOM   2009  CG  LEU A1076     -16.553 -42.228 -76.825  1.00 55.76           C  
ANISOU 2009  CG  LEU A1076     5763   5235  10189  -1275  -1023   -857       C  
ATOM   2010  CD1 LEU A1076     -17.109 -40.827 -77.011  1.00 49.74           C  
ANISOU 2010  CD1 LEU A1076     4836   4750   9312  -1238  -1090   -645       C  
ATOM   2011  CD2 LEU A1076     -17.617 -43.151 -76.255  1.00 78.46           C  
ANISOU 2011  CD2 LEU A1076     8510   7930  13372  -1465  -1122   -767       C  
ATOM   2012  N   LYS A1077     -14.185 -44.300 -80.319  1.00 86.38           N  
ANISOU 2012  N   LYS A1077    10455   8933  13433  -1397   -899  -2114       N  
ATOM   2013  CA  LYS A1077     -14.037 -45.091 -81.537  1.00 89.54           C  
ANISOU 2013  CA  LYS A1077    11125   9289  13606  -1555   -915  -2574       C  
ATOM   2014  C   LYS A1077     -13.381 -46.433 -81.239  1.00 99.55           C  
ANISOU 2014  C   LYS A1077    12461  10115  15247  -1450   -771  -2902       C  
ATOM   2015  O   LYS A1077     -13.711 -47.448 -81.864  1.00 86.14           O  
ANISOU 2015  O   LYS A1077    10944   8208  13575  -1624   -881  -3259       O  
ATOM   2016  CB  LYS A1077     -13.229 -44.310 -82.573  1.00 68.72           C  
ANISOU 2016  CB  LYS A1077     8660   6984  10468  -1537   -718  -2729       C  
ATOM   2017  CG  LYS A1077     -13.127 -44.988 -83.929  1.00 69.79           C  
ANISOU 2017  CG  LYS A1077     9131   7163  10223  -1743   -702  -3231       C  
ATOM   2018  CD  LYS A1077     -12.444 -44.084 -84.943  1.00 87.93           C  
ANISOU 2018  CD  LYS A1077    11610   9860  11938  -1786   -492  -3299       C  
ATOM   2019  CE  LYS A1077     -12.411 -44.724 -86.321  1.00118.85           C  
ANISOU 2019  CE  LYS A1077    15919  13878  15359  -2038   -461  -3818       C  
ATOM   2020  NZ  LYS A1077     -11.814 -43.817 -87.341  1.00130.71           N  
ANISOU 2020  NZ  LYS A1077    17639  15818  16206  -2144   -244  -3834       N  
ATOM   2021  N   LEU A1078     -12.449 -46.456 -80.282  1.00 92.94           N  
ANISOU 2021  N   LEU A1078    11482   9101  14731  -1169   -562  -2786       N  
ATOM   2022  CA  LEU A1078     -11.849 -47.718 -79.860  1.00 77.65           C  
ANISOU 2022  CA  LEU A1078     9565   6682  13257  -1037   -487  -3010       C  
ATOM   2023  C   LEU A1078     -12.842 -48.571 -79.081  1.00 70.99           C  
ANISOU 2023  C   LEU A1078     8678   5509  12786  -1190   -750  -2806       C  
ATOM   2024  O   LEU A1078     -12.916 -49.788 -79.285  1.00 81.50           O  
ANISOU 2024  O   LEU A1078    10130   6442  14394  -1261   -820  -3082       O  
ATOM   2025  CB  LEU A1078     -10.603 -47.453 -79.015  1.00 63.24           C  
ANISOU 2025  CB  LEU A1078     7569   4769  11688   -709   -273  -2873       C  
ATOM   2026  CG  LEU A1078      -9.288 -47.157 -79.736  1.00 64.59           C  
ANISOU 2026  CG  LEU A1078     7742   5064  11736   -521     63  -3203       C  
ATOM   2027  CD1 LEU A1078      -8.186 -46.859 -78.729  1.00 63.52           C  
ANISOU 2027  CD1 LEU A1078     7365   4832  11937   -224    176  -2982       C  
ATOM   2028  CD2 LEU A1078      -8.902 -48.327 -80.621  1.00 70.05           C  
ANISOU 2028  CD2 LEU A1078     8598   5462  12555   -516    202  -3789       C  
ATOM   2029  N   ALA A1079     -13.616 -47.948 -78.189  1.00 86.90           N  
ANISOU 2029  N   ALA A1079    10519   7680  14819  -1253   -870  -2331       N  
ATOM   2030  CA  ALA A1079     -14.509 -48.707 -77.320  1.00 72.94           C  
ANISOU 2030  CA  ALA A1079     8678   5629  13405  -1415  -1049  -2079       C  
ATOM   2031  C   ALA A1079     -15.637 -49.362 -78.108  1.00 70.27           C  
ANISOU 2031  C   ALA A1079     8418   5224  13056  -1747  -1287  -2263       C  
ATOM   2032  O   ALA A1079     -16.062 -50.476 -77.780  1.00110.85           O  
ANISOU 2032  O   ALA A1079    13611  10101  18404  -1840  -1365  -2194       O  
ATOM   2033  CB  ALA A1079     -15.073 -47.798 -76.229  1.00100.05           C  
ANISOU 2033  CB  ALA A1079    11901   9307  16805  -1410  -1040  -1578       C  
ATOM   2034  N   ASN A1080     -16.139 -48.689 -79.146  1.00 74.49           N  
ANISOU 2034  N   ASN A1080     8989   6113  13202  -1895  -1395  -2398       N  
ATOM   2035  CA  ASN A1080     -17.217 -49.260 -79.946  1.00 87.00           C  
ANISOU 2035  CA  ASN A1080    10642   7652  14761  -2244  -1698  -2582       C  
ATOM   2036  C   ASN A1080     -16.767 -50.478 -80.742  1.00 95.99           C  
ANISOU 2036  C   ASN A1080    12092   8501  15880  -2282  -1674  -3068       C  
ATOM   2037  O   ASN A1080     -17.614 -51.269 -81.169  1.00126.74           O  
ANISOU 2037  O   ASN A1080    16081  12293  19782  -2544  -1890  -3160       O  
ATOM   2038  CB  ASN A1080     -17.794 -48.205 -80.891  1.00 93.14           C  
ANISOU 2038  CB  ASN A1080    11412   8915  15064  -2376  -1867  -2553       C  
ATOM   2039  CG  ASN A1080     -18.768 -47.273 -80.198  1.00 94.43           C  
ANISOU 2039  CG  ASN A1080    11230   9328  15320  -2409  -1977  -2049       C  
ATOM   2040  OD1 ASN A1080     -18.783 -47.172 -78.971  1.00 92.40           O  
ANISOU 2040  OD1 ASN A1080    10771   8978  15358  -2280  -1816  -1734       O  
ATOM   2041  ND2 ASN A1080     -19.592 -46.588 -80.982  1.00109.25           N  
ANISOU 2041  ND2 ASN A1080    13041  11521  16948  -2583  -2255  -1978       N  
ATOM   2042  N   GLU A1081     -15.464 -50.646 -80.950  1.00 98.82           N  
ANISOU 2042  N   GLU A1081    12593   8734  16218  -2017  -1395  -3375       N  
ATOM   2043  CA  GLU A1081     -14.923 -51.804 -81.646  1.00 93.02           C  
ANISOU 2043  CA  GLU A1081    12132   7718  15493  -1982  -1297  -3837       C  
ATOM   2044  C   GLU A1081     -14.620 -52.965 -80.706  1.00 92.69           C  
ANISOU 2044  C   GLU A1081    12053   7232  15934  -1814  -1242  -3661       C  
ATOM   2045  O   GLU A1081     -14.036 -53.963 -81.142  1.00127.34           O  
ANISOU 2045  O   GLU A1081    16624  11326  20434  -1717  -1141  -4011       O  
ATOM   2046  CB  GLU A1081     -13.660 -51.410 -82.415  1.00102.96           C  
ANISOU 2046  CB  GLU A1081    13521   9108  16493  -1770   -971  -4273       C  
ATOM   2047  CG  GLU A1081     -13.898 -50.365 -83.493  1.00117.14           C  
ANISOU 2047  CG  GLU A1081    15435  11379  17694  -1977  -1011  -4476       C  
ATOM   2048  CD  GLU A1081     -12.609 -49.809 -84.063  1.00128.49           C  
ANISOU 2048  CD  GLU A1081    16956  13061  18804  -1750   -586  -4730       C  
ATOM   2049  OE1 GLU A1081     -11.532 -50.107 -83.503  1.00132.81           O  
ANISOU 2049  OE1 GLU A1081    17372  13349  19741  -1428   -291  -4806       O  
ATOM   2050  OE2 GLU A1081     -12.671 -49.073 -85.070  1.00124.75           O  
ANISOU 2050  OE2 GLU A1081    16663  13039  17696  -1909   -559  -4828       O  
ATOM   2051  N   GLY A1082     -15.001 -52.858 -79.432  1.00 80.18           N  
ANISOU 2051  N   GLY A1082    10248   5601  14618  -1786  -1308  -3126       N  
ATOM   2052  CA  GLY A1082     -14.764 -53.907 -78.464  1.00 87.72           C  
ANISOU 2052  CA  GLY A1082    11180   6168  15981  -1670  -1303  -2892       C  
ATOM   2053  C   GLY A1082     -13.374 -53.942 -77.872  1.00 99.66           C  
ANISOU 2053  C   GLY A1082    12627   7541  17696  -1280  -1104  -2845       C  
ATOM   2054  O   GLY A1082     -13.128 -54.743 -76.961  1.00131.99           O  
ANISOU 2054  O   GLY A1082    16691  11331  22127  -1181  -1152  -2583       O  
ATOM   2055  N   LYS A1083     -12.455 -53.104 -78.352  1.00 78.76           N  
ANISOU 2055  N   LYS A1083     9945   5116  14863  -1076   -901  -3073       N  
ATOM   2056  CA  LYS A1083     -11.080 -53.072 -77.857  1.00 78.17           C  
ANISOU 2056  CA  LYS A1083     9748   4952  15001   -708   -718  -3037       C  
ATOM   2057  C   LYS A1083     -11.068 -52.337 -76.519  1.00 89.39           C  
ANISOU 2057  C   LYS A1083    10981   6499  16486   -637   -782  -2483       C  
ATOM   2058  O   LYS A1083     -10.796 -51.137 -76.425  1.00 81.16           O  
ANISOU 2058  O   LYS A1083     9828   5756  15253   -571   -686  -2401       O  
ATOM   2059  CB  LYS A1083     -10.163 -52.417 -78.881  1.00 78.24           C  
ANISOU 2059  CB  LYS A1083     9767   5186  14775   -559   -439  -3480       C  
ATOM   2060  CG  LYS A1083     -10.269 -53.039 -80.267  1.00 84.94           C  
ANISOU 2060  CG  LYS A1083    10865   5982  15425   -683   -352  -4063       C  
ATOM   2061  CD  LYS A1083      -9.543 -52.216 -81.317  1.00 99.32           C  
ANISOU 2061  CD  LYS A1083    12730   8135  16872   -622    -40  -4479       C  
ATOM   2062  CE  LYS A1083      -9.768 -52.785 -82.709  1.00108.79           C  
ANISOU 2062  CE  LYS A1083    14247   9347  17741   -806     34  -5058       C  
ATOM   2063  NZ  LYS A1083      -9.125 -51.955 -83.765  1.00136.33           N  
ANISOU 2063  NZ  LYS A1083    17823  13229  20746   -807    373  -5450       N  
ATOM   2064  N   VAL A1084     -11.372 -53.089 -75.459  1.00 86.46           N  
ANISOU 2064  N   VAL A1084    10599   5881  16369   -673   -945  -2101       N  
ATOM   2065  CA  VAL A1084     -11.514 -52.497 -74.132  1.00 75.85           C  
ANISOU 2065  CA  VAL A1084     9143   4657  15018   -672  -1015  -1573       C  
ATOM   2066  C   VAL A1084     -10.166 -52.014 -73.609  1.00 74.91           C  
ANISOU 2066  C   VAL A1084     8898   4586  14980   -356   -940  -1487       C  
ATOM   2067  O   VAL A1084     -10.038 -50.879 -73.136  1.00 91.23           O  
ANISOU 2067  O   VAL A1084    10870   6924  16867   -319   -896  -1292       O  
ATOM   2068  CB  VAL A1084     -12.164 -53.505 -73.166  1.00 73.92           C  
ANISOU 2068  CB  VAL A1084     8963   4139  14983   -832  -1191  -1199       C  
ATOM   2069  CG1 VAL A1084     -12.261 -52.917 -71.767  1.00 71.22           C  
ANISOU 2069  CG1 VAL A1084     8558   3934  14568   -854  -1233   -674       C  
ATOM   2070  CG2 VAL A1084     -13.537 -53.917 -73.676  1.00 88.20           C  
ANISOU 2070  CG2 VAL A1084    10846   5935  16733  -1174  -1267  -1269       C  
ATOM   2071  N   LYS A1085      -9.144 -52.870 -73.682  1.00 73.33           N  
ANISOU 2071  N   LYS A1085     8671   4113  15079   -130   -936  -1634       N  
ATOM   2072  CA  LYS A1085      -7.835 -52.517 -73.139  1.00 72.78           C  
ANISOU 2072  CA  LYS A1085     8426   4076  15150    153   -914  -1526       C  
ATOM   2073  C   LYS A1085      -7.233 -51.321 -73.866  1.00 81.29           C  
ANISOU 2073  C   LYS A1085     9383   5491  16012    266   -677  -1792       C  
ATOM   2074  O   LYS A1085      -6.576 -50.475 -73.247  1.00 67.21           O  
ANISOU 2074  O   LYS A1085     7457   3886  14194    386   -679  -1585       O  
ATOM   2075  CB  LYS A1085      -6.891 -53.721 -73.205  1.00 78.25           C  
ANISOU 2075  CB  LYS A1085     9061   4399  16271    363   -957  -1668       C  
ATOM   2076  CG  LYS A1085      -6.758 -54.368 -74.581  1.00118.43           C  
ANISOU 2076  CG  LYS A1085    14212   9350  21437    402   -760  -2242       C  
ATOM   2077  CD  LYS A1085      -7.779 -55.481 -74.783  1.00139.81           C  
ANISOU 2077  CD  LYS A1085    17141  11751  24232    187   -892  -2294       C  
ATOM   2078  CE  LYS A1085      -8.705 -55.174 -75.949  1.00117.61           C  
ANISOU 2078  CE  LYS A1085    14501   9121  21063    -51   -773  -2664       C  
ATOM   2079  NZ  LYS A1085      -9.866 -56.105 -76.005  1.00124.92           N  
ANISOU 2079  NZ  LYS A1085    15622   9798  22045   -332   -954  -2632       N  
ATOM   2080  N   GLU A1086      -7.447 -51.230 -75.181  1.00 70.57           N  
ANISOU 2080  N   GLU A1086     8103   4223  14486    202   -480  -2251       N  
ATOM   2081  CA  GLU A1086      -6.936 -50.086 -75.929  1.00 68.30           C  
ANISOU 2081  CA  GLU A1086     7734   4260  13958    266   -231  -2499       C  
ATOM   2082  C   GLU A1086      -7.668 -48.807 -75.544  1.00 75.31           C  
ANISOU 2082  C   GLU A1086     8623   5438  14552    112   -286  -2228       C  
ATOM   2083  O   GLU A1086      -7.060 -47.733 -75.477  1.00 64.61           O  
ANISOU 2083  O   GLU A1086     7140   4309  13100    214   -167  -2188       O  
ATOM   2084  CB  GLU A1086      -7.056 -50.346 -77.430  1.00 71.27           C  
ANISOU 2084  CB  GLU A1086     8258   4672  14148    183    -16  -3061       C  
ATOM   2085  CG  GLU A1086      -6.412 -51.643 -77.886  1.00104.34           C  
ANISOU 2085  CG  GLU A1086    12466   8550  18628    327     70  -3384       C  
ATOM   2086  CD  GLU A1086      -6.578 -51.883 -79.372  1.00120.15           C  
ANISOU 2086  CD  GLU A1086    14677  10619  20355    211    296  -3971       C  
ATOM   2087  OE1 GLU A1086      -6.729 -50.894 -80.121  1.00109.71           O  
ANISOU 2087  OE1 GLU A1086    13423   9645  18615     87    464  -4162       O  
ATOM   2088  OE2 GLU A1086      -6.563 -53.059 -79.791  1.00118.94           O  
ANISOU 2088  OE2 GLU A1086    14644  10168  20379    225    297  -4245       O  
ATOM   2089  N   ALA A1087      -8.974 -48.904 -75.284  1.00 62.15           N  
ANISOU 2089  N   ALA A1087     7075   3764  12776   -142   -460  -2036       N  
ATOM   2090  CA  ALA A1087      -9.733 -47.734 -74.858  1.00 64.04           C  
ANISOU 2090  CA  ALA A1087     7277   4290  12765   -288   -507  -1752       C  
ATOM   2091  C   ALA A1087      -9.308 -47.278 -73.469  1.00 68.78           C  
ANISOU 2091  C   ALA A1087     7777   4906  13449   -167   -577  -1326       C  
ATOM   2092  O   ALA A1087      -9.260 -46.074 -73.192  1.00 61.85           O  
ANISOU 2092  O   ALA A1087     6827   4388  12283   -146   -513  -1158       O  
ATOM   2093  CB  ALA A1087     -11.230 -48.040 -74.889  1.00 58.39           C  
ANISOU 2093  CB  ALA A1087     6641   3582  11962   -593   -661  -1638       C  
ATOM   2094  N   GLN A1088      -8.997 -48.227 -72.583  1.00 57.98           N  
ANISOU 2094  N   GLN A1088     6427   3279  12324    -97   -718  -1108       N  
ATOM   2095  CA  GLN A1088      -8.525 -47.871 -71.249  1.00 75.20           C  
ANISOU 2095  CA  GLN A1088     8562   5479  14531    -13   -833   -712       C  
ATOM   2096  C   GLN A1088      -7.152 -47.214 -71.308  1.00 74.12           C  
ANISOU 2096  C   GLN A1088     8263   5450  14448    239   -765   -810       C  
ATOM   2097  O   GLN A1088      -6.866 -46.290 -70.536  1.00 69.65           O  
ANISOU 2097  O   GLN A1088     7652   5040  13774    272   -812   -582       O  
ATOM   2098  CB  GLN A1088      -8.492 -49.113 -70.361  1.00 62.72           C  
ANISOU 2098  CB  GLN A1088     7064   3595  13171    -28  -1038   -445       C  
ATOM   2099  CG  GLN A1088      -9.860 -49.724 -70.108  1.00 61.36           C  
ANISOU 2099  CG  GLN A1088     7032   3329  12953   -315  -1097   -268       C  
ATOM   2100  CD  GLN A1088      -9.778 -51.096 -69.465  1.00 65.78           C  
ANISOU 2100  CD  GLN A1088     7691   3536  13766   -338  -1283    -56       C  
ATOM   2101  OE1 GLN A1088      -9.351 -52.064 -70.095  1.00 69.13           O  
ANISOU 2101  OE1 GLN A1088     8112   3704  14451   -231  -1308   -303       O  
ATOM   2102  NE2 GLN A1088     -10.190 -51.186 -68.205  1.00 66.39           N  
ANISOU 2102  NE2 GLN A1088     7870   3588  13765   -492  -1402    406       N  
ATOM   2103  N   ALA A1089      -6.286 -47.680 -72.211  1.00 58.51           N  
ANISOU 2103  N   ALA A1089     6188   3394  12649    402   -639  -1160       N  
ATOM   2104  CA  ALA A1089      -4.988 -47.037 -72.385  1.00 67.25           C  
ANISOU 2104  CA  ALA A1089     7082   4636  13832    606   -523  -1274       C  
ATOM   2105  C   ALA A1089      -5.148 -45.621 -72.923  1.00 72.53           C  
ANISOU 2105  C   ALA A1089     7721   5616  14219    558   -332  -1377       C  
ATOM   2106  O   ALA A1089      -4.454 -44.697 -72.481  1.00 85.68           O  
ANISOU 2106  O   ALA A1089     9247   7444  15862    644   -332  -1244       O  
ATOM   2107  CB  ALA A1089      -4.106 -47.871 -73.312  1.00 73.89           C  
ANISOU 2107  CB  ALA A1089     7810   5333  14930    762   -355  -1659       C  
ATOM   2108  N   ALA A1090      -6.060 -45.432 -73.880  1.00 63.87           N  
ANISOU 2108  N   ALA A1090     6761   4670  12837    388   -198  -1577       N  
ATOM   2109  CA  ALA A1090      -6.349 -44.089 -74.369  1.00 61.58           C  
ANISOU 2109  CA  ALA A1090     6473   4830  12095    282    -65  -1548       C  
ATOM   2110  C   ALA A1090      -6.955 -43.219 -73.277  1.00 55.49           C  
ANISOU 2110  C   ALA A1090     5715   4232  11135    202   -213  -1148       C  
ATOM   2111  O   ALA A1090      -6.741 -42.001 -73.265  1.00 70.85           O  
ANISOU 2111  O   ALA A1090     7599   6457  12865    204   -144  -1061       O  
ATOM   2112  CB  ALA A1090      -7.285 -44.158 -75.576  1.00 51.75           C  
ANISOU 2112  CB  ALA A1090     5389   3735  10540     85     16  -1777       C  
ATOM   2113  N   ALA A1091      -7.711 -43.820 -72.355  1.00 63.50           N  
ANISOU 2113  N   ALA A1091     6819   5075  12232    117   -392   -913       N  
ATOM   2114  CA  ALA A1091      -8.257 -43.059 -71.236  1.00 48.96           C  
ANISOU 2114  CA  ALA A1091     5004   3400  10198     40   -472   -578       C  
ATOM   2115  C   ALA A1091      -7.150 -42.571 -70.311  1.00 48.20           C  
ANISOU 2115  C   ALA A1091     4837   3305  10174    185   -554   -427       C  
ATOM   2116  O   ALA A1091      -7.207 -41.443 -69.807  1.00 67.67           O  
ANISOU 2116  O   ALA A1091     7295   6007  12409    161   -537   -302       O  
ATOM   2117  CB  ALA A1091      -9.268 -43.905 -70.465  1.00 52.43           C  
ANISOU 2117  CB  ALA A1091     5558   3667  10696   -119   -591   -360       C  
ATOM   2118  N   GLU A1092      -6.135 -43.405 -70.076  1.00 57.31           N  
ANISOU 2118  N   GLU A1092     5923   4169  11682    337   -672   -447       N  
ATOM   2119  CA  GLU A1092      -4.992 -42.968 -69.282  1.00 79.95           C  
ANISOU 2119  CA  GLU A1092     8678   7032  14667    470   -813   -310       C  
ATOM   2120  C   GLU A1092      -4.222 -41.861 -69.990  1.00 67.93           C  
ANISOU 2120  C   GLU A1092     6974   5756  13079    544   -634   -498       C  
ATOM   2121  O   GLU A1092      -3.700 -40.945 -69.342  1.00 59.65           O  
ANISOU 2121  O   GLU A1092     5868   4849  11949    553   -720   -368       O  
ATOM   2122  CB  GLU A1092      -4.073 -44.152 -68.983  1.00 63.88           C  
ANISOU 2122  CB  GLU A1092     6553   4630  13088    629  -1007   -282       C  
ATOM   2123  CG  GLU A1092      -4.428 -44.931 -67.725  1.00 84.72           C  
ANISOU 2123  CG  GLU A1092     9375   7069  15745    542  -1304     90       C  
ATOM   2124  CD  GLU A1092      -4.136 -44.156 -66.452  1.00108.78           C  
ANISOU 2124  CD  GLU A1092    12494  10223  18614    503  -1533    408       C  
ATOM   2125  OE1 GLU A1092      -4.942 -43.273 -66.089  1.00100.67           O  
ANISOU 2125  OE1 GLU A1092    11612   9505  17132    333  -1417    480       O  
ATOM   2126  OE2 GLU A1092      -3.095 -44.425 -65.818  1.00141.08           O  
ANISOU 2126  OE2 GLU A1092    16494  14200  22911    608  -1809    554       O  
ATOM   2127  N   GLN A1093      -4.139 -41.927 -71.321  1.00 66.57           N  
ANISOU 2127  N   GLN A1093     6733   5641  12921    565   -386   -805       N  
ATOM   2128  CA  GLN A1093      -3.399 -40.912 -72.063  1.00 63.58           C  
ANISOU 2128  CA  GLN A1093     6195   5501  12463    593   -179   -952       C  
ATOM   2129  C   GLN A1093      -4.108 -39.564 -72.014  1.00 77.58           C  
ANISOU 2129  C   GLN A1093     8066   7579  13833    443   -144   -812       C  
ATOM   2130  O   GLN A1093      -3.460 -38.523 -71.853  1.00 70.68           O  
ANISOU 2130  O   GLN A1093     7080   6843  12930    449   -125   -754       O  
ATOM   2131  CB  GLN A1093      -3.195 -41.358 -73.510  1.00 71.29           C  
ANISOU 2131  CB  GLN A1093     7133   6491  13464    612    110  -1314       C  
ATOM   2132  CG  GLN A1093      -2.265 -40.455 -74.304  1.00 93.29           C  
ANISOU 2132  CG  GLN A1093     9738   9510  16198    623    375  -1455       C  
ATOM   2133  CD  GLN A1093      -2.154 -40.863 -75.758  1.00 88.45           C  
ANISOU 2133  CD  GLN A1093     9155   8971  15481    592    710  -1827       C  
ATOM   2134  OE1 GLN A1093      -3.110 -40.740 -76.524  1.00 66.57           O  
ANISOU 2134  OE1 GLN A1093     6619   6361  12316    420    769  -1888       O  
ATOM   2135  NE2 GLN A1093      -0.983 -41.354 -76.147  1.00 91.53           N  
ANISOU 2135  NE2 GLN A1093     9301   9248  16227    752    931  -2090       N  
ATOM   2136  N   LEU A1094      -5.438 -39.559 -72.149  1.00 58.71           N  
ANISOU 2136  N   LEU A1094     5855   5265  11188    308   -148   -758       N  
ATOM   2137  CA  LEU A1094      -6.171 -38.300 -72.073  1.00 56.42           C  
ANISOU 2137  CA  LEU A1094     5620   5209  10607    202   -128   -627       C  
ATOM   2138  C   LEU A1094      -6.229 -37.772 -70.645  1.00 57.91           C  
ANISOU 2138  C   LEU A1094     5844   5392  10766    206   -277   -411       C  
ATOM   2139  O   LEU A1094      -6.382 -36.563 -70.441  1.00 71.75           O  
ANISOU 2139  O   LEU A1094     7598   7291  12373    171   -253   -347       O  
ATOM   2140  CB  LEU A1094      -7.579 -38.463 -72.655  1.00 49.58           C  
ANISOU 2140  CB  LEU A1094     4868   4418   9551     69   -110   -635       C  
ATOM   2141  CG  LEU A1094      -8.543 -39.540 -72.146  1.00 60.83           C  
ANISOU 2141  CG  LEU A1094     6381   5686  11045     -1   -213   -570       C  
ATOM   2142  CD1 LEU A1094      -9.237 -39.125 -70.859  1.00 97.43           C  
ANISOU 2142  CD1 LEU A1094    11052  10358  15610    -47   -276   -331       C  
ATOM   2143  CD2 LEU A1094      -9.571 -39.882 -73.218  1.00 75.43           C  
ANISOU 2143  CD2 LEU A1094     8281   7592  12786   -138   -199   -684       C  
ATOM   2144  N   LYS A1095      -6.117 -38.655 -69.649  1.00 46.22           N  
ANISOU 2144  N   LYS A1095     4421   3732   9409    233   -436   -297       N  
ATOM   2145  CA  LYS A1095      -5.993 -38.194 -68.270  1.00 46.09           C  
ANISOU 2145  CA  LYS A1095     4484   3733   9294    211   -588   -108       C  
ATOM   2146  C   LYS A1095      -4.710 -37.396 -68.083  1.00 52.11           C  
ANISOU 2146  C   LYS A1095     5114   4530  10154    285   -668   -133       C  
ATOM   2147  O   LYS A1095      -4.716 -36.314 -67.483  1.00 72.66           O  
ANISOU 2147  O   LYS A1095     7767   7251  12589    233   -700    -89       O  
ATOM   2148  CB  LYS A1095      -6.027 -39.382 -67.308  1.00 42.21           C  
ANISOU 2148  CB  LYS A1095     4110   3037   8891    195   -781     71       C  
ATOM   2149  CG  LYS A1095      -5.696 -39.005 -65.870  1.00 43.23           C  
ANISOU 2149  CG  LYS A1095     4368   3198   8859    148   -982    272       C  
ATOM   2150  CD  LYS A1095      -5.635 -40.221 -64.958  1.00 63.44           C  
ANISOU 2150  CD  LYS A1095     7071   5543  11492    110  -1218    517       C  
ATOM   2151  CE  LYS A1095      -5.241 -39.824 -63.542  1.00 72.15           C  
ANISOU 2151  CE  LYS A1095     8354   6714  12346     28  -1459    727       C  
ATOM   2152  NZ  LYS A1095      -5.160 -41.000 -62.631  1.00 88.52           N  
ANISOU 2152  NZ  LYS A1095    10605   8576  14451    -39  -1737   1043       N  
ATOM   2153  N   THR A1096      -3.594 -37.923 -68.592  1.00 68.86           N  
ANISOU 2153  N   THR A1096     7043   6531  12589    402   -693   -229       N  
ATOM   2154  CA  THR A1096      -2.329 -37.199 -68.524  1.00 49.95           C  
ANISOU 2154  CA  THR A1096     4443   4170  10366    455   -755   -258       C  
ATOM   2155  C   THR A1096      -2.394 -35.906 -69.326  1.00 53.20           C  
ANISOU 2155  C   THR A1096     4803   4786  10626    380   -537   -350       C  
ATOM   2156  O   THR A1096      -1.868 -34.872 -68.897  1.00 62.57           O  
ANISOU 2156  O   THR A1096     5935   6034  11805    333   -617   -308       O  
ATOM   2157  CB  THR A1096      -1.192 -38.088 -69.027  1.00 60.88           C  
ANISOU 2157  CB  THR A1096     5561   5379  12190    613   -755   -372       C  
ATOM   2158  OG1 THR A1096      -1.105 -39.265 -68.213  1.00 77.15           O  
ANISOU 2158  OG1 THR A1096     7673   7187  14452    691  -1024   -233       O  
ATOM   2159  CG2 THR A1096       0.132 -37.345 -68.974  1.00 67.16           C  
ANISOU 2159  CG2 THR A1096     6068   6219  13231    649   -808   -394       C  
ATOM   2160  N   THR A1097      -3.042 -35.943 -70.494  1.00 49.80           N  
ANISOU 2160  N   THR A1097     4406   4444  10071    345   -297   -461       N  
ATOM   2161  CA  THR A1097      -3.177 -34.737 -71.305  1.00 51.77           C  
ANISOU 2161  CA  THR A1097     4642   4870  10159    253   -128   -481       C  
ATOM   2162  C   THR A1097      -3.998 -33.677 -70.582  1.00 49.48           C  
ANISOU 2162  C   THR A1097     4498   4632   9669    180   -217   -355       C  
ATOM   2163  O   THR A1097      -3.658 -32.488 -70.611  1.00 61.45           O  
ANISOU 2163  O   THR A1097     5972   6195  11182    127   -207   -324       O  
ATOM   2164  CB  THR A1097      -3.816 -35.078 -72.652  1.00 44.53           C  
ANISOU 2164  CB  THR A1097     3789   4046   9085    202     76   -592       C  
ATOM   2165  OG1 THR A1097      -3.083 -36.136 -73.281  1.00 88.79           O  
ANISOU 2165  OG1 THR A1097     9282   9577  14876    280    201   -784       O  
ATOM   2166  CG2 THR A1097      -3.816 -33.861 -73.564  1.00 39.42           C  
ANISOU 2166  CG2 THR A1097     3138   3571   8268     89    217   -553       C  
ATOM   2167  N   ARG A1098      -5.085 -34.090 -69.927  1.00 47.96           N  
ANISOU 2167  N   ARG A1098     4466   4415   9342    172   -281   -296       N  
ATOM   2168  CA  ARG A1098      -5.907 -33.144 -69.180  1.00 42.84           C  
ANISOU 2168  CA  ARG A1098     3933   3809   8535    126   -304   -232       C  
ATOM   2169  C   ARG A1098      -5.127 -32.529 -68.025  1.00 37.05           C  
ANISOU 2169  C   ARG A1098     3229   3033   7816    118   -458   -216       C  
ATOM   2170  O   ARG A1098      -5.205 -31.317 -67.789  1.00 63.59           O  
ANISOU 2170  O   ARG A1098     6620   6407  11134     82   -449   -240       O  
ATOM   2171  CB  ARG A1098      -7.164 -33.840 -68.662  1.00 40.29           C  
ANISOU 2171  CB  ARG A1098     3733   3484   8090    101   -287   -182       C  
ATOM   2172  CG  ARG A1098      -8.055 -32.957 -67.806  1.00 44.29           C  
ANISOU 2172  CG  ARG A1098     4331   4039   8458     71   -239   -163       C  
ATOM   2173  CD  ARG A1098      -8.759 -33.766 -66.731  1.00 59.44           C  
ANISOU 2173  CD  ARG A1098     6383   5955  10247     18   -232    -94       C  
ATOM   2174  NE  ARG A1098      -7.809 -34.351 -65.788  1.00 52.47           N  
ANISOU 2174  NE  ARG A1098     5609   5006   9322      2   -414    -26       N  
ATOM   2175  CZ  ARG A1098      -8.155 -35.018 -64.691  1.00 65.23           C  
ANISOU 2175  CZ  ARG A1098     7398   6618  10768    -80   -457     89       C  
ATOM   2176  NH1 ARG A1098      -9.436 -35.185 -64.391  1.00 60.42           N  
ANISOU 2176  NH1 ARG A1098     6845   6080  10031   -159   -266    122       N  
ATOM   2177  NH2 ARG A1098      -7.221 -35.514 -63.893  1.00 80.15           N  
ANISOU 2177  NH2 ARG A1098     9393   8436  12627    -98   -699    197       N  
ATOM   2178  N   ASN A1099      -4.372 -33.351 -67.292  1.00 54.10           N  
ANISOU 2178  N   ASN A1099     5388   5116  10052    144   -637   -174       N  
ATOM   2179  CA  ASN A1099      -3.591 -32.838 -66.171  1.00 68.48           C  
ANISOU 2179  CA  ASN A1099     7255   6908  11857    106   -862   -149       C  
ATOM   2180  C   ASN A1099      -2.514 -31.871 -66.644  1.00 56.20           C  
ANISOU 2180  C   ASN A1099     5500   5347  10506     88   -886   -212       C  
ATOM   2181  O   ASN A1099      -2.266 -30.843 -66.005  1.00 73.78           O  
ANISOU 2181  O   ASN A1099     7788   7566  12678     11   -995   -247       O  
ATOM   2182  CB  ASN A1099      -2.963 -33.995 -65.392  1.00 88.27           C  
ANISOU 2182  CB  ASN A1099     9779   9315  14444    137  -1120    -33       C  
ATOM   2183  CG  ASN A1099      -3.980 -34.768 -64.577  1.00 78.36           C  
ANISOU 2183  CG  ASN A1099     8781   8060  12931     84  -1134     85       C  
ATOM   2184  OD1 ASN A1099      -5.014 -34.230 -64.184  1.00 86.43           O  
ANISOU 2184  OD1 ASN A1099     9977   9185  13677      7   -981     56       O  
ATOM   2185  ND2 ASN A1099      -3.687 -36.037 -64.313  1.00 83.18           N  
ANISOU 2185  ND2 ASN A1099     9398   8535  13670    121  -1306    226       N  
ATOM   2186  N   ALA A1100      -1.866 -32.181 -67.767  1.00 58.32           N  
ANISOU 2186  N   ALA A1100     5532   5616  11011    137   -763   -244       N  
ATOM   2187  CA  ALA A1100      -0.780 -31.332 -68.242  1.00 55.61           C  
ANISOU 2187  CA  ALA A1100     4961   5280  10889     86   -744   -277       C  
ATOM   2188  C   ALA A1100      -1.296 -30.024 -68.828  1.00 75.45           C  
ANISOU 2188  C   ALA A1100     7539   7840  13288    -11   -582   -280       C  
ATOM   2189  O   ALA A1100      -0.586 -29.012 -68.797  1.00 73.66           O  
ANISOU 2189  O   ALA A1100     7211   7577  13199   -107   -633   -276       O  
ATOM   2190  CB  ALA A1100       0.059 -32.087 -69.272  1.00 53.51           C  
ANISOU 2190  CB  ALA A1100     4415   5021  10894    157   -583   -334       C  
ATOM   2191  N   TYR A1101      -2.523 -30.016 -69.351  1.00 75.49           N  
ANISOU 2191  N   TYR A1101     7696   7897  13089      3   -425   -266       N  
ATOM   2192  CA  TYR A1101      -3.081 -28.831 -69.993  1.00 54.97           C  
ANISOU 2192  CA  TYR A1101     5146   5306  10433    -66   -315   -221       C  
ATOM   2193  C   TYR A1101      -3.817 -27.912 -69.022  1.00 49.55           C  
ANISOU 2193  C   TYR A1101     4628   4528   9670    -71   -408   -249       C  
ATOM   2194  O   TYR A1101      -3.678 -26.688 -69.110  1.00 51.61           O  
ANISOU 2194  O   TYR A1101     4887   4693  10028   -137   -423   -237       O  
ATOM   2195  CB  TYR A1101      -4.039 -29.240 -71.118  1.00 69.21           C  
ANISOU 2195  CB  TYR A1101     7000   7207  12092    -52   -152   -180       C  
ATOM   2196  CG  TYR A1101      -3.473 -29.068 -72.511  1.00 76.07           C  
ANISOU 2196  CG  TYR A1101     7765   8170  12967   -140     15   -136       C  
ATOM   2197  CD1 TYR A1101      -3.406 -27.813 -73.104  1.00 74.97           C  
ANISOU 2197  CD1 TYR A1101     7628   8016  12841   -256     51     -7       C  
ATOM   2198  CD2 TYR A1101      -3.018 -30.160 -73.236  1.00 57.34           C  
ANISOU 2198  CD2 TYR A1101     5314   5890  10581   -121    156   -228       C  
ATOM   2199  CE1 TYR A1101      -2.892 -27.652 -74.378  1.00 75.01           C  
ANISOU 2199  CE1 TYR A1101     7578   8140  12781   -384    232     69       C  
ATOM   2200  CE2 TYR A1101      -2.503 -30.008 -74.510  1.00 58.94           C  
ANISOU 2200  CE2 TYR A1101     5455   6220  10721   -227    373   -222       C  
ATOM   2201  CZ  TYR A1101      -2.442 -28.752 -75.076  1.00 72.93           C  
ANISOU 2201  CZ  TYR A1101     7249   8020  12440   -375    415    -54       C  
ATOM   2202  OH  TYR A1101      -1.930 -28.596 -76.344  1.00 93.67           O  
ANISOU 2202  OH  TYR A1101     9850  10805  14935   -527    656    -13       O  
ATOM   2203  N   ILE A1102      -4.593 -28.471 -68.096  1.00 53.80           N  
ANISOU 2203  N   ILE A1102     5315   5078  10049    -13   -445   -296       N  
ATOM   2204  CA  ILE A1102      -5.585 -27.716 -67.347  1.00 48.78           C  
ANISOU 2204  CA  ILE A1102     4833   4389   9313      3   -415   -368       C  
ATOM   2205  C   ILE A1102      -5.172 -27.503 -65.894  1.00 63.03           C  
ANISOU 2205  C   ILE A1102     6794   6153  11003    -43   -563   -485       C  
ATOM   2206  O   ILE A1102      -5.450 -26.448 -65.320  1.00 69.94           O  
ANISOU 2206  O   ILE A1102     7778   6933  11864    -64   -554   -617       O  
ATOM   2207  CB  ILE A1102      -6.961 -28.412 -67.433  1.00 43.85           C  
ANISOU 2207  CB  ILE A1102     4254   3842   8565     67   -277   -342       C  
ATOM   2208  CG1 ILE A1102      -7.374 -28.587 -68.897  1.00 41.67           C  
ANISOU 2208  CG1 ILE A1102     3857   3615   8361     79   -199   -235       C  
ATOM   2209  CG2 ILE A1102      -8.017 -27.634 -66.662  1.00 55.40           C  
ANISOU 2209  CG2 ILE A1102     5813   5255   9981    103   -177   -449       C  
ATOM   2210  CD1 ILE A1102      -7.398 -27.296 -69.685  1.00 47.41           C  
ANISOU 2210  CD1 ILE A1102     4528   4263   9223     60   -193   -172       C  
ATOM   2211  N   GLN A1103      -4.498 -28.485 -65.288  1.00 58.76           N  
ANISOU 2211  N   GLN A1103     6279   5663  10384    -66   -724   -444       N  
ATOM   2212  CA  GLN A1103      -4.319 -28.485 -63.837  1.00 64.90           C  
ANISOU 2212  CA  GLN A1103     7278   6448  10933   -138   -897   -516       C  
ATOM   2213  C   GLN A1103      -3.567 -27.254 -63.342  1.00 62.16           C  
ANISOU 2213  C   GLN A1103     6974   6000  10645   -235  -1061   -657       C  
ATOM   2214  O   GLN A1103      -3.756 -26.838 -62.193  1.00 64.50           O  
ANISOU 2214  O   GLN A1103     7523   6295  10689   -311  -1134   -804       O  
ATOM   2215  CB  GLN A1103      -3.598 -29.760 -63.403  1.00 89.95           C  
ANISOU 2215  CB  GLN A1103    10444   9656  14078   -148  -1124   -374       C  
ATOM   2216  CG  GLN A1103      -3.996 -30.257 -62.027  1.00 93.81           C  
ANISOU 2216  CG  GLN A1103    11238  10211  14193   -229  -1231   -347       C  
ATOM   2217  CD  GLN A1103      -3.531 -31.676 -61.765  1.00110.30           C  
ANISOU 2217  CD  GLN A1103    13320  12289  16301   -218  -1449   -128       C  
ATOM   2218  OE1 GLN A1103      -2.602 -32.167 -62.407  1.00116.26           O  
ANISOU 2218  OE1 GLN A1103    13816  12961  17396   -139  -1589    -50       O  
ATOM   2219  NE2 GLN A1103      -4.182 -32.345 -60.821  1.00112.27           N  
ANISOU 2219  NE2 GLN A1103    13843  12605  16211   -299  -1460    -23       N  
ATOM   2220  N   LYS A1104      -2.719 -26.657 -64.182  1.00 73.22           N  
ANISOU 2220  N   LYS A1104     8146   7315  12360   -260  -1109   -626       N  
ATOM   2221  CA  LYS A1104      -2.025 -25.436 -63.785  1.00 51.82           C  
ANISOU 2221  CA  LYS A1104     5455   4466   9768   -383  -1273   -754       C  
ATOM   2222  C   LYS A1104      -2.971 -24.250 -63.653  1.00 53.70           C  
ANISOU 2222  C   LYS A1104     5857   4569   9976   -370  -1103   -928       C  
ATOM   2223  O   LYS A1104      -2.654 -23.298 -62.931  1.00 63.43           O  
ANISOU 2223  O   LYS A1104     7226   5661  11213   -474  -1241  -1120       O  
ATOM   2224  CB  LYS A1104      -0.916 -25.105 -64.784  1.00 46.63           C  
ANISOU 2224  CB  LYS A1104     4478   3749   9489   -444  -1316   -644       C  
ATOM   2225  CG  LYS A1104      -1.372 -25.079 -66.233  1.00 44.54           C  
ANISOU 2225  CG  LYS A1104     4062   3511   9352   -376  -1024   -512       C  
ATOM   2226  CD  LYS A1104      -0.268 -24.584 -67.151  1.00 55.67           C  
ANISOU 2226  CD  LYS A1104     5193   4879  11081   -492  -1010   -410       C  
ATOM   2227  CE  LYS A1104      -0.566 -24.919 -68.603  1.00 86.63           C  
ANISOU 2227  CE  LYS A1104     8992   8906  15015   -450   -728   -261       C  
ATOM   2228  NZ  LYS A1104      -0.574 -26.391 -68.833  1.00 86.29           N  
ANISOU 2228  NZ  LYS A1104     8880   9027  14879   -330   -655   -251       N  
ATOM   2229  N   TYR A1105      -4.118 -24.283 -64.327  1.00 69.71           N  
ANISOU 2229  N   TYR A1105     7863   6612  12012   -242   -832   -880       N  
ATOM   2230  CA  TYR A1105      -5.097 -23.210 -64.237  1.00 46.31           C  
ANISOU 2230  CA  TYR A1105     4994   3486   9115   -180   -670  -1035       C  
ATOM   2231  C   TYR A1105      -6.072 -23.393 -63.083  1.00 55.51           C  
ANISOU 2231  C   TYR A1105     6393   4721   9977   -131   -525  -1249       C  
ATOM   2232  O   TYR A1105      -6.814 -22.457 -62.764  1.00 57.37           O  
ANISOU 2232  O   TYR A1105     6711   4801  10288    -68   -374  -1463       O  
ATOM   2233  CB  TYR A1105      -5.870 -23.096 -65.555  1.00 50.53           C  
ANISOU 2233  CB  TYR A1105     5351   3995   9852    -71   -497   -849       C  
ATOM   2234  CG  TYR A1105      -4.983 -22.800 -66.743  1.00 44.05           C  
ANISOU 2234  CG  TYR A1105     4344   3127   9264   -156   -573   -637       C  
ATOM   2235  CD1 TYR A1105      -3.897 -21.944 -66.624  1.00 52.28           C  
ANISOU 2235  CD1 TYR A1105     5358   4009  10497   -301   -730   -669       C  
ATOM   2236  CD2 TYR A1105      -5.222 -23.387 -67.978  1.00 55.54           C  
ANISOU 2236  CD2 TYR A1105     5663   4713  10728   -125   -475   -414       C  
ATOM   2237  CE1 TYR A1105      -3.080 -21.673 -67.702  1.00 56.55           C  
ANISOU 2237  CE1 TYR A1105     5712   4529  11244   -414   -741   -458       C  
ATOM   2238  CE2 TYR A1105      -4.408 -23.122 -69.063  1.00 57.64           C  
ANISOU 2238  CE2 TYR A1105     5789   4977  11135   -235   -483   -231       C  
ATOM   2239  CZ  TYR A1105      -3.339 -22.264 -68.919  1.00 44.47           C  
ANISOU 2239  CZ  TYR A1105     4069   3159   9667   -381   -594   -240       C  
ATOM   2240  OH  TYR A1105      -2.524 -21.994 -69.994  1.00 77.10           O  
ANISOU 2240  OH  TYR A1105     8046   7311  13938   -524   -546    -41       O  
ATOM   2241  N   LEU A1106      -6.087 -24.568 -62.451  1.00 62.39           N  
ANISOU 2241  N   LEU A1106     7370   5807  10530   -163   -550  -1193       N  
ATOM   2242  CA  LEU A1106      -6.933 -24.795 -61.286  1.00 51.55           C  
ANISOU 2242  CA  LEU A1106     6247   4542   8796   -176   -384  -1369       C  
ATOM   2243  C   LEU A1106      -6.414 -24.092 -60.040  1.00 53.07           C  
ANISOU 2243  C   LEU A1106     6739   4685   8741   -315   -524  -1650       C  
ATOM   2244  O   LEU A1106      -7.153 -23.992 -59.054  1.00 69.64           O  
ANISOU 2244  O   LEU A1106     9086   6861  10512   -342   -318  -1876       O  
ATOM   2245  CB  LEU A1106      -7.062 -26.297 -61.019  1.00 49.83           C  
ANISOU 2245  CB  LEU A1106     6076   4545   8312   -210   -398  -1158       C  
ATOM   2246  CG  LEU A1106      -8.190 -27.074 -61.708  1.00 50.77           C  
ANISOU 2246  CG  LEU A1106     6032   4751   8507   -106   -142  -1007       C  
ATOM   2247  CD1 LEU A1106      -8.695 -26.372 -62.964  1.00 44.50           C  
ANISOU 2247  CD1 LEU A1106     4977   3830   8100     29    -24   -987       C  
ATOM   2248  CD2 LEU A1106      -7.724 -28.486 -62.038  1.00 57.49           C  
ANISOU 2248  CD2 LEU A1106     6821   5694   9330   -135   -300   -739       C  
ATOM   2249  N   ARG A 365      -5.175 -23.608 -60.058  1.00111.88           N  
ANISOU 2249  N   ARG A 365    16078  16377  10056   4346   2119  -5472       N  
ATOM   2250  CA  ARG A 365      -4.637 -22.876 -58.924  1.00111.44           C  
ANISOU 2250  CA  ARG A 365    15933  16596   9812   4224   2115  -5414       C  
ATOM   2251  C   ARG A 365      -5.279 -21.495 -58.825  1.00105.37           C  
ANISOU 2251  C   ARG A 365    15231  15685   9121   3350   2429  -5190       C  
ATOM   2252  O   ARG A 365      -5.860 -20.977 -59.783  1.00102.55           O  
ANISOU 2252  O   ARG A 365    14816  15314   8834   2883   2634  -5098       O  
ATOM   2253  CB  ARG A 365      -3.118 -22.739 -59.046  1.00117.97           C  
ANISOU 2253  CB  ARG A 365    15965  18755  10104   4651   1925  -5632       C  
ATOM   2254  CG  ARG A 365      -2.373 -24.063 -59.127  1.00129.78           C  
ANISOU 2254  CG  ARG A 365    17359  20480  11473   5563   1562  -5901       C  
ATOM   2255  CD  ARG A 365      -0.864 -23.854 -59.094  1.00152.88           C  
ANISOU 2255  CD  ARG A 365    19472  24730  13886   5938   1370  -6114       C  
ATOM   2256  NE  ARG A 365      -0.352 -23.269 -60.330  1.00169.26           N  
ANISOU 2256  NE  ARG A 365    20744  27908  15658   5702   1456  -6184       N  
ATOM   2257  CZ  ARG A 365       0.272 -23.958 -61.281  1.00172.33           C  
ANISOU 2257  CZ  ARG A 365    20670  28983  15824   6215   1252  -6448       C  
ATOM   2258  NH1 ARG A 365       0.468 -25.261 -61.138  1.00180.15           N  
ANISOU 2258  NH1 ARG A 365    21934  29648  16865   7008    930  -6686       N  
ATOM   2259  NH2 ARG A 365       0.706 -23.343 -62.373  1.00164.81           N  
ANISOU 2259  NH2 ARG A 365    18957  29074  14591   5918   1332  -6466       N  
ATOM   2260  N   GLN A 366      -5.173 -20.902 -57.641  1.00103.58           N  
ANISOU 2260  N   GLN A 366    15137  15350   8868   3153   2430  -5101       N  
ATOM   2261  CA  GLN A 366      -5.664 -19.550 -57.434  1.00 98.54           C  
ANISOU 2261  CA  GLN A 366    14515  14663   8262   2369   2640  -4917       C  
ATOM   2262  C   GLN A 366      -4.654 -18.533 -57.956  1.00103.24           C  
ANISOU 2262  C   GLN A 366    14141  16648   8438   2057   2625  -4946       C  
ATOM   2263  O   GLN A 366      -3.468 -18.826 -58.129  1.00107.45           O  
ANISOU 2263  O   GLN A 366    14066  18149   8610   2506   2456  -5101       O  
ATOM   2264  CB  GLN A 366      -5.939 -19.298 -55.950  1.00109.48           C  
ANISOU 2264  CB  GLN A 366    16349  15449   9799   2237   2610  -4833       C  
ATOM   2265  CG  GLN A 366      -7.068 -20.132 -55.360  1.00122.59           C  
ANISOU 2265  CG  GLN A 366    18566  15955  12056   2260   2522  -4759       C  
ATOM   2266  CD  GLN A 366      -8.436 -19.505 -55.565  1.00127.13           C  
ANISOU 2266  CD  GLN A 366    19264  15931  13109   1731   2434  -4499       C  
ATOM   2267  OE1 GLN A 366      -8.653 -18.753 -56.515  1.00141.88           O  
ANISOU 2267  OE1 GLN A 366    20982  18027  14898   1374   2543  -4393       O  
ATOM   2268  NE2 GLN A 366      -9.364 -19.806 -54.664  1.00106.84           N  
ANISOU 2268  NE2 GLN A 366    17131  12453  11011   1641   2270  -4141       N  
ATOM   2269  N   ASN A 367      -5.142 -17.322 -58.214  1.00112.34           N  
ANISOU 2269  N   ASN A 367    15078  17905   9700   1164   2781  -4770       N  
ATOM   2270  CA  ASN A 367      -4.266 -16.233 -58.614  1.00103.62           C  
ANISOU 2270  CA  ASN A 367    13006  18075   8289    581   2769  -4693       C  
ATOM   2271  C   ASN A 367      -3.547 -15.670 -57.388  1.00107.11           C  
ANISOU 2271  C   ASN A 367    13238  18913   8545    482   2653  -4693       C  
ATOM   2272  O   ASN A 367      -3.729 -16.137 -56.259  1.00121.35           O  
ANISOU 2272  O   ASN A 367    15636  20024  10448    891   2588  -4779       O  
ATOM   2273  CB  ASN A 367      -5.058 -15.154 -59.350  1.00 96.61           C  
ANISOU 2273  CB  ASN A 367    11961  17087   7661   -485   2947  -4445       C  
ATOM   2274  CG  ASN A 367      -6.364 -14.812 -58.661  1.00105.92           C  
ANISOU 2274  CG  ASN A 367    13953  16891   9399   -995   3050  -4284       C  
ATOM   2275  OD1 ASN A 367      -6.551 -15.101 -57.479  1.00124.96           O  
ANISOU 2275  OD1 ASN A 367    16909  18618  11953   -702   2979  -4310       O  
ATOM   2276  ND2 ASN A 367      -7.278 -14.195 -59.400  1.00108.20           N  
ANISOU 2276  ND2 ASN A 367    14320  16746  10047  -1757   3179  -4067       N  
ATOM   2277  N   ARG A 368      -2.713 -14.651 -57.613  1.00108.23           N  
ANISOU 2277  N   ARG A 368    12516  20158   8447    -87   2585  -4530       N  
ATOM   2278  CA  ARG A 368      -1.932 -14.077 -56.520  1.00104.76           C  
ANISOU 2278  CA  ARG A 368    11813  20071   7920   -192   2386  -4418       C  
ATOM   2279  C   ARG A 368      -2.828 -13.499 -55.433  1.00 99.24           C  
ANISOU 2279  C   ARG A 368    11762  18195   7751   -695   2354  -4191       C  
ATOM   2280  O   ARG A 368      -2.532 -13.632 -54.239  1.00100.06           O  
ANISOU 2280  O   ARG A 368    12109  18075   7833   -378   2225  -4238       O  
ATOM   2281  CB  ARG A 368      -0.990 -12.998 -57.052  1.00108.03           C  
ANISOU 2281  CB  ARG A 368    11187  21781   8078   -843   2277  -4187       C  
ATOM   2282  CG  ARG A 368       0.301 -13.517 -57.659  1.00124.08           C  
ANISOU 2282  CG  ARG A 368    12448  25210   9485   -223   2215  -4417       C  
ATOM   2283  CD  ARG A 368       1.226 -12.360 -58.001  1.00122.13           C  
ANISOU 2283  CD  ARG A 368    11176  26251   8976   -954   2090  -4127       C  
ATOM   2284  NE  ARG A 368       2.513 -12.807 -58.524  1.00156.74           N  
ANISOU 2284  NE  ARG A 368    14812  31807  12934   -390   1910  -4241       N  
ATOM   2285  CZ  ARG A 368       3.486 -11.986 -58.907  1.00170.46           C  
ANISOU 2285  CZ  ARG A 368    15597  34781  14387   -878   1741  -4003       C  
ATOM   2286  NH1 ARG A 368       3.317 -10.673 -58.829  1.00174.57           N  
ANISOU 2286  NH1 ARG A 368    15803  35468  15058  -1954   1702  -3594       N  
ATOM   2287  NH2 ARG A 368       4.626 -12.477 -59.373  1.00161.27           N  
ANISOU 2287  NH2 ARG A 368    13800  34653  12822   -316   1566  -4153       N  
ATOM   2288  N   GLU A 369      -3.927 -12.850 -55.825  1.00 94.06           N  
ANISOU 2288  N   GLU A 369    11372  16805   7560  -1474   2462  -3959       N  
ATOM   2289  CA  GLU A 369      -4.793 -12.198 -54.848  1.00 89.05           C  
ANISOU 2289  CA  GLU A 369    11276  15134   7427  -2000   2419  -3769       C  
ATOM   2290  C   GLU A 369      -5.439 -13.217 -53.916  1.00 93.82           C  
ANISOU 2290  C   GLU A 369    12796  14703   8148  -1322   2487  -3947       C  
ATOM   2291  O   GLU A 369      -5.445 -13.039 -52.693  1.00 96.93           O  
ANISOU 2291  O   GLU A 369    13467  14726   8636  -1286   2374  -3916       O  
ATOM   2292  CB  GLU A 369      -5.859 -11.369 -55.564  1.00 98.55           C  
ANISOU 2292  CB  GLU A 369    12570  15771   9103  -2925   2510  -3523       C  
ATOM   2293  N   LYS A 370      -5.985 -14.297 -54.480  1.00 91.05           N  
ANISOU 2293  N   LYS A 370    12914  13894   7788   -785   2648  -4124       N  
ATOM   2294  CA  LYS A 370      -6.657 -15.298 -53.658  1.00 91.59           C  
ANISOU 2294  CA  LYS A 370    13865  12946   7990   -185   2680  -4239       C  
ATOM   2295  C   LYS A 370      -5.674 -16.018 -52.743  1.00 99.19           C  
ANISOU 2295  C   LYS A 370    14809  14306   8571    641   2501  -4426       C  
ATOM   2296  O   LYS A 370      -6.002 -16.326 -51.590  1.00105.32           O  
ANISOU 2296  O   LYS A 370    16148  14408   9459    865   2440  -4397       O  
ATOM   2297  CB  LYS A 370      -7.395 -16.297 -54.548  1.00101.55           C  
ANISOU 2297  CB  LYS A 370    15543  13662   9378    231   2782  -4312       C  
ATOM   2298  N   ARG A 371      -4.465 -16.295 -53.237  1.00 95.18           N  
ANISOU 2298  N   ARG A 371    13643  14922   7599   1099   2407  -4617       N  
ATOM   2299  CA  ARG A 371      -3.457 -16.943 -52.405  1.00 99.96           C  
ANISOU 2299  CA  ARG A 371    14175  15969   7837   1884   2212  -4811       C  
ATOM   2300  C   ARG A 371      -3.053 -16.057 -51.235  1.00122.19           C  
ANISOU 2300  C   ARG A 371    16822  18923  10679   1498   2075  -4630       C  
ATOM   2301  O   ARG A 371      -2.828 -16.549 -50.123  1.00130.73           O  
ANISOU 2301  O   ARG A 371    18253  19740  11677   1987   1945  -4691       O  
ATOM   2302  CB  ARG A 371      -2.237 -17.310 -53.250  1.00106.04           C  
ANISOU 2302  CB  ARG A 371    14187  17960   8143   2372   2127  -5025       C  
ATOM   2303  CG  ARG A 371      -2.353 -18.655 -53.946  1.00125.35           C  
ANISOU 2303  CG  ARG A 371    16913  20033  10682   3064   2078  -5126       C  
ATOM   2304  CD  ARG A 371      -1.840 -18.590 -55.373  1.00111.50           C  
ANISOU 2304  CD  ARG A 371    14446  19195   8724   3026   2110  -5195       C  
ATOM   2305  NE  ARG A 371      -0.457 -18.131 -55.457  1.00116.74           N  
ANISOU 2305  NE  ARG A 371    14190  21223   8945   3086   1972  -5264       N  
ATOM   2306  CZ  ARG A 371       0.189 -17.935 -56.602  1.00123.35           C  
ANISOU 2306  CZ  ARG A 371    14248  23082   9536   2999   1962  -5292       C  
ATOM   2307  NH1 ARG A 371       1.448 -17.517 -56.595  1.00145.15           N  
ANISOU 2307  NH1 ARG A 371    16171  27074  11905   3027   1819  -5318       N  
ATOM   2308  NH2 ARG A 371      -0.425 -18.157 -57.756  1.00119.17           N  
ANISOU 2308  NH2 ARG A 371    13769  22359   9152   2871   2084  -5278       N  
ATOM   2309  N   PHE A 372      -2.964 -14.744 -51.461  1.00131.09           N  
ANISOU 2309  N   PHE A 372    17420  20451  11937    614   2071  -4399       N  
ATOM   2310  CA  PHE A 372      -2.571 -13.844 -50.383  1.00137.27           C  
ANISOU 2310  CA  PHE A 372    18010  21375  12771    232   1898  -4248       C  
ATOM   2311  C   PHE A 372      -3.701 -13.635 -49.383  1.00123.67           C  
ANISOU 2311  C   PHE A 372    17044  18470  11475    -60   1931  -4125       C  
ATOM   2312  O   PHE A 372      -3.439 -13.448 -48.190  1.00138.09           O  
ANISOU 2312  O   PHE A 372    18985  20213  13271     29   1787  -4110       O  
ATOM   2313  CB  PHE A 372      -2.107 -12.504 -50.952  1.00141.25           C  
ANISOU 2313  CB  PHE A 372    17696  22664  13309   -628   1814  -4031       C  
ATOM   2314  CG  PHE A 372      -1.381 -11.647 -49.956  1.00152.82           C  
ANISOU 2314  CG  PHE A 372    18796  24533  14734   -898   1568  -3924       C  
ATOM   2315  CD1 PHE A 372      -0.161 -12.050 -49.440  1.00156.56           C  
ANISOU 2315  CD1 PHE A 372    18922  25801  14764   -273   1418  -4074       C  
ATOM   2316  CD2 PHE A 372      -1.915 -10.439 -49.538  1.00159.92           C  
ANISOU 2316  CD2 PHE A 372    19697  25014  16053  -1757   1460  -3697       C  
ATOM   2317  CE1 PHE A 372       0.512 -11.269 -48.523  1.00167.81           C  
ANISOU 2317  CE1 PHE A 372    20014  27593  16155   -512   1182  -3979       C  
ATOM   2318  CE2 PHE A 372      -1.244  -9.652 -48.621  1.00162.97           C  
ANISOU 2318  CE2 PHE A 372    19745  25759  16417  -1982   1197  -3623       C  
ATOM   2319  CZ  PHE A 372      -0.030 -10.069 -48.114  1.00168.98           C  
ANISOU 2319  CZ  PHE A 372    20169  27311  16726  -1365   1067  -3754       C  
ATOM   2320  N   THR A 373      -4.955 -13.658 -49.844  1.00 98.17           N  
ANISOU 2320  N   THR A 373    14314  14361   8626   -406   2117  -4044       N  
ATOM   2321  CA  THR A 373      -6.077 -13.613 -48.912  1.00 84.04           C  
ANISOU 2321  CA  THR A 373    13268  11464   7199   -596   2167  -3957       C  
ATOM   2322  C   THR A 373      -6.084 -14.843 -48.014  1.00 92.37           C  
ANISOU 2322  C   THR A 373    14931  12095   8069    258   2141  -4080       C  
ATOM   2323  O   THR A 373      -6.453 -14.761 -46.837  1.00 84.46           O  
ANISOU 2323  O   THR A 373    14334  10592   7166    238   2086  -4018       O  
ATOM   2324  CB  THR A 373      -7.400 -13.502 -49.670  1.00 83.24           C  
ANISOU 2324  CB  THR A 373    13573  10537   7519  -1078   2376  -3860       C  
ATOM   2325  OG1 THR A 373      -7.510 -14.580 -50.606  1.00133.46           O  
ANISOU 2325  OG1 THR A 373    20114  16846  13747   -541   2511  -3989       O  
ATOM   2326  CG2 THR A 373      -7.487 -12.177 -50.412  1.00 84.28           C  
ANISOU 2326  CG2 THR A 373    13149  10976   7896  -2017   2350  -3694       C  
ATOM   2327  N   PHE A 374      -5.682 -15.994 -48.556  1.00 88.95           N  
ANISOU 2327  N   PHE A 374    14560  11871   7367   1016   2150  -4259       N  
ATOM   2328  CA  PHE A 374      -5.537 -17.189 -47.732  1.00 92.62           C  
ANISOU 2328  CA  PHE A 374    15540  12006   7646   1860   2044  -4369       C  
ATOM   2329  C   PHE A 374      -4.393 -17.032 -46.739  1.00108.40           C  
ANISOU 2329  C   PHE A 374    17188  14682   9316   2155   1824  -4421       C  
ATOM   2330  O   PHE A 374      -4.485 -17.502 -45.598  1.00106.71           O  
ANISOU 2330  O   PHE A 374    17432  14054   9058   2499   1721  -4391       O  
ATOM   2331  CB  PHE A 374      -5.317 -18.414 -48.620  1.00 94.50           C  
ANISOU 2331  CB  PHE A 374    15723  12342   7839   2489   2005  -4492       C  
ATOM   2332  CG  PHE A 374      -5.069 -19.682 -47.854  1.00102.42           C  
ANISOU 2332  CG  PHE A 374    17013  13049   8851   3195   1776  -4451       C  
ATOM   2333  CD1 PHE A 374      -6.119 -20.369 -47.269  1.00109.18           C  
ANISOU 2333  CD1 PHE A 374    18405  12945  10133   3167   1707  -4169       C  
ATOM   2334  CD2 PHE A 374      -3.785 -20.186 -47.717  1.00103.83           C  
ANISOU 2334  CD2 PHE A 374    16865  13976   8611   3878   1578  -4659       C  
ATOM   2335  CE1 PHE A 374      -5.895 -21.537 -46.563  1.00124.87           C  
ANISOU 2335  CE1 PHE A 374    20701  14674  12069   3798   1467  -4104       C  
ATOM   2336  CE2 PHE A 374      -3.554 -21.354 -47.012  1.00117.47           C  
ANISOU 2336  CE2 PHE A 374    18907  15396  10331   4538   1326  -4628       C  
ATOM   2337  CZ  PHE A 374      -4.611 -22.029 -46.434  1.00131.24           C  
ANISOU 2337  CZ  PHE A 374    21275  16137  12452   4495   1273  -4352       C  
ATOM   2338  N   VAL A 375      -3.306 -16.377 -47.154  1.00 99.42           N  
ANISOU 2338  N   VAL A 375    15229  14611   7937   2011   1741  -4479       N  
ATOM   2339  CA  VAL A 375      -2.199 -16.110 -46.239  1.00102.10           C  
ANISOU 2339  CA  VAL A 375    15181  15631   7983   2221   1527  -4517       C  
ATOM   2340  C   VAL A 375      -2.658 -15.200 -45.108  1.00 99.04           C  
ANISOU 2340  C   VAL A 375    14983  14813   7837   1651   1481  -4332       C  
ATOM   2341  O   VAL A 375      -2.351 -15.432 -43.934  1.00130.08           O  
ANISOU 2341  O   VAL A 375    19120  18678  11628   1985   1340  -4346       O  
ATOM   2342  CB  VAL A 375      -1.005 -15.507 -47.000  1.00105.74           C  
ANISOU 2342  CB  VAL A 375    14677  17343   8154   2082   1452  -4578       C  
ATOM   2343  CG1 VAL A 375       0.064 -15.039 -46.025  1.00109.01           C  
ANISOU 2343  CG1 VAL A 375    14674  18420   8324   2160   1226  -4576       C  
ATOM   2344  CG2 VAL A 375      -0.430 -16.520 -47.976  1.00123.10           C  
ANISOU 2344  CG2 VAL A 375    16662  20081  10028   2799   1467  -4836       C  
ATOM   2345  N   LEU A 376      -3.404 -14.147 -45.446  1.00 94.76           N  
ANISOU 2345  N   LEU A 376    14363  13981   7661    790   1576  -4172       N  
ATOM   2346  CA  LEU A 376      -3.938 -13.269 -44.412  1.00105.80           C  
ANISOU 2346  CA  LEU A 376    15951  14928   9321    258   1511  -4051       C  
ATOM   2347  C   LEU A 376      -4.985 -13.981 -43.566  1.00106.17           C  
ANISOU 2347  C   LEU A 376    16868  13965   9505    509   1606  -4023       C  
ATOM   2348  O   LEU A 376      -5.193 -13.618 -42.403  1.00117.50           O  
ANISOU 2348  O   LEU A 376    18507  15152  10987    385   1518  -3984       O  
ATOM   2349  CB  LEU A 376      -4.527 -12.010 -45.046  1.00100.24           C  
ANISOU 2349  CB  LEU A 376    14966  14108   9012   -702   1547  -3913       C  
ATOM   2350  CG  LEU A 376      -3.551 -11.192 -45.893  1.00109.49           C  
ANISOU 2350  CG  LEU A 376    15242  16286  10073  -1086   1421  -3862       C  
ATOM   2351  CD1 LEU A 376      -4.275 -10.072 -46.622  1.00100.39           C  
ANISOU 2351  CD1 LEU A 376    13899  14885   9359  -2037   1437  -3694       C  
ATOM   2352  CD2 LEU A 376      -2.424 -10.640 -45.034  1.00111.05           C  
ANISOU 2352  CD2 LEU A 376    14942  17211  10042  -1040   1148  -3875       C  
ATOM   2353  N   ALA A 377      -5.646 -14.996 -44.126  1.00 97.13           N  
ANISOU 2353  N   ALA A 377    16229  12262   8416    858   1767  -4038       N  
ATOM   2354  CA  ALA A 377      -6.621 -15.757 -43.352  1.00 95.65           C  
ANISOU 2354  CA  ALA A 377    16841  11149   8351   1100   1827  -3955       C  
ATOM   2355  C   ALA A 377      -5.938 -16.592 -42.274  1.00115.27           C  
ANISOU 2355  C   ALA A 377    19520  13789  10488   1828   1644  -3999       C  
ATOM   2356  O   ALA A 377      -6.393 -16.621 -41.123  1.00115.77           O  
ANISOU 2356  O   ALA A 377    19872  13464  10653   1771   1578  -3842       O  
ATOM   2357  CB  ALA A 377      -7.450 -16.645 -44.280  1.00 89.91           C  
ANISOU 2357  CB  ALA A 377    16223   9931   8008   1217   1876  -3771       C  
ATOM   2358  N   VAL A 378      -4.841 -17.275 -42.621  1.00109.29           N  
ANISOU 2358  N   VAL A 378    18476  13668   9383   2486   1518  -4162       N  
ATOM   2359  CA  VAL A 378      -4.113 -18.060 -41.629  1.00109.39           C  
ANISOU 2359  CA  VAL A 378    18637  13859   9069   3193   1302  -4213       C  
ATOM   2360  C   VAL A 378      -3.368 -17.156 -40.657  1.00120.35           C  
ANISOU 2360  C   VAL A 378    19601  15826  10301   2972   1157  -4205       C  
ATOM   2361  O   VAL A 378      -3.063 -17.578 -39.534  1.00140.14           O  
ANISOU 2361  O   VAL A 378    22340  18301  12607   3365   1000  -4183       O  
ATOM   2362  CB  VAL A 378      -3.148 -19.058 -42.304  1.00114.89           C  
ANISOU 2362  CB  VAL A 378    19064  15074   9515   3947   1162  -4392       C  
ATOM   2363  CG1 VAL A 378      -3.870 -19.843 -43.401  1.00125.53           C  
ANISOU 2363  CG1 VAL A 378    20584  15907  11205   3973   1256  -4309       C  
ATOM   2364  CG2 VAL A 378      -1.929 -18.345 -42.860  1.00121.90           C  
ANISOU 2364  CG2 VAL A 378    19096  17102  10119   3900   1110  -4579       C  
ATOM   2365  N   VAL A 379      -3.054 -15.922 -41.060  1.00102.27           N  
ANISOU 2365  N   VAL A 379    16688  14065   8104   2346   1175  -4212       N  
ATOM   2366  CA  VAL A 379      -2.501 -14.958 -40.115  1.00100.82           C  
ANISOU 2366  CA  VAL A 379    16141  14315   7852   2048   1013  -4194       C  
ATOM   2367  C   VAL A 379      -3.552 -14.571 -39.085  1.00102.75           C  
ANISOU 2367  C   VAL A 379    16894  13820   8327   1672   1055  -4080       C  
ATOM   2368  O   VAL A 379      -3.266 -14.487 -37.884  1.00117.35           O  
ANISOU 2368  O   VAL A 379    18816  15758  10013   1824    909  -4079       O  
ATOM   2369  CB  VAL A 379      -1.954 -13.724 -40.857  1.00102.56           C  
ANISOU 2369  CB  VAL A 379    15571  15236   8161   1424    969  -4196       C  
ATOM   2370  CG1 VAL A 379      -1.706 -12.579 -39.886  1.00104.32           C  
ANISOU 2370  CG1 VAL A 379    15513  15671   8452    964    784  -4161       C  
ATOM   2371  CG2 VAL A 379      -0.672 -14.075 -41.601  1.00105.24           C  
ANISOU 2371  CG2 VAL A 379    15300  16539   8148   1861    884  -4319       C  
ATOM   2372  N   ILE A 380      -4.788 -14.345 -39.537  1.00113.46           N  
ANISOU 2372  N   ILE A 380    18597  14465  10046   1191   1253  -3995       N  
ATOM   2373  CA  ILE A 380      -5.887 -14.085 -38.613  1.00114.54           C  
ANISOU 2373  CA  ILE A 380    19242  13893  10383    876   1314  -3908       C  
ATOM   2374  C   ILE A 380      -6.108 -15.287 -37.704  1.00110.10           C  
ANISOU 2374  C   ILE A 380    19307  12933   9592   1505   1297  -3832       C  
ATOM   2375  O   ILE A 380      -6.334 -15.137 -36.496  1.00105.95           O  
ANISOU 2375  O   ILE A 380    18998  12277   8982   1484   1226  -3789       O  
ATOM   2376  CB  ILE A 380      -7.162 -13.715 -39.394  1.00105.52           C  
ANISOU 2376  CB  ILE A 380    18351  12071   9673    286   1533  -3842       C  
ATOM   2377  CG1 ILE A 380      -7.082 -12.270 -39.895  1.00101.45           C  
ANISOU 2377  CG1 ILE A 380    17250  11862   9434   -483   1471  -3882       C  
ATOM   2378  CG2 ILE A 380      -8.405 -13.934 -38.543  1.00 92.45           C  
ANISOU 2378  CG2 ILE A 380    16984   9758   8385    174   1529  -3546       C  
ATOM   2379  CD1 ILE A 380      -8.324 -11.802 -40.621  1.00102.16           C  
ANISOU 2379  CD1 ILE A 380    17406  11343  10067  -1062   1591  -3717       C  
ATOM   2380  N   GLY A 381      -6.031 -16.496 -38.264  1.00109.75           N  
ANISOU 2380  N   GLY A 381    19498  12726   9475   2057   1318  -3790       N  
ATOM   2381  CA  GLY A 381      -6.182 -17.689 -37.447  1.00111.84           C  
ANISOU 2381  CA  GLY A 381    20200  12647   9649   2593   1207  -3605       C  
ATOM   2382  C   GLY A 381      -5.112 -17.804 -36.378  1.00118.89           C  
ANISOU 2382  C   GLY A 381    21074  14061  10038   3098    994  -3744       C  
ATOM   2383  O   GLY A 381      -5.406 -18.134 -35.227  1.00128.78           O  
ANISOU 2383  O   GLY A 381    22686  15056  11190   3222    915  -3595       O  
ATOM   2384  N   VAL A 382      -3.858 -17.528 -36.742  1.00116.86           N  
ANISOU 2384  N   VAL A 382    20196  14628   9577   3302    864  -3923       N  
ATOM   2385  CA  VAL A 382      -2.776 -17.559 -35.761  1.00107.97           C  
ANISOU 2385  CA  VAL A 382    18823  14096   8106   3687    624  -3981       C  
ATOM   2386  C   VAL A 382      -2.996 -16.495 -34.693  1.00105.86           C  
ANISOU 2386  C   VAL A 382    18457  13890   7874   3181    595  -3943       C  
ATOM   2387  O   VAL A 382      -2.801 -16.744 -33.497  1.00117.28           O  
ANISOU 2387  O   VAL A 382    20099  15369   9092   3443    454  -3890       O  
ATOM   2388  CB  VAL A 382      -1.414 -17.391 -36.463  1.00110.74           C  
ANISOU 2388  CB  VAL A 382    18453  15368   8256   3939    503  -4177       C  
ATOM   2389  CG1 VAL A 382      -0.315 -17.119 -35.447  1.00114.56           C  
ANISOU 2389  CG1 VAL A 382    18588  16510   8428   4179    264  -4239       C  
ATOM   2390  CG2 VAL A 382      -1.086 -18.632 -37.279  1.00113.53           C  
ANISOU 2390  CG2 VAL A 382    18935  15714   8488   4629    463  -4274       C  
ATOM   2391  N   PHE A 383      -3.420 -15.298 -35.104  1.00103.59           N  
ANISOU 2391  N   PHE A 383    17867  13613   7881   2456    700  -3978       N  
ATOM   2392  CA  PHE A 383      -3.662 -14.220 -34.149  1.00109.29           C  
ANISOU 2392  CA  PHE A 383    18466  14380   8680   1972    631  -3999       C  
ATOM   2393  C   PHE A 383      -4.757 -14.598 -33.159  1.00106.80           C  
ANISOU 2393  C   PHE A 383    18813  13394   8371   1960    714  -3875       C  
ATOM   2394  O   PHE A 383      -4.628 -14.366 -31.952  1.00120.30           O  
ANISOU 2394  O   PHE A 383    20555  15258   9896   2008    586  -3886       O  
ATOM   2395  CB  PHE A 383      -4.026 -12.938 -34.898  1.00 98.51           C  
ANISOU 2395  CB  PHE A 383    16701  13033   7694   1193    688  -4059       C  
ATOM   2396  CG  PHE A 383      -4.200 -11.740 -34.008  1.00 97.08           C  
ANISOU 2396  CG  PHE A 383    16318  12929   7637    698    547  -4140       C  
ATOM   2397  CD1 PHE A 383      -3.110 -10.961 -33.657  1.00112.04           C  
ANISOU 2397  CD1 PHE A 383    17607  15545   9417    636    286  -4243       C  
ATOM   2398  CD2 PHE A 383      -5.452 -11.388 -33.529  1.00102.32           C  
ANISOU 2398  CD2 PHE A 383    17380  12959   8536    307    652  -4132       C  
ATOM   2399  CE1 PHE A 383      -3.263  -9.856 -32.840  1.00107.70           C  
ANISOU 2399  CE1 PHE A 383    16868  15047   9005    208    107  -4351       C  
ATOM   2400  CE2 PHE A 383      -5.612 -10.284 -32.710  1.00 99.19           C  
ANISOU 2400  CE2 PHE A 383    16779  12653   8256   -105    486  -4267       C  
ATOM   2401  CZ  PHE A 383      -4.516  -9.517 -32.366  1.00100.73           C  
ANISOU 2401  CZ  PHE A 383    16383  13533   8356   -148    200  -4383       C  
ATOM   2402  N   VAL A 384      -5.849 -15.183 -33.657  1.00109.41           N  
ANISOU 2402  N   VAL A 384    19661  13009   8900   1890    923  -3748       N  
ATOM   2403  CA  VAL A 384      -6.933 -15.596 -32.773  1.00109.22           C  
ANISOU 2403  CA  VAL A 384    20189  12393   8916   1837   1000  -3557       C  
ATOM   2404  C   VAL A 384      -6.478 -16.728 -31.862  1.00119.05           C  
ANISOU 2404  C   VAL A 384    21818  13682   9735   2525    851  -3443       C  
ATOM   2405  O   VAL A 384      -6.752 -16.718 -30.658  1.00107.16           O  
ANISOU 2405  O   VAL A 384    20530  12146   8041   2529    793  -3362       O  
ATOM   2406  CB  VAL A 384      -8.175 -15.989 -33.594  1.00107.82           C  
ANISOU 2406  CB  VAL A 384    20176  11544   9246   1538   1189  -3291       C  
ATOM   2407  CG1 VAL A 384      -9.248 -16.577 -32.687  1.00103.09           C  
ANISOU 2407  CG1 VAL A 384    20026  10441   8703   1519   1227  -2980       C  
ATOM   2408  CG2 VAL A 384      -8.715 -14.782 -34.343  1.00101.32           C  
ANISOU 2408  CG2 VAL A 384    18942  10681   8873    837   1286  -3364       C  
ATOM   2409  N   VAL A 385      -5.765 -17.713 -32.415  1.00102.79           N  
ANISOU 2409  N   VAL A 385    19801  11728   7527   3116    757  -3435       N  
ATOM   2410  CA  VAL A 385      -5.294 -18.837 -31.609  1.00107.33           C  
ANISOU 2410  CA  VAL A 385    20694  12320   7767   3778    549  -3301       C  
ATOM   2411  C   VAL A 385      -4.371 -18.352 -30.496  1.00112.73           C  
ANISOU 2411  C   VAL A 385    21030  13662   8140   3897    348  -3385       C  
ATOM   2412  O   VAL A 385      -4.423 -18.849 -29.364  1.00125.58           O  
ANISOU 2412  O   VAL A 385    22974  15226   9513   4142    222  -3227       O  
ATOM   2413  CB  VAL A 385      -4.609 -19.885 -32.506  1.00116.39           C  
ANISOU 2413  CB  VAL A 385    21848  13515   8861   4403    433  -3352       C  
ATOM   2414  CG1 VAL A 385      -3.778 -20.851 -31.676  1.00115.61           C  
ANISOU 2414  CG1 VAL A 385    21897  13621   8410   5110    129  -3288       C  
ATOM   2415  CG2 VAL A 385      -5.649 -20.647 -33.314  1.00121.99           C  
ANISOU 2415  CG2 VAL A 385    22998  13454   9898   4354    564  -3167       C  
ATOM   2416  N   CYS A 386      -3.532 -17.356 -30.789  1.00114.74           N  
ANISOU 2416  N   CYS A 386    20623  14564   8411   3697    300  -3614       N  
ATOM   2417  CA  CYS A 386      -2.565 -16.896 -29.796  1.00129.75           C  
ANISOU 2417  CA  CYS A 386    22158  17113  10026   3837     84  -3709       C  
ATOM   2418  C   CYS A 386      -3.237 -16.115 -28.672  1.00119.83           C  
ANISOU 2418  C   CYS A 386    21000  15764   8767   3403    105  -3690       C  
ATOM   2419  O   CYS A 386      -2.834 -16.225 -27.508  1.00115.32           O  
ANISOU 2419  O   CYS A 386    20461  15466   7889   3646    -63  -3662       O  
ATOM   2420  CB  CYS A 386      -1.487 -16.044 -30.465  1.00135.12           C  
ANISOU 2420  CB  CYS A 386    22083  18517  10741   3714      1  -3932       C  
ATOM   2421  SG  CYS A 386      -0.354 -16.964 -31.532  1.00148.32           S  
ANISOU 2421  SG  CYS A 386    23493  20604  12258   4368    -92  -4023       S  
ATOM   2422  N   TRP A 387      -4.265 -15.329 -28.993  1.00114.47           N  
ANISOU 2422  N   TRP A 387    20358  14719   8415   2778    294  -3725       N  
ATOM   2423  CA  TRP A 387      -4.846 -14.395 -28.037  1.00118.52           C  
ANISOU 2423  CA  TRP A 387    20840  15236   8955   2339    287  -3804       C  
ATOM   2424  C   TRP A 387      -6.183 -14.844 -27.456  1.00131.59           C  
ANISOU 2424  C   TRP A 387    23112  16279  10606   2211    453  -3619       C  
ATOM   2425  O   TRP A 387      -6.634 -14.249 -26.472  1.00137.24           O  
ANISOU 2425  O   TRP A 387    23835  17070  11241   1965    430  -3689       O  
ATOM   2426  CB  TRP A 387      -5.022 -13.014 -28.685  1.00111.13           C  
ANISOU 2426  CB  TRP A 387    19435  14386   8405   1685    311  -4020       C  
ATOM   2427  CG  TRP A 387      -3.755 -12.214 -28.800  1.00119.60           C  
ANISOU 2427  CG  TRP A 387    19818  16180   9446   1662     76  -4200       C  
ATOM   2428  CD1 TRP A 387      -3.055 -11.940 -29.940  1.00115.35           C  
ANISOU 2428  CD1 TRP A 387    18825  15949   9055   1577     48  -4248       C  
ATOM   2429  CD2 TRP A 387      -3.043 -11.579 -27.731  1.00131.20           C  
ANISOU 2429  CD2 TRP A 387    20956  18184  10711   1709   -176  -4342       C  
ATOM   2430  NE1 TRP A 387      -1.951 -11.175 -29.646  1.00117.35           N  
ANISOU 2430  NE1 TRP A 387    18481  16893   9215   1548   -211  -4385       N  
ATOM   2431  CE2 TRP A 387      -1.921 -10.940 -28.297  1.00129.28           C  
ANISOU 2431  CE2 TRP A 387    20067  18528  10525   1637   -358  -4454       C  
ATOM   2432  CE3 TRP A 387      -3.244 -11.490 -26.350  1.00125.90           C  
ANISOU 2432  CE3 TRP A 387    20456  17584   9798   1802   -273  -4381       C  
ATOM   2433  CZ2 TRP A 387      -1.005 -10.223 -27.530  1.00126.87           C  
ANISOU 2433  CZ2 TRP A 387    19307  18823  10077   1656   -646  -4599       C  
ATOM   2434  CZ3 TRP A 387      -2.333 -10.778 -25.591  1.00122.95           C  
ANISOU 2434  CZ3 TRP A 387    19631  17814   9272   1843   -550  -4554       C  
ATOM   2435  CH2 TRP A 387      -1.228 -10.154 -26.182  1.00123.83           C  
ANISOU 2435  CH2 TRP A 387    19123  18449   9477   1771   -740  -4660       C  
ATOM   2436  N   PHE A 388      -6.830 -15.870 -28.025  1.00127.07           N  
ANISOU 2436  N   PHE A 388    23038  15134  10110   2373    604  -3393       N  
ATOM   2437  CA  PHE A 388      -8.165 -16.230 -27.545  1.00114.62           C  
ANISOU 2437  CA  PHE A 388    21931  12998   8621   2148    759  -3151       C  
ATOM   2438  C   PHE A 388      -8.162 -16.756 -26.114  1.00119.93           C  
ANISOU 2438  C   PHE A 388    22952  13813   8804   2452    641  -3008       C  
ATOM   2439  O   PHE A 388      -8.937 -16.236 -25.292  1.00142.78           O  
ANISOU 2439  O   PHE A 388    25838  16706  11704   2095    702  -2994       O  
ATOM   2440  CB  PHE A 388      -8.826 -17.223 -28.505  1.00129.92           C  
ANISOU 2440  CB  PHE A 388    24231  14299  10834   2229    895  -2882       C  
ATOM   2441  CG  PHE A 388     -10.161 -17.719 -28.030  1.00128.38           C  
ANISOU 2441  CG  PHE A 388    24496  13553  10728   2027   1021  -2559       C  
ATOM   2442  CD1 PHE A 388     -11.291 -16.925 -28.144  1.00119.35           C  
ANISOU 2442  CD1 PHE A 388    23147  12196  10005   1404   1189  -2526       C  
ATOM   2443  CD2 PHE A 388     -10.285 -18.973 -27.455  1.00133.11           C  
ANISOU 2443  CD2 PHE A 388    25736  13874  10965   2476    939  -2282       C  
ATOM   2444  CE1 PHE A 388     -12.521 -17.376 -27.701  1.00118.19           C  
ANISOU 2444  CE1 PHE A 388    23394  11613   9899   1225   1305  -2222       C  
ATOM   2445  CE2 PHE A 388     -11.512 -19.430 -27.011  1.00132.45           C  
ANISOU 2445  CE2 PHE A 388    26118  13309  10897   2269   1051  -1969       C  
ATOM   2446  CZ  PHE A 388     -12.631 -18.630 -27.134  1.00123.53           C  
ANISOU 2446  CZ  PHE A 388    24748  12014  10174   1638   1252  -1941       C  
ATOM   2447  N   PRO A 389      -7.360 -17.763 -25.742  1.00118.66           N  
ANISOU 2447  N   PRO A 389    22938  13819   8330   3048    444  -2838       N  
ATOM   2448  CA  PRO A 389      -7.451 -18.273 -24.362  1.00129.27           C  
ANISOU 2448  CA  PRO A 389    24560  15292   9265   3258    316  -2616       C  
ATOM   2449  C   PRO A 389      -7.117 -17.232 -23.310  1.00131.85           C  
ANISOU 2449  C   PRO A 389    24487  16229   9380   3074    230  -2847       C  
ATOM   2450  O   PRO A 389      -7.617 -17.320 -22.182  1.00139.36           O  
ANISOU 2450  O   PRO A 389    25644  17264  10044   3020    217  -2711       O  
ATOM   2451  CB  PRO A 389      -6.447 -19.434 -24.348  1.00131.76           C  
ANISOU 2451  CB  PRO A 389    25001  15704   9356   3942     62  -2452       C  
ATOM   2452  CG  PRO A 389      -5.492 -19.115 -25.437  1.00135.16           C  
ANISOU 2452  CG  PRO A 389    24977  16397   9983   4084     28  -2732       C  
ATOM   2453  CD  PRO A 389      -6.321 -18.477 -26.507  1.00117.34           C  
ANISOU 2453  CD  PRO A 389    22663  13770   8150   3565    300  -2849       C  
ATOM   2454  N   PHE A 390      -6.290 -16.242 -23.649  1.00141.18           N  
ANISOU 2454  N   PHE A 390    25089  17862  10691   2968    153  -3187       N  
ATOM   2455  CA  PHE A 390      -5.981 -15.174 -22.707  1.00146.92           C  
ANISOU 2455  CA  PHE A 390    25414  19135  11273   2778     31  -3445       C  
ATOM   2456  C   PHE A 390      -7.213 -14.322 -22.422  1.00144.80           C  
ANISOU 2456  C   PHE A 390    25191  18652  11174   2207    195  -3578       C  
ATOM   2457  O   PHE A 390      -7.605 -14.140 -21.263  1.00160.57           O  
ANISOU 2457  O   PHE A 390    27260  20858  12892   2154    161  -3590       O  
ATOM   2458  CB  PHE A 390      -4.838 -14.317 -23.251  1.00156.85           C  
ANISOU 2458  CB  PHE A 390    26037  20873  12685   2755   -122  -3745       C  
ATOM   2459  CG  PHE A 390      -4.826 -12.920 -22.715  1.00158.43           C  
ANISOU 2459  CG  PHE A 390    25791  21433  12971   2348   -227  -4073       C  
ATOM   2460  CD1 PHE A 390      -4.479 -12.672 -21.399  1.00150.98           C  
ANISOU 2460  CD1 PHE A 390    24738  20951  11676   2497   -409  -4159       C  
ATOM   2461  CD2 PHE A 390      -5.176 -11.854 -23.524  1.00159.58           C  
ANISOU 2461  CD2 PHE A 390    25628  21442  13563   1817   -177  -4299       C  
ATOM   2462  CE1 PHE A 390      -4.473 -11.386 -20.904  1.00147.44           C  
ANISOU 2462  CE1 PHE A 390    23877  20816  11327   2153   -551  -4500       C  
ATOM   2463  CE2 PHE A 390      -5.172 -10.567 -23.036  1.00155.89           C  
ANISOU 2463  CE2 PHE A 390    24755  21257  13220   1452   -343  -4617       C  
ATOM   2464  CZ  PHE A 390      -4.821 -10.334 -21.724  1.00147.82           C  
ANISOU 2464  CZ  PHE A 390    23626  20687  11852   1634   -534  -4734       C  
ATOM   2465  N   PHE A 391      -7.839 -13.788 -23.475  1.00126.73           N  
ANISOU 2465  N   PHE A 391    22823  15975   9352   1776    363  -3686       N  
ATOM   2466  CA  PHE A 391      -9.057 -13.005 -23.291  1.00128.24           C  
ANISOU 2466  CA  PHE A 391    22888  15944   9893   1209    498  -3764       C  
ATOM   2467  C   PHE A 391     -10.183 -13.847 -22.708  1.00138.52           C  
ANISOU 2467  C   PHE A 391    24660  16900  11070   1211    661  -3423       C  
ATOM   2468  O   PHE A 391     -11.035 -13.324 -21.979  1.00147.57           O  
ANISOU 2468  O   PHE A 391    25703  18114  12252    912    709  -3491       O  
ATOM   2469  CB  PHE A 391      -9.499 -12.391 -24.620  1.00121.41           C  
ANISOU 2469  CB  PHE A 391    21772  14712   9646    768    615  -3848       C  
ATOM   2470  CG  PHE A 391      -8.662 -11.227 -25.057  1.00121.15           C  
ANISOU 2470  CG  PHE A 391    21230  15031   9768    566    432  -4217       C  
ATOM   2471  CD1 PHE A 391      -8.968  -9.945 -24.636  1.00113.77           C  
ANISOU 2471  CD1 PHE A 391    19887  14269   9072    156    299  -4521       C  
ATOM   2472  CD2 PHE A 391      -7.573 -11.413 -25.889  1.00116.84           C  
ANISOU 2472  CD2 PHE A 391    20602  14664   9127    803    354  -4263       C  
ATOM   2473  CE1 PHE A 391      -8.202  -8.872 -25.037  1.00108.42           C  
ANISOU 2473  CE1 PHE A 391    18785  13869   8542    -68     68  -4839       C  
ATOM   2474  CE2 PHE A 391      -6.802 -10.344 -26.293  1.00118.28           C  
ANISOU 2474  CE2 PHE A 391    20184  15229   9527    558    152  -4503       C  
ATOM   2475  CZ  PHE A 391      -7.116  -9.072 -25.866  1.00111.60           C  
ANISOU 2475  CZ  PHE A 391    19032  14479   8893    104     -3  -4797       C  
ATOM   2476  N   PHE A 392     -10.205 -15.145 -23.017  1.00132.07           N  
ANISOU 2476  N   PHE A 392    24361  15727  10091   1557    722  -3068       N  
ATOM   2477  CA  PHE A 392     -11.263 -16.015 -22.514  1.00141.61           C  
ANISOU 2477  CA  PHE A 392    26094  16571  11142   1548    848  -2700       C  
ATOM   2478  C   PHE A 392     -11.208 -16.123 -20.995  1.00160.58           C  
ANISOU 2478  C   PHE A 392    28583  19447  12985   1699    735  -2640       C  
ATOM   2479  O   PHE A 392     -12.213 -15.906 -20.307  1.00162.75           O  
ANISOU 2479  O   PHE A 392    28882  19736  13217   1401    841  -2581       O  
ATOM   2480  CB  PHE A 392     -11.148 -17.395 -23.162  1.00136.73           C  
ANISOU 2480  CB  PHE A 392    26046  15469  10436   1945    854  -2356       C  
ATOM   2481  CG  PHE A 392     -12.312 -18.299 -22.879  1.00146.82           C  
ANISOU 2481  CG  PHE A 392    27924  16249  11612   1873    976  -1946       C  
ATOM   2482  CD1 PHE A 392     -13.486 -18.181 -23.604  1.00142.34           C  
ANISOU 2482  CD1 PHE A 392    27415  15142  11527   1445   1198  -1848       C  
ATOM   2483  CD2 PHE A 392     -12.231 -19.274 -21.898  1.00154.92           C  
ANISOU 2483  CD2 PHE A 392    29396  17365  12100   2212    834  -1601       C  
ATOM   2484  CE1 PHE A 392     -14.561 -19.012 -23.352  1.00140.28           C  
ANISOU 2484  CE1 PHE A 392    27726  14425  11150   1363   1304  -1460       C  
ATOM   2485  CE2 PHE A 392     -13.303 -20.110 -21.641  1.00158.48           C  
ANISOU 2485  CE2 PHE A 392    30372  17377  12466   2099    914  -1162       C  
ATOM   2486  CZ  PHE A 392     -14.469 -19.978 -22.369  1.00152.41           C  
ANISOU 2486  CZ  PHE A 392    29775  16056  12077   1685   1169  -1124       C  
ATOM   2487  N   THR A 393     -10.034 -16.453 -20.451  1.00164.73           N  
ANISOU 2487  N   THR A 393    29103  20412  13074   2173    506  -2651       N  
ATOM   2488  CA  THR A 393      -9.904 -16.587 -19.005  1.00169.68           C  
ANISOU 2488  CA  THR A 393    29765  21540  13165   2335    372  -2560       C  
ATOM   2489  C   THR A 393      -9.912 -15.234 -18.307  1.00164.92           C  
ANISOU 2489  C   THR A 393    28580  21472  12609   2022    332  -2981       C  
ATOM   2490  O   THR A 393     -10.393 -15.130 -17.173  1.00167.19           O  
ANISOU 2490  O   THR A 393    28846  22090  12587   1934    328  -2943       O  
ATOM   2491  CB  THR A 393      -8.629 -17.352 -18.655  1.00184.07           C  
ANISOU 2491  CB  THR A 393    31618  23666  14655   2921    102  -2404       C  
ATOM   2492  OG1 THR A 393      -7.527 -16.816 -19.398  1.00193.17           O  
ANISOU 2492  OG1 THR A 393    32329  25021  16048   3059     -5  -2723       O  
ATOM   2493  CG2 THR A 393      -8.788 -18.829 -18.978  1.00182.51           C  
ANISOU 2493  CG2 THR A 393    31971  22956  14418   3232     64  -1908       C  
ATOM   2494  N   TYR A 394      -9.384 -14.192 -18.956  1.00154.46           N  
ANISOU 2494  N   TYR A 394    26776  20262  11651   1854    277  -3385       N  
ATOM   2495  CA  TYR A 394      -9.414 -12.864 -18.351  1.00145.61           C  
ANISOU 2495  CA  TYR A 394    25124  19581  10619   1553    184  -3814       C  
ATOM   2496  C   TYR A 394     -10.840 -12.347 -18.212  1.00143.57           C  
ANISOU 2496  C   TYR A 394    24797  19116  10639   1071    370  -3887       C  
ATOM   2497  O   TYR A 394     -11.136 -11.594 -17.279  1.00154.22           O  
ANISOU 2497  O   TYR A 394    25840  20879  11876    914    300  -4153       O  
ATOM   2498  CB  TYR A 394      -8.566 -11.890 -19.168  1.00144.32           C  
ANISOU 2498  CB  TYR A 394    24507  19523  10805   1445     42  -4183       C  
ATOM   2499  CG  TYR A 394      -8.516 -10.490 -18.598  1.00148.95           C  
ANISOU 2499  CG  TYR A 394    24565  20507  11522   1143   -129  -4642       C  
ATOM   2500  CD1 TYR A 394      -7.991 -10.250 -17.335  1.00159.83           C  
ANISOU 2500  CD1 TYR A 394    25757  22469  12501   1343   -329  -4770       C  
ATOM   2501  CD2 TYR A 394      -9.001  -9.409 -19.321  1.00141.27           C  
ANISOU 2501  CD2 TYR A 394    23262  19305  11108    656   -120  -4936       C  
ATOM   2502  CE1 TYR A 394      -7.946  -8.971 -16.811  1.00164.41           C  
ANISOU 2502  CE1 TYR A 394    25876  23348  13244   1068   -513  -5182       C  
ATOM   2503  CE2 TYR A 394      -8.958  -8.127 -18.806  1.00146.84           C  
ANISOU 2503  CE2 TYR A 394    23519  20305  11970    368   -321  -5353       C  
ATOM   2504  CZ  TYR A 394      -8.431  -7.914 -17.551  1.00156.19           C  
ANISOU 2504  CZ  TYR A 394    24583  22000  12763    579   -517  -5458       C  
ATOM   2505  OH  TYR A 394      -8.392  -6.638 -17.038  1.00157.90           O  
ANISOU 2505  OH  TYR A 394    24428  22365  13202    336   -760  -5784       O  
ATOM   2506  N   THR A 395     -11.732 -12.737 -19.124  1.00127.83           N  
ANISOU 2506  N   THR A 395    23047  16507   9015    860    588  -3667       N  
ATOM   2507  CA  THR A 395     -13.146 -12.428 -18.953  1.00124.00           C  
ANISOU 2507  CA  THR A 395    22524  15825   8765    478    756  -3660       C  
ATOM   2508  C   THR A 395     -13.805 -13.344 -17.932  1.00140.66           C  
ANISOU 2508  C   THR A 395    25049  18036  10358    594    850  -3307       C  
ATOM   2509  O   THR A 395     -14.744 -12.926 -17.245  1.00150.91           O  
ANISOU 2509  O   THR A 395    26189  19532  11617    360    915  -3404       O  
ATOM   2510  CB  THR A 395     -13.881 -12.538 -20.289  1.00128.22           C  
ANISOU 2510  CB  THR A 395    23155  15669   9894    212    938  -3503       C  
ATOM   2511  OG1 THR A 395     -13.502 -13.755 -20.945  1.00150.84           O  
ANISOU 2511  OG1 THR A 395    26526  18143  12644    498   1006  -3129       O  
ATOM   2512  CG2 THR A 395     -13.549 -11.357 -21.181  1.00124.73           C  
ANISOU 2512  CG2 THR A 395    22171  15201  10022    -37    833  -3860       C  
ATOM   2513  N   LEU A 396     -13.334 -14.588 -17.825  1.00145.65           N  
ANISOU 2513  N   LEU A 396    26192  18559  10590    967    827  -2892       N  
ATOM   2514  CA  LEU A 396     -13.912 -15.523 -16.867  1.00154.32           C  
ANISOU 2514  CA  LEU A 396    27701  19756  11179   1063    871  -2475       C  
ATOM   2515  C   LEU A 396     -13.651 -15.093 -15.429  1.00142.78           C  
ANISOU 2515  C   LEU A 396    25933  19092   9225   1137    732  -2642       C  
ATOM   2516  O   LEU A 396     -14.483 -15.346 -14.551  1.00140.53           O  
ANISOU 2516  O   LEU A 396    25732  19043   8622   1010    809  -2450       O  
ATOM   2517  CB  LEU A 396     -13.361 -16.927 -17.116  1.00168.43           C  
ANISOU 2517  CB  LEU A 396    30081  21227  12690   1486    790  -1991       C  
ATOM   2518  CG  LEU A 396     -14.388 -18.038 -17.345  1.00171.16           C  
ANISOU 2518  CG  LEU A 396    31028  20996  13010   1400    932  -1459       C  
ATOM   2519  CD1 LEU A 396     -15.216 -17.770 -18.592  1.00159.58           C  
ANISOU 2519  CD1 LEU A 396    29592  18871  12172   1056   1156  -1543       C  
ATOM   2520  CD2 LEU A 396     -13.706 -19.396 -17.428  1.00171.54           C  
ANISOU 2520  CD2 LEU A 396    31629  20803  12746   1888    741  -1003       C  
ATOM   2521  N   THR A 397     -12.515 -14.441 -15.170  1.00142.85           N  
ANISOU 2521  N   THR A 397    25564  19552   9160   1330    524  -2992       N  
ATOM   2522  CA  THR A 397     -12.220 -13.973 -13.821  1.00152.54           C  
ANISOU 2522  CA  THR A 397    26468  21540   9949   1397    376  -3190       C  
ATOM   2523  C   THR A 397     -13.168 -12.861 -13.389  1.00154.35           C  
ANISOU 2523  C   THR A 397    26259  22039  10350    989    458  -3605       C  
ATOM   2524  O   THR A 397     -13.383 -12.666 -12.188  1.00168.08           O  
ANISOU 2524  O   THR A 397    27817  24374  11673    967    414  -3688       O  
ATOM   2525  CB  THR A 397     -10.772 -13.492 -13.734  1.00153.04           C  
ANISOU 2525  CB  THR A 397    26218  21964   9968   1684    116  -3477       C  
ATOM   2526  OG1 THR A 397     -10.556 -12.445 -14.689  1.00157.18           O  
ANISOU 2526  OG1 THR A 397    26381  22285  11057   1455     97  -3906       O  
ATOM   2527  CG2 THR A 397      -9.812 -14.634 -14.020  1.00156.71           C  
ANISOU 2527  CG2 THR A 397    27062  22275  10205   2171     -4  -3091       C  
ATOM   2528  N   ALA A 398     -13.746 -12.130 -14.346  1.00135.54           N  
ANISOU 2528  N   ALA A 398    23674  19243   8581    676    555  -3870       N  
ATOM   2529  CA  ALA A 398     -14.647 -11.037 -13.999  1.00133.13           C  
ANISOU 2529  CA  ALA A 398    22904  19173   8506    365    572  -4302       C  
ATOM   2530  C   ALA A 398     -15.968 -11.547 -13.436  1.00143.89           C  
ANISOU 2530  C   ALA A 398    24460  20580   9632    240    767  -4034       C  
ATOM   2531  O   ALA A 398     -16.607 -10.853 -12.638  1.00158.04           O  
ANISOU 2531  O   ALA A 398    25878  22854  11317    149    735  -4355       O  
ATOM   2532  CB  ALA A 398     -14.896 -10.155 -15.222  1.00125.63           C  
ANISOU 2532  CB  ALA A 398    21674  17726   8334    126    558  -4587       C  
ATOM   2533  N   VAL A 399     -16.392 -12.748 -13.833  1.00148.61           N  
ANISOU 2533  N   VAL A 399    25628  20699  10138    252    946  -3457       N  
ATOM   2534  CA  VAL A 399     -17.636 -13.330 -13.345  1.00154.27           C  
ANISOU 2534  CA  VAL A 399    26571  21429  10614     89   1132  -3122       C  
ATOM   2535  C   VAL A 399     -17.392 -14.347 -12.233  1.00166.93           C  
ANISOU 2535  C   VAL A 399    28464  23495  11465    301   1088  -2667       C  
ATOM   2536  O   VAL A 399     -18.308 -15.087 -11.864  1.00166.46           O  
ANISOU 2536  O   VAL A 399    28673  23423  11153    177   1223  -2236       O  
ATOM   2537  CB  VAL A 399     -18.443 -13.959 -14.492  1.00149.42           C  
ANISOU 2537  CB  VAL A 399    26384  19954  10434   -115   1341  -2757       C  
ATOM   2538  CG1 VAL A 399     -18.816 -12.901 -15.519  1.00137.15           C  
ANISOU 2538  CG1 VAL A 399    24471  17998   9641   -368   1368  -3163       C  
ATOM   2539  CG2 VAL A 399     -17.658 -15.088 -15.141  1.00142.93           C  
ANISOU 2539  CG2 VAL A 399    26116  18642   9548    140   1314  -2313       C  
ATOM   2540  N   GLY A 400     -16.177 -14.400 -11.692  1.00177.61           N  
ANISOU 2540  N   GLY A 400    29749  25258  12475    604    880  -2721       N  
ATOM   2541  CA  GLY A 400     -15.877 -15.295 -10.592  1.00188.12           C  
ANISOU 2541  CA  GLY A 400    31290  27062  13124    811    784  -2283       C  
ATOM   2542  C   GLY A 400     -15.389 -16.662 -11.022  1.00193.42           C  
ANISOU 2542  C   GLY A 400    32577  27227  13688   1082    718  -1651       C  
ATOM   2543  O   GLY A 400     -16.127 -17.648 -10.931  1.00204.85           O  
ANISOU 2543  O   GLY A 400    34421  28434  14978    993    799  -1089       O  
ATOM   2544  N   CYS A 401     -14.145 -16.736 -11.492  1.00184.67           N  
ANISOU 2544  N   CYS A 401    31525  25961  12679   1424    541  -1740       N  
ATOM   2545  CA  CYS A 401     -13.533 -17.997 -11.883  1.00182.81           C  
ANISOU 2545  CA  CYS A 401    31827  25293  12337   1776    410  -1218       C  
ATOM   2546  C   CYS A 401     -12.060 -17.975 -11.504  1.00190.30           C  
ANISOU 2546  C   CYS A 401    32622  26633  13050   2221    129  -1348       C  
ATOM   2547  O   CYS A 401     -11.403 -16.932 -11.558  1.00189.33           O  
ANISOU 2547  O   CYS A 401    32034  26811  13093   2244     68  -1890       O  
ATOM   2548  CB  CYS A 401     -13.690 -18.266 -13.386  1.00174.27           C  
ANISOU 2548  CB  CYS A 401    31066  23349  11801   1751    526  -1177       C  
ATOM   2549  SG  CYS A 401     -15.393 -18.569 -13.916  1.00175.11           S  
ANISOU 2549  SG  CYS A 401    31459  22863  12213   1276    828   -898       S  
ATOM   2550  N   SER A 402     -11.547 -19.141 -11.120  1.00197.43           N  
ANISOU 2550  N   SER A 402    33902  27515  13600   2567    -75   -831       N  
ATOM   2551  CA  SER A 402     -10.182 -19.276 -10.634  1.00195.95           C  
ANISOU 2551  CA  SER A 402    33583  27723  13144   3021   -371   -880       C  
ATOM   2552  C   SER A 402      -9.269 -19.789 -11.739  1.00192.91           C  
ANISOU 2552  C   SER A 402    33450  26828  13018   3427   -508   -858       C  
ATOM   2553  O   SER A 402      -9.633 -20.699 -12.490  1.00190.50           O  
ANISOU 2553  O   SER A 402    33644  25872  12865   3489   -489   -489       O  
ATOM   2554  CB  SER A 402     -10.125 -20.221  -9.432  1.00192.31           C  
ANISOU 2554  CB  SER A 402    33318  27622  12130   3161   -565   -334       C  
ATOM   2555  OG  SER A 402     -10.591 -21.514  -9.779  1.00189.46           O  
ANISOU 2555  OG  SER A 402    33542  26667  11775   3207   -618    307       O  
ATOM   2556  N   VAL A 403      -8.080 -19.201 -11.829  1.00185.88           N  
ANISOU 2556  N   VAL A 403    32184  26262  12179   3703   -663  -1262       N  
ATOM   2557  CA  VAL A 403      -7.064 -19.615 -12.795  1.00174.57           C  
ANISOU 2557  CA  VAL A 403    30814  24510  11004   4104   -814  -1300       C  
ATOM   2558  C   VAL A 403      -5.698 -19.570 -12.119  1.00174.79           C  
ANISOU 2558  C   VAL A 403    30553  25115  10746   4534  -1117  -1422       C  
ATOM   2559  O   VAL A 403      -5.425 -18.646 -11.338  1.00178.79           O  
ANISOU 2559  O   VAL A 403    30617  26226  11089   4430  -1145  -1753       O  
ATOM   2560  CB  VAL A 403      -7.090 -18.730 -14.053  1.00167.18           C  
ANISOU 2560  CB  VAL A 403    29600  23285  10638   3884   -626  -1753       C  
ATOM   2561  CG1 VAL A 403      -8.240 -19.128 -14.965  1.00160.74           C  
ANISOU 2561  CG1 VAL A 403    29168  21742  10165   3590   -379  -1541       C  
ATOM   2562  CG2 VAL A 403      -7.197 -17.262 -13.665  1.00160.49           C  
ANISOU 2562  CG2 VAL A 403    28216  22918   9843   3547   -545  -2284       C  
ATOM   2563  N   PRO A 404      -4.821 -20.539 -12.374  1.00169.30           N  
ANISOU 2563  N   PRO A 404    30036  24239  10049   5005  -1363  -1177       N  
ATOM   2564  CA  PRO A 404      -3.486 -20.505 -11.768  1.00178.30           C  
ANISOU 2564  CA  PRO A 404    30892  25922  10932   5431  -1659  -1305       C  
ATOM   2565  C   PRO A 404      -2.674 -19.323 -12.275  1.00171.17           C  
ANISOU 2565  C   PRO A 404    29402  25342  10293   5417  -1633  -1896       C  
ATOM   2566  O   PRO A 404      -2.904 -18.791 -13.363  1.00166.12           O  
ANISOU 2566  O   PRO A 404    28618  24398  10102   5192  -1446  -2149       O  
ATOM   2567  CB  PRO A 404      -2.859 -21.836 -12.203  1.00180.72           C  
ANISOU 2567  CB  PRO A 404    31546  25822  11297   5924  -1919   -947       C  
ATOM   2568  CG  PRO A 404      -4.017 -22.705 -12.573  1.00173.03           C  
ANISOU 2568  CG  PRO A 404    31125  24172  10447   5733  -1814   -493       C  
ATOM   2569  CD  PRO A 404      -5.053 -21.779 -13.134  1.00158.70           C  
ANISOU 2569  CD  PRO A 404    29192  22189   8917   5191  -1424   -755       C  
ATOM   2570  N   ARG A 405      -1.699 -18.919 -11.457  1.00160.19           N  
ANISOU 2570  N   ARG A 405    27664  24587   8614   5649  -1850  -2090       N  
ATOM   2571  CA  ARG A 405      -0.878 -17.759 -11.792  1.00156.81           C  
ANISOU 2571  CA  ARG A 405    26647  24531   8403   5616  -1884  -2619       C  
ATOM   2572  C   ARG A 405       0.042 -18.055 -12.970  1.00170.18           C  
ANISOU 2572  C   ARG A 405    28214  26012  10433   5913  -1960  -2698       C  
ATOM   2573  O   ARG A 405       0.132 -17.262 -13.914  1.00152.02           O  
ANISOU 2573  O   ARG A 405    25586  23645   8529   5687  -1841  -3018       O  
ATOM   2574  CB  ARG A 405      -0.069 -17.321 -10.571  1.00160.82           C  
ANISOU 2574  CB  ARG A 405    26762  25706   8637   5742  -2098  -2748       C  
ATOM   2575  N   THR A 406       0.742 -19.192 -12.929  1.00203.64           N  
ANISOU 2575  N   THR A 406    32688  30170  14515   6421  -2183  -2415       N  
ATOM   2576  CA  THR A 406       1.638 -19.548 -14.026  1.00212.93           C  
ANISOU 2576  CA  THR A 406    33726  31210  15968   6764  -2274  -2518       C  
ATOM   2577  C   THR A 406       0.862 -19.818 -15.309  1.00206.87           C  
ANISOU 2577  C   THR A 406    33189  29792  15622   6567  -2038  -2461       C  
ATOM   2578  O   THR A 406       1.305 -19.440 -16.400  1.00218.80           O  
ANISOU 2578  O   THR A 406    34388  31289  17458   6563  -1971  -2721       O  
ATOM   2579  CB  THR A 406       2.480 -20.765 -13.647  1.00219.46           C  
ANISOU 2579  CB  THR A 406    34787  32061  16537   7382  -2606  -2246       C  
ATOM   2580  OG1 THR A 406       1.617 -21.860 -13.314  1.00222.06           O  
ANISOU 2580  OG1 THR A 406    35739  31893  16740   7408  -2639  -1759       O  
ATOM   2581  CG2 THR A 406       3.372 -20.447 -12.457  1.00221.70           C  
ANISOU 2581  CG2 THR A 406    34793  33021  16423   7594  -2848  -2336       C  
ATOM   2582  N   LEU A 407      -0.297 -20.472 -15.199  1.00185.46           N  
ANISOU 2582  N   LEU A 407    31006  26563  12897   6391  -1917  -2106       N  
ATOM   2583  CA  LEU A 407      -1.122 -20.720 -16.376  1.00181.65           C  
ANISOU 2583  CA  LEU A 407    30769  25435  12817   6182  -1690  -2043       C  
ATOM   2584  C   LEU A 407      -1.667 -19.419 -16.951  1.00171.59           C  
ANISOU 2584  C   LEU A 407    29149  24191  11858   5625  -1395  -2400       C  
ATOM   2585  O   LEU A 407      -1.669 -19.226 -18.173  1.00145.08           O  
ANISOU 2585  O   LEU A 407    25667  20574   8884   5531  -1264  -2559       O  
ATOM   2586  CB  LEU A 407      -2.261 -21.678 -16.022  1.00180.61           C  
ANISOU 2586  CB  LEU A 407    31272  24768  12582   6085  -1653  -1553       C  
ATOM   2587  CG  LEU A 407      -3.304 -21.994 -17.097  1.00167.87           C  
ANISOU 2587  CG  LEU A 407    29989  22433  11360   5829  -1418  -1431       C  
ATOM   2588  CD1 LEU A 407      -3.677 -23.465 -17.049  1.00168.97           C  
ANISOU 2588  CD1 LEU A 407    30746  22012  11444   6108  -1609   -917       C  
ATOM   2589  CD2 LEU A 407      -4.547 -21.131 -16.923  1.00162.14           C  
ANISOU 2589  CD2 LEU A 407    29261  21641  10706   5192  -1090  -1495       C  
ATOM   2590  N   PHE A 408      -2.136 -18.514 -16.087  1.00179.01           N  
ANISOU 2590  N   PHE A 408    29920  25453  12641   5257  -1314  -2539       N  
ATOM   2591  CA  PHE A 408      -2.631 -17.226 -16.559  1.00174.73           C  
ANISOU 2591  CA  PHE A 408    29033  24935  12420   4735  -1107  -2907       C  
ATOM   2592  C   PHE A 408      -1.515 -16.392 -17.173  1.00165.58           C  
ANISOU 2592  C   PHE A 408    27283  24152  11477   4782  -1215  -3287       C  
ATOM   2593  O   PHE A 408      -1.774 -15.558 -18.048  1.00170.59           O  
ANISOU 2593  O   PHE A 408    27657  24657  12504   4403  -1077  -3530       O  
ATOM   2594  CB  PHE A 408      -3.293 -16.466 -15.409  1.00187.31           C  
ANISOU 2594  CB  PHE A 408    30547  26851  13770   4408  -1065  -3024       C  
ATOM   2595  CG  PHE A 408      -4.107 -15.284 -15.849  1.00186.81           C  
ANISOU 2595  CG  PHE A 408    30253  26666  14059   3848   -866  -3361       C  
ATOM   2596  CD1 PHE A 408      -5.407 -15.452 -16.296  1.00178.75           C  
ANISOU 2596  CD1 PHE A 408    29579  25101  13237   3501   -602  -3221       C  
ATOM   2597  CD2 PHE A 408      -3.577 -14.005 -15.811  1.00190.50           C  
ANISOU 2597  CD2 PHE A 408    30158  27544  14679   3665   -980  -3813       C  
ATOM   2598  CE1 PHE A 408      -6.163 -14.368 -16.699  1.00176.79           C  
ANISOU 2598  CE1 PHE A 408    29115  24720  13339   2990   -446  -3543       C  
ATOM   2599  CE2 PHE A 408      -4.327 -12.916 -16.213  1.00188.00           C  
ANISOU 2599  CE2 PHE A 408    29618  27067  14745   3139   -857  -4118       C  
ATOM   2600  CZ  PHE A 408      -5.622 -13.098 -16.657  1.00182.36           C  
ANISOU 2600  CZ  PHE A 408    29238  25807  14241   2801   -585  -3987       C  
ATOM   2601  N   LYS A 409      -0.273 -16.604 -16.733  1.00149.92           N  
ANISOU 2601  N   LYS A 409    25074  22645   9245   5225  -1477  -3322       N  
ATOM   2602  CA  LYS A 409       0.858 -15.895 -17.323  1.00142.92           C  
ANISOU 2602  CA  LYS A 409    23607  22163   8532   5288  -1600  -3637       C  
ATOM   2603  C   LYS A 409       1.186 -16.441 -18.708  1.00154.55           C  
ANISOU 2603  C   LYS A 409    25081  23354  10285   5461  -1537  -3597       C  
ATOM   2604  O   LYS A 409       1.439 -15.675 -19.644  1.00152.29           O  
ANISOU 2604  O   LYS A 409    24384  23163  10317   5207  -1475  -3827       O  
ATOM   2605  CB  LYS A 409       2.075 -15.991 -16.403  1.00147.75           C  
ANISOU 2605  CB  LYS A 409    23980  23385   8774   5722  -1902  -3683       C  
ATOM   2606  N   PHE A 410       1.188 -17.768 -18.857  1.00173.27           N  
ANISOU 2606  N   PHE A 410    27899  25393  12542   5894  -1581  -3305       N  
ATOM   2607  CA  PHE A 410       1.522 -18.368 -20.143  1.00180.43           C  
ANISOU 2607  CA  PHE A 410    28809  26063  13685   6137  -1552  -3305       C  
ATOM   2608  C   PHE A 410       0.449 -18.125 -21.195  1.00178.24           C  
ANISOU 2608  C   PHE A 410    28674  25245  13805   5684  -1254  -3307       C  
ATOM   2609  O   PHE A 410       0.740 -18.233 -22.392  1.00180.83           O  
ANISOU 2609  O   PHE A 410    28837  25496  14373   5751  -1195  -3406       O  
ATOM   2610  CB  PHE A 410       1.757 -19.871 -19.981  1.00186.37           C  
ANISOU 2610  CB  PHE A 410    30028  26545  14240   6742  -1743  -3016       C  
ATOM   2611  CG  PHE A 410       3.169 -20.233 -19.615  1.00192.11           C  
ANISOU 2611  CG  PHE A 410    30487  27801  14703   7319  -2061  -3103       C  
ATOM   2612  CD1 PHE A 410       4.199 -19.320 -19.770  1.00191.42           C  
ANISOU 2612  CD1 PHE A 410    29747  28370  14614   7302  -2124  -3426       C  
ATOM   2613  CD2 PHE A 410       3.466 -21.492 -19.124  1.00198.30           C  
ANISOU 2613  CD2 PHE A 410    31671  28417  15257   7871  -2327  -2848       C  
ATOM   2614  CE1 PHE A 410       5.499 -19.659 -19.437  1.00197.26           C  
ANISOU 2614  CE1 PHE A 410    30229  29613  15107   7838  -2414  -3511       C  
ATOM   2615  CE2 PHE A 410       4.759 -21.837 -18.790  1.00205.73           C  
ANISOU 2615  CE2 PHE A 410    32371  29831  15968   8418  -2637  -2945       C  
ATOM   2616  CZ  PHE A 410       5.779 -20.919 -18.946  1.00204.99           C  
ANISOU 2616  CZ  PHE A 410    31616  30416  15855   8409  -2664  -3286       C  
ATOM   2617  N   PHE A 411      -0.775 -17.793 -20.778  1.00165.95           N  
ANISOU 2617  N   PHE A 411    27397  23349  12307   5230  -1068  -3212       N  
ATOM   2618  CA  PHE A 411      -1.845 -17.584 -21.745  1.00144.47           C  
ANISOU 2618  CA  PHE A 411    24840  20081   9970   4796   -788  -3205       C  
ATOM   2619  C   PHE A 411      -1.602 -16.333 -22.583  1.00129.57           C  
ANISOU 2619  C   PHE A 411    22387  18431   8415   4380   -705  -3539       C  
ATOM   2620  O   PHE A 411      -1.785 -16.359 -23.806  1.00130.47           O  
ANISOU 2620  O   PHE A 411    22459  18274   8840   4253   -565  -3573       O  
ATOM   2621  CB  PHE A 411      -3.196 -17.518 -21.034  1.00148.63           C  
ANISOU 2621  CB  PHE A 411    25773  20249  10452   4421   -624  -3035       C  
ATOM   2622  CG  PHE A 411      -3.958 -18.814 -21.070  1.00161.37           C  
ANISOU 2622  CG  PHE A 411    28042  21258  12014   4608   -578  -2630       C  
ATOM   2623  CD1 PHE A 411      -3.423 -19.930 -21.692  1.00163.13           C  
ANISOU 2623  CD1 PHE A 411    28469  21253  12259   5112   -715  -2477       C  
ATOM   2624  CD2 PHE A 411      -5.215 -18.913 -20.498  1.00167.72           C  
ANISOU 2624  CD2 PHE A 411    29238  21731  12756   4281   -424  -2411       C  
ATOM   2625  CE1 PHE A 411      -4.123 -21.123 -21.733  1.00160.63           C  
ANISOU 2625  CE1 PHE A 411    28761  20333  11937   5279   -736  -2096       C  
ATOM   2626  CE2 PHE A 411      -5.921 -20.103 -20.538  1.00170.38           C  
ANISOU 2626  CE2 PHE A 411    30170  21505  13061   4417   -415  -1994       C  
ATOM   2627  CZ  PHE A 411      -5.374 -21.209 -21.156  1.00164.48           C  
ANISOU 2627  CZ  PHE A 411    29645  20478  12372   4912   -588  -1829       C  
ATOM   2628  N   PHE A 412      -1.192 -15.229 -21.954  1.00141.23           N  
ANISOU 2628  N   PHE A 412    23415  20409   9837   4152   -818  -3780       N  
ATOM   2629  CA  PHE A 412      -0.795 -14.064 -22.735  1.00150.22           C  
ANISOU 2629  CA  PHE A 412    23973  21811  11293   3773   -829  -4060       C  
ATOM   2630  C   PHE A 412       0.653 -14.134 -23.200  1.00158.30           C  
ANISOU 2630  C   PHE A 412    24529  23385  12234   4133  -1019  -4152       C  
ATOM   2631  O   PHE A 412       1.040 -13.372 -24.094  1.00159.73           O  
ANISOU 2631  O   PHE A 412    24235  23779  12677   3849  -1023  -4309       O  
ATOM   2632  CB  PHE A 412      -1.032 -12.760 -21.956  1.00158.31           C  
ANISOU 2632  CB  PHE A 412    24693  23086  12373   3328   -918  -4304       C  
ATOM   2633  CG  PHE A 412      -0.296 -12.669 -20.647  1.00174.51           C  
ANISOU 2633  CG  PHE A 412    26601  25674  14031   3625  -1164  -4368       C  
ATOM   2634  CD1 PHE A 412       1.050 -12.337 -20.606  1.00181.78           C  
ANISOU 2634  CD1 PHE A 412    27018  27195  14856   3849  -1411  -4504       C  
ATOM   2635  CD2 PHE A 412      -0.966 -12.869 -19.453  1.00183.78           C  
ANISOU 2635  CD2 PHE A 412    28113  26792  14921   3652  -1150  -4294       C  
ATOM   2636  CE1 PHE A 412       1.719 -12.240 -19.402  1.00189.51           C  
ANISOU 2636  CE1 PHE A 412    27867  28657  15482   4120  -1643  -4569       C  
ATOM   2637  CE2 PHE A 412      -0.304 -12.768 -18.246  1.00184.65           C  
ANISOU 2637  CE2 PHE A 412    28082  27421  14656   3916  -1378  -4358       C  
ATOM   2638  CZ  PHE A 412       1.040 -12.455 -18.219  1.00187.28           C  
ANISOU 2638  CZ  PHE A 412    27940  28300  14917   4157  -1627  -4501       C  
ATOM   2639  N   TRP A 413       1.461 -15.022 -22.614  1.00170.47           N  
ANISOU 2639  N   TRP A 413    26177  25182  13412   4737  -1191  -4049       N  
ATOM   2640  CA  TRP A 413       2.766 -15.324 -23.192  1.00177.60           C  
ANISOU 2640  CA  TRP A 413    26696  26556  14228   5157  -1347  -4127       C  
ATOM   2641  C   TRP A 413       2.618 -15.893 -24.596  1.00166.64           C  
ANISOU 2641  C   TRP A 413    25377  24876  13063   5233  -1189  -4088       C  
ATOM   2642  O   TRP A 413       3.472 -15.656 -25.458  1.00164.90           O  
ANISOU 2642  O   TRP A 413    24664  25084  12905   5299  -1237  -4227       O  
ATOM   2643  CB  TRP A 413       3.520 -16.307 -22.295  1.00200.73           C  
ANISOU 2643  CB  TRP A 413    29819  29704  16744   5821  -1572  -4015       C  
ATOM   2644  CG  TRP A 413       4.964 -15.978 -22.071  1.00215.51           C  
ANISOU 2644  CG  TRP A 413    31127  32332  18424   6109  -1825  -4190       C  
ATOM   2645  CD1 TRP A 413       5.464 -14.933 -21.351  1.00214.02           C  
ANISOU 2645  CD1 TRP A 413    30508  32645  18167   5887  -1974  -4354       C  
ATOM   2646  CD2 TRP A 413       6.097 -16.717 -22.546  1.00222.24           C  
ANISOU 2646  CD2 TRP A 413    31781  33535  19126   6694  -1982  -4232       C  
ATOM   2647  NE1 TRP A 413       6.837 -14.966 -21.359  1.00219.29           N  
ANISOU 2647  NE1 TRP A 413    30721  33948  18652   6269  -2200  -4464       N  
ATOM   2648  CE2 TRP A 413       7.250 -16.052 -22.085  1.00223.20           C  
ANISOU 2648  CE2 TRP A 413    31338  34383  19083   6772  -2201  -4401       C  
ATOM   2649  CE3 TRP A 413       6.247 -17.872 -23.321  1.00216.94           C  
ANISOU 2649  CE3 TRP A 413    31339  32639  18449   7176  -1982  -4169       C  
ATOM   2650  CZ2 TRP A 413       8.537 -16.502 -22.374  1.00219.15           C  
ANISOU 2650  CZ2 TRP A 413    30476  34406  18384   7303  -2394  -4500       C  
ATOM   2651  CZ3 TRP A 413       7.527 -18.317 -23.606  1.00213.64           C  
ANISOU 2651  CZ3 TRP A 413    30569  32756  17849   7729  -2191  -4304       C  
ATOM   2652  CH2 TRP A 413       8.654 -17.634 -23.133  1.00214.24           C  
ANISOU 2652  CH2 TRP A 413    30075  33581  17746   7783  -2381  -4462       C  
ATOM   2653  N   PHE A 414       1.537 -16.640 -24.841  1.00157.15           N  
ANISOU 2653  N   PHE A 414    24762  22977  11969   5220  -1009  -3896       N  
ATOM   2654  CA  PHE A 414       1.233 -17.096 -26.192  1.00150.44           C  
ANISOU 2654  CA  PHE A 414    24001  21790  11370   5232   -847  -3879       C  
ATOM   2655  C   PHE A 414       0.852 -15.936 -27.101  1.00137.57           C  
ANISOU 2655  C   PHE A 414    21989  20176  10104   4571   -669  -4021       C  
ATOM   2656  O   PHE A 414       1.136 -15.975 -28.303  1.00131.98           O  
ANISOU 2656  O   PHE A 414    21029  19567   9552   4571   -598  -4092       O  
ATOM   2657  CB  PHE A 414       0.105 -18.128 -26.159  1.00160.84           C  
ANISOU 2657  CB  PHE A 414    26058  22317  12738   5335   -726  -3621       C  
ATOM   2658  CG  PHE A 414       0.475 -19.418 -25.484  1.00179.24           C  
ANISOU 2658  CG  PHE A 414    28790  24550  14764   6000   -951  -3435       C  
ATOM   2659  CD1 PHE A 414       1.800 -19.798 -25.360  1.00186.33           C  
ANISOU 2659  CD1 PHE A 414    29387  25992  15418   6563  -1213  -3551       C  
ATOM   2660  CD2 PHE A 414      -0.505 -20.254 -24.977  1.00185.53           C  
ANISOU 2660  CD2 PHE A 414    30255  24712  15526   6047   -928  -3130       C  
ATOM   2661  CE1 PHE A 414       2.141 -20.986 -24.741  1.00194.16           C  
ANISOU 2661  CE1 PHE A 414    30754  26858  16160   7174  -1469  -3382       C  
ATOM   2662  CE2 PHE A 414      -0.174 -21.443 -24.357  1.00192.95           C  
ANISOU 2662  CE2 PHE A 414    31569  25531  16212   6624  -1192  -2920       C  
ATOM   2663  CZ  PHE A 414       1.154 -21.810 -24.239  1.00196.40           C  
ANISOU 2663  CZ  PHE A 414    31716  26476  16430   7197  -1474  -3055       C  
ATOM   2664  N   GLY A 415       0.211 -14.902 -26.553  1.00134.10           N  
ANISOU 2664  N   GLY A 415    21491  19658   9804   4010   -619  -4072       N  
ATOM   2665  CA  GLY A 415      -0.104 -13.736 -27.356  1.00132.43           C  
ANISOU 2665  CA  GLY A 415    20894  19457   9965   3364   -523  -4208       C  
ATOM   2666  C   GLY A 415       1.109 -12.881 -27.662  1.00139.38           C  
ANISOU 2666  C   GLY A 415    21027  21085  10846   3271   -722  -4378       C  
ATOM   2667  O   GLY A 415       1.143 -12.189 -28.685  1.00141.38           O  
ANISOU 2667  O   GLY A 415    20895  21441  11382   2853   -676  -4437       O  
ATOM   2668  N   TYR A 416       2.119 -12.916 -26.791  1.00138.69           N  
ANISOU 2668  N   TYR A 416    20716  21540  10441   3637   -958  -4434       N  
ATOM   2669  CA  TYR A 416       3.327 -12.131 -27.020  1.00144.97           C  
ANISOU 2669  CA  TYR A 416    20784  23084  11213   3562  -1173  -4572       C  
ATOM   2670  C   TYR A 416       4.133 -12.685 -28.188  1.00155.36           C  
ANISOU 2670  C   TYR A 416    21805  24755  12469   3871  -1144  -4566       C  
ATOM   2671  O   TYR A 416       4.587 -11.930 -29.056  1.00163.97           O  
ANISOU 2671  O   TYR A 416    22327  26248  13726   3518  -1178  -4621       O  
ATOM   2672  CB  TYR A 416       4.176 -12.093 -25.749  1.00152.81           C  
ANISOU 2672  CB  TYR A 416    21647  24547  11869   3908  -1433  -4634       C  
ATOM   2673  CG  TYR A 416       3.861 -10.928 -24.841  1.00156.18           C  
ANISOU 2673  CG  TYR A 416    21926  25009  12405   3449  -1574  -4758       C  
ATOM   2674  CD1 TYR A 416       3.440  -9.712 -25.362  1.00148.85           C  
ANISOU 2674  CD1 TYR A 416    20672  24003  11880   2761  -1595  -4858       C  
ATOM   2675  CD2 TYR A 416       3.984 -11.043 -23.462  1.00169.87           C  
ANISOU 2675  CD2 TYR A 416    23837  26861  13843   3712  -1718  -4788       C  
ATOM   2676  CE1 TYR A 416       3.151  -8.644 -24.537  1.00152.32           C  
ANISOU 2676  CE1 TYR A 416    20968  24458  12449   2376  -1779  -5021       C  
ATOM   2677  CE2 TYR A 416       3.698  -9.979 -22.629  1.00171.46           C  
ANISOU 2677  CE2 TYR A 416    23885  27129  14135   3332  -1869  -4953       C  
ATOM   2678  CZ  TYR A 416       3.282  -8.782 -23.172  1.00168.23           C  
ANISOU 2678  CZ  TYR A 416    23153  26617  14152   2679  -1911  -5087       C  
ATOM   2679  OH  TYR A 416       2.995  -7.719 -22.348  1.00183.26           O  
ANISOU 2679  OH  TYR A 416    24893  28565  16171   2335  -2115  -5299       O  
ATOM   2680  N   CYS A 417       4.320 -14.005 -28.230  1.00157.87           N  
ANISOU 2680  N   CYS A 417    22485  24952  12547   4528  -1109  -4502       N  
ATOM   2681  CA  CYS A 417       5.088 -14.622 -29.306  1.00165.66           C  
ANISOU 2681  CA  CYS A 417    23195  26305  13443   4913  -1103  -4555       C  
ATOM   2682  C   CYS A 417       4.362 -14.599 -30.646  1.00147.09           C  
ANISOU 2682  C   CYS A 417    20878  23618  11393   4581   -859  -4528       C  
ATOM   2683  O   CYS A 417       4.911 -15.104 -31.632  1.00137.26           O  
ANISOU 2683  O   CYS A 417    19392  22688  10071   4884   -834  -4595       O  
ATOM   2684  CB  CYS A 417       5.453 -16.061 -28.934  1.00179.41           C  
ANISOU 2684  CB  CYS A 417    25342  27946  14878   5743  -1198  -4528       C  
ATOM   2685  SG  CYS A 417       4.054 -17.108 -28.480  1.00187.60           S  
ANISOU 2685  SG  CYS A 417    27352  27942  15987   5885  -1061  -4313       S  
ATOM   2686  N   ASN A 418       3.152 -14.037 -30.707  1.00143.55           N  
ANISOU 2686  N   ASN A 418    20707  22565  11269   3986   -686  -4451       N  
ATOM   2687  CA  ASN A 418       2.476 -13.865 -31.988  1.00148.67           C  
ANISOU 2687  CA  ASN A 418    21338  22922  12228   3593   -467  -4423       C  
ATOM   2688  C   ASN A 418       3.205 -12.861 -32.872  1.00143.02           C  
ANISOU 2688  C   ASN A 418    19836  22888  11618   3170   -533  -4490       C  
ATOM   2689  O   ASN A 418       3.141 -12.958 -34.103  1.00137.45           O  
ANISOU 2689  O   ASN A 418    18949  22252  11023   3057   -398  -4485       O  
ATOM   2690  CB  ASN A 418       1.029 -13.425 -31.761  1.00149.65           C  
ANISOU 2690  CB  ASN A 418    21918  22261  12679   3037   -295  -4338       C  
ATOM   2691  CG  ASN A 418       0.309 -13.092 -33.054  1.00153.00           C  
ANISOU 2691  CG  ASN A 418    22294  22379  13460   2549    -86  -4308       C  
ATOM   2692  OD1 ASN A 418      -0.261 -13.968 -33.702  1.00159.43           O  
ANISOU 2692  OD1 ASN A 418    23509  22738  14327   2765     96  -4246       O  
ATOM   2693  ND2 ASN A 418       0.329 -11.818 -33.433  1.00147.69           N  
ANISOU 2693  ND2 ASN A 418    21130  21937  13049   1881   -142  -4346       N  
ATOM   2694  N   SER A 419       3.905 -11.900 -32.264  1.00134.37           N  
ANISOU 2694  N   SER A 419    18256  22317  10482   2924   -761  -4538       N  
ATOM   2695  CA  SER A 419       4.606 -10.885 -33.042  1.00133.10           C  
ANISOU 2695  CA  SER A 419    17323  22817  10433   2456   -878  -4547       C  
ATOM   2696  C   SER A 419       5.782 -11.470 -33.811  1.00146.19           C  
ANISOU 2696  C   SER A 419    18513  25253  11779   2933   -911  -4595       C  
ATOM   2697  O   SER A 419       6.115 -10.979 -34.895  1.00140.38           O  
ANISOU 2697  O   SER A 419    17234  24980  11124   2587   -894  -4560       O  
ATOM   2698  CB  SER A 419       5.076  -9.759 -32.122  1.00124.58           C  
ANISOU 2698  CB  SER A 419    15866  22072   9397   2113  -1168  -4584       C  
ATOM   2699  OG  SER A 419       3.972  -9.062 -31.573  1.00132.72           O  
ANISOU 2699  OG  SER A 419    17223  22451  10752   1604  -1158  -4589       O  
ATOM   2700  N   SER A 420       6.426 -12.504 -33.272  1.00155.47           N  
ANISOU 2700  N   SER A 420    19866  26616  12589   3719   -978  -4678       N  
ATOM   2701  CA  SER A 420       7.500 -13.183 -33.986  1.00161.59           C  
ANISOU 2701  CA  SER A 420    20234  28111  13052   4269  -1018  -4782       C  
ATOM   2702  C   SER A 420       6.982 -14.274 -34.909  1.00168.64           C  
ANISOU 2702  C   SER A 420    21501  28627  13947   4648   -807  -4825       C  
ATOM   2703  O   SER A 420       7.630 -14.585 -35.916  1.00178.05           O  
ANISOU 2703  O   SER A 420    22259  30413  14979   4887   -785  -4926       O  
ATOM   2704  CB  SER A 420       8.499 -13.787 -32.996  1.00167.94           C  
ANISOU 2704  CB  SER A 420    21024  29308  13478   4971  -1242  -4883       C  
ATOM   2705  OG  SER A 420       7.903 -14.842 -32.262  1.00173.35           O  
ANISOU 2705  OG  SER A 420    22485  29284  14097   5475  -1210  -4872       O  
ATOM   2706  N   LEU A 421       5.832 -14.865 -34.581  1.00161.48           N  
ANISOU 2706  N   LEU A 421    21373  26775  13208   4715   -667  -4755       N  
ATOM   2707  CA  LEU A 421       5.212 -15.859 -35.446  1.00154.67           C  
ANISOU 2707  CA  LEU A 421    20916  25441  12410   5021   -490  -4780       C  
ATOM   2708  C   LEU A 421       4.554 -15.236 -36.668  1.00158.71           C  
ANISOU 2708  C   LEU A 421    21236  25844  13224   4383   -271  -4724       C  
ATOM   2709  O   LEU A 421       4.245 -15.954 -37.624  1.00149.58           O  
ANISOU 2709  O   LEU A 421    20233  24507  12094   4621   -134  -4780       O  
ATOM   2710  CB  LEU A 421       4.174 -16.664 -34.662  1.00143.52           C  
ANISOU 2710  CB  LEU A 421    20393  23048  11089   5244   -438  -4672       C  
ATOM   2711  CG  LEU A 421       4.367 -18.176 -34.606  1.00148.27           C  
ANISOU 2711  CG  LEU A 421    21431  23419  11485   6120   -541  -4742       C  
ATOM   2712  CD1 LEU A 421       5.689 -18.519 -33.938  1.00154.20           C  
ANISOU 2712  CD1 LEU A 421    21873  24854  11861   6728   -824  -4871       C  
ATOM   2713  CD2 LEU A 421       3.206 -18.840 -33.877  1.00147.21           C  
ANISOU 2713  CD2 LEU A 421    22162  22285  11487   6176   -494  -4552       C  
ATOM   2714  N   ASN A 422       4.339 -13.917 -36.659  1.00164.33           N  
ANISOU 2714  N   ASN A 422    21611  26653  14174   3583   -268  -4620       N  
ATOM   2715  CA  ASN A 422       3.667 -13.278 -37.789  1.00156.56           C  
ANISOU 2715  CA  ASN A 422    20460  25519  13506   2921    -91  -4538       C  
ATOM   2716  C   ASN A 422       4.554 -13.194 -39.027  1.00138.10           C  
ANISOU 2716  C   ASN A 422    17398  24077  10996   2942    -91  -4596       C  
ATOM   2717  O   ASN A 422       4.077 -13.537 -40.123  1.00128.57           O  
ANISOU 2717  O   ASN A 422    16254  22714   9882   2897     99  -4604       O  
ATOM   2718  CB  ASN A 422       3.144 -11.900 -37.368  1.00157.44           C  
ANISOU 2718  CB  ASN A 422    20449  25411  13960   2067   -153  -4419       C  
ATOM   2719  CG  ASN A 422       2.185 -11.304 -38.379  1.00140.88           C  
ANISOU 2719  CG  ASN A 422    18359  22911  12258   1368     21  -4316       C  
ATOM   2720  OD1 ASN A 422       0.984 -11.570 -38.341  1.00132.92           O  
ANISOU 2720  OD1 ASN A 422    17970  21037  11496   1245    203  -4277       O  
ATOM   2721  ND2 ASN A 422       2.709 -10.488 -39.286  1.00133.82           N  
ANISOU 2721  ND2 ASN A 422    16762  22659  11423    885    -49  -4250       N  
ATOM   2722  N   PRO A 423       5.819 -12.756 -38.948  1.00138.43           N  
ANISOU 2722  N   PRO A 423    16727  25096  10774   2998   -294  -4635       N  
ATOM   2723  CA  PRO A 423       6.613 -12.643 -40.183  1.00130.36           C  
ANISOU 2723  CA  PRO A 423    14967  25002   9560   2961   -279  -4668       C  
ATOM   2724  C   PRO A 423       6.926 -13.976 -40.838  1.00144.54           C  
ANISOU 2724  C   PRO A 423    16864  27000  11055   3795   -185  -4889       C  
ATOM   2725  O   PRO A 423       7.010 -14.036 -42.071  1.00164.00           O  
ANISOU 2725  O   PRO A 423    18960  29893  13461   3712    -65  -4925       O  
ATOM   2726  CB  PRO A 423       7.895 -11.936 -39.717  1.00135.57           C  
ANISOU 2726  CB  PRO A 423    14901  26620   9988   2886   -548  -4650       C  
ATOM   2727  CG  PRO A 423       7.531 -11.278 -38.436  1.00147.74           C  
ANISOU 2727  CG  PRO A 423    16750  27634  11750   2574   -692  -4564       C  
ATOM   2728  CD  PRO A 423       6.550 -12.199 -37.795  1.00151.20           C  
ANISOU 2728  CD  PRO A 423    18113  27063  12274   2990   -549  -4627       C  
ATOM   2729  N   VAL A 424       7.104 -15.047 -40.060  1.00142.66           N  
ANISOU 2729  N   VAL A 424    17100  26479  10625   4600   -268  -5046       N  
ATOM   2730  CA  VAL A 424       7.486 -16.326 -40.648  1.00143.69           C  
ANISOU 2730  CA  VAL A 424    17298  26813  10483   5452   -263  -5299       C  
ATOM   2731  C   VAL A 424       6.352 -16.946 -41.454  1.00141.13           C  
ANISOU 2731  C   VAL A 424    17513  25710  10398   5469    -44  -5311       C  
ATOM   2732  O   VAL A 424       6.604 -17.811 -42.300  1.00141.19           O  
ANISOU 2732  O   VAL A 424    17441  25976  10229   6029    -26  -5534       O  
ATOM   2733  CB  VAL A 424       7.972 -17.304 -39.561  1.00147.48           C  
ANISOU 2733  CB  VAL A 424    18164  27136  10735   6293   -476  -5441       C  
ATOM   2734  CG1 VAL A 424       9.194 -16.743 -38.851  1.00159.74           C  
ANISOU 2734  CG1 VAL A 424    19129  29546  12019   6335   -698  -5460       C  
ATOM   2735  CG2 VAL A 424       6.858 -17.601 -38.571  1.00147.84           C  
ANISOU 2735  CG2 VAL A 424    19113  26012  11048   6238   -444  -5282       C  
ATOM   2736  N   ILE A 425       5.106 -16.528 -41.216  1.00133.15           N  
ANISOU 2736  N   ILE A 425    17039  23765   9786   4885    107  -5098       N  
ATOM   2737  CA  ILE A 425       3.990 -17.037 -42.008  1.00126.98           C  
ANISOU 2737  CA  ILE A 425    16754  22233   9257   4832    319  -5085       C  
ATOM   2738  C   ILE A 425       4.152 -16.636 -43.468  1.00127.04           C  
ANISOU 2738  C   ILE A 425    16158  22866   9247   4502    458  -5124       C  
ATOM   2739  O   ILE A 425       3.810 -17.398 -44.381  1.00127.19           O  
ANISOU 2739  O   ILE A 425    16343  22720   9264   4825    569  -5261       O  
ATOM   2740  CB  ILE A 425       2.652 -16.540 -41.429  1.00124.06           C  
ANISOU 2740  CB  ILE A 425    17006  20820   9309   4208    451  -4845       C  
ATOM   2741  CG1 ILE A 425       2.478 -17.032 -39.993  1.00128.25           C  
ANISOU 2741  CG1 ILE A 425    18131  20798   9801   4570    318  -4799       C  
ATOM   2742  CG2 ILE A 425       1.488 -17.008 -42.289  1.00127.68           C  
ANISOU 2742  CG2 ILE A 425    17952  20515  10046   4103    674  -4816       C  
ATOM   2743  CD1 ILE A 425       1.236 -16.500 -39.314  1.00116.44           C  
ANISOU 2743  CD1 ILE A 425    17175  18411   8657   3975    434  -4589       C  
ATOM   2744  N   TYR A 426       4.687 -15.438 -43.711  1.00130.63           N  
ANISOU 2744  N   TYR A 426    15887  24064   9681   3849    427  -4995       N  
ATOM   2745  CA  TYR A 426       4.915 -14.994 -45.082  1.00127.87           C  
ANISOU 2745  CA  TYR A 426    14886  24425   9272   3475    534  -4982       C  
ATOM   2746  C   TYR A 426       5.960 -15.858 -45.776  1.00138.03           C  
ANISOU 2746  C   TYR A 426    15704  26652  10088   4260    480  -5282       C  
ATOM   2747  O   TYR A 426       5.805 -16.206 -46.952  1.00142.94           O  
ANISOU 2747  O   TYR A 426    16158  27511  10644   4345    617  -5393       O  
ATOM   2748  CB  TYR A 426       5.339 -13.525 -45.093  1.00129.68           C  
ANISOU 2748  CB  TYR A 426    14422  25271   9581   2600    439  -4736       C  
ATOM   2749  CG  TYR A 426       4.366 -12.597 -44.399  1.00135.14           C  
ANISOU 2749  CG  TYR A 426    15508  25093  10745   1840    435  -4496       C  
ATOM   2750  CD1 TYR A 426       3.108 -12.349 -44.934  1.00126.33           C  
ANISOU 2750  CD1 TYR A 426    14794  23170  10035   1309    626  -4372       C  
ATOM   2751  CD2 TYR A 426       4.711 -11.957 -43.215  1.00131.51           C  
ANISOU 2751  CD2 TYR A 426    15001  24642  10324   1668    225  -4422       C  
ATOM   2752  CE1 TYR A 426       2.219 -11.498 -44.305  1.00112.50           C  
ANISOU 2752  CE1 TYR A 426    13377  20654   8713    644    602  -4200       C  
ATOM   2753  CE2 TYR A 426       3.828 -11.104 -42.579  1.00127.71           C  
ANISOU 2753  CE2 TYR A 426    14851  23409  10265   1014    194  -4261       C  
ATOM   2754  CZ  TYR A 426       2.584 -10.878 -43.129  1.00119.74           C  
ANISOU 2754  CZ  TYR A 426    14226  21619   9652    511    380  -4160       C  
ATOM   2755  OH  TYR A 426       1.702 -10.030 -42.500  1.00117.98           O  
ANISOU 2755  OH  TYR A 426    14309  20673   9846   -110    331  -4044       O  
ATOM   2756  N   THR A 427       7.033 -16.214 -45.066  1.00138.44           N  
ANISOU 2756  N   THR A 427    15527  27273   9802   4855    268  -5440       N  
ATOM   2757  CA  THR A 427       8.057 -17.066 -45.661  1.00144.50           C  
ANISOU 2757  CA  THR A 427    15837  28917  10151   5649    174  -5754       C  
ATOM   2758  C   THR A 427       7.525 -18.463 -45.952  1.00144.98           C  
ANISOU 2758  C   THR A 427    16531  28132  10421   6340    158  -5891       C  
ATOM   2759  O   THR A 427       7.918 -19.084 -46.947  1.00148.49           O  
ANISOU 2759  O   THR A 427    16635  28990  10794   6711    119  -6041       O  
ATOM   2760  CB  THR A 427       9.277 -17.139 -44.740  1.00149.29           C  
ANISOU 2760  CB  THR A 427    16107  30182  10435   6109    -83  -5858       C  
ATOM   2761  OG1 THR A 427       9.759 -15.815 -44.477  1.00148.95           O  
ANISOU 2761  OG1 THR A 427    15462  30775  10357   5360   -133  -5618       O  
ATOM   2762  CG2 THR A 427      10.391 -17.958 -45.379  1.00155.97           C  
ANISOU 2762  CG2 THR A 427    16391  31845  11026   6828   -242  -6091       C  
ATOM   2763  N   ILE A 428       6.613 -18.960 -45.115  1.00141.70           N  
ANISOU 2763  N   ILE A 428    17020  26554  10267   6487    158  -5830       N  
ATOM   2764  CA  ILE A 428       6.091 -20.310 -45.293  1.00142.39           C  
ANISOU 2764  CA  ILE A 428    17736  25799  10568   7108     82  -5914       C  
ATOM   2765  C   ILE A 428       5.135 -20.366 -46.479  1.00139.08           C  
ANISOU 2765  C   ILE A 428    17466  24950  10427   6761    306  -5853       C  
ATOM   2766  O   ILE A 428       5.252 -21.240 -47.347  1.00152.77           O  
ANISOU 2766  O   ILE A 428    19130  26726  12190   7207    229  -5999       O  
ATOM   2767  CB  ILE A 428       5.411 -20.793 -43.998  1.00140.23           C  
ANISOU 2767  CB  ILE A 428    18348  24464  10470   7306     -4  -5802       C  
ATOM   2768  CG1 ILE A 428       6.438 -20.941 -42.874  1.00148.90           C  
ANISOU 2768  CG1 ILE A 428    19307  26002  11267   7784   -268  -5892       C  
ATOM   2769  CG2 ILE A 428       4.689 -22.109 -44.233  1.00140.38           C  
ANISOU 2769  CG2 ILE A 428    19043  23533  10763   7791    -91  -5810       C  
ATOM   2770  CD1 ILE A 428       5.833 -21.376 -41.555  1.00152.77           C  
ANISOU 2770  CD1 ILE A 428    20622  25552  11873   7960   -369  -5758       C  
ATOM   2771  N   PHE A 429       4.178 -19.436 -46.538  1.00133.22           N  
ANISOU 2771  N   PHE A 429    16928  23797   9893   5966    560  -5654       N  
ATOM   2772  CA  PHE A 429       3.075 -19.549 -47.484  1.00129.32           C  
ANISOU 2772  CA  PHE A 429    16754  22662   9720   5637    774  -5573       C  
ATOM   2773  C   PHE A 429       3.196 -18.638 -48.700  1.00132.07           C  
ANISOU 2773  C   PHE A 429    16398  23798   9983   5027    957  -5545       C  
ATOM   2774  O   PHE A 429       2.475 -18.853 -49.680  1.00136.06           O  
ANISOU 2774  O   PHE A 429    17052  23944  10701   4862   1109  -5520       O  
ATOM   2775  CB  PHE A 429       1.743 -19.263 -46.782  1.00123.11           C  
ANISOU 2775  CB  PHE A 429    16770  20725   9281   5181    923  -5368       C  
ATOM   2776  CG  PHE A 429       1.344 -20.315 -45.788  1.00123.48           C  
ANISOU 2776  CG  PHE A 429    17593  19837   9486   5712    764  -5316       C  
ATOM   2777  CD1 PHE A 429       0.677 -21.459 -46.199  1.00123.44           C  
ANISOU 2777  CD1 PHE A 429    18097  19046   9760   6059    724  -5287       C  
ATOM   2778  CD2 PHE A 429       1.637 -20.162 -44.443  1.00124.12           C  
ANISOU 2778  CD2 PHE A 429    17865  19862   9433   5833    627  -5273       C  
ATOM   2779  CE1 PHE A 429       0.309 -22.428 -45.286  1.00124.16           C  
ANISOU 2779  CE1 PHE A 429    18854  18331   9991   6490    533  -5186       C  
ATOM   2780  CE2 PHE A 429       1.270 -21.129 -43.527  1.00124.80           C  
ANISOU 2780  CE2 PHE A 429    18638  19142   9637   6287    464  -5185       C  
ATOM   2781  CZ  PHE A 429       0.606 -22.263 -43.950  1.00124.88           C  
ANISOU 2781  CZ  PHE A 429    19134  18393   9922   6604    409  -5129       C  
ATOM   2782  N   ASN A 430       4.070 -17.636 -48.673  1.00143.45           N  
ANISOU 2782  N   ASN A 430    17070  26308  11126   4655    930  -5520       N  
ATOM   2783  CA  ASN A 430       4.203 -16.699 -49.780  1.00149.88           C  
ANISOU 2783  CA  ASN A 430    17164  27934  11850   3972   1070  -5421       C  
ATOM   2784  C   ASN A 430       5.593 -16.803 -50.389  1.00163.97           C  
ANISOU 2784  C   ASN A 430    18024  31034  13242   4298    920  -5534       C  
ATOM   2785  O   ASN A 430       6.578 -17.040 -49.682  1.00163.62           O  
ANISOU 2785  O   ASN A 430    17744  31477  12947   4778    714  -5648       O  
ATOM   2786  CB  ASN A 430       3.932 -15.261 -49.326  1.00139.31           C  
ANISOU 2786  CB  ASN A 430    15651  26541  10741   2956   1085  -5075       C  
ATOM   2787  CG  ASN A 430       3.860 -14.287 -50.487  1.00129.45           C  
ANISOU 2787  CG  ASN A 430    13758  25879   9547   2113   1189  -4858       C  
ATOM   2788  OD1 ASN A 430       4.849 -13.640 -50.833  1.00130.15           O  
ANISOU 2788  OD1 ASN A 430    12984  27117   9350   1844   1085  -4775       O  
ATOM   2789  ND2 ASN A 430       2.685 -14.182 -51.099  1.00127.23           N  
ANISOU 2789  ND2 ASN A 430    13888  24821   9633   1674   1380  -4743       N  
ATOM   2790  N   HIS A 431       5.664 -16.617 -51.707  1.00168.41           N  
ANISOU 2790  N   HIS A 431    18052  32185  13750   4026   1015  -5499       N  
ATOM   2791  CA  HIS A 431       6.922 -16.723 -52.434  1.00178.51           C  
ANISOU 2791  CA  HIS A 431    18410  34758  14657   4300    873  -5602       C  
ATOM   2792  C   HIS A 431       7.607 -15.376 -52.625  1.00175.94           C  
ANISOU 2792  C   HIS A 431    17180  35593  14077   3508    869  -5361       C  
ATOM   2793  O   HIS A 431       8.841 -15.322 -52.676  1.00187.45           O  
ANISOU 2793  O   HIS A 431    17886  38159  15176   3743    694  -5421       O  
ATOM   2794  CB  HIS A 431       6.683 -17.377 -53.799  1.00186.17           C  
ANISOU 2794  CB  HIS A 431    19270  35792  15675   4508    926  -5707       C  
ATOM   2795  CG  HIS A 431       7.934 -17.838 -54.480  1.00193.21           C  
ANISOU 2795  CG  HIS A 431    19355  37868  16187   5029    719  -5910       C  
ATOM   2796  ND1 HIS A 431       8.386 -17.288 -55.660  1.00191.60           N  
ANISOU 2796  ND1 HIS A 431    18298  38741  15760   4605    740  -5812       N  
ATOM   2797  CD2 HIS A 431       8.826 -18.801 -54.148  1.00196.60           C  
ANISOU 2797  CD2 HIS A 431    19693  38594  16411   5930    457  -6207       C  
ATOM   2798  CE1 HIS A 431       9.503 -17.892 -56.025  1.00197.24           C  
ANISOU 2798  CE1 HIS A 431    18427  40386  16130   5234    506  -6058       C  
ATOM   2799  NE2 HIS A 431       9.792 -18.814 -55.124  1.00201.12           N  
ANISOU 2799  NE2 HIS A 431    19364  40421  16631   6050    330  -6314       N  
ATOM   2800  N   ASP A 432       6.838 -14.290 -52.730  1.00162.87           N  
ANISOU 2800  N   ASP A 432    15565  33715  12603   2547   1028  -5078       N  
ATOM   2801  CA  ASP A 432       7.437 -12.970 -52.906  1.00166.84           C  
ANISOU 2801  CA  ASP A 432    15217  35278  12896   1686    973  -4784       C  
ATOM   2802  C   ASP A 432       8.143 -12.511 -51.636  1.00164.71           C  
ANISOU 2802  C   ASP A 432    14852  35116  12616   1674    730  -4690       C  
ATOM   2803  O   ASP A 432       9.271 -12.008 -51.688  1.00163.96           O  
ANISOU 2803  O   ASP A 432    13917  36204  12175   1539    571  -4602       O  
ATOM   2804  CB  ASP A 432       6.369 -11.959 -53.324  1.00168.26           C  
ANISOU 2804  CB  ASP A 432    15554  34796  13582    595   1059  -4379       C  
ATOM   2805  CG  ASP A 432       6.009 -12.066 -54.791  1.00181.75           C  
ANISOU 2805  CG  ASP A 432    16974  36893  15191    379   1258  -4373       C  
ATOM   2806  OD1 ASP A 432       6.912 -12.357 -55.604  1.00183.58           O  
ANISOU 2806  OD1 ASP A 432    16497  38157  15096    672   1170  -4435       O  
ATOM   2807  OD2 ASP A 432       4.826 -11.859 -55.133  1.00181.16           O  
ANISOU 2807  OD2 ASP A 432    17408  35868  15558   -103   1399  -4225       O  
ATOM   2808  N   PHE A 433       7.486 -12.666 -50.483  1.00152.67           N  
ANISOU 2808  N   PHE A 433    14163  32391  11454   1800    693  -4696       N  
ATOM   2809  CA  PHE A 433       8.117 -12.302 -49.218  1.00157.01           C  
ANISOU 2809  CA  PHE A 433    14679  32991  11987   1854    461  -4641       C  
ATOM   2810  C   PHE A 433       9.363 -13.139 -48.964  1.00163.37           C  
ANISOU 2810  C   PHE A 433    15130  34693  12249   2806    344  -4974       C  
ATOM   2811  O   PHE A 433      10.395 -12.615 -48.528  1.00181.52           O  
ANISOU 2811  O   PHE A 433    16828  37823  14319   2718    143  -4894       O  
ATOM   2812  CB  PHE A 433       7.119 -12.464 -48.072  1.00167.46           C  
ANISOU 2812  CB  PHE A 433    16994  32887  13746   1900    468  -4627       C  
ATOM   2813  CG  PHE A 433       6.398 -11.198 -47.710  1.00162.60           C  
ANISOU 2813  CG  PHE A 433    16488  31667  13626    884    406  -4272       C  
ATOM   2814  CD1 PHE A 433       7.101 -10.031 -47.462  1.00168.09           C  
ANISOU 2814  CD1 PHE A 433    16514  33024  14328    250    164  -4025       C  
ATOM   2815  CD2 PHE A 433       5.016 -11.173 -47.622  1.00143.17           C  
ANISOU 2815  CD2 PHE A 433    14788  27975  11636    570    557  -4199       C  
ATOM   2816  CE1 PHE A 433       6.440  -8.866 -47.127  1.00159.04           C  
ANISOU 2816  CE1 PHE A 433    15466  31292  13670   -655     43  -3739       C  
ATOM   2817  CE2 PHE A 433       4.349 -10.011 -47.288  1.00136.58           C  
ANISOU 2817  CE2 PHE A 433    14039  26590  11265   -327    468  -3926       C  
ATOM   2818  CZ  PHE A 433       5.062  -8.856 -47.041  1.00143.35           C  
ANISOU 2818  CZ  PHE A 433    14235  28087  12146   -930    195  -3709       C  
ATOM   2819  N   ARG A 434       9.288 -14.443 -49.237  1.00150.83           N  
ANISOU 2819  N   ARG A 434    13904  32936  10471   3728    434  -5356       N  
ATOM   2820  CA  ARG A 434      10.439 -15.315 -49.029  1.00158.65           C  
ANISOU 2820  CA  ARG A 434    14594  34502  11183   4629    231  -5609       C  
ATOM   2821  C   ARG A 434      11.579 -14.967 -49.979  1.00167.85           C  
ANISOU 2821  C   ARG A 434    14643  37140  11991   4512    154  -5580       C  
ATOM   2822  O   ARG A 434      12.752 -15.005 -49.589  1.00180.81           O  
ANISOU 2822  O   ARG A 434    15747  39634  13317   4866    -41  -5674       O  
ATOM   2823  CB  ARG A 434      10.016 -16.774 -49.194  1.00158.91           C  
ANISOU 2823  CB  ARG A 434    15289  33694  11395   5496    215  -5872       C  
ATOM   2824  CG  ARG A 434      11.155 -17.776 -49.205  1.00170.46           C  
ANISOU 2824  CG  ARG A 434    16419  35760  12587   6437    -39  -6171       C  
ATOM   2825  CD  ARG A 434      10.609 -19.191 -49.148  1.00174.32           C  
ANISOU 2825  CD  ARG A 434    17697  35236  13299   7227   -125  -6396       C  
ATOM   2826  NE  ARG A 434       9.387 -19.323 -49.936  1.00167.38           N  
ANISOU 2826  NE  ARG A 434    17286  33560  12749   6907     90  -6307       N  
ATOM   2827  CZ  ARG A 434       8.641 -20.421 -49.985  1.00167.59           C  
ANISOU 2827  CZ  ARG A 434    18064  32568  13044   7395     49  -6421       C  
ATOM   2828  NH1 ARG A 434       8.990 -21.494 -49.288  1.00183.59           N  
ANISOU 2828  NH1 ARG A 434    20461  34245  15049   8217   -223  -6621       N  
ATOM   2829  NH2 ARG A 434       7.544 -20.447 -50.729  1.00152.72           N  
ANISOU 2829  NH2 ARG A 434    16555  30017  11454   7041    257  -6321       N  
ATOM   2830  N   ARG A 435      11.256 -14.621 -51.228  1.00170.73           N  
ANISOU 2830  N   ARG A 435    14632  37844  12393   4005    292  -5439       N  
ATOM   2831  CA  ARG A 435      12.294 -14.221 -52.173  1.00193.74           C  
ANISOU 2831  CA  ARG A 435    16453  42204  14954   3798    200  -5359       C  
ATOM   2832  C   ARG A 435      12.935 -12.902 -51.761  1.00197.76           C  
ANISOU 2832  C   ARG A 435    16281  43604  15256   3022    116  -5041       C  
ATOM   2833  O   ARG A 435      14.151 -12.727 -51.896  1.00212.99           O  
ANISOU 2833  O   ARG A 435    17364  46748  16816   3127    -58  -5035       O  
ATOM   2834  CB  ARG A 435      11.712 -14.116 -53.583  1.00198.42           C  
ANISOU 2834  CB  ARG A 435    16854  42892  15646   3366    342  -5241       C  
ATOM   2835  CG  ARG A 435      12.713 -13.654 -54.632  1.00206.50           C  
ANISOU 2835  CG  ARG A 435    16763  45418  16279   3057    204  -5110       C  
ATOM   2836  CD  ARG A 435      12.966 -14.731 -55.673  1.00214.00           C  
ANISOU 2836  CD  ARG A 435    17575  46654  17083   3753    124  -5419       C  
ATOM   2837  NE  ARG A 435      14.075 -14.383 -56.557  1.00229.52           N  
ANISOU 2837  NE  ARG A 435    18510  50143  18553   3564    -94  -5346       N  
ATOM   2838  CZ  ARG A 435      14.456 -15.111 -57.601  1.00241.90           C  
ANISOU 2838  CZ  ARG A 435    19768  52276  19866   4023   -220  -5587       C  
ATOM   2839  NH1 ARG A 435      13.815 -16.232 -57.900  1.00242.42           N  
ANISOU 2839  NH1 ARG A 435    20438  51492  20178   4701   -146  -5909       N  
ATOM   2840  NH2 ARG A 435      15.479 -14.717 -58.347  1.00246.61           N  
ANISOU 2840  NH2 ARG A 435    19509  54291  19902   3784   -457  -5504       N  
ATOM   2841  N   ALA A 436      12.133 -11.964 -51.252  1.00186.04           N  
ANISOU 2841  N   ALA A 436    15155  41539  13992   2222    193  -4773       N  
ATOM   2842  CA  ALA A 436      12.676 -10.681 -50.819  1.00177.73           C  
ANISOU 2842  CA  ALA A 436    13540  40981  13007   1394    -34  -4362       C  
ATOM   2843  C   ALA A 436      13.552 -10.841 -49.583  1.00180.04           C  
ANISOU 2843  C   ALA A 436    13833  41431  13142   1915   -257  -4501       C  
ATOM   2844  O   ALA A 436      14.575 -10.160 -49.449  1.00186.76           O  
ANISOU 2844  O   ALA A 436    13905  43294  13760   1621   -467  -4315       O  
ATOM   2845  CB  ALA A 436      11.541  -9.695 -50.554  1.00166.76           C  
ANISOU 2845  CB  ALA A 436    12628  38455  12277    416    -58  -3971       C  
ATOM   2846  N   PHE A 437      13.165 -11.733 -48.667  1.00177.86           N  
ANISOU 2846  N   PHE A 437    14418  40169  12990   2669   -232  -4803       N  
ATOM   2847  CA  PHE A 437      14.006 -12.006 -47.505  1.00168.92           C  
ANISOU 2847  CA  PHE A 437    13313  39193  11674   3245   -443  -4963       C  
ATOM   2848  C   PHE A 437      15.316 -12.659 -47.921  1.00182.37           C  
ANISOU 2848  C   PHE A 437    14281  42228  12781   3992   -506  -5262       C  
ATOM   2849  O   PHE A 437      16.379 -12.338 -47.376  1.00185.46           O  
ANISOU 2849  O   PHE A 437    14145  43398  12924   4069   -713  -5232       O  
ATOM   2850  CB  PHE A 437      13.261 -12.894 -46.508  1.00161.76           C  
ANISOU 2850  CB  PHE A 437    13492  36952  11018   3886   -408  -5194       C  
ATOM   2851  CG  PHE A 437      12.001 -12.281 -45.966  1.00154.83           C  
ANISOU 2851  CG  PHE A 437    13333  34762  10733   3207   -358  -4922       C  
ATOM   2852  CD1 PHE A 437      11.846 -10.905 -45.916  1.00154.34           C  
ANISOU 2852  CD1 PHE A 437    12941  34731  10968   2170   -467  -4526       C  
ATOM   2853  CD2 PHE A 437      10.970 -13.083 -45.507  1.00150.90           C  
ANISOU 2853  CD2 PHE A 437    13826  33011  10499   3609   -232  -5068       C  
ATOM   2854  CE1 PHE A 437      10.685 -10.343 -45.419  1.00148.51           C  
ANISOU 2854  CE1 PHE A 437    12843  32810  10775   1587   -444  -4332       C  
ATOM   2855  CE2 PHE A 437       9.808 -12.528 -45.010  1.00144.82           C  
ANISOU 2855  CE2 PHE A 437    13683  31101  10242   3002   -179  -4842       C  
ATOM   2856  CZ  PHE A 437       9.666 -11.156 -44.965  1.00142.62           C  
ANISOU 2856  CZ  PHE A 437    13060  30878  10250   2009   -281  -4499       C  
ATOM   2857  N   LYS A 438      15.259 -13.578 -48.888  1.00187.30           N  
ANISOU 2857  N   LYS A 438    14859  42897  13410   4511   -396  -5476       N  
ATOM   2858  CA  LYS A 438      16.477 -14.199 -49.396  1.00205.75           C  
ANISOU 2858  CA  LYS A 438    16459  46313  15403   5162   -546  -5703       C  
ATOM   2859  C   LYS A 438      17.355 -13.188 -50.122  1.00214.25           C  
ANISOU 2859  C   LYS A 438    16364  48880  16162   4482   -591  -5423       C  
ATOM   2860  O   LYS A 438      18.585 -13.303 -50.090  1.00236.02           O  
ANISOU 2860  O   LYS A 438    18391  52711  18574   4848   -760  -5529       O  
ATOM   2861  CB  LYS A 438      16.123 -15.361 -50.325  1.00210.17           C  
ANISOU 2861  CB  LYS A 438    17284  46524  16048   5781   -522  -5980       C  
ATOM   2862  CG  LYS A 438      17.295 -16.257 -50.689  1.00221.29           C  
ANISOU 2862  CG  LYS A 438    18156  48822  17104   6637   -778  -6320       C  
ATOM   2863  CD  LYS A 438      17.774 -17.054 -49.487  1.00231.43           C  
ANISOU 2863  CD  LYS A 438    19860  49711  18361   7505   -970  -6603       C  
ATOM   2864  CE  LYS A 438      18.873 -18.029 -49.874  1.00238.78           C  
ANISOU 2864  CE  LYS A 438    20326  51449  18948   8391  -1272  -6983       C  
ATOM   2865  NZ  LYS A 438      19.326 -18.849 -48.717  1.00235.02           N  
ANISOU 2865  NZ  LYS A 438    20281  50558  18457   9244  -1496  -7256       N  
ATOM   2866  N   LYS A 439      16.748 -12.194 -50.772  1.00195.87           N  
ANISOU 2866  N   LYS A 439    13824  46650  13948   3474   -457  -5045       N  
ATOM   2867  CA  LYS A 439      17.535 -11.180 -51.469  1.00191.75           C  
ANISOU 2867  CA  LYS A 439    12708  47062  13086   2669   -319  -4652       C  
ATOM   2868  C   LYS A 439      18.223 -10.241 -50.486  1.00194.90           C  
ANISOU 2868  C   LYS A 439    12946  47699  13407   2242   -331  -4378       C  
ATOM   2869  O   LYS A 439      19.372  -9.838 -50.703  1.00207.12           O  
ANISOU 2869  O   LYS A 439    14092  50046  14560   2072   -300  -4203       O  
ATOM   2870  CB  LYS A 439      16.645 -10.393 -52.430  1.00188.52           C  
ANISOU 2870  CB  LYS A 439    12406  46418  12804   1679   -198  -4266       C  
ATOM   2871  N   ILE A 440      17.537  -9.880 -49.400  1.00192.83           N  
ANISOU 2871  N   ILE A 440    13134  46443  13688   2016   -554  -4268       N  
ATOM   2872  CA  ILE A 440      18.142  -9.015 -48.392  1.00200.45           C  
ANISOU 2872  CA  ILE A 440    14076  47246  14839   1617   -746  -3969       C  
ATOM   2873  C   ILE A 440      19.257  -9.752 -47.658  1.00201.47           C  
ANISOU 2873  C   ILE A 440    14026  47926  14599   2551   -823  -4328       C  
ATOM   2874  O   ILE A 440      20.285  -9.161 -47.304  1.00194.93           O  
ANISOU 2874  O   ILE A 440    12878  47541  13647   2324   -873  -4113       O  
ATOM   2875  CB  ILE A 440      17.064  -8.496 -47.422  1.00188.23           C  
ANISOU 2875  CB  ILE A 440    13149  44489  13880   1182   -988  -3833       C  
ATOM   2876  CG1 ILE A 440      16.089  -7.569 -48.151  1.00184.04           C  
ANISOU 2876  CG1 ILE A 440    12740  43403  13784    136   -914  -3415       C  
ATOM   2877  CG2 ILE A 440      17.695  -7.775 -46.239  1.00179.82           C  
ANISOU 2877  CG2 ILE A 440    12089  43234  12999    970  -1222  -3639       C  
ATOM   2878  CD1 ILE A 440      16.732  -6.305 -48.683  1.00186.03           C  
ANISOU 2878  CD1 ILE A 440    12648  43920  14115   -780   -881  -2832       C  
ATOM   2879  N   LEU A 441      19.083 -11.056 -47.436  1.00206.74           N  
ANISOU 2879  N   LEU A 441    14961  48480  15109   3619   -860  -4863       N  
ATOM   2880  CA  LEU A 441      20.059 -11.819 -46.666  1.00209.83           C  
ANISOU 2880  CA  LEU A 441    15287  49202  15238   4557   -974  -5213       C  
ATOM   2881  C   LEU A 441      21.274 -12.202 -47.504  1.00219.48           C  
ANISOU 2881  C   LEU A 441    15780  51709  15904   4964   -751  -5409       C  
ATOM   2882  O   LEU A 441      22.401 -12.203 -46.998  1.00218.87           O  
ANISOU 2882  O   LEU A 441    15457  52173  15531   5240   -797  -5477       O  
ATOM   2883  CB  LEU A 441      19.402 -13.071 -46.083  1.00205.42           C  
ANISOU 2883  CB  LEU A 441    15586  47676  14786   5498  -1100  -5634       C  
ATOM   2884  N   CYS A 442      21.069 -12.531 -48.780  1.00218.30           N  
ANISOU 2884  N   CYS A 442    15536  51722  15684   4901   -676  -5425       N  
ATOM   2885  CA  CYS A 442      22.173 -12.996 -49.614  1.00233.48           C  
ANISOU 2885  CA  CYS A 442    17121  54474  17117   5226   -681  -5576       C  
ATOM   2886  C   CYS A 442      23.124 -11.856 -49.959  1.00253.49           C  
ANISOU 2886  C   CYS A 442    19141  57942  19231   4408   -529  -5157       C  
ATOM   2887  O   CYS A 442      24.329 -11.933 -49.694  1.00264.97           O  
ANISOU 2887  O   CYS A 442    20274  60092  20312   4701   -560  -5250       O  
ATOM   2888  CB  CYS A 442      21.629 -13.650 -50.885  1.00239.75           C  
ANISOU 2888  CB  CYS A 442    18008  55180  17906   5340   -892  -5692       C  
ATOM   2889  SG  CYS A 442      22.890 -14.433 -51.924  1.00261.65           S  
ANISOU 2889  SG  CYS A 442    20333  58972  20112   5897  -1010  -5989       S  
ATOM   2890  N   ARG A 443      22.600 -10.787 -50.551  1.00257.87           N  
ANISOU 2890  N   ARG A 443    19633  58500  19846   3376   -377  -4671       N  
ATOM   2891  CA  ARG A 443      23.424  -9.649 -50.944  1.00266.49           C  
ANISOU 2891  CA  ARG A 443    20294  60399  20561   2541   -261  -4179       C  
ATOM   2892  C   ARG A 443      23.538  -8.643 -49.806  1.00272.49           C  
ANISOU 2892  C   ARG A 443    21139  60553  21843   1976   -431  -3765       C  
ATOM   2893  O   ARG A 443      22.752  -8.665 -48.861  1.00270.16           O  
ANISOU 2893  O   ARG A 443    21257  59301  22092   2048   -577  -3825       O  
ATOM   2894  CB  ARG A 443      22.853  -8.969 -52.192  1.00258.53           C  
ANISOU 2894  CB  ARG A 443    19267  59421  19542   1672   -154  -3752       C  
ATOM   2895  CG  ARG A 443      23.241  -9.624 -53.517  1.00259.66           C  
ANISOU 2895  CG  ARG A 443    19179  60129  19351   1972   -159  -3926       C  
ATOM   2896  CD  ARG A 443      22.554 -10.967 -53.717  1.00256.37           C  
ANISOU 2896  CD  ARG A 443    19080  59161  19168   2851   -279  -4484       C  
ATOM   2897  NE  ARG A 443      22.823 -11.530 -55.037  1.00266.83           N  
ANISOU 2897  NE  ARG A 443    20192  61010  20179   3063   -326  -4638       N  
ATOM   2898  CZ  ARG A 443      22.038 -11.359 -56.096  1.00264.56           C  
ANISOU 2898  CZ  ARG A 443    19989  60541  19991   2611   -286  -4464       C  
ATOM   2899  NH1 ARG A 443      20.928 -10.642 -55.991  1.00262.74           N  
ANISOU 2899  NH1 ARG A 443    20082  59581  20168   1908   -190  -4126       N  
ATOM   2900  NH2 ARG A 443      22.360 -11.908 -57.259  1.00261.22           N  
ANISOU 2900  NH2 ARG A 443    19320  60671  19261   2863   -355  -4640       N  
TER    2901      ARG A 443                                                      
HETATM 2902  C1  E3F A1201      -4.271  -7.354 -20.435  1.00139.57           C  
HETATM 2903  N1  E3F A1201      -0.660  -7.765 -21.401  1.00143.90           N  
HETATM 2904  O1  E3F A1201      -3.083  -7.458 -16.551  1.00188.19           O  
HETATM 2905  C2  E3F A1201      -3.121  -7.484 -21.208  1.00142.29           C  
HETATM 2906  N2  E3F A1201      -0.499  -8.100 -17.092  1.00155.85           N  
HETATM 2907  O2  E3F A1201      -2.344  -9.831 -16.309  1.00170.14           O  
HETATM 2908  C3  E3F A1201      -3.189  -7.237 -22.571  1.00142.85           C  
HETATM 2909  O3  E3F A1201      -6.681  -6.203 -22.934  1.00113.70           O  
HETATM 2910  C4  E3F A1201      -4.364  -6.775 -23.148  1.00131.14           C  
HETATM 2911  C5  E3F A1201      -5.510  -6.627 -22.375  1.00124.27           C  
HETATM 2912  C6  E3F A1201      -5.460  -6.926 -21.018  1.00131.89           C  
HETATM 2913  C7  E3F A1201      -1.929  -7.947 -20.620  1.00142.70           C  
HETATM 2914  C8  E3F A1201      -1.015  -8.279 -22.733  1.00144.83           C  
HETATM 2915  C9  E3F A1201      -2.047  -7.334 -23.334  1.00144.90           C  
HETATM 2916  C10 E3F A1201      -1.778  -7.517 -19.148  1.00148.06           C  
HETATM 2917  C11 E3F A1201      -0.692  -8.396 -18.537  1.00154.24           C  
HETATM 2918  C12 E3F A1201       0.584  -8.182 -19.297  1.00153.35           C  
HETATM 2919  C13 E3F A1201       0.369  -8.603 -20.753  1.00147.07           C  
HETATM 2920  C14 E3F A1201      -0.046  -6.700 -16.929  1.00141.61           C  
HETATM 2921  C15 E3F A1201       1.224  -6.477 -17.738  1.00145.33           C  
HETATM 2922  C16 E3F A1201       1.028  -6.734 -19.220  1.00149.21           C  
HETATM 2923  C17 E3F A1201      -1.504  -8.021 -14.419  1.00172.99           C  
HETATM 2924  C18 E3F A1201      -6.550  -5.939 -24.336  1.00107.93           C  
HETATM 2925  C19 E3F A1201      -0.362  -8.931 -13.958  1.00169.17           C  
HETATM 2926  S1  E3F A1201      -1.917  -8.368 -16.168  1.00173.57           S  
HETATM 2927  C1  PEG A1202     -16.643  -1.746 -25.599  1.00120.27           C  
HETATM 2928  O1  PEG A1202     -18.030  -1.559 -25.544  1.00128.98           O  
HETATM 2929  C2  PEG A1202     -15.938  -0.393 -25.639  1.00115.92           C  
HETATM 2930  O2  PEG A1202     -14.636  -0.541 -25.147  1.00122.37           O  
HETATM 2931  C3  PEG A1202     -13.888   0.641 -25.133  1.00125.17           C  
HETATM 2932  C4  PEG A1202     -14.048   1.349 -23.790  1.00123.05           C  
HETATM 2933  O4  PEG A1202     -15.018   2.354 -23.900  1.00112.70           O  
HETATM 2934  C1  PEG A1203     -26.196 -30.969 -58.534  1.00115.14           C  
HETATM 2935  O1  PEG A1203     -26.453 -31.473 -59.816  1.00104.93           O  
HETATM 2936  C2  PEG A1203     -24.709 -30.648 -58.416  1.00114.13           C  
HETATM 2937  O2  PEG A1203     -24.520 -29.704 -57.403  1.00109.10           O  
HETATM 2938  C3  PEG A1203     -23.188 -29.563 -57.001  1.00104.88           C  
HETATM 2939  C4  PEG A1203     -23.161 -28.966 -55.597  1.00107.76           C  
HETATM 2940  O4  PEG A1203     -21.840 -28.671 -55.235  1.00 99.86           O  
HETATM 2941  C1  PEG A1204     -22.062 -36.283 -66.849  1.00 94.85           C  
HETATM 2942  O1  PEG A1204     -22.734 -36.296 -68.076  1.00 81.89           O  
HETATM 2943  C2  PEG A1204     -22.824 -37.152 -65.854  1.00105.18           C  
HETATM 2944  O2  PEG A1204     -22.046 -37.313 -64.705  1.00113.98           O  
HETATM 2945  C3  PEG A1204     -21.504 -38.594 -64.580  1.00115.48           C  
HETATM 2946  C4  PEG A1204     -20.781 -38.700 -63.241  1.00111.39           C  
HETATM 2947  O4  PEG A1204     -20.593 -40.053 -62.935  1.00115.54           O  
HETATM 2948  C1  PEG A1205     -20.741 -32.593 -65.713  1.00 98.72           C  
HETATM 2949  O1  PEG A1205     -21.360 -32.999 -66.902  1.00 85.11           O  
HETATM 2950  C2  PEG A1205     -21.456 -33.245 -64.534  1.00109.88           C  
HETATM 2951  O2  PEG A1205     -20.816 -32.888 -63.343  1.00112.22           O  
HETATM 2952  C3  PEG A1205     -21.683 -32.837 -62.248  1.00108.66           C  
HETATM 2953  C4  PEG A1205     -20.912 -33.184 -60.978  1.00108.37           C  
HETATM 2954  O4  PEG A1205     -21.773 -33.114 -59.877  1.00108.76           O  
HETATM 2955  C1  PEG A1206      -9.553 -17.332 -51.709  1.00 84.76           C  
HETATM 2956  O1  PEG A1206     -10.426 -16.239 -51.783  1.00 74.63           O  
HETATM 2957  C2  PEG A1206      -9.074 -17.496 -50.270  1.00 89.71           C  
HETATM 2958  O2  PEG A1206     -10.176 -17.734 -49.441  1.00 87.41           O  
HETATM 2959  C3  PEG A1206      -9.834 -17.962 -48.105  1.00 82.93           C  
HETATM 2960  C4  PEG A1206     -11.054 -18.481 -47.348  1.00 84.00           C  
HETATM 2961  O4  PEG A1206     -10.683 -18.804 -46.037  1.00 97.63           O  
HETATM 2962  C1  OLA A1207     -16.137   1.035 -51.200  1.00116.95           C  
HETATM 2963  O1  OLA A1207     -16.422   0.252 -52.133  1.00115.13           O  
HETATM 2964  O2  OLA A1207     -15.613   2.137 -51.476  1.00129.18           O  
HETATM 2965  C2  OLA A1207     -16.416   0.651 -49.763  1.00 93.29           C  
HETATM 2966  C3  OLA A1207     -15.685   1.603 -48.823  1.00 82.04           C  
HETATM 2967  C4  OLA A1207     -16.612   2.141 -47.738  1.00 85.48           C  
HETATM 2968  CAC FLC A1208      -1.651 -14.660 -65.508  1.00118.77           C  
HETATM 2969  CA  FLC A1208      -1.582 -13.616 -64.398  1.00122.73           C  
HETATM 2970  CB  FLC A1208      -0.836 -14.205 -63.205  1.00121.33           C  
HETATM 2971  CBC FLC A1208      -1.859 -14.706 -62.187  1.00120.74           C  
HETATM 2972  CG  FLC A1208       0.039 -13.124 -62.573  1.00114.97           C  
HETATM 2973  CGC FLC A1208       1.202 -13.779 -61.832  1.00119.37           C  
HETATM 2974  OA1 FLC A1208      -1.397 -14.321 -66.691  1.00130.95           O  
HETATM 2975  OA2 FLC A1208      -1.956 -15.852 -65.242  1.00112.50           O  
HETATM 2976  OB1 FLC A1208      -2.940 -15.214 -62.584  1.00120.77           O  
HETATM 2977  OB2 FLC A1208      -1.627 -14.607 -60.954  1.00116.57           O  
HETATM 2978  OG1 FLC A1208       1.222 -15.026 -61.665  1.00132.20           O  
HETATM 2979  OG2 FLC A1208       2.141 -13.069 -61.389  1.00114.30           O  
HETATM 2980  OHB FLC A1208      -0.031 -15.269 -63.634  1.00124.22           O  
CONECT  542 1108                                                                
CONECT 1108  542                                                                
CONECT 2902 2905 2912                                                           
CONECT 2903 2913 2914 2919                                                      
CONECT 2904 2926                                                                
CONECT 2905 2902 2908 2913                                                      
CONECT 2906 2917 2920 2926                                                      
CONECT 2907 2926                                                                
CONECT 2908 2905 2910 2915                                                      
CONECT 2909 2911 2924                                                           
CONECT 2910 2908 2911                                                           
CONECT 2911 2909 2910 2912                                                      
CONECT 2912 2902 2911                                                           
CONECT 2913 2903 2905 2916                                                      
CONECT 2914 2903 2915                                                           
CONECT 2915 2908 2914                                                           
CONECT 2916 2913 2917                                                           
CONECT 2917 2906 2916 2918                                                      
CONECT 2918 2917 2919 2922                                                      
CONECT 2919 2903 2918                                                           
CONECT 2920 2906 2921                                                           
CONECT 2921 2920 2922                                                           
CONECT 2922 2918 2921                                                           
CONECT 2923 2925 2926                                                           
CONECT 2924 2909                                                                
CONECT 2925 2923                                                                
CONECT 2926 2904 2906 2907 2923                                                 
CONECT 2927 2928 2929                                                           
CONECT 2928 2927                                                                
CONECT 2929 2927 2930                                                           
CONECT 2930 2929 2931                                                           
CONECT 2931 2930 2932                                                           
CONECT 2932 2931 2933                                                           
CONECT 2933 2932                                                                
CONECT 2934 2935 2936                                                           
CONECT 2935 2934                                                                
CONECT 2936 2934 2937                                                           
CONECT 2937 2936 2938                                                           
CONECT 2938 2937 2939                                                           
CONECT 2939 2938 2940                                                           
CONECT 2940 2939                                                                
CONECT 2941 2942 2943                                                           
CONECT 2942 2941                                                                
CONECT 2943 2941 2944                                                           
CONECT 2944 2943 2945                                                           
CONECT 2945 2944 2946                                                           
CONECT 2946 2945 2947                                                           
CONECT 2947 2946                                                                
CONECT 2948 2949 2950                                                           
CONECT 2949 2948                                                                
CONECT 2950 2948 2951                                                           
CONECT 2951 2950 2952                                                           
CONECT 2952 2951 2953                                                           
CONECT 2953 2952 2954                                                           
CONECT 2954 2953                                                                
CONECT 2955 2956 2957                                                           
CONECT 2956 2955                                                                
CONECT 2957 2955 2958                                                           
CONECT 2958 2957 2959                                                           
CONECT 2959 2958 2960                                                           
CONECT 2960 2959 2961                                                           
CONECT 2961 2960                                                                
CONECT 2962 2963 2964 2965                                                      
CONECT 2963 2962                                                                
CONECT 2964 2962                                                                
CONECT 2965 2962 2966                                                           
CONECT 2966 2965 2967                                                           
CONECT 2967 2966                                                                
CONECT 2968 2969 2974 2975                                                      
CONECT 2969 2968 2970                                                           
CONECT 2970 2969 2971 2972 2980                                                 
CONECT 2971 2970 2976 2977                                                      
CONECT 2972 2970 2973                                                           
CONECT 2973 2972 2978 2979                                                      
CONECT 2974 2968                                                                
CONECT 2975 2968                                                                
CONECT 2976 2971                                                                
CONECT 2977 2971                                                                
CONECT 2978 2973                                                                
CONECT 2979 2973                                                                
CONECT 2980 2970                                                                
MASTER      376    0    8   18    0    0   11    6 2979    1   81   31          
END